data_9GK6
# 
_entry.id   9GK6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9GK6         pdb_00009gk6 10.2210/pdb9gk6/pdb 
WWPDB D_1292141214 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GK6 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              paul.2.rowland@gsk.com 
_pdbx_contact_author.name_first         Paul 
_pdbx_contact_author.name_last          Rowland 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9858-1514 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Convery, M.' 1 ? 
'Rowland, P.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                2107 
_citation.page_last                 2114 
_citation.title                     
'Optimization of Potent and Selective Cyclohexyl Acid ERAP1 Inhibitors Using Structure- and Property-Based Drug Design.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.4c00401 
_citation.pdbx_database_id_PubMed   39691536 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hryczanek, R.P.'   1  0009-0003-7005-4477 
primary 'Hackett, A.S.'     2  ?                   
primary 'Rowland, P.'       3  ?                   
primary 'Chung, C.W.'       4  0000-0002-2480-3110 
primary 'Convery, M.A.'     5  ?                   
primary 'Holmes, D.S.'      6  ?                   
primary 'Hutchinson, J.P.'  7  ?                   
primary 'Kitchen, S.'       8  ?                   
primary 'Korczynska, J.'    9  ?                   
primary 'Law, R.P.'         10 0000-0002-2585-4585 
primary 'Lea, J.D.'         11 ?                   
primary 'Liddle, J.'        12 ?                   
primary 'Lonsdale, R.'      13 0000-0001-9160-4659 
primary 'Neu, M.'           14 ?                   
primary 'Nickels, L.'       15 ?                   
primary 'Phillipou, A.'     16 ?                   
primary 'Rowedder, J.E.'    17 ?                   
primary 'Schneck, J.L.'     18 ?                   
primary 'Scott-Stevens, P.' 19 ?                   
primary 'Sheehan, H.'       20 ?                   
primary 'Tayler, C.L.'      21 ?                   
primary 'Temponeras, I.'    22 ?                   
primary 'Tinworth, C.P.'    23 0000-0002-2756-707X 
primary 'Walker, A.L.'      24 ?                   
primary 'Wojno-Picon, J.'   25 ?                   
primary 'Young, R.J.'       26 0000-0002-7763-0575 
primary 'Lindsay, D.M.'     27 0000-0003-4498-5094 
primary 'Stratikos, E.'     28 0000-0002-3566-2309 
# 
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 'Endoplasmic reticulum aminopeptidase 1'                                                              105371.414 
1    3.4.11.- ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                                            65.409     
1    ?        ? ? ? 
3 non-polymer syn D-MALATE                                                                                              134.087    
2    ?        ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                                        62.068     
16   ?        ? ? ? 
5 non-polymer syn '1-[2-(6-chloranyl-3-oxidanylidene-1,4-benzothiazin-4-yl)ethanoylamino]cyclohexane-1-carboxylic acid' 382.862    
1    ?        ? ? ? 
6 water       nat water                                                                                                 18.015     
1230 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;ARTS-1,Adipocyte-derived leucine aminopeptidase,A-LAP,Aminopeptidase PILS,Puromycin-insensitive leucyl-specific aminopeptidase,PILS-AP,Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
;
# 
_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       
;MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHAQLTTLTFWGTT
KVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGQLSETFH
GFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTV
KMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAME
NWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYF
FGKCFDAMEVDALQSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWD
SMASIGSGGVDVKTMMNTWTLQRGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTK
TDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLK
HETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQ
RAEGYFRKWKESNGQLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGD
KIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQL
RCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERMENLYFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHAQLTTLTFWGTT
KVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGQLSETFH
GFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTV
KMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAME
NWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYF
FGKCFDAMEVDALQSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWD
SMASIGSGGVDVKTMMNTWTLQRGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTK
TDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLK
HETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQ
RAEGYFRKWKESNGQLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGD
KIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQL
RCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERMENLYFQ
;
_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 'ZINC ION'                                                                                            ZN    
3 D-MALATE                                                                                              MLT   
4 1,2-ETHANEDIOL                                                                                        EDO   
5 '1-[2-(6-chloranyl-3-oxidanylidene-1,4-benzothiazin-4-yl)ethanoylamino]cyclohexane-1-carboxylic acid' A1IMM 
6 water                                                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   VAL n 
1 3   PHE n 
1 4   LEU n 
1 5   PRO n 
1 6   LEU n 
1 7   LYS n 
1 8   TRP n 
1 9   SER n 
1 10  LEU n 
1 11  ALA n 
1 12  THR n 
1 13  MET n 
1 14  SER n 
1 15  PHE n 
1 16  LEU n 
1 17  LEU n 
1 18  SER n 
1 19  SER n 
1 20  LEU n 
1 21  LEU n 
1 22  ALA n 
1 23  LEU n 
1 24  LEU n 
1 25  THR n 
1 26  VAL n 
1 27  SER n 
1 28  THR n 
1 29  PRO n 
1 30  SER n 
1 31  TRP n 
1 32  CYS n 
1 33  GLN n 
1 34  SER n 
1 35  THR n 
1 36  GLU n 
1 37  ALA n 
1 38  SER n 
1 39  PRO n 
1 40  LYS n 
1 41  ARG n 
1 42  SER n 
1 43  ASP n 
1 44  GLY n 
1 45  THR n 
1 46  PRO n 
1 47  PHE n 
1 48  PRO n 
1 49  TRP n 
1 50  ASN n 
1 51  LYS n 
1 52  ILE n 
1 53  ARG n 
1 54  LEU n 
1 55  PRO n 
1 56  GLU n 
1 57  TYR n 
1 58  VAL n 
1 59  ILE n 
1 60  PRO n 
1 61  VAL n 
1 62  HIS n 
1 63  TYR n 
1 64  ASP n 
1 65  LEU n 
1 66  LEU n 
1 67  ILE n 
1 68  HIS n 
1 69  ALA n 
1 70  GLN n 
1 71  LEU n 
1 72  THR n 
1 73  THR n 
1 74  LEU n 
1 75  THR n 
1 76  PHE n 
1 77  TRP n 
1 78  GLY n 
1 79  THR n 
1 80  THR n 
1 81  LYS n 
1 82  VAL n 
1 83  GLU n 
1 84  ILE n 
1 85  THR n 
1 86  ALA n 
1 87  SER n 
1 88  GLN n 
1 89  PRO n 
1 90  THR n 
1 91  SER n 
1 92  THR n 
1 93  ILE n 
1 94  ILE n 
1 95  LEU n 
1 96  HIS n 
1 97  SER n 
1 98  HIS n 
1 99  HIS n 
1 100 LEU n 
1 101 GLN n 
1 102 ILE n 
1 103 SER n 
1 104 ARG n 
1 105 ALA n 
1 106 THR n 
1 107 LEU n 
1 108 ARG n 
1 109 LYS n 
1 110 GLY n 
1 111 ALA n 
1 112 GLY n 
1 113 GLU n 
1 114 ARG n 
1 115 LEU n 
1 116 SER n 
1 117 GLU n 
1 118 GLU n 
1 119 PRO n 
1 120 LEU n 
1 121 GLN n 
1 122 VAL n 
1 123 LEU n 
1 124 GLU n 
1 125 HIS n 
1 126 PRO n 
1 127 ARG n 
1 128 GLN n 
1 129 GLU n 
1 130 GLN n 
1 131 ILE n 
1 132 ALA n 
1 133 LEU n 
1 134 LEU n 
1 135 ALA n 
1 136 PRO n 
1 137 GLU n 
1 138 PRO n 
1 139 LEU n 
1 140 LEU n 
1 141 VAL n 
1 142 GLY n 
1 143 LEU n 
1 144 PRO n 
1 145 TYR n 
1 146 THR n 
1 147 VAL n 
1 148 VAL n 
1 149 ILE n 
1 150 HIS n 
1 151 TYR n 
1 152 ALA n 
1 153 GLY n 
1 154 GLN n 
1 155 LEU n 
1 156 SER n 
1 157 GLU n 
1 158 THR n 
1 159 PHE n 
1 160 HIS n 
1 161 GLY n 
1 162 PHE n 
1 163 TYR n 
1 164 LYS n 
1 165 SER n 
1 166 THR n 
1 167 TYR n 
1 168 ARG n 
1 169 THR n 
1 170 LYS n 
1 171 GLU n 
1 172 GLY n 
1 173 GLU n 
1 174 LEU n 
1 175 ARG n 
1 176 ILE n 
1 177 LEU n 
1 178 ALA n 
1 179 SER n 
1 180 THR n 
1 181 GLN n 
1 182 PHE n 
1 183 GLU n 
1 184 PRO n 
1 185 THR n 
1 186 ALA n 
1 187 ALA n 
1 188 ARG n 
1 189 MET n 
1 190 ALA n 
1 191 PHE n 
1 192 PRO n 
1 193 CYS n 
1 194 PHE n 
1 195 ASP n 
1 196 GLU n 
1 197 PRO n 
1 198 ALA n 
1 199 PHE n 
1 200 LYS n 
1 201 ALA n 
1 202 SER n 
1 203 PHE n 
1 204 SER n 
1 205 ILE n 
1 206 LYS n 
1 207 ILE n 
1 208 ARG n 
1 209 ARG n 
1 210 GLU n 
1 211 PRO n 
1 212 ARG n 
1 213 HIS n 
1 214 LEU n 
1 215 ALA n 
1 216 ILE n 
1 217 SER n 
1 218 ASN n 
1 219 MET n 
1 220 PRO n 
1 221 LEU n 
1 222 VAL n 
1 223 LYS n 
1 224 SER n 
1 225 VAL n 
1 226 THR n 
1 227 VAL n 
1 228 ALA n 
1 229 GLU n 
1 230 GLY n 
1 231 LEU n 
1 232 ILE n 
1 233 GLU n 
1 234 ASP n 
1 235 HIS n 
1 236 PHE n 
1 237 ASP n 
1 238 VAL n 
1 239 THR n 
1 240 VAL n 
1 241 LYS n 
1 242 MET n 
1 243 SER n 
1 244 THR n 
1 245 TYR n 
1 246 LEU n 
1 247 VAL n 
1 248 ALA n 
1 249 PHE n 
1 250 ILE n 
1 251 ILE n 
1 252 SER n 
1 253 ASP n 
1 254 PHE n 
1 255 GLU n 
1 256 SER n 
1 257 VAL n 
1 258 SER n 
1 259 LYS n 
1 260 ILE n 
1 261 THR n 
1 262 LYS n 
1 263 SER n 
1 264 GLY n 
1 265 VAL n 
1 266 LYS n 
1 267 VAL n 
1 268 SER n 
1 269 VAL n 
1 270 TYR n 
1 271 ALA n 
1 272 VAL n 
1 273 PRO n 
1 274 ASP n 
1 275 LYS n 
1 276 ILE n 
1 277 ASN n 
1 278 GLN n 
1 279 ALA n 
1 280 ASP n 
1 281 TYR n 
1 282 ALA n 
1 283 LEU n 
1 284 ASP n 
1 285 ALA n 
1 286 ALA n 
1 287 VAL n 
1 288 THR n 
1 289 LEU n 
1 290 LEU n 
1 291 GLU n 
1 292 PHE n 
1 293 TYR n 
1 294 GLU n 
1 295 ASP n 
1 296 TYR n 
1 297 PHE n 
1 298 SER n 
1 299 ILE n 
1 300 PRO n 
1 301 TYR n 
1 302 PRO n 
1 303 LEU n 
1 304 PRO n 
1 305 LYS n 
1 306 GLN n 
1 307 ASP n 
1 308 LEU n 
1 309 ALA n 
1 310 ALA n 
1 311 ILE n 
1 312 PRO n 
1 313 ASP n 
1 314 PHE n 
1 315 GLN n 
1 316 SER n 
1 317 GLY n 
1 318 ALA n 
1 319 MET n 
1 320 GLU n 
1 321 ASN n 
1 322 TRP n 
1 323 GLY n 
1 324 LEU n 
1 325 THR n 
1 326 THR n 
1 327 TYR n 
1 328 ARG n 
1 329 GLU n 
1 330 SER n 
1 331 ALA n 
1 332 LEU n 
1 333 LEU n 
1 334 PHE n 
1 335 ASP n 
1 336 ALA n 
1 337 GLU n 
1 338 LYS n 
1 339 SER n 
1 340 SER n 
1 341 ALA n 
1 342 SER n 
1 343 SER n 
1 344 LYS n 
1 345 LEU n 
1 346 GLY n 
1 347 ILE n 
1 348 THR n 
1 349 MET n 
1 350 THR n 
1 351 VAL n 
1 352 ALA n 
1 353 HIS n 
1 354 GLU n 
1 355 LEU n 
1 356 ALA n 
1 357 HIS n 
1 358 GLN n 
1 359 TRP n 
1 360 PHE n 
1 361 GLY n 
1 362 ASN n 
1 363 LEU n 
1 364 VAL n 
1 365 THR n 
1 366 MET n 
1 367 GLU n 
1 368 TRP n 
1 369 TRP n 
1 370 ASN n 
1 371 ASP n 
1 372 LEU n 
1 373 TRP n 
1 374 LEU n 
1 375 ASN n 
1 376 GLU n 
1 377 GLY n 
1 378 PHE n 
1 379 ALA n 
1 380 LYS n 
1 381 PHE n 
1 382 MET n 
1 383 GLU n 
1 384 PHE n 
1 385 VAL n 
1 386 SER n 
1 387 VAL n 
1 388 SER n 
1 389 VAL n 
1 390 THR n 
1 391 HIS n 
1 392 PRO n 
1 393 GLU n 
1 394 LEU n 
1 395 LYS n 
1 396 VAL n 
1 397 GLY n 
1 398 ASP n 
1 399 TYR n 
1 400 PHE n 
1 401 PHE n 
1 402 GLY n 
1 403 LYS n 
1 404 CYS n 
1 405 PHE n 
1 406 ASP n 
1 407 ALA n 
1 408 MET n 
1 409 GLU n 
1 410 VAL n 
1 411 ASP n 
1 412 ALA n 
1 413 LEU n 
1 414 GLN n 
1 415 SER n 
1 416 SER n 
1 417 HIS n 
1 418 PRO n 
1 419 VAL n 
1 420 SER n 
1 421 THR n 
1 422 PRO n 
1 423 VAL n 
1 424 GLU n 
1 425 ASN n 
1 426 PRO n 
1 427 ALA n 
1 428 GLN n 
1 429 ILE n 
1 430 ARG n 
1 431 GLU n 
1 432 MET n 
1 433 PHE n 
1 434 ASP n 
1 435 ASP n 
1 436 VAL n 
1 437 SER n 
1 438 TYR n 
1 439 ASP n 
1 440 LYS n 
1 441 GLY n 
1 442 ALA n 
1 443 CYS n 
1 444 ILE n 
1 445 LEU n 
1 446 ASN n 
1 447 MET n 
1 448 LEU n 
1 449 ARG n 
1 450 GLU n 
1 451 TYR n 
1 452 LEU n 
1 453 SER n 
1 454 ALA n 
1 455 ASP n 
1 456 ALA n 
1 457 PHE n 
1 458 LYS n 
1 459 SER n 
1 460 GLY n 
1 461 ILE n 
1 462 VAL n 
1 463 GLN n 
1 464 TYR n 
1 465 LEU n 
1 466 GLN n 
1 467 LYS n 
1 468 HIS n 
1 469 SER n 
1 470 TYR n 
1 471 LYS n 
1 472 ASN n 
1 473 THR n 
1 474 LYS n 
1 475 ASN n 
1 476 GLU n 
1 477 ASP n 
1 478 LEU n 
1 479 TRP n 
1 480 ASP n 
1 481 SER n 
1 482 MET n 
1 483 ALA n 
1 484 SER n 
1 485 ILE n 
1 486 GLY n 
1 487 SER n 
1 488 GLY n 
1 489 GLY n 
1 490 VAL n 
1 491 ASP n 
1 492 VAL n 
1 493 LYS n 
1 494 THR n 
1 495 MET n 
1 496 MET n 
1 497 ASN n 
1 498 THR n 
1 499 TRP n 
1 500 THR n 
1 501 LEU n 
1 502 GLN n 
1 503 ARG n 
1 504 GLY n 
1 505 PHE n 
1 506 PRO n 
1 507 LEU n 
1 508 ILE n 
1 509 THR n 
1 510 ILE n 
1 511 THR n 
1 512 VAL n 
1 513 ARG n 
1 514 GLY n 
1 515 ARG n 
1 516 ASN n 
1 517 VAL n 
1 518 HIS n 
1 519 MET n 
1 520 LYS n 
1 521 GLN n 
1 522 GLU n 
1 523 HIS n 
1 524 TYR n 
1 525 MET n 
1 526 LYS n 
1 527 GLY n 
1 528 SER n 
1 529 ASP n 
1 530 GLY n 
1 531 ALA n 
1 532 PRO n 
1 533 ASP n 
1 534 THR n 
1 535 GLY n 
1 536 TYR n 
1 537 LEU n 
1 538 TRP n 
1 539 HIS n 
1 540 VAL n 
1 541 PRO n 
1 542 LEU n 
1 543 THR n 
1 544 PHE n 
1 545 ILE n 
1 546 THR n 
1 547 SER n 
1 548 LYS n 
1 549 SER n 
1 550 ASP n 
1 551 MET n 
1 552 VAL n 
1 553 HIS n 
1 554 ARG n 
1 555 PHE n 
1 556 LEU n 
1 557 LEU n 
1 558 LYS n 
1 559 THR n 
1 560 LYS n 
1 561 THR n 
1 562 ASP n 
1 563 VAL n 
1 564 LEU n 
1 565 ILE n 
1 566 LEU n 
1 567 PRO n 
1 568 GLU n 
1 569 GLU n 
1 570 VAL n 
1 571 GLU n 
1 572 TRP n 
1 573 ILE n 
1 574 LYS n 
1 575 PHE n 
1 576 ASN n 
1 577 VAL n 
1 578 GLY n 
1 579 MET n 
1 580 ASN n 
1 581 GLY n 
1 582 TYR n 
1 583 TYR n 
1 584 ILE n 
1 585 VAL n 
1 586 HIS n 
1 587 TYR n 
1 588 GLU n 
1 589 ASP n 
1 590 ASP n 
1 591 GLY n 
1 592 TRP n 
1 593 ASP n 
1 594 SER n 
1 595 LEU n 
1 596 THR n 
1 597 GLY n 
1 598 LEU n 
1 599 LEU n 
1 600 LYS n 
1 601 GLY n 
1 602 THR n 
1 603 HIS n 
1 604 THR n 
1 605 ALA n 
1 606 VAL n 
1 607 SER n 
1 608 SER n 
1 609 ASN n 
1 610 ASP n 
1 611 ARG n 
1 612 ALA n 
1 613 SER n 
1 614 LEU n 
1 615 ILE n 
1 616 ASN n 
1 617 ASN n 
1 618 ALA n 
1 619 PHE n 
1 620 GLN n 
1 621 LEU n 
1 622 VAL n 
1 623 SER n 
1 624 ILE n 
1 625 GLY n 
1 626 LYS n 
1 627 LEU n 
1 628 SER n 
1 629 ILE n 
1 630 GLU n 
1 631 LYS n 
1 632 ALA n 
1 633 LEU n 
1 634 ASP n 
1 635 LEU n 
1 636 SER n 
1 637 LEU n 
1 638 TYR n 
1 639 LEU n 
1 640 LYS n 
1 641 HIS n 
1 642 GLU n 
1 643 THR n 
1 644 GLU n 
1 645 ILE n 
1 646 MET n 
1 647 PRO n 
1 648 VAL n 
1 649 PHE n 
1 650 GLN n 
1 651 GLY n 
1 652 LEU n 
1 653 ASN n 
1 654 GLU n 
1 655 LEU n 
1 656 ILE n 
1 657 PRO n 
1 658 MET n 
1 659 TYR n 
1 660 LYS n 
1 661 LEU n 
1 662 MET n 
1 663 GLU n 
1 664 LYS n 
1 665 ARG n 
1 666 ASP n 
1 667 MET n 
1 668 ASN n 
1 669 GLU n 
1 670 VAL n 
1 671 GLU n 
1 672 THR n 
1 673 GLN n 
1 674 PHE n 
1 675 LYS n 
1 676 ALA n 
1 677 PHE n 
1 678 LEU n 
1 679 ILE n 
1 680 ARG n 
1 681 LEU n 
1 682 LEU n 
1 683 ARG n 
1 684 ASP n 
1 685 LEU n 
1 686 ILE n 
1 687 ASP n 
1 688 LYS n 
1 689 GLN n 
1 690 THR n 
1 691 TRP n 
1 692 THR n 
1 693 ASP n 
1 694 GLU n 
1 695 GLY n 
1 696 SER n 
1 697 VAL n 
1 698 SER n 
1 699 GLU n 
1 700 ARG n 
1 701 MET n 
1 702 LEU n 
1 703 ARG n 
1 704 SER n 
1 705 GLN n 
1 706 LEU n 
1 707 LEU n 
1 708 LEU n 
1 709 LEU n 
1 710 ALA n 
1 711 CYS n 
1 712 VAL n 
1 713 HIS n 
1 714 ASN n 
1 715 TYR n 
1 716 GLN n 
1 717 PRO n 
1 718 CYS n 
1 719 VAL n 
1 720 GLN n 
1 721 ARG n 
1 722 ALA n 
1 723 GLU n 
1 724 GLY n 
1 725 TYR n 
1 726 PHE n 
1 727 ARG n 
1 728 LYS n 
1 729 TRP n 
1 730 LYS n 
1 731 GLU n 
1 732 SER n 
1 733 ASN n 
1 734 GLY n 
1 735 GLN n 
1 736 LEU n 
1 737 SER n 
1 738 LEU n 
1 739 PRO n 
1 740 VAL n 
1 741 ASP n 
1 742 VAL n 
1 743 THR n 
1 744 LEU n 
1 745 ALA n 
1 746 VAL n 
1 747 PHE n 
1 748 ALA n 
1 749 VAL n 
1 750 GLY n 
1 751 ALA n 
1 752 GLN n 
1 753 SER n 
1 754 THR n 
1 755 GLU n 
1 756 GLY n 
1 757 TRP n 
1 758 ASP n 
1 759 PHE n 
1 760 LEU n 
1 761 TYR n 
1 762 SER n 
1 763 LYS n 
1 764 TYR n 
1 765 GLN n 
1 766 PHE n 
1 767 SER n 
1 768 LEU n 
1 769 SER n 
1 770 SER n 
1 771 THR n 
1 772 GLU n 
1 773 LYS n 
1 774 SER n 
1 775 GLN n 
1 776 ILE n 
1 777 GLU n 
1 778 PHE n 
1 779 ALA n 
1 780 LEU n 
1 781 CYS n 
1 782 ARG n 
1 783 THR n 
1 784 GLN n 
1 785 ASN n 
1 786 LYS n 
1 787 GLU n 
1 788 LYS n 
1 789 LEU n 
1 790 GLN n 
1 791 TRP n 
1 792 LEU n 
1 793 LEU n 
1 794 ASP n 
1 795 GLU n 
1 796 SER n 
1 797 PHE n 
1 798 LYS n 
1 799 GLY n 
1 800 ASP n 
1 801 LYS n 
1 802 ILE n 
1 803 LYS n 
1 804 THR n 
1 805 GLN n 
1 806 GLU n 
1 807 PHE n 
1 808 PRO n 
1 809 GLN n 
1 810 ILE n 
1 811 LEU n 
1 812 THR n 
1 813 LEU n 
1 814 ILE n 
1 815 GLY n 
1 816 ARG n 
1 817 ASN n 
1 818 PRO n 
1 819 VAL n 
1 820 GLY n 
1 821 TYR n 
1 822 PRO n 
1 823 LEU n 
1 824 ALA n 
1 825 TRP n 
1 826 GLN n 
1 827 PHE n 
1 828 LEU n 
1 829 ARG n 
1 830 LYS n 
1 831 ASN n 
1 832 TRP n 
1 833 ASN n 
1 834 LYS n 
1 835 LEU n 
1 836 VAL n 
1 837 GLN n 
1 838 LYS n 
1 839 PHE n 
1 840 GLU n 
1 841 LEU n 
1 842 GLY n 
1 843 SER n 
1 844 SER n 
1 845 SER n 
1 846 ILE n 
1 847 ALA n 
1 848 HIS n 
1 849 MET n 
1 850 VAL n 
1 851 MET n 
1 852 GLY n 
1 853 THR n 
1 854 THR n 
1 855 ASN n 
1 856 GLN n 
1 857 PHE n 
1 858 SER n 
1 859 THR n 
1 860 ARG n 
1 861 THR n 
1 862 ARG n 
1 863 LEU n 
1 864 GLU n 
1 865 GLU n 
1 866 VAL n 
1 867 LYS n 
1 868 GLY n 
1 869 PHE n 
1 870 PHE n 
1 871 SER n 
1 872 SER n 
1 873 LEU n 
1 874 LYS n 
1 875 GLU n 
1 876 ASN n 
1 877 GLY n 
1 878 SER n 
1 879 GLN n 
1 880 LEU n 
1 881 ARG n 
1 882 CYS n 
1 883 VAL n 
1 884 GLN n 
1 885 GLN n 
1 886 THR n 
1 887 ILE n 
1 888 GLU n 
1 889 THR n 
1 890 ILE n 
1 891 GLU n 
1 892 GLU n 
1 893 ASN n 
1 894 ILE n 
1 895 GLY n 
1 896 TRP n 
1 897 MET n 
1 898 ASP n 
1 899 LYS n 
1 900 ASN n 
1 901 PHE n 
1 902 ASP n 
1 903 LYS n 
1 904 ILE n 
1 905 ARG n 
1 906 VAL n 
1 907 TRP n 
1 908 LEU n 
1 909 GLN n 
1 910 SER n 
1 911 GLU n 
1 912 LYS n 
1 913 LEU n 
1 914 GLU n 
1 915 ARG n 
1 916 MET n 
1 917 GLU n 
1 918 ASN n 
1 919 LEU n 
1 920 TYR n 
1 921 PHE n 
1 922 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   485 human ? 'ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154' ? ? ? ? ? ? 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 486 922 human ? 'ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154' ? ? ? ? ? ? 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1IMM non-polymer         . '1-[2-(6-chloranyl-3-oxidanylidene-1,4-benzothiazin-4-yl)ethanoylamino]cyclohexane-1-carboxylic acid' 
'1-[2-(6-chloro-3-oxo-3,4-dihydro-2H-1,4-benzothiazin-4-yl)acetamido]cyclohexane-1-carboxylic acid' 'C17 H19 Cl N2 O4 S' 382.862 
ALA   'L-peptide linking' y ALANINE                                                                                               
?                                                                                                   'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE                                                                                              
?                                                                                                   'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                            
?                                                                                                   'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                       
?                                                                                                   'C4 H7 N O4'         133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                              
?                                                                                                   'C3 H7 N O2 S'       121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                                                                        
'ETHYLENE GLYCOL'                                                                                   'C2 H6 O2'           62.068  
GLN   'L-peptide linking' y GLUTAMINE                                                                                             
?                                                                                                   'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                       
?                                                                                                   'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE                                                                                               
?                                                                                                   'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                             
?                                                                                                   'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER                                                                                                 
?                                                                                                   'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                            
?                                                                                                   'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                               
?                                                                                                   'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE                                                                                                
?                                                                                                   'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE                                                                                            
?                                                                                                   'C5 H11 N O2 S'      149.211 
MLT   non-polymer         . D-MALATE                                                                                              
'(2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID'                                           'C4 H6 O5'           134.087 
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 
ZN    non-polymer         . 'ZINC ION'                                                                                            
?                                                                                                   'Zn 2'               65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   VAL 2   2   ?   ?   ?   A . n 
A 1 3   PHE 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   ?   ?   ?   A . n 
A 1 5   PRO 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   LYS 7   7   ?   ?   ?   A . n 
A 1 8   TRP 8   8   ?   ?   ?   A . n 
A 1 9   SER 9   9   ?   ?   ?   A . n 
A 1 10  LEU 10  10  ?   ?   ?   A . n 
A 1 11  ALA 11  11  ?   ?   ?   A . n 
A 1 12  THR 12  12  ?   ?   ?   A . n 
A 1 13  MET 13  13  ?   ?   ?   A . n 
A 1 14  SER 14  14  ?   ?   ?   A . n 
A 1 15  PHE 15  15  ?   ?   ?   A . n 
A 1 16  LEU 16  16  ?   ?   ?   A . n 
A 1 17  LEU 17  17  ?   ?   ?   A . n 
A 1 18  SER 18  18  ?   ?   ?   A . n 
A 1 19  SER 19  19  ?   ?   ?   A . n 
A 1 20  LEU 20  20  ?   ?   ?   A . n 
A 1 21  LEU 21  21  ?   ?   ?   A . n 
A 1 22  ALA 22  22  ?   ?   ?   A . n 
A 1 23  LEU 23  23  ?   ?   ?   A . n 
A 1 24  LEU 24  24  ?   ?   ?   A . n 
A 1 25  THR 25  25  ?   ?   ?   A . n 
A 1 26  VAL 26  26  ?   ?   ?   A . n 
A 1 27  SER 27  27  ?   ?   ?   A . n 
A 1 28  THR 28  28  ?   ?   ?   A . n 
A 1 29  PRO 29  29  ?   ?   ?   A . n 
A 1 30  SER 30  30  ?   ?   ?   A . n 
A 1 31  TRP 31  31  ?   ?   ?   A . n 
A 1 32  CYS 32  32  ?   ?   ?   A . n 
A 1 33  GLN 33  33  ?   ?   ?   A . n 
A 1 34  SER 34  34  ?   ?   ?   A . n 
A 1 35  THR 35  35  ?   ?   ?   A . n 
A 1 36  GLU 36  36  ?   ?   ?   A . n 
A 1 37  ALA 37  37  ?   ?   ?   A . n 
A 1 38  SER 38  38  ?   ?   ?   A . n 
A 1 39  PRO 39  39  ?   ?   ?   A . n 
A 1 40  LYS 40  40  ?   ?   ?   A . n 
A 1 41  ARG 41  41  ?   ?   ?   A . n 
A 1 42  SER 42  42  ?   ?   ?   A . n 
A 1 43  ASP 43  43  ?   ?   ?   A . n 
A 1 44  GLY 44  44  ?   ?   ?   A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  TRP 49  49  49  TRP TRP A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  HIS 62  62  62  HIS HIS A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  HIS 68  68  68  HIS HIS A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  TRP 77  77  77  TRP TRP A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  GLN 88  88  88  GLN GLN A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  HIS 99  99  99  HIS HIS A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 GLN 101 101 101 GLN GLN A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ALA 111 111 ?   ?   ?   A . n 
A 1 112 GLY 112 112 ?   ?   ?   A . n 
A 1 113 GLU 113 113 ?   ?   ?   A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 GLU 124 124 124 GLU GLU A . n 
A 1 125 HIS 125 125 125 HIS HIS A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 PRO 144 144 144 PRO PRO A . n 
A 1 145 TYR 145 145 145 TYR TYR A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 HIS 150 150 150 HIS HIS A . n 
A 1 151 TYR 151 151 151 TYR TYR A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 HIS 160 160 160 HIS HIS A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 GLN 181 181 181 GLN GLN A . n 
A 1 182 PHE 182 182 182 PHE PHE A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 THR 185 185 185 THR THR A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 MET 189 189 189 MET MET A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 CYS 193 193 193 CYS CYS A . n 
A 1 194 PHE 194 194 194 PHE PHE A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 PHE 199 199 199 PHE PHE A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 LYS 206 206 206 LYS LYS A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 ARG 208 208 208 ARG ARG A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 HIS 213 213 213 HIS HIS A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 MET 219 219 219 MET MET A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 SER 224 224 224 SER SER A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 HIS 235 235 235 HIS HIS A . n 
A 1 236 PHE 236 236 236 PHE PHE A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 THR 244 244 244 THR THR A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 PHE 249 249 249 PHE PHE A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 GLU 255 255 255 GLU GLU A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 THR 261 261 261 THR THR A . n 
A 1 262 LYS 262 262 262 LYS LYS A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 VAL 267 267 267 VAL VAL A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 TYR 270 270 270 TYR TYR A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 PRO 273 273 273 PRO PRO A . n 
A 1 274 ASP 274 274 274 ASP ASP A . n 
A 1 275 LYS 275 275 275 LYS LYS A . n 
A 1 276 ILE 276 276 276 ILE ILE A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLN 278 278 278 GLN GLN A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 ASP 280 280 280 ASP ASP A . n 
A 1 281 TYR 281 281 281 TYR TYR A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 ASP 284 284 284 ASP ASP A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 THR 288 288 288 THR THR A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 GLU 291 291 291 GLU GLU A . n 
A 1 292 PHE 292 292 292 PHE PHE A . n 
A 1 293 TYR 293 293 293 TYR TYR A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 SER 298 298 298 SER SER A . n 
A 1 299 ILE 299 299 299 ILE ILE A . n 
A 1 300 PRO 300 300 300 PRO PRO A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 PRO 302 302 302 PRO PRO A . n 
A 1 303 LEU 303 303 303 LEU LEU A . n 
A 1 304 PRO 304 304 304 PRO PRO A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 GLN 306 306 306 GLN GLN A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 LEU 308 308 308 LEU LEU A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
A 1 311 ILE 311 311 311 ILE ILE A . n 
A 1 312 PRO 312 312 312 PRO PRO A . n 
A 1 313 ASP 313 313 313 ASP ASP A . n 
A 1 314 PHE 314 314 314 PHE PHE A . n 
A 1 315 GLN 315 315 315 GLN GLN A . n 
A 1 316 SER 316 316 316 SER SER A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 ALA 318 318 318 ALA ALA A . n 
A 1 319 MET 319 319 319 MET MET A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 ASN 321 321 321 ASN ASN A . n 
A 1 322 TRP 322 322 322 TRP TRP A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 THR 325 325 325 THR THR A . n 
A 1 326 THR 326 326 326 THR THR A . n 
A 1 327 TYR 327 327 327 TYR TYR A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 GLU 329 329 329 GLU GLU A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 PHE 334 334 334 PHE PHE A . n 
A 1 335 ASP 335 335 335 ASP ASP A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 LYS 338 338 338 LYS LYS A . n 
A 1 339 SER 339 339 339 SER SER A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 ALA 341 341 341 ALA ALA A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 GLY 346 346 346 GLY GLY A . n 
A 1 347 ILE 347 347 347 ILE ILE A . n 
A 1 348 THR 348 348 348 THR THR A . n 
A 1 349 MET 349 349 349 MET MET A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 ALA 352 352 352 ALA ALA A . n 
A 1 353 HIS 353 353 353 HIS HIS A . n 
A 1 354 GLU 354 354 354 GLU GLU A . n 
A 1 355 LEU 355 355 355 LEU LEU A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 HIS 357 357 357 HIS HIS A . n 
A 1 358 GLN 358 358 358 GLN GLN A . n 
A 1 359 TRP 359 359 359 TRP TRP A . n 
A 1 360 PHE 360 360 360 PHE PHE A . n 
A 1 361 GLY 361 361 361 GLY GLY A . n 
A 1 362 ASN 362 362 362 ASN ASN A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 VAL 364 364 364 VAL VAL A . n 
A 1 365 THR 365 365 365 THR THR A . n 
A 1 366 MET 366 366 366 MET MET A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 TRP 368 368 368 TRP TRP A . n 
A 1 369 TRP 369 369 369 TRP TRP A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 ASP 371 371 371 ASP ASP A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 TRP 373 373 373 TRP TRP A . n 
A 1 374 LEU 374 374 374 LEU LEU A . n 
A 1 375 ASN 375 375 375 ASN ASN A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 GLY 377 377 377 GLY GLY A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 ALA 379 379 379 ALA ALA A . n 
A 1 380 LYS 380 380 380 LYS LYS A . n 
A 1 381 PHE 381 381 381 PHE PHE A . n 
A 1 382 MET 382 382 382 MET MET A . n 
A 1 383 GLU 383 383 383 GLU GLU A . n 
A 1 384 PHE 384 384 384 PHE PHE A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 SER 386 386 386 SER SER A . n 
A 1 387 VAL 387 387 387 VAL VAL A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 VAL 389 389 389 VAL VAL A . n 
A 1 390 THR 390 390 390 THR THR A . n 
A 1 391 HIS 391 391 391 HIS HIS A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 LYS 395 395 395 LYS LYS A . n 
A 1 396 VAL 396 396 396 VAL VAL A . n 
A 1 397 GLY 397 397 397 GLY GLY A . n 
A 1 398 ASP 398 398 398 ASP ASP A . n 
A 1 399 TYR 399 399 399 TYR TYR A . n 
A 1 400 PHE 400 400 400 PHE PHE A . n 
A 1 401 PHE 401 401 401 PHE PHE A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 LYS 403 403 403 LYS LYS A . n 
A 1 404 CYS 404 404 404 CYS CYS A . n 
A 1 405 PHE 405 405 405 PHE PHE A . n 
A 1 406 ASP 406 406 406 ASP ASP A . n 
A 1 407 ALA 407 407 407 ALA ALA A . n 
A 1 408 MET 408 408 408 MET MET A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 VAL 410 410 410 VAL VAL A . n 
A 1 411 ASP 411 411 411 ASP ASP A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 LEU 413 413 413 LEU LEU A . n 
A 1 414 GLN 414 414 414 GLN GLN A . n 
A 1 415 SER 415 415 415 SER SER A . n 
A 1 416 SER 416 416 416 SER SER A . n 
A 1 417 HIS 417 417 417 HIS HIS A . n 
A 1 418 PRO 418 418 418 PRO PRO A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 SER 420 420 420 SER SER A . n 
A 1 421 THR 421 421 421 THR THR A . n 
A 1 422 PRO 422 422 422 PRO PRO A . n 
A 1 423 VAL 423 423 423 VAL VAL A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 ASN 425 425 425 ASN ASN A . n 
A 1 426 PRO 426 426 426 PRO PRO A . n 
A 1 427 ALA 427 427 427 ALA ALA A . n 
A 1 428 GLN 428 428 428 GLN GLN A . n 
A 1 429 ILE 429 429 429 ILE ILE A . n 
A 1 430 ARG 430 430 430 ARG ARG A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 MET 432 432 432 MET MET A . n 
A 1 433 PHE 433 433 433 PHE PHE A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 ASP 435 435 435 ASP ASP A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 SER 437 437 437 SER SER A . n 
A 1 438 TYR 438 438 438 TYR TYR A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 GLY 441 441 441 GLY GLY A . n 
A 1 442 ALA 442 442 442 ALA ALA A . n 
A 1 443 CYS 443 443 443 CYS CYS A . n 
A 1 444 ILE 444 444 444 ILE ILE A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 ASN 446 446 446 ASN ASN A . n 
A 1 447 MET 447 447 447 MET MET A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 ARG 449 449 449 ARG ARG A . n 
A 1 450 GLU 450 450 450 GLU GLU A . n 
A 1 451 TYR 451 451 451 TYR TYR A . n 
A 1 452 LEU 452 452 452 LEU LEU A . n 
A 1 453 SER 453 453 453 SER SER A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 ASP 455 455 455 ASP ASP A . n 
A 1 456 ALA 456 456 456 ALA ALA A . n 
A 1 457 PHE 457 457 457 PHE PHE A . n 
A 1 458 LYS 458 458 458 LYS LYS A . n 
A 1 459 SER 459 459 459 SER SER A . n 
A 1 460 GLY 460 460 460 GLY GLY A . n 
A 1 461 ILE 461 461 461 ILE ILE A . n 
A 1 462 VAL 462 462 462 VAL VAL A . n 
A 1 463 GLN 463 463 463 GLN GLN A . n 
A 1 464 TYR 464 464 464 TYR TYR A . n 
A 1 465 LEU 465 465 465 LEU LEU A . n 
A 1 466 GLN 466 466 466 GLN GLN A . n 
A 1 467 LYS 467 467 467 LYS LYS A . n 
A 1 468 HIS 468 468 468 HIS HIS A . n 
A 1 469 SER 469 469 469 SER SER A . n 
A 1 470 TYR 470 470 470 TYR TYR A . n 
A 1 471 LYS 471 471 471 LYS LYS A . n 
A 1 472 ASN 472 472 472 ASN ASN A . n 
A 1 473 THR 473 473 473 THR THR A . n 
A 1 474 LYS 474 474 474 LYS LYS A . n 
A 1 475 ASN 475 475 475 ASN ASN A . n 
A 1 476 GLU 476 476 476 GLU GLU A . n 
A 1 477 ASP 477 477 477 ASP ASP A . n 
A 1 478 LEU 478 478 478 LEU LEU A . n 
A 1 479 TRP 479 479 479 TRP TRP A . n 
A 1 480 ASP 480 480 480 ASP ASP A . n 
A 1 481 SER 481 481 481 SER SER A . n 
A 1 482 MET 482 482 482 MET MET A . n 
A 1 483 ALA 483 483 483 ALA ALA A . n 
A 1 484 SER 484 484 484 SER SER A . n 
A 1 485 ILE 485 485 485 ILE ILE A . n 
A 1 486 GLY 486 511 ?   ?   ?   A . n 
A 1 487 SER 487 512 ?   ?   ?   A . n 
A 1 488 GLY 488 513 513 GLY GLY A . n 
A 1 489 GLY 489 514 514 GLY GLY A . n 
A 1 490 VAL 490 515 515 VAL VAL A . n 
A 1 491 ASP 491 516 516 ASP ASP A . n 
A 1 492 VAL 492 517 517 VAL VAL A . n 
A 1 493 LYS 493 518 518 LYS LYS A . n 
A 1 494 THR 494 519 519 THR THR A . n 
A 1 495 MET 495 520 520 MET MET A . n 
A 1 496 MET 496 521 521 MET MET A . n 
A 1 497 ASN 497 522 522 ASN ASN A . n 
A 1 498 THR 498 523 523 THR THR A . n 
A 1 499 TRP 499 524 524 TRP TRP A . n 
A 1 500 THR 500 525 525 THR THR A . n 
A 1 501 LEU 501 526 526 LEU LEU A . n 
A 1 502 GLN 502 527 527 GLN GLN A . n 
A 1 503 ARG 503 528 528 ARG ARG A . n 
A 1 504 GLY 504 529 529 GLY GLY A . n 
A 1 505 PHE 505 530 530 PHE PHE A . n 
A 1 506 PRO 506 531 531 PRO PRO A . n 
A 1 507 LEU 507 532 532 LEU LEU A . n 
A 1 508 ILE 508 533 533 ILE ILE A . n 
A 1 509 THR 509 534 534 THR THR A . n 
A 1 510 ILE 510 535 535 ILE ILE A . n 
A 1 511 THR 511 536 536 THR THR A . n 
A 1 512 VAL 512 537 537 VAL VAL A . n 
A 1 513 ARG 513 538 538 ARG ARG A . n 
A 1 514 GLY 514 539 539 GLY GLY A . n 
A 1 515 ARG 515 540 540 ARG ARG A . n 
A 1 516 ASN 516 541 541 ASN ASN A . n 
A 1 517 VAL 517 542 542 VAL VAL A . n 
A 1 518 HIS 518 543 543 HIS HIS A . n 
A 1 519 MET 519 544 544 MET MET A . n 
A 1 520 LYS 520 545 545 LYS LYS A . n 
A 1 521 GLN 521 546 546 GLN GLN A . n 
A 1 522 GLU 522 547 547 GLU GLU A . n 
A 1 523 HIS 523 548 548 HIS HIS A . n 
A 1 524 TYR 524 549 549 TYR TYR A . n 
A 1 525 MET 525 550 550 MET MET A . n 
A 1 526 LYS 526 551 551 LYS LYS A . n 
A 1 527 GLY 527 552 552 GLY GLY A . n 
A 1 528 SER 528 553 ?   ?   ?   A . n 
A 1 529 ASP 529 554 ?   ?   ?   A . n 
A 1 530 GLY 530 555 ?   ?   ?   A . n 
A 1 531 ALA 531 556 ?   ?   ?   A . n 
A 1 532 PRO 532 557 ?   ?   ?   A . n 
A 1 533 ASP 533 558 ?   ?   ?   A . n 
A 1 534 THR 534 559 ?   ?   ?   A . n 
A 1 535 GLY 535 560 560 GLY GLY A . n 
A 1 536 TYR 536 561 561 TYR TYR A . n 
A 1 537 LEU 537 562 562 LEU LEU A . n 
A 1 538 TRP 538 563 563 TRP TRP A . n 
A 1 539 HIS 539 564 564 HIS HIS A . n 
A 1 540 VAL 540 565 565 VAL VAL A . n 
A 1 541 PRO 541 566 566 PRO PRO A . n 
A 1 542 LEU 542 567 567 LEU LEU A . n 
A 1 543 THR 543 568 568 THR THR A . n 
A 1 544 PHE 544 569 569 PHE PHE A . n 
A 1 545 ILE 545 570 570 ILE ILE A . n 
A 1 546 THR 546 571 571 THR THR A . n 
A 1 547 SER 547 572 572 SER SER A . n 
A 1 548 LYS 548 573 573 LYS LYS A . n 
A 1 549 SER 549 574 574 SER SER A . n 
A 1 550 ASP 550 575 575 ASP ASP A . n 
A 1 551 MET 551 576 576 MET MET A . n 
A 1 552 VAL 552 577 577 VAL VAL A . n 
A 1 553 HIS 553 578 578 HIS HIS A . n 
A 1 554 ARG 554 579 579 ARG ARG A . n 
A 1 555 PHE 555 580 580 PHE PHE A . n 
A 1 556 LEU 556 581 581 LEU LEU A . n 
A 1 557 LEU 557 582 582 LEU LEU A . n 
A 1 558 LYS 558 583 583 LYS LYS A . n 
A 1 559 THR 559 584 584 THR THR A . n 
A 1 560 LYS 560 585 585 LYS LYS A . n 
A 1 561 THR 561 586 586 THR THR A . n 
A 1 562 ASP 562 587 587 ASP ASP A . n 
A 1 563 VAL 563 588 588 VAL VAL A . n 
A 1 564 LEU 564 589 589 LEU LEU A . n 
A 1 565 ILE 565 590 590 ILE ILE A . n 
A 1 566 LEU 566 591 591 LEU LEU A . n 
A 1 567 PRO 567 592 592 PRO PRO A . n 
A 1 568 GLU 568 593 593 GLU GLU A . n 
A 1 569 GLU 569 594 594 GLU GLU A . n 
A 1 570 VAL 570 595 595 VAL VAL A . n 
A 1 571 GLU 571 596 596 GLU GLU A . n 
A 1 572 TRP 572 597 597 TRP TRP A . n 
A 1 573 ILE 573 598 598 ILE ILE A . n 
A 1 574 LYS 574 599 599 LYS LYS A . n 
A 1 575 PHE 575 600 600 PHE PHE A . n 
A 1 576 ASN 576 601 601 ASN ASN A . n 
A 1 577 VAL 577 602 602 VAL VAL A . n 
A 1 578 GLY 578 603 603 GLY GLY A . n 
A 1 579 MET 579 604 604 MET MET A . n 
A 1 580 ASN 580 605 605 ASN ASN A . n 
A 1 581 GLY 581 606 606 GLY GLY A . n 
A 1 582 TYR 582 607 607 TYR TYR A . n 
A 1 583 TYR 583 608 608 TYR TYR A . n 
A 1 584 ILE 584 609 609 ILE ILE A . n 
A 1 585 VAL 585 610 610 VAL VAL A . n 
A 1 586 HIS 586 611 611 HIS HIS A . n 
A 1 587 TYR 587 612 612 TYR TYR A . n 
A 1 588 GLU 588 613 613 GLU GLU A . n 
A 1 589 ASP 589 614 614 ASP ASP A . n 
A 1 590 ASP 590 615 615 ASP ASP A . n 
A 1 591 GLY 591 616 616 GLY GLY A . n 
A 1 592 TRP 592 617 617 TRP TRP A . n 
A 1 593 ASP 593 618 618 ASP ASP A . n 
A 1 594 SER 594 619 619 SER SER A . n 
A 1 595 LEU 595 620 620 LEU LEU A . n 
A 1 596 THR 596 621 621 THR THR A . n 
A 1 597 GLY 597 622 622 GLY GLY A . n 
A 1 598 LEU 598 623 623 LEU LEU A . n 
A 1 599 LEU 599 624 624 LEU LEU A . n 
A 1 600 LYS 600 625 625 LYS LYS A . n 
A 1 601 GLY 601 626 626 GLY GLY A . n 
A 1 602 THR 602 627 627 THR THR A . n 
A 1 603 HIS 603 628 628 HIS HIS A . n 
A 1 604 THR 604 629 629 THR THR A . n 
A 1 605 ALA 605 630 630 ALA ALA A . n 
A 1 606 VAL 606 631 631 VAL VAL A . n 
A 1 607 SER 607 632 632 SER SER A . n 
A 1 608 SER 608 633 633 SER SER A . n 
A 1 609 ASN 609 634 634 ASN ASN A . n 
A 1 610 ASP 610 635 635 ASP ASP A . n 
A 1 611 ARG 611 636 636 ARG ARG A . n 
A 1 612 ALA 612 637 637 ALA ALA A . n 
A 1 613 SER 613 638 638 SER SER A . n 
A 1 614 LEU 614 639 639 LEU LEU A . n 
A 1 615 ILE 615 640 640 ILE ILE A . n 
A 1 616 ASN 616 641 641 ASN ASN A . n 
A 1 617 ASN 617 642 642 ASN ASN A . n 
A 1 618 ALA 618 643 643 ALA ALA A . n 
A 1 619 PHE 619 644 644 PHE PHE A . n 
A 1 620 GLN 620 645 645 GLN GLN A . n 
A 1 621 LEU 621 646 646 LEU LEU A . n 
A 1 622 VAL 622 647 647 VAL VAL A . n 
A 1 623 SER 623 648 648 SER SER A . n 
A 1 624 ILE 624 649 649 ILE ILE A . n 
A 1 625 GLY 625 650 650 GLY GLY A . n 
A 1 626 LYS 626 651 651 LYS LYS A . n 
A 1 627 LEU 627 652 652 LEU LEU A . n 
A 1 628 SER 628 653 653 SER SER A . n 
A 1 629 ILE 629 654 654 ILE ILE A . n 
A 1 630 GLU 630 655 655 GLU GLU A . n 
A 1 631 LYS 631 656 656 LYS LYS A . n 
A 1 632 ALA 632 657 657 ALA ALA A . n 
A 1 633 LEU 633 658 658 LEU LEU A . n 
A 1 634 ASP 634 659 659 ASP ASP A . n 
A 1 635 LEU 635 660 660 LEU LEU A . n 
A 1 636 SER 636 661 661 SER SER A . n 
A 1 637 LEU 637 662 662 LEU LEU A . n 
A 1 638 TYR 638 663 663 TYR TYR A . n 
A 1 639 LEU 639 664 664 LEU LEU A . n 
A 1 640 LYS 640 665 665 LYS LYS A . n 
A 1 641 HIS 641 666 666 HIS HIS A . n 
A 1 642 GLU 642 667 667 GLU GLU A . n 
A 1 643 THR 643 668 668 THR THR A . n 
A 1 644 GLU 644 669 669 GLU GLU A . n 
A 1 645 ILE 645 670 670 ILE ILE A . n 
A 1 646 MET 646 671 671 MET MET A . n 
A 1 647 PRO 647 672 672 PRO PRO A . n 
A 1 648 VAL 648 673 673 VAL VAL A . n 
A 1 649 PHE 649 674 674 PHE PHE A . n 
A 1 650 GLN 650 675 675 GLN GLN A . n 
A 1 651 GLY 651 676 676 GLY GLY A . n 
A 1 652 LEU 652 677 677 LEU LEU A . n 
A 1 653 ASN 653 678 678 ASN ASN A . n 
A 1 654 GLU 654 679 679 GLU GLU A . n 
A 1 655 LEU 655 680 680 LEU LEU A . n 
A 1 656 ILE 656 681 681 ILE ILE A . n 
A 1 657 PRO 657 682 682 PRO PRO A . n 
A 1 658 MET 658 683 683 MET MET A . n 
A 1 659 TYR 659 684 684 TYR TYR A . n 
A 1 660 LYS 660 685 685 LYS LYS A . n 
A 1 661 LEU 661 686 686 LEU LEU A . n 
A 1 662 MET 662 687 687 MET MET A . n 
A 1 663 GLU 663 688 688 GLU GLU A . n 
A 1 664 LYS 664 689 689 LYS LYS A . n 
A 1 665 ARG 665 690 690 ARG ARG A . n 
A 1 666 ASP 666 691 691 ASP ASP A . n 
A 1 667 MET 667 692 692 MET MET A . n 
A 1 668 ASN 668 693 693 ASN ASN A . n 
A 1 669 GLU 669 694 694 GLU GLU A . n 
A 1 670 VAL 670 695 695 VAL VAL A . n 
A 1 671 GLU 671 696 696 GLU GLU A . n 
A 1 672 THR 672 697 697 THR THR A . n 
A 1 673 GLN 673 698 698 GLN GLN A . n 
A 1 674 PHE 674 699 699 PHE PHE A . n 
A 1 675 LYS 675 700 700 LYS LYS A . n 
A 1 676 ALA 676 701 701 ALA ALA A . n 
A 1 677 PHE 677 702 702 PHE PHE A . n 
A 1 678 LEU 678 703 703 LEU LEU A . n 
A 1 679 ILE 679 704 704 ILE ILE A . n 
A 1 680 ARG 680 705 705 ARG ARG A . n 
A 1 681 LEU 681 706 706 LEU LEU A . n 
A 1 682 LEU 682 707 707 LEU LEU A . n 
A 1 683 ARG 683 708 708 ARG ARG A . n 
A 1 684 ASP 684 709 709 ASP ASP A . n 
A 1 685 LEU 685 710 710 LEU LEU A . n 
A 1 686 ILE 686 711 711 ILE ILE A . n 
A 1 687 ASP 687 712 712 ASP ASP A . n 
A 1 688 LYS 688 713 713 LYS LYS A . n 
A 1 689 GLN 689 714 714 GLN GLN A . n 
A 1 690 THR 690 715 715 THR THR A . n 
A 1 691 TRP 691 716 716 TRP TRP A . n 
A 1 692 THR 692 717 717 THR THR A . n 
A 1 693 ASP 693 718 718 ASP ASP A . n 
A 1 694 GLU 694 719 719 GLU GLU A . n 
A 1 695 GLY 695 720 720 GLY GLY A . n 
A 1 696 SER 696 721 721 SER SER A . n 
A 1 697 VAL 697 722 722 VAL VAL A . n 
A 1 698 SER 698 723 723 SER SER A . n 
A 1 699 GLU 699 724 724 GLU GLU A . n 
A 1 700 ARG 700 725 725 ARG ARG A . n 
A 1 701 MET 701 726 726 MET MET A . n 
A 1 702 LEU 702 727 727 LEU LEU A . n 
A 1 703 ARG 703 728 728 ARG ARG A . n 
A 1 704 SER 704 729 729 SER SER A . n 
A 1 705 GLN 705 730 730 GLN GLN A . n 
A 1 706 LEU 706 731 731 LEU LEU A . n 
A 1 707 LEU 707 732 732 LEU LEU A . n 
A 1 708 LEU 708 733 733 LEU LEU A . n 
A 1 709 LEU 709 734 734 LEU LEU A . n 
A 1 710 ALA 710 735 735 ALA ALA A . n 
A 1 711 CYS 711 736 736 CYS CYS A . n 
A 1 712 VAL 712 737 737 VAL VAL A . n 
A 1 713 HIS 713 738 738 HIS HIS A . n 
A 1 714 ASN 714 739 739 ASN ASN A . n 
A 1 715 TYR 715 740 740 TYR TYR A . n 
A 1 716 GLN 716 741 741 GLN GLN A . n 
A 1 717 PRO 717 742 742 PRO PRO A . n 
A 1 718 CYS 718 743 743 CYS CYS A . n 
A 1 719 VAL 719 744 744 VAL VAL A . n 
A 1 720 GLN 720 745 745 GLN GLN A . n 
A 1 721 ARG 721 746 746 ARG ARG A . n 
A 1 722 ALA 722 747 747 ALA ALA A . n 
A 1 723 GLU 723 748 748 GLU GLU A . n 
A 1 724 GLY 724 749 749 GLY GLY A . n 
A 1 725 TYR 725 750 750 TYR TYR A . n 
A 1 726 PHE 726 751 751 PHE PHE A . n 
A 1 727 ARG 727 752 752 ARG ARG A . n 
A 1 728 LYS 728 753 753 LYS LYS A . n 
A 1 729 TRP 729 754 754 TRP TRP A . n 
A 1 730 LYS 730 755 755 LYS LYS A . n 
A 1 731 GLU 731 756 756 GLU GLU A . n 
A 1 732 SER 732 757 757 SER SER A . n 
A 1 733 ASN 733 758 758 ASN ASN A . n 
A 1 734 GLY 734 759 759 GLY GLY A . n 
A 1 735 GLN 735 760 760 GLN GLN A . n 
A 1 736 LEU 736 761 761 LEU LEU A . n 
A 1 737 SER 737 762 762 SER SER A . n 
A 1 738 LEU 738 763 763 LEU LEU A . n 
A 1 739 PRO 739 764 764 PRO PRO A . n 
A 1 740 VAL 740 765 765 VAL VAL A . n 
A 1 741 ASP 741 766 766 ASP ASP A . n 
A 1 742 VAL 742 767 767 VAL VAL A . n 
A 1 743 THR 743 768 768 THR THR A . n 
A 1 744 LEU 744 769 769 LEU LEU A . n 
A 1 745 ALA 745 770 770 ALA ALA A . n 
A 1 746 VAL 746 771 771 VAL VAL A . n 
A 1 747 PHE 747 772 772 PHE PHE A . n 
A 1 748 ALA 748 773 773 ALA ALA A . n 
A 1 749 VAL 749 774 774 VAL VAL A . n 
A 1 750 GLY 750 775 775 GLY GLY A . n 
A 1 751 ALA 751 776 776 ALA ALA A . n 
A 1 752 GLN 752 777 777 GLN GLN A . n 
A 1 753 SER 753 778 778 SER SER A . n 
A 1 754 THR 754 779 779 THR THR A . n 
A 1 755 GLU 755 780 780 GLU GLU A . n 
A 1 756 GLY 756 781 781 GLY GLY A . n 
A 1 757 TRP 757 782 782 TRP TRP A . n 
A 1 758 ASP 758 783 783 ASP ASP A . n 
A 1 759 PHE 759 784 784 PHE PHE A . n 
A 1 760 LEU 760 785 785 LEU LEU A . n 
A 1 761 TYR 761 786 786 TYR TYR A . n 
A 1 762 SER 762 787 787 SER SER A . n 
A 1 763 LYS 763 788 788 LYS LYS A . n 
A 1 764 TYR 764 789 789 TYR TYR A . n 
A 1 765 GLN 765 790 790 GLN GLN A . n 
A 1 766 PHE 766 791 791 PHE PHE A . n 
A 1 767 SER 767 792 792 SER SER A . n 
A 1 768 LEU 768 793 793 LEU LEU A . n 
A 1 769 SER 769 794 794 SER SER A . n 
A 1 770 SER 770 795 795 SER SER A . n 
A 1 771 THR 771 796 796 THR THR A . n 
A 1 772 GLU 772 797 797 GLU GLU A . n 
A 1 773 LYS 773 798 798 LYS LYS A . n 
A 1 774 SER 774 799 799 SER SER A . n 
A 1 775 GLN 775 800 800 GLN GLN A . n 
A 1 776 ILE 776 801 801 ILE ILE A . n 
A 1 777 GLU 777 802 802 GLU GLU A . n 
A 1 778 PHE 778 803 803 PHE PHE A . n 
A 1 779 ALA 779 804 804 ALA ALA A . n 
A 1 780 LEU 780 805 805 LEU LEU A . n 
A 1 781 CYS 781 806 806 CYS CYS A . n 
A 1 782 ARG 782 807 807 ARG ARG A . n 
A 1 783 THR 783 808 808 THR THR A . n 
A 1 784 GLN 784 809 809 GLN GLN A . n 
A 1 785 ASN 785 810 810 ASN ASN A . n 
A 1 786 LYS 786 811 811 LYS LYS A . n 
A 1 787 GLU 787 812 812 GLU GLU A . n 
A 1 788 LYS 788 813 813 LYS LYS A . n 
A 1 789 LEU 789 814 814 LEU LEU A . n 
A 1 790 GLN 790 815 815 GLN GLN A . n 
A 1 791 TRP 791 816 816 TRP TRP A . n 
A 1 792 LEU 792 817 817 LEU LEU A . n 
A 1 793 LEU 793 818 818 LEU LEU A . n 
A 1 794 ASP 794 819 819 ASP ASP A . n 
A 1 795 GLU 795 820 820 GLU GLU A . n 
A 1 796 SER 796 821 821 SER SER A . n 
A 1 797 PHE 797 822 822 PHE PHE A . n 
A 1 798 LYS 798 823 823 LYS LYS A . n 
A 1 799 GLY 799 824 824 GLY GLY A . n 
A 1 800 ASP 800 825 825 ASP ASP A . n 
A 1 801 LYS 801 826 826 LYS LYS A . n 
A 1 802 ILE 802 827 827 ILE ILE A . n 
A 1 803 LYS 803 828 828 LYS LYS A . n 
A 1 804 THR 804 829 829 THR THR A . n 
A 1 805 GLN 805 830 830 GLN GLN A . n 
A 1 806 GLU 806 831 831 GLU GLU A . n 
A 1 807 PHE 807 832 832 PHE PHE A . n 
A 1 808 PRO 808 833 833 PRO PRO A . n 
A 1 809 GLN 809 834 834 GLN GLN A . n 
A 1 810 ILE 810 835 835 ILE ILE A . n 
A 1 811 LEU 811 836 836 LEU LEU A . n 
A 1 812 THR 812 837 837 THR THR A . n 
A 1 813 LEU 813 838 838 LEU LEU A . n 
A 1 814 ILE 814 839 839 ILE ILE A . n 
A 1 815 GLY 815 840 840 GLY GLY A . n 
A 1 816 ARG 816 841 841 ARG ARG A . n 
A 1 817 ASN 817 842 842 ASN ASN A . n 
A 1 818 PRO 818 843 843 PRO PRO A . n 
A 1 819 VAL 819 844 844 VAL VAL A . n 
A 1 820 GLY 820 845 845 GLY GLY A . n 
A 1 821 TYR 821 846 846 TYR TYR A . n 
A 1 822 PRO 822 847 847 PRO PRO A . n 
A 1 823 LEU 823 848 848 LEU LEU A . n 
A 1 824 ALA 824 849 849 ALA ALA A . n 
A 1 825 TRP 825 850 850 TRP TRP A . n 
A 1 826 GLN 826 851 851 GLN GLN A . n 
A 1 827 PHE 827 852 852 PHE PHE A . n 
A 1 828 LEU 828 853 853 LEU LEU A . n 
A 1 829 ARG 829 854 854 ARG ARG A . n 
A 1 830 LYS 830 855 855 LYS LYS A . n 
A 1 831 ASN 831 856 856 ASN ASN A . n 
A 1 832 TRP 832 857 857 TRP TRP A . n 
A 1 833 ASN 833 858 858 ASN ASN A . n 
A 1 834 LYS 834 859 859 LYS LYS A . n 
A 1 835 LEU 835 860 860 LEU LEU A . n 
A 1 836 VAL 836 861 861 VAL VAL A . n 
A 1 837 GLN 837 862 862 GLN GLN A . n 
A 1 838 LYS 838 863 863 LYS LYS A . n 
A 1 839 PHE 839 864 864 PHE PHE A . n 
A 1 840 GLU 840 865 865 GLU GLU A . n 
A 1 841 LEU 841 866 866 LEU LEU A . n 
A 1 842 GLY 842 867 867 GLY GLY A . n 
A 1 843 SER 843 868 868 SER SER A . n 
A 1 844 SER 844 869 869 SER SER A . n 
A 1 845 SER 845 870 870 SER SER A . n 
A 1 846 ILE 846 871 871 ILE ILE A . n 
A 1 847 ALA 847 872 872 ALA ALA A . n 
A 1 848 HIS 848 873 873 HIS HIS A . n 
A 1 849 MET 849 874 874 MET MET A . n 
A 1 850 VAL 850 875 875 VAL VAL A . n 
A 1 851 MET 851 876 876 MET MET A . n 
A 1 852 GLY 852 877 877 GLY GLY A . n 
A 1 853 THR 853 878 878 THR THR A . n 
A 1 854 THR 854 879 879 THR THR A . n 
A 1 855 ASN 855 880 880 ASN ASN A . n 
A 1 856 GLN 856 881 881 GLN GLN A . n 
A 1 857 PHE 857 882 882 PHE PHE A . n 
A 1 858 SER 858 883 883 SER SER A . n 
A 1 859 THR 859 884 884 THR THR A . n 
A 1 860 ARG 860 885 885 ARG ARG A . n 
A 1 861 THR 861 886 886 THR THR A . n 
A 1 862 ARG 862 887 887 ARG ARG A . n 
A 1 863 LEU 863 888 888 LEU LEU A . n 
A 1 864 GLU 864 889 889 GLU GLU A . n 
A 1 865 GLU 865 890 890 GLU GLU A . n 
A 1 866 VAL 866 891 891 VAL VAL A . n 
A 1 867 LYS 867 892 892 LYS LYS A . n 
A 1 868 GLY 868 893 893 GLY GLY A . n 
A 1 869 PHE 869 894 894 PHE PHE A . n 
A 1 870 PHE 870 895 895 PHE PHE A . n 
A 1 871 SER 871 896 896 SER SER A . n 
A 1 872 SER 872 897 897 SER SER A . n 
A 1 873 LEU 873 898 898 LEU LEU A . n 
A 1 874 LYS 874 899 899 LYS LYS A . n 
A 1 875 GLU 875 900 900 GLU GLU A . n 
A 1 876 ASN 876 901 901 ASN ASN A . n 
A 1 877 GLY 877 902 902 GLY GLY A . n 
A 1 878 SER 878 903 903 SER SER A . n 
A 1 879 GLN 879 904 904 GLN GLN A . n 
A 1 880 LEU 880 905 905 LEU LEU A . n 
A 1 881 ARG 881 906 906 ARG ARG A . n 
A 1 882 CYS 882 907 907 CYS CYS A . n 
A 1 883 VAL 883 908 908 VAL VAL A . n 
A 1 884 GLN 884 909 909 GLN GLN A . n 
A 1 885 GLN 885 910 910 GLN GLN A . n 
A 1 886 THR 886 911 911 THR THR A . n 
A 1 887 ILE 887 912 912 ILE ILE A . n 
A 1 888 GLU 888 913 913 GLU GLU A . n 
A 1 889 THR 889 914 914 THR THR A . n 
A 1 890 ILE 890 915 915 ILE ILE A . n 
A 1 891 GLU 891 916 916 GLU GLU A . n 
A 1 892 GLU 892 917 917 GLU GLU A . n 
A 1 893 ASN 893 918 918 ASN ASN A . n 
A 1 894 ILE 894 919 919 ILE ILE A . n 
A 1 895 GLY 895 920 920 GLY GLY A . n 
A 1 896 TRP 896 921 921 TRP TRP A . n 
A 1 897 MET 897 922 922 MET MET A . n 
A 1 898 ASP 898 923 923 ASP ASP A . n 
A 1 899 LYS 899 924 924 LYS LYS A . n 
A 1 900 ASN 900 925 925 ASN ASN A . n 
A 1 901 PHE 901 926 926 PHE PHE A . n 
A 1 902 ASP 902 927 927 ASP ASP A . n 
A 1 903 LYS 903 928 928 LYS LYS A . n 
A 1 904 ILE 904 929 929 ILE ILE A . n 
A 1 905 ARG 905 930 930 ARG ARG A . n 
A 1 906 VAL 906 931 931 VAL VAL A . n 
A 1 907 TRP 907 932 932 TRP TRP A . n 
A 1 908 LEU 908 933 933 LEU LEU A . n 
A 1 909 GLN 909 934 934 GLN GLN A . n 
A 1 910 SER 910 935 935 SER SER A . n 
A 1 911 GLU 911 936 ?   ?   ?   A . n 
A 1 912 LYS 912 937 ?   ?   ?   A . n 
A 1 913 LEU 913 938 ?   ?   ?   A . n 
A 1 914 GLU 914 939 ?   ?   ?   A . n 
A 1 915 ARG 915 940 ?   ?   ?   A . n 
A 1 916 MET 916 941 ?   ?   ?   A . n 
A 1 917 GLU 917 942 ?   ?   ?   A . n 
A 1 918 ASN 918 943 ?   ?   ?   A . n 
A 1 919 LEU 919 944 ?   ?   ?   A . n 
A 1 920 TYR 920 945 ?   ?   ?   A . n 
A 1 921 PHE 921 946 ?   ?   ?   A . n 
A 1 922 GLN 922 947 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IMM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IMM 
_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 ZN    1    1001 2000 ZN    ZN  A . 
C 3 MLT   1    1002 3000 MLT   MLT A . 
D 3 MLT   1    1003 3001 MLT   MLT A . 
E 4 EDO   1    1004 3500 EDO   EDO A . 
F 4 EDO   1    1005 3501 EDO   EDO A . 
G 4 EDO   1    1006 3502 EDO   EDO A . 
H 4 EDO   1    1007 3503 EDO   EDO A . 
I 4 EDO   1    1008 3504 EDO   EDO A . 
J 4 EDO   1    1009 3505 EDO   EDO A . 
K 4 EDO   1    1010 3506 EDO   EDO A . 
L 4 EDO   1    1011 3507 EDO   EDO A . 
M 4 EDO   1    1012 3508 EDO   EDO A . 
N 4 EDO   1    1013 3509 EDO   EDO A . 
O 4 EDO   1    1014 3510 EDO   EDO A . 
P 4 EDO   1    1015 3511 EDO   EDO A . 
Q 4 EDO   1    1016 3512 EDO   EDO A . 
R 4 EDO   1    1017 3513 EDO   EDO A . 
S 4 EDO   1    1018 3514 EDO   EDO A . 
T 4 EDO   1    1019 3515 EDO   EDO A . 
U 5 A1IMM 1    1020 4000 A1IMM LIG A . 
V 6 HOH   1    1101 886  HOH   HOH A . 
V 6 HOH   2    1102 1207 HOH   HOH A . 
V 6 HOH   3    1103 617  HOH   HOH A . 
V 6 HOH   4    1104 932  HOH   HOH A . 
V 6 HOH   5    1105 444  HOH   HOH A . 
V 6 HOH   6    1106 878  HOH   HOH A . 
V 6 HOH   7    1107 871  HOH   HOH A . 
V 6 HOH   8    1108 870  HOH   HOH A . 
V 6 HOH   9    1109 1055 HOH   HOH A . 
V 6 HOH   10   1110 588  HOH   HOH A . 
V 6 HOH   11   1111 266  HOH   HOH A . 
V 6 HOH   12   1112 789  HOH   HOH A . 
V 6 HOH   13   1113 939  HOH   HOH A . 
V 6 HOH   14   1114 1229 HOH   HOH A . 
V 6 HOH   15   1115 1179 HOH   HOH A . 
V 6 HOH   16   1116 587  HOH   HOH A . 
V 6 HOH   17   1117 1097 HOH   HOH A . 
V 6 HOH   18   1118 1026 HOH   HOH A . 
V 6 HOH   19   1119 897  HOH   HOH A . 
V 6 HOH   20   1120 156  HOH   HOH A . 
V 6 HOH   21   1121 250  HOH   HOH A . 
V 6 HOH   22   1122 86   HOH   HOH A . 
V 6 HOH   23   1123 716  HOH   HOH A . 
V 6 HOH   24   1124 1193 HOH   HOH A . 
V 6 HOH   25   1125 916  HOH   HOH A . 
V 6 HOH   26   1126 552  HOH   HOH A . 
V 6 HOH   27   1127 456  HOH   HOH A . 
V 6 HOH   28   1128 866  HOH   HOH A . 
V 6 HOH   29   1129 20   HOH   HOH A . 
V 6 HOH   30   1130 971  HOH   HOH A . 
V 6 HOH   31   1131 247  HOH   HOH A . 
V 6 HOH   32   1132 463  HOH   HOH A . 
V 6 HOH   33   1133 435  HOH   HOH A . 
V 6 HOH   34   1134 860  HOH   HOH A . 
V 6 HOH   35   1135 1204 HOH   HOH A . 
V 6 HOH   36   1136 414  HOH   HOH A . 
V 6 HOH   37   1137 34   HOH   HOH A . 
V 6 HOH   38   1138 375  HOH   HOH A . 
V 6 HOH   39   1139 867  HOH   HOH A . 
V 6 HOH   40   1140 697  HOH   HOH A . 
V 6 HOH   41   1141 963  HOH   HOH A . 
V 6 HOH   42   1142 606  HOH   HOH A . 
V 6 HOH   43   1143 126  HOH   HOH A . 
V 6 HOH   44   1144 709  HOH   HOH A . 
V 6 HOH   45   1145 965  HOH   HOH A . 
V 6 HOH   46   1146 489  HOH   HOH A . 
V 6 HOH   47   1147 370  HOH   HOH A . 
V 6 HOH   48   1148 268  HOH   HOH A . 
V 6 HOH   49   1149 338  HOH   HOH A . 
V 6 HOH   50   1150 515  HOH   HOH A . 
V 6 HOH   51   1151 217  HOH   HOH A . 
V 6 HOH   52   1152 8    HOH   HOH A . 
V 6 HOH   53   1153 471  HOH   HOH A . 
V 6 HOH   54   1154 896  HOH   HOH A . 
V 6 HOH   55   1155 568  HOH   HOH A . 
V 6 HOH   56   1156 613  HOH   HOH A . 
V 6 HOH   57   1157 645  HOH   HOH A . 
V 6 HOH   58   1158 1211 HOH   HOH A . 
V 6 HOH   59   1159 254  HOH   HOH A . 
V 6 HOH   60   1160 67   HOH   HOH A . 
V 6 HOH   61   1161 438  HOH   HOH A . 
V 6 HOH   62   1162 291  HOH   HOH A . 
V 6 HOH   63   1163 815  HOH   HOH A . 
V 6 HOH   64   1164 500  HOH   HOH A . 
V 6 HOH   65   1165 885  HOH   HOH A . 
V 6 HOH   66   1166 439  HOH   HOH A . 
V 6 HOH   67   1167 169  HOH   HOH A . 
V 6 HOH   68   1168 590  HOH   HOH A . 
V 6 HOH   69   1169 1201 HOH   HOH A . 
V 6 HOH   70   1170 1217 HOH   HOH A . 
V 6 HOH   71   1171 929  HOH   HOH A . 
V 6 HOH   72   1172 880  HOH   HOH A . 
V 6 HOH   73   1173 953  HOH   HOH A . 
V 6 HOH   74   1174 605  HOH   HOH A . 
V 6 HOH   75   1175 791  HOH   HOH A . 
V 6 HOH   76   1176 849  HOH   HOH A . 
V 6 HOH   77   1177 889  HOH   HOH A . 
V 6 HOH   78   1178 12   HOH   HOH A . 
V 6 HOH   79   1179 503  HOH   HOH A . 
V 6 HOH   80   1180 136  HOH   HOH A . 
V 6 HOH   81   1181 1104 HOH   HOH A . 
V 6 HOH   82   1182 373  HOH   HOH A . 
V 6 HOH   83   1183 423  HOH   HOH A . 
V 6 HOH   84   1184 346  HOH   HOH A . 
V 6 HOH   85   1185 193  HOH   HOH A . 
V 6 HOH   86   1186 38   HOH   HOH A . 
V 6 HOH   87   1187 243  HOH   HOH A . 
V 6 HOH   88   1188 937  HOH   HOH A . 
V 6 HOH   89   1189 813  HOH   HOH A . 
V 6 HOH   90   1190 1053 HOH   HOH A . 
V 6 HOH   91   1191 431  HOH   HOH A . 
V 6 HOH   92   1192 924  HOH   HOH A . 
V 6 HOH   93   1193 1212 HOH   HOH A . 
V 6 HOH   94   1194 756  HOH   HOH A . 
V 6 HOH   95   1195 874  HOH   HOH A . 
V 6 HOH   96   1196 486  HOH   HOH A . 
V 6 HOH   97   1197 97   HOH   HOH A . 
V 6 HOH   98   1198 233  HOH   HOH A . 
V 6 HOH   99   1199 907  HOH   HOH A . 
V 6 HOH   100  1200 228  HOH   HOH A . 
V 6 HOH   101  1201 143  HOH   HOH A . 
V 6 HOH   102  1202 484  HOH   HOH A . 
V 6 HOH   103  1203 167  HOH   HOH A . 
V 6 HOH   104  1204 1069 HOH   HOH A . 
V 6 HOH   105  1205 549  HOH   HOH A . 
V 6 HOH   106  1206 199  HOH   HOH A . 
V 6 HOH   107  1207 530  HOH   HOH A . 
V 6 HOH   108  1208 369  HOH   HOH A . 
V 6 HOH   109  1209 523  HOH   HOH A . 
V 6 HOH   110  1210 1077 HOH   HOH A . 
V 6 HOH   111  1211 334  HOH   HOH A . 
V 6 HOH   112  1212 58   HOH   HOH A . 
V 6 HOH   113  1213 572  HOH   HOH A . 
V 6 HOH   114  1214 837  HOH   HOH A . 
V 6 HOH   115  1215 900  HOH   HOH A . 
V 6 HOH   116  1216 790  HOH   HOH A . 
V 6 HOH   117  1217 290  HOH   HOH A . 
V 6 HOH   118  1218 165  HOH   HOH A . 
V 6 HOH   119  1219 1008 HOH   HOH A . 
V 6 HOH   120  1220 731  HOH   HOH A . 
V 6 HOH   121  1221 421  HOH   HOH A . 
V 6 HOH   122  1222 70   HOH   HOH A . 
V 6 HOH   123  1223 492  HOH   HOH A . 
V 6 HOH   124  1224 192  HOH   HOH A . 
V 6 HOH   125  1225 304  HOH   HOH A . 
V 6 HOH   126  1226 1036 HOH   HOH A . 
V 6 HOH   127  1227 1142 HOH   HOH A . 
V 6 HOH   128  1228 467  HOH   HOH A . 
V 6 HOH   129  1229 1062 HOH   HOH A . 
V 6 HOH   130  1230 223  HOH   HOH A . 
V 6 HOH   131  1231 497  HOH   HOH A . 
V 6 HOH   132  1232 39   HOH   HOH A . 
V 6 HOH   133  1233 822  HOH   HOH A . 
V 6 HOH   134  1234 6    HOH   HOH A . 
V 6 HOH   135  1235 884  HOH   HOH A . 
V 6 HOH   136  1236 774  HOH   HOH A . 
V 6 HOH   137  1237 1087 HOH   HOH A . 
V 6 HOH   138  1238 1215 HOH   HOH A . 
V 6 HOH   139  1239 25   HOH   HOH A . 
V 6 HOH   140  1240 88   HOH   HOH A . 
V 6 HOH   141  1241 1054 HOH   HOH A . 
V 6 HOH   142  1242 368  HOH   HOH A . 
V 6 HOH   143  1243 599  HOH   HOH A . 
V 6 HOH   144  1244 1192 HOH   HOH A . 
V 6 HOH   145  1245 546  HOH   HOH A . 
V 6 HOH   146  1246 558  HOH   HOH A . 
V 6 HOH   147  1247 195  HOH   HOH A . 
V 6 HOH   148  1248 17   HOH   HOH A . 
V 6 HOH   149  1249 62   HOH   HOH A . 
V 6 HOH   150  1250 178  HOH   HOH A . 
V 6 HOH   151  1251 457  HOH   HOH A . 
V 6 HOH   152  1252 468  HOH   HOH A . 
V 6 HOH   153  1253 44   HOH   HOH A . 
V 6 HOH   154  1254 208  HOH   HOH A . 
V 6 HOH   155  1255 505  HOH   HOH A . 
V 6 HOH   156  1256 11   HOH   HOH A . 
V 6 HOH   157  1257 551  HOH   HOH A . 
V 6 HOH   158  1258 30   HOH   HOH A . 
V 6 HOH   159  1259 288  HOH   HOH A . 
V 6 HOH   160  1260 1134 HOH   HOH A . 
V 6 HOH   161  1261 1160 HOH   HOH A . 
V 6 HOH   162  1262 168  HOH   HOH A . 
V 6 HOH   163  1263 84   HOH   HOH A . 
V 6 HOH   164  1264 212  HOH   HOH A . 
V 6 HOH   165  1265 206  HOH   HOH A . 
V 6 HOH   166  1266 1017 HOH   HOH A . 
V 6 HOH   167  1267 218  HOH   HOH A . 
V 6 HOH   168  1268 377  HOH   HOH A . 
V 6 HOH   169  1269 903  HOH   HOH A . 
V 6 HOH   170  1270 487  HOH   HOH A . 
V 6 HOH   171  1271 553  HOH   HOH A . 
V 6 HOH   172  1272 91   HOH   HOH A . 
V 6 HOH   173  1273 350  HOH   HOH A . 
V 6 HOH   174  1274 851  HOH   HOH A . 
V 6 HOH   175  1275 219  HOH   HOH A . 
V 6 HOH   176  1276 3    HOH   HOH A . 
V 6 HOH   177  1277 658  HOH   HOH A . 
V 6 HOH   178  1278 672  HOH   HOH A . 
V 6 HOH   179  1279 767  HOH   HOH A . 
V 6 HOH   180  1280 1103 HOH   HOH A . 
V 6 HOH   181  1281 54   HOH   HOH A . 
V 6 HOH   182  1282 1151 HOH   HOH A . 
V 6 HOH   183  1283 36   HOH   HOH A . 
V 6 HOH   184  1284 55   HOH   HOH A . 
V 6 HOH   185  1285 883  HOH   HOH A . 
V 6 HOH   186  1286 583  HOH   HOH A . 
V 6 HOH   187  1287 519  HOH   HOH A . 
V 6 HOH   188  1288 60   HOH   HOH A . 
V 6 HOH   189  1289 1226 HOH   HOH A . 
V 6 HOH   190  1290 65   HOH   HOH A . 
V 6 HOH   191  1291 793  HOH   HOH A . 
V 6 HOH   192  1292 201  HOH   HOH A . 
V 6 HOH   193  1293 524  HOH   HOH A . 
V 6 HOH   194  1294 407  HOH   HOH A . 
V 6 HOH   195  1295 251  HOH   HOH A . 
V 6 HOH   196  1296 451  HOH   HOH A . 
V 6 HOH   197  1297 310  HOH   HOH A . 
V 6 HOH   198  1298 677  HOH   HOH A . 
V 6 HOH   199  1299 48   HOH   HOH A . 
V 6 HOH   200  1300 607  HOH   HOH A . 
V 6 HOH   201  1301 211  HOH   HOH A . 
V 6 HOH   202  1302 719  HOH   HOH A . 
V 6 HOH   203  1303 1094 HOH   HOH A . 
V 6 HOH   204  1304 316  HOH   HOH A . 
V 6 HOH   205  1305 1213 HOH   HOH A . 
V 6 HOH   206  1306 213  HOH   HOH A . 
V 6 HOH   207  1307 63   HOH   HOH A . 
V 6 HOH   208  1308 321  HOH   HOH A . 
V 6 HOH   209  1309 183  HOH   HOH A . 
V 6 HOH   210  1310 575  HOH   HOH A . 
V 6 HOH   211  1311 320  HOH   HOH A . 
V 6 HOH   212  1312 177  HOH   HOH A . 
V 6 HOH   213  1313 5    HOH   HOH A . 
V 6 HOH   214  1314 649  HOH   HOH A . 
V 6 HOH   215  1315 1105 HOH   HOH A . 
V 6 HOH   216  1316 847  HOH   HOH A . 
V 6 HOH   217  1317 510  HOH   HOH A . 
V 6 HOH   218  1318 449  HOH   HOH A . 
V 6 HOH   219  1319 873  HOH   HOH A . 
V 6 HOH   220  1320 322  HOH   HOH A . 
V 6 HOH   221  1321 1219 HOH   HOH A . 
V 6 HOH   222  1322 245  HOH   HOH A . 
V 6 HOH   223  1323 2    HOH   HOH A . 
V 6 HOH   224  1324 859  HOH   HOH A . 
V 6 HOH   225  1325 1191 HOH   HOH A . 
V 6 HOH   226  1326 273  HOH   HOH A . 
V 6 HOH   227  1327 80   HOH   HOH A . 
V 6 HOH   228  1328 1052 HOH   HOH A . 
V 6 HOH   229  1329 205  HOH   HOH A . 
V 6 HOH   230  1330 1111 HOH   HOH A . 
V 6 HOH   231  1331 1129 HOH   HOH A . 
V 6 HOH   232  1332 191  HOH   HOH A . 
V 6 HOH   233  1333 18   HOH   HOH A . 
V 6 HOH   234  1334 1019 HOH   HOH A . 
V 6 HOH   235  1335 696  HOH   HOH A . 
V 6 HOH   236  1336 912  HOH   HOH A . 
V 6 HOH   237  1337 162  HOH   HOH A . 
V 6 HOH   238  1338 43   HOH   HOH A . 
V 6 HOH   239  1339 982  HOH   HOH A . 
V 6 HOH   240  1340 15   HOH   HOH A . 
V 6 HOH   241  1341 413  HOH   HOH A . 
V 6 HOH   242  1342 249  HOH   HOH A . 
V 6 HOH   243  1343 85   HOH   HOH A . 
V 6 HOH   244  1344 313  HOH   HOH A . 
V 6 HOH   245  1345 1146 HOH   HOH A . 
V 6 HOH   246  1346 522  HOH   HOH A . 
V 6 HOH   247  1347 93   HOH   HOH A . 
V 6 HOH   248  1348 857  HOH   HOH A . 
V 6 HOH   249  1349 526  HOH   HOH A . 
V 6 HOH   250  1350 891  HOH   HOH A . 
V 6 HOH   251  1351 687  HOH   HOH A . 
V 6 HOH   252  1352 198  HOH   HOH A . 
V 6 HOH   253  1353 283  HOH   HOH A . 
V 6 HOH   254  1354 113  HOH   HOH A . 
V 6 HOH   255  1355 286  HOH   HOH A . 
V 6 HOH   256  1356 779  HOH   HOH A . 
V 6 HOH   257  1357 285  HOH   HOH A . 
V 6 HOH   258  1358 275  HOH   HOH A . 
V 6 HOH   259  1359 72   HOH   HOH A . 
V 6 HOH   260  1360 363  HOH   HOH A . 
V 6 HOH   261  1361 682  HOH   HOH A . 
V 6 HOH   262  1362 447  HOH   HOH A . 
V 6 HOH   263  1363 214  HOH   HOH A . 
V 6 HOH   264  1364 385  HOH   HOH A . 
V 6 HOH   265  1365 264  HOH   HOH A . 
V 6 HOH   266  1366 381  HOH   HOH A . 
V 6 HOH   267  1367 1083 HOH   HOH A . 
V 6 HOH   268  1368 103  HOH   HOH A . 
V 6 HOH   269  1369 711  HOH   HOH A . 
V 6 HOH   270  1370 812  HOH   HOH A . 
V 6 HOH   271  1371 747  HOH   HOH A . 
V 6 HOH   272  1372 276  HOH   HOH A . 
V 6 HOH   273  1373 707  HOH   HOH A . 
V 6 HOH   274  1374 383  HOH   HOH A . 
V 6 HOH   275  1375 234  HOH   HOH A . 
V 6 HOH   276  1376 227  HOH   HOH A . 
V 6 HOH   277  1377 106  HOH   HOH A . 
V 6 HOH   278  1378 1099 HOH   HOH A . 
V 6 HOH   279  1379 28   HOH   HOH A . 
V 6 HOH   280  1380 302  HOH   HOH A . 
V 6 HOH   281  1381 305  HOH   HOH A . 
V 6 HOH   282  1382 511  HOH   HOH A . 
V 6 HOH   283  1383 64   HOH   HOH A . 
V 6 HOH   284  1384 902  HOH   HOH A . 
V 6 HOH   285  1385 539  HOH   HOH A . 
V 6 HOH   286  1386 26   HOH   HOH A . 
V 6 HOH   287  1387 108  HOH   HOH A . 
V 6 HOH   288  1388 1090 HOH   HOH A . 
V 6 HOH   289  1389 555  HOH   HOH A . 
V 6 HOH   290  1390 152  HOH   HOH A . 
V 6 HOH   291  1391 147  HOH   HOH A . 
V 6 HOH   292  1392 102  HOH   HOH A . 
V 6 HOH   293  1393 189  HOH   HOH A . 
V 6 HOH   294  1394 13   HOH   HOH A . 
V 6 HOH   295  1395 164  HOH   HOH A . 
V 6 HOH   296  1396 95   HOH   HOH A . 
V 6 HOH   297  1397 130  HOH   HOH A . 
V 6 HOH   298  1398 307  HOH   HOH A . 
V 6 HOH   299  1399 151  HOH   HOH A . 
V 6 HOH   300  1400 4    HOH   HOH A . 
V 6 HOH   301  1401 434  HOH   HOH A . 
V 6 HOH   302  1402 634  HOH   HOH A . 
V 6 HOH   303  1403 194  HOH   HOH A . 
V 6 HOH   304  1404 632  HOH   HOH A . 
V 6 HOH   305  1405 845  HOH   HOH A . 
V 6 HOH   306  1406 596  HOH   HOH A . 
V 6 HOH   307  1407 33   HOH   HOH A . 
V 6 HOH   308  1408 238  HOH   HOH A . 
V 6 HOH   309  1409 71   HOH   HOH A . 
V 6 HOH   310  1410 215  HOH   HOH A . 
V 6 HOH   311  1411 314  HOH   HOH A . 
V 6 HOH   312  1412 1190 HOH   HOH A . 
V 6 HOH   313  1413 615  HOH   HOH A . 
V 6 HOH   314  1414 229  HOH   HOH A . 
V 6 HOH   315  1415 87   HOH   HOH A . 
V 6 HOH   316  1416 715  HOH   HOH A . 
V 6 HOH   317  1417 46   HOH   HOH A . 
V 6 HOH   318  1418 154  HOH   HOH A . 
V 6 HOH   319  1419 242  HOH   HOH A . 
V 6 HOH   320  1420 983  HOH   HOH A . 
V 6 HOH   321  1421 564  HOH   HOH A . 
V 6 HOH   322  1422 433  HOH   HOH A . 
V 6 HOH   323  1423 740  HOH   HOH A . 
V 6 HOH   324  1424 728  HOH   HOH A . 
V 6 HOH   325  1425 303  HOH   HOH A . 
V 6 HOH   326  1426 287  HOH   HOH A . 
V 6 HOH   327  1427 881  HOH   HOH A . 
V 6 HOH   328  1428 481  HOH   HOH A . 
V 6 HOH   329  1429 127  HOH   HOH A . 
V 6 HOH   330  1430 104  HOH   HOH A . 
V 6 HOH   331  1431 972  HOH   HOH A . 
V 6 HOH   332  1432 284  HOH   HOH A . 
V 6 HOH   333  1433 977  HOH   HOH A . 
V 6 HOH   334  1434 45   HOH   HOH A . 
V 6 HOH   335  1435 598  HOH   HOH A . 
V 6 HOH   336  1436 365  HOH   HOH A . 
V 6 HOH   337  1437 41   HOH   HOH A . 
V 6 HOH   338  1438 610  HOH   HOH A . 
V 6 HOH   339  1439 299  HOH   HOH A . 
V 6 HOH   340  1440 175  HOH   HOH A . 
V 6 HOH   341  1441 437  HOH   HOH A . 
V 6 HOH   342  1442 400  HOH   HOH A . 
V 6 HOH   343  1443 516  HOH   HOH A . 
V 6 HOH   344  1444 89   HOH   HOH A . 
V 6 HOH   345  1445 118  HOH   HOH A . 
V 6 HOH   346  1446 176  HOH   HOH A . 
V 6 HOH   347  1447 542  HOH   HOH A . 
V 6 HOH   348  1448 129  HOH   HOH A . 
V 6 HOH   349  1449 226  HOH   HOH A . 
V 6 HOH   350  1450 258  HOH   HOH A . 
V 6 HOH   351  1451 390  HOH   HOH A . 
V 6 HOH   352  1452 602  HOH   HOH A . 
V 6 HOH   353  1453 32   HOH   HOH A . 
V 6 HOH   354  1454 35   HOH   HOH A . 
V 6 HOH   355  1455 31   HOH   HOH A . 
V 6 HOH   356  1456 137  HOH   HOH A . 
V 6 HOH   357  1457 210  HOH   HOH A . 
V 6 HOH   358  1458 930  HOH   HOH A . 
V 6 HOH   359  1459 190  HOH   HOH A . 
V 6 HOH   360  1460 879  HOH   HOH A . 
V 6 HOH   361  1461 1095 HOH   HOH A . 
V 6 HOH   362  1462 68   HOH   HOH A . 
V 6 HOH   363  1463 309  HOH   HOH A . 
V 6 HOH   364  1464 502  HOH   HOH A . 
V 6 HOH   365  1465 946  HOH   HOH A . 
V 6 HOH   366  1466 9    HOH   HOH A . 
V 6 HOH   367  1467 115  HOH   HOH A . 
V 6 HOH   368  1468 105  HOH   HOH A . 
V 6 HOH   369  1469 540  HOH   HOH A . 
V 6 HOH   370  1470 491  HOH   HOH A . 
V 6 HOH   371  1471 10   HOH   HOH A . 
V 6 HOH   372  1472 170  HOH   HOH A . 
V 6 HOH   373  1473 61   HOH   HOH A . 
V 6 HOH   374  1474 454  HOH   HOH A . 
V 6 HOH   375  1475 216  HOH   HOH A . 
V 6 HOH   376  1476 144  HOH   HOH A . 
V 6 HOH   377  1477 868  HOH   HOH A . 
V 6 HOH   378  1478 222  HOH   HOH A . 
V 6 HOH   379  1479 7    HOH   HOH A . 
V 6 HOH   380  1480 128  HOH   HOH A . 
V 6 HOH   381  1481 116  HOH   HOH A . 
V 6 HOH   382  1482 863  HOH   HOH A . 
V 6 HOH   383  1483 112  HOH   HOH A . 
V 6 HOH   384  1484 203  HOH   HOH A . 
V 6 HOH   385  1485 710  HOH   HOH A . 
V 6 HOH   386  1486 663  HOH   HOH A . 
V 6 HOH   387  1487 332  HOH   HOH A . 
V 6 HOH   388  1488 1172 HOH   HOH A . 
V 6 HOH   389  1489 619  HOH   HOH A . 
V 6 HOH   390  1490 641  HOH   HOH A . 
V 6 HOH   391  1491 527  HOH   HOH A . 
V 6 HOH   392  1492 125  HOH   HOH A . 
V 6 HOH   393  1493 57   HOH   HOH A . 
V 6 HOH   394  1494 395  HOH   HOH A . 
V 6 HOH   395  1495 1033 HOH   HOH A . 
V 6 HOH   396  1496 440  HOH   HOH A . 
V 6 HOH   397  1497 744  HOH   HOH A . 
V 6 HOH   398  1498 100  HOH   HOH A . 
V 6 HOH   399  1499 236  HOH   HOH A . 
V 6 HOH   400  1500 202  HOH   HOH A . 
V 6 HOH   401  1501 905  HOH   HOH A . 
V 6 HOH   402  1502 561  HOH   HOH A . 
V 6 HOH   403  1503 909  HOH   HOH A . 
V 6 HOH   404  1504 585  HOH   HOH A . 
V 6 HOH   405  1505 566  HOH   HOH A . 
V 6 HOH   406  1506 621  HOH   HOH A . 
V 6 HOH   407  1507 311  HOH   HOH A . 
V 6 HOH   408  1508 686  HOH   HOH A . 
V 6 HOH   409  1509 647  HOH   HOH A . 
V 6 HOH   410  1510 667  HOH   HOH A . 
V 6 HOH   411  1511 298  HOH   HOH A . 
V 6 HOH   412  1512 535  HOH   HOH A . 
V 6 HOH   413  1513 969  HOH   HOH A . 
V 6 HOH   414  1514 133  HOH   HOH A . 
V 6 HOH   415  1515 760  HOH   HOH A . 
V 6 HOH   416  1516 131  HOH   HOH A . 
V 6 HOH   417  1517 255  HOH   HOH A . 
V 6 HOH   418  1518 1057 HOH   HOH A . 
V 6 HOH   419  1519 323  HOH   HOH A . 
V 6 HOH   420  1520 752  HOH   HOH A . 
V 6 HOH   421  1521 520  HOH   HOH A . 
V 6 HOH   422  1522 163  HOH   HOH A . 
V 6 HOH   423  1523 374  HOH   HOH A . 
V 6 HOH   424  1524 83   HOH   HOH A . 
V 6 HOH   425  1525 293  HOH   HOH A . 
V 6 HOH   426  1526 16   HOH   HOH A . 
V 6 HOH   427  1527 73   HOH   HOH A . 
V 6 HOH   428  1528 543  HOH   HOH A . 
V 6 HOH   429  1529 1098 HOH   HOH A . 
V 6 HOH   430  1530 282  HOH   HOH A . 
V 6 HOH   431  1531 784  HOH   HOH A . 
V 6 HOH   432  1532 22   HOH   HOH A . 
V 6 HOH   433  1533 81   HOH   HOH A . 
V 6 HOH   434  1534 74   HOH   HOH A . 
V 6 HOH   435  1535 360  HOH   HOH A . 
V 6 HOH   436  1536 94   HOH   HOH A . 
V 6 HOH   437  1537 424  HOH   HOH A . 
V 6 HOH   438  1538 96   HOH   HOH A . 
V 6 HOH   439  1539 47   HOH   HOH A . 
V 6 HOH   440  1540 141  HOH   HOH A . 
V 6 HOH   441  1541 14   HOH   HOH A . 
V 6 HOH   442  1542 172  HOH   HOH A . 
V 6 HOH   443  1543 692  HOH   HOH A . 
V 6 HOH   444  1544 188  HOH   HOH A . 
V 6 HOH   445  1545 1075 HOH   HOH A . 
V 6 HOH   446  1546 730  HOH   HOH A . 
V 6 HOH   447  1547 429  HOH   HOH A . 
V 6 HOH   448  1548 376  HOH   HOH A . 
V 6 HOH   449  1549 412  HOH   HOH A . 
V 6 HOH   450  1550 224  HOH   HOH A . 
V 6 HOH   451  1551 159  HOH   HOH A . 
V 6 HOH   452  1552 513  HOH   HOH A . 
V 6 HOH   453  1553 134  HOH   HOH A . 
V 6 HOH   454  1554 263  HOH   HOH A . 
V 6 HOH   455  1555 364  HOH   HOH A . 
V 6 HOH   456  1556 415  HOH   HOH A . 
V 6 HOH   457  1557 981  HOH   HOH A . 
V 6 HOH   458  1558 138  HOH   HOH A . 
V 6 HOH   459  1559 187  HOH   HOH A . 
V 6 HOH   460  1560 650  HOH   HOH A . 
V 6 HOH   461  1561 739  HOH   HOH A . 
V 6 HOH   462  1562 544  HOH   HOH A . 
V 6 HOH   463  1563 477  HOH   HOH A . 
V 6 HOH   464  1564 729  HOH   HOH A . 
V 6 HOH   465  1565 714  HOH   HOH A . 
V 6 HOH   466  1566 1108 HOH   HOH A . 
V 6 HOH   467  1567 382  HOH   HOH A . 
V 6 HOH   468  1568 160  HOH   HOH A . 
V 6 HOH   469  1569 603  HOH   HOH A . 
V 6 HOH   470  1570 418  HOH   HOH A . 
V 6 HOH   471  1571 1133 HOH   HOH A . 
V 6 HOH   472  1572 949  HOH   HOH A . 
V 6 HOH   473  1573 899  HOH   HOH A . 
V 6 HOH   474  1574 69   HOH   HOH A . 
V 6 HOH   475  1575 601  HOH   HOH A . 
V 6 HOH   476  1576 24   HOH   HOH A . 
V 6 HOH   477  1577 622  HOH   HOH A . 
V 6 HOH   478  1578 908  HOH   HOH A . 
V 6 HOH   479  1579 629  HOH   HOH A . 
V 6 HOH   480  1580 493  HOH   HOH A . 
V 6 HOH   481  1581 157  HOH   HOH A . 
V 6 HOH   482  1582 361  HOH   HOH A . 
V 6 HOH   483  1583 1208 HOH   HOH A . 
V 6 HOH   484  1584 107  HOH   HOH A . 
V 6 HOH   485  1585 679  HOH   HOH A . 
V 6 HOH   486  1586 21   HOH   HOH A . 
V 6 HOH   487  1587 825  HOH   HOH A . 
V 6 HOH   488  1588 702  HOH   HOH A . 
V 6 HOH   489  1589 428  HOH   HOH A . 
V 6 HOH   490  1590 627  HOH   HOH A . 
V 6 HOH   491  1591 987  HOH   HOH A . 
V 6 HOH   492  1592 371  HOH   HOH A . 
V 6 HOH   493  1593 259  HOH   HOH A . 
V 6 HOH   494  1594 1203 HOH   HOH A . 
V 6 HOH   495  1595 145  HOH   HOH A . 
V 6 HOH   496  1596 665  HOH   HOH A . 
V 6 HOH   497  1597 483  HOH   HOH A . 
V 6 HOH   498  1598 1063 HOH   HOH A . 
V 6 HOH   499  1599 90   HOH   HOH A . 
V 6 HOH   500  1600 708  HOH   HOH A . 
V 6 HOH   501  1601 398  HOH   HOH A . 
V 6 HOH   502  1602 200  HOH   HOH A . 
V 6 HOH   503  1603 455  HOH   HOH A . 
V 6 HOH   504  1604 771  HOH   HOH A . 
V 6 HOH   505  1605 656  HOH   HOH A . 
V 6 HOH   506  1606 557  HOH   HOH A . 
V 6 HOH   507  1607 244  HOH   HOH A . 
V 6 HOH   508  1608 1195 HOH   HOH A . 
V 6 HOH   509  1609 943  HOH   HOH A . 
V 6 HOH   510  1610 221  HOH   HOH A . 
V 6 HOH   511  1611 1049 HOH   HOH A . 
V 6 HOH   512  1612 267  HOH   HOH A . 
V 6 HOH   513  1613 378  HOH   HOH A . 
V 6 HOH   514  1614 856  HOH   HOH A . 
V 6 HOH   515  1615 999  HOH   HOH A . 
V 6 HOH   516  1616 638  HOH   HOH A . 
V 6 HOH   517  1617 1027 HOH   HOH A . 
V 6 HOH   518  1618 1    HOH   HOH A . 
V 6 HOH   519  1619 51   HOH   HOH A . 
V 6 HOH   520  1620 934  HOH   HOH A . 
V 6 HOH   521  1621 289  HOH   HOH A . 
V 6 HOH   522  1622 895  HOH   HOH A . 
V 6 HOH   523  1623 161  HOH   HOH A . 
V 6 HOH   524  1624 359  HOH   HOH A . 
V 6 HOH   525  1625 1004 HOH   HOH A . 
V 6 HOH   526  1626 1200 HOH   HOH A . 
V 6 HOH   527  1627 98   HOH   HOH A . 
V 6 HOH   528  1628 269  HOH   HOH A . 
V 6 HOH   529  1629 186  HOH   HOH A . 
V 6 HOH   530  1630 53   HOH   HOH A . 
V 6 HOH   531  1631 562  HOH   HOH A . 
V 6 HOH   532  1632 488  HOH   HOH A . 
V 6 HOH   533  1633 700  HOH   HOH A . 
V 6 HOH   534  1634 257  HOH   HOH A . 
V 6 HOH   535  1635 50   HOH   HOH A . 
V 6 HOH   536  1636 832  HOH   HOH A . 
V 6 HOH   537  1637 1081 HOH   HOH A . 
V 6 HOH   538  1638 40   HOH   HOH A . 
V 6 HOH   539  1639 248  HOH   HOH A . 
V 6 HOH   540  1640 146  HOH   HOH A . 
V 6 HOH   541  1641 1110 HOH   HOH A . 
V 6 HOH   542  1642 396  HOH   HOH A . 
V 6 HOH   543  1643 171  HOH   HOH A . 
V 6 HOH   544  1644 688  HOH   HOH A . 
V 6 HOH   545  1645 531  HOH   HOH A . 
V 6 HOH   546  1646 978  HOH   HOH A . 
V 6 HOH   547  1647 75   HOH   HOH A . 
V 6 HOH   548  1648 76   HOH   HOH A . 
V 6 HOH   549  1649 691  HOH   HOH A . 
V 6 HOH   550  1650 442  HOH   HOH A . 
V 6 HOH   551  1651 1197 HOH   HOH A . 
V 6 HOH   552  1652 443  HOH   HOH A . 
V 6 HOH   553  1653 386  HOH   HOH A . 
V 6 HOH   554  1654 342  HOH   HOH A . 
V 6 HOH   555  1655 1088 HOH   HOH A . 
V 6 HOH   556  1656 751  HOH   HOH A . 
V 6 HOH   557  1657 569  HOH   HOH A . 
V 6 HOH   558  1658 333  HOH   HOH A . 
V 6 HOH   559  1659 1086 HOH   HOH A . 
V 6 HOH   560  1660 23   HOH   HOH A . 
V 6 HOH   561  1661 662  HOH   HOH A . 
V 6 HOH   562  1662 689  HOH   HOH A . 
V 6 HOH   563  1663 593  HOH   HOH A . 
V 6 HOH   564  1664 410  HOH   HOH A . 
V 6 HOH   565  1665 408  HOH   HOH A . 
V 6 HOH   566  1666 308  HOH   HOH A . 
V 6 HOH   567  1667 1214 HOH   HOH A . 
V 6 HOH   568  1668 828  HOH   HOH A . 
V 6 HOH   569  1669 482  HOH   HOH A . 
V 6 HOH   570  1670 181  HOH   HOH A . 
V 6 HOH   571  1671 548  HOH   HOH A . 
V 6 HOH   572  1672 384  HOH   HOH A . 
V 6 HOH   573  1673 1184 HOH   HOH A . 
V 6 HOH   574  1674 668  HOH   HOH A . 
V 6 HOH   575  1675 319  HOH   HOH A . 
V 6 HOH   576  1676 831  HOH   HOH A . 
V 6 HOH   577  1677 142  HOH   HOH A . 
V 6 HOH   578  1678 139  HOH   HOH A . 
V 6 HOH   579  1679 56   HOH   HOH A . 
V 6 HOH   580  1680 685  HOH   HOH A . 
V 6 HOH   581  1681 436  HOH   HOH A . 
V 6 HOH   582  1682 678  HOH   HOH A . 
V 6 HOH   583  1683 295  HOH   HOH A . 
V 6 HOH   584  1684 173  HOH   HOH A . 
V 6 HOH   585  1685 402  HOH   HOH A . 
V 6 HOH   586  1686 821  HOH   HOH A . 
V 6 HOH   587  1687 296  HOH   HOH A . 
V 6 HOH   588  1688 237  HOH   HOH A . 
V 6 HOH   589  1689 42   HOH   HOH A . 
V 6 HOH   590  1690 699  HOH   HOH A . 
V 6 HOH   591  1691 536  HOH   HOH A . 
V 6 HOH   592  1692 196  HOH   HOH A . 
V 6 HOH   593  1693 1121 HOH   HOH A . 
V 6 HOH   594  1694 507  HOH   HOH A . 
V 6 HOH   595  1695 773  HOH   HOH A . 
V 6 HOH   596  1696 485  HOH   HOH A . 
V 6 HOH   597  1697 261  HOH   HOH A . 
V 6 HOH   598  1698 652  HOH   HOH A . 
V 6 HOH   599  1699 984  HOH   HOH A . 
V 6 HOH   600  1700 854  HOH   HOH A . 
V 6 HOH   601  1701 600  HOH   HOH A . 
V 6 HOH   602  1702 366  HOH   HOH A . 
V 6 HOH   603  1703 846  HOH   HOH A . 
V 6 HOH   604  1704 262  HOH   HOH A . 
V 6 HOH   605  1705 123  HOH   HOH A . 
V 6 HOH   606  1706 1181 HOH   HOH A . 
V 6 HOH   607  1707 37   HOH   HOH A . 
V 6 HOH   608  1708 184  HOH   HOH A . 
V 6 HOH   609  1709 919  HOH   HOH A . 
V 6 HOH   610  1710 121  HOH   HOH A . 
V 6 HOH   611  1711 1082 HOH   HOH A . 
V 6 HOH   612  1712 1150 HOH   HOH A . 
V 6 HOH   613  1713 567  HOH   HOH A . 
V 6 HOH   614  1714 758  HOH   HOH A . 
V 6 HOH   615  1715 633  HOH   HOH A . 
V 6 HOH   616  1716 149  HOH   HOH A . 
V 6 HOH   617  1717 425  HOH   HOH A . 
V 6 HOH   618  1718 1101 HOH   HOH A . 
V 6 HOH   619  1719 1198 HOH   HOH A . 
V 6 HOH   620  1720 328  HOH   HOH A . 
V 6 HOH   621  1721 869  HOH   HOH A . 
V 6 HOH   622  1722 153  HOH   HOH A . 
V 6 HOH   623  1723 29   HOH   HOH A . 
V 6 HOH   624  1724 781  HOH   HOH A . 
V 6 HOH   625  1725 480  HOH   HOH A . 
V 6 HOH   626  1726 329  HOH   HOH A . 
V 6 HOH   627  1727 936  HOH   HOH A . 
V 6 HOH   628  1728 432  HOH   HOH A . 
V 6 HOH   629  1729 82   HOH   HOH A . 
V 6 HOH   630  1730 279  HOH   HOH A . 
V 6 HOH   631  1731 379  HOH   HOH A . 
V 6 HOH   632  1732 478  HOH   HOH A . 
V 6 HOH   633  1733 737  HOH   HOH A . 
V 6 HOH   634  1734 1116 HOH   HOH A . 
V 6 HOH   635  1735 469  HOH   HOH A . 
V 6 HOH   636  1736 462  HOH   HOH A . 
V 6 HOH   637  1737 27   HOH   HOH A . 
V 6 HOH   638  1738 693  HOH   HOH A . 
V 6 HOH   639  1739 877  HOH   HOH A . 
V 6 HOH   640  1740 660  HOH   HOH A . 
V 6 HOH   641  1741 420  HOH   HOH A . 
V 6 HOH   642  1742 713  HOH   HOH A . 
V 6 HOH   643  1743 78   HOH   HOH A . 
V 6 HOH   644  1744 623  HOH   HOH A . 
V 6 HOH   645  1745 976  HOH   HOH A . 
V 6 HOH   646  1746 197  HOH   HOH A . 
V 6 HOH   647  1747 537  HOH   HOH A . 
V 6 HOH   648  1748 1114 HOH   HOH A . 
V 6 HOH   649  1749 185  HOH   HOH A . 
V 6 HOH   650  1750 312  HOH   HOH A . 
V 6 HOH   651  1751 628  HOH   HOH A . 
V 6 HOH   652  1752 876  HOH   HOH A . 
V 6 HOH   653  1753 446  HOH   HOH A . 
V 6 HOH   654  1754 426  HOH   HOH A . 
V 6 HOH   655  1755 336  HOH   HOH A . 
V 6 HOH   656  1756 956  HOH   HOH A . 
V 6 HOH   657  1757 253  HOH   HOH A . 
V 6 HOH   658  1758 862  HOH   HOH A . 
V 6 HOH   659  1759 738  HOH   HOH A . 
V 6 HOH   660  1760 99   HOH   HOH A . 
V 6 HOH   661  1761 945  HOH   HOH A . 
V 6 HOH   662  1762 380  HOH   HOH A . 
V 6 HOH   663  1763 411  HOH   HOH A . 
V 6 HOH   664  1764 231  HOH   HOH A . 
V 6 HOH   665  1765 802  HOH   HOH A . 
V 6 HOH   666  1766 362  HOH   HOH A . 
V 6 HOH   667  1767 1079 HOH   HOH A . 
V 6 HOH   668  1768 406  HOH   HOH A . 
V 6 HOH   669  1769 367  HOH   HOH A . 
V 6 HOH   670  1770 122  HOH   HOH A . 
V 6 HOH   671  1771 970  HOH   HOH A . 
V 6 HOH   672  1772 521  HOH   HOH A . 
V 6 HOH   673  1773 990  HOH   HOH A . 
V 6 HOH   674  1774 476  HOH   HOH A . 
V 6 HOH   675  1775 661  HOH   HOH A . 
V 6 HOH   676  1776 755  HOH   HOH A . 
V 6 HOH   677  1777 274  HOH   HOH A . 
V 6 HOH   678  1778 246  HOH   HOH A . 
V 6 HOH   679  1779 317  HOH   HOH A . 
V 6 HOH   680  1780 448  HOH   HOH A . 
V 6 HOH   681  1781 331  HOH   HOH A . 
V 6 HOH   682  1782 906  HOH   HOH A . 
V 6 HOH   683  1783 594  HOH   HOH A . 
V 6 HOH   684  1784 79   HOH   HOH A . 
V 6 HOH   685  1785 92   HOH   HOH A . 
V 6 HOH   686  1786 532  HOH   HOH A . 
V 6 HOH   687  1787 1006 HOH   HOH A . 
V 6 HOH   688  1788 466  HOH   HOH A . 
V 6 HOH   689  1789 209  HOH   HOH A . 
V 6 HOH   690  1790 766  HOH   HOH A . 
V 6 HOH   691  1791 416  HOH   HOH A . 
V 6 HOH   692  1792 120  HOH   HOH A . 
V 6 HOH   693  1793 914  HOH   HOH A . 
V 6 HOH   694  1794 986  HOH   HOH A . 
V 6 HOH   695  1795 653  HOH   HOH A . 
V 6 HOH   696  1796 915  HOH   HOH A . 
V 6 HOH   697  1797 620  HOH   HOH A . 
V 6 HOH   698  1798 501  HOH   HOH A . 
V 6 HOH   699  1799 445  HOH   HOH A . 
V 6 HOH   700  1800 260  HOH   HOH A . 
V 6 HOH   701  1801 111  HOH   HOH A . 
V 6 HOH   702  1802 782  HOH   HOH A . 
V 6 HOH   703  1803 265  HOH   HOH A . 
V 6 HOH   704  1804 441  HOH   HOH A . 
V 6 HOH   705  1805 473  HOH   HOH A . 
V 6 HOH   706  1806 135  HOH   HOH A . 
V 6 HOH   707  1807 1135 HOH   HOH A . 
V 6 HOH   708  1808 353  HOH   HOH A . 
V 6 HOH   709  1809 347  HOH   HOH A . 
V 6 HOH   710  1810 180  HOH   HOH A . 
V 6 HOH   711  1811 351  HOH   HOH A . 
V 6 HOH   712  1812 315  HOH   HOH A . 
V 6 HOH   713  1813 836  HOH   HOH A . 
V 6 HOH   714  1814 207  HOH   HOH A . 
V 6 HOH   715  1815 394  HOH   HOH A . 
V 6 HOH   716  1816 140  HOH   HOH A . 
V 6 HOH   717  1817 132  HOH   HOH A . 
V 6 HOH   718  1818 49   HOH   HOH A . 
V 6 HOH   719  1819 271  HOH   HOH A . 
V 6 HOH   720  1820 721  HOH   HOH A . 
V 6 HOH   721  1821 318  HOH   HOH A . 
V 6 HOH   722  1822 582  HOH   HOH A . 
V 6 HOH   723  1823 252  HOH   HOH A . 
V 6 HOH   724  1824 644  HOH   HOH A . 
V 6 HOH   725  1825 393  HOH   HOH A . 
V 6 HOH   726  1826 356  HOH   HOH A . 
V 6 HOH   727  1827 278  HOH   HOH A . 
V 6 HOH   728  1828 842  HOH   HOH A . 
V 6 HOH   729  1829 272  HOH   HOH A . 
V 6 HOH   730  1830 830  HOH   HOH A . 
V 6 HOH   731  1831 297  HOH   HOH A . 
V 6 HOH   732  1832 545  HOH   HOH A . 
V 6 HOH   733  1833 785  HOH   HOH A . 
V 6 HOH   734  1834 514  HOH   HOH A . 
V 6 HOH   735  1835 479  HOH   HOH A . 
V 6 HOH   736  1836 996  HOH   HOH A . 
V 6 HOH   737  1837 301  HOH   HOH A . 
V 6 HOH   738  1838 306  HOH   HOH A . 
V 6 HOH   739  1839 117  HOH   HOH A . 
V 6 HOH   740  1840 450  HOH   HOH A . 
V 6 HOH   741  1841 1194 HOH   HOH A . 
V 6 HOH   742  1842 718  HOH   HOH A . 
V 6 HOH   743  1843 281  HOH   HOH A . 
V 6 HOH   744  1844 890  HOH   HOH A . 
V 6 HOH   745  1845 506  HOH   HOH A . 
V 6 HOH   746  1846 119  HOH   HOH A . 
V 6 HOH   747  1847 1034 HOH   HOH A . 
V 6 HOH   748  1848 66   HOH   HOH A . 
V 6 HOH   749  1849 1122 HOH   HOH A . 
V 6 HOH   750  1850 458  HOH   HOH A . 
V 6 HOH   751  1851 472  HOH   HOH A . 
V 6 HOH   752  1852 77   HOH   HOH A . 
V 6 HOH   753  1853 109  HOH   HOH A . 
V 6 HOH   754  1854 1080 HOH   HOH A . 
V 6 HOH   755  1855 1157 HOH   HOH A . 
V 6 HOH   756  1856 235  HOH   HOH A . 
V 6 HOH   757  1857 422  HOH   HOH A . 
V 6 HOH   758  1858 810  HOH   HOH A . 
V 6 HOH   759  1859 19   HOH   HOH A . 
V 6 HOH   760  1860 204  HOH   HOH A . 
V 6 HOH   761  1861 150  HOH   HOH A . 
V 6 HOH   762  1862 901  HOH   HOH A . 
V 6 HOH   763  1863 232  HOH   HOH A . 
V 6 HOH   764  1864 474  HOH   HOH A . 
V 6 HOH   765  1865 399  HOH   HOH A . 
V 6 HOH   766  1866 1070 HOH   HOH A . 
V 6 HOH   767  1867 772  HOH   HOH A . 
V 6 HOH   768  1868 973  HOH   HOH A . 
V 6 HOH   769  1869 1162 HOH   HOH A . 
V 6 HOH   770  1870 124  HOH   HOH A . 
V 6 HOH   771  1871 591  HOH   HOH A . 
V 6 HOH   772  1872 529  HOH   HOH A . 
V 6 HOH   773  1873 166  HOH   HOH A . 
V 6 HOH   774  1874 148  HOH   HOH A . 
V 6 HOH   775  1875 875  HOH   HOH A . 
V 6 HOH   776  1876 704  HOH   HOH A . 
V 6 HOH   777  1877 1056 HOH   HOH A . 
V 6 HOH   778  1878 345  HOH   HOH A . 
V 6 HOH   779  1879 372  HOH   HOH A . 
V 6 HOH   780  1880 1022 HOH   HOH A . 
V 6 HOH   781  1881 804  HOH   HOH A . 
V 6 HOH   782  1882 630  HOH   HOH A . 
V 6 HOH   783  1883 823  HOH   HOH A . 
V 6 HOH   784  1884 52   HOH   HOH A . 
V 6 HOH   785  1885 640  HOH   HOH A . 
V 6 HOH   786  1886 609  HOH   HOH A . 
V 6 HOH   787  1887 1085 HOH   HOH A . 
V 6 HOH   788  1888 349  HOH   HOH A . 
V 6 HOH   789  1889 270  HOH   HOH A . 
V 6 HOH   790  1890 920  HOH   HOH A . 
V 6 HOH   791  1891 1059 HOH   HOH A . 
V 6 HOH   792  1892 1042 HOH   HOH A . 
V 6 HOH   793  1893 586  HOH   HOH A . 
V 6 HOH   794  1894 174  HOH   HOH A . 
V 6 HOH   795  1895 182  HOH   HOH A . 
V 6 HOH   796  1896 680  HOH   HOH A . 
V 6 HOH   797  1897 565  HOH   HOH A . 
V 6 HOH   798  1898 1230 HOH   HOH A . 
V 6 HOH   799  1899 720  HOH   HOH A . 
V 6 HOH   800  1900 635  HOH   HOH A . 
V 6 HOH   801  1901 637  HOH   HOH A . 
V 6 HOH   802  1902 388  HOH   HOH A . 
V 6 HOH   803  1903 1128 HOH   HOH A . 
V 6 HOH   804  1904 913  HOH   HOH A . 
V 6 HOH   805  1905 512  HOH   HOH A . 
V 6 HOH   806  1906 922  HOH   HOH A . 
V 6 HOH   807  1907 592  HOH   HOH A . 
V 6 HOH   808  1908 864  HOH   HOH A . 
V 6 HOH   809  1909 625  HOH   HOH A . 
V 6 HOH   810  1910 550  HOH   HOH A . 
V 6 HOH   811  1911 727  HOH   HOH A . 
V 6 HOH   812  1912 355  HOH   HOH A . 
V 6 HOH   813  1913 1043 HOH   HOH A . 
V 6 HOH   814  1914 1149 HOH   HOH A . 
V 6 HOH   815  1915 1040 HOH   HOH A . 
V 6 HOH   816  1916 961  HOH   HOH A . 
V 6 HOH   817  1917 354  HOH   HOH A . 
V 6 HOH   818  1918 1045 HOH   HOH A . 
V 6 HOH   819  1919 959  HOH   HOH A . 
V 6 HOH   820  1920 358  HOH   HOH A . 
V 6 HOH   821  1921 571  HOH   HOH A . 
V 6 HOH   822  1922 768  HOH   HOH A . 
V 6 HOH   823  1923 101  HOH   HOH A . 
V 6 HOH   824  1924 459  HOH   HOH A . 
V 6 HOH   825  1925 694  HOH   HOH A . 
V 6 HOH   826  1926 1013 HOH   HOH A . 
V 6 HOH   827  1927 1115 HOH   HOH A . 
V 6 HOH   828  1928 799  HOH   HOH A . 
V 6 HOH   829  1929 911  HOH   HOH A . 
V 6 HOH   830  1930 827  HOH   HOH A . 
V 6 HOH   831  1931 935  HOH   HOH A . 
V 6 HOH   832  1932 695  HOH   HOH A . 
V 6 HOH   833  1933 1047 HOH   HOH A . 
V 6 HOH   834  1934 942  HOH   HOH A . 
V 6 HOH   835  1935 470  HOH   HOH A . 
V 6 HOH   836  1936 698  HOH   HOH A . 
V 6 HOH   837  1937 1216 HOH   HOH A . 
V 6 HOH   838  1938 865  HOH   HOH A . 
V 6 HOH   839  1939 584  HOH   HOH A . 
V 6 HOH   840  1940 855  HOH   HOH A . 
V 6 HOH   841  1941 114  HOH   HOH A . 
V 6 HOH   842  1942 597  HOH   HOH A . 
V 6 HOH   843  1943 280  HOH   HOH A . 
V 6 HOH   844  1944 960  HOH   HOH A . 
V 6 HOH   845  1945 1089 HOH   HOH A . 
V 6 HOH   846  1946 225  HOH   HOH A . 
V 6 HOH   847  1947 787  HOH   HOH A . 
V 6 HOH   848  1948 926  HOH   HOH A . 
V 6 HOH   849  1949 241  HOH   HOH A . 
V 6 HOH   850  1950 809  HOH   HOH A . 
V 6 HOH   851  1951 833  HOH   HOH A . 
V 6 HOH   852  1952 967  HOH   HOH A . 
V 6 HOH   853  1953 1050 HOH   HOH A . 
V 6 HOH   854  1954 861  HOH   HOH A . 
V 6 HOH   855  1955 509  HOH   HOH A . 
V 6 HOH   856  1956 409  HOH   HOH A . 
V 6 HOH   857  1957 673  HOH   HOH A . 
V 6 HOH   858  1958 1196 HOH   HOH A . 
V 6 HOH   859  1959 904  HOH   HOH A . 
V 6 HOH   860  1960 816  HOH   HOH A . 
V 6 HOH   861  1961 757  HOH   HOH A . 
V 6 HOH   862  1962 581  HOH   HOH A . 
V 6 HOH   863  1963 1076 HOH   HOH A . 
V 6 HOH   864  1964 1124 HOH   HOH A . 
V 6 HOH   865  1965 950  HOH   HOH A . 
V 6 HOH   866  1966 820  HOH   HOH A . 
V 6 HOH   867  1967 1066 HOH   HOH A . 
V 6 HOH   868  1968 1144 HOH   HOH A . 
V 6 HOH   869  1969 563  HOH   HOH A . 
V 6 HOH   870  1970 858  HOH   HOH A . 
V 6 HOH   871  1971 778  HOH   HOH A . 
V 6 HOH   872  1972 335  HOH   HOH A . 
V 6 HOH   873  1973 997  HOH   HOH A . 
V 6 HOH   874  1974 1035 HOH   HOH A . 
V 6 HOH   875  1975 636  HOH   HOH A . 
V 6 HOH   876  1976 726  HOH   HOH A . 
V 6 HOH   877  1977 732  HOH   HOH A . 
V 6 HOH   878  1978 1118 HOH   HOH A . 
V 6 HOH   879  1979 917  HOH   HOH A . 
V 6 HOH   880  1980 910  HOH   HOH A . 
V 6 HOH   881  1981 893  HOH   HOH A . 
V 6 HOH   882  1982 608  HOH   HOH A . 
V 6 HOH   883  1983 1176 HOH   HOH A . 
V 6 HOH   884  1984 1038 HOH   HOH A . 
V 6 HOH   885  1985 733  HOH   HOH A . 
V 6 HOH   886  1986 734  HOH   HOH A . 
V 6 HOH   887  1987 674  HOH   HOH A . 
V 6 HOH   888  1988 788  HOH   HOH A . 
V 6 HOH   889  1989 337  HOH   HOH A . 
V 6 HOH   890  1990 754  HOH   HOH A . 
V 6 HOH   891  1991 1209 HOH   HOH A . 
V 6 HOH   892  1992 294  HOH   HOH A . 
V 6 HOH   893  1993 179  HOH   HOH A . 
V 6 HOH   894  1994 887  HOH   HOH A . 
V 6 HOH   895  1995 1161 HOH   HOH A . 
V 6 HOH   896  1996 684  HOH   HOH A . 
V 6 HOH   897  1997 1005 HOH   HOH A . 
V 6 HOH   898  1998 964  HOH   HOH A . 
V 6 HOH   899  1999 826  HOH   HOH A . 
V 6 HOH   900  2000 1010 HOH   HOH A . 
V 6 HOH   901  2001 292  HOH   HOH A . 
V 6 HOH   902  2002 1123 HOH   HOH A . 
V 6 HOH   903  2003 792  HOH   HOH A . 
V 6 HOH   904  2004 498  HOH   HOH A . 
V 6 HOH   905  2005 852  HOH   HOH A . 
V 6 HOH   906  2006 927  HOH   HOH A . 
V 6 HOH   907  2007 460  HOH   HOH A . 
V 6 HOH   908  2008 1185 HOH   HOH A . 
V 6 HOH   909  2009 918  HOH   HOH A . 
V 6 HOH   910  2010 464  HOH   HOH A . 
V 6 HOH   911  2011 805  HOH   HOH A . 
V 6 HOH   912  2012 829  HOH   HOH A . 
V 6 HOH   913  2013 389  HOH   HOH A . 
V 6 HOH   914  2014 1091 HOH   HOH A . 
V 6 HOH   915  2015 888  HOH   HOH A . 
V 6 HOH   916  2016 712  HOH   HOH A . 
V 6 HOH   917  2017 762  HOH   HOH A . 
V 6 HOH   918  2018 1028 HOH   HOH A . 
V 6 HOH   919  2019 1174 HOH   HOH A . 
V 6 HOH   920  2020 850  HOH   HOH A . 
V 6 HOH   921  2021 533  HOH   HOH A . 
V 6 HOH   922  2022 1153 HOH   HOH A . 
V 6 HOH   923  2023 1041 HOH   HOH A . 
V 6 HOH   924  2024 110  HOH   HOH A . 
V 6 HOH   925  2025 508  HOH   HOH A . 
V 6 HOH   926  2026 654  HOH   HOH A . 
V 6 HOH   927  2027 1205 HOH   HOH A . 
V 6 HOH   928  2028 835  HOH   HOH A . 
V 6 HOH   929  2029 1024 HOH   HOH A . 
V 6 HOH   930  2030 703  HOH   HOH A . 
V 6 HOH   931  2031 818  HOH   HOH A . 
V 6 HOH   932  2032 690  HOH   HOH A . 
V 6 HOH   933  2033 1171 HOH   HOH A . 
V 6 HOH   934  2034 538  HOH   HOH A . 
V 6 HOH   935  2035 1202 HOH   HOH A . 
V 6 HOH   936  2036 475  HOH   HOH A . 
V 6 HOH   937  2037 761  HOH   HOH A . 
V 6 HOH   938  2038 1011 HOH   HOH A . 
V 6 HOH   939  2039 1210 HOH   HOH A . 
V 6 HOH   940  2040 518  HOH   HOH A . 
V 6 HOH   941  2041 574  HOH   HOH A . 
V 6 HOH   942  2042 528  HOH   HOH A . 
V 6 HOH   943  2043 777  HOH   HOH A . 
V 6 HOH   944  2044 1199 HOH   HOH A . 
V 6 HOH   945  2045 1158 HOH   HOH A . 
V 6 HOH   946  2046 1221 HOH   HOH A . 
V 6 HOH   947  2047 681  HOH   HOH A . 
V 6 HOH   948  2048 882  HOH   HOH A . 
V 6 HOH   949  2049 783  HOH   HOH A . 
V 6 HOH   950  2050 158  HOH   HOH A . 
V 6 HOH   951  2051 1021 HOH   HOH A . 
V 6 HOH   952  2052 1119 HOH   HOH A . 
V 6 HOH   953  2053 940  HOH   HOH A . 
V 6 HOH   954  2054 430  HOH   HOH A . 
V 6 HOH   955  2055 753  HOH   HOH A . 
V 6 HOH   956  2056 765  HOH   HOH A . 
V 6 HOH   957  2057 770  HOH   HOH A . 
V 6 HOH   958  2058 841  HOH   HOH A . 
V 6 HOH   959  2059 1224 HOH   HOH A . 
V 6 HOH   960  2060 1009 HOH   HOH A . 
V 6 HOH   961  2061 921  HOH   HOH A . 
V 6 HOH   962  2062 657  HOH   HOH A . 
V 6 HOH   963  2063 1112 HOH   HOH A . 
V 6 HOH   964  2064 573  HOH   HOH A . 
V 6 HOH   965  2065 1165 HOH   HOH A . 
V 6 HOH   966  2066 676  HOH   HOH A . 
V 6 HOH   967  2067 612  HOH   HOH A . 
V 6 HOH   968  2068 1067 HOH   HOH A . 
V 6 HOH   969  2069 848  HOH   HOH A . 
V 6 HOH   970  2070 499  HOH   HOH A . 
V 6 HOH   971  2071 817  HOH   HOH A . 
V 6 HOH   972  2072 872  HOH   HOH A . 
V 6 HOH   973  2073 642  HOH   HOH A . 
V 6 HOH   974  2074 1120 HOH   HOH A . 
V 6 HOH   975  2075 339  HOH   HOH A . 
V 6 HOH   976  2076 1175 HOH   HOH A . 
V 6 HOH   977  2077 504  HOH   HOH A . 
V 6 HOH   978  2078 387  HOH   HOH A . 
V 6 HOH   979  2079 343  HOH   HOH A . 
V 6 HOH   980  2080 745  HOH   HOH A . 
V 6 HOH   981  2081 392  HOH   HOH A . 
V 6 HOH   982  2082 819  HOH   HOH A . 
V 6 HOH   983  2083 1046 HOH   HOH A . 
V 6 HOH   984  2084 357  HOH   HOH A . 
V 6 HOH   985  2085 1130 HOH   HOH A . 
V 6 HOH   986  2086 1061 HOH   HOH A . 
V 6 HOH   987  2087 631  HOH   HOH A . 
V 6 HOH   988  2088 1170 HOH   HOH A . 
V 6 HOH   989  2089 240  HOH   HOH A . 
V 6 HOH   990  2090 892  HOH   HOH A . 
V 6 HOH   991  2091 1183 HOH   HOH A . 
V 6 HOH   992  2092 624  HOH   HOH A . 
V 6 HOH   993  2093 1222 HOH   HOH A . 
V 6 HOH   994  2094 330  HOH   HOH A . 
V 6 HOH   995  2095 898  HOH   HOH A . 
V 6 HOH   996  2096 397  HOH   HOH A . 
V 6 HOH   997  2097 798  HOH   HOH A . 
V 6 HOH   998  2098 1187 HOH   HOH A . 
V 6 HOH   999  2099 968  HOH   HOH A . 
V 6 HOH   1000 2100 1228 HOH   HOH A . 
V 6 HOH   1001 2101 1126 HOH   HOH A . 
V 6 HOH   1002 2102 494  HOH   HOH A . 
V 6 HOH   1003 2103 1180 HOH   HOH A . 
V 6 HOH   1004 2104 991  HOH   HOH A . 
V 6 HOH   1005 2105 348  HOH   HOH A . 
V 6 HOH   1006 2106 496  HOH   HOH A . 
V 6 HOH   1007 2107 404  HOH   HOH A . 
V 6 HOH   1008 2108 838  HOH   HOH A . 
V 6 HOH   1009 2109 1155 HOH   HOH A . 
V 6 HOH   1010 2110 1015 HOH   HOH A . 
V 6 HOH   1011 2111 1058 HOH   HOH A . 
V 6 HOH   1012 2112 614  HOH   HOH A . 
V 6 HOH   1013 2113 742  HOH   HOH A . 
V 6 HOH   1014 2114 1188 HOH   HOH A . 
V 6 HOH   1015 2115 780  HOH   HOH A . 
V 6 HOH   1016 2116 352  HOH   HOH A . 
V 6 HOH   1017 2117 706  HOH   HOH A . 
V 6 HOH   1018 2118 958  HOH   HOH A . 
V 6 HOH   1019 2119 894  HOH   HOH A . 
V 6 HOH   1020 2120 725  HOH   HOH A . 
V 6 HOH   1021 2121 465  HOH   HOH A . 
V 6 HOH   1022 2122 643  HOH   HOH A . 
V 6 HOH   1023 2123 1020 HOH   HOH A . 
V 6 HOH   1024 2124 952  HOH   HOH A . 
V 6 HOH   1025 2125 1000 HOH   HOH A . 
V 6 HOH   1026 2126 941  HOH   HOH A . 
V 6 HOH   1027 2127 844  HOH   HOH A . 
V 6 HOH   1028 2128 341  HOH   HOH A . 
V 6 HOH   1029 2129 1007 HOH   HOH A . 
V 6 HOH   1030 2130 1106 HOH   HOH A . 
V 6 HOH   1031 2131 1140 HOH   HOH A . 
V 6 HOH   1032 2132 669  HOH   HOH A . 
V 6 HOH   1033 2133 405  HOH   HOH A . 
V 6 HOH   1034 2134 979  HOH   HOH A . 
V 6 HOH   1035 2135 556  HOH   HOH A . 
V 6 HOH   1036 2136 1084 HOH   HOH A . 
V 6 HOH   1037 2137 570  HOH   HOH A . 
V 6 HOH   1038 2138 419  HOH   HOH A . 
V 6 HOH   1039 2139 578  HOH   HOH A . 
V 6 HOH   1040 2140 324  HOH   HOH A . 
V 6 HOH   1041 2141 974  HOH   HOH A . 
V 6 HOH   1042 2142 923  HOH   HOH A . 
V 6 HOH   1043 2143 853  HOH   HOH A . 
V 6 HOH   1044 2144 490  HOH   HOH A . 
V 6 HOH   1045 2145 403  HOH   HOH A . 
V 6 HOH   1046 2146 724  HOH   HOH A . 
V 6 HOH   1047 2147 664  HOH   HOH A . 
V 6 HOH   1048 2148 717  HOH   HOH A . 
V 6 HOH   1049 2149 675  HOH   HOH A . 
V 6 HOH   1050 2150 1064 HOH   HOH A . 
V 6 HOH   1051 2151 775  HOH   HOH A . 
V 6 HOH   1052 2152 453  HOH   HOH A . 
V 6 HOH   1053 2153 814  HOH   HOH A . 
V 6 HOH   1054 2154 966  HOH   HOH A . 
V 6 HOH   1055 2155 670  HOH   HOH A . 
V 6 HOH   1056 2156 928  HOH   HOH A . 
V 6 HOH   1057 2157 1003 HOH   HOH A . 
V 6 HOH   1058 2158 797  HOH   HOH A . 
V 6 HOH   1059 2159 340  HOH   HOH A . 
V 6 HOH   1060 2160 541  HOH   HOH A . 
V 6 HOH   1061 2161 1137 HOH   HOH A . 
V 6 HOH   1062 2162 1107 HOH   HOH A . 
V 6 HOH   1063 2163 1113 HOH   HOH A . 
V 6 HOH   1064 2164 1173 HOH   HOH A . 
V 6 HOH   1065 2165 683  HOH   HOH A . 
V 6 HOH   1066 2166 1031 HOH   HOH A . 
V 6 HOH   1067 2167 611  HOH   HOH A . 
V 6 HOH   1068 2168 1018 HOH   HOH A . 
V 6 HOH   1069 2169 579  HOH   HOH A . 
V 6 HOH   1070 2170 1189 HOH   HOH A . 
V 6 HOH   1071 2171 807  HOH   HOH A . 
V 6 HOH   1072 2172 992  HOH   HOH A . 
V 6 HOH   1073 2173 155  HOH   HOH A . 
V 6 HOH   1074 2174 1139 HOH   HOH A . 
V 6 HOH   1075 2175 517  HOH   HOH A . 
V 6 HOH   1076 2176 326  HOH   HOH A . 
V 6 HOH   1077 2177 1225 HOH   HOH A . 
V 6 HOH   1078 2178 988  HOH   HOH A . 
V 6 HOH   1079 2179 938  HOH   HOH A . 
V 6 HOH   1080 2180 59   HOH   HOH A . 
V 6 HOH   1081 2181 803  HOH   HOH A . 
V 6 HOH   1082 2182 1154 HOH   HOH A . 
V 6 HOH   1083 2183 800  HOH   HOH A . 
V 6 HOH   1084 2184 1044 HOH   HOH A . 
V 6 HOH   1085 2185 1177 HOH   HOH A . 
V 6 HOH   1086 2186 580  HOH   HOH A . 
V 6 HOH   1087 2187 1147 HOH   HOH A . 
V 6 HOH   1088 2188 417  HOH   HOH A . 
V 6 HOH   1089 2189 1032 HOH   HOH A . 
V 6 HOH   1090 2190 495  HOH   HOH A . 
V 6 HOH   1091 2191 1125 HOH   HOH A . 
V 6 HOH   1092 2192 525  HOH   HOH A . 
V 6 HOH   1093 2193 534  HOH   HOH A . 
V 6 HOH   1094 2194 985  HOH   HOH A . 
V 6 HOH   1095 2195 595  HOH   HOH A . 
V 6 HOH   1096 2196 801  HOH   HOH A . 
V 6 HOH   1097 2197 1138 HOH   HOH A . 
V 6 HOH   1098 2198 1223 HOH   HOH A . 
V 6 HOH   1099 2199 1148 HOH   HOH A . 
V 6 HOH   1100 2200 256  HOH   HOH A . 
V 6 HOH   1101 2201 839  HOH   HOH A . 
V 6 HOH   1102 2202 547  HOH   HOH A . 
V 6 HOH   1103 2203 722  HOH   HOH A . 
V 6 HOH   1104 2204 1023 HOH   HOH A . 
V 6 HOH   1105 2205 995  HOH   HOH A . 
V 6 HOH   1106 2206 1182 HOH   HOH A . 
V 6 HOH   1107 2207 1168 HOH   HOH A . 
V 6 HOH   1108 2208 325  HOH   HOH A . 
V 6 HOH   1109 2209 736  HOH   HOH A . 
V 6 HOH   1110 2210 1131 HOH   HOH A . 
V 6 HOH   1111 2211 277  HOH   HOH A . 
V 6 HOH   1112 2212 344  HOH   HOH A . 
V 6 HOH   1113 2213 1014 HOH   HOH A . 
V 6 HOH   1114 2214 604  HOH   HOH A . 
V 6 HOH   1115 2215 759  HOH   HOH A . 
V 6 HOH   1116 2216 735  HOH   HOH A . 
V 6 HOH   1117 2217 1136 HOH   HOH A . 
V 6 HOH   1118 2218 1156 HOH   HOH A . 
V 6 HOH   1119 2219 560  HOH   HOH A . 
V 6 HOH   1120 2220 843  HOH   HOH A . 
V 6 HOH   1121 2221 1012 HOH   HOH A . 
V 6 HOH   1122 2222 1002 HOH   HOH A . 
V 6 HOH   1123 2223 401  HOH   HOH A . 
V 6 HOH   1124 2224 427  HOH   HOH A . 
V 6 HOH   1125 2225 1102 HOH   HOH A . 
V 6 HOH   1126 2226 1071 HOH   HOH A . 
V 6 HOH   1127 2227 957  HOH   HOH A . 
V 6 HOH   1128 2228 794  HOH   HOH A . 
V 6 HOH   1129 2229 651  HOH   HOH A . 
V 6 HOH   1130 2230 840  HOH   HOH A . 
V 6 HOH   1131 2231 1100 HOH   HOH A . 
V 6 HOH   1132 2232 626  HOH   HOH A . 
V 6 HOH   1133 2233 824  HOH   HOH A . 
V 6 HOH   1134 2234 577  HOH   HOH A . 
V 6 HOH   1135 2235 220  HOH   HOH A . 
V 6 HOH   1136 2236 461  HOH   HOH A . 
V 6 HOH   1137 2237 701  HOH   HOH A . 
V 6 HOH   1138 2238 776  HOH   HOH A . 
V 6 HOH   1139 2239 1143 HOH   HOH A . 
V 6 HOH   1140 2240 954  HOH   HOH A . 
V 6 HOH   1141 2241 576  HOH   HOH A . 
V 6 HOH   1142 2242 1029 HOH   HOH A . 
V 6 HOH   1143 2243 1163 HOH   HOH A . 
V 6 HOH   1144 2244 1159 HOH   HOH A . 
V 6 HOH   1145 2245 944  HOH   HOH A . 
V 6 HOH   1146 2246 1117 HOH   HOH A . 
V 6 HOH   1147 2247 994  HOH   HOH A . 
V 6 HOH   1148 2248 962  HOH   HOH A . 
V 6 HOH   1149 2249 1206 HOH   HOH A . 
V 6 HOH   1150 2250 811  HOH   HOH A . 
V 6 HOH   1151 2251 948  HOH   HOH A . 
V 6 HOH   1152 2252 1025 HOH   HOH A . 
V 6 HOH   1153 2253 808  HOH   HOH A . 
V 6 HOH   1154 2254 1164 HOH   HOH A . 
V 6 HOH   1155 2255 1109 HOH   HOH A . 
V 6 HOH   1156 2256 1037 HOH   HOH A . 
V 6 HOH   1157 2257 998  HOH   HOH A . 
V 6 HOH   1158 2258 769  HOH   HOH A . 
V 6 HOH   1159 2259 1132 HOH   HOH A . 
V 6 HOH   1160 2260 933  HOH   HOH A . 
V 6 HOH   1161 2261 300  HOH   HOH A . 
V 6 HOH   1162 2262 1048 HOH   HOH A . 
V 6 HOH   1163 2263 646  HOH   HOH A . 
V 6 HOH   1164 2264 1167 HOH   HOH A . 
V 6 HOH   1165 2265 796  HOH   HOH A . 
V 6 HOH   1166 2266 1227 HOH   HOH A . 
V 6 HOH   1167 2267 1218 HOH   HOH A . 
V 6 HOH   1168 2268 1220 HOH   HOH A . 
V 6 HOH   1169 2269 666  HOH   HOH A . 
V 6 HOH   1170 2270 925  HOH   HOH A . 
V 6 HOH   1171 2271 452  HOH   HOH A . 
V 6 HOH   1172 2272 648  HOH   HOH A . 
V 6 HOH   1173 2273 1030 HOH   HOH A . 
V 6 HOH   1174 2274 1096 HOH   HOH A . 
V 6 HOH   1175 2275 1127 HOH   HOH A . 
V 6 HOH   1176 2276 1152 HOH   HOH A . 
V 6 HOH   1177 2277 993  HOH   HOH A . 
V 6 HOH   1178 2278 955  HOH   HOH A . 
V 6 HOH   1179 2279 618  HOH   HOH A . 
V 6 HOH   1180 2280 230  HOH   HOH A . 
V 6 HOH   1181 2281 763  HOH   HOH A . 
V 6 HOH   1182 2282 1051 HOH   HOH A . 
V 6 HOH   1183 2283 391  HOH   HOH A . 
V 6 HOH   1184 2284 1060 HOH   HOH A . 
V 6 HOH   1185 2285 1072 HOH   HOH A . 
V 6 HOH   1186 2286 975  HOH   HOH A . 
V 6 HOH   1187 2287 1141 HOH   HOH A . 
V 6 HOH   1188 2288 834  HOH   HOH A . 
V 6 HOH   1189 2289 1065 HOH   HOH A . 
V 6 HOH   1190 2290 741  HOH   HOH A . 
V 6 HOH   1191 2291 1166 HOH   HOH A . 
V 6 HOH   1192 2292 559  HOH   HOH A . 
V 6 HOH   1193 2293 659  HOH   HOH A . 
V 6 HOH   1194 2294 1074 HOH   HOH A . 
V 6 HOH   1195 2295 1178 HOH   HOH A . 
V 6 HOH   1196 2296 746  HOH   HOH A . 
V 6 HOH   1197 2297 1068 HOH   HOH A . 
V 6 HOH   1198 2298 931  HOH   HOH A . 
V 6 HOH   1199 2299 951  HOH   HOH A . 
V 6 HOH   1200 2300 554  HOH   HOH A . 
V 6 HOH   1201 2301 1078 HOH   HOH A . 
V 6 HOH   1202 2302 1073 HOH   HOH A . 
V 6 HOH   1203 2303 750  HOH   HOH A . 
V 6 HOH   1204 2304 655  HOH   HOH A . 
V 6 HOH   1205 2305 743  HOH   HOH A . 
V 6 HOH   1206 2306 1001 HOH   HOH A . 
V 6 HOH   1207 2307 1145 HOH   HOH A . 
V 6 HOH   1208 2308 748  HOH   HOH A . 
V 6 HOH   1209 2309 327  HOH   HOH A . 
V 6 HOH   1210 2310 947  HOH   HOH A . 
V 6 HOH   1211 2311 806  HOH   HOH A . 
V 6 HOH   1212 2312 589  HOH   HOH A . 
V 6 HOH   1213 2313 980  HOH   HOH A . 
V 6 HOH   1214 2314 786  HOH   HOH A . 
V 6 HOH   1215 2315 1169 HOH   HOH A . 
V 6 HOH   1216 2316 1092 HOH   HOH A . 
V 6 HOH   1217 2317 989  HOH   HOH A . 
V 6 HOH   1218 2318 639  HOH   HOH A . 
V 6 HOH   1219 2319 239  HOH   HOH A . 
V 6 HOH   1220 2320 1039 HOH   HOH A . 
V 6 HOH   1221 2321 764  HOH   HOH A . 
V 6 HOH   1222 2322 616  HOH   HOH A . 
V 6 HOH   1223 2323 795  HOH   HOH A . 
V 6 HOH   1224 2324 1186 HOH   HOH A . 
V 6 HOH   1225 2325 671  HOH   HOH A . 
V 6 HOH   1226 2326 749  HOH   HOH A . 
V 6 HOH   1227 2327 723  HOH   HOH A . 
V 6 HOH   1228 2328 1016 HOH   HOH A . 
V 6 HOH   1229 2329 705  HOH   HOH A . 
V 6 HOH   1230 2330 1093 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ARG 114 ? CG  ? A ARG 114 CG  
2 1 Y 1 A ARG 114 ? CD  ? A ARG 114 CD  
3 1 Y 1 A ARG 114 ? NE  ? A ARG 114 NE  
4 1 Y 1 A ARG 114 ? CZ  ? A ARG 114 CZ  
5 1 Y 1 A ARG 114 ? NH1 ? A ARG 114 NH1 
6 1 Y 1 A ARG 114 ? NH2 ? A ARG 114 NH2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? '2.11.8 (23-JAN-2024)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                      3 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GK6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     112.728 
_cell.length_a_esd                 ? 
_cell.length_b                     140.610 
_cell.length_b_esd                 ? 
_cell.length_c                     57.542 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GK6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GK6 
_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             2.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.16 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '25% w/v PEG 1500, 0.1 M MMT buffer pH 5.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-10-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.91587 
_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                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.91587 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GK6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.327 
_reflns.d_resolution_low                               58 
_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                                     199707 
_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                           94.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.9 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.33 
_reflns_shell.d_res_low                                     1.37 
_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                             9980 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.657 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.09210 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            -0.30100 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            0.20900 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               21.80 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.959 
_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                                 9GK6 
_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                            1.327 
_refine.ls_d_res_low                             57.54 
_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                     199707 
_refine.ls_number_reflns_R_free                  10035 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.6 
_refine.ls_percent_reflns_R_free                 5.020 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1729 
_refine.ls_R_factor_R_free                       0.1898 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1720 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.052 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.056 
_refine.pdbx_overall_SU_R_Blow_DPI               0.056 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.052 
_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_analyze.entry_id                        9GK6 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.327 
_refine_hist.d_res_low                        57.54 
_refine_hist.number_atoms_solvent             1230 
_refine_hist.number_atoms_total               8233 
_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        6895 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         108 
_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' ? 0.012 ? 7339 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.15  ? 9954 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2592 ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 1253 ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 7339 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 4.50  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 14.58 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 945  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 8719 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.33 
_refine_ls_shell.d_res_low                        1.35 
_refine_ls_shell.number_reflns_all                3995 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             217 
_refine_ls_shell.number_reflns_R_work             3778 
_refine_ls_shell.percent_reflns_obs               41.53 
_refine_ls_shell.percent_reflns_R_free            5.43 
_refine_ls_shell.R_factor_all                     0.2528 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2521 
_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   51 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2650 
# 
_struct.entry_id                     9GK6 
_struct.title                        
'ERAP1 in complex with 1-[2-(6-chloro-3-oxo-3,4-dihydro-2H-1,4-benzothiazin-4-yl)acetamido]cyclohexane-1-carboxylic acid' 
_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        9GK6 
_struct_keywords.text            'ERAP1, PEPTIDE BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'PEPTIDE BINDING 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 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 4 ? 
S N N 4 ? 
T N N 4 ? 
U N N 5 ? 
V N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ERAP1_HUMAN Q9NZ08 ? 1 
;MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTT
KVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFH
GFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTV
KMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAME
NWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYF
FGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWD
SMASI
;
1   
2 UNP ERAP1_HUMAN Q9NZ08 ? 1 
;GVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPE
EVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPV
FQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRK
WKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFP
QILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIE
TIEENIGWMDKNFDKIRVWLQSEKLERM
;
514 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GK6 A 1   ? 485 ? Q9NZ08 1   ? 485 ? 1   485 
2 2 9GK6 A 489 ? 916 ? Q9NZ08 514 ? 941 ? 514 941 
# 
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 9GK6 GLN A 70  ? UNP Q9NZ08 ASN 70  conflict         70  1  
1 9GK6 GLN A 154 ? UNP Q9NZ08 ASN 154 conflict         154 2  
1 9GK6 GLN A 414 ? UNP Q9NZ08 ASN 414 conflict         414 3  
1 9GK6 GLY A 486 ? UNP Q9NZ08 ?   ?   linker           511 4  
1 9GK6 SER A 487 ? UNP Q9NZ08 ?   ?   linker           512 5  
1 9GK6 GLY A 488 ? UNP Q9NZ08 ?   ?   linker           513 6  
2 9GK6 ARG A 503 ? UNP Q9NZ08 LYS 528 conflict         528 7  
2 9GK6 GLN A 735 ? UNP Q9NZ08 ASN 760 conflict         760 8  
2 9GK6 GLU A 917 ? UNP Q9NZ08 ?   ?   'expression tag' 942 9  
2 9GK6 ASN A 918 ? UNP Q9NZ08 ?   ?   'expression tag' 943 10 
2 9GK6 LEU A 919 ? UNP Q9NZ08 ?   ?   'expression tag' 944 11 
2 9GK6 TYR A 920 ? UNP Q9NZ08 ?   ?   'expression tag' 945 12 
2 9GK6 PHE A 921 ? UNP Q9NZ08 ?   ?   'expression tag' 946 13 
2 9GK6 GLN A 922 ? UNP Q9NZ08 ?   ?   'expression tag' 947 14 
# 
_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,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 186 ? ALA A 190 ? ALA A 186 ALA A 190 5 ? 5  
HELX_P HELX_P2  AA2 SER A 243 ? VAL A 247 ? SER A 243 VAL A 247 5 ? 5  
HELX_P HELX_P3  AA3 VAL A 272 ? GLN A 278 ? VAL A 272 GLN A 278 5 ? 7  
HELX_P HELX_P4  AA4 ALA A 279 ? SER A 298 ? ALA A 279 SER A 298 1 ? 20 
HELX_P HELX_P5  AA5 SER A 330 ? LEU A 332 ? SER A 330 LEU A 332 5 ? 3  
HELX_P HELX_P6  AA6 SER A 340 ? HIS A 357 ? SER A 340 HIS A 357 1 ? 18 
HELX_P HELX_P7  AA7 TRP A 368 ? ASP A 371 ? TRP A 368 ASP A 371 5 ? 4  
HELX_P HELX_P8  AA8 LEU A 372 ? HIS A 391 ? LEU A 372 HIS A 391 1 ? 20 
HELX_P HELX_P9  AA9 PRO A 392 ? ASP A 398 ? PRO A 392 ASP A 398 5 ? 7  
HELX_P HELX_P10 AB1 TYR A 399 ? ALA A 412 ? TYR A 399 ALA A 412 1 ? 14 
HELX_P HELX_P11 AB2 ASN A 425 ? GLU A 431 ? ASN A 425 GLU A 431 1 ? 7  
HELX_P HELX_P12 AB3 ASP A 434 ? SER A 453 ? ASP A 434 SER A 453 1 ? 20 
HELX_P HELX_P13 AB4 SER A 453 ? HIS A 468 ? SER A 453 HIS A 468 1 ? 16 
HELX_P HELX_P14 AB5 LYS A 474 ? SER A 484 ? LYS A 474 SER A 484 1 ? 11 
HELX_P HELX_P15 AB6 VAL A 492 ? LEU A 501 ? VAL A 517 LEU A 526 1 ? 10 
HELX_P HELX_P16 AB7 VAL A 577 ? ASN A 580 ? VAL A 602 ASN A 605 5 ? 4  
HELX_P HELX_P17 AB8 ASP A 590 ? HIS A 603 ? ASP A 615 HIS A 628 1 ? 14 
HELX_P HELX_P18 AB9 THR A 604 ? VAL A 606 ? THR A 629 VAL A 631 5 ? 3  
HELX_P HELX_P19 AC1 SER A 607 ? ILE A 624 ? SER A 632 ILE A 649 1 ? 18 
HELX_P HELX_P20 AC2 SER A 628 ? LEU A 637 ? SER A 653 LEU A 662 1 ? 10 
HELX_P HELX_P21 AC3 TYR A 638 ? GLU A 642 ? TYR A 663 GLU A 667 5 ? 5  
HELX_P HELX_P22 AC4 GLU A 644 ? GLU A 663 ? GLU A 669 GLU A 688 1 ? 20 
HELX_P HELX_P23 AC5 MET A 667 ? GLN A 689 ? MET A 692 GLN A 714 1 ? 23 
HELX_P HELX_P24 AC6 SER A 696 ? HIS A 713 ? SER A 721 HIS A 738 1 ? 18 
HELX_P HELX_P25 AC7 TYR A 715 ? SER A 732 ? TYR A 740 SER A 757 1 ? 18 
HELX_P HELX_P26 AC8 PRO A 739 ? ALA A 751 ? PRO A 764 ALA A 776 1 ? 13 
HELX_P HELX_P27 AC9 SER A 753 ? GLN A 765 ? SER A 778 GLN A 790 1 ? 13 
HELX_P HELX_P28 AD1 SER A 769 ? CYS A 781 ? SER A 794 CYS A 806 1 ? 13 
HELX_P HELX_P29 AD2 ASN A 785 ? GLY A 799 ? ASN A 810 GLY A 824 1 ? 15 
HELX_P HELX_P30 AD3 LYS A 803 ? GLN A 805 ? LYS A 828 GLN A 830 5 ? 3  
HELX_P HELX_P31 AD4 GLU A 806 ? ARG A 816 ? GLU A 831 ARG A 841 1 ? 11 
HELX_P HELX_P32 AD5 GLY A 820 ? GLU A 840 ? GLY A 845 GLU A 865 1 ? 21 
HELX_P HELX_P33 AD6 SER A 843 ? ASN A 855 ? SER A 868 ASN A 880 1 ? 13 
HELX_P HELX_P34 AD7 THR A 859 ? LEU A 873 ? THR A 884 LEU A 898 1 ? 15 
HELX_P HELX_P35 AD8 LYS A 874 ? GLY A 877 ? LYS A 899 GLY A 902 5 ? 4  
HELX_P HELX_P36 AD9 LEU A 880 ? SER A 910 ? LEU A 905 SER A 935 1 ? 31 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 404 SG  ? ? ? 1_555 A CYS 443 SG ? ? A CYS 404  A CYS 443  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc1 metalc ? ? A HIS 353 NE2 ? ? ? 1_555 B ZN  .   ZN ? ? A HIS 353  A ZN  1001 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc2 metalc ? ? A HIS 357 NE2 ? ? ? 1_555 B ZN  .   ZN ? ? A HIS 357  A ZN  1001 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc3 metalc ? ? A GLU 376 OE1 ? ? ? 1_555 B ZN  .   ZN ? ? A GLU 376  A ZN  1001 1_555 ? ? ? ? ? ? ? 1.953 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C MLT .   O4 ? ? A ZN  1001 A MLT 1002 1_555 ? ? ? ? ? ? ? 2.682 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C MLT .   O5 ? ? A ZN  1001 A MLT 1002 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 353 ? A HIS 353  ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 NE2 ? A HIS 357 ? A HIS 357  ? 1_555 102.4 ? 
2  NE2 ? A HIS 353 ? A HIS 353  ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 OE1 ? A GLU 376 ? A GLU 376  ? 1_555 111.8 ? 
3  NE2 ? A HIS 357 ? A HIS 357  ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 OE1 ? A GLU 376 ? A GLU 376  ? 1_555 102.7 ? 
4  NE2 ? A HIS 353 ? A HIS 353  ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 O4  ? C MLT .   ? A MLT 1002 ? 1_555 85.0  ? 
5  NE2 ? A HIS 357 ? A HIS 357  ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 O4  ? C MLT .   ? A MLT 1002 ? 1_555 95.6  ? 
6  OE1 ? A GLU 376 ? A GLU 376  ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 O4  ? C MLT .   ? A MLT 1002 ? 1_555 151.4 ? 
7  NE2 ? A HIS 353 ? A HIS 353  ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 O5  ? C MLT .   ? A MLT 1002 ? 1_555 104.6 ? 
8  NE2 ? A HIS 357 ? A HIS 357  ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 O5  ? C MLT .   ? A MLT 1002 ? 1_555 135.7 ? 
9  OE1 ? A GLU 376 ? A GLU 376  ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 O5  ? C MLT .   ? A MLT 1002 ? 1_555 99.0  ? 
10 O4  ? C MLT .   ? A MLT 1002 ? 1_555 ZN ? B ZN . ? A ZN 1001 ? 1_555 O5  ? C MLT .   ? A MLT 1002 ? 1_555 53.2  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       404 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      443 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        404 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       443 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           183 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            183 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    184 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     184 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.29 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 2 ? 
AA7 ? 4 ? 
AA8 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 116 ? PRO A 119 ? SER A 116 PRO A 119 
AA1 2 GLN A 101 ? LYS A 109 ? GLN A 101 LYS A 109 
AA1 3 TYR A 145 ? GLN A 154 ? TYR A 145 GLN A 154 
AA1 4 THR A 75  ? ALA A 86  ? THR A 75  ALA A 86  
AA1 5 VAL A 58  ? ALA A 69  ? VAL A 58  ALA A 69  
AA1 6 SER A 202 ? ARG A 209 ? SER A 202 ARG A 209 
AA1 7 LEU A 231 ? PHE A 236 ? LEU A 231 PHE A 236 
AA1 8 LEU A 221 ? VAL A 227 ? LEU A 221 VAL A 227 
AA2 1 THR A 92  ? HIS A 96  ? THR A 92  HIS A 96  
AA2 2 GLN A 130 ? LEU A 134 ? GLN A 130 LEU A 134 
AA2 3 GLN A 121 ? HIS A 125 ? GLN A 121 HIS A 125 
AA3 1 GLY A 161 ? ARG A 168 ? GLY A 161 ARG A 168 
AA3 2 LEU A 174 ? GLN A 181 ? LEU A 174 GLN A 181 
AA4 1 LEU A 214 ? SER A 217 ? LEU A 214 SER A 217 
AA4 2 PHE A 249 ? SER A 252 ? PHE A 249 SER A 252 
AA5 1 GLU A 255 ? ILE A 260 ? GLU A 255 ILE A 260 
AA5 2 LYS A 266 ? ALA A 271 ? LYS A 266 ALA A 271 
AA5 3 LYS A 305 ? ILE A 311 ? LYS A 305 ILE A 311 
AA5 4 LEU A 324 ? ARG A 328 ? LEU A 324 ARG A 328 
AA5 5 ALA A 318 ? MET A 319 ? ALA A 318 MET A 319 
AA6 1 VAL A 364 ? MET A 366 ? VAL A 364 MET A 366 
AA6 2 LYS A 471 ? THR A 473 ? LYS A 471 THR A 473 
AA7 1 THR A 561 ? ILE A 565 ? THR A 586 ILE A 590 
AA7 2 ASN A 516 ? TYR A 524 ? ASN A 541 TYR A 549 
AA7 3 PHE A 505 ? ARG A 513 ? PHE A 530 ARG A 538 
AA7 4 ILE A 584 ? TYR A 587 ? ILE A 609 TYR A 612 
AA8 1 SER A 549 ? LEU A 557 ? SER A 574 LEU A 582 
AA8 2 VAL A 540 ? THR A 546 ? VAL A 565 THR A 571 
AA8 3 ILE A 573 ? PHE A 575 ? ILE A 598 PHE A 600 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 118 ? O GLU A 118 N LEU A 107 ? N LEU A 107 
AA1 2 3 N ARG A 108 ? N ARG A 108 O THR A 146 ? O THR A 146 
AA1 3 4 O TYR A 145 ? O TYR A 145 N ILE A 84  ? N ILE A 84  
AA1 4 5 O TRP A 77  ? O TRP A 77  N HIS A 68  ? N HIS A 68  
AA1 5 6 N TYR A 63  ? N TYR A 63  O SER A 204 ? O SER A 204 
AA1 6 7 N ILE A 207 ? N ILE A 207 O ASP A 234 ? O ASP A 234 
AA1 7 8 O HIS A 235 ? O HIS A 235 N LYS A 223 ? N LYS A 223 
AA2 1 2 N ILE A 93  ? N ILE A 93  O LEU A 133 ? O LEU A 133 
AA2 2 3 O GLN A 130 ? O GLN A 130 N HIS A 125 ? N HIS A 125 
AA3 1 2 N SER A 165 ? N SER A 165 O LEU A 177 ? O LEU A 177 
AA4 1 2 N LEU A 214 ? N LEU A 214 O SER A 252 ? O SER A 252 
AA5 1 2 N LYS A 259 ? N LYS A 259 O VAL A 267 ? O VAL A 267 
AA5 2 3 N TYR A 270 ? N TYR A 270 O ALA A 310 ? O ALA A 310 
AA5 3 4 N ILE A 311 ? N ILE A 311 O TYR A 327 ? O TYR A 327 
AA5 4 5 O THR A 326 ? O THR A 326 N MET A 319 ? N MET A 319 
AA6 1 2 N THR A 365 ? N THR A 365 O THR A 473 ? O THR A 473 
AA7 1 2 O LEU A 564 ? O LEU A 589 N VAL A 517 ? N VAL A 542 
AA7 2 3 O GLU A 522 ? O GLU A 547 N LEU A 507 ? N LEU A 532 
AA7 3 4 N ILE A 510 ? N ILE A 535 O HIS A 586 ? O HIS A 611 
AA8 1 2 O LEU A 557 ? O LEU A 582 N VAL A 540 ? N VAL A 565 
AA8 2 3 N ILE A 545 ? N ILE A 570 O LYS A 574 ? O LYS A 599 
# 
_pdbx_entry_details.entry_id                   9GK6 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O A HOH 1118 ? ? O A HOH 1133 ? ? 1.85 
2  1 O A HOH 1107 ? ? O A HOH 1188 ? ? 1.89 
3  1 O A HOH 1124 ? ? O A HOH 2013 ? ? 1.99 
4  1 O A HOH 1192 ? ? O A HOH 1228 ? ? 2.00 
5  1 O A HOH 1221 ? ? O A HOH 1918 ? ? 2.03 
6  1 O A HOH 1185 ? ? O A HOH 1244 ? ? 2.06 
7  1 O A HOH 1244 ? ? O A HOH 1583 ? ? 2.07 
8  1 O A HOH 1270 ? ? O A HOH 2301 ? ? 2.08 
9  1 O A HOH 1147 ? ? O A HOH 1841 ? ? 2.09 
10 1 O A HOH 1173 ? ? O A HOH 2107 ? ? 2.11 
11 1 O A HOH 1141 ? ? O A HOH 1960 ? ? 2.12 
12 1 O A HOH 2036 ? ? O A HOH 2213 ? ? 2.13 
13 1 O A HOH 1270 ? ? O A HOH 1654 ? ? 2.14 
14 1 O A HOH 1486 ? ? O A HOH 1657 ? ? 2.16 
# 
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 SER A 316 ? ? -79.93  -162.61 
2  1 LEU A 332 ? ? -132.64 -36.49  
3  1 GLU A 424 ? ? -131.90 -54.29  
4  1 SER A 453 ? ? 97.46   149.84  
5  1 TYR A 561 ? ? -35.49  135.48  
6  1 ASN A 601 ? ? 69.26   67.84   
7  1 ASP A 614 ? ? 60.00   -128.51 
8  1 LEU A 761 ? ? -39.99  114.90  
9  1 GLU A 865 ? ? 85.60   140.62  
10 1 SER A 883 ? ? -151.14 31.22   
11 1 LYS A 899 ? ? 50.07   -119.88 
12 1 ASN A 901 ? ? -94.03  35.70   
# 
_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         30.6968 
_pdbx_refine_tls.origin_y         32.9281 
_pdbx_refine_tls.origin_z         12.2069 
_pdbx_refine_tls.T[1][1]          -0.0171 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0101 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0042 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0096 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0141 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0084 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.1221 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0737 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0918 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.1667 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0935 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.1812 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0081 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0338 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0149 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0261 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0123 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0004 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0049 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0183 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0204 
_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   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2328 ? 6.04 . 
2 1 O ? A HOH 2329 ? 6.07 . 
3 1 O ? A HOH 2330 ? 6.83 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A VAL 2   ? A VAL 2   
3  1 Y 1 A PHE 3   ? A PHE 3   
4  1 Y 1 A LEU 4   ? A LEU 4   
5  1 Y 1 A PRO 5   ? A PRO 5   
6  1 Y 1 A LEU 6   ? A LEU 6   
7  1 Y 1 A LYS 7   ? A LYS 7   
8  1 Y 1 A TRP 8   ? A TRP 8   
9  1 Y 1 A SER 9   ? A SER 9   
10 1 Y 1 A LEU 10  ? A LEU 10  
11 1 Y 1 A ALA 11  ? A ALA 11  
12 1 Y 1 A THR 12  ? A THR 12  
13 1 Y 1 A MET 13  ? A MET 13  
14 1 Y 1 A SER 14  ? A SER 14  
15 1 Y 1 A PHE 15  ? A PHE 15  
16 1 Y 1 A LEU 16  ? A LEU 16  
17 1 Y 1 A LEU 17  ? A LEU 17  
18 1 Y 1 A SER 18  ? A SER 18  
19 1 Y 1 A SER 19  ? A SER 19  
20 1 Y 1 A LEU 20  ? A LEU 20  
21 1 Y 1 A LEU 21  ? A LEU 21  
22 1 Y 1 A ALA 22  ? A ALA 22  
23 1 Y 1 A LEU 23  ? A LEU 23  
24 1 Y 1 A LEU 24  ? A LEU 24  
25 1 Y 1 A THR 25  ? A THR 25  
26 1 Y 1 A VAL 26  ? A VAL 26  
27 1 Y 1 A SER 27  ? A SER 27  
28 1 Y 1 A THR 28  ? A THR 28  
29 1 Y 1 A PRO 29  ? A PRO 29  
30 1 Y 1 A SER 30  ? A SER 30  
31 1 Y 1 A TRP 31  ? A TRP 31  
32 1 Y 1 A CYS 32  ? A CYS 32  
33 1 Y 1 A GLN 33  ? A GLN 33  
34 1 Y 1 A SER 34  ? A SER 34  
35 1 Y 1 A THR 35  ? A THR 35  
36 1 Y 1 A GLU 36  ? A GLU 36  
37 1 Y 1 A ALA 37  ? A ALA 37  
38 1 Y 1 A SER 38  ? A SER 38  
39 1 Y 1 A PRO 39  ? A PRO 39  
40 1 Y 1 A LYS 40  ? A LYS 40  
41 1 Y 1 A ARG 41  ? A ARG 41  
42 1 Y 1 A SER 42  ? A SER 42  
43 1 Y 1 A ASP 43  ? A ASP 43  
44 1 Y 1 A GLY 44  ? A GLY 44  
45 1 Y 1 A ALA 111 ? A ALA 111 
46 1 Y 1 A GLY 112 ? A GLY 112 
47 1 Y 1 A GLU 113 ? A GLU 113 
48 1 Y 1 A GLY 511 ? A GLY 486 
49 1 Y 1 A SER 512 ? A SER 487 
50 1 Y 1 A SER 553 ? A SER 528 
51 1 Y 1 A ASP 554 ? A ASP 529 
52 1 Y 1 A GLY 555 ? A GLY 530 
53 1 Y 1 A ALA 556 ? A ALA 531 
54 1 Y 1 A PRO 557 ? A PRO 532 
55 1 Y 1 A ASP 558 ? A ASP 533 
56 1 Y 1 A THR 559 ? A THR 534 
57 1 Y 1 A GLU 936 ? A GLU 911 
58 1 Y 1 A LYS 937 ? A LYS 912 
59 1 Y 1 A LEU 938 ? A LEU 913 
60 1 Y 1 A GLU 939 ? A GLU 914 
61 1 Y 1 A ARG 940 ? A ARG 915 
62 1 Y 1 A MET 941 ? A MET 916 
63 1 Y 1 A GLU 942 ? A GLU 917 
64 1 Y 1 A ASN 943 ? A ASN 918 
65 1 Y 1 A LEU 944 ? A LEU 919 
66 1 Y 1 A TYR 945 ? A TYR 920 
67 1 Y 1 A PHE 946 ? A PHE 921 
68 1 Y 1 A GLN 947 ? A GLN 922 
# 
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 
A1IMM N1   N  N N 1   
A1IMM C4   C  N N 2   
A1IMM C5   C  N N 3   
A1IMM C6   C  N N 4   
A1IMM C7   C  N N 5   
A1IMM C8   C  N N 6   
A1IMM C10  C  N N 7   
A1IMM C13  C  Y N 8   
A1IMM C15  C  Y N 9   
A1IMM CL   CL N N 10  
A1IMM C14  C  Y N 11  
A1IMM C12  C  Y N 12  
A1IMM C16  C  Y N 13  
A1IMM C11  C  Y N 14  
A1IMM S    S  N N 15  
A1IMM C9   C  N N 16  
A1IMM O3   O  N N 17  
A1IMM O2   O  N N 18  
A1IMM N    N  N N 19  
A1IMM C1   C  N N 20  
A1IMM C    C  N N 21  
A1IMM O1   O  N N 22  
A1IMM O    O  N N 23  
A1IMM C3   C  N N 24  
A1IMM C2   C  N N 25  
A1IMM H1   H  N N 26  
A1IMM H2   H  N N 27  
A1IMM H3   H  N N 28  
A1IMM H4   H  N N 29  
A1IMM H5   H  N N 30  
A1IMM H6   H  N N 31  
A1IMM H7   H  N N 32  
A1IMM H8   H  N N 33  
A1IMM H9   H  N N 34  
A1IMM H10  H  N N 35  
A1IMM H11  H  N N 36  
A1IMM H12  H  N N 37  
A1IMM H13  H  N N 38  
A1IMM H14  H  N N 39  
A1IMM H15  H  N N 40  
A1IMM H16  H  N N 41  
A1IMM H17  H  N N 42  
A1IMM H18  H  N N 43  
A1IMM H19  H  N N 44  
ALA   N    N  N N 45  
ALA   CA   C  N S 46  
ALA   C    C  N N 47  
ALA   O    O  N N 48  
ALA   CB   C  N N 49  
ALA   OXT  O  N N 50  
ALA   H    H  N N 51  
ALA   H2   H  N N 52  
ALA   HA   H  N N 53  
ALA   HB1  H  N N 54  
ALA   HB2  H  N N 55  
ALA   HB3  H  N N 56  
ALA   HXT  H  N N 57  
ARG   N    N  N N 58  
ARG   CA   C  N S 59  
ARG   C    C  N N 60  
ARG   O    O  N N 61  
ARG   CB   C  N N 62  
ARG   CG   C  N N 63  
ARG   CD   C  N N 64  
ARG   NE   N  N N 65  
ARG   CZ   C  N N 66  
ARG   NH1  N  N N 67  
ARG   NH2  N  N N 68  
ARG   OXT  O  N N 69  
ARG   H    H  N N 70  
ARG   H2   H  N N 71  
ARG   HA   H  N N 72  
ARG   HB2  H  N N 73  
ARG   HB3  H  N N 74  
ARG   HG2  H  N N 75  
ARG   HG3  H  N N 76  
ARG   HD2  H  N N 77  
ARG   HD3  H  N N 78  
ARG   HE   H  N N 79  
ARG   HH11 H  N N 80  
ARG   HH12 H  N N 81  
ARG   HH21 H  N N 82  
ARG   HH22 H  N N 83  
ARG   HXT  H  N N 84  
ASN   N    N  N N 85  
ASN   CA   C  N S 86  
ASN   C    C  N N 87  
ASN   O    O  N N 88  
ASN   CB   C  N N 89  
ASN   CG   C  N N 90  
ASN   OD1  O  N N 91  
ASN   ND2  N  N N 92  
ASN   OXT  O  N N 93  
ASN   H    H  N N 94  
ASN   H2   H  N N 95  
ASN   HA   H  N N 96  
ASN   HB2  H  N N 97  
ASN   HB3  H  N N 98  
ASN   HD21 H  N N 99  
ASN   HD22 H  N N 100 
ASN   HXT  H  N N 101 
ASP   N    N  N N 102 
ASP   CA   C  N S 103 
ASP   C    C  N N 104 
ASP   O    O  N N 105 
ASP   CB   C  N N 106 
ASP   CG   C  N N 107 
ASP   OD1  O  N N 108 
ASP   OD2  O  N N 109 
ASP   OXT  O  N N 110 
ASP   H    H  N N 111 
ASP   H2   H  N N 112 
ASP   HA   H  N N 113 
ASP   HB2  H  N N 114 
ASP   HB3  H  N N 115 
ASP   HD2  H  N N 116 
ASP   HXT  H  N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
EDO   C1   C  N N 132 
EDO   O1   O  N N 133 
EDO   C2   C  N N 134 
EDO   O2   O  N N 135 
EDO   H11  H  N N 136 
EDO   H12  H  N N 137 
EDO   HO1  H  N N 138 
EDO   H21  H  N N 139 
EDO   H22  H  N N 140 
EDO   HO2  H  N N 141 
GLN   N    N  N N 142 
GLN   CA   C  N S 143 
GLN   C    C  N N 144 
GLN   O    O  N N 145 
GLN   CB   C  N N 146 
GLN   CG   C  N N 147 
GLN   CD   C  N N 148 
GLN   OE1  O  N N 149 
GLN   NE2  N  N N 150 
GLN   OXT  O  N N 151 
GLN   H    H  N N 152 
GLN   H2   H  N N 153 
GLN   HA   H  N N 154 
GLN   HB2  H  N N 155 
GLN   HB3  H  N N 156 
GLN   HG2  H  N N 157 
GLN   HG3  H  N N 158 
GLN   HE21 H  N N 159 
GLN   HE22 H  N N 160 
GLN   HXT  H  N N 161 
GLU   N    N  N N 162 
GLU   CA   C  N S 163 
GLU   C    C  N N 164 
GLU   O    O  N N 165 
GLU   CB   C  N N 166 
GLU   CG   C  N N 167 
GLU   CD   C  N N 168 
GLU   OE1  O  N N 169 
GLU   OE2  O  N N 170 
GLU   OXT  O  N N 171 
GLU   H    H  N N 172 
GLU   H2   H  N N 173 
GLU   HA   H  N N 174 
GLU   HB2  H  N N 175 
GLU   HB3  H  N N 176 
GLU   HG2  H  N N 177 
GLU   HG3  H  N N 178 
GLU   HE2  H  N N 179 
GLU   HXT  H  N N 180 
GLY   N    N  N N 181 
GLY   CA   C  N N 182 
GLY   C    C  N N 183 
GLY   O    O  N N 184 
GLY   OXT  O  N N 185 
GLY   H    H  N N 186 
GLY   H2   H  N N 187 
GLY   HA2  H  N N 188 
GLY   HA3  H  N N 189 
GLY   HXT  H  N N 190 
HIS   N    N  N N 191 
HIS   CA   C  N S 192 
HIS   C    C  N N 193 
HIS   O    O  N N 194 
HIS   CB   C  N N 195 
HIS   CG   C  Y N 196 
HIS   ND1  N  Y N 197 
HIS   CD2  C  Y N 198 
HIS   CE1  C  Y N 199 
HIS   NE2  N  Y N 200 
HIS   OXT  O  N N 201 
HIS   H    H  N N 202 
HIS   H2   H  N N 203 
HIS   HA   H  N N 204 
HIS   HB2  H  N N 205 
HIS   HB3  H  N N 206 
HIS   HD1  H  N N 207 
HIS   HD2  H  N N 208 
HIS   HE1  H  N N 209 
HIS   HE2  H  N N 210 
HIS   HXT  H  N N 211 
HOH   O    O  N N 212 
HOH   H1   H  N N 213 
HOH   H2   H  N N 214 
ILE   N    N  N N 215 
ILE   CA   C  N S 216 
ILE   C    C  N N 217 
ILE   O    O  N N 218 
ILE   CB   C  N S 219 
ILE   CG1  C  N N 220 
ILE   CG2  C  N N 221 
ILE   CD1  C  N N 222 
ILE   OXT  O  N N 223 
ILE   H    H  N N 224 
ILE   H2   H  N N 225 
ILE   HA   H  N N 226 
ILE   HB   H  N N 227 
ILE   HG12 H  N N 228 
ILE   HG13 H  N N 229 
ILE   HG21 H  N N 230 
ILE   HG22 H  N N 231 
ILE   HG23 H  N N 232 
ILE   HD11 H  N N 233 
ILE   HD12 H  N N 234 
ILE   HD13 H  N N 235 
ILE   HXT  H  N N 236 
LEU   N    N  N N 237 
LEU   CA   C  N S 238 
LEU   C    C  N N 239 
LEU   O    O  N N 240 
LEU   CB   C  N N 241 
LEU   CG   C  N N 242 
LEU   CD1  C  N N 243 
LEU   CD2  C  N N 244 
LEU   OXT  O  N N 245 
LEU   H    H  N N 246 
LEU   H2   H  N N 247 
LEU   HA   H  N N 248 
LEU   HB2  H  N N 249 
LEU   HB3  H  N N 250 
LEU   HG   H  N N 251 
LEU   HD11 H  N N 252 
LEU   HD12 H  N N 253 
LEU   HD13 H  N N 254 
LEU   HD21 H  N N 255 
LEU   HD22 H  N N 256 
LEU   HD23 H  N N 257 
LEU   HXT  H  N N 258 
LYS   N    N  N N 259 
LYS   CA   C  N S 260 
LYS   C    C  N N 261 
LYS   O    O  N N 262 
LYS   CB   C  N N 263 
LYS   CG   C  N N 264 
LYS   CD   C  N N 265 
LYS   CE   C  N N 266 
LYS   NZ   N  N N 267 
LYS   OXT  O  N N 268 
LYS   H    H  N N 269 
LYS   H2   H  N N 270 
LYS   HA   H  N N 271 
LYS   HB2  H  N N 272 
LYS   HB3  H  N N 273 
LYS   HG2  H  N N 274 
LYS   HG3  H  N N 275 
LYS   HD2  H  N N 276 
LYS   HD3  H  N N 277 
LYS   HE2  H  N N 278 
LYS   HE3  H  N N 279 
LYS   HZ1  H  N N 280 
LYS   HZ2  H  N N 281 
LYS   HZ3  H  N N 282 
LYS   HXT  H  N N 283 
MET   N    N  N N 284 
MET   CA   C  N S 285 
MET   C    C  N N 286 
MET   O    O  N N 287 
MET   CB   C  N N 288 
MET   CG   C  N N 289 
MET   SD   S  N N 290 
MET   CE   C  N N 291 
MET   OXT  O  N N 292 
MET   H    H  N N 293 
MET   H2   H  N N 294 
MET   HA   H  N N 295 
MET   HB2  H  N N 296 
MET   HB3  H  N N 297 
MET   HG2  H  N N 298 
MET   HG3  H  N N 299 
MET   HE1  H  N N 300 
MET   HE2  H  N N 301 
MET   HE3  H  N N 302 
MET   HXT  H  N N 303 
MLT   C1   C  N N 304 
MLT   O1   O  N N 305 
MLT   O2   O  N N 306 
MLT   C2   C  N R 307 
MLT   O3   O  N N 308 
MLT   C3   C  N N 309 
MLT   C4   C  N N 310 
MLT   O4   O  N N 311 
MLT   O5   O  N N 312 
MLT   H2   H  N N 313 
MLT   HO3  H  N N 314 
MLT   H31  H  N N 315 
MLT   H32  H  N N 316 
MLT   HO5  H  N N 317 
MLT   H6   H  N N 318 
PHE   N    N  N N 319 
PHE   CA   C  N S 320 
PHE   C    C  N N 321 
PHE   O    O  N N 322 
PHE   CB   C  N N 323 
PHE   CG   C  Y N 324 
PHE   CD1  C  Y N 325 
PHE   CD2  C  Y N 326 
PHE   CE1  C  Y N 327 
PHE   CE2  C  Y N 328 
PHE   CZ   C  Y N 329 
PHE   OXT  O  N N 330 
PHE   H    H  N N 331 
PHE   H2   H  N N 332 
PHE   HA   H  N N 333 
PHE   HB2  H  N N 334 
PHE   HB3  H  N N 335 
PHE   HD1  H  N N 336 
PHE   HD2  H  N N 337 
PHE   HE1  H  N N 338 
PHE   HE2  H  N N 339 
PHE   HZ   H  N N 340 
PHE   HXT  H  N N 341 
PRO   N    N  N N 342 
PRO   CA   C  N S 343 
PRO   C    C  N N 344 
PRO   O    O  N N 345 
PRO   CB   C  N N 346 
PRO   CG   C  N N 347 
PRO   CD   C  N N 348 
PRO   OXT  O  N N 349 
PRO   H    H  N N 350 
PRO   HA   H  N N 351 
PRO   HB2  H  N N 352 
PRO   HB3  H  N N 353 
PRO   HG2  H  N N 354 
PRO   HG3  H  N N 355 
PRO   HD2  H  N N 356 
PRO   HD3  H  N N 357 
PRO   HXT  H  N N 358 
SER   N    N  N N 359 
SER   CA   C  N S 360 
SER   C    C  N N 361 
SER   O    O  N N 362 
SER   CB   C  N N 363 
SER   OG   O  N N 364 
SER   OXT  O  N N 365 
SER   H    H  N N 366 
SER   H2   H  N N 367 
SER   HA   H  N N 368 
SER   HB2  H  N N 369 
SER   HB3  H  N N 370 
SER   HG   H  N N 371 
SER   HXT  H  N N 372 
THR   N    N  N N 373 
THR   CA   C  N S 374 
THR   C    C  N N 375 
THR   O    O  N N 376 
THR   CB   C  N R 377 
THR   OG1  O  N N 378 
THR   CG2  C  N N 379 
THR   OXT  O  N N 380 
THR   H    H  N N 381 
THR   H2   H  N N 382 
THR   HA   H  N N 383 
THR   HB   H  N N 384 
THR   HG1  H  N N 385 
THR   HG21 H  N N 386 
THR   HG22 H  N N 387 
THR   HG23 H  N N 388 
THR   HXT  H  N N 389 
TRP   N    N  N N 390 
TRP   CA   C  N S 391 
TRP   C    C  N N 392 
TRP   O    O  N N 393 
TRP   CB   C  N N 394 
TRP   CG   C  Y N 395 
TRP   CD1  C  Y N 396 
TRP   CD2  C  Y N 397 
TRP   NE1  N  Y N 398 
TRP   CE2  C  Y N 399 
TRP   CE3  C  Y N 400 
TRP   CZ2  C  Y N 401 
TRP   CZ3  C  Y N 402 
TRP   CH2  C  Y N 403 
TRP   OXT  O  N N 404 
TRP   H    H  N N 405 
TRP   H2   H  N N 406 
TRP   HA   H  N N 407 
TRP   HB2  H  N N 408 
TRP   HB3  H  N N 409 
TRP   HD1  H  N N 410 
TRP   HE1  H  N N 411 
TRP   HE3  H  N N 412 
TRP   HZ2  H  N N 413 
TRP   HZ3  H  N N 414 
TRP   HH2  H  N N 415 
TRP   HXT  H  N N 416 
TYR   N    N  N N 417 
TYR   CA   C  N S 418 
TYR   C    C  N N 419 
TYR   O    O  N N 420 
TYR   CB   C  N N 421 
TYR   CG   C  Y N 422 
TYR   CD1  C  Y N 423 
TYR   CD2  C  Y N 424 
TYR   CE1  C  Y N 425 
TYR   CE2  C  Y N 426 
TYR   CZ   C  Y N 427 
TYR   OH   O  N N 428 
TYR   OXT  O  N N 429 
TYR   H    H  N N 430 
TYR   H2   H  N N 431 
TYR   HA   H  N N 432 
TYR   HB2  H  N N 433 
TYR   HB3  H  N N 434 
TYR   HD1  H  N N 435 
TYR   HD2  H  N N 436 
TYR   HE1  H  N N 437 
TYR   HE2  H  N N 438 
TYR   HH   H  N N 439 
TYR   HXT  H  N N 440 
VAL   N    N  N N 441 
VAL   CA   C  N S 442 
VAL   C    C  N N 443 
VAL   O    O  N N 444 
VAL   CB   C  N N 445 
VAL   CG1  C  N N 446 
VAL   CG2  C  N N 447 
VAL   OXT  O  N N 448 
VAL   H    H  N N 449 
VAL   H2   H  N N 450 
VAL   HA   H  N N 451 
VAL   HB   H  N N 452 
VAL   HG11 H  N N 453 
VAL   HG12 H  N N 454 
VAL   HG13 H  N N 455 
VAL   HG21 H  N N 456 
VAL   HG22 H  N N 457 
VAL   HG23 H  N N 458 
VAL   HXT  H  N N 459 
ZN    ZN   ZN N N 460 
# 
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 
A1IMM CL  C14  sing N N 1   
A1IMM C13 C12  doub Y N 2   
A1IMM C13 C14  sing Y N 3   
A1IMM C12 C11  sing Y N 4   
A1IMM C14 C15  doub Y N 5   
A1IMM C11 C16  doub Y N 6   
A1IMM C11 S    sing N N 7   
A1IMM C15 C16  sing Y N 8   
A1IMM C16 N1   sing N N 9   
A1IMM S   C10  sing N N 10  
A1IMM C5  C4   sing N N 11  
A1IMM C5  C6   sing N N 12  
A1IMM C4  C3   sing N N 13  
A1IMM C6  C1   sing N N 14  
A1IMM N1  C8   sing N N 15  
A1IMM N1  C9   sing N N 16  
A1IMM C10 C9   sing N N 17  
A1IMM C3  C2   sing N N 18  
A1IMM C8  C7   sing N N 19  
A1IMM C9  O3   doub N N 20  
A1IMM C7  N    sing N N 21  
A1IMM C7  O2   doub N N 22  
A1IMM N   C1   sing N N 23  
A1IMM C1  C2   sing N N 24  
A1IMM C1  C    sing N N 25  
A1IMM O1  C    doub N N 26  
A1IMM C   O    sing N N 27  
A1IMM C4  H1   sing N N 28  
A1IMM C4  H2   sing N N 29  
A1IMM C5  H3   sing N N 30  
A1IMM C5  H4   sing N N 31  
A1IMM C6  H5   sing N N 32  
A1IMM C6  H6   sing N N 33  
A1IMM C8  H7   sing N N 34  
A1IMM C8  H8   sing N N 35  
A1IMM C10 H9   sing N N 36  
A1IMM C10 H10  sing N N 37  
A1IMM C13 H11  sing N N 38  
A1IMM C15 H12  sing N N 39  
A1IMM C12 H13  sing N N 40  
A1IMM N   H14  sing N N 41  
A1IMM O   H15  sing N N 42  
A1IMM C3  H16  sing N N 43  
A1IMM C3  H17  sing N N 44  
A1IMM C2  H18  sing N N 45  
A1IMM C2  H19  sing N N 46  
ALA   N   CA   sing N N 47  
ALA   N   H    sing N N 48  
ALA   N   H2   sing N N 49  
ALA   CA  C    sing N N 50  
ALA   CA  CB   sing N N 51  
ALA   CA  HA   sing N N 52  
ALA   C   O    doub N N 53  
ALA   C   OXT  sing N N 54  
ALA   CB  HB1  sing N N 55  
ALA   CB  HB2  sing N N 56  
ALA   CB  HB3  sing N N 57  
ALA   OXT HXT  sing N N 58  
ARG   N   CA   sing N N 59  
ARG   N   H    sing N N 60  
ARG   N   H2   sing N N 61  
ARG   CA  C    sing N N 62  
ARG   CA  CB   sing N N 63  
ARG   CA  HA   sing N N 64  
ARG   C   O    doub N N 65  
ARG   C   OXT  sing N N 66  
ARG   CB  CG   sing N N 67  
ARG   CB  HB2  sing N N 68  
ARG   CB  HB3  sing N N 69  
ARG   CG  CD   sing N N 70  
ARG   CG  HG2  sing N N 71  
ARG   CG  HG3  sing N N 72  
ARG   CD  NE   sing N N 73  
ARG   CD  HD2  sing N N 74  
ARG   CD  HD3  sing N N 75  
ARG   NE  CZ   sing N N 76  
ARG   NE  HE   sing N N 77  
ARG   CZ  NH1  sing N N 78  
ARG   CZ  NH2  doub N N 79  
ARG   NH1 HH11 sing N N 80  
ARG   NH1 HH12 sing N N 81  
ARG   NH2 HH21 sing N N 82  
ARG   NH2 HH22 sing N N 83  
ARG   OXT HXT  sing N N 84  
ASN   N   CA   sing N N 85  
ASN   N   H    sing N N 86  
ASN   N   H2   sing N N 87  
ASN   CA  C    sing N N 88  
ASN   CA  CB   sing N N 89  
ASN   CA  HA   sing N N 90  
ASN   C   O    doub N N 91  
ASN   C   OXT  sing N N 92  
ASN   CB  CG   sing N N 93  
ASN   CB  HB2  sing N N 94  
ASN   CB  HB3  sing N N 95  
ASN   CG  OD1  doub N N 96  
ASN   CG  ND2  sing N N 97  
ASN   ND2 HD21 sing N N 98  
ASN   ND2 HD22 sing N N 99  
ASN   OXT HXT  sing N N 100 
ASP   N   CA   sing N N 101 
ASP   N   H    sing N N 102 
ASP   N   H2   sing N N 103 
ASP   CA  C    sing N N 104 
ASP   CA  CB   sing N N 105 
ASP   CA  HA   sing N N 106 
ASP   C   O    doub N N 107 
ASP   C   OXT  sing N N 108 
ASP   CB  CG   sing N N 109 
ASP   CB  HB2  sing N N 110 
ASP   CB  HB3  sing N N 111 
ASP   CG  OD1  doub N N 112 
ASP   CG  OD2  sing N N 113 
ASP   OD2 HD2  sing N N 114 
ASP   OXT HXT  sing N N 115 
CYS   N   CA   sing N N 116 
CYS   N   H    sing N N 117 
CYS   N   H2   sing N N 118 
CYS   CA  C    sing N N 119 
CYS   CA  CB   sing N N 120 
CYS   CA  HA   sing N N 121 
CYS   C   O    doub N N 122 
CYS   C   OXT  sing N N 123 
CYS   CB  SG   sing N N 124 
CYS   CB  HB2  sing N N 125 
CYS   CB  HB3  sing N N 126 
CYS   SG  HG   sing N N 127 
CYS   OXT HXT  sing N N 128 
EDO   C1  O1   sing N N 129 
EDO   C1  C2   sing N N 130 
EDO   C1  H11  sing N N 131 
EDO   C1  H12  sing N N 132 
EDO   O1  HO1  sing N N 133 
EDO   C2  O2   sing N N 134 
EDO   C2  H21  sing N N 135 
EDO   C2  H22  sing N N 136 
EDO   O2  HO2  sing N N 137 
GLN   N   CA   sing N N 138 
GLN   N   H    sing N N 139 
GLN   N   H2   sing N N 140 
GLN   CA  C    sing N N 141 
GLN   CA  CB   sing N N 142 
GLN   CA  HA   sing N N 143 
GLN   C   O    doub N N 144 
GLN   C   OXT  sing N N 145 
GLN   CB  CG   sing N N 146 
GLN   CB  HB2  sing N N 147 
GLN   CB  HB3  sing N N 148 
GLN   CG  CD   sing N N 149 
GLN   CG  HG2  sing N N 150 
GLN   CG  HG3  sing N N 151 
GLN   CD  OE1  doub N N 152 
GLN   CD  NE2  sing N N 153 
GLN   NE2 HE21 sing N N 154 
GLN   NE2 HE22 sing N N 155 
GLN   OXT HXT  sing N N 156 
GLU   N   CA   sing N N 157 
GLU   N   H    sing N N 158 
GLU   N   H2   sing N N 159 
GLU   CA  C    sing N N 160 
GLU   CA  CB   sing N N 161 
GLU   CA  HA   sing N N 162 
GLU   C   O    doub N N 163 
GLU   C   OXT  sing N N 164 
GLU   CB  CG   sing N N 165 
GLU   CB  HB2  sing N N 166 
GLU   CB  HB3  sing N N 167 
GLU   CG  CD   sing N N 168 
GLU   CG  HG2  sing N N 169 
GLU   CG  HG3  sing N N 170 
GLU   CD  OE1  doub N N 171 
GLU   CD  OE2  sing N N 172 
GLU   OE2 HE2  sing N N 173 
GLU   OXT HXT  sing N N 174 
GLY   N   CA   sing N N 175 
GLY   N   H    sing N N 176 
GLY   N   H2   sing N N 177 
GLY   CA  C    sing N N 178 
GLY   CA  HA2  sing N N 179 
GLY   CA  HA3  sing N N 180 
GLY   C   O    doub N N 181 
GLY   C   OXT  sing N N 182 
GLY   OXT HXT  sing N N 183 
HIS   N   CA   sing N N 184 
HIS   N   H    sing N N 185 
HIS   N   H2   sing N N 186 
HIS   CA  C    sing N N 187 
HIS   CA  CB   sing N N 188 
HIS   CA  HA   sing N N 189 
HIS   C   O    doub N N 190 
HIS   C   OXT  sing N N 191 
HIS   CB  CG   sing N N 192 
HIS   CB  HB2  sing N N 193 
HIS   CB  HB3  sing N N 194 
HIS   CG  ND1  sing Y N 195 
HIS   CG  CD2  doub Y N 196 
HIS   ND1 CE1  doub Y N 197 
HIS   ND1 HD1  sing N N 198 
HIS   CD2 NE2  sing Y N 199 
HIS   CD2 HD2  sing N N 200 
HIS   CE1 NE2  sing Y N 201 
HIS   CE1 HE1  sing N N 202 
HIS   NE2 HE2  sing N N 203 
HIS   OXT HXT  sing N N 204 
HOH   O   H1   sing N N 205 
HOH   O   H2   sing N N 206 
ILE   N   CA   sing N N 207 
ILE   N   H    sing N N 208 
ILE   N   H2   sing N N 209 
ILE   CA  C    sing N N 210 
ILE   CA  CB   sing N N 211 
ILE   CA  HA   sing N N 212 
ILE   C   O    doub N N 213 
ILE   C   OXT  sing N N 214 
ILE   CB  CG1  sing N N 215 
ILE   CB  CG2  sing N N 216 
ILE   CB  HB   sing N N 217 
ILE   CG1 CD1  sing N N 218 
ILE   CG1 HG12 sing N N 219 
ILE   CG1 HG13 sing N N 220 
ILE   CG2 HG21 sing N N 221 
ILE   CG2 HG22 sing N N 222 
ILE   CG2 HG23 sing N N 223 
ILE   CD1 HD11 sing N N 224 
ILE   CD1 HD12 sing N N 225 
ILE   CD1 HD13 sing N N 226 
ILE   OXT HXT  sing N N 227 
LEU   N   CA   sing N N 228 
LEU   N   H    sing N N 229 
LEU   N   H2   sing N N 230 
LEU   CA  C    sing N N 231 
LEU   CA  CB   sing N N 232 
LEU   CA  HA   sing N N 233 
LEU   C   O    doub N N 234 
LEU   C   OXT  sing N N 235 
LEU   CB  CG   sing N N 236 
LEU   CB  HB2  sing N N 237 
LEU   CB  HB3  sing N N 238 
LEU   CG  CD1  sing N N 239 
LEU   CG  CD2  sing N N 240 
LEU   CG  HG   sing N N 241 
LEU   CD1 HD11 sing N N 242 
LEU   CD1 HD12 sing N N 243 
LEU   CD1 HD13 sing N N 244 
LEU   CD2 HD21 sing N N 245 
LEU   CD2 HD22 sing N N 246 
LEU   CD2 HD23 sing N N 247 
LEU   OXT HXT  sing N N 248 
LYS   N   CA   sing N N 249 
LYS   N   H    sing N N 250 
LYS   N   H2   sing N N 251 
LYS   CA  C    sing N N 252 
LYS   CA  CB   sing N N 253 
LYS   CA  HA   sing N N 254 
LYS   C   O    doub N N 255 
LYS   C   OXT  sing N N 256 
LYS   CB  CG   sing N N 257 
LYS   CB  HB2  sing N N 258 
LYS   CB  HB3  sing N N 259 
LYS   CG  CD   sing N N 260 
LYS   CG  HG2  sing N N 261 
LYS   CG  HG3  sing N N 262 
LYS   CD  CE   sing N N 263 
LYS   CD  HD2  sing N N 264 
LYS   CD  HD3  sing N N 265 
LYS   CE  NZ   sing N N 266 
LYS   CE  HE2  sing N N 267 
LYS   CE  HE3  sing N N 268 
LYS   NZ  HZ1  sing N N 269 
LYS   NZ  HZ2  sing N N 270 
LYS   NZ  HZ3  sing N N 271 
LYS   OXT HXT  sing N N 272 
MET   N   CA   sing N N 273 
MET   N   H    sing N N 274 
MET   N   H2   sing N N 275 
MET   CA  C    sing N N 276 
MET   CA  CB   sing N N 277 
MET   CA  HA   sing N N 278 
MET   C   O    doub N N 279 
MET   C   OXT  sing N N 280 
MET   CB  CG   sing N N 281 
MET   CB  HB2  sing N N 282 
MET   CB  HB3  sing N N 283 
MET   CG  SD   sing N N 284 
MET   CG  HG2  sing N N 285 
MET   CG  HG3  sing N N 286 
MET   SD  CE   sing N N 287 
MET   CE  HE1  sing N N 288 
MET   CE  HE2  sing N N 289 
MET   CE  HE3  sing N N 290 
MET   OXT HXT  sing N N 291 
MLT   C1  O1   doub N N 292 
MLT   C1  O2   sing N N 293 
MLT   C1  C2   sing N N 294 
MLT   C2  O3   sing N N 295 
MLT   C2  C3   sing N N 296 
MLT   C2  H2   sing N N 297 
MLT   O3  HO3  sing N N 298 
MLT   C3  C4   sing N N 299 
MLT   C3  H31  sing N N 300 
MLT   C3  H32  sing N N 301 
MLT   C4  O4   doub N N 302 
MLT   C4  O5   sing N N 303 
MLT   O5  HO5  sing N N 304 
MLT   O2  H6   sing N N 305 
PHE   N   CA   sing N N 306 
PHE   N   H    sing N N 307 
PHE   N   H2   sing N N 308 
PHE   CA  C    sing N N 309 
PHE   CA  CB   sing N N 310 
PHE   CA  HA   sing N N 311 
PHE   C   O    doub N N 312 
PHE   C   OXT  sing N N 313 
PHE   CB  CG   sing N N 314 
PHE   CB  HB2  sing N N 315 
PHE   CB  HB3  sing N N 316 
PHE   CG  CD1  doub Y N 317 
PHE   CG  CD2  sing Y N 318 
PHE   CD1 CE1  sing Y N 319 
PHE   CD1 HD1  sing N N 320 
PHE   CD2 CE2  doub Y N 321 
PHE   CD2 HD2  sing N N 322 
PHE   CE1 CZ   doub Y N 323 
PHE   CE1 HE1  sing N N 324 
PHE   CE2 CZ   sing Y N 325 
PHE   CE2 HE2  sing N N 326 
PHE   CZ  HZ   sing N N 327 
PHE   OXT HXT  sing N N 328 
PRO   N   CA   sing N N 329 
PRO   N   CD   sing N N 330 
PRO   N   H    sing N N 331 
PRO   CA  C    sing N N 332 
PRO   CA  CB   sing N N 333 
PRO   CA  HA   sing N N 334 
PRO   C   O    doub N N 335 
PRO   C   OXT  sing N N 336 
PRO   CB  CG   sing N N 337 
PRO   CB  HB2  sing N N 338 
PRO   CB  HB3  sing N N 339 
PRO   CG  CD   sing N N 340 
PRO   CG  HG2  sing N N 341 
PRO   CG  HG3  sing N N 342 
PRO   CD  HD2  sing N N 343 
PRO   CD  HD3  sing N N 344 
PRO   OXT HXT  sing N N 345 
SER   N   CA   sing N N 346 
SER   N   H    sing N N 347 
SER   N   H2   sing N N 348 
SER   CA  C    sing N N 349 
SER   CA  CB   sing N N 350 
SER   CA  HA   sing N N 351 
SER   C   O    doub N N 352 
SER   C   OXT  sing N N 353 
SER   CB  OG   sing N N 354 
SER   CB  HB2  sing N N 355 
SER   CB  HB3  sing N N 356 
SER   OG  HG   sing N N 357 
SER   OXT HXT  sing N N 358 
THR   N   CA   sing N N 359 
THR   N   H    sing N N 360 
THR   N   H2   sing N N 361 
THR   CA  C    sing N N 362 
THR   CA  CB   sing N N 363 
THR   CA  HA   sing N N 364 
THR   C   O    doub N N 365 
THR   C   OXT  sing N N 366 
THR   CB  OG1  sing N N 367 
THR   CB  CG2  sing N N 368 
THR   CB  HB   sing N N 369 
THR   OG1 HG1  sing N N 370 
THR   CG2 HG21 sing N N 371 
THR   CG2 HG22 sing N N 372 
THR   CG2 HG23 sing N N 373 
THR   OXT HXT  sing N N 374 
TRP   N   CA   sing N N 375 
TRP   N   H    sing N N 376 
TRP   N   H2   sing N N 377 
TRP   CA  C    sing N N 378 
TRP   CA  CB   sing N N 379 
TRP   CA  HA   sing N N 380 
TRP   C   O    doub N N 381 
TRP   C   OXT  sing N N 382 
TRP   CB  CG   sing N N 383 
TRP   CB  HB2  sing N N 384 
TRP   CB  HB3  sing N N 385 
TRP   CG  CD1  doub Y N 386 
TRP   CG  CD2  sing Y N 387 
TRP   CD1 NE1  sing Y N 388 
TRP   CD1 HD1  sing N N 389 
TRP   CD2 CE2  doub Y N 390 
TRP   CD2 CE3  sing Y N 391 
TRP   NE1 CE2  sing Y N 392 
TRP   NE1 HE1  sing N N 393 
TRP   CE2 CZ2  sing Y N 394 
TRP   CE3 CZ3  doub Y N 395 
TRP   CE3 HE3  sing N N 396 
TRP   CZ2 CH2  doub Y N 397 
TRP   CZ2 HZ2  sing N N 398 
TRP   CZ3 CH2  sing Y N 399 
TRP   CZ3 HZ3  sing N N 400 
TRP   CH2 HH2  sing N N 401 
TRP   OXT HXT  sing N N 402 
TYR   N   CA   sing N N 403 
TYR   N   H    sing N N 404 
TYR   N   H2   sing N N 405 
TYR   CA  C    sing N N 406 
TYR   CA  CB   sing N N 407 
TYR   CA  HA   sing N N 408 
TYR   C   O    doub N N 409 
TYR   C   OXT  sing N N 410 
TYR   CB  CG   sing N N 411 
TYR   CB  HB2  sing N N 412 
TYR   CB  HB3  sing N N 413 
TYR   CG  CD1  doub Y N 414 
TYR   CG  CD2  sing Y N 415 
TYR   CD1 CE1  sing Y N 416 
TYR   CD1 HD1  sing N N 417 
TYR   CD2 CE2  doub Y N 418 
TYR   CD2 HD2  sing N N 419 
TYR   CE1 CZ   doub Y N 420 
TYR   CE1 HE1  sing N N 421 
TYR   CE2 CZ   sing Y N 422 
TYR   CE2 HE2  sing N N 423 
TYR   CZ  OH   sing N N 424 
TYR   OH  HH   sing N N 425 
TYR   OXT HXT  sing N N 426 
VAL   N   CA   sing N N 427 
VAL   N   H    sing N N 428 
VAL   N   H2   sing N N 429 
VAL   CA  C    sing N N 430 
VAL   CA  CB   sing N N 431 
VAL   CA  HA   sing N N 432 
VAL   C   O    doub N N 433 
VAL   C   OXT  sing N N 434 
VAL   CB  CG1  sing N N 435 
VAL   CB  CG2  sing N N 436 
VAL   CB  HB   sing N N 437 
VAL   CG1 HG11 sing N N 438 
VAL   CG1 HG12 sing N N 439 
VAL   CG1 HG13 sing N N 440 
VAL   CG2 HG21 sing N N 441 
VAL   CG2 HG22 sing N N 442 
VAL   CG2 HG23 sing N N 443 
VAL   OXT HXT  sing N N 444 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9GK6 
_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]   0.008871 
_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]   0.007112 
_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]   0.017379 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
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   . THR   A 1 45  ? 49.948 2.761   38.414  1.00 48.73  ? 45   THR   A N   1 
ATOM   2    C  CA  . THR   A 1 45  ? 50.434 2.527   37.058  1.00 48.63  ? 45   THR   A CA  1 
ATOM   3    C  C   . THR   A 1 45  ? 50.476 3.830   36.262  1.00 47.34  ? 45   THR   A C   1 
ATOM   4    O  O   . THR   A 1 45  ? 49.433 4.456   36.057  1.00 48.16  ? 45   THR   A O   1 
ATOM   5    C  CB  . THR   A 1 45  ? 49.548 1.503   36.332  1.00 50.65  ? 45   THR   A CB  1 
ATOM   6    O  OG1 . THR   A 1 45  ? 49.355 0.352   37.159  1.00 52.52  ? 45   THR   A OG1 1 
ATOM   7    C  CG2 . THR   A 1 45  ? 50.125 1.090   34.982  1.00 51.00  ? 45   THR   A CG2 1 
ATOM   8    N  N   . PRO   A 1 46  ? 51.666 4.234   35.778  1.00 45.25  ? 46   PRO   A N   1 
ATOM   9    C  CA  . PRO   A 1 46  ? 51.755 5.460   34.968  1.00 43.16  ? 46   PRO   A CA  1 
ATOM   10   C  C   . PRO   A 1 46  ? 50.987 5.318   33.649  1.00 39.47  ? 46   PRO   A C   1 
ATOM   11   O  O   . PRO   A 1 46  ? 50.844 4.203   33.119  1.00 40.25  ? 46   PRO   A O   1 
ATOM   12   C  CB  . PRO   A 1 46  ? 53.263 5.612   34.706  1.00 44.83  ? 46   PRO   A CB  1 
ATOM   13   C  CG  . PRO   A 1 46  ? 53.939 4.698   35.704  1.00 46.02  ? 46   PRO   A CG  1 
ATOM   14   C  CD  . PRO   A 1 46  ? 52.978 3.576   35.920  1.00 44.61  ? 46   PRO   A CD  1 
ATOM   15   N  N   . PHE   A 1 47  ? 50.482 6.440   33.117  1.00 34.86  ? 47   PHE   A N   1 
ATOM   16   C  CA  . PHE   A 1 47  ? 49.712 6.380   31.876  1.00 30.08  ? 47   PHE   A CA  1 
ATOM   17   C  C   . PHE   A 1 47  ? 50.668 6.110   30.714  1.00 27.86  ? 47   PHE   A C   1 
ATOM   18   O  O   . PHE   A 1 47  ? 51.661 6.804   30.589  1.00 29.59  ? 47   PHE   A O   1 
ATOM   19   C  CB  . PHE   A 1 47  ? 48.919 7.668   31.702  1.00 27.82  ? 47   PHE   A CB  1 
ATOM   20   C  CG  . PHE   A 1 47  ? 47.847 7.538   30.651  1.00 25.13  ? 47   PHE   A CG  1 
ATOM   21   C  CD1 . PHE   A 1 47  ? 46.679 6.847   30.912  1.00 24.32  ? 47   PHE   A CD1 1 
ATOM   22   C  CD2 . PHE   A 1 47  ? 48.015 8.090   29.398  1.00 24.00  ? 47   PHE   A CD2 1 
ATOM   23   C  CE1 . PHE   A 1 47  ? 45.685 6.736   29.952  1.00 23.73  ? 47   PHE   A CE1 1 
ATOM   24   C  CE2 . PHE   A 1 47  ? 47.030 7.956   28.432  1.00 22.96  ? 47   PHE   A CE2 1 
ATOM   25   C  CZ  . PHE   A 1 47  ? 45.876 7.275   28.709  1.00 22.84  ? 47   PHE   A CZ  1 
ATOM   26   N  N   . PRO   A 1 48  ? 50.423 5.085   29.873  1.00 26.34  ? 48   PRO   A N   1 
ATOM   27   C  CA  . PRO   A 1 48  ? 51.415 4.708   28.854  1.00 26.69  ? 48   PRO   A CA  1 
ATOM   28   C  C   . PRO   A 1 48  ? 51.450 5.530   27.565  1.00 28.16  ? 48   PRO   A C   1 
ATOM   29   O  O   . PRO   A 1 48  ? 51.860 4.997   26.525  1.00 30.75  ? 48   PRO   A O   1 
ATOM   30   C  CB  . PRO   A 1 48  ? 51.060 3.251   28.557  1.00 27.21  ? 48   PRO   A CB  1 
ATOM   31   C  CG  . PRO   A 1 48  ? 49.576 3.210   28.736  1.00 27.95  ? 48   PRO   A CG  1 
ATOM   32   C  CD  . PRO   A 1 48  ? 49.318 4.111   29.926  1.00 25.71  ? 48   PRO   A CD  1 
ATOM   33   N  N   . TRP   A 1 49  ? 51.013 6.797   27.603  1.00 25.65  ? 49   TRP   A N   1 
ATOM   34   C  CA  . TRP   A 1 49  ? 51.078 7.649   26.405  1.00 24.52  ? 49   TRP   A CA  1 
ATOM   35   C  C   . TRP   A 1 49  ? 51.203 9.072   26.877  1.00 25.59  ? 49   TRP   A C   1 
ATOM   36   O  O   . TRP   A 1 49  ? 50.429 9.501   27.728  1.00 27.27  ? 49   TRP   A O   1 
ATOM   37   C  CB  . TRP   A 1 49  ? 49.817 7.450   25.540  1.00 23.25  ? 49   TRP   A CB  1 
ATOM   38   C  CG  . TRP   A 1 49  ? 49.867 8.174   24.225  1.00 22.67  ? 49   TRP   A CG  1 
ATOM   39   C  CD1 . TRP   A 1 49  ? 49.133 9.271   23.863  1.00 22.39  ? 49   TRP   A CD1 1 
ATOM   40   C  CD2 . TRP   A 1 49  ? 50.723 7.877   23.109  1.00 22.37  ? 49   TRP   A CD2 1 
ATOM   41   N  NE1 . TRP   A 1 49  ? 49.502 9.693   22.607  1.00 22.10  ? 49   TRP   A NE1 1 
ATOM   42   C  CE2 . TRP   A 1 49  ? 50.446 8.827   22.103  1.00 23.60  ? 49   TRP   A CE2 1 
ATOM   43   C  CE3 . TRP   A 1 49  ? 51.670 6.872   22.846  1.00 23.66  ? 49   TRP   A CE3 1 
ATOM   44   C  CZ2 . TRP   A 1 49  ? 51.103 8.823   20.876  1.00 25.26  ? 49   TRP   A CZ2 1 
ATOM   45   C  CZ3 . TRP   A 1 49  ? 52.293 6.848   21.623  1.00 25.63  ? 49   TRP   A CZ3 1 
ATOM   46   C  CH2 . TRP   A 1 49  ? 52.035 7.827   20.658  1.00 25.79  ? 49   TRP   A CH2 1 
ATOM   47   N  N   . ASN   A 1 50  ? 52.172 9.825   26.334  1.00 25.62  ? 50   ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 50  ? 52.452 11.178  26.818  1.00 26.90  ? 50   ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 50  ? 52.229 12.276  25.787  1.00 27.68  ? 50   ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 50  ? 52.852 13.344  25.890  1.00 29.35  ? 50   ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 50  ? 53.904 11.260  27.315  1.00 30.95  ? 50   ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 50  ? 54.924 11.025  26.231  1.00 38.27  ? 50   ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 50  ? 54.605 10.637  25.092  1.00 39.90  ? 50   ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 50  ? 56.196 11.260  26.562  1.00 40.91  ? 50   ASN   A ND2 1 
ATOM   55   N  N   . LYS   A 1 51  ? 51.432 12.007  24.748  1.00 25.40  ? 51   LYS   A N   1 
ATOM   56   C  CA  . LYS   A 1 51  ? 51.225 13.036  23.703  1.00 22.72  ? 51   LYS   A CA  1 
ATOM   57   C  C   . LYS   A 1 51  ? 49.735 13.371  23.599  1.00 22.38  ? 51   LYS   A C   1 
ATOM   58   O  O   . LYS   A 1 51  ? 48.890 12.501  23.833  1.00 22.12  ? 51   LYS   A O   1 
ATOM   59   C  CB  . LYS   A 1 51  ? 51.697 12.516  22.348  1.00 24.53  ? 51   LYS   A CB  1 
ATOM   60   C  CG  . LYS   A 1 51  ? 53.225 12.263  22.269  1.00 30.44  ? 51   LYS   A CG  1 
ATOM   61   C  CD  . LYS   A 1 51  ? 53.557 11.717  20.890  1.00 37.61  ? 51   LYS   A CD  1 
ATOM   62   C  CE  . LYS   A 1 51  ? 54.803 10.859  20.850  1.00 44.50  ? 51   LYS   A CE  1 
ATOM   63   N  NZ  . LYS   A 1 51  ? 55.136 10.468  19.448  1.00 47.80  ? 51   LYS   A NZ  1 
ATOM   64   N  N   . ILE   A 1 52  ? 49.436 14.622  23.234  1.00 21.47  ? 52   ILE   A N   1 
ATOM   65   C  CA  . ILE   A 1 52  ? 48.035 15.022  23.032  1.00 21.65  ? 52   ILE   A CA  1 
ATOM   66   C  C   . ILE   A 1 52  ? 47.458 14.291  21.827  1.00 20.50  ? 52   ILE   A C   1 
ATOM   67   O  O   . ILE   A 1 52  ? 46.300 13.840  21.878  1.00 19.52  ? 52   ILE   A O   1 
ATOM   68   C  CB  . ILE   A 1 52  ? 47.913 16.542  22.882  1.00 23.44  ? 52   ILE   A CB  1 
ATOM   69   C  CG1 . ILE   A 1 52  ? 48.154 17.237  24.226  1.00 27.45  ? 52   ILE   A CG1 1 
ATOM   70   C  CG2 . ILE   A 1 52  ? 46.522 16.958  22.313  1.00 23.39  ? 52   ILE   A CG2 1 
ATOM   71   C  CD1 . ILE   A 1 52  ? 47.136 16.914  25.283  1.00 31.46  ? 52   ILE   A CD1 1 
ATOM   72   N  N   . ARG   A 1 53  ? 48.232 14.185  20.749  1.00 19.92  ? 53   ARG   A N   1 
ATOM   73   C  CA  . ARG   A 1 53  ? 47.795 13.425  19.584  1.00 19.21  ? 53   ARG   A CA  1 
ATOM   74   C  C   . ARG   A 1 53  ? 47.833 11.952  19.866  1.00 20.02  ? 53   ARG   A C   1 
ATOM   75   O  O   . ARG   A 1 53  ? 48.758 11.476  20.549  1.00 20.33  ? 53   ARG   A O   1 
ATOM   76   C  CB  . ARG   A 1 53  ? 48.651 13.724  18.364  1.00 19.17  ? 53   ARG   A CB  1 
ATOM   77   C  CG  . ARG   A 1 53  ? 48.533 15.155  17.929  1.00 20.61  ? 53   ARG   A CG  1 
ATOM   78   C  CD  . ARG   A 1 53  ? 47.152 15.449  17.287  1.00 18.63  ? 53   ARG   A CD  1 
ATOM   79   N  NE  . ARG   A 1 53  ? 46.945 14.831  15.980  1.00 18.78  ? 53   ARG   A NE  1 
ATOM   80   C  CZ  . ARG   A 1 53  ? 47.370 15.370  14.832  1.00 21.97  ? 53   ARG   A CZ  1 
ATOM   81   N  NH1 . ARG   A 1 53  ? 48.149 16.447  14.846  1.00 22.24  ? 53   ARG   A NH1 1 
ATOM   82   N  NH2 . ARG   A 1 53  ? 47.101 14.776  13.671  1.00 23.51  ? 53   ARG   A NH2 1 
ATOM   83   N  N   . LEU   A 1 54  ? 46.864 11.199  19.349  1.00 19.67  ? 54   LEU   A N   1 
ATOM   84   C  CA  . LEU   A 1 54  ? 46.828 9.752   19.559  1.00 20.06  ? 54   LEU   A CA  1 
ATOM   85   C  C   . LEU   A 1 54  ? 47.947 9.054   18.786  1.00 20.41  ? 54   LEU   A C   1 
ATOM   86   O  O   . LEU   A 1 54  ? 48.441 9.569   17.776  1.00 20.42  ? 54   LEU   A O   1 
ATOM   87   C  CB  . LEU   A 1 54  ? 45.479 9.206   19.037  1.00 20.47  ? 54   LEU   A CB  1 
ATOM   88   C  CG  . LEU   A 1 54  ? 44.245 9.643   19.795  1.00 21.36  ? 54   LEU   A CG  1 
ATOM   89   C  CD1 . LEU   A 1 54  ? 43.013 9.056   19.130  1.00 22.12  ? 54   LEU   A CD1 1 
ATOM   90   C  CD2 . LEU   A 1 54  ? 44.333 9.201   21.252  1.00 21.94  ? 54   LEU   A CD2 1 
ATOM   91   N  N   . PRO   A 1 55  ? 48.285 7.823   19.187  1.00 19.49  ? 55   PRO   A N   1 
ATOM   92   C  CA  . PRO   A 1 55  ? 49.223 7.035   18.371  1.00 20.24  ? 55   PRO   A CA  1 
ATOM   93   C  C   . PRO   A 1 55  ? 48.694 6.822   16.952  1.00 22.08  ? 55   PRO   A C   1 
ATOM   94   O  O   . PRO   A 1 55  ? 47.460 6.808   16.730  1.00 21.78  ? 55   PRO   A O   1 
ATOM   95   C  CB  . PRO   A 1 55  ? 49.235 5.692   19.087  1.00 20.58  ? 55   PRO   A CB  1 
ATOM   96   C  CG  . PRO   A 1 55  ? 48.839 5.981   20.509  1.00 20.90  ? 55   PRO   A CG  1 
ATOM   97   C  CD  . PRO   A 1 55  ? 47.786 7.056   20.353  1.00 18.57  ? 55   PRO   A CD  1 
ATOM   98   N  N   . GLU   A 1 56  ? 49.606 6.706   15.979  1.00 23.03  ? 56   GLU   A N   1 
ATOM   99   C  CA  . GLU   A 1 56  ? 49.176 6.530   14.595  1.00 24.99  ? 56   GLU   A CA  1 
ATOM   100  C  C   . GLU   A 1 56  ? 48.989 5.072   14.200  1.00 25.66  ? 56   GLU   A C   1 
ATOM   101  O  O   . GLU   A 1 56  ? 48.465 4.820   13.119  1.00 27.29  ? 56   GLU   A O   1 
ATOM   102  C  CB  . GLU   A 1 56  ? 50.198 7.165   13.650  1.00 29.17  ? 56   GLU   A CB  1 
ATOM   103  C  CG  . GLU   A 1 56  ? 50.470 8.621   13.952  1.00 37.04  ? 56   GLU   A CG  1 
ATOM   104  C  CD  . GLU   A 1 56  ? 51.009 9.384   12.761  1.00 47.09  ? 56   GLU   A CD  1 
ATOM   105  O  OE1 . GLU   A 1 56  ? 52.200 9.183   12.425  1.00 49.45  ? 56   GLU   A OE1 1 
ATOM   106  O  OE2 . GLU   A 1 56  ? 50.244 10.182  12.167  1.00 48.67  ? 56   GLU   A OE2 1 
ATOM   107  N  N   . TYR   A 1 57  ? 49.359 4.106   15.068  1.00 24.56  ? 57   TYR   A N   1 
ATOM   108  C  CA  . TYR   A 1 57  ? 49.373 2.709   14.650  1.00 25.62  ? 57   TYR   A CA  1 
ATOM   109  C  C   . TYR   A 1 57  ? 48.188 1.850   15.028  1.00 25.52  ? 57   TYR   A C   1 
ATOM   110  O  O   . TYR   A 1 57  ? 48.229 0.663   14.745  1.00 26.66  ? 57   TYR   A O   1 
ATOM   111  C  CB  . TYR   A 1 57  ? 50.659 2.022   15.122  1.00 26.23  ? 57   TYR   A CB  1 
ATOM   112  C  CG  . TYR   A 1 57  ? 51.016 2.297   16.558  1.00 27.23  ? 57   TYR   A CG  1 
ATOM   113  C  CD1 . TYR   A 1 57  ? 50.477 1.538   17.583  1.00 29.16  ? 57   TYR   A CD1 1 
ATOM   114  C  CD2 . TYR   A 1 57  ? 51.936 3.282   16.891  1.00 28.43  ? 57   TYR   A CD2 1 
ATOM   115  C  CE1 . TYR   A 1 57  ? 50.789 1.795   18.911  1.00 30.96  ? 57   TYR   A CE1 1 
ATOM   116  C  CE2 . TYR   A 1 57  ? 52.287 3.523   18.215  1.00 29.96  ? 57   TYR   A CE2 1 
ATOM   117  C  CZ  . TYR   A 1 57  ? 51.716 2.770   19.221  1.00 31.50  ? 57   TYR   A CZ  1 
ATOM   118  O  OH  . TYR   A 1 57  ? 52.053 2.980   20.539  1.00 34.60  ? 57   TYR   A OH  1 
ATOM   119  N  N   . VAL   A 1 58  ? 47.120 2.419   15.614  1.00 23.53  ? 58   VAL   A N   1 
ATOM   120  C  CA  . VAL   A 1 58  ? 45.912 1.669   15.863  1.00 21.99  ? 58   VAL   A CA  1 
ATOM   121  C  C   . VAL   A 1 58  ? 44.825 2.507   15.152  1.00 21.89  ? 58   VAL   A C   1 
ATOM   122  O  O   . VAL   A 1 58  ? 44.697 3.702   15.416  1.00 23.45  ? 58   VAL   A O   1 
ATOM   123  C  CB  . VAL   A 1 58  ? 45.575 1.483   17.348  1.00 23.04  ? 58   VAL   A CB  1 
ATOM   124  C  CG1 . VAL   A 1 58  ? 44.245 0.734   17.486  1.00 23.61  ? 58   VAL   A CG1 1 
ATOM   125  C  CG2 . VAL   A 1 58  ? 46.695 0.699   18.058  1.00 23.85  ? 58   VAL   A CG2 1 
ATOM   126  N  N   . ILE   A 1 59  ? 44.156 1.892   14.187  1.00 21.17  ? 59   ILE   A N   1 
ATOM   127  C  CA  . ILE   A 1 59  ? 43.209 2.575   13.321  1.00 22.42  ? 59   ILE   A CA  1 
ATOM   128  C  C   . ILE   A 1 59  ? 41.834 1.971   13.383  1.00 21.16  ? 59   ILE   A C   1 
ATOM   129  O  O   . ILE   A 1 59  ? 41.672 0.775   13.127  1.00 20.85  ? 59   ILE   A O   1 
ATOM   130  C  CB  . ILE   A 1 59  ? 43.771 2.388   11.862  1.00 25.56  ? 59   ILE   A CB  1 
ATOM   131  C  CG1 . ILE   A 1 59  ? 45.186 3.015   11.732  1.00 28.48  ? 59   ILE   A CG1 1 
ATOM   132  C  CG2 . ILE   A 1 59  ? 42.812 2.939   10.815  1.00 28.02  ? 59   ILE   A CG2 1 
ATOM   133  C  CD1 . ILE   A 1 59  ? 45.179 4.419   12.020  1.00 30.54  ? 59   ILE   A CD1 1 
ATOM   134  N  N   . PRO   A 1 60  ? 40.809 2.806   13.606  1.00 18.26  ? 60   PRO   A N   1 
ATOM   135  C  CA  . PRO   A 1 60  ? 39.432 2.283   13.547  1.00 17.60  ? 60   PRO   A CA  1 
ATOM   136  C  C   . PRO   A 1 60  ? 38.900 2.178   12.130  1.00 17.79  ? 60   PRO   A C   1 
ATOM   137  O  O   . PRO   A 1 60  ? 39.334 2.962   11.255  1.00 17.76  ? 60   PRO   A O   1 
ATOM   138  C  CB  . PRO   A 1 60  ? 38.635 3.321   14.323  1.00 18.37  ? 60   PRO   A CB  1 
ATOM   139  C  CG  . PRO   A 1 60  ? 39.369 4.654   14.028  1.00 18.17  ? 60   PRO   A CG  1 
ATOM   140  C  CD  . PRO   A 1 60  ? 40.855 4.244   13.948  1.00 18.83  ? 60   PRO   A CD  1 
ATOM   141  N  N   . VAL   A 1 61  ? 37.981 1.251   11.886  1.00 17.73  ? 61   VAL   A N   1 
ATOM   142  C  CA  . VAL   A 1 61  ? 37.309 1.134   10.605  1.00 19.81  ? 61   VAL   A CA  1 
ATOM   143  C  C   . VAL   A 1 61  ? 35.794 1.349   10.755  1.00 17.97  ? 61   VAL   A C   1 
ATOM   144  O  O   . VAL   A 1 61  ? 35.167 1.884   9.848   1.00 17.65  ? 61   VAL   A O   1 
ATOM   145  C  CB  . VAL   A 1 61  ? 37.616 -0.202  9.871   1.00 25.56  ? 61   VAL   A CB  1 
ATOM   146  C  CG1 . VAL   A 1 61  ? 37.262 -1.360  10.723  1.00 27.36  ? 61   VAL   A CG1 1 
ATOM   147  C  CG2 . VAL   A 1 61  ? 36.884 -0.309  8.538   1.00 28.23  ? 61   VAL   A CG2 1 
ATOM   148  N  N   . HIS   A 1 62  ? 35.217 0.932   11.890  1.00 17.33  ? 62   HIS   A N   1 
ATOM   149  C  CA  . HIS   A 1 62  ? 33.765 0.966   12.015  1.00 16.55  ? 62   HIS   A CA  1 
ATOM   150  C  C   . HIS   A 1 62  ? 33.401 1.042   13.473  1.00 16.20  ? 62   HIS   A C   1 
ATOM   151  O  O   . HIS   A 1 62  ? 34.034 0.371   14.299  1.00 17.35  ? 62   HIS   A O   1 
ATOM   152  C  CB  . HIS   A 1 62  ? 33.157 -0.349  11.382  1.00 17.20  ? 62   HIS   A CB  1 
ATOM   153  C  CG  . HIS   A 1 62  ? 31.665 -0.487  11.626  1.00 18.28  ? 62   HIS   A CG  1 
ATOM   154  N  ND1 . HIS   A 1 62  ? 30.731 0.267   10.927  1.00 18.88  ? 62   HIS   A ND1 1 
ATOM   155  C  CD2 . HIS   A 1 62  ? 31.014 -1.230  12.560  1.00 18.88  ? 62   HIS   A CD2 1 
ATOM   156  C  CE1 . HIS   A 1 62  ? 29.546 -0.054  11.433  1.00 20.22  ? 62   HIS   A CE1 1 
ATOM   157  N  NE2 . HIS   A 1 62  ? 29.661 -0.954  12.418  1.00 20.04  ? 62   HIS   A NE2 1 
ATOM   158  N  N   . TYR   A 1 63  ? 32.398 1.845   13.809  1.00 15.60  ? 63   TYR   A N   1 
ATOM   159  C  CA  . TYR   A 1 63  ? 31.882 1.917   15.159  1.00 15.26  ? 63   TYR   A CA  1 
ATOM   160  C  C   . TYR   A 1 63  ? 30.435 1.499   15.187  1.00 16.26  ? 63   TYR   A C   1 
ATOM   161  O  O   . TYR   A 1 63  ? 29.659 1.827   14.291  1.00 16.71  ? 63   TYR   A O   1 
ATOM   162  C  CB  . TYR   A 1 63  ? 31.846 3.386   15.660  1.00 14.63  ? 63   TYR   A CB  1 
ATOM   163  C  CG  . TYR   A 1 63  ? 33.183 4.015   15.916  1.00 14.25  ? 63   TYR   A CG  1 
ATOM   164  C  CD1 . TYR   A 1 63  ? 33.937 4.534   14.876  1.00 14.83  ? 63   TYR   A CD1 1 
ATOM   165  C  CD2 . TYR   A 1 63  ? 33.639 4.216   17.213  1.00 13.73  ? 63   TYR   A CD2 1 
ATOM   166  C  CE1 . TYR   A 1 63  ? 35.146 5.179   15.109  1.00 14.77  ? 63   TYR   A CE1 1 
ATOM   167  C  CE2 . TYR   A 1 63  ? 34.831 4.890   17.467  1.00 14.23  ? 63   TYR   A CE2 1 
ATOM   168  C  CZ  . TYR   A 1 63  ? 35.572 5.388   16.401  1.00 14.64  ? 63   TYR   A CZ  1 
ATOM   169  O  OH  . TYR   A 1 63  ? 36.748 6.060   16.631  1.00 15.70  ? 63   TYR   A OH  1 
ATOM   170  N  N   A ASP   A 1 64  ? 30.062 0.742   16.222  0.50 15.72  ? 64   ASP   A N   1 
ATOM   171  N  N   B ASP   A 1 64  ? 30.073 0.748   16.236  0.50 15.69  ? 64   ASP   A N   1 
ATOM   172  C  CA  A ASP   A 1 64  ? 28.658 0.449   16.473  0.50 15.81  ? 64   ASP   A CA  1 
ATOM   173  C  CA  B ASP   A 1 64  ? 28.684 0.451   16.557  0.50 15.74  ? 64   ASP   A CA  1 
ATOM   174  C  C   A ASP   A 1 64  ? 28.364 1.159   17.797  0.50 16.70  ? 64   ASP   A C   1 
ATOM   175  C  C   B ASP   A 1 64  ? 28.428 1.229   17.831  0.50 16.44  ? 64   ASP   A C   1 
ATOM   176  O  O   A ASP   A 1 64  ? 28.975 0.831   18.812  0.50 16.90  ? 64   ASP   A O   1 
ATOM   177  O  O   B ASP   A 1 64  ? 29.123 1.022   18.835  0.50 16.09  ? 64   ASP   A O   1 
ATOM   178  C  CB  A ASP   A 1 64  ? 28.416 -1.072  16.594  0.50 17.45  ? 64   ASP   A CB  1 
ATOM   179  C  CB  B ASP   A 1 64  ? 28.465 -1.057  16.815  0.50 17.61  ? 64   ASP   A CB  1 
ATOM   180  C  CG  A ASP   A 1 64  ? 26.955 -1.376  16.740  0.50 20.27  ? 64   ASP   A CG  1 
ATOM   181  C  CG  B ASP   A 1 64  ? 28.625 -1.870  15.555  0.50 22.34  ? 64   ASP   A CG  1 
ATOM   182  O  OD1 A ASP   A 1 64  ? 26.472 -1.379  17.882  0.50 20.12  ? 64   ASP   A OD1 1 
ATOM   183  O  OD1 B ASP   A 1 64  ? 27.909 -1.577  14.554  0.50 23.23  ? 64   ASP   A OD1 1 
ATOM   184  O  OD2 A ASP   A 1 64  ? 26.273 -1.541  15.698  0.50 23.31  ? 64   ASP   A OD2 1 
ATOM   185  O  OD2 B ASP   A 1 64  ? 29.469 -2.797  15.550  0.50 24.60  ? 64   ASP   A OD2 1 
ATOM   186  N  N   . LEU   A 1 65  ? 27.504 2.196   17.784  1.00 16.09  ? 65   LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 65  ? 27.210 2.986   18.971  1.00 16.35  ? 65   LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 65  ? 25.831 2.716   19.435  1.00 17.40  ? 65   LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 65  ? 24.891 3.017   18.695  1.00 19.65  ? 65   LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 65  ? 27.337 4.502   18.679  1.00 16.31  ? 65   LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 65  ? 28.656 4.977   18.056  1.00 17.23  ? 65   LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 65  ? 28.625 6.499   17.827  1.00 17.62  ? 65   LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 65  ? 29.846 4.585   18.896  1.00 18.28  ? 65   LEU   A CD2 1 
ATOM   194  N  N   . LEU   A 1 66  ? 25.679 2.192   20.645  1.00 15.28  ? 66   LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 66  ? 24.342 2.063   21.222  1.00 16.29  ? 66   LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 66  ? 24.264 3.125   22.343  1.00 17.05  ? 66   LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 66  ? 25.162 3.204   23.185  1.00 18.04  ? 66   LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 66  ? 24.152 0.647   21.814  1.00 16.74  ? 66   LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 66  ? 22.925 0.448   22.690  1.00 18.56  ? 66   LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 66  ? 21.627 0.682   21.927  1.00 18.96  ? 66   LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 66  ? 22.917 -0.988  23.254  1.00 20.46  ? 66   LEU   A CD2 1 
ATOM   202  N  N   . ILE   A 1 67  ? 23.232 3.977   22.312  1.00 16.87  ? 67   ILE   A N   1 
ATOM   203  C  CA  . ILE   A 1 67  ? 23.094 5.041   23.297  1.00 17.63  ? 67   ILE   A CA  1 
ATOM   204  C  C   . ILE   A 1 67  ? 21.685 4.974   23.876  1.00 16.29  ? 67   ILE   A C   1 
ATOM   205  O  O   . ILE   A 1 67  ? 20.722 4.920   23.114  1.00 16.48  ? 67   ILE   A O   1 
ATOM   206  C  CB  . ILE   A 1 67  ? 23.252 6.440   22.614  1.00 20.41  ? 67   ILE   A CB  1 
ATOM   207  C  CG1 . ILE   A 1 67  ? 24.626 6.623   21.911  1.00 23.62  ? 67   ILE   A CG1 1 
ATOM   208  C  CG2 . ILE   A 1 67  ? 22.952 7.583   23.660  1.00 22.64  ? 67   ILE   A CG2 1 
ATOM   209  C  CD1 . ILE   A 1 67  ? 25.751 7.129   22.745  1.00 25.89  ? 67   ILE   A CD1 1 
ATOM   210  N  N   . HIS   A 1 68  ? 21.566 5.006   25.215  1.00 16.62  ? 68   HIS   A N   1 
ATOM   211  C  CA  . HIS   A 1 68  ? 20.259 5.098   25.860  1.00 17.28  ? 68   HIS   A CA  1 
ATOM   212  C  C   . HIS   A 1 68  ? 20.305 6.361   26.737  1.00 17.12  ? 68   HIS   A C   1 
ATOM   213  O  O   . HIS   A 1 68  ? 21.004 6.371   27.734  1.00 16.92  ? 68   HIS   A O   1 
ATOM   214  C  CB  . HIS   A 1 68  ? 19.993 3.888   26.768  1.00 19.14  ? 68   HIS   A CB  1 
ATOM   215  C  CG  . HIS   A 1 68  ? 18.754 4.053   27.621  1.00 20.25  ? 68   HIS   A CG  1 
ATOM   216  N  ND1 . HIS   A 1 68  ? 18.654 3.446   28.854  1.00 22.26  ? 68   HIS   A ND1 1 
ATOM   217  C  CD2 . HIS   A 1 68  ? 17.659 4.830   27.428  1.00 21.01  ? 68   HIS   A CD2 1 
ATOM   218  C  CE1 . HIS   A 1 68  ? 17.483 3.824   29.358  1.00 22.84  ? 68   HIS   A CE1 1 
ATOM   219  N  NE2 . HIS   A 1 68  ? 16.859 4.684   28.553  1.00 22.09  ? 68   HIS   A NE2 1 
ATOM   220  N  N   . ALA   A 1 69  ? 19.543 7.396   26.379  1.00 17.57  ? 69   ALA   A N   1 
ATOM   221  C  CA  . ALA   A 1 69  ? 19.461 8.573   27.247  1.00 17.85  ? 69   ALA   A CA  1 
ATOM   222  C  C   . ALA   A 1 69  ? 18.157 8.509   28.010  1.00 17.91  ? 69   ALA   A C   1 
ATOM   223  O  O   . ALA   A 1 69  ? 17.093 8.214   27.446  1.00 18.59  ? 69   ALA   A O   1 
ATOM   224  C  CB  . ALA   A 1 69  ? 19.499 9.857   26.429  1.00 19.27  ? 69   ALA   A CB  1 
ATOM   225  N  N   . GLN   A 1 70  ? 18.240 8.845   29.274  1.00 17.85  ? 70   GLN   A N   1 
ATOM   226  C  CA  . GLN   A 1 70  ? 17.079 8.853   30.147  1.00 19.53  ? 70   GLN   A CA  1 
ATOM   227  C  C   . GLN   A 1 70  ? 16.786 10.311  30.386  1.00 20.11  ? 70   GLN   A C   1 
ATOM   228  O  O   . GLN   A 1 70  ? 17.463 10.935  31.206  1.00 21.88  ? 70   GLN   A O   1 
ATOM   229  C  CB  . GLN   A 1 70  ? 17.470 8.160   31.463  1.00 21.98  ? 70   GLN   A CB  1 
ATOM   230  C  CG  . GLN   A 1 70  ? 16.311 7.720   32.322  1.00 25.13  ? 70   GLN   A CG  1 
ATOM   231  C  CD  . GLN   A 1 70  ? 16.846 6.795   33.381  1.00 27.44  ? 70   GLN   A CD  1 
ATOM   232  O  OE1 . GLN   A 1 70  ? 17.509 7.199   34.338  1.00 28.05  ? 70   GLN   A OE1 1 
ATOM   233  N  NE2 . GLN   A 1 70  ? 16.550 5.525   33.234  1.00 30.04  ? 70   GLN   A NE2 1 
ATOM   234  N  N   . LEU   A 1 71  ? 15.781 10.856  29.676  1.00 20.15  ? 71   LEU   A N   1 
ATOM   235  C  CA  . LEU   A 1 71  ? 15.564 12.312  29.748  1.00 22.57  ? 71   LEU   A CA  1 
ATOM   236  C  C   . LEU   A 1 71  ? 14.941 12.785  31.053  1.00 25.06  ? 71   LEU   A C   1 
ATOM   237  O  O   . LEU   A 1 71  ? 14.971 13.983  31.321  1.00 27.79  ? 71   LEU   A O   1 
ATOM   238  C  CB  . LEU   A 1 71  ? 14.789 12.839  28.546  1.00 23.04  ? 71   LEU   A CB  1 
ATOM   239  C  CG  . LEU   A 1 71  ? 15.442 12.660  27.148  1.00 26.88  ? 71   LEU   A CG  1 
ATOM   240  C  CD1 . LEU   A 1 71  ? 14.746 13.549  26.112  1.00 25.87  ? 71   LEU   A CD1 1 
ATOM   241  C  CD2 . LEU   A 1 71  ? 16.936 12.931  27.148  1.00 29.22  ? 71   LEU   A CD2 1 
ATOM   242  N  N   . THR   A 1 72  ? 14.429 11.885  31.883  1.00 24.22  ? 72   THR   A N   1 
ATOM   243  C  CA  . THR   A 1 72  ? 13.885 12.262  33.182  1.00 25.69  ? 72   THR   A CA  1 
ATOM   244  C  C   . THR   A 1 72  ? 14.982 12.416  34.241  1.00 25.92  ? 72   THR   A C   1 
ATOM   245  O  O   . THR   A 1 72  ? 14.732 13.063  35.258  1.00 28.72  ? 72   THR   A O   1 
ATOM   246  C  CB  . THR   A 1 72  ? 12.866 11.224  33.658  1.00 28.15  ? 72   THR   A CB  1 
ATOM   247  O  OG1 . THR   A 1 72  ? 13.499 9.924   33.644  1.00 29.68  ? 72   THR   A OG1 1 
ATOM   248  C  CG2 . THR   A 1 72  ? 11.604 11.216  32.818  1.00 29.11  ? 72   THR   A CG2 1 
ATOM   249  N  N   . THR   A 1 73  ? 16.151 11.779  34.079  1.00 23.08  ? 73   THR   A N   1 
ATOM   250  C  CA  . THR   A 1 73  ? 17.240 11.909  35.066  1.00 22.01  ? 73   THR   A CA  1 
ATOM   251  C  C   . THR   A 1 73  ? 18.502 12.576  34.450  1.00 21.68  ? 73   THR   A C   1 
ATOM   252  O  O   . THR   A 1 73  ? 19.480 12.855  35.159  1.00 21.91  ? 73   THR   A O   1 
ATOM   253  C  CB  . THR   A 1 73  ? 17.715 10.542  35.569  1.00 23.33  ? 73   THR   A CB  1 
ATOM   254  O  OG1 . THR   A 1 73  ? 18.151 9.754   34.454  1.00 22.04  ? 73   THR   A OG1 1 
ATOM   255  C  CG2 . THR   A 1 73  ? 16.634 9.793   36.356  1.00 24.20  ? 73   THR   A CG2 1 
ATOM   256  N  N   . LEU   A 1 74  ? 18.501 12.721  33.130  1.00 20.19  ? 74   LEU   A N   1 
ATOM   257  C  CA  . LEU   A 1 74  ? 19.601 13.304  32.367  1.00 21.20  ? 74   LEU   A CA  1 
ATOM   258  C  C   . LEU   A 1 74  ? 20.825 12.395  32.356  1.00 22.19  ? 74   LEU   A C   1 
ATOM   259  O  O   . LEU   A 1 74  ? 21.924 12.843  32.009  1.00 23.93  ? 74   LEU   A O   1 
ATOM   260  C  CB  . LEU   A 1 74  ? 19.906 14.731  32.855  1.00 22.19  ? 74   LEU   A CB  1 
ATOM   261  C  CG  . LEU   A 1 74  ? 18.677 15.667  32.999  1.00 24.37  ? 74   LEU   A CG  1 
ATOM   262  C  CD1 . LEU   A 1 74  ? 19.076 17.012  33.664  1.00 26.09  ? 74   LEU   A CD1 1 
ATOM   263  C  CD2 . LEU   A 1 74  ? 18.027 15.888  31.656  1.00 24.53  ? 74   LEU   A CD2 1 
ATOM   264  N  N   . THR   A 1 75  ? 20.687 11.116  32.709  1.00 21.49  ? 75   THR   A N   1 
ATOM   265  C  CA  . THR   A 1 75  ? 21.798 10.171  32.639  1.00 20.69  ? 75   THR   A CA  1 
ATOM   266  C  C   . THR   A 1 75  ? 21.715 9.521   31.249  1.00 19.20  ? 75   THR   A C   1 
ATOM   267  O  O   . THR   A 1 75  ? 20.633 9.404   30.671  1.00 19.33  ? 75   THR   A O   1 
ATOM   268  C  CB  . THR   A 1 75  ? 21.609 9.062   33.697  1.00 23.73  ? 75   THR   A CB  1 
ATOM   269  O  OG1 . THR   A 1 75  ? 21.686 9.643   35.011  1.00 27.31  ? 75   THR   A OG1 1 
ATOM   270  C  CG2 . THR   A 1 75  ? 22.707 8.000   33.628  1.00 24.33  ? 75   THR   A CG2 1 
ATOM   271  N  N   . PHE   A 1 76  ? 22.849 9.088   30.707  1.00 15.88  ? 76   PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 76  ? 22.821 8.281   29.512  1.00 15.40  ? 76   PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 76  ? 23.821 7.157   29.693  1.00 16.02  ? 76   PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 76  ? 24.780 7.283   30.462  1.00 16.71  ? 76   PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 76  ? 23.027 9.100   28.220  1.00 15.02  ? 76   PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 76  ? 24.397 9.712   28.011  1.00 14.41  ? 76   PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 76  ? 24.731 10.924  28.594  1.00 15.66  ? 76   PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 76  ? 25.357 9.063   27.239  1.00 14.81  ? 76   PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 76  ? 25.984 11.507  28.355  1.00 16.14  ? 76   PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 76  ? 26.595 9.647   27.000  1.00 15.80  ? 76   PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 76  ? 26.913 10.845  27.581  1.00 15.36  ? 76   PHE   A CZ  1 
ATOM   282  N  N   . TRP   A 1 77  ? 23.573 6.057   28.996  1.00 16.23  ? 77   TRP   A N   1 
ATOM   283  C  CA  . TRP   A 1 77  ? 24.488 4.914   29.011  1.00 16.36  ? 77   TRP   A CA  1 
ATOM   284  C  C   . TRP   A 1 77  ? 24.787 4.547   27.585  1.00 17.45  ? 77   TRP   A C   1 
ATOM   285  O  O   . TRP   A 1 77  ? 23.970 4.795   26.686  1.00 17.62  ? 77   TRP   A O   1 
ATOM   286  C  CB  . TRP   A 1 77  ? 23.790 3.697   29.639  1.00 18.44  ? 77   TRP   A CB  1 
ATOM   287  C  CG  . TRP   A 1 77  ? 23.502 3.831   31.090  1.00 20.65  ? 77   TRP   A CG  1 
ATOM   288  C  CD1 . TRP   A 1 77  ? 24.328 3.502   32.127  1.00 22.58  ? 77   TRP   A CD1 1 
ATOM   289  C  CD2 . TRP   A 1 77  ? 22.345 4.440   31.667  1.00 21.52  ? 77   TRP   A CD2 1 
ATOM   290  N  NE1 . TRP   A 1 77  ? 23.708 3.789   33.323  1.00 23.62  ? 77   TRP   A NE1 1 
ATOM   291  C  CE2 . TRP   A 1 77  ? 22.505 4.395   33.069  1.00 22.80  ? 77   TRP   A CE2 1 
ATOM   292  C  CE3 . TRP   A 1 77  ? 21.160 4.958   31.136  1.00 23.01  ? 77   TRP   A CE3 1 
ATOM   293  C  CZ2 . TRP   A 1 77  ? 21.524 4.841   33.940  1.00 24.94  ? 77   TRP   A CZ2 1 
ATOM   294  C  CZ3 . TRP   A 1 77  ? 20.210 5.464   32.009  1.00 24.97  ? 77   TRP   A CZ3 1 
ATOM   295  C  CH2 . TRP   A 1 77  ? 20.402 5.396   33.390  1.00 25.30  ? 77   TRP   A CH2 1 
ATOM   296  N  N   . GLY   A 1 78  ? 25.969 4.013   27.362  1.00 16.51  ? 78   GLY   A N   1 
ATOM   297  C  CA  . GLY   A 1 78  ? 26.309 3.550   26.035  1.00 16.48  ? 78   GLY   A CA  1 
ATOM   298  C  C   . GLY   A 1 78  ? 27.129 2.279   26.013  1.00 15.06  ? 78   GLY   A C   1 
ATOM   299  O  O   . GLY   A 1 78  ? 27.768 1.899   26.998  1.00 16.48  ? 78   GLY   A O   1 
ATOM   300  N  N   . THR   A 1 79  ? 27.072 1.619   24.870  1.00 15.86  ? 79   THR   A N   1 
ATOM   301  C  CA  . THR   A 1 79  ? 27.987 0.551   24.541  1.00 15.65  ? 79   THR   A CA  1 
ATOM   302  C  C   . THR   A 1 79  ? 28.568 0.936   23.182  1.00 14.95  ? 79   THR   A C   1 
ATOM   303  O  O   . THR   A 1 79  ? 27.836 1.009   22.179  1.00 16.61  ? 79   THR   A O   1 
ATOM   304  C  CB  . THR   A 1 79  ? 27.350 -0.819  24.422  1.00 17.69  ? 79   THR   A CB  1 
ATOM   305  O  OG1 . THR   A 1 79  ? 26.685 -1.147  25.644  1.00 19.05  ? 79   THR   A OG1 1 
ATOM   306  C  CG2 . THR   A 1 79  ? 28.407 -1.906  24.136  1.00 17.65  ? 79   THR   A CG2 1 
ATOM   307  N  N   . THR   A 1 80  ? 29.883 1.108   23.137  1.00 14.31  ? 80   THR   A N   1 
ATOM   308  C  CA  . THR   A 1 80  ? 30.594 1.415   21.911  1.00 14.47  ? 80   THR   A CA  1 
ATOM   309  C  C   . THR   A 1 80  ? 31.403 0.198   21.494  1.00 16.34  ? 80   THR   A C   1 
ATOM   310  O  O   . THR   A 1 80  ? 32.148 -0.342  22.322  1.00 17.37  ? 80   THR   A O   1 
ATOM   311  C  CB  . THR   A 1 80  ? 31.557 2.609   22.140  1.00 16.24  ? 80   THR   A CB  1 
ATOM   312  O  OG1 . THR   A 1 80  ? 30.739 3.782   22.353  1.00 15.75  ? 80   THR   A OG1 1 
ATOM   313  C  CG2 . THR   A 1 80  ? 32.453 2.861   20.937  1.00 15.40  ? 80   THR   A CG2 1 
ATOM   314  N  N   . LYS   A 1 81  ? 31.262 -0.231  20.250  1.00 16.09  ? 81   LYS   A N   1 
ATOM   315  C  CA  . LYS   A 1 81  ? 32.063 -1.352  19.719  1.00 17.35  ? 81   LYS   A CA  1 
ATOM   316  C  C   . LYS   A 1 81  ? 32.850 -0.736  18.563  1.00 17.44  ? 81   LYS   A C   1 
ATOM   317  O  O   . LYS   A 1 81  ? 32.254 -0.154  17.664  1.00 19.43  ? 81   LYS   A O   1 
ATOM   318  C  CB  . LYS   A 1 81  ? 31.173 -2.474  19.154  1.00 19.26  ? 81   LYS   A CB  1 
ATOM   319  C  CG  . LYS   A 1 81  ? 30.204 -3.030  20.153  1.00 24.17  ? 81   LYS   A CG  1 
ATOM   320  C  CD  . LYS   A 1 81  ? 29.365 -4.161  19.517  1.00 29.26  ? 81   LYS   A CD  1 
ATOM   321  C  CE  . LYS   A 1 81  ? 28.352 -4.697  20.485  1.00 37.34  ? 81   LYS   A CE  1 
ATOM   322  N  NZ  . LYS   A 1 81  ? 27.382 -5.591  19.787  1.00 41.30  ? 81   LYS   A NZ  1 
ATOM   323  N  N   . VAL   A 1 82  ? 34.180 -0.770  18.597  1.00 16.30  ? 82   VAL   A N   1 
ATOM   324  C  CA  . VAL   A 1 82  ? 35.003 -0.149  17.552  1.00 17.14  ? 82   VAL   A CA  1 
ATOM   325  C  C   . VAL   A 1 82  ? 35.929 -1.188  16.948  1.00 17.68  ? 82   VAL   A C   1 
ATOM   326  O  O   . VAL   A 1 82  ? 36.673 -1.850  17.687  1.00 18.23  ? 82   VAL   A O   1 
ATOM   327  C  CB  . VAL   A 1 82  ? 35.692 1.133   18.015  1.00 19.08  ? 82   VAL   A CB  1 
ATOM   328  C  CG1 . VAL   A 1 82  ? 36.587 0.971   19.225  1.00 22.28  ? 82   VAL   A CG1 1 
ATOM   329  C  CG2 . VAL   A 1 82  ? 36.447 1.797   16.860  1.00 18.51  ? 82   VAL   A CG2 1 
ATOM   330  N  N   . GLU   A 1 83  ? 35.743 -1.453  15.660  1.00 17.60  ? 83   GLU   A N   1 
ATOM   331  C  CA  . GLU   A 1 83  ? 36.562 -2.417  14.907  1.00 17.27  ? 83   GLU   A CA  1 
ATOM   332  C  C   . GLU   A 1 83  ? 37.858 -1.709  14.577  1.00 18.66  ? 83   GLU   A C   1 
ATOM   333  O  O   . GLU   A 1 83  ? 37.818 -0.602  14.009  1.00 19.64  ? 83   GLU   A O   1 
ATOM   334  C  CB  . GLU   A 1 83  ? 35.834 -2.833  13.633  1.00 19.72  ? 83   GLU   A CB  1 
ATOM   335  C  CG  . GLU   A 1 83  ? 34.589 -3.674  13.883  1.00 26.09  ? 83   GLU   A CG  1 
ATOM   336  C  CD  . GLU   A 1 83  ? 33.807 -4.015  12.621  1.00 36.87  ? 83   GLU   A CD  1 
ATOM   337  O  OE1 . GLU   A 1 83  ? 32.613 -4.380  12.751  1.00 38.16  ? 83   GLU   A OE1 1 
ATOM   338  O  OE2 . GLU   A 1 83  ? 34.382 -3.908  11.509  1.00 37.59  ? 83   GLU   A OE2 1 
ATOM   339  N  N   . ILE   A 1 84  ? 39.001 -2.275  14.984  1.00 18.21  ? 84   ILE   A N   1 
ATOM   340  C  CA  . ILE   A 1 84  ? 40.303 -1.669  14.789  1.00 18.59  ? 84   ILE   A CA  1 
ATOM   341  C  C   . ILE   A 1 84  ? 41.299 -2.656  14.184  1.00 19.43  ? 84   ILE   A C   1 
ATOM   342  O  O   . ILE   A 1 84  ? 41.084 -3.887  14.176  1.00 20.70  ? 84   ILE   A O   1 
ATOM   343  C  CB  . ILE   A 1 84  ? 40.848 -1.217  16.168  1.00 18.64  ? 84   ILE   A CB  1 
ATOM   344  C  CG1 . ILE   A 1 84  ? 40.959 -2.436  17.150  1.00 19.56  ? 84   ILE   A CG1 1 
ATOM   345  C  CG2 . ILE   A 1 84  ? 40.004 -0.095  16.799  1.00 18.70  ? 84   ILE   A CG2 1 
ATOM   346  C  CD1 . ILE   A 1 84  ? 41.760 -2.112  18.320  1.00 19.79  ? 84   ILE   A CD1 1 
ATOM   347  N  N   . THR   A 1 85  ? 42.386 -2.086  13.641  1.00 20.61  ? 85   THR   A N   1 
ATOM   348  C  CA  . THR   A 1 85  ? 43.545 -2.892  13.268  1.00 23.22  ? 85   THR   A CA  1 
ATOM   349  C  C   . THR   A 1 85  ? 44.787 -2.153  13.796  1.00 24.59  ? 85   THR   A C   1 
ATOM   350  O  O   . THR   A 1 85  ? 44.843 -0.899  13.839  1.00 24.73  ? 85   THR   A O   1 
ATOM   351  C  CB  . THR   A 1 85  ? 43.643 -3.177  11.776  1.00 27.56  ? 85   THR   A CB  1 
ATOM   352  O  OG1 . THR   A 1 85  ? 43.861 -1.953  11.084  1.00 31.87  ? 85   THR   A OG1 1 
ATOM   353  C  CG2 . THR   A 1 85  ? 42.447 -3.958  11.220  1.00 27.56  ? 85   THR   A CG2 1 
ATOM   354  N  N   . ALA   A 1 86  ? 45.817 -2.928  14.153  1.00 25.32  ? 86   ALA   A N   1 
ATOM   355  C  CA  . ALA   A 1 86  ? 47.082 -2.376  14.602  1.00 26.55  ? 86   ALA   A CA  1 
ATOM   356  C  C   . ALA   A 1 86  ? 48.139 -2.685  13.535  1.00 28.20  ? 86   ALA   A C   1 
ATOM   357  O  O   . ALA   A 1 86  ? 48.188 -3.813  13.024  1.00 28.31  ? 86   ALA   A O   1 
ATOM   358  C  CB  . ALA   A 1 86  ? 47.481 -3.004  15.938  1.00 27.14  ? 86   ALA   A CB  1 
ATOM   359  N  N   . SER   A 1 87  ? 48.944 -1.680  13.185  1.00 27.65  ? 87   SER   A N   1 
ATOM   360  C  CA  . SER   A 1 87  ? 50.038 -1.856  12.213  1.00 28.88  ? 87   SER   A CA  1 
ATOM   361  C  C   . SER   A 1 87  ? 51.382 -2.182  12.875  1.00 30.98  ? 87   SER   A C   1 
ATOM   362  O  O   . SER   A 1 87  ? 52.352 -2.414  12.169  1.00 31.69  ? 87   SER   A O   1 
ATOM   363  C  CB  . SER   A 1 87  ? 50.212 -0.620  11.344  1.00 30.56  ? 87   SER   A CB  1 
ATOM   364  O  OG  . SER   A 1 87  ? 50.566 0.520   12.115  1.00 31.72  ? 87   SER   A OG  1 
ATOM   365  N  N   . GLN   A 1 88  ? 51.453 -2.101  14.197  1.00 31.25  ? 88   GLN   A N   1 
ATOM   366  C  CA  . GLN   A 1 88  ? 52.609 -2.428  15.029  1.00 33.11  ? 88   GLN   A CA  1 
ATOM   367  C  C   . GLN   A 1 88  ? 52.071 -3.324  16.111  1.00 33.22  ? 88   GLN   A C   1 
ATOM   368  O  O   . GLN   A 1 88  ? 50.942 -3.088  16.589  1.00 33.09  ? 88   GLN   A O   1 
ATOM   369  C  CB  . GLN   A 1 88  ? 53.052 -1.162  15.780  1.00 35.97  ? 88   GLN   A CB  1 
ATOM   370  C  CG  . GLN   A 1 88  ? 54.048 -0.279  15.097  1.00 40.17  ? 88   GLN   A CG  1 
ATOM   371  C  CD  . GLN   A 1 88  ? 54.527 0.805   16.041  1.00 43.85  ? 88   GLN   A CD  1 
ATOM   372  O  OE1 . GLN   A 1 88  ? 54.481 0.689   17.287  1.00 44.56  ? 88   GLN   A OE1 1 
ATOM   373  N  NE2 . GLN   A 1 88  ? 55.010 1.887   15.468  1.00 44.91  ? 88   GLN   A NE2 1 
ATOM   374  N  N   . PRO   A 1 89  ? 52.857 -4.294  16.611  1.00 32.60  ? 89   PRO   A N   1 
ATOM   375  C  CA  . PRO   A 1 89  ? 52.383 -5.070  17.761  1.00 32.26  ? 89   PRO   A CA  1 
ATOM   376  C  C   . PRO   A 1 89  ? 52.268 -4.117  18.956  1.00 30.69  ? 89   PRO   A C   1 
ATOM   377  O  O   . PRO   A 1 89  ? 53.107 -3.215  19.144  1.00 31.67  ? 89   PRO   A O   1 
ATOM   378  C  CB  . PRO   A 1 89  ? 53.492 -6.125  17.978  1.00 33.64  ? 89   PRO   A CB  1 
ATOM   379  C  CG  . PRO   A 1 89  ? 54.303 -6.105  16.732  1.00 34.19  ? 89   PRO   A CG  1 
ATOM   380  C  CD  . PRO   A 1 89  ? 54.218 -4.707  16.208  1.00 32.34  ? 89   PRO   A CD  1 
ATOM   381  N  N   . THR   A 1 90  ? 51.126 -4.171  19.621  1.00 27.56  ? 90   THR   A N   1 
ATOM   382  C  CA  . THR   A 1 90  ? 50.909 -3.374  20.812  1.00 26.11  ? 90   THR   A CA  1 
ATOM   383  C  C   . THR   A 1 90  ? 49.941 -4.118  21.691  1.00 25.41  ? 90   THR   A C   1 
ATOM   384  O  O   . THR   A 1 90  ? 49.090 -4.882  21.209  1.00 26.67  ? 90   THR   A O   1 
ATOM   385  C  CB  . THR   A 1 90  ? 50.296 -1.994  20.482  1.00 28.08  ? 90   THR   A CB  1 
ATOM   386  O  OG1 . THR   A 1 90  ? 50.207 -1.255  21.716  1.00 27.78  ? 90   THR   A OG1 1 
ATOM   387  C  CG2 . THR   A 1 90  ? 48.897 -2.113  19.860  1.00 29.17  ? 90   THR   A CG2 1 
ATOM   388  N  N   . SER   A 1 91  ? 50.077 -3.923  22.988  1.00 24.35  ? 91   SER   A N   1 
ATOM   389  C  CA  . SER   A 1 91  ? 49.123 -4.478  23.941  1.00 24.69  ? 91   SER   A CA  1 
ATOM   390  C  C   . SER   A 1 91  ? 48.257 -3.333  24.529  1.00 26.07  ? 91   SER   A C   1 
ATOM   391  O  O   . SER   A 1 91  ? 47.475 -3.583  25.437  1.00 26.87  ? 91   SER   A O   1 
ATOM   392  C  CB  . SER   A 1 91  ? 49.849 -5.180  25.080  1.00 27.43  ? 91   SER   A CB  1 
ATOM   393  O  OG  . SER   A 1 91  ? 50.589 -6.286  24.570  1.00 29.97  ? 91   SER   A OG  1 
ATOM   394  N  N   . THR   A 1 92  ? 48.405 -2.101  24.011  1.00 25.72  ? 92   THR   A N   1 
ATOM   395  C  CA  . THR   A 1 92  ? 47.759 -0.941  24.569  1.00 26.80  ? 92   THR   A CA  1 
ATOM   396  C  C   . THR   A 1 92  ? 47.065 -0.151  23.495  1.00 25.52  ? 92   THR   A C   1 
ATOM   397  O  O   . THR   A 1 92  ? 47.667 0.178   22.462  1.00 25.42  ? 92   THR   A O   1 
ATOM   398  C  CB  . THR   A 1 92  ? 48.831 -0.061  25.185  1.00 30.78  ? 92   THR   A CB  1 
ATOM   399  O  OG1 . THR   A 1 92  ? 49.655 -0.839  26.063  1.00 33.93  ? 92   THR   A OG1 1 
ATOM   400  C  CG2 . THR   A 1 92  ? 48.253 1.103   25.940  1.00 31.91  ? 92   THR   A CG2 1 
ATOM   401  N  N   . ILE   A 1 93  ? 45.800 0.167   23.761  1.00 23.81  ? 93   ILE   A N   1 
ATOM   402  C  CA  . ILE   A 1 93  ? 45.000 0.987   22.838  1.00 22.74  ? 93   ILE   A CA  1 
ATOM   403  C  C   . ILE   A 1 93  ? 44.708 2.312   23.519  1.00 21.41  ? 93   ILE   A C   1 
ATOM   404  O  O   . ILE   A 1 93  ? 44.128 2.336   24.605  1.00 21.34  ? 93   ILE   A O   1 
ATOM   405  C  CB  . ILE   A 1 93  ? 43.710 0.242   22.498  1.00 23.18  ? 93   ILE   A CB  1 
ATOM   406  C  CG1 . ILE   A 1 93  ? 44.054 -1.117  21.834  1.00 25.76  ? 93   ILE   A CG1 1 
ATOM   407  C  CG2 . ILE   A 1 93  ? 42.810 1.104   21.579  1.00 22.46  ? 93   ILE   A CG2 1 
ATOM   408  C  CD1 . ILE   A 1 93  ? 42.995 -2.148  22.006  1.00 27.05  ? 93   ILE   A CD1 1 
ATOM   409  N  N   . ILE   A 1 94  ? 45.128 3.411   22.893  1.00 21.72  ? 94   ILE   A N   1 
ATOM   410  C  CA  . ILE   A 1 94  ? 44.872 4.730   23.461  1.00 20.85  ? 94   ILE   A CA  1 
ATOM   411  C  C   . ILE   A 1 94  ? 43.737 5.346   22.662  1.00 20.53  ? 94   ILE   A C   1 
ATOM   412  O  O   . ILE   A 1 94  ? 43.797 5.343   21.428  1.00 21.87  ? 94   ILE   A O   1 
ATOM   413  C  CB  . ILE   A 1 94  ? 46.098 5.671   23.328  1.00 22.43  ? 94   ILE   A CB  1 
ATOM   414  C  CG1 . ILE   A 1 94  ? 47.396 5.036   23.866  1.00 23.07  ? 94   ILE   A CG1 1 
ATOM   415  C  CG2 . ILE   A 1 94  ? 45.809 7.021   23.999  1.00 22.73  ? 94   ILE   A CG2 1 
ATOM   416  C  CD1 . ILE   A 1 94  ? 47.260 4.686   25.417  1.00 24.17  ? 94   ILE   A CD1 1 
ATOM   417  N  N   . LEU   A 1 95  ? 42.766 5.869   23.355  1.00 19.26  ? 95   LEU   A N   1 
ATOM   418  C  CA  . LEU   A 1 95  ? 41.716 6.591   22.630  1.00 20.12  ? 95   LEU   A CA  1 
ATOM   419  C  C   . LEU   A 1 95  ? 41.131 7.664   23.511  1.00 18.43  ? 95   LEU   A C   1 
ATOM   420  O  O   . LEU   A 1 95  ? 41.640 7.926   24.588  1.00 19.06  ? 95   LEU   A O   1 
ATOM   421  C  CB  . LEU   A 1 95  ? 40.719 5.648   21.991  1.00 21.72  ? 95   LEU   A CB  1 
ATOM   422  C  CG  . LEU   A 1 95  ? 39.811 4.903   22.916  1.00 21.39  ? 95   LEU   A CG  1 
ATOM   423  C  CD1 . LEU   A 1 95  ? 38.565 4.455   22.178  1.00 23.71  ? 95   LEU   A CD1 1 
ATOM   424  C  CD2 . LEU   A 1 95  ? 40.534 3.713   23.592  1.00 23.67  ? 95   LEU   A CD2 1 
ATOM   425  N  N   . HIS   A 1 96  ? 40.187 8.483   22.973  1.00 15.30  ? 96   HIS   A N   1 
ATOM   426  C  CA  . HIS   A 1 96  ? 39.668 9.611   23.720  1.00 15.56  ? 96   HIS   A CA  1 
ATOM   427  C  C   . HIS   A 1 96  ? 38.435 9.290   24.481  1.00 16.06  ? 96   HIS   A C   1 
ATOM   428  O  O   . HIS   A 1 96  ? 37.603 8.522   24.024  1.00 16.91  ? 96   HIS   A O   1 
ATOM   429  C  CB  . HIS   A 1 96  ? 39.330 10.783  22.780  1.00 15.51  ? 96   HIS   A CB  1 
ATOM   430  C  CG  . HIS   A 1 96  ? 40.530 11.422  22.180  1.00 14.61  ? 96   HIS   A CG  1 
ATOM   431  N  ND1 . HIS   A 1 96  ? 40.811 11.295  20.833  1.00 15.76  ? 96   HIS   A ND1 1 
ATOM   432  C  CD2 . HIS   A 1 96  ? 41.426 12.268  22.741  1.00 15.57  ? 96   HIS   A CD2 1 
ATOM   433  C  CE1 . HIS   A 1 96  ? 41.875 12.064  20.601  1.00 16.52  ? 96   HIS   A CE1 1 
ATOM   434  N  NE2 . HIS   A 1 96  ? 42.289 12.675  21.716  1.00 16.23  ? 96   HIS   A NE2 1 
ATOM   435  N  N   . SER   A 1 97  ? 38.287 9.905   25.630  1.00 15.58  ? 97   SER   A N   1 
ATOM   436  C  CA  . SER   A 1 97  ? 37.072 9.781   26.453  1.00 16.92  ? 97   SER   A CA  1 
ATOM   437  C  C   . SER   A 1 97  ? 37.111 10.950  27.443  1.00 16.87  ? 97   SER   A C   1 
ATOM   438  O  O   . SER   A 1 97  ? 38.179 11.209  28.028  1.00 18.40  ? 97   SER   A O   1 
ATOM   439  C  CB  . SER   A 1 97  ? 37.063 8.442   27.196  1.00 17.38  ? 97   SER   A CB  1 
ATOM   440  O  OG  . SER   A 1 97  ? 35.850 8.263   27.920  1.00 18.00  ? 97   SER   A OG  1 
ATOM   441  N  N   . HIS   A 1 98  ? 35.997 11.683  27.623  1.00 16.22  ? 98   HIS   A N   1 
ATOM   442  C  CA  . HIS   A 1 98  ? 35.996 12.817  28.535  1.00 16.47  ? 98   HIS   A CA  1 
ATOM   443  C  C   . HIS   A 1 98  ? 34.672 12.799  29.297  1.00 17.35  ? 98   HIS   A C   1 
ATOM   444  O  O   . HIS   A 1 98  ? 33.592 12.846  28.687  1.00 17.36  ? 98   HIS   A O   1 
ATOM   445  C  CB  . HIS   A 1 98  ? 36.098 14.120  27.709  1.00 17.05  ? 98   HIS   A CB  1 
ATOM   446  C  CG  . HIS   A 1 98  ? 36.056 15.389  28.525  1.00 20.57  ? 98   HIS   A CG  1 
ATOM   447  N  ND1 . HIS   A 1 98  ? 36.995 15.653  29.509  1.00 22.78  ? 98   HIS   A ND1 1 
ATOM   448  C  CD2 . HIS   A 1 98  ? 35.202 16.444  28.451  1.00 22.98  ? 98   HIS   A CD2 1 
ATOM   449  C  CE1 . HIS   A 1 98  ? 36.669 16.830  30.023  1.00 25.07  ? 98   HIS   A CE1 1 
ATOM   450  N  NE2 . HIS   A 1 98  ? 35.591 17.349  29.419  1.00 25.02  ? 98   HIS   A NE2 1 
ATOM   451  N  N   . HIS   A 1 99  ? 34.759 12.703  30.644  1.00 17.04  ? 99   HIS   A N   1 
ATOM   452  C  CA  . HIS   A 1 99  ? 33.599 12.696  31.535  1.00 18.49  ? 99   HIS   A CA  1 
ATOM   453  C  C   . HIS   A 1 99  ? 32.687 11.501  31.345  1.00 18.98  ? 99   HIS   A C   1 
ATOM   454  O  O   . HIS   A 1 99  ? 31.524 11.545  31.769  1.00 22.10  ? 99   HIS   A O   1 
ATOM   455  C  CB  . HIS   A 1 99  ? 32.813 14.002  31.511  1.00 19.95  ? 99   HIS   A CB  1 
ATOM   456  C  CG  . HIS   A 1 99  ? 33.565 15.172  32.087  1.00 25.41  ? 99   HIS   A CG  1 
ATOM   457  N  ND1 . HIS   A 1 99  ? 33.074 16.467  31.961  1.00 28.59  ? 99   HIS   A ND1 1 
ATOM   458  C  CD2 . HIS   A 1 99  ? 34.726 15.211  32.792  1.00 28.58  ? 99   HIS   A CD2 1 
ATOM   459  C  CE1 . HIS   A 1 99  ? 33.977 17.247  32.561  1.00 30.33  ? 99   HIS   A CE1 1 
ATOM   460  N  NE2 . HIS   A 1 99  ? 34.980 16.534  33.079  1.00 30.87  ? 99   HIS   A NE2 1 
ATOM   461  N  N   . LEU   A 1 100 ? 33.227 10.390  30.849  1.00 16.96  ? 100  LEU   A N   1 
ATOM   462  C  CA  . LEU   A 1 100 ? 32.437 9.149   30.766  1.00 16.65  ? 100  LEU   A CA  1 
ATOM   463  C  C   . LEU   A 1 100 ? 32.944 8.192   31.856  1.00 17.99  ? 100  LEU   A C   1 
ATOM   464  O  O   . LEU   A 1 100 ? 34.153 8.071   32.055  1.00 19.29  ? 100  LEU   A O   1 
ATOM   465  C  CB  . LEU   A 1 100 ? 32.604 8.501   29.393  1.00 16.62  ? 100  LEU   A CB  1 
ATOM   466  C  CG  . LEU   A 1 100 ? 32.110 9.393   28.218  1.00 16.97  ? 100  LEU   A CG  1 
ATOM   467  C  CD1 . LEU   A 1 100 ? 32.405 8.680   26.923  1.00 19.21  ? 100  LEU   A CD1 1 
ATOM   468  C  CD2 . LEU   A 1 100 ? 30.610 9.691   28.353  1.00 17.93  ? 100  LEU   A CD2 1 
ATOM   469  N  N   . GLN   A 1 101 ? 32.034 7.510   32.532  1.00 17.51  ? 101  GLN   A N   1 
ATOM   470  C  CA  . GLN   A 1 101 ? 32.390 6.529   33.565  1.00 17.52  ? 101  GLN   A CA  1 
ATOM   471  C  C   . GLN   A 1 101 ? 32.359 5.178   32.918  1.00 17.45  ? 101  GLN   A C   1 
ATOM   472  O  O   . GLN   A 1 101 ? 31.292 4.673   32.584  1.00 17.57  ? 101  GLN   A O   1 
ATOM   473  C  CB  . GLN   A 1 101 ? 31.354 6.587   34.690  1.00 21.06  ? 101  GLN   A CB  1 
ATOM   474  C  CG  . GLN   A 1 101 ? 31.383 7.885   35.475  1.00 30.17  ? 101  GLN   A CG  1 
ATOM   475  C  CD  . GLN   A 1 101 ? 30.599 7.808   36.775  1.00 43.93  ? 101  GLN   A CD  1 
ATOM   476  O  OE1 . GLN   A 1 101 ? 30.043 6.755   37.161  1.00 48.19  ? 101  GLN   A OE1 1 
ATOM   477  N  NE2 . GLN   A 1 101 ? 30.526 8.934   37.484  1.00 46.83  ? 101  GLN   A NE2 1 
ATOM   478  N  N   . ILE   A 1 102 ? 33.525 4.566   32.748  1.00 17.41  ? 102  ILE   A N   1 
ATOM   479  C  CA  . ILE   A 1 102 ? 33.627 3.298   32.053  1.00 18.61  ? 102  ILE   A CA  1 
ATOM   480  C  C   . ILE   A 1 102 ? 33.435 2.166   33.014  1.00 19.65  ? 102  ILE   A C   1 
ATOM   481  O  O   . ILE   A 1 102 ? 34.178 2.084   33.998  1.00 21.41  ? 102  ILE   A O   1 
ATOM   482  C  CB  . ILE   A 1 102 ? 34.998 3.202   31.352  1.00 20.15  ? 102  ILE   A CB  1 
ATOM   483  C  CG1 . ILE   A 1 102 ? 35.136 4.383   30.343  1.00 23.43  ? 102  ILE   A CG1 1 
ATOM   484  C  CG2 . ILE   A 1 102 ? 35.155 1.830   30.668  1.00 21.56  ? 102  ILE   A CG2 1 
ATOM   485  C  CD1 . ILE   A 1 102 ? 36.394 4.503   29.752  1.00 27.05  ? 102  ILE   A CD1 1 
ATOM   486  N  N   . SER   A 1 103 ? 32.442 1.313   32.765  1.00 18.47  ? 103  SER   A N   1 
ATOM   487  C  CA  . SER   A 1 103 ? 32.237 0.180   33.680  1.00 19.49  ? 103  SER   A CA  1 
ATOM   488  C  C   . SER   A 1 103 ? 32.957 -1.068  33.249  1.00 20.22  ? 103  SER   A C   1 
ATOM   489  O  O   . SER   A 1 103 ? 33.237 -1.910  34.116  1.00 21.59  ? 103  SER   A O   1 
ATOM   490  C  CB  . SER   A 1 103 ? 30.760 -0.092  33.807  1.00 21.99  ? 103  SER   A CB  1 
ATOM   491  O  OG  . SER   A 1 103 ? 30.213 -0.426  32.547  1.00 23.03  ? 103  SER   A OG  1 
ATOM   492  N  N   . ARG   A 1 104 ? 33.181 -1.265  31.945  1.00 19.81  ? 104  ARG   A N   1 
ATOM   493  C  CA  . ARG   A 1 104 ? 33.819 -2.507  31.479  1.00 21.32  ? 104  ARG   A CA  1 
ATOM   494  C  C   . ARG   A 1 104 ? 34.355 -2.262  30.089  1.00 21.54  ? 104  ARG   A C   1 
ATOM   495  O  O   . ARG   A 1 104 ? 33.735 -1.546  29.295  1.00 20.48  ? 104  ARG   A O   1 
ATOM   496  C  CB  . ARG   A 1 104 ? 32.734 -3.618  31.407  1.00 24.02  ? 104  ARG   A CB  1 
ATOM   497  C  CG  . ARG   A 1 104 ? 33.245 -4.986  30.881  1.00 30.38  ? 104  ARG   A CG  1 
ATOM   498  C  CD  . ARG   A 1 104 ? 32.671 -6.215  31.570  1.00 38.98  ? 104  ARG   A CD  1 
ATOM   499  N  NE  . ARG   A 1 104 ? 31.213 -6.344  31.501  1.00 45.12  ? 104  ARG   A NE  1 
ATOM   500  C  CZ  . ARG   A 1 104 ? 30.566 -7.509  31.424  1.00 48.24  ? 104  ARG   A CZ  1 
ATOM   501  N  NH1 . ARG   A 1 104 ? 31.242 -8.649  31.362  1.00 48.33  ? 104  ARG   A NH1 1 
ATOM   502  N  NH2 . ARG   A 1 104 ? 29.239 -7.538  31.370  1.00 49.15  ? 104  ARG   A NH2 1 
ATOM   503  N  N   . ALA   A 1 105 ? 35.519 -2.839  29.779  1.00 20.45  ? 105  ALA   A N   1 
ATOM   504  C  CA  . ALA   A 1 105 ? 36.087 -2.771  28.430  1.00 20.43  ? 105  ALA   A CA  1 
ATOM   505  C  C   . ALA   A 1 105 ? 36.606 -4.162  28.093  1.00 20.56  ? 105  ALA   A C   1 
ATOM   506  O  O   . ALA   A 1 105 ? 37.212 -4.829  28.964  1.00 22.25  ? 105  ALA   A O   1 
ATOM   507  C  CB  . ALA   A 1 105 ? 37.228 -1.771  28.339  1.00 20.51  ? 105  ALA   A CB  1 
ATOM   508  N  N   . THR   A 1 106 ? 36.334 -4.638  26.893  1.00 20.89  ? 106  THR   A N   1 
ATOM   509  C  CA  . THR   A 1 106 ? 36.752 -5.971  26.468  1.00 22.23  ? 106  THR   A CA  1 
ATOM   510  C  C   . THR   A 1 106 ? 37.260 -5.940  25.024  1.00 21.29  ? 106  THR   A C   1 
ATOM   511  O  O   . THR   A 1 106 ? 36.899 -5.055  24.244  1.00 20.63  ? 106  THR   A O   1 
ATOM   512  C  CB  . THR   A 1 106 ? 35.503 -6.869  26.489  1.00 26.58  ? 106  THR   A CB  1 
ATOM   513  O  OG1 . THR   A 1 106 ? 34.863 -6.765  27.778  1.00 30.74  ? 106  THR   A OG1 1 
ATOM   514  C  CG2 . THR   A 1 106 ? 35.834 -8.312  26.191  1.00 27.79  ? 106  THR   A CG2 1 
ATOM   515  N  N   . LEU   A 1 107 ? 38.182 -6.852  24.669  1.00 21.25  ? 107  LEU   A N   1 
ATOM   516  C  CA  . LEU   A 1 107 ? 38.724 -6.944  23.332  1.00 21.84  ? 107  LEU   A CA  1 
ATOM   517  C  C   . LEU   A 1 107 ? 38.238 -8.211  22.725  1.00 23.01  ? 107  LEU   A C   1 
ATOM   518  O  O   . LEU   A 1 107 ? 38.487 -9.304  23.287  1.00 23.31  ? 107  LEU   A O   1 
ATOM   519  C  CB  . LEU   A 1 107 ? 40.243 -6.960  23.382  1.00 22.63  ? 107  LEU   A CB  1 
ATOM   520  C  CG  . LEU   A 1 107 ? 40.926 -6.940  22.037  1.00 25.54  ? 107  LEU   A CG  1 
ATOM   521  C  CD1 . LEU   A 1 107 ? 40.754 -5.591  21.380  1.00 25.86  ? 107  LEU   A CD1 1 
ATOM   522  C  CD2 . LEU   A 1 107 ? 42.408 -7.214  22.205  1.00 27.54  ? 107  LEU   A CD2 1 
ATOM   523  N  N   . ARG   A 1 108 ? 37.539 -8.125  21.632  1.00 23.34  ? 108  ARG   A N   1 
ATOM   524  C  CA  . ARG   A 1 108 ? 37.070 -9.306  20.920  1.00 24.30  ? 108  ARG   A CA  1 
ATOM   525  C  C   . ARG   A 1 108 ? 37.907 -9.544  19.690  1.00 24.73  ? 108  ARG   A C   1 
ATOM   526  O  O   . ARG   A 1 108 ? 38.365 -8.598  19.035  1.00 23.72  ? 108  ARG   A O   1 
ATOM   527  C  CB  . ARG   A 1 108 ? 35.629 -9.153  20.480  1.00 25.85  ? 108  ARG   A CB  1 
ATOM   528  C  CG  . ARG   A 1 108 ? 34.644 -9.035  21.597  1.00 30.27  ? 108  ARG   A CG  1 
ATOM   529  C  CD  . ARG   A 1 108 ? 33.270 -8.985  21.002  1.00 34.09  ? 108  ARG   A CD  1 
ATOM   530  N  NE  . ARG   A 1 108 ? 32.276 -8.899  22.059  1.00 37.80  ? 108  ARG   A NE  1 
ATOM   531  C  CZ  . ARG   A 1 108 ? 31.025 -8.498  21.886  1.00 40.65  ? 108  ARG   A CZ  1 
ATOM   532  N  NH1 . ARG   A 1 108 ? 30.595 -8.136  20.680  1.00 40.75  ? 108  ARG   A NH1 1 
ATOM   533  N  NH2 . ARG   A 1 108 ? 30.194 -8.446  22.916  1.00 41.81  ? 108  ARG   A NH2 1 
ATOM   534  N  N   . LYS   A 1 109 ? 38.175 -10.816 19.392  1.00 25.57  ? 109  LYS   A N   1 
ATOM   535  C  CA  . LYS   A 1 109 ? 38.871 -11.258 18.196  1.00 28.62  ? 109  LYS   A CA  1 
ATOM   536  C  C   . LYS   A 1 109 ? 37.955 -12.363 17.662  1.00 33.09  ? 109  LYS   A C   1 
ATOM   537  O  O   . LYS   A 1 109 ? 37.542 -13.227 18.443  1.00 33.39  ? 109  LYS   A O   1 
ATOM   538  C  CB  . LYS   A 1 109 ? 40.248 -11.820 18.566  1.00 32.51  ? 109  LYS   A CB  1 
ATOM   539  C  CG  . LYS   A 1 109 ? 41.095 -12.168 17.365  1.00 37.56  ? 109  LYS   A CG  1 
ATOM   540  C  CD  . LYS   A 1 109 ? 42.440 -12.758 17.757  1.00 41.07  ? 109  LYS   A CD  1 
ATOM   541  C  CE  . LYS   A 1 109 ? 43.313 -12.879 16.527  1.00 43.29  ? 109  LYS   A CE  1 
ATOM   542  N  NZ  . LYS   A 1 109 ? 42.562 -13.445 15.377  1.00 44.27  ? 109  LYS   A NZ  1 
ATOM   543  N  N   . GLY   A 1 110 ? 37.566 -12.300 16.406  1.00 34.86  ? 110  GLY   A N   1 
ATOM   544  C  CA  . GLY   A 1 110 ? 36.696 -13.308 15.805  1.00 37.17  ? 110  GLY   A CA  1 
ATOM   545  C  C   . GLY   A 1 110 ? 35.208 -13.102 16.014  1.00 39.67  ? 110  GLY   A C   1 
ATOM   546  O  O   . GLY   A 1 110 ? 34.778 -12.092 16.582  1.00 41.76  ? 110  GLY   A O   1 
ATOM   547  N  N   . ARG   A 1 114 ? 34.570 -18.523 16.478  1.00 43.21  ? 114  ARG   A N   1 
ATOM   548  C  CA  . ARG   A 1 114 ? 35.967 -18.291 16.847  1.00 43.24  ? 114  ARG   A CA  1 
ATOM   549  C  C   . ARG   A 1 114 ? 36.144 -17.119 17.819  1.00 42.18  ? 114  ARG   A C   1 
ATOM   550  O  O   . ARG   A 1 114 ? 37.278 -16.689 18.023  1.00 43.17  ? 114  ARG   A O   1 
ATOM   551  C  CB  . ARG   A 1 114 ? 36.795 -18.026 15.579  1.00 44.96  ? 114  ARG   A CB  1 
ATOM   552  N  N   . LEU   A 1 115 ? 35.053 -16.568 18.380  1.00 40.50  ? 115  LEU   A N   1 
ATOM   553  C  CA  . LEU   A 1 115 ? 35.155 -15.412 19.262  1.00 39.21  ? 115  LEU   A CA  1 
ATOM   554  C  C   . LEU   A 1 115 ? 35.920 -15.705 20.519  1.00 37.41  ? 115  LEU   A C   1 
ATOM   555  O  O   . LEU   A 1 115 ? 35.770 -16.759 21.141  1.00 37.50  ? 115  LEU   A O   1 
ATOM   556  C  CB  . LEU   A 1 115 ? 33.763 -14.841 19.601  1.00 40.21  ? 115  LEU   A CB  1 
ATOM   557  C  CG  . LEU   A 1 115 ? 33.720 -13.675 20.572  1.00 42.69  ? 115  LEU   A CG  1 
ATOM   558  C  CD1 . LEU   A 1 115 ? 34.326 -12.450 19.935  1.00 43.69  ? 115  LEU   A CD1 1 
ATOM   559  C  CD2 . LEU   A 1 115 ? 32.302 -13.325 20.946  1.00 43.98  ? 115  LEU   A CD2 1 
ATOM   560  N  N   . SER   A 1 116 ? 36.834 -14.845 20.811  1.00 34.70  ? 116  SER   A N   1 
ATOM   561  C  CA  . SER   A 1 116 ? 37.572 -14.856 22.036  1.00 33.18  ? 116  SER   A CA  1 
ATOM   562  C  C   . SER   A 1 116 ? 37.447 -13.444 22.532  1.00 32.55  ? 116  SER   A C   1 
ATOM   563  O  O   . SER   A 1 116 ? 37.390 -12.463 21.749  1.00 32.49  ? 116  SER   A O   1 
ATOM   564  C  CB  . SER   A 1 116 ? 39.024 -15.307 21.875  1.00 32.95  ? 116  SER   A CB  1 
ATOM   565  O  OG  . SER   A 1 116 ? 39.855 -14.351 21.225  1.00 35.68  ? 116  SER   A OG  1 
ATOM   566  N  N   . GLU   A 1 117 ? 37.266 -13.339 23.802  1.00 31.42  ? 117  GLU   A N   1 
ATOM   567  C  CA  . GLU   A 1 117 ? 37.204 -12.077 24.479  1.00 30.17  ? 117  GLU   A CA  1 
ATOM   568  C  C   . GLU   A 1 117 ? 38.321 -12.066 25.432  1.00 29.76  ? 117  GLU   A C   1 
ATOM   569  O  O   . GLU   A 1 117 ? 38.697 -13.114 25.995  1.00 30.40  ? 117  GLU   A O   1 
ATOM   570  C  CB  . GLU   A 1 117 ? 35.920 -11.965 25.284  1.00 30.69  ? 117  GLU   A CB  1 
ATOM   571  C  CG  . GLU   A 1 117 ? 34.700 -11.862 24.416  1.00 36.21  ? 117  GLU   A CG  1 
ATOM   572  C  CD  . GLU   A 1 117 ? 33.533 -11.184 25.099  1.00 39.33  ? 117  GLU   A CD  1 
ATOM   573  O  OE1 . GLU   A 1 117 ? 33.592 -10.949 26.332  1.00 33.80  ? 117  GLU   A OE1 1 
ATOM   574  O  OE2 . GLU   A 1 117 ? 32.558 -10.875 24.381  1.00 46.73  ? 117  GLU   A OE2 1 
ATOM   575  N  N   . GLU   A 1 118 ? 38.827 -10.903 25.695  1.00 28.32  ? 118  GLU   A N   1 
ATOM   576  C  CA  . GLU   A 1 118 ? 39.839 -10.672 26.681  1.00 28.54  ? 118  GLU   A CA  1 
ATOM   577  C  C   . GLU   A 1 118 ? 39.431 -9.420  27.435  1.00 27.39  ? 118  GLU   A C   1 
ATOM   578  O  O   . GLU   A 1 118 ? 39.190 -8.383  26.802  1.00 24.82  ? 118  GLU   A O   1 
ATOM   579  C  CB  . GLU   A 1 118 ? 41.187 -10.408 25.985  1.00 34.05  ? 118  GLU   A CB  1 
ATOM   580  C  CG  . GLU   A 1 118 ? 41.648 -11.499 25.025  1.00 43.80  ? 118  GLU   A CG  1 
ATOM   581  C  CD  . GLU   A 1 118 ? 42.778 -11.066 24.104  1.00 53.38  ? 118  GLU   A CD  1 
ATOM   582  O  OE1 . GLU   A 1 118 ? 42.810 -11.508 22.930  1.00 57.23  ? 118  GLU   A OE1 1 
ATOM   583  O  OE2 . GLU   A 1 118 ? 43.617 -10.251 24.551  1.00 53.92  ? 118  GLU   A OE2 1 
ATOM   584  N  N   . PRO   A 1 119 ? 39.361 -9.439  28.760  1.00 27.71  ? 119  PRO   A N   1 
ATOM   585  C  CA  . PRO   A 1 119 ? 39.083 -8.206  29.497  1.00 27.57  ? 119  PRO   A CA  1 
ATOM   586  C  C   . PRO   A 1 119 ? 40.220 -7.218  29.313  1.00 26.12  ? 119  PRO   A C   1 
ATOM   587  O  O   . PRO   A 1 119 ? 41.402 -7.611  29.238  1.00 27.32  ? 119  PRO   A O   1 
ATOM   588  C  CB  . PRO   A 1 119 ? 39.020 -8.682  30.957  1.00 29.29  ? 119  PRO   A CB  1 
ATOM   589  C  CG  . PRO   A 1 119 ? 40.005 -9.805  30.987  1.00 30.10  ? 119  PRO   A CG  1 
ATOM   590  C  CD  . PRO   A 1 119 ? 39.681 -10.555 29.684  1.00 28.40  ? 119  PRO   A CD  1 
ATOM   591  N  N   . LEU   A 1 120 ? 39.881 -5.937  29.201  1.00 23.59  ? 120  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 120 ? 40.902 -4.928  29.097  1.00 23.79  ? 120  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 120 ? 40.963 -4.139  30.393  1.00 25.94  ? 120  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 120 ? 39.916 -3.788  30.967  1.00 27.79  ? 120  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 120 ? 40.580 -3.979  27.940  1.00 22.98  ? 120  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 120 ? 40.584 -4.584  26.538  1.00 23.86  ? 120  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 120 ? 39.855 -3.626  25.541  1.00 23.54  ? 120  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 120 ? 42.012 -4.786  26.039  1.00 25.66  ? 120  LEU   A CD2 1 
ATOM   599  N  N   . GLN   A 1 121 ? 42.180 -3.811  30.835  1.00 25.76  ? 121  GLN   A N   1 
ATOM   600  C  CA  . GLN   A 1 121 ? 42.332 -2.952  32.008  1.00 26.01  ? 121  GLN   A CA  1 
ATOM   601  C  C   . GLN   A 1 121 ? 42.202 -1.529  31.495  1.00 26.24  ? 121  GLN   A C   1 
ATOM   602  O  O   . GLN   A 1 121 ? 42.764 -1.196  30.446  1.00 25.97  ? 121  GLN   A O   1 
ATOM   603  C  CB  . GLN   A 1 121 ? 43.730 -3.139  32.624  1.00 30.46  ? 121  GLN   A CB  1 
ATOM   604  C  CG  . GLN   A 1 121 ? 44.105 -2.124  33.687  1.00 37.18  ? 121  GLN   A CG  1 
ATOM   605  C  CD  . GLN   A 1 121 ? 45.374 -2.519  34.412  1.00 46.63  ? 121  GLN   A CD  1 
ATOM   606  O  OE1 . GLN   A 1 121 ? 45.745 -3.701  34.490  1.00 48.83  ? 121  GLN   A OE1 1 
ATOM   607  N  NE2 . GLN   A 1 121 ? 46.057 -1.533  34.973  1.00 48.75  ? 121  GLN   A NE2 1 
ATOM   608  N  N   . VAL   A 1 122 ? 41.541 -0.680  32.280  1.00 25.16  ? 122  VAL   A N   1 
ATOM   609  C  CA  . VAL   A 1 122 ? 41.325 0.697   31.837  1.00 24.14  ? 122  VAL   A CA  1 
ATOM   610  C  C   . VAL   A 1 122 ? 42.076 1.662   32.706  1.00 24.96  ? 122  VAL   A C   1 
ATOM   611  O  O   . VAL   A 1 122 ? 41.941 1.622   33.936  1.00 27.67  ? 122  VAL   A O   1 
ATOM   612  C  CB  . VAL   A 1 122 ? 39.812 1.027   31.890  1.00 24.30  ? 122  VAL   A CB  1 
ATOM   613  C  CG1 . VAL   A 1 122 ? 39.545 2.461   31.411  1.00 24.99  ? 122  VAL   A CG1 1 
ATOM   614  C  CG2 . VAL   A 1 122 ? 38.984 0.021   31.110  1.00 24.43  ? 122  VAL   A CG2 1 
ATOM   615  N  N   . LEU   A 1 123 ? 42.866 2.519   32.094  1.00 23.06  ? 123  LEU   A N   1 
ATOM   616  C  CA  . LEU   A 1 123 ? 43.549 3.636   32.747  1.00 23.43  ? 123  LEU   A CA  1 
ATOM   617  C  C   . LEU   A 1 123 ? 43.031 4.944   32.120  1.00 24.85  ? 123  LEU   A C   1 
ATOM   618  O  O   . LEU   A 1 123 ? 42.569 4.938   30.964  1.00 24.23  ? 123  LEU   A O   1 
ATOM   619  C  CB  . LEU   A 1 123 ? 45.077 3.580   32.531  1.00 25.03  ? 123  LEU   A CB  1 
ATOM   620  C  CG  . LEU   A 1 123 ? 45.806 2.303   32.944  1.00 27.07  ? 123  LEU   A CG  1 
ATOM   621  C  CD1 . LEU   A 1 123 ? 47.296 2.431   32.606  1.00 27.44  ? 123  LEU   A CD1 1 
ATOM   622  C  CD2 . LEU   A 1 123 ? 45.600 1.977   34.436  1.00 28.70  ? 123  LEU   A CD2 1 
ATOM   623  N  N   . GLU   A 1 124 ? 43.105 6.046   32.869  1.00 24.18  ? 124  GLU   A N   1 
ATOM   624  C  CA  . GLU   A 1 124 ? 42.644 7.321   32.303  1.00 24.31  ? 124  GLU   A CA  1 
ATOM   625  C  C   . GLU   A 1 124 ? 43.635 8.408   32.509  1.00 25.13  ? 124  GLU   A C   1 
ATOM   626  O  O   . GLU   A 1 124 ? 44.339 8.439   33.524  1.00 26.10  ? 124  GLU   A O   1 
ATOM   627  C  CB  . GLU   A 1 124 ? 41.288 7.738   32.888  1.00 27.68  ? 124  GLU   A CB  1 
ATOM   628  C  CG  . GLU   A 1 124 ? 41.335 8.101   34.355  1.00 33.87  ? 124  GLU   A CG  1 
ATOM   629  C  CD  . GLU   A 1 124 ? 40.092 8.807   34.858  1.00 42.84  ? 124  GLU   A CD  1 
ATOM   630  O  OE1 . GLU   A 1 124 ? 39.027 8.706   34.202  1.00 40.48  ? 124  GLU   A OE1 1 
ATOM   631  O  OE2 . GLU   A 1 124 ? 40.187 9.453   35.928  1.00 48.15  ? 124  GLU   A OE2 1 
ATOM   632  N  N   . HIS   A 1 125 ? 43.684 9.345   31.557  1.00 23.16  ? 125  HIS   A N   1 
ATOM   633  C  CA  . HIS   A 1 125 ? 44.498 10.536  31.717  1.00 23.06  ? 125  HIS   A CA  1 
ATOM   634  C  C   . HIS   A 1 125 ? 43.526 11.683  31.394  1.00 23.58  ? 125  HIS   A C   1 
ATOM   635  O  O   . HIS   A 1 125 ? 43.446 12.148  30.239  1.00 23.08  ? 125  HIS   A O   1 
ATOM   636  C  CB  . HIS   A 1 125 ? 45.678 10.566  30.740  1.00 25.39  ? 125  HIS   A CB  1 
ATOM   637  C  CG  . HIS   A 1 125 ? 46.689 11.621  31.093  1.00 32.17  ? 125  HIS   A CG  1 
ATOM   638  N  ND1 . HIS   A 1 125 ? 46.359 12.971  31.089  1.00 34.52  ? 125  HIS   A ND1 1 
ATOM   639  C  CD2 . HIS   A 1 125 ? 47.984 11.494  31.476  1.00 34.38  ? 125  HIS   A CD2 1 
ATOM   640  C  CE1 . HIS   A 1 125 ? 47.457 13.618  31.448  1.00 35.97  ? 125  HIS   A CE1 1 
ATOM   641  N  NE2 . HIS   A 1 125 ? 48.465 12.771  31.688  1.00 35.60  ? 125  HIS   A NE2 1 
ATOM   642  N  N   . PRO   A 1 126 ? 42.804 12.166  32.404  1.00 23.37  ? 126  PRO   A N   1 
ATOM   643  C  CA  . PRO   A 1 126 ? 41.793 13.206  32.135  1.00 23.62  ? 126  PRO   A CA  1 
ATOM   644  C  C   . PRO   A 1 126 ? 42.291 14.502  31.494  1.00 24.58  ? 126  PRO   A C   1 
ATOM   645  O  O   . PRO   A 1 126 ? 41.537 15.038  30.691  1.00 22.87  ? 126  PRO   A O   1 
ATOM   646  C  CB  . PRO   A 1 126 ? 41.142 13.467  33.503  1.00 25.15  ? 126  PRO   A CB  1 
ATOM   647  C  CG  . PRO   A 1 126 ? 41.452 12.235  34.320  1.00 26.37  ? 126  PRO   A CG  1 
ATOM   648  C  CD  . PRO   A 1 126 ? 42.745 11.685  33.804  1.00 24.38  ? 126  PRO   A CD  1 
ATOM   649  N  N   . ARG   A 1 127 ? 43.489 15.009  31.801  1.00 25.84  ? 127  ARG   A N   1 
ATOM   650  C  CA  . ARG   A 1 127 ? 43.977 16.244  31.181  1.00 27.54  ? 127  ARG   A CA  1 
ATOM   651  C  C   . ARG   A 1 127 ? 44.209 16.049  29.672  1.00 26.03  ? 127  ARG   A C   1 
ATOM   652  O  O   . ARG   A 1 127 ? 43.876 16.940  28.880  1.00 27.37  ? 127  ARG   A O   1 
ATOM   653  C  CB  . ARG   A 1 127 ? 45.278 16.717  31.850  1.00 32.45  ? 127  ARG   A CB  1 
ATOM   654  C  CG  . ARG   A 1 127 ? 45.110 17.272  33.251  1.00 41.12  ? 127  ARG   A CG  1 
ATOM   655  C  CD  . ARG   A 1 127 ? 46.411 17.919  33.729  1.00 48.73  ? 127  ARG   A CD  1 
ATOM   656  N  NE  . ARG   A 1 127 ? 46.572 19.276  33.195  1.00 55.20  ? 127  ARG   A NE  1 
ATOM   657  C  CZ  . ARG   A 1 127 ? 47.386 19.602  32.196  1.00 59.57  ? 127  ARG   A CZ  1 
ATOM   658  N  NH1 . ARG   A 1 127 ? 48.136 18.675  31.611  1.00 59.84  ? 127  ARG   A NH1 1 
ATOM   659  N  NH2 . ARG   A 1 127 ? 47.464 20.860  31.779  1.00 60.46  ? 127  ARG   A NH2 1 
ATOM   660  N  N   . GLN   A 1 128 ? 44.731 14.879  29.259  1.00 24.28  ? 128  GLN   A N   1 
ATOM   661  C  CA  . GLN   A 1 128 ? 44.896 14.599  27.817  1.00 23.14  ? 128  GLN   A CA  1 
ATOM   662  C  C   . GLN   A 1 128 ? 43.546 14.101  27.199  1.00 20.03  ? 128  GLN   A C   1 
ATOM   663  O  O   . GLN   A 1 128 ? 43.512 13.805  25.992  1.00 19.23  ? 128  GLN   A O   1 
ATOM   664  C  CB  . GLN   A 1 128 ? 45.995 13.521  27.592  1.00 25.09  ? 128  GLN   A CB  1 
ATOM   665  C  CG  . GLN   A 1 128 ? 47.401 14.053  27.839  1.00 29.53  ? 128  GLN   A CG  1 
ATOM   666  C  CD  . GLN   A 1 128 ? 48.535 13.038  27.976  1.00 32.14  ? 128  GLN   A CD  1 
ATOM   667  O  OE1 . GLN   A 1 128 ? 49.603 13.389  28.496  1.00 37.52  ? 128  GLN   A OE1 1 
ATOM   668  N  NE2 . GLN   A 1 128 ? 48.387 11.796  27.509  1.00 29.27  ? 128  GLN   A NE2 1 
ATOM   669  N  N   . GLU   A 1 129 ? 42.486 13.943  28.015  1.00 18.85  ? 129  GLU   A N   1 
ATOM   670  C  CA  . GLU   A 1 129 ? 41.173 13.426  27.587  1.00 17.40  ? 129  GLU   A CA  1 
ATOM   671  C  C   . GLU   A 1 129 ? 41.328 12.079  26.908  1.00 17.73  ? 129  GLU   A C   1 
ATOM   672  O  O   . GLU   A 1 129 ? 40.635 11.760  25.949  1.00 17.72  ? 129  GLU   A O   1 
ATOM   673  C  CB  . GLU   A 1 129 ? 40.474 14.467  26.665  1.00 17.25  ? 129  GLU   A CB  1 
ATOM   674  C  CG  . GLU   A 1 129 ? 40.305 15.780  27.430  1.00 19.94  ? 129  GLU   A CG  1 
ATOM   675  C  CD  . GLU   A 1 129 ? 39.600 16.895  26.690  1.00 21.90  ? 129  GLU   A CD  1 
ATOM   676  O  OE1 . GLU   A 1 129 ? 39.201 16.657  25.533  1.00 18.05  ? 129  GLU   A OE1 1 
ATOM   677  O  OE2 . GLU   A 1 129 ? 39.480 18.010  27.250  1.00 25.48  ? 129  GLU   A OE2 1 
ATOM   678  N  N   . GLN   A 1 130 ? 42.229 11.226  27.468  1.00 16.84  ? 130  GLN   A N   1 
ATOM   679  C  CA  . GLN   A 1 130 ? 42.491 9.908   26.917  1.00 18.12  ? 130  GLN   A CA  1 
ATOM   680  C  C   . GLN   A 1 130 ? 42.243 8.811   27.914  1.00 18.71  ? 130  GLN   A C   1 
ATOM   681  O  O   . GLN   A 1 130 ? 42.236 9.050   29.130  1.00 19.70  ? 130  GLN   A O   1 
ATOM   682  C  CB  . GLN   A 1 130 ? 43.967 9.821   26.527  1.00 18.89  ? 130  GLN   A CB  1 
ATOM   683  C  CG  . GLN   A 1 130 ? 44.226 10.700  25.291  1.00 17.42  ? 130  GLN   A CG  1 
ATOM   684  C  CD  . GLN   A 1 130 ? 45.699 10.902  25.024  1.00 20.11  ? 130  GLN   A CD  1 
ATOM   685  O  OE1 . GLN   A 1 130 ? 46.574 10.443  25.790  1.00 21.32  ? 130  GLN   A OE1 1 
ATOM   686  N  NE2 . GLN   A 1 130 ? 46.057 11.590  23.933  1.00 20.21  ? 130  GLN   A NE2 1 
ATOM   687  N  N   . ILE   A 1 131 ? 41.966 7.622   27.397  1.00 18.36  ? 131  ILE   A N   1 
ATOM   688  C  CA  . ILE   A 1 131 ? 41.948 6.399   28.192  1.00 19.38  ? 131  ILE   A CA  1 
ATOM   689  C  C   . ILE   A 1 131 ? 42.909 5.430   27.509  1.00 20.30  ? 131  ILE   A C   1 
ATOM   690  O  O   . ILE   A 1 131 ? 43.251 5.557   26.327  1.00 20.16  ? 131  ILE   A O   1 
ATOM   691  C  CB  . ILE   A 1 131 ? 40.541 5.782   28.337  1.00 20.65  ? 131  ILE   A CB  1 
ATOM   692  C  CG1 . ILE   A 1 131 ? 39.884 5.633   26.951  1.00 22.58  ? 131  ILE   A CG1 1 
ATOM   693  C  CG2 . ILE   A 1 131 ? 39.709 6.634   29.271  1.00 19.29  ? 131  ILE   A CG2 1 
ATOM   694  C  CD1 . ILE   A 1 131 ? 38.612 4.730   26.946  1.00 23.18  ? 131  ILE   A CD1 1 
ATOM   695  N  N   . ALA   A 1 132 ? 43.441 4.471   28.308  1.00 20.47  ? 132  ALA   A N   1 
ATOM   696  C  CA  . ALA   A 1 132 ? 44.339 3.452   27.742  1.00 21.98  ? 132  ALA   A CA  1 
ATOM   697  C  C   . ALA   A 1 132 ? 43.720 2.125   28.119  1.00 21.33  ? 132  ALA   A C   1 
ATOM   698  O  O   . ALA   A 1 132 ? 43.292 1.927   29.270  1.00 23.60  ? 132  ALA   A O   1 
ATOM   699  C  CB  . ALA   A 1 132 ? 45.760 3.558   28.332  1.00 22.54  ? 132  ALA   A CB  1 
ATOM   700  N  N   . LEU   A 1 133 ? 43.597 1.246   27.139  1.00 21.37  ? 133  LEU   A N   1 
ATOM   701  C  CA  . LEU   A 1 133 ? 43.050 -0.087  27.326  1.00 22.25  ? 133  LEU   A CA  1 
ATOM   702  C  C   . LEU   A 1 133 ? 44.190 -1.073  27.146  1.00 23.04  ? 133  LEU   A C   1 
ATOM   703  O  O   . LEU   A 1 133 ? 44.844 -1.076  26.114  1.00 22.45  ? 133  LEU   A O   1 
ATOM   704  C  CB  . LEU   A 1 133 ? 41.949 -0.382  26.326  1.00 22.58  ? 133  LEU   A CB  1 
ATOM   705  C  CG  . LEU   A 1 133 ? 40.875 0.729   26.228  1.00 24.02  ? 133  LEU   A CG  1 
ATOM   706  C  CD1 . LEU   A 1 133 ? 39.897 0.408   25.151  1.00 25.08  ? 133  LEU   A CD1 1 
ATOM   707  C  CD2 . LEU   A 1 133 ? 40.158 0.931   27.578  1.00 24.36  ? 133  LEU   A CD2 1 
ATOM   708  N  N   . LEU   A 1 134 ? 44.410 -1.906  28.176  1.00 24.33  ? 134  LEU   A N   1 
ATOM   709  C  CA  . LEU   A 1 134 ? 45.527 -2.866  28.245  1.00 26.28  ? 134  LEU   A CA  1 
ATOM   710  C  C   . LEU   A 1 134 ? 45.052 -4.292  28.054  1.00 25.17  ? 134  LEU   A C   1 
ATOM   711  O  O   . LEU   A 1 134 ? 44.231 -4.772  28.828  1.00 25.44  ? 134  LEU   A O   1 
ATOM   712  C  CB  . LEU   A 1 134 ? 46.199 -2.754  29.616  1.00 28.70  ? 134  LEU   A CB  1 
ATOM   713  C  CG  . LEU   A 1 134 ? 46.547 -1.359  30.134  1.00 32.87  ? 134  LEU   A CG  1 
ATOM   714  C  CD1 . LEU   A 1 134 ? 47.271 -1.442  31.481  1.00 34.46  ? 134  LEU   A CD1 1 
ATOM   715  C  CD2 . LEU   A 1 134 ? 47.337 -0.544  29.134  1.00 35.56  ? 134  LEU   A CD2 1 
ATOM   716  N  N   . ALA   A 1 135 ? 45.577 -4.978  27.030  1.00 25.20  ? 135  ALA   A N   1 
ATOM   717  C  CA  . ALA   A 1 135 ? 45.198 -6.339  26.687  1.00 25.99  ? 135  ALA   A CA  1 
ATOM   718  C  C   . ALA   A 1 135 ? 46.178 -7.321  27.341  1.00 27.09  ? 135  ALA   A C   1 
ATOM   719  O  O   . ALA   A 1 135 ? 47.350 -6.985  27.493  1.00 27.93  ? 135  ALA   A O   1 
ATOM   720  C  CB  . ALA   A 1 135 ? 45.265 -6.495  25.177  1.00 26.60  ? 135  ALA   A CB  1 
ATOM   721  N  N   . PRO   A 1 136 ? 45.709 -8.536  27.645  1.00 28.12  ? 136  PRO   A N   1 
ATOM   722  C  CA  . PRO   A 1 136 ? 46.582 -9.535  28.301  1.00 28.68  ? 136  PRO   A CA  1 
ATOM   723  C  C   . PRO   A 1 136 ? 47.652 -10.135 27.398  1.00 29.43  ? 136  PRO   A C   1 
ATOM   724  O  O   . PRO   A 1 136 ? 48.514 -10.881 27.883  1.00 30.05  ? 136  PRO   A O   1 
ATOM   725  C  CB  . PRO   A 1 136 ? 45.592 -10.609 28.755  1.00 30.62  ? 136  PRO   A CB  1 
ATOM   726  C  CG  . PRO   A 1 136 ? 44.485 -10.517 27.794  1.00 31.24  ? 136  PRO   A CG  1 
ATOM   727  C  CD  . PRO   A 1 136 ? 44.329 -9.039  27.522  1.00 28.78  ? 136  PRO   A CD  1 
ATOM   728  N  N   . GLU   A 1 137 ? 47.595 -9.850  26.096  1.00 28.01  ? 137  GLU   A N   1 
ATOM   729  C  CA  . GLU   A 1 137 ? 48.555 -10.332 25.103  1.00 28.01  ? 137  GLU   A CA  1 
ATOM   730  C  C   . GLU   A 1 137 ? 48.533 -9.388  23.911  1.00 28.43  ? 137  GLU   A C   1 
ATOM   731  O  O   . GLU   A 1 137 ? 47.552 -8.643  23.744  1.00 27.54  ? 137  GLU   A O   1 
ATOM   732  C  CB  . GLU   A 1 137 ? 48.266 -11.815 24.732  1.00 30.62  ? 137  GLU   A CB  1 
ATOM   733  C  CG  . GLU   A 1 137 ? 46.984 -12.094 23.964  1.00 34.46  ? 137  GLU   A CG  1 
ATOM   734  C  CD  . GLU   A 1 137 ? 46.517 -13.528 24.184  1.00 38.88  ? 137  GLU   A CD  1 
ATOM   735  O  OE1 . GLU   A 1 137 ? 46.524 -13.981 25.352  1.00 42.32  ? 137  GLU   A OE1 1 
ATOM   736  O  OE2 . GLU   A 1 137 ? 46.161 -14.206 23.194  1.00 37.47  ? 137  GLU   A OE2 1 
ATOM   737  N  N   . PRO   A 1 138 ? 49.613 -9.286  23.137  1.00 27.94  ? 138  PRO   A N   1 
ATOM   738  C  CA  . PRO   A 1 138 ? 49.625 -8.316  22.042  1.00 28.35  ? 138  PRO   A CA  1 
ATOM   739  C  C   . PRO   A 1 138 ? 48.612 -8.604  20.977  1.00 28.84  ? 138  PRO   A C   1 
ATOM   740  O  O   . PRO   A 1 138 ? 48.288 -9.764  20.695  1.00 28.97  ? 138  PRO   A O   1 
ATOM   741  C  CB  . PRO   A 1 138 ? 51.067 -8.383  21.486  1.00 29.43  ? 138  PRO   A CB  1 
ATOM   742  C  CG  . PRO   A 1 138 ? 51.848 -9.136  22.499  1.00 29.82  ? 138  PRO   A CG  1 
ATOM   743  C  CD  . PRO   A 1 138 ? 50.891 -10.039 23.210  1.00 28.11  ? 138  PRO   A CD  1 
ATOM   744  N  N   . LEU   A 1 139 ? 48.111 -7.512  20.348  1.00 28.01  ? 139  LEU   A N   1 
ATOM   745  C  CA  . LEU   A 1 139 ? 47.245 -7.666  19.198  1.00 28.28  ? 139  LEU   A CA  1 
ATOM   746  C  C   . LEU   A 1 139 ? 48.153 -8.177  18.043  1.00 30.08  ? 139  LEU   A C   1 
ATOM   747  O  O   . LEU   A 1 139 ? 49.323 -7.792  17.960  1.00 31.65  ? 139  LEU   A O   1 
ATOM   748  C  CB  . LEU   A 1 139 ? 46.688 -6.286  18.825  1.00 26.64  ? 139  LEU   A CB  1 
ATOM   749  C  CG  . LEU   A 1 139 ? 45.394 -5.870  19.536  1.00 26.66  ? 139  LEU   A CG  1 
ATOM   750  C  CD1 . LEU   A 1 139 ? 45.604 -5.615  21.014  1.00 26.16  ? 139  LEU   A CD1 1 
ATOM   751  C  CD2 . LEU   A 1 139 ? 44.844 -4.580  18.919  1.00 26.33  ? 139  LEU   A CD2 1 
ATOM   752  N  N   . LEU   A 1 140 ? 47.618 -9.024  17.165  1.00 30.23  ? 140  LEU   A N   1 
ATOM   753  C  CA  . LEU   A 1 140 ? 48.386 -9.492  16.008  1.00 31.70  ? 140  LEU   A CA  1 
ATOM   754  C  C   . LEU   A 1 140 ? 48.234 -8.429  14.913  1.00 31.95  ? 140  LEU   A C   1 
ATOM   755  O  O   . LEU   A 1 140 ? 47.128 -7.924  14.688  1.00 31.10  ? 140  LEU   A O   1 
ATOM   756  C  CB  . LEU   A 1 140 ? 47.869 -10.856 15.551  1.00 33.28  ? 140  LEU   A CB  1 
ATOM   757  C  CG  . LEU   A 1 140 ? 47.987 -11.993 16.584  1.00 37.40  ? 140  LEU   A CG  1 
ATOM   758  C  CD1 . LEU   A 1 140 ? 47.405 -13.265 16.029  1.00 39.13  ? 140  LEU   A CD1 1 
ATOM   759  C  CD2 . LEU   A 1 140 ? 49.438 -12.226 16.985  1.00 38.15  ? 140  LEU   A CD2 1 
ATOM   760  N  N   . VAL   A 1 141 ? 49.337 -8.012  14.312  1.00 31.82  ? 141  VAL   A N   1 
ATOM   761  C  CA  . VAL   A 1 141 ? 49.332 -6.974  13.303  1.00 31.73  ? 141  VAL   A CA  1 
ATOM   762  C  C   . VAL   A 1 141 ? 48.453 -7.321  12.092  1.00 30.49  ? 141  VAL   A C   1 
ATOM   763  O  O   . VAL   A 1 141 ? 48.471 -8.467  11.619  1.00 30.49  ? 141  VAL   A O   1 
ATOM   764  C  CB  . VAL   A 1 141 ? 50.807 -6.697  12.900  1.00 34.66  ? 141  VAL   A CB  1 
ATOM   765  C  CG1 . VAL   A 1 141 ? 50.893 -5.757  11.714  1.00 35.47  ? 141  VAL   A CG1 1 
ATOM   766  C  CG2 . VAL   A 1 141 ? 51.589 -6.143  14.089  1.00 35.46  ? 141  VAL   A CG2 1 
ATOM   767  N  N   . GLY   A 1 142 ? 47.654 -6.351  11.647  1.00 29.89  ? 142  GLY   A N   1 
ATOM   768  C  CA  . GLY   A 1 142 ? 46.840 -6.491  10.445  1.00 30.62  ? 142  GLY   A CA  1 
ATOM   769  C  C   . GLY   A 1 142 ? 45.550 -7.268  10.582  1.00 32.35  ? 142  GLY   A C   1 
ATOM   770  O  O   . GLY   A 1 142 ? 44.783 -7.354  9.620   1.00 34.78  ? 142  GLY   A O   1 
ATOM   771  N  N   . LEU   A 1 143 ? 45.300 -7.841  11.756  1.00 31.06  ? 143  LEU   A N   1 
ATOM   772  C  CA  . LEU   A 1 143 ? 44.075 -8.609  11.981  1.00 30.80  ? 143  LEU   A CA  1 
ATOM   773  C  C   . LEU   A 1 143 ? 43.019 -7.750  12.646  1.00 28.56  ? 143  LEU   A C   1 
ATOM   774  O  O   . LEU   A 1 143 ? 43.346 -6.923  13.491  1.00 26.63  ? 143  LEU   A O   1 
ATOM   775  C  CB  . LEU   A 1 143 ? 44.374 -9.862  12.823  1.00 31.99  ? 143  LEU   A CB  1 
ATOM   776  C  CG  . LEU   A 1 143 ? 45.360 -10.844 12.161  1.00 35.63  ? 143  LEU   A CG  1 
ATOM   777  C  CD1 . LEU   A 1 143 ? 45.540 -12.066 13.001  1.00 36.72  ? 143  LEU   A CD1 1 
ATOM   778  C  CD2 . LEU   A 1 143 ? 44.895 -11.248 10.753  1.00 37.60  ? 143  LEU   A CD2 1 
ATOM   779  N  N   . PRO   A 1 144 ? 41.744 -7.971  12.310  1.00 28.21  ? 144  PRO   A N   1 
ATOM   780  C  CA  . PRO   A 1 144 ? 40.685 -7.180  12.951  1.00 26.71  ? 144  PRO   A CA  1 
ATOM   781  C  C   . PRO   A 1 144 ? 40.404 -7.596  14.392  1.00 24.09  ? 144  PRO   A C   1 
ATOM   782  O  O   . PRO   A 1 144 ? 40.442 -8.778  14.745  1.00 25.35  ? 144  PRO   A O   1 
ATOM   783  C  CB  . PRO   A 1 144 ? 39.461 -7.419  12.056  1.00 28.52  ? 144  PRO   A CB  1 
ATOM   784  C  CG  . PRO   A 1 144 ? 39.703 -8.721  11.406  1.00 29.93  ? 144  PRO   A CG  1 
ATOM   785  C  CD  . PRO   A 1 144 ? 41.205 -8.947  11.339  1.00 29.33  ? 144  PRO   A CD  1 
ATOM   786  N  N   . TYR   A 1 145 ? 40.190 -6.584  15.230  1.00 21.44  ? 145  TYR   A N   1 
ATOM   787  C  CA  . TYR   A 1 145 ? 39.729 -6.770  16.602  1.00 21.09  ? 145  TYR   A CA  1 
ATOM   788  C  C   . TYR   A 1 145 ? 38.586 -5.807  16.852  1.00 20.30  ? 145  TYR   A C   1 
ATOM   789  O  O   . TYR   A 1 145 ? 38.479 -4.780  16.158  1.00 19.39  ? 145  TYR   A O   1 
ATOM   790  C  CB  . TYR   A 1 145 ? 40.804 -6.417  17.608  1.00 21.10  ? 145  TYR   A CB  1 
ATOM   791  C  CG  . TYR   A 1 145 ? 41.925 -7.423  17.645  1.00 22.40  ? 145  TYR   A CG  1 
ATOM   792  C  CD1 . TYR   A 1 145 ? 42.977 -7.347  16.752  1.00 23.40  ? 145  TYR   A CD1 1 
ATOM   793  C  CD2 . TYR   A 1 145 ? 41.970 -8.399  18.623  1.00 23.07  ? 145  TYR   A CD2 1 
ATOM   794  C  CE1 . TYR   A 1 145 ? 44.020 -8.272  16.778  1.00 24.73  ? 145  TYR   A CE1 1 
ATOM   795  C  CE2 . TYR   A 1 145 ? 43.007 -9.322  18.665  1.00 23.73  ? 145  TYR   A CE2 1 
ATOM   796  C  CZ  . TYR   A 1 145 ? 44.029 -9.249  17.742  1.00 25.25  ? 145  TYR   A CZ  1 
ATOM   797  O  OH  . TYR   A 1 145 ? 45.082 -10.142 17.783  1.00 27.30  ? 145  TYR   A OH  1 
ATOM   798  N  N   . THR   A 1 146 ? 37.793 -6.077  17.860  1.00 19.18  ? 146  THR   A N   1 
ATOM   799  C  CA  . THR   A 1 146 ? 36.715 -5.171  18.230  1.00 19.90  ? 146  THR   A CA  1 
ATOM   800  C  C   . THR   A 1 146 ? 36.826 -4.799  19.684  1.00 19.45  ? 146  THR   A C   1 
ATOM   801  O  O   . THR   A 1 146 ? 36.794 -5.684  20.567  1.00 19.78  ? 146  THR   A O   1 
ATOM   802  C  CB  . THR   A 1 146 ? 35.338 -5.777  17.925  1.00 21.06  ? 146  THR   A CB  1 
ATOM   803  O  OG1 . THR   A 1 146 ? 35.243 -6.122  16.525  1.00 24.25  ? 146  THR   A OG1 1 
ATOM   804  C  CG2 . THR   A 1 146 ? 34.212 -4.806  18.275  1.00 20.32  ? 146  THR   A CG2 1 
ATOM   805  N  N   . VAL   A 1 147 ? 37.017 -3.519  19.977  1.00 18.97  ? 147  VAL   A N   1 
ATOM   806  C  CA  . VAL   A 1 147 ? 37.035 -3.036  21.342  1.00 19.09  ? 147  VAL   A CA  1 
ATOM   807  C  C   . VAL   A 1 147 ? 35.576 -2.760  21.767  1.00 18.31  ? 147  VAL   A C   1 
ATOM   808  O  O   . VAL   A 1 147 ? 34.860 -2.059  21.049  1.00 19.14  ? 147  VAL   A O   1 
ATOM   809  C  CB  . VAL   A 1 147 ? 37.848 -1.742  21.424  1.00 22.69  ? 147  VAL   A CB  1 
ATOM   810  C  CG1 . VAL   A 1 147 ? 37.792 -1.183  22.841  1.00 24.59  ? 147  VAL   A CG1 1 
ATOM   811  C  CG2 . VAL   A 1 147 ? 39.291 -2.000  21.003  1.00 23.83  ? 147  VAL   A CG2 1 
ATOM   812  N  N   . VAL   A 1 148 ? 35.130 -3.310  22.891  1.00 17.66  ? 148  VAL   A N   1 
ATOM   813  C  CA  . VAL   A 1 148 ? 33.766 -3.098  23.373  1.00 17.73  ? 148  VAL   A CA  1 
ATOM   814  C  C   . VAL   A 1 148 ? 33.845 -2.366  24.706  1.00 18.69  ? 148  VAL   A C   1 
ATOM   815  O  O   . VAL   A 1 148 ? 34.474 -2.859  25.643  1.00 20.01  ? 148  VAL   A O   1 
ATOM   816  C  CB  . VAL   A 1 148 ? 33.037 -4.457  23.540  1.00 18.68  ? 148  VAL   A CB  1 
ATOM   817  C  CG1 . VAL   A 1 148 ? 31.594 -4.227  24.027  1.00 19.60  ? 148  VAL   A CG1 1 
ATOM   818  C  CG2 . VAL   A 1 148 ? 33.028 -5.212  22.205  1.00 20.61  ? 148  VAL   A CG2 1 
ATOM   819  N  N   . ILE   A 1 149 ? 33.237 -1.177  24.805  1.00 17.86  ? 149  ILE   A N   1 
ATOM   820  C  CA  . ILE   A 1 149 ? 33.268 -0.378  26.002  1.00 17.58  ? 149  ILE   A CA  1 
ATOM   821  C  C   . ILE   A 1 149 ? 31.870 -0.039  26.470  1.00 17.79  ? 149  ILE   A C   1 
ATOM   822  O  O   . ILE   A 1 149 ? 31.067 0.537   25.718  1.00 17.33  ? 149  ILE   A O   1 
ATOM   823  C  CB  . ILE   A 1 149 ? 34.065 0.939   25.742  1.00 17.85  ? 149  ILE   A CB  1 
ATOM   824  C  CG1 . ILE   A 1 149 ? 35.495 0.594   25.236  1.00 19.41  ? 149  ILE   A CG1 1 
ATOM   825  C  CG2 . ILE   A 1 149 ? 34.155 1.792   27.029  1.00 18.33  ? 149  ILE   A CG2 1 
ATOM   826  C  CD1 . ILE   A 1 149 ? 36.252 1.877   24.767  1.00 21.42  ? 149  ILE   A CD1 1 
ATOM   827  N  N   . HIS   A 1 150 ? 31.577 -0.358  27.742  1.00 17.06  ? 150  HIS   A N   1 
ATOM   828  C  CA  . HIS   A 1 150 ? 30.320 -0.006  28.367  1.00 16.59  ? 150  HIS   A CA  1 
ATOM   829  C  C   . HIS   A 1 150 ? 30.576 1.157   29.291  1.00 16.32  ? 150  HIS   A C   1 
ATOM   830  O  O   . HIS   A 1 150 ? 31.569 1.192   30.033  1.00 16.54  ? 150  HIS   A O   1 
ATOM   831  C  CB  . HIS   A 1 150 ? 29.815 -1.201  29.200  1.00 17.70  ? 150  HIS   A CB  1 
ATOM   832  C  CG  . HIS   A 1 150 ? 29.461 -2.396  28.362  1.00 20.01  ? 150  HIS   A CG  1 
ATOM   833  N  ND1 . HIS   A 1 150 ? 28.168 -2.606  27.959  1.00 22.39  ? 150  HIS   A ND1 1 
ATOM   834  C  CD2 . HIS   A 1 150 ? 30.207 -3.472  28.017  1.00 22.60  ? 150  HIS   A CD2 1 
ATOM   835  C  CE1 . HIS   A 1 150 ? 28.175 -3.745  27.284  1.00 22.78  ? 150  HIS   A CE1 1 
ATOM   836  N  NE2 . HIS   A 1 150 ? 29.374 -4.303  27.295  1.00 23.65  ? 150  HIS   A NE2 1 
ATOM   837  N  N   . TYR   A 1 151 ? 29.699 2.201   29.203  1.00 16.01  ? 151  TYR   A N   1 
ATOM   838  C  CA  . TYR   A 1 151 ? 29.927 3.393   29.995  1.00 15.90  ? 151  TYR   A CA  1 
ATOM   839  C  C   . TYR   A 1 151 ? 28.652 4.130   30.300  1.00 15.42  ? 151  TYR   A C   1 
ATOM   840  O  O   . TYR   A 1 151 ? 27.577 3.842   29.740  1.00 15.57  ? 151  TYR   A O   1 
ATOM   841  C  CB  . TYR   A 1 151 ? 30.906 4.367   29.258  1.00 16.23  ? 151  TYR   A CB  1 
ATOM   842  C  CG  . TYR   A 1 151 ? 30.330 4.861   27.948  1.00 15.42  ? 151  TYR   A CG  1 
ATOM   843  C  CD1 . TYR   A 1 151 ? 30.417 4.092   26.800  1.00 15.19  ? 151  TYR   A CD1 1 
ATOM   844  C  CD2 . TYR   A 1 151 ? 29.630 6.053   27.884  1.00 15.71  ? 151  TYR   A CD2 1 
ATOM   845  C  CE1 . TYR   A 1 151 ? 29.839 4.512   25.607  1.00 15.09  ? 151  TYR   A CE1 1 
ATOM   846  C  CE2 . TYR   A 1 151 ? 29.038 6.478   26.705  1.00 15.90  ? 151  TYR   A CE2 1 
ATOM   847  C  CZ  . TYR   A 1 151 ? 29.164 5.713   25.566  1.00 16.04  ? 151  TYR   A CZ  1 
ATOM   848  O  OH  . TYR   A 1 151 ? 28.571 6.161   24.419  1.00 15.46  ? 151  TYR   A OH  1 
ATOM   849  N  N   . ALA   A 1 152 ? 28.779 5.145   31.168  1.00 16.54  ? 152  ALA   A N   1 
ATOM   850  C  CA  . ALA   A 1 152 ? 27.661 6.000   31.510  1.00 17.14  ? 152  ALA   A CA  1 
ATOM   851  C  C   . ALA   A 1 152 ? 28.164 7.446   31.510  1.00 17.01  ? 152  ALA   A C   1 
ATOM   852  O  O   . ALA   A 1 152 ? 29.334 7.705   31.723  1.00 17.32  ? 152  ALA   A O   1 
ATOM   853  C  CB  . ALA   A 1 152 ? 27.139 5.631   32.900  1.00 17.98  ? 152  ALA   A CB  1 
ATOM   854  N  N   . GLY   A 1 153 ? 27.238 8.367   31.341  1.00 17.10  ? 153  GLY   A N   1 
ATOM   855  C  CA  . GLY   A 1 153 ? 27.544 9.775   31.448  1.00 17.40  ? 153  GLY   A CA  1 
ATOM   856  C  C   . GLY   A 1 153 ? 26.304 10.533  31.870  1.00 17.08  ? 153  GLY   A C   1 
ATOM   857  O  O   . GLY   A 1 153 ? 25.228 9.966   32.111  1.00 16.90  ? 153  GLY   A O   1 
ATOM   858  N  N   . GLN   A 1 154 ? 26.485 11.856  31.993  1.00 17.04  ? 154  GLN   A N   1 
ATOM   859  C  CA  . GLN   A 1 154 ? 25.352 12.704  32.296  1.00 16.35  ? 154  GLN   A CA  1 
ATOM   860  C  C   . GLN   A 1 154 ? 25.231 13.669  31.118  1.00 15.89  ? 154  GLN   A C   1 
ATOM   861  O  O   . GLN   A 1 154 ? 26.252 14.163  30.629  1.00 16.47  ? 154  GLN   A O   1 
ATOM   862  C  CB  . GLN   A 1 154 ? 25.565 13.521  33.578  1.00 20.61  ? 154  GLN   A CB  1 
ATOM   863  C  CG  . GLN   A 1 154 ? 25.543 12.669  34.847  1.00 25.96  ? 154  GLN   A CG  1 
ATOM   864  C  CD  . GLN   A 1 154 ? 24.146 12.125  35.130  1.00 34.51  ? 154  GLN   A CD  1 
ATOM   865  O  OE1 . GLN   A 1 154 ? 23.117 12.844  35.131  1.00 37.72  ? 154  GLN   A OE1 1 
ATOM   866  N  NE2 . GLN   A 1 154 ? 24.074 10.832  35.384  1.00 35.14  ? 154  GLN   A NE2 1 
ATOM   867  N  N   . LEU   A 1 155 ? 24.007 13.988  30.673  1.00 14.83  ? 155  LEU   A N   1 
ATOM   868  C  CA  . LEU   A 1 155 ? 23.824 14.954  29.584  1.00 15.70  ? 155  LEU   A CA  1 
ATOM   869  C  C   . LEU   A 1 155 ? 24.490 16.264  29.970  1.00 15.18  ? 155  LEU   A C   1 
ATOM   870  O  O   . LEU   A 1 155 ? 24.418 16.685  31.142  1.00 15.69  ? 155  LEU   A O   1 
ATOM   871  C  CB  . LEU   A 1 155 ? 22.343 15.204  29.318  1.00 16.62  ? 155  LEU   A CB  1 
ATOM   872  C  CG  . LEU   A 1 155 ? 21.535 14.050  28.691  1.00 18.85  ? 155  LEU   A CG  1 
ATOM   873  C  CD1 . LEU   A 1 155 ? 20.056 14.443  28.564  1.00 20.06  ? 155  LEU   A CD1 1 
ATOM   874  C  CD2 . LEU   A 1 155 ? 22.108 13.623  27.331  1.00 19.66  ? 155  LEU   A CD2 1 
ATOM   875  N  N   . SER   A 1 156 ? 25.162 16.881  28.991  1.00 14.21  ? 156  SER   A N   1 
ATOM   876  C  CA  . SER   A 1 156 ? 25.849 18.122  29.327  1.00 14.53  ? 156  SER   A CA  1 
ATOM   877  C  C   . SER   A 1 156 ? 24.847 19.253  29.530  1.00 14.30  ? 156  SER   A C   1 
ATOM   878  O  O   . SER   A 1 156 ? 23.801 19.326  28.852  1.00 14.90  ? 156  SER   A O   1 
ATOM   879  C  CB  . SER   A 1 156 ? 26.754 18.506  28.163  1.00 15.70  ? 156  SER   A CB  1 
ATOM   880  O  OG  . SER   A 1 156 ? 27.537 19.624  28.571  1.00 16.72  ? 156  SER   A OG  1 
ATOM   881  N  N   . GLU   A 1 157 ? 25.190 20.140  30.472  1.00 14.43  ? 157  GLU   A N   1 
ATOM   882  C  CA  . GLU   A 1 157 ? 24.432 21.363  30.663  1.00 14.58  ? 157  GLU   A CA  1 
ATOM   883  C  C   . GLU   A 1 157 ? 25.046 22.524  29.845  1.00 15.02  ? 157  GLU   A C   1 
ATOM   884  O  O   . GLU   A 1 157 ? 24.610 23.660  29.996  1.00 15.97  ? 157  GLU   A O   1 
ATOM   885  C  CB  . GLU   A 1 157 ? 24.341 21.725  32.150  1.00 17.25  ? 157  GLU   A CB  1 
ATOM   886  C  CG  . GLU   A 1 157 ? 23.610 20.637  32.918  1.00 19.92  ? 157  GLU   A CG  1 
ATOM   887  C  CD  . GLU   A 1 157 ? 22.103 20.746  32.755  1.00 25.47  ? 157  GLU   A CD  1 
ATOM   888  O  OE1 . GLU   A 1 157 ? 21.606 21.874  32.530  1.00 27.95  ? 157  GLU   A OE1 1 
ATOM   889  O  OE2 . GLU   A 1 157 ? 21.409 19.709  32.874  1.00 30.20  ? 157  GLU   A OE2 1 
ATOM   890  N  N   . THR   A 1 158 ? 26.024 22.221  29.005  1.00 13.53  ? 158  THR   A N   1 
ATOM   891  C  CA  . THR   A 1 158 ? 26.608 23.215  28.091  1.00 13.96  ? 158  THR   A CA  1 
ATOM   892  C  C   . THR   A 1 158 ? 25.877 23.093  26.748  1.00 14.53  ? 158  THR   A C   1 
ATOM   893  O  O   . THR   A 1 158 ? 24.805 22.501  26.660  1.00 14.72  ? 158  THR   A O   1 
ATOM   894  C  CB  . THR   A 1 158 ? 28.103 22.911  27.932  1.00 14.58  ? 158  THR   A CB  1 
ATOM   895  O  OG1 . THR   A 1 158 ? 28.295 21.781  27.092  1.00 14.75  ? 158  THR   A OG1 1 
ATOM   896  C  CG2 . THR   A 1 158 ? 28.813 22.739  29.263  1.00 15.51  ? 158  THR   A CG2 1 
ATOM   897  N  N   . PHE   A 1 159 ? 26.462 23.701  25.700  1.00 13.64  ? 159  PHE   A N   1 
ATOM   898  C  CA  . PHE   A 1 159 ? 25.957 23.542  24.338  1.00 13.48  ? 159  PHE   A CA  1 
ATOM   899  C  C   . PHE   A 1 159 ? 26.809 22.588  23.490  1.00 13.85  ? 159  PHE   A C   1 
ATOM   900  O  O   . PHE   A 1 159 ? 26.736 22.606  22.270  1.00 14.29  ? 159  PHE   A O   1 
ATOM   901  C  CB  . PHE   A 1 159 ? 25.915 24.903  23.619  1.00 13.33  ? 159  PHE   A CB  1 
ATOM   902  C  CG  . PHE   A 1 159 ? 25.119 25.966  24.313  1.00 14.48  ? 159  PHE   A CG  1 
ATOM   903  C  CD1 . PHE   A 1 159 ? 23.759 26.013  24.185  1.00 18.88  ? 159  PHE   A CD1 1 
ATOM   904  C  CD2 . PHE   A 1 159 ? 25.745 27.015  24.953  1.00 15.60  ? 159  PHE   A CD2 1 
ATOM   905  C  CE1 . PHE   A 1 159 ? 23.032 27.063  24.727  1.00 20.22  ? 159  PHE   A CE1 1 
ATOM   906  C  CE2 . PHE   A 1 159 ? 25.020 28.049  25.531  1.00 16.61  ? 159  PHE   A CE2 1 
ATOM   907  C  CZ  . PHE   A 1 159 ? 23.668 28.072  25.424  1.00 17.88  ? 159  PHE   A CZ  1 
ATOM   908  N  N   . HIS   A 1 160 ? 27.607 21.742  24.141  1.00 13.21  ? 160  HIS   A N   1 
ATOM   909  C  CA  . HIS   A 1 160 ? 28.433 20.800  23.390  1.00 13.04  ? 160  HIS   A CA  1 
ATOM   910  C  C   . HIS   A 1 160 ? 28.364 19.408  24.034  1.00 13.09  ? 160  HIS   A C   1 
ATOM   911  O  O   . HIS   A 1 160 ? 27.816 19.243  25.100  1.00 13.89  ? 160  HIS   A O   1 
ATOM   912  C  CB  . HIS   A 1 160 ? 29.893 21.282  23.284  1.00 13.45  ? 160  HIS   A CB  1 
ATOM   913  C  CG  . HIS   A 1 160 ? 30.583 21.342  24.586  1.00 15.18  ? 160  HIS   A CG  1 
ATOM   914  N  ND1 . HIS   A 1 160 ? 30.572 22.487  25.356  1.00 16.42  ? 160  HIS   A ND1 1 
ATOM   915  C  CD2 . HIS   A 1 160 ? 31.346 20.405  25.210  1.00 15.44  ? 160  HIS   A CD2 1 
ATOM   916  C  CE1 . HIS   A 1 160 ? 31.253 22.190  26.464  1.00 17.74  ? 160  HIS   A CE1 1 
ATOM   917  N  NE2 . HIS   A 1 160 ? 31.716 20.944  26.433  1.00 16.64  ? 160  HIS   A NE2 1 
ATOM   918  N  N   . GLY   A 1 161 ? 28.869 18.438  23.300  1.00 12.87  ? 161  GLY   A N   1 
ATOM   919  C  CA  . GLY   A 1 161 ? 28.721 17.042  23.702  1.00 12.98  ? 161  GLY   A CA  1 
ATOM   920  C  C   . GLY   A 1 161 ? 27.302 16.605  23.401  1.00 12.59  ? 161  GLY   A C   1 
ATOM   921  O  O   . GLY   A 1 161 ? 26.638 17.098  22.477  1.00 13.11  ? 161  GLY   A O   1 
ATOM   922  N  N   . PHE   A 1 162 ? 26.800 15.665  24.197  1.00 12.49  ? 162  PHE   A N   1 
ATOM   923  C  CA  . PHE   A 1 162 ? 25.402 15.224  24.121  1.00 12.95  ? 162  PHE   A CA  1 
ATOM   924  C  C   . PHE   A 1 162 ? 24.736 16.024  25.221  1.00 13.98  ? 162  PHE   A C   1 
ATOM   925  O  O   . PHE   A 1 162 ? 24.955 15.778  26.405  1.00 14.21  ? 162  PHE   A O   1 
ATOM   926  C  CB  . PHE   A 1 162 ? 25.382 13.721  24.417  1.00 13.19  ? 162  PHE   A CB  1 
ATOM   927  C  CG  . PHE   A 1 162 ? 24.064 12.999  24.262  1.00 13.47  ? 162  PHE   A CG  1 
ATOM   928  C  CD1 . PHE   A 1 162 ? 23.055 13.505  23.450  1.00 14.10  ? 162  PHE   A CD1 1 
ATOM   929  C  CD2 . PHE   A 1 162 ? 23.877 11.764  24.848  1.00 14.63  ? 162  PHE   A CD2 1 
ATOM   930  C  CE1 . PHE   A 1 162 ? 21.874 12.793  23.244  1.00 14.69  ? 162  PHE   A CE1 1 
ATOM   931  C  CE2 . PHE   A 1 162 ? 22.695 11.057  24.664  1.00 15.04  ? 162  PHE   A CE2 1 
ATOM   932  C  CZ  . PHE   A 1 162 ? 21.684 11.583  23.886  1.00 15.75  ? 162  PHE   A CZ  1 
ATOM   933  N  N   . TYR   A 1 163 ? 23.966 17.053  24.851  1.00 13.01  ? 163  TYR   A N   1 
ATOM   934  C  CA  . TYR   A 1 163 ? 23.528 18.058  25.783  1.00 12.70  ? 163  TYR   A CA  1 
ATOM   935  C  C   . TYR   A 1 163 ? 22.028 18.224  25.859  1.00 13.18  ? 163  TYR   A C   1 
ATOM   936  O  O   . TYR   A 1 163 ? 21.275 17.842  24.959  1.00 14.22  ? 163  TYR   A O   1 
ATOM   937  C  CB  . TYR   A 1 163 ? 24.203 19.440  25.457  1.00 12.95  ? 163  TYR   A CB  1 
ATOM   938  C  CG  . TYR   A 1 163 ? 23.726 20.140  24.192  1.00 12.22  ? 163  TYR   A CG  1 
ATOM   939  C  CD1 . TYR   A 1 163 ? 24.332 19.897  22.971  1.00 12.59  ? 163  TYR   A CD1 1 
ATOM   940  C  CD2 . TYR   A 1 163 ? 22.722 21.091  24.244  1.00 12.38  ? 163  TYR   A CD2 1 
ATOM   941  C  CE1 . TYR   A 1 163 ? 23.950 20.580  21.834  1.00 12.66  ? 163  TYR   A CE1 1 
ATOM   942  C  CE2 . TYR   A 1 163 ? 22.351 21.795  23.116  1.00 13.20  ? 163  TYR   A CE2 1 
ATOM   943  C  CZ  . TYR   A 1 163 ? 22.982 21.545  21.916  1.00 12.93  ? 163  TYR   A CZ  1 
ATOM   944  O  OH  . TYR   A 1 163 ? 22.628 22.252  20.784  1.00 13.38  ? 163  TYR   A OH  1 
ATOM   945  N  N   . LYS   A 1 164 ? 21.600 18.799  26.972  1.00 13.25  ? 164  LYS   A N   1 
ATOM   946  C  CA  . LYS   A 1 164 ? 20.170 19.030  27.199  1.00 13.71  ? 164  LYS   A CA  1 
ATOM   947  C  C   . LYS   A 1 164 ? 19.700 20.328  26.572  1.00 14.20  ? 164  LYS   A C   1 
ATOM   948  O  O   . LYS   A 1 164 ? 20.378 21.344  26.684  1.00 15.12  ? 164  LYS   A O   1 
ATOM   949  C  CB  . LYS   A 1 164 ? 19.953 19.149  28.728  1.00 16.26  ? 164  LYS   A CB  1 
ATOM   950  C  CG  . LYS   A 1 164 ? 18.494 19.385  29.130  1.00 17.53  ? 164  LYS   A CG  1 
ATOM   951  C  CD  . LYS   A 1 164 ? 18.377 19.491  30.648  1.00 23.10  ? 164  LYS   A CD  1 
ATOM   952  C  CE  . LYS   A 1 164 ? 18.751 20.870  31.082  1.00 30.56  ? 164  LYS   A CE  1 
ATOM   953  N  NZ  . LYS   A 1 164 ? 18.621 21.016  32.566  1.00 33.76  ? 164  LYS   A NZ  1 
ATOM   954  N  N   . SER   A 1 165 ? 18.549 20.312  25.930  1.00 12.90  ? 165  SER   A N   1 
ATOM   955  C  CA  . SER   A 1 165 ? 17.940 21.522  25.390  1.00 13.83  ? 165  SER   A CA  1 
ATOM   956  C  C   . SER   A 1 165 ? 16.463 21.509  25.869  1.00 15.36  ? 165  SER   A C   1 
ATOM   957  O  O   . SER   A 1 165 ? 15.904 20.435  26.129  1.00 15.58  ? 165  SER   A O   1 
ATOM   958  C  CB  . SER   A 1 165 ? 18.029 21.516  23.855  1.00 14.67  ? 165  SER   A CB  1 
ATOM   959  O  OG  . SER   A 1 165 ? 17.351 22.626  23.273  1.00 14.88  ? 165  SER   A OG  1 
ATOM   960  N  N   . THR   A 1 166 ? 15.874 22.684  26.110  1.00 14.38  ? 166  THR   A N   1 
ATOM   961  C  CA  . THR   A 1 166 ? 14.494 22.740  26.590  1.00 14.14  ? 166  THR   A CA  1 
ATOM   962  C  C   . THR   A 1 166 ? 13.751 23.823  25.869  1.00 15.00  ? 166  THR   A C   1 
ATOM   963  O  O   . THR   A 1 166 ? 14.326 24.758  25.285  1.00 15.36  ? 166  THR   A O   1 
ATOM   964  C  CB  . THR   A 1 166 ? 14.456 23.061  28.136  1.00 17.31  ? 166  THR   A CB  1 
ATOM   965  O  OG1 . THR   A 1 166 ? 14.897 24.422  28.350  1.00 19.34  ? 166  THR   A OG1 1 
ATOM   966  C  CG2 . THR   A 1 166 ? 15.287 22.097  28.962  1.00 18.23  ? 166  THR   A CG2 1 
ATOM   967  N  N   . TYR   A 1 167 ? 12.429 23.737  25.955  1.00 14.94  ? 167  TYR   A N   1 
ATOM   968  C  CA  . TYR   A 1 167 ? 11.601 24.824  25.511  1.00 15.43  ? 167  TYR   A CA  1 
ATOM   969  C  C   . TYR   A 1 167 ? 10.265 24.721  26.195  1.00 16.04  ? 167  TYR   A C   1 
ATOM   970  O  O   . TYR   A 1 167 ? 9.964  23.679  26.769  1.00 16.96  ? 167  TYR   A O   1 
ATOM   971  C  CB  . TYR   A 1 167 ? 11.498 24.807  23.986  1.00 16.40  ? 167  TYR   A CB  1 
ATOM   972  C  CG  . TYR   A 1 167 ? 10.537 23.796  23.461  1.00 17.74  ? 167  TYR   A CG  1 
ATOM   973  C  CD1 . TYR   A 1 167 ? 10.921 22.474  23.248  1.00 19.69  ? 167  TYR   A CD1 1 
ATOM   974  C  CD2 . TYR   A 1 167 ? 9.271  24.177  23.082  1.00 21.32  ? 167  TYR   A CD2 1 
ATOM   975  C  CE1 . TYR   A 1 167 ? 9.992  21.531  22.798  1.00 20.50  ? 167  TYR   A CE1 1 
ATOM   976  C  CE2 . TYR   A 1 167 ? 8.356  23.265  22.631  1.00 22.87  ? 167  TYR   A CE2 1 
ATOM   977  C  CZ  . TYR   A 1 167 ? 8.715  21.967  22.465  1.00 22.47  ? 167  TYR   A CZ  1 
ATOM   978  O  OH  . TYR   A 1 167 ? 7.721  21.236  21.887  1.00 27.98  ? 167  TYR   A OH  1 
ATOM   979  N  N   . ARG   A 1 168 ? 9.463  25.772  26.102  1.00 16.75  ? 168  ARG   A N   1 
ATOM   980  C  CA  . ARG   A 1 168 ? 8.144  25.750  26.728  1.00 18.29  ? 168  ARG   A CA  1 
ATOM   981  C  C   . ARG   A 1 168 ? 7.091  25.754  25.649  1.00 19.64  ? 168  ARG   A C   1 
ATOM   982  O  O   . ARG   A 1 168 ? 7.194  26.533  24.708  1.00 19.36  ? 168  ARG   A O   1 
ATOM   983  C  CB  . ARG   A 1 168 ? 7.978  27.001  27.618  1.00 22.48  ? 168  ARG   A CB  1 
ATOM   984  C  CG  . ARG   A 1 168 ? 8.820  26.911  28.886  1.00 30.61  ? 168  ARG   A CG  1 
ATOM   985  C  CD  . ARG   A 1 168 ? 8.256  27.642  30.100  1.00 37.01  ? 168  ARG   A CD  1 
ATOM   986  N  NE  . ARG   A 1 168 ? 8.973  27.254  31.320  1.00 40.92  ? 168  ARG   A NE  1 
ATOM   987  C  CZ  . ARG   A 1 168 ? 8.507  26.402  32.228  1.00 42.94  ? 168  ARG   A CZ  1 
ATOM   988  N  NH1 . ARG   A 1 168 ? 7.304  25.864  32.088  1.00 43.44  ? 168  ARG   A NH1 1 
ATOM   989  N  NH2 . ARG   A 1 168 ? 9.228  26.107  33.300  1.00 44.25  ? 168  ARG   A NH2 1 
ATOM   990  N  N   . THR   A 1 169 ? 6.087  24.895  25.786  1.00 21.43  ? 169  THR   A N   1 
ATOM   991  C  CA  . THR   A 1 169 ? 4.998  24.920  24.789  1.00 23.26  ? 169  THR   A CA  1 
ATOM   992  C  C   . THR   A 1 169 ? 4.179  26.190  24.964  1.00 24.96  ? 169  THR   A C   1 
ATOM   993  O  O   . THR   A 1 169 ? 4.235  26.841  26.034  1.00 22.72  ? 169  THR   A O   1 
ATOM   994  C  CB  . THR   A 1 169 ? 4.160  23.680  24.814  1.00 25.46  ? 169  THR   A CB  1 
ATOM   995  O  OG1 . THR   A 1 169 ? 3.454  23.665  26.044  1.00 25.50  ? 169  THR   A OG1 1 
ATOM   996  C  CG2 . THR   A 1 169 ? 4.993  22.412  24.662  1.00 26.15  ? 169  THR   A CG2 1 
ATOM   997  N  N   . LYS   A 1 170 ? 3.431  26.577  23.898  1.00 27.43  ? 170  LYS   A N   1 
ATOM   998  C  CA  . LYS   A 1 170 ? 2.604  27.790  24.020  1.00 30.37  ? 170  LYS   A CA  1 
ATOM   999  C  C   . LYS   A 1 170 ? 1.572  27.660  25.151  1.00 33.07  ? 170  LYS   A C   1 
ATOM   1000 O  O   . LYS   A 1 170 ? 1.165  28.652  25.784  1.00 34.18  ? 170  LYS   A O   1 
ATOM   1001 C  CB  . LYS   A 1 170 ? 1.981  28.209  22.670  1.00 32.63  ? 170  LYS   A CB  1 
ATOM   1002 C  CG  . LYS   A 1 170 ? 1.230  27.122  21.926  1.00 36.64  ? 170  LYS   A CG  1 
ATOM   1003 C  CD  . LYS   A 1 170 ? 0.947  27.553  20.487  1.00 40.25  ? 170  LYS   A CD  1 
ATOM   1004 C  CE  . LYS   A 1 170 ? -0.031 26.597  19.845  1.00 43.23  ? 170  LYS   A CE  1 
ATOM   1005 N  NZ  . LYS   A 1 170 ? 0.319  25.198  20.161  1.00 43.91  ? 170  LYS   A NZ  1 
ATOM   1006 N  N   . GLU   A 1 171 ? 1.271  26.409  25.495  1.00 33.93  ? 171  GLU   A N   1 
ATOM   1007 C  CA  . GLU   A 1 171 ? 0.395  25.989  26.536  1.00 34.08  ? 171  GLU   A CA  1 
ATOM   1008 C  C   . GLU   A 1 171 ? 1.067  26.005  27.946  1.00 35.18  ? 171  GLU   A C   1 
ATOM   1009 O  O   . GLU   A 1 171 ? 0.373  25.803  28.926  1.00 36.67  ? 171  GLU   A O   1 
ATOM   1010 C  CB  . GLU   A 1 171 ? -0.197 24.609  26.126  1.00 34.76  ? 171  GLU   A CB  1 
ATOM   1011 C  CG  . GLU   A 1 171 ? -0.971 24.668  24.794  1.00 36.19  ? 171  GLU   A CG  1 
ATOM   1012 C  CD  . GLU   A 1 171 ? -0.208 24.169  23.570  1.00 39.25  ? 171  GLU   A CD  1 
ATOM   1013 O  OE1 . GLU   A 1 171 ? 0.918  23.658  23.762  1.00 36.79  ? 171  GLU   A OE1 1 
ATOM   1014 O  OE2 . GLU   A 1 171 ? -0.725 24.285  22.428  1.00 36.84  ? 171  GLU   A OE2 1 
ATOM   1015 N  N   . GLY   A 1 172 ? 2.397  26.239  28.036  1.00 33.68  ? 172  GLY   A N   1 
ATOM   1016 C  CA  . GLY   A 1 172 ? 3.165  26.378  29.279  1.00 32.41  ? 172  GLY   A CA  1 
ATOM   1017 C  C   . GLY   A 1 172 ? 4.007  25.206  29.784  1.00 31.33  ? 172  GLY   A C   1 
ATOM   1018 O  O   . GLY   A 1 172 ? 4.695  25.325  30.798  1.00 31.92  ? 172  GLY   A O   1 
ATOM   1019 N  N   . GLU   A 1 173 ? 3.974  24.075  29.089  1.00 29.38  ? 173  GLU   A N   1 
ATOM   1020 C  CA  . GLU   A 1 173 ? 4.676  22.869  29.508  1.00 28.51  ? 173  GLU   A CA  1 
ATOM   1021 C  C   . GLU   A 1 173 ? 6.185  22.934  29.180  1.00 26.88  ? 173  GLU   A C   1 
ATOM   1022 O  O   . GLU   A 1 173 ? 6.540  23.174  28.029  1.00 25.64  ? 173  GLU   A O   1 
ATOM   1023 C  CB  . GLU   A 1 173 ? 4.057  21.659  28.779  1.00 31.23  ? 173  GLU   A CB  1 
ATOM   1024 C  CG  . GLU   A 1 173 ? 4.698  20.316  29.134  1.00 37.86  ? 173  GLU   A CG  1 
ATOM   1025 C  CD  . GLU   A 1 173 ? 4.583  19.251  28.052  1.00 45.65  ? 173  GLU   A CD  1 
ATOM   1026 O  OE1 . GLU   A 1 173 ? 3.709  19.384  27.163  1.00 48.04  ? 173  GLU   A OE1 1 
ATOM   1027 O  OE2 . GLU   A 1 173 ? 5.366  18.275  28.099  1.00 47.73  ? 173  GLU   A OE2 1 
ATOM   1028 N  N   . LEU   A 1 174 ? 7.053  22.689  30.165  1.00 25.82  ? 174  LEU   A N   1 
ATOM   1029 C  CA  . LEU   A 1 174 ? 8.497  22.599  29.892  1.00 25.59  ? 174  LEU   A CA  1 
ATOM   1030 C  C   . LEU   A 1 174 ? 8.761  21.227  29.199  1.00 24.38  ? 174  LEU   A C   1 
ATOM   1031 O  O   . LEU   A 1 174 ? 8.272  20.195  29.644  1.00 26.98  ? 174  LEU   A O   1 
ATOM   1032 C  CB  . LEU   A 1 174 ? 9.287  22.702  31.203  1.00 27.58  ? 174  LEU   A CB  1 
ATOM   1033 C  CG  . LEU   A 1 174 ? 10.817 22.674  31.054  1.00 31.13  ? 174  LEU   A CG  1 
ATOM   1034 C  CD1 . LEU   A 1 174 ? 11.317 23.841  30.228  1.00 31.39  ? 174  LEU   A CD1 1 
ATOM   1035 C  CD2 . LEU   A 1 174 ? 11.499 22.646  32.419  1.00 33.52  ? 174  LEU   A CD2 1 
ATOM   1036 N  N   . ARG   A 1 175 ? 9.443  21.228  28.053  1.00 19.06  ? 175  ARG   A N   1 
ATOM   1037 C  CA  . ARG   A 1 175 ? 9.774  20.019  27.325  1.00 17.14  ? 175  ARG   A CA  1 
ATOM   1038 C  C   . ARG   A 1 175 ? 11.289 19.907  27.271  1.00 16.19  ? 175  ARG   A C   1 
ATOM   1039 O  O   . ARG   A 1 175 ? 11.974 20.904  27.069  1.00 17.61  ? 175  ARG   A O   1 
ATOM   1040 C  CB  . ARG   A 1 175 ? 9.248  20.067  25.858  1.00 17.36  ? 175  ARG   A CB  1 
ATOM   1041 C  CG  . ARG   A 1 175 ? 7.701  20.093  25.772  1.00 22.74  ? 175  ARG   A CG  1 
ATOM   1042 C  CD  . ARG   A 1 175 ? 7.180  18.778  25.263  1.00 28.08  ? 175  ARG   A CD  1 
ATOM   1043 N  NE  . ARG   A 1 175 ? 5.713  18.742  25.189  1.00 31.64  ? 175  ARG   A NE  1 
ATOM   1044 C  CZ  . ARG   A 1 175 ? 5.008  18.833  24.062  1.00 38.12  ? 175  ARG   A CZ  1 
ATOM   1045 N  NH1 . ARG   A 1 175 ? 5.622  19.029  22.898  1.00 39.54  ? 175  ARG   A NH1 1 
ATOM   1046 N  NH2 . ARG   A 1 175 ? 3.682  18.755  24.092  1.00 37.13  ? 175  ARG   A NH2 1 
ATOM   1047 N  N   . ILE   A 1 176 ? 11.798 18.702  27.464  1.00 15.67  ? 176  ILE   A N   1 
ATOM   1048 C  CA  . ILE   A 1 176 ? 13.225 18.440  27.495  1.00 16.54  ? 176  ILE   A CA  1 
ATOM   1049 C  C   . ILE   A 1 176 ? 13.580 17.565  26.322  1.00 17.16  ? 176  ILE   A C   1 
ATOM   1050 O  O   . ILE   A 1 176 ? 12.881 16.560  26.050  1.00 17.88  ? 176  ILE   A O   1 
ATOM   1051 C  CB  . ILE   A 1 176 ? 13.575 17.702  28.805  1.00 19.52  ? 176  ILE   A CB  1 
ATOM   1052 C  CG1 . ILE   A 1 176 ? 13.211 18.588  30.023  1.00 24.22  ? 176  ILE   A CG1 1 
ATOM   1053 C  CG2 . ILE   A 1 176 ? 15.043 17.300  28.831  1.00 21.54  ? 176  ILE   A CG2 1 
ATOM   1054 C  CD1 . ILE   A 1 176 ? 13.449 17.910  31.408  1.00 27.65  ? 176  ILE   A CD1 1 
ATOM   1055 N  N   . LEU   A 1 177 ? 14.642 17.959  25.590  1.00 15.20  ? 177  LEU   A N   1 
ATOM   1056 C  CA  . LEU   A 1 177 ? 15.161 17.120  24.504  1.00 14.71  ? 177  LEU   A CA  1 
ATOM   1057 C  C   . LEU   A 1 177 ? 16.671 16.955  24.695  1.00 13.77  ? 177  LEU   A C   1 
ATOM   1058 O  O   . LEU   A 1 177 ? 17.252 17.606  25.556  1.00 14.56  ? 177  LEU   A O   1 
ATOM   1059 C  CB  . LEU   A 1 177 ? 14.886 17.739  23.122  1.00 15.59  ? 177  LEU   A CB  1 
ATOM   1060 C  CG  . LEU   A 1 177 ? 15.504 19.096  22.852  1.00 17.53  ? 177  LEU   A CG  1 
ATOM   1061 C  CD1 . LEU   A 1 177 ? 16.121 19.125  21.459  1.00 18.55  ? 177  LEU   A CD1 1 
ATOM   1062 C  CD2 . LEU   A 1 177 ? 14.445 20.213  23.010  1.00 18.87  ? 177  LEU   A CD2 1 
ATOM   1063 N  N   . ALA   A 1 178 ? 17.284 16.099  23.894  1.00 13.22  ? 178  ALA   A N   1 
ATOM   1064 C  CA  . ALA   A 1 178 ? 18.744 15.901  23.978  1.00 13.68  ? 178  ALA   A CA  1 
ATOM   1065 C  C   . ALA   A 1 178 ? 19.254 15.955  22.579  1.00 13.35  ? 178  ALA   A C   1 
ATOM   1066 O  O   . ALA   A 1 178 ? 18.660 15.365  21.663  1.00 13.76  ? 178  ALA   A O   1 
ATOM   1067 C  CB  . ALA   A 1 178 ? 19.060 14.542  24.580  1.00 15.32  ? 178  ALA   A CB  1 
ATOM   1068 N  N   . SER   A 1 179 ? 20.372 16.678  22.373  1.00 12.30  ? 179  SER   A N   1 
ATOM   1069 C  CA  . SER   A 1 179 ? 20.926 16.847  21.021  1.00 12.39  ? 179  SER   A CA  1 
ATOM   1070 C  C   . SER   A 1 179 ? 22.441 16.835  21.119  1.00 12.39  ? 179  SER   A C   1 
ATOM   1071 O  O   . SER   A 1 179 ? 22.986 16.767  22.227  1.00 13.75  ? 179  SER   A O   1 
ATOM   1072 C  CB  . SER   A 1 179 ? 20.411 18.181  20.437  1.00 13.40  ? 179  SER   A CB  1 
ATOM   1073 O  OG  . SER   A 1 179 ? 20.673 18.249  19.044  1.00 14.83  ? 179  SER   A OG  1 
ATOM   1074 N  N   . THR   A 1 180 ? 23.113 16.790  19.989  1.00 12.06  ? 180  THR   A N   1 
ATOM   1075 C  CA  . THR   A 1 180 ? 24.571 16.717  19.958  1.00 11.87  ? 180  THR   A CA  1 
ATOM   1076 C  C   . THR   A 1 180 ? 25.214 17.889  19.274  1.00 12.14  ? 180  THR   A C   1 
ATOM   1077 O  O   . THR   A 1 180 ? 24.620 18.507  18.355  1.00 12.49  ? 180  THR   A O   1 
ATOM   1078 C  CB  . THR   A 1 180 ? 25.020 15.421  19.257  1.00 12.49  ? 180  THR   A CB  1 
ATOM   1079 O  OG1 . THR   A 1 180 ? 24.465 15.410  17.937  1.00 13.07  ? 180  THR   A OG1 1 
ATOM   1080 C  CG2 . THR   A 1 180 ? 24.577 14.182  20.021  1.00 12.49  ? 180  THR   A CG2 1 
ATOM   1081 N  N   . GLN   A 1 181 ? 26.413 18.227  19.752  1.00 12.30  ? 181  GLN   A N   1 
ATOM   1082 C  CA  . GLN   A 1 181 ? 27.266 19.196  19.037  1.00 12.30  ? 181  GLN   A CA  1 
ATOM   1083 C  C   . GLN   A 1 181 ? 28.698 18.736  19.342  1.00 12.92  ? 181  GLN   A C   1 
ATOM   1084 O  O   . GLN   A 1 181 ? 29.144 18.861  20.494  1.00 13.43  ? 181  GLN   A O   1 
ATOM   1085 C  CB  . GLN   A 1 181 ? 27.004 20.666  19.432  1.00 12.64  ? 181  GLN   A CB  1 
ATOM   1086 C  CG  . GLN   A 1 181 ? 28.153 21.582  18.937  1.00 12.83  ? 181  GLN   A CG  1 
ATOM   1087 C  CD  . GLN   A 1 181 ? 28.224 21.620  17.414  1.00 14.59  ? 181  GLN   A CD  1 
ATOM   1088 O  OE1 . GLN   A 1 181 ? 27.184 21.492  16.740  1.00 14.69  ? 181  GLN   A OE1 1 
ATOM   1089 N  NE2 . GLN   A 1 181 ? 29.421 21.734  16.855  1.00 15.28  ? 181  GLN   A NE2 1 
ATOM   1090 N  N   . PHE   A 1 182 ? 29.392 18.129  18.359  1.00 11.69  ? 182  PHE   A N   1 
ATOM   1091 C  CA  . PHE   A 1 182 ? 30.720 17.533  18.625  1.00 11.68  ? 182  PHE   A CA  1 
ATOM   1092 C  C   . PHE   A 1 182 ? 31.847 18.304  18.060  1.00 12.38  ? 182  PHE   A C   1 
ATOM   1093 O  O   . PHE   A 1 182 ? 32.919 18.219  18.599  1.00 13.29  ? 182  PHE   A O   1 
ATOM   1094 C  CB  . PHE   A 1 182 ? 30.742 16.099  18.078  1.00 11.86  ? 182  PHE   A CB  1 
ATOM   1095 C  CG  . PHE   A 1 182 ? 29.748 15.150  18.732  1.00 12.46  ? 182  PHE   A CG  1 
ATOM   1096 C  CD1 . PHE   A 1 182 ? 29.314 15.349  20.034  1.00 12.65  ? 182  PHE   A CD1 1 
ATOM   1097 C  CD2 . PHE   A 1 182 ? 29.317 14.021  18.064  1.00 13.92  ? 182  PHE   A CD2 1 
ATOM   1098 C  CE1 . PHE   A 1 182 ? 28.447 14.436  20.652  1.00 12.93  ? 182  PHE   A CE1 1 
ATOM   1099 C  CE2 . PHE   A 1 182 ? 28.446 13.102  18.685  1.00 15.00  ? 182  PHE   A CE2 1 
ATOM   1100 C  CZ  . PHE   A 1 182 ? 28.018 13.328  19.956  1.00 14.07  ? 182  PHE   A CZ  1 
ATOM   1101 N  N   . GLU   A 1 183 ? 31.657 19.071  16.965  1.00 11.82  ? 183  GLU   A N   1 
ATOM   1102 C  CA  . GLU   A 1 183 ? 32.837 19.751  16.427  1.00 11.86  ? 183  GLU   A CA  1 
ATOM   1103 C  C   . GLU   A 1 183 ? 33.317 20.859  17.358  1.00 12.51  ? 183  GLU   A C   1 
ATOM   1104 O  O   . GLU   A 1 183 ? 32.528 21.701  17.781  1.00 13.92  ? 183  GLU   A O   1 
ATOM   1105 C  CB  . GLU   A 1 183 ? 32.549 20.354  15.030  1.00 12.30  ? 183  GLU   A CB  1 
ATOM   1106 C  CG  . GLU   A 1 183 ? 33.846 20.716  14.316  1.00 12.42  ? 183  GLU   A CG  1 
ATOM   1107 C  CD  . GLU   A 1 183 ? 33.655 21.365  12.944  1.00 13.19  ? 183  GLU   A CD  1 
ATOM   1108 O  OE1 . GLU   A 1 183 ? 32.526 21.829  12.678  1.00 14.52  ? 183  GLU   A OE1 1 
ATOM   1109 O  OE2 . GLU   A 1 183 ? 34.620 21.380  12.136  1.00 12.79  ? 183  GLU   A OE2 1 
ATOM   1110 N  N   . PRO   A 1 184 ? 34.627 20.936  17.621  1.00 13.05  ? 184  PRO   A N   1 
ATOM   1111 C  CA  . PRO   A 1 184 ? 35.679 20.053  17.135  1.00 12.26  ? 184  PRO   A CA  1 
ATOM   1112 C  C   . PRO   A 1 184 ? 35.941 18.756  17.945  1.00 13.12  ? 184  PRO   A C   1 
ATOM   1113 O  O   . PRO   A 1 184 ? 36.150 17.723  17.303  1.00 13.59  ? 184  PRO   A O   1 
ATOM   1114 C  CB  . PRO   A 1 184 ? 36.928 20.964  17.142  1.00 13.70  ? 184  PRO   A CB  1 
ATOM   1115 C  CG  . PRO   A 1 184 ? 36.673 21.898  18.258  1.00 14.25  ? 184  PRO   A CG  1 
ATOM   1116 C  CD  . PRO   A 1 184 ? 35.168 22.134  18.306  1.00 13.18  ? 184  PRO   A CD  1 
ATOM   1117 N  N   . THR   A 1 185 ? 36.022 18.816  19.288  1.00 13.23  ? 185  THR   A N   1 
ATOM   1118 C  CA  . THR   A 1 185 ? 36.566 17.674  20.032  1.00 12.73  ? 185  THR   A CA  1 
ATOM   1119 C  C   . THR   A 1 185 ? 35.623 17.119  21.086  1.00 13.46  ? 185  THR   A C   1 
ATOM   1120 O  O   . THR   A 1 185 ? 36.077 16.530  22.055  1.00 13.51  ? 185  THR   A O   1 
ATOM   1121 C  CB  . THR   A 1 185 ? 37.894 18.108  20.732  1.00 14.51  ? 185  THR   A CB  1 
ATOM   1122 O  OG1 . THR   A 1 185 ? 37.623 19.088  21.733  1.00 15.01  ? 185  THR   A OG1 1 
ATOM   1123 C  CG2 . THR   A 1 185 ? 38.961 18.663  19.750  1.00 14.95  ? 185  THR   A CG2 1 
ATOM   1124 N  N   . ALA   A 1 186 ? 34.291 17.271  20.921  1.00 12.61  ? 186  ALA   A N   1 
ATOM   1125 C  CA  . ALA   A 1 186 ? 33.355 16.802  21.940  1.00 12.67  ? 186  ALA   A CA  1 
ATOM   1126 C  C   . ALA   A 1 186 ? 32.724 15.459  21.628  1.00 13.28  ? 186  ALA   A C   1 
ATOM   1127 O  O   . ALA   A 1 186 ? 31.961 14.967  22.499  1.00 13.36  ? 186  ALA   A O   1 
ATOM   1128 C  CB  . ALA   A 1 186 ? 32.298 17.857  22.251  1.00 13.00  ? 186  ALA   A CB  1 
ATOM   1129 N  N   . ALA   A 1 187 ? 33.021 14.780  20.492  1.00 12.77  ? 187  ALA   A N   1 
ATOM   1130 C  CA  . ALA   A 1 187 ? 32.428 13.411  20.312  1.00 12.82  ? 187  ALA   A CA  1 
ATOM   1131 C  C   . ALA   A 1 187 ? 32.858 12.500  21.451  1.00 13.72  ? 187  ALA   A C   1 
ATOM   1132 O  O   . ALA   A 1 187 ? 32.030 11.720  21.922  1.00 13.63  ? 187  ALA   A O   1 
ATOM   1133 C  CB  . ALA   A 1 187 ? 32.884 12.785  19.004  1.00 13.36  ? 187  ALA   A CB  1 
ATOM   1134 N  N   . ARG   A 1 188 ? 34.077 12.706  21.953  1.00 13.48  ? 188  ARG   A N   1 
ATOM   1135 C  CA  . ARG   A 1 188 ? 34.618 11.912  23.076  1.00 13.28  ? 188  ARG   A CA  1 
ATOM   1136 C  C   . ARG   A 1 188 ? 33.844 12.095  24.380  1.00 14.56  ? 188  ARG   A C   1 
ATOM   1137 O  O   . ARG   A 1 188 ? 34.141 11.369  25.347  1.00 14.98  ? 188  ARG   A O   1 
ATOM   1138 C  CB  . ARG   A 1 188 ? 36.078 12.309  23.262  1.00 14.31  ? 188  ARG   A CB  1 
ATOM   1139 C  CG  . ARG   A 1 188 ? 36.229 13.755  23.713  1.00 13.85  ? 188  ARG   A CG  1 
ATOM   1140 C  CD  . ARG   A 1 188 ? 37.671 14.247  23.689  1.00 14.41  ? 188  ARG   A CD  1 
ATOM   1141 N  NE  . ARG   A 1 188 ? 38.216 14.340  22.322  1.00 14.05  ? 188  ARG   A NE  1 
ATOM   1142 C  CZ  . ARG   A 1 188 ? 39.368 14.956  22.043  1.00 14.69  ? 188  ARG   A CZ  1 
ATOM   1143 N  NH1 . ARG   A 1 188 ? 40.064 15.558  23.012  1.00 15.29  ? 188  ARG   A NH1 1 
ATOM   1144 N  NH2 . ARG   A 1 188 ? 39.818 14.999  20.794  1.00 14.27  ? 188  ARG   A NH2 1 
ATOM   1145 N  N   . MET   A 1 189 ? 32.940 13.072  24.457  1.00 14.09  ? 189  MET   A N   1 
ATOM   1146 C  CA  . MET   A 1 189 ? 32.076 13.297  25.610  1.00 14.75  ? 189  MET   A CA  1 
ATOM   1147 C  C   . MET   A 1 189 ? 30.776 12.482  25.468  1.00 13.85  ? 189  MET   A C   1 
ATOM   1148 O  O   . MET   A 1 189 ? 29.985 12.452  26.437  1.00 14.55  ? 189  MET   A O   1 
ATOM   1149 C  CB  . MET   A 1 189 ? 31.682 14.807  25.685  1.00 17.81  ? 189  MET   A CB  1 
ATOM   1150 C  CG  . MET   A 1 189 ? 32.811 15.601  26.218  1.00 20.63  ? 189  MET   A CG  1 
ATOM   1151 S  SD  . MET   A 1 189 ? 32.246 17.298  26.294  1.00 18.80  ? 189  MET   A SD  1 
ATOM   1152 C  CE  . MET   A 1 189 ? 31.041 17.222  27.619  1.00 19.18  ? 189  MET   A CE  1 
ATOM   1153 N  N   . ALA   A 1 190 ? 30.538 11.859  24.308  1.00 13.41  ? 190  ALA   A N   1 
ATOM   1154 C  CA  . ALA   A 1 190 ? 29.348 11.072  24.106  1.00 14.13  ? 190  ALA   A CA  1 
ATOM   1155 C  C   . ALA   A 1 190 ? 29.666 9.606   23.920  1.00 14.20  ? 190  ALA   A C   1 
ATOM   1156 O  O   . ALA   A 1 190 ? 28.834 8.770   24.316  1.00 14.44  ? 190  ALA   A O   1 
ATOM   1157 C  CB  . ALA   A 1 190 ? 28.585 11.594  22.899  1.00 14.76  ? 190  ALA   A CB  1 
ATOM   1158 N  N   . PHE   A 1 191 ? 30.827 9.288   23.326  1.00 14.29  ? 191  PHE   A N   1 
ATOM   1159 C  CA  . PHE   A 1 191 ? 31.238 7.895   23.161  1.00 14.64  ? 191  PHE   A CA  1 
ATOM   1160 C  C   . PHE   A 1 191 ? 32.739 7.898   23.087  1.00 14.70  ? 191  PHE   A C   1 
ATOM   1161 O  O   . PHE   A 1 191 ? 33.352 8.801   22.510  1.00 15.05  ? 191  PHE   A O   1 
ATOM   1162 C  CB  . PHE   A 1 191 ? 30.637 7.225   21.924  1.00 14.76  ? 191  PHE   A CB  1 
ATOM   1163 C  CG  . PHE   A 1 191 ? 30.911 7.956   20.637  1.00 15.08  ? 191  PHE   A CG  1 
ATOM   1164 C  CD1 . PHE   A 1 191 ? 30.124 9.026   20.257  1.00 15.52  ? 191  PHE   A CD1 1 
ATOM   1165 C  CD2 . PHE   A 1 191 ? 31.891 7.504   19.766  1.00 15.92  ? 191  PHE   A CD2 1 
ATOM   1166 C  CE1 . PHE   A 1 191 ? 30.388 9.699   19.068  1.00 16.01  ? 191  PHE   A CE1 1 
ATOM   1167 C  CE2 . PHE   A 1 191 ? 32.099 8.145   18.559  1.00 16.52  ? 191  PHE   A CE2 1 
ATOM   1168 C  CZ  . PHE   A 1 191 ? 31.360 9.244   18.241  1.00 16.57  ? 191  PHE   A CZ  1 
ATOM   1169 N  N   . PRO   A 1 192 ? 33.409 6.891   23.654  1.00 13.49  ? 192  PRO   A N   1 
ATOM   1170 C  CA  . PRO   A 1 192 ? 34.876 6.820   23.539  1.00 14.85  ? 192  PRO   A CA  1 
ATOM   1171 C  C   . PRO   A 1 192 ? 35.244 6.548   22.091  1.00 15.60  ? 192  PRO   A C   1 
ATOM   1172 O  O   . PRO   A 1 192 ? 34.592 5.765   21.399  1.00 15.58  ? 192  PRO   A O   1 
ATOM   1173 C  CB  . PRO   A 1 192 ? 35.220 5.620   24.432  1.00 15.88  ? 192  PRO   A CB  1 
ATOM   1174 C  CG  . PRO   A 1 192 ? 34.003 4.785   24.431  1.00 17.56  ? 192  PRO   A CG  1 
ATOM   1175 C  CD  . PRO   A 1 192 ? 32.839 5.735   24.398  1.00 14.89  ? 192  PRO   A CD  1 
ATOM   1176 N  N   . CYS   A 1 193 ? 36.287 7.226   21.622  1.00 15.14  ? 193  CYS   A N   1 
ATOM   1177 C  CA  . CYS   A 1 193 ? 36.615 7.104   20.194  1.00 15.06  ? 193  CYS   A CA  1 
ATOM   1178 C  C   . CYS   A 1 193 ? 37.986 7.629   19.873  1.00 15.10  ? 193  CYS   A C   1 
ATOM   1179 O  O   . CYS   A 1 193 ? 38.598 8.261   20.713  1.00 15.15  ? 193  CYS   A O   1 
ATOM   1180 C  CB  . CYS   A 1 193 ? 35.527 7.805   19.354  1.00 15.61  ? 193  CYS   A CB  1 
ATOM   1181 S  SG  . CYS   A 1 193 ? 35.262 9.584   19.736  1.00 15.36  ? 193  CYS   A SG  1 
ATOM   1182 N  N   . PHE   A 1 194 ? 38.431 7.409   18.647  1.00 14.67  ? 194  PHE   A N   1 
ATOM   1183 C  CA  . PHE   A 1 194 ? 39.692 7.976   18.166  1.00 14.72  ? 194  PHE   A CA  1 
ATOM   1184 C  C   . PHE   A 1 194 ? 39.281 9.335   17.595  1.00 14.47  ? 194  PHE   A C   1 
ATOM   1185 O  O   . PHE   A 1 194 ? 38.933 9.476   16.421  1.00 14.08  ? 194  PHE   A O   1 
ATOM   1186 C  CB  . PHE   A 1 194 ? 40.301 7.076   17.068  1.00 15.03  ? 194  PHE   A CB  1 
ATOM   1187 C  CG  . PHE   A 1 194 ? 40.679 5.706   17.595  1.00 16.04  ? 194  PHE   A CG  1 
ATOM   1188 C  CD1 . PHE   A 1 194 ? 39.727 4.718   17.735  1.00 17.42  ? 194  PHE   A CD1 1 
ATOM   1189 C  CD2 . PHE   A 1 194 ? 41.998 5.408   17.916  1.00 17.74  ? 194  PHE   A CD2 1 
ATOM   1190 C  CE1 . PHE   A 1 194 ? 40.083 3.430   18.199  1.00 18.42  ? 194  PHE   A CE1 1 
ATOM   1191 C  CE2 . PHE   A 1 194 ? 42.346 4.136   18.389  1.00 19.48  ? 194  PHE   A CE2 1 
ATOM   1192 C  CZ  . PHE   A 1 194 ? 41.387 3.156   18.523  1.00 19.18  ? 194  PHE   A CZ  1 
ATOM   1193 N  N   . ASP   A 1 195 ? 39.219 10.318  18.459  1.00 13.61  ? 195  ASP   A N   1 
ATOM   1194 C  CA  . ASP   A 1 195 ? 38.530 11.591  18.156  1.00 13.05  ? 195  ASP   A CA  1 
ATOM   1195 C  C   . ASP   A 1 195 ? 39.439 12.637  17.533  1.00 13.70  ? 195  ASP   A C   1 
ATOM   1196 O  O   . ASP   A 1 195 ? 39.680 13.720  18.114  1.00 14.40  ? 195  ASP   A O   1 
ATOM   1197 C  CB  . ASP   A 1 195 ? 37.835 12.108  19.421  1.00 13.22  ? 195  ASP   A CB  1 
ATOM   1198 C  CG  . ASP   A 1 195 ? 36.811 13.212  19.227  1.00 13.27  ? 195  ASP   A CG  1 
ATOM   1199 O  OD1 . ASP   A 1 195 ? 36.410 13.459  18.068  1.00 13.30  ? 195  ASP   A OD1 1 
ATOM   1200 O  OD2 . ASP   A 1 195 ? 36.405 13.825  20.236  1.00 13.96  ? 195  ASP   A OD2 1 
ATOM   1201 N  N   . GLU   A 1 196 ? 39.942 12.303  16.338  1.00 13.14  ? 196  GLU   A N   1 
ATOM   1202 C  CA  . GLU   A 1 196 ? 40.720 13.244  15.516  1.00 14.43  ? 196  GLU   A CA  1 
ATOM   1203 C  C   . GLU   A 1 196 ? 40.181 13.069  14.118  1.00 15.16  ? 196  GLU   A C   1 
ATOM   1204 O  O   . GLU   A 1 196 ? 39.815 11.953  13.718  1.00 14.86  ? 196  GLU   A O   1 
ATOM   1205 C  CB  . GLU   A 1 196 ? 42.240 12.958  15.512  1.00 14.95  ? 196  GLU   A CB  1 
ATOM   1206 C  CG  . GLU   A 1 196 ? 42.828 12.962  16.913  1.00 17.03  ? 196  GLU   A CG  1 
ATOM   1207 C  CD  . GLU   A 1 196 ? 44.317 12.709  16.985  1.00 19.42  ? 196  GLU   A CD  1 
ATOM   1208 O  OE1 . GLU   A 1 196 ? 44.965 12.447  15.944  1.00 19.62  ? 196  GLU   A OE1 1 
ATOM   1209 O  OE2 . GLU   A 1 196 ? 44.812 12.729  18.132  1.00 20.16  ? 196  GLU   A OE2 1 
ATOM   1210 N  N   . PRO   A 1 197 ? 40.102 14.152  13.339  1.00 14.37  ? 197  PRO   A N   1 
ATOM   1211 C  CA  . PRO   A 1 197 ? 39.371 14.084  12.077  1.00 13.97  ? 197  PRO   A CA  1 
ATOM   1212 C  C   . PRO   A 1 197 ? 39.927 13.192  11.003  1.00 14.68  ? 197  PRO   A C   1 
ATOM   1213 O  O   . PRO   A 1 197 ? 39.161 12.879  10.082  1.00 14.31  ? 197  PRO   A O   1 
ATOM   1214 C  CB  . PRO   A 1 197 ? 39.284 15.561  11.614  1.00 14.92  ? 197  PRO   A CB  1 
ATOM   1215 C  CG  . PRO   A 1 197 ? 40.426 16.270  12.332  1.00 15.01  ? 197  PRO   A CG  1 
ATOM   1216 C  CD  . PRO   A 1 197 ? 40.472 15.546  13.691  1.00 14.33  ? 197  PRO   A CD  1 
ATOM   1217 N  N   . ALA   A 1 198 ? 41.192 12.792  11.078  1.00 13.84  ? 198  ALA   A N   1 
ATOM   1218 C  CA  . ALA   A 1 198 ? 41.741 11.918  10.068  1.00 15.21  ? 198  ALA   A CA  1 
ATOM   1219 C  C   . ALA   A 1 198 ? 41.533 10.433  10.373  1.00 16.54  ? 198  ALA   A C   1 
ATOM   1220 O  O   . ALA   A 1 198 ? 41.848 9.613   9.520   1.00 17.95  ? 198  ALA   A O   1 
ATOM   1221 C  CB  . ALA   A 1 198 ? 43.230 12.226  9.866   1.00 16.54  ? 198  ALA   A CB  1 
ATOM   1222 N  N   . PHE   A 1 199 ? 40.939 10.086  11.549  1.00 15.40  ? 199  PHE   A N   1 
ATOM   1223 C  CA  . PHE   A 1 199 ? 40.645 8.678   11.827  1.00 16.06  ? 199  PHE   A CA  1 
ATOM   1224 C  C   . PHE   A 1 199 ? 39.206 8.440   11.337  1.00 15.74  ? 199  PHE   A C   1 
ATOM   1225 O  O   . PHE   A 1 199 ? 38.284 8.280   12.159  1.00 16.00  ? 199  PHE   A O   1 
ATOM   1226 C  CB  . PHE   A 1 199 ? 40.748 8.380   13.334  1.00 16.28  ? 199  PHE   A CB  1 
ATOM   1227 C  CG  . PHE   A 1 199 ? 42.149 8.344   13.870  1.00 18.91  ? 199  PHE   A CG  1 
ATOM   1228 C  CD1 . PHE   A 1 199 ? 43.013 7.329   13.519  1.00 22.63  ? 199  PHE   A CD1 1 
ATOM   1229 C  CD2 . PHE   A 1 199 ? 42.572 9.281   14.788  1.00 21.78  ? 199  PHE   A CD2 1 
ATOM   1230 C  CE1 . PHE   A 1 199 ? 44.306 7.274   14.060  1.00 24.04  ? 199  PHE   A CE1 1 
ATOM   1231 C  CE2 . PHE   A 1 199 ? 43.858 9.237   15.311  1.00 23.23  ? 199  PHE   A CE2 1 
ATOM   1232 C  CZ  . PHE   A 1 199 ? 44.708 8.209   14.969  1.00 23.05  ? 199  PHE   A CZ  1 
ATOM   1233 N  N   . LYS   A 1 200 ? 39.012 8.447   10.000  1.00 15.79  ? 200  LYS   A N   1 
ATOM   1234 C  CA  . LYS   A 1 200 ? 37.652 8.284   9.480   1.00 14.94  ? 200  LYS   A CA  1 
ATOM   1235 C  C   . LYS   A 1 200 ? 37.192 6.852   9.634   1.00 15.79  ? 200  LYS   A C   1 
ATOM   1236 O  O   . LYS   A 1 200 ? 38.008 5.908   9.612   1.00 16.26  ? 200  LYS   A O   1 
ATOM   1237 C  CB  . LYS   A 1 200 ? 37.512 8.719   8.039   1.00 15.38  ? 200  LYS   A CB  1 
ATOM   1238 C  CG  . LYS   A 1 200 ? 37.783 10.216  7.861   1.00 15.14  ? 200  LYS   A CG  1 
ATOM   1239 C  CD  . LYS   A 1 200 ? 37.333 10.647  6.478   1.00 15.22  ? 200  LYS   A CD  1 
ATOM   1240 C  CE  . LYS   A 1 200 ? 37.421 12.158  6.392   1.00 15.21  ? 200  LYS   A CE  1 
ATOM   1241 N  NZ  . LYS   A 1 200 ? 36.855 12.709  5.097   1.00 14.51  ? 200  LYS   A NZ  1 
ATOM   1242 N  N   . ALA   A 1 201 ? 35.884 6.679   9.783   1.00 15.33  ? 201  ALA   A N   1 
ATOM   1243 C  CA  . ALA   A 1 201 ? 35.303 5.350   9.995   1.00 15.26  ? 201  ALA   A CA  1 
ATOM   1244 C  C   . ALA   A 1 201 ? 33.823 5.405   9.663   1.00 14.96  ? 201  ALA   A C   1 
ATOM   1245 O  O   . ALA   A 1 201 ? 33.246 6.488   9.523   1.00 15.15  ? 201  ALA   A O   1 
ATOM   1246 C  CB  . ALA   A 1 201 ? 35.467 4.987   11.479  1.00 16.87  ? 201  ALA   A CB  1 
ATOM   1247 N  N   . SER   A 1 202 ? 33.186 4.233   9.482   1.00 15.13  ? 202  SER   A N   1 
ATOM   1248 C  CA  . SER   A 1 202 ? 31.726 4.216   9.352   1.00 15.38  ? 202  SER   A CA  1 
ATOM   1249 C  C   . SER   A 1 202 ? 31.101 4.038   10.740  1.00 15.10  ? 202  SER   A C   1 
ATOM   1250 O  O   . SER   A 1 202 ? 31.751 3.502   11.660  1.00 15.88  ? 202  SER   A O   1 
ATOM   1251 C  CB  . SER   A 1 202 ? 31.264 3.097   8.429   1.00 16.60  ? 202  SER   A CB  1 
ATOM   1252 O  OG  . SER   A 1 202 ? 31.716 1.842   8.932   1.00 18.35  ? 202  SER   A OG  1 
ATOM   1253 N  N   . PHE   A 1 203 ? 29.850 4.487   10.902  1.00 14.81  ? 203  PHE   A N   1 
ATOM   1254 C  CA  . PHE   A 1 203 ? 29.168 4.438   12.187  1.00 15.40  ? 203  PHE   A CA  1 
ATOM   1255 C  C   . PHE   A 1 203 ? 27.777 3.863   12.056  1.00 15.68  ? 203  PHE   A C   1 
ATOM   1256 O  O   . PHE   A 1 203 ? 26.991 4.334   11.218  1.00 15.33  ? 203  PHE   A O   1 
ATOM   1257 C  CB  . PHE   A 1 203 ? 29.005 5.864   12.788  1.00 15.06  ? 203  PHE   A CB  1 
ATOM   1258 C  CG  . PHE   A 1 203 ? 30.322 6.550   13.071  1.00 15.26  ? 203  PHE   A CG  1 
ATOM   1259 C  CD1 . PHE   A 1 203 ? 31.021 7.183   12.058  1.00 14.96  ? 203  PHE   A CD1 1 
ATOM   1260 C  CD2 . PHE   A 1 203 ? 30.834 6.605   14.356  1.00 15.02  ? 203  PHE   A CD2 1 
ATOM   1261 C  CE1 . PHE   A 1 203 ? 32.259 7.783   12.311  1.00 15.67  ? 203  PHE   A CE1 1 
ATOM   1262 C  CE2 . PHE   A 1 203 ? 32.070 7.219   14.609  1.00 15.77  ? 203  PHE   A CE2 1 
ATOM   1263 C  CZ  . PHE   A 1 203 ? 32.766 7.813   13.581  1.00 15.09  ? 203  PHE   A CZ  1 
ATOM   1264 N  N   . SER   A 1 204 ? 27.472 2.857   12.875  1.00 15.13  ? 204  SER   A N   1 
ATOM   1265 C  CA  . SER   A 1 204 ? 26.112 2.296   12.933  1.00 15.72  ? 204  SER   A CA  1 
ATOM   1266 C  C   . SER   A 1 204 ? 25.561 2.700   14.285  1.00 16.00  ? 204  SER   A C   1 
ATOM   1267 O  O   . SER   A 1 204 ? 26.102 2.286   15.312  1.00 17.95  ? 204  SER   A O   1 
ATOM   1268 C  CB  . SER   A 1 204 ? 26.151 0.781   12.850  1.00 17.81  ? 204  SER   A CB  1 
ATOM   1269 O  OG  . SER   A 1 204 ? 26.493 0.427   11.521  1.00 19.07  ? 204  SER   A OG  1 
ATOM   1270 N  N   . ILE   A 1 205 ? 24.507 3.506   14.299  1.00 15.96  ? 205  ILE   A N   1 
ATOM   1271 C  CA  . ILE   A 1 205 ? 23.976 4.063   15.539  1.00 15.68  ? 205  ILE   A CA  1 
ATOM   1272 C  C   . ILE   A 1 205 ? 22.648 3.491   15.900  1.00 16.08  ? 205  ILE   A C   1 
ATOM   1273 O  O   . ILE   A 1 205 ? 21.792 3.333   15.058  1.00 15.83  ? 205  ILE   A O   1 
ATOM   1274 C  CB  . ILE   A 1 205 ? 23.904 5.603   15.366  1.00 16.47  ? 205  ILE   A CB  1 
ATOM   1275 C  CG1 . ILE   A 1 205 ? 25.365 6.126   15.146  1.00 18.23  ? 205  ILE   A CG1 1 
ATOM   1276 C  CG2 . ILE   A 1 205 ? 23.226 6.262   16.579  1.00 17.03  ? 205  ILE   A CG2 1 
ATOM   1277 C  CD1 . ILE   A 1 205 ? 25.450 7.495   14.615  1.00 19.82  ? 205  ILE   A CD1 1 
ATOM   1278 N  N   . LYS   A 1 206 ? 22.505 3.166   17.201  1.00 15.41  ? 206  LYS   A N   1 
ATOM   1279 C  CA  . LYS   A 1 206 ? 21.281 2.619   17.773  1.00 15.92  ? 206  LYS   A CA  1 
ATOM   1280 C  C   . LYS   A 1 206 ? 20.944 3.456   18.977  1.00 15.09  ? 206  LYS   A C   1 
ATOM   1281 O  O   . LYS   A 1 206 ? 21.818 3.721   19.802  1.00 15.62  ? 206  LYS   A O   1 
ATOM   1282 C  CB  . LYS   A 1 206 ? 21.474 1.132   18.184  1.00 18.24  ? 206  LYS   A CB  1 
ATOM   1283 C  CG  . LYS   A 1 206 ? 21.627 0.224   16.983  1.00 21.22  ? 206  LYS   A CG  1 
ATOM   1284 C  CD  . LYS   A 1 206 ? 22.014 -1.206  17.406  1.00 27.75  ? 206  LYS   A CD  1 
ATOM   1285 C  CE  . LYS   A 1 206 ? 22.422 -2.058  16.207  1.00 34.15  ? 206  LYS   A CE  1 
ATOM   1286 N  NZ  . LYS   A 1 206 ? 23.303 -1.333  15.219  1.00 36.65  ? 206  LYS   A NZ  1 
ATOM   1287 N  N   A ILE   A 1 207 ? 19.693 3.902   19.074  0.50 15.41  ? 207  ILE   A N   1 
ATOM   1288 N  N   B ILE   A 1 207 ? 19.686 3.935   19.063  0.50 14.75  ? 207  ILE   A N   1 
ATOM   1289 C  CA  A ILE   A 1 207 ? 19.284 4.743   20.191  0.50 15.78  ? 207  ILE   A CA  1 
ATOM   1290 C  CA  B ILE   A 1 207 ? 19.232 4.824   20.140  0.50 14.32  ? 207  ILE   A CA  1 
ATOM   1291 C  C   A ILE   A 1 207 ? 18.143 4.085   20.904  0.50 15.31  ? 207  ILE   A C   1 
ATOM   1292 C  C   B ILE   A 1 207 ? 18.085 4.185   20.898  0.50 14.86  ? 207  ILE   A C   1 
ATOM   1293 O  O   A ILE   A 1 207 ? 17.197 3.665   20.261  0.50 16.11  ? 207  ILE   A O   1 
ATOM   1294 O  O   B ILE   A 1 207 ? 17.045 3.938   20.290  0.50 16.07  ? 207  ILE   A O   1 
ATOM   1295 C  CB  A ILE   A 1 207 ? 18.880 6.149   19.726  0.50 16.34  ? 207  ILE   A CB  1 
ATOM   1296 C  CB  B ILE   A 1 207 ? 18.758 6.176   19.550  0.50 13.63  ? 207  ILE   A CB  1 
ATOM   1297 C  CG1 A ILE   A 1 207 ? 19.999 6.780   18.879  0.50 18.46  ? 207  ILE   A CG1 1 
ATOM   1298 C  CG1 B ILE   A 1 207 ? 19.911 6.890   18.797  0.50 14.73  ? 207  ILE   A CG1 1 
ATOM   1299 C  CG2 A ILE   A 1 207 ? 18.551 7.012   20.969  0.50 16.26  ? 207  ILE   A CG2 1 
ATOM   1300 C  CG2 B ILE   A 1 207 ? 18.156 7.077   20.670  0.50 13.92  ? 207  ILE   A CG2 1 
ATOM   1301 C  CD1 A ILE   A 1 207 ? 19.623 8.061   18.318  0.50 20.16  ? 207  ILE   A CD1 1 
ATOM   1302 C  CD1 B ILE   A 1 207 ? 21.120 7.320   19.701  0.50 14.57  ? 207  ILE   A CD1 1 
ATOM   1303 N  N   . ARG   A 1 208 ? 18.235 3.959   22.218  1.00 15.17  ? 208  ARG   A N   1 
ATOM   1304 C  CA  . ARG   A 1 208 ? 17.121 3.434   23.009  1.00 16.04  ? 208  ARG   A CA  1 
ATOM   1305 C  C   . ARG   A 1 208 ? 16.403 4.647   23.596  1.00 17.40  ? 208  ARG   A C   1 
ATOM   1306 O  O   . ARG   A 1 208 ? 17.054 5.535   24.171  1.00 17.89  ? 208  ARG   A O   1 
ATOM   1307 C  CB  . ARG   A 1 208 ? 17.592 2.503   24.122  1.00 18.09  ? 208  ARG   A CB  1 
ATOM   1308 C  CG  . ARG   A 1 208 ? 17.971 1.138   23.579  1.00 20.15  ? 208  ARG   A CG  1 
ATOM   1309 C  CD  . ARG   A 1 208 ? 18.423 0.186   24.676  1.00 23.46  ? 208  ARG   A CD  1 
ATOM   1310 N  NE  . ARG   A 1 208 ? 18.789 -1.115  24.114  1.00 25.27  ? 208  ARG   A NE  1 
ATOM   1311 C  CZ  . ARG   A 1 208 ? 19.296 -2.112  24.845  1.00 29.26  ? 208  ARG   A CZ  1 
ATOM   1312 N  NH1 . ARG   A 1 208 ? 19.485 -1.957  26.154  1.00 27.91  ? 208  ARG   A NH1 1 
ATOM   1313 N  NH2 . ARG   A 1 208 ? 19.596 -3.272  24.277  1.00 31.17  ? 208  ARG   A NH2 1 
ATOM   1314 N  N   . ARG   A 1 209 ? 15.081 4.670   23.499  1.00 16.86  ? 209  ARG   A N   1 
ATOM   1315 C  CA  . ARG   A 1 209 ? 14.310 5.822   23.909  1.00 16.89  ? 209  ARG   A CA  1 
ATOM   1316 C  C   . ARG   A 1 209 ? 12.930 5.418   24.359  1.00 17.89  ? 209  ARG   A C   1 
ATOM   1317 O  O   . ARG   A 1 209 ? 12.455 4.285   24.111  1.00 18.69  ? 209  ARG   A O   1 
ATOM   1318 C  CB  . ARG   A 1 209 ? 14.168 6.775   22.696  1.00 18.55  ? 209  ARG   A CB  1 
ATOM   1319 C  CG  . ARG   A 1 209 ? 13.480 6.081   21.516  1.00 20.66  ? 209  ARG   A CG  1 
ATOM   1320 C  CD  . ARG   A 1 209 ? 12.740 6.946   20.565  1.00 23.55  ? 209  ARG   A CD  1 
ATOM   1321 N  NE  . ARG   A 1 209 ? 12.350 6.168   19.394  1.00 19.59  ? 209  ARG   A NE  1 
ATOM   1322 C  CZ  . ARG   A 1 209 ? 11.148 5.660   19.165  1.00 19.81  ? 209  ARG   A CZ  1 
ATOM   1323 N  NH1 . ARG   A 1 209 ? 10.157 5.862   20.029  1.00 18.63  ? 209  ARG   A NH1 1 
ATOM   1324 N  NH2 . ARG   A 1 209 ? 10.934 4.918   18.082  1.00 19.10  ? 209  ARG   A NH2 1 
ATOM   1325 N  N   . GLU   A 1 210 ? 12.287 6.330   25.062  1.00 17.94  ? 210  GLU   A N   1 
ATOM   1326 C  CA  . GLU   A 1 210 ? 10.895 6.119   25.441  1.00 17.75  ? 210  GLU   A CA  1 
ATOM   1327 C  C   . GLU   A 1 210 ? 10.024 6.238   24.183  1.00 18.45  ? 210  GLU   A C   1 
ATOM   1328 O  O   . GLU   A 1 210 ? 10.308 7.030   23.266  1.00 18.48  ? 210  GLU   A O   1 
ATOM   1329 C  CB  . GLU   A 1 210 ? 10.455 7.173   26.458  1.00 19.85  ? 210  GLU   A CB  1 
ATOM   1330 C  CG  . GLU   A 1 210 ? 11.193 7.147   27.781  1.00 23.06  ? 210  GLU   A CG  1 
ATOM   1331 C  CD  . GLU   A 1 210 ? 10.683 8.261   28.677  1.00 27.33  ? 210  GLU   A CD  1 
ATOM   1332 O  OE1 . GLU   A 1 210 ? 9.471  8.249   29.010  1.00 27.47  ? 210  GLU   A OE1 1 
ATOM   1333 O  OE2 . GLU   A 1 210 ? 11.491 9.145   29.051  1.00 25.43  ? 210  GLU   A OE2 1 
ATOM   1334 N  N   . PRO   A 1 211 ? 8.871  5.550   24.165  1.00 18.20  ? 211  PRO   A N   1 
ATOM   1335 C  CA  . PRO   A 1 211 ? 7.987  5.656   22.988  1.00 18.44  ? 211  PRO   A CA  1 
ATOM   1336 C  C   . PRO   A 1 211 ? 7.486  7.088   22.703  1.00 18.67  ? 211  PRO   A C   1 
ATOM   1337 O  O   . PRO   A 1 211 ? 7.180  7.416   21.548  1.00 20.30  ? 211  PRO   A O   1 
ATOM   1338 C  CB  . PRO   A 1 211 ? 6.784  4.781   23.383  1.00 20.13  ? 211  PRO   A CB  1 
ATOM   1339 C  CG  . PRO   A 1 211 ? 7.383  3.748   24.275  1.00 21.07  ? 211  PRO   A CG  1 
ATOM   1340 C  CD  . PRO   A 1 211 ? 8.442  4.462   25.078  1.00 18.92  ? 211  PRO   A CD  1 
ATOM   1341 N  N   . ARG   A 1 212 ? 7.446  7.941   23.740  1.00 18.90  ? 212  ARG   A N   1 
ATOM   1342 C  CA  . ARG   A 1 212 ? 6.952  9.321   23.546  1.00 19.73  ? 212  ARG   A CA  1 
ATOM   1343 C  C   . ARG   A 1 212 ? 7.914  10.199  22.746  1.00 19.82  ? 212  ARG   A C   1 
ATOM   1344 O  O   . ARG   A 1 212 ? 7.557  11.333  22.363  1.00 21.50  ? 212  ARG   A O   1 
ATOM   1345 C  CB  . ARG   A 1 212 ? 6.615  10.004  24.900  1.00 20.41  ? 212  ARG   A CB  1 
ATOM   1346 C  CG  . ARG   A 1 212 ? 7.832  10.265  25.827  1.00 23.65  ? 212  ARG   A CG  1 
ATOM   1347 C  CD  . ARG   A 1 212 ? 7.412  10.791  27.213  1.00 24.85  ? 212  ARG   A CD  1 
ATOM   1348 N  NE  . ARG   A 1 212 ? 8.548  10.730  28.138  1.00 26.10  ? 212  ARG   A NE  1 
ATOM   1349 C  CZ  . ARG   A 1 212 ? 9.143  11.793  28.673  1.00 29.95  ? 212  ARG   A CZ  1 
ATOM   1350 N  NH1 . ARG   A 1 212 ? 8.657  13.012  28.458  1.00 29.45  ? 212  ARG   A NH1 1 
ATOM   1351 N  NH2 . ARG   A 1 212 ? 10.218 11.644  29.445  1.00 30.50  ? 212  ARG   A NH2 1 
ATOM   1352 N  N   . HIS   A 1 213 ? 9.163  9.725   22.564  1.00 17.45  ? 213  HIS   A N   1 
ATOM   1353 C  CA  . HIS   A 1 213 ? 10.144 10.550  21.859  1.00 17.13  ? 213  HIS   A CA  1 
ATOM   1354 C  C   . HIS   A 1 213 ? 10.434 10.026  20.467  1.00 18.05  ? 213  HIS   A C   1 
ATOM   1355 O  O   . HIS   A 1 213 ? 10.272 8.837   20.167  1.00 19.19  ? 213  HIS   A O   1 
ATOM   1356 C  CB  . HIS   A 1 213 ? 11.449 10.572  22.664  1.00 18.50  ? 213  HIS   A CB  1 
ATOM   1357 C  CG  . HIS   A 1 213 ? 11.347 11.268  23.984  1.00 20.75  ? 213  HIS   A CG  1 
ATOM   1358 N  ND1 . HIS   A 1 213 ? 11.825 10.674  25.152  1.00 22.76  ? 213  HIS   A ND1 1 
ATOM   1359 C  CD2 . HIS   A 1 213 ? 10.875 12.500  24.285  1.00 22.54  ? 213  HIS   A CD2 1 
ATOM   1360 C  CE1 . HIS   A 1 213 ? 11.591 11.539  26.126  1.00 23.95  ? 213  HIS   A CE1 1 
ATOM   1361 N  NE2 . HIS   A 1 213 ? 11.020 12.651  25.665  1.00 23.49  ? 213  HIS   A NE2 1 
ATOM   1362 N  N   . LEU   A 1 214 ? 10.887 10.923  19.608  1.00 17.10  ? 214  LEU   A N   1 
ATOM   1363 C  CA  . LEU   A 1 214 ? 11.399 10.606  18.296  1.00 17.24  ? 214  LEU   A CA  1 
ATOM   1364 C  C   . LEU   A 1 214 ? 12.919 10.672  18.354  1.00 15.52  ? 214  LEU   A C   1 
ATOM   1365 O  O   . LEU   A 1 214 ? 13.444 11.641  18.928  1.00 16.18  ? 214  LEU   A O   1 
ATOM   1366 C  CB  . LEU   A 1 214 ? 10.875 11.689  17.321  1.00 18.37  ? 214  LEU   A CB  1 
ATOM   1367 C  CG  . LEU   A 1 214 ? 11.461 11.681  15.902  1.00 20.64  ? 214  LEU   A CG  1 
ATOM   1368 C  CD1 . LEU   A 1 214 ? 11.033 10.446  15.117  1.00 21.62  ? 214  LEU   A CD1 1 
ATOM   1369 C  CD2 . LEU   A 1 214 ? 10.975 12.900  15.136  1.00 23.63  ? 214  LEU   A CD2 1 
ATOM   1370 N  N   . ALA   A 1 215 ? 13.623 9.738   17.711  1.00 14.13  ? 215  ALA   A N   1 
ATOM   1371 C  CA  . ALA   A 1 215 ? 15.070 9.866   17.571  1.00 14.00  ? 215  ALA   A CA  1 
ATOM   1372 C  C   . ALA   A 1 215 ? 15.363 10.013  16.068  1.00 14.40  ? 215  ALA   A C   1 
ATOM   1373 O  O   . ALA   A 1 215 ? 14.794 9.312   15.226  1.00 15.67  ? 215  ALA   A O   1 
ATOM   1374 C  CB  . ALA   A 1 215 ? 15.807 8.646   18.176  1.00 14.90  ? 215  ALA   A CB  1 
ATOM   1375 N  N   . ILE   A 1 216 ? 16.304 10.899  15.751  1.00 13.63  ? 216  ILE   A N   1 
ATOM   1376 C  CA  . ILE   A 1 216 ? 16.870 11.030  14.409  1.00 13.79  ? 216  ILE   A CA  1 
ATOM   1377 C  C   . ILE   A 1 216 ? 18.394 11.042  14.518  1.00 13.46  ? 216  ILE   A C   1 
ATOM   1378 O  O   . ILE   A 1 216 ? 18.943 11.345  15.586  1.00 13.83  ? 216  ILE   A O   1 
ATOM   1379 C  CB  . ILE   A 1 216 ? 16.345 12.225  13.586  1.00 15.18  ? 216  ILE   A CB  1 
ATOM   1380 C  CG1 . ILE   A 1 216 ? 16.620 13.527  14.317  1.00 14.44  ? 216  ILE   A CG1 1 
ATOM   1381 C  CG2 . ILE   A 1 216 ? 14.855 12.031  13.293  1.00 16.43  ? 216  ILE   A CG2 1 
ATOM   1382 C  CD1 . ILE   A 1 216 ? 16.120 14.780  13.496  1.00 16.49  ? 216  ILE   A CD1 1 
ATOM   1383 N  N   . SER   A 1 217 ? 19.071 10.687  13.426  1.00 12.48  ? 217  SER   A N   1 
ATOM   1384 C  CA  . SER   A 1 217 ? 20.530 10.616  13.441  1.00 13.91  ? 217  SER   A CA  1 
ATOM   1385 C  C   . SER   A 1 217 ? 21.049 10.915  12.043  1.00 12.89  ? 217  SER   A C   1 
ATOM   1386 O  O   . SER   A 1 217 ? 20.304 11.468  11.206  1.00 13.71  ? 217  SER   A O   1 
ATOM   1387 C  CB  . SER   A 1 217 ? 20.949 9.244   13.997  1.00 13.54  ? 217  SER   A CB  1 
ATOM   1388 O  OG  . SER   A 1 217 ? 22.363 9.129   14.134  1.00 13.65  ? 217  SER   A OG  1 
ATOM   1389 N  N   . ASN   A 1 218 ? 22.316 10.612  11.771  1.00 12.74  ? 218  ASN   A N   1 
ATOM   1390 C  CA  . ASN   A 1 218 ? 22.860 10.922  10.443  1.00 13.34  ? 218  ASN   A CA  1 
ATOM   1391 C  C   . ASN   A 1 218 ? 22.112 10.240  9.297   1.00 13.84  ? 218  ASN   A C   1 
ATOM   1392 O  O   . ASN   A 1 218 ? 21.877 10.818  8.236   1.00 14.46  ? 218  ASN   A O   1 
ATOM   1393 C  CB  . ASN   A 1 218 ? 24.325 10.479  10.389  1.00 13.74  ? 218  ASN   A CB  1 
ATOM   1394 C  CG  . ASN   A 1 218 ? 25.150 11.181  11.430  1.00 13.87  ? 218  ASN   A CG  1 
ATOM   1395 O  OD1 . ASN   A 1 218 ? 25.270 10.736  12.559  1.00 13.86  ? 218  ASN   A OD1 1 
ATOM   1396 N  ND2 . ASN   A 1 218 ? 25.781 12.298  11.037  1.00 13.88  ? 218  ASN   A ND2 1 
ATOM   1397 N  N   . MET   A 1 219 ? 21.799 8.943   9.494   1.00 14.22  ? 219  MET   A N   1 
ATOM   1398 C  CA  . MET   A 1 219 ? 21.251 8.097   8.428   1.00 14.85  ? 219  MET   A CA  1 
ATOM   1399 C  C   . MET   A 1 219 ? 19.785 7.750   8.662   1.00 14.82  ? 219  MET   A C   1 
ATOM   1400 O  O   . MET   A 1 219 ? 19.281 7.926   9.752   1.00 14.73  ? 219  MET   A O   1 
ATOM   1401 C  CB  . MET   A 1 219 ? 22.083 6.790   8.385   1.00 15.25  ? 219  MET   A CB  1 
ATOM   1402 C  CG  . MET   A 1 219 ? 23.516 7.020   8.079   1.00 15.70  ? 219  MET   A CG  1 
ATOM   1403 S  SD  . MET   A 1 219 ? 23.865 7.777   6.484   1.00 18.52  ? 219  MET   A SD  1 
ATOM   1404 C  CE  . MET   A 1 219 ? 23.359 6.586   5.412   1.00 20.56  ? 219  MET   A CE  1 
ATOM   1405 N  N   . PRO   A 1 220 ? 19.102 7.237   7.618   1.00 15.31  ? 220  PRO   A N   1 
ATOM   1406 C  CA  . PRO   A 1 220 ? 17.717 6.823   7.819   1.00 15.63  ? 220  PRO   A CA  1 
ATOM   1407 C  C   . PRO   A 1 220 ? 17.522 5.786   8.911   1.00 16.71  ? 220  PRO   A C   1 
ATOM   1408 O  O   . PRO   A 1 220 ? 18.406 4.953   9.176   1.00 16.54  ? 220  PRO   A O   1 
ATOM   1409 C  CB  . PRO   A 1 220 ? 17.331 6.214   6.454   1.00 16.99  ? 220  PRO   A CB  1 
ATOM   1410 C  CG  . PRO   A 1 220 ? 18.265 6.907   5.486   1.00 16.90  ? 220  PRO   A CG  1 
ATOM   1411 C  CD  . PRO   A 1 220 ? 19.554 6.984   6.226   1.00 15.28  ? 220  PRO   A CD  1 
ATOM   1412 N  N   . LEU   A 1 221 ? 16.342 5.832   9.485   1.00 15.77  ? 221  LEU   A N   1 
ATOM   1413 C  CA  . LEU   A 1 221 ? 15.888 4.845   10.455  1.00 16.93  ? 221  LEU   A CA  1 
ATOM   1414 C  C   . LEU   A 1 221 ? 15.503 3.587   9.675   1.00 18.91  ? 221  LEU   A C   1 
ATOM   1415 O  O   . LEU   A 1 221 ? 14.644 3.658   8.764   1.00 20.56  ? 221  LEU   A O   1 
ATOM   1416 C  CB  . LEU   A 1 221 ? 14.649 5.381   11.157  1.00 17.41  ? 221  LEU   A CB  1 
ATOM   1417 C  CG  . LEU   A 1 221 ? 13.966 4.413   12.142  1.00 20.05  ? 221  LEU   A CG  1 
ATOM   1418 C  CD1 . LEU   A 1 221 ? 14.841 4.206   13.343  1.00 20.95  ? 221  LEU   A CD1 1 
ATOM   1419 C  CD2 . LEU   A 1 221 ? 12.610 4.937   12.533  1.00 21.90  ? 221  LEU   A CD2 1 
ATOM   1420 N  N   . VAL   A 1 222 ? 16.149 2.443   10.007  1.00 18.49  ? 222  VAL   A N   1 
ATOM   1421 C  CA  . VAL   A 1 222 ? 15.827 1.227   9.258   1.00 20.80  ? 222  VAL   A CA  1 
ATOM   1422 C  C   . VAL   A 1 222 ? 14.930 0.299   10.040  1.00 22.88  ? 222  VAL   A C   1 
ATOM   1423 O  O   . VAL   A 1 222 ? 14.234 -0.482  9.405   1.00 24.13  ? 222  VAL   A O   1 
ATOM   1424 C  CB  . VAL   A 1 222 ? 17.086 0.527   8.701   1.00 22.74  ? 222  VAL   A CB  1 
ATOM   1425 C  CG1 . VAL   A 1 222 ? 17.787 1.426   7.691   1.00 23.72  ? 222  VAL   A CG1 1 
ATOM   1426 C  CG2 . VAL   A 1 222 ? 18.040 0.102   9.796   1.00 24.08  ? 222  VAL   A CG2 1 
ATOM   1427 N  N   . LYS   A 1 223 ? 14.887 0.396   11.371  1.00 21.69  ? 223  LYS   A N   1 
ATOM   1428 C  CA  . LYS   A 1 223 ? 14.050 -0.517  12.168  1.00 22.51  ? 223  LYS   A CA  1 
ATOM   1429 C  C   . LYS   A 1 223 ? 13.901 0.017   13.578  1.00 21.64  ? 223  LYS   A C   1 
ATOM   1430 O  O   . LYS   A 1 223 ? 14.791 0.708   14.060  1.00 20.43  ? 223  LYS   A O   1 
ATOM   1431 C  CB  . LYS   A 1 223 ? 14.741 -1.901  12.232  1.00 25.37  ? 223  LYS   A CB  1 
ATOM   1432 C  CG  . LYS   A 1 223 ? 13.852 -3.021  12.782  1.00 31.98  ? 223  LYS   A CG  1 
ATOM   1433 C  CD  . LYS   A 1 223 ? 14.615 -4.322  12.893  1.00 37.05  ? 223  LYS   A CD  1 
ATOM   1434 C  CE  . LYS   A 1 223 ? 14.707 -5.026  11.554  1.00 41.96  ? 223  LYS   A CE  1 
ATOM   1435 N  NZ  . LYS   A 1 223 ? 15.222 -6.420  11.681  1.00 43.50  ? 223  LYS   A NZ  1 
ATOM   1436 N  N   . SER   A 1 224 ? 12.761 -0.218  14.218  1.00 21.34  ? 224  SER   A N   1 
ATOM   1437 C  CA  . SER   A 1 224 ? 12.542 0.155   15.619  1.00 21.77  ? 224  SER   A CA  1 
ATOM   1438 C  C   . SER   A 1 224 ? 12.093 -1.113  16.303  1.00 23.26  ? 224  SER   A C   1 
ATOM   1439 O  O   . SER   A 1 224 ? 11.183 -1.774  15.811  1.00 25.17  ? 224  SER   A O   1 
ATOM   1440 C  CB  . SER   A 1 224 ? 11.448 1.196   15.767  1.00 21.19  ? 224  SER   A CB  1 
ATOM   1441 O  OG  . SER   A 1 224 ? 11.866 2.404   15.144  1.00 21.56  ? 224  SER   A OG  1 
ATOM   1442 N  N   . VAL   A 1 225 ? 12.777 -1.490  17.360  1.00 21.80  ? 225  VAL   A N   1 
ATOM   1443 C  CA  . VAL   A 1 225 ? 12.518 -2.764  18.037  1.00 22.49  ? 225  VAL   A CA  1 
ATOM   1444 C  C   . VAL   A 1 225 ? 12.112 -2.503  19.485  1.00 22.12  ? 225  VAL   A C   1 
ATOM   1445 O  O   . VAL   A 1 225 ? 12.804 -1.754  20.169  1.00 22.20  ? 225  VAL   A O   1 
ATOM   1446 C  CB  . VAL   A 1 225 ? 13.849 -3.564  18.044  1.00 25.09  ? 225  VAL   A CB  1 
ATOM   1447 C  CG1 . VAL   A 1 225 ? 13.681 -4.896  18.769  1.00 26.55  ? 225  VAL   A CG1 1 
ATOM   1448 C  CG2 . VAL   A 1 225 ? 14.378 -3.782  16.620  1.00 27.85  ? 225  VAL   A CG2 1 
ATOM   1449 N  N   . THR   A 1 226 ? 11.083 -3.184  19.989  1.00 21.99  ? 226  THR   A N   1 
ATOM   1450 C  CA  . THR   A 1 226 ? 10.736 -3.026  21.390  1.00 22.53  ? 226  THR   A CA  1 
ATOM   1451 C  C   . THR   A 1 226 ? 11.778 -3.792  22.209  1.00 22.57  ? 226  THR   A C   1 
ATOM   1452 O  O   . THR   A 1 226 ? 12.110 -4.949  21.877  1.00 23.49  ? 226  THR   A O   1 
ATOM   1453 C  CB  . THR   A 1 226 ? 9.306  -3.531  21.614  1.00 26.98  ? 226  THR   A CB  1 
ATOM   1454 O  OG1 . THR   A 1 226 ? 8.439  -2.670  20.861  1.00 29.40  ? 226  THR   A OG1 1 
ATOM   1455 C  CG2 . THR   A 1 226 ? 8.909  -3.522  23.091  1.00 28.45  ? 226  THR   A CG2 1 
ATOM   1456 N  N   . VAL   A 1 227 ? 12.347 -3.157  23.250  1.00 20.92  ? 227  VAL   A N   1 
ATOM   1457 C  CA  . VAL   A 1 227 ? 13.304 -3.839  24.117  1.00 21.28  ? 227  VAL   A CA  1 
ATOM   1458 C  C   . VAL   A 1 227 ? 12.726 -3.818  25.560  1.00 21.84  ? 227  VAL   A C   1 
ATOM   1459 O  O   . VAL   A 1 227 ? 11.588 -3.368  25.762  1.00 23.85  ? 227  VAL   A O   1 
ATOM   1460 C  CB  . VAL   A 1 227 ? 14.744 -3.272  23.959  1.00 21.68  ? 227  VAL   A CB  1 
ATOM   1461 C  CG1 . VAL   A 1 227 ? 15.257 -3.490  22.545  1.00 22.96  ? 227  VAL   A CG1 1 
ATOM   1462 C  CG2 . VAL   A 1 227 ? 14.775 -1.796  24.315  1.00 22.05  ? 227  VAL   A CG2 1 
ATOM   1463 N  N   . ALA   A 1 228 ? 13.477 -4.300  26.525  1.00 22.09  ? 228  ALA   A N   1 
ATOM   1464 C  CA  . ALA   A 1 228 ? 12.997 -4.393  27.890  1.00 22.85  ? 228  ALA   A CA  1 
ATOM   1465 C  C   . ALA   A 1 228 ? 12.657 -3.037  28.509  1.00 23.81  ? 228  ALA   A C   1 
ATOM   1466 O  O   . ALA   A 1 228 ? 13.150 -1.982  28.070  1.00 23.50  ? 228  ALA   A O   1 
ATOM   1467 C  CB  . ALA   A 1 228 ? 14.055 -5.085  28.742  1.00 23.98  ? 228  ALA   A CB  1 
ATOM   1468 N  N   . GLU   A 1 229 ? 11.786 -3.085  29.532  1.00 25.42  ? 229  GLU   A N   1 
ATOM   1469 C  CA  . GLU   A 1 229 ? 11.444 -1.961  30.365  1.00 27.85  ? 229  GLU   A CA  1 
ATOM   1470 C  C   . GLU   A 1 229 ? 10.829 -0.778  29.616  1.00 28.29  ? 229  GLU   A C   1 
ATOM   1471 O  O   . GLU   A 1 229 ? 11.163 0.363   29.911  1.00 30.11  ? 229  GLU   A O   1 
ATOM   1472 C  CB  . GLU   A 1 229 ? 12.681 -1.552  31.175  1.00 30.48  ? 229  GLU   A CB  1 
ATOM   1473 C  CG  . GLU   A 1 229 ? 13.173 -2.727  32.005  1.00 37.53  ? 229  GLU   A CG  1 
ATOM   1474 C  CD  . GLU   A 1 229 ? 14.327 -2.442  32.936  1.00 45.35  ? 229  GLU   A CD  1 
ATOM   1475 O  OE1 . GLU   A 1 229 ? 15.485 -2.369  32.466  1.00 46.70  ? 229  GLU   A OE1 1 
ATOM   1476 O  OE2 . GLU   A 1 229 ? 14.065 -2.303  34.150  1.00 47.24  ? 229  GLU   A OE2 1 
ATOM   1477 N  N   . GLY   A 1 230 ? 9.932  -1.085  28.687  1.00 27.40  ? 230  GLY   A N   1 
ATOM   1478 C  CA  . GLY   A 1 230 ? 9.137  -0.101  27.965  1.00 27.60  ? 230  GLY   A CA  1 
ATOM   1479 C  C   . GLY   A 1 230 ? 9.892  0.830   27.043  1.00 26.73  ? 230  GLY   A C   1 
ATOM   1480 O  O   . GLY   A 1 230 ? 9.424  1.944   26.790  1.00 29.50  ? 230  GLY   A O   1 
ATOM   1481 N  N   . LEU   A 1 231 ? 11.067 0.413   26.573  1.00 22.36  ? 231  LEU   A N   1 
ATOM   1482 C  CA  . LEU   A 1 231 ? 11.853 1.252   25.660  1.00 21.16  ? 231  LEU   A CA  1 
ATOM   1483 C  C   . LEU   A 1 231 ? 11.796 0.713   24.247  1.00 20.51  ? 231  LEU   A C   1 
ATOM   1484 O  O   . LEU   A 1 231 ? 11.492 -0.457  24.007  1.00 21.11  ? 231  LEU   A O   1 
ATOM   1485 C  CB  . LEU   A 1 231 ? 13.312 1.302   26.127  1.00 21.48  ? 231  LEU   A CB  1 
ATOM   1486 C  CG  . LEU   A 1 231 ? 13.512 1.843   27.537  1.00 25.51  ? 231  LEU   A CG  1 
ATOM   1487 C  CD1 . LEU   A 1 231 ? 14.997 1.852   27.882  1.00 28.30  ? 231  LEU   A CD1 1 
ATOM   1488 C  CD2 . LEU   A 1 231 ? 12.833 3.222   27.720  1.00 28.58  ? 231  LEU   A CD2 1 
ATOM   1489 N  N   . ILE   A 1 232 ? 12.135 1.579   23.299  1.00 18.61  ? 232  ILE   A N   1 
ATOM   1490 C  CA  . ILE   A 1 232 ? 12.257 1.214   21.886  1.00 17.59  ? 232  ILE   A CA  1 
ATOM   1491 C  C   . ILE   A 1 232 ? 13.661 1.481   21.455  1.00 17.47  ? 232  ILE   A C   1 
ATOM   1492 O  O   . ILE   A 1 232 ? 14.216 2.514   21.814  1.00 17.52  ? 232  ILE   A O   1 
ATOM   1493 C  CB  . ILE   A 1 232 ? 11.271 2.016   21.023  1.00 19.34  ? 232  ILE   A CB  1 
ATOM   1494 C  CG1 . ILE   A 1 232 ? 9.821  1.676   21.473  1.00 23.22  ? 232  ILE   A CG1 1 
ATOM   1495 C  CG2 . ILE   A 1 232 ? 11.451 1.723   19.512  1.00 19.83  ? 232  ILE   A CG2 1 
ATOM   1496 C  CD1 . ILE   A 1 232 ? 8.865  2.556   20.976  1.00 26.42  ? 232  ILE   A CD1 1 
ATOM   1497 N  N   . GLU   A 1 233 ? 14.255 0.594   20.678  1.00 16.40  ? 233  GLU   A N   1 
ATOM   1498 C  CA  . GLU   A 1 233 ? 15.591 0.752   20.193  1.00 16.65  ? 233  GLU   A CA  1 
ATOM   1499 C  C   . GLU   A 1 233 ? 15.494 1.003   18.689  1.00 17.74  ? 233  GLU   A C   1 
ATOM   1500 O  O   . GLU   A 1 233 ? 15.048 0.148   17.931  1.00 18.93  ? 233  GLU   A O   1 
ATOM   1501 C  CB  . GLU   A 1 233 ? 16.354 -0.536  20.527  1.00 19.91  ? 233  GLU   A CB  1 
ATOM   1502 C  CG  . GLU   A 1 233 ? 17.761 -0.532  19.984  1.00 21.25  ? 233  GLU   A CG  1 
ATOM   1503 C  CD  . GLU   A 1 233 ? 18.360 -1.888  20.313  1.00 27.96  ? 233  GLU   A CD  1 
ATOM   1504 O  OE1 . GLU   A 1 233 ? 18.285 -2.806  19.460  1.00 30.52  ? 233  GLU   A OE1 1 
ATOM   1505 O  OE2 . GLU   A 1 233 ? 18.782 -2.065  21.478  1.00 25.38  ? 233  GLU   A OE2 1 
ATOM   1506 N  N   . ASP   A 1 234 ? 15.887 2.213   18.252  1.00 15.90  ? 234  ASP   A N   1 
ATOM   1507 C  CA  . ASP   A 1 234 ? 15.869 2.582   16.844  1.00 16.63  ? 234  ASP   A CA  1 
ATOM   1508 C  C   . ASP   A 1 234 ? 17.226 2.200   16.272  1.00 17.60  ? 234  ASP   A C   1 
ATOM   1509 O  O   . ASP   A 1 234 ? 18.252 2.477   16.901  1.00 18.42  ? 234  ASP   A O   1 
ATOM   1510 C  CB  . ASP   A 1 234 ? 15.724 4.113   16.743  1.00 16.39  ? 234  ASP   A CB  1 
ATOM   1511 C  CG  . ASP   A 1 234 ? 14.330 4.600   17.055  1.00 17.21  ? 234  ASP   A CG  1 
ATOM   1512 O  OD1 . ASP   A 1 234 ? 13.359 3.780   16.963  1.00 17.85  ? 234  ASP   A OD1 1 
ATOM   1513 O  OD2 . ASP   A 1 234 ? 14.195 5.763   17.438  1.00 18.19  ? 234  ASP   A OD2 1 
ATOM   1514 N  N   . HIS   A 1 235 ? 17.241 1.628   15.059  1.00 15.86  ? 235  HIS   A N   1 
ATOM   1515 C  CA  . HIS   A 1 235 ? 18.503 1.288   14.385  1.00 16.44  ? 235  HIS   A CA  1 
ATOM   1516 C  C   . HIS   A 1 235 ? 18.614 2.170   13.150  1.00 16.51  ? 235  HIS   A C   1 
ATOM   1517 O  O   . HIS   A 1 235 ? 17.694 2.205   12.329  1.00 17.59  ? 235  HIS   A O   1 
ATOM   1518 C  CB  . HIS   A 1 235 ? 18.436 -0.177  13.896  1.00 17.83  ? 235  HIS   A CB  1 
ATOM   1519 C  CG  . HIS   A 1 235 ? 18.309 -1.202  14.980  1.00 21.78  ? 235  HIS   A CG  1 
ATOM   1520 N  ND1 . HIS   A 1 235 ? 18.281 -2.555  14.679  1.00 26.04  ? 235  HIS   A ND1 1 
ATOM   1521 C  CD2 . HIS   A 1 235 ? 18.184 -1.050  16.317  1.00 25.03  ? 235  HIS   A CD2 1 
ATOM   1522 C  CE1 . HIS   A 1 235 ? 18.199 -3.187  15.843  1.00 25.88  ? 235  HIS   A CE1 1 
ATOM   1523 N  NE2 . HIS   A 1 235 ? 18.135 -2.334  16.861  1.00 25.26  ? 235  HIS   A NE2 1 
ATOM   1524 N  N   . PHE   A 1 236 ? 19.693 2.937   13.039  1.00 15.14  ? 236  PHE   A N   1 
ATOM   1525 C  CA  . PHE   A 1 236 ? 19.918 3.765   11.858  1.00 15.43  ? 236  PHE   A CA  1 
ATOM   1526 C  C   . PHE   A 1 236 ? 20.907 3.066   10.923  1.00 15.90  ? 236  PHE   A C   1 
ATOM   1527 O  O   . PHE   A 1 236 ? 21.768 2.302   11.382  1.00 16.90  ? 236  PHE   A O   1 
ATOM   1528 C  CB  . PHE   A 1 236 ? 20.437 5.135   12.326  1.00 14.61  ? 236  PHE   A CB  1 
ATOM   1529 C  CG  . PHE   A 1 236 ? 19.418 5.837   13.186  1.00 14.34  ? 236  PHE   A CG  1 
ATOM   1530 C  CD1 . PHE   A 1 236 ? 18.397 6.576   12.608  1.00 14.82  ? 236  PHE   A CD1 1 
ATOM   1531 C  CD2 . PHE   A 1 236 ? 19.430 5.698   14.572  1.00 14.41  ? 236  PHE   A CD2 1 
ATOM   1532 C  CE1 . PHE   A 1 236 ? 17.407 7.161   13.392  1.00 15.86  ? 236  PHE   A CE1 1 
ATOM   1533 C  CE2 . PHE   A 1 236 ? 18.423 6.285   15.355  1.00 15.14  ? 236  PHE   A CE2 1 
ATOM   1534 C  CZ  . PHE   A 1 236 ? 17.464 7.062   14.761  1.00 16.16  ? 236  PHE   A CZ  1 
ATOM   1535 N  N   . ASP   A 1 237 ? 20.803 3.323   9.628   1.00 15.74  ? 237  ASP   A N   1 
ATOM   1536 C  CA  . ASP   A 1 237 ? 21.703 2.679   8.667   1.00 15.98  ? 237  ASP   A CA  1 
ATOM   1537 C  C   . ASP   A 1 237 ? 23.159 3.111   8.884   1.00 16.48  ? 237  ASP   A C   1 
ATOM   1538 O  O   . ASP   A 1 237 ? 23.407 4.173   9.466   1.00 16.52  ? 237  ASP   A O   1 
ATOM   1539 C  CB  . ASP   A 1 237 ? 21.245 2.943   7.241   1.00 18.28  ? 237  ASP   A CB  1 
ATOM   1540 C  CG  . ASP   A 1 237 ? 21.598 1.813   6.262   1.00 25.09  ? 237  ASP   A CG  1 
ATOM   1541 O  OD1 . ASP   A 1 237 ? 22.306 0.851   6.680   1.00 23.05  ? 237  ASP   A OD1 1 
ATOM   1542 O  OD2 . ASP   A 1 237 ? 21.194 1.907   5.085   1.00 27.96  ? 237  ASP   A OD2 1 
ATOM   1543 N  N   . VAL   A 1 238 ? 24.104 2.342   8.385   1.00 16.61  ? 238  VAL   A N   1 
ATOM   1544 C  CA  . VAL   A 1 238 ? 25.501 2.664   8.561   1.00 16.66  ? 238  VAL   A CA  1 
ATOM   1545 C  C   . VAL   A 1 238 ? 25.851 3.909   7.758   1.00 16.59  ? 238  VAL   A C   1 
ATOM   1546 O  O   . VAL   A 1 238 ? 25.386 4.086   6.627   1.00 16.96  ? 238  VAL   A O   1 
ATOM   1547 C  CB  . VAL   A 1 238 ? 26.399 1.441   8.159   1.00 17.05  ? 238  VAL   A CB  1 
ATOM   1548 C  CG1 . VAL   A 1 238 ? 26.278 1.071   6.680   1.00 18.67  ? 238  VAL   A CG1 1 
ATOM   1549 C  CG2 . VAL   A 1 238 ? 27.860 1.684   8.547   1.00 17.39  ? 238  VAL   A CG2 1 
ATOM   1550 N  N   . THR   A 1 239 ? 26.666 4.797   8.364   1.00 15.27  ? 239  THR   A N   1 
ATOM   1551 C  CA  . THR   A 1 239 ? 27.104 5.972   7.609   1.00 15.81  ? 239  THR   A CA  1 
ATOM   1552 C  C   . THR   A 1 239 ? 28.174 5.551   6.590   1.00 16.60  ? 239  THR   A C   1 
ATOM   1553 O  O   . THR   A 1 239 ? 28.797 4.484   6.667   1.00 17.25  ? 239  THR   A O   1 
ATOM   1554 C  CB  . THR   A 1 239 ? 27.743 7.023   8.573   1.00 15.44  ? 239  THR   A CB  1 
ATOM   1555 O  OG1 . THR   A 1 239 ? 29.002 6.540   9.068   1.00 16.06  ? 239  THR   A OG1 1 
ATOM   1556 C  CG2 . THR   A 1 239 ? 26.824 7.463   9.675   1.00 15.40  ? 239  THR   A CG2 1 
ATOM   1557 N  N   . VAL   A 1 240 ? 28.464 6.489   5.651   1.00 17.14  ? 240  VAL   A N   1 
ATOM   1558 C  CA  . VAL   A 1 240 ? 29.665 6.409   4.854   1.00 17.18  ? 240  VAL   A CA  1 
ATOM   1559 C  C   . VAL   A 1 240 ? 30.871 6.701   5.821   1.00 16.26  ? 240  VAL   A C   1 
ATOM   1560 O  O   . VAL   A 1 240 ? 30.706 7.047   7.007   1.00 16.80  ? 240  VAL   A O   1 
ATOM   1561 C  CB  . VAL   A 1 240 ? 29.635 7.493   3.739   1.00 18.16  ? 240  VAL   A CB  1 
ATOM   1562 C  CG1 . VAL   A 1 240 ? 28.551 7.176   2.729   1.00 20.27  ? 240  VAL   A CG1 1 
ATOM   1563 C  CG2 . VAL   A 1 240 ? 29.438 8.874   4.363   1.00 19.17  ? 240  VAL   A CG2 1 
ATOM   1564 N  N   . LYS   A 1 241 ? 32.101 6.533   5.318   1.00 16.12  ? 241  LYS   A N   1 
ATOM   1565 C  CA  . LYS   A 1 241 ? 33.298 6.809   6.091   1.00 16.48  ? 241  LYS   A CA  1 
ATOM   1566 C  C   . LYS   A 1 241 ? 33.379 8.313   6.384   1.00 16.07  ? 241  LYS   A C   1 
ATOM   1567 O  O   . LYS   A 1 241 ? 33.255 9.111   5.449   1.00 16.11  ? 241  LYS   A O   1 
ATOM   1568 C  CB  . LYS   A 1 241 ? 34.491 6.418   5.262   1.00 20.43  ? 241  LYS   A CB  1 
ATOM   1569 C  CG  . LYS   A 1 241 ? 35.736 6.378   6.037   1.00 25.74  ? 241  LYS   A CG  1 
ATOM   1570 C  CD  . LYS   A 1 241 ? 36.814 5.639   5.220   1.00 29.53  ? 241  LYS   A CD  1 
ATOM   1571 C  CE  . LYS   A 1 241 ? 38.059 5.570   6.048   1.00 34.89  ? 241  LYS   A CE  1 
ATOM   1572 N  NZ  . LYS   A 1 241 ? 39.225 5.102   5.262   1.00 36.32  ? 241  LYS   A NZ  1 
ATOM   1573 N  N   . MET   A 1 242 ? 33.530 8.669   7.654   1.00 15.24  ? 242  MET   A N   1 
ATOM   1574 C  CA  . MET   A 1 242 ? 33.498 10.076  8.052   1.00 14.78  ? 242  MET   A CA  1 
ATOM   1575 C  C   . MET   A 1 242 ? 34.187 10.276  9.397   1.00 14.48  ? 242  MET   A C   1 
ATOM   1576 O  O   . MET   A 1 242 ? 34.507 9.315   10.093  1.00 14.75  ? 242  MET   A O   1 
ATOM   1577 C  CB  . MET   A 1 242 ? 32.044 10.586  8.127   1.00 14.04  ? 242  MET   A CB  1 
ATOM   1578 C  CG  . MET   A 1 242 ? 31.288 10.041  9.336   1.00 14.84  ? 242  MET   A CG  1 
ATOM   1579 S  SD  . MET   A 1 242 ? 29.560 10.597  9.244   1.00 15.71  ? 242  MET   A SD  1 
ATOM   1580 C  CE  . MET   A 1 242 ? 29.123 10.457  11.004  1.00 15.49  ? 242  MET   A CE  1 
ATOM   1581 N  N   . SER   A 1 243 ? 34.426 11.536  9.762   1.00 14.00  ? 243  SER   A N   1 
ATOM   1582 C  CA  . SER   A 1 243 ? 35.069 11.907  11.000  1.00 13.24  ? 243  SER   A CA  1 
ATOM   1583 C  C   . SER   A 1 243 ? 34.101 11.833  12.187  1.00 13.24  ? 243  SER   A C   1 
ATOM   1584 O  O   . SER   A 1 243 ? 32.899 12.077  12.023  1.00 13.53  ? 243  SER   A O   1 
ATOM   1585 C  CB  . SER   A 1 243 ? 35.580 13.340  10.881  1.00 14.64  ? 243  SER   A CB  1 
ATOM   1586 O  OG  . SER   A 1 243 ? 36.435 13.485  9.746   1.00 14.93  ? 243  SER   A OG  1 
ATOM   1587 N  N   . THR   A 1 244 ? 34.636 11.537  13.381  1.00 13.13  ? 244  THR   A N   1 
ATOM   1588 C  CA  . THR   A 1 244 ? 33.807 11.428  14.567  1.00 13.05  ? 244  THR   A CA  1 
ATOM   1589 C  C   . THR   A 1 244 ? 33.021 12.710  14.862  1.00 13.46  ? 244  THR   A C   1 
ATOM   1590 O  O   . THR   A 1 244 ? 31.925 12.651  15.383  1.00 13.80  ? 244  THR   A O   1 
ATOM   1591 C  CB  . THR   A 1 244 ? 34.642 11.153  15.811  1.00 13.52  ? 244  THR   A CB  1 
ATOM   1592 O  OG1 . THR   A 1 244 ? 35.784 12.066  15.851  1.00 13.39  ? 244  THR   A OG1 1 
ATOM   1593 C  CG2 . THR   A 1 244 ? 35.196 9.713   15.805  1.00 14.29  ? 244  THR   A CG2 1 
ATOM   1594 N  N   . TYR   A 1 245 ? 33.598 13.861  14.478  1.00 12.46  ? 245  TYR   A N   1 
ATOM   1595 C  CA  . TYR   A 1 245 ? 32.911 15.118  14.849  1.00 12.88  ? 245  TYR   A CA  1 
ATOM   1596 C  C   . TYR   A 1 245 ? 31.587 15.318  14.109  1.00 13.45  ? 245  TYR   A C   1 
ATOM   1597 O  O   . TYR   A 1 245 ? 30.831 16.242  14.465  1.00 13.50  ? 245  TYR   A O   1 
ATOM   1598 C  CB  . TYR   A 1 245 ? 33.812 16.369  14.725  1.00 12.79  ? 245  TYR   A CB  1 
ATOM   1599 C  CG  . TYR   A 1 245 ? 34.086 16.815  13.305  1.00 12.23  ? 245  TYR   A CG  1 
ATOM   1600 C  CD1 . TYR   A 1 245 ? 33.194 17.634  12.621  1.00 12.40  ? 245  TYR   A CD1 1 
ATOM   1601 C  CD2 . TYR   A 1 245 ? 35.288 16.532  12.688  1.00 13.34  ? 245  TYR   A CD2 1 
ATOM   1602 C  CE1 . TYR   A 1 245 ? 33.475 18.092  11.326  1.00 12.58  ? 245  TYR   A CE1 1 
ATOM   1603 C  CE2 . TYR   A 1 245 ? 35.558 16.952  11.382  1.00 13.45  ? 245  TYR   A CE2 1 
ATOM   1604 C  CZ  . TYR   A 1 245 ? 34.663 17.760  10.721  1.00 12.62  ? 245  TYR   A CZ  1 
ATOM   1605 O  OH  . TYR   A 1 245 ? 34.954 18.202  9.425   1.00 13.55  ? 245  TYR   A OH  1 
ATOM   1606 N  N   . LEU   A 1 246 ? 31.333 14.506  13.077  1.00 13.06  ? 246  LEU   A N   1 
ATOM   1607 C  CA  . LEU   A 1 246 ? 30.109 14.642  12.300  1.00 13.14  ? 246  LEU   A CA  1 
ATOM   1608 C  C   . LEU   A 1 246 ? 28.994 13.718  12.768  1.00 13.11  ? 246  LEU   A C   1 
ATOM   1609 O  O   . LEU   A 1 246 ? 27.890 13.810  12.233  1.00 13.06  ? 246  LEU   A O   1 
ATOM   1610 C  CB  . LEU   A 1 246 ? 30.413 14.372  10.820  1.00 12.97  ? 246  LEU   A CB  1 
ATOM   1611 C  CG  . LEU   A 1 246 ? 31.286 15.426  10.199  1.00 13.04  ? 246  LEU   A CG  1 
ATOM   1612 C  CD1 . LEU   A 1 246 ? 31.778 14.943  8.820   1.00 14.12  ? 246  LEU   A CD1 1 
ATOM   1613 C  CD2 . LEU   A 1 246 ? 30.476 16.731  10.069  1.00 13.69  ? 246  LEU   A CD2 1 
ATOM   1614 N  N   . VAL   A 1 247 ? 29.236 12.841  13.765  1.00 12.72  ? 247  VAL   A N   1 
ATOM   1615 C  CA  . VAL   A 1 247 ? 28.143 12.011  14.277  1.00 12.80  ? 247  VAL   A CA  1 
ATOM   1616 C  C   . VAL   A 1 247 ? 27.118 12.903  14.951  1.00 12.69  ? 247  VAL   A C   1 
ATOM   1617 O  O   . VAL   A 1 247 ? 27.486 13.881  15.602  1.00 13.29  ? 247  VAL   A O   1 
ATOM   1618 C  CB  . VAL   A 1 247 ? 28.752 11.021  15.297  1.00 13.00  ? 247  VAL   A CB  1 
ATOM   1619 C  CG1 . VAL   A 1 247 ? 27.648 10.279  16.073  1.00 14.09  ? 247  VAL   A CG1 1 
ATOM   1620 C  CG2 . VAL   A 1 247 ? 29.665 10.019  14.590  1.00 15.03  ? 247  VAL   A CG2 1 
ATOM   1621 N  N   . ALA   A 1 248 ? 25.834 12.565  14.807  1.00 12.74  ? 248  ALA   A N   1 
ATOM   1622 C  CA  . ALA   A 1 248 ? 24.791 13.347  15.428  1.00 12.91  ? 248  ALA   A CA  1 
ATOM   1623 C  C   . ALA   A 1 248 ? 23.602 12.484  15.771  1.00 12.98  ? 248  ALA   A C   1 
ATOM   1624 O  O   . ALA   A 1 248 ? 23.290 11.528  15.046  1.00 13.45  ? 248  ALA   A O   1 
ATOM   1625 C  CB  . ALA   A 1 248 ? 24.335 14.494  14.501  1.00 13.20  ? 248  ALA   A CB  1 
ATOM   1626 N  N   . PHE   A 1 249 ? 22.887 12.885  16.799  1.00 12.62  ? 249  PHE   A N   1 
ATOM   1627 C  CA  . PHE   A 1 249 ? 21.627 12.234  17.155  1.00 13.07  ? 249  PHE   A CA  1 
ATOM   1628 C  C   . PHE   A 1 249 ? 20.826 13.148  18.059  1.00 13.52  ? 249  PHE   A C   1 
ATOM   1629 O  O   . PHE   A 1 249 ? 21.394 13.962  18.811  1.00 14.15  ? 249  PHE   A O   1 
ATOM   1630 C  CB  . PHE   A 1 249 ? 21.833 10.821  17.817  1.00 13.80  ? 249  PHE   A CB  1 
ATOM   1631 C  CG  . PHE   A 1 249 ? 22.990 10.667  18.774  1.00 14.06  ? 249  PHE   A CG  1 
ATOM   1632 C  CD1 . PHE   A 1 249 ? 22.843 10.974  20.120  1.00 14.43  ? 249  PHE   A CD1 1 
ATOM   1633 C  CD2 . PHE   A 1 249 ? 24.239 10.240  18.324  1.00 14.74  ? 249  PHE   A CD2 1 
ATOM   1634 C  CE1 . PHE   A 1 249 ? 23.913 10.832  20.991  1.00 14.61  ? 249  PHE   A CE1 1 
ATOM   1635 C  CE2 . PHE   A 1 249 ? 25.312 10.124  19.195  1.00 15.14  ? 249  PHE   A CE2 1 
ATOM   1636 C  CZ  . PHE   A 1 249 ? 25.124 10.393  20.532  1.00 13.81  ? 249  PHE   A CZ  1 
ATOM   1637 N  N   . ILE   A 1 250 ? 19.509 13.091  17.904  1.00 12.73  ? 250  ILE   A N   1 
ATOM   1638 C  CA  . ILE   A 1 250 ? 18.622 13.993  18.631  1.00 12.89  ? 250  ILE   A CA  1 
ATOM   1639 C  C   . ILE   A 1 250 ? 17.433 13.165  19.129  1.00 13.14  ? 250  ILE   A C   1 
ATOM   1640 O  O   . ILE   A 1 250 ? 16.842 12.424  18.328  1.00 13.72  ? 250  ILE   A O   1 
ATOM   1641 C  CB  . ILE   A 1 250 ? 18.080 15.089  17.665  1.00 13.06  ? 250  ILE   A CB  1 
ATOM   1642 C  CG1 . ILE   A 1 250 ? 19.237 15.861  17.027  1.00 13.89  ? 250  ILE   A CG1 1 
ATOM   1643 C  CG2 . ILE   A 1 250 ? 17.191 16.050  18.457  1.00 14.82  ? 250  ILE   A CG2 1 
ATOM   1644 C  CD1 . ILE   A 1 250 ? 18.798 16.925  15.971  1.00 14.99  ? 250  ILE   A CD1 1 
ATOM   1645 N  N   . ILE   A 1 251 ? 17.063 13.347  20.385  1.00 13.35  ? 251  ILE   A N   1 
ATOM   1646 C  CA  . ILE   A 1 251 ? 15.881 12.680  20.963  1.00 13.66  ? 251  ILE   A CA  1 
ATOM   1647 C  C   . ILE   A 1 251 ? 14.959 13.834  21.353  1.00 13.58  ? 251  ILE   A C   1 
ATOM   1648 O  O   . ILE   A 1 251 ? 15.330 14.673  22.182  1.00 14.06  ? 251  ILE   A O   1 
ATOM   1649 C  CB  . ILE   A 1 251 ? 16.308 11.820  22.141  1.00 14.92  ? 251  ILE   A CB  1 
ATOM   1650 C  CG1 . ILE   A 1 251 ? 17.240 10.681  21.642  1.00 18.29  ? 251  ILE   A CG1 1 
ATOM   1651 C  CG2 . ILE   A 1 251 ? 15.057 11.185  22.766  1.00 16.58  ? 251  ILE   A CG2 1 
ATOM   1652 C  CD1 . ILE   A 1 251 ? 18.704 11.036  21.759  1.00 24.45  ? 251  ILE   A CD1 1 
ATOM   1653 N  N   . SER   A 1 252 ? 13.743 13.898  20.744  1.00 12.98  ? 252  SER   A N   1 
ATOM   1654 C  CA  . SER   A 1 252 ? 12.917 15.099  20.899  1.00 13.83  ? 252  SER   A CA  1 
ATOM   1655 C  C   . SER   A 1 252 ? 11.475 14.760  20.588  1.00 14.69  ? 252  SER   A C   1 
ATOM   1656 O  O   . SER   A 1 252 ? 11.120 13.625  20.381  1.00 15.67  ? 252  SER   A O   1 
ATOM   1657 C  CB  . SER   A 1 252 ? 13.390 16.140  19.872  1.00 14.61  ? 252  SER   A CB  1 
ATOM   1658 O  OG  . SER   A 1 252 ? 12.954 15.777  18.573  1.00 15.02  ? 252  SER   A OG  1 
ATOM   1659 N  N   . ASP   A 1 253 ? 10.667 15.818  20.519  1.00 15.39  ? 253  ASP   A N   1 
ATOM   1660 C  CA  A ASP   A 1 253 ? 9.258  15.798  20.157  0.50 15.42  ? 253  ASP   A CA  1 
ATOM   1661 C  CA  B ASP   A 1 253 ? 9.282  15.635  20.054  0.50 16.10  ? 253  ASP   A CA  1 
ATOM   1662 C  C   . ASP   A 1 253 ? 9.075  16.473  18.780  1.00 15.58  ? 253  ASP   A C   1 
ATOM   1663 O  O   . ASP   A 1 253 ? 7.971  16.944  18.500  1.00 16.16  ? 253  ASP   A O   1 
ATOM   1664 C  CB  A ASP   A 1 253 ? 8.466  16.613  21.226  0.50 15.48  ? 253  ASP   A CB  1 
ATOM   1665 C  CB  B ASP   A 1 253 ? 8.244  15.964  21.145  0.50 18.51  ? 253  ASP   A CB  1 
ATOM   1666 C  CG  A ASP   A 1 253 ? 8.694  18.119  21.194  0.50 16.01  ? 253  ASP   A CG  1 
ATOM   1667 C  CG  B ASP   A 1 253 ? 8.246  14.998  22.307  0.50 26.54  ? 253  ASP   A CG  1 
ATOM   1668 O  OD1 A ASP   A 1 253 ? 9.660  18.568  20.546  0.50 19.41  ? 253  ASP   A OD1 1 
ATOM   1669 O  OD1 B ASP   A 1 253 ? 8.375  13.783  22.061  0.50 27.08  ? 253  ASP   A OD1 1 
ATOM   1670 O  OD2 A ASP   A 1 253 ? 7.833  18.865  21.727  0.50 20.16  ? 253  ASP   A OD2 1 
ATOM   1671 O  OD2 B ASP   A 1 253 ? 8.101  15.458  23.465  0.50 30.56  ? 253  ASP   A OD2 1 
ATOM   1672 N  N   . PHE   A 1 254 ? 10.124 16.648  17.978  1.00 14.10  ? 254  PHE   A N   1 
ATOM   1673 C  CA  . PHE   A 1 254 ? 10.008 17.468  16.769  1.00 13.40  ? 254  PHE   A CA  1 
ATOM   1674 C  C   . PHE   A 1 254 ? 9.036  16.964  15.735  1.00 14.33  ? 254  PHE   A C   1 
ATOM   1675 O  O   . PHE   A 1 254 ? 8.874  15.750  15.506  1.00 15.95  ? 254  PHE   A O   1 
ATOM   1676 C  CB  . PHE   A 1 254 ? 11.365 17.578  16.056  1.00 14.38  ? 254  PHE   A CB  1 
ATOM   1677 C  CG  . PHE   A 1 254 ? 12.498 18.347  16.706  1.00 15.01  ? 254  PHE   A CG  1 
ATOM   1678 C  CD1 . PHE   A 1 254 ? 12.248 19.267  17.704  1.00 15.45  ? 254  PHE   A CD1 1 
ATOM   1679 C  CD2 . PHE   A 1 254 ? 13.815 18.109  16.332  1.00 15.49  ? 254  PHE   A CD2 1 
ATOM   1680 C  CE1 . PHE   A 1 254 ? 13.312 19.978  18.306  1.00 16.86  ? 254  PHE   A CE1 1 
ATOM   1681 C  CE2 . PHE   A 1 254 ? 14.872 18.834  16.924  1.00 15.03  ? 254  PHE   A CE2 1 
ATOM   1682 C  CZ  . PHE   A 1 254 ? 14.607 19.731  17.922  1.00 15.35  ? 254  PHE   A CZ  1 
ATOM   1683 N  N   . GLU   A 1 255 ? 8.346  17.933  15.128  1.00 12.56  ? 255  GLU   A N   1 
ATOM   1684 C  CA  . GLU   A 1 255 ? 7.584  17.695  13.912  1.00 13.39  ? 255  GLU   A CA  1 
ATOM   1685 C  C   . GLU   A 1 255 ? 8.538  17.847  12.698  1.00 14.04  ? 255  GLU   A C   1 
ATOM   1686 O  O   . GLU   A 1 255 ? 9.606  18.451  12.831  1.00 13.24  ? 255  GLU   A O   1 
ATOM   1687 C  CB  . GLU   A 1 255 ? 6.475  18.770  13.766  1.00 13.60  ? 255  GLU   A CB  1 
ATOM   1688 C  CG  . GLU   A 1 255 ? 5.292  18.546  14.673  1.00 14.61  ? 255  GLU   A CG  1 
ATOM   1689 C  CD  . GLU   A 1 255 ? 4.268  17.552  14.159  1.00 16.80  ? 255  GLU   A CD  1 
ATOM   1690 O  OE1 . GLU   A 1 255 ? 4.273  17.233  12.945  1.00 17.05  ? 255  GLU   A OE1 1 
ATOM   1691 O  OE2 . GLU   A 1 255 ? 3.439  17.109  14.992  1.00 17.22  ? 255  GLU   A OE2 1 
ATOM   1692 N  N   . SER   A 1 256 ? 8.103  17.428  11.499  1.00 14.45  ? 256  SER   A N   1 
ATOM   1693 C  CA  . SER   A 1 256 ? 8.890  17.612  10.302  1.00 14.53  ? 256  SER   A CA  1 
ATOM   1694 C  C   . SER   A 1 256 ? 8.045  17.830  9.095   1.00 14.95  ? 256  SER   A C   1 
ATOM   1695 O  O   . SER   A 1 256 ? 6.833  17.545  9.094   1.00 15.72  ? 256  SER   A O   1 
ATOM   1696 C  CB  . SER   A 1 256 ? 9.827  16.434  10.084  1.00 16.02  ? 256  SER   A CB  1 
ATOM   1697 O  OG  . SER   A 1 256 ? 9.071  15.238  9.876   1.00 19.11  ? 256  SER   A OG  1 
ATOM   1698 N  N   . VAL   A 1 257 ? 8.686  18.388  8.069   1.00 14.03  ? 257  VAL   A N   1 
ATOM   1699 C  CA  . VAL   A 1 257 ? 8.195  18.550  6.701   1.00 14.64  ? 257  VAL   A CA  1 
ATOM   1700 C  C   . VAL   A 1 257 ? 9.269  18.088  5.759   1.00 14.58  ? 257  VAL   A C   1 
ATOM   1701 O  O   . VAL   A 1 257 ? 10.458 18.156  6.096   1.00 14.96  ? 257  VAL   A O   1 
ATOM   1702 C  CB  . VAL   A 1 257 ? 7.723  19.957  6.380   1.00 15.38  ? 257  VAL   A CB  1 
ATOM   1703 C  CG1 . VAL   A 1 257 ? 6.406  20.232  7.118   1.00 16.16  ? 257  VAL   A CG1 1 
ATOM   1704 C  CG2 . VAL   A 1 257 ? 8.802  20.985  6.733   1.00 15.58  ? 257  VAL   A CG2 1 
ATOM   1705 N  N   . SER   A 1 258 ? 8.895  17.607  4.552   1.00 14.42  ? 258  SER   A N   1 
ATOM   1706 C  CA  A SER   A 1 258 ? 9.886  17.090  3.630   0.50 15.52  ? 258  SER   A CA  1 
ATOM   1707 C  CA  B SER   A 1 258 ? 9.874  17.053  3.633   0.50 15.89  ? 258  SER   A CA  1 
ATOM   1708 C  C   . SER   A 1 258 ? 9.584  17.390  2.190   1.00 16.41  ? 258  SER   A C   1 
ATOM   1709 O  O   . SER   A 1 258 ? 8.432  17.673  1.837   1.00 17.12  ? 258  SER   A O   1 
ATOM   1710 C  CB  A SER   A 1 258 ? 10.025 15.587  3.811   0.50 16.30  ? 258  SER   A CB  1 
ATOM   1711 C  CB  B SER   A 1 258 ? 9.914  15.532  3.762   0.50 17.81  ? 258  SER   A CB  1 
ATOM   1712 O  OG  A SER   A 1 258 ? 8.793  14.948  3.533   0.50 15.73  ? 258  SER   A OG  1 
ATOM   1713 O  OG  B SER   A 1 258 ? 10.037 15.071  5.098   0.50 19.28  ? 258  SER   A OG  1 
ATOM   1714 N  N   . LYS   A 1 259 ? 10.608 17.292  1.361   1.00 15.06  ? 259  LYS   A N   1 
ATOM   1715 C  CA  . LYS   A 1 259 ? 10.501 17.503  -0.074  1.00 15.95  ? 259  LYS   A CA  1 
ATOM   1716 C  C   . LYS   A 1 259 ? 11.666 16.685  -0.683  1.00 17.58  ? 259  LYS   A C   1 
ATOM   1717 O  O   . LYS   A 1 259 ? 12.742 16.619  -0.095  1.00 17.94  ? 259  LYS   A O   1 
ATOM   1718 C  CB  . LYS   A 1 259 ? 10.643 19.003  -0.413  1.00 17.28  ? 259  LYS   A CB  1 
ATOM   1719 C  CG  . LYS   A 1 259 ? 10.502 19.366  -1.908  1.00 20.34  ? 259  LYS   A CG  1 
ATOM   1720 C  CD  . LYS   A 1 259 ? 10.373 20.874  -2.048  1.00 23.82  ? 259  LYS   A CD  1 
ATOM   1721 C  CE  . LYS   A 1 259 ? 10.166 21.325  -3.486  1.00 28.58  ? 259  LYS   A CE  1 
ATOM   1722 N  NZ  . LYS   A 1 259 ? 10.266 22.805  -3.600  1.00 31.48  ? 259  LYS   A NZ  1 
ATOM   1723 N  N   . ILE   A 1 260 ? 11.453 16.094  -1.856  1.00 18.14  ? 260  ILE   A N   1 
ATOM   1724 C  CA  . ILE   A 1 260 ? 12.484 15.244  -2.478  1.00 18.66  ? 260  ILE   A CA  1 
ATOM   1725 C  C   . ILE   A 1 260 ? 13.179 15.993  -3.584  1.00 18.60  ? 260  ILE   A C   1 
ATOM   1726 O  O   . ILE   A 1 260 ? 12.506 16.642  -4.406  1.00 20.01  ? 260  ILE   A O   1 
ATOM   1727 C  CB  . ILE   A 1 260 ? 11.808 13.988  -3.077  1.00 21.22  ? 260  ILE   A CB  1 
ATOM   1728 C  CG1 . ILE   A 1 260 ? 10.855 13.316  -2.100  1.00 25.19  ? 260  ILE   A CG1 1 
ATOM   1729 C  CG2 . ILE   A 1 260 ? 12.839 13.012  -3.639  1.00 21.70  ? 260  ILE   A CG2 1 
ATOM   1730 C  CD1 . ILE   A 1 260 ? 11.461 12.802  -0.937  1.00 28.67  ? 260  ILE   A CD1 1 
ATOM   1731 N  N   . THR   A 1 261 ? 14.534 15.916  -3.639  1.00 17.38  ? 261  THR   A N   1 
ATOM   1732 C  CA  . THR   A 1 261 ? 15.253 16.594  -4.710  1.00 17.38  ? 261  THR   A CA  1 
ATOM   1733 C  C   . THR   A 1 261 ? 15.047 15.826  -6.033  1.00 19.20  ? 261  THR   A C   1 
ATOM   1734 O  O   . THR   A 1 261 ? 14.574 14.667  -6.033  1.00 19.69  ? 261  THR   A O   1 
ATOM   1735 C  CB  . THR   A 1 261 ? 16.771 16.608  -4.420  1.00 17.20  ? 261  THR   A CB  1 
ATOM   1736 O  OG1 . THR   A 1 261 ? 17.257 15.265  -4.407  1.00 17.28  ? 261  THR   A OG1 1 
ATOM   1737 C  CG2 . THR   A 1 261 ? 17.126 17.315  -3.131  1.00 18.49  ? 261  THR   A CG2 1 
ATOM   1738 N  N   . LYS   A 1 262 ? 15.467 16.462  -7.143  1.00 19.61  ? 262  LYS   A N   1 
ATOM   1739 C  CA  . LYS   A 1 262 ? 15.440 15.771  -8.437  1.00 20.36  ? 262  LYS   A CA  1 
ATOM   1740 C  C   . LYS   A 1 262 ? 16.299 14.491  -8.409  1.00 22.12  ? 262  LYS   A C   1 
ATOM   1741 O  O   . LYS   A 1 262 ? 16.004 13.528  -9.124  1.00 23.36  ? 262  LYS   A O   1 
ATOM   1742 C  CB  . LYS   A 1 262 ? 16.026 16.721  -9.493  1.00 23.90  ? 262  LYS   A CB  1 
ATOM   1743 C  CG  . LYS   A 1 262 ? 15.171 17.941  -9.756  1.00 30.69  ? 262  LYS   A CG  1 
ATOM   1744 C  CD  . LYS   A 1 262 ? 16.025 19.030  -10.446 1.00 35.46  ? 262  LYS   A CD  1 
ATOM   1745 C  CE  . LYS   A 1 262 ? 15.210 20.265  -10.750 1.00 40.85  ? 262  LYS   A CE  1 
ATOM   1746 N  NZ  . LYS   A 1 262 ? 14.336 20.669  -9.616  1.00 43.52  ? 262  LYS   A NZ  1 
ATOM   1747 N  N   . SER   A 1 263 ? 17.363 14.465  -7.586  1.00 20.55  ? 263  SER   A N   1 
ATOM   1748 C  CA  . SER   A 1 263 ? 18.206 13.278  -7.462  1.00 20.70  ? 263  SER   A CA  1 
ATOM   1749 C  C   . SER   A 1 263 ? 17.631 12.207  -6.545  1.00 20.82  ? 263  SER   A C   1 
ATOM   1750 O  O   . SER   A 1 263 ? 18.247 11.151  -6.384  1.00 22.53  ? 263  SER   A O   1 
ATOM   1751 C  CB  . SER   A 1 263 ? 19.588 13.657  -6.954  1.00 21.99  ? 263  SER   A CB  1 
ATOM   1752 O  OG  . SER   A 1 263 ? 19.465 14.406  -5.746  1.00 24.55  ? 263  SER   A OG  1 
ATOM   1753 N  N   . GLY   A 1 264 ? 16.471 12.456  -5.916  1.00 19.19  ? 264  GLY   A N   1 
ATOM   1754 C  CA  . GLY   A 1 264 ? 15.841 11.459  -5.069  1.00 19.76  ? 264  GLY   A CA  1 
ATOM   1755 C  C   . GLY   A 1 264 ? 16.191 11.552  -3.604  1.00 19.30  ? 264  GLY   A C   1 
ATOM   1756 O  O   . GLY   A 1 264 ? 15.794 10.671  -2.851  1.00 20.53  ? 264  GLY   A O   1 
ATOM   1757 N  N   . VAL   A 1 265 ? 16.913 12.605  -3.185  1.00 18.50  ? 265  VAL   A N   1 
ATOM   1758 C  CA  . VAL   A 1 265 ? 17.266 12.728  -1.767  1.00 17.72  ? 265  VAL   A CA  1 
ATOM   1759 C  C   . VAL   A 1 265 ? 16.094 13.310  -0.999  1.00 16.43  ? 265  VAL   A C   1 
ATOM   1760 O  O   . VAL   A 1 265 ? 15.531 14.326  -1.434  1.00 16.79  ? 265  VAL   A O   1 
ATOM   1761 C  CB  . VAL   A 1 265 ? 18.458 13.676  -1.645  1.00 16.59  ? 265  VAL   A CB  1 
ATOM   1762 C  CG1 . VAL   A 1 265 ? 18.809 13.923  -0.165  1.00 16.45  ? 265  VAL   A CG1 1 
ATOM   1763 C  CG2 . VAL   A 1 265 ? 19.645 13.124  -2.398  1.00 18.27  ? 265  VAL   A CG2 1 
ATOM   1764 N  N   . LYS   A 1 266 ? 15.725 12.700  0.127   1.00 15.89  ? 266  LYS   A N   1 
ATOM   1765 C  CA  . LYS   A 1 266 ? 14.631 13.215  0.939   1.00 15.71  ? 266  LYS   A CA  1 
ATOM   1766 C  C   . LYS   A 1 266 ? 15.183 14.306  1.872   1.00 15.64  ? 266  LYS   A C   1 
ATOM   1767 O  O   . LYS   A 1 266 ? 15.972 14.003  2.777   1.00 16.25  ? 266  LYS   A O   1 
ATOM   1768 C  CB  . LYS   A 1 266 ? 13.965 12.109  1.757   1.00 15.70  ? 266  LYS   A CB  1 
ATOM   1769 C  CG  . LYS   A 1 266 ? 12.732 12.593  2.512   1.00 17.57  ? 266  LYS   A CG  1 
ATOM   1770 C  CD  . LYS   A 1 266 ? 12.023 11.443  3.251   1.00 19.38  ? 266  LYS   A CD  1 
ATOM   1771 C  CE  . LYS   A 1 266 ? 10.739 11.933  3.873   1.00 21.67  ? 266  LYS   A CE  1 
ATOM   1772 N  NZ  . LYS   A 1 266 ? 9.997  10.797  4.540   1.00 25.55  ? 266  LYS   A NZ  1 
ATOM   1773 N  N   . VAL   A 1 267 ? 14.762 15.557  1.665   1.00 14.83  ? 267  VAL   A N   1 
ATOM   1774 C  CA  . VAL   A 1 267 ? 15.225 16.658  2.520   1.00 13.87  ? 267  VAL   A CA  1 
ATOM   1775 C  C   . VAL   A 1 267 ? 14.106 16.952  3.483   1.00 14.12  ? 267  VAL   A C   1 
ATOM   1776 O  O   . VAL   A 1 267 ? 12.949 17.049  3.073   1.00 14.92  ? 267  VAL   A O   1 
ATOM   1777 C  CB  . VAL   A 1 267 ? 15.537 17.880  1.654   1.00 15.40  ? 267  VAL   A CB  1 
ATOM   1778 C  CG1 . VAL   A 1 267 ? 16.023 19.041  2.531   1.00 15.37  ? 267  VAL   A CG1 1 
ATOM   1779 C  CG2 . VAL   A 1 267 ? 16.637 17.531  0.657   1.00 16.30  ? 267  VAL   A CG2 1 
ATOM   1780 N  N   . SER   A 1 268 ? 14.406 17.087  4.781   1.00 13.88  ? 268  SER   A N   1 
ATOM   1781 C  CA  . SER   A 1 268 ? 13.399 17.409  5.773   1.00 13.37  ? 268  SER   A CA  1 
ATOM   1782 C  C   . SER   A 1 268 ? 13.855 18.499  6.698   1.00 14.32  ? 268  SER   A C   1 
ATOM   1783 O  O   . SER   A 1 268 ? 15.049 18.593  6.968   1.00 15.36  ? 268  SER   A O   1 
ATOM   1784 C  CB  . SER   A 1 268 ? 13.073 16.218  6.668   1.00 14.31  ? 268  SER   A CB  1 
ATOM   1785 O  OG  . SER   A 1 268 ? 12.584 15.106  5.942   1.00 16.19  ? 268  SER   A OG  1 
ATOM   1786 N  N   . VAL   A 1 269 ? 12.918 19.314  7.170   1.00 13.20  ? 269  VAL   A N   1 
ATOM   1787 C  CA  . VAL   A 1 269 ? 13.152 20.263  8.245   1.00 12.76  ? 269  VAL   A CA  1 
ATOM   1788 C  C   . VAL   A 1 269 ? 12.432 19.760  9.470   1.00 12.95  ? 269  VAL   A C   1 
ATOM   1789 O  O   . VAL   A 1 269 ? 11.269 19.344  9.373   1.00 13.86  ? 269  VAL   A O   1 
ATOM   1790 C  CB  . VAL   A 1 269 ? 12.737 21.695  7.890   1.00 13.74  ? 269  VAL   A CB  1 
ATOM   1791 C  CG1 . VAL   A 1 269 ? 12.873 22.605  9.114   1.00 14.67  ? 269  VAL   A CG1 1 
ATOM   1792 C  CG2 . VAL   A 1 269 ? 13.566 22.233  6.703   1.00 13.94  ? 269  VAL   A CG2 1 
ATOM   1793 N  N   . TYR   A 1 270 ? 13.132 19.747  10.609  1.00 12.76  ? 270  TYR   A N   1 
ATOM   1794 C  CA  . TYR   A 1 270 ? 12.569 19.365  11.889  1.00 13.23  ? 270  TYR   A CA  1 
ATOM   1795 C  C   . TYR   A 1 270 ? 12.588 20.548  12.814  1.00 12.94  ? 270  TYR   A C   1 
ATOM   1796 O  O   . TYR   A 1 270 ? 13.551 21.324  12.843  1.00 13.25  ? 270  TYR   A O   1 
ATOM   1797 C  CB  . TYR   A 1 270 ? 13.425 18.247  12.543  1.00 13.33  ? 270  TYR   A CB  1 
ATOM   1798 C  CG  . TYR   A 1 270 ? 13.191 16.879  11.947  1.00 12.65  ? 270  TYR   A CG  1 
ATOM   1799 C  CD1 . TYR   A 1 270 ? 13.827 16.498  10.784  1.00 13.02  ? 270  TYR   A CD1 1 
ATOM   1800 C  CD2 . TYR   A 1 270 ? 12.361 15.957  12.579  1.00 12.70  ? 270  TYR   A CD2 1 
ATOM   1801 C  CE1 . TYR   A 1 270 ? 13.662 15.223  10.251  1.00 13.15  ? 270  TYR   A CE1 1 
ATOM   1802 C  CE2 . TYR   A 1 270 ? 12.185 14.682  12.060  1.00 14.06  ? 270  TYR   A CE2 1 
ATOM   1803 C  CZ  . TYR   A 1 270 ? 12.824 14.327  10.889  1.00 14.78  ? 270  TYR   A CZ  1 
ATOM   1804 O  OH  . TYR   A 1 270 ? 12.582 13.067  10.337  1.00 16.86  ? 270  TYR   A OH  1 
ATOM   1805 N  N   . ALA   A 1 271 ? 11.511 20.725  13.573  1.00 12.89  ? 271  ALA   A N   1 
ATOM   1806 C  CA  . ALA   A 1 271 ? 11.428 21.806  14.536  1.00 13.16  ? 271  ALA   A CA  1 
ATOM   1807 C  C   . ALA   A 1 271 ? 10.412 21.467  15.595  1.00 12.65  ? 271  ALA   A C   1 
ATOM   1808 O  O   . ALA   A 1 271 ? 9.615  20.542  15.386  1.00 12.63  ? 271  ALA   A O   1 
ATOM   1809 C  CB  . ALA   A 1 271 ? 11.025 23.126  13.820  1.00 14.49  ? 271  ALA   A CB  1 
ATOM   1810 N  N   . VAL   A 1 272 ? 10.359 22.229  16.702  1.00 12.98  ? 272  VAL   A N   1 
ATOM   1811 C  CA  . VAL   A 1 272 ? 9.343  21.987  17.709  1.00 13.92  ? 272  VAL   A CA  1 
ATOM   1812 C  C   . VAL   A 1 272 ? 7.951  22.158  17.044  1.00 13.46  ? 272  VAL   A C   1 
ATOM   1813 O  O   . VAL   A 1 272 ? 7.770  22.923  16.081  1.00 13.07  ? 272  VAL   A O   1 
ATOM   1814 C  CB  . VAL   A 1 272 ? 9.490  22.917  18.924  1.00 14.41  ? 272  VAL   A CB  1 
ATOM   1815 C  CG1 . VAL   A 1 272 ? 10.833 22.636  19.631  1.00 15.81  ? 272  VAL   A CG1 1 
ATOM   1816 C  CG2 . VAL   A 1 272 ? 9.364  24.390  18.532  1.00 14.89  ? 272  VAL   A CG2 1 
ATOM   1817 N  N   . PRO   A 1 273 ? 6.957  21.414  17.512  1.00 13.59  ? 273  PRO   A N   1 
ATOM   1818 C  CA  . PRO   A 1 273 ? 5.625  21.493  16.886  1.00 13.55  ? 273  PRO   A CA  1 
ATOM   1819 C  C   . PRO   A 1 273 ? 5.097  22.903  16.694  1.00 14.12  ? 273  PRO   A C   1 
ATOM   1820 O  O   . PRO   A 1 273 ? 4.566  23.191  15.620  1.00 14.54  ? 273  PRO   A O   1 
ATOM   1821 C  CB  . PRO   A 1 273 ? 4.737  20.641  17.806  1.00 14.77  ? 273  PRO   A CB  1 
ATOM   1822 C  CG  . PRO   A 1 273 ? 5.716  19.602  18.396  1.00 14.86  ? 273  PRO   A CG  1 
ATOM   1823 C  CD  . PRO   A 1 273 ? 7.012  20.409  18.598  1.00 14.05  ? 273  PRO   A CD  1 
ATOM   1824 N  N   . ASP   A 1 274 ? 5.279  23.810  17.683  1.00 14.32  ? 274  ASP   A N   1 
ATOM   1825 C  CA  . ASP   A 1 274 ? 4.739  25.151  17.562  1.00 14.56  ? 274  ASP   A CA  1 
ATOM   1826 C  C   . ASP   A 1 274 ? 5.456  26.004  16.504  1.00 13.79  ? 274  ASP   A C   1 
ATOM   1827 O  O   . ASP   A 1 274 ? 4.964  27.087  16.216  1.00 14.55  ? 274  ASP   A O   1 
ATOM   1828 C  CB  . ASP   A 1 274 ? 4.886  25.907  18.896  1.00 18.14  ? 274  ASP   A CB  1 
ATOM   1829 C  CG  . ASP   A 1 274 ? 3.959  25.479  19.993  1.00 24.65  ? 274  ASP   A CG  1 
ATOM   1830 O  OD1 . ASP   A 1 274 ? 2.978  24.790  19.694  1.00 22.74  ? 274  ASP   A OD1 1 
ATOM   1831 O  OD2 . ASP   A 1 274 ? 4.257  25.796  21.179  1.00 26.29  ? 274  ASP   A OD2 1 
ATOM   1832 N  N   . LYS   A 1 275 ? 6.564  25.518  15.933  1.00 13.65  ? 275  LYS   A N   1 
ATOM   1833 C  CA  . LYS   A 1 275 ? 7.325  26.298  14.937  1.00 13.14  ? 275  LYS   A CA  1 
ATOM   1834 C  C   . LYS   A 1 275 ? 7.493  25.582  13.612  1.00 12.32  ? 275  LYS   A C   1 
ATOM   1835 O  O   . LYS   A 1 275 ? 8.107  26.146  12.721  1.00 12.46  ? 275  LYS   A O   1 
ATOM   1836 C  CB  . LYS   A 1 275 ? 8.715  26.638  15.506  1.00 13.42  ? 275  LYS   A CB  1 
ATOM   1837 C  CG  . LYS   A 1 275 ? 8.587  27.587  16.720  1.00 13.23  ? 275  LYS   A CG  1 
ATOM   1838 C  CD  . LYS   A 1 275 ? 9.967  28.162  17.163  1.00 13.79  ? 275  LYS   A CD  1 
ATOM   1839 C  CE  . LYS   A 1 275 ? 9.814  29.029  18.387  1.00 15.40  ? 275  LYS   A CE  1 
ATOM   1840 N  NZ  . LYS   A 1 275 ? 11.075 29.769  18.681  1.00 18.32  ? 275  LYS   A NZ  1 
ATOM   1841 N  N   . ILE   A 1 276 ? 6.927  24.356  13.427  1.00 12.27  ? 276  ILE   A N   1 
ATOM   1842 C  CA  . ILE   A 1 276 ? 7.126  23.683  12.117  1.00 12.78  ? 276  ILE   A CA  1 
ATOM   1843 C  C   . ILE   A 1 276 ? 6.449  24.483  11.009  1.00 12.96  ? 276  ILE   A C   1 
ATOM   1844 O  O   . ILE   A 1 276 ? 6.868  24.371  9.857   1.00 13.58  ? 276  ILE   A O   1 
ATOM   1845 C  CB  . ILE   A 1 276 ? 6.655  22.216  12.174  1.00 13.04  ? 276  ILE   A CB  1 
ATOM   1846 C  CG1 . ILE   A 1 276 ? 7.179  21.400  11.018  1.00 14.09  ? 276  ILE   A CG1 1 
ATOM   1847 C  CG2 . ILE   A 1 276 ? 5.118  22.117  12.287  1.00 14.41  ? 276  ILE   A CG2 1 
ATOM   1848 C  CD1 . ILE   A 1 276 ? 8.768  21.337  10.925  1.00 14.57  ? 276  ILE   A CD1 1 
ATOM   1849 N  N   . ASN   A 1 277 ? 5.421  25.318  11.335  1.00 12.47  ? 277  ASN   A N   1 
ATOM   1850 C  CA  . ASN   A 1 277 ? 4.830  26.162  10.303  1.00 12.90  ? 277  ASN   A CA  1 
ATOM   1851 C  C   . ASN   A 1 277 ? 5.781  27.230  9.798   1.00 13.90  ? 277  ASN   A C   1 
ATOM   1852 O  O   . ASN   A 1 277 ? 5.439  27.927  8.846   1.00 15.85  ? 277  ASN   A O   1 
ATOM   1853 C  CB  . ASN   A 1 277 ? 3.517  26.785  10.752  1.00 14.55  ? 277  ASN   A CB  1 
ATOM   1854 C  CG  . ASN   A 1 277 ? 3.638  27.735  11.920  1.00 15.59  ? 277  ASN   A CG  1 
ATOM   1855 O  OD1 . ASN   A 1 277 ? 4.736  28.181  12.255  1.00 15.73  ? 277  ASN   A OD1 1 
ATOM   1856 N  ND2 . ASN   A 1 277 ? 2.519  28.075  12.541  1.00 15.44  ? 277  ASN   A ND2 1 
ATOM   1857 N  N   . GLN   A 1 278 ? 6.983  27.352  10.357  1.00 12.17  ? 278  GLN   A N   1 
ATOM   1858 C  CA  . GLN   A 1 278 ? 7.986  28.287  9.860   1.00 12.44  ? 278  GLN   A CA  1 
ATOM   1859 C  C   . GLN   A 1 278 ? 9.082  27.599  9.066   1.00 12.45  ? 278  GLN   A C   1 
ATOM   1860 O  O   . GLN   A 1 278 ? 10.082 28.234  8.721   1.00 13.96  ? 278  GLN   A O   1 
ATOM   1861 C  CB  . GLN   A 1 278 ? 8.653  29.021  11.035  1.00 13.78  ? 278  GLN   A CB  1 
ATOM   1862 C  CG  . GLN   A 1 278 ? 7.660  29.850  11.836  1.00 14.65  ? 278  GLN   A CG  1 
ATOM   1863 C  CD  . GLN   A 1 278 ? 8.364  30.610  12.909  1.00 16.75  ? 278  GLN   A CD  1 
ATOM   1864 O  OE1 . GLN   A 1 278 ? 9.395  31.248  12.620  1.00 19.13  ? 278  GLN   A OE1 1 
ATOM   1865 N  NE2 . GLN   A 1 278 ? 7.872  30.583  14.133  1.00 15.07  ? 278  GLN   A NE2 1 
ATOM   1866 N  N   . ALA   A 1 279 ? 8.881  26.327  8.717   1.00 12.34  ? 279  ALA   A N   1 
ATOM   1867 C  CA  . ALA   A 1 279 ? 9.944  25.559  8.071   1.00 13.29  ? 279  ALA   A CA  1 
ATOM   1868 C  C   . ALA   A 1 279 ? 10.023 25.632  6.556   1.00 14.26  ? 279  ALA   A C   1 
ATOM   1869 O  O   . ALA   A 1 279 ? 11.009 25.155  5.998   1.00 14.25  ? 279  ALA   A O   1 
ATOM   1870 C  CB  . ALA   A 1 279 ? 9.783  24.107  8.458   1.00 14.39  ? 279  ALA   A CB  1 
ATOM   1871 N  N   . ASP   A 1 280 ? 8.970  26.149  5.892   1.00 14.59  ? 280  ASP   A N   1 
ATOM   1872 C  CA  . ASP   A 1 280 ? 8.929  25.988  4.441   1.00 14.58  ? 280  ASP   A CA  1 
ATOM   1873 C  C   . ASP   A 1 280 ? 9.978  26.736  3.673   1.00 14.58  ? 280  ASP   A C   1 
ATOM   1874 O  O   . ASP   A 1 280 ? 10.480 26.174  2.689   1.00 15.13  ? 280  ASP   A O   1 
ATOM   1875 C  CB  . ASP   A 1 280 ? 7.543  26.359  3.885   1.00 16.07  ? 280  ASP   A CB  1 
ATOM   1876 C  CG  . ASP   A 1 280 ? 7.303  25.720  2.528   1.00 18.45  ? 280  ASP   A CG  1 
ATOM   1877 O  OD1 . ASP   A 1 280 ? 7.453  24.469  2.422   1.00 19.96  ? 280  ASP   A OD1 1 
ATOM   1878 O  OD2 . ASP   A 1 280 ? 7.052  26.489  1.550   1.00 23.02  ? 280  ASP   A OD2 1 
ATOM   1879 N  N   . TYR   A 1 281 ? 10.374 27.949  4.081   1.00 14.15  ? 281  TYR   A N   1 
ATOM   1880 C  CA  . TYR   A 1 281 ? 11.394 28.676  3.340   1.00 14.24  ? 281  TYR   A CA  1 
ATOM   1881 C  C   . TYR   A 1 281 ? 12.708 27.894  3.310   1.00 14.43  ? 281  TYR   A C   1 
ATOM   1882 O  O   . TYR   A 1 281 ? 13.289 27.703  2.247   1.00 14.73  ? 281  TYR   A O   1 
ATOM   1883 C  CB  . TYR   A 1 281 ? 11.568 30.076  3.926   1.00 14.44  ? 281  TYR   A CB  1 
ATOM   1884 C  CG  . TYR   A 1 281 ? 12.604 30.847  3.149   1.00 15.66  ? 281  TYR   A CG  1 
ATOM   1885 C  CD1 . TYR   A 1 281 ? 12.276 31.460  1.949   1.00 18.37  ? 281  TYR   A CD1 1 
ATOM   1886 C  CD2 . TYR   A 1 281 ? 13.927 30.880  3.556   1.00 15.29  ? 281  TYR   A CD2 1 
ATOM   1887 C  CE1 . TYR   A 1 281 ? 13.242 32.065  1.164   1.00 18.80  ? 281  TYR   A CE1 1 
ATOM   1888 C  CE2 . TYR   A 1 281 ? 14.903 31.521  2.795   1.00 16.68  ? 281  TYR   A CE2 1 
ATOM   1889 C  CZ  . TYR   A 1 281 ? 14.549 32.100  1.593   1.00 18.49  ? 281  TYR   A CZ  1 
ATOM   1890 O  OH  . TYR   A 1 281 ? 15.471 32.735  0.812   1.00 19.35  ? 281  TYR   A OH  1 
ATOM   1891 N  N   . ALA   A 1 282 ? 13.141 27.417  4.485   1.00 13.04  ? 282  ALA   A N   1 
ATOM   1892 C  CA  . ALA   A 1 282 ? 14.374 26.656  4.548   1.00 13.13  ? 282  ALA   A CA  1 
ATOM   1893 C  C   . ALA   A 1 282 ? 14.280 25.360  3.828   1.00 13.17  ? 282  ALA   A C   1 
ATOM   1894 O  O   . ALA   A 1 282 ? 15.275 24.931  3.227   1.00 13.74  ? 282  ALA   A O   1 
ATOM   1895 C  CB  . ALA   A 1 282 ? 14.730 26.383  6.005   1.00 14.56  ? 282  ALA   A CB  1 
ATOM   1896 N  N   . LEU   A 1 283 ? 13.119 24.696  3.858   1.00 12.77  ? 283  LEU   A N   1 
ATOM   1897 C  CA  . LEU   A 1 283 ? 12.991 23.418  3.151   1.00 13.43  ? 283  LEU   A CA  1 
ATOM   1898 C  C   . LEU   A 1 283 ? 13.173 23.637  1.644   1.00 14.55  ? 283  LEU   A C   1 
ATOM   1899 O  O   . LEU   A 1 283 ? 13.930 22.898  0.987   1.00 14.85  ? 283  LEU   A O   1 
ATOM   1900 C  CB  . LEU   A 1 283 ? 11.598 22.834  3.460   1.00 13.94  ? 283  LEU   A CB  1 
ATOM   1901 C  CG  . LEU   A 1 283 ? 11.287 21.548  2.704   1.00 14.29  ? 283  LEU   A CG  1 
ATOM   1902 C  CD1 . LEU   A 1 283 ? 12.285 20.414  3.053   1.00 16.23  ? 283  LEU   A CD1 1 
ATOM   1903 C  CD2 . LEU   A 1 283 ? 9.837  21.086  2.970   1.00 16.44  ? 283  LEU   A CD2 1 
ATOM   1904 N  N   . ASP   A 1 284 ? 12.509 24.661  1.114   1.00 14.46  ? 284  ASP   A N   1 
ATOM   1905 C  CA  A ASP   A 1 284 ? 12.651 24.930  -0.321  0.50 15.19  ? 284  ASP   A CA  1 
ATOM   1906 C  CA  B ASP   A 1 284 ? 12.607 24.964  -0.303  0.50 15.89  ? 284  ASP   A CA  1 
ATOM   1907 C  C   . ASP   A 1 284 ? 14.053 25.356  -0.662  1.00 14.86  ? 284  ASP   A C   1 
ATOM   1908 O  O   . ASP   A 1 284 ? 14.605 24.895  -1.685  1.00 15.95  ? 284  ASP   A O   1 
ATOM   1909 C  CB  A ASP   A 1 284 ? 11.657 25.973  -0.771  0.50 15.86  ? 284  ASP   A CB  1 
ATOM   1910 C  CB  B ASP   A 1 284 ? 11.613 26.090  -0.590  0.50 18.70  ? 284  ASP   A CB  1 
ATOM   1911 C  CG  A ASP   A 1 284 ? 10.259 25.474  -0.997  0.50 17.56  ? 284  ASP   A CG  1 
ATOM   1912 C  CG  B ASP   A 1 284 ? 11.683 26.621  -1.991  0.50 24.91  ? 284  ASP   A CG  1 
ATOM   1913 O  OD1 A ASP   A 1 284 ? 10.058 24.243  -0.991  0.50 16.40  ? 284  ASP   A OD1 1 
ATOM   1914 O  OD1 B ASP   A 1 284 ? 11.133 25.972  -2.888  0.50 27.22  ? 284  ASP   A OD1 1 
ATOM   1915 O  OD2 A ASP   A 1 284 ? 9.368  26.321  -1.220  0.50 22.24  ? 284  ASP   A OD2 1 
ATOM   1916 O  OD2 B ASP   A 1 284 ? 12.311 27.682  -2.188  0.50 27.47  ? 284  ASP   A OD2 1 
ATOM   1917 N  N   . ALA   A 1 285 ? 14.662 26.183  0.178   1.00 13.89  ? 285  ALA   A N   1 
ATOM   1918 C  CA  . ALA   A 1 285 ? 16.032 26.638  -0.096  1.00 13.84  ? 285  ALA   A CA  1 
ATOM   1919 C  C   . ALA   A 1 285 ? 16.989 25.466  -0.055  1.00 14.50  ? 285  ALA   A C   1 
ATOM   1920 O  O   . ALA   A 1 285 ? 17.909 25.401  -0.902  1.00 14.54  ? 285  ALA   A O   1 
ATOM   1921 C  CB  . ALA   A 1 285 ? 16.445 27.716  0.927   1.00 14.85  ? 285  ALA   A CB  1 
ATOM   1922 N  N   . ALA   A 1 286 ? 16.824 24.563  0.920   1.00 13.81  ? 286  ALA   A N   1 
ATOM   1923 C  CA  . ALA   A 1 286 ? 17.731 23.422  1.033   1.00 13.29  ? 286  ALA   A CA  1 
ATOM   1924 C  C   . ALA   A 1 286 ? 17.649 22.521  -0.187  1.00 14.03  ? 286  ALA   A C   1 
ATOM   1925 O  O   . ALA   A 1 286 ? 18.670 22.019  -0.645  1.00 14.48  ? 286  ALA   A O   1 
ATOM   1926 C  CB  . ALA   A 1 286 ? 17.457 22.606  2.285   1.00 13.86  ? 286  ALA   A CB  1 
ATOM   1927 N  N   . VAL   A 1 287 ? 16.434 22.248  -0.677  1.00 13.83  ? 287  VAL   A N   1 
ATOM   1928 C  CA  . VAL   A 1 287 ? 16.325 21.422  -1.893  1.00 14.86  ? 287  VAL   A CA  1 
ATOM   1929 C  C   . VAL   A 1 287 ? 17.044 22.091  -3.078  1.00 15.24  ? 287  VAL   A C   1 
ATOM   1930 O  O   . VAL   A 1 287 ? 17.833 21.435  -3.773  1.00 16.02  ? 287  VAL   A O   1 
ATOM   1931 C  CB  . VAL   A 1 287 ? 14.835 21.157  -2.188  1.00 15.40  ? 287  VAL   A CB  1 
ATOM   1932 C  CG1 . VAL   A 1 287 ? 14.638 20.609  -3.628  1.00 17.52  ? 287  VAL   A CG1 1 
ATOM   1933 C  CG2 . VAL   A 1 287 ? 14.239 20.201  -1.153  1.00 16.11  ? 287  VAL   A CG2 1 
ATOM   1934 N  N   . THR   A 1 288 ? 16.792 23.378  -3.299  1.00 14.58  ? 288  THR   A N   1 
ATOM   1935 C  CA  . THR   A 1 288 ? 17.432 24.108  -4.401  1.00 14.57  ? 288  THR   A CA  1 
ATOM   1936 C  C   . THR   A 1 288 ? 18.946 24.129  -4.253  1.00 14.75  ? 288  THR   A C   1 
ATOM   1937 O  O   . THR   A 1 288 ? 19.667 23.907  -5.232  1.00 15.19  ? 288  THR   A O   1 
ATOM   1938 C  CB  . THR   A 1 288 ? 16.836 25.523  -4.460  1.00 16.40  ? 288  THR   A CB  1 
ATOM   1939 O  OG1 . THR   A 1 288 ? 15.406 25.425  -4.639  1.00 18.01  ? 288  THR   A OG1 1 
ATOM   1940 C  CG2 . THR   A 1 288 ? 17.453 26.367  -5.577  1.00 18.13  ? 288  THR   A CG2 1 
ATOM   1941 N  N   . LEU   A 1 289 ? 19.448 24.366  -3.033  1.00 14.27  ? 289  LEU   A N   1 
ATOM   1942 C  CA  . LEU   A 1 289 ? 20.888 24.449  -2.824  1.00 14.98  ? 289  LEU   A CA  1 
ATOM   1943 C  C   . LEU   A 1 289 ? 21.544 23.075  -2.919  1.00 14.97  ? 289  LEU   A C   1 
ATOM   1944 O  O   . LEU   A 1 289 ? 22.618 22.957  -3.527  1.00 14.61  ? 289  LEU   A O   1 
ATOM   1945 C  CB  . LEU   A 1 289 ? 21.185 25.155  -1.489  1.00 14.73  ? 289  LEU   A CB  1 
ATOM   1946 C  CG  . LEU   A 1 289 ? 20.972 26.636  -1.607  1.00 14.68  ? 289  LEU   A CG  1 
ATOM   1947 C  CD1 . LEU   A 1 289 ? 20.756 27.242  -0.192  1.00 15.67  ? 289  LEU   A CD1 1 
ATOM   1948 C  CD2 . LEU   A 1 289 ? 22.248 27.249  -2.224  1.00 16.41  ? 289  LEU   A CD2 1 
ATOM   1949 N  N   . LEU   A 1 290 ? 20.893 21.990  -2.406  1.00 14.38  ? 290  LEU   A N   1 
ATOM   1950 C  CA  . LEU   A 1 290 ? 21.503 20.668  -2.542  1.00 14.52  ? 290  LEU   A CA  1 
ATOM   1951 C  C   . LEU   A 1 290 ? 21.599 20.321  -4.049  1.00 16.50  ? 290  LEU   A C   1 
ATOM   1952 O  O   . LEU   A 1 290 ? 22.626 19.832  -4.503  1.00 16.96  ? 290  LEU   A O   1 
ATOM   1953 C  CB  . LEU   A 1 290 ? 20.710 19.595  -1.782  1.00 15.38  ? 290  LEU   A CB  1 
ATOM   1954 C  CG  . LEU   A 1 290 ? 21.534 18.331  -1.522  1.00 17.83  ? 290  LEU   A CG  1 
ATOM   1955 C  CD1 . LEU   A 1 290 ? 22.616 18.593  -0.464  1.00 17.94  ? 290  LEU   A CD1 1 
ATOM   1956 C  CD2 . LEU   A 1 290 ? 20.633 17.206  -1.031  1.00 20.03  ? 290  LEU   A CD2 1 
ATOM   1957 N  N   . GLU   A 1 291 ? 20.562 20.626  -4.824  1.00 16.17  ? 291  GLU   A N   1 
ATOM   1958 C  CA  . GLU   A 1 291 ? 20.582 20.350  -6.265  1.00 16.24  ? 291  GLU   A CA  1 
ATOM   1959 C  C   . GLU   A 1 291 ? 21.654 21.156  -6.940  1.00 16.97  ? 291  GLU   A C   1 
ATOM   1960 O  O   . GLU   A 1 291 ? 22.366 20.640  -7.805  1.00 18.49  ? 291  GLU   A O   1 
ATOM   1961 C  CB  . GLU   A 1 291 ? 19.231 20.670  -6.904  1.00 16.79  ? 291  GLU   A CB  1 
ATOM   1962 C  CG  . GLU   A 1 291 ? 18.139 19.746  -6.420  1.00 18.53  ? 291  GLU   A CG  1 
ATOM   1963 C  CD  . GLU   A 1 291 ? 16.747 20.029  -6.930  1.00 20.41  ? 291  GLU   A CD  1 
ATOM   1964 O  OE1 . GLU   A 1 291 ? 16.554 21.092  -7.563  1.00 27.42  ? 291  GLU   A OE1 1 
ATOM   1965 O  OE2 . GLU   A 1 291 ? 15.850 19.186  -6.713  1.00 18.54  ? 291  GLU   A OE2 1 
ATOM   1966 N  N   . PHE   A 1 292 ? 21.843 22.402  -6.523  1.00 15.73  ? 292  PHE   A N   1 
ATOM   1967 C  CA  . PHE   A 1 292 ? 22.877 23.264  -7.078  1.00 15.78  ? 292  PHE   A CA  1 
ATOM   1968 C  C   . PHE   A 1 292 ? 24.245 22.628  -6.875  1.00 16.14  ? 292  PHE   A C   1 
ATOM   1969 O  O   . PHE   A 1 292 ? 25.031 22.538  -7.822  1.00 16.88  ? 292  PHE   A O   1 
ATOM   1970 C  CB  . PHE   A 1 292 ? 22.857 24.700  -6.476  1.00 15.71  ? 292  PHE   A CB  1 
ATOM   1971 C  CG  . PHE   A 1 292 ? 24.072 25.493  -6.854  1.00 15.55  ? 292  PHE   A CG  1 
ATOM   1972 C  CD1 . PHE   A 1 292 ? 25.228 25.432  -6.086  1.00 16.44  ? 292  PHE   A CD1 1 
ATOM   1973 C  CD2 . PHE   A 1 292 ? 24.107 26.209  -8.039  1.00 17.52  ? 292  PHE   A CD2 1 
ATOM   1974 C  CE1 . PHE   A 1 292 ? 26.398 26.075  -6.504  1.00 17.52  ? 292  PHE   A CE1 1 
ATOM   1975 C  CE2 . PHE   A 1 292 ? 25.263 26.875  -8.427  1.00 17.91  ? 292  PHE   A CE2 1 
ATOM   1976 C  CZ  . PHE   A 1 292 ? 26.398 26.818  -7.649  1.00 18.03  ? 292  PHE   A CZ  1 
ATOM   1977 N  N   . TYR   A 1 293 ? 24.560 22.216  -5.608  1.00 15.22  ? 293  TYR   A N   1 
ATOM   1978 C  CA  . TYR   A 1 293 ? 25.883 21.684  -5.350  1.00 14.65  ? 293  TYR   A CA  1 
ATOM   1979 C  C   . TYR   A 1 293 ? 26.091 20.353  -6.041  1.00 15.09  ? 293  TYR   A C   1 
ATOM   1980 O  O   . TYR   A 1 293 ? 27.194 20.123  -6.548  1.00 16.53  ? 293  TYR   A O   1 
ATOM   1981 C  CB  . TYR   A 1 293 ? 26.037 21.514  -3.832  1.00 14.08  ? 293  TYR   A CB  1 
ATOM   1982 C  CG  . TYR   A 1 293 ? 26.214 22.802  -3.064  1.00 13.46  ? 293  TYR   A CG  1 
ATOM   1983 C  CD1 . TYR   A 1 293 ? 27.185 23.722  -3.428  1.00 13.70  ? 293  TYR   A CD1 1 
ATOM   1984 C  CD2 . TYR   A 1 293 ? 25.395 23.108  -1.986  1.00 13.42  ? 293  TYR   A CD2 1 
ATOM   1985 C  CE1 . TYR   A 1 293 ? 27.374 24.891  -2.708  1.00 13.09  ? 293  TYR   A CE1 1 
ATOM   1986 C  CE2 . TYR   A 1 293 ? 25.580 24.274  -1.245  1.00 13.59  ? 293  TYR   A CE2 1 
ATOM   1987 C  CZ  . TYR   A 1 293 ? 26.581 25.154  -1.601  1.00 13.36  ? 293  TYR   A CZ  1 
ATOM   1988 O  OH  . TYR   A 1 293 ? 26.821 26.300  -0.868  1.00 13.52  ? 293  TYR   A OH  1 
ATOM   1989 N  N   . GLU   A 1 294 ? 25.074 19.481  -6.121  1.00 15.99  ? 294  GLU   A N   1 
ATOM   1990 C  CA  . GLU   A 1 294 ? 25.279 18.199  -6.825  1.00 16.57  ? 294  GLU   A CA  1 
ATOM   1991 C  C   . GLU   A 1 294 ? 25.657 18.449  -8.279  1.00 18.36  ? 294  GLU   A C   1 
ATOM   1992 O  O   . GLU   A 1 294 ? 26.573 17.777  -8.805  1.00 19.75  ? 294  GLU   A O   1 
ATOM   1993 C  CB  . GLU   A 1 294 ? 24.025 17.342  -6.767  1.00 17.54  ? 294  GLU   A CB  1 
ATOM   1994 C  CG  . GLU   A 1 294 ? 23.697 16.867  -5.363  1.00 19.44  ? 294  GLU   A CG  1 
ATOM   1995 C  CD  . GLU   A 1 294 ? 22.584 15.841  -5.370  1.00 21.59  ? 294  GLU   A CD  1 
ATOM   1996 O  OE1 . GLU   A 1 294 ? 21.426 16.216  -5.664  1.00 24.92  ? 294  GLU   A OE1 1 
ATOM   1997 O  OE2 . GLU   A 1 294 ? 22.883 14.650  -5.147  1.00 20.61  ? 294  GLU   A OE2 1 
ATOM   1998 N  N   A ASP   A 1 295 ? 25.001 19.408  -8.913  0.50 18.17  ? 295  ASP   A N   1 
ATOM   1999 N  N   B ASP   A 1 295 ? 25.001 19.441  -8.906  0.50 18.79  ? 295  ASP   A N   1 
ATOM   2000 C  CA  A ASP   A 1 295 ? 25.337 19.707  -10.304 0.50 18.47  ? 295  ASP   A CA  1 
ATOM   2001 C  CA  B ASP   A 1 295 ? 25.234 19.824  -10.311 0.50 19.76  ? 295  ASP   A CA  1 
ATOM   2002 C  C   A ASP   A 1 295 ? 26.704 20.393  -10.367 0.50 19.13  ? 295  ASP   A C   1 
ATOM   2003 C  C   B ASP   A 1 295 ? 26.536 20.577  -10.512 0.50 20.17  ? 295  ASP   A C   1 
ATOM   2004 O  O   A ASP   A 1 295 ? 27.572 20.001  -11.160 0.50 19.80  ? 295  ASP   A O   1 
ATOM   2005 O  O   B ASP   A 1 295 ? 27.136 20.496  -11.594 0.50 21.16  ? 295  ASP   A O   1 
ATOM   2006 C  CB  A ASP   A 1 295 ? 24.253 20.595  -10.937 0.50 19.74  ? 295  ASP   A CB  1 
ATOM   2007 C  CB  B ASP   A 1 295 ? 24.102 20.737  -10.807 0.50 21.87  ? 295  ASP   A CB  1 
ATOM   2008 C  CG  A ASP   A 1 295 ? 24.607 21.081  -12.330 0.50 25.89  ? 295  ASP   A CG  1 
ATOM   2009 C  CG  B ASP   A 1 295 ? 22.759 20.068  -10.946 0.50 29.91  ? 295  ASP   A CG  1 
ATOM   2010 O  OD1 A ASP   A 1 295 ? 24.487 20.285  -13.284 0.50 27.94  ? 295  ASP   A OD1 1 
ATOM   2011 O  OD1 B ASP   A 1 295 ? 22.718 18.822  -10.970 0.50 32.67  ? 295  ASP   A OD1 1 
ATOM   2012 O  OD2 A ASP   A 1 295 ? 25.040 22.242  -12.454 0.50 28.24  ? 295  ASP   A OD2 1 
ATOM   2013 O  OD2 B ASP   A 1 295 ? 21.735 20.791  -10.977 0.50 33.39  ? 295  ASP   A OD2 1 
ATOM   2014 N  N   . TYR   A 1 296 ? 26.915 21.416  -9.543  1.00 19.24  ? 296  TYR   A N   1 
ATOM   2015 C  CA  . TYR   A 1 296 ? 28.135 22.218  -9.607  1.00 18.95  ? 296  TYR   A CA  1 
ATOM   2016 C  C   . TYR   A 1 296 ? 29.388 21.390  -9.415  1.00 20.98  ? 296  TYR   A C   1 
ATOM   2017 O  O   . TYR   A 1 296 ? 30.353 21.522  -10.183 1.00 22.27  ? 296  TYR   A O   1 
ATOM   2018 C  CB  . TYR   A 1 296 ? 28.058 23.337  -8.565  1.00 18.65  ? 296  TYR   A CB  1 
ATOM   2019 C  CG  . TYR   A 1 296 ? 29.089 24.403  -8.789  1.00 18.98  ? 296  TYR   A CG  1 
ATOM   2020 C  CD1 . TYR   A 1 296 ? 28.901 25.380  -9.753  1.00 19.30  ? 296  TYR   A CD1 1 
ATOM   2021 C  CD2 . TYR   A 1 296 ? 30.274 24.414  -8.067  1.00 19.89  ? 296  TYR   A CD2 1 
ATOM   2022 C  CE1 . TYR   A 1 296 ? 29.843 26.381  -9.955  1.00 19.81  ? 296  TYR   A CE1 1 
ATOM   2023 C  CE2 . TYR   A 1 296 ? 31.254 25.373  -8.301  1.00 20.76  ? 296  TYR   A CE2 1 
ATOM   2024 C  CZ  . TYR   A 1 296 ? 31.038 26.354  -9.247  1.00 20.37  ? 296  TYR   A CZ  1 
ATOM   2025 O  OH  . TYR   A 1 296 ? 31.994 27.333  -9.468  1.00 22.31  ? 296  TYR   A OH  1 
ATOM   2026 N  N   . PHE   A 1 297 ? 29.384 20.523  -8.405  1.00 19.23  ? 297  PHE   A N   1 
ATOM   2027 C  CA  . PHE   A 1 297 ? 30.557 19.711  -8.116  1.00 19.52  ? 297  PHE   A CA  1 
ATOM   2028 C  C   . PHE   A 1 297 ? 30.662 18.448  -8.950  1.00 20.96  ? 297  PHE   A C   1 
ATOM   2029 O  O   . PHE   A 1 297 ? 31.690 17.768  -8.825  1.00 23.13  ? 297  PHE   A O   1 
ATOM   2030 C  CB  . PHE   A 1 297 ? 30.559 19.310  -6.626  1.00 18.54  ? 297  PHE   A CB  1 
ATOM   2031 C  CG  . PHE   A 1 297 ? 30.584 20.478  -5.660  1.00 18.66  ? 297  PHE   A CG  1 
ATOM   2032 C  CD1 . PHE   A 1 297 ? 31.439 21.553  -5.859  1.00 19.63  ? 297  PHE   A CD1 1 
ATOM   2033 C  CD2 . PHE   A 1 297 ? 29.796 20.472  -4.522  1.00 18.69  ? 297  PHE   A CD2 1 
ATOM   2034 C  CE1 . PHE   A 1 297 ? 31.510 22.580  -4.930  1.00 19.24  ? 297  PHE   A CE1 1 
ATOM   2035 C  CE2 . PHE   A 1 297 ? 29.878 21.496  -3.592  1.00 18.27  ? 297  PHE   A CE2 1 
ATOM   2036 C  CZ  . PHE   A 1 297 ? 30.699 22.574  -3.827  1.00 18.00  ? 297  PHE   A CZ  1 
ATOM   2037 N  N   . SER   A 1 298 ? 29.576 18.062  -9.657  1.00 20.09  ? 298  SER   A N   1 
ATOM   2038 C  CA  . SER   A 1 298 ? 29.522 16.806  -10.399 1.00 21.12  ? 298  SER   A CA  1 
ATOM   2039 C  C   . SER   A 1 298 ? 29.734 15.598  -9.478  1.00 21.31  ? 298  SER   A C   1 
ATOM   2040 O  O   . SER   A 1 298 ? 30.293 14.570  -9.893  1.00 22.88  ? 298  SER   A O   1 
ATOM   2041 C  CB  . SER   A 1 298 ? 30.563 16.778  -11.521 1.00 23.50  ? 298  SER   A CB  1 
ATOM   2042 O  OG  . SER   A 1 298 ? 30.194 17.738  -12.492 1.00 29.21  ? 298  SER   A OG  1 
ATOM   2043 N  N   . ILE   A 1 299 ? 29.334 15.725  -8.211  1.00 18.66  ? 299  ILE   A N   1 
ATOM   2044 C  CA  . ILE   A 1 299 ? 29.485 14.644  -7.231  1.00 18.57  ? 299  ILE   A CA  1 
ATOM   2045 C  C   . ILE   A 1 299 ? 28.196 14.584  -6.488  1.00 18.62  ? 299  ILE   A C   1 
ATOM   2046 O  O   . ILE   A 1 299 ? 27.879 15.501  -5.731  1.00 18.15  ? 299  ILE   A O   1 
ATOM   2047 C  CB  . ILE   A 1 299 ? 30.643 14.915  -6.232  1.00 20.13  ? 299  ILE   A CB  1 
ATOM   2048 C  CG1 . ILE   A 1 299 ? 32.003 14.992  -6.970  1.00 22.17  ? 299  ILE   A CG1 1 
ATOM   2049 C  CG2 . ILE   A 1 299 ? 30.653 13.833  -5.143  1.00 20.64  ? 299  ILE   A CG2 1 
ATOM   2050 C  CD1 . ILE   A 1 299 ? 33.122 15.443  -6.049  1.00 25.02  ? 299  ILE   A CD1 1 
ATOM   2051 N  N   . PRO   A 1 300 ? 27.417 13.526  -6.661  1.00 18.38  ? 300  PRO   A N   1 
ATOM   2052 C  CA  . PRO   A 1 300 ? 26.122 13.461  -5.979  1.00 18.29  ? 300  PRO   A CA  1 
ATOM   2053 C  C   . PRO   A 1 300 ? 26.244 13.481  -4.472  1.00 17.48  ? 300  PRO   A C   1 
ATOM   2054 O  O   . PRO   A 1 300 ? 27.239 13.018  -3.906  1.00 17.85  ? 300  PRO   A O   1 
ATOM   2055 C  CB  . PRO   A 1 300 ? 25.557 12.122  -6.434  1.00 20.14  ? 300  PRO   A CB  1 
ATOM   2056 C  CG  . PRO   A 1 300 ? 26.198 11.917  -7.827  1.00 21.69  ? 300  PRO   A CG  1 
ATOM   2057 C  CD  . PRO   A 1 300 ? 27.611 12.401  -7.611  1.00 18.59  ? 300  PRO   A CD  1 
ATOM   2058 N  N   . TYR   A 1 301 ? 25.220 13.996  -3.805  1.00 16.71  ? 301  TYR   A N   1 
ATOM   2059 C  CA  . TYR   A 1 301 ? 25.148 13.853  -2.341  1.00 16.54  ? 301  TYR   A CA  1 
ATOM   2060 C  C   . TYR   A 1 301 ? 24.924 12.342  -2.072  1.00 18.23  ? 301  TYR   A C   1 
ATOM   2061 O  O   . TYR   A 1 301 ? 24.095 11.726  -2.743  1.00 18.72  ? 301  TYR   A O   1 
ATOM   2062 C  CB  . TYR   A 1 301 ? 23.965 14.666  -1.845  1.00 15.33  ? 301  TYR   A CB  1 
ATOM   2063 C  CG  . TYR   A 1 301 ? 23.672 14.488  -0.366  1.00 14.71  ? 301  TYR   A CG  1 
ATOM   2064 C  CD1 . TYR   A 1 301 ? 24.425 15.147  0.600   1.00 15.36  ? 301  TYR   A CD1 1 
ATOM   2065 C  CD2 . TYR   A 1 301 ? 22.591 13.731  0.058   1.00 15.54  ? 301  TYR   A CD2 1 
ATOM   2066 C  CE1 . TYR   A 1 301 ? 24.117 15.035  1.952   1.00 15.28  ? 301  TYR   A CE1 1 
ATOM   2067 C  CE2 . TYR   A 1 301 ? 22.287 13.602  1.406   1.00 15.42  ? 301  TYR   A CE2 1 
ATOM   2068 C  CZ  . TYR   A 1 301 ? 23.027 14.291  2.344   1.00 15.76  ? 301  TYR   A CZ  1 
ATOM   2069 O  OH  . TYR   A 1 301 ? 22.712 14.153  3.671   1.00 15.84  ? 301  TYR   A OH  1 
ATOM   2070 N  N   . PRO   A 1 302 ? 25.713 11.724  -1.171  1.00 17.50  ? 302  PRO   A N   1 
ATOM   2071 C  CA  . PRO   A 1 302 ? 25.764 10.258  -1.158  1.00 17.08  ? 302  PRO   A CA  1 
ATOM   2072 C  C   . PRO   A 1 302 ? 24.789 9.547   -0.228  1.00 18.44  ? 302  PRO   A C   1 
ATOM   2073 O  O   . PRO   A 1 302 ? 24.799 8.306   -0.169  1.00 19.87  ? 302  PRO   A O   1 
ATOM   2074 C  CB  . PRO   A 1 302 ? 27.221 9.994   -0.747  1.00 18.96  ? 302  PRO   A CB  1 
ATOM   2075 C  CG  . PRO   A 1 302 ? 27.499 11.121  0.258   1.00 19.11  ? 302  PRO   A CG  1 
ATOM   2076 C  CD  . PRO   A 1 302 ? 26.861 12.311  -0.442  1.00 17.80  ? 302  PRO   A CD  1 
ATOM   2077 N  N   . LEU   A 1 303 ? 24.033 10.309  0.589   1.00 16.20  ? 303  LEU   A N   1 
ATOM   2078 C  CA  . LEU   A 1 303 ? 23.124 9.690   1.563   1.00 16.18  ? 303  LEU   A CA  1 
ATOM   2079 C  C   . LEU   A 1 303 ? 21.696 9.786   1.071   1.00 15.88  ? 303  LEU   A C   1 
ATOM   2080 O  O   . LEU   A 1 303 ? 21.371 10.655  0.219   1.00 17.25  ? 303  LEU   A O   1 
ATOM   2081 C  CB  . LEU   A 1 303 ? 23.269 10.417  2.943   1.00 16.07  ? 303  LEU   A CB  1 
ATOM   2082 C  CG  . LEU   A 1 303 ? 24.680 10.700  3.443   1.00 16.73  ? 303  LEU   A CG  1 
ATOM   2083 C  CD1 . LEU   A 1 303 ? 24.625 11.305  4.843   1.00 17.48  ? 303  LEU   A CD1 1 
ATOM   2084 C  CD2 . LEU   A 1 303 ? 25.558 9.443   3.439   1.00 17.96  ? 303  LEU   A CD2 1 
ATOM   2085 N  N   . PRO   A 1 304 ? 20.801 8.935   1.577   1.00 16.24  ? 304  PRO   A N   1 
ATOM   2086 C  CA  . PRO   A 1 304 ? 19.420 8.977   1.071   1.00 16.98  ? 304  PRO   A CA  1 
ATOM   2087 C  C   . PRO   A 1 304 ? 18.609 10.167  1.512   1.00 16.64  ? 304  PRO   A C   1 
ATOM   2088 O  O   . PRO   A 1 304 ? 17.538 10.442  0.947   1.00 17.21  ? 304  PRO   A O   1 
ATOM   2089 C  CB  . PRO   A 1 304 ? 18.788 7.687   1.601   1.00 18.55  ? 304  PRO   A CB  1 
ATOM   2090 C  CG  . PRO   A 1 304 ? 19.945 6.835   2.116   1.00 19.58  ? 304  PRO   A CG  1 
ATOM   2091 C  CD  . PRO   A 1 304 ? 21.037 7.799   2.491   1.00 17.05  ? 304  PRO   A CD  1 
ATOM   2092 N  N   . LYS   A 1 305 ? 19.045 10.822  2.598   1.00 15.32  ? 305  LYS   A N   1 
ATOM   2093 C  CA  . LYS   A 1 305 ? 18.259 11.908  3.159   1.00 14.83  ? 305  LYS   A CA  1 
ATOM   2094 C  C   . LYS   A 1 305 ? 19.166 12.952  3.765   1.00 14.94  ? 305  LYS   A C   1 
ATOM   2095 O  O   . LYS   A 1 305 ? 20.341 12.701  4.013   1.00 14.94  ? 305  LYS   A O   1 
ATOM   2096 C  CB  . LYS   A 1 305 ? 17.220 11.392  4.169   1.00 14.66  ? 305  LYS   A CB  1 
ATOM   2097 C  CG  . LYS   A 1 305 ? 17.790 10.745  5.454   1.00 15.65  ? 305  LYS   A CG  1 
ATOM   2098 C  CD  . LYS   A 1 305 ? 18.110 11.784  6.601   1.00 14.34  ? 305  LYS   A CD  1 
ATOM   2099 C  CE  . LYS   A 1 305 ? 18.514 11.044  7.870   1.00 14.82  ? 305  LYS   A CE  1 
ATOM   2100 N  NZ  . LYS   A 1 305 ? 18.922 12.054  8.943   1.00 13.95  ? 305  LYS   A NZ  1 
ATOM   2101 N  N   . GLN   A 1 306 ? 18.617 14.158  3.911   1.00 14.40  ? 306  GLN   A N   1 
ATOM   2102 C  CA  . GLN   A 1 306 ? 19.340 15.271  4.532   1.00 14.05  ? 306  GLN   A CA  1 
ATOM   2103 C  C   . GLN   A 1 306 ? 18.339 15.971  5.426   1.00 14.26  ? 306  GLN   A C   1 
ATOM   2104 O  O   . GLN   A 1 306 ? 17.284 16.401  4.934   1.00 14.69  ? 306  GLN   A O   1 
ATOM   2105 C  CB  . GLN   A 1 306 ? 19.865 16.273  3.457   1.00 14.50  ? 306  GLN   A CB  1 
ATOM   2106 C  CG  . GLN   A 1 306 ? 20.564 17.508  4.139   1.00 15.03  ? 306  GLN   A CG  1 
ATOM   2107 C  CD  . GLN   A 1 306 ? 21.888 17.081  4.821   1.00 15.10  ? 306  GLN   A CD  1 
ATOM   2108 O  OE1 . GLN   A 1 306 ? 21.897 16.530  5.932   1.00 17.90  ? 306  GLN   A OE1 1 
ATOM   2109 N  NE2 . GLN   A 1 306 ? 23.003 17.352  4.183   1.00 17.39  ? 306  GLN   A NE2 1 
ATOM   2110 N  N   . ASP   A 1 307 ? 18.627 16.040  6.731   1.00 13.50  ? 307  ASP   A N   1 
ATOM   2111 C  CA  . ASP   A 1 307 ? 17.737 16.721  7.640   1.00 12.58  ? 307  ASP   A CA  1 
ATOM   2112 C  C   . ASP   A 1 307 ? 18.347 18.051  8.075   1.00 13.54  ? 307  ASP   A C   1 
ATOM   2113 O  O   . ASP   A 1 307 ? 19.570 18.227  8.110   1.00 14.50  ? 307  ASP   A O   1 
ATOM   2114 C  CB  . ASP   A 1 307 ? 17.505 15.855  8.896   1.00 12.76  ? 307  ASP   A CB  1 
ATOM   2115 C  CG  . ASP   A 1 307 ? 16.662 14.655  8.596   1.00 14.75  ? 307  ASP   A CG  1 
ATOM   2116 O  OD1 . ASP   A 1 307 ? 15.938 14.683  7.577   1.00 15.28  ? 307  ASP   A OD1 1 
ATOM   2117 O  OD2 . ASP   A 1 307 ? 16.770 13.637  9.366   1.00 15.39  ? 307  ASP   A OD2 1 
ATOM   2118 N  N   . LEU   A 1 308 ? 17.463 18.998  8.345   1.00 13.09  ? 308  LEU   A N   1 
ATOM   2119 C  CA  . LEU   A 1 308 ? 17.850 20.325  8.880   1.00 12.55  ? 308  LEU   A CA  1 
ATOM   2120 C  C   . LEU   A 1 308 ? 17.017 20.499  10.129  1.00 12.98  ? 308  LEU   A C   1 
ATOM   2121 O  O   . LEU   A 1 308 ? 15.775 20.614  10.033  1.00 13.58  ? 308  LEU   A O   1 
ATOM   2122 C  CB  . LEU   A 1 308 ? 17.515 21.433  7.871   1.00 12.38  ? 308  LEU   A CB  1 
ATOM   2123 C  CG  . LEU   A 1 308 ? 18.326 21.424  6.565   1.00 12.94  ? 308  LEU   A CG  1 
ATOM   2124 C  CD1 . LEU   A 1 308 ? 17.708 20.510  5.509   1.00 13.24  ? 308  LEU   A CD1 1 
ATOM   2125 C  CD2 . LEU   A 1 308 ? 18.440 22.847  5.985   1.00 13.98  ? 308  LEU   A CD2 1 
ATOM   2126 N  N   . ALA   A 1 309 ? 17.645 20.439  11.306  1.00 11.86  ? 309  ALA   A N   1 
ATOM   2127 C  CA  . ALA   A 1 309 ? 16.913 20.490  12.560  1.00 11.79  ? 309  ALA   A CA  1 
ATOM   2128 C  C   . ALA   A 1 309 ? 17.175 21.779  13.325  1.00 11.71  ? 309  ALA   A C   1 
ATOM   2129 O  O   . ALA   A 1 309 ? 18.330 22.125  13.584  1.00 12.15  ? 309  ALA   A O   1 
ATOM   2130 C  CB  . ALA   A 1 309 ? 17.298 19.288  13.443  1.00 13.80  ? 309  ALA   A CB  1 
ATOM   2131 N  N   . ALA   A 1 310 ? 16.096 22.456  13.740  1.00 11.24  ? 310  ALA   A N   1 
ATOM   2132 C  CA  . ALA   A 1 310 ? 16.177 23.706  14.469  1.00 12.02  ? 310  ALA   A CA  1 
ATOM   2133 C  C   . ALA   A 1 310 ? 16.150 23.370  15.969  1.00 12.56  ? 310  ALA   A C   1 
ATOM   2134 O  O   . ALA   A 1 310 ? 15.150 22.867  16.478  1.00 12.80  ? 310  ALA   A O   1 
ATOM   2135 C  CB  . ALA   A 1 310 ? 14.969 24.567  14.106  1.00 12.25  ? 310  ALA   A CB  1 
ATOM   2136 N  N   . ILE   A 1 311 ? 17.250 23.644  16.651  1.00 11.69  ? 311  ILE   A N   1 
ATOM   2137 C  CA  . ILE   A 1 311 ? 17.393 23.257  18.059  1.00 11.89  ? 311  ILE   A CA  1 
ATOM   2138 C  C   . ILE   A 1 311 ? 17.079 24.419  18.962  1.00 12.85  ? 311  ILE   A C   1 
ATOM   2139 O  O   . ILE   A 1 311 ? 17.582 25.499  18.713  1.00 13.56  ? 311  ILE   A O   1 
ATOM   2140 C  CB  . ILE   A 1 311 ? 18.818 22.741  18.329  1.00 12.47  ? 311  ILE   A CB  1 
ATOM   2141 C  CG1 . ILE   A 1 311 ? 19.350 21.826  17.198  1.00 12.23  ? 311  ILE   A CG1 1 
ATOM   2142 C  CG2 . ILE   A 1 311 ? 18.868 22.009  19.686  1.00 13.17  ? 311  ILE   A CG2 1 
ATOM   2143 C  CD1 . ILE   A 1 311 ? 18.482 20.540  16.967  1.00 13.94  ? 311  ILE   A CD1 1 
ATOM   2144 N  N   . PRO   A 1 312 ? 16.258 24.250  20.003  1.00 12.59  ? 312  PRO   A N   1 
ATOM   2145 C  CA  . PRO   A 1 312 ? 15.902 25.412  20.838  1.00 12.65  ? 312  PRO   A CA  1 
ATOM   2146 C  C   . PRO   A 1 312 ? 17.090 26.072  21.525  1.00 13.31  ? 312  PRO   A C   1 
ATOM   2147 O  O   . PRO   A 1 312 ? 17.010 27.257  21.860  1.00 13.86  ? 312  PRO   A O   1 
ATOM   2148 C  CB  . PRO   A 1 312 ? 14.895 24.843  21.833  1.00 12.97  ? 312  PRO   A CB  1 
ATOM   2149 C  CG  . PRO   A 1 312 ? 14.244 23.713  21.027  1.00 13.92  ? 312  PRO   A CG  1 
ATOM   2150 C  CD  . PRO   A 1 312 ? 15.405 23.083  20.292  1.00 12.91  ? 312  PRO   A CD  1 
ATOM   2151 N  N   . ASP   A 1 313 ? 18.164 25.321  21.779  1.00 12.87  ? 313  ASP   A N   1 
ATOM   2152 C  CA  . ASP   A 1 313 ? 19.393 25.873  22.417  1.00 12.25  ? 313  ASP   A CA  1 
ATOM   2153 C  C   . ASP   A 1 313 ? 20.554 25.462  21.545  1.00 12.36  ? 313  ASP   A C   1 
ATOM   2154 O  O   . ASP   A 1 313 ? 20.767 24.262  21.320  1.00 12.78  ? 313  ASP   A O   1 
ATOM   2155 C  CB  . ASP   A 1 313 ? 19.623 25.292  23.823  1.00 13.42  ? 313  ASP   A CB  1 
ATOM   2156 C  CG  . ASP   A 1 313 ? 18.458 25.607  24.726  1.00 15.07  ? 313  ASP   A CG  1 
ATOM   2157 O  OD1 . ASP   A 1 313 ? 18.317 26.774  25.152  1.00 15.03  ? 313  ASP   A OD1 1 
ATOM   2158 O  OD2 . ASP   A 1 313 ? 17.649 24.707  24.982  1.00 16.23  ? 313  ASP   A OD2 1 
ATOM   2159 N  N   . PHE   A 1 314 ? 21.296 26.454  21.018  1.00 11.89  ? 314  PHE   A N   1 
ATOM   2160 C  CA  . PHE   A 1 314 ? 22.382 26.133  20.135  1.00 11.53  ? 314  PHE   A CA  1 
ATOM   2161 C  C   . PHE   A 1 314 ? 23.418 27.248  20.222  1.00 12.43  ? 314  PHE   A C   1 
ATOM   2162 O  O   . PHE   A 1 314 ? 23.068 28.431  20.218  1.00 13.48  ? 314  PHE   A O   1 
ATOM   2163 C  CB  . PHE   A 1 314 ? 21.815 25.927  18.707  1.00 11.54  ? 314  PHE   A CB  1 
ATOM   2164 C  CG  . PHE   A 1 314 ? 22.711 25.151  17.804  1.00 11.55  ? 314  PHE   A CG  1 
ATOM   2165 C  CD1 . PHE   A 1 314 ? 22.641 23.781  17.750  1.00 12.48  ? 314  PHE   A CD1 1 
ATOM   2166 C  CD2 . PHE   A 1 314 ? 23.643 25.791  16.999  1.00 11.30  ? 314  PHE   A CD2 1 
ATOM   2167 C  CE1 . PHE   A 1 314 ? 23.512 23.063  16.957  1.00 12.92  ? 314  PHE   A CE1 1 
ATOM   2168 C  CE2 . PHE   A 1 314 ? 24.475 25.065  16.161  1.00 12.56  ? 314  PHE   A CE2 1 
ATOM   2169 C  CZ  . PHE   A 1 314 ? 24.416 23.700  16.148  1.00 13.01  ? 314  PHE   A CZ  1 
ATOM   2170 N  N   . GLN   A 1 315 ? 24.698 26.883  20.332  1.00 12.26  ? 315  GLN   A N   1 
ATOM   2171 C  CA  . GLN   A 1 315 ? 25.741 27.895  20.566  1.00 11.72  ? 315  GLN   A CA  1 
ATOM   2172 C  C   . GLN   A 1 315 ? 26.149 28.690  19.330  1.00 12.62  ? 315  GLN   A C   1 
ATOM   2173 O  O   . GLN   A 1 315 ? 26.142 29.923  19.381  1.00 13.02  ? 315  GLN   A O   1 
ATOM   2174 C  CB  . GLN   A 1 315 ? 26.968 27.250  21.219  1.00 12.53  ? 315  GLN   A CB  1 
ATOM   2175 C  CG  . GLN   A 1 315 ? 28.102 28.254  21.492  1.00 12.13  ? 315  GLN   A CG  1 
ATOM   2176 C  CD  . GLN   A 1 315 ? 29.116 27.661  22.445  1.00 15.57  ? 315  GLN   A CD  1 
ATOM   2177 O  OE1 . GLN   A 1 315 ? 28.806 26.768  23.260  1.00 16.13  ? 315  GLN   A OE1 1 
ATOM   2178 N  NE2 . GLN   A 1 315 ? 30.317 28.212  22.456  1.00 14.21  ? 315  GLN   A NE2 1 
ATOM   2179 N  N   . SER   A 1 316 ? 26.637 27.989  18.326  1.00 12.50  ? 316  SER   A N   1 
ATOM   2180 C  CA  . SER   A 1 316 ? 27.016 28.657  17.102  1.00 12.48  ? 316  SER   A CA  1 
ATOM   2181 C  C   . SER   A 1 316 ? 25.749 28.929  16.254  1.00 12.90  ? 316  SER   A C   1 
ATOM   2182 O  O   . SER   A 1 316 ? 24.637 28.905  16.772  1.00 12.69  ? 316  SER   A O   1 
ATOM   2183 C  CB  . SER   A 1 316 ? 28.039 27.803  16.359  1.00 14.27  ? 316  SER   A CB  1 
ATOM   2184 O  OG  . SER   A 1 316 ? 27.463 26.533  16.084  1.00 17.62  ? 316  SER   A OG  1 
ATOM   2185 N  N   . GLY   A 1 317 ? 25.927 29.206  14.965  1.00 13.20  ? 317  GLY   A N   1 
ATOM   2186 C  CA  . GLY   A 1 317 ? 24.771 29.428  14.107  1.00 12.70  ? 317  GLY   A CA  1 
ATOM   2187 C  C   . GLY   A 1 317 ? 24.147 28.097  13.650  1.00 12.61  ? 317  GLY   A C   1 
ATOM   2188 O  O   . GLY   A 1 317 ? 22.934 27.934  13.586  1.00 11.94  ? 317  GLY   A O   1 
ATOM   2189 N  N   . ALA   A 1 318 ? 25.007 27.136  13.321  1.00 12.05  ? 318  ALA   A N   1 
ATOM   2190 C  CA  . ALA   A 1 318 ? 24.565 25.867  12.720  1.00 12.67  ? 318  ALA   A CA  1 
ATOM   2191 C  C   . ALA   A 1 318 ? 25.737 24.899  12.678  1.00 11.66  ? 318  ALA   A C   1 
ATOM   2192 O  O   . ALA   A 1 318 ? 26.878 25.290  12.997  1.00 12.58  ? 318  ALA   A O   1 
ATOM   2193 C  CB  . ALA   A 1 318 ? 24.019 26.134  11.276  1.00 12.77  ? 318  ALA   A CB  1 
ATOM   2194 N  N   . MET   A 1 319 ? 25.478 23.632  12.293  1.00 11.45  ? 319  MET   A N   1 
ATOM   2195 C  CA  . MET   A 1 319 ? 26.554 22.633  12.227  1.00 11.47  ? 319  MET   A CA  1 
ATOM   2196 C  C   . MET   A 1 319 ? 26.195 21.632  11.124  1.00 12.13  ? 319  MET   A C   1 
ATOM   2197 O  O   . MET   A 1 319 ? 25.016 21.284  10.952  1.00 13.48  ? 319  MET   A O   1 
ATOM   2198 C  CB  . MET   A 1 319 ? 26.670 21.923  13.591  1.00 12.14  ? 319  MET   A CB  1 
ATOM   2199 C  CG  . MET   A 1 319 ? 27.644 20.766  13.571  1.00 12.89  ? 319  MET   A CG  1 
ATOM   2200 S  SD  . MET   A 1 319 ? 29.327 21.316  13.192  1.00 12.74  ? 319  MET   A SD  1 
ATOM   2201 C  CE  . MET   A 1 319 ? 29.967 19.759  12.470  1.00 13.46  ? 319  MET   A CE  1 
ATOM   2202 N  N   . GLU   A 1 320 ? 27.208 21.159  10.417  1.00 11.45  ? 320  GLU   A N   1 
ATOM   2203 C  CA  . GLU   A 1 320 ? 27.000 20.407  9.198   1.00 11.10  ? 320  GLU   A CA  1 
ATOM   2204 C  C   . GLU   A 1 320 ? 26.981 18.902  9.315   1.00 12.65  ? 320  GLU   A C   1 
ATOM   2205 O  O   . GLU   A 1 320 ? 27.275 18.224  8.318   1.00 13.30  ? 320  GLU   A O   1 
ATOM   2206 C  CB  . GLU   A 1 320 ? 28.123 20.794  8.230   1.00 11.95  ? 320  GLU   A CB  1 
ATOM   2207 C  CG  . GLU   A 1 320 ? 29.517 20.334  8.691   1.00 12.76  ? 320  GLU   A CG  1 
ATOM   2208 C  CD  . GLU   A 1 320 ? 30.398 21.394  9.302   1.00 12.67  ? 320  GLU   A CD  1 
ATOM   2209 O  OE1 . GLU   A 1 320 ? 29.868 22.355  9.932   1.00 11.84  ? 320  GLU   A OE1 1 
ATOM   2210 O  OE2 . GLU   A 1 320 ? 31.636 21.269  9.159   1.00 13.11  ? 320  GLU   A OE2 1 
ATOM   2211 N  N   . ASN   A 1 321 ? 26.582 18.349  10.468  1.00 12.42  ? 321  ASN   A N   1 
ATOM   2212 C  CA  . ASN   A 1 321 ? 26.606 16.880  10.638  1.00 13.05  ? 321  ASN   A CA  1 
ATOM   2213 C  C   . ASN   A 1 321 ? 25.996 16.161  9.451   1.00 13.56  ? 321  ASN   A C   1 
ATOM   2214 O  O   . ASN   A 1 321 ? 24.933 16.552  8.982   1.00 13.72  ? 321  ASN   A O   1 
ATOM   2215 C  CB  . ASN   A 1 321 ? 25.891 16.460  11.911  1.00 12.32  ? 321  ASN   A CB  1 
ATOM   2216 C  CG  . ASN   A 1 321 ? 26.111 17.380  13.080  1.00 12.90  ? 321  ASN   A CG  1 
ATOM   2217 O  OD1 . ASN   A 1 321 ? 27.185 17.379  13.699  1.00 13.12  ? 321  ASN   A OD1 1 
ATOM   2218 N  ND2 . ASN   A 1 321 ? 25.118 18.207  13.359  1.00 12.56  ? 321  ASN   A ND2 1 
ATOM   2219 N  N   . TRP   A 1 322 ? 26.736 15.191  8.912   1.00 12.66  ? 322  TRP   A N   1 
ATOM   2220 C  CA  . TRP   A 1 322 ? 26.379 14.606  7.615   1.00 13.22  ? 322  TRP   A CA  1 
ATOM   2221 C  C   . TRP   A 1 322 ? 25.028 13.918  7.669   1.00 13.66  ? 322  TRP   A C   1 
ATOM   2222 O  O   . TRP   A 1 322 ? 24.900 12.924  8.385   1.00 14.15  ? 322  TRP   A O   1 
ATOM   2223 C  CB  . TRP   A 1 322 ? 27.483 13.622  7.207   1.00 13.69  ? 322  TRP   A CB  1 
ATOM   2224 C  CG  . TRP   A 1 322 ? 27.770 13.512  5.739   1.00 13.58  ? 322  TRP   A CG  1 
ATOM   2225 C  CD1 . TRP   A 1 322 ? 27.026 13.964  4.674   1.00 14.54  ? 322  TRP   A CD1 1 
ATOM   2226 C  CD2 . TRP   A 1 322 ? 28.938 12.899  5.196   1.00 14.12  ? 322  TRP   A CD2 1 
ATOM   2227 N  NE1 . TRP   A 1 322 ? 27.710 13.693  3.486   1.00 14.72  ? 322  TRP   A NE1 1 
ATOM   2228 C  CE2 . TRP   A 1 322 ? 28.905 13.084  3.790   1.00 14.25  ? 322  TRP   A CE2 1 
ATOM   2229 C  CE3 . TRP   A 1 322 ? 30.063 12.342  5.772   1.00 14.50  ? 322  TRP   A CE3 1 
ATOM   2230 C  CZ2 . TRP   A 1 322 ? 29.914 12.592  2.945   1.00 14.93  ? 322  TRP   A CZ2 1 
ATOM   2231 C  CZ3 . TRP   A 1 322 ? 31.082 11.887  4.939   1.00 14.96  ? 322  TRP   A CZ3 1 
ATOM   2232 C  CH2 . TRP   A 1 322 ? 31.006 12.035  3.543   1.00 14.95  ? 322  TRP   A CH2 1 
ATOM   2233 N  N   . GLY   A 1 323 ? 24.034 14.432  6.948   1.00 13.26  ? 323  GLY   A N   1 
ATOM   2234 C  CA  . GLY   A 1 323 ? 22.702 13.850  7.002   1.00 12.81  ? 323  GLY   A CA  1 
ATOM   2235 C  C   . GLY   A 1 323 ? 21.797 14.434  8.075   1.00 13.66  ? 323  GLY   A C   1 
ATOM   2236 O  O   . GLY   A 1 323 ? 20.575 14.207  8.069   1.00 13.45  ? 323  GLY   A O   1 
ATOM   2237 N  N   . LEU   A 1 324 ? 22.375 15.214  9.019   1.00 12.82  ? 324  LEU   A N   1 
ATOM   2238 C  CA  . LEU   A 1 324 ? 21.584 15.793  10.105  1.00 12.85  ? 324  LEU   A CA  1 
ATOM   2239 C  C   . LEU   A 1 324 ? 22.180 17.133  10.499  1.00 13.43  ? 324  LEU   A C   1 
ATOM   2240 O  O   . LEU   A 1 324 ? 22.873 17.257  11.519  1.00 12.67  ? 324  LEU   A O   1 
ATOM   2241 C  CB  . LEU   A 1 324 ? 21.535 14.834  11.310  1.00 12.82  ? 324  LEU   A CB  1 
ATOM   2242 C  CG  . LEU   A 1 324 ? 20.783 15.334  12.547  1.00 13.68  ? 324  LEU   A CG  1 
ATOM   2243 C  CD1 . LEU   A 1 324 ? 19.386 15.897  12.194  1.00 13.97  ? 324  LEU   A CD1 1 
ATOM   2244 C  CD2 . LEU   A 1 324 ? 20.568 14.194  13.562  1.00 14.27  ? 324  LEU   A CD2 1 
ATOM   2245 N  N   . THR   A 1 325 ? 21.985 18.110  9.622   1.00 12.88  ? 325  THR   A N   1 
ATOM   2246 C  CA  . THR   A 1 325 ? 22.502 19.454  9.916   1.00 12.08  ? 325  THR   A CA  1 
ATOM   2247 C  C   . THR   A 1 325 ? 21.602 20.084  10.963  1.00 12.17  ? 325  THR   A C   1 
ATOM   2248 O  O   . THR   A 1 325 ? 20.395 19.833  10.973  1.00 12.79  ? 325  THR   A O   1 
ATOM   2249 C  CB  . THR   A 1 325 ? 22.640 20.264  8.628   1.00 13.25  ? 325  THR   A CB  1 
ATOM   2250 O  OG1 . THR   A 1 325 ? 21.349 20.506  8.018   1.00 13.55  ? 325  THR   A OG1 1 
ATOM   2251 C  CG2 . THR   A 1 325 ? 23.561 19.550  7.617   1.00 13.95  ? 325  THR   A CG2 1 
ATOM   2252 N  N   . THR   A 1 326 ? 22.221 20.883  11.867  1.00 11.57  ? 326  THR   A N   1 
ATOM   2253 C  CA  . THR   A 1 326 ? 21.529 21.480  13.002  1.00 11.56  ? 326  THR   A CA  1 
ATOM   2254 C  C   . THR   A 1 326 ? 21.704 22.991  12.971  1.00 11.59  ? 326  THR   A C   1 
ATOM   2255 O  O   . THR   A 1 326 ? 22.673 23.511  12.426  1.00 12.00  ? 326  THR   A O   1 
ATOM   2256 C  CB  . THR   A 1 326 ? 22.048 20.882  14.306  1.00 12.24  ? 326  THR   A CB  1 
ATOM   2257 O  OG1 . THR   A 1 326 ? 23.466 20.990  14.275  1.00 12.87  ? 326  THR   A OG1 1 
ATOM   2258 C  CG2 . THR   A 1 326 ? 21.592 19.414  14.490  1.00 12.27  ? 326  THR   A CG2 1 
ATOM   2259 N  N   . TYR   A 1 327 ? 20.742 23.686  13.571  1.00 11.45  ? 327  TYR   A N   1 
ATOM   2260 C  CA  . TYR   A 1 327 ? 20.693 25.131  13.476  1.00 11.76  ? 327  TYR   A CA  1 
ATOM   2261 C  C   . TYR   A 1 327 ? 20.137 25.744  14.691  1.00 11.50  ? 327  TYR   A C   1 
ATOM   2262 O  O   . TYR   A 1 327 ? 19.221 25.194  15.291  1.00 11.92  ? 327  TYR   A O   1 
ATOM   2263 C  CB  . TYR   A 1 327 ? 19.708 25.551  12.321  1.00 11.68  ? 327  TYR   A CB  1 
ATOM   2264 C  CG  . TYR   A 1 327 ? 20.097 24.978  10.980  1.00 11.05  ? 327  TYR   A CG  1 
ATOM   2265 C  CD1 . TYR   A 1 327 ? 19.808 23.658  10.653  1.00 11.93  ? 327  TYR   A CD1 1 
ATOM   2266 C  CD2 . TYR   A 1 327 ? 20.758 25.755  10.033  1.00 11.94  ? 327  TYR   A CD2 1 
ATOM   2267 C  CE1 . TYR   A 1 327 ? 20.298 23.083  9.499   1.00 10.87  ? 327  TYR   A CE1 1 
ATOM   2268 C  CE2 . TYR   A 1 327 ? 21.195 25.203  8.833   1.00 11.85  ? 327  TYR   A CE2 1 
ATOM   2269 C  CZ  . TYR   A 1 327 ? 21.007 23.857  8.591   1.00 11.93  ? 327  TYR   A CZ  1 
ATOM   2270 O  OH  . TYR   A 1 327 ? 21.462 23.284  7.424   1.00 12.88  ? 327  TYR   A OH  1 
ATOM   2271 N  N   . ARG   A 1 328 ? 20.549 26.994  14.987  1.00 11.61  ? 328  ARG   A N   1 
ATOM   2272 C  CA  . ARG   A 1 328 ? 19.733 27.819  15.887  1.00 11.84  ? 328  ARG   A CA  1 
ATOM   2273 C  C   . ARG   A 1 328 ? 18.355 27.985  15.203  1.00 12.93  ? 328  ARG   A C   1 
ATOM   2274 O  O   . ARG   A 1 328 ? 18.284 28.096  13.955  1.00 12.95  ? 328  ARG   A O   1 
ATOM   2275 C  CB  . ARG   A 1 328 ? 20.331 29.224  15.995  1.00 13.22  ? 328  ARG   A CB  1 
ATOM   2276 C  CG  . ARG   A 1 328 ? 21.364 29.361  17.097  1.00 13.55  ? 328  ARG   A CG  1 
ATOM   2277 C  CD  . ARG   A 1 328 ? 21.965 30.766  17.088  1.00 13.92  ? 328  ARG   A CD  1 
ATOM   2278 N  NE  . ARG   A 1 328 ? 23.001 30.858  18.114  1.00 13.01  ? 328  ARG   A NE  1 
ATOM   2279 C  CZ  . ARG   A 1 328 ? 22.883 31.529  19.254  1.00 13.27  ? 328  ARG   A CZ  1 
ATOM   2280 N  NH1 . ARG   A 1 328 ? 21.787 32.259  19.500  1.00 13.87  ? 328  ARG   A NH1 1 
ATOM   2281 N  NH2 . ARG   A 1 328 ? 23.906 31.569  20.116  1.00 12.86  ? 328  ARG   A NH2 1 
ATOM   2282 N  N   . GLU   A 1 329 ? 17.291 28.096  16.001  1.00 12.37  ? 329  GLU   A N   1 
ATOM   2283 C  CA  . GLU   A 1 329 ? 15.979 28.378  15.404  1.00 11.90  ? 329  GLU   A CA  1 
ATOM   2284 C  C   . GLU   A 1 329 ? 16.043 29.664  14.558  1.00 12.84  ? 329  GLU   A C   1 
ATOM   2285 O  O   . GLU   A 1 329 ? 15.494 29.702  13.456  1.00 13.29  ? 329  GLU   A O   1 
ATOM   2286 C  CB  . GLU   A 1 329 ? 14.932 28.523  16.528  1.00 12.49  ? 329  GLU   A CB  1 
ATOM   2287 C  CG  . GLU   A 1 329 ? 14.564 27.187  17.111  1.00 13.27  ? 329  GLU   A CG  1 
ATOM   2288 C  CD  . GLU   A 1 329 ? 13.600 27.251  18.279  1.00 13.05  ? 329  GLU   A CD  1 
ATOM   2289 O  OE1 . GLU   A 1 329 ? 13.523 28.323  18.924  1.00 15.33  ? 329  GLU   A OE1 1 
ATOM   2290 O  OE2 . GLU   A 1 329 ? 12.932 26.223  18.548  1.00 15.27  ? 329  GLU   A OE2 1 
ATOM   2291 N  N   . SER   A 1 330 ? 16.819 30.667  15.037  1.00 11.53  ? 330  SER   A N   1 
ATOM   2292 C  CA  . SER   A 1 330 ? 16.939 31.926  14.269  1.00 12.20  ? 330  SER   A CA  1 
ATOM   2293 C  C   . SER   A 1 330 ? 17.632 31.791  12.934  1.00 13.08  ? 330  SER   A C   1 
ATOM   2294 O  O   . SER   A 1 330 ? 17.502 32.694  12.083  1.00 13.56  ? 330  SER   A O   1 
ATOM   2295 C  CB  . SER   A 1 330 ? 17.656 32.984  15.101  1.00 12.87  ? 330  SER   A CB  1 
ATOM   2296 O  OG  . SER   A 1 330 ? 18.964 32.511  15.450  1.00 14.90  ? 330  SER   A OG  1 
ATOM   2297 N  N   . ALA   A 1 331 ? 18.440 30.738  12.772  1.00 12.95  ? 331  ALA   A N   1 
ATOM   2298 C  CA  . ALA   A 1 331 ? 19.169 30.547  11.525  1.00 13.32  ? 331  ALA   A CA  1 
ATOM   2299 C  C   . ALA   A 1 331 ? 18.426 29.676  10.527  1.00 13.38  ? 331  ALA   A C   1 
ATOM   2300 O  O   . ALA   A 1 331 ? 18.950 29.444  9.436   1.00 13.76  ? 331  ALA   A O   1 
ATOM   2301 C  CB  . ALA   A 1 331 ? 20.525 29.927  11.827  1.00 13.57  ? 331  ALA   A CB  1 
ATOM   2302 N  N   . LEU   A 1 332 ? 17.212 29.204  10.860  1.00 13.09  ? 332  LEU   A N   1 
ATOM   2303 C  CA  . LEU   A 1 332 ? 16.479 28.317  9.963   1.00 12.52  ? 332  LEU   A CA  1 
ATOM   2304 C  C   . LEU   A 1 332 ? 15.048 28.671  9.738   1.00 12.53  ? 332  LEU   A C   1 
ATOM   2305 O  O   . LEU   A 1 332 ? 14.515 28.407  8.643   1.00 13.56  ? 332  LEU   A O   1 
ATOM   2306 C  CB  . LEU   A 1 332 ? 16.552 26.884  10.555  1.00 12.94  ? 332  LEU   A CB  1 
ATOM   2307 C  CG  . LEU   A 1 332 ? 16.157 25.770  9.581   1.00 13.50  ? 332  LEU   A CG  1 
ATOM   2308 C  CD1 . LEU   A 1 332 ? 17.203 25.689  8.426   1.00 13.76  ? 332  LEU   A CD1 1 
ATOM   2309 C  CD2 . LEU   A 1 332 ? 16.100 24.391  10.272  1.00 13.65  ? 332  LEU   A CD2 1 
ATOM   2310 N  N   . LEU   A 1 333 ? 14.389 29.159  10.776  1.00 12.47  ? 333  LEU   A N   1 
ATOM   2311 C  CA  . LEU   A 1 333 ? 12.932 29.338  10.775  1.00 13.37  ? 333  LEU   A CA  1 
ATOM   2312 C  C   . LEU   A 1 333 ? 12.493 30.711  10.365  1.00 13.58  ? 333  LEU   A C   1 
ATOM   2313 O  O   . LEU   A 1 333 ? 12.936 31.716  10.940  1.00 14.42  ? 333  LEU   A O   1 
ATOM   2314 C  CB  . LEU   A 1 333 ? 12.371 28.952  12.142  1.00 13.11  ? 333  LEU   A CB  1 
ATOM   2315 C  CG  . LEU   A 1 333 ? 12.742 27.528  12.608  1.00 12.68  ? 333  LEU   A CG  1 
ATOM   2316 C  CD1 . LEU   A 1 333 ? 12.123 27.248  13.974  1.00 14.48  ? 333  LEU   A CD1 1 
ATOM   2317 C  CD2 . LEU   A 1 333 ? 12.209 26.453  11.623  1.00 15.52  ? 333  LEU   A CD2 1 
ATOM   2318 N  N   . PHE   A 1 334 ? 11.599 30.773  9.374   1.00 12.97  ? 334  PHE   A N   1 
ATOM   2319 C  CA  . PHE   A 1 334 ? 11.181 32.022  8.770   1.00 13.96  ? 334  PHE   A CA  1 
ATOM   2320 C  C   . PHE   A 1 334 ? 9.678  32.222  8.924   1.00 14.06  ? 334  PHE   A C   1 
ATOM   2321 O  O   . PHE   A 1 334 ? 8.884  31.384  8.486   1.00 14.56  ? 334  PHE   A O   1 
ATOM   2322 C  CB  . PHE   A 1 334 ? 11.530 31.977  7.265   1.00 14.23  ? 334  PHE   A CB  1 
ATOM   2323 C  CG  . PHE   A 1 334 ? 11.179 33.246  6.527   1.00 15.54  ? 334  PHE   A CG  1 
ATOM   2324 C  CD1 . PHE   A 1 334 ? 11.957 34.378  6.665   1.00 17.08  ? 334  PHE   A CD1 1 
ATOM   2325 C  CD2 . PHE   A 1 334 ? 10.080 33.295  5.690   1.00 17.61  ? 334  PHE   A CD2 1 
ATOM   2326 C  CE1 . PHE   A 1 334 ? 11.584 35.578  6.046   1.00 18.83  ? 334  PHE   A CE1 1 
ATOM   2327 C  CE2 . PHE   A 1 334 ? 9.738  34.488  5.037   1.00 19.12  ? 334  PHE   A CE2 1 
ATOM   2328 C  CZ  . PHE   A 1 334 ? 10.480 35.611  5.260   1.00 18.17  ? 334  PHE   A CZ  1 
ATOM   2329 N  N   . ASP   A 1 335 ? 9.294  33.359  9.518   1.00 13.74  ? 335  ASP   A N   1 
ATOM   2330 C  CA  . ASP   A 1 335 ? 7.884  33.724  9.699   1.00 14.21  ? 335  ASP   A CA  1 
ATOM   2331 C  C   . ASP   A 1 335 ? 7.633  34.815  8.666   1.00 14.96  ? 335  ASP   A C   1 
ATOM   2332 O  O   . ASP   A 1 335 ? 8.218  35.894  8.771   1.00 15.15  ? 335  ASP   A O   1 
ATOM   2333 C  CB  . ASP   A 1 335 ? 7.695  34.250  11.136  1.00 15.35  ? 335  ASP   A CB  1 
ATOM   2334 C  CG  . ASP   A 1 335 ? 6.311  34.786  11.423  1.00 19.91  ? 335  ASP   A CG  1 
ATOM   2335 O  OD1 . ASP   A 1 335 ? 5.617  35.186  10.462  1.00 18.97  ? 335  ASP   A OD1 1 
ATOM   2336 O  OD2 . ASP   A 1 335 ? 5.957  34.905  12.624  1.00 20.31  ? 335  ASP   A OD2 1 
ATOM   2337 N  N   . ALA   A 1 336 ? 6.839  34.531  7.641   1.00 14.91  ? 336  ALA   A N   1 
ATOM   2338 C  CA  . ALA   A 1 336 ? 6.662  35.491  6.553   1.00 16.46  ? 336  ALA   A CA  1 
ATOM   2339 C  C   . ALA   A 1 336 ? 6.106  36.823  6.992   1.00 17.78  ? 336  ALA   A C   1 
ATOM   2340 O  O   . ALA   A 1 336 ? 6.256  37.793  6.236   1.00 21.01  ? 336  ALA   A O   1 
ATOM   2341 C  CB  . ALA   A 1 336 ? 5.789  34.885  5.460   1.00 18.47  ? 336  ALA   A CB  1 
ATOM   2342 N  N   . GLU   A 1 337 ? 5.493  36.915  8.176   1.00 16.63  ? 337  GLU   A N   1 
ATOM   2343 C  CA  . GLU   A 1 337 ? 4.963  38.169  8.660   1.00 17.79  ? 337  GLU   A CA  1 
ATOM   2344 C  C   . GLU   A 1 337 ? 5.871  38.927  9.590   1.00 18.09  ? 337  GLU   A C   1 
ATOM   2345 O  O   . GLU   A 1 337 ? 5.712  40.144  9.722   1.00 22.20  ? 337  GLU   A O   1 
ATOM   2346 C  CB  . GLU   A 1 337 ? 3.606  37.973  9.332   1.00 20.52  ? 337  GLU   A CB  1 
ATOM   2347 C  CG  . GLU   A 1 337 ? 2.513  37.535  8.368   1.00 24.54  ? 337  GLU   A CG  1 
ATOM   2348 C  CD  . GLU   A 1 337 ? 1.210  37.358  9.116   1.00 30.31  ? 337  GLU   A CD  1 
ATOM   2349 O  OE1 . GLU   A 1 337 ? 1.196  36.627  10.134  1.00 30.75  ? 337  GLU   A OE1 1 
ATOM   2350 O  OE2 . GLU   A 1 337 ? 0.213  37.998  8.713   1.00 29.12  ? 337  GLU   A OE2 1 
ATOM   2351 N  N   . LYS   A 1 338 ? 6.771  38.235  10.284  1.00 15.41  ? 338  LYS   A N   1 
ATOM   2352 C  CA  . LYS   A 1 338 ? 7.586  38.912  11.318  1.00 15.37  ? 338  LYS   A CA  1 
ATOM   2353 C  C   . LYS   A 1 338 ? 9.087  38.825  11.072  1.00 15.03  ? 338  LYS   A C   1 
ATOM   2354 O  O   . LYS   A 1 338 ? 9.812  39.574  11.715  1.00 16.47  ? 338  LYS   A O   1 
ATOM   2355 C  CB  . LYS   A 1 338 ? 7.317  38.294  12.688  1.00 17.05  ? 338  LYS   A CB  1 
ATOM   2356 C  CG  . LYS   A 1 338 ? 5.945  38.706  13.281  1.00 23.20  ? 338  LYS   A CG  1 
ATOM   2357 C  CD  . LYS   A 1 338 ? 5.787  38.107  14.688  1.00 29.12  ? 338  LYS   A CD  1 
ATOM   2358 C  CE  . LYS   A 1 338 ? 4.438  38.486  15.246  1.00 35.12  ? 338  LYS   A CE  1 
ATOM   2359 N  NZ  . LYS   A 1 338 ? 4.256  39.948  15.132  1.00 37.26  ? 338  LYS   A NZ  1 
ATOM   2360 N  N   . SER   A 1 339 ? 9.559  37.950  10.190  1.00 14.38  ? 339  SER   A N   1 
ATOM   2361 C  CA  . SER   A 1 339 ? 10.991 37.830  9.961   1.00 14.39  ? 339  SER   A CA  1 
ATOM   2362 C  C   . SER   A 1 339 ? 11.510 39.001  9.150   1.00 15.28  ? 339  SER   A C   1 
ATOM   2363 O  O   . SER   A 1 339 ? 10.849 39.502  8.248   1.00 16.56  ? 339  SER   A O   1 
ATOM   2364 C  CB  . SER   A 1 339 ? 11.304 36.539  9.221   1.00 14.82  ? 339  SER   A CB  1 
ATOM   2365 O  OG  . SER   A 1 339 ? 11.255 35.452  10.143  1.00 15.61  ? 339  SER   A OG  1 
ATOM   2366 N  N   . SER   A 1 340 ? 12.736 39.439  9.484   1.00 14.84  ? 340  SER   A N   1 
ATOM   2367 C  CA  . SER   A 1 340 ? 13.351 40.550  8.772   1.00 15.42  ? 340  SER   A CA  1 
ATOM   2368 C  C   . SER   A 1 340 ? 13.928 40.090  7.423   1.00 15.67  ? 340  SER   A C   1 
ATOM   2369 O  O   . SER   A 1 340 ? 14.152 38.895  7.189   1.00 15.70  ? 340  SER   A O   1 
ATOM   2370 C  CB  . SER   A 1 340 ? 14.474 41.111  9.627   1.00 17.19  ? 340  SER   A CB  1 
ATOM   2371 O  OG  . SER   A 1 340 ? 15.453 40.094  9.806   1.00 16.09  ? 340  SER   A OG  1 
ATOM   2372 N  N   . ALA   A 1 341 ? 14.266 41.067  6.557   1.00 15.05  ? 341  ALA   A N   1 
ATOM   2373 C  CA  . ALA   A 1 341 ? 14.918 40.792  5.318   1.00 15.42  ? 341  ALA   A CA  1 
ATOM   2374 C  C   . ALA   A 1 341 ? 16.317 40.208  5.613   1.00 15.03  ? 341  ALA   A C   1 
ATOM   2375 O  O   . ALA   A 1 341 ? 16.749 39.274  4.931   1.00 15.57  ? 341  ALA   A O   1 
ATOM   2376 C  CB  . ALA   A 1 341 ? 15.077 42.104  4.546   1.00 16.80  ? 341  ALA   A CB  1 
ATOM   2377 N  N   . SER   A 1 342 ? 17.021 40.740  6.606   1.00 15.47  ? 342  SER   A N   1 
ATOM   2378 C  CA  A SER   A 1 342 ? 18.349 40.222  6.981   0.50 16.46  ? 342  SER   A CA  1 
ATOM   2379 C  CA  B SER   A 1 342 ? 18.357 40.207  6.934   0.50 16.10  ? 342  SER   A CA  1 
ATOM   2380 C  C   . SER   A 1 342 ? 18.237 38.773  7.440   1.00 16.70  ? 342  SER   A C   1 
ATOM   2381 O  O   . SER   A 1 342 ? 19.143 37.966  7.161   1.00 16.37  ? 342  SER   A O   1 
ATOM   2382 C  CB  A SER   A 1 342 ? 18.939 41.058  8.110   0.50 19.20  ? 342  SER   A CB  1 
ATOM   2383 C  CB  B SER   A 1 342 ? 19.063 41.089  7.952   0.50 18.06  ? 342  SER   A CB  1 
ATOM   2384 O  OG  A SER   A 1 342 ? 20.179 40.523  8.545   0.50 21.99  ? 342  SER   A OG  1 
ATOM   2385 O  OG  B SER   A 1 342 ? 18.317 41.174  9.152   0.50 18.70  ? 342  SER   A OG  1 
ATOM   2386 N  N   . SER   A 1 343 ? 17.146 38.418  8.128   1.00 16.28  ? 343  SER   A N   1 
ATOM   2387 C  CA  A SER   A 1 343 ? 16.940 37.038  8.588   0.50 17.87  ? 343  SER   A CA  1 
ATOM   2388 C  CA  B SER   A 1 343 ? 17.053 37.032  8.595   0.50 17.34  ? 343  SER   A CA  1 
ATOM   2389 C  C   . SER   A 1 343 ? 16.732 36.109  7.424   1.00 17.54  ? 343  SER   A C   1 
ATOM   2390 O  O   . SER   A 1 343 ? 17.239 34.970  7.400   1.00 18.22  ? 343  SER   A O   1 
ATOM   2391 C  CB  A SER   A 1 343 ? 15.710 36.964  9.488   0.50 20.46  ? 343  SER   A CB  1 
ATOM   2392 C  CB  B SER   A 1 343 ? 16.087 36.896  9.755   0.50 18.71  ? 343  SER   A CB  1 
ATOM   2393 O  OG  A SER   A 1 343 ? 16.076 37.289  10.815  0.50 24.29  ? 343  SER   A OG  1 
ATOM   2394 O  OG  B SER   A 1 343 ? 14.778 37.025  9.245   0.50 18.89  ? 343  SER   A OG  1 
ATOM   2395 N  N   . LYS   A 1 344 ? 15.961 36.549  6.420   1.00 16.64  ? 344  LYS   A N   1 
ATOM   2396 C  CA  . LYS   A 1 344 ? 15.692 35.733  5.225   1.00 17.40  ? 344  LYS   A CA  1 
ATOM   2397 C  C   . LYS   A 1 344 ? 17.013 35.469  4.502   1.00 17.10  ? 344  LYS   A C   1 
ATOM   2398 O  O   . LYS   A 1 344 ? 17.340 34.319  4.123   1.00 17.84  ? 344  LYS   A O   1 
ATOM   2399 C  CB  . LYS   A 1 344 ? 14.699 36.436  4.292   1.00 20.46  ? 344  LYS   A CB  1 
ATOM   2400 C  CG  . LYS   A 1 344 ? 14.326 35.541  3.110   1.00 27.44  ? 344  LYS   A CG  1 
ATOM   2401 C  CD  . LYS   A 1 344 ? 13.190 36.106  2.245   1.00 33.04  ? 344  LYS   A CD  1 
ATOM   2402 C  CE  . LYS   A 1 344 ? 12.075 35.110  2.118   1.00 38.85  ? 344  LYS   A CE  1 
ATOM   2403 N  NZ  . LYS   A 1 344 ? 10.962 35.591  1.248   1.00 42.67  ? 344  LYS   A NZ  1 
ATOM   2404 N  N   . LEU   A 1 345 ? 17.830 36.521  4.332   1.00 15.93  ? 345  LEU   A N   1 
ATOM   2405 C  CA  . LEU   A 1 345 ? 19.142 36.370  3.718   1.00 16.40  ? 345  LEU   A CA  1 
ATOM   2406 C  C   . LEU   A 1 345 ? 19.998 35.427  4.572   1.00 15.55  ? 345  LEU   A C   1 
ATOM   2407 O  O   . LEU   A 1 345 ? 20.626 34.516  4.023   1.00 15.51  ? 345  LEU   A O   1 
ATOM   2408 C  CB  . LEU   A 1 345 ? 19.769 37.781  3.656   1.00 17.09  ? 345  LEU   A CB  1 
ATOM   2409 C  CG  . LEU   A 1 345 ? 21.235 37.844  3.298   1.00 19.51  ? 345  LEU   A CG  1 
ATOM   2410 C  CD1 . LEU   A 1 345 ? 21.493 37.280  1.914   1.00 20.21  ? 345  LEU   A CD1 1 
ATOM   2411 C  CD2 . LEU   A 1 345 ? 21.710 39.323  3.350   1.00 21.03  ? 345  LEU   A CD2 1 
ATOM   2412 N  N   . GLY   A 1 346 ? 20.025 35.617  5.878   1.00 14.65  ? 346  GLY   A N   1 
ATOM   2413 C  CA  . GLY   A 1 346 ? 20.845 34.794  6.760   1.00 14.17  ? 346  GLY   A CA  1 
ATOM   2414 C  C   . GLY   A 1 346 ? 20.462 33.327  6.729   1.00 14.32  ? 346  GLY   A C   1 
ATOM   2415 O  O   . GLY   A 1 346 ? 21.347 32.470  6.812   1.00 14.98  ? 346  GLY   A O   1 
ATOM   2416 N  N   . ILE   A 1 347 ? 19.170 33.005  6.694   1.00 13.29  ? 347  ILE   A N   1 
ATOM   2417 C  CA  . ILE   A 1 347 ? 18.763 31.580  6.611   1.00 13.56  ? 347  ILE   A CA  1 
ATOM   2418 C  C   . ILE   A 1 347 ? 19.279 30.997  5.314   1.00 14.00  ? 347  ILE   A C   1 
ATOM   2419 O  O   . ILE   A 1 347 ? 19.837 29.902  5.263   1.00 13.18  ? 347  ILE   A O   1 
ATOM   2420 C  CB  . ILE   A 1 347 ? 17.220 31.434  6.667   1.00 13.95  ? 347  ILE   A CB  1 
ATOM   2421 C  CG1 . ILE   A 1 347 ? 16.689 31.763  8.085   1.00 13.78  ? 347  ILE   A CG1 1 
ATOM   2422 C  CG2 . ILE   A 1 347 ? 16.785 30.010  6.227   1.00 14.92  ? 347  ILE   A CG2 1 
ATOM   2423 C  CD1 . ILE   A 1 347 ? 15.196 32.013  8.092   1.00 16.08  ? 347  ILE   A CD1 1 
ATOM   2424 N  N   . THR   A 1 348 ? 19.131 31.773  4.197   1.00 13.34  ? 348  THR   A N   1 
ATOM   2425 C  CA  . THR   A 1 348 ? 19.555 31.239  2.916   1.00 12.94  ? 348  THR   A CA  1 
ATOM   2426 C  C   . THR   A 1 348 ? 21.044 30.948  2.944   1.00 12.38  ? 348  THR   A C   1 
ATOM   2427 O  O   . THR   A 1 348 ? 21.467 29.893  2.455   1.00 14.01  ? 348  THR   A O   1 
ATOM   2428 C  CB  . THR   A 1 348 ? 19.217 32.247  1.813   1.00 13.72  ? 348  THR   A CB  1 
ATOM   2429 O  OG1 . THR   A 1 348 ? 17.852 32.701  1.960   1.00 15.44  ? 348  THR   A OG1 1 
ATOM   2430 C  CG2 . THR   A 1 348 ? 19.379 31.633  0.448   1.00 15.31  ? 348  THR   A CG2 1 
ATOM   2431 N  N   . MET   A 1 349 ? 21.846 31.909  3.467   1.00 12.53  ? 349  MET   A N   1 
ATOM   2432 C  CA  . MET   A 1 349 ? 23.292 31.736  3.491   1.00 12.17  ? 349  MET   A CA  1 
ATOM   2433 C  C   . MET   A 1 349 ? 23.694 30.643  4.465   1.00 12.73  ? 349  MET   A C   1 
ATOM   2434 O  O   . MET   A 1 349 ? 24.665 29.915  4.182   1.00 13.61  ? 349  MET   A O   1 
ATOM   2435 C  CB  . MET   A 1 349 ? 23.926 33.053  3.876   1.00 12.77  ? 349  MET   A CB  1 
ATOM   2436 C  CG  . MET   A 1 349 ? 23.627 34.145  2.859   1.00 13.92  ? 349  MET   A CG  1 
ATOM   2437 S  SD  . MET   A 1 349 ? 24.279 33.824  1.190   1.00 17.34  ? 349  MET   A SD  1 
ATOM   2438 C  CE  . MET   A 1 349 ? 25.842 34.667  1.363   1.00 18.13  ? 349  MET   A CE  1 
ATOM   2439 N  N   . THR   A 1 350 ? 22.988 30.492  5.579   1.00 12.74  ? 350  THR   A N   1 
ATOM   2440 C  CA  . THR   A 1 350 ? 23.370 29.453  6.556   1.00 12.25  ? 350  THR   A CA  1 
ATOM   2441 C  C   . THR   A 1 350 ? 23.095 28.065  5.985   1.00 12.64  ? 350  THR   A C   1 
ATOM   2442 O  O   . THR   A 1 350 ? 23.946 27.167  6.050   1.00 12.44  ? 350  THR   A O   1 
ATOM   2443 C  CB  . THR   A 1 350 ? 22.631 29.662  7.875   1.00 12.65  ? 350  THR   A CB  1 
ATOM   2444 O  OG1 . THR   A 1 350 ? 23.010 30.951  8.414   1.00 13.51  ? 350  THR   A OG1 1 
ATOM   2445 C  CG2 . THR   A 1 350 ? 23.032 28.611  8.878   1.00 12.51  ? 350  THR   A CG2 1 
ATOM   2446 N  N   . VAL   A 1 351 ? 21.931 27.897  5.352   1.00 12.41  ? 351  VAL   A N   1 
ATOM   2447 C  CA  . VAL   A 1 351 ? 21.643 26.638  4.676   1.00 12.44  ? 351  VAL   A CA  1 
ATOM   2448 C  C   . VAL   A 1 351 ? 22.682 26.378  3.560   1.00 12.55  ? 351  VAL   A C   1 
ATOM   2449 O  O   . VAL   A 1 351 ? 23.204 25.266  3.456   1.00 13.63  ? 351  VAL   A O   1 
ATOM   2450 C  CB  . VAL   A 1 351 ? 20.202 26.659  4.120   1.00 13.42  ? 351  VAL   A CB  1 
ATOM   2451 C  CG1 . VAL   A 1 351 ? 19.965 25.456  3.211   1.00 14.89  ? 351  VAL   A CG1 1 
ATOM   2452 C  CG2 . VAL   A 1 351 ? 19.212 26.650  5.297   1.00 13.91  ? 351  VAL   A CG2 1 
ATOM   2453 N  N   . ALA   A 1 352 ? 23.053 27.407  2.793   1.00 12.82  ? 352  ALA   A N   1 
ATOM   2454 C  CA  . ALA   A 1 352 ? 24.060 27.231  1.733   1.00 12.87  ? 352  ALA   A CA  1 
ATOM   2455 C  C   . ALA   A 1 352 ? 25.396 26.816  2.343   1.00 12.84  ? 352  ALA   A C   1 
ATOM   2456 O  O   . ALA   A 1 352 ? 26.101 26.014  1.740   1.00 12.91  ? 352  ALA   A O   1 
ATOM   2457 C  CB  . ALA   A 1 352 ? 24.212 28.507  0.937   1.00 13.45  ? 352  ALA   A CB  1 
ATOM   2458 N  N   . HIS   A 1 353 ? 25.753 27.391  3.502   1.00 12.08  ? 353  HIS   A N   1 
ATOM   2459 C  CA  . HIS   A 1 353 ? 27.006 27.053  4.157   1.00 12.36  ? 353  HIS   A CA  1 
ATOM   2460 C  C   . HIS   A 1 353 ? 26.999 25.625  4.639   1.00 12.25  ? 353  HIS   A C   1 
ATOM   2461 O  O   . HIS   A 1 353 ? 27.951 24.872  4.333   1.00 12.91  ? 353  HIS   A O   1 
ATOM   2462 C  CB  . HIS   A 1 353 ? 27.170 28.006  5.353   1.00 12.86  ? 353  HIS   A CB  1 
ATOM   2463 C  CG  . HIS   A 1 353 ? 28.484 27.887  6.052   1.00 11.81  ? 353  HIS   A CG  1 
ATOM   2464 N  ND1 . HIS   A 1 353 ? 29.478 28.826  5.880   1.00 13.69  ? 353  HIS   A ND1 1 
ATOM   2465 C  CD2 . HIS   A 1 353 ? 28.929 26.954  6.939   1.00 12.39  ? 353  HIS   A CD2 1 
ATOM   2466 C  CE1 . HIS   A 1 353 ? 30.518 28.417  6.599   1.00 13.58  ? 353  HIS   A CE1 1 
ATOM   2467 N  NE2 . HIS   A 1 353 ? 30.213 27.302  7.277   1.00 13.37  ? 353  HIS   A NE2 1 
ATOM   2468 N  N   . GLU   A 1 354 ? 25.938 25.213  5.351   1.00 12.08  ? 354  GLU   A N   1 
ATOM   2469 C  CA  . GLU   A 1 354 ? 25.923 23.840  5.869   1.00 12.65  ? 354  GLU   A CA  1 
ATOM   2470 C  C   . GLU   A 1 354 ? 25.877 22.828  4.725   1.00 13.11  ? 354  GLU   A C   1 
ATOM   2471 O  O   . GLU   A 1 354 ? 26.524 21.776  4.826   1.00 13.63  ? 354  GLU   A O   1 
ATOM   2472 C  CB  . GLU   A 1 354 ? 24.716 23.640  6.776   1.00 13.02  ? 354  GLU   A CB  1 
ATOM   2473 C  CG  . GLU   A 1 354 ? 24.712 24.584  7.976   1.00 12.36  ? 354  GLU   A CG  1 
ATOM   2474 C  CD  . GLU   A 1 354 ? 26.042 24.666  8.692   1.00 14.70  ? 354  GLU   A CD  1 
ATOM   2475 O  OE1 . GLU   A 1 354 ? 26.665 23.602  8.899   1.00 15.50  ? 354  GLU   A OE1 1 
ATOM   2476 O  OE2 . GLU   A 1 354 ? 26.487 25.797  9.010   1.00 14.75  ? 354  GLU   A OE2 1 
ATOM   2477 N  N   . LEU   A 1 355 ? 25.190 23.165  3.625   1.00 13.22  ? 355  LEU   A N   1 
ATOM   2478 C  CA  . LEU   A 1 355 ? 25.149 22.218  2.510   1.00 13.07  ? 355  LEU   A CA  1 
ATOM   2479 C  C   . LEU   A 1 355 ? 26.466 22.199  1.749   1.00 13.25  ? 355  LEU   A C   1 
ATOM   2480 O  O   . LEU   A 1 355 ? 26.921 21.124  1.324   1.00 13.34  ? 355  LEU   A O   1 
ATOM   2481 C  CB  . LEU   A 1 355 ? 23.956 22.454  1.619   1.00 12.89  ? 355  LEU   A CB  1 
ATOM   2482 C  CG  . LEU   A 1 355 ? 22.601 22.212  2.332   1.00 14.04  ? 355  LEU   A CG  1 
ATOM   2483 C  CD1 . LEU   A 1 355 ? 21.459 22.416  1.357   1.00 14.35  ? 355  LEU   A CD1 1 
ATOM   2484 C  CD2 . LEU   A 1 355 ? 22.514 20.807  3.000   1.00 15.40  ? 355  LEU   A CD2 1 
ATOM   2485 N  N   . ALA   A 1 356 ? 27.172 23.336  1.634   1.00 13.28  ? 356  ALA   A N   1 
ATOM   2486 C  CA  . ALA   A 1 356 ? 28.521 23.282  1.015   1.00 13.00  ? 356  ALA   A CA  1 
ATOM   2487 C  C   . ALA   A 1 356 ? 29.429 22.333  1.778   1.00 12.88  ? 356  ALA   A C   1 
ATOM   2488 O  O   . ALA   A 1 356 ? 30.233 21.601  1.186   1.00 13.06  ? 356  ALA   A O   1 
ATOM   2489 C  CB  . ALA   A 1 356 ? 29.175 24.659  1.049   1.00 12.86  ? 356  ALA   A CB  1 
ATOM   2490 N  N   . HIS   A 1 357 ? 29.289 22.341  3.120   1.00 12.13  ? 357  HIS   A N   1 
ATOM   2491 C  CA  . HIS   A 1 357 ? 30.134 21.473  3.931   1.00 12.29  ? 357  HIS   A CA  1 
ATOM   2492 C  C   . HIS   A 1 357 ? 29.923 20.012  3.630   1.00 12.85  ? 357  HIS   A C   1 
ATOM   2493 O  O   . HIS   A 1 357 ? 30.812 19.222  3.989   1.00 13.15  ? 357  HIS   A O   1 
ATOM   2494 C  CB  . HIS   A 1 357 ? 29.853 21.673  5.431   1.00 12.31  ? 357  HIS   A CB  1 
ATOM   2495 C  CG  . HIS   A 1 357 ? 30.625 22.751  6.118   1.00 11.42  ? 357  HIS   A CG  1 
ATOM   2496 N  ND1 . HIS   A 1 357 ? 31.987 22.841  5.996   1.00 11.67  ? 357  HIS   A ND1 1 
ATOM   2497 C  CD2 . HIS   A 1 357 ? 30.200 23.659  7.038   1.00 11.90  ? 357  HIS   A CD2 1 
ATOM   2498 C  CE1 . HIS   A 1 357 ? 32.351 23.841  6.815   1.00 12.57  ? 357  HIS   A CE1 1 
ATOM   2499 N  NE2 . HIS   A 1 357 ? 31.318 24.372  7.434   1.00 11.87  ? 357  HIS   A NE2 1 
ATOM   2500 N  N   . GLN   A 1 358 ? 28.787 19.596  3.045   1.00 12.32  ? 358  GLN   A N   1 
ATOM   2501 C  CA  . GLN   A 1 358 ? 28.661 18.161  2.757   1.00 13.13  ? 358  GLN   A CA  1 
ATOM   2502 C  C   . GLN   A 1 358 ? 29.774 17.687  1.846   1.00 13.72  ? 358  GLN   A C   1 
ATOM   2503 O  O   . GLN   A 1 358 ? 30.161 16.529  1.926   1.00 14.21  ? 358  GLN   A O   1 
ATOM   2504 C  CB  . GLN   A 1 358 ? 27.266 17.805  2.205   1.00 13.21  ? 358  GLN   A CB  1 
ATOM   2505 C  CG  . GLN   A 1 358 ? 26.115 18.393  3.028   1.00 13.02  ? 358  GLN   A CG  1 
ATOM   2506 C  CD  . GLN   A 1 358 ? 26.110 17.973  4.469   1.00 13.94  ? 358  GLN   A CD  1 
ATOM   2507 O  OE1 . GLN   A 1 358 ? 25.818 16.793  4.775   1.00 13.91  ? 358  GLN   A OE1 1 
ATOM   2508 N  NE2 . GLN   A 1 358 ? 26.360 18.873  5.428   1.00 13.65  ? 358  GLN   A NE2 1 
ATOM   2509 N  N   . TRP   A 1 359 ? 30.331 18.609  1.026   1.00 13.38  ? 359  TRP   A N   1 
ATOM   2510 C  CA  . TRP   A 1 359 ? 31.452 18.307  0.158   1.00 13.73  ? 359  TRP   A CA  1 
ATOM   2511 C  C   . TRP   A 1 359 ? 32.722 18.851  0.825   1.00 14.00  ? 359  TRP   A C   1 
ATOM   2512 O  O   . TRP   A 1 359 ? 33.665 18.087  1.091   1.00 14.73  ? 359  TRP   A O   1 
ATOM   2513 C  CB  . TRP   A 1 359 ? 31.216 18.975  -1.226  1.00 14.54  ? 359  TRP   A CB  1 
ATOM   2514 C  CG  . TRP   A 1 359 ? 30.163 18.281  -2.029  1.00 14.77  ? 359  TRP   A CG  1 
ATOM   2515 C  CD1 . TRP   A 1 359 ? 30.364 17.343  -3.014  1.00 15.79  ? 359  TRP   A CD1 1 
ATOM   2516 C  CD2 . TRP   A 1 359 ? 28.728 18.457  -1.927  1.00 14.36  ? 359  TRP   A CD2 1 
ATOM   2517 N  NE1 . TRP   A 1 359 ? 29.143 16.899  -3.501  1.00 15.68  ? 359  TRP   A NE1 1 
ATOM   2518 C  CE2 . TRP   A 1 359 ? 28.125 17.590  -2.869  1.00 16.30  ? 359  TRP   A CE2 1 
ATOM   2519 C  CE3 . TRP   A 1 359 ? 27.892 19.264  -1.136  1.00 14.84  ? 359  TRP   A CE3 1 
ATOM   2520 C  CZ2 . TRP   A 1 359 ? 26.728 17.514  -3.042  1.00 16.28  ? 359  TRP   A CZ2 1 
ATOM   2521 C  CZ3 . TRP   A 1 359 ? 26.514 19.187  -1.306  1.00 15.33  ? 359  TRP   A CZ3 1 
ATOM   2522 C  CH2 . TRP   A 1 359 ? 25.941 18.305  -2.235  1.00 15.62  ? 359  TRP   A CH2 1 
ATOM   2523 N  N   . PHE   A 1 360 ? 32.742 20.157  1.135   1.00 13.54  ? 360  PHE   A N   1 
ATOM   2524 C  CA  . PHE   A 1 360 ? 33.893 20.780  1.783   1.00 13.51  ? 360  PHE   A CA  1 
ATOM   2525 C  C   . PHE   A 1 360 ? 33.817 20.682  3.274   1.00 13.03  ? 360  PHE   A C   1 
ATOM   2526 O  O   . PHE   A 1 360 ? 33.418 21.617  3.976   1.00 13.33  ? 360  PHE   A O   1 
ATOM   2527 C  CB  . PHE   A 1 360 ? 34.002 22.272  1.368   1.00 13.60  ? 360  PHE   A CB  1 
ATOM   2528 C  CG  . PHE   A 1 360 ? 34.445 22.415  -0.067  1.00 14.63  ? 360  PHE   A CG  1 
ATOM   2529 C  CD1 . PHE   A 1 360 ? 35.758 22.184  -0.420  1.00 14.65  ? 360  PHE   A CD1 1 
ATOM   2530 C  CD2 . PHE   A 1 360 ? 33.547 22.780  -1.057  1.00 16.29  ? 360  PHE   A CD2 1 
ATOM   2531 C  CE1 . PHE   A 1 360 ? 36.196 22.359  -1.724  1.00 15.69  ? 360  PHE   A CE1 1 
ATOM   2532 C  CE2 . PHE   A 1 360 ? 33.997 23.001  -2.380  1.00 17.35  ? 360  PHE   A CE2 1 
ATOM   2533 C  CZ  . PHE   A 1 360 ? 35.311 22.746  -2.699  1.00 16.86  ? 360  PHE   A CZ  1 
ATOM   2534 N  N   . GLY   A 1 361 ? 34.198 19.502  3.764   1.00 13.53  ? 361  GLY   A N   1 
ATOM   2535 C  CA  . GLY   A 1 361 ? 34.307 19.260  5.200   1.00 13.76  ? 361  GLY   A CA  1 
ATOM   2536 C  C   . GLY   A 1 361 ? 33.945 17.833  5.519   1.00 13.46  ? 361  GLY   A C   1 
ATOM   2537 O  O   . GLY   A 1 361 ? 34.616 17.180  6.330   1.00 13.75  ? 361  GLY   A O   1 
ATOM   2538 N  N   . ASN   A 1 362 ? 32.872 17.363  4.905   1.00 12.94  ? 362  ASN   A N   1 
ATOM   2539 C  CA  . ASN   A 1 362 ? 32.386 16.005  5.214   1.00 12.94  ? 362  ASN   A CA  1 
ATOM   2540 C  C   . ASN   A 1 362 ? 33.002 14.991  4.269   1.00 13.75  ? 362  ASN   A C   1 
ATOM   2541 O  O   . ASN   A 1 362 ? 33.677 14.061  4.709   1.00 15.13  ? 362  ASN   A O   1 
ATOM   2542 C  CB  . ASN   A 1 362 ? 30.833 15.928  5.197   1.00 13.17  ? 362  ASN   A CB  1 
ATOM   2543 C  CG  . ASN   A 1 362 ? 30.153 16.820  6.204   1.00 13.57  ? 362  ASN   A CG  1 
ATOM   2544 O  OD1 . ASN   A 1 362 ? 30.804 17.626  6.882   1.00 13.34  ? 362  ASN   A OD1 1 
ATOM   2545 N  ND2 . ASN   A 1 362 ? 28.821 16.702  6.333   1.00 13.42  ? 362  ASN   A ND2 1 
ATOM   2546 N  N   . LEU   A 1 363 ? 32.794 15.171  2.961   1.00 13.52  ? 363  LEU   A N   1 
ATOM   2547 C  CA  . LEU   A 1 363 ? 33.364 14.258  1.966   1.00 13.79  ? 363  LEU   A CA  1 
ATOM   2548 C  C   . LEU   A 1 363 ? 34.869 14.397  1.981   1.00 14.64  ? 363  LEU   A C   1 
ATOM   2549 O  O   . LEU   A 1 363 ? 35.598 13.389  2.005   1.00 15.94  ? 363  LEU   A O   1 
ATOM   2550 C  CB  . LEU   A 1 363 ? 32.823 14.662  0.587   1.00 14.88  ? 363  LEU   A CB  1 
ATOM   2551 C  CG  . LEU   A 1 363 ? 33.354 13.838  -0.576  1.00 16.47  ? 363  LEU   A CG  1 
ATOM   2552 C  CD1 . LEU   A 1 363 ? 32.827 12.435  -0.457  1.00 17.70  ? 363  LEU   A CD1 1 
ATOM   2553 C  CD2 . LEU   A 1 363 ? 32.911 14.502  -1.896  1.00 17.10  ? 363  LEU   A CD2 1 
ATOM   2554 N  N   . VAL   A 1 364 ? 35.364 15.645  1.964   1.00 13.57  ? 364  VAL   A N   1 
ATOM   2555 C  CA  . VAL   A 1 364 ? 36.781 15.895  2.046   1.00 13.76  ? 364  VAL   A CA  1 
ATOM   2556 C  C   . VAL   A 1 364 ? 36.980 16.702  3.302   1.00 13.99  ? 364  VAL   A C   1 
ATOM   2557 O  O   . VAL   A 1 364 ? 36.312 17.726  3.502   1.00 15.32  ? 364  VAL   A O   1 
ATOM   2558 C  CB  . VAL   A 1 364 ? 37.310 16.693  0.834   1.00 15.28  ? 364  VAL   A CB  1 
ATOM   2559 C  CG1 . VAL   A 1 364 ? 38.781 17.054  1.060   1.00 16.94  ? 364  VAL   A CG1 1 
ATOM   2560 C  CG2 . VAL   A 1 364 ? 37.130 15.877  -0.462  1.00 15.97  ? 364  VAL   A CG2 1 
ATOM   2561 N  N   . THR   A 1 365 ? 37.888 16.239  4.187   1.00 14.05  ? 365  THR   A N   1 
ATOM   2562 C  CA  . THR   A 1 365 ? 38.061 16.869  5.486   1.00 13.73  ? 365  THR   A CA  1 
ATOM   2563 C  C   . THR   A 1 365 ? 39.492 17.281  5.693   1.00 14.47  ? 365  THR   A C   1 
ATOM   2564 O  O   . THR   A 1 365 ? 40.395 16.545  5.278   1.00 14.42  ? 365  THR   A O   1 
ATOM   2565 C  CB  . THR   A 1 365 ? 37.680 15.830  6.557   1.00 14.62  ? 365  THR   A CB  1 
ATOM   2566 O  OG1 . THR   A 1 365 ? 36.410 15.252  6.233   1.00 14.08  ? 365  THR   A OG1 1 
ATOM   2567 C  CG2 . THR   A 1 365 ? 37.666 16.397  7.988   1.00 14.33  ? 365  THR   A CG2 1 
ATOM   2568 N  N   . MET   A 1 366 ? 39.767 18.401  6.395   1.00 13.72  ? 366  MET   A N   1 
ATOM   2569 C  CA  . MET   A 1 366 ? 41.187 18.707  6.687   1.00 14.98  ? 366  MET   A CA  1 
ATOM   2570 C  C   . MET   A 1 366 ? 41.824 17.579  7.524   1.00 14.59  ? 366  MET   A C   1 
ATOM   2571 O  O   . MET   A 1 366 ? 41.135 16.938  8.339   1.00 14.34  ? 366  MET   A O   1 
ATOM   2572 C  CB  . MET   A 1 366 ? 41.348 20.071  7.376   1.00 15.50  ? 366  MET   A CB  1 
ATOM   2573 C  CG  . MET   A 1 366 ? 40.937 20.119  8.838   1.00 15.62  ? 366  MET   A CG  1 
ATOM   2574 S  SD  . MET   A 1 366 ? 39.138 20.255  8.988   1.00 15.02  ? 366  MET   A SD  1 
ATOM   2575 C  CE  . MET   A 1 366 ? 38.863 19.064  10.349  1.00 15.68  ? 366  MET   A CE  1 
ATOM   2576 N  N   A GLU   A 1 367 ? 43.115 17.307  7.303   0.50 14.29  ? 367  GLU   A N   1 
ATOM   2577 N  N   B GLU   A 1 367 ? 43.112 17.326  7.303   0.50 14.02  ? 367  GLU   A N   1 
ATOM   2578 C  CA  A GLU   A 1 367 ? 43.790 16.260  8.084   0.50 14.57  ? 367  GLU   A CA  1 
ATOM   2579 C  CA  B GLU   A 1 367 ? 43.836 16.290  8.047   0.50 14.05  ? 367  GLU   A CA  1 
ATOM   2580 C  C   A GLU   A 1 367 ? 43.844 16.641  9.566   0.50 15.29  ? 367  GLU   A C   1 
ATOM   2581 C  C   B GLU   A 1 367 ? 43.957 16.631  9.537   0.50 14.78  ? 367  GLU   A C   1 
ATOM   2582 O  O   A GLU   A 1 367 ? 43.650 15.784  10.435  0.50 15.90  ? 367  GLU   A O   1 
ATOM   2583 O  O   B GLU   A 1 367 ? 43.948 15.734  10.381  0.50 14.80  ? 367  GLU   A O   1 
ATOM   2584 C  CB  A GLU   A 1 367 ? 45.215 16.043  7.561   0.50 16.67  ? 367  GLU   A CB  1 
ATOM   2585 C  CB  B GLU   A 1 367 ? 45.237 16.149  7.444   0.50 15.37  ? 367  GLU   A CB  1 
ATOM   2586 C  CG  A GLU   A 1 367 ? 45.906 14.839  8.223   0.50 19.86  ? 367  GLU   A CG  1 
ATOM   2587 C  CG  B GLU   A 1 367 ? 46.074 15.062  8.121   0.50 19.55  ? 367  GLU   A CG  1 
ATOM   2588 C  CD  A GLU   A 1 367 ? 46.743 15.127  9.457   0.50 26.42  ? 367  GLU   A CD  1 
ATOM   2589 C  CD  B GLU   A 1 367 ? 47.290 14.726  7.292   0.50 25.53  ? 367  GLU   A CD  1 
ATOM   2590 O  OE1 A GLU   A 1 367 ? 46.842 14.243  10.343  0.50 28.73  ? 367  GLU   A OE1 1 
ATOM   2591 O  OE1 B GLU   A 1 367 ? 48.132 15.631  7.108   0.50 26.82  ? 367  GLU   A OE1 1 
ATOM   2592 O  OE2 A GLU   A 1 367 ? 47.301 16.242  9.540   0.50 29.25  ? 367  GLU   A OE2 1 
ATOM   2593 O  OE2 B GLU   A 1 367 ? 47.361 13.596  6.756   0.50 29.34  ? 367  GLU   A OE2 1 
ATOM   2594 N  N   . TRP   A 1 368 ? 44.114 17.917  9.852   1.00 14.53  ? 368  TRP   A N   1 
ATOM   2595 C  CA  . TRP   A 1 368 ? 44.205 18.376  11.224  1.00 14.14  ? 368  TRP   A CA  1 
ATOM   2596 C  C   . TRP   A 1 368 ? 43.721 19.823  11.282  1.00 14.89  ? 368  TRP   A C   1 
ATOM   2597 O  O   . TRP   A 1 368 ? 43.702 20.521  10.232  1.00 14.32  ? 368  TRP   A O   1 
ATOM   2598 C  CB  . TRP   A 1 368 ? 45.640 18.166  11.789  1.00 14.92  ? 368  TRP   A CB  1 
ATOM   2599 C  CG  . TRP   A 1 368 ? 45.815 18.582  13.200  1.00 14.78  ? 368  TRP   A CG  1 
ATOM   2600 C  CD1 . TRP   A 1 368 ? 46.587 19.613  13.653  1.00 16.34  ? 368  TRP   A CD1 1 
ATOM   2601 C  CD2 . TRP   A 1 368 ? 45.162 18.026  14.365  1.00 14.40  ? 368  TRP   A CD2 1 
ATOM   2602 N  NE1 . TRP   A 1 368 ? 46.396 19.792  15.007  1.00 15.72  ? 368  TRP   A NE1 1 
ATOM   2603 C  CE2 . TRP   A 1 368 ? 45.562 18.800  15.481  1.00 15.06  ? 368  TRP   A CE2 1 
ATOM   2604 C  CE3 . TRP   A 1 368 ? 44.299 16.936  14.569  1.00 14.33  ? 368  TRP   A CE3 1 
ATOM   2605 C  CZ2 . TRP   A 1 368 ? 45.145 18.525  16.778  1.00 15.32  ? 368  TRP   A CZ2 1 
ATOM   2606 C  CZ3 . TRP   A 1 368 ? 43.857 16.673  15.854  1.00 15.53  ? 368  TRP   A CZ3 1 
ATOM   2607 C  CH2 . TRP   A 1 368 ? 44.257 17.478  16.942  1.00 14.69  ? 368  TRP   A CH2 1 
ATOM   2608 N  N   . TRP   A 1 369 ? 43.399 20.279  12.475  1.00 14.20  ? 369  TRP   A N   1 
ATOM   2609 C  CA  . TRP   A 1 369 ? 42.758 21.577  12.696  1.00 13.59  ? 369  TRP   A CA  1 
ATOM   2610 C  C   . TRP   A 1 369 ? 43.605 22.767  12.289  1.00 14.14  ? 369  TRP   A C   1 
ATOM   2611 O  O   . TRP   A 1 369 ? 43.041 23.844  12.108  1.00 13.90  ? 369  TRP   A O   1 
ATOM   2612 C  CB  . TRP   A 1 369 ? 42.316 21.679  14.149  1.00 13.76  ? 369  TRP   A CB  1 
ATOM   2613 C  CG  . TRP   A 1 369 ? 41.417 20.534  14.562  1.00 13.18  ? 369  TRP   A CG  1 
ATOM   2614 C  CD1 . TRP   A 1 369 ? 41.796 19.433  15.287  1.00 14.51  ? 369  TRP   A CD1 1 
ATOM   2615 C  CD2 . TRP   A 1 369 ? 40.032 20.329  14.204  1.00 12.81  ? 369  TRP   A CD2 1 
ATOM   2616 N  NE1 . TRP   A 1 369 ? 40.716 18.587  15.458  1.00 14.12  ? 369  TRP   A NE1 1 
ATOM   2617 C  CE2 . TRP   A 1 369 ? 39.635 19.100  14.775  1.00 13.61  ? 369  TRP   A CE2 1 
ATOM   2618 C  CE3 . TRP   A 1 369 ? 39.092 21.065  13.443  1.00 13.70  ? 369  TRP   A CE3 1 
ATOM   2619 C  CZ2 . TRP   A 1 369 ? 38.358 18.587  14.615  1.00 13.49  ? 369  TRP   A CZ2 1 
ATOM   2620 C  CZ3 . TRP   A 1 369 ? 37.798 20.567  13.311  1.00 13.80  ? 369  TRP   A CZ3 1 
ATOM   2621 C  CH2 . TRP   A 1 369 ? 37.438 19.344  13.915  1.00 14.60  ? 369  TRP   A CH2 1 
ATOM   2622 N  N   . ASN   A 1 370 ? 44.925 22.576  12.116  1.00 13.75  ? 370  ASN   A N   1 
ATOM   2623 C  CA  . ASN   A 1 370 ? 45.765 23.665  11.611  1.00 13.86  ? 370  ASN   A CA  1 
ATOM   2624 C  C   . ASN   A 1 370 ? 45.254 24.179  10.254  1.00 14.60  ? 370  ASN   A C   1 
ATOM   2625 O  O   . ASN   A 1 370 ? 45.416 25.356  9.937   1.00 14.82  ? 370  ASN   A O   1 
ATOM   2626 C  CB  . ASN   A 1 370 ? 47.235 23.220  11.490  1.00 14.70  ? 370  ASN   A CB  1 
ATOM   2627 C  CG  . ASN   A 1 370 ? 47.455 22.080  10.557  1.00 19.28  ? 370  ASN   A CG  1 
ATOM   2628 O  OD1 . ASN   A 1 370 ? 46.735 21.094  10.547  1.00 19.27  ? 370  ASN   A OD1 1 
ATOM   2629 N  ND2 . ASN   A 1 370 ? 48.496 22.174  9.747   1.00 21.83  ? 370  ASN   A ND2 1 
ATOM   2630 N  N   . ASP   A 1 371 ? 44.594 23.281  9.488   1.00 14.10  ? 371  ASP   A N   1 
ATOM   2631 C  CA  . ASP   A 1 371 ? 44.050 23.598  8.163   1.00 13.60  ? 371  ASP   A CA  1 
ATOM   2632 C  C   . ASP   A 1 371 ? 42.517 23.611  8.173   1.00 13.88  ? 371  ASP   A C   1 
ATOM   2633 O  O   . ASP   A 1 371 ? 41.890 23.347  7.143   1.00 14.17  ? 371  ASP   A O   1 
ATOM   2634 C  CB  . ASP   A 1 371 ? 44.581 22.642  7.102   1.00 15.24  ? 371  ASP   A CB  1 
ATOM   2635 C  CG  . ASP   A 1 371 ? 46.053 22.811  6.843   1.00 17.68  ? 371  ASP   A CG  1 
ATOM   2636 O  OD1 . ASP   A 1 371 ? 46.576 23.932  7.068   1.00 18.05  ? 371  ASP   A OD1 1 
ATOM   2637 O  OD2 . ASP   A 1 371 ? 46.692 21.830  6.383   1.00 17.02  ? 371  ASP   A OD2 1 
ATOM   2638 N  N   . LEU   A 1 372 ? 41.900 23.965  9.312   1.00 13.14  ? 372  LEU   A N   1 
ATOM   2639 C  CA  . LEU   A 1 372 ? 40.436 24.108  9.347   1.00 13.11  ? 372  LEU   A CA  1 
ATOM   2640 C  C   . LEU   A 1 372 ? 39.906 25.009  8.240   1.00 13.34  ? 372  LEU   A C   1 
ATOM   2641 O  O   . LEU   A 1 372 ? 38.778 24.814  7.803   1.00 13.55  ? 372  LEU   A O   1 
ATOM   2642 C  CB  . LEU   A 1 372 ? 40.028 24.678  10.712  1.00 13.96  ? 372  LEU   A CB  1 
ATOM   2643 C  CG  . LEU   A 1 372 ? 38.529 24.958  10.857  1.00 13.36  ? 372  LEU   A CG  1 
ATOM   2644 C  CD1 . LEU   A 1 372 ? 37.703 23.644  10.771  1.00 13.32  ? 372  LEU   A CD1 1 
ATOM   2645 C  CD2 . LEU   A 1 372 ? 38.280 25.727  12.122  1.00 14.15  ? 372  LEU   A CD2 1 
ATOM   2646 N  N   . TRP   A 1 373 ? 40.705 25.980  7.769   1.00 13.66  ? 373  TRP   A N   1 
ATOM   2647 C  CA  . TRP   A 1 373 ? 40.211 26.859  6.713   1.00 13.13  ? 373  TRP   A CA  1 
ATOM   2648 C  C   . TRP   A 1 373 ? 39.818 26.107  5.447   1.00 14.15  ? 373  TRP   A C   1 
ATOM   2649 O  O   . TRP   A 1 373 ? 38.970 26.601  4.685   1.00 13.26  ? 373  TRP   A O   1 
ATOM   2650 C  CB  . TRP   A 1 373 ? 41.222 27.956  6.389   1.00 13.31  ? 373  TRP   A CB  1 
ATOM   2651 C  CG  . TRP   A 1 373 ? 42.268 27.497  5.405   1.00 13.57  ? 373  TRP   A CG  1 
ATOM   2652 C  CD1 . TRP   A 1 373 ? 43.351 26.681  5.640   1.00 13.57  ? 373  TRP   A CD1 1 
ATOM   2653 C  CD2 . TRP   A 1 373 ? 42.259 27.766  4.013   1.00 13.56  ? 373  TRP   A CD2 1 
ATOM   2654 N  NE1 . TRP   A 1 373 ? 44.032 26.459  4.463   1.00 14.77  ? 373  TRP   A NE1 1 
ATOM   2655 C  CE2 . TRP   A 1 373 ? 43.390 27.129  3.452   1.00 14.45  ? 373  TRP   A CE2 1 
ATOM   2656 C  CE3 . TRP   A 1 373 ? 41.404 28.510  3.180   1.00 15.42  ? 373  TRP   A CE3 1 
ATOM   2657 C  CZ2 . TRP   A 1 373 ? 43.677 27.188  2.091   1.00 15.39  ? 373  TRP   A CZ2 1 
ATOM   2658 C  CZ3 . TRP   A 1 373 ? 41.695 28.577  1.833   1.00 16.98  ? 373  TRP   A CZ3 1 
ATOM   2659 C  CH2 . TRP   A 1 373 ? 42.826 27.938  1.306   1.00 16.41  ? 373  TRP   A CH2 1 
ATOM   2660 N  N   . LEU   A 1 374 ? 40.375 24.920  5.220   1.00 13.74  ? 374  LEU   A N   1 
ATOM   2661 C  CA  . LEU   A 1 374 ? 39.984 24.166  4.027   1.00 13.95  ? 374  LEU   A CA  1 
ATOM   2662 C  C   . LEU   A 1 374 ? 38.502 23.806  4.066   1.00 14.09  ? 374  LEU   A C   1 
ATOM   2663 O  O   . LEU   A 1 374 ? 37.863 23.719  3.032   1.00 14.09  ? 374  LEU   A O   1 
ATOM   2664 C  CB  . LEU   A 1 374 ? 40.815 22.868  3.900   1.00 13.62  ? 374  LEU   A CB  1 
ATOM   2665 C  CG  . LEU   A 1 374 ? 42.285 23.108  3.605   1.00 14.64  ? 374  LEU   A CG  1 
ATOM   2666 C  CD1 . LEU   A 1 374 ? 43.041 21.770  3.733   1.00 15.72  ? 374  LEU   A CD1 1 
ATOM   2667 C  CD2 . LEU   A 1 374 ? 42.464 23.640  2.157   1.00 15.32  ? 374  LEU   A CD2 1 
ATOM   2668 N  N   . ASN   A 1 375 ? 37.988 23.603  5.284   1.00 13.68  ? 375  ASN   A N   1 
ATOM   2669 C  CA  . ASN   A 1 375 ? 36.568 23.372  5.477   1.00 12.13  ? 375  ASN   A CA  1 
ATOM   2670 C  C   . ASN   A 1 375 ? 35.842 24.741  5.503   1.00 13.33  ? 375  ASN   A C   1 
ATOM   2671 O  O   . ASN   A 1 375 ? 34.858 24.938  4.772   1.00 13.97  ? 375  ASN   A O   1 
ATOM   2672 C  CB  . ASN   A 1 375 ? 36.307 22.735  6.859   1.00 12.28  ? 375  ASN   A CB  1 
ATOM   2673 C  CG  . ASN   A 1 375 ? 36.571 21.257  6.967   1.00 15.08  ? 375  ASN   A CG  1 
ATOM   2674 O  OD1 . ASN   A 1 375 ? 37.272 20.648  6.155   1.00 14.62  ? 375  ASN   A OD1 1 
ATOM   2675 N  ND2 . ASN   A 1 375 ? 35.968 20.639  8.015   1.00 13.88  ? 375  ASN   A ND2 1 
ATOM   2676 N  N   . GLU   A 1 376 ? 36.319 25.678  6.345   1.00 12.56  ? 376  GLU   A N   1 
ATOM   2677 C  CA  . GLU   A 1 376 ? 35.481 26.857  6.635   1.00 12.95  ? 376  GLU   A CA  1 
ATOM   2678 C  C   . GLU   A 1 376 ? 35.556 27.938  5.614   1.00 13.20  ? 376  GLU   A C   1 
ATOM   2679 O  O   . GLU   A 1 376 ? 34.555 28.603  5.336   1.00 13.19  ? 376  GLU   A O   1 
ATOM   2680 C  CB  . GLU   A 1 376 ? 35.792 27.408  8.032   1.00 12.96  ? 376  GLU   A CB  1 
ATOM   2681 C  CG  . GLU   A 1 376 ? 35.462 26.383  9.146   1.00 12.70  ? 376  GLU   A CG  1 
ATOM   2682 C  CD  . GLU   A 1 376 ? 33.991 25.950  9.158   1.00 14.40  ? 376  GLU   A CD  1 
ATOM   2683 O  OE1 . GLU   A 1 376 ? 33.181 26.620  8.486   1.00 12.61  ? 376  GLU   A OE1 1 
ATOM   2684 O  OE2 . GLU   A 1 376 ? 33.648 24.935  9.817   1.00 14.07  ? 376  GLU   A OE2 1 
ATOM   2685 N  N   . GLY   A 1 377 ? 36.760 28.198  5.097   1.00 12.87  ? 377  GLY   A N   1 
ATOM   2686 C  CA  . GLY   A 1 377 ? 36.897 29.228  4.056   1.00 13.13  ? 377  GLY   A CA  1 
ATOM   2687 C  C   . GLY   A 1 377 ? 36.113 28.832  2.824   1.00 13.11  ? 377  GLY   A C   1 
ATOM   2688 O  O   . GLY   A 1 377 ? 35.443 29.665  2.183   1.00 13.37  ? 377  GLY   A O   1 
ATOM   2689 N  N   . PHE   A 1 378 ? 36.172 27.538  2.471   1.00 13.70  ? 378  PHE   A N   1 
ATOM   2690 C  CA  . PHE   A 1 378 ? 35.407 27.052  1.347   1.00 14.26  ? 378  PHE   A CA  1 
ATOM   2691 C  C   . PHE   A 1 378 ? 33.927 27.111  1.575   1.00 13.83  ? 378  PHE   A C   1 
ATOM   2692 O  O   . PHE   A 1 378 ? 33.202 27.502  0.679   1.00 13.87  ? 378  PHE   A O   1 
ATOM   2693 C  CB  . PHE   A 1 378 ? 35.799 25.621  0.937   1.00 14.76  ? 378  PHE   A CB  1 
ATOM   2694 C  CG  . PHE   A 1 378 ? 36.701 25.594  -0.264  1.00 15.93  ? 378  PHE   A CG  1 
ATOM   2695 C  CD1 . PHE   A 1 378 ? 36.225 25.958  -1.515  1.00 16.84  ? 378  PHE   A CD1 1 
ATOM   2696 C  CD2 . PHE   A 1 378 ? 38.023 25.168  -0.149  1.00 17.32  ? 378  PHE   A CD2 1 
ATOM   2697 C  CE1 . PHE   A 1 378 ? 37.061 25.924  -2.636  1.00 17.95  ? 378  PHE   A CE1 1 
ATOM   2698 C  CE2 . PHE   A 1 378 ? 38.866 25.167  -1.264  1.00 18.43  ? 378  PHE   A CE2 1 
ATOM   2699 C  CZ  . PHE   A 1 378 ? 38.372 25.535  -2.494  1.00 18.15  ? 378  PHE   A CZ  1 
ATOM   2700 N  N   . ALA   A 1 379 ? 33.425 26.683  2.755   1.00 12.83  ? 379  ALA   A N   1 
ATOM   2701 C  CA  . ALA   A 1 379 ? 31.975 26.747  2.998   1.00 12.39  ? 379  ALA   A CA  1 
ATOM   2702 C  C   . ALA   A 1 379 ? 31.474 28.175  2.984   1.00 12.95  ? 379  ALA   A C   1 
ATOM   2703 O  O   . ALA   A 1 379 ? 30.400 28.466  2.408   1.00 14.02  ? 379  ALA   A O   1 
ATOM   2704 C  CB  . ALA   A 1 379 ? 31.660 26.072  4.318   1.00 13.44  ? 379  ALA   A CB  1 
ATOM   2705 N  N   . LYS   A 1 380 ? 32.279 29.097  3.560   1.00 12.27  ? 380  LYS   A N   1 
ATOM   2706 C  CA  . LYS   A 1 380 ? 31.867 30.505  3.571   1.00 12.44  ? 380  LYS   A CA  1 
ATOM   2707 C  C   . LYS   A 1 380 ? 31.850 31.042  2.130   1.00 13.72  ? 380  LYS   A C   1 
ATOM   2708 O  O   . LYS   A 1 380 ? 30.880 31.693  1.734   1.00 14.61  ? 380  LYS   A O   1 
ATOM   2709 C  CB  . LYS   A 1 380 ? 32.854 31.308  4.435   1.00 12.88  ? 380  LYS   A CB  1 
ATOM   2710 C  CG  . LYS   A 1 380 ? 32.604 32.837  4.471   1.00 15.77  ? 380  LYS   A CG  1 
ATOM   2711 C  CD  . LYS   A 1 380 ? 31.269 33.254  4.984   1.00 16.28  ? 380  LYS   A CD  1 
ATOM   2712 C  CE  . LYS   A 1 380 ? 31.068 32.705  6.375   1.00 18.57  ? 380  LYS   A CE  1 
ATOM   2713 N  NZ  . LYS   A 1 380 ? 29.676 33.081  6.887   1.00 21.76  ? 380  LYS   A NZ  1 
ATOM   2714 N  N   . PHE   A 1 381 ? 32.884 30.718  1.336   1.00 13.55  ? 381  PHE   A N   1 
ATOM   2715 C  CA  . PHE   A 1 381 ? 32.911 31.248  -0.034  1.00 13.54  ? 381  PHE   A CA  1 
ATOM   2716 C  C   . PHE   A 1 381 ? 31.792 30.629  -0.851  1.00 13.83  ? 381  PHE   A C   1 
ATOM   2717 O  O   . PHE   A 1 381 ? 31.156 31.322  -1.669  1.00 14.36  ? 381  PHE   A O   1 
ATOM   2718 C  CB  . PHE   A 1 381 ? 34.274 30.871  -0.649  1.00 13.73  ? 381  PHE   A CB  1 
ATOM   2719 C  CG  . PHE   A 1 381 ? 34.468 31.460  -2.020  1.00 16.30  ? 381  PHE   A CG  1 
ATOM   2720 C  CD1 . PHE   A 1 381 ? 34.185 32.789  -2.257  1.00 17.67  ? 381  PHE   A CD1 1 
ATOM   2721 C  CD2 . PHE   A 1 381 ? 34.897 30.670  -3.068  1.00 17.65  ? 381  PHE   A CD2 1 
ATOM   2722 C  CE1 . PHE   A 1 381 ? 34.387 33.344  -3.528  1.00 18.49  ? 381  PHE   A CE1 1 
ATOM   2723 C  CE2 . PHE   A 1 381 ? 35.118 31.230  -4.340  1.00 18.61  ? 381  PHE   A CE2 1 
ATOM   2724 C  CZ  . PHE   A 1 381 ? 34.803 32.543  -4.555  1.00 17.83  ? 381  PHE   A CZ  1 
ATOM   2725 N  N   . MET   A 1 382 ? 31.522 29.333  -0.669  1.00 13.88  ? 382  MET   A N   1 
ATOM   2726 C  CA  . MET   A 1 382 ? 30.496 28.679  -1.473  1.00 14.25  ? 382  MET   A CA  1 
ATOM   2727 C  C   . MET   A 1 382 ? 29.095 29.215  -1.163  1.00 14.60  ? 382  MET   A C   1 
ATOM   2728 O  O   . MET   A 1 382 ? 28.210 29.077  -2.023  1.00 15.21  ? 382  MET   A O   1 
ATOM   2729 C  CB  . MET   A 1 382 ? 30.508 27.146  -1.287  1.00 15.18  ? 382  MET   A CB  1 
ATOM   2730 C  CG  . MET   A 1 382 ? 31.661 26.470  -1.937  1.00 16.17  ? 382  MET   A CG  1 
ATOM   2731 S  SD  . MET   A 1 382 ? 31.848 26.806  -3.746  1.00 19.66  ? 382  MET   A SD  1 
ATOM   2732 C  CE  . MET   A 1 382 ? 30.360 26.294  -4.378  1.00 22.16  ? 382  MET   A CE  1 
ATOM   2733 N  N   . GLU   A 1 383 ? 28.886 29.876  -0.021  1.00 13.94  ? 383  GLU   A N   1 
ATOM   2734 C  CA  . GLU   A 1 383 ? 27.566 30.532  0.216   1.00 14.27  ? 383  GLU   A CA  1 
ATOM   2735 C  C   . GLU   A 1 383 ? 27.310 31.540  -0.912  1.00 15.83  ? 383  GLU   A C   1 
ATOM   2736 O  O   . GLU   A 1 383 ? 26.190 31.631  -1.421  1.00 17.32  ? 383  GLU   A O   1 
ATOM   2737 C  CB  . GLU   A 1 383 ? 27.576 31.400  1.471   1.00 14.96  ? 383  GLU   A CB  1 
ATOM   2738 C  CG  . GLU   A 1 383 ? 27.762 30.651  2.768   1.00 13.78  ? 383  GLU   A CG  1 
ATOM   2739 C  CD  . GLU   A 1 383 ? 27.918 31.578  3.947   1.00 15.40  ? 383  GLU   A CD  1 
ATOM   2740 O  OE1 . GLU   A 1 383 ? 27.407 32.723  3.913   1.00 16.44  ? 383  GLU   A OE1 1 
ATOM   2741 O  OE2 . GLU   A 1 383 ? 28.520 31.138  4.948   1.00 15.65  ? 383  GLU   A OE2 1 
ATOM   2742 N  N   . PHE   A 1 384 ? 28.331 32.297  -1.273  1.00 15.50  ? 384  PHE   A N   1 
ATOM   2743 C  CA  A PHE   A 1 384 ? 28.164 33.330  -2.292  0.50 14.71  ? 384  PHE   A CA  1 
ATOM   2744 C  CA  B PHE   A 1 384 ? 28.288 33.365  -2.287  0.50 17.28  ? 384  PHE   A CA  1 
ATOM   2745 C  C   . PHE   A 1 384 ? 28.142 32.765  -3.673  1.00 16.82  ? 384  PHE   A C   1 
ATOM   2746 O  O   . PHE   A 1 384 ? 27.305 33.190  -4.487  1.00 17.08  ? 384  PHE   A O   1 
ATOM   2747 C  CB  A PHE   A 1 384 ? 29.260 34.365  -2.142  0.50 12.17  ? 384  PHE   A CB  1 
ATOM   2748 C  CB  B PHE   A 1 384 ? 29.613 34.190  -2.177  0.50 18.49  ? 384  PHE   A CB  1 
ATOM   2749 C  CG  A PHE   A 1 384 ? 29.132 35.080  -0.824  0.50 9.71   ? 384  PHE   A CG  1 
ATOM   2750 C  CG  B PHE   A 1 384 ? 30.047 34.981  -3.392  0.50 21.20  ? 384  PHE   A CG  1 
ATOM   2751 C  CD1 A PHE   A 1 384 ? 29.620 34.510  0.353   0.50 10.22  ? 384  PHE   A CD1 1 
ATOM   2752 C  CD1 B PHE   A 1 384 ? 29.419 36.152  -3.730  0.50 22.72  ? 384  PHE   A CD1 1 
ATOM   2753 C  CD2 A PHE   A 1 384 ? 28.481 36.306  -0.738  0.50 9.80   ? 384  PHE   A CD2 1 
ATOM   2754 C  CD2 B PHE   A 1 384 ? 31.037 34.502  -4.241  0.50 23.56  ? 384  PHE   A CD2 1 
ATOM   2755 C  CE1 A PHE   A 1 384 ? 29.516 35.188  1.562   0.50 9.13   ? 384  PHE   A CE1 1 
ATOM   2756 C  CE1 B PHE   A 1 384 ? 29.824 36.872  -4.847  0.50 23.91  ? 384  PHE   A CE1 1 
ATOM   2757 C  CE2 A PHE   A 1 384 ? 28.341 36.947  0.484   0.50 10.01  ? 384  PHE   A CE2 1 
ATOM   2758 C  CE2 B PHE   A 1 384 ? 31.419 35.218  -5.360  0.50 24.46  ? 384  PHE   A CE2 1 
ATOM   2759 C  CZ  A PHE   A 1 384 ? 28.846 36.386  1.621   0.50 9.32   ? 384  PHE   A CZ  1 
ATOM   2760 C  CZ  B PHE   A 1 384 ? 30.780 36.380  -5.679  0.50 24.16  ? 384  PHE   A CZ  1 
ATOM   2761 N  N   . VAL   A 1 385 ? 28.960 31.745  -3.960  1.00 15.38  ? 385  VAL   A N   1 
ATOM   2762 C  CA  . VAL   A 1 385 ? 28.933 31.131  -5.287  1.00 15.91  ? 385  VAL   A CA  1 
ATOM   2763 C  C   . VAL   A 1 385 ? 27.563 30.523  -5.560  1.00 16.70  ? 385  VAL   A C   1 
ATOM   2764 O  O   . VAL   A 1 385 ? 26.990 30.730  -6.634  1.00 18.87  ? 385  VAL   A O   1 
ATOM   2765 C  CB  . VAL   A 1 385 ? 30.069 30.082  -5.430  1.00 17.72  ? 385  VAL   A CB  1 
ATOM   2766 C  CG1 . VAL   A 1 385 ? 29.938 29.302  -6.749  1.00 18.99  ? 385  VAL   A CG1 1 
ATOM   2767 C  CG2 . VAL   A 1 385 ? 31.439 30.740  -5.338  1.00 18.82  ? 385  VAL   A CG2 1 
ATOM   2768 N  N   . SER   A 1 386 ? 26.990 29.830  -4.568  1.00 15.27  ? 386  SER   A N   1 
ATOM   2769 C  CA  . SER   A 1 386 ? 25.737 29.159  -4.748  1.00 14.96  ? 386  SER   A CA  1 
ATOM   2770 C  C   . SER   A 1 386 ? 24.531 30.067  -4.733  1.00 16.21  ? 386  SER   A C   1 
ATOM   2771 O  O   . SER   A 1 386 ? 23.710 30.008  -5.648  1.00 17.12  ? 386  SER   A O   1 
ATOM   2772 C  CB  . SER   A 1 386 ? 25.526 28.051  -3.707  1.00 15.01  ? 386  SER   A CB  1 
ATOM   2773 O  OG  . SER   A 1 386 ? 25.465 28.586  -2.391  1.00 14.66  ? 386  SER   A OG  1 
ATOM   2774 N  N   . VAL   A 1 387 ? 24.416 30.903  -3.681  1.00 15.78  ? 387  VAL   A N   1 
ATOM   2775 C  CA  . VAL   A 1 387 ? 23.208 31.726  -3.548  1.00 15.24  ? 387  VAL   A CA  1 
ATOM   2776 C  C   . VAL   A 1 387 ? 23.141 32.761  -4.676  1.00 16.88  ? 387  VAL   A C   1 
ATOM   2777 O  O   . VAL   A 1 387 ? 22.018 33.129  -5.089  1.00 17.14  ? 387  VAL   A O   1 
ATOM   2778 C  CB  . VAL   A 1 387 ? 23.141 32.297  -2.129  1.00 14.94  ? 387  VAL   A CB  1 
ATOM   2779 C  CG1 . VAL   A 1 387 ? 21.933 33.229  -1.969  1.00 16.84  ? 387  VAL   A CG1 1 
ATOM   2780 C  CG2 . VAL   A 1 387 ? 23.015 31.136  -1.137  1.00 15.94  ? 387  VAL   A CG2 1 
ATOM   2781 N  N   . SER   A 1 388 ? 24.294 33.177  -5.244  1.00 16.63  ? 388  SER   A N   1 
ATOM   2782 C  CA  A SER   A 1 388 ? 24.300 34.088  -6.401  0.50 17.48  ? 388  SER   A CA  1 
ATOM   2783 C  CA  B SER   A 1 388 ? 24.231 34.118  -6.367  0.50 17.63  ? 388  SER   A CA  1 
ATOM   2784 C  C   . SER   A 1 388 ? 23.509 33.510  -7.561  1.00 19.36  ? 388  SER   A C   1 
ATOM   2785 O  O   . SER   A 1 388 ? 22.933 34.277  -8.346  1.00 20.16  ? 388  SER   A O   1 
ATOM   2786 C  CB  A SER   A 1 388 ? 25.725 34.360  -6.867  0.50 17.31  ? 388  SER   A CB  1 
ATOM   2787 C  CB  B SER   A 1 388 ? 25.605 34.646  -6.733  0.50 17.78  ? 388  SER   A CB  1 
ATOM   2788 O  OG  A SER   A 1 388 ? 26.425 35.188  -5.953  0.50 18.62  ? 388  SER   A OG  1 
ATOM   2789 O  OG  B SER   A 1 388 ? 26.444 33.562  -7.075  0.50 19.14  ? 388  SER   A OG  1 
ATOM   2790 N  N   . VAL   A 1 389 ? 23.483 32.170  -7.689  1.00 18.51  ? 389  VAL   A N   1 
ATOM   2791 C  CA  . VAL   A 1 389 ? 22.751 31.464  -8.723  1.00 19.09  ? 389  VAL   A CA  1 
ATOM   2792 C  C   . VAL   A 1 389 ? 21.355 31.061  -8.261  1.00 20.57  ? 389  VAL   A C   1 
ATOM   2793 O  O   . VAL   A 1 389 ? 20.386 31.177  -9.029  1.00 22.72  ? 389  VAL   A O   1 
ATOM   2794 C  CB  . VAL   A 1 389 ? 23.540 30.192  -9.165  1.00 20.54  ? 389  VAL   A CB  1 
ATOM   2795 C  CG1 . VAL   A 1 389 ? 22.714 29.340  -10.150 1.00 21.59  ? 389  VAL   A CG1 1 
ATOM   2796 C  CG2 . VAL   A 1 389 ? 24.895 30.543  -9.748  1.00 21.00  ? 389  VAL   A CG2 1 
ATOM   2797 N  N   . THR   A 1 390 ? 21.222 30.496  -7.044  1.00 18.87  ? 390  THR   A N   1 
ATOM   2798 C  CA  . THR   A 1 390 ? 19.928 29.972  -6.619  1.00 19.13  ? 390  THR   A CA  1 
ATOM   2799 C  C   . THR   A 1 390 ? 18.911 31.030  -6.246  1.00 20.74  ? 390  THR   A C   1 
ATOM   2800 O  O   . THR   A 1 390 ? 17.711 30.811  -6.404  1.00 21.75  ? 390  THR   A O   1 
ATOM   2801 C  CB  . THR   A 1 390 ? 20.096 28.987  -5.478  1.00 18.58  ? 390  THR   A CB  1 
ATOM   2802 O  OG1 . THR   A 1 390 ? 20.657 29.685  -4.375  1.00 18.43  ? 390  THR   A OG1 1 
ATOM   2803 C  CG2 . THR   A 1 390 ? 20.982 27.788  -5.849  1.00 18.48  ? 390  THR   A CG2 1 
ATOM   2804 N  N   . HIS   A 1 391 ? 19.375 32.122  -5.652  1.00 20.10  ? 391  HIS   A N   1 
ATOM   2805 C  CA  . HIS   A 1 391 ? 18.461 33.174  -5.169  1.00 20.17  ? 391  HIS   A CA  1 
ATOM   2806 C  C   . HIS   A 1 391 ? 19.001 34.495  -5.701  1.00 21.39  ? 391  HIS   A C   1 
ATOM   2807 O  O   . HIS   A 1 391 ? 19.469 35.345  -4.917  1.00 22.16  ? 391  HIS   A O   1 
ATOM   2808 C  CB  . HIS   A 1 391 ? 18.386 33.146  -3.616  1.00 20.42  ? 391  HIS   A CB  1 
ATOM   2809 C  CG  . HIS   A 1 391 ? 17.776 31.905  -3.048  1.00 20.64  ? 391  HIS   A CG  1 
ATOM   2810 N  ND1 . HIS   A 1 391 ? 18.487 30.701  -2.971  1.00 20.26  ? 391  HIS   A ND1 1 
ATOM   2811 C  CD2 . HIS   A 1 391 ? 16.565 31.724  -2.478  1.00 21.82  ? 391  HIS   A CD2 1 
ATOM   2812 C  CE1 . HIS   A 1 391 ? 17.666 29.837  -2.410  1.00 21.10  ? 391  HIS   A CE1 1 
ATOM   2813 N  NE2 . HIS   A 1 391 ? 16.499 30.415  -2.078  1.00 22.23  ? 391  HIS   A NE2 1 
ATOM   2814 N  N   . PRO   A 1 392 ? 18.931 34.701  -7.032  1.00 22.48  ? 392  PRO   A N   1 
ATOM   2815 C  CA  . PRO   A 1 392 ? 19.536 35.904  -7.611  1.00 23.30  ? 392  PRO   A CA  1 
ATOM   2816 C  C   . PRO   A 1 392 ? 18.921 37.212  -7.115  1.00 24.35  ? 392  PRO   A C   1 
ATOM   2817 O  O   . PRO   A 1 392 ? 19.634 38.219  -7.101  1.00 26.07  ? 392  PRO   A O   1 
ATOM   2818 C  CB  . PRO   A 1 392 ? 19.373 35.713  -9.124  1.00 24.81  ? 392  PRO   A CB  1 
ATOM   2819 C  CG  . PRO   A 1 392 ? 18.280 34.700  -9.278  1.00 25.57  ? 392  PRO   A CG  1 
ATOM   2820 C  CD  . PRO   A 1 392 ? 18.378 33.803  -8.072  1.00 22.82  ? 392  PRO   A CD  1 
ATOM   2821 N  N   . GLU   A 1 393 ? 17.675 37.174  -6.592  1.00 24.12  ? 393  GLU   A N   1 
ATOM   2822 C  CA  . GLU   A 1 393 ? 16.991 38.356  -6.043  1.00 25.94  ? 393  GLU   A CA  1 
ATOM   2823 C  C   . GLU   A 1 393 ? 17.710 38.915  -4.802  1.00 25.65  ? 393  GLU   A C   1 
ATOM   2824 O  O   . GLU   A 1 393 ? 17.539 40.093  -4.469  1.00 26.97  ? 393  GLU   A O   1 
ATOM   2825 C  CB  . GLU   A 1 393 ? 15.511 38.032  -5.698  1.00 29.17  ? 393  GLU   A CB  1 
ATOM   2826 C  CG  . GLU   A 1 393 ? 15.318 37.155  -4.464  1.00 32.55  ? 393  GLU   A CG  1 
ATOM   2827 C  CD  . GLU   A 1 393 ? 15.403 35.644  -4.611  1.00 32.79  ? 393  GLU   A CD  1 
ATOM   2828 O  OE1 . GLU   A 1 393 ? 15.731 35.150  -5.717  1.00 27.71  ? 393  GLU   A OE1 1 
ATOM   2829 O  OE2 . GLU   A 1 393 ? 15.108 34.947  -3.610  1.00 36.15  ? 393  GLU   A OE2 1 
ATOM   2830 N  N   . LEU   A 1 394 ? 18.510 38.083  -4.103  1.00 23.50  ? 394  LEU   A N   1 
ATOM   2831 C  CA  . LEU   A 1 394 ? 19.221 38.557  -2.903  1.00 22.02  ? 394  LEU   A CA  1 
ATOM   2832 C  C   . LEU   A 1 394 ? 20.488 39.330  -3.282  1.00 23.07  ? 394  LEU   A C   1 
ATOM   2833 O  O   . LEU   A 1 394 ? 21.036 39.987  -2.388  1.00 24.82  ? 394  LEU   A O   1 
ATOM   2834 C  CB  . LEU   A 1 394 ? 19.554 37.377  -1.975  1.00 21.47  ? 394  LEU   A CB  1 
ATOM   2835 C  CG  . LEU   A 1 394 ? 18.357 36.555  -1.458  1.00 22.69  ? 394  LEU   A CG  1 
ATOM   2836 C  CD1 . LEU   A 1 394 ? 18.827 35.355  -0.637  1.00 22.31  ? 394  LEU   A CD1 1 
ATOM   2837 C  CD2 . LEU   A 1 394 ? 17.431 37.414  -0.583  1.00 23.66  ? 394  LEU   A CD2 1 
ATOM   2838 N  N   . LYS   A 1 395 ? 20.986 39.243  -4.534  1.00 22.48  ? 395  LYS   A N   1 
ATOM   2839 C  CA  . LYS   A 1 395 ? 22.205 39.932  -4.994  1.00 23.00  ? 395  LYS   A CA  1 
ATOM   2840 C  C   . LYS   A 1 395 ? 23.367 39.752  -3.972  1.00 22.76  ? 395  LYS   A C   1 
ATOM   2841 O  O   . LYS   A 1 395 ? 24.003 40.737  -3.585  1.00 23.92  ? 395  LYS   A O   1 
ATOM   2842 C  CB  . LYS   A 1 395 ? 21.922 41.430  -5.241  1.00 26.26  ? 395  LYS   A CB  1 
ATOM   2843 C  CG  . LYS   A 1 395 ? 20.756 41.699  -6.183  1.00 31.24  ? 395  LYS   A CG  1 
ATOM   2844 C  CD  . LYS   A 1 395 ? 21.114 41.300  -7.578  1.00 39.41  ? 395  LYS   A CD  1 
ATOM   2845 C  CE  . LYS   A 1 395 ? 20.157 41.888  -8.594  1.00 46.26  ? 395  LYS   A CE  1 
ATOM   2846 N  NZ  . LYS   A 1 395 ? 20.305 43.370  -8.680  1.00 50.14  ? 395  LYS   A NZ  1 
ATOM   2847 N  N   . VAL   A 1 396 ? 23.583 38.508  -3.476  1.00 21.27  ? 396  VAL   A N   1 
ATOM   2848 C  CA  . VAL   A 1 396 ? 24.542 38.291  -2.381  1.00 21.38  ? 396  VAL   A CA  1 
ATOM   2849 C  C   . VAL   A 1 396 ? 25.974 38.559  -2.752  1.00 21.63  ? 396  VAL   A C   1 
ATOM   2850 O  O   . VAL   A 1 396 ? 26.743 38.917  -1.868  1.00 21.07  ? 396  VAL   A O   1 
ATOM   2851 C  CB  . VAL   A 1 396 ? 24.438 36.918  -1.693  1.00 21.43  ? 396  VAL   A CB  1 
ATOM   2852 C  CG1 . VAL   A 1 396 ? 23.041 36.682  -1.170  1.00 21.09  ? 396  VAL   A CG1 1 
ATOM   2853 C  CG2 . VAL   A 1 396 ? 24.869 35.792  -2.634  1.00 22.12  ? 396  VAL   A CG2 1 
ATOM   2854 N  N   . GLY   A 1 397 ? 26.332 38.442  -4.034  1.00 20.56  ? 397  GLY   A N   1 
ATOM   2855 C  CA  . GLY   A 1 397 ? 27.701 38.764  -4.450  1.00 21.51  ? 397  GLY   A CA  1 
ATOM   2856 C  C   . GLY   A 1 397 ? 28.083 40.192  -4.107  1.00 22.91  ? 397  GLY   A C   1 
ATOM   2857 O  O   . GLY   A 1 397 ? 29.260 40.480  -3.852  1.00 24.96  ? 397  GLY   A O   1 
ATOM   2858 N  N   . ASP   A 1 398 ? 27.078 41.080  -4.010  1.00 22.21  ? 398  ASP   A N   1 
ATOM   2859 C  CA  . ASP   A 1 398 ? 27.276 42.490  -3.672  1.00 22.31  ? 398  ASP   A CA  1 
ATOM   2860 C  C   . ASP   A 1 398 ? 27.824 42.683  -2.263  1.00 20.72  ? 398  ASP   A C   1 
ATOM   2861 O  O   . ASP   A 1 398 ? 28.443 43.718  -1.964  1.00 21.05  ? 398  ASP   A O   1 
ATOM   2862 C  CB  . ASP   A 1 398 ? 25.952 43.291  -3.711  1.00 24.24  ? 398  ASP   A CB  1 
ATOM   2863 C  CG  . ASP   A 1 398 ? 25.397 43.558  -5.105  1.00 30.66  ? 398  ASP   A CG  1 
ATOM   2864 O  OD1 . ASP   A 1 398 ? 26.059 43.163  -6.094  1.00 30.60  ? 398  ASP   A OD1 1 
ATOM   2865 O  OD2 . ASP   A 1 398 ? 24.301 44.181  -5.204  1.00 32.09  ? 398  ASP   A OD2 1 
ATOM   2866 N  N   . TYR   A 1 399 ? 27.542 41.725  -1.367  1.00 19.35  ? 399  TYR   A N   1 
ATOM   2867 C  CA  . TYR   A 1 399 ? 27.918 41.797  0.046   1.00 19.32  ? 399  TYR   A CA  1 
ATOM   2868 C  C   . TYR   A 1 399 ? 29.187 41.118  0.381   1.00 19.54  ? 399  TYR   A C   1 
ATOM   2869 O  O   . TYR   A 1 399 ? 29.705 41.319  1.502   1.00 20.42  ? 399  TYR   A O   1 
ATOM   2870 C  CB  . TYR   A 1 399 ? 26.822 41.128  0.920   1.00 20.29  ? 399  TYR   A CB  1 
ATOM   2871 C  CG  . TYR   A 1 399 ? 25.437 41.672  0.671   1.00 21.94  ? 399  TYR   A CG  1 
ATOM   2872 C  CD1 . TYR   A 1 399 ? 25.208 43.029  0.640   1.00 24.32  ? 399  TYR   A CD1 1 
ATOM   2873 C  CD2 . TYR   A 1 399 ? 24.360 40.821  0.460   1.00 23.24  ? 399  TYR   A CD2 1 
ATOM   2874 C  CE1 . TYR   A 1 399 ? 23.961 43.543  0.323   1.00 25.86  ? 399  TYR   A CE1 1 
ATOM   2875 C  CE2 . TYR   A 1 399 ? 23.109 41.322  0.125   1.00 25.06  ? 399  TYR   A CE2 1 
ATOM   2876 C  CZ  . TYR   A 1 399 ? 22.912 42.686  0.094   1.00 26.85  ? 399  TYR   A CZ  1 
ATOM   2877 O  OH  . TYR   A 1 399 ? 21.673 43.257  -0.138  1.00 31.28  ? 399  TYR   A OH  1 
ATOM   2878 N  N   . PHE   A 1 400 ? 29.744 40.328  -0.537  1.00 19.03  ? 400  PHE   A N   1 
ATOM   2879 C  CA  . PHE   A 1 400 ? 30.897 39.486  -0.184  1.00 18.23  ? 400  PHE   A CA  1 
ATOM   2880 C  C   . PHE   A 1 400 ? 32.069 40.246  0.372   1.00 17.98  ? 400  PHE   A C   1 
ATOM   2881 O  O   . PHE   A 1 400 ? 32.705 39.825  1.378   1.00 18.70  ? 400  PHE   A O   1 
ATOM   2882 C  CB  . PHE   A 1 400 ? 31.304 38.631  -1.381  1.00 18.13  ? 400  PHE   A CB  1 
ATOM   2883 C  CG  . PHE   A 1 400 ? 32.455 37.724  -1.029  1.00 19.52  ? 400  PHE   A CG  1 
ATOM   2884 C  CD1 . PHE   A 1 400 ? 32.267 36.631  -0.208  1.00 21.12  ? 400  PHE   A CD1 1 
ATOM   2885 C  CD2 . PHE   A 1 400 ? 33.747 38.028  -1.431  1.00 20.25  ? 400  PHE   A CD2 1 
ATOM   2886 C  CE1 . PHE   A 1 400 ? 33.342 35.812  0.145   1.00 21.73  ? 400  PHE   A CE1 1 
ATOM   2887 C  CE2 . PHE   A 1 400 ? 34.808 37.204  -1.080  1.00 20.45  ? 400  PHE   A CE2 1 
ATOM   2888 C  CZ  . PHE   A 1 400 ? 34.601 36.115  -0.292  1.00 19.84  ? 400  PHE   A CZ  1 
ATOM   2889 N  N   . PHE   A 1 401 ? 32.401 41.348  -0.265  1.00 18.50  ? 401  PHE   A N   1 
ATOM   2890 C  CA  . PHE   A 1 401 ? 33.579 42.103  0.160   1.00 18.35  ? 401  PHE   A CA  1 
ATOM   2891 C  C   . PHE   A 1 401 ? 33.539 42.494  1.615   1.00 17.35  ? 401  PHE   A C   1 
ATOM   2892 O  O   . PHE   A 1 401 ? 34.573 42.675  2.205   1.00 16.79  ? 401  PHE   A O   1 
ATOM   2893 C  CB  . PHE   A 1 401 ? 33.833 43.312  -0.734  1.00 18.49  ? 401  PHE   A CB  1 
ATOM   2894 C  CG  . PHE   A 1 401 ? 32.990 44.504  -0.357  1.00 18.24  ? 401  PHE   A CG  1 
ATOM   2895 C  CD1 . PHE   A 1 401 ? 31.687 44.608  -0.788  1.00 19.99  ? 401  PHE   A CD1 1 
ATOM   2896 C  CD2 . PHE   A 1 401 ? 33.468 45.453  0.526   1.00 19.21  ? 401  PHE   A CD2 1 
ATOM   2897 C  CE1 . PHE   A 1 401 ? 30.887 45.680  -0.403  1.00 20.88  ? 401  PHE   A CE1 1 
ATOM   2898 C  CE2 . PHE   A 1 401 ? 32.680 46.535  0.902   1.00 20.57  ? 401  PHE   A CE2 1 
ATOM   2899 C  CZ  . PHE   A 1 401 ? 31.383 46.621  0.468   1.00 21.07  ? 401  PHE   A CZ  1 
ATOM   2900 N  N   . GLY   A 1 402 ? 32.329 42.678  2.179   1.00 16.50  ? 402  GLY   A N   1 
ATOM   2901 C  CA  . GLY   A 1 402 ? 32.248 43.098  3.574   1.00 16.85  ? 402  GLY   A CA  1 
ATOM   2902 C  C   . GLY   A 1 402 ? 32.864 42.075  4.513   1.00 16.63  ? 402  GLY   A C   1 
ATOM   2903 O  O   . GLY   A 1 402 ? 33.390 42.438  5.572   1.00 19.48  ? 402  GLY   A O   1 
ATOM   2904 N  N   . LYS   A 1 403 ? 32.825 40.814  4.129   1.00 16.36  ? 403  LYS   A N   1 
ATOM   2905 C  CA  . LYS   A 1 403 ? 33.444 39.732  4.938   1.00 17.35  ? 403  LYS   A CA  1 
ATOM   2906 C  C   . LYS   A 1 403 ? 34.969 39.923  4.934   1.00 18.05  ? 403  LYS   A C   1 
ATOM   2907 O  O   . LYS   A 1 403 ? 35.648 39.658  5.946   1.00 17.45  ? 403  LYS   A O   1 
ATOM   2908 C  CB  . LYS   A 1 403 ? 33.080 38.367  4.341   1.00 21.10  ? 403  LYS   A CB  1 
ATOM   2909 C  CG  . LYS   A 1 403 ? 31.583 38.046  4.370   1.00 24.72  ? 403  LYS   A CG  1 
ATOM   2910 C  CD  . LYS   A 1 403 ? 30.958 38.223  5.749   1.00 31.04  ? 403  LYS   A CD  1 
ATOM   2911 C  CE  . LYS   A 1 403 ? 29.501 37.808  5.729   1.00 37.52  ? 403  LYS   A CE  1 
ATOM   2912 N  NZ  . LYS   A 1 403 ? 28.866 37.985  7.059   1.00 40.97  ? 403  LYS   A NZ  1 
ATOM   2913 N  N   . CYS   A 1 404 ? 35.519 40.373  3.815   1.00 17.23  ? 404  CYS   A N   1 
ATOM   2914 C  CA  . CYS   A 1 404 ? 36.949 40.653  3.717   1.00 16.27  ? 404  CYS   A CA  1 
ATOM   2915 C  C   . CYS   A 1 404 ? 37.341 41.818  4.564   1.00 15.91  ? 404  CYS   A C   1 
ATOM   2916 O  O   . CYS   A 1 404 ? 38.379 41.743  5.199   1.00 17.14  ? 404  CYS   A O   1 
ATOM   2917 C  CB  . CYS   A 1 404 ? 37.347 40.854  2.269   1.00 16.08  ? 404  CYS   A CB  1 
ATOM   2918 S  SG  . CYS   A 1 404 ? 36.718 39.542  1.182   1.00 19.24  ? 404  CYS   A SG  1 
ATOM   2919 N  N   . PHE   A 1 405 ? 36.518 42.863  4.650   1.00 15.93  ? 405  PHE   A N   1 
ATOM   2920 C  CA  . PHE   A 1 405 ? 36.831 43.949  5.565   1.00 16.70  ? 405  PHE   A CA  1 
ATOM   2921 C  C   . PHE   A 1 405 ? 36.698 43.498  7.032   1.00 18.11  ? 405  PHE   A C   1 
ATOM   2922 O  O   . PHE   A 1 405 ? 37.515 43.920  7.868   1.00 19.87  ? 405  PHE   A O   1 
ATOM   2923 C  CB  . PHE   A 1 405 ? 35.951 45.159  5.266   1.00 17.62  ? 405  PHE   A CB  1 
ATOM   2924 C  CG  . PHE   A 1 405 ? 36.405 45.890  4.030   1.00 18.78  ? 405  PHE   A CG  1 
ATOM   2925 C  CD1 . PHE   A 1 405 ? 37.744 45.897  3.656   1.00 20.33  ? 405  PHE   A CD1 1 
ATOM   2926 C  CD2 . PHE   A 1 405 ? 35.522 46.653  3.315   1.00 20.25  ? 405  PHE   A CD2 1 
ATOM   2927 C  CE1 . PHE   A 1 405 ? 38.181 46.652  2.589   1.00 21.37  ? 405  PHE   A CE1 1 
ATOM   2928 C  CE2 . PHE   A 1 405 ? 35.952 47.378  2.198   1.00 21.13  ? 405  PHE   A CE2 1 
ATOM   2929 C  CZ  . PHE   A 1 405 ? 37.267 47.361  1.842   1.00 20.70  ? 405  PHE   A CZ  1 
ATOM   2930 N  N   . ASP   A 1 406 ? 35.788 42.522  7.317   1.00 18.42  ? 406  ASP   A N   1 
ATOM   2931 C  CA  . ASP   A 1 406 ? 35.737 41.963  8.699   1.00 19.29  ? 406  ASP   A CA  1 
ATOM   2932 C  C   . ASP   A 1 406 ? 37.063 41.258  9.015   1.00 19.77  ? 406  ASP   A C   1 
ATOM   2933 O  O   . ASP   A 1 406 ? 37.624 41.405  10.113  1.00 21.08  ? 406  ASP   A O   1 
ATOM   2934 C  CB  . ASP   A 1 406 ? 34.588 40.946  8.860   1.00 20.15  ? 406  ASP   A CB  1 
ATOM   2935 C  CG  . ASP   A 1 406 ? 33.184 41.544  8.857   1.00 27.29  ? 406  ASP   A CG  1 
ATOM   2936 O  OD1 . ASP   A 1 406 ? 33.069 42.788  8.962   1.00 27.08  ? 406  ASP   A OD1 1 
ATOM   2937 O  OD2 . ASP   A 1 406 ? 32.204 40.761  8.721   1.00 29.80  ? 406  ASP   A OD2 1 
ATOM   2938 N  N   . ALA   A 1 407 ? 37.564 40.461  8.071   1.00 18.22  ? 407  ALA   A N   1 
ATOM   2939 C  CA  . ALA   A 1 407 ? 38.832 39.752  8.310   1.00 18.10  ? 407  ALA   A CA  1 
ATOM   2940 C  C   . ALA   A 1 407 ? 39.989 40.771  8.457   1.00 17.96  ? 407  ALA   A C   1 
ATOM   2941 O  O   . ALA   A 1 407 ? 40.862 40.596  9.301   1.00 17.08  ? 407  ALA   A O   1 
ATOM   2942 C  CB  . ALA   A 1 407 ? 39.117 38.808  7.174   1.00 18.99  ? 407  ALA   A CB  1 
ATOM   2943 N  N   . MET   A 1 408 ? 40.000 41.836  7.643   1.00 16.78  ? 408  MET   A N   1 
ATOM   2944 C  CA  . MET   A 1 408 ? 41.102 42.809  7.723   1.00 15.71  ? 408  MET   A CA  1 
ATOM   2945 C  C   . MET   A 1 408 ? 41.186 43.524  9.028   1.00 18.91  ? 408  MET   A C   1 
ATOM   2946 O  O   . MET   A 1 408 ? 42.286 43.924  9.412   1.00 20.22  ? 408  MET   A O   1 
ATOM   2947 C  CB  . MET   A 1 408 ? 41.031 43.817  6.597   1.00 15.18  ? 408  MET   A CB  1 
ATOM   2948 C  CG  . MET   A 1 408 ? 41.347 43.208  5.307   1.00 15.15  ? 408  MET   A CG  1 
ATOM   2949 S  SD  . MET   A 1 408 ? 41.192 44.529  4.046   1.00 21.87  ? 408  MET   A SD  1 
ATOM   2950 C  CE  . MET   A 1 408 ? 42.194 43.846  2.906   1.00 19.92  ? 408  MET   A CE  1 
ATOM   2951 N  N   . GLU   A 1 409 ? 40.038 43.652  9.745   1.00 19.67  ? 409  GLU   A N   1 
ATOM   2952 C  CA  . GLU   A 1 409 ? 40.063 44.309  11.054  1.00 23.14  ? 409  GLU   A CA  1 
ATOM   2953 C  C   . GLU   A 1 409 ? 40.926 43.542  12.018  1.00 24.35  ? 409  GLU   A C   1 
ATOM   2954 O  O   . GLU   A 1 409 ? 41.821 44.139  12.612  1.00 26.89  ? 409  GLU   A O   1 
ATOM   2955 C  CB  . GLU   A 1 409 ? 38.650 44.459  11.642  1.00 26.77  ? 409  GLU   A CB  1 
ATOM   2956 C  CG  . GLU   A 1 409 ? 38.566 45.624  12.617  1.00 37.68  ? 409  GLU   A CG  1 
ATOM   2957 C  CD  . GLU   A 1 409 ? 38.694 46.979  11.940  1.00 49.11  ? 409  GLU   A CD  1 
ATOM   2958 O  OE1 . GLU   A 1 409 ? 38.456 47.071  10.711  1.00 51.93  ? 409  GLU   A OE1 1 
ATOM   2959 O  OE2 . GLU   A 1 409 ? 39.026 47.956  12.646  1.00 54.27  ? 409  GLU   A OE2 1 
ATOM   2960 N  N   . VAL   A 1 410 ? 40.748 42.237  12.054  1.00 23.64  ? 410  VAL   A N   1 
ATOM   2961 C  CA  . VAL   A 1 410 ? 41.510 41.368  12.920  1.00 23.61  ? 410  VAL   A CA  1 
ATOM   2962 C  C   . VAL   A 1 410 ? 42.964 41.205  12.397  1.00 19.71  ? 410  VAL   A C   1 
ATOM   2963 O  O   . VAL   A 1 410 ? 43.960 41.247  13.135  1.00 17.84  ? 410  VAL   A O   1 
ATOM   2964 C  CB  . VAL   A 1 410 ? 40.770 40.005  13.160  1.00 27.19  ? 410  VAL   A CB  1 
ATOM   2965 C  CG1 . VAL   A 1 410 ? 39.290 40.226  13.452  1.00 30.24  ? 410  VAL   A CG1 1 
ATOM   2966 C  CG2 . VAL   A 1 410 ? 40.897 39.040  12.005  1.00 27.86  ? 410  VAL   A CG2 1 
ATOM   2967 N  N   . ASP   A 1 411 ? 43.076 41.070  11.066  1.00 15.82  ? 411  ASP   A N   1 
ATOM   2968 C  CA  . ASP   A 1 411 ? 44.334 40.709  10.451  1.00 15.49  ? 411  ASP   A CA  1 
ATOM   2969 C  C   . ASP   A 1 411 ? 45.333 41.841  10.300  1.00 17.16  ? 411  ASP   A C   1 
ATOM   2970 O  O   . ASP   A 1 411 ? 46.487 41.600  9.941   1.00 19.16  ? 411  ASP   A O   1 
ATOM   2971 C  CB  . ASP   A 1 411 ? 43.987 40.088  9.108   1.00 15.35  ? 411  ASP   A CB  1 
ATOM   2972 C  CG  . ASP   A 1 411 ? 44.968 39.094  8.558   1.00 16.16  ? 411  ASP   A CG  1 
ATOM   2973 O  OD1 . ASP   A 1 411 ? 45.712 38.460  9.366   1.00 15.72  ? 411  ASP   A OD1 1 
ATOM   2974 O  OD2 . ASP   A 1 411 ? 45.007 38.943  7.323   1.00 15.18  ? 411  ASP   A OD2 1 
ATOM   2975 N  N   . ALA   A 1 412 ? 44.934 43.058  10.637  1.00 16.42  ? 412  ALA   A N   1 
ATOM   2976 C  CA  . ALA   A 1 412 ? 45.842 44.194  10.665  1.00 17.49  ? 412  ALA   A CA  1 
ATOM   2977 C  C   . ALA   A 1 412 ? 46.630 44.270  11.959  1.00 17.71  ? 412  ALA   A C   1 
ATOM   2978 O  O   . ALA   A 1 412 ? 47.502 45.128  12.092  1.00 19.20  ? 412  ALA   A O   1 
ATOM   2979 C  CB  . ALA   A 1 412 ? 45.026 45.474  10.517  1.00 19.29  ? 412  ALA   A CB  1 
ATOM   2980 N  N   . LEU   A 1 413 ? 46.284 43.422  12.958  1.00 17.34  ? 413  LEU   A N   1 
ATOM   2981 C  CA  . LEU   A 1 413 ? 46.921 43.506  14.257  1.00 18.80  ? 413  LEU   A CA  1 
ATOM   2982 C  C   . LEU   A 1 413 ? 48.125 42.667  14.306  1.00 20.96  ? 413  LEU   A C   1 
ATOM   2983 O  O   . LEU   A 1 413 ? 48.164 41.576  13.696  1.00 21.12  ? 413  LEU   A O   1 
ATOM   2984 C  CB  . LEU   A 1 413 ? 45.917 43.090  15.324  1.00 18.23  ? 413  LEU   A CB  1 
ATOM   2985 C  CG  . LEU   A 1 413 ? 44.669 43.979  15.377  1.00 19.65  ? 413  LEU   A CG  1 
ATOM   2986 C  CD1 . LEU   A 1 413 ? 43.629 43.361  16.307  1.00 19.31  ? 413  LEU   A CD1 1 
ATOM   2987 C  CD2 . LEU   A 1 413 ? 45.033 45.423  15.755  1.00 22.43  ? 413  LEU   A CD2 1 
ATOM   2988 N  N   . GLN   A 1 414 ? 49.082 43.095  15.141  1.00 21.70  ? 414  GLN   A N   1 
ATOM   2989 C  CA  . GLN   A 1 414 ? 50.404 42.487  15.195  1.00 23.88  ? 414  GLN   A CA  1 
ATOM   2990 C  C   . GLN   A 1 414 ? 50.373 41.031  15.465  1.00 23.75  ? 414  GLN   A C   1 
ATOM   2991 O  O   . GLN   A 1 414 ? 51.215 40.316  14.907  1.00 26.04  ? 414  GLN   A O   1 
ATOM   2992 C  CB  . GLN   A 1 414 ? 51.351 43.210  16.190  1.00 26.77  ? 414  GLN   A CB  1 
ATOM   2993 C  CG  . GLN   A 1 414 ? 50.708 43.446  17.550  1.00 34.24  ? 414  GLN   A CG  1 
ATOM   2994 C  CD  . GLN   A 1 414 ? 51.443 44.214  18.647  1.00 38.76  ? 414  GLN   A CD  1 
ATOM   2995 O  OE1 . GLN   A 1 414 ? 51.647 43.698  19.775  1.00 37.02  ? 414  GLN   A OE1 1 
ATOM   2996 N  NE2 . GLN   A 1 414 ? 51.744 45.486  18.384  1.00 41.07  ? 414  GLN   A NE2 1 
ATOM   2997 N  N   . SER   A 1 415 ? 49.441 40.554  16.288  1.00 23.07  ? 415  SER   A N   1 
ATOM   2998 C  CA  . SER   A 1 415 ? 49.437 39.170  16.676  1.00 23.78  ? 415  SER   A CA  1 
ATOM   2999 C  C   . SER   A 1 415 ? 48.408 38.345  15.949  1.00 23.11  ? 415  SER   A C   1 
ATOM   3000 O  O   . SER   A 1 415 ? 48.185 37.215  16.357  1.00 23.58  ? 415  SER   A O   1 
ATOM   3001 C  CB  . SER   A 1 415 ? 49.297 39.038  18.204  1.00 24.06  ? 415  SER   A CB  1 
ATOM   3002 O  OG  . SER   A 1 415 ? 50.353 39.732  18.876  1.00 24.72  ? 415  SER   A OG  1 
ATOM   3003 N  N   . SER   A 1 416 ? 47.842 38.823  14.790  1.00 21.04  ? 416  SER   A N   1 
ATOM   3004 C  CA  . SER   A 1 416 ? 46.918 37.952  14.006  1.00 20.13  ? 416  SER   A CA  1 
ATOM   3005 C  C   . SER   A 1 416 ? 47.689 36.670  13.617  1.00 20.17  ? 416  SER   A C   1 
ATOM   3006 O  O   . SER   A 1 416 ? 48.933 36.728  13.547  1.00 23.09  ? 416  SER   A O   1 
ATOM   3007 C  CB  . SER   A 1 416 ? 46.506 38.632  12.686  1.00 18.61  ? 416  SER   A CB  1 
ATOM   3008 O  OG  . SER   A 1 416 ? 45.513 37.853  12.011  1.00 19.15  ? 416  SER   A OG  1 
ATOM   3009 N  N   . HIS   A 1 417 ? 46.999 35.583  13.315  1.00 17.14  ? 417  HIS   A N   1 
ATOM   3010 C  CA  . HIS   A 1 417 ? 47.705 34.344  12.961  1.00 16.23  ? 417  HIS   A CA  1 
ATOM   3011 C  C   . HIS   A 1 417 ? 47.555 34.063  11.474  1.00 15.83  ? 417  HIS   A C   1 
ATOM   3012 O  O   . HIS   A 1 417 ? 46.531 34.397  10.865  1.00 15.31  ? 417  HIS   A O   1 
ATOM   3013 C  CB  . HIS   A 1 417 ? 47.138 33.157  13.787  1.00 15.97  ? 417  HIS   A CB  1 
ATOM   3014 C  CG  . HIS   A 1 417 ? 45.681 32.872  13.542  1.00 15.25  ? 417  HIS   A CG  1 
ATOM   3015 N  ND1 . HIS   A 1 417 ? 45.256 32.081  12.484  1.00 15.52  ? 417  HIS   A ND1 1 
ATOM   3016 C  CD2 . HIS   A 1 417 ? 44.585 33.320  14.207  1.00 15.40  ? 417  HIS   A CD2 1 
ATOM   3017 C  CE1 . HIS   A 1 417 ? 43.927 32.044  12.555  1.00 16.83  ? 417  HIS   A CE1 1 
ATOM   3018 N  NE2 . HIS   A 1 417 ? 43.480 32.762  13.580  1.00 15.51  ? 417  HIS   A NE2 1 
ATOM   3019 N  N   . PRO   A 1 418 ? 48.503 33.331  10.896  1.00 15.35  ? 418  PRO   A N   1 
ATOM   3020 C  CA  . PRO   A 1 418 ? 48.342 32.910  9.508   1.00 14.99  ? 418  PRO   A CA  1 
ATOM   3021 C  C   . PRO   A 1 418 ? 47.104 32.020  9.355   1.00 14.49  ? 418  PRO   A C   1 
ATOM   3022 O  O   . PRO   A 1 418 ? 46.686 31.315  10.308  1.00 15.00  ? 418  PRO   A O   1 
ATOM   3023 C  CB  . PRO   A 1 418 ? 49.629 32.119  9.219   1.00 15.49  ? 418  PRO   A CB  1 
ATOM   3024 C  CG  . PRO   A 1 418 ? 50.588 32.528  10.250  1.00 17.72  ? 418  PRO   A CG  1 
ATOM   3025 C  CD  . PRO   A 1 418 ? 49.775 32.833  11.475  1.00 16.25  ? 418  PRO   A CD  1 
ATOM   3026 N  N   . VAL   A 1 419 ? 46.536 31.963  8.165   1.00 14.02  ? 419  VAL   A N   1 
ATOM   3027 C  CA  . VAL   A 1 419 ? 45.355 31.121  7.880   1.00 13.43  ? 419  VAL   A CA  1 
ATOM   3028 C  C   . VAL   A 1 419 ? 45.600 29.667  8.299   1.00 14.53  ? 419  VAL   A C   1 
ATOM   3029 O  O   . VAL   A 1 419 ? 44.722 29.034  8.910   1.00 15.00  ? 419  VAL   A O   1 
ATOM   3030 C  CB  . VAL   A 1 419 ? 44.983 31.234  6.385   1.00 14.31  ? 419  VAL   A CB  1 
ATOM   3031 C  CG1 . VAL   A 1 419 ? 43.962 30.188  6.003   1.00 16.10  ? 419  VAL   A CG1 1 
ATOM   3032 C  CG2 . VAL   A 1 419 ? 44.382 32.609  6.096   1.00 14.51  ? 419  VAL   A CG2 1 
ATOM   3033 N  N   . SER   A 1 420 ? 46.787 29.142  7.987   1.00 13.69  ? 420  SER   A N   1 
ATOM   3034 C  CA  A SER   A 1 420 ? 47.162 27.807  8.448   0.50 14.72  ? 420  SER   A CA  1 
ATOM   3035 C  CA  B SER   A 1 420 ? 47.158 27.800  8.411   0.50 15.30  ? 420  SER   A CA  1 
ATOM   3036 C  C   . SER   A 1 420 ? 48.188 27.996  9.513   1.00 16.06  ? 420  SER   A C   1 
ATOM   3037 O  O   . SER   A 1 420 ? 49.209 28.663  9.287   1.00 16.54  ? 420  SER   A O   1 
ATOM   3038 C  CB  A SER   A 1 420 ? 47.795 27.024  7.315   0.50 14.95  ? 420  SER   A CB  1 
ATOM   3039 C  CB  B SER   A 1 420 ? 47.779 27.062  7.230   0.50 17.04  ? 420  SER   A CB  1 
ATOM   3040 O  OG  A SER   A 1 420 ? 46.767 26.554  6.469   0.50 14.64  ? 420  SER   A OG  1 
ATOM   3041 O  OG  B SER   A 1 420 ? 48.293 25.794  7.594   0.50 19.24  ? 420  SER   A OG  1 
ATOM   3042 N  N   . THR   A 1 421 ? 47.921 27.497  10.739  1.00 15.69  ? 421  THR   A N   1 
ATOM   3043 C  CA  . THR   A 1 421 ? 48.847 27.705  11.856  1.00 16.06  ? 421  THR   A CA  1 
ATOM   3044 C  C   . THR   A 1 421 ? 48.692 26.544  12.825  1.00 17.04  ? 421  THR   A C   1 
ATOM   3045 O  O   . THR   A 1 421 ? 47.616 25.945  12.899  1.00 16.44  ? 421  THR   A O   1 
ATOM   3046 C  CB  . THR   A 1 421 ? 48.515 29.068  12.479  1.00 16.93  ? 421  THR   A CB  1 
ATOM   3047 O  OG1 . THR   A 1 421 ? 49.544 29.487  13.384  1.00 18.16  ? 421  THR   A OG1 1 
ATOM   3048 C  CG2 . THR   A 1 421 ? 47.144 29.081  13.170  1.00 17.63  ? 421  THR   A CG2 1 
ATOM   3049 N  N   . PRO   A 1 422 ? 49.753 26.165  13.545  1.00 16.84  ? 422  PRO   A N   1 
ATOM   3050 C  CA  . PRO   A 1 422 ? 49.662 24.979  14.399  1.00 16.72  ? 422  PRO   A CA  1 
ATOM   3051 C  C   . PRO   A 1 422 ? 48.790 25.143  15.619  1.00 16.91  ? 422  PRO   A C   1 
ATOM   3052 O  O   . PRO   A 1 422 ? 48.810 26.176  16.279  1.00 18.42  ? 422  PRO   A O   1 
ATOM   3053 C  CB  . PRO   A 1 422 ? 51.111 24.739  14.862  1.00 17.11  ? 422  PRO   A CB  1 
ATOM   3054 C  CG  . PRO   A 1 422 ? 51.964 25.605  14.023  1.00 19.00  ? 422  PRO   A CG  1 
ATOM   3055 C  CD  . PRO   A 1 422 ? 51.126 26.720  13.499  1.00 17.07  ? 422  PRO   A CD  1 
ATOM   3056 N  N   . VAL   A 1 423 ? 48.000 24.084  15.918  1.00 15.47  ? 423  VAL   A N   1 
ATOM   3057 C  CA  . VAL   A 1 423 ? 47.199 24.048  17.133  1.00 15.84  ? 423  VAL   A CA  1 
ATOM   3058 C  C   . VAL   A 1 423 ? 47.293 22.624  17.698  1.00 16.14  ? 423  VAL   A C   1 
ATOM   3059 O  O   . VAL   A 1 423 ? 47.490 21.661  16.942  1.00 16.51  ? 423  VAL   A O   1 
ATOM   3060 C  CB  . VAL   A 1 423 ? 45.730 24.447  16.881  1.00 16.46  ? 423  VAL   A CB  1 
ATOM   3061 C  CG1 . VAL   A 1 423 ? 45.636 25.934  16.481  1.00 17.57  ? 423  VAL   A CG1 1 
ATOM   3062 C  CG2 . VAL   A 1 423 ? 45.098 23.573  15.798  1.00 16.67  ? 423  VAL   A CG2 1 
ATOM   3063 N  N   . GLU   A 1 424 ? 47.101 22.519  18.999  1.00 16.02  ? 424  GLU   A N   1 
ATOM   3064 C  CA  . GLU   A 1 424 ? 47.204 21.197  19.624  1.00 18.05  ? 424  GLU   A CA  1 
ATOM   3065 C  C   . GLU   A 1 424 ? 46.069 20.851  20.544  1.00 17.24  ? 424  GLU   A C   1 
ATOM   3066 O  O   . GLU   A 1 424 ? 45.507 19.771  20.416  1.00 18.99  ? 424  GLU   A O   1 
ATOM   3067 C  CB  . GLU   A 1 424 ? 48.529 21.069  20.412  1.00 20.58  ? 424  GLU   A CB  1 
ATOM   3068 C  CG  . GLU   A 1 424 ? 48.723 19.645  20.931  1.00 31.60  ? 424  GLU   A CG  1 
ATOM   3069 C  CD  . GLU   A 1 424 ? 50.140 19.164  21.188  1.00 44.00  ? 424  GLU   A CD  1 
ATOM   3070 O  OE1 . GLU   A 1 424 ? 50.560 18.178  20.538  1.00 47.64  ? 424  GLU   A OE1 1 
ATOM   3071 O  OE2 . GLU   A 1 424 ? 50.825 19.767  22.044  1.00 48.85  ? 424  GLU   A OE2 1 
ATOM   3072 N  N   . ASN   A 1 425 ? 45.786 21.702  21.530  1.00 16.36  ? 425  ASN   A N   1 
ATOM   3073 C  CA  . ASN   A 1 425 ? 44.781 21.342  22.530  1.00 16.85  ? 425  ASN   A CA  1 
ATOM   3074 C  C   . ASN   A 1 425 ? 43.382 21.834  22.121  1.00 16.03  ? 425  ASN   A C   1 
ATOM   3075 O  O   . ASN   A 1 425 ? 43.240 22.662  21.222  1.00 15.47  ? 425  ASN   A O   1 
ATOM   3076 C  CB  . ASN   A 1 425 ? 45.230 21.839  23.918  1.00 18.64  ? 425  ASN   A CB  1 
ATOM   3077 C  CG  . ASN   A 1 425 ? 45.223 23.311  24.101  1.00 22.30  ? 425  ASN   A CG  1 
ATOM   3078 O  OD1 . ASN   A 1 425 ? 44.265 23.994  23.738  1.00 22.44  ? 425  ASN   A OD1 1 
ATOM   3079 N  ND2 . ASN   A 1 425 ? 46.312 23.856  24.677  1.00 24.92  ? 425  ASN   A ND2 1 
ATOM   3080 N  N   . PRO   A 1 426 ? 42.337 21.319  22.777  1.00 15.85  ? 426  PRO   A N   1 
ATOM   3081 C  CA  . PRO   A 1 426 ? 40.972 21.684  22.370  1.00 15.50  ? 426  PRO   A CA  1 
ATOM   3082 C  C   . PRO   A 1 426 ? 40.699 23.189  22.337  1.00 15.67  ? 426  PRO   A C   1 
ATOM   3083 O  O   . PRO   A 1 426 ? 39.997 23.671  21.424  1.00 14.78  ? 426  PRO   A O   1 
ATOM   3084 C  CB  . PRO   A 1 426 ? 40.122 20.924  23.399  1.00 16.37  ? 426  PRO   A CB  1 
ATOM   3085 C  CG  . PRO   A 1 426 ? 40.967 19.630  23.578  1.00 17.48  ? 426  PRO   A CG  1 
ATOM   3086 C  CD  . PRO   A 1 426 ? 42.332 20.234  23.784  1.00 16.34  ? 426  PRO   A CD  1 
ATOM   3087 N  N   . ALA   A 1 427 ? 41.235 23.944  23.329  1.00 15.50  ? 427  ALA   A N   1 
ATOM   3088 C  CA  . ALA   A 1 427 ? 40.957 25.385  23.335  1.00 16.29  ? 427  ALA   A CA  1 
ATOM   3089 C  C   . ALA   A 1 427 ? 41.596 26.068  22.132  1.00 15.54  ? 427  ALA   A C   1 
ATOM   3090 O  O   . ALA   A 1 427 ? 40.982 26.908  21.485  1.00 15.32  ? 427  ALA   A O   1 
ATOM   3091 C  CB  . ALA   A 1 427 ? 41.442 26.005  24.628  1.00 17.30  ? 427  ALA   A CB  1 
ATOM   3092 N  N   . GLN   A 1 428 ? 42.843 25.655  21.788  1.00 15.30  ? 428  GLN   A N   1 
ATOM   3093 C  CA  . GLN   A 1 428 ? 43.498 26.217  20.609  1.00 15.40  ? 428  GLN   A CA  1 
ATOM   3094 C  C   . GLN   A 1 428 ? 42.790 25.833  19.319  1.00 14.44  ? 428  GLN   A C   1 
ATOM   3095 O  O   . GLN   A 1 428 ? 42.673 26.648  18.393  1.00 14.77  ? 428  GLN   A O   1 
ATOM   3096 C  CB  . GLN   A 1 428 ? 44.944 25.711  20.549  1.00 16.85  ? 428  GLN   A CB  1 
ATOM   3097 C  CG  . GLN   A 1 428 ? 45.803 26.149  21.729  1.00 19.12  ? 428  GLN   A CG  1 
ATOM   3098 C  CD  . GLN   A 1 428 ? 47.129 25.415  21.785  1.00 21.90  ? 428  GLN   A CD  1 
ATOM   3099 O  OE1 . GLN   A 1 428 ? 47.271 24.281  21.306  1.00 19.40  ? 428  GLN   A OE1 1 
ATOM   3100 N  NE2 . GLN   A 1 428 ? 48.128 26.075  22.383  1.00 21.79  ? 428  GLN   A NE2 1 
ATOM   3101 N  N   . ILE   A 1 429 ? 42.239 24.593  19.264  1.00 14.52  ? 429  ILE   A N   1 
ATOM   3102 C  CA  . ILE   A 1 429 ? 41.504 24.190  18.087  1.00 13.83  ? 429  ILE   A CA  1 
ATOM   3103 C  C   . ILE   A 1 429 ? 40.228 25.045  17.945  1.00 13.84  ? 429  ILE   A C   1 
ATOM   3104 O  O   . ILE   A 1 429 ? 39.893 25.495  16.838  1.00 13.61  ? 429  ILE   A O   1 
ATOM   3105 C  CB  . ILE   A 1 429 ? 41.159 22.707  18.242  1.00 14.16  ? 429  ILE   A CB  1 
ATOM   3106 C  CG1 . ILE   A 1 429 ? 42.474 21.873  18.165  1.00 14.34  ? 429  ILE   A CG1 1 
ATOM   3107 C  CG2 . ILE   A 1 429 ? 40.170 22.294  17.147  1.00 14.39  ? 429  ILE   A CG2 1 
ATOM   3108 C  CD1 . ILE   A 1 429 ? 42.217 20.412  18.603  1.00 14.72  ? 429  ILE   A CD1 1 
ATOM   3109 N  N   . ARG   A 1 430 ? 39.504 25.276  19.070  1.00 13.23  ? 430  ARG   A N   1 
ATOM   3110 C  CA  . ARG   A 1 430 ? 38.290 26.084  18.992  1.00 12.57  ? 430  ARG   A CA  1 
ATOM   3111 C  C   . ARG   A 1 430 ? 38.604 27.504  18.522  1.00 13.80  ? 430  ARG   A C   1 
ATOM   3112 O  O   . ARG   A 1 430 ? 37.761 28.105  17.812  1.00 13.76  ? 430  ARG   A O   1 
ATOM   3113 C  CB  . ARG   A 1 430 ? 37.592 26.109  20.332  1.00 13.01  ? 430  ARG   A CB  1 
ATOM   3114 C  CG  . ARG   A 1 430 ? 36.889 24.765  20.626  1.00 14.50  ? 430  ARG   A CG  1 
ATOM   3115 C  CD  . ARG   A 1 430 ? 36.055 24.856  21.895  1.00 16.31  ? 430  ARG   A CD  1 
ATOM   3116 N  NE  . ARG   A 1 430 ? 36.868 25.007  23.092  1.00 14.42  ? 430  ARG   A NE  1 
ATOM   3117 C  CZ  . ARG   A 1 430 ? 37.248 23.999  23.882  1.00 15.44  ? 430  ARG   A CZ  1 
ATOM   3118 N  NH1 . ARG   A 1 430 ? 37.026 22.746  23.521  1.00 16.14  ? 430  ARG   A NH1 1 
ATOM   3119 N  NH2 . ARG   A 1 430 ? 37.916 24.241  24.990  1.00 14.99  ? 430  ARG   A NH2 1 
ATOM   3120 N  N   . GLU   A 1 431 ? 39.813 28.017  18.844  1.00 12.63  ? 431  GLU   A N   1 
ATOM   3121 C  CA  . GLU   A 1 431 ? 40.183 29.361  18.382  1.00 13.05  ? 431  GLU   A CA  1 
ATOM   3122 C  C   . GLU   A 1 431 ? 40.296 29.419  16.875  1.00 13.95  ? 431  GLU   A C   1 
ATOM   3123 O  O   . GLU   A 1 431 ? 40.303 30.529  16.318  1.00 15.00  ? 431  GLU   A O   1 
ATOM   3124 C  CB  . GLU   A 1 431 ? 41.510 29.817  19.000  1.00 13.06  ? 431  GLU   A CB  1 
ATOM   3125 C  CG  . GLU   A 1 431 ? 41.351 30.048  20.491  1.00 14.74  ? 431  GLU   A CG  1 
ATOM   3126 C  CD  . GLU   A 1 431 ? 42.577 30.614  21.150  1.00 17.78  ? 431  GLU   A CD  1 
ATOM   3127 O  OE1 . GLU   A 1 431 ? 43.694 30.129  20.863  1.00 19.73  ? 431  GLU   A OE1 1 
ATOM   3128 O  OE2 . GLU   A 1 431 ? 42.413 31.523  21.986  1.00 17.06  ? 431  GLU   A OE2 1 
ATOM   3129 N  N   . MET   A 1 432 ? 40.452 28.282  16.181  1.00 13.38  ? 432  MET   A N   1 
ATOM   3130 C  CA  . MET   A 1 432 ? 40.508 28.331  14.710  1.00 13.46  ? 432  MET   A CA  1 
ATOM   3131 C  C   . MET   A 1 432 ? 39.156 28.661  14.099  1.00 14.05  ? 432  MET   A C   1 
ATOM   3132 O  O   . MET   A 1 432 ? 39.112 29.019  12.917  1.00 13.41  ? 432  MET   A O   1 
ATOM   3133 C  CB  . MET   A 1 432 ? 41.036 27.040  14.125  1.00 14.07  ? 432  MET   A CB  1 
ATOM   3134 C  CG  . MET   A 1 432 ? 42.483 26.748  14.518  1.00 13.98  ? 432  MET   A CG  1 
ATOM   3135 S  SD  . MET   A 1 432 ? 43.656 27.988  13.891  1.00 17.41  ? 432  MET   A SD  1 
ATOM   3136 C  CE  . MET   A 1 432 ? 43.607 27.555  12.121  1.00 16.42  ? 432  MET   A CE  1 
ATOM   3137 N  N   . PHE   A 1 433 ? 38.061 28.592  14.873  1.00 13.52  ? 433  PHE   A N   1 
ATOM   3138 C  CA  . PHE   A 1 433 ? 36.762 28.952  14.319  1.00 14.08  ? 433  PHE   A CA  1 
ATOM   3139 C  C   . PHE   A 1 433 ? 36.623 30.471  14.482  1.00 16.05  ? 433  PHE   A C   1 
ATOM   3140 O  O   . PHE   A 1 433 ? 36.103 30.975  15.492  1.00 18.99  ? 433  PHE   A O   1 
ATOM   3141 C  CB  . PHE   A 1 433 ? 35.655 28.187  15.047  1.00 12.66  ? 433  PHE   A CB  1 
ATOM   3142 C  CG  . PHE   A 1 433 ? 35.704 26.692  14.761  1.00 13.41  ? 433  PHE   A CG  1 
ATOM   3143 C  CD1 . PHE   A 1 433 ? 36.595 25.853  15.442  1.00 14.13  ? 433  PHE   A CD1 1 
ATOM   3144 C  CD2 . PHE   A 1 433 ? 34.860 26.122  13.822  1.00 14.00  ? 433  PHE   A CD2 1 
ATOM   3145 C  CE1 . PHE   A 1 433 ? 36.663 24.487  15.138  1.00 14.69  ? 433  PHE   A CE1 1 
ATOM   3146 C  CE2 . PHE   A 1 433 ? 34.929 24.776  13.535  1.00 13.94  ? 433  PHE   A CE2 1 
ATOM   3147 C  CZ  . PHE   A 1 433 ? 35.814 23.957  14.202  1.00 13.44  ? 433  PHE   A CZ  1 
ATOM   3148 N  N   . ASP   A 1 434 ? 37.309 31.208  13.607  1.00 13.74  ? 434  ASP   A N   1 
ATOM   3149 C  CA  . ASP   A 1 434 ? 37.434 32.660  13.730  1.00 13.45  ? 434  ASP   A CA  1 
ATOM   3150 C  C   . ASP   A 1 434 ? 37.345 33.323  12.373  1.00 13.92  ? 434  ASP   A C   1 
ATOM   3151 O  O   . ASP   A 1 434 ? 37.198 32.654  11.360  1.00 13.97  ? 434  ASP   A O   1 
ATOM   3152 C  CB  . ASP   A 1 434 ? 38.685 33.043  14.534  1.00 14.47  ? 434  ASP   A CB  1 
ATOM   3153 C  CG  . ASP   A 1 434 ? 40.012 32.916  13.776  1.00 16.37  ? 434  ASP   A CG  1 
ATOM   3154 O  OD1 . ASP   A 1 434 ? 39.995 32.425  12.629  1.00 15.11  ? 434  ASP   A OD1 1 
ATOM   3155 O  OD2 . ASP   A 1 434 ? 41.065 33.274  14.365  1.00 17.49  ? 434  ASP   A OD2 1 
ATOM   3156 N  N   . ASP   A 1 435 ? 37.439 34.650  12.350  1.00 14.70  ? 435  ASP   A N   1 
ATOM   3157 C  CA  . ASP   A 1 435 ? 37.265 35.360  11.087  1.00 14.83  ? 435  ASP   A CA  1 
ATOM   3158 C  C   . ASP   A 1 435 ? 38.408 35.115  10.106  1.00 14.73  ? 435  ASP   A C   1 
ATOM   3159 O  O   . ASP   A 1 435 ? 38.231 35.413  8.918   1.00 15.21  ? 435  ASP   A O   1 
ATOM   3160 C  CB  . ASP   A 1 435 ? 37.039 36.855  11.326  1.00 17.86  ? 435  ASP   A CB  1 
ATOM   3161 C  CG  . ASP   A 1 435 ? 35.724 37.179  12.017  1.00 25.62  ? 435  ASP   A CG  1 
ATOM   3162 O  OD1 . ASP   A 1 435 ? 34.823 36.299  12.045  1.00 24.02  ? 435  ASP   A OD1 1 
ATOM   3163 O  OD2 . ASP   A 1 435 ? 35.596 38.309  12.535  1.00 29.17  ? 435  ASP   A OD2 1 
ATOM   3164 N  N   . VAL   A 1 436 ? 39.574 34.670  10.588  1.00 14.74  ? 436  VAL   A N   1 
ATOM   3165 C  CA  . VAL   A 1 436 ? 40.663 34.362  9.666   1.00 14.15  ? 436  VAL   A CA  1 
ATOM   3166 C  C   . VAL   A 1 436 ? 40.299 33.081  8.909   1.00 14.42  ? 436  VAL   A C   1 
ATOM   3167 O  O   . VAL   A 1 436 ? 40.375 33.062  7.695   1.00 14.78  ? 436  VAL   A O   1 
ATOM   3168 C  CB  . VAL   A 1 436 ? 42.005 34.235  10.401  1.00 15.63  ? 436  VAL   A CB  1 
ATOM   3169 C  CG1 . VAL   A 1 436 ? 43.108 33.831  9.427   1.00 15.23  ? 436  VAL   A CG1 1 
ATOM   3170 C  CG2 . VAL   A 1 436 ? 42.365 35.576  11.064  1.00 16.65  ? 436  VAL   A CG2 1 
ATOM   3171 N  N   . SER   A 1 437 ? 39.877 32.007  9.600   1.00 13.85  ? 437  SER   A N   1 
ATOM   3172 C  CA  . SER   A 1 437 ? 39.564 30.764  8.863   1.00 13.04  ? 437  SER   A CA  1 
ATOM   3173 C  C   . SER   A 1 437 ? 38.380 30.973  7.939   1.00 13.63  ? 437  SER   A C   1 
ATOM   3174 O  O   . SER   A 1 437 ? 38.364 30.444  6.822   1.00 14.73  ? 437  SER   A O   1 
ATOM   3175 C  CB  . SER   A 1 437 ? 39.229 29.639  9.858   1.00 14.16  ? 437  SER   A CB  1 
ATOM   3176 O  OG  . SER   A 1 437 ? 40.378 29.270  10.599  1.00 14.37  ? 437  SER   A OG  1 
ATOM   3177 N  N   . TYR   A 1 438 ? 37.334 31.652  8.444   1.00 13.74  ? 438  TYR   A N   1 
ATOM   3178 C  CA  . TYR   A 1 438 ? 36.107 31.779  7.655   1.00 13.74  ? 438  TYR   A CA  1 
ATOM   3179 C  C   . TYR   A 1 438 ? 36.221 32.877  6.573   1.00 13.31  ? 438  TYR   A C   1 
ATOM   3180 O  O   . TYR   A 1 438 ? 36.044 32.606  5.392   1.00 13.48  ? 438  TYR   A O   1 
ATOM   3181 C  CB  . TYR   A 1 438 ? 34.930 32.108  8.601   1.00 13.71  ? 438  TYR   A CB  1 
ATOM   3182 C  CG  . TYR   A 1 438 ? 34.364 30.932  9.366   1.00 13.00  ? 438  TYR   A CG  1 
ATOM   3183 C  CD1 . TYR   A 1 438 ? 35.020 30.421  10.470  1.00 13.80  ? 438  TYR   A CD1 1 
ATOM   3184 C  CD2 . TYR   A 1 438 ? 33.121 30.451  9.074   1.00 13.21  ? 438  TYR   A CD2 1 
ATOM   3185 C  CE1 . TYR   A 1 438 ? 34.486 29.364  11.190  1.00 13.92  ? 438  TYR   A CE1 1 
ATOM   3186 C  CE2 . TYR   A 1 438 ? 32.544 29.433  9.822   1.00 12.97  ? 438  TYR   A CE2 1 
ATOM   3187 C  CZ  . TYR   A 1 438 ? 33.235 28.896  10.882  1.00 13.90  ? 438  TYR   A CZ  1 
ATOM   3188 O  OH  . TYR   A 1 438 ? 32.697 27.878  11.650  1.00 15.28  ? 438  TYR   A OH  1 
ATOM   3189 N  N   . ASP   A 1 439 ? 36.420 34.118  7.034   1.00 13.21  ? 439  ASP   A N   1 
ATOM   3190 C  CA  . ASP   A 1 439 ? 36.334 35.269  6.138   1.00 13.53  ? 439  ASP   A CA  1 
ATOM   3191 C  C   . ASP   A 1 439 ? 37.610 35.484  5.364   1.00 13.66  ? 439  ASP   A C   1 
ATOM   3192 O  O   . ASP   A 1 439 ? 37.541 35.609  4.148   1.00 13.81  ? 439  ASP   A O   1 
ATOM   3193 C  CB  . ASP   A 1 439 ? 36.008 36.518  6.921   1.00 14.48  ? 439  ASP   A CB  1 
ATOM   3194 C  CG  . ASP   A 1 439 ? 34.648 36.530  7.564   1.00 18.81  ? 439  ASP   A CG  1 
ATOM   3195 O  OD1 . ASP   A 1 439 ? 33.742 35.761  7.095   1.00 19.02  ? 439  ASP   A OD1 1 
ATOM   3196 O  OD2 . ASP   A 1 439 ? 34.468 37.326  8.500   1.00 21.71  ? 439  ASP   A OD2 1 
ATOM   3197 N  N   . LYS   A 1 440 ? 38.797 35.474  6.031   1.00 13.97  ? 440  LYS   A N   1 
ATOM   3198 C  CA  . LYS   A 1 440 ? 40.034 35.581  5.217   1.00 13.30  ? 440  LYS   A CA  1 
ATOM   3199 C  C   . LYS   A 1 440 ? 40.133 34.352  4.293   1.00 14.64  ? 440  LYS   A C   1 
ATOM   3200 O  O   . LYS   A 1 440 ? 40.444 34.493  3.104   1.00 15.04  ? 440  LYS   A O   1 
ATOM   3201 C  CB  . LYS   A 1 440 ? 41.284 35.785  6.053   1.00 13.93  ? 440  LYS   A CB  1 
ATOM   3202 C  CG  . LYS   A 1 440 ? 42.510 35.846  5.143   1.00 14.37  ? 440  LYS   A CG  1 
ATOM   3203 C  CD  . LYS   A 1 440 ? 43.724 36.175  5.978   1.00 14.33  ? 440  LYS   A CD  1 
ATOM   3204 C  CE  . LYS   A 1 440 ? 45.001 36.173  5.126   1.00 14.12  ? 440  LYS   A CE  1 
ATOM   3205 N  NZ  . LYS   A 1 440 ? 46.174 36.626  5.898   1.00 14.54  ? 440  LYS   A NZ  1 
ATOM   3206 N  N   . GLY   A 1 441 ? 39.782 33.154  4.781   1.00 14.59  ? 441  GLY   A N   1 
ATOM   3207 C  CA  . GLY   A 1 441 ? 39.797 31.960  3.930   1.00 14.63  ? 441  GLY   A CA  1 
ATOM   3208 C  C   . GLY   A 1 441 ? 38.935 32.146  2.699   1.00 14.64  ? 441  GLY   A C   1 
ATOM   3209 O  O   . GLY   A 1 441 ? 39.366 31.869  1.581   1.00 14.24  ? 441  GLY   A O   1 
ATOM   3210 N  N   . ALA   A 1 442 ? 37.697 32.632  2.892   1.00 13.92  ? 442  ALA   A N   1 
ATOM   3211 C  CA  . ALA   A 1 442 ? 36.843 32.854  1.712   1.00 14.18  ? 442  ALA   A CA  1 
ATOM   3212 C  C   . ALA   A 1 442 ? 37.423 33.952  0.804   1.00 13.81  ? 442  ALA   A C   1 
ATOM   3213 O  O   . ALA   A 1 442 ? 37.324 33.823  -0.424  1.00 15.23  ? 442  ALA   A O   1 
ATOM   3214 C  CB  . ALA   A 1 442 ? 35.431 33.241  2.144   1.00 14.49  ? 442  ALA   A CB  1 
ATOM   3215 N  N   . CYS   A 1 443 ? 37.961 35.006  1.413   1.00 13.77  ? 443  CYS   A N   1 
ATOM   3216 C  CA  . CYS   A 1 443 ? 38.446 36.112  0.598   1.00 14.25  ? 443  CYS   A CA  1 
ATOM   3217 C  C   . CYS   A 1 443 ? 39.663 35.748  -0.218  1.00 15.48  ? 443  CYS   A C   1 
ATOM   3218 O  O   . CYS   A 1 443 ? 39.762 36.213  -1.388  1.00 16.09  ? 443  CYS   A O   1 
ATOM   3219 C  CB  . CYS   A 1 443 ? 38.694 37.283  1.514   1.00 15.91  ? 443  CYS   A CB  1 
ATOM   3220 S  SG  . CYS   A 1 443 ? 37.166 37.871  2.261   1.00 19.56  ? 443  CYS   A SG  1 
ATOM   3221 N  N   . ILE   A 1 444 ? 40.554 34.875  0.295   1.00 14.04  ? 444  ILE   A N   1 
ATOM   3222 C  CA  . ILE   A 1 444 ? 41.708 34.503  -0.538  1.00 15.02  ? 444  ILE   A CA  1 
ATOM   3223 C  C   . ILE   A 1 444 ? 41.267 33.535  -1.626  1.00 15.63  ? 444  ILE   A C   1 
ATOM   3224 O  O   . ILE   A 1 444 ? 41.843 33.548  -2.723  1.00 15.11  ? 444  ILE   A O   1 
ATOM   3225 C  CB  . ILE   A 1 444 ? 42.912 34.028  0.287   1.00 15.75  ? 444  ILE   A CB  1 
ATOM   3226 C  CG1 . ILE   A 1 444 ? 42.574 32.702  1.006   1.00 16.19  ? 444  ILE   A CG1 1 
ATOM   3227 C  CG2 . ILE   A 1 444 ? 43.372 35.117  1.257   1.00 15.90  ? 444  ILE   A CG2 1 
ATOM   3228 C  CD1 . ILE   A 1 444 ? 43.835 32.145  1.743   1.00 16.89  ? 444  ILE   A CD1 1 
ATOM   3229 N  N   . LEU   A 1 445 ? 40.223 32.698  -1.373  1.00 14.79  ? 445  LEU   A N   1 
ATOM   3230 C  CA  . LEU   A 1 445 ? 39.698 31.843  -2.433  1.00 14.83  ? 445  LEU   A CA  1 
ATOM   3231 C  C   . LEU   A 1 445 ? 39.017 32.687  -3.503  1.00 13.91  ? 445  LEU   A C   1 
ATOM   3232 O  O   . LEU   A 1 445 ? 39.148 32.377  -4.684  1.00 14.74  ? 445  LEU   A O   1 
ATOM   3233 C  CB  . LEU   A 1 445 ? 38.708 30.831  -1.879  1.00 14.79  ? 445  LEU   A CB  1 
ATOM   3234 C  CG  . LEU   A 1 445 ? 39.327 29.814  -0.956  1.00 14.73  ? 445  LEU   A CG  1 
ATOM   3235 C  CD1 . LEU   A 1 445 ? 38.220 28.976  -0.325  1.00 15.16  ? 445  LEU   A CD1 1 
ATOM   3236 C  CD2 . LEU   A 1 445 ? 40.247 28.874  -1.741  1.00 15.22  ? 445  LEU   A CD2 1 
ATOM   3237 N  N   . ASN   A 1 446 ? 38.298 33.771  -3.103  1.00 14.42  ? 446  ASN   A N   1 
ATOM   3238 C  CA  . ASN   A 1 446 ? 37.687 34.670  -4.104  1.00 14.61  ? 446  ASN   A CA  1 
ATOM   3239 C  C   . ASN   A 1 446 ? 38.754 35.302  -4.954  1.00 15.93  ? 446  ASN   A C   1 
ATOM   3240 O  O   . ASN   A 1 446 ? 38.655 35.293  -6.184  1.00 15.86  ? 446  ASN   A O   1 
ATOM   3241 C  CB  . ASN   A 1 446 ? 36.921 35.772  -3.367  1.00 14.42  ? 446  ASN   A CB  1 
ATOM   3242 C  CG  . ASN   A 1 446 ? 36.202 36.672  -4.374  1.00 17.89  ? 446  ASN   A CG  1 
ATOM   3243 O  OD1 . ASN   A 1 446 ? 35.384 36.219  -5.182  1.00 18.19  ? 446  ASN   A OD1 1 
ATOM   3244 N  ND2 . ASN   A 1 446 ? 36.534 37.936  -4.301  1.00 19.18  ? 446  ASN   A ND2 1 
ATOM   3245 N  N   . MET   A 1 447 ? 39.846 35.744  -4.300  1.00 15.74  ? 447  MET   A N   1 
ATOM   3246 C  CA  . MET   A 1 447 ? 40.919 36.373  -5.050  1.00 15.84  ? 447  MET   A CA  1 
ATOM   3247 C  C   . MET   A 1 447 ? 41.536 35.342  -6.014  1.00 15.70  ? 447  MET   A C   1 
ATOM   3248 O  O   . MET   A 1 447 ? 41.825 35.654  -7.180  1.00 17.12  ? 447  MET   A O   1 
ATOM   3249 C  CB  . MET   A 1 447 ? 41.910 36.941  -4.034  1.00 17.25  ? 447  MET   A CB  1 
ATOM   3250 C  CG  . MET   A 1 447 ? 43.113 37.539  -4.610  1.00 19.35  ? 447  MET   A CG  1 
ATOM   3251 S  SD  . MET   A 1 447 ? 44.070 38.405  -3.327  1.00 17.05  ? 447  MET   A SD  1 
ATOM   3252 C  CE  . MET   A 1 447 ? 44.422 37.038  -2.160  1.00 18.52  ? 447  MET   A CE  1 
ATOM   3253 N  N   . LEU   A 1 448 ? 41.751 34.098  -5.558  1.00 15.43  ? 448  LEU   A N   1 
ATOM   3254 C  CA  . LEU   A 1 448 ? 42.308 33.046  -6.390  1.00 16.15  ? 448  LEU   A CA  1 
ATOM   3255 C  C   . LEU   A 1 448 ? 41.383 32.674  -7.567  1.00 16.67  ? 448  LEU   A C   1 
ATOM   3256 O  O   . LEU   A 1 448 ? 41.864 32.449  -8.692  1.00 17.98  ? 448  LEU   A O   1 
ATOM   3257 C  CB  . LEU   A 1 448 ? 42.624 31.774  -5.551  1.00 16.55  ? 448  LEU   A CB  1 
ATOM   3258 C  CG  . LEU   A 1 448 ? 43.159 30.609  -6.306  1.00 17.74  ? 448  LEU   A CG  1 
ATOM   3259 C  CD1 . LEU   A 1 448 ? 44.512 30.973  -6.978  1.00 18.48  ? 448  LEU   A CD1 1 
ATOM   3260 C  CD2 . LEU   A 1 448 ? 43.283 29.376  -5.397  1.00 18.29  ? 448  LEU   A CD2 1 
ATOM   3261 N  N   . ARG   A 1 449 ? 40.069 32.648  -7.345  1.00 15.15  ? 449  ARG   A N   1 
ATOM   3262 C  CA  . ARG   A 1 449 ? 39.102 32.345  -8.399  1.00 15.74  ? 449  ARG   A CA  1 
ATOM   3263 C  C   . ARG   A 1 449 ? 39.103 33.445  -9.444  1.00 16.42  ? 449  ARG   A C   1 
ATOM   3264 O  O   . ARG   A 1 449 ? 39.050 33.138  -10.628 1.00 17.25  ? 449  ARG   A O   1 
ATOM   3265 C  CB  . ARG   A 1 449 ? 37.682 32.212  -7.801  1.00 16.00  ? 449  ARG   A CB  1 
ATOM   3266 C  CG  . ARG   A 1 449 ? 36.622 31.880  -8.848  1.00 16.91  ? 449  ARG   A CG  1 
ATOM   3267 C  CD  . ARG   A 1 449 ? 35.300 31.603  -8.101  1.00 19.09  ? 449  ARG   A CD  1 
ATOM   3268 N  NE  . ARG   A 1 449 ? 34.150 31.337  -8.952  1.00 19.16  ? 449  ARG   A NE  1 
ATOM   3269 C  CZ  . ARG   A 1 449 ? 33.108 32.153  -9.088  1.00 20.34  ? 449  ARG   A CZ  1 
ATOM   3270 N  NH1 . ARG   A 1 449 ? 33.114 33.358  -8.524  1.00 21.49  ? 449  ARG   A NH1 1 
ATOM   3271 N  NH2 . ARG   A 1 449 ? 32.073 31.797  -9.837  1.00 21.34  ? 449  ARG   A NH2 1 
ATOM   3272 N  N   . GLU   A 1 450 ? 39.184 34.707  -9.012  1.00 15.29  ? 450  GLU   A N   1 
ATOM   3273 C  CA  . GLU   A 1 450 ? 39.227 35.795  -10.000 1.00 15.32  ? 450  GLU   A CA  1 
ATOM   3274 C  C   . GLU   A 1 450 ? 40.515 35.719  -10.807 1.00 17.07  ? 450  GLU   A C   1 
ATOM   3275 O  O   . GLU   A 1 450 ? 40.506 35.996  -12.036 1.00 17.42  ? 450  GLU   A O   1 
ATOM   3276 C  CB  . GLU   A 1 450 ? 39.137 37.138  -9.302  1.00 16.70  ? 450  GLU   A CB  1 
ATOM   3277 C  CG  . GLU   A 1 450 ? 37.784 37.408  -8.664  1.00 19.13  ? 450  GLU   A CG  1 
ATOM   3278 C  CD  . GLU   A 1 450 ? 36.672 37.537  -9.686  1.00 23.65  ? 450  GLU   A CD  1 
ATOM   3279 O  OE1 . GLU   A 1 450 ? 35.700 36.757  -9.601  1.00 24.22  ? 450  GLU   A OE1 1 
ATOM   3280 O  OE2 . GLU   A 1 450 ? 36.765 38.432  -10.567 1.00 24.44  ? 450  GLU   A OE2 1 
ATOM   3281 N  N   . TYR   A 1 451 ? 41.607 35.353  -10.155 1.00 16.69  ? 451  TYR   A N   1 
ATOM   3282 C  CA  . TYR   A 1 451 ? 42.911 35.251  -10.811 1.00 18.09  ? 451  TYR   A CA  1 
ATOM   3283 C  C   . TYR   A 1 451 ? 42.947 34.107  -11.839 1.00 18.23  ? 451  TYR   A C   1 
ATOM   3284 O  O   . TYR   A 1 451 ? 43.421 34.281  -12.974 1.00 18.33  ? 451  TYR   A O   1 
ATOM   3285 C  CB  . TYR   A 1 451 ? 43.992 35.075  -9.739  1.00 18.41  ? 451  TYR   A CB  1 
ATOM   3286 C  CG  . TYR   A 1 451 ? 45.361 34.779  -10.302 1.00 17.77  ? 451  TYR   A CG  1 
ATOM   3287 C  CD1 . TYR   A 1 451 ? 46.079 35.751  -10.988 1.00 19.15  ? 451  TYR   A CD1 1 
ATOM   3288 C  CD2 . TYR   A 1 451 ? 45.952 33.541  -10.120 1.00 18.50  ? 451  TYR   A CD2 1 
ATOM   3289 C  CE1 . TYR   A 1 451 ? 47.355 35.489  -11.476 1.00 19.93  ? 451  TYR   A CE1 1 
ATOM   3290 C  CE2 . TYR   A 1 451 ? 47.208 33.251  -10.648 1.00 18.98  ? 451  TYR   A CE2 1 
ATOM   3291 C  CZ  . TYR   A 1 451 ? 47.919 34.249  -11.283 1.00 20.52  ? 451  TYR   A CZ  1 
ATOM   3292 O  OH  . TYR   A 1 451 ? 49.177 33.974  -11.785 1.00 23.61  ? 451  TYR   A OH  1 
ATOM   3293 N  N   . LEU   A 1 452 ? 42.483 32.898  -11.450 1.00 17.62  ? 452  LEU   A N   1 
ATOM   3294 C  CA  . LEU   A 1 452 ? 42.534 31.759  -12.353 1.00 17.72  ? 452  LEU   A CA  1 
ATOM   3295 C  C   . LEU   A 1 452 ? 41.418 31.744  -13.377 1.00 18.09  ? 452  LEU   A C   1 
ATOM   3296 O  O   . LEU   A 1 452 ? 41.541 31.052  -14.394 1.00 19.02  ? 452  LEU   A O   1 
ATOM   3297 C  CB  . LEU   A 1 452 ? 42.431 30.442  -11.550 1.00 18.64  ? 452  LEU   A CB  1 
ATOM   3298 C  CG  . LEU   A 1 452 ? 43.552 30.182  -10.594 1.00 20.50  ? 452  LEU   A CG  1 
ATOM   3299 C  CD1 . LEU   A 1 452 ? 43.268 28.878  -9.842  1.00 20.78  ? 452  LEU   A CD1 1 
ATOM   3300 C  CD2 . LEU   A 1 452 ? 44.922 30.083  -11.311 1.00 22.42  ? 452  LEU   A CD2 1 
ATOM   3301 N  N   . SER   A 1 453 ? 40.296 32.371  -13.047 1.00 17.71  ? 453  SER   A N   1 
ATOM   3302 C  CA  . SER   A 1 453 ? 38.996 32.408  -13.720 1.00 17.31  ? 453  SER   A CA  1 
ATOM   3303 C  C   . SER   A 1 453 ? 38.067 31.403  -13.083 1.00 17.45  ? 453  SER   A C   1 
ATOM   3304 O  O   . SER   A 1 453 ? 38.521 30.357  -12.590 1.00 17.83  ? 453  SER   A O   1 
ATOM   3305 C  CB  . SER   A 1 453 ? 39.088 32.144  -15.225 1.00 18.66  ? 453  SER   A CB  1 
ATOM   3306 O  OG  . SER   A 1 453 ? 39.259 30.763  -15.530 1.00 20.23  ? 453  SER   A OG  1 
ATOM   3307 N  N   . ALA   A 1 454 ? 36.760 31.706  -13.108 1.00 16.94  ? 454  ALA   A N   1 
ATOM   3308 C  CA  . ALA   A 1 454 ? 35.768 30.810  -12.494 1.00 17.51  ? 454  ALA   A CA  1 
ATOM   3309 C  C   . ALA   A 1 454 ? 35.796 29.407  -13.051 1.00 18.21  ? 454  ALA   A C   1 
ATOM   3310 O  O   . ALA   A 1 454 ? 35.686 28.442  -12.272 1.00 18.65  ? 454  ALA   A O   1 
ATOM   3311 C  CB  . ALA   A 1 454 ? 34.388 31.403  -12.662 1.00 18.58  ? 454  ALA   A CB  1 
ATOM   3312 N  N   . ASP   A 1 455 ? 35.956 29.236  -14.364 1.00 18.24  ? 455  ASP   A N   1 
ATOM   3313 C  CA  . ASP   A 1 455 ? 35.986 27.873  -14.920 1.00 18.32  ? 455  ASP   A CA  1 
ATOM   3314 C  C   . ASP   A 1 455 ? 37.216 27.067  -14.515 1.00 18.67  ? 455  ASP   A C   1 
ATOM   3315 O  O   . ASP   A 1 455 ? 37.081 25.863  -14.174 1.00 18.55  ? 455  ASP   A O   1 
ATOM   3316 C  CB  . ASP   A 1 455 ? 35.826 27.902  -16.450 1.00 19.87  ? 455  ASP   A CB  1 
ATOM   3317 C  CG  . ASP   A 1 455 ? 34.439 28.357  -16.864 1.00 26.85  ? 455  ASP   A CG  1 
ATOM   3318 O  OD1 . ASP   A 1 455 ? 33.480 28.213  -16.049 1.00 30.93  ? 455  ASP   A OD1 1 
ATOM   3319 O  OD2 . ASP   A 1 455 ? 34.302 28.853  -17.973 1.00 29.93  ? 455  ASP   A OD2 1 
ATOM   3320 N  N   . ALA   A 1 456 ? 38.382 27.702  -14.483 1.00 17.75  ? 456  ALA   A N   1 
ATOM   3321 C  CA  . ALA   A 1 456 ? 39.605 26.954  -14.088 1.00 17.41  ? 456  ALA   A CA  1 
ATOM   3322 C  C   . ALA   A 1 456 ? 39.512 26.609  -12.587 1.00 17.27  ? 456  ALA   A C   1 
ATOM   3323 O  O   . ALA   A 1 456 ? 39.889 25.501  -12.171 1.00 17.59  ? 456  ALA   A O   1 
ATOM   3324 C  CB  . ALA   A 1 456 ? 40.862 27.799  -14.361 1.00 19.07  ? 456  ALA   A CB  1 
ATOM   3325 N  N   . PHE   A 1 457 ? 39.024 27.564  -11.791 1.00 16.38  ? 457  PHE   A N   1 
ATOM   3326 C  CA  . PHE   A 1 457 ? 38.885 27.337  -10.351 1.00 15.95  ? 457  PHE   A CA  1 
ATOM   3327 C  C   . PHE   A 1 457 ? 37.880 26.207  -10.090 1.00 17.30  ? 457  PHE   A C   1 
ATOM   3328 O  O   . PHE   A 1 457 ? 38.141 25.307  -9.270  1.00 16.91  ? 457  PHE   A O   1 
ATOM   3329 C  CB  . PHE   A 1 457 ? 38.434 28.644  -9.703  1.00 16.17  ? 457  PHE   A CB  1 
ATOM   3330 C  CG  . PHE   A 1 457 ? 38.318 28.558  -8.196  1.00 16.10  ? 457  PHE   A CG  1 
ATOM   3331 C  CD1 . PHE   A 1 457 ? 39.383 28.907  -7.385  1.00 17.46  ? 457  PHE   A CD1 1 
ATOM   3332 C  CD2 . PHE   A 1 457 ? 37.102 28.284  -7.600  1.00 16.95  ? 457  PHE   A CD2 1 
ATOM   3333 C  CE1 . PHE   A 1 457 ? 39.246 28.897  -5.990  1.00 18.19  ? 457  PHE   A CE1 1 
ATOM   3334 C  CE2 . PHE   A 1 457 ? 36.977 28.239  -6.215  1.00 17.35  ? 457  PHE   A CE2 1 
ATOM   3335 C  CZ  . PHE   A 1 457 ? 38.036 28.598  -5.422  1.00 17.94  ? 457  PHE   A CZ  1 
ATOM   3336 N  N   . LYS   A 1 458 ? 36.774 26.188  -10.837 1.00 16.99  ? 458  LYS   A N   1 
ATOM   3337 C  CA  . LYS   A 1 458 ? 35.788 25.112  -10.705 1.00 17.05  ? 458  LYS   A CA  1 
ATOM   3338 C  C   . LYS   A 1 458 ? 36.366 23.770  -11.072 1.00 17.67  ? 458  LYS   A C   1 
ATOM   3339 O  O   . LYS   A 1 458 ? 36.192 22.767  -10.320 1.00 17.99  ? 458  LYS   A O   1 
ATOM   3340 C  CB  . LYS   A 1 458 ? 34.565 25.412  -11.575 1.00 17.49  ? 458  LYS   A CB  1 
ATOM   3341 C  CG  . LYS   A 1 458 ? 33.466 24.350  -11.463 1.00 19.62  ? 458  LYS   A CG  1 
ATOM   3342 C  CD  . LYS   A 1 458 ? 32.264 24.776  -12.309 1.00 20.95  ? 458  LYS   A CD  1 
ATOM   3343 C  CE  . LYS   A 1 458 ? 31.143 23.745  -12.311 1.00 25.29  ? 458  LYS   A CE  1 
ATOM   3344 N  NZ  . LYS   A 1 458 ? 30.040 24.174  -13.231 1.00 26.48  ? 458  LYS   A NZ  1 
ATOM   3345 N  N   . SER   A 1 459 ? 37.118 23.699  -12.175 1.00 17.93  ? 459  SER   A N   1 
ATOM   3346 C  CA  . SER   A 1 459 ? 37.751 22.415  -12.524 1.00 17.98  ? 459  SER   A CA  1 
ATOM   3347 C  C   . SER   A 1 459 ? 38.703 21.949  -11.396 1.00 17.66  ? 459  SER   A C   1 
ATOM   3348 O  O   . SER   A 1 459 ? 38.745 20.750  -11.089 1.00 18.24  ? 459  SER   A O   1 
ATOM   3349 C  CB  . SER   A 1 459 ? 38.544 22.563  -13.837 1.00 21.68  ? 459  SER   A CB  1 
ATOM   3350 O  OG  . SER   A 1 459 ? 37.678 22.830  -14.929 1.00 25.64  ? 459  SER   A OG  1 
ATOM   3351 N  N   . GLY   A 1 460 ? 39.443 22.878  -10.790 1.00 17.86  ? 460  GLY   A N   1 
ATOM   3352 C  CA  . GLY   A 1 460 ? 40.377 22.569  -9.712  1.00 18.19  ? 460  GLY   A CA  1 
ATOM   3353 C  C   . GLY   A 1 460 ? 39.607 22.033  -8.509  1.00 18.46  ? 460  GLY   A C   1 
ATOM   3354 O  O   . GLY   A 1 460 ? 40.006 20.983  -7.954  1.00 18.74  ? 460  GLY   A O   1 
ATOM   3355 N  N   . ILE   A 1 461 ? 38.439 22.658  -8.167  1.00 18.31  ? 461  ILE   A N   1 
ATOM   3356 C  CA  . ILE   A 1 461 ? 37.535 22.227  -7.040  1.00 20.47  ? 461  ILE   A CA  1 
ATOM   3357 C  C   . ILE   A 1 461 ? 37.136 20.811  -7.250  1.00 18.63  ? 461  ILE   A C   1 
ATOM   3358 O  O   . ILE   A 1 461 ? 37.159 19.985  -6.310  1.00 18.26  ? 461  ILE   A O   1 
ATOM   3359 C  CB  . ILE   A 1 461 ? 36.138 23.090  -6.982  1.00 22.56  ? 461  ILE   A CB  1 
ATOM   3360 C  CG1 . ILE   A 1 461 ? 36.266 24.395  -6.289  1.00 25.71  ? 461  ILE   A CG1 1 
ATOM   3361 C  CG2 . ILE   A 1 461 ? 34.917 22.273  -6.346  1.00 25.83  ? 461  ILE   A CG2 1 
ATOM   3362 C  CD1 . ILE   A 1 461 ? 35.020 25.139  -6.407  1.00 24.70  ? 461  ILE   A CD1 1 
ATOM   3363 N  N   . VAL   A 1 462 ? 36.611 20.504  -8.434  1.00 17.15  ? 462  VAL   A N   1 
ATOM   3364 C  CA  . VAL   A 1 462 ? 36.043 19.234  -8.755  1.00 18.40  ? 462  VAL   A CA  1 
ATOM   3365 C  C   . VAL   A 1 462 ? 37.105 18.165  -8.682  1.00 18.38  ? 462  VAL   A C   1 
ATOM   3366 O  O   . VAL   A 1 462 ? 36.867 17.112  -8.067  1.00 18.86  ? 462  VAL   A O   1 
ATOM   3367 C  CB  . VAL   A 1 462 ? 35.349 19.265  -10.131 1.00 20.15  ? 462  VAL   A CB  1 
ATOM   3368 C  CG1 . VAL   A 1 462 ? 34.909 17.875  -10.551 1.00 21.02  ? 462  VAL   A CG1 1 
ATOM   3369 C  CG2 . VAL   A 1 462 ? 34.150 20.239  -10.106 1.00 21.57  ? 462  VAL   A CG2 1 
ATOM   3370 N  N   . GLN   A 1 463 ? 38.284 18.416  -9.252  1.00 17.76  ? 463  GLN   A N   1 
ATOM   3371 C  CA  . GLN   A 1 463 ? 39.363 17.419  -9.194  1.00 17.50  ? 463  GLN   A CA  1 
ATOM   3372 C  C   . GLN   A 1 463 ? 39.786 17.159  -7.741  1.00 17.53  ? 463  GLN   A C   1 
ATOM   3373 O  O   . GLN   A 1 463 ? 40.064 16.012  -7.354  1.00 17.13  ? 463  GLN   A O   1 
ATOM   3374 C  CB  . GLN   A 1 463 ? 40.550 17.911  -10.039 1.00 19.11  ? 463  GLN   A CB  1 
ATOM   3375 C  CG  . GLN   A 1 463 ? 41.619 16.824  -10.293 1.00 27.70  ? 463  GLN   A CG  1 
ATOM   3376 C  CD  . GLN   A 1 463 ? 42.668 16.706  -9.206  1.00 35.45  ? 463  GLN   A CD  1 
ATOM   3377 O  OE1 . GLN   A 1 463 ? 42.693 17.470  -8.239  1.00 36.26  ? 463  GLN   A OE1 1 
ATOM   3378 N  NE2 . GLN   A 1 463 ? 43.553 15.724  -9.328  1.00 37.79  ? 463  GLN   A NE2 1 
ATOM   3379 N  N   . TYR   A 1 464 ? 39.840 18.231  -6.927  1.00 16.47  ? 464  TYR   A N   1 
ATOM   3380 C  CA  . TYR   A 1 464 ? 40.240 18.102  -5.545  1.00 16.10  ? 464  TYR   A CA  1 
ATOM   3381 C  C   . TYR   A 1 464 ? 39.222 17.260  -4.783  1.00 16.49  ? 464  TYR   A C   1 
ATOM   3382 O  O   . TYR   A 1 464 ? 39.599 16.339  -4.051  1.00 16.80  ? 464  TYR   A O   1 
ATOM   3383 C  CB  . TYR   A 1 464 ? 40.297 19.527  -4.995  1.00 16.23  ? 464  TYR   A CB  1 
ATOM   3384 C  CG  . TYR   A 1 464 ? 40.446 19.636  -3.508  1.00 16.06  ? 464  TYR   A CG  1 
ATOM   3385 C  CD1 . TYR   A 1 464 ? 41.697 19.529  -2.904  1.00 15.80  ? 464  TYR   A CD1 1 
ATOM   3386 C  CD2 . TYR   A 1 464 ? 39.359 19.975  -2.712  1.00 15.92  ? 464  TYR   A CD2 1 
ATOM   3387 C  CE1 . TYR   A 1 464 ? 41.854 19.738  -1.524  1.00 15.91  ? 464  TYR   A CE1 1 
ATOM   3388 C  CE2 . TYR   A 1 464 ? 39.488 20.121  -1.333  1.00 15.31  ? 464  TYR   A CE2 1 
ATOM   3389 C  CZ  . TYR   A 1 464 ? 40.747 20.061  -0.750  1.00 15.99  ? 464  TYR   A CZ  1 
ATOM   3390 O  OH  . TYR   A 1 464 ? 40.863 20.339  0.598   1.00 16.85  ? 464  TYR   A OH  1 
ATOM   3391 N  N   . LEU   A 1 465 ? 37.939 17.549  -4.977  1.00 15.50  ? 465  LEU   A N   1 
ATOM   3392 C  CA  . LEU   A 1 465 ? 36.902 16.792  -4.249  1.00 15.25  ? 465  LEU   A CA  1 
ATOM   3393 C  C   . LEU   A 1 465 ? 36.883 15.355  -4.683  1.00 16.82  ? 465  LEU   A C   1 
ATOM   3394 O  O   . LEU   A 1 465 ? 36.738 14.460  -3.830  1.00 17.96  ? 465  LEU   A O   1 
ATOM   3395 C  CB  . LEU   A 1 465 ? 35.535 17.428  -4.433  1.00 15.44  ? 465  LEU   A CB  1 
ATOM   3396 C  CG  . LEU   A 1 465 ? 35.305 18.770  -3.770  1.00 15.17  ? 465  LEU   A CG  1 
ATOM   3397 C  CD1 . LEU   A 1 465 ? 33.963 19.360  -4.266  1.00 16.87  ? 465  LEU   A CD1 1 
ATOM   3398 C  CD2 . LEU   A 1 465 ? 35.269 18.628  -2.270  1.00 15.55  ? 465  LEU   A CD2 1 
ATOM   3399 N  N   . GLN   A 1 466 ? 37.033 15.101  -5.987  1.00 17.25  ? 466  GLN   A N   1 
ATOM   3400 C  CA  . GLN   A 1 466 ? 36.989 13.706  -6.461  1.00 17.74  ? 466  GLN   A CA  1 
ATOM   3401 C  C   . GLN   A 1 466 ? 38.197 12.919  -5.969  1.00 19.08  ? 466  GLN   A C   1 
ATOM   3402 O  O   . GLN   A 1 466 ? 38.037 11.800  -5.437  1.00 21.19  ? 466  GLN   A O   1 
ATOM   3403 C  CB  . GLN   A 1 466 ? 36.894 13.680  -8.016  1.00 19.71  ? 466  GLN   A CB  1 
ATOM   3404 C  CG  . GLN   A 1 466 ? 35.505 14.120  -8.475  1.00 24.61  ? 466  GLN   A CG  1 
ATOM   3405 C  CD  . GLN   A 1 466 ? 35.281 14.126  -9.976  1.00 32.78  ? 466  GLN   A CD  1 
ATOM   3406 O  OE1 . GLN   A 1 466 ? 36.213 14.196  -10.753 1.00 32.57  ? 466  GLN   A OE1 1 
ATOM   3407 N  NE2 . GLN   A 1 466 ? 34.015 14.129  -10.401 1.00 34.78  ? 466  GLN   A NE2 1 
ATOM   3408 N  N   . LYS   A 1 467 ? 39.391 13.500  -6.065  1.00 17.71  ? 467  LYS   A N   1 
ATOM   3409 C  CA  . LYS   A 1 467 ? 40.617 12.795  -5.690  1.00 18.43  ? 467  LYS   A CA  1 
ATOM   3410 C  C   . LYS   A 1 467 ? 40.664 12.463  -4.221  1.00 18.48  ? 467  LYS   A C   1 
ATOM   3411 O  O   . LYS   A 1 467 ? 41.207 11.433  -3.831  1.00 20.62  ? 467  LYS   A O   1 
ATOM   3412 C  CB  . LYS   A 1 467 ? 41.844 13.648  -6.067  1.00 19.70  ? 467  LYS   A CB  1 
ATOM   3413 C  CG  . LYS   A 1 467 ? 43.160 12.987  -5.703  1.00 25.58  ? 467  LYS   A CG  1 
ATOM   3414 C  CD  . LYS   A 1 467 ? 44.341 13.578  -6.415  1.00 30.76  ? 467  LYS   A CD  1 
ATOM   3415 C  CE  . LYS   A 1 467 ? 45.500 12.596  -6.435  1.00 37.60  ? 467  LYS   A CE  1 
ATOM   3416 N  NZ  . LYS   A 1 467 ? 46.711 13.245  -6.990  1.00 41.03  ? 467  LYS   A NZ  1 
ATOM   3417 N  N   . HIS   A 1 468 ? 40.159 13.385  -3.378  1.00 16.69  ? 468  HIS   A N   1 
ATOM   3418 C  CA  . HIS   A 1 468 ? 40.265 13.216  -1.948  1.00 15.66  ? 468  HIS   A CA  1 
ATOM   3419 C  C   . HIS   A 1 468 ? 38.970 12.794  -1.275  1.00 16.18  ? 468  HIS   A C   1 
ATOM   3420 O  O   . HIS   A 1 468 ? 38.884 12.856  -0.042  1.00 16.05  ? 468  HIS   A O   1 
ATOM   3421 C  CB  . HIS   A 1 468 ? 40.847 14.499  -1.329  1.00 16.76  ? 468  HIS   A CB  1 
ATOM   3422 C  CG  . HIS   A 1 468 ? 42.190 14.853  -1.904  1.00 17.92  ? 468  HIS   A CG  1 
ATOM   3423 N  ND1 . HIS   A 1 468 ? 43.335 14.159  -1.527  1.00 19.32  ? 468  HIS   A ND1 1 
ATOM   3424 C  CD2 . HIS   A 1 468 ? 42.531 15.795  -2.818  1.00 18.38  ? 468  HIS   A CD2 1 
ATOM   3425 C  CE1 . HIS   A 1 468 ? 44.326 14.681  -2.230  1.00 19.30  ? 468  HIS   A CE1 1 
ATOM   3426 N  NE2 . HIS   A 1 468 ? 43.899 15.659  -3.025  1.00 18.85  ? 468  HIS   A NE2 1 
ATOM   3427 N  N   . SER   A 1 469 ? 37.985 12.327  -2.041  1.00 15.55  ? 469  SER   A N   1 
ATOM   3428 C  CA  . SER   A 1 469 ? 36.727 11.867  -1.462  1.00 15.98  ? 469  SER   A CA  1 
ATOM   3429 C  C   . SER   A 1 469 ? 36.936 10.800  -0.403  1.00 16.32  ? 469  SER   A C   1 
ATOM   3430 O  O   . SER   A 1 469 ? 37.696 9.834   -0.603  1.00 17.15  ? 469  SER   A O   1 
ATOM   3431 C  CB  . SER   A 1 469 ? 35.870 11.261  -2.572  1.00 17.61  ? 469  SER   A CB  1 
ATOM   3432 O  OG  . SER   A 1 469 ? 35.255 12.280  -3.351  1.00 17.97  ? 469  SER   A OG  1 
ATOM   3433 N  N   . TYR   A 1 470 ? 36.270 11.007  0.747   1.00 16.04  ? 470  TYR   A N   1 
ATOM   3434 C  CA  . TYR   A 1 470 ? 36.329 10.094  1.895   1.00 16.42  ? 470  TYR   A CA  1 
ATOM   3435 C  C   . TYR   A 1 470 ? 37.701 10.017  2.518   1.00 16.83  ? 470  TYR   A C   1 
ATOM   3436 O  O   . TYR   A 1 470 ? 37.987 9.062   3.275   1.00 17.59  ? 470  TYR   A O   1 
ATOM   3437 C  CB  . TYR   A 1 470 ? 35.781 8.685   1.531   1.00 15.93  ? 470  TYR   A CB  1 
ATOM   3438 C  CG  . TYR   A 1 470 ? 34.375 8.772   0.982   1.00 15.69  ? 470  TYR   A CG  1 
ATOM   3439 C  CD1 . TYR   A 1 470 ? 33.314 9.101   1.802   1.00 17.00  ? 470  TYR   A CD1 1 
ATOM   3440 C  CD2 . TYR   A 1 470 ? 34.136 8.687   -0.387  1.00 16.32  ? 470  TYR   A CD2 1 
ATOM   3441 C  CE1 . TYR   A 1 470 ? 32.028 9.229   1.294   1.00 17.71  ? 470  TYR   A CE1 1 
ATOM   3442 C  CE2 . TYR   A 1 470 ? 32.858 8.785   -0.901  1.00 18.47  ? 470  TYR   A CE2 1 
ATOM   3443 C  CZ  . TYR   A 1 470 ? 31.811 9.095   -0.069  1.00 19.95  ? 470  TYR   A CZ  1 
ATOM   3444 O  OH  . TYR   A 1 470 ? 30.543 9.231   -0.576  1.00 22.53  ? 470  TYR   A OH  1 
ATOM   3445 N  N   . LYS   A 1 471 ? 38.522 11.067  2.315   1.00 15.71  ? 471  LYS   A N   1 
ATOM   3446 C  CA  . LYS   A 1 471 ? 39.875 11.139  2.838   1.00 15.99  ? 471  LYS   A CA  1 
ATOM   3447 C  C   . LYS   A 1 471 ? 40.126 12.539  3.416   1.00 15.52  ? 471  LYS   A C   1 
ATOM   3448 O  O   . LYS   A 1 471 ? 39.184 13.310  3.605   1.00 15.33  ? 471  LYS   A O   1 
ATOM   3449 C  CB  . LYS   A 1 471 ? 40.891 10.779  1.731   1.00 18.83  ? 471  LYS   A CB  1 
ATOM   3450 C  CG  . LYS   A 1 471 ? 40.690 9.330   1.239   1.00 21.63  ? 471  LYS   A CG  1 
ATOM   3451 C  CD  . LYS   A 1 471 ? 41.630 9.047   0.086   1.00 28.98  ? 471  LYS   A CD  1 
ATOM   3452 C  CE  . LYS   A 1 471 ? 41.684 7.568   -0.250  1.00 37.12  ? 471  LYS   A CE  1 
ATOM   3453 N  NZ  . LYS   A 1 471 ? 40.530 7.127   -1.097  1.00 42.61  ? 471  LYS   A NZ  1 
ATOM   3454 N  N   . ASN   A 1 472 ? 41.387 12.832  3.771   1.00 15.11  ? 472  ASN   A N   1 
ATOM   3455 C  CA  . ASN   A 1 472 ? 41.729 14.095  4.400   1.00 14.97  ? 472  ASN   A CA  1 
ATOM   3456 C  C   . ASN   A 1 472 ? 42.803 14.809  3.603   1.00 15.39  ? 472  ASN   A C   1 
ATOM   3457 O  O   . ASN   A 1 472 ? 43.602 14.180  2.905   1.00 17.46  ? 472  ASN   A O   1 
ATOM   3458 C  CB  . ASN   A 1 472 ? 42.206 13.911  5.850   1.00 15.10  ? 472  ASN   A CB  1 
ATOM   3459 C  CG  . ASN   A 1 472 ? 41.160 13.308  6.745   1.00 15.69  ? 472  ASN   A CG  1 
ATOM   3460 O  OD1 . ASN   A 1 472 ? 40.803 12.138  6.636   1.00 15.82  ? 472  ASN   A OD1 1 
ATOM   3461 N  ND2 . ASN   A 1 472 ? 40.597 14.102  7.619   1.00 14.92  ? 472  ASN   A ND2 1 
ATOM   3462 N  N   . THR   A 1 473 ? 42.785 16.142  3.689   1.00 14.70  ? 473  THR   A N   1 
ATOM   3463 C  CA  . THR   A 1 473 ? 43.731 16.949  2.920   1.00 15.12  ? 473  THR   A CA  1 
ATOM   3464 C  C   . THR   A 1 473 ? 44.480 17.976  3.764   1.00 15.77  ? 473  THR   A C   1 
ATOM   3465 O  O   . THR   A 1 473 ? 44.076 18.329  4.878   1.00 17.06  ? 473  THR   A O   1 
ATOM   3466 C  CB  . THR   A 1 473 ? 42.946 17.752  1.849   1.00 15.88  ? 473  THR   A CB  1 
ATOM   3467 O  OG1 . THR   A 1 473 ? 41.876 18.432  2.506   1.00 15.75  ? 473  THR   A OG1 1 
ATOM   3468 C  CG2 . THR   A 1 473 ? 42.382 16.846  0.777   1.00 16.64  ? 473  THR   A CG2 1 
ATOM   3469 N  N   . LYS   A 1 474 ? 45.569 18.503  3.197   1.00 15.42  ? 474  LYS   A N   1 
ATOM   3470 C  CA  . LYS   A 1 474 ? 46.309 19.613  3.762   1.00 16.02  ? 474  LYS   A CA  1 
ATOM   3471 C  C   . LYS   A 1 474 ? 46.369 20.671  2.666   1.00 16.49  ? 474  LYS   A C   1 
ATOM   3472 O  O   . LYS   A 1 474 ? 46.060 20.412  1.502   1.00 16.30  ? 474  LYS   A O   1 
ATOM   3473 C  CB  . LYS   A 1 474 ? 47.714 19.181  4.213   1.00 20.47  ? 474  LYS   A CB  1 
ATOM   3474 C  CG  . LYS   A 1 474 ? 48.457 18.440  3.148   1.00 28.25  ? 474  LYS   A CG  1 
ATOM   3475 C  CD  . LYS   A 1 474 ? 49.879 18.099  3.581   1.00 36.96  ? 474  LYS   A CD  1 
ATOM   3476 C  CE  . LYS   A 1 474 ? 49.899 17.163  4.762   1.00 43.15  ? 474  LYS   A CE  1 
ATOM   3477 N  NZ  . LYS   A 1 474 ? 49.752 17.903  6.040   1.00 46.41  ? 474  LYS   A NZ  1 
ATOM   3478 N  N   . ASN   A 1 475 ? 46.860 21.865  3.002   1.00 18.81  ? 475  ASN   A N   1 
ATOM   3479 C  CA  . ASN   A 1 475 ? 46.951 22.934  1.967   1.00 20.05  ? 475  ASN   A CA  1 
ATOM   3480 C  C   . ASN   A 1 475 ? 47.538 22.565  0.678   1.00 21.70  ? 475  ASN   A C   1 
ATOM   3481 O  O   . ASN   A 1 475 ? 47.031 22.927  -0.393  1.00 21.99  ? 475  ASN   A O   1 
ATOM   3482 C  CB  . ASN   A 1 475 ? 47.715 24.085  2.514   1.00 22.03  ? 475  ASN   A CB  1 
ATOM   3483 C  CG  . ASN   A 1 475 ? 46.948 24.836  3.503   1.00 24.65  ? 475  ASN   A CG  1 
ATOM   3484 O  OD1 . ASN   A 1 475 ? 45.858 24.424  3.988   1.00 23.40  ? 475  ASN   A OD1 1 
ATOM   3485 N  ND2 . ASN   A 1 475 ? 47.420 26.021  3.744   1.00 24.15  ? 475  ASN   A ND2 1 
ATOM   3486 N  N   . GLU   A 1 476 ? 48.665 21.884  0.736   1.00 21.93  ? 476  GLU   A N   1 
ATOM   3487 C  CA  . GLU   A 1 476 ? 49.383 21.539  -0.479  1.00 22.37  ? 476  GLU   A CA  1 
ATOM   3488 C  C   . GLU   A 1 476 ? 48.540 20.715  -1.461  1.00 21.83  ? 476  GLU   A C   1 
ATOM   3489 O  O   . GLU   A 1 476 ? 48.683 20.871  -2.665  1.00 23.43  ? 476  GLU   A O   1 
ATOM   3490 C  CB  . GLU   A 1 476 ? 50.675 20.810  -0.105  1.00 26.55  ? 476  GLU   A CB  1 
ATOM   3491 C  CG  . GLU   A 1 476 ? 51.595 20.557  -1.284  1.00 35.22  ? 476  GLU   A CG  1 
ATOM   3492 C  CD  . GLU   A 1 476 ? 53.031 20.320  -0.856  1.00 45.32  ? 476  GLU   A CD  1 
ATOM   3493 O  OE1 . GLU   A 1 476 ? 53.246 19.856  0.292   1.00 46.35  ? 476  GLU   A OE1 1 
ATOM   3494 O  OE2 . GLU   A 1 476 ? 53.942 20.598  -1.672  1.00 47.60  ? 476  GLU   A OE2 1 
ATOM   3495 N  N   . ASP   A 1 477 ? 47.562 19.918  -0.950  1.00 19.01  ? 477  ASP   A N   1 
ATOM   3496 C  CA  . ASP   A 1 477 ? 46.719 19.147  -1.857  1.00 18.30  ? 477  ASP   A CA  1 
ATOM   3497 C  C   . ASP   A 1 477 ? 45.846 20.091  -2.683  1.00 17.96  ? 477  ASP   A C   1 
ATOM   3498 O  O   . ASP   A 1 477 ? 45.591 19.820  -3.843  1.00 18.87  ? 477  ASP   A O   1 
ATOM   3499 C  CB  . ASP   A 1 477 ? 45.845 18.180  -1.055  1.00 18.23  ? 477  ASP   A CB  1 
ATOM   3500 C  CG  . ASP   A 1 477 ? 46.665 17.171  -0.305  1.00 21.61  ? 477  ASP   A CG  1 
ATOM   3501 O  OD1 . ASP   A 1 477 ? 47.570 16.530  -0.943  1.00 22.85  ? 477  ASP   A OD1 1 
ATOM   3502 O  OD2 . ASP   A 1 477 ? 46.394 16.953  0.903   1.00 19.50  ? 477  ASP   A OD2 1 
ATOM   3503 N  N   . LEU   A 1 478 ? 45.360 21.189  -2.078  1.00 18.06  ? 478  LEU   A N   1 
ATOM   3504 C  CA  . LEU   A 1 478 ? 44.513 22.111  -2.784  1.00 18.17  ? 478  LEU   A CA  1 
ATOM   3505 C  C   . LEU   A 1 478 ? 45.316 22.791  -3.871  1.00 19.06  ? 478  LEU   A C   1 
ATOM   3506 O  O   . LEU   A 1 478 ? 44.848 22.868  -5.008  1.00 19.90  ? 478  LEU   A O   1 
ATOM   3507 C  CB  . LEU   A 1 478 ? 43.944 23.164  -1.826  1.00 18.32  ? 478  LEU   A CB  1 
ATOM   3508 C  CG  . LEU   A 1 478 ? 43.046 24.208  -2.485  1.00 17.77  ? 478  LEU   A CG  1 
ATOM   3509 C  CD1 . LEU   A 1 478 ? 41.884 23.569  -3.232  1.00 18.62  ? 478  LEU   A CD1 1 
ATOM   3510 C  CD2 . LEU   A 1 478 ? 42.558 25.204  -1.466  1.00 18.51  ? 478  LEU   A CD2 1 
ATOM   3511 N  N   . TRP   A 1 479 ? 46.570 23.207  -3.568  1.00 19.49  ? 479  TRP   A N   1 
ATOM   3512 C  CA  . TRP   A 1 479 ? 47.373 23.860  -4.612  1.00 19.90  ? 479  TRP   A CA  1 
ATOM   3513 C  C   . TRP   A 1 479 ? 47.670 22.902  -5.718  1.00 20.03  ? 479  TRP   A C   1 
ATOM   3514 O  O   . TRP   A 1 479 ? 47.615 23.289  -6.894  1.00 20.48  ? 479  TRP   A O   1 
ATOM   3515 C  CB  . TRP   A 1 479 ? 48.695 24.409  -4.062  1.00 20.42  ? 479  TRP   A CB  1 
ATOM   3516 C  CG  . TRP   A 1 479 ? 48.624 25.141  -2.736  1.00 19.30  ? 479  TRP   A CG  1 
ATOM   3517 C  CD1 . TRP   A 1 479 ? 49.573 25.094  -1.751  1.00 20.72  ? 479  TRP   A CD1 1 
ATOM   3518 C  CD2 . TRP   A 1 479 ? 47.569 25.995  -2.235  1.00 18.33  ? 479  TRP   A CD2 1 
ATOM   3519 N  NE1 . TRP   A 1 479 ? 49.191 25.879  -0.692  1.00 20.17  ? 479  TRP   A NE1 1 
ATOM   3520 C  CE2 . TRP   A 1 479 ? 47.951 26.402  -0.941  1.00 18.68  ? 479  TRP   A CE2 1 
ATOM   3521 C  CE3 . TRP   A 1 479 ? 46.314 26.395  -2.719  1.00 18.72  ? 479  TRP   A CE3 1 
ATOM   3522 C  CZ2 . TRP   A 1 479 ? 47.140 27.198  -0.146  1.00 18.77  ? 479  TRP   A CZ2 1 
ATOM   3523 C  CZ3 . TRP   A 1 479 ? 45.524 27.214  -1.926  1.00 19.22  ? 479  TRP   A CZ3 1 
ATOM   3524 C  CH2 . TRP   A 1 479 ? 45.946 27.595  -0.648  1.00 18.48  ? 479  TRP   A CH2 1 
ATOM   3525 N  N   . ASP   A 1 480 ? 47.985 21.648  -5.395  1.00 19.52  ? 480  ASP   A N   1 
ATOM   3526 C  CA  . ASP   A 1 480 ? 48.293 20.645  -6.407  1.00 20.47  ? 480  ASP   A CA  1 
ATOM   3527 C  C   . ASP   A 1 480 ? 47.101 20.452  -7.325  1.00 21.15  ? 480  ASP   A C   1 
ATOM   3528 O  O   . ASP   A 1 480 ? 47.282 20.346  -8.547  1.00 21.29  ? 480  ASP   A O   1 
ATOM   3529 C  CB  . ASP   A 1 480 ? 48.631 19.299  -5.752  1.00 23.21  ? 480  ASP   A CB  1 
ATOM   3530 C  CG  . ASP   A 1 480 ? 49.974 19.235  -5.060  1.00 28.48  ? 480  ASP   A CG  1 
ATOM   3531 O  OD1 . ASP   A 1 480 ? 50.798 20.134  -5.290  1.00 29.83  ? 480  ASP   A OD1 1 
ATOM   3532 O  OD2 . ASP   A 1 480 ? 50.179 18.293  -4.248  1.00 31.96  ? 480  ASP   A OD2 1 
ATOM   3533 N  N   . SER   A 1 481 ? 45.871 20.391  -6.738  1.00 20.70  ? 481  SER   A N   1 
ATOM   3534 C  CA  . SER   A 1 481 ? 44.677 20.217  -7.569  1.00 20.63  ? 481  SER   A CA  1 
ATOM   3535 C  C   . SER   A 1 481 ? 44.442 21.397  -8.479  1.00 22.20  ? 481  SER   A C   1 
ATOM   3536 O  O   . SER   A 1 481 ? 44.094 21.229  -9.645  1.00 22.97  ? 481  SER   A O   1 
ATOM   3537 C  CB  . SER   A 1 481 ? 43.440 20.025  -6.701  1.00 20.49  ? 481  SER   A CB  1 
ATOM   3538 O  OG  . SER   A 1 481 ? 43.542 18.764  -6.060  1.00 22.36  ? 481  SER   A OG  1 
ATOM   3539 N  N   . MET   A 1 482 ? 44.585 22.605  -7.931  1.00 22.09  ? 482  MET   A N   1 
ATOM   3540 C  CA  . MET   A 1 482 ? 44.328 23.815  -8.677  1.00 24.34  ? 482  MET   A CA  1 
ATOM   3541 C  C   . MET   A 1 482 ? 45.303 23.941  -9.840  1.00 26.66  ? 482  MET   A C   1 
ATOM   3542 O  O   . MET   A 1 482 ? 44.867 24.329  -10.938 1.00 28.30  ? 482  MET   A O   1 
ATOM   3543 C  CB  . MET   A 1 482 ? 44.292 25.039  -7.721  1.00 24.28  ? 482  MET   A CB  1 
ATOM   3544 C  CG  . MET   A 1 482 ? 43.027 25.039  -6.862  1.00 28.17  ? 482  MET   A CG  1 
ATOM   3545 S  SD  . MET   A 1 482 ? 41.618 25.644  -7.866  1.00 31.61  ? 482  MET   A SD  1 
ATOM   3546 C  CE  . MET   A 1 482 ? 40.295 25.425  -6.657  1.00 34.60  ? 482  MET   A CE  1 
ATOM   3547 N  N   . ALA   A 1 483 ? 46.566 23.499  -9.667  1.00 27.54  ? 483  ALA   A N   1 
ATOM   3548 C  CA  . ALA   A 1 483 ? 47.586 23.558  -10.727 1.00 30.58  ? 483  ALA   A CA  1 
ATOM   3549 C  C   . ALA   A 1 483 ? 47.482 22.421  -11.749 1.00 33.27  ? 483  ALA   A C   1 
ATOM   3550 O  O   . ALA   A 1 483 ? 48.089 22.508  -12.818 1.00 35.26  ? 483  ALA   A O   1 
ATOM   3551 C  CB  . ALA   A 1 483 ? 48.970 23.537  -10.117 1.00 30.70  ? 483  ALA   A CB  1 
ATOM   3552 N  N   . SER   A 1 484 ? 46.781 21.333  -11.414 1.00 33.85  ? 484  SER   A N   1 
ATOM   3553 C  CA  . SER   A 1 484 ? 46.633 20.189  -12.320 1.00 35.76  ? 484  SER   A CA  1 
ATOM   3554 C  C   . SER   A 1 484 ? 45.718 20.480  -13.527 1.00 37.11  ? 484  SER   A C   1 
ATOM   3555 O  O   . SER   A 1 484 ? 45.627 19.643  -14.416 1.00 39.29  ? 484  SER   A O   1 
ATOM   3556 C  CB  . SER   A 1 484 ? 46.069 18.995  -11.557 1.00 38.53  ? 484  SER   A CB  1 
ATOM   3557 O  OG  . SER   A 1 484 ? 44.710 19.229  -11.211 1.00 41.66  ? 484  SER   A OG  1 
ATOM   3558 N  N   . ILE   A 1 485 ? 45.031 21.625  -13.549 1.00 36.17  ? 485  ILE   A N   1 
ATOM   3559 C  CA  . ILE   A 1 485 ? 44.066 21.984  -14.590 1.00 36.65  ? 485  ILE   A CA  1 
ATOM   3560 C  C   . ILE   A 1 485 ? 44.714 22.516  -15.880 1.00 38.28  ? 485  ILE   A C   1 
ATOM   3561 O  O   . ILE   A 1 485 ? 45.391 23.548  -15.847 1.00 38.66  ? 485  ILE   A O   1 
ATOM   3562 C  CB  . ILE   A 1 485 ? 43.042 22.969  -14.002 1.00 36.62  ? 485  ILE   A CB  1 
ATOM   3563 C  CG1 . ILE   A 1 485 ? 42.354 22.348  -12.762 1.00 37.06  ? 485  ILE   A CG1 1 
ATOM   3564 C  CG2 . ILE   A 1 485 ? 42.026 23.451  -15.030 1.00 37.06  ? 485  ILE   A CG2 1 
ATOM   3565 C  CD1 . ILE   A 1 485 ? 41.762 20.879  -12.975 1.00 37.79  ? 485  ILE   A CD1 1 
ATOM   3566 N  N   . GLY   A 1 488 ? 48.655 20.897  -17.370 1.00 44.47  ? 513  GLY   A N   1 
ATOM   3567 C  CA  . GLY   A 1 488 ? 49.366 21.657  -16.354 1.00 44.88  ? 513  GLY   A CA  1 
ATOM   3568 C  C   . GLY   A 1 488 ? 49.070 23.135  -16.454 1.00 45.02  ? 513  GLY   A C   1 
ATOM   3569 O  O   . GLY   A 1 488 ? 49.547 23.815  -17.367 1.00 45.57  ? 513  GLY   A O   1 
ATOM   3570 N  N   . GLY   A 1 489 ? 48.281 23.633  -15.517 1.00 44.28  ? 514  GLY   A N   1 
ATOM   3571 C  CA  . GLY   A 1 489 ? 47.898 25.034  -15.518 1.00 43.66  ? 514  GLY   A CA  1 
ATOM   3572 C  C   . GLY   A 1 489 ? 48.862 25.932  -14.784 1.00 42.64  ? 514  GLY   A C   1 
ATOM   3573 O  O   . GLY   A 1 489 ? 50.040 25.608  -14.585 1.00 43.07  ? 514  GLY   A O   1 
ATOM   3574 N  N   . VAL   A 1 490 ? 48.354 27.071  -14.369 1.00 40.46  ? 515  VAL   A N   1 
ATOM   3575 C  CA  . VAL   A 1 490 ? 49.140 28.058  -13.656 1.00 37.98  ? 515  VAL   A CA  1 
ATOM   3576 C  C   . VAL   A 1 490 ? 49.444 27.523  -12.284 1.00 35.27  ? 515  VAL   A C   1 
ATOM   3577 O  O   . VAL   A 1 490 ? 48.548 27.018  -11.622 1.00 34.97  ? 515  VAL   A O   1 
ATOM   3578 C  CB  . VAL   A 1 490 ? 48.292 29.335  -13.575 1.00 38.11  ? 515  VAL   A CB  1 
ATOM   3579 C  CG1 . VAL   A 1 490 ? 48.952 30.380  -12.691 1.00 38.99  ? 515  VAL   A CG1 1 
ATOM   3580 C  CG2 . VAL   A 1 490 ? 48.033 29.880  -14.978 1.00 38.33  ? 515  VAL   A CG2 1 
ATOM   3581 N  N   . ASP   A 1 491 ? 50.712 27.574  -11.888 1.00 32.95  ? 516  ASP   A N   1 
ATOM   3582 C  CA  . ASP   A 1 491 ? 51.103 27.099  -10.576 1.00 31.22  ? 516  ASP   A CA  1 
ATOM   3583 C  C   . ASP   A 1 491 ? 50.761 28.226  -9.611  1.00 29.46  ? 516  ASP   A C   1 
ATOM   3584 O  O   . ASP   A 1 491 ? 51.078 29.397  -9.844  1.00 30.83  ? 516  ASP   A O   1 
ATOM   3585 C  CB  . ASP   A 1 491 ? 52.592 26.714  -10.559 1.00 31.97  ? 516  ASP   A CB  1 
ATOM   3586 C  CG  . ASP   A 1 491 ? 52.967 25.897  -9.343  1.00 34.76  ? 516  ASP   A CG  1 
ATOM   3587 O  OD1 . ASP   A 1 491 ? 53.024 24.633  -9.461  1.00 34.75  ? 516  ASP   A OD1 1 
ATOM   3588 O  OD2 . ASP   A 1 491 ? 53.210 26.509  -8.265  1.00 35.42  ? 516  ASP   A OD2 1 
ATOM   3589 N  N   . VAL   A 1 492 ? 50.098 27.813  -8.532  1.00 25.01  ? 517  VAL   A N   1 
ATOM   3590 C  CA  . VAL   A 1 492 ? 49.354 28.490  -7.472  1.00 26.18  ? 517  VAL   A CA  1 
ATOM   3591 C  C   . VAL   A 1 492 ? 50.097 28.343  -6.115  1.00 23.22  ? 517  VAL   A C   1 
ATOM   3592 O  O   . VAL   A 1 492 ? 49.813 29.089  -5.168  1.00 21.18  ? 517  VAL   A O   1 
ATOM   3593 C  CB  . VAL   A 1 492 ? 47.997 27.637  -7.479  1.00 30.06  ? 517  VAL   A CB  1 
ATOM   3594 C  CG1 . VAL   A 1 492 ? 47.082 27.922  -6.318  1.00 30.89  ? 517  VAL   A CG1 1 
ATOM   3595 C  CG2 . VAL   A 1 492 ? 47.231 27.763  -8.813  1.00 31.77  ? 517  VAL   A CG2 1 
ATOM   3596 N  N   . LYS   A 1 493 ? 51.008 27.366  -5.978  1.00 21.90  ? 518  LYS   A N   1 
ATOM   3597 C  CA  . LYS   A 1 493 ? 51.629 27.095  -4.676  1.00 20.57  ? 518  LYS   A CA  1 
ATOM   3598 C  C   . LYS   A 1 493 ? 52.386 28.243  -4.092  1.00 18.88  ? 518  LYS   A C   1 
ATOM   3599 O  O   . LYS   A 1 493 ? 52.127 28.602  -2.932  1.00 17.68  ? 518  LYS   A O   1 
ATOM   3600 C  CB  . LYS   A 1 493 ? 52.542 25.866  -4.771  1.00 23.03  ? 518  LYS   A CB  1 
ATOM   3601 C  CG  . LYS   A 1 493 ? 53.158 25.459  -3.428  1.00 25.29  ? 518  LYS   A CG  1 
ATOM   3602 C  CD  . LYS   A 1 493 ? 53.864 24.077  -3.561  1.00 31.21  ? 518  LYS   A CD  1 
ATOM   3603 C  CE  . LYS   A 1 493 ? 52.817 23.041  -3.891  1.00 38.13  ? 518  LYS   A CE  1 
ATOM   3604 N  NZ  . LYS   A 1 493 ? 53.414 21.725  -4.231  1.00 39.63  ? 518  LYS   A NZ  1 
ATOM   3605 N  N   . THR   A 1 494 ? 53.329 28.882  -4.845  1.00 18.14  ? 519  THR   A N   1 
ATOM   3606 C  CA  . THR   A 1 494 ? 54.081 29.973  -4.252  1.00 18.79  ? 519  THR   A CA  1 
ATOM   3607 C  C   . THR   A 1 494 ? 53.149 31.138  -3.840  1.00 17.72  ? 519  THR   A C   1 
ATOM   3608 O  O   . THR   A 1 494 ? 53.219 31.649  -2.745  1.00 17.71  ? 519  THR   A O   1 
ATOM   3609 C  CB  . THR   A 1 494 ? 55.208 30.457  -5.192  1.00 21.48  ? 519  THR   A CB  1 
ATOM   3610 O  OG1 . THR   A 1 494 ? 56.096 29.318  -5.391  1.00 24.69  ? 519  THR   A OG1 1 
ATOM   3611 C  CG2 . THR   A 1 494 ? 55.962 31.607  -4.605  1.00 22.88  ? 519  THR   A CG2 1 
ATOM   3612 N  N   . MET   A 1 495 ? 52.217 31.449  -4.716  1.00 18.04  ? 520  MET   A N   1 
ATOM   3613 C  CA  . MET   A 1 495 ? 51.267 32.542  -4.454  1.00 16.97  ? 520  MET   A CA  1 
ATOM   3614 C  C   . MET   A 1 495 ? 50.434 32.233  -3.225  1.00 16.77  ? 520  MET   A C   1 
ATOM   3615 O  O   . MET   A 1 495 ? 50.342 33.053  -2.295  1.00 16.10  ? 520  MET   A O   1 
ATOM   3616 C  CB  . MET   A 1 495 ? 50.346 32.740  -5.662  1.00 17.57  ? 520  MET   A CB  1 
ATOM   3617 C  CG  . MET   A 1 495 ? 49.105 33.600  -5.307  1.00 18.22  ? 520  MET   A CG  1 
ATOM   3618 S  SD  . MET   A 1 495 ? 47.995 33.759  -6.754  1.00 25.21  ? 520  MET   A SD  1 
ATOM   3619 C  CE  . MET   A 1 495 ? 48.729 35.049  -7.502  1.00 27.46  ? 520  MET   A CE  1 
ATOM   3620 N  N   . MET   A 1 496 ? 49.829 31.034  -3.220  1.00 15.81  ? 521  MET   A N   1 
ATOM   3621 C  CA  . MET   A 1 496 ? 48.888 30.750  -2.133  1.00 14.95  ? 521  MET   A CA  1 
ATOM   3622 C  C   . MET   A 1 496 ? 49.560 30.464  -0.823  1.00 15.56  ? 521  MET   A C   1 
ATOM   3623 O  O   . MET   A 1 496 ? 48.953 30.759  0.225   1.00 15.30  ? 521  MET   A O   1 
ATOM   3624 C  CB  . MET   A 1 496 ? 47.882 29.701  -2.529  1.00 16.47  ? 521  MET   A CB  1 
ATOM   3625 C  CG  . MET   A 1 496 ? 47.005 30.140  -3.681  1.00 16.23  ? 521  MET   A CG  1 
ATOM   3626 S  SD  . MET   A 1 496 ? 46.091 31.704  -3.408  1.00 18.35  ? 521  MET   A SD  1 
ATOM   3627 C  CE  . MET   A 1 496 ? 45.071 31.243  -2.070  1.00 19.59  ? 521  MET   A CE  1 
ATOM   3628 N  N   . ASN   A 1 497 ? 50.827 30.070  -0.811  1.00 15.48  ? 522  ASN   A N   1 
ATOM   3629 C  CA  . ASN   A 1 497 ? 51.561 29.984  0.436   1.00 16.00  ? 522  ASN   A CA  1 
ATOM   3630 C  C   . ASN   A 1 497 ? 51.750 31.377  1.039   1.00 15.28  ? 522  ASN   A C   1 
ATOM   3631 O  O   . ASN   A 1 497 ? 51.732 31.531  2.250   1.00 15.14  ? 522  ASN   A O   1 
ATOM   3632 C  CB  . ASN   A 1 497 ? 52.894 29.264  0.233   1.00 17.02  ? 522  ASN   A CB  1 
ATOM   3633 C  CG  . ASN   A 1 497 ? 52.731 27.746  0.229   1.00 19.79  ? 522  ASN   A CG  1 
ATOM   3634 O  OD1 . ASN   A 1 497 ? 51.681 27.197  0.568   1.00 20.80  ? 522  ASN   A OD1 1 
ATOM   3635 N  ND2 . ASN   A 1 497 ? 53.811 27.066  -0.243  1.00 23.48  ? 522  ASN   A ND2 1 
ATOM   3636 N  N   . THR   A 1 498 ? 51.949 32.435  0.187   1.00 14.21  ? 523  THR   A N   1 
ATOM   3637 C  CA  . THR   A 1 498 ? 52.083 33.769  0.760   1.00 14.42  ? 523  THR   A CA  1 
ATOM   3638 C  C   . THR   A 1 498 ? 50.798 34.193  1.492   1.00 14.50  ? 523  THR   A C   1 
ATOM   3639 O  O   . THR   A 1 498 ? 50.882 34.931  2.457   1.00 14.98  ? 523  THR   A O   1 
ATOM   3640 C  CB  . THR   A 1 498 ? 52.524 34.841  -0.277  1.00 15.03  ? 523  THR   A CB  1 
ATOM   3641 O  OG1 . THR   A 1 498 ? 51.465 35.217  -1.182  1.00 15.35  ? 523  THR   A OG1 1 
ATOM   3642 C  CG2 . THR   A 1 498 ? 53.769 34.401  -1.049  1.00 15.90  ? 523  THR   A CG2 1 
ATOM   3643 N  N   . TRP   A 1 499 ? 49.635 33.730  1.025   1.00 13.90  ? 524  TRP   A N   1 
ATOM   3644 C  CA  . TRP   A 1 499 ? 48.358 34.130  1.638   1.00 13.57  ? 524  TRP   A CA  1 
ATOM   3645 C  C   . TRP   A 1 499 ? 47.935 33.228  2.777   1.00 13.56  ? 524  TRP   A C   1 
ATOM   3646 O  O   . TRP   A 1 499 ? 47.016 33.599  3.502   1.00 14.32  ? 524  TRP   A O   1 
ATOM   3647 C  CB  . TRP   A 1 499 ? 47.258 34.149  0.578   1.00 13.42  ? 524  TRP   A CB  1 
ATOM   3648 C  CG  . TRP   A 1 499 ? 47.501 35.218  -0.457  1.00 12.31  ? 524  TRP   A CG  1 
ATOM   3649 C  CD1 . TRP   A 1 499 ? 47.908 35.035  -1.752  1.00 13.30  ? 524  TRP   A CD1 1 
ATOM   3650 C  CD2 . TRP   A 1 499 ? 47.402 36.631  -0.256  1.00 13.11  ? 524  TRP   A CD2 1 
ATOM   3651 N  NE1 . TRP   A 1 499 ? 48.102 36.268  -2.369  1.00 13.06  ? 524  TRP   A NE1 1 
ATOM   3652 C  CE2 . TRP   A 1 499 ? 47.753 37.254  -1.476  1.00 12.83  ? 524  TRP   A CE2 1 
ATOM   3653 C  CE3 . TRP   A 1 499 ? 47.046 37.435  0.837   1.00 13.80  ? 524  TRP   A CE3 1 
ATOM   3654 C  CZ2 . TRP   A 1 499 ? 47.750 38.638  -1.628  1.00 13.85  ? 524  TRP   A CZ2 1 
ATOM   3655 C  CZ3 . TRP   A 1 499 ? 47.073 38.814  0.694   1.00 13.87  ? 524  TRP   A CZ3 1 
ATOM   3656 C  CH2 . TRP   A 1 499 ? 47.435 39.402  -0.529  1.00 15.08  ? 524  TRP   A CH2 1 
ATOM   3657 N  N   . THR   A 1 500 ? 48.543 32.043  2.930   1.00 14.27  ? 525  THR   A N   1 
ATOM   3658 C  CA  . THR   A 1 500 ? 48.130 31.091  4.001   1.00 13.82  ? 525  THR   A CA  1 
ATOM   3659 C  C   . THR   A 1 500 ? 49.150 30.895  5.077   1.00 15.26  ? 525  THR   A C   1 
ATOM   3660 O  O   . THR   A 1 500 ? 48.775 30.486  6.187   1.00 15.27  ? 525  THR   A O   1 
ATOM   3661 C  CB  . THR   A 1 500 ? 47.734 29.751  3.420   1.00 14.84  ? 525  THR   A CB  1 
ATOM   3662 O  OG1 . THR   A 1 500 ? 48.797 29.258  2.573   1.00 15.90  ? 525  THR   A OG1 1 
ATOM   3663 C  CG2 . THR   A 1 500 ? 46.416 29.816  2.645   1.00 16.08  ? 525  THR   A CG2 1 
ATOM   3664 N  N   . LEU   A 1 501 ? 50.448 31.199  4.808   1.00 16.32  ? 526  LEU   A N   1 
ATOM   3665 C  CA  . LEU   A 1 501 ? 51.487 30.944  5.798   1.00 17.57  ? 526  LEU   A CA  1 
ATOM   3666 C  C   . LEU   A 1 501 ? 52.070 32.194  6.475   1.00 18.98  ? 526  LEU   A C   1 
ATOM   3667 O  O   . LEU   A 1 501 ? 52.970 32.078  7.333   1.00 21.75  ? 526  LEU   A O   1 
ATOM   3668 C  CB  . LEU   A 1 501 ? 52.618 30.092  5.170   1.00 17.95  ? 526  LEU   A CB  1 
ATOM   3669 C  CG  . LEU   A 1 501 ? 52.135 28.775  4.575   1.00 19.37  ? 526  LEU   A CG  1 
ATOM   3670 C  CD1 . LEU   A 1 501 ? 53.283 28.018  3.901   1.00 20.32  ? 526  LEU   A CD1 1 
ATOM   3671 C  CD2 . LEU   A 1 501 ? 51.552 27.827  5.650   1.00 19.42  ? 526  LEU   A CD2 1 
ATOM   3672 N  N   . GLN   A 1 502 ? 51.628 33.372  6.064   1.00 17.87  ? 527  GLN   A N   1 
ATOM   3673 C  CA  . GLN   A 1 502 ? 52.019 34.665  6.615   1.00 19.12  ? 527  GLN   A CA  1 
ATOM   3674 C  C   . GLN   A 1 502 ? 50.765 35.301  7.142   1.00 16.96  ? 527  GLN   A C   1 
ATOM   3675 O  O   . GLN   A 1 502 ? 49.735 35.291  6.456   1.00 15.85  ? 527  GLN   A O   1 
ATOM   3676 C  CB  . GLN   A 1 502 ? 52.490 35.678  5.494   1.00 22.66  ? 527  GLN   A CB  1 
ATOM   3677 C  CG  . GLN   A 1 502 ? 53.748 35.311  4.784   1.00 28.08  ? 527  GLN   A CG  1 
ATOM   3678 C  CD  . GLN   A 1 502 ? 54.139 36.417  3.870   1.00 25.94  ? 527  GLN   A CD  1 
ATOM   3679 O  OE1 . GLN   A 1 502 ? 55.181 37.100  4.036   1.00 30.59  ? 527  GLN   A OE1 1 
ATOM   3680 N  NE2 . GLN   A 1 502 ? 53.359 36.621  2.851   1.00 16.78  ? 527  GLN   A NE2 1 
ATOM   3681 N  N   . ARG   A 1 503 ? 50.836 35.927  8.310   1.00 16.55  ? 528  ARG   A N   1 
ATOM   3682 C  CA  . ARG   A 1 503 ? 49.687 36.698  8.776   1.00 16.81  ? 528  ARG   A CA  1 
ATOM   3683 C  C   . ARG   A 1 503 ? 49.535 37.973  7.923   1.00 16.02  ? 528  ARG   A C   1 
ATOM   3684 O  O   . ARG   A 1 503 ? 50.498 38.406  7.216   1.00 16.47  ? 528  ARG   A O   1 
ATOM   3685 C  CB  . ARG   A 1 503 ? 49.890 37.112  10.245  1.00 17.96  ? 528  ARG   A CB  1 
ATOM   3686 C  CG  . ARG   A 1 503 ? 50.979 38.162  10.402  1.00 19.96  ? 528  ARG   A CG  1 
ATOM   3687 C  CD  . ARG   A 1 503 ? 51.177 38.668  11.836  1.00 25.89  ? 528  ARG   A CD  1 
ATOM   3688 N  NE  . ARG   A 1 503 ? 51.476 37.567  12.732  1.00 28.40  ? 528  ARG   A NE  1 
ATOM   3689 C  CZ  . ARG   A 1 503 ? 52.699 37.162  13.060  1.00 32.25  ? 528  ARG   A CZ  1 
ATOM   3690 N  NH1 . ARG   A 1 503 ? 52.866 36.151  13.907  1.00 33.15  ? 528  ARG   A NH1 1 
ATOM   3691 N  NH2 . ARG   A 1 503 ? 53.767 37.777  12.563  1.00 33.38  ? 528  ARG   A NH2 1 
ATOM   3692 N  N   . GLY   A 1 504 ? 48.388 38.613  8.028   1.00 15.68  ? 529  GLY   A N   1 
ATOM   3693 C  CA  . GLY   A 1 504 ? 48.214 39.943  7.506   1.00 16.01  ? 529  GLY   A CA  1 
ATOM   3694 C  C   . GLY   A 1 504 ? 48.025 40.051  6.017   1.00 15.15  ? 529  GLY   A C   1 
ATOM   3695 O  O   . GLY   A 1 504 ? 47.696 39.081  5.321   1.00 14.54  ? 529  GLY   A O   1 
ATOM   3696 N  N   . PHE   A 1 505 ? 48.143 41.288  5.557   1.00 13.32  ? 530  PHE   A N   1 
ATOM   3697 C  CA  . PHE   A 1 505 ? 47.942 41.548  4.144   1.00 13.85  ? 530  PHE   A CA  1 
ATOM   3698 C  C   . PHE   A 1 505 ? 48.760 42.793  3.799   1.00 13.63  ? 530  PHE   A C   1 
ATOM   3699 O  O   . PHE   A 1 505 ? 49.176 43.568  4.674   1.00 13.71  ? 530  PHE   A O   1 
ATOM   3700 C  CB  . PHE   A 1 505 ? 46.421 41.788  3.886   1.00 14.09  ? 530  PHE   A CB  1 
ATOM   3701 C  CG  . PHE   A 1 505 ? 45.832 42.869  4.757   1.00 13.56  ? 530  PHE   A CG  1 
ATOM   3702 C  CD1 . PHE   A 1 505 ? 45.839 44.184  4.354   1.00 14.85  ? 530  PHE   A CD1 1 
ATOM   3703 C  CD2 . PHE   A 1 505 ? 45.252 42.557  5.987   1.00 13.88  ? 530  PHE   A CD2 1 
ATOM   3704 C  CE1 . PHE   A 1 505 ? 45.284 45.186  5.156   1.00 14.38  ? 530  PHE   A CE1 1 
ATOM   3705 C  CE2 . PHE   A 1 505 ? 44.734 43.558  6.809   1.00 14.39  ? 530  PHE   A CE2 1 
ATOM   3706 C  CZ  . PHE   A 1 505 ? 44.736 44.868  6.383   1.00 15.23  ? 530  PHE   A CZ  1 
ATOM   3707 N  N   . PRO   A 1 506 ? 48.959 43.034  2.492   1.00 13.09  ? 531  PRO   A N   1 
ATOM   3708 C  CA  . PRO   A 1 506 ? 49.763 44.178  2.094   1.00 13.46  ? 531  PRO   A CA  1 
ATOM   3709 C  C   . PRO   A 1 506 ? 48.969 45.454  1.865   1.00 13.15  ? 531  PRO   A C   1 
ATOM   3710 O  O   . PRO   A 1 506 ? 47.778 45.450  1.518   1.00 13.35  ? 531  PRO   A O   1 
ATOM   3711 C  CB  . PRO   A 1 506 ? 50.356 43.707  0.760   1.00 14.14  ? 531  PRO   A CB  1 
ATOM   3712 C  CG  . PRO   A 1 506 ? 49.324 42.787  0.175   1.00 13.85  ? 531  PRO   A CG  1 
ATOM   3713 C  CD  . PRO   A 1 506 ? 48.671 42.107  1.367   1.00 13.28  ? 531  PRO   A CD  1 
ATOM   3714 N  N   . LEU   A 1 507 ? 49.688 46.550  2.046   1.00 13.05  ? 532  LEU   A N   1 
ATOM   3715 C  CA  . LEU   A 1 507 ? 49.338 47.838  1.541   1.00 13.10  ? 532  LEU   A CA  1 
ATOM   3716 C  C   . LEU   A 1 507 ? 50.053 47.946  0.163   1.00 12.63  ? 532  LEU   A C   1 
ATOM   3717 O  O   . LEU   A 1 507 ? 51.279 47.755  0.064   1.00 13.02  ? 532  LEU   A O   1 
ATOM   3718 C  CB  . LEU   A 1 507 ? 49.893 48.930  2.466   1.00 14.54  ? 532  LEU   A CB  1 
ATOM   3719 C  CG  . LEU   A 1 507 ? 49.790 50.346  1.888   1.00 15.74  ? 532  LEU   A CG  1 
ATOM   3720 C  CD1 . LEU   A 1 507 ? 48.327 50.765  1.668   1.00 16.15  ? 532  LEU   A CD1 1 
ATOM   3721 C  CD2 . LEU   A 1 507 ? 50.552 51.357  2.744   1.00 17.73  ? 532  LEU   A CD2 1 
ATOM   3722 N  N   . ILE   A 1 508 ? 49.278 48.254  -0.882  1.00 12.26  ? 533  ILE   A N   1 
ATOM   3723 C  CA  . ILE   A 1 508 ? 49.800 48.483  -2.240  1.00 12.12  ? 533  ILE   A CA  1 
ATOM   3724 C  C   . ILE   A 1 508 ? 49.806 49.959  -2.417  1.00 12.48  ? 533  ILE   A C   1 
ATOM   3725 O  O   . ILE   A 1 508 ? 48.736 50.592  -2.283  1.00 13.34  ? 533  ILE   A O   1 
ATOM   3726 C  CB  . ILE   A 1 508 ? 48.904 47.819  -3.290  1.00 13.15  ? 533  ILE   A CB  1 
ATOM   3727 C  CG1 . ILE   A 1 508 ? 48.716 46.337  -2.994  1.00 13.75  ? 533  ILE   A CG1 1 
ATOM   3728 C  CG2 . ILE   A 1 508 ? 49.475 48.053  -4.705  1.00 13.71  ? 533  ILE   A CG2 1 
ATOM   3729 C  CD1 . ILE   A 1 508 ? 50.080 45.496  -2.976  1.00 14.39  ? 533  ILE   A CD1 1 
ATOM   3730 N  N   . THR   A 1 509 ? 50.990 50.563  -2.674  1.00 12.68  ? 534  THR   A N   1 
ATOM   3731 C  CA  . THR   A 1 509 ? 51.073 52.017  -2.903  1.00 12.59  ? 534  THR   A CA  1 
ATOM   3732 C  C   . THR   A 1 509 ? 51.267 52.275  -4.387  1.00 12.96  ? 534  THR   A C   1 
ATOM   3733 O  O   . THR   A 1 509 ? 52.165 51.677  -5.008  1.00 13.45  ? 534  THR   A O   1 
ATOM   3734 C  CB  . THR   A 1 509 ? 52.185 52.652  -2.089  1.00 13.93  ? 534  THR   A CB  1 
ATOM   3735 O  OG1 . THR   A 1 509 ? 51.936 52.397  -0.689  1.00 15.07  ? 534  THR   A OG1 1 
ATOM   3736 C  CG2 . THR   A 1 509 ? 52.256 54.154  -2.306  1.00 15.13  ? 534  THR   A CG2 1 
ATOM   3737 N  N   . ILE   A 1 510 ? 50.431 53.158  -4.924  1.00 12.53  ? 535  ILE   A N   1 
ATOM   3738 C  CA  . ILE   A 1 510 ? 50.424 53.493  -6.363  1.00 12.75  ? 535  ILE   A CA  1 
ATOM   3739 C  C   . ILE   A 1 510 ? 50.910 54.925  -6.552  1.00 14.49  ? 535  ILE   A C   1 
ATOM   3740 O  O   . ILE   A 1 510 ? 50.406 55.845  -5.896  1.00 15.89  ? 535  ILE   A O   1 
ATOM   3741 C  CB  . ILE   A 1 510 ? 48.961 53.398  -6.870  1.00 13.68  ? 535  ILE   A CB  1 
ATOM   3742 C  CG1 . ILE   A 1 510 ? 48.401 51.992  -6.626  1.00 14.08  ? 535  ILE   A CG1 1 
ATOM   3743 C  CG2 . ILE   A 1 510 ? 48.876 53.809  -8.354  1.00 14.59  ? 535  ILE   A CG2 1 
ATOM   3744 C  CD1 . ILE   A 1 510 ? 49.186 50.857  -7.324  1.00 14.17  ? 535  ILE   A CD1 1 
ATOM   3745 N  N   . THR   A 1 511 ? 51.857 55.121  -7.471  1.00 14.34  ? 536  THR   A N   1 
ATOM   3746 C  CA  . THR   A 1 511 ? 52.362 56.456  -7.767  1.00 14.59  ? 536  THR   A CA  1 
ATOM   3747 C  C   . THR   A 1 511 ? 52.321 56.610  -9.285  1.00 14.80  ? 536  THR   A C   1 
ATOM   3748 O  O   . THR   A 1 511 ? 52.937 55.831  -9.988  1.00 14.67  ? 536  THR   A O   1 
ATOM   3749 C  CB  . THR   A 1 511 ? 53.793 56.595  -7.273  1.00 16.07  ? 536  THR   A CB  1 
ATOM   3750 O  OG1 . THR   A 1 511 ? 53.877 56.152  -5.913  1.00 17.63  ? 536  THR   A OG1 1 
ATOM   3751 C  CG2 . THR   A 1 511 ? 54.320 58.010  -7.417  1.00 17.11  ? 536  THR   A CG2 1 
ATOM   3752 N  N   . VAL   A 1 512 ? 51.575 57.592  -9.778  1.00 15.61  ? 537  VAL   A N   1 
ATOM   3753 C  CA  . VAL   A 1 512 ? 51.369 57.798  -11.218 1.00 15.77  ? 537  VAL   A CA  1 
ATOM   3754 C  C   . VAL   A 1 512 ? 52.133 59.006  -11.682 1.00 16.89  ? 537  VAL   A C   1 
ATOM   3755 O  O   . VAL   A 1 512 ? 51.989 60.096  -11.095 1.00 17.93  ? 537  VAL   A O   1 
ATOM   3756 C  CB  . VAL   A 1 512 ? 49.861 57.938  -11.529 1.00 17.81  ? 537  VAL   A CB  1 
ATOM   3757 C  CG1 . VAL   A 1 512 ? 49.660 58.048  -13.044 1.00 19.81  ? 537  VAL   A CG1 1 
ATOM   3758 C  CG2 . VAL   A 1 512 ? 49.096 56.727  -11.001 1.00 18.58  ? 537  VAL   A CG2 1 
ATOM   3759 N  N   . ARG   A 1 513 ? 52.942 58.849  -12.728 1.00 15.94  ? 538  ARG   A N   1 
ATOM   3760 C  CA  . ARG   A 1 513 ? 53.652 59.985  -13.306 1.00 16.22  ? 538  ARG   A CA  1 
ATOM   3761 C  C   . ARG   A 1 513 ? 53.420 59.858  -14.805 1.00 15.64  ? 538  ARG   A C   1 
ATOM   3762 O  O   . ARG   A 1 513 ? 54.070 59.054  -15.465 1.00 16.12  ? 538  ARG   A O   1 
ATOM   3763 C  CB  . ARG   A 1 513 ? 55.142 59.890  -12.964 1.00 19.52  ? 538  ARG   A CB  1 
ATOM   3764 C  CG  . ARG   A 1 513 ? 55.302 60.133  -11.480 1.00 26.27  ? 538  ARG   A CG  1 
ATOM   3765 C  CD  . ARG   A 1 513 ? 56.673 59.972  -10.852 1.00 33.85  ? 538  ARG   A CD  1 
ATOM   3766 N  NE  . ARG   A 1 513 ? 56.805 60.297  -9.407  1.00 39.79  ? 538  ARG   A NE  1 
ATOM   3767 C  CZ  . ARG   A 1 513 ? 55.920 60.926  -8.619  1.00 44.05  ? 538  ARG   A CZ  1 
ATOM   3768 N  NH1 . ARG   A 1 513 ? 56.209 61.166  -7.346  1.00 41.57  ? 538  ARG   A NH1 1 
ATOM   3769 N  NH2 . ARG   A 1 513 ? 54.723 61.264  -9.086  1.00 45.85  ? 538  ARG   A NH2 1 
ATOM   3770 N  N   . GLY   A 1 514 ? 52.432 60.581  -15.305 1.00 17.25  ? 539  GLY   A N   1 
ATOM   3771 C  CA  . GLY   A 1 514 ? 52.026 60.437  -16.701 1.00 17.95  ? 539  GLY   A CA  1 
ATOM   3772 C  C   . GLY   A 1 514 ? 51.497 59.030  -16.965 1.00 17.60  ? 539  GLY   A C   1 
ATOM   3773 O  O   . GLY   A 1 514 ? 50.582 58.551  -16.276 1.00 18.65  ? 539  GLY   A O   1 
ATOM   3774 N  N   . ARG   A 1 515 ? 52.103 58.332  -17.916 1.00 15.89  ? 540  ARG   A N   1 
ATOM   3775 C  CA  . ARG   A 1 515 ? 51.696 56.956  -18.217 1.00 14.67  ? 540  ARG   A CA  1 
ATOM   3776 C  C   . ARG   A 1 515 ? 52.357 55.928  -17.290 1.00 14.22  ? 540  ARG   A C   1 
ATOM   3777 O  O   . ARG   A 1 515 ? 51.945 54.787  -17.255 1.00 14.21  ? 540  ARG   A O   1 
ATOM   3778 C  CB  . ARG   A 1 515 ? 52.051 56.552  -19.668 1.00 15.99  ? 540  ARG   A CB  1 
ATOM   3779 C  CG  . ARG   A 1 515 ? 51.337 57.397  -20.720 1.00 18.51  ? 540  ARG   A CG  1 
ATOM   3780 C  CD  . ARG   A 1 515 ? 51.987 57.183  -22.112 1.00 20.39  ? 540  ARG   A CD  1 
ATOM   3781 N  NE  . ARG   A 1 515 ? 51.983 55.777  -22.511 1.00 23.26  ? 540  ARG   A NE  1 
ATOM   3782 C  CZ  . ARG   A 1 515 ? 52.667 55.271  -23.518 1.00 24.30  ? 540  ARG   A CZ  1 
ATOM   3783 N  NH1 . ARG   A 1 515 ? 53.515 56.038  -24.210 1.00 27.18  ? 540  ARG   A NH1 1 
ATOM   3784 N  NH2 . ARG   A 1 515 ? 52.580 53.980  -23.799 1.00 24.83  ? 540  ARG   A NH2 1 
ATOM   3785 N  N   . ASN   A 1 516 ? 53.355 56.341  -16.479 1.00 13.84  ? 541  ASN   A N   1 
ATOM   3786 C  CA  . ASN   A 1 516 ? 54.090 55.418  -15.638 1.00 13.70  ? 541  ASN   A CA  1 
ATOM   3787 C  C   . ASN   A 1 516 ? 53.354 55.176  -14.319 1.00 14.23  ? 541  ASN   A C   1 
ATOM   3788 O  O   . ASN   A 1 516 ? 53.100 56.126  -13.575 1.00 14.54  ? 541  ASN   A O   1 
ATOM   3789 C  CB  . ASN   A 1 516 ? 55.461 56.095  -15.359 1.00 13.96  ? 541  ASN   A CB  1 
ATOM   3790 C  CG  . ASN   A 1 516 ? 56.390 55.169  -14.660 1.00 15.55  ? 541  ASN   A CG  1 
ATOM   3791 O  OD1 . ASN   A 1 516 ? 56.249 54.884  -13.470 1.00 16.56  ? 541  ASN   A OD1 1 
ATOM   3792 N  ND2 . ASN   A 1 516 ? 57.373 54.676  -15.397 1.00 17.27  ? 541  ASN   A ND2 1 
ATOM   3793 N  N   . VAL   A 1 517 ? 52.998 53.897  -14.045 1.00 13.38  ? 542  VAL   A N   1 
ATOM   3794 C  CA  . VAL   A 1 517 ? 52.334 53.538  -12.801 1.00 12.78  ? 542  VAL   A CA  1 
ATOM   3795 C  C   . VAL   A 1 517 ? 53.279 52.673  -12.015 1.00 13.10  ? 542  VAL   A C   1 
ATOM   3796 O  O   . VAL   A 1 517 ? 53.621 51.553  -12.410 1.00 14.49  ? 542  VAL   A O   1 
ATOM   3797 C  CB  . VAL   A 1 517 ? 51.045 52.769  -13.125 1.00 13.62  ? 542  VAL   A CB  1 
ATOM   3798 C  CG1 . VAL   A 1 517 ? 50.368 52.303  -11.831 1.00 14.90  ? 542  VAL   A CG1 1 
ATOM   3799 C  CG2 . VAL   A 1 517 ? 50.104 53.664  -13.930 1.00 14.71  ? 542  VAL   A CG2 1 
ATOM   3800 N  N   . HIS   A 1 518 ? 53.771 53.240  -10.914 1.00 12.03  ? 543  HIS   A N   1 
ATOM   3801 C  CA  . HIS   A 1 518 ? 54.698 52.544  -10.041 1.00 12.62  ? 543  HIS   A CA  1 
ATOM   3802 C  C   . HIS   A 1 518 ? 53.910 51.876  -8.925  1.00 12.88  ? 543  HIS   A C   1 
ATOM   3803 O  O   . HIS   A 1 518 ? 52.984 52.514  -8.361  1.00 13.05  ? 543  HIS   A O   1 
ATOM   3804 C  CB  . HIS   A 1 518 ? 55.668 53.607  -9.463  1.00 13.83  ? 543  HIS   A CB  1 
ATOM   3805 C  CG  . HIS   A 1 518 ? 56.748 53.062  -8.608  1.00 15.53  ? 543  HIS   A CG  1 
ATOM   3806 N  ND1 . HIS   A 1 518 ? 58.023 52.819  -9.133  1.00 17.40  ? 543  HIS   A ND1 1 
ATOM   3807 C  CD2 . HIS   A 1 518 ? 56.743 52.741  -7.292  1.00 17.09  ? 543  HIS   A CD2 1 
ATOM   3808 C  CE1 . HIS   A 1 518 ? 58.743 52.326  -8.117  1.00 19.79  ? 543  HIS   A CE1 1 
ATOM   3809 N  NE2 . HIS   A 1 518 ? 58.039 52.267  -6.999  1.00 19.66  ? 543  HIS   A NE2 1 
ATOM   3810 N  N   . MET   A 1 519 ? 54.255 50.623  -8.637  1.00 12.43  ? 544  MET   A N   1 
ATOM   3811 C  CA  . MET   A 1 519 ? 53.563 49.864  -7.599  1.00 13.07  ? 544  MET   A CA  1 
ATOM   3812 C  C   . MET   A 1 519 ? 54.566 49.394  -6.555  1.00 13.92  ? 544  MET   A C   1 
ATOM   3813 O  O   . MET   A 1 519 ? 55.668 48.949  -6.910  1.00 14.84  ? 544  MET   A O   1 
ATOM   3814 C  CB  . MET   A 1 519 ? 52.915 48.607  -8.223  1.00 14.18  ? 544  MET   A CB  1 
ATOM   3815 C  CG  . MET   A 1 519 ? 51.767 48.940  -9.183  1.00 15.25  ? 544  MET   A CG  1 
ATOM   3816 S  SD  . MET   A 1 519 ? 51.436 47.611  -10.364 1.00 15.99  ? 544  MET   A SD  1 
ATOM   3817 C  CE  . MET   A 1 519 ? 52.801 47.896  -11.528 1.00 14.00  ? 544  MET   A CE  1 
ATOM   3818 N  N   . LYS   A 1 520 ? 54.193 49.440  -5.273  1.00 13.37  ? 545  LYS   A N   1 
ATOM   3819 C  CA  . LYS   A 1 520 ? 55.016 48.893  -4.208  1.00 13.48  ? 545  LYS   A CA  1 
ATOM   3820 C  C   . LYS   A 1 520 ? 54.093 48.131  -3.273  1.00 13.32  ? 545  LYS   A C   1 
ATOM   3821 O  O   . LYS   A 1 520 ? 52.917 48.476  -3.129  1.00 13.68  ? 545  LYS   A O   1 
ATOM   3822 C  CB  . LYS   A 1 520 ? 55.643 50.081  -3.428  1.00 16.71  ? 545  LYS   A CB  1 
ATOM   3823 C  CG  . LYS   A 1 520 ? 56.395 49.700  -2.157  1.00 22.17  ? 545  LYS   A CG  1 
ATOM   3824 C  CD  . LYS   A 1 520 ? 56.704 50.918  -1.221  1.00 25.59  ? 545  LYS   A CD  1 
ATOM   3825 C  CE  . LYS   A 1 520 ? 57.352 50.321  0.032   1.00 29.24  ? 545  LYS   A CE  1 
ATOM   3826 N  NZ  . LYS   A 1 520 ? 57.286 51.207  1.224   1.00 30.70  ? 545  LYS   A NZ  1 
ATOM   3827 N  N   . GLN   A 1 521 ? 54.628 47.115  -2.616  1.00 11.90  ? 546  GLN   A N   1 
ATOM   3828 C  CA  . GLN   A 1 521 ? 53.880 46.437  -1.545  1.00 12.68  ? 546  GLN   A CA  1 
ATOM   3829 C  C   . GLN   A 1 521 ? 54.672 46.455  -0.251  1.00 13.86  ? 546  GLN   A C   1 
ATOM   3830 O  O   . GLN   A 1 521 ? 55.920 46.466  -0.239  1.00 14.54  ? 546  GLN   A O   1 
ATOM   3831 C  CB  . GLN   A 1 521 ? 53.535 44.993  -1.898  1.00 13.38  ? 546  GLN   A CB  1 
ATOM   3832 C  CG  . GLN   A 1 521 ? 54.789 44.135  -2.156  1.00 13.24  ? 546  GLN   A CG  1 
ATOM   3833 C  CD  . GLN   A 1 521 ? 54.396 42.660  -2.198  1.00 14.02  ? 546  GLN   A CD  1 
ATOM   3834 O  OE1 . GLN   A 1 521 ? 53.970 42.074  -1.179  1.00 14.72  ? 546  GLN   A OE1 1 
ATOM   3835 N  NE2 . GLN   A 1 521 ? 54.531 42.023  -3.367  1.00 14.29  ? 546  GLN   A NE2 1 
ATOM   3836 N  N   . GLU   A 1 522 ? 53.936 46.516  0.851   1.00 13.81  ? 547  GLU   A N   1 
ATOM   3837 C  CA  . GLU   A 1 522 ? 54.527 46.394  2.194   1.00 14.55  ? 547  GLU   A CA  1 
ATOM   3838 C  C   . GLU   A 1 522 ? 53.489 45.831  3.116   1.00 15.71  ? 547  GLU   A C   1 
ATOM   3839 O  O   . GLU   A 1 522 ? 52.297 45.978  2.833   1.00 15.74  ? 547  GLU   A O   1 
ATOM   3840 C  CB  . GLU   A 1 522 ? 55.048 47.737  2.740   1.00 16.58  ? 547  GLU   A CB  1 
ATOM   3841 C  CG  . GLU   A 1 522 ? 53.931 48.705  3.039   1.00 18.05  ? 547  GLU   A CG  1 
ATOM   3842 C  CD  . GLU   A 1 522 ? 54.445 50.124  3.051   1.00 22.32  ? 547  GLU   A CD  1 
ATOM   3843 O  OE1 . GLU   A 1 522 ? 54.598 50.737  1.964   1.00 19.69  ? 547  GLU   A OE1 1 
ATOM   3844 O  OE2 . GLU   A 1 522 ? 54.722 50.618  4.173   1.00 26.36  ? 547  GLU   A OE2 1 
ATOM   3845 N  N   . HIS   A 1 523 ? 53.887 45.215  4.230   1.00 15.43  ? 548  HIS   A N   1 
ATOM   3846 C  CA  . HIS   A 1 523 ? 52.866 44.698  5.177   1.00 16.00  ? 548  HIS   A CA  1 
ATOM   3847 C  C   . HIS   A 1 523 ? 52.071 45.827  5.798   1.00 17.29  ? 548  HIS   A C   1 
ATOM   3848 O  O   . HIS   A 1 523 ? 52.683 46.747  6.376   1.00 18.08  ? 548  HIS   A O   1 
ATOM   3849 C  CB  . HIS   A 1 523 ? 53.570 43.921  6.273   1.00 17.31  ? 548  HIS   A CB  1 
ATOM   3850 C  CG  . HIS   A 1 523 ? 52.685 43.383  7.369   1.00 20.27  ? 548  HIS   A CG  1 
ATOM   3851 N  ND1 . HIS   A 1 523 ? 53.191 43.160  8.657   1.00 25.14  ? 548  HIS   A ND1 1 
ATOM   3852 C  CD2 . HIS   A 1 523 ? 51.384 42.999  7.347   1.00 20.05  ? 548  HIS   A CD2 1 
ATOM   3853 C  CE1 . HIS   A 1 523 ? 52.189 42.635  9.367   1.00 24.76  ? 548  HIS   A CE1 1 
ATOM   3854 N  NE2 . HIS   A 1 523 ? 51.095 42.465  8.624   1.00 22.47  ? 548  HIS   A NE2 1 
ATOM   3855 N  N   . TYR   A 1 524 ? 50.715 45.765  5.743   1.00 16.18  ? 549  TYR   A N   1 
ATOM   3856 C  CA  . TYR   A 1 524 ? 49.901 46.754  6.423   1.00 16.18  ? 549  TYR   A CA  1 
ATOM   3857 C  C   . TYR   A 1 524 ? 49.767 46.308  7.899   1.00 17.60  ? 549  TYR   A C   1 
ATOM   3858 O  O   . TYR   A 1 524 ? 49.260 45.206  8.148   1.00 17.99  ? 549  TYR   A O   1 
ATOM   3859 C  CB  . TYR   A 1 524 ? 48.495 46.832  5.795   1.00 15.63  ? 549  TYR   A CB  1 
ATOM   3860 C  CG  . TYR   A 1 524 ? 47.582 47.780  6.549   1.00 15.46  ? 549  TYR   A CG  1 
ATOM   3861 C  CD1 . TYR   A 1 524 ? 46.847 47.343  7.637   1.00 16.95  ? 549  TYR   A CD1 1 
ATOM   3862 C  CD2 . TYR   A 1 524 ? 47.503 49.123  6.205   1.00 16.20  ? 549  TYR   A CD2 1 
ATOM   3863 C  CE1 . TYR   A 1 524 ? 46.020 48.204  8.345   1.00 16.81  ? 549  TYR   A CE1 1 
ATOM   3864 C  CE2 . TYR   A 1 524 ? 46.666 50.000  6.897   1.00 16.67  ? 549  TYR   A CE2 1 
ATOM   3865 C  CZ  . TYR   A 1 524 ? 45.950 49.535  7.986   1.00 17.15  ? 549  TYR   A CZ  1 
ATOM   3866 O  OH  . TYR   A 1 524 ? 45.155 50.382  8.736   1.00 17.73  ? 549  TYR   A OH  1 
ATOM   3867 N  N   . MET   A 1 525 ? 50.187 47.152  8.848   1.00 19.11  ? 550  MET   A N   1 
ATOM   3868 C  CA  . MET   A 1 525 ? 50.016 46.758  10.254  1.00 21.90  ? 550  MET   A CA  1 
ATOM   3869 C  C   . MET   A 1 525 ? 49.784 47.972  11.105  1.00 22.31  ? 550  MET   A C   1 
ATOM   3870 O  O   . MET   A 1 525 ? 50.500 48.970  10.999  1.00 22.57  ? 550  MET   A O   1 
ATOM   3871 C  CB  . MET   A 1 525 ? 51.214 45.966  10.742  1.00 25.49  ? 550  MET   A CB  1 
ATOM   3872 C  CG  . MET   A 1 525 ? 51.078 45.511  12.166  1.00 29.89  ? 550  MET   A CG  1 
ATOM   3873 S  SD  . MET   A 1 525 ? 52.467 44.444  12.635  1.00 37.07  ? 550  MET   A SD  1 
ATOM   3874 C  CE  . MET   A 1 525 ? 53.712 45.696  13.006  1.00 38.74  ? 550  MET   A CE  1 
ATOM   3875 N  N   . LYS   A 1 526 ? 48.838 47.839  12.042  1.00 21.06  ? 551  LYS   A N   1 
ATOM   3876 C  CA  . LYS   A 1 526 ? 48.600 48.920  13.003  1.00 22.13  ? 551  LYS   A CA  1 
ATOM   3877 C  C   . LYS   A 1 526 ? 49.612 48.754  14.162  1.00 25.44  ? 551  LYS   A C   1 
ATOM   3878 O  O   . LYS   A 1 526 ? 49.936 47.633  14.525  1.00 25.39  ? 551  LYS   A O   1 
ATOM   3879 C  CB  . LYS   A 1 526 ? 47.151 48.823  13.525  1.00 21.47  ? 551  LYS   A CB  1 
ATOM   3880 C  CG  . LYS   A 1 526 ? 46.188 49.223  12.417  1.00 22.82  ? 551  LYS   A CG  1 
ATOM   3881 C  CD  . LYS   A 1 526 ? 44.795 49.355  12.877  1.00 23.69  ? 551  LYS   A CD  1 
ATOM   3882 C  CE  . LYS   A 1 526 ? 43.882 49.594  11.708  1.00 23.25  ? 551  LYS   A CE  1 
ATOM   3883 N  NZ  . LYS   A 1 526 ? 42.493 49.959  12.177  1.00 25.01  ? 551  LYS   A NZ  1 
ATOM   3884 N  N   . GLY   A 1 527 ? 50.084 49.856  14.723  1.00 27.61  ? 552  GLY   A N   1 
ATOM   3885 C  CA  . GLY   A 1 527 ? 51.039 49.795  15.834  1.00 30.75  ? 552  GLY   A CA  1 
ATOM   3886 C  C   . GLY   A 1 527 ? 52.480 49.555  15.417  1.00 33.66  ? 552  GLY   A C   1 
ATOM   3887 O  O   . GLY   A 1 527 ? 52.888 49.950  14.318  1.00 35.68  ? 552  GLY   A O   1 
ATOM   3888 N  N   . GLY   A 1 535 ? 59.605 42.449  6.159   1.00 36.60  ? 560  GLY   A N   1 
ATOM   3889 C  CA  . GLY   A 1 535 ? 60.054 41.289  5.392   1.00 35.95  ? 560  GLY   A CA  1 
ATOM   3890 C  C   . GLY   A 1 535 ? 58.966 40.751  4.477   1.00 33.63  ? 560  GLY   A C   1 
ATOM   3891 O  O   . GLY   A 1 535 ? 59.209 40.439  3.307   1.00 35.71  ? 560  GLY   A O   1 
ATOM   3892 N  N   . TYR   A 1 536 ? 57.751 40.698  4.974   1.00 28.85  ? 561  TYR   A N   1 
ATOM   3893 C  CA  . TYR   A 1 536 ? 56.568 40.182  4.288   1.00 25.23  ? 561  TYR   A CA  1 
ATOM   3894 C  C   . TYR   A 1 536 ? 56.519 40.457  2.778   1.00 22.66  ? 561  TYR   A C   1 
ATOM   3895 O  O   . TYR   A 1 536 ? 56.811 41.564  2.356   1.00 24.65  ? 561  TYR   A O   1 
ATOM   3896 C  CB  . TYR   A 1 536 ? 55.332 40.871  4.878   1.00 25.71  ? 561  TYR   A CB  1 
ATOM   3897 C  CG  . TYR   A 1 536 ? 55.033 40.568  6.329   1.00 27.38  ? 561  TYR   A CG  1 
ATOM   3898 C  CD1 . TYR   A 1 536 ? 55.709 41.227  7.353   1.00 29.33  ? 561  TYR   A CD1 1 
ATOM   3899 C  CD2 . TYR   A 1 536 ? 54.010 39.692  6.679   1.00 28.83  ? 561  TYR   A CD2 1 
ATOM   3900 C  CE1 . TYR   A 1 536 ? 55.395 40.994  8.689   1.00 31.62  ? 561  TYR   A CE1 1 
ATOM   3901 C  CE2 . TYR   A 1 536 ? 53.686 39.453  8.008   1.00 30.58  ? 561  TYR   A CE2 1 
ATOM   3902 C  CZ  . TYR   A 1 536 ? 54.376 40.111  9.012   1.00 32.74  ? 561  TYR   A CZ  1 
ATOM   3903 O  OH  . TYR   A 1 536 ? 54.051 39.879  10.337  1.00 34.74  ? 561  TYR   A OH  1 
ATOM   3904 N  N   . LEU   A 1 537 ? 56.156 39.461  1.986   1.00 18.76  ? 562  LEU   A N   1 
ATOM   3905 C  CA  . LEU   A 1 537 ? 56.001 39.648  0.548   1.00 17.75  ? 562  LEU   A CA  1 
ATOM   3906 C  C   . LEU   A 1 537 ? 54.898 38.728  0.091   1.00 16.02  ? 562  LEU   A C   1 
ATOM   3907 O  O   . LEU   A 1 537 ? 54.853 37.581  0.515   1.00 16.32  ? 562  LEU   A O   1 
ATOM   3908 C  CB  . LEU   A 1 537 ? 57.304 39.227  -0.151  1.00 21.09  ? 562  LEU   A CB  1 
ATOM   3909 C  CG  . LEU   A 1 537 ? 57.485 39.791  -1.506  1.00 26.88  ? 562  LEU   A CG  1 
ATOM   3910 C  CD1 . LEU   A 1 537 ? 57.684 41.346  -1.435  1.00 27.95  ? 562  LEU   A CD1 1 
ATOM   3911 C  CD2 . LEU   A 1 537 ? 58.711 39.188  -2.145  1.00 29.43  ? 562  LEU   A CD2 1 
ATOM   3912 N  N   . TRP   A 1 538 ? 54.033 39.209  -0.769  1.00 14.45  ? 563  TRP   A N   1 
ATOM   3913 C  CA  . TRP   A 1 538 ? 52.961 38.398  -1.320  1.00 14.13  ? 563  TRP   A CA  1 
ATOM   3914 C  C   . TRP   A 1 538 ? 53.006 38.384  -2.851  1.00 14.02  ? 563  TRP   A C   1 
ATOM   3915 O  O   . TRP   A 1 538 ? 53.537 39.310  -3.473  1.00 15.23  ? 563  TRP   A O   1 
ATOM   3916 C  CB  . TRP   A 1 538 ? 51.576 38.992  -0.930  1.00 13.82  ? 563  TRP   A CB  1 
ATOM   3917 C  CG  . TRP   A 1 538 ? 51.242 38.800  0.515   1.00 13.04  ? 563  TRP   A CG  1 
ATOM   3918 C  CD1 . TRP   A 1 538 ? 50.488 37.792  1.036   1.00 14.87  ? 563  TRP   A CD1 1 
ATOM   3919 C  CD2 . TRP   A 1 538 ? 51.558 39.686  1.608   1.00 12.36  ? 563  TRP   A CD2 1 
ATOM   3920 N  NE1 . TRP   A 1 538 ? 50.372 37.962  2.408   1.00 14.48  ? 563  TRP   A NE1 1 
ATOM   3921 C  CE2 . TRP   A 1 538 ? 50.998 39.123  2.774   1.00 13.34  ? 563  TRP   A CE2 1 
ATOM   3922 C  CE3 . TRP   A 1 538 ? 52.318 40.870  1.726   1.00 13.51  ? 563  TRP   A CE3 1 
ATOM   3923 C  CZ2 . TRP   A 1 538 ? 51.148 39.715  4.032   1.00 13.66  ? 563  TRP   A CZ2 1 
ATOM   3924 C  CZ3 . TRP   A 1 538 ? 52.404 41.483  2.956   1.00 14.70  ? 563  TRP   A CZ3 1 
ATOM   3925 C  CH2 . TRP   A 1 538 ? 51.788 40.919  4.083   1.00 13.93  ? 563  TRP   A CH2 1 
ATOM   3926 N  N   . HIS   A 1 539 ? 52.347 37.402  -3.452  1.00 13.94  ? 564  HIS   A N   1 
ATOM   3927 C  CA  . HIS   A 1 539 ? 52.044 37.449  -4.885  1.00 13.65  ? 564  HIS   A CA  1 
ATOM   3928 C  C   . HIS   A 1 539 ? 50.638 37.997  -4.942  1.00 13.21  ? 564  HIS   A C   1 
ATOM   3929 O  O   . HIS   A 1 539 ? 49.680 37.310  -4.538  1.00 14.14  ? 564  HIS   A O   1 
ATOM   3930 C  CB  . HIS   A 1 539 ? 52.096 36.054  -5.516  1.00 15.44  ? 564  HIS   A CB  1 
ATOM   3931 C  CG  . HIS   A 1 539 ? 53.483 35.531  -5.717  1.00 15.99  ? 564  HIS   A CG  1 
ATOM   3932 N  ND1 . HIS   A 1 539 ? 53.748 34.592  -6.679  1.00 17.62  ? 564  HIS   A ND1 1 
ATOM   3933 C  CD2 . HIS   A 1 539 ? 54.626 35.848  -5.077  1.00 16.55  ? 564  HIS   A CD2 1 
ATOM   3934 C  CE1 . HIS   A 1 539 ? 55.053 34.340  -6.602  1.00 17.58  ? 564  HIS   A CE1 1 
ATOM   3935 N  NE2 . HIS   A 1 539 ? 55.640 35.073  -5.673  1.00 17.74  ? 564  HIS   A NE2 1 
ATOM   3936 N  N   . VAL   A 1 540 ? 50.517 39.269  -5.364  1.00 13.31  ? 565  VAL   A N   1 
ATOM   3937 C  CA  . VAL   A 1 540 ? 49.259 39.978  -5.311  1.00 13.08  ? 565  VAL   A CA  1 
ATOM   3938 C  C   . VAL   A 1 540 ? 48.659 40.112  -6.675  1.00 13.82  ? 565  VAL   A C   1 
ATOM   3939 O  O   . VAL   A 1 540 ? 49.206 40.819  -7.529  1.00 13.77  ? 565  VAL   A O   1 
ATOM   3940 C  CB  . VAL   A 1 540 ? 49.406 41.390  -4.687  1.00 13.64  ? 565  VAL   A CB  1 
ATOM   3941 C  CG1 . VAL   A 1 540 ? 48.013 41.962  -4.365  1.00 15.67  ? 565  VAL   A CG1 1 
ATOM   3942 C  CG2 . VAL   A 1 540 ? 50.277 41.387  -3.455  1.00 14.29  ? 565  VAL   A CG2 1 
ATOM   3943 N  N   . PRO   A 1 541 ? 47.513 39.492  -6.932  1.00 14.15  ? 566  PRO   A N   1 
ATOM   3944 C  CA  . PRO   A 1 541 ? 46.873 39.652  -8.253  1.00 13.93  ? 566  PRO   A CA  1 
ATOM   3945 C  C   . PRO   A 1 541 ? 46.127 40.986  -8.254  1.00 15.21  ? 566  PRO   A C   1 
ATOM   3946 O  O   . PRO   A 1 541 ? 44.978 41.099  -7.749  1.00 17.95  ? 566  PRO   A O   1 
ATOM   3947 C  CB  . PRO   A 1 541 ? 45.871 38.486  -8.322  1.00 15.20  ? 566  PRO   A CB  1 
ATOM   3948 C  CG  . PRO   A 1 541 ? 45.705 38.037  -6.929  1.00 18.19  ? 566  PRO   A CG  1 
ATOM   3949 C  CD  . PRO   A 1 541 ? 46.802 38.540  -6.044  1.00 15.30  ? 566  PRO   A CD  1 
ATOM   3950 N  N   . LEU   A 1 542 ? 46.794 42.038  -8.746  1.00 13.51  ? 567  LEU   A N   1 
ATOM   3951 C  CA  . LEU   A 1 542 ? 46.174 43.344  -8.775  1.00 12.91  ? 567  LEU   A CA  1 
ATOM   3952 C  C   . LEU   A 1 542 ? 45.208 43.476  -9.901  1.00 12.67  ? 567  LEU   A C   1 
ATOM   3953 O  O   . LEU   A 1 542 ? 45.338 42.861  -10.961 1.00 13.56  ? 567  LEU   A O   1 
ATOM   3954 C  CB  . LEU   A 1 542 ? 47.263 44.448  -8.936  1.00 13.54  ? 567  LEU   A CB  1 
ATOM   3955 C  CG  . LEU   A 1 542 ? 48.353 44.475  -7.873  1.00 13.99  ? 567  LEU   A CG  1 
ATOM   3956 C  CD1 . LEU   A 1 542 ? 49.392 45.553  -8.189  1.00 13.68  ? 567  LEU   A CD1 1 
ATOM   3957 C  CD2 . LEU   A 1 542 ? 47.754 44.840  -6.505  1.00 14.96  ? 567  LEU   A CD2 1 
ATOM   3958 N  N   . THR   A 1 543 ? 44.226 44.371  -9.698  1.00 12.45  ? 568  THR   A N   1 
ATOM   3959 C  CA  . THR   A 1 543 ? 43.312 44.748  -10.747 1.00 13.21  ? 568  THR   A CA  1 
ATOM   3960 C  C   . THR   A 1 543 ? 43.130 46.245  -10.715 1.00 12.28  ? 568  THR   A C   1 
ATOM   3961 O  O   . THR   A 1 543 ? 43.291 46.865  -9.648  1.00 12.44  ? 568  THR   A O   1 
ATOM   3962 C  CB  . THR   A 1 543 ? 41.939 44.118  -10.541 1.00 14.46  ? 568  THR   A CB  1 
ATOM   3963 O  OG1 . THR   A 1 543 ? 41.441 44.415  -9.246  1.00 15.26  ? 568  THR   A OG1 1 
ATOM   3964 C  CG2 . THR   A 1 543 ? 41.957 42.611  -10.778 1.00 15.96  ? 568  THR   A CG2 1 
ATOM   3965 N  N   . PHE   A 1 544 ? 42.822 46.850  -11.862 1.00 12.41  ? 569  PHE   A N   1 
ATOM   3966 C  CA  . PHE   A 1 544 ? 42.548 48.287  -11.879 1.00 12.00  ? 569  PHE   A CA  1 
ATOM   3967 C  C   . PHE   A 1 544 ? 41.648 48.651  -13.047 1.00 11.46  ? 569  PHE   A C   1 
ATOM   3968 O  O   . PHE   A 1 544 ? 41.553 47.946  -14.056 1.00 12.37  ? 569  PHE   A O   1 
ATOM   3969 C  CB  . PHE   A 1 544 ? 43.859 49.139  -11.944 1.00 12.12  ? 569  PHE   A CB  1 
ATOM   3970 C  CG  . PHE   A 1 544 ? 44.628 48.986  -13.231 1.00 12.59  ? 569  PHE   A CG  1 
ATOM   3971 C  CD1 . PHE   A 1 544 ? 44.409 49.844  -14.290 1.00 13.20  ? 569  PHE   A CD1 1 
ATOM   3972 C  CD2 . PHE   A 1 544 ? 45.641 48.045  -13.343 1.00 14.32  ? 569  PHE   A CD2 1 
ATOM   3973 C  CE1 . PHE   A 1 544 ? 45.149 49.729  -15.481 1.00 14.38  ? 569  PHE   A CE1 1 
ATOM   3974 C  CE2 . PHE   A 1 544 ? 46.400 47.962  -14.507 1.00 14.71  ? 569  PHE   A CE2 1 
ATOM   3975 C  CZ  . PHE   A 1 544 ? 46.167 48.824  -15.547 1.00 14.64  ? 569  PHE   A CZ  1 
ATOM   3976 N  N   . ILE   A 1 545 ? 40.989 49.776  -12.892 1.00 12.28  ? 570  ILE   A N   1 
ATOM   3977 C  CA  . ILE   A 1 545 ? 40.258 50.496  -13.934 1.00 12.29  ? 570  ILE   A CA  1 
ATOM   3978 C  C   . ILE   A 1 545 ? 40.788 51.925  -13.933 1.00 12.81  ? 570  ILE   A C   1 
ATOM   3979 O  O   . ILE   A 1 545 ? 41.452 52.365  -12.980 1.00 12.94  ? 570  ILE   A O   1 
ATOM   3980 C  CB  . ILE   A 1 545 ? 38.742 50.459  -13.702 1.00 13.21  ? 570  ILE   A CB  1 
ATOM   3981 C  CG1 . ILE   A 1 545 ? 38.379 51.006  -12.311 1.00 14.11  ? 570  ILE   A CG1 1 
ATOM   3982 C  CG2 . ILE   A 1 545 ? 38.187 49.058  -13.958 1.00 14.02  ? 570  ILE   A CG2 1 
ATOM   3983 C  CD1 . ILE   A 1 545 ? 36.828 51.137  -12.101 1.00 17.67  ? 570  ILE   A CD1 1 
ATOM   3984 N  N   . THR   A 1 546 ? 40.476 52.678  -14.994 1.00 12.84  ? 571  THR   A N   1 
ATOM   3985 C  CA  . THR   A 1 546 ? 40.921 54.082  -15.057 1.00 12.96  ? 571  THR   A CA  1 
ATOM   3986 C  C   . THR   A 1 546 ? 39.799 54.943  -15.644 1.00 13.83  ? 571  THR   A C   1 
ATOM   3987 O  O   . THR   A 1 546 ? 38.789 54.416  -16.130 1.00 13.99  ? 571  THR   A O   1 
ATOM   3988 C  CB  . THR   A 1 546 ? 42.144 54.232  -15.977 1.00 13.76  ? 571  THR   A CB  1 
ATOM   3989 O  OG1 . THR   A 1 546 ? 41.668 54.097  -17.339 1.00 13.37  ? 571  THR   A OG1 1 
ATOM   3990 C  CG2 . THR   A 1 546 ? 43.225 53.263  -15.680 1.00 13.50  ? 571  THR   A CG2 1 
ATOM   3991 N  N   . SER   A 1 547 ? 40.029 56.266  -15.696 1.00 13.62  ? 572  SER   A N   1 
ATOM   3992 C  CA  . SER   A 1 547 ? 39.075 57.169  -16.329 1.00 13.25  ? 572  SER   A CA  1 
ATOM   3993 C  C   . SER   A 1 547 ? 38.867 56.881  -17.792 1.00 15.63  ? 572  SER   A C   1 
ATOM   3994 O  O   . SER   A 1 547 ? 37.845 57.320  -18.345 1.00 16.56  ? 572  SER   A O   1 
ATOM   3995 C  CB  . SER   A 1 547 ? 39.501 58.633  -16.158 1.00 14.53  ? 572  SER   A CB  1 
ATOM   3996 O  OG  . SER   A 1 547 ? 40.683 58.894  -16.908 1.00 16.87  ? 572  SER   A OG  1 
ATOM   3997 N  N   . LYS   A 1 548 ? 39.823 56.191  -18.428 1.00 14.46  ? 573  LYS   A N   1 
ATOM   3998 C  CA  . LYS   A 1 548 ? 39.732 55.863  -19.848 1.00 14.35  ? 573  LYS   A CA  1 
ATOM   3999 C  C   . LYS   A 1 548 ? 39.327 54.456  -20.146 1.00 15.08  ? 573  LYS   A C   1 
ATOM   4000 O  O   . LYS   A 1 548 ? 39.044 54.164  -21.311 1.00 16.25  ? 573  LYS   A O   1 
ATOM   4001 C  CB  . LYS   A 1 548 ? 41.045 56.172  -20.578 1.00 16.89  ? 573  LYS   A CB  1 
ATOM   4002 C  CG  . LYS   A 1 548 ? 41.277 57.677  -20.662 1.00 20.49  ? 573  LYS   A CG  1 
ATOM   4003 C  CD  . LYS   A 1 548 ? 42.390 57.980  -21.624 1.00 27.33  ? 573  LYS   A CD  1 
ATOM   4004 C  CE  . LYS   A 1 548 ? 42.282 59.341  -22.209 1.00 33.98  ? 573  LYS   A CE  1 
ATOM   4005 N  NZ  . LYS   A 1 548 ? 42.834 60.341  -21.266 1.00 36.41  ? 573  LYS   A NZ  1 
ATOM   4006 N  N   . SER   A 1 549 ? 39.343 53.567  -19.157 1.00 14.54  ? 574  SER   A N   1 
ATOM   4007 C  CA  . SER   A 1 549 ? 38.991 52.170  -19.420 1.00 13.30  ? 574  SER   A CA  1 
ATOM   4008 C  C   . SER   A 1 549 ? 38.311 51.539  -18.240 1.00 14.98  ? 574  SER   A C   1 
ATOM   4009 O  O   . SER   A 1 549 ? 38.929 51.459  -17.170 1.00 14.19  ? 574  SER   A O   1 
ATOM   4010 C  CB  . SER   A 1 549 ? 40.251 51.357  -19.719 1.00 13.64  ? 574  SER   A CB  1 
ATOM   4011 O  OG  . SER   A 1 549 ? 39.914 50.002  -19.973 1.00 13.52  ? 574  SER   A OG  1 
ATOM   4012 N  N   . ASP   A 1 550 ? 37.098 51.025  -18.416 1.00 14.51  ? 575  ASP   A N   1 
ATOM   4013 C  CA  . ASP   A 1 550 ? 36.437 50.293  -17.355 1.00 15.39  ? 575  ASP   A CA  1 
ATOM   4014 C  C   . ASP   A 1 550 ? 36.538 48.784  -17.521 1.00 15.51  ? 575  ASP   A C   1 
ATOM   4015 O  O   . ASP   A 1 550 ? 35.894 48.025  -16.798 1.00 16.66  ? 575  ASP   A O   1 
ATOM   4016 C  CB  . ASP   A 1 550 ? 34.977 50.741  -17.147 1.00 16.73  ? 575  ASP   A CB  1 
ATOM   4017 C  CG  . ASP   A 1 550 ? 34.062 50.372  -18.277 1.00 21.94  ? 575  ASP   A CG  1 
ATOM   4018 O  OD1 . ASP   A 1 550 ? 34.513 49.707  -19.214 1.00 21.29  ? 575  ASP   A OD1 1 
ATOM   4019 O  OD2 . ASP   A 1 550 ? 32.865 50.752  -18.221 1.00 25.70  ? 575  ASP   A OD2 1 
ATOM   4020 N  N   . MET   A 1 551 ? 37.405 48.316  -18.441 1.00 14.24  ? 576  MET   A N   1 
ATOM   4021 C  CA  . MET   A 1 551 ? 37.767 46.912  -18.475 1.00 14.38  ? 576  MET   A CA  1 
ATOM   4022 C  C   . MET   A 1 551 ? 38.606 46.641  -17.196 1.00 14.67  ? 576  MET   A C   1 
ATOM   4023 O  O   . MET   A 1 551 ? 39.395 47.512  -16.804 1.00 15.15  ? 576  MET   A O   1 
ATOM   4024 C  CB  . MET   A 1 551 ? 38.630 46.602  -19.699 1.00 14.34  ? 576  MET   A CB  1 
ATOM   4025 C  CG  . MET   A 1 551 ? 39.384 45.282  -19.588 1.00 14.87  ? 576  MET   A CG  1 
ATOM   4026 S  SD  . MET   A 1 551 ? 40.217 44.964  -21.174 1.00 16.28  ? 576  MET   A SD  1 
ATOM   4027 C  CE  . MET   A 1 551 ? 41.463 43.773  -20.611 1.00 17.13  ? 576  MET   A CE  1 
ATOM   4028 N  N   . VAL   A 1 552 ? 38.453 45.471  -16.595 1.00 14.02  ? 577  VAL   A N   1 
ATOM   4029 C  CA  . VAL   A 1 552 ? 39.299 45.157  -15.433 1.00 14.05  ? 577  VAL   A CA  1 
ATOM   4030 C  C   . VAL   A 1 552 ? 40.675 44.716  -15.942 1.00 14.65  ? 577  VAL   A C   1 
ATOM   4031 O  O   . VAL   A 1 552 ? 40.816 43.684  -16.615 1.00 16.86  ? 577  VAL   A O   1 
ATOM   4032 C  CB  . VAL   A 1 552 ? 38.623 44.078  -14.607 1.00 16.43  ? 577  VAL   A CB  1 
ATOM   4033 C  CG1 . VAL   A 1 552 ? 39.525 43.653  -13.429 1.00 18.50  ? 577  VAL   A CG1 1 
ATOM   4034 C  CG2 . VAL   A 1 552 ? 37.263 44.599  -14.111 1.00 19.25  ? 577  VAL   A CG2 1 
ATOM   4035 N  N   . HIS   A 1 553 ? 41.680 45.532  -15.678 1.00 12.89  ? 578  HIS   A N   1 
ATOM   4036 C  CA  . HIS   A 1 553 ? 43.027 45.205  -16.069 1.00 13.41  ? 578  HIS   A CA  1 
ATOM   4037 C  C   . HIS   A 1 553 ? 43.706 44.460  -14.973 1.00 14.55  ? 578  HIS   A C   1 
ATOM   4038 O  O   . HIS   A 1 553 ? 43.502 44.760  -13.805 1.00 15.44  ? 578  HIS   A O   1 
ATOM   4039 C  CB  . HIS   A 1 553 ? 43.752 46.496  -16.358 1.00 12.96  ? 578  HIS   A CB  1 
ATOM   4040 C  CG  . HIS   A 1 553 ? 43.163 47.211  -17.530 1.00 13.88  ? 578  HIS   A CG  1 
ATOM   4041 N  ND1 . HIS   A 1 553 ? 43.545 46.889  -18.824 1.00 15.69  ? 578  HIS   A ND1 1 
ATOM   4042 C  CD2 . HIS   A 1 553 ? 42.173 48.127  -17.585 1.00 14.51  ? 578  HIS   A CD2 1 
ATOM   4043 C  CE1 . HIS   A 1 553 ? 42.803 47.631  -19.633 1.00 15.82  ? 578  HIS   A CE1 1 
ATOM   4044 N  NE2 . HIS   A 1 553 ? 41.972 48.417  -18.946 1.00 15.34  ? 578  HIS   A NE2 1 
ATOM   4045 N  N   . ARG   A 1 554 ? 44.520 43.497  -15.338 1.00 14.47  ? 579  ARG   A N   1 
ATOM   4046 C  CA  A ARG   A 1 554 ? 45.189 42.674  -14.332 0.50 15.14  ? 579  ARG   A CA  1 
ATOM   4047 C  CA  B ARG   A 1 554 ? 45.183 42.635  -14.380 0.50 14.34  ? 579  ARG   A CA  1 
ATOM   4048 C  C   . ARG   A 1 554 ? 46.697 42.821  -14.357 1.00 14.55  ? 579  ARG   A C   1 
ATOM   4049 O  O   . ARG   A 1 554 ? 47.307 43.014  -15.409 1.00 16.77  ? 579  ARG   A O   1 
ATOM   4050 C  CB  A ARG   A 1 554 ? 44.766 41.198  -14.475 0.50 17.92  ? 579  ARG   A CB  1 
ATOM   4051 C  CB  B ARG   A 1 554 ? 44.926 41.206  -14.848 0.50 14.58  ? 579  ARG   A CB  1 
ATOM   4052 C  CG  A ARG   A 1 554 ? 43.283 41.001  -14.115 0.50 20.43  ? 579  ARG   A CG  1 
ATOM   4053 C  CG  B ARG   A 1 554 ? 43.427 40.847  -14.917 0.50 16.07  ? 579  ARG   A CG  1 
ATOM   4054 C  CD  A ARG   A 1 554 ? 42.745 39.575  -14.162 0.50 23.99  ? 579  ARG   A CD  1 
ATOM   4055 C  CD  B ARG   A 1 554 ? 43.167 39.577  -15.715 0.50 17.48  ? 579  ARG   A CD  1 
ATOM   4056 N  NE  A ARG   A 1 554 ? 41.285 39.573  -14.332 0.50 25.71  ? 579  ARG   A NE  1 
ATOM   4057 N  NE  B ARG   A 1 554 ? 43.999 38.476  -15.248 0.50 19.27  ? 579  ARG   A NE  1 
ATOM   4058 C  CZ  A ARG   A 1 554 ? 40.396 39.584  -13.343 0.50 25.00  ? 579  ARG   A CZ  1 
ATOM   4059 C  CZ  B ARG   A 1 554 ? 43.581 37.470  -14.491 0.50 19.61  ? 579  ARG   A CZ  1 
ATOM   4060 N  NH1 A ARG   A 1 554 ? 40.796 39.599  -12.082 0.50 18.84  ? 579  ARG   A NH1 1 
ATOM   4061 N  NH1 B ARG   A 1 554 ? 44.438 36.566  -14.057 0.50 17.33  ? 579  ARG   A NH1 1 
ATOM   4062 N  NH2 A ARG   A 1 554 ? 39.095 39.602  -13.611 0.50 26.92  ? 579  ARG   A NH2 1 
ATOM   4063 N  NH2 B ARG   A 1 554 ? 42.307 37.394  -14.117 0.50 19.35  ? 579  ARG   A NH2 1 
ATOM   4064 N  N   . PHE   A 1 555 ? 47.303 42.748  -13.161 1.00 13.17  ? 580  PHE   A N   1 
ATOM   4065 C  CA  . PHE   A 1 555 ? 48.767 42.806  -13.094 1.00 13.53  ? 580  PHE   A CA  1 
ATOM   4066 C  C   . PHE   A 1 555 ? 49.156 41.982  -11.891 1.00 13.66  ? 580  PHE   A C   1 
ATOM   4067 O  O   . PHE   A 1 555 ? 48.737 42.326  -10.777 1.00 14.87  ? 580  PHE   A O   1 
ATOM   4068 C  CB  . PHE   A 1 555 ? 49.256 44.258  -12.929 1.00 14.33  ? 580  PHE   A CB  1 
ATOM   4069 C  CG  . PHE   A 1 555 ? 50.762 44.347  -13.027 1.00 14.47  ? 580  PHE   A CG  1 
ATOM   4070 C  CD1 . PHE   A 1 555 ? 51.556 44.160  -11.911 1.00 15.67  ? 580  PHE   A CD1 1 
ATOM   4071 C  CD2 . PHE   A 1 555 ? 51.368 44.664  -14.220 1.00 16.83  ? 580  PHE   A CD2 1 
ATOM   4072 C  CE1 . PHE   A 1 555 ? 52.940 44.225  -12.014 1.00 15.22  ? 580  PHE   A CE1 1 
ATOM   4073 C  CE2 . PHE   A 1 555 ? 52.753 44.748  -14.317 1.00 17.38  ? 580  PHE   A CE2 1 
ATOM   4074 C  CZ  . PHE   A 1 555 ? 53.524 44.491  -13.214 1.00 15.23  ? 580  PHE   A CZ  1 
ATOM   4075 N  N   . LEU   A 1 556 ? 50.034 40.984  -12.038 1.00 14.08  ? 581  LEU   A N   1 
ATOM   4076 C  CA  . LEU   A 1 556 ? 50.453 40.180  -10.886 1.00 14.41  ? 581  LEU   A CA  1 
ATOM   4077 C  C   . LEU   A 1 556 ? 51.730 40.784  -10.275 1.00 14.67  ? 581  LEU   A C   1 
ATOM   4078 O  O   . LEU   A 1 556 ? 52.799 40.759  -10.898 1.00 16.13  ? 581  LEU   A O   1 
ATOM   4079 C  CB  . LEU   A 1 556 ? 50.697 38.732  -11.323 1.00 14.64  ? 581  LEU   A CB  1 
ATOM   4080 C  CG  . LEU   A 1 556 ? 51.144 37.794  -10.217 1.00 17.36  ? 581  LEU   A CG  1 
ATOM   4081 C  CD1 . LEU   A 1 556 ? 50.096 37.693  -9.147  1.00 17.80  ? 581  LEU   A CD1 1 
ATOM   4082 C  CD2 . LEU   A 1 556 ? 51.407 36.379  -10.776 1.00 18.84  ? 581  LEU   A CD2 1 
ATOM   4083 N  N   . LEU   A 1 557 ? 51.625 41.318  -9.050  1.00 13.51  ? 582  LEU   A N   1 
ATOM   4084 C  CA  . LEU   A 1 557 ? 52.778 41.921  -8.383  1.00 12.69  ? 582  LEU   A CA  1 
ATOM   4085 C  C   . LEU   A 1 557 ? 53.380 40.865  -7.490  1.00 14.12  ? 582  LEU   A C   1 
ATOM   4086 O  O   . LEU   A 1 557 ? 52.784 40.465  -6.487  1.00 15.08  ? 582  LEU   A O   1 
ATOM   4087 C  CB  . LEU   A 1 557 ? 52.291 43.096  -7.558  1.00 12.48  ? 582  LEU   A CB  1 
ATOM   4088 C  CG  . LEU   A 1 557 ? 53.429 43.769  -6.746  1.00 13.64  ? 582  LEU   A CG  1 
ATOM   4089 C  CD1 . LEU   A 1 557 ? 54.441 44.488  -7.675  1.00 14.51  ? 582  LEU   A CD1 1 
ATOM   4090 C  CD2 . LEU   A 1 557 ? 52.866 44.775  -5.752  1.00 16.18  ? 582  LEU   A CD2 1 
ATOM   4091 N  N   . LYS   A 1 558 ? 54.508 40.325  -7.870  1.00 13.81  ? 583  LYS   A N   1 
ATOM   4092 C  CA  . LYS   A 1 558 ? 55.163 39.253  -7.094  1.00 14.76  ? 583  LYS   A CA  1 
ATOM   4093 C  C   . LYS   A 1 558 ? 56.349 39.744  -6.298  1.00 16.60  ? 583  LYS   A C   1 
ATOM   4094 O  O   . LYS   A 1 558 ? 57.003 38.944  -5.653  1.00 18.83  ? 583  LYS   A O   1 
ATOM   4095 C  CB  . LYS   A 1 558 ? 55.800 38.198  -8.019  1.00 19.15  ? 583  LYS   A CB  1 
ATOM   4096 C  CG  . LYS   A 1 558 ? 54.869 37.531  -8.943  1.00 21.97  ? 583  LYS   A CG  1 
ATOM   4097 C  CD  . LYS   A 1 558 ? 55.667 36.478  -9.636  1.00 23.48  ? 583  LYS   A CD  1 
ATOM   4098 C  CE  . LYS   A 1 558 ? 54.902 35.959  -10.803 1.00 29.32  ? 583  LYS   A CE  1 
ATOM   4099 N  NZ  . LYS   A 1 558 ? 55.701 34.957  -11.555 1.00 31.65  ? 583  LYS   A NZ  1 
ATOM   4100 N  N   . THR   A 1 559 ? 56.667 41.017  -6.389  1.00 14.52  ? 584  THR   A N   1 
ATOM   4101 C  CA  . THR   A 1 559 ? 57.910 41.581  -5.873  1.00 13.94  ? 584  THR   A CA  1 
ATOM   4102 C  C   . THR   A 1 559 ? 57.621 42.812  -5.081  1.00 13.59  ? 584  THR   A C   1 
ATOM   4103 O  O   . THR   A 1 559 ? 56.481 43.312  -5.053  1.00 13.55  ? 584  THR   A O   1 
ATOM   4104 C  CB  . THR   A 1 559 ? 58.806 41.883  -7.096  1.00 14.25  ? 584  THR   A CB  1 
ATOM   4105 O  OG1 . THR   A 1 559 ? 58.111 42.773  -7.988  1.00 13.53  ? 584  THR   A OG1 1 
ATOM   4106 C  CG2 . THR   A 1 559 ? 59.231 40.624  -7.845  1.00 15.09  ? 584  THR   A CG2 1 
ATOM   4107 N  N   . LYS   A 1 560 ? 58.659 43.372  -4.438  1.00 14.26  ? 585  LYS   A N   1 
ATOM   4108 C  CA  . LYS   A 1 560 ? 58.471 44.568  -3.627  1.00 13.60  ? 585  LYS   A CA  1 
ATOM   4109 C  C   . LYS   A 1 560 ? 57.950 45.720  -4.455  1.00 14.15  ? 585  LYS   A C   1 
ATOM   4110 O  O   . LYS   A 1 560 ? 57.095 46.491  -3.993  1.00 14.40  ? 585  LYS   A O   1 
ATOM   4111 C  CB  . LYS   A 1 560 ? 59.801 44.946  -2.931  1.00 15.81  ? 585  LYS   A CB  1 
ATOM   4112 C  CG  . LYS   A 1 560 ? 59.581 46.110  -1.946  1.00 20.34  ? 585  LYS   A CG  1 
ATOM   4113 C  CD  . LYS   A 1 560 ? 60.819 46.394  -1.091  1.00 26.98  ? 585  LYS   A CD  1 
ATOM   4114 C  CE  . LYS   A 1 560 ? 60.627 47.610  -0.215  1.00 33.00  ? 585  LYS   A CE  1 
ATOM   4115 N  NZ  . LYS   A 1 560 ? 61.550 47.572  0.971   1.00 36.05  ? 585  LYS   A NZ  1 
ATOM   4116 N  N   . THR   A 1 561 ? 58.515 45.881  -5.664  1.00 14.04  ? 586  THR   A N   1 
ATOM   4117 C  CA  . THR   A 1 561 ? 58.036 46.943  -6.543  1.00 13.56  ? 586  THR   A CA  1 
ATOM   4118 C  C   . THR   A 1 561 ? 57.907 46.434  -7.969  1.00 12.83  ? 586  THR   A C   1 
ATOM   4119 O  O   . THR   A 1 561 ? 58.509 45.412  -8.349  1.00 13.66  ? 586  THR   A O   1 
ATOM   4120 C  CB  . THR   A 1 561 ? 58.943 48.224  -6.542  1.00 14.95  ? 586  THR   A CB  1 
ATOM   4121 O  OG1 . THR   A 1 561 ? 60.032 48.044  -7.477  1.00 15.70  ? 586  THR   A OG1 1 
ATOM   4122 C  CG2 . THR   A 1 561 ? 59.412 48.620  -5.153  1.00 15.62  ? 586  THR   A CG2 1 
ATOM   4123 N  N   . ASP   A 1 562 ? 57.168 47.197  -8.775  1.00 12.62  ? 587  ASP   A N   1 
ATOM   4124 C  CA  . ASP   A 1 562 ? 57.109 46.923  -10.213 1.00 12.41  ? 587  ASP   A CA  1 
ATOM   4125 C  C   . ASP   A 1 562 ? 56.567 48.186  -10.867 1.00 12.24  ? 587  ASP   A C   1 
ATOM   4126 O  O   . ASP   A 1 562 ? 56.315 49.197  -10.193 1.00 12.49  ? 587  ASP   A O   1 
ATOM   4127 C  CB  . ASP   A 1 562 ? 56.272 45.687  -10.521 1.00 12.73  ? 587  ASP   A CB  1 
ATOM   4128 C  CG  . ASP   A 1 562 ? 56.753 44.906  -11.712 1.00 13.40  ? 587  ASP   A CG  1 
ATOM   4129 O  OD1 . ASP   A 1 562 ? 57.345 45.528  -12.646 1.00 14.19  ? 587  ASP   A OD1 1 
ATOM   4130 O  OD2 . ASP   A 1 562 ? 56.495 43.668  -11.759 1.00 14.48  ? 587  ASP   A OD2 1 
ATOM   4131 N  N   . VAL   A 1 563 ? 56.454 48.143  -12.191 1.00 12.55  ? 588  VAL   A N   1 
ATOM   4132 C  CA  . VAL   A 1 563 ? 55.957 49.278  -12.946 1.00 13.02  ? 588  VAL   A CA  1 
ATOM   4133 C  C   . VAL   A 1 563 ? 55.141 48.760  -14.104 1.00 14.43  ? 588  VAL   A C   1 
ATOM   4134 O  O   . VAL   A 1 563 ? 55.436 47.706  -14.659 1.00 14.85  ? 588  VAL   A O   1 
ATOM   4135 C  CB  . VAL   A 1 563 ? 57.150 50.133  -13.475 1.00 15.46  ? 588  VAL   A CB  1 
ATOM   4136 C  CG1 . VAL   A 1 563 ? 58.095 49.280  -14.291 1.00 18.32  ? 588  VAL   A CG1 1 
ATOM   4137 C  CG2 . VAL   A 1 563 ? 56.669 51.347  -14.286 1.00 17.94  ? 588  VAL   A CG2 1 
ATOM   4138 N  N   . LEU   A 1 564 ? 54.108 49.512  -14.458 1.00 12.86  ? 589  LEU   A N   1 
ATOM   4139 C  CA  . LEU   A 1 564 ? 53.383 49.261  -15.714 1.00 13.64  ? 589  LEU   A CA  1 
ATOM   4140 C  C   . LEU   A 1 564 ? 53.174 50.575  -16.398 1.00 13.85  ? 589  LEU   A C   1 
ATOM   4141 O  O   . LEU   A 1 564 ? 53.213 51.644  -15.755 1.00 13.52  ? 589  LEU   A O   1 
ATOM   4142 C  CB  . LEU   A 1 564 ? 52.055 48.494  -15.517 1.00 14.74  ? 589  LEU   A CB  1 
ATOM   4143 C  CG  . LEU   A 1 564 ? 50.973 49.162  -14.717 1.00 15.47  ? 589  LEU   A CG  1 
ATOM   4144 C  CD1 . LEU   A 1 564 ? 50.127 50.130  -15.593 1.00 16.32  ? 589  LEU   A CD1 1 
ATOM   4145 C  CD2 . LEU   A 1 564 ? 50.068 48.092  -14.059 1.00 16.02  ? 589  LEU   A CD2 1 
ATOM   4146 N  N   . ILE   A 1 565 ? 53.015 50.540  -17.722 1.00 13.96  ? 590  ILE   A N   1 
ATOM   4147 C  CA  . ILE   A 1 565 ? 52.852 51.757  -18.507 1.00 14.41  ? 590  ILE   A CA  1 
ATOM   4148 C  C   . ILE   A 1 565 ? 51.443 51.787  -19.111 1.00 14.49  ? 590  ILE   A C   1 
ATOM   4149 O  O   . ILE   A 1 565 ? 51.100 50.885  -19.864 1.00 15.96  ? 590  ILE   A O   1 
ATOM   4150 C  CB  . ILE   A 1 565 ? 53.882 51.815  -19.667 1.00 15.53  ? 590  ILE   A CB  1 
ATOM   4151 C  CG1 . ILE   A 1 565 ? 55.329 51.584  -19.137 1.00 16.64  ? 590  ILE   A CG1 1 
ATOM   4152 C  CG2 . ILE   A 1 565 ? 53.753 53.096  -20.481 1.00 17.31  ? 590  ILE   A CG2 1 
ATOM   4153 C  CD1 . ILE   A 1 565 ? 55.770 52.581  -18.120 1.00 17.80  ? 590  ILE   A CD1 1 
ATOM   4154 N  N   . LEU   A 1 566 ? 50.656 52.776  -18.756 1.00 13.78  ? 591  LEU   A N   1 
ATOM   4155 C  CA  . LEU   A 1 566 ? 49.315 52.907  -19.320 1.00 13.87  ? 591  LEU   A CA  1 
ATOM   4156 C  C   . LEU   A 1 566 ? 49.434 53.279  -20.787 1.00 14.96  ? 591  LEU   A C   1 
ATOM   4157 O  O   . LEU   A 1 566 ? 50.388 53.914  -21.203 1.00 15.23  ? 591  LEU   A O   1 
ATOM   4158 C  CB  . LEU   A 1 566 ? 48.535 54.000  -18.587 1.00 13.61  ? 591  LEU   A CB  1 
ATOM   4159 C  CG  . LEU   A 1 566 ? 48.245 53.687  -17.139 1.00 15.25  ? 591  LEU   A CG  1 
ATOM   4160 C  CD1 . LEU   A 1 566 ? 47.701 54.947  -16.417 1.00 16.29  ? 591  LEU   A CD1 1 
ATOM   4161 C  CD2 . LEU   A 1 566 ? 47.238 52.523  -17.044 1.00 15.77  ? 591  LEU   A CD2 1 
ATOM   4162 N  N   . PRO   A 1 567 ? 48.435 52.927  -21.594 1.00 14.20  ? 592  PRO   A N   1 
ATOM   4163 C  CA  . PRO   A 1 567 ? 48.513 53.261  -23.041 1.00 14.91  ? 592  PRO   A CA  1 
ATOM   4164 C  C   . PRO   A 1 567 ? 48.457 54.748  -23.291 1.00 15.61  ? 592  PRO   A C   1 
ATOM   4165 O  O   . PRO   A 1 567 ? 49.007 55.218  -24.305 1.00 17.42  ? 592  PRO   A O   1 
ATOM   4166 C  CB  . PRO   A 1 567 ? 47.268 52.590  -23.638 1.00 16.53  ? 592  PRO   A CB  1 
ATOM   4167 C  CG  . PRO   A 1 567 ? 46.512 52.077  -22.540 1.00 18.46  ? 592  PRO   A CG  1 
ATOM   4168 C  CD  . PRO   A 1 567 ? 47.274 52.090  -21.261 1.00 15.47  ? 592  PRO   A CD  1 
ATOM   4169 N  N   . GLU   A 1 568 ? 47.768 55.500  -22.429 1.00 15.24  ? 593  GLU   A N   1 
ATOM   4170 C  CA  . GLU   A 1 568 ? 47.572 56.931  -22.517 1.00 15.98  ? 593  GLU   A CA  1 
ATOM   4171 C  C   . GLU   A 1 568 ? 47.405 57.444  -21.089 1.00 15.96  ? 593  GLU   A C   1 
ATOM   4172 O  O   . GLU   A 1 568 ? 46.911 56.703  -20.224 1.00 15.78  ? 593  GLU   A O   1 
ATOM   4173 C  CB  . GLU   A 1 568 ? 46.243 57.248  -23.260 1.00 20.70  ? 593  GLU   A CB  1 
ATOM   4174 C  CG  . GLU   A 1 568 ? 46.162 56.647  -24.635 1.00 24.22  ? 593  GLU   A CG  1 
ATOM   4175 C  CD  . GLU   A 1 568 ? 44.916 57.065  -25.373 1.00 22.56  ? 593  GLU   A CD  1 
ATOM   4176 O  OE1 . GLU   A 1 568 ? 43.885 56.341  -25.310 1.00 18.41  ? 593  GLU   A OE1 1 
ATOM   4177 O  OE2 . GLU   A 1 568 ? 44.992 58.119  -26.046 1.00 22.85  ? 593  GLU   A OE2 1 
ATOM   4178 N  N   . GLU   A 1 569 ? 47.706 58.730  -20.873 1.00 16.36  ? 594  GLU   A N   1 
ATOM   4179 C  CA  . GLU   A 1 569 ? 47.488 59.333  -19.544 1.00 16.25  ? 594  GLU   A CA  1 
ATOM   4180 C  C   . GLU   A 1 569 ? 46.009 59.289  -19.166 1.00 16.25  ? 594  GLU   A C   1 
ATOM   4181 O  O   . GLU   A 1 569 ? 45.139 59.361  -20.026 1.00 16.72  ? 594  GLU   A O   1 
ATOM   4182 C  CB  . GLU   A 1 569 ? 47.979 60.803  -19.512 1.00 18.87  ? 594  GLU   A CB  1 
ATOM   4183 C  CG  . GLU   A 1 569 ? 49.480 60.848  -19.751 1.00 23.02  ? 594  GLU   A CG  1 
ATOM   4184 C  CD  . GLU   A 1 569 ? 50.204 62.128  -19.382 1.00 34.99  ? 594  GLU   A CD  1 
ATOM   4185 O  OE1 . GLU   A 1 569 ? 49.601 62.983  -18.696 1.00 34.48  ? 594  GLU   A OE1 1 
ATOM   4186 O  OE2 . GLU   A 1 569 ? 51.402 62.245  -19.732 1.00 41.02  ? 594  GLU   A OE2 1 
ATOM   4187 N  N   . VAL   A 1 570 ? 45.727 59.198  -17.862 1.00 14.75  ? 595  VAL   A N   1 
ATOM   4188 C  CA  . VAL   A 1 570 ? 44.366 59.121  -17.329 1.00 14.80  ? 595  VAL   A CA  1 
ATOM   4189 C  C   . VAL   A 1 570 ? 44.179 60.206  -16.254 1.00 16.56  ? 595  VAL   A C   1 
ATOM   4190 O  O   . VAL   A 1 570 ? 45.142 60.763  -15.699 1.00 19.18  ? 595  VAL   A O   1 
ATOM   4191 C  CB  . VAL   A 1 570 ? 44.090 57.715  -16.747 1.00 15.16  ? 595  VAL   A CB  1 
ATOM   4192 C  CG1 . VAL   A 1 570 ? 44.235 56.668  -17.840 1.00 15.55  ? 595  VAL   A CG1 1 
ATOM   4193 C  CG2 . VAL   A 1 570 ? 45.017 57.386  -15.553 1.00 16.06  ? 595  VAL   A CG2 1 
ATOM   4194 N  N   . GLU   A 1 571 ? 42.920 60.477  -15.935 1.00 16.40  ? 596  GLU   A N   1 
ATOM   4195 C  CA  . GLU   A 1 571 ? 42.559 61.445  -14.906 1.00 17.25  ? 596  GLU   A CA  1 
ATOM   4196 C  C   . GLU   A 1 571 ? 42.577 60.810  -13.527 1.00 18.14  ? 596  GLU   A C   1 
ATOM   4197 O  O   . GLU   A 1 571 ? 42.709 61.512  -12.524 1.00 19.60  ? 596  GLU   A O   1 
ATOM   4198 C  CB  . GLU   A 1 571 ? 41.153 62.037  -15.195 1.00 18.66  ? 596  GLU   A CB  1 
ATOM   4199 C  CG  . GLU   A 1 571 ? 41.119 62.880  -16.452 1.00 26.05  ? 596  GLU   A CG  1 
ATOM   4200 C  CD  . GLU   A 1 571 ? 39.767 63.501  -16.769 1.00 33.10  ? 596  GLU   A CD  1 
ATOM   4201 O  OE1 . GLU   A 1 571 ? 39.423 63.546  -17.970 1.00 37.52  ? 596  GLU   A OE1 1 
ATOM   4202 O  OE2 . GLU   A 1 571 ? 39.040 63.888  -15.828 1.00 33.81  ? 596  GLU   A OE2 1 
ATOM   4203 N  N   . TRP   A 1 572 ? 42.368 59.497  -13.453 1.00 15.36  ? 597  TRP   A N   1 
ATOM   4204 C  CA  . TRP   A 1 572 ? 42.368 58.749  -12.211 1.00 15.19  ? 597  TRP   A CA  1 
ATOM   4205 C  C   . TRP   A 1 572 ? 42.515 57.291  -12.539 1.00 14.60  ? 597  TRP   A C   1 
ATOM   4206 O  O   . TRP   A 1 572 ? 42.254 56.854  -13.672 1.00 14.02  ? 597  TRP   A O   1 
ATOM   4207 C  CB  . TRP   A 1 572 ? 41.090 58.998  -11.384 1.00 16.10  ? 597  TRP   A CB  1 
ATOM   4208 C  CG  . TRP   A 1 572 ? 39.821 58.705  -12.115 1.00 15.48  ? 597  TRP   A CG  1 
ATOM   4209 C  CD1 . TRP   A 1 572 ? 39.009 59.623  -12.707 1.00 17.28  ? 597  TRP   A CD1 1 
ATOM   4210 C  CD2 . TRP   A 1 572 ? 39.156 57.424  -12.253 1.00 14.42  ? 597  TRP   A CD2 1 
ATOM   4211 N  NE1 . TRP   A 1 572 ? 37.901 59.001  -13.241 1.00 17.31  ? 597  TRP   A NE1 1 
ATOM   4212 C  CE2 . TRP   A 1 572 ? 37.969 57.650  -12.982 1.00 15.73  ? 597  TRP   A CE2 1 
ATOM   4213 C  CE3 . TRP   A 1 572 ? 39.466 56.114  -11.867 1.00 14.58  ? 597  TRP   A CE3 1 
ATOM   4214 C  CZ2 . TRP   A 1 572 ? 37.089 56.612  -13.322 1.00 14.66  ? 597  TRP   A CZ2 1 
ATOM   4215 C  CZ3 . TRP   A 1 572 ? 38.595 55.087  -12.217 1.00 15.20  ? 597  TRP   A CZ3 1 
ATOM   4216 C  CH2 . TRP   A 1 572 ? 37.418 55.347  -12.923 1.00 15.24  ? 597  TRP   A CH2 1 
ATOM   4217 N  N   . ILE   A 1 573 ? 43.004 56.543  -11.556 1.00 13.84  ? 598  ILE   A N   1 
ATOM   4218 C  CA  . ILE   A 1 573 ? 43.161 55.110  -11.651 1.00 13.51  ? 598  ILE   A CA  1 
ATOM   4219 C  C   . ILE   A 1 573 ? 42.686 54.522  -10.323 1.00 13.88  ? 598  ILE   A C   1 
ATOM   4220 O  O   . ILE   A 1 573 ? 42.853 55.170  -9.272  1.00 15.61  ? 598  ILE   A O   1 
ATOM   4221 C  CB  . ILE   A 1 573 ? 44.615 54.698  -11.982 1.00 14.75  ? 598  ILE   A CB  1 
ATOM   4222 C  CG1 . ILE   A 1 573 ? 44.772 53.209  -12.142 1.00 14.62  ? 598  ILE   A CG1 1 
ATOM   4223 C  CG2 . ILE   A 1 573 ? 45.614 55.262  -10.952 1.00 18.34  ? 598  ILE   A CG2 1 
ATOM   4224 C  CD1 . ILE   A 1 573 ? 46.049 52.786  -12.926 1.00 14.88  ? 598  ILE   A CD1 1 
ATOM   4225 N  N   . LYS   A 1 574 ? 41.984 53.382  -10.369 1.00 12.33  ? 599  LYS   A N   1 
ATOM   4226 C  CA  . LYS   A 1 574 ? 41.443 52.795  -9.140  1.00 12.74  ? 599  LYS   A CA  1 
ATOM   4227 C  C   . LYS   A 1 574 ? 41.790 51.323  -9.125  1.00 12.33  ? 599  LYS   A C   1 
ATOM   4228 O  O   . LYS   A 1 574 ? 41.381 50.557  -9.997  1.00 12.58  ? 599  LYS   A O   1 
ATOM   4229 C  CB  . LYS   A 1 574 ? 39.906 53.029  -9.087  1.00 14.77  ? 599  LYS   A CB  1 
ATOM   4230 C  CG  . LYS   A 1 574 ? 39.317 52.912  -7.673  1.00 15.02  ? 599  LYS   A CG  1 
ATOM   4231 C  CD  . LYS   A 1 574 ? 38.991 51.463  -7.364  1.00 15.77  ? 599  LYS   A CD  1 
ATOM   4232 C  CE  . LYS   A 1 574 ? 38.504 51.322  -5.909  1.00 15.74  ? 599  LYS   A CE  1 
ATOM   4233 N  NZ  . LYS   A 1 574 ? 38.482 49.895  -5.542  1.00 15.82  ? 599  LYS   A NZ  1 
ATOM   4234 N  N   . PHE   A 1 575 ? 42.615 50.929  -8.157  1.00 12.18  ? 600  PHE   A N   1 
ATOM   4235 C  CA  . PHE   A 1 575 ? 43.040 49.539  -7.992  1.00 12.30  ? 600  PHE   A CA  1 
ATOM   4236 C  C   . PHE   A 1 575 ? 42.083 48.785  -7.057  1.00 12.77  ? 600  PHE   A C   1 
ATOM   4237 O  O   . PHE   A 1 575 ? 41.403 49.377  -6.206  1.00 13.53  ? 600  PHE   A O   1 
ATOM   4238 C  CB  . PHE   A 1 575 ? 44.465 49.458  -7.412  1.00 12.76  ? 600  PHE   A CB  1 
ATOM   4239 C  CG  . PHE   A 1 575 ? 45.533 49.555  -8.476  1.00 12.52  ? 600  PHE   A CG  1 
ATOM   4240 C  CD1 . PHE   A 1 575 ? 45.834 50.766  -9.073  1.00 12.42  ? 600  PHE   A CD1 1 
ATOM   4241 C  CD2 . PHE   A 1 575 ? 46.214 48.438  -8.882  1.00 12.43  ? 600  PHE   A CD2 1 
ATOM   4242 C  CE1 . PHE   A 1 575 ? 46.824 50.844  -10.072 1.00 13.70  ? 600  PHE   A CE1 1 
ATOM   4243 C  CE2 . PHE   A 1 575 ? 47.206 48.504  -9.877  1.00 13.44  ? 600  PHE   A CE2 1 
ATOM   4244 C  CZ  . PHE   A 1 575 ? 47.520 49.720  -10.452 1.00 13.32  ? 600  PHE   A CZ  1 
ATOM   4245 N  N   . ASN   A 1 576 ? 42.103 47.473  -7.191  1.00 12.31  ? 601  ASN   A N   1 
ATOM   4246 C  CA  . ASN   A 1 576 ? 41.289 46.532  -6.413  1.00 13.02  ? 601  ASN   A CA  1 
ATOM   4247 C  C   . ASN   A 1 576 ? 39.841 46.652  -6.788  1.00 13.66  ? 601  ASN   A C   1 
ATOM   4248 O  O   . ASN   A 1 576 ? 39.007 47.155  -6.007  1.00 14.43  ? 601  ASN   A O   1 
ATOM   4249 C  CB  . ASN   A 1 576 ? 41.515 46.673  -4.887  1.00 13.23  ? 601  ASN   A CB  1 
ATOM   4250 C  CG  . ASN   A 1 576 ? 41.112 45.410  -4.175  1.00 13.64  ? 601  ASN   A CG  1 
ATOM   4251 O  OD1 . ASN   A 1 576 ? 40.464 44.534  -4.747  1.00 14.62  ? 601  ASN   A OD1 1 
ATOM   4252 N  ND2 . ASN   A 1 576 ? 41.500 45.300  -2.881  1.00 14.05  ? 601  ASN   A ND2 1 
ATOM   4253 N  N   . VAL   A 1 577 ? 39.550 46.252  -8.002  1.00 13.37  ? 602  VAL   A N   1 
ATOM   4254 C  CA  . VAL   A 1 577 ? 38.245 46.479  -8.598  1.00 13.19  ? 602  VAL   A CA  1 
ATOM   4255 C  C   . VAL   A 1 577 ? 37.216 45.585  -7.948  1.00 14.06  ? 602  VAL   A C   1 
ATOM   4256 O  O   . VAL   A 1 577 ? 37.379 44.364  -7.893  1.00 15.48  ? 602  VAL   A O   1 
ATOM   4257 C  CB  . VAL   A 1 577 ? 38.297 46.280  -10.122 1.00 13.98  ? 602  VAL   A CB  1 
ATOM   4258 C  CG1 . VAL   A 1 577 ? 36.934 46.635  -10.747 1.00 15.42  ? 602  VAL   A CG1 1 
ATOM   4259 C  CG2 . VAL   A 1 577 ? 39.372 47.167  -10.712 1.00 15.56  ? 602  VAL   A CG2 1 
ATOM   4260 N  N   . GLY   A 1 578 ? 36.173 46.220  -7.425  1.00 14.36  ? 603  GLY   A N   1 
ATOM   4261 C  CA  . GLY   A 1 578 ? 35.121 45.458  -6.756  1.00 16.85  ? 603  GLY   A CA  1 
ATOM   4262 C  C   . GLY   A 1 578 ? 35.578 44.998  -5.386  1.00 17.61  ? 603  GLY   A C   1 
ATOM   4263 O  O   . GLY   A 1 578 ? 34.853 44.245  -4.742  1.00 19.92  ? 603  GLY   A O   1 
ATOM   4264 N  N   . MET   A 1 579 ? 36.765 45.384  -4.910  1.00 16.31  ? 604  MET   A N   1 
ATOM   4265 C  CA  . MET   A 1 579 ? 37.279 44.865  -3.616  1.00 16.05  ? 604  MET   A CA  1 
ATOM   4266 C  C   . MET   A 1 579 ? 37.343 43.336  -3.636  1.00 17.39  ? 604  MET   A C   1 
ATOM   4267 O  O   . MET   A 1 579 ? 37.048 42.667  -2.635  1.00 18.85  ? 604  MET   A O   1 
ATOM   4268 C  CB  . MET   A 1 579 ? 36.516 45.432  -2.397  1.00 17.56  ? 604  MET   A CB  1 
ATOM   4269 C  CG  . MET   A 1 579 ? 37.449 46.020  -1.344  1.00 19.70  ? 604  MET   A CG  1 
ATOM   4270 S  SD  . MET   A 1 579 ? 38.706 44.868  -0.735  1.00 20.83  ? 604  MET   A SD  1 
ATOM   4271 C  CE  . MET   A 1 579 ? 37.704 43.852  0.460   1.00 19.15  ? 604  MET   A CE  1 
ATOM   4272 N  N   . ASN   A 1 580 ? 37.744 42.772  -4.789  1.00 16.15  ? 605  ASN   A N   1 
ATOM   4273 C  CA  . ASN   A 1 580 ? 37.969 41.351  -4.925  1.00 16.38  ? 605  ASN   A CA  1 
ATOM   4274 C  C   . ASN   A 1 580 ? 39.360 40.869  -4.467  1.00 16.66  ? 605  ASN   A C   1 
ATOM   4275 O  O   . ASN   A 1 580 ? 39.596 39.655  -4.379  1.00 19.31  ? 605  ASN   A O   1 
ATOM   4276 C  CB  . ASN   A 1 580 ? 37.688 40.860  -6.334  1.00 17.50  ? 605  ASN   A CB  1 
ATOM   4277 C  CG  . ASN   A 1 580 ? 36.215 40.829  -6.607  1.00 19.71  ? 605  ASN   A CG  1 
ATOM   4278 O  OD1 . ASN   A 1 580 ? 35.466 40.076  -5.997  1.00 19.55  ? 605  ASN   A OD1 1 
ATOM   4279 N  ND2 . ASN   A 1 580 ? 35.726 41.735  -7.470  1.00 20.72  ? 605  ASN   A ND2 1 
ATOM   4280 N  N   . GLY   A 1 581 ? 40.222 41.787  -4.109  1.00 15.54  ? 606  GLY   A N   1 
ATOM   4281 C  CA  . GLY   A 1 581 ? 41.551 41.443  -3.623  1.00 14.63  ? 606  GLY   A CA  1 
ATOM   4282 C  C   . GLY   A 1 581 ? 41.707 41.726  -2.140  1.00 13.84  ? 606  GLY   A C   1 
ATOM   4283 O  O   . GLY   A 1 581 ? 41.172 42.691  -1.607  1.00 14.12  ? 606  GLY   A O   1 
ATOM   4284 N  N   . TYR   A 1 582 ? 42.496 40.851  -1.453  1.00 13.80  ? 607  TYR   A N   1 
ATOM   4285 C  CA  . TYR   A 1 582 ? 42.723 40.978  -0.016  1.00 14.13  ? 607  TYR   A CA  1 
ATOM   4286 C  C   . TYR   A 1 582 ? 43.946 41.870  0.237   1.00 13.73  ? 607  TYR   A C   1 
ATOM   4287 O  O   . TYR   A 1 582 ? 45.002 41.438  0.672   1.00 13.64  ? 607  TYR   A O   1 
ATOM   4288 C  CB  . TYR   A 1 582 ? 42.905 39.549  0.571   1.00 13.23  ? 607  TYR   A CB  1 
ATOM   4289 C  CG  . TYR   A 1 582 ? 42.785 39.505  2.073   1.00 13.71  ? 607  TYR   A CG  1 
ATOM   4290 C  CD1 . TYR   A 1 582 ? 41.566 39.751  2.700   1.00 13.09  ? 607  TYR   A CD1 1 
ATOM   4291 C  CD2 . TYR   A 1 582 ? 43.904 39.341  2.867   1.00 14.11  ? 607  TYR   A CD2 1 
ATOM   4292 C  CE1 . TYR   A 1 582 ? 41.456 39.762  4.087   1.00 14.96  ? 607  TYR   A CE1 1 
ATOM   4293 C  CE2 . TYR   A 1 582 ? 43.810 39.358  4.249   1.00 14.53  ? 607  TYR   A CE2 1 
ATOM   4294 C  CZ  . TYR   A 1 582 ? 42.591 39.575  4.850   1.00 15.10  ? 607  TYR   A CZ  1 
ATOM   4295 O  OH  . TYR   A 1 582 ? 42.534 39.565  6.232   1.00 15.72  ? 607  TYR   A OH  1 
ATOM   4296 N  N   . TYR   A 1 583 ? 43.748 43.158  -0.027  1.00 12.77  ? 608  TYR   A N   1 
ATOM   4297 C  CA  . TYR   A 1 583 ? 44.793 44.155  0.158   1.00 12.80  ? 608  TYR   A CA  1 
ATOM   4298 C  C   . TYR   A 1 583 ? 44.179 45.550  0.182   1.00 13.10  ? 608  TYR   A C   1 
ATOM   4299 O  O   . TYR   A 1 583 ? 43.014 45.708  -0.234  1.00 14.05  ? 608  TYR   A O   1 
ATOM   4300 C  CB  . TYR   A 1 583 ? 45.886 44.042  -0.955  1.00 13.19  ? 608  TYR   A CB  1 
ATOM   4301 C  CG  . TYR   A 1 583 ? 45.380 44.200  -2.376  1.00 12.08  ? 608  TYR   A CG  1 
ATOM   4302 C  CD1 . TYR   A 1 583 ? 45.321 45.445  -2.974  1.00 12.36  ? 608  TYR   A CD1 1 
ATOM   4303 C  CD2 . TYR   A 1 583 ? 44.954 43.099  -3.122  1.00 13.08  ? 608  TYR   A CD2 1 
ATOM   4304 C  CE1 . TYR   A 1 583 ? 44.898 45.600  -4.290  1.00 13.45  ? 608  TYR   A CE1 1 
ATOM   4305 C  CE2 . TYR   A 1 583 ? 44.568 43.236  -4.452  1.00 12.87  ? 608  TYR   A CE2 1 
ATOM   4306 C  CZ  . TYR   A 1 583 ? 44.483 44.496  -5.008  1.00 13.71  ? 608  TYR   A CZ  1 
ATOM   4307 O  OH  . TYR   A 1 583 ? 44.046 44.684  -6.300  1.00 14.79  ? 608  TYR   A OH  1 
ATOM   4308 N  N   A ILE   A 1 584 ? 44.924 46.518  0.614   0.50 13.42  ? 609  ILE   A N   1 
ATOM   4309 N  N   B ILE   A 1 584 ? 44.904 46.544  0.794   0.50 13.31  ? 609  ILE   A N   1 
ATOM   4310 C  CA  A ILE   A 1 584 ? 44.430 47.861  0.564   0.50 12.82  ? 609  ILE   A CA  1 
ATOM   4311 C  CA  B ILE   A 1 584 ? 44.527 47.975  0.923   0.50 12.82  ? 609  ILE   A CA  1 
ATOM   4312 C  C   A ILE   A 1 584 ? 45.318 48.653  -0.339  0.50 11.71  ? 609  ILE   A C   1 
ATOM   4313 C  C   B ILE   A 1 584 ? 45.399 48.784  -0.051  0.50 12.44  ? 609  ILE   A C   1 
ATOM   4314 O  O   A ILE   A 1 584 ? 46.406 48.184  -0.729  0.50 10.83  ? 609  ILE   A O   1 
ATOM   4315 O  O   B ILE   A 1 584 ? 46.576 48.442  -0.212  0.50 12.25  ? 609  ILE   A O   1 
ATOM   4316 C  CB  A ILE   A 1 584 ? 44.236 48.393  1.962   0.50 13.66  ? 609  ILE   A CB  1 
ATOM   4317 C  CB  B ILE   A 1 584 ? 44.724 48.453  2.399   0.50 12.75  ? 609  ILE   A CB  1 
ATOM   4318 C  CG1 A ILE   A 1 584 ? 45.558 48.521  2.670   0.50 13.62  ? 609  ILE   A CG1 1 
ATOM   4319 C  CG1 B ILE   A 1 584 ? 43.672 47.785  3.294   0.50 14.37  ? 609  ILE   A CG1 1 
ATOM   4320 C  CG2 A ILE   A 1 584 ? 43.249 47.527  2.756   0.50 14.94  ? 609  ILE   A CG2 1 
ATOM   4321 C  CG2 B ILE   A 1 584 ? 44.597 49.987  2.520   0.50 12.39  ? 609  ILE   A CG2 1 
ATOM   4322 C  CD1 A ILE   A 1 584 ? 45.391 49.504  3.766   0.50 16.39  ? 609  ILE   A CD1 1 
ATOM   4323 C  CD1 B ILE   A 1 584 ? 43.687 48.220  4.801   0.50 15.05  ? 609  ILE   A CD1 1 
ATOM   4324 N  N   . VAL   A 1 585 ? 44.843 49.836  -0.714  1.00 11.41  ? 610  VAL   A N   1 
ATOM   4325 C  CA  . VAL   A 1 585 ? 45.575 50.653  -1.669  1.00 11.91  ? 610  VAL   A CA  1 
ATOM   4326 C  C   . VAL   A 1 585 ? 45.722 52.054  -1.184  1.00 13.27  ? 610  VAL   A C   1 
ATOM   4327 O  O   . VAL   A 1 585 ? 44.717 52.673  -0.794  1.00 13.56  ? 610  VAL   A O   1 
ATOM   4328 C  CB  . VAL   A 1 585 ? 44.897 50.624  -3.070  1.00 12.52  ? 610  VAL   A CB  1 
ATOM   4329 C  CG1 . VAL   A 1 585 ? 45.794 51.326  -4.092  1.00 14.23  ? 610  VAL   A CG1 1 
ATOM   4330 C  CG2 . VAL   A 1 585 ? 44.598 49.199  -3.534  1.00 12.55  ? 610  VAL   A CG2 1 
ATOM   4331 N  N   . HIS   A 1 586 ? 46.932 52.582  -1.297  1.00 12.42  ? 611  HIS   A N   1 
ATOM   4332 C  CA  . HIS   A 1 586 ? 47.224 53.982  -1.056  1.00 12.41  ? 611  HIS   A CA  1 
ATOM   4333 C  C   . HIS   A 1 586 ? 47.699 54.618  -2.375  1.00 12.82  ? 611  HIS   A C   1 
ATOM   4334 O  O   . HIS   A 1 586 ? 48.366 53.960  -3.166  1.00 15.01  ? 611  HIS   A O   1 
ATOM   4335 C  CB  . HIS   A 1 586 ? 48.357 54.124  -0.021  1.00 13.34  ? 611  HIS   A CB  1 
ATOM   4336 C  CG  . HIS   A 1 586 ? 48.758 55.560  0.266   1.00 13.97  ? 611  HIS   A CG  1 
ATOM   4337 N  ND1 . HIS   A 1 586 ? 47.790 56.563  0.510   1.00 14.06  ? 611  HIS   A ND1 1 
ATOM   4338 C  CD2 . HIS   A 1 586 ? 49.996 56.104  0.367   1.00 15.36  ? 611  HIS   A CD2 1 
ATOM   4339 C  CE1 . HIS   A 1 586 ? 48.478 57.665  0.754   1.00 16.02  ? 611  HIS   A CE1 1 
ATOM   4340 N  NE2 . HIS   A 1 586 ? 49.807 57.457  0.642   1.00 15.82  ? 611  HIS   A NE2 1 
ATOM   4341 N  N   . TYR   A 1 587 ? 47.361 55.872  -2.585  1.00 13.39  ? 612  TYR   A N   1 
ATOM   4342 C  CA  . TYR   A 1 587 ? 47.744 56.603  -3.785  1.00 14.63  ? 612  TYR   A CA  1 
ATOM   4343 C  C   . TYR   A 1 587 ? 48.596 57.782  -3.371  1.00 15.77  ? 612  TYR   A C   1 
ATOM   4344 O  O   . TYR   A 1 587 ? 48.177 58.556  -2.519  1.00 16.95  ? 612  TYR   A O   1 
ATOM   4345 C  CB  . TYR   A 1 587 ? 46.492 57.111  -4.508  1.00 14.34  ? 612  TYR   A CB  1 
ATOM   4346 C  CG  . TYR   A 1 587 ? 45.560 55.998  -4.934  1.00 13.82  ? 612  TYR   A CG  1 
ATOM   4347 C  CD1 . TYR   A 1 587 ? 44.602 55.489  -4.056  1.00 13.56  ? 612  TYR   A CD1 1 
ATOM   4348 C  CD2 . TYR   A 1 587 ? 45.711 55.369  -6.169  1.00 13.68  ? 612  TYR   A CD2 1 
ATOM   4349 C  CE1 . TYR   A 1 587 ? 43.781 54.421  -4.420  1.00 13.76  ? 612  TYR   A CE1 1 
ATOM   4350 C  CE2 . TYR   A 1 587 ? 44.887 54.324  -6.547  1.00 13.53  ? 612  TYR   A CE2 1 
ATOM   4351 C  CZ  . TYR   A 1 587 ? 43.940 53.833  -5.669  1.00 13.81  ? 612  TYR   A CZ  1 
ATOM   4352 O  OH  . TYR   A 1 587 ? 43.125 52.794  -6.064  1.00 16.36  ? 612  TYR   A OH  1 
ATOM   4353 N  N   . GLU   A 1 588 ? 49.811 57.883  -3.906  1.00 15.98  ? 613  GLU   A N   1 
ATOM   4354 C  CA  . GLU   A 1 588 ? 50.675 59.019  -3.543  1.00 16.90  ? 613  GLU   A CA  1 
ATOM   4355 C  C   . GLU   A 1 588 ? 50.268 60.283  -4.296  1.00 19.23  ? 613  GLU   A C   1 
ATOM   4356 O  O   . GLU   A 1 588 ? 49.405 60.267  -5.187  1.00 19.51  ? 613  GLU   A O   1 
ATOM   4357 C  CB  . GLU   A 1 588 ? 52.155 58.671  -3.832  1.00 18.44  ? 613  GLU   A CB  1 
ATOM   4358 C  CG  . GLU   A 1 588 ? 52.603 57.597  -2.864  1.00 18.67  ? 613  GLU   A CG  1 
ATOM   4359 C  CD  . GLU   A 1 588 ? 54.105 57.364  -2.834  1.00 22.36  ? 613  GLU   A CD  1 
ATOM   4360 O  OE1 . GLU   A 1 588 ? 54.768 57.581  -3.878  1.00 22.82  ? 613  GLU   A OE1 1 
ATOM   4361 O  OE2 . GLU   A 1 588 ? 54.612 56.937  -1.770  1.00 23.79  ? 613  GLU   A OE2 1 
ATOM   4362 N  N   . ASP   A 1 589 ? 50.897 61.406  -3.884  1.00 20.42  ? 614  ASP   A N   1 
ATOM   4363 C  CA  . ASP   A 1 589 ? 50.760 62.681  -4.579  1.00 20.80  ? 614  ASP   A CA  1 
ATOM   4364 C  C   . ASP   A 1 589 ? 49.290 63.153  -4.611  1.00 20.62  ? 614  ASP   A C   1 
ATOM   4365 O  O   . ASP   A 1 589 ? 48.650 63.132  -3.556  1.00 21.31  ? 614  ASP   A O   1 
ATOM   4366 C  CB  . ASP   A 1 589 ? 51.416 62.587  -5.967  1.00 23.07  ? 614  ASP   A CB  1 
ATOM   4367 C  CG  . ASP   A 1 589 ? 52.827 62.066  -5.906  1.00 29.83  ? 614  ASP   A CG  1 
ATOM   4368 O  OD1 . ASP   A 1 589 ? 53.575 62.487  -4.993  1.00 31.04  ? 614  ASP   A OD1 1 
ATOM   4369 O  OD2 . ASP   A 1 589 ? 53.156 61.193  -6.706  1.00 33.49  ? 614  ASP   A OD2 1 
ATOM   4370 N  N   . ASP   A 1 590 ? 48.726 63.510  -5.781  1.00 21.05  ? 615  ASP   A N   1 
ATOM   4371 C  CA  . ASP   A 1 590 ? 47.331 63.979  -5.833  1.00 21.86  ? 615  ASP   A CA  1 
ATOM   4372 C  C   . ASP   A 1 590 ? 46.294 62.852  -5.929  1.00 21.62  ? 615  ASP   A C   1 
ATOM   4373 O  O   . ASP   A 1 590 ? 45.132 63.119  -6.210  1.00 21.42  ? 615  ASP   A O   1 
ATOM   4374 C  CB  . ASP   A 1 590 ? 47.145 64.973  -7.019  1.00 23.77  ? 615  ASP   A CB  1 
ATOM   4375 C  CG  . ASP   A 1 590 ? 47.383 64.378  -8.391  1.00 31.68  ? 615  ASP   A CG  1 
ATOM   4376 O  OD1 . ASP   A 1 590 ? 47.829 63.217  -8.466  1.00 33.98  ? 615  ASP   A OD1 1 
ATOM   4377 O  OD2 . ASP   A 1 590 ? 47.157 65.100  -9.411  1.00 33.90  ? 615  ASP   A OD2 1 
ATOM   4378 N  N   . GLY   A 1 591 ? 46.712 61.601  -5.734  1.00 20.16  ? 616  GLY   A N   1 
ATOM   4379 C  CA  . GLY   A 1 591 ? 45.810 60.468  -5.943  1.00 18.91  ? 616  GLY   A CA  1 
ATOM   4380 C  C   . GLY   A 1 591 ? 44.553 60.511  -5.108  1.00 17.72  ? 616  GLY   A C   1 
ATOM   4381 O  O   . GLY   A 1 591 ? 43.451 60.343  -5.643  1.00 17.81  ? 616  GLY   A O   1 
ATOM   4382 N  N   . TRP   A 1 592 ? 44.706 60.749  -3.801  1.00 17.64  ? 617  TRP   A N   1 
ATOM   4383 C  CA  . TRP   A 1 592 ? 43.522 60.806  -2.936  1.00 17.21  ? 617  TRP   A CA  1 
ATOM   4384 C  C   . TRP   A 1 592 ? 42.641 62.011  -3.241  1.00 18.35  ? 617  TRP   A C   1 
ATOM   4385 O  O   . TRP   A 1 592 ? 41.425 61.914  -3.142  1.00 19.13  ? 617  TRP   A O   1 
ATOM   4386 C  CB  . TRP   A 1 592 ? 43.872 60.687  -1.439  1.00 16.06  ? 617  TRP   A CB  1 
ATOM   4387 C  CG  . TRP   A 1 592 ? 44.095 59.248  -1.058  1.00 15.09  ? 617  TRP   A CG  1 
ATOM   4388 C  CD1 . TRP   A 1 592 ? 45.285 58.662  -0.749  1.00 15.50  ? 617  TRP   A CD1 1 
ATOM   4389 C  CD2 . TRP   A 1 592 ? 43.097 58.217  -0.984  1.00 14.39  ? 617  TRP   A CD2 1 
ATOM   4390 N  NE1 . TRP   A 1 592 ? 45.084 57.319  -0.462  1.00 15.02  ? 617  TRP   A NE1 1 
ATOM   4391 C  CE2 . TRP   A 1 592 ? 43.747 57.022  -0.624  1.00 14.35  ? 617  TRP   A CE2 1 
ATOM   4392 C  CE3 . TRP   A 1 592 ? 41.709 58.191  -1.212  1.00 14.67  ? 617  TRP   A CE3 1 
ATOM   4393 C  CZ2 . TRP   A 1 592 ? 43.066 55.813  -0.497  1.00 14.38  ? 617  TRP   A CZ2 1 
ATOM   4394 C  CZ3 . TRP   A 1 592 ? 41.028 57.006  -1.028  1.00 14.50  ? 617  TRP   A CZ3 1 
ATOM   4395 C  CH2 . TRP   A 1 592 ? 41.703 55.825  -0.702  1.00 14.68  ? 617  TRP   A CH2 1 
ATOM   4396 N  N   . ASP   A 1 593 ? 43.244 63.133  -3.663  1.00 18.04  ? 618  ASP   A N   1 
ATOM   4397 C  CA  . ASP   A 1 593 ? 42.456 64.289  -4.103  1.00 17.69  ? 618  ASP   A CA  1 
ATOM   4398 C  C   . ASP   A 1 593 ? 41.676 63.956  -5.345  1.00 18.23  ? 618  ASP   A C   1 
ATOM   4399 O  O   . ASP   A 1 593 ? 40.513 64.350  -5.448  1.00 19.66  ? 618  ASP   A O   1 
ATOM   4400 C  CB  . ASP   A 1 593 ? 43.392 65.483  -4.358  1.00 17.43  ? 618  ASP   A CB  1 
ATOM   4401 C  CG  . ASP   A 1 593 ? 43.778 66.228  -3.087  1.00 25.04  ? 618  ASP   A CG  1 
ATOM   4402 O  OD1 . ASP   A 1 593 ? 43.215 65.908  -1.999  1.00 25.74  ? 618  ASP   A OD1 1 
ATOM   4403 O  OD2 . ASP   A 1 593 ? 44.621 67.143  -3.169  1.00 27.68  ? 618  ASP   A OD2 1 
ATOM   4404 N  N   . SER   A 1 594 ? 42.266 63.235  -6.284  1.00 17.67  ? 619  SER   A N   1 
ATOM   4405 C  CA  A SER   A 1 594 ? 41.581 62.863  -7.520  0.50 17.75  ? 619  SER   A CA  1 
ATOM   4406 C  CA  B SER   A 1 594 ? 41.610 62.862  -7.516  0.50 18.38  ? 619  SER   A CA  1 
ATOM   4407 C  C   . SER   A 1 594 ? 40.415 61.930  -7.247  1.00 18.35  ? 619  SER   A C   1 
ATOM   4408 O  O   . SER   A 1 594 ? 39.319 62.094  -7.835  1.00 19.62  ? 619  SER   A O   1 
ATOM   4409 C  CB  A SER   A 1 594 ? 42.541 62.181  -8.489  0.50 18.93  ? 619  SER   A CB  1 
ATOM   4410 C  CB  B SER   A 1 594 ? 42.622 62.168  -8.419  0.50 21.37  ? 619  SER   A CB  1 
ATOM   4411 O  OG  A SER   A 1 594 ? 43.451 63.130  -9.012  0.50 19.04  ? 619  SER   A OG  1 
ATOM   4412 O  OG  B SER   A 1 594 ? 42.005 61.750  -9.617  0.50 24.81  ? 619  SER   A OG  1 
ATOM   4413 N  N   . LEU   A 1 595 ? 40.629 60.936  -6.354  1.00 17.13  ? 620  LEU   A N   1 
ATOM   4414 C  CA  . LEU   A 1 595 ? 39.537 60.015  -6.080  1.00 15.90  ? 620  LEU   A CA  1 
ATOM   4415 C  C   . LEU   A 1 595 ? 38.469 60.682  -5.213  1.00 16.12  ? 620  LEU   A C   1 
ATOM   4416 O  O   . LEU   A 1 595 ? 37.303 60.369  -5.385  1.00 16.36  ? 620  LEU   A O   1 
ATOM   4417 C  CB  . LEU   A 1 595 ? 40.104 58.764  -5.429  1.00 15.91  ? 620  LEU   A CB  1 
ATOM   4418 C  CG  . LEU   A 1 595 ? 40.977 57.959  -6.378  1.00 17.10  ? 620  LEU   A CG  1 
ATOM   4419 C  CD1 . LEU   A 1 595 ? 41.841 56.968  -5.576  1.00 17.98  ? 620  LEU   A CD1 1 
ATOM   4420 C  CD2 . LEU   A 1 595 ? 40.116 57.219  -7.429  1.00 18.49  ? 620  LEU   A CD2 1 
ATOM   4421 N  N   . THR   A 1 596 ? 38.860 61.614  -4.315  1.00 15.25  ? 621  THR   A N   1 
ATOM   4422 C  CA  . THR   A 1 596 ? 37.877 62.367  -3.539  1.00 16.45  ? 621  THR   A CA  1 
ATOM   4423 C  C   . THR   A 1 596 ? 37.005 63.200  -4.504  1.00 17.84  ? 621  THR   A C   1 
ATOM   4424 O  O   . THR   A 1 596 ? 35.777 63.216  -4.373  1.00 18.47  ? 621  THR   A O   1 
ATOM   4425 C  CB  . THR   A 1 596 ? 38.576 63.280  -2.538  1.00 18.40  ? 621  THR   A CB  1 
ATOM   4426 O  OG1 . THR   A 1 596 ? 39.307 62.471  -1.582  1.00 19.06  ? 621  THR   A OG1 1 
ATOM   4427 C  CG2 . THR   A 1 596 ? 37.585 64.144  -1.799  1.00 19.98  ? 621  THR   A CG2 1 
ATOM   4428 N  N   . GLY   A 1 597 ? 37.653 63.838  -5.480  1.00 17.32  ? 622  GLY   A N   1 
ATOM   4429 C  CA  . GLY   A 1 597 ? 36.920 64.633  -6.480  1.00 17.80  ? 622  GLY   A CA  1 
ATOM   4430 C  C   . GLY   A 1 597 ? 35.988 63.779  -7.317  1.00 17.91  ? 622  GLY   A C   1 
ATOM   4431 O  O   . GLY   A 1 597 ? 34.872 64.194  -7.648  1.00 19.19  ? 622  GLY   A O   1 
ATOM   4432 N  N   . LEU   A 1 598 ? 36.405 62.560  -7.668  1.00 16.97  ? 623  LEU   A N   1 
ATOM   4433 C  CA  . LEU   A 1 598 ? 35.571 61.646  -8.416  1.00 17.25  ? 623  LEU   A CA  1 
ATOM   4434 C  C   . LEU   A 1 598 ? 34.324 61.296  -7.614  1.00 18.30  ? 623  LEU   A C   1 
ATOM   4435 O  O   . LEU   A 1 598 ? 33.215 61.345  -8.151  1.00 19.50  ? 623  LEU   A O   1 
ATOM   4436 C  CB  . LEU   A 1 598 ? 36.372 60.378  -8.723  1.00 18.23  ? 623  LEU   A CB  1 
ATOM   4437 C  CG  . LEU   A 1 598 ? 35.699 59.412  -9.661  1.00 22.81  ? 623  LEU   A CG  1 
ATOM   4438 C  CD1 . LEU   A 1 598 ? 35.508 60.072  -11.043 1.00 25.30  ? 623  LEU   A CD1 1 
ATOM   4439 C  CD2 . LEU   A 1 598 ? 36.565 58.202  -9.868  1.00 23.56  ? 623  LEU   A CD2 1 
ATOM   4440 N  N   . LEU   A 1 599 ? 34.497 60.977  -6.304  1.00 16.88  ? 624  LEU   A N   1 
ATOM   4441 C  CA  . LEU   A 1 599 ? 33.333 60.643  -5.483  1.00 16.30  ? 624  LEU   A CA  1 
ATOM   4442 C  C   . LEU   A 1 599 ? 32.415 61.857  -5.315  1.00 17.60  ? 624  LEU   A C   1 
ATOM   4443 O  O   . LEU   A 1 599 ? 31.210 61.684  -5.269  1.00 18.03  ? 624  LEU   A O   1 
ATOM   4444 C  CB  . LEU   A 1 599 ? 33.800 60.148  -4.129  1.00 15.84  ? 624  LEU   A CB  1 
ATOM   4445 C  CG  . LEU   A 1 599 ? 34.511 58.781  -4.174  1.00 16.43  ? 624  LEU   A CG  1 
ATOM   4446 C  CD1 . LEU   A 1 599 ? 35.148 58.492  -2.827  1.00 16.29  ? 624  LEU   A CD1 1 
ATOM   4447 C  CD2 . LEU   A 1 599 ? 33.496 57.672  -4.519  1.00 17.70  ? 624  LEU   A CD2 1 
ATOM   4448 N  N   . LYS   A 1 600 ? 32.981 63.053  -5.229  1.00 17.66  ? 625  LYS   A N   1 
ATOM   4449 C  CA  . LYS   A 1 600 ? 32.158 64.248  -5.025  1.00 18.07  ? 625  LYS   A CA  1 
ATOM   4450 C  C   . LYS   A 1 600 ? 31.429 64.695  -6.257  1.00 20.46  ? 625  LYS   A C   1 
ATOM   4451 O  O   . LYS   A 1 600 ? 30.310 65.208  -6.151  1.00 22.33  ? 625  LYS   A O   1 
ATOM   4452 C  CB  . LYS   A 1 600 ? 33.012 65.358  -4.449  1.00 20.11  ? 625  LYS   A CB  1 
ATOM   4453 C  CG  . LYS   A 1 600 ? 33.198 65.000  -2.974  1.00 25.07  ? 625  LYS   A CG  1 
ATOM   4454 C  CD  . LYS   A 1 600 ? 33.956 66.011  -2.226  1.00 26.03  ? 625  LYS   A CD  1 
ATOM   4455 C  CE  . LYS   A 1 600 ? 34.087 65.561  -0.795  1.00 23.26  ? 625  LYS   A CE  1 
ATOM   4456 N  NZ  . LYS   A 1 600 ? 34.578 66.657  0.073   1.00 26.39  ? 625  LYS   A NZ  1 
ATOM   4457 N  N   . GLY   A 1 601 ? 32.043 64.523  -7.408  1.00 21.37  ? 626  GLY   A N   1 
ATOM   4458 C  CA  . GLY   A 1 601 ? 31.477 65.039  -8.647  1.00 22.85  ? 626  GLY   A CA  1 
ATOM   4459 C  C   . GLY   A 1 601 ? 30.696 64.077  -9.490  1.00 23.55  ? 626  GLY   A C   1 
ATOM   4460 O  O   . GLY   A 1 601 ? 29.746 64.489  -10.177 1.00 24.53  ? 626  GLY   A O   1 
ATOM   4461 N  N   . THR   A 1 602 ? 31.177 62.834  -9.584  1.00 23.85  ? 627  THR   A N   1 
ATOM   4462 C  CA  . THR   A 1 602 ? 30.549 61.830  -10.441 1.00 23.88  ? 627  THR   A CA  1 
ATOM   4463 C  C   . THR   A 1 602 ? 30.770 60.490  -9.760  1.00 22.31  ? 627  THR   A C   1 
ATOM   4464 O  O   . THR   A 1 602 ? 31.498 59.627  -10.278 1.00 21.60  ? 627  THR   A O   1 
ATOM   4465 C  CB  . THR   A 1 602 ? 31.218 61.802  -11.848 1.00 27.70  ? 627  THR   A CB  1 
ATOM   4466 O  OG1 . THR   A 1 602 ? 32.627 61.606  -11.680 1.00 30.22  ? 627  THR   A OG1 1 
ATOM   4467 C  CG2 . THR   A 1 602 ? 30.938 63.052  -12.703 1.00 28.71  ? 627  THR   A CG2 1 
ATOM   4468 N  N   . HIS   A 1 603 ? 30.122 60.284  -8.601  1.00 20.92  ? 628  HIS   A N   1 
ATOM   4469 C  CA  . HIS   A 1 603 ? 30.395 59.049  -7.832  1.00 19.86  ? 628  HIS   A CA  1 
ATOM   4470 C  C   . HIS   A 1 603 ? 30.038 57.788  -8.556  1.00 20.22  ? 628  HIS   A C   1 
ATOM   4471 O  O   . HIS   A 1 603 ? 30.645 56.747  -8.268  1.00 19.94  ? 628  HIS   A O   1 
ATOM   4472 C  CB  . HIS   A 1 603 ? 29.746 59.088  -6.434  1.00 20.73  ? 628  HIS   A CB  1 
ATOM   4473 C  CG  . HIS   A 1 603 ? 28.259 58.916  -6.408  1.00 22.94  ? 628  HIS   A CG  1 
ATOM   4474 N  ND1 . HIS   A 1 603 ? 27.405 60.010  -6.541  1.00 27.57  ? 628  HIS   A ND1 1 
ATOM   4475 C  CD2 . HIS   A 1 603 ? 27.509 57.800  -6.222  1.00 24.91  ? 628  HIS   A CD2 1 
ATOM   4476 C  CE1 . HIS   A 1 603 ? 26.176 59.517  -6.455  1.00 27.84  ? 628  HIS   A CE1 1 
ATOM   4477 N  NE2 . HIS   A 1 603 ? 26.193 58.195  -6.219  1.00 25.43  ? 628  HIS   A NE2 1 
ATOM   4478 N  N   . THR   A 1 604 ? 29.077 57.828  -9.492  1.00 20.66  ? 629  THR   A N   1 
ATOM   4479 C  CA  . THR   A 1 604 ? 28.708 56.623  -10.232 1.00 21.75  ? 629  THR   A CA  1 
ATOM   4480 C  C   . THR   A 1 604 ? 29.735 56.242  -11.321 1.00 23.04  ? 629  THR   A C   1 
ATOM   4481 O  O   . THR   A 1 604 ? 29.522 55.232  -11.995 1.00 24.50  ? 629  THR   A O   1 
ATOM   4482 C  CB  . THR   A 1 604 ? 27.294 56.716  -10.781 1.00 25.03  ? 629  THR   A CB  1 
ATOM   4483 O  OG1 . THR   A 1 604 ? 27.207 57.835  -11.680 1.00 27.49  ? 629  THR   A OG1 1 
ATOM   4484 C  CG2 . THR   A 1 604 ? 26.255 56.871  -9.666  1.00 25.91  ? 629  THR   A CG2 1 
ATOM   4485 N  N   . ALA   A 1 605 ? 30.839 56.998  -11.457 1.00 21.94  ? 630  ALA   A N   1 
ATOM   4486 C  CA  . ALA   A 1 605 ? 31.936 56.634  -12.365 1.00 22.22  ? 630  ALA   A CA  1 
ATOM   4487 C  C   . ALA   A 1 605 ? 32.546 55.291  -11.943 1.00 21.82  ? 630  ALA   A C   1 
ATOM   4488 O  O   . ALA   A 1 605 ? 33.173 54.637  -12.783 1.00 22.60  ? 630  ALA   A O   1 
ATOM   4489 C  CB  . ALA   A 1 605 ? 33.010 57.712  -12.354 1.00 22.89  ? 630  ALA   A CB  1 
ATOM   4490 N  N   . VAL   A 1 606 ? 32.413 54.885  -10.642 1.00 19.77  ? 631  VAL   A N   1 
ATOM   4491 C  CA  . VAL   A 1 606 ? 32.875 53.589  -10.158 1.00 18.71  ? 631  VAL   A CA  1 
ATOM   4492 C  C   . VAL   A 1 606 ? 31.698 52.884  -9.439  1.00 16.89  ? 631  VAL   A C   1 
ATOM   4493 O  O   . VAL   A 1 606 ? 30.722 53.540  -9.046  1.00 17.82  ? 631  VAL   A O   1 
ATOM   4494 C  CB  . VAL   A 1 606 ? 34.157 53.621  -9.300  1.00 19.02  ? 631  VAL   A CB  1 
ATOM   4495 C  CG1 . VAL   A 1 606 ? 35.324 54.252  -10.083 1.00 20.92  ? 631  VAL   A CG1 1 
ATOM   4496 C  CG2 . VAL   A 1 606 ? 33.900 54.395  -7.984  1.00 19.01  ? 631  VAL   A CG2 1 
ATOM   4497 N  N   . SER   A 1 607 ? 31.768 51.577  -9.339  1.00 16.37  ? 632  SER   A N   1 
ATOM   4498 C  CA  . SER   A 1 607 ? 30.698 50.793  -8.766  1.00 15.41  ? 632  SER   A CA  1 
ATOM   4499 C  C   . SER   A 1 607 ? 30.510 51.104  -7.285  1.00 14.58  ? 632  SER   A C   1 
ATOM   4500 O  O   . SER   A 1 607 ? 31.395 51.623  -6.589  1.00 15.11  ? 632  SER   A O   1 
ATOM   4501 C  CB  . SER   A 1 607 ? 31.009 49.308  -8.898  1.00 16.67  ? 632  SER   A CB  1 
ATOM   4502 O  OG  . SER   A 1 607 ? 31.992 48.932  -7.943  1.00 17.47  ? 632  SER   A OG  1 
ATOM   4503 N  N   . SER   A 1 608 ? 29.350 50.717  -6.779  1.00 15.52  ? 633  SER   A N   1 
ATOM   4504 C  CA  A SER   A 1 608 ? 29.036 50.876  -5.352  0.35 14.95  ? 633  SER   A CA  1 
ATOM   4505 C  CA  B SER   A 1 608 ? 29.031 50.909  -5.363  0.35 15.53  ? 633  SER   A CA  1 
ATOM   4506 C  CA  C SER   A 1 608 ? 29.007 50.874  -5.375  0.30 15.37  ? 633  SER   A CA  1 
ATOM   4507 C  C   . SER   A 1 608 ? 30.085 50.235  -4.466  1.00 15.18  ? 633  SER   A C   1 
ATOM   4508 O  O   . SER   A 1 608 ? 30.510 50.840  -3.473  1.00 15.29  ? 633  SER   A O   1 
ATOM   4509 C  CB  A SER   A 1 608 ? 27.689 50.240  -5.049  0.35 15.52  ? 633  SER   A CB  1 
ATOM   4510 C  CB  B SER   A 1 608 ? 27.633 50.377  -5.068  0.35 17.68  ? 633  SER   A CB  1 
ATOM   4511 C  CB  C SER   A 1 608 ? 27.645 50.229  -5.139  0.30 16.94  ? 633  SER   A CB  1 
ATOM   4512 O  OG  A SER   A 1 608 ? 26.724 50.974  -5.767  0.35 14.29  ? 633  SER   A OG  1 
ATOM   4513 O  OG  B SER   A 1 608 ? 27.521 49.031  -5.494  0.35 19.55  ? 633  SER   A OG  1 
ATOM   4514 O  OG  C SER   A 1 608 ? 27.308 50.257  -3.767  0.30 18.35  ? 633  SER   A OG  1 
ATOM   4515 N  N   . ASN   A 1 609 ? 30.551 49.019  -4.841  1.00 15.35  ? 634  ASN   A N   1 
ATOM   4516 C  CA  . ASN   A 1 609 ? 31.565 48.365  -4.024  1.00 15.60  ? 634  ASN   A CA  1 
ATOM   4517 C  C   . ASN   A 1 609 ? 32.938 49.009  -4.118  1.00 14.24  ? 634  ASN   A C   1 
ATOM   4518 O  O   . ASN   A 1 609 ? 33.695 49.001  -3.153  1.00 13.99  ? 634  ASN   A O   1 
ATOM   4519 C  CB  . ASN   A 1 609 ? 31.621 46.905  -4.289  1.00 16.72  ? 634  ASN   A CB  1 
ATOM   4520 C  CG  . ASN   A 1 609 ? 30.346 46.214  -3.765  1.00 19.47  ? 634  ASN   A CG  1 
ATOM   4521 O  OD1 . ASN   A 1 609 ? 29.467 46.823  -3.100  1.00 19.52  ? 634  ASN   A OD1 1 
ATOM   4522 N  ND2 . ASN   A 1 609 ? 30.263 44.916  -4.013  1.00 18.70  ? 634  ASN   A ND2 1 
ATOM   4523 N  N   . ASP   A 1 610 ? 33.221 49.631  -5.270  1.00 13.69  ? 635  ASP   A N   1 
ATOM   4524 C  CA  . ASP   A 1 610 ? 34.446 50.405  -5.381  1.00 13.01  ? 635  ASP   A CA  1 
ATOM   4525 C  C   . ASP   A 1 610 ? 34.363 51.656  -4.510  1.00 13.45  ? 635  ASP   A C   1 
ATOM   4526 O  O   . ASP   A 1 610 ? 35.374 52.012  -3.887  1.00 14.08  ? 635  ASP   A O   1 
ATOM   4527 C  CB  . ASP   A 1 610 ? 34.714 50.753  -6.861  1.00 13.55  ? 635  ASP   A CB  1 
ATOM   4528 C  CG  . ASP   A 1 610 ? 35.288 49.552  -7.578  1.00 16.01  ? 635  ASP   A CG  1 
ATOM   4529 O  OD1 . ASP   A 1 610 ? 36.319 49.028  -7.125  1.00 15.83  ? 635  ASP   A OD1 1 
ATOM   4530 O  OD2 . ASP   A 1 610 ? 34.596 49.000  -8.490  1.00 20.14  ? 635  ASP   A OD2 1 
ATOM   4531 N  N   . ARG   A 1 611 ? 33.180 52.300  -4.422  1.00 13.39  ? 636  ARG   A N   1 
ATOM   4532 C  CA  . ARG   A 1 611 ? 33.081 53.460  -3.518  1.00 13.16  ? 636  ARG   A CA  1 
ATOM   4533 C  C   . ARG   A 1 611 ? 33.237 52.967  -2.061  1.00 13.35  ? 636  ARG   A C   1 
ATOM   4534 O  O   . ARG   A 1 611 ? 33.978 53.601  -1.294  1.00 13.94  ? 636  ARG   A O   1 
ATOM   4535 C  CB  . ARG   A 1 611 ? 31.722 54.097  -3.692  1.00 13.28  ? 636  ARG   A CB  1 
ATOM   4536 C  CG  . ARG   A 1 611 ? 31.550 54.617  -5.123  1.00 13.59  ? 636  ARG   A CG  1 
ATOM   4537 C  CD  . ARG   A 1 611 ? 30.407 55.573  -5.255  1.00 15.33  ? 636  ARG   A CD  1 
ATOM   4538 N  NE  . ARG   A 1 611 ? 29.090 54.993  -5.014  1.00 15.29  ? 636  ARG   A NE  1 
ATOM   4539 C  CZ  . ARG   A 1 611 ? 28.295 54.426  -5.913  1.00 16.31  ? 636  ARG   A CZ  1 
ATOM   4540 N  NH1 . ARG   A 1 611 ? 28.750 54.130  -7.129  1.00 16.35  ? 636  ARG   A NH1 1 
ATOM   4541 N  NH2 . ARG   A 1 611 ? 27.041 54.131  -5.599  1.00 16.68  ? 636  ARG   A NH2 1 
ATOM   4542 N  N   . ALA   A 1 612 ? 32.646 51.816  -1.697  1.00 12.94  ? 637  ALA   A N   1 
ATOM   4543 C  CA  . ALA   A 1 612 ? 32.844 51.303  -0.330  1.00 12.65  ? 637  ALA   A CA  1 
ATOM   4544 C  C   . ALA   A 1 612 ? 34.323 51.030  -0.052  1.00 13.80  ? 637  ALA   A C   1 
ATOM   4545 O  O   . ALA   A 1 612 ? 34.816 51.312  1.047   1.00 14.32  ? 637  ALA   A O   1 
ATOM   4546 C  CB  . ALA   A 1 612 ? 32.031 50.010  -0.134  1.00 12.85  ? 637  ALA   A CB  1 
ATOM   4547 N  N   . SER   A 1 613 ? 35.055 50.500  -1.052  1.00 13.36  ? 638  SER   A N   1 
ATOM   4548 C  CA  . SER   A 1 613 ? 36.462 50.223  -0.828  1.00 13.30  ? 638  SER   A CA  1 
ATOM   4549 C  C   . SER   A 1 613 ? 37.271 51.488  -0.573  1.00 13.28  ? 638  SER   A C   1 
ATOM   4550 O  O   . SER   A 1 613 ? 38.194 51.461  0.228   1.00 13.78  ? 638  SER   A O   1 
ATOM   4551 C  CB  . SER   A 1 613 ? 37.006 49.376  -1.973  1.00 15.25  ? 638  SER   A CB  1 
ATOM   4552 O  OG  . SER   A 1 613 ? 37.204 50.161  -3.124  1.00 18.02  ? 638  SER   A OG  1 
ATOM   4553 N  N   . LEU   A 1 614 ? 36.941 52.584  -1.266  1.00 12.45  ? 639  LEU   A N   1 
ATOM   4554 C  CA  . LEU   A 1 614 ? 37.685 53.839  -1.057  1.00 12.79  ? 639  LEU   A CA  1 
ATOM   4555 C  C   . LEU   A 1 614 ? 37.399 54.389  0.340   1.00 13.10  ? 639  LEU   A C   1 
ATOM   4556 O  O   . LEU   A 1 614 ? 38.306 54.902  0.978   1.00 13.55  ? 639  LEU   A O   1 
ATOM   4557 C  CB  . LEU   A 1 614 ? 37.263 54.858  -2.123  1.00 13.17  ? 639  LEU   A CB  1 
ATOM   4558 C  CG  . LEU   A 1 614 ? 37.732 54.433  -3.555  1.00 14.57  ? 639  LEU   A CG  1 
ATOM   4559 C  CD1 . LEU   A 1 614 ? 37.102 55.363  -4.586  1.00 15.40  ? 639  LEU   A CD1 1 
ATOM   4560 C  CD2 . LEU   A 1 614 ? 39.260 54.546  -3.623  1.00 14.73  ? 639  LEU   A CD2 1 
ATOM   4561 N  N   . ILE   A 1 615 ? 36.126 54.302  0.812   1.00 12.87  ? 640  ILE   A N   1 
ATOM   4562 C  CA  . ILE   A 1 615 ? 35.806 54.796  2.157   1.00 12.81  ? 640  ILE   A CA  1 
ATOM   4563 C  C   . ILE   A 1 615 ? 36.607 53.984  3.189   1.00 14.11  ? 640  ILE   A C   1 
ATOM   4564 O  O   . ILE   A 1 615 ? 37.309 54.549  4.055   1.00 14.02  ? 640  ILE   A O   1 
ATOM   4565 C  CB  . ILE   A 1 615 ? 34.282 54.567  2.401   1.00 13.88  ? 640  ILE   A CB  1 
ATOM   4566 C  CG1 . ILE   A 1 615 ? 33.451 55.503  1.519   1.00 14.89  ? 640  ILE   A CG1 1 
ATOM   4567 C  CG2 . ILE   A 1 615 ? 33.974 54.803  3.913   1.00 15.04  ? 640  ILE   A CG2 1 
ATOM   4568 C  CD1 . ILE   A 1 615 ? 31.992 55.035  1.444   1.00 15.96  ? 640  ILE   A CD1 1 
ATOM   4569 N  N   . ASN   A 1 616 ? 36.569 52.641  3.067   1.00 13.44  ? 641  ASN   A N   1 
ATOM   4570 C  CA  . ASN   A 1 616 ? 37.295 51.823  4.027   1.00 13.89  ? 641  ASN   A CA  1 
ATOM   4571 C  C   . ASN   A 1 616 ? 38.801 52.111  3.997   1.00 14.12  ? 641  ASN   A C   1 
ATOM   4572 O  O   . ASN   A 1 616 ? 39.414 52.329  5.029   1.00 14.13  ? 641  ASN   A O   1 
ATOM   4573 C  CB  . ASN   A 1 616 ? 37.066 50.328  3.765   1.00 14.30  ? 641  ASN   A CB  1 
ATOM   4574 C  CG  . ASN   A 1 616 ? 38.019 49.448  4.544   1.00 16.36  ? 641  ASN   A CG  1 
ATOM   4575 O  OD1 . ASN   A 1 616 ? 39.167 49.257  4.133   1.00 16.53  ? 641  ASN   A OD1 1 
ATOM   4576 N  ND2 . ASN   A 1 616 ? 37.619 48.999  5.718   1.00 18.51  ? 641  ASN   A ND2 1 
ATOM   4577 N  N   . ASN   A 1 617 ? 39.362 52.150  2.777   1.00 13.17  ? 642  ASN   A N   1 
ATOM   4578 C  CA  . ASN   A 1 617 ? 40.802 52.288  2.702   1.00 13.59  ? 642  ASN   A CA  1 
ATOM   4579 C  C   . ASN   A 1 617 ? 41.261 53.635  3.173   1.00 13.73  ? 642  ASN   A C   1 
ATOM   4580 O  O   . ASN   A 1 617 ? 42.279 53.718  3.833   1.00 14.03  ? 642  ASN   A O   1 
ATOM   4581 C  CB  . ASN   A 1 617 ? 41.300 52.017  1.294   1.00 13.95  ? 642  ASN   A CB  1 
ATOM   4582 C  CG  . ASN   A 1 617 ? 41.277 50.561  0.878   1.00 15.00  ? 642  ASN   A CG  1 
ATOM   4583 O  OD1 . ASN   A 1 617 ? 41.860 50.257  -0.204  1.00 14.62  ? 642  ASN   A OD1 1 
ATOM   4584 N  ND2 . ASN   A 1 617 ? 40.664 49.626  1.614   1.00 14.70  ? 642  ASN   A ND2 1 
ATOM   4585 N  N   . ALA   A 1 618 ? 40.497 54.706  2.900   1.00 14.05  ? 643  ALA   A N   1 
ATOM   4586 C  CA  . ALA   A 1 618 ? 40.914 56.029  3.351   1.00 14.09  ? 643  ALA   A CA  1 
ATOM   4587 C  C   . ALA   A 1 618 ? 41.045 56.047  4.889   1.00 14.84  ? 643  ALA   A C   1 
ATOM   4588 O  O   . ALA   A 1 618 ? 42.055 56.540  5.420   1.00 14.40  ? 643  ALA   A O   1 
ATOM   4589 C  CB  . ALA   A 1 618 ? 39.885 57.078  2.900   1.00 14.70  ? 643  ALA   A CB  1 
ATOM   4590 N  N   . PHE   A 1 619 ? 40.057 55.486  5.593   1.00 14.84  ? 644  PHE   A N   1 
ATOM   4591 C  CA  . PHE   A 1 619 ? 40.132 55.497  7.060   1.00 15.26  ? 644  PHE   A CA  1 
ATOM   4592 C  C   . PHE   A 1 619 ? 41.196 54.547  7.577   1.00 15.75  ? 644  PHE   A C   1 
ATOM   4593 O  O   . PHE   A 1 619 ? 41.843 54.857  8.600   1.00 17.08  ? 644  PHE   A O   1 
ATOM   4594 C  CB  . PHE   A 1 619 ? 38.734 55.249  7.644   1.00 14.54  ? 644  PHE   A CB  1 
ATOM   4595 C  CG  . PHE   A 1 619 ? 37.859 56.484  7.509   1.00 14.76  ? 644  PHE   A CG  1 
ATOM   4596 C  CD1 . PHE   A 1 619 ? 37.949 57.517  8.418   1.00 15.50  ? 644  PHE   A CD1 1 
ATOM   4597 C  CD2 . PHE   A 1 619 ? 36.971 56.607  6.478   1.00 15.32  ? 644  PHE   A CD2 1 
ATOM   4598 C  CE1 . PHE   A 1 619 ? 37.189 58.674  8.271   1.00 15.45  ? 644  PHE   A CE1 1 
ATOM   4599 C  CE2 . PHE   A 1 619 ? 36.165 57.742  6.342   1.00 14.86  ? 644  PHE   A CE2 1 
ATOM   4600 C  CZ  . PHE   A 1 619 ? 36.290 58.794  7.232   1.00 14.50  ? 644  PHE   A CZ  1 
ATOM   4601 N  N   A GLN   A 1 620 ? 41.414 53.393  6.912   0.50 14.71  ? 645  GLN   A N   1 
ATOM   4602 N  N   B GLN   A 1 620 ? 41.421 53.439  6.915   0.50 14.38  ? 645  GLN   A N   1 
ATOM   4603 C  CA  A GLN   A 1 620 ? 42.503 52.462  7.316   0.50 14.80  ? 645  GLN   A CA  1 
ATOM   4604 C  CA  B GLN   A 1 620 ? 42.508 52.539  7.329   0.50 14.27  ? 645  GLN   A CA  1 
ATOM   4605 C  C   A GLN   A 1 620 ? 43.865 53.176  7.184   0.50 15.00  ? 645  GLN   A C   1 
ATOM   4606 C  C   B GLN   A 1 620 ? 43.878 53.175  7.166   0.50 14.79  ? 645  GLN   A C   1 
ATOM   4607 O  O   A GLN   A 1 620 ? 44.793 52.896  7.938   0.50 15.98  ? 645  GLN   A O   1 
ATOM   4608 O  O   B GLN   A 1 620 ? 44.810 52.871  7.907   0.50 15.77  ? 645  GLN   A O   1 
ATOM   4609 C  CB  A GLN   A 1 620 ? 42.567 51.134  6.482   0.50 16.33  ? 645  GLN   A CB  1 
ATOM   4610 C  CB  B GLN   A 1 620 ? 42.410 51.210  6.624   0.50 15.30  ? 645  GLN   A CB  1 
ATOM   4611 C  CG  A GLN   A 1 620 ? 41.450 50.054  6.682   0.50 16.94  ? 645  GLN   A CG  1 
ATOM   4612 C  CG  B GLN   A 1 620 ? 41.165 50.471  7.065   0.50 16.20  ? 645  GLN   A CG  1 
ATOM   4613 C  CD  A GLN   A 1 620 ? 41.866 48.597  6.410   0.50 18.39  ? 645  GLN   A CD  1 
ATOM   4614 C  CD  B GLN   A 1 620 ? 41.441 49.814  8.376   0.50 17.70  ? 645  GLN   A CD  1 
ATOM   4615 O  OE1 A GLN   A 1 620 ? 42.895 48.135  6.933   0.50 20.08  ? 645  GLN   A OE1 1 
ATOM   4616 O  OE1 B GLN   A 1 620 ? 41.418 50.456  9.431   0.50 15.86  ? 645  GLN   A OE1 1 
ATOM   4617 N  NE2 A GLN   A 1 620 ? 41.042 47.789  5.669   0.50 15.38  ? 645  GLN   A NE2 1 
ATOM   4618 N  NE2 B GLN   A 1 620 ? 41.702 48.520  8.339   0.50 18.84  ? 645  GLN   A NE2 1 
ATOM   4619 N  N   . LEU   A 1 621 ? 44.013 54.061  6.176   1.00 14.90  ? 646  LEU   A N   1 
ATOM   4620 C  CA  . LEU   A 1 621 ? 45.288 54.768  5.977   1.00 14.77  ? 646  LEU   A CA  1 
ATOM   4621 C  C   . LEU   A 1 621 ? 45.540 55.840  7.017   1.00 16.29  ? 646  LEU   A C   1 
ATOM   4622 O  O   . LEU   A 1 621 ? 46.681 56.136  7.294   1.00 15.92  ? 646  LEU   A O   1 
ATOM   4623 C  CB  . LEU   A 1 621 ? 45.319 55.367  4.574   1.00 14.33  ? 646  LEU   A CB  1 
ATOM   4624 C  CG  . LEU   A 1 621 ? 45.382 54.250  3.520   1.00 15.62  ? 646  LEU   A CG  1 
ATOM   4625 C  CD1 . LEU   A 1 621 ? 45.124 54.833  2.119   1.00 17.45  ? 646  LEU   A CD1 1 
ATOM   4626 C  CD2 . LEU   A 1 621 ? 46.725 53.493  3.566   1.00 16.24  ? 646  LEU   A CD2 1 
ATOM   4627 N  N   . VAL   A 1 622 ? 44.469 56.361  7.661   1.00 16.97  ? 647  VAL   A N   1 
ATOM   4628 C  CA  . VAL   A 1 622 ? 44.666 57.299  8.778   1.00 16.83  ? 647  VAL   A CA  1 
ATOM   4629 C  C   . VAL   A 1 622 ? 45.377 56.566  9.907   1.00 17.67  ? 647  VAL   A C   1 
ATOM   4630 O  O   . VAL   A 1 622 ? 46.332 57.087  10.477  1.00 17.86  ? 647  VAL   A O   1 
ATOM   4631 C  CB  . VAL   A 1 622 ? 43.278 57.775  9.272   1.00 17.52  ? 647  VAL   A CB  1 
ATOM   4632 C  CG1 . VAL   A 1 622 ? 43.406 58.561  10.585  1.00 19.15  ? 647  VAL   A CG1 1 
ATOM   4633 C  CG2 . VAL   A 1 622 ? 42.590 58.588  8.213   1.00 18.11  ? 647  VAL   A CG2 1 
ATOM   4634 N  N   . SER   A 1 623 ? 44.967 55.310  10.140  1.00 18.31  ? 648  SER   A N   1 
ATOM   4635 C  CA  . SER   A 1 623 ? 45.488 54.521  11.222  1.00 20.11  ? 648  SER   A CA  1 
ATOM   4636 C  C   . SER   A 1 623 ? 47.005 54.349  11.144  1.00 22.30  ? 648  SER   A C   1 
ATOM   4637 O  O   . SER   A 1 623 ? 47.660 54.272  12.175  1.00 24.67  ? 648  SER   A O   1 
ATOM   4638 C  CB  . SER   A 1 623 ? 44.754 53.188  11.300  1.00 22.48  ? 648  SER   A CB  1 
ATOM   4639 O  OG  . SER   A 1 623 ? 43.350 53.441  11.239  1.00 23.95  ? 648  SER   A OG  1 
ATOM   4640 N  N   . ILE   A 1 624 ? 47.593 54.307  9.918   1.00 19.41  ? 649  ILE   A N   1 
ATOM   4641 C  CA  . ILE   A 1 624 ? 49.041 54.137  9.749   1.00 20.07  ? 649  ILE   A CA  1 
ATOM   4642 C  C   . ILE   A 1 624 ? 49.767 55.397  9.252   1.00 21.24  ? 649  ILE   A C   1 
ATOM   4643 O  O   . ILE   A 1 624 ? 50.907 55.314  8.802   1.00 23.29  ? 649  ILE   A O   1 
ATOM   4644 C  CB  . ILE   A 1 624 ? 49.355 52.915  8.853   1.00 20.44  ? 649  ILE   A CB  1 
ATOM   4645 C  CG1 . ILE   A 1 624 ? 48.788 53.149  7.439   1.00 19.68  ? 649  ILE   A CG1 1 
ATOM   4646 C  CG2 . ILE   A 1 624 ? 48.822 51.619  9.483   1.00 21.04  ? 649  ILE   A CG2 1 
ATOM   4647 C  CD1 . ILE   A 1 624 ? 49.436 52.146  6.365   1.00 20.03  ? 649  ILE   A CD1 1 
ATOM   4648 N  N   . GLY   A 1 625 ? 49.123 56.550  9.359   1.00 21.13  ? 650  GLY   A N   1 
ATOM   4649 C  CA  . GLY   A 1 625 ? 49.731 57.839  9.068   1.00 20.35  ? 650  GLY   A CA  1 
ATOM   4650 C  C   . GLY   A 1 625 ? 49.980 58.126  7.606   1.00 20.84  ? 650  GLY   A C   1 
ATOM   4651 O  O   . GLY   A 1 625 ? 50.751 59.031  7.269   1.00 23.00  ? 650  GLY   A O   1 
ATOM   4652 N  N   . LYS   A 1 626 ? 49.272 57.414  6.709   1.00 18.52  ? 651  LYS   A N   1 
ATOM   4653 C  CA  . LYS   A 1 626 ? 49.427 57.664  5.261   1.00 17.90  ? 651  LYS   A CA  1 
ATOM   4654 C  C   . LYS   A 1 626 ? 48.459 58.695  4.707   1.00 18.21  ? 651  LYS   A C   1 
ATOM   4655 O  O   . LYS   A 1 626 ? 48.671 59.199  3.586   1.00 19.19  ? 651  LYS   A O   1 
ATOM   4656 C  CB  . LYS   A 1 626 ? 49.249 56.363  4.455   1.00 18.17  ? 651  LYS   A CB  1 
ATOM   4657 C  CG  . LYS   A 1 626 ? 50.372 55.339  4.637   1.00 21.21  ? 651  LYS   A CG  1 
ATOM   4658 C  CD  . LYS   A 1 626 ? 51.630 55.823  3.940   1.00 24.72  ? 651  LYS   A CD  1 
ATOM   4659 C  CE  . LYS   A 1 626 ? 52.684 54.751  4.037   1.00 26.46  ? 651  LYS   A CE  1 
ATOM   4660 N  NZ  . LYS   A 1 626 ? 53.937 55.197  3.336   1.00 27.12  ? 651  LYS   A NZ  1 
ATOM   4661 N  N   . LEU   A 1 627 ? 47.342 58.933  5.418   1.00 16.83  ? 652  LEU   A N   1 
ATOM   4662 C  CA  . LEU   A 1 627 ? 46.343 59.924  5.013   1.00 16.58  ? 652  LEU   A CA  1 
ATOM   4663 C  C   . LEU   A 1 627 ? 45.881 60.597  6.312   1.00 16.92  ? 652  LEU   A C   1 
ATOM   4664 O  O   . LEU   A 1 627 ? 45.741 59.907  7.322   1.00 18.91  ? 652  LEU   A O   1 
ATOM   4665 C  CB  . LEU   A 1 627 ? 45.155 59.221  4.323   1.00 17.30  ? 652  LEU   A CB  1 
ATOM   4666 C  CG  . LEU   A 1 627 ? 44.120 60.144  3.684   1.00 18.32  ? 652  LEU   A CG  1 
ATOM   4667 C  CD1 . LEU   A 1 627 ? 44.762 60.984  2.518   1.00 19.17  ? 652  LEU   A CD1 1 
ATOM   4668 C  CD2 . LEU   A 1 627 ? 42.930 59.359  3.132   1.00 18.74  ? 652  LEU   A CD2 1 
ATOM   4669 N  N   . SER   A 1 628 ? 45.626 61.893  6.294   1.00 16.13  ? 653  SER   A N   1 
ATOM   4670 C  CA  . SER   A 1 628 ? 45.176 62.556  7.534   1.00 16.52  ? 653  SER   A CA  1 
ATOM   4671 C  C   . SER   A 1 628 ? 43.714 62.241  7.791   1.00 16.54  ? 653  SER   A C   1 
ATOM   4672 O  O   . SER   A 1 628 ? 42.940 61.971  6.868   1.00 16.16  ? 653  SER   A O   1 
ATOM   4673 C  CB  . SER   A 1 628 ? 45.347 64.061  7.422   1.00 18.90  ? 653  SER   A CB  1 
ATOM   4674 O  OG  . SER   A 1 628 ? 44.465 64.585  6.445   1.00 20.86  ? 653  SER   A OG  1 
ATOM   4675 N  N   . ILE   A 1 629 ? 43.321 62.338  9.075   1.00 15.86  ? 654  ILE   A N   1 
ATOM   4676 C  CA  . ILE   A 1 629 ? 41.901 62.141  9.406   1.00 15.88  ? 654  ILE   A CA  1 
ATOM   4677 C  C   . ILE   A 1 629 ? 41.026 63.179  8.717   1.00 16.58  ? 654  ILE   A C   1 
ATOM   4678 O  O   . ILE   A 1 629 ? 39.925 62.876  8.284   1.00 16.14  ? 654  ILE   A O   1 
ATOM   4679 C  CB  . ILE   A 1 629 ? 41.730 62.109  10.953  1.00 16.22  ? 654  ILE   A CB  1 
ATOM   4680 C  CG1 . ILE   A 1 629 ? 40.274 61.817  11.353  1.00 17.30  ? 654  ILE   A CG1 1 
ATOM   4681 C  CG2 . ILE   A 1 629 ? 42.124 63.466  11.556  1.00 17.41  ? 654  ILE   A CG2 1 
ATOM   4682 C  CD1 . ILE   A 1 629 ? 39.682 60.478  10.880  1.00 18.40  ? 654  ILE   A CD1 1 
ATOM   4683 N  N   . GLU   A 1 630 ? 41.574 64.408  8.484   1.00 16.25  ? 655  GLU   A N   1 
ATOM   4684 C  CA  . GLU   A 1 630 ? 40.792 65.458  7.831   1.00 16.05  ? 655  GLU   A CA  1 
ATOM   4685 C  C   . GLU   A 1 630 ? 40.505 65.067  6.402   1.00 16.33  ? 655  GLU   A C   1 
ATOM   4686 O  O   . GLU   A 1 630 ? 39.393 65.252  5.940   1.00 17.22  ? 655  GLU   A O   1 
ATOM   4687 C  CB  . GLU   A 1 630 ? 41.531 66.813  7.880   1.00 17.86  ? 655  GLU   A CB  1 
ATOM   4688 C  CG  . GLU   A 1 630 ? 41.669 67.349  9.297   1.00 18.72  ? 655  GLU   A CG  1 
ATOM   4689 C  CD  . GLU   A 1 630 ? 43.006 67.042  9.950   1.00 19.01  ? 655  GLU   A CD  1 
ATOM   4690 O  OE1 . GLU   A 1 630 ? 43.701 66.094  9.511   1.00 19.22  ? 655  GLU   A OE1 1 
ATOM   4691 O  OE2 . GLU   A 1 630 ? 43.358 67.722  10.942  1.00 20.60  ? 655  GLU   A OE2 1 
ATOM   4692 N  N   . LYS   A 1 631 ? 41.504 64.509  5.694   1.00 16.51  ? 656  LYS   A N   1 
ATOM   4693 C  CA  . LYS   A 1 631 ? 41.275 64.134  4.303   1.00 16.51  ? 656  LYS   A CA  1 
ATOM   4694 C  C   . LYS   A 1 631 ? 40.292 62.942  4.195   1.00 16.09  ? 656  LYS   A C   1 
ATOM   4695 O  O   . LYS   A 1 631 ? 39.510 62.862  3.233   1.00 16.16  ? 656  LYS   A O   1 
ATOM   4696 C  CB  . LYS   A 1 631 ? 42.616 63.835  3.600   1.00 17.30  ? 656  LYS   A CB  1 
ATOM   4697 C  CG  . LYS   A 1 631 ? 43.454 65.126  3.324   1.00 22.07  ? 656  LYS   A CG  1 
ATOM   4698 C  CD  . LYS   A 1 631 ? 42.769 66.060  2.399   1.00 30.11  ? 656  LYS   A CD  1 
ATOM   4699 C  CE  . LYS   A 1 631 ? 43.651 67.164  1.857   1.00 35.93  ? 656  LYS   A CE  1 
ATOM   4700 N  NZ  . LYS   A 1 631 ? 43.011 67.787  0.659   1.00 38.57  ? 656  LYS   A NZ  1 
ATOM   4701 N  N   . ALA   A 1 632 ? 40.364 61.991  5.141   1.00 14.60  ? 657  ALA   A N   1 
ATOM   4702 C  CA  . ALA   A 1 632 ? 39.416 60.862  5.101   1.00 14.68  ? 657  ALA   A CA  1 
ATOM   4703 C  C   . ALA   A 1 632 ? 37.999 61.371  5.419   1.00 14.60  ? 657  ALA   A C   1 
ATOM   4704 O  O   . ALA   A 1 632 ? 37.033 61.027  4.732   1.00 15.38  ? 657  ALA   A O   1 
ATOM   4705 C  CB  . ALA   A 1 632 ? 39.849 59.779  6.085   1.00 15.02  ? 657  ALA   A CB  1 
ATOM   4706 N  N   . LEU   A 1 633 ? 37.879 62.265  6.403   1.00 14.92  ? 658  LEU   A N   1 
ATOM   4707 C  CA  . LEU   A 1 633 ? 36.560 62.844  6.710   1.00 15.80  ? 658  LEU   A CA  1 
ATOM   4708 C  C   . LEU   A 1 633 ? 36.052 63.686  5.536   1.00 16.20  ? 658  LEU   A C   1 
ATOM   4709 O  O   . LEU   A 1 633 ? 34.880 63.604  5.175   1.00 17.34  ? 658  LEU   A O   1 
ATOM   4710 C  CB  . LEU   A 1 633 ? 36.613 63.665  7.987   1.00 15.65  ? 658  LEU   A CB  1 
ATOM   4711 C  CG  . LEU   A 1 633 ? 36.782 62.838  9.257   1.00 16.52  ? 658  LEU   A CG  1 
ATOM   4712 C  CD1 . LEU   A 1 633 ? 37.130 63.783  10.448  1.00 18.51  ? 658  LEU   A CD1 1 
ATOM   4713 C  CD2 . LEU   A 1 633 ? 35.521 62.015  9.580   1.00 17.79  ? 658  LEU   A CD2 1 
ATOM   4714 N  N   . ASP   A 1 634 ? 36.937 64.445  4.878   1.00 15.96  ? 659  ASP   A N   1 
ATOM   4715 C  CA  . ASP   A 1 634 ? 36.521 65.217  3.684   1.00 15.78  ? 659  ASP   A CA  1 
ATOM   4716 C  C   . ASP   A 1 634 ? 36.005 64.280  2.591   1.00 16.46  ? 659  ASP   A C   1 
ATOM   4717 O  O   . ASP   A 1 634 ? 35.007 64.591  1.950   1.00 18.70  ? 659  ASP   A O   1 
ATOM   4718 C  CB  . ASP   A 1 634 ? 37.708 66.001  3.105   1.00 17.56  ? 659  ASP   A CB  1 
ATOM   4719 C  CG  . ASP   A 1 634 ? 38.160 67.174  3.925   1.00 22.92  ? 659  ASP   A CG  1 
ATOM   4720 O  OD1 . ASP   A 1 634 ? 37.391 67.615  4.811   1.00 24.82  ? 659  ASP   A OD1 1 
ATOM   4721 O  OD2 . ASP   A 1 634 ? 39.255 67.691  3.642   1.00 27.75  ? 659  ASP   A OD2 1 
ATOM   4722 N  N   . LEU   A 1 635 ? 36.662 63.118  2.406   1.00 16.34  ? 660  LEU   A N   1 
ATOM   4723 C  CA  . LEU   A 1 635 ? 36.177 62.164  1.411   1.00 16.72  ? 660  LEU   A CA  1 
ATOM   4724 C  C   . LEU   A 1 635 ? 34.787 61.660  1.824   1.00 17.36  ? 660  LEU   A C   1 
ATOM   4725 O  O   . LEU   A 1 635 ? 33.901 61.573  0.975   1.00 18.19  ? 660  LEU   A O   1 
ATOM   4726 C  CB  . LEU   A 1 635 ? 37.188 61.022  1.262   1.00 16.72  ? 660  LEU   A CB  1 
ATOM   4727 C  CG  . LEU   A 1 635 ? 36.773 59.880  0.301   1.00 16.95  ? 660  LEU   A CG  1 
ATOM   4728 C  CD1 . LEU   A 1 635 ? 38.056 59.211  -0.253  1.00 18.59  ? 660  LEU   A CD1 1 
ATOM   4729 C  CD2 . LEU   A 1 635 ? 35.921 58.828  1.033   1.00 17.78  ? 660  LEU   A CD2 1 
ATOM   4730 N  N   . SER   A 1 636 ? 34.555 61.439  3.147   1.00 16.66  ? 661  SER   A N   1 
ATOM   4731 C  CA  . SER   A 1 636 ? 33.266 60.904  3.573   1.00 17.48  ? 661  SER   A CA  1 
ATOM   4732 C  C   . SER   A 1 636 ? 32.099 61.853  3.318   1.00 17.02  ? 661  SER   A C   1 
ATOM   4733 O  O   . SER   A 1 636 ? 30.944 61.396  3.217   1.00 17.48  ? 661  SER   A O   1 
ATOM   4734 C  CB  . SER   A 1 636 ? 33.309 60.517  5.052   1.00 16.96  ? 661  SER   A CB  1 
ATOM   4735 O  OG  . SER   A 1 636 ? 33.246 61.637  5.915   1.00 18.87  ? 661  SER   A OG  1 
ATOM   4736 N  N   . LEU   A 1 637 ? 32.383 63.143  3.133   1.00 16.79  ? 662  LEU   A N   1 
ATOM   4737 C  CA  . LEU   A 1 637 ? 31.315 64.119  2.833   1.00 17.13  ? 662  LEU   A CA  1 
ATOM   4738 C  C   . LEU   A 1 637 ? 30.541 63.775  1.571   1.00 16.96  ? 662  LEU   A C   1 
ATOM   4739 O  O   . LEU   A 1 637 ? 29.380 64.206  1.424   1.00 17.39  ? 662  LEU   A O   1 
ATOM   4740 C  CB  . LEU   A 1 637 ? 31.901 65.522  2.672   1.00 17.90  ? 662  LEU   A CB  1 
ATOM   4741 C  CG  . LEU   A 1 637 ? 32.471 66.109  3.941   1.00 20.51  ? 662  LEU   A CG  1 
ATOM   4742 C  CD1 . LEU   A 1 637 ? 33.042 67.500  3.706   1.00 21.51  ? 662  LEU   A CD1 1 
ATOM   4743 C  CD2 . LEU   A 1 637 ? 31.368 66.286  5.018   1.00 22.27  ? 662  LEU   A CD2 1 
ATOM   4744 N  N   . TYR   A 1 638 ? 31.135 63.001  0.636   1.00 16.15  ? 663  TYR   A N   1 
ATOM   4745 C  CA  . TYR   A 1 638 ? 30.410 62.653  -0.586  1.00 16.57  ? 663  TYR   A CA  1 
ATOM   4746 C  C   . TYR   A 1 638 ? 29.151 61.831  -0.240  1.00 16.71  ? 663  TYR   A C   1 
ATOM   4747 O  O   . TYR   A 1 638 ? 28.224 61.760  -1.022  1.00 17.86  ? 663  TYR   A O   1 
ATOM   4748 C  CB  . TYR   A 1 638 ? 31.318 61.893  -1.613  1.00 16.16  ? 663  TYR   A CB  1 
ATOM   4749 C  CG  . TYR   A 1 638 ? 31.092 60.391  -1.625  1.00 15.10  ? 663  TYR   A CG  1 
ATOM   4750 C  CD1 . TYR   A 1 638 ? 30.133 59.816  -2.455  1.00 16.03  ? 663  TYR   A CD1 1 
ATOM   4751 C  CD2 . TYR   A 1 638 ? 31.788 59.556  -0.756  1.00 15.10  ? 663  TYR   A CD2 1 
ATOM   4752 C  CE1 . TYR   A 1 638 ? 29.838 58.462  -2.376  1.00 16.43  ? 663  TYR   A CE1 1 
ATOM   4753 C  CE2 . TYR   A 1 638 ? 31.529 58.188  -0.702  1.00 14.79  ? 663  TYR   A CE2 1 
ATOM   4754 C  CZ  . TYR   A 1 638 ? 30.534 57.650  -1.498  1.00 15.55  ? 663  TYR   A CZ  1 
ATOM   4755 O  OH  . TYR   A 1 638 ? 30.223 56.323  -1.378  1.00 15.30  ? 663  TYR   A OH  1 
ATOM   4756 N  N   . LEU   A 1 639 ? 29.143 61.149  0.918   1.00 15.54  ? 664  LEU   A N   1 
ATOM   4757 C  CA  . LEU   A 1 639 ? 28.025 60.289  1.296   1.00 15.19  ? 664  LEU   A CA  1 
ATOM   4758 C  C   . LEU   A 1 639 ? 26.700 61.040  1.394   1.00 15.72  ? 664  LEU   A C   1 
ATOM   4759 O  O   . LEU   A 1 639 ? 25.660 60.371  1.302   1.00 16.58  ? 664  LEU   A O   1 
ATOM   4760 C  CB  . LEU   A 1 639 ? 28.297 59.570  2.613   1.00 14.76  ? 664  LEU   A CB  1 
ATOM   4761 C  CG  . LEU   A 1 639 ? 29.347 58.464  2.535   1.00 14.97  ? 664  LEU   A CG  1 
ATOM   4762 C  CD1 . LEU   A 1 639 ? 29.791 58.043  3.968   1.00 15.67  ? 664  LEU   A CD1 1 
ATOM   4763 C  CD2 . LEU   A 1 639 ? 28.778 57.252  1.784   1.00 15.92  ? 664  LEU   A CD2 1 
ATOM   4764 N  N   . LYS   A 1 640 ? 26.713 62.392  1.419   1.00 15.94  ? 665  LYS   A N   1 
ATOM   4765 C  CA  . LYS   A 1 640 ? 25.431 63.108  1.396   1.00 17.92  ? 665  LYS   A CA  1 
ATOM   4766 C  C   . LYS   A 1 640 ? 24.617 62.781  0.125   1.00 20.25  ? 665  LYS   A C   1 
ATOM   4767 O  O   . LYS   A 1 640 ? 23.397 62.871  0.152   1.00 22.36  ? 665  LYS   A O   1 
ATOM   4768 C  CB  . LYS   A 1 640 ? 25.656 64.612  1.532   1.00 22.15  ? 665  LYS   A CB  1 
ATOM   4769 C  CG  . LYS   A 1 640 ? 26.532 65.259  0.509   1.00 31.57  ? 665  LYS   A CG  1 
ATOM   4770 C  CD  . LYS   A 1 640 ? 26.347 66.777  0.593   1.00 40.14  ? 665  LYS   A CD  1 
ATOM   4771 C  CE  . LYS   A 1 640 ? 27.412 67.551  -0.145  1.00 45.89  ? 665  LYS   A CE  1 
ATOM   4772 N  NZ  . LYS   A 1 640 ? 27.064 69.000  -0.231  1.00 49.32  ? 665  LYS   A NZ  1 
ATOM   4773 N  N   . HIS   A 1 641 ? 25.277 62.307  -0.942  1.00 18.65  ? 666  HIS   A N   1 
ATOM   4774 C  CA  . HIS   A 1 641 ? 24.579 61.959  -2.183  1.00 20.37  ? 666  HIS   A CA  1 
ATOM   4775 C  C   . HIS   A 1 641 ? 24.617 60.469  -2.502  1.00 19.78  ? 666  HIS   A C   1 
ATOM   4776 O  O   . HIS   A 1 641 ? 24.206 60.054  -3.598  1.00 20.87  ? 666  HIS   A O   1 
ATOM   4777 C  CB  . HIS   A 1 641 ? 25.152 62.793  -3.351  1.00 24.37  ? 666  HIS   A CB  1 
ATOM   4778 C  CG  . HIS   A 1 641 ? 24.975 64.262  -3.144  1.00 31.75  ? 666  HIS   A CG  1 
ATOM   4779 N  ND1 . HIS   A 1 641 ? 26.062 65.111  -3.005  1.00 36.07  ? 666  HIS   A ND1 1 
ATOM   4780 C  CD2 . HIS   A 1 641 ? 23.839 64.979  -2.978  1.00 34.99  ? 666  HIS   A CD2 1 
ATOM   4781 C  CE1 . HIS   A 1 641 ? 25.557 66.322  -2.819  1.00 36.82  ? 666  HIS   A CE1 1 
ATOM   4782 N  NE2 . HIS   A 1 641 ? 24.226 66.296  -2.775  1.00 36.72  ? 666  HIS   A NE2 1 
ATOM   4783 N  N   . GLU   A 1 642 ? 25.078 59.640  -1.535  1.00 17.58  ? 667  GLU   A N   1 
ATOM   4784 C  CA  . GLU   A 1 642 ? 25.127 58.230  -1.747  1.00 17.16  ? 667  GLU   A CA  1 
ATOM   4785 C  C   . GLU   A 1 642 ? 23.760 57.613  -1.533  1.00 18.06  ? 667  GLU   A C   1 
ATOM   4786 O  O   . GLU   A 1 642 ? 23.000 58.045  -0.626  1.00 19.44  ? 667  GLU   A O   1 
ATOM   4787 C  CB  . GLU   A 1 642 ? 26.146 57.599  -0.778  1.00 16.83  ? 667  GLU   A CB  1 
ATOM   4788 C  CG  . GLU   A 1 642 ? 26.326 56.095  -0.943  1.00 15.65  ? 667  GLU   A CG  1 
ATOM   4789 C  CD  . GLU   A 1 642 ? 26.764 55.693  -2.349  1.00 16.38  ? 667  GLU   A CD  1 
ATOM   4790 O  OE1 . GLU   A 1 642 ? 27.967 55.868  -2.676  1.00 15.86  ? 667  GLU   A OE1 1 
ATOM   4791 O  OE2 . GLU   A 1 642 ? 25.909 55.203  -3.126  1.00 15.98  ? 667  GLU   A OE2 1 
ATOM   4792 N  N   . THR   A 1 643 ? 23.433 56.621  -2.351  1.00 17.65  ? 668  THR   A N   1 
ATOM   4793 C  CA  . THR   A 1 643 ? 22.152 55.936  -2.282  1.00 17.24  ? 668  THR   A CA  1 
ATOM   4794 C  C   . THR   A 1 643 ? 22.282 54.456  -1.979  1.00 16.92  ? 668  THR   A C   1 
ATOM   4795 O  O   . THR   A 1 643 ? 21.267 53.850  -1.636  1.00 17.06  ? 668  THR   A O   1 
ATOM   4796 C  CB  . THR   A 1 643 ? 21.478 56.064  -3.670  1.00 19.94  ? 668  THR   A CB  1 
ATOM   4797 O  OG1 . THR   A 1 643 ? 22.345 55.471  -4.658  1.00 20.16  ? 668  THR   A OG1 1 
ATOM   4798 C  CG2 . THR   A 1 643 ? 21.157 57.522  -4.008  1.00 21.87  ? 668  THR   A CG2 1 
ATOM   4799 N  N   . GLU   A 1 644 ? 23.473 53.834  -2.176  1.00 15.87  ? 669  GLU   A N   1 
ATOM   4800 C  CA  . GLU   A 1 644 ? 23.575 52.408  -2.151  1.00 15.50  ? 669  GLU   A CA  1 
ATOM   4801 C  C   . GLU   A 1 644 ? 23.997 51.832  -0.814  1.00 15.87  ? 669  GLU   A C   1 
ATOM   4802 O  O   . GLU   A 1 644 ? 24.841 52.407  -0.096  1.00 15.41  ? 669  GLU   A O   1 
ATOM   4803 C  CB  . GLU   A 1 644 ? 24.515 51.945  -3.273  1.00 17.64  ? 669  GLU   A CB  1 
ATOM   4804 C  CG  . GLU   A 1 644 ? 24.060 52.472  -4.639  1.00 18.02  ? 669  GLU   A CG  1 
ATOM   4805 C  CD  . GLU   A 1 644 ? 22.633 52.083  -5.023  1.00 22.38  ? 669  GLU   A CD  1 
ATOM   4806 O  OE1 . GLU   A 1 644 ? 22.370 50.876  -5.229  1.00 23.95  ? 669  GLU   A OE1 1 
ATOM   4807 O  OE2 . GLU   A 1 644 ? 21.784 52.999  -5.113  1.00 23.79  ? 669  GLU   A OE2 1 
ATOM   4808 N  N   . ILE   A 1 645 ? 23.429 50.699  -0.485  1.00 14.90  ? 670  ILE   A N   1 
ATOM   4809 C  CA  . ILE   A 1 645 ? 23.636 50.107  0.831   1.00 15.11  ? 670  ILE   A CA  1 
ATOM   4810 C  C   . ILE   A 1 645 ? 25.097 49.869  1.182   1.00 15.46  ? 670  ILE   A C   1 
ATOM   4811 O  O   . ILE   A 1 645 ? 25.500 50.172  2.311   1.00 15.18  ? 670  ILE   A O   1 
ATOM   4812 C  CB  . ILE   A 1 645 ? 22.794 48.847  1.015   1.00 15.40  ? 670  ILE   A CB  1 
ATOM   4813 C  CG1 . ILE   A 1 645 ? 22.815 48.365  2.449   1.00 15.96  ? 670  ILE   A CG1 1 
ATOM   4814 C  CG2 . ILE   A 1 645 ? 23.209 47.731  0.027   1.00 16.71  ? 670  ILE   A CG2 1 
ATOM   4815 C  CD1 . ILE   A 1 645 ? 21.810 47.111  2.663   1.00 16.37  ? 670  ILE   A CD1 1 
ATOM   4816 N  N   . MET   A 1 646 ? 25.898 49.290  0.264   1.00 15.29  ? 671  MET   A N   1 
ATOM   4817 C  CA  . MET   A 1 646 ? 27.271 48.950  0.656   1.00 14.08  ? 671  MET   A CA  1 
ATOM   4818 C  C   . MET   A 1 646 ? 28.118 50.174  1.023   1.00 13.36  ? 671  MET   A C   1 
ATOM   4819 O  O   . MET   A 1 646 ? 28.693 50.156  2.112   1.00 13.73  ? 671  MET   A O   1 
ATOM   4820 C  CB  . MET   A 1 646 ? 27.950 48.019  -0.343  1.00 15.22  ? 671  MET   A CB  1 
ATOM   4821 C  CG  . MET   A 1 646 ? 27.346 46.640  -0.272  1.00 19.23  ? 671  MET   A CG  1 
ATOM   4822 S  SD  . MET   A 1 646 ? 27.614 45.807  1.354   1.00 20.94  ? 671  MET   A SD  1 
ATOM   4823 C  CE  . MET   A 1 646 ? 26.065 46.119  2.250   1.00 22.78  ? 671  MET   A CE  1 
ATOM   4824 N  N   . PRO   A 1 647 ? 28.199 51.218  0.203   1.00 13.47  ? 672  PRO   A N   1 
ATOM   4825 C  CA  . PRO   A 1 647 ? 29.001 52.383  0.622   1.00 12.65  ? 672  PRO   A CA  1 
ATOM   4826 C  C   . PRO   A 1 647 ? 28.382 53.092  1.836   1.00 13.19  ? 672  PRO   A C   1 
ATOM   4827 O  O   . PRO   A 1 647 ? 29.133 53.592  2.669   1.00 13.88  ? 672  PRO   A O   1 
ATOM   4828 C  CB  . PRO   A 1 647 ? 29.122 53.227  -0.648  1.00 13.94  ? 672  PRO   A CB  1 
ATOM   4829 C  CG  . PRO   A 1 647 ? 27.900 52.774  -1.505  1.00 14.61  ? 672  PRO   A CG  1 
ATOM   4830 C  CD  . PRO   A 1 647 ? 27.793 51.302  -1.220  1.00 13.72  ? 672  PRO   A CD  1 
ATOM   4831 N  N   . VAL   A 1 648 ? 27.005 53.134  1.960   1.00 13.36  ? 673  VAL   A N   1 
ATOM   4832 C  CA  . VAL   A 1 648 ? 26.460 53.776  3.177   1.00 12.81  ? 673  VAL   A CA  1 
ATOM   4833 C  C   . VAL   A 1 648 ? 26.893 52.980  4.402   1.00 13.07  ? 673  VAL   A C   1 
ATOM   4834 O  O   . VAL   A 1 648 ? 27.387 53.561  5.390   1.00 13.90  ? 673  VAL   A O   1 
ATOM   4835 C  CB  . VAL   A 1 648 ? 24.927 53.873  3.109   1.00 14.20  ? 673  VAL   A CB  1 
ATOM   4836 C  CG1 . VAL   A 1 648 ? 24.367 54.334  4.465   1.00 14.93  ? 673  VAL   A CG1 1 
ATOM   4837 C  CG2 . VAL   A 1 648 ? 24.536 54.872  2.034   1.00 15.73  ? 673  VAL   A CG2 1 
ATOM   4838 N  N   . PHE   A 1 649 ? 26.744 51.645  4.337   1.00 13.21  ? 674  PHE   A N   1 
ATOM   4839 C  CA  . PHE   A 1 649 ? 27.132 50.819  5.473   1.00 12.81  ? 674  PHE   A CA  1 
ATOM   4840 C  C   . PHE   A 1 649 ? 28.608 50.913  5.742   1.00 13.98  ? 674  PHE   A C   1 
ATOM   4841 O  O   . PHE   A 1 649 ? 29.014 50.836  6.900   1.00 14.20  ? 674  PHE   A O   1 
ATOM   4842 C  CB  . PHE   A 1 649 ? 26.690 49.359  5.280   1.00 13.24  ? 674  PHE   A CB  1 
ATOM   4843 C  CG  . PHE   A 1 649 ? 25.224 49.060  5.578   1.00 14.06  ? 674  PHE   A CG  1 
ATOM   4844 C  CD1 . PHE   A 1 649 ? 24.307 50.077  5.711   1.00 14.63  ? 674  PHE   A CD1 1 
ATOM   4845 C  CD2 . PHE   A 1 649 ? 24.779 47.750  5.656   1.00 14.72  ? 674  PHE   A CD2 1 
ATOM   4846 C  CE1 . PHE   A 1 649 ? 22.968 49.795  5.995   1.00 15.42  ? 674  PHE   A CE1 1 
ATOM   4847 C  CE2 . PHE   A 1 649 ? 23.464 47.467  5.967   1.00 15.71  ? 674  PHE   A CE2 1 
ATOM   4848 C  CZ  . PHE   A 1 649 ? 22.565 48.499  6.125   1.00 14.83  ? 674  PHE   A CZ  1 
ATOM   4849 N  N   . GLN   A 1 650 ? 29.442 51.033  4.688   1.00 13.48  ? 675  GLN   A N   1 
ATOM   4850 C  CA  . GLN   A 1 650 ? 30.870 51.196  4.950   1.00 13.52  ? 675  GLN   A CA  1 
ATOM   4851 C  C   . GLN   A 1 650 ? 31.151 52.509  5.650   1.00 13.75  ? 675  GLN   A C   1 
ATOM   4852 O  O   . GLN   A 1 650 ? 32.020 52.557  6.533   1.00 14.22  ? 675  GLN   A O   1 
ATOM   4853 C  CB  . GLN   A 1 650 ? 31.698 51.083  3.653   1.00 14.70  ? 675  GLN   A CB  1 
ATOM   4854 C  CG  . GLN   A 1 650 ? 33.184 50.815  3.924   1.00 16.34  ? 675  GLN   A CG  1 
ATOM   4855 C  CD  . GLN   A 1 650 ? 33.315 49.490  4.609   1.00 19.38  ? 675  GLN   A CD  1 
ATOM   4856 O  OE1 . GLN   A 1 650 ? 32.711 48.499  4.167   1.00 22.73  ? 675  GLN   A OE1 1 
ATOM   4857 N  NE2 . GLN   A 1 650 ? 34.070 49.427  5.700   1.00 18.40  ? 675  GLN   A NE2 1 
ATOM   4858 N  N   . GLY   A 1 651 ? 30.401 53.554  5.307   1.00 13.53  ? 676  GLY   A N   1 
ATOM   4859 C  CA  . GLY   A 1 651 ? 30.561 54.823  6.014   1.00 13.69  ? 676  GLY   A CA  1 
ATOM   4860 C  C   . GLY   A 1 651 ? 30.195 54.668  7.483   1.00 14.14  ? 676  GLY   A C   1 
ATOM   4861 O  O   . GLY   A 1 651 ? 30.910 55.162  8.349   1.00 14.15  ? 676  GLY   A O   1 
ATOM   4862 N  N   . LEU   A 1 652 ? 29.115 53.926  7.761   1.00 12.93  ? 677  LEU   A N   1 
ATOM   4863 C  CA  . LEU   A 1 652 ? 28.741 53.675  9.167   1.00 12.82  ? 677  LEU   A CA  1 
ATOM   4864 C  C   . LEU   A 1 652 ? 29.853 52.858  9.845   1.00 13.71  ? 677  LEU   A C   1 
ATOM   4865 O  O   . LEU   A 1 652 ? 30.203 53.114  11.014  1.00 13.84  ? 677  LEU   A O   1 
ATOM   4866 C  CB  . LEU   A 1 652 ? 27.413 52.883  9.252   1.00 13.07  ? 677  LEU   A CB  1 
ATOM   4867 C  CG  . LEU   A 1 652 ? 26.213 53.583  8.625   1.00 14.97  ? 677  LEU   A CG  1 
ATOM   4868 C  CD1 . LEU   A 1 652 ? 24.942 52.743  8.825   1.00 15.88  ? 677  LEU   A CD1 1 
ATOM   4869 C  CD2 . LEU   A 1 652 ? 26.004 54.977  9.212   1.00 16.11  ? 677  LEU   A CD2 1 
ATOM   4870 N  N   . ASN   A 1 653 ? 30.398 51.843  9.160   1.00 12.36  ? 678  ASN   A N   1 
ATOM   4871 C  CA  . ASN   A 1 653 ? 31.438 51.017  9.753   1.00 13.26  ? 678  ASN   A CA  1 
ATOM   4872 C  C   . ASN   A 1 653 ? 32.671 51.783  10.125  1.00 13.48  ? 678  ASN   A C   1 
ATOM   4873 O  O   . ASN   A 1 653 ? 33.386 51.345  11.029  1.00 14.69  ? 678  ASN   A O   1 
ATOM   4874 C  CB  . ASN   A 1 653 ? 31.806 49.884  8.801   1.00 14.54  ? 678  ASN   A CB  1 
ATOM   4875 C  CG  . ASN   A 1 653 ? 30.701 48.876  8.679   1.00 17.73  ? 678  ASN   A CG  1 
ATOM   4876 O  OD1 . ASN   A 1 653 ? 29.717 48.852  9.445   1.00 18.24  ? 678  ASN   A OD1 1 
ATOM   4877 N  ND2 . ASN   A 1 653 ? 30.846 47.973  7.696   1.00 19.28  ? 678  ASN   A ND2 1 
ATOM   4878 N  N   . GLU   A 1 654 ? 32.972 52.860  9.413   1.00 13.24  ? 679  GLU   A N   1 
ATOM   4879 C  CA  . GLU   A 1 654 ? 34.170 53.639  9.727   1.00 13.28  ? 679  GLU   A CA  1 
ATOM   4880 C  C   . GLU   A 1 654 ? 33.860 54.752  10.702  1.00 13.19  ? 679  GLU   A C   1 
ATOM   4881 O  O   . GLU   A 1 654 ? 34.702 55.029  11.557  1.00 15.22  ? 679  GLU   A O   1 
ATOM   4882 C  CB  . GLU   A 1 654 ? 34.778 54.292  8.472   1.00 14.11  ? 679  GLU   A CB  1 
ATOM   4883 C  CG  . GLU   A 1 654 ? 35.119 53.281  7.383   1.00 15.44  ? 679  GLU   A CG  1 
ATOM   4884 C  CD  . GLU   A 1 654 ? 36.060 52.188  7.802   1.00 20.40  ? 679  GLU   A CD  1 
ATOM   4885 O  OE1 . GLU   A 1 654 ? 36.912 52.435  8.685   1.00 18.35  ? 679  GLU   A OE1 1 
ATOM   4886 O  OE2 . GLU   A 1 654 ? 35.941 51.057  7.257   1.00 21.36  ? 679  GLU   A OE2 1 
ATOM   4887 N  N   . LEU   A 1 655 ? 32.698 55.400  10.605  1.00 12.51  ? 680  LEU   A N   1 
ATOM   4888 C  CA  . LEU   A 1 655 ? 32.418 56.563  11.452  1.00 13.18  ? 680  LEU   A CA  1 
ATOM   4889 C  C   . LEU   A 1 655 ? 31.825 56.189  12.806  1.00 13.48  ? 680  LEU   A C   1 
ATOM   4890 O  O   . LEU   A 1 655 ? 32.197 56.806  13.823  1.00 13.81  ? 680  LEU   A O   1 
ATOM   4891 C  CB  . LEU   A 1 655 ? 31.453 57.482  10.731  1.00 12.68  ? 680  LEU   A CB  1 
ATOM   4892 C  CG  . LEU   A 1 655 ? 32.031 58.091  9.449   1.00 14.42  ? 680  LEU   A CG  1 
ATOM   4893 C  CD1 . LEU   A 1 655 ? 30.944 58.835  8.685   1.00 15.11  ? 680  LEU   A CD1 1 
ATOM   4894 C  CD2 . LEU   A 1 655 ? 33.199 59.033  9.732   1.00 15.79  ? 680  LEU   A CD2 1 
ATOM   4895 N  N   . ILE   A 1 656 ? 30.911 55.204  12.837  1.00 12.77  ? 681  ILE   A N   1 
ATOM   4896 C  CA  . ILE   A 1 656 ? 30.282 54.907  14.137  1.00 12.13  ? 681  ILE   A CA  1 
ATOM   4897 C  C   . ILE   A 1 656 ? 31.288 54.485  15.210  1.00 12.76  ? 681  ILE   A C   1 
ATOM   4898 O  O   . ILE   A 1 656 ? 31.212 55.009  16.340  1.00 12.60  ? 681  ILE   A O   1 
ATOM   4899 C  CB  . ILE   A 1 656 ? 29.140 53.902  13.979  1.00 12.41  ? 681  ILE   A CB  1 
ATOM   4900 C  CG1 . ILE   A 1 656 ? 28.016 54.601  13.264  1.00 14.08  ? 681  ILE   A CG1 1 
ATOM   4901 C  CG2 . ILE   A 1 656 ? 28.676 53.366  15.347  1.00 13.58  ? 681  ILE   A CG2 1 
ATOM   4902 C  CD1 . ILE   A 1 656 ? 26.810 53.655  12.987  1.00 15.19  ? 681  ILE   A CD1 1 
ATOM   4903 N  N   . PRO   A 1 657 ? 32.296 53.658  14.925  1.00 12.65  ? 682  PRO   A N   1 
ATOM   4904 C  CA  . PRO   A 1 657 ? 33.251 53.321  15.987  1.00 12.43  ? 682  PRO   A CA  1 
ATOM   4905 C  C   . PRO   A 1 657 ? 33.928 54.520  16.617  1.00 12.93  ? 682  PRO   A C   1 
ATOM   4906 O  O   . PRO   A 1 657 ? 34.304 54.460  17.811  1.00 13.67  ? 682  PRO   A O   1 
ATOM   4907 C  CB  . PRO   A 1 657 ? 34.248 52.392  15.292  1.00 13.46  ? 682  PRO   A CB  1 
ATOM   4908 C  CG  . PRO   A 1 657 ? 33.412 51.751  14.219  1.00 13.82  ? 682  PRO   A CG  1 
ATOM   4909 C  CD  . PRO   A 1 657 ? 32.549 52.857  13.690  1.00 12.73  ? 682  PRO   A CD  1 
ATOM   4910 N  N   . MET   A 1 658 ? 34.053 55.616  15.874  1.00 12.19  ? 683  MET   A N   1 
ATOM   4911 C  CA  . MET   A 1 658 ? 34.702 56.815  16.454  1.00 13.09  ? 683  MET   A CA  1 
ATOM   4912 C  C   . MET   A 1 658 ? 33.875 57.381  17.599  1.00 13.28  ? 683  MET   A C   1 
ATOM   4913 O  O   . MET   A 1 658 ? 34.441 57.698  18.666  1.00 13.80  ? 683  MET   A O   1 
ATOM   4914 C  CB  . MET   A 1 658 ? 34.891 57.895  15.386  1.00 13.60  ? 683  MET   A CB  1 
ATOM   4915 C  CG  . MET   A 1 658 ? 35.721 57.369  14.225  1.00 14.04  ? 683  MET   A CG  1 
ATOM   4916 S  SD  . MET   A 1 658 ? 35.999 58.673  13.010  1.00 15.54  ? 683  MET   A SD  1 
ATOM   4917 C  CE  . MET   A 1 658 ? 36.797 57.678  11.719  1.00 15.52  ? 683  MET   A CE  1 
ATOM   4918 N  N   . TYR   A 1 659 ? 32.534 57.459  17.422  1.00 13.28  ? 684  TYR   A N   1 
ATOM   4919 C  CA  . TYR   A 1 659 ? 31.735 57.957  18.539  1.00 12.70  ? 684  TYR   A CA  1 
ATOM   4920 C  C   . TYR   A 1 659 ? 31.571 56.895  19.614  1.00 13.04  ? 684  TYR   A C   1 
ATOM   4921 O  O   . TYR   A 1 659 ? 31.361 57.286  20.779  1.00 13.70  ? 684  TYR   A O   1 
ATOM   4922 C  CB  . TYR   A 1 659 ? 30.432 58.630  18.133  1.00 13.32  ? 684  TYR   A CB  1 
ATOM   4923 C  CG  . TYR   A 1 659 ? 29.275 57.741  17.740  1.00 13.00  ? 684  TYR   A CG  1 
ATOM   4924 C  CD1 . TYR   A 1 659 ? 28.665 56.905  18.667  1.00 13.45  ? 684  TYR   A CD1 1 
ATOM   4925 C  CD2 . TYR   A 1 659 ? 28.727 57.812  16.472  1.00 13.01  ? 684  TYR   A CD2 1 
ATOM   4926 C  CE1 . TYR   A 1 659 ? 27.564 56.140  18.333  1.00 13.29  ? 684  TYR   A CE1 1 
ATOM   4927 C  CE2 . TYR   A 1 659 ? 27.610 57.065  16.129  1.00 13.91  ? 684  TYR   A CE2 1 
ATOM   4928 C  CZ  . TYR   A 1 659 ? 27.040 56.219  17.054  1.00 14.44  ? 684  TYR   A CZ  1 
ATOM   4929 O  OH  . TYR   A 1 659 ? 25.932 55.508  16.660  1.00 16.92  ? 684  TYR   A OH  1 
ATOM   4930 N  N   . LYS   A 1 660 ? 31.685 55.581  19.281  1.00 12.00  ? 685  LYS   A N   1 
ATOM   4931 C  CA  . LYS   A 1 660 ? 31.626 54.585  20.343  1.00 12.15  ? 685  LYS   A CA  1 
ATOM   4932 C  C   . LYS   A 1 660 ? 32.827 54.745  21.308  1.00 13.07  ? 685  LYS   A C   1 
ATOM   4933 O  O   . LYS   A 1 660 ? 32.695 54.463  22.512  1.00 13.97  ? 685  LYS   A O   1 
ATOM   4934 C  CB  . LYS   A 1 660 ? 31.578 53.172  19.779  1.00 11.88  ? 685  LYS   A CB  1 
ATOM   4935 C  CG  . LYS   A 1 660 ? 30.368 52.865  18.870  1.00 12.46  ? 685  LYS   A CG  1 
ATOM   4936 C  CD  . LYS   A 1 660 ? 29.016 53.158  19.491  1.00 13.72  ? 685  LYS   A CD  1 
ATOM   4937 C  CE  . LYS   A 1 660 ? 28.644 52.157  20.570  1.00 13.99  ? 685  LYS   A CE  1 
ATOM   4938 N  NZ  . LYS   A 1 660 ? 27.332 52.577  21.202  1.00 14.15  ? 685  LYS   A NZ  1 
ATOM   4939 N  N   . LEU   A 1 661 ? 33.984 55.157  20.781  1.00 13.13  ? 686  LEU   A N   1 
ATOM   4940 C  CA  . LEU   A 1 661 ? 35.106 55.450  21.646  1.00 12.20  ? 686  LEU   A CA  1 
ATOM   4941 C  C   . LEU   A 1 661 ? 34.762 56.689  22.512  1.00 12.85  ? 686  LEU   A C   1 
ATOM   4942 O  O   . LEU   A 1 661 ? 35.024 56.684  23.716  1.00 13.27  ? 686  LEU   A O   1 
ATOM   4943 C  CB  . LEU   A 1 661 ? 36.384 55.753  20.835  1.00 12.52  ? 686  LEU   A CB  1 
ATOM   4944 C  CG  . LEU   A 1 661 ? 36.942 54.577  19.995  1.00 13.21  ? 686  LEU   A CG  1 
ATOM   4945 C  CD1 . LEU   A 1 661 ? 38.287 54.998  19.369  1.00 14.75  ? 686  LEU   A CD1 1 
ATOM   4946 C  CD2 . LEU   A 1 661 ? 37.152 53.326  20.825  1.00 14.13  ? 686  LEU   A CD2 1 
ATOM   4947 N  N   . MET   A 1 662 ? 34.230 57.731  21.879  1.00 13.18  ? 687  MET   A N   1 
ATOM   4948 C  CA  . MET   A 1 662 ? 33.925 58.974  22.602  1.00 13.08  ? 687  MET   A CA  1 
ATOM   4949 C  C   . MET   A 1 662 ? 32.917 58.751  23.711  1.00 14.52  ? 687  MET   A C   1 
ATOM   4950 O  O   . MET   A 1 662 ? 33.001 59.417  24.760  1.00 14.66  ? 687  MET   A O   1 
ATOM   4951 C  CB  . MET   A 1 662 ? 33.380 60.015  21.648  1.00 14.77  ? 687  MET   A CB  1 
ATOM   4952 C  CG  . MET   A 1 662 ? 34.397 60.416  20.573  1.00 15.08  ? 687  MET   A CG  1 
ATOM   4953 S  SD  . MET   A 1 662 ? 33.564 61.425  19.340  1.00 17.45  ? 687  MET   A SD  1 
ATOM   4954 C  CE  . MET   A 1 662 ? 34.930 61.520  18.068  1.00 18.03  ? 687  MET   A CE  1 
ATOM   4955 N  N   . GLU   A 1 663 ? 31.945 57.873  23.501  1.00 13.51  ? 688  GLU   A N   1 
ATOM   4956 C  CA  . GLU   A 1 663 ? 30.928 57.594  24.531  1.00 13.49  ? 688  GLU   A CA  1 
ATOM   4957 C  C   . GLU   A 1 663 ? 31.499 57.087  25.840  1.00 14.41  ? 688  GLU   A C   1 
ATOM   4958 O  O   . GLU   A 1 663 ? 30.846 57.232  26.890  1.00 15.79  ? 688  GLU   A O   1 
ATOM   4959 C  CB  . GLU   A 1 663 ? 29.942 56.524  24.017  1.00 13.24  ? 688  GLU   A CB  1 
ATOM   4960 C  CG  . GLU   A 1 663 ? 28.961 57.090  22.986  1.00 14.12  ? 688  GLU   A CG  1 
ATOM   4961 C  CD  . GLU   A 1 663 ? 27.990 56.064  22.428  1.00 14.97  ? 688  GLU   A CD  1 
ATOM   4962 O  OE1 . GLU   A 1 663 ? 28.271 54.846  22.548  1.00 16.04  ? 688  GLU   A OE1 1 
ATOM   4963 O  OE2 . GLU   A 1 663 ? 26.970 56.477  21.830  1.00 15.31  ? 688  GLU   A OE2 1 
ATOM   4964 N  N   . LYS   A 1 664 ? 32.708 56.504  25.787  1.00 14.25  ? 689  LYS   A N   1 
ATOM   4965 C  CA  . LYS   A 1 664 ? 33.339 55.976  26.990  1.00 15.23  ? 689  LYS   A CA  1 
ATOM   4966 C  C   . LYS   A 1 664 ? 34.464 56.889  27.480  1.00 16.93  ? 689  LYS   A C   1 
ATOM   4967 O  O   . LYS   A 1 664 ? 35.344 56.428  28.223  1.00 18.77  ? 689  LYS   A O   1 
ATOM   4968 C  CB  . LYS   A 1 664 ? 33.862 54.563  26.717  1.00 15.92  ? 689  LYS   A CB  1 
ATOM   4969 C  CG  . LYS   A 1 664 ? 32.716 53.667  26.213  1.00 14.82  ? 689  LYS   A CG  1 
ATOM   4970 C  CD  . LYS   A 1 664 ? 33.212 52.283  25.829  1.00 14.71  ? 689  LYS   A CD  1 
ATOM   4971 C  CE  . LYS   A 1 664 ? 32.098 51.432  25.214  1.00 16.37  ? 689  LYS   A CE  1 
ATOM   4972 N  NZ  . LYS   A 1 664 ? 31.607 52.075  23.922  1.00 16.16  ? 689  LYS   A NZ  1 
ATOM   4973 N  N   . ARG   A 1 665 ? 34.446 58.162  27.064  1.00 14.68  ? 690  ARG   A N   1 
ATOM   4974 C  CA  . ARG   A 1 665 ? 35.483 59.132  27.451  1.00 15.42  ? 690  ARG   A CA  1 
ATOM   4975 C  C   . ARG   A 1 665 ? 34.757 60.431  27.886  1.00 16.78  ? 690  ARG   A C   1 
ATOM   4976 O  O   . ARG   A 1 665 ? 33.541 60.599  27.687  1.00 16.32  ? 690  ARG   A O   1 
ATOM   4977 C  CB  . ARG   A 1 665 ? 36.400 59.435  26.250  1.00 16.32  ? 690  ARG   A CB  1 
ATOM   4978 C  CG  . ARG   A 1 665 ? 37.268 58.254  25.779  1.00 15.16  ? 690  ARG   A CG  1 
ATOM   4979 C  CD  . ARG   A 1 665 ? 38.422 57.979  26.688  1.00 15.39  ? 690  ARG   A CD  1 
ATOM   4980 N  NE  . ARG   A 1 665 ? 39.380 59.091  26.724  1.00 15.76  ? 690  ARG   A NE  1 
ATOM   4981 C  CZ  . ARG   A 1 665 ? 40.376 59.258  25.861  1.00 17.68  ? 690  ARG   A CZ  1 
ATOM   4982 N  NH1 . ARG   A 1 665 ? 40.585 58.373  24.897  1.00 15.53  ? 690  ARG   A NH1 1 
ATOM   4983 N  NH2 . ARG   A 1 665 ? 41.180 60.320  25.955  1.00 18.37  ? 690  ARG   A NH2 1 
ATOM   4984 N  N   . ASP   A 1 666 ? 35.527 61.363  28.448  1.00 17.17  ? 691  ASP   A N   1 
ATOM   4985 C  CA  . ASP   A 1 666 ? 34.976 62.660  28.876  1.00 18.24  ? 691  ASP   A CA  1 
ATOM   4986 C  C   . ASP   A 1 666 ? 35.018 63.591  27.691  1.00 18.53  ? 691  ASP   A C   1 
ATOM   4987 O  O   . ASP   A 1 666 ? 35.886 64.459  27.558  1.00 20.12  ? 691  ASP   A O   1 
ATOM   4988 C  CB  . ASP   A 1 666 ? 35.893 63.200  30.000  1.00 19.70  ? 691  ASP   A CB  1 
ATOM   4989 C  CG  . ASP   A 1 666 ? 35.444 64.558  30.514  1.00 25.84  ? 691  ASP   A CG  1 
ATOM   4990 O  OD1 . ASP   A 1 666 ? 34.257 64.884  30.357  1.00 23.09  ? 691  ASP   A OD1 1 
ATOM   4991 O  OD2 . ASP   A 1 666 ? 36.303 65.298  31.084  1.00 30.38  ? 691  ASP   A OD2 1 
ATOM   4992 N  N   . MET   A 1 667 ? 34.119 63.329  26.720  1.00 16.70  ? 692  MET   A N   1 
ATOM   4993 C  CA  . MET   A 1 667 ? 34.159 64.009  25.414  1.00 17.35  ? 692  MET   A CA  1 
ATOM   4994 C  C   . MET   A 1 667 ? 32.761 64.368  24.958  1.00 18.13  ? 692  MET   A C   1 
ATOM   4995 O  O   . MET   A 1 667 ? 32.434 64.305  23.762  1.00 17.19  ? 692  MET   A O   1 
ATOM   4996 C  CB  . MET   A 1 667 ? 34.761 63.014  24.364  1.00 17.14  ? 692  MET   A CB  1 
ATOM   4997 C  CG  . MET   A 1 667 ? 36.206 62.771  24.636  1.00 16.24  ? 692  MET   A CG  1 
ATOM   4998 S  SD  . MET   A 1 667 ? 36.850 61.553  23.431  1.00 18.12  ? 692  MET   A SD  1 
ATOM   4999 C  CE  . MET   A 1 667 ? 38.615 61.675  23.817  1.00 19.78  ? 692  MET   A CE  1 
ATOM   5000 N  N   . ASN   A 1 668 ? 31.919 64.827  25.884  1.00 17.86  ? 693  ASN   A N   1 
ATOM   5001 C  CA  . ASN   A 1 668 ? 30.522 65.088  25.505  1.00 17.85  ? 693  ASN   A CA  1 
ATOM   5002 C  C   . ASN   A 1 668 ? 30.356 66.060  24.331  1.00 18.36  ? 693  ASN   A C   1 
ATOM   5003 O  O   . ASN   A 1 668 ? 29.499 65.808  23.466  1.00 18.38  ? 693  ASN   A O   1 
ATOM   5004 C  CB  . ASN   A 1 668 ? 29.750 65.558  26.751  1.00 21.12  ? 693  ASN   A CB  1 
ATOM   5005 C  CG  . ASN   A 1 668 ? 28.462 66.144  26.414  1.00 27.94  ? 693  ASN   A CG  1 
ATOM   5006 O  OD1 . ASN   A 1 668 ? 27.518 65.417  26.166  1.00 31.13  ? 693  ASN   A OD1 1 
ATOM   5007 N  ND2 . ASN   A 1 668 ? 28.474 67.478  26.252  1.00 28.02  ? 693  ASN   A ND2 1 
ATOM   5008 N  N   . GLU   A 1 669 ? 31.079 67.171  24.328  1.00 18.97  ? 694  GLU   A N   1 
ATOM   5009 C  CA  . GLU   A 1 669 ? 30.893 68.170  23.314  1.00 18.81  ? 694  GLU   A CA  1 
ATOM   5010 C  C   . GLU   A 1 669 ? 31.199 67.623  21.906  1.00 19.13  ? 694  GLU   A C   1 
ATOM   5011 O  O   . GLU   A 1 669 ? 30.361 67.774  21.006  1.00 19.79  ? 694  GLU   A O   1 
ATOM   5012 C  CB  . GLU   A 1 669 ? 31.695 69.440  23.638  1.00 21.40  ? 694  GLU   A CB  1 
ATOM   5013 C  CG  . GLU   A 1 669 ? 31.367 69.995  25.023  1.00 26.85  ? 694  GLU   A CG  1 
ATOM   5014 C  CD  . GLU   A 1 669 ? 32.108 69.392  26.213  1.00 32.02  ? 694  GLU   A CD  1 
ATOM   5015 O  OE1 . GLU   A 1 669 ? 31.829 69.885  27.331  1.00 36.61  ? 694  GLU   A OE1 1 
ATOM   5016 O  OE2 . GLU   A 1 669 ? 32.911 68.428  26.067  1.00 28.16  ? 694  GLU   A OE2 1 
ATOM   5017 N  N   . VAL   A 1 670 ? 32.375 67.021  21.725  1.00 17.72  ? 695  VAL   A N   1 
ATOM   5018 C  CA  . VAL   A 1 670 ? 32.781 66.459  20.434  1.00 17.60  ? 695  VAL   A CA  1 
ATOM   5019 C  C   . VAL   A 1 670 ? 31.913 65.263  20.102  1.00 17.26  ? 695  VAL   A C   1 
ATOM   5020 O  O   . VAL   A 1 670 ? 31.500 65.138  18.956  1.00 16.87  ? 695  VAL   A O   1 
ATOM   5021 C  CB  . VAL   A 1 670 ? 34.264 66.107  20.462  1.00 18.32  ? 695  VAL   A CB  1 
ATOM   5022 C  CG1 . VAL   A 1 670 ? 34.678 65.329  19.215  1.00 19.11  ? 695  VAL   A CG1 1 
ATOM   5023 C  CG2 . VAL   A 1 670 ? 35.103 67.374  20.574  1.00 19.18  ? 695  VAL   A CG2 1 
ATOM   5024 N  N   . GLU   A 1 671 ? 31.522 64.443  21.081  1.00 15.84  ? 696  GLU   A N   1 
ATOM   5025 C  CA  . GLU   A 1 671 ? 30.646 63.300  20.823  1.00 16.36  ? 696  GLU   A CA  1 
ATOM   5026 C  C   . GLU   A 1 671 ? 29.319 63.796  20.242  1.00 16.86  ? 696  GLU   A C   1 
ATOM   5027 O  O   . GLU   A 1 671 ? 28.831 63.271  19.236  1.00 16.95  ? 696  GLU   A O   1 
ATOM   5028 C  CB  . GLU   A 1 671 ? 30.371 62.561  22.140  1.00 17.06  ? 696  GLU   A CB  1 
ATOM   5029 C  CG  . GLU   A 1 671 ? 29.381 61.418  21.974  1.00 17.67  ? 696  GLU   A CG  1 
ATOM   5030 C  CD  . GLU   A 1 671 ? 28.754 60.999  23.286  1.00 21.28  ? 696  GLU   A CD  1 
ATOM   5031 O  OE1 . GLU   A 1 671 ? 29.379 61.206  24.345  1.00 24.55  ? 696  GLU   A OE1 1 
ATOM   5032 O  OE2 . GLU   A 1 671 ? 27.614 60.506  23.276  1.00 18.89  ? 696  GLU   A OE2 1 
ATOM   5033 N  N   . THR   A 1 672 ? 28.750 64.853  20.852  1.00 16.83  ? 697  THR   A N   1 
ATOM   5034 C  CA  . THR   A 1 672 ? 27.490 65.392  20.367  1.00 17.03  ? 697  THR   A CA  1 
ATOM   5035 C  C   . THR   A 1 672 ? 27.629 65.946  18.944  1.00 16.81  ? 697  THR   A C   1 
ATOM   5036 O  O   . THR   A 1 672 ? 26.772 65.677  18.103  1.00 17.18  ? 697  THR   A O   1 
ATOM   5037 C  CB  . THR   A 1 672 ? 26.944 66.451  21.355  1.00 19.05  ? 697  THR   A CB  1 
ATOM   5038 O  OG1 . THR   A 1 672 ? 26.639 65.771  22.568  1.00 20.02  ? 697  THR   A OG1 1 
ATOM   5039 C  CG2 . THR   A 1 672 ? 25.682 67.124  20.847  1.00 20.99  ? 697  THR   A CG2 1 
ATOM   5040 N  N   . GLN   A 1 673 ? 28.675 66.719  18.692  1.00 15.99  ? 698  GLN   A N   1 
ATOM   5041 C  CA  . GLN   A 1 673 ? 28.883 67.326  17.378  1.00 16.02  ? 698  GLN   A CA  1 
ATOM   5042 C  C   . GLN   A 1 673 ? 29.158 66.237  16.332  1.00 16.90  ? 698  GLN   A C   1 
ATOM   5043 O  O   . GLN   A 1 673 ? 28.724 66.390  15.186  1.00 18.11  ? 698  GLN   A O   1 
ATOM   5044 C  CB  . GLN   A 1 673 ? 30.064 68.272  17.436  1.00 16.35  ? 698  GLN   A CB  1 
ATOM   5045 C  CG  . GLN   A 1 673 ? 29.747 69.585  18.161  1.00 18.78  ? 698  GLN   A CG  1 
ATOM   5046 C  CD  . GLN   A 1 673 ? 30.942 70.489  18.280  1.00 29.94  ? 698  GLN   A CD  1 
ATOM   5047 O  OE1 . GLN   A 1 673 ? 32.016 70.236  17.747  1.00 34.81  ? 698  GLN   A OE1 1 
ATOM   5048 N  NE2 . GLN   A 1 673 ? 30.764 71.594  18.995  1.00 32.63  ? 698  GLN   A NE2 1 
ATOM   5049 N  N   . PHE   A 1 674 ? 29.867 65.169  16.709  1.00 15.66  ? 699  PHE   A N   1 
ATOM   5050 C  CA  . PHE   A 1 674 ? 30.188 64.109  15.750  1.00 16.03  ? 699  PHE   A CA  1 
ATOM   5051 C  C   . PHE   A 1 674 ? 28.912 63.374  15.399  1.00 16.25  ? 699  PHE   A C   1 
ATOM   5052 O  O   . PHE   A 1 674 ? 28.665 63.127  14.189  1.00 16.18  ? 699  PHE   A O   1 
ATOM   5053 C  CB  . PHE   A 1 674 ? 31.188 63.143  16.389  1.00 15.20  ? 699  PHE   A CB  1 
ATOM   5054 C  CG  . PHE   A 1 674 ? 31.729 62.120  15.401  1.00 15.00  ? 699  PHE   A CG  1 
ATOM   5055 C  CD1 . PHE   A 1 674 ? 31.027 60.957  15.143  1.00 16.27  ? 699  PHE   A CD1 1 
ATOM   5056 C  CD2 . PHE   A 1 674 ? 32.869 62.389  14.659  1.00 15.58  ? 699  PHE   A CD2 1 
ATOM   5057 C  CE1 . PHE   A 1 674 ? 31.488 60.034  14.214  1.00 16.69  ? 699  PHE   A CE1 1 
ATOM   5058 C  CE2 . PHE   A 1 674 ? 33.330 61.474  13.697  1.00 16.09  ? 699  PHE   A CE2 1 
ATOM   5059 C  CZ  . PHE   A 1 674 ? 32.651 60.287  13.517  1.00 16.28  ? 699  PHE   A CZ  1 
ATOM   5060 N  N   . LYS   A 1 675 ? 28.058 63.045  16.363  1.00 15.59  ? 700  LYS   A N   1 
ATOM   5061 C  CA  . LYS   A 1 675 ? 26.780 62.398  16.059  1.00 15.79  ? 700  LYS   A CA  1 
ATOM   5062 C  C   . LYS   A 1 675 ? 25.871 63.285  15.217  1.00 16.80  ? 700  LYS   A C   1 
ATOM   5063 O  O   . LYS   A 1 675 ? 25.242 62.803  14.271  1.00 16.70  ? 700  LYS   A O   1 
ATOM   5064 C  CB  . LYS   A 1 675 ? 26.060 61.956  17.328  1.00 16.55  ? 700  LYS   A CB  1 
ATOM   5065 C  CG  . LYS   A 1 675 ? 26.845 60.889  18.105  1.00 15.38  ? 700  LYS   A CG  1 
ATOM   5066 C  CD  . LYS   A 1 675 ? 26.182 60.627  19.476  1.00 15.87  ? 700  LYS   A CD  1 
ATOM   5067 C  CE  . LYS   A 1 675 ? 26.751 59.330  20.074  1.00 17.28  ? 700  LYS   A CE  1 
ATOM   5068 N  NZ  . LYS   A 1 675 ? 26.218 59.093  21.452  1.00 17.74  ? 700  LYS   A NZ  1 
ATOM   5069 N  N   . ALA   A 1 676 ? 25.871 64.585  15.488  1.00 15.94  ? 701  ALA   A N   1 
ATOM   5070 C  CA  . ALA   A 1 676 ? 25.084 65.510  14.682  1.00 16.09  ? 701  ALA   A CA  1 
ATOM   5071 C  C   . ALA   A 1 676 ? 25.599 65.548  13.234  1.00 17.16  ? 701  ALA   A C   1 
ATOM   5072 O  O   . ALA   A 1 676 ? 24.811 65.635  12.287  1.00 17.31  ? 701  ALA   A O   1 
ATOM   5073 C  CB  . ALA   A 1 676 ? 25.118 66.902  15.309  1.00 17.01  ? 701  ALA   A CB  1 
ATOM   5074 N  N   . PHE   A 1 677 ? 26.924 65.504  13.059  1.00 16.96  ? 702  PHE   A N   1 
ATOM   5075 C  CA  . PHE   A 1 677 ? 27.541 65.479  11.724  1.00 16.57  ? 702  PHE   A CA  1 
ATOM   5076 C  C   . PHE   A 1 677 ? 27.077 64.203  10.984  1.00 16.44  ? 702  PHE   A C   1 
ATOM   5077 O  O   . PHE   A 1 677 ? 26.698 64.284  9.824   1.00 16.86  ? 702  PHE   A O   1 
ATOM   5078 C  CB  . PHE   A 1 677 ? 29.072 65.518  11.853  1.00 17.37  ? 702  PHE   A CB  1 
ATOM   5079 C  CG  . PHE   A 1 677 ? 29.821 64.875  10.712  1.00 20.13  ? 702  PHE   A CG  1 
ATOM   5080 C  CD1 . PHE   A 1 677 ? 29.823 65.451  9.456   1.00 22.37  ? 702  PHE   A CD1 1 
ATOM   5081 C  CD2 . PHE   A 1 677 ? 30.467 63.672  10.888  1.00 21.61  ? 702  PHE   A CD2 1 
ATOM   5082 C  CE1 . PHE   A 1 677 ? 30.413 64.803  8.383   1.00 23.45  ? 702  PHE   A CE1 1 
ATOM   5083 C  CE2 . PHE   A 1 677 ? 31.121 63.056  9.822   1.00 23.25  ? 702  PHE   A CE2 1 
ATOM   5084 C  CZ  . PHE   A 1 677 ? 31.092 63.638  8.588   1.00 22.86  ? 702  PHE   A CZ  1 
ATOM   5085 N  N   . LEU   A 1 678 ? 27.100 63.060  11.656  1.00 15.62  ? 703  LEU   A N   1 
ATOM   5086 C  CA  . LEU   A 1 678 ? 26.706 61.807  11.002  1.00 15.19  ? 703  LEU   A CA  1 
ATOM   5087 C  C   . LEU   A 1 678 ? 25.255 61.853  10.553  1.00 16.07  ? 703  LEU   A C   1 
ATOM   5088 O  O   . LEU   A 1 678 ? 24.936 61.444  9.413   1.00 16.32  ? 703  LEU   A O   1 
ATOM   5089 C  CB  . LEU   A 1 678 ? 26.947 60.629  11.948  1.00 15.00  ? 703  LEU   A CB  1 
ATOM   5090 C  CG  . LEU   A 1 678 ? 26.526 59.269  11.423  1.00 15.24  ? 703  LEU   A CG  1 
ATOM   5091 C  CD1 . LEU   A 1 678 ? 27.283 58.894  10.192  1.00 17.25  ? 703  LEU   A CD1 1 
ATOM   5092 C  CD2 . LEU   A 1 678 ? 26.688 58.196  12.550  1.00 16.55  ? 703  LEU   A CD2 1 
ATOM   5093 N  N   . ILE   A 1 679 ? 24.353 62.364  11.405  1.00 15.48  ? 704  ILE   A N   1 
ATOM   5094 C  CA  . ILE   A 1 679 ? 22.936 62.432  11.007  1.00 16.23  ? 704  ILE   A CA  1 
ATOM   5095 C  C   . ILE   A 1 679 ? 22.751 63.446  9.886   1.00 16.95  ? 704  ILE   A C   1 
ATOM   5096 O  O   . ILE   A 1 679 ? 21.994 63.211  8.934   1.00 17.15  ? 704  ILE   A O   1 
ATOM   5097 C  CB  . ILE   A 1 679 ? 22.034 62.787  12.225  1.00 17.60  ? 704  ILE   A CB  1 
ATOM   5098 C  CG1 . ILE   A 1 679 ? 22.101 61.669  13.268  1.00 18.56  ? 704  ILE   A CG1 1 
ATOM   5099 C  CG2 . ILE   A 1 679 ? 20.585 63.029  11.793  1.00 19.62  ? 704  ILE   A CG2 1 
ATOM   5100 C  CD1 . ILE   A 1 679 ? 21.790 60.228  12.680  1.00 18.77  ? 704  ILE   A CD1 1 
ATOM   5101 N  N   . ARG   A 1 680 ? 23.445 64.574  9.954   1.00 17.25  ? 705  ARG   A N   1 
ATOM   5102 C  CA  . ARG   A 1 680 ? 23.362 65.591  8.886   1.00 18.64  ? 705  ARG   A CA  1 
ATOM   5103 C  C   . ARG   A 1 680 ? 23.819 64.997  7.553   1.00 19.20  ? 705  ARG   A C   1 
ATOM   5104 O  O   . ARG   A 1 680 ? 23.178 65.236  6.500   1.00 20.27  ? 705  ARG   A O   1 
ATOM   5105 C  CB  . ARG   A 1 680 ? 24.244 66.804  9.282   1.00 22.44  ? 705  ARG   A CB  1 
ATOM   5106 C  CG  . ARG   A 1 680 ? 24.191 67.990  8.371   1.00 28.99  ? 705  ARG   A CG  1 
ATOM   5107 C  CD  . ARG   A 1 680 ? 24.747 69.240  9.097   1.00 32.09  ? 705  ARG   A CD  1 
ATOM   5108 N  NE  . ARG   A 1 680 ? 26.192 69.153  9.333   1.00 36.50  ? 705  ARG   A NE  1 
ATOM   5109 C  CZ  . ARG   A 1 680 ? 26.770 69.111  10.535  1.00 38.70  ? 705  ARG   A CZ  1 
ATOM   5110 N  NH1 . ARG   A 1 680 ? 28.090 69.040  10.640  1.00 38.96  ? 705  ARG   A NH1 1 
ATOM   5111 N  NH2 . ARG   A 1 680 ? 26.034 69.184  11.638  1.00 38.89  ? 705  ARG   A NH2 1 
ATOM   5112 N  N   . LEU   A 1 681 ? 24.889 64.209  7.592   1.00 17.81  ? 706  LEU   A N   1 
ATOM   5113 C  CA  . LEU   A 1 681 ? 25.456 63.604  6.398   1.00 18.09  ? 706  LEU   A CA  1 
ATOM   5114 C  C   . LEU   A 1 681 ? 24.444 62.697  5.695   1.00 18.17  ? 706  LEU   A C   1 
ATOM   5115 O  O   . LEU   A 1 681 ? 24.354 62.679  4.454   1.00 19.29  ? 706  LEU   A O   1 
ATOM   5116 C  CB  . LEU   A 1 681 ? 26.698 62.832  6.811   1.00 18.12  ? 706  LEU   A CB  1 
ATOM   5117 C  CG  . LEU   A 1 681 ? 27.484 62.137  5.711   1.00 18.92  ? 706  LEU   A CG  1 
ATOM   5118 C  CD1 . LEU   A 1 681 ? 28.090 63.186  4.758   1.00 19.81  ? 706  LEU   A CD1 1 
ATOM   5119 C  CD2 . LEU   A 1 681 ? 28.639 61.375  6.341   1.00 19.24  ? 706  LEU   A CD2 1 
ATOM   5120 N  N   . LEU   A 1 682 ? 23.685 61.936  6.473   1.00 16.22  ? 707  LEU   A N   1 
ATOM   5121 C  CA  . LEU   A 1 682 ? 22.743 60.973  5.904   1.00 15.38  ? 707  LEU   A CA  1 
ATOM   5122 C  C   . LEU   A 1 682 ? 21.287 61.428  5.944   1.00 15.78  ? 707  LEU   A C   1 
ATOM   5123 O  O   . LEU   A 1 682 ? 20.396 60.648  5.629   1.00 16.31  ? 707  LEU   A O   1 
ATOM   5124 C  CB  . LEU   A 1 682 ? 22.881 59.660  6.677   1.00 15.51  ? 707  LEU   A CB  1 
ATOM   5125 C  CG  . LEU   A 1 682 ? 24.287 59.018  6.578   1.00 18.25  ? 707  LEU   A CG  1 
ATOM   5126 C  CD1 . LEU   A 1 682 ? 24.382 57.743  7.411   1.00 19.62  ? 707  LEU   A CD1 1 
ATOM   5127 C  CD2 . LEU   A 1 682 ? 24.716 58.757  5.113   1.00 20.48  ? 707  LEU   A CD2 1 
ATOM   5128 N  N   . ARG   A 1 683 ? 21.026 62.666  6.365   1.00 16.09  ? 708  ARG   A N   1 
ATOM   5129 C  CA  . ARG   A 1 683 ? 19.677 63.152  6.561   1.00 16.90  ? 708  ARG   A CA  1 
ATOM   5130 C  C   . ARG   A 1 683 ? 18.790 63.020  5.349   1.00 16.88  ? 708  ARG   A C   1 
ATOM   5131 O  O   . ARG   A 1 683 ? 17.644 62.590  5.488   1.00 17.13  ? 708  ARG   A O   1 
ATOM   5132 C  CB  . ARG   A 1 683 ? 19.736 64.617  7.027   1.00 18.77  ? 708  ARG   A CB  1 
ATOM   5133 C  CG  . ARG   A 1 683 ? 18.368 65.112  7.404   1.00 21.79  ? 708  ARG   A CG  1 
ATOM   5134 C  CD  . ARG   A 1 683 ? 18.390 66.571  7.782   1.00 27.79  ? 708  ARG   A CD  1 
ATOM   5135 N  NE  . ARG   A 1 683 ? 17.081 66.968  8.283   1.00 35.51  ? 708  ARG   A NE  1 
ATOM   5136 C  CZ  . ARG   A 1 683 ? 16.765 68.207  8.653   1.00 40.77  ? 708  ARG   A CZ  1 
ATOM   5137 N  NH1 . ARG   A 1 683 ? 15.544 68.479  9.106   1.00 40.86  ? 708  ARG   A NH1 1 
ATOM   5138 N  NH2 . ARG   A 1 683 ? 17.665 69.183  8.572   1.00 40.83  ? 708  ARG   A NH2 1 
ATOM   5139 N  N   . ASP   A 1 684 ? 19.310 63.362  4.163   1.00 16.69  ? 709  ASP   A N   1 
ATOM   5140 C  CA  . ASP   A 1 684 ? 18.429 63.281  2.972   1.00 18.38  ? 709  ASP   A CA  1 
ATOM   5141 C  C   . ASP   A 1 684 ? 18.017 61.852  2.692   1.00 18.40  ? 709  ASP   A C   1 
ATOM   5142 O  O   . ASP   A 1 684 ? 16.848 61.584  2.350   1.00 19.43  ? 709  ASP   A O   1 
ATOM   5143 C  CB  . ASP   A 1 684 ? 19.108 63.892  1.761   1.00 21.04  ? 709  ASP   A CB  1 
ATOM   5144 C  CG  . ASP   A 1 684 ? 19.309 65.394  1.854   1.00 25.93  ? 709  ASP   A CG  1 
ATOM   5145 O  OD1 . ASP   A 1 684 ? 18.603 66.035  2.649   1.00 26.68  ? 709  ASP   A OD1 1 
ATOM   5146 O  OD2 . ASP   A 1 684 ? 20.189 65.916  1.130   1.00 27.57  ? 709  ASP   A OD2 1 
ATOM   5147 N  N   . LEU   A 1 685 ? 18.951 60.906  2.891   1.00 16.42  ? 710  LEU   A N   1 
ATOM   5148 C  CA  . LEU   A 1 685 ? 18.632 59.502  2.676   1.00 17.20  ? 710  LEU   A CA  1 
ATOM   5149 C  C   . LEU   A 1 685 ? 17.685 59.002  3.767   1.00 17.05  ? 710  LEU   A C   1 
ATOM   5150 O  O   . LEU   A 1 685 ? 16.762 58.230  3.500   1.00 18.27  ? 710  LEU   A O   1 
ATOM   5151 C  CB  . LEU   A 1 685 ? 19.923 58.685  2.659   1.00 17.61  ? 710  LEU   A CB  1 
ATOM   5152 C  CG  . LEU   A 1 685 ? 19.788 57.234  2.218   1.00 19.08  ? 710  LEU   A CG  1 
ATOM   5153 C  CD1 . LEU   A 1 685 ? 19.158 57.103  0.815   1.00 19.55  ? 710  LEU   A CD1 1 
ATOM   5154 C  CD2 . LEU   A 1 685 ? 21.163 56.571  2.221   1.00 18.85  ? 710  LEU   A CD2 1 
ATOM   5155 N  N   . ILE   A 1 686 ? 17.879 59.433  5.011   1.00 16.19  ? 711  ILE   A N   1 
ATOM   5156 C  CA  . ILE   A 1 686 ? 16.971 59.059  6.101   1.00 16.79  ? 711  ILE   A CA  1 
ATOM   5157 C  C   . ILE   A 1 686 ? 15.535 59.569  5.792   1.00 17.14  ? 711  ILE   A C   1 
ATOM   5158 O  O   . ILE   A 1 686 ? 14.580 58.808  5.881   1.00 17.32  ? 711  ILE   A O   1 
ATOM   5159 C  CB  . ILE   A 1 686 ? 17.471 59.668  7.438   1.00 16.36  ? 711  ILE   A CB  1 
ATOM   5160 C  CG1 . ILE   A 1 686 ? 18.730 58.887  7.895   1.00 16.75  ? 711  ILE   A CG1 1 
ATOM   5161 C  CG2 . ILE   A 1 686 ? 16.390 59.603  8.540   1.00 18.19  ? 711  ILE   A CG2 1 
ATOM   5162 C  CD1 . ILE   A 1 686 ? 19.493 59.694  8.969   1.00 17.81  ? 711  ILE   A CD1 1 
ATOM   5163 N  N   . ASP   A 1 687 ? 15.429 60.840  5.374   1.00 18.27  ? 712  ASP   A N   1 
ATOM   5164 C  CA  . ASP   A 1 687 ? 14.125 61.462  5.089   1.00 18.21  ? 712  ASP   A CA  1 
ATOM   5165 C  C   . ASP   A 1 687 ? 13.403 60.772  3.928   1.00 20.13  ? 712  ASP   A C   1 
ATOM   5166 O  O   . ASP   A 1 687 ? 12.158 60.804  3.868   1.00 22.29  ? 712  ASP   A O   1 
ATOM   5167 C  CB  . ASP   A 1 687 ? 14.340 62.939  4.761   1.00 19.51  ? 712  ASP   A CB  1 
ATOM   5168 C  CG  . ASP   A 1 687 ? 14.611 63.821  5.969   1.00 21.00  ? 712  ASP   A CG  1 
ATOM   5169 O  OD1 . ASP   A 1 687 ? 14.418 63.349  7.110   1.00 22.41  ? 712  ASP   A OD1 1 
ATOM   5170 O  OD2 . ASP   A 1 687 ? 15.041 64.986  5.768   1.00 24.06  ? 712  ASP   A OD2 1 
ATOM   5171 N  N   . LYS   A 1 688 ? 14.146 60.214  2.976   1.00 18.60  ? 713  LYS   A N   1 
ATOM   5172 C  CA  . LYS   A 1 688 ? 13.549 59.535  1.818   1.00 20.01  ? 713  LYS   A CA  1 
ATOM   5173 C  C   . LYS   A 1 688 ? 12.981 58.154  2.187   1.00 20.66  ? 713  LYS   A C   1 
ATOM   5174 O  O   . LYS   A 1 688 ? 12.203 57.608  1.391   1.00 21.63  ? 713  LYS   A O   1 
ATOM   5175 C  CB  . LYS   A 1 688 ? 14.589 59.403  0.687   1.00 23.42  ? 713  LYS   A CB  1 
ATOM   5176 C  CG  . LYS   A 1 688 ? 14.683 60.669  -0.155  1.00 28.59  ? 713  LYS   A CG  1 
ATOM   5177 C  CD  . LYS   A 1 688 ? 15.827 60.637  -1.141  1.00 32.13  ? 713  LYS   A CD  1 
ATOM   5178 C  CE  . LYS   A 1 688 ? 16.055 61.999  -1.752  1.00 36.54  ? 713  LYS   A CE  1 
ATOM   5179 N  NZ  . LYS   A 1 688 ? 17.276 62.031  -2.601  1.00 39.79  ? 713  LYS   A NZ  1 
ATOM   5180 N  N   . GLN   A 1 689 ? 13.308 57.597  3.401   1.00 18.18  ? 714  GLN   A N   1 
ATOM   5181 C  CA  . GLN   A 1 689 ? 12.825 56.259  3.693   1.00 17.66  ? 714  GLN   A CA  1 
ATOM   5182 C  C   . GLN   A 1 689 ? 11.332 56.211  3.980   1.00 18.72  ? 714  GLN   A C   1 
ATOM   5183 O  O   . GLN   A 1 689 ? 10.806 57.066  4.705   1.00 20.71  ? 714  GLN   A O   1 
ATOM   5184 C  CB  . GLN   A 1 689 ? 13.569 55.628  4.890   1.00 16.68  ? 714  GLN   A CB  1 
ATOM   5185 C  CG  . GLN   A 1 689 ? 15.078 55.555  4.697   1.00 16.85  ? 714  GLN   A CG  1 
ATOM   5186 C  CD  . GLN   A 1 689 ? 15.448 54.821  3.416   1.00 18.52  ? 714  GLN   A CD  1 
ATOM   5187 O  OE1 . GLN   A 1 689 ? 15.013 53.675  3.207   1.00 18.43  ? 714  GLN   A OE1 1 
ATOM   5188 N  NE2 . GLN   A 1 689 ? 16.202 55.484  2.549   1.00 17.24  ? 714  GLN   A NE2 1 
ATOM   5189 N  N   . THR   A 1 690 ? 10.665 55.199  3.428   1.00 18.20  ? 715  THR   A N   1 
ATOM   5190 C  CA  . THR   A 1 690 ? 9.266  54.983  3.744   1.00 18.65  ? 715  THR   A CA  1 
ATOM   5191 C  C   . THR   A 1 690 ? 9.208  54.063  4.949   1.00 18.42  ? 715  THR   A C   1 
ATOM   5192 O  O   . THR   A 1 690 ? 10.142 53.294  5.207   1.00 17.56  ? 715  THR   A O   1 
ATOM   5193 C  CB  . THR   A 1 690 ? 8.511  54.358  2.569   1.00 20.71  ? 715  THR   A CB  1 
ATOM   5194 O  OG1 . THR   A 1 690 ? 9.086  53.078  2.257   1.00 20.25  ? 715  THR   A OG1 1 
ATOM   5195 C  CG2 . THR   A 1 690 ? 8.523  55.277  1.349   1.00 21.79  ? 715  THR   A CG2 1 
ATOM   5196 N  N   . TRP   A 1 691 ? 8.143  54.149  5.702   1.00 17.86  ? 716  TRP   A N   1 
ATOM   5197 C  CA  . TRP   A 1 691 ? 7.936  53.332  6.889   1.00 17.72  ? 716  TRP   A CA  1 
ATOM   5198 C  C   . TRP   A 1 691 ? 7.081  52.145  6.487   1.00 19.12  ? 716  TRP   A C   1 
ATOM   5199 O  O   . TRP   A 1 691 ? 5.895  52.048  6.835   1.00 20.35  ? 716  TRP   A O   1 
ATOM   5200 C  CB  . TRP   A 1 691 ? 7.303  54.174  8.010   1.00 17.88  ? 716  TRP   A CB  1 
ATOM   5201 C  CG  . TRP   A 1 691 ? 8.317  55.137  8.573   1.00 18.35  ? 716  TRP   A CG  1 
ATOM   5202 C  CD1 . TRP   A 1 691 ? 9.067  56.044  7.877   1.00 20.13  ? 716  TRP   A CD1 1 
ATOM   5203 C  CD2 . TRP   A 1 691 ? 8.821  55.153  9.920   1.00 18.27  ? 716  TRP   A CD2 1 
ATOM   5204 N  NE1 . TRP   A 1 691 ? 9.945  56.689  8.731   1.00 20.72  ? 716  TRP   A NE1 1 
ATOM   5205 C  CE2 . TRP   A 1 691 ? 9.804  56.164  9.991   1.00 19.00  ? 716  TRP   A CE2 1 
ATOM   5206 C  CE3 . TRP   A 1 691 ? 8.510  54.438  11.084  1.00 19.42  ? 716  TRP   A CE3 1 
ATOM   5207 C  CZ2 . TRP   A 1 691 ? 10.490 56.462  11.172  1.00 19.43  ? 716  TRP   A CZ2 1 
ATOM   5208 C  CZ3 . TRP   A 1 691 ? 9.231  54.702  12.244  1.00 19.35  ? 716  TRP   A CZ3 1 
ATOM   5209 C  CH2 . TRP   A 1 691 ? 10.173 55.736  12.285  1.00 19.41  ? 716  TRP   A CH2 1 
ATOM   5210 N  N   . THR   A 1 692 ? 7.699  51.269  5.682   1.00 17.60  ? 717  THR   A N   1 
ATOM   5211 C  CA  . THR   A 1 692 ? 7.038  50.131  5.068   1.00 18.20  ? 717  THR   A CA  1 
ATOM   5212 C  C   . THR   A 1 692 ? 8.052  48.973  4.931   1.00 18.53  ? 717  THR   A C   1 
ATOM   5213 O  O   . THR   A 1 692 ? 9.221  49.103  5.313   1.00 18.13  ? 717  THR   A O   1 
ATOM   5214 C  CB  . THR   A 1 692 ? 6.615  50.516  3.585   1.00 19.63  ? 717  THR   A CB  1 
ATOM   5215 O  OG1 . THR   A 1 692 ? 7.785  50.590  2.737   1.00 20.65  ? 717  THR   A OG1 1 
ATOM   5216 C  CG2 . THR   A 1 692 ? 5.750  51.778  3.495   1.00 20.23  ? 717  THR   A CG2 1 
ATOM   5217 N  N   . ASP   A 1 693 ? 7.588  47.828  4.398   1.00 19.50  ? 718  ASP   A N   1 
ATOM   5218 C  CA  . ASP   A 1 693 ? 8.421  46.702  4.063   1.00 18.42  ? 718  ASP   A CA  1 
ATOM   5219 C  C   . ASP   A 1 693 ? 8.627  46.582  2.539   1.00 19.91  ? 718  ASP   A C   1 
ATOM   5220 O  O   . ASP   A 1 693 ? 8.919  45.482  2.054   1.00 21.21  ? 718  ASP   A O   1 
ATOM   5221 C  CB  . ASP   A 1 693 ? 7.856  45.400  4.646   1.00 18.76  ? 718  ASP   A CB  1 
ATOM   5222 C  CG  . ASP   A 1 693 ? 7.921  45.366  6.153   1.00 22.40  ? 718  ASP   A CG  1 
ATOM   5223 O  OD1 . ASP   A 1 693 ? 8.760  46.108  6.739   1.00 21.40  ? 718  ASP   A OD1 1 
ATOM   5224 O  OD2 . ASP   A 1 693 ? 7.141  44.596  6.776   1.00 23.69  ? 718  ASP   A OD2 1 
ATOM   5225 N  N   . GLU   A 1 694 ? 8.503  47.707  1.812   1.00 20.65  ? 719  GLU   A N   1 
ATOM   5226 C  CA  . GLU   A 1 694 ? 8.632  47.691  0.357   1.00 21.84  ? 719  GLU   A CA  1 
ATOM   5227 C  C   . GLU   A 1 694 ? 10.061 47.532  -0.131  1.00 23.24  ? 719  GLU   A C   1 
ATOM   5228 O  O   . GLU   A 1 694 ? 11.015 47.876  0.566   1.00 22.21  ? 719  GLU   A O   1 
ATOM   5229 C  CB  . GLU   A 1 694 ? 8.057  48.979  -0.206  1.00 23.19  ? 719  GLU   A CB  1 
ATOM   5230 C  CG  . GLU   A 1 694 ? 6.576  49.112  0.046   1.00 24.97  ? 719  GLU   A CG  1 
ATOM   5231 C  CD  . GLU   A 1 694 ? 5.993  50.467  -0.317  1.00 30.35  ? 719  GLU   A CD  1 
ATOM   5232 O  OE1 . GLU   A 1 694 ? 6.723  51.322  -0.871  1.00 30.02  ? 719  GLU   A OE1 1 
ATOM   5233 O  OE2 . GLU   A 1 694 ? 4.787  50.667  -0.052  1.00 36.12  ? 719  GLU   A OE2 1 
ATOM   5234 N  N   . GLY   A 1 695 ? 10.198 47.054  -1.360  1.00 24.28  ? 720  GLY   A N   1 
ATOM   5235 C  CA  . GLY   A 1 695 ? 11.489 46.989  -2.010  1.00 25.14  ? 720  GLY   A CA  1 
ATOM   5236 C  C   . GLY   A 1 695 ? 12.223 45.683  -1.953  1.00 23.75  ? 720  GLY   A C   1 
ATOM   5237 O  O   . GLY   A 1 695 ? 11.765 44.698  -1.371  1.00 23.88  ? 720  GLY   A O   1 
ATOM   5238 N  N   . SER   A 1 696 ? 13.428 45.716  -2.498  1.00 24.70  ? 721  SER   A N   1 
ATOM   5239 C  CA  . SER   A 1 696 ? 14.334 44.587  -2.493  1.00 24.84  ? 721  SER   A CA  1 
ATOM   5240 C  C   . SER   A 1 696 ? 14.944 44.355  -1.100  1.00 24.39  ? 721  SER   A C   1 
ATOM   5241 O  O   . SER   A 1 696 ? 14.838 45.232  -0.222  1.00 24.64  ? 721  SER   A O   1 
ATOM   5242 C  CB  . SER   A 1 696 ? 15.453 44.856  -3.491  1.00 27.21  ? 721  SER   A CB  1 
ATOM   5243 O  OG  . SER   A 1 696 ? 16.159 46.014  -3.051  1.00 29.02  ? 721  SER   A OG  1 
ATOM   5244 N  N   . VAL   A 1 697 ? 15.630 43.236  -0.885  1.00 22.63  ? 722  VAL   A N   1 
ATOM   5245 C  CA  . VAL   A 1 697 ? 16.251 42.951  0.398   1.00 22.33  ? 722  VAL   A CA  1 
ATOM   5246 C  C   . VAL   A 1 697 ? 17.267 44.078  0.771   1.00 21.58  ? 722  VAL   A C   1 
ATOM   5247 O  O   . VAL   A 1 697 ? 17.328 44.472  1.936   1.00 20.32  ? 722  VAL   A O   1 
ATOM   5248 C  CB  . VAL   A 1 697 ? 16.832 41.499  0.421   1.00 25.33  ? 722  VAL   A CB  1 
ATOM   5249 C  CG1 . VAL   A 1 697 ? 17.687 41.261  1.636   1.00 25.67  ? 722  VAL   A CG1 1 
ATOM   5250 C  CG2 . VAL   A 1 697 ? 15.688 40.468  0.366   1.00 27.10  ? 722  VAL   A CG2 1 
ATOM   5251 N  N   A SER   A 1 698 ? 17.975 44.638  -0.227  0.50 20.32  ? 723  SER   A N   1 
ATOM   5252 N  N   B SER   A 1 698 ? 17.994 44.642  -0.220  0.50 20.90  ? 723  SER   A N   1 
ATOM   5253 C  CA  A SER   A 1 698 ? 18.934 45.708  0.051   0.50 18.91  ? 723  SER   A CA  1 
ATOM   5254 C  CA  B SER   A 1 698 ? 18.946 45.718  0.090   0.50 20.05  ? 723  SER   A CA  1 
ATOM   5255 C  C   A SER   A 1 698 ? 18.201 46.965  0.482   0.50 18.02  ? 723  SER   A C   1 
ATOM   5256 C  C   B SER   A 1 698 ? 18.205 46.976  0.493   0.50 18.59  ? 723  SER   A C   1 
ATOM   5257 O  O   A SER   A 1 698 ? 18.620 47.629  1.435   0.50 17.95  ? 723  SER   A O   1 
ATOM   5258 O  O   B SER   A 1 698 ? 18.623 47.657  1.434   0.50 18.50  ? 723  SER   A O   1 
ATOM   5259 C  CB  A SER   A 1 698 ? 19.798 46.002  -1.172  0.50 17.89  ? 723  SER   A CB  1 
ATOM   5260 C  CB  B SER   A 1 698 ? 19.861 46.018  -1.090  0.50 20.89  ? 723  SER   A CB  1 
ATOM   5261 O  OG  A SER   A 1 698 ? 19.010 46.281  -2.324  0.50 18.30  ? 723  SER   A OG  1 
ATOM   5262 O  OG  B SER   A 1 698 ? 20.821 44.993  -1.276  0.50 24.35  ? 723  SER   A OG  1 
ATOM   5263 N  N   . GLU   A 1 699 ? 17.093 47.288  -0.181  1.00 18.34  ? 724  GLU   A N   1 
ATOM   5264 C  CA  . GLU   A 1 699 ? 16.318 48.483  0.165   1.00 18.07  ? 724  GLU   A CA  1 
ATOM   5265 C  C   . GLU   A 1 699 ? 15.743 48.330  1.573   1.00 17.20  ? 724  GLU   A C   1 
ATOM   5266 O  O   . GLU   A 1 699 ? 15.769 49.298  2.358   1.00 16.03  ? 724  GLU   A O   1 
ATOM   5267 C  CB  . GLU   A 1 699 ? 15.210 48.738  -0.869  1.00 20.57  ? 724  GLU   A CB  1 
ATOM   5268 C  CG  . GLU   A 1 699 ? 15.781 49.281  -2.167  1.00 25.17  ? 724  GLU   A CG  1 
ATOM   5269 C  CD  . GLU   A 1 699 ? 14.822 49.286  -3.349  1.00 32.73  ? 724  GLU   A CD  1 
ATOM   5270 O  OE1 . GLU   A 1 699 ? 13.941 48.400  -3.420  1.00 29.41  ? 724  GLU   A OE1 1 
ATOM   5271 O  OE2 . GLU   A 1 699 ? 14.960 50.182  -4.210  1.00 37.77  ? 724  GLU   A OE2 1 
ATOM   5272 N  N   . ARG   A 1 700 ? 15.283 47.106  1.910   1.00 16.54  ? 725  ARG   A N   1 
ATOM   5273 C  CA  . ARG   A 1 700 ? 14.756 46.856  3.252   1.00 15.32  ? 725  ARG   A CA  1 
ATOM   5274 C  C   . ARG   A 1 700 ? 15.796 46.960  4.335   1.00 15.77  ? 725  ARG   A C   1 
ATOM   5275 O  O   . ARG   A 1 700 ? 15.561 47.561  5.378   1.00 14.72  ? 725  ARG   A O   1 
ATOM   5276 C  CB  . ARG   A 1 700 ? 14.068 45.478  3.305   1.00 16.63  ? 725  ARG   A CB  1 
ATOM   5277 C  CG  . ARG   A 1 700 ? 12.867 45.426  2.313   1.00 17.30  ? 725  ARG   A CG  1 
ATOM   5278 C  CD  . ARG   A 1 700 ? 12.026 44.158  2.487   1.00 19.01  ? 725  ARG   A CD  1 
ATOM   5279 N  NE  . ARG   A 1 700 ? 11.564 44.049  3.859   1.00 20.28  ? 725  ARG   A NE  1 
ATOM   5280 C  CZ  . ARG   A 1 700 ? 11.041 42.952  4.404   1.00 24.24  ? 725  ARG   A CZ  1 
ATOM   5281 N  NH1 . ARG   A 1 700 ? 10.881 41.853  3.679   1.00 25.45  ? 725  ARG   A NH1 1 
ATOM   5282 N  NH2 . ARG   A 1 700 ? 10.687 42.943  5.686   1.00 23.69  ? 725  ARG   A NH2 1 
ATOM   5283 N  N   . MET   A 1 701 ? 16.985 46.372  4.111   1.00 15.70  ? 726  MET   A N   1 
ATOM   5284 C  CA  . MET   A 1 701 ? 18.038 46.426  5.118   1.00 15.14  ? 726  MET   A CA  1 
ATOM   5285 C  C   . MET   A 1 701 ? 18.544 47.851  5.300   1.00 14.16  ? 726  MET   A C   1 
ATOM   5286 O  O   . MET   A 1 701 ? 18.828 48.281  6.439   1.00 14.43  ? 726  MET   A O   1 
ATOM   5287 C  CB  . MET   A 1 701 ? 19.192 45.474  4.771   1.00 15.93  ? 726  MET   A CB  1 
ATOM   5288 C  CG  . MET   A 1 701 ? 18.742 44.045  4.864   1.00 15.82  ? 726  MET   A CG  1 
ATOM   5289 S  SD  . MET   A 1 701 ? 20.107 42.852  4.714   1.00 19.90  ? 726  MET   A SD  1 
ATOM   5290 C  CE  . MET   A 1 701 ? 20.629 43.169  3.067   1.00 20.94  ? 726  MET   A CE  1 
ATOM   5291 N  N   . LEU   A 1 702 ? 18.661 48.616  4.202   1.00 14.83  ? 727  LEU   A N   1 
ATOM   5292 C  CA  . LEU   A 1 702 ? 19.080 50.001  4.300   1.00 14.40  ? 727  LEU   A CA  1 
ATOM   5293 C  C   . LEU   A 1 702 ? 18.057 50.815  5.086   1.00 14.54  ? 727  LEU   A C   1 
ATOM   5294 O  O   . LEU   A 1 702 ? 18.424 51.560  6.004   1.00 14.61  ? 727  LEU   A O   1 
ATOM   5295 C  CB  . LEU   A 1 702 ? 19.258 50.563  2.889   1.00 15.74  ? 727  LEU   A CB  1 
ATOM   5296 C  CG  . LEU   A 1 702 ? 19.707 52.014  2.806   1.00 15.46  ? 727  LEU   A CG  1 
ATOM   5297 C  CD1 . LEU   A 1 702 ? 21.043 52.256  3.522   1.00 15.90  ? 727  LEU   A CD1 1 
ATOM   5298 C  CD2 . LEU   A 1 702 ? 19.854 52.403  1.325   1.00 17.46  ? 727  LEU   A CD2 1 
ATOM   5299 N  N   . ARG   A 1 703 ? 16.781 50.628  4.780   1.00 14.00  ? 728  ARG   A N   1 
ATOM   5300 C  CA  . ARG   A 1 703 ? 15.738 51.352  5.513   1.00 14.28  ? 728  ARG   A CA  1 
ATOM   5301 C  C   . ARG   A 1 703 ? 15.797 51.091  7.004   1.00 14.46  ? 728  ARG   A C   1 
ATOM   5302 O  O   . ARG   A 1 703 ? 15.804 52.025  7.824   1.00 13.92  ? 728  ARG   A O   1 
ATOM   5303 C  CB  . ARG   A 1 703 ? 14.358 50.854  4.988   1.00 15.10  ? 728  ARG   A CB  1 
ATOM   5304 C  CG  . ARG   A 1 703 ? 13.168 51.355  5.808   1.00 14.96  ? 728  ARG   A CG  1 
ATOM   5305 C  CD  . ARG   A 1 703 ? 11.847 50.685  5.410   1.00 17.81  ? 728  ARG   A CD  1 
ATOM   5306 N  NE  . ARG   A 1 703 ? 11.491 51.054  4.041   1.00 16.41  ? 728  ARG   A NE  1 
ATOM   5307 C  CZ  . ARG   A 1 703 ? 11.400 50.201  3.015   1.00 18.89  ? 728  ARG   A CZ  1 
ATOM   5308 N  NH1 . ARG   A 1 703 ? 11.539 48.890  3.209   1.00 17.76  ? 728  ARG   A NH1 1 
ATOM   5309 N  NH2 . ARG   A 1 703 ? 11.166 50.655  1.788   1.00 19.50  ? 728  ARG   A NH2 1 
ATOM   5310 N  N   . SER   A 1 704 ? 15.831 49.807  7.373   1.00 13.83  ? 729  SER   A N   1 
ATOM   5311 C  CA  . SER   A 1 704 ? 15.786 49.460  8.808   1.00 14.15  ? 729  SER   A CA  1 
ATOM   5312 C  C   . SER   A 1 704 ? 16.941 50.059  9.570   1.00 14.16  ? 729  SER   A C   1 
ATOM   5313 O  O   . SER   A 1 704 ? 16.791 50.584  10.694  1.00 14.25  ? 729  SER   A O   1 
ATOM   5314 C  CB  . SER   A 1 704 ? 15.745 47.936  8.966   1.00 14.54  ? 729  SER   A CB  1 
ATOM   5315 O  OG  . SER   A 1 704 ? 15.701 47.535  10.337  1.00 15.84  ? 729  SER   A OG  1 
ATOM   5316 N  N   . GLN   A 1 705 ? 18.148 49.971  8.962   1.00 12.97  ? 730  GLN   A N   1 
ATOM   5317 C  CA  . GLN   A 1 705 ? 19.338 50.489  9.649   1.00 13.15  ? 730  GLN   A CA  1 
ATOM   5318 C  C   . GLN   A 1 705 ? 19.306 51.989  9.784   1.00 14.09  ? 730  GLN   A C   1 
ATOM   5319 O  O   . GLN   A 1 705 ? 19.677 52.528  10.849  1.00 14.53  ? 730  GLN   A O   1 
ATOM   5320 C  CB  . GLN   A 1 705 ? 20.597 50.050  8.863   1.00 14.14  ? 730  GLN   A CB  1 
ATOM   5321 C  CG  . GLN   A 1 705 ? 21.903 50.493  9.509   1.00 16.63  ? 730  GLN   A CG  1 
ATOM   5322 C  CD  . GLN   A 1 705 ? 22.128 49.796  10.812  1.00 23.23  ? 730  GLN   A CD  1 
ATOM   5323 O  OE1 . GLN   A 1 705 ? 22.417 48.598  10.871  1.00 27.52  ? 730  GLN   A OE1 1 
ATOM   5324 N  NE2 . GLN   A 1 705 ? 21.967 50.507  11.924  1.00 23.43  ? 730  GLN   A NE2 1 
ATOM   5325 N  N   . LEU   A 1 706 ? 18.847 52.686  8.742   1.00 13.17  ? 731  LEU   A N   1 
ATOM   5326 C  CA  . LEU   A 1 706 ? 18.811 54.135  8.785   1.00 13.62  ? 731  LEU   A CA  1 
ATOM   5327 C  C   . LEU   A 1 706 ? 17.777 54.631  9.763   1.00 13.64  ? 731  LEU   A C   1 
ATOM   5328 O  O   . LEU   A 1 706 ? 18.053 55.614  10.474  1.00 14.70  ? 731  LEU   A O   1 
ATOM   5329 C  CB  . LEU   A 1 706 ? 18.479 54.690  7.398   1.00 14.64  ? 731  LEU   A CB  1 
ATOM   5330 C  CG  . LEU   A 1 706 ? 19.593 54.591  6.360   1.00 16.58  ? 731  LEU   A CG  1 
ATOM   5331 C  CD1 . LEU   A 1 706 ? 19.079 55.043  5.033   1.00 16.66  ? 731  LEU   A CD1 1 
ATOM   5332 C  CD2 . LEU   A 1 706 ? 20.877 55.368  6.834   1.00 17.79  ? 731  LEU   A CD2 1 
ATOM   5333 N  N   . LEU   A 1 707 ? 16.587 54.019  9.790   1.00 13.55  ? 732  LEU   A N   1 
ATOM   5334 C  CA  . LEU   A 1 707 ? 15.568 54.499  10.748  1.00 13.53  ? 732  LEU   A CA  1 
ATOM   5335 C  C   . LEU   A 1 707 ? 16.028 54.239  12.175  1.00 14.08  ? 732  LEU   A C   1 
ATOM   5336 O  O   . LEU   A 1 707 ? 15.825 55.067  13.069  1.00 15.10  ? 732  LEU   A O   1 
ATOM   5337 C  CB  . LEU   A 1 707 ? 14.195 53.817  10.494  1.00 14.89  ? 732  LEU   A CB  1 
ATOM   5338 C  CG  . LEU   A 1 707 ? 13.578 54.159  9.133   1.00 16.67  ? 732  LEU   A CG  1 
ATOM   5339 C  CD1 . LEU   A 1 707 ? 12.252 53.423  8.927   1.00 17.96  ? 732  LEU   A CD1 1 
ATOM   5340 C  CD2 . LEU   A 1 707 ? 13.474 55.678  8.894   1.00 17.85  ? 732  LEU   A CD2 1 
ATOM   5341 N  N   . LEU   A 1 708 ? 16.668 53.089  12.425  1.00 14.13  ? 733  LEU   A N   1 
ATOM   5342 C  CA  . LEU   A 1 708 ? 17.147 52.794  13.791  1.00 14.09  ? 733  LEU   A CA  1 
ATOM   5343 C  C   . LEU   A 1 708 ? 18.227 53.810  14.178  1.00 15.12  ? 733  LEU   A C   1 
ATOM   5344 O  O   . LEU   A 1 708 ? 18.171 54.373  15.279  1.00 16.09  ? 733  LEU   A O   1 
ATOM   5345 C  CB  . LEU   A 1 708 ? 17.709 51.392  13.847  1.00 14.09  ? 733  LEU   A CB  1 
ATOM   5346 C  CG  . LEU   A 1 708 ? 18.336 51.012  15.196  1.00 14.97  ? 733  LEU   A CG  1 
ATOM   5347 C  CD1 . LEU   A 1 708 ? 17.307 51.070  16.355  1.00 16.17  ? 733  LEU   A CD1 1 
ATOM   5348 C  CD2 . LEU   A 1 708 ? 18.977 49.620  15.085  1.00 15.46  ? 733  LEU   A CD2 1 
ATOM   5349 N  N   . LEU   A 1 709 ? 19.164 54.086  13.261  1.00 13.81  ? 734  LEU   A N   1 
ATOM   5350 C  CA  . LEU   A 1 709 ? 20.241 55.055  13.542  1.00 13.98  ? 734  LEU   A CA  1 
ATOM   5351 C  C   . LEU   A 1 709 ? 19.641 56.427  13.860  1.00 14.92  ? 734  LEU   A C   1 
ATOM   5352 O  O   . LEU   A 1 709 ? 20.032 57.042  14.852  1.00 15.43  ? 734  LEU   A O   1 
ATOM   5353 C  CB  . LEU   A 1 709 ? 21.159 55.141  12.303  1.00 13.96  ? 734  LEU   A CB  1 
ATOM   5354 C  CG  . LEU   A 1 709 ? 22.255 56.189  12.445  1.00 14.85  ? 734  LEU   A CG  1 
ATOM   5355 C  CD1 . LEU   A 1 709 ? 23.350 55.696  13.403  1.00 16.11  ? 734  LEU   A CD1 1 
ATOM   5356 C  CD2 . LEU   A 1 709 ? 22.820 56.527  11.058  1.00 16.91  ? 734  LEU   A CD2 1 
ATOM   5357 N  N   . ALA   A 1 710 ? 18.716 56.894  13.026  1.00 14.44  ? 735  ALA   A N   1 
ATOM   5358 C  CA  . ALA   A 1 710 ? 18.100 58.204  13.250  1.00 15.91  ? 735  ALA   A CA  1 
ATOM   5359 C  C   . ALA   A 1 710 ? 17.382 58.269  14.585  1.00 16.77  ? 735  ALA   A C   1 
ATOM   5360 O  O   . ALA   A 1 710 ? 17.538 59.276  15.299  1.00 18.07  ? 735  ALA   A O   1 
ATOM   5361 C  CB  . ALA   A 1 710 ? 17.148 58.520  12.118  1.00 16.46  ? 735  ALA   A CB  1 
ATOM   5362 N  N   . CYS   A 1 711 ? 16.616 57.235  14.933  1.00 16.58  ? 736  CYS   A N   1 
ATOM   5363 C  CA  . CYS   A 1 711 ? 15.888 57.255  16.209  1.00 17.20  ? 736  CYS   A CA  1 
ATOM   5364 C  C   . CYS   A 1 711 ? 16.813 57.210  17.374  1.00 18.66  ? 736  CYS   A C   1 
ATOM   5365 O  O   . CYS   A 1 711 ? 16.565 57.893  18.373  1.00 19.42  ? 736  CYS   A O   1 
ATOM   5366 C  CB  . CYS   A 1 711 ? 14.882 56.125  16.267  1.00 16.14  ? 736  CYS   A CB  1 
ATOM   5367 S  SG  . CYS   A 1 711 ? 13.386 56.430  15.293  1.00 19.36  ? 736  CYS   A SG  1 
ATOM   5368 N  N   . VAL   A 1 712 ? 17.864 56.356  17.336  1.00 18.26  ? 737  VAL   A N   1 
ATOM   5369 C  CA  . VAL   A 1 712 ? 18.839 56.314  18.423  1.00 18.89  ? 737  VAL   A CA  1 
ATOM   5370 C  C   . VAL   A 1 712 ? 19.501 57.673  18.649  1.00 19.41  ? 737  VAL   A C   1 
ATOM   5371 O  O   . VAL   A 1 712 ? 19.792 58.025  19.808  1.00 21.25  ? 737  VAL   A O   1 
ATOM   5372 C  CB  . VAL   A 1 712 ? 19.862 55.202  18.091  1.00 20.84  ? 737  VAL   A CB  1 
ATOM   5373 C  CG1 . VAL   A 1 712 ? 21.201 55.386  18.828  1.00 23.19  ? 737  VAL   A CG1 1 
ATOM   5374 C  CG2 . VAL   A 1 712 ? 19.233 53.846  18.366  1.00 20.85  ? 737  VAL   A CG2 1 
ATOM   5375 N  N   . HIS   A 1 713 ? 19.691 58.454  17.597  1.00 19.24  ? 738  HIS   A N   1 
ATOM   5376 C  CA  . HIS   A 1 713 ? 20.331 59.754  17.736  1.00 20.32  ? 738  HIS   A CA  1 
ATOM   5377 C  C   . HIS   A 1 713 ? 19.335 60.933  17.898  1.00 21.80  ? 738  HIS   A C   1 
ATOM   5378 O  O   . HIS   A 1 713 ? 19.706 62.093  17.655  1.00 22.75  ? 738  HIS   A O   1 
ATOM   5379 C  CB  . HIS   A 1 713 ? 21.345 59.978  16.623  1.00 21.38  ? 738  HIS   A CB  1 
ATOM   5380 C  CG  . HIS   A 1 713 ? 22.485 59.018  16.777  1.00 23.06  ? 738  HIS   A CG  1 
ATOM   5381 N  ND1 . HIS   A 1 713 ? 23.164 58.882  18.000  1.00 27.03  ? 738  HIS   A ND1 1 
ATOM   5382 C  CD2 . HIS   A 1 713 ? 22.913 58.041  15.947  1.00 21.00  ? 738  HIS   A CD2 1 
ATOM   5383 C  CE1 . HIS   A 1 713 ? 24.038 57.906  17.814  1.00 26.23  ? 738  HIS   A CE1 1 
ATOM   5384 N  NE2 . HIS   A 1 713 ? 23.949 57.405  16.573  1.00 21.76  ? 738  HIS   A NE2 1 
ATOM   5385 N  N   A ASN   A 1 714 ? 18.084 60.599  18.248  0.50 21.43  ? 739  ASN   A N   1 
ATOM   5386 N  N   B ASN   A 1 714 ? 18.100 60.647  18.275  0.50 21.53  ? 739  ASN   A N   1 
ATOM   5387 C  CA  A ASN   A 1 714 ? 16.972 61.497  18.586  0.50 22.28  ? 739  ASN   A CA  1 
ATOM   5388 C  CA  B ASN   A 1 714 ? 17.137 61.721  18.560  0.50 22.24  ? 739  ASN   A CA  1 
ATOM   5389 C  C   A ASN   A 1 714 ? 16.576 62.434  17.468  0.50 23.27  ? 739  ASN   A C   1 
ATOM   5390 C  C   B ASN   A 1 714 ? 16.825 62.608  17.368  0.50 23.64  ? 739  ASN   A C   1 
ATOM   5391 O  O   A ASN   A 1 714 ? 16.056 63.519  17.744  0.50 23.08  ? 739  ASN   A O   1 
ATOM   5392 O  O   B ASN   A 1 714 ? 16.655 63.837  17.510  0.50 23.84  ? 739  ASN   A O   1 
ATOM   5393 C  CB  A ASN   A 1 714 ? 17.264 62.258  19.882  0.50 24.67  ? 739  ASN   A CB  1 
ATOM   5394 C  CB  B ASN   A 1 714 ? 17.638 62.566  19.734  0.50 24.04  ? 739  ASN   A CB  1 
ATOM   5395 C  CG  A ASN   A 1 714 ? 17.730 61.356  20.996  0.50 27.16  ? 739  ASN   A CG  1 
ATOM   5396 C  CG  B ASN   A 1 714 ? 16.523 63.340  20.365  0.50 26.61  ? 739  ASN   A CG  1 
ATOM   5397 O  OD1 A ASN   A 1 714 ? 18.908 61.324  21.356  0.50 30.12  ? 739  ASN   A OD1 1 
ATOM   5398 O  OD1 B ASN   A 1 714 ? 15.406 62.848  20.450  0.50 27.79  ? 739  ASN   A OD1 1 
ATOM   5399 N  ND2 A ASN   A 1 714 ? 16.838 60.558  21.533  0.50 26.43  ? 739  ASN   A ND2 1 
ATOM   5400 N  ND2 B ASN   A 1 714 ? 16.795 64.584  20.763  0.50 27.86  ? 739  ASN   A ND2 1 
ATOM   5401 N  N   . TYR   A 1 715 ? 16.744 62.005  16.188  1.00 23.00  ? 740  TYR   A N   1 
ATOM   5402 C  CA  . TYR   A 1 715 ? 16.338 62.777  14.999  1.00 22.21  ? 740  TYR   A CA  1 
ATOM   5403 C  C   . TYR   A 1 715 ? 14.809 62.851  15.092  1.00 24.12  ? 740  TYR   A C   1 
ATOM   5404 O  O   . TYR   A 1 715 ? 14.109 61.844  14.964  1.00 24.08  ? 740  TYR   A O   1 
ATOM   5405 C  CB  . TYR   A 1 715 ? 16.761 62.078  13.717  1.00 21.23  ? 740  TYR   A CB  1 
ATOM   5406 C  CG  . TYR   A 1 715 ? 16.377 62.840  12.470  1.00 20.84  ? 740  TYR   A CG  1 
ATOM   5407 C  CD1 . TYR   A 1 715 ? 16.758 64.167  12.292  1.00 21.69  ? 740  TYR   A CD1 1 
ATOM   5408 C  CD2 . TYR   A 1 715 ? 15.608 62.249  11.483  1.00 20.22  ? 740  TYR   A CD2 1 
ATOM   5409 C  CE1 . TYR   A 1 715 ? 16.426 64.861  11.131  1.00 22.75  ? 740  TYR   A CE1 1 
ATOM   5410 C  CE2 . TYR   A 1 715 ? 15.263 62.933  10.326  1.00 21.51  ? 740  TYR   A CE2 1 
ATOM   5411 C  CZ  . TYR   A 1 715 ? 15.641 64.254  10.166  1.00 22.41  ? 740  TYR   A CZ  1 
ATOM   5412 O  OH  . TYR   A 1 715 ? 15.296 64.935  9.019   1.00 23.34  ? 740  TYR   A OH  1 
ATOM   5413 N  N   . GLN   A 1 716 ? 14.302 64.024  15.539  1.00 24.19  ? 741  GLN   A N   1 
ATOM   5414 C  CA  . GLN   A 1 716 ? 12.890 64.157  15.875  1.00 25.17  ? 741  GLN   A CA  1 
ATOM   5415 C  C   . GLN   A 1 716 ? 11.885 63.709  14.840  1.00 23.65  ? 741  GLN   A C   1 
ATOM   5416 O  O   . GLN   A 1 716 ? 10.939 63.044  15.265  1.00 24.28  ? 741  GLN   A O   1 
ATOM   5417 C  CB  . GLN   A 1 716 ? 12.569 65.595  16.337  1.00 27.74  ? 741  GLN   A CB  1 
ATOM   5418 C  CG  . GLN   A 1 716 ? 13.115 65.803  17.763  1.00 34.38  ? 741  GLN   A CG  1 
ATOM   5419 C  CD  . GLN   A 1 716 ? 12.586 64.788  18.779  1.00 42.32  ? 741  GLN   A CD  1 
ATOM   5420 O  OE1 . GLN   A 1 716 ? 13.345 64.048  19.427  1.00 43.33  ? 741  GLN   A OE1 1 
ATOM   5421 N  NE2 . GLN   A 1 716 ? 11.264 64.703  18.906  1.00 44.57  ? 741  GLN   A NE2 1 
ATOM   5422 N  N   . PRO   A 1 717 ? 12.045 63.907  13.516  1.00 23.78  ? 742  PRO   A N   1 
ATOM   5423 C  CA  . PRO   A 1 717 ? 11.048 63.353  12.580  1.00 23.92  ? 742  PRO   A CA  1 
ATOM   5424 C  C   . PRO   A 1 717 ? 10.887 61.841  12.703  1.00 23.62  ? 742  PRO   A C   1 
ATOM   5425 O  O   . PRO   A 1 717 ? 9.769  61.306  12.647  1.00 24.46  ? 742  PRO   A O   1 
ATOM   5426 C  CB  . PRO   A 1 717 ? 11.579 63.762  11.208  1.00 25.39  ? 742  PRO   A CB  1 
ATOM   5427 C  CG  . PRO   A 1 717 ? 12.339 65.023  11.496  1.00 26.21  ? 742  PRO   A CG  1 
ATOM   5428 C  CD  . PRO   A 1 717 ? 13.049 64.711  12.797  1.00 24.14  ? 742  PRO   A CD  1 
ATOM   5429 N  N   . CYS   A 1 718 ? 12.011 61.138  12.903  1.00 22.53  ? 743  CYS   A N   1 
ATOM   5430 C  CA  . CYS   A 1 718 ? 11.927 59.695  13.031  1.00 22.37  ? 743  CYS   A CA  1 
ATOM   5431 C  C   . CYS   A 1 718 ? 11.444 59.283  14.433  1.00 21.39  ? 743  CYS   A C   1 
ATOM   5432 O  O   . CYS   A 1 718 ? 10.575 58.413  14.533  1.00 21.35  ? 743  CYS   A O   1 
ATOM   5433 C  CB  . CYS   A 1 718 ? 13.250 59.056  12.611  1.00 22.79  ? 743  CYS   A CB  1 
ATOM   5434 S  SG  . CYS   A 1 718 ? 13.594 59.188  10.811  1.00 27.07  ? 743  CYS   A SG  1 
ATOM   5435 N  N   . VAL   A 1 719 ? 11.911 59.952  15.501  1.00 20.68  ? 744  VAL   A N   1 
ATOM   5436 C  CA  . VAL   A 1 719 ? 11.440 59.630  16.858  1.00 21.15  ? 744  VAL   A CA  1 
ATOM   5437 C  C   . VAL   A 1 719 ? 9.914  59.800  16.981  1.00 22.67  ? 744  VAL   A C   1 
ATOM   5438 O  O   . VAL   A 1 719 ? 9.222  58.919  17.499  1.00 22.87  ? 744  VAL   A O   1 
ATOM   5439 C  CB  . VAL   A 1 719 ? 12.163 60.459  17.945  1.00 23.59  ? 744  VAL   A CB  1 
ATOM   5440 C  CG1 . VAL   A 1 719 ? 11.620 60.127  19.342  1.00 24.35  ? 744  VAL   A CG1 1 
ATOM   5441 C  CG2 . VAL   A 1 719 ? 13.666 60.215  17.902  1.00 24.67  ? 744  VAL   A CG2 1 
ATOM   5442 N  N   . GLN   A 1 720 ? 9.380  60.889  16.399  1.00 23.07  ? 745  GLN   A N   1 
ATOM   5443 C  CA  . GLN   A 1 720 ? 7.944  61.144  16.517  1.00 24.46  ? 745  GLN   A CA  1 
ATOM   5444 C  C   . GLN   A 1 720 ? 7.124  60.084  15.805  1.00 23.25  ? 745  GLN   A C   1 
ATOM   5445 O  O   . GLN   A 1 720 ? 6.093  59.622  16.325  1.00 23.15  ? 745  GLN   A O   1 
ATOM   5446 C  CB  . GLN   A 1 720 ? 7.623  62.567  16.071  1.00 28.33  ? 745  GLN   A CB  1 
ATOM   5447 C  CG  . GLN   A 1 720 ? 8.226  63.599  17.028  1.00 37.43  ? 745  GLN   A CG  1 
ATOM   5448 C  CD  . GLN   A 1 720 ? 7.699  63.474  18.453  1.00 48.69  ? 745  GLN   A CD  1 
ATOM   5449 O  OE1 . GLN   A 1 720 ? 6.522  63.154  18.692  1.00 52.72  ? 745  GLN   A OE1 1 
ATOM   5450 N  NE2 . GLN   A 1 720 ? 8.558  63.715  19.440  1.00 50.81  ? 745  GLN   A NE2 1 
ATOM   5451 N  N   . ARG   A 1 721 ? 7.605  59.658  14.620  1.00 22.09  ? 746  ARG   A N   1 
ATOM   5452 C  CA  . ARG   A 1 721 ? 6.932  58.646  13.876  1.00 21.94  ? 746  ARG   A CA  1 
ATOM   5453 C  C   . ARG   A 1 721 ? 6.985  57.302  14.638  1.00 20.59  ? 746  ARG   A C   1 
ATOM   5454 O  O   . ARG   A 1 721 ? 5.989  56.566  14.735  1.00 21.04  ? 746  ARG   A O   1 
ATOM   5455 C  CB  . ARG   A 1 721 ? 7.602  58.513  12.523  1.00 26.05  ? 746  ARG   A CB  1 
ATOM   5456 C  CG  . ARG   A 1 721 ? 6.783  57.762  11.542  1.00 32.67  ? 746  ARG   A CG  1 
ATOM   5457 C  CD  . ARG   A 1 721 ? 6.806  58.565  10.275  1.00 37.84  ? 746  ARG   A CD  1 
ATOM   5458 N  NE  . ARG   A 1 721 ? 6.047  57.891  9.231   1.00 41.09  ? 746  ARG   A NE  1 
ATOM   5459 C  CZ  . ARG   A 1 721 ? 6.298  58.003  7.934   1.00 42.59  ? 746  ARG   A CZ  1 
ATOM   5460 N  NH1 . ARG   A 1 721 ? 7.306  58.758  7.507   1.00 42.56  ? 746  ARG   A NH1 1 
ATOM   5461 N  NH2 . ARG   A 1 721 ? 5.557  57.352  7.055   1.00 42.36  ? 746  ARG   A NH2 1 
ATOM   5462 N  N   . ALA   A 1 722 ? 8.172  56.986  15.208  1.00 19.49  ? 747  ALA   A N   1 
ATOM   5463 C  CA  . ALA   A 1 722 ? 8.334  55.748  15.953  1.00 18.57  ? 747  ALA   A CA  1 
ATOM   5464 C  C   . ALA   A 1 722 ? 7.466  55.715  17.226  1.00 19.96  ? 747  ALA   A C   1 
ATOM   5465 O  O   . ALA   A 1 722 ? 6.883  54.675  17.566  1.00 19.39  ? 747  ALA   A O   1 
ATOM   5466 C  CB  . ALA   A 1 722 ? 9.812  55.558  16.310  1.00 19.30  ? 747  ALA   A CB  1 
ATOM   5467 N  N   . GLU   A 1 723 ? 7.379  56.840  17.905  1.00 20.94  ? 748  GLU   A N   1 
ATOM   5468 C  CA  . GLU   A 1 723 ? 6.551  56.943  19.108  1.00 22.01  ? 748  GLU   A CA  1 
ATOM   5469 C  C   . GLU   A 1 723 ? 5.076  56.698  18.778  1.00 23.13  ? 748  GLU   A C   1 
ATOM   5470 O  O   . GLU   A 1 723 ? 4.380  56.044  19.558  1.00 24.05  ? 748  GLU   A O   1 
ATOM   5471 C  CB  . GLU   A 1 723 ? 6.677  58.335  19.719  1.00 25.57  ? 748  GLU   A CB  1 
ATOM   5472 C  CG  . GLU   A 1 723 ? 7.964  58.593  20.463  1.00 31.53  ? 748  GLU   A CG  1 
ATOM   5473 C  CD  . GLU   A 1 723 ? 8.105  59.996  21.031  1.00 42.57  ? 748  GLU   A CD  1 
ATOM   5474 O  OE1 . GLU   A 1 723 ? 7.280  60.871  20.680  1.00 45.04  ? 748  GLU   A OE1 1 
ATOM   5475 O  OE2 . GLU   A 1 723 ? 9.069  60.229  21.797  1.00 46.61  ? 748  GLU   A OE2 1 
ATOM   5476 N  N   . GLY   A 1 724 ? 4.623  57.185  17.614  1.00 23.57  ? 749  GLY   A N   1 
ATOM   5477 C  CA  . GLY   A 1 724 ? 3.238  57.007  17.184  1.00 22.84  ? 749  GLY   A CA  1 
ATOM   5478 C  C   . GLY   A 1 724 ? 2.932  55.571  16.866  1.00 21.90  ? 749  GLY   A C   1 
ATOM   5479 O  O   . GLY   A 1 724 ? 1.919  55.042  17.306  1.00 23.57  ? 749  GLY   A O   1 
ATOM   5480 N  N   . TYR   A 1 725 ? 3.855  54.861  16.153  1.00 20.25  ? 750  TYR   A N   1 
ATOM   5481 C  CA  . TYR   A 1 725 ? 3.656  53.455  15.897  1.00 20.76  ? 750  TYR   A CA  1 
ATOM   5482 C  C   . TYR   A 1 725 ? 3.667  52.690  17.219  1.00 20.52  ? 750  TYR   A C   1 
ATOM   5483 O  O   . TYR   A 1 725 ? 2.866  51.792  17.383  1.00 22.34  ? 750  TYR   A O   1 
ATOM   5484 C  CB  . TYR   A 1 725 ? 4.769  52.929  15.002  1.00 21.30  ? 750  TYR   A CB  1 
ATOM   5485 C  CG  . TYR   A 1 725 ? 4.474  53.016  13.520  1.00 21.83  ? 750  TYR   A CG  1 
ATOM   5486 C  CD1 . TYR   A 1 725 ? 3.559  52.155  12.923  1.00 23.74  ? 750  TYR   A CD1 1 
ATOM   5487 C  CD2 . TYR   A 1 725 ? 5.191  53.872  12.700  1.00 22.76  ? 750  TYR   A CD2 1 
ATOM   5488 C  CE1 . TYR   A 1 725 ? 3.307  52.209  11.555  1.00 25.86  ? 750  TYR   A CE1 1 
ATOM   5489 C  CE2 . TYR   A 1 725 ? 4.921  53.963  11.344  1.00 25.11  ? 750  TYR   A CE2 1 
ATOM   5490 C  CZ  . TYR   A 1 725 ? 3.989  53.119  10.772  1.00 27.54  ? 750  TYR   A CZ  1 
ATOM   5491 O  OH  . TYR   A 1 725 ? 3.780  53.199  9.410   1.00 31.99  ? 750  TYR   A OH  1 
ATOM   5492 N  N   . PHE   A 1 726 ? 4.621  53.006  18.141  1.00 19.32  ? 751  PHE   A N   1 
ATOM   5493 C  CA  . PHE   A 1 726 ? 4.682  52.241  19.389  1.00 19.32  ? 751  PHE   A CA  1 
ATOM   5494 C  C   . PHE   A 1 726 ? 3.410  52.409  20.218  1.00 20.93  ? 751  PHE   A C   1 
ATOM   5495 O  O   . PHE   A 1 726 ? 2.894  51.414  20.717  1.00 20.51  ? 751  PHE   A O   1 
ATOM   5496 C  CB  . PHE   A 1 726 ? 5.914  52.643  20.223  1.00 18.42  ? 751  PHE   A CB  1 
ATOM   5497 C  CG  . PHE   A 1 726 ? 6.122  51.693  21.375  1.00 17.74  ? 751  PHE   A CG  1 
ATOM   5498 C  CD1 . PHE   A 1 726 ? 6.770  50.475  21.185  1.00 17.27  ? 751  PHE   A CD1 1 
ATOM   5499 C  CD2 . PHE   A 1 726 ? 5.660  52.005  22.652  1.00 18.57  ? 751  PHE   A CD2 1 
ATOM   5500 C  CE1 . PHE   A 1 726 ? 6.960  49.588  22.249  1.00 18.64  ? 751  PHE   A CE1 1 
ATOM   5501 C  CE2 . PHE   A 1 726 ? 5.846  51.117  23.708  1.00 19.12  ? 751  PHE   A CE2 1 
ATOM   5502 C  CZ  . PHE   A 1 726 ? 6.521  49.925  23.506  1.00 19.00  ? 751  PHE   A CZ  1 
ATOM   5503 N  N   . ARG   A 1 727 ? 2.909  53.647  20.311  1.00 21.79  ? 752  ARG   A N   1 
ATOM   5504 C  CA  . ARG   A 1 727 ? 1.684  53.942  21.081  1.00 24.28  ? 752  ARG   A CA  1 
ATOM   5505 C  C   . ARG   A 1 727 ? 0.518  53.195  20.475  1.00 25.59  ? 752  ARG   A C   1 
ATOM   5506 O  O   . ARG   A 1 727 ? -0.170 52.468  21.190  1.00 26.46  ? 752  ARG   A O   1 
ATOM   5507 C  CB  . ARG   A 1 727 ? 1.446  55.444  21.063  1.00 26.54  ? 752  ARG   A CB  1 
ATOM   5508 C  CG  . ARG   A 1 727 ? 0.196  55.906  21.848  1.00 31.73  ? 752  ARG   A CG  1 
ATOM   5509 C  CD  . ARG   A 1 727 ? 0.101  57.414  21.798  1.00 37.76  ? 752  ARG   A CD  1 
ATOM   5510 N  NE  . ARG   A 1 727 ? -0.198 57.886  20.442  1.00 44.64  ? 752  ARG   A NE  1 
ATOM   5511 C  CZ  . ARG   A 1 727 ? 0.604  58.654  19.713  1.00 48.54  ? 752  ARG   A CZ  1 
ATOM   5512 N  NH1 . ARG   A 1 727 ? 1.784  59.036  20.188  1.00 48.79  ? 752  ARG   A NH1 1 
ATOM   5513 N  NH2 . ARG   A 1 727 ? 0.241  59.029  18.493  1.00 49.42  ? 752  ARG   A NH2 1 
ATOM   5514 N  N   . LYS   A 1 728 ? 0.371  53.253  19.149  1.00 26.21  ? 753  LYS   A N   1 
ATOM   5515 C  CA  . LYS   A 1 728 ? -0.733 52.547  18.481  1.00 27.51  ? 753  LYS   A CA  1 
ATOM   5516 C  C   . LYS   A 1 728 ? -0.630 51.042  18.612  1.00 26.45  ? 753  LYS   A C   1 
ATOM   5517 O  O   . LYS   A 1 728 ? -1.625 50.345  18.901  1.00 28.30  ? 753  LYS   A O   1 
ATOM   5518 C  CB  . LYS   A 1 728 ? -0.836 53.000  17.022  1.00 30.97  ? 753  LYS   A CB  1 
ATOM   5519 C  CG  . LYS   A 1 728 ? -1.235 54.476  16.932  1.00 37.78  ? 753  LYS   A CG  1 
ATOM   5520 C  CD  . LYS   A 1 728 ? -1.234 54.981  15.498  1.00 44.61  ? 753  LYS   A CD  1 
ATOM   5521 C  CE  . LYS   A 1 728 ? -1.233 56.491  15.419  1.00 48.87  ? 753  LYS   A CE  1 
ATOM   5522 N  NZ  . LYS   A 1 728 ? -1.063 56.950  14.012  1.00 51.44  ? 753  LYS   A NZ  1 
ATOM   5523 N  N   . TRP   A 1 729 ? 0.604  50.512  18.516  1.00 24.31  ? 754  TRP   A N   1 
ATOM   5524 C  CA  . TRP   A 1 729 ? 0.821  49.108  18.679  1.00 23.40  ? 754  TRP   A CA  1 
ATOM   5525 C  C   . TRP   A 1 729 ? 0.478  48.687  20.145  1.00 24.98  ? 754  TRP   A C   1 
ATOM   5526 O  O   . TRP   A 1 729 ? -0.291 47.750  20.364  1.00 26.05  ? 754  TRP   A O   1 
ATOM   5527 C  CB  . TRP   A 1 729 ? 2.286  48.809  18.353  1.00 23.76  ? 754  TRP   A CB  1 
ATOM   5528 C  CG  . TRP   A 1 729 ? 2.637  47.388  18.518  1.00 23.96  ? 754  TRP   A CG  1 
ATOM   5529 C  CD1 . TRP   A 1 729 ? 2.320  46.372  17.670  1.00 25.21  ? 754  TRP   A CD1 1 
ATOM   5530 C  CD2 . TRP   A 1 729 ? 3.521  46.839  19.494  1.00 23.58  ? 754  TRP   A CD2 1 
ATOM   5531 N  NE1 . TRP   A 1 729 ? 2.892  45.208  18.097  1.00 25.35  ? 754  TRP   A NE1 1 
ATOM   5532 C  CE2 . TRP   A 1 729 ? 3.637  45.461  19.224  1.00 25.08  ? 754  TRP   A CE2 1 
ATOM   5533 C  CE3 . TRP   A 1 729 ? 4.201  47.370  20.603  1.00 24.22  ? 754  TRP   A CE3 1 
ATOM   5534 C  CZ2 . TRP   A 1 729 ? 4.392  44.606  20.017  1.00 25.09  ? 754  TRP   A CZ2 1 
ATOM   5535 C  CZ3 . TRP   A 1 729 ? 4.965  46.513  21.385  1.00 24.43  ? 754  TRP   A CZ3 1 
ATOM   5536 C  CH2 . TRP   A 1 729 ? 5.064  45.155  21.082  1.00 24.89  ? 754  TRP   A CH2 1 
ATOM   5537 N  N   . LYS   A 1 730 ? 0.979  49.429  21.142  1.00 23.56  ? 755  LYS   A N   1 
ATOM   5538 C  CA  . LYS   A 1 730 ? 0.729  49.113  22.543  1.00 24.31  ? 755  LYS   A CA  1 
ATOM   5539 C  C   . LYS   A 1 730 ? -0.785 49.233  22.879  1.00 26.00  ? 755  LYS   A C   1 
ATOM   5540 O  O   . LYS   A 1 730 ? -1.329 48.334  23.532  1.00 26.25  ? 755  LYS   A O   1 
ATOM   5541 C  CB  . LYS   A 1 730 ? 1.537  50.068  23.425  1.00 24.66  ? 755  LYS   A CB  1 
ATOM   5542 C  CG  . LYS   A 1 730 ? 1.444  49.761  24.913  1.00 27.84  ? 755  LYS   A CG  1 
ATOM   5543 C  CD  . LYS   A 1 730 ? 2.448  50.634  25.668  1.00 30.57  ? 755  LYS   A CD  1 
ATOM   5544 C  CE  . LYS   A 1 730 ? 2.242  50.582  27.167  1.00 34.54  ? 755  LYS   A CE  1 
ATOM   5545 N  NZ  . LYS   A 1 730 ? 1.088  51.429  27.572  1.00 36.27  ? 755  LYS   A NZ  1 
ATOM   5546 N  N   . GLU   A 1 731 ? -1.442 50.281  22.394  1.00 27.04  ? 756  GLU   A N   1 
ATOM   5547 C  CA  . GLU   A 1 731 ? -2.890 50.490  22.651  1.00 28.06  ? 756  GLU   A CA  1 
ATOM   5548 C  C   . GLU   A 1 731 ? -3.748 49.413  22.021  1.00 29.92  ? 756  GLU   A C   1 
ATOM   5549 O  O   . GLU   A 1 731 ? -4.837 49.112  22.535  1.00 30.14  ? 756  GLU   A O   1 
ATOM   5550 C  CB  . GLU   A 1 731 ? -3.328 51.900  22.234  1.00 30.51  ? 756  GLU   A CB  1 
ATOM   5551 C  CG  . GLU   A 1 731 ? -2.800 52.935  23.211  1.00 36.04  ? 756  GLU   A CG  1 
ATOM   5552 C  CD  . GLU   A 1 731 ? -3.091 54.378  22.850  1.00 42.48  ? 756  GLU   A CD  1 
ATOM   5553 O  OE1 . GLU   A 1 731 ? -3.474 54.639  21.687  1.00 44.53  ? 756  GLU   A OE1 1 
ATOM   5554 O  OE2 . GLU   A 1 731 ? -2.907 55.254  23.725  1.00 44.13  ? 756  GLU   A OE2 1 
ATOM   5555 N  N   . SER   A 1 732 ? -3.275 48.815  20.924  1.00 30.04  ? 757  SER   A N   1 
ATOM   5556 C  CA  . SER   A 1 732 ? -3.958 47.702  20.277  1.00 30.94  ? 757  SER   A CA  1 
ATOM   5557 C  C   . SER   A 1 732 ? -3.620 46.362  20.957  1.00 31.29  ? 757  SER   A C   1 
ATOM   5558 O  O   . SER   A 1 732 ? -3.998 45.319  20.444  1.00 32.01  ? 757  SER   A O   1 
ATOM   5559 C  CB  . SER   A 1 732 ? -3.588 47.636  18.799  1.00 32.08  ? 757  SER   A CB  1 
ATOM   5560 O  OG  . SER   A 1 732 ? -2.284 47.098  18.620  1.00 33.82  ? 757  SER   A OG  1 
ATOM   5561 N  N   . ASN   A 1 733 ? -2.868 46.381  22.085  1.00 31.11  ? 758  ASN   A N   1 
ATOM   5562 C  CA  . ASN   A 1 733 ? -2.364 45.217  22.794  1.00 32.91  ? 758  ASN   A CA  1 
ATOM   5563 C  C   . ASN   A 1 733 ? -1.472 44.366  21.886  1.00 36.13  ? 758  ASN   A C   1 
ATOM   5564 O  O   . ASN   A 1 733 ? -1.496 43.139  21.945  1.00 36.45  ? 758  ASN   A O   1 
ATOM   5565 C  CB  . ASN   A 1 733 ? -3.485 44.378  23.439  1.00 33.79  ? 758  ASN   A CB  1 
ATOM   5566 C  CG  . ASN   A 1 733 ? -2.937 43.356  24.398  1.00 37.54  ? 758  ASN   A CG  1 
ATOM   5567 O  OD1 . ASN   A 1 733 ? -1.833 43.511  24.942  1.00 38.78  ? 758  ASN   A OD1 1 
ATOM   5568 N  ND2 . ASN   A 1 733 ? -3.667 42.267  24.601  1.00 38.09  ? 758  ASN   A ND2 1 
ATOM   5569 N  N   . GLY   A 1 734 ? -0.707 45.030  21.022  1.00 38.08  ? 759  GLY   A N   1 
ATOM   5570 C  CA  . GLY   A 1 734 ? 0.186  44.343  20.104  1.00 40.96  ? 759  GLY   A CA  1 
ATOM   5571 C  C   . GLY   A 1 734 ? -0.501 43.666  18.938  1.00 44.26  ? 759  GLY   A C   1 
ATOM   5572 O  O   . GLY   A 1 734 ? 0.171  43.001  18.150  1.00 45.00  ? 759  GLY   A O   1 
ATOM   5573 N  N   . GLN   A 1 735 ? -1.842 43.826  18.779  1.00 45.80  ? 760  GLN   A N   1 
ATOM   5574 C  CA  . GLN   A 1 735 ? -2.549 43.202  17.648  1.00 47.55  ? 760  GLN   A CA  1 
ATOM   5575 C  C   . GLN   A 1 735 ? -1.968 43.687  16.322  1.00 48.37  ? 760  GLN   A C   1 
ATOM   5576 O  O   . GLN   A 1 735 ? -1.407 42.873  15.591  1.00 49.43  ? 760  GLN   A O   1 
ATOM   5577 C  CB  . GLN   A 1 735 ? -4.080 43.431  17.707  1.00 49.27  ? 760  GLN   A CB  1 
ATOM   5578 C  CG  . GLN   A 1 735 ? -4.763 42.598  18.769  1.00 53.64  ? 760  GLN   A CG  1 
ATOM   5579 C  CD  . GLN   A 1 735 ? -6.139 42.160  18.349  1.00 57.91  ? 760  GLN   A CD  1 
ATOM   5580 O  OE1 . GLN   A 1 735 ? -6.418 40.964  18.226  1.00 58.45  ? 760  GLN   A OE1 1 
ATOM   5581 N  NE2 . GLN   A 1 735 ? -7.027 43.121  18.115  1.00 59.82  ? 760  GLN   A NE2 1 
ATOM   5582 N  N   . LEU   A 1 736 ? -1.968 45.025  16.120  1.00 47.68  ? 761  LEU   A N   1 
ATOM   5583 C  CA  . LEU   A 1 736 ? -1.446 45.773  14.977  1.00 47.72  ? 761  LEU   A CA  1 
ATOM   5584 C  C   . LEU   A 1 736 ? -0.113 45.227  14.436  1.00 45.52  ? 761  LEU   A C   1 
ATOM   5585 O  O   . LEU   A 1 736 ? 0.873  45.234  15.150  1.00 46.31  ? 761  LEU   A O   1 
ATOM   5586 C  CB  . LEU   A 1 736 ? -1.239 47.233  15.429  1.00 48.85  ? 761  LEU   A CB  1 
ATOM   5587 C  CG  . LEU   A 1 736 ? -0.896 48.273  14.374  1.00 51.76  ? 761  LEU   A CG  1 
ATOM   5588 C  CD1 . LEU   A 1 736 ? -2.110 49.132  14.046  1.00 52.89  ? 761  LEU   A CD1 1 
ATOM   5589 C  CD2 . LEU   A 1 736 ? 0.188  49.197  14.871  1.00 52.71  ? 761  LEU   A CD2 1 
ATOM   5590 N  N   . SER   A 1 737 ? -0.097 44.712  13.197  1.00 42.83  ? 762  SER   A N   1 
ATOM   5591 C  CA  . SER   A 1 737 ? 1.149  44.274  12.572  1.00 39.86  ? 762  SER   A CA  1 
ATOM   5592 C  C   . SER   A 1 737 ? 1.886  45.558  12.150  1.00 35.86  ? 762  SER   A C   1 
ATOM   5593 O  O   . SER   A 1 737 ? 1.311  46.471  11.560  1.00 36.84  ? 762  SER   A O   1 
ATOM   5594 C  CB  . SER   A 1 737 ? 0.886  43.401  11.346  1.00 41.96  ? 762  SER   A CB  1 
ATOM   5595 O  OG  . SER   A 1 737 ? 0.819  42.017  11.651  1.00 44.95  ? 762  SER   A OG  1 
ATOM   5596 N  N   . LEU   A 1 738 ? 3.094  45.686  12.612  1.00 30.65  ? 763  LEU   A N   1 
ATOM   5597 C  CA  . LEU   A 1 738 ? 3.954  46.822  12.283  1.00 26.74  ? 763  LEU   A CA  1 
ATOM   5598 C  C   . LEU   A 1 738 ? 4.758  46.388  11.098  1.00 22.62  ? 763  LEU   A C   1 
ATOM   5599 O  O   . LEU   A 1 738 ? 5.113  45.195  11.016  1.00 23.57  ? 763  LEU   A O   1 
ATOM   5600 C  CB  . LEU   A 1 738 ? 4.961  46.976  13.421  1.00 27.39  ? 763  LEU   A CB  1 
ATOM   5601 C  CG  . LEU   A 1 738 ? 4.443  47.485  14.730  1.00 29.18  ? 763  LEU   A CG  1 
ATOM   5602 C  CD1 . LEU   A 1 738 ? 5.514  47.321  15.826  1.00 29.46  ? 763  LEU   A CD1 1 
ATOM   5603 C  CD2 . LEU   A 1 738 ? 4.047  48.925  14.598  1.00 30.32  ? 763  LEU   A CD2 1 
ATOM   5604 N  N   . PRO   A 1 739 ? 5.254  47.323  10.243  1.00 20.18  ? 764  PRO   A N   1 
ATOM   5605 C  CA  . PRO   A 1 739 ? 6.206  46.891  9.215   1.00 18.31  ? 764  PRO   A CA  1 
ATOM   5606 C  C   . PRO   A 1 739 ? 7.443  46.333  9.915   1.00 17.94  ? 764  PRO   A C   1 
ATOM   5607 O  O   . PRO   A 1 739 ? 7.937  46.947  10.878  1.00 17.34  ? 764  PRO   A O   1 
ATOM   5608 C  CB  . PRO   A 1 739 ? 6.513  48.190  8.442   1.00 19.37  ? 764  PRO   A CB  1 
ATOM   5609 C  CG  . PRO   A 1 739 ? 5.272  49.086  8.716   1.00 20.44  ? 764  PRO   A CG  1 
ATOM   5610 C  CD  . PRO   A 1 739 ? 4.970  48.766  10.154  1.00 20.05  ? 764  PRO   A CD  1 
ATOM   5611 N  N   . VAL   A 1 740 ? 7.917  45.162  9.486   1.00 17.43  ? 765  VAL   A N   1 
ATOM   5612 C  CA  . VAL   A 1 740 ? 9.098  44.594  10.121  1.00 16.26  ? 765  VAL   A CA  1 
ATOM   5613 C  C   . VAL   A 1 740 ? 10.308 45.539  10.059  1.00 16.16  ? 765  VAL   A C   1 
ATOM   5614 O  O   . VAL   A 1 740 ? 11.098 45.632  11.002  1.00 15.88  ? 765  VAL   A O   1 
ATOM   5615 C  CB  . VAL   A 1 740 ? 9.433  43.211  9.535   1.00 17.81  ? 765  VAL   A CB  1 
ATOM   5616 C  CG1 . VAL   A 1 740 ? 10.694 42.641  10.186  1.00 19.06  ? 765  VAL   A CG1 1 
ATOM   5617 C  CG2 . VAL   A 1 740 ? 8.241  42.272  9.719   1.00 17.91  ? 765  VAL   A CG2 1 
ATOM   5618 N  N   . ASP   A 1 741 ? 10.407 46.265  8.935   1.00 15.95  ? 766  ASP   A N   1 
ATOM   5619 C  CA  . ASP   A 1 741 ? 11.589 47.108  8.712   1.00 15.22  ? 766  ASP   A CA  1 
ATOM   5620 C  C   . ASP   A 1 741 ? 11.679 48.309  9.604   1.00 15.01  ? 766  ASP   A C   1 
ATOM   5621 O  O   . ASP   A 1 741 ? 12.772 48.858  9.753   1.00 15.48  ? 766  ASP   A O   1 
ATOM   5622 C  CB  . ASP   A 1 741 ? 11.657 47.543  7.266   1.00 14.94  ? 766  ASP   A CB  1 
ATOM   5623 C  CG  . ASP   A 1 741 ? 11.765 46.422  6.271   1.00 15.76  ? 766  ASP   A CG  1 
ATOM   5624 O  OD1 . ASP   A 1 741 ? 11.942 45.264  6.700   1.00 17.50  ? 766  ASP   A OD1 1 
ATOM   5625 O  OD2 . ASP   A 1 741 ? 11.675 46.708  5.053   1.00 18.07  ? 766  ASP   A OD2 1 
ATOM   5626 N  N   . VAL   A 1 742 ? 10.563 48.713  10.228  1.00 15.26  ? 767  VAL   A N   1 
ATOM   5627 C  CA  . VAL   A 1 742 ? 10.592 49.812  11.172  1.00 14.69  ? 767  VAL   A CA  1 
ATOM   5628 C  C   . VAL   A 1 742 ? 10.534 49.321  12.608  1.00 14.10  ? 767  VAL   A C   1 
ATOM   5629 O  O   . VAL   A 1 742 ? 10.624 50.132  13.512  1.00 15.71  ? 767  VAL   A O   1 
ATOM   5630 C  CB  . VAL   A 1 742 ? 9.442  50.840  10.927  1.00 15.41  ? 767  VAL   A CB  1 
ATOM   5631 C  CG1 . VAL   A 1 742 ? 9.406  51.245  9.459   1.00 16.25  ? 767  VAL   A CG1 1 
ATOM   5632 C  CG2 . VAL   A 1 742 ? 8.089  50.273  11.384  1.00 16.46  ? 767  VAL   A CG2 1 
ATOM   5633 N  N   . THR   A 1 743 ? 10.383 47.995  12.832  1.00 14.16  ? 768  THR   A N   1 
ATOM   5634 C  CA  . THR   A 1 743 ? 10.196 47.468  14.165  1.00 14.99  ? 768  THR   A CA  1 
ATOM   5635 C  C   . THR   A 1 743 ? 11.399 47.736  15.078  1.00 15.88  ? 768  THR   A C   1 
ATOM   5636 O  O   . THR   A 1 743 ? 11.183 48.042  16.248  1.00 16.45  ? 768  THR   A O   1 
ATOM   5637 C  CB  . THR   A 1 743 ? 9.788  46.000  14.084  1.00 16.73  ? 768  THR   A CB  1 
ATOM   5638 O  OG1 . THR   A 1 743 ? 8.512  45.930  13.426  1.00 17.33  ? 768  THR   A OG1 1 
ATOM   5639 C  CG2 . THR   A 1 743 ? 9.628  45.389  15.442  1.00 16.92  ? 768  THR   A CG2 1 
ATOM   5640 N  N   . LEU   A 1 744 ? 12.648 47.609  14.590  1.00 14.97  ? 769  LEU   A N   1 
ATOM   5641 C  CA  . LEU   A 1 744 ? 13.785 47.907  15.482  1.00 15.53  ? 769  LEU   A CA  1 
ATOM   5642 C  C   . LEU   A 1 744 ? 13.739 49.348  15.982  1.00 15.63  ? 769  LEU   A C   1 
ATOM   5643 O  O   . LEU   A 1 744 ? 13.848 49.600  17.177  1.00 16.00  ? 769  LEU   A O   1 
ATOM   5644 C  CB  . LEU   A 1 744 ? 15.111 47.693  14.730  1.00 17.02  ? 769  LEU   A CB  1 
ATOM   5645 C  CG  . LEU   A 1 744 ? 15.614 46.292  14.748  1.00 17.83  ? 769  LEU   A CG  1 
ATOM   5646 C  CD1 . LEU   A 1 744 ? 16.750 46.167  13.804  1.00 18.06  ? 769  LEU   A CD1 1 
ATOM   5647 C  CD2 . LEU   A 1 744 ? 16.049 45.904  16.190  1.00 17.66  ? 769  LEU   A CD2 1 
ATOM   5648 N  N   . ALA   A 1 745 ? 13.466 50.306  15.068  1.00 15.42  ? 770  ALA   A N   1 
ATOM   5649 C  CA  . ALA   A 1 745 ? 13.383 51.710  15.480  1.00 15.68  ? 770  ALA   A CA  1 
ATOM   5650 C  C   . ALA   A 1 745 ? 12.197 51.907  16.448  1.00 16.86  ? 770  ALA   A C   1 
ATOM   5651 O  O   . ALA   A 1 745 ? 12.364 52.572  17.468  1.00 17.98  ? 770  ALA   A O   1 
ATOM   5652 C  CB  . ALA   A 1 745 ? 13.230 52.608  14.257  1.00 15.91  ? 770  ALA   A CB  1 
ATOM   5653 N  N   . VAL   A 1 746 ? 11.041 51.328  16.133  1.00 15.91  ? 771  VAL   A N   1 
ATOM   5654 C  CA  . VAL   A 1 746 ? 9.851  51.511  16.959  1.00 15.31  ? 771  VAL   A CA  1 
ATOM   5655 C  C   . VAL   A 1 746 ? 10.040 50.920  18.335  1.00 15.34  ? 771  VAL   A C   1 
ATOM   5656 O  O   . VAL   A 1 746 ? 9.762  51.604  19.337  1.00 15.90  ? 771  VAL   A O   1 
ATOM   5657 C  CB  . VAL   A 1 746 ? 8.608  50.928  16.242  1.00 16.53  ? 771  VAL   A CB  1 
ATOM   5658 C  CG1 . VAL   A 1 746 ? 7.393  50.870  17.182  1.00 18.24  ? 771  VAL   A CG1 1 
ATOM   5659 C  CG2 . VAL   A 1 746 ? 8.285  51.765  15.003  1.00 18.04  ? 771  VAL   A CG2 1 
ATOM   5660 N  N   . PHE   A 1 747 ? 10.542 49.705  18.410  1.00 14.80  ? 772  PHE   A N   1 
ATOM   5661 C  CA  . PHE   A 1 747 ? 10.761 49.087  19.719  1.00 14.73  ? 772  PHE   A CA  1 
ATOM   5662 C  C   . PHE   A 1 747 ? 11.887 49.808  20.493  1.00 15.27  ? 772  PHE   A C   1 
ATOM   5663 O  O   . PHE   A 1 747 ? 11.785 49.966  21.706  1.00 15.92  ? 772  PHE   A O   1 
ATOM   5664 C  CB  . PHE   A 1 747 ? 11.129 47.620  19.548  1.00 14.53  ? 772  PHE   A CB  1 
ATOM   5665 C  CG  . PHE   A 1 747 ? 10.003 46.665  19.186  1.00 15.81  ? 772  PHE   A CG  1 
ATOM   5666 C  CD1 . PHE   A 1 747 ? 8.687  47.111  19.070  1.00 17.47  ? 772  PHE   A CD1 1 
ATOM   5667 C  CD2 . PHE   A 1 747 ? 10.250 45.314  19.032  1.00 15.64  ? 772  PHE   A CD2 1 
ATOM   5668 C  CE1 . PHE   A 1 747 ? 7.664  46.212  18.795  1.00 18.53  ? 772  PHE   A CE1 1 
ATOM   5669 C  CE2 . PHE   A 1 747 ? 9.230  44.427  18.745  1.00 17.19  ? 772  PHE   A CE2 1 
ATOM   5670 C  CZ  . PHE   A 1 747 ? 7.938  44.870  18.670  1.00 17.83  ? 772  PHE   A CZ  1 
ATOM   5671 N  N   . ALA   A 1 748 ? 12.964 50.261  19.804  1.00 15.60  ? 773  ALA   A N   1 
ATOM   5672 C  CA  . ALA   A 1 748 ? 14.043 50.935  20.520  1.00 15.82  ? 773  ALA   A CA  1 
ATOM   5673 C  C   . ALA   A 1 748 ? 13.561 52.217  21.146  1.00 17.19  ? 773  ALA   A C   1 
ATOM   5674 O  O   . ALA   A 1 748 ? 14.012 52.561  22.230  1.00 17.80  ? 773  ALA   A O   1 
ATOM   5675 C  CB  . ALA   A 1 748 ? 15.236 51.198  19.590  1.00 16.14  ? 773  ALA   A CB  1 
ATOM   5676 N  N   . VAL   A 1 749 ? 12.686 52.937  20.449  1.00 16.12  ? 774  VAL   A N   1 
ATOM   5677 C  CA  . VAL   A 1 749 ? 12.131 54.157  21.004  1.00 16.87  ? 774  VAL   A CA  1 
ATOM   5678 C  C   . VAL   A 1 749 ? 11.147 53.806  22.132  1.00 17.44  ? 774  VAL   A C   1 
ATOM   5679 O  O   . VAL   A 1 749 ? 11.184 54.456  23.195  1.00 19.02  ? 774  VAL   A O   1 
ATOM   5680 C  CB  . VAL   A 1 749 ? 11.443 54.959  19.888  1.00 18.17  ? 774  VAL   A CB  1 
ATOM   5681 C  CG1 . VAL   A 1 749 ? 10.597 56.082  20.463  1.00 18.29  ? 774  VAL   A CG1 1 
ATOM   5682 C  CG2 . VAL   A 1 749 ? 12.507 55.558  18.963  1.00 19.52  ? 774  VAL   A CG2 1 
ATOM   5683 N  N   . GLY   A 1 750 ? 10.277 52.834  21.895  1.00 16.55  ? 775  GLY   A N   1 
ATOM   5684 C  CA  . GLY   A 1 750 ? 9.262  52.503  22.891  1.00 17.64  ? 775  GLY   A CA  1 
ATOM   5685 C  C   . GLY   A 1 750 ? 9.839  52.022  24.200  1.00 18.66  ? 775  GLY   A C   1 
ATOM   5686 O  O   . GLY   A 1 750 ? 9.305  52.339  25.269  1.00 19.96  ? 775  GLY   A O   1 
ATOM   5687 N  N   . ALA   A 1 751 ? 10.961 51.269  24.148  1.00 18.95  ? 776  ALA   A N   1 
ATOM   5688 C  CA  . ALA   A 1 751 ? 11.520 50.725  25.383  1.00 19.53  ? 776  ALA   A CA  1 
ATOM   5689 C  C   . ALA   A 1 751 ? 12.273 51.751  26.240  1.00 19.10  ? 776  ALA   A C   1 
ATOM   5690 O  O   . ALA   A 1 751 ? 12.827 51.364  27.268  1.00 19.27  ? 776  ALA   A O   1 
ATOM   5691 C  CB  . ALA   A 1 751 ? 12.381 49.514  25.082  1.00 20.97  ? 776  ALA   A CB  1 
ATOM   5692 N  N   . GLN   A 1 752 ? 12.291 53.018  25.830  1.00 18.73  ? 777  GLN   A N   1 
ATOM   5693 C  CA  . GLN   A 1 752 ? 12.945 54.125  26.570  1.00 19.86  ? 777  GLN   A CA  1 
ATOM   5694 C  C   . GLN   A 1 752 ? 12.166 54.615  27.796  1.00 23.87  ? 777  GLN   A C   1 
ATOM   5695 O  O   . GLN   A 1 752 ? 12.703 55.415  28.573  1.00 26.46  ? 777  GLN   A O   1 
ATOM   5696 C  CB  . GLN   A 1 752 ? 13.291 55.300  25.667  1.00 20.12  ? 777  GLN   A CB  1 
ATOM   5697 C  CG  . GLN   A 1 752 ? 14.350 54.883  24.632  1.00 19.77  ? 777  GLN   A CG  1 
ATOM   5698 C  CD  . GLN   A 1 752 ? 15.719 54.727  25.268  1.00 24.51  ? 777  GLN   A CD  1 
ATOM   5699 O  OE1 . GLN   A 1 752 ? 16.329 55.698  25.693  1.00 28.34  ? 777  GLN   A OE1 1 
ATOM   5700 N  NE2 . GLN   A 1 752 ? 16.229 53.523  25.334  1.00 24.38  ? 777  GLN   A NE2 1 
ATOM   5701 N  N   . SER   A 1 753 ? 10.890 54.242  27.897  1.00 22.66  ? 778  SER   A N   1 
ATOM   5702 C  CA  . SER   A 1 753 ? 10.130 54.585  29.085  1.00 23.11  ? 778  SER   A CA  1 
ATOM   5703 C  C   . SER   A 1 753 ? 9.955  53.296  29.840  1.00 22.03  ? 778  SER   A C   1 
ATOM   5704 O  O   . SER   A 1 753 ? 9.948  52.174  29.282  1.00 21.05  ? 778  SER   A O   1 
ATOM   5705 C  CB  . SER   A 1 753 ? 8.769  55.199  28.729  1.00 24.46  ? 778  SER   A CB  1 
ATOM   5706 O  OG  . SER   A 1 753 ? 7.860  54.216  28.242  1.00 24.20  ? 778  SER   A OG  1 
ATOM   5707 N  N   . THR   A 1 754 ? 9.671  53.436  31.148  1.00 22.15  ? 779  THR   A N   1 
ATOM   5708 C  CA  . THR   A 1 754 ? 9.475  52.256  31.965  1.00 22.06  ? 779  THR   A CA  1 
ATOM   5709 C  C   . THR   A 1 754 ? 8.225  51.488  31.512  1.00 21.81  ? 779  THR   A C   1 
ATOM   5710 O  O   . THR   A 1 754 ? 8.295  50.272  31.381  1.00 21.07  ? 779  THR   A O   1 
ATOM   5711 C  CB  . THR   A 1 754 ? 9.313  52.707  33.424  1.00 25.57  ? 779  THR   A CB  1 
ATOM   5712 O  OG1 . THR   A 1 754 ? 10.524 53.360  33.844  1.00 27.78  ? 779  THR   A OG1 1 
ATOM   5713 C  CG2 . THR   A 1 754 ? 9.031  51.536  34.328  1.00 26.01  ? 779  THR   A CG2 1 
ATOM   5714 N  N   . GLU   A 1 755 ? 7.120  52.201  31.195  1.00 21.74  ? 780  GLU   A N   1 
ATOM   5715 C  CA  . GLU   A 1 755 ? 5.932  51.495  30.716  1.00 22.08  ? 780  GLU   A CA  1 
ATOM   5716 C  C   . GLU   A 1 755 ? 6.173  50.755  29.394  1.00 20.79  ? 780  GLU   A C   1 
ATOM   5717 O  O   . GLU   A 1 755 ? 5.689  49.643  29.209  1.00 20.65  ? 780  GLU   A O   1 
ATOM   5718 C  CB  . GLU   A 1 755 ? 4.744  52.455  30.603  1.00 25.34  ? 780  GLU   A CB  1 
ATOM   5719 C  CG  . GLU   A 1 755 ? 4.192  52.869  31.956  1.00 31.11  ? 780  GLU   A CG  1 
ATOM   5720 C  CD  . GLU   A 1 755 ? 3.000  53.810  31.879  1.00 38.96  ? 780  GLU   A CD  1 
ATOM   5721 O  OE1 . GLU   A 1 755 ? 2.594  54.177  30.749  1.00 35.26  ? 780  GLU   A OE1 1 
ATOM   5722 O  OE2 . GLU   A 1 755 ? 2.482  54.189  32.958  1.00 42.12  ? 780  GLU   A OE2 1 
ATOM   5723 N  N   . GLY   A 1 756 ? 6.938  51.383  28.500  1.00 19.54  ? 781  GLY   A N   1 
ATOM   5724 C  CA  . GLY   A 1 756 ? 7.185  50.779  27.193  1.00 19.75  ? 781  GLY   A CA  1 
ATOM   5725 C  C   . GLY   A 1 756 ? 8.108  49.578  27.288  1.00 19.33  ? 781  GLY   A C   1 
ATOM   5726 O  O   . GLY   A 1 756 ? 7.875  48.544  26.682  1.00 19.40  ? 781  GLY   A O   1 
ATOM   5727 N  N   . TRP   A 1 757 ? 9.152  49.698  28.111  1.00 18.31  ? 782  TRP   A N   1 
ATOM   5728 C  CA  . TRP   A 1 757 ? 10.083 48.575  28.348  1.00 18.42  ? 782  TRP   A CA  1 
ATOM   5729 C  C   . TRP   A 1 757 ? 9.314  47.358  28.916  1.00 19.23  ? 782  TRP   A C   1 
ATOM   5730 O  O   . TRP   A 1 757 ? 9.396  46.244  28.405  1.00 18.25  ? 782  TRP   A O   1 
ATOM   5731 C  CB  . TRP   A 1 757 ? 11.177 49.029  29.338  1.00 17.99  ? 782  TRP   A CB  1 
ATOM   5732 C  CG  . TRP   A 1 757 ? 12.399 48.154  29.376  1.00 18.03  ? 782  TRP   A CG  1 
ATOM   5733 C  CD1 . TRP   A 1 757 ? 13.587 48.408  28.755  1.00 16.82  ? 782  TRP   A CD1 1 
ATOM   5734 C  CD2 . TRP   A 1 757 ? 12.578 46.921  30.098  1.00 17.82  ? 782  TRP   A CD2 1 
ATOM   5735 N  NE1 . TRP   A 1 757 ? 14.506 47.420  29.060  1.00 16.73  ? 782  TRP   A NE1 1 
ATOM   5736 C  CE2 . TRP   A 1 757 ? 13.904 46.484  29.860  1.00 17.47  ? 782  TRP   A CE2 1 
ATOM   5737 C  CE3 . TRP   A 1 757 ? 11.745 46.120  30.889  1.00 19.39  ? 782  TRP   A CE3 1 
ATOM   5738 C  CZ2 . TRP   A 1 757 ? 14.422 45.310  30.412  1.00 18.23  ? 782  TRP   A CZ2 1 
ATOM   5739 C  CZ3 . TRP   A 1 757 ? 12.244 44.924  31.383  1.00 19.47  ? 782  TRP   A CZ3 1 
ATOM   5740 C  CH2 . TRP   A 1 757 ? 13.580 44.546  31.174  1.00 19.95  ? 782  TRP   A CH2 1 
ATOM   5741 N  N   . ASP   A 1 758 ? 8.502  47.639  29.964  1.00 19.33  ? 783  ASP   A N   1 
ATOM   5742 C  CA  . ASP   A 1 758 ? 7.723  46.567  30.573  1.00 20.90  ? 783  ASP   A CA  1 
ATOM   5743 C  C   . ASP   A 1 758 ? 6.738  45.940  29.595  1.00 21.51  ? 783  ASP   A C   1 
ATOM   5744 O  O   . ASP   A 1 758 ? 6.593  44.728  29.580  1.00 20.65  ? 783  ASP   A O   1 
ATOM   5745 C  CB  . ASP   A 1 758 ? 6.973  47.119  31.811  1.00 22.65  ? 783  ASP   A CB  1 
ATOM   5746 C  CG  . ASP   A 1 758 ? 7.894  47.435  32.984  1.00 26.28  ? 783  ASP   A CG  1 
ATOM   5747 O  OD1 . ASP   A 1 758 ? 9.067  46.977  32.963  1.00 26.21  ? 783  ASP   A OD1 1 
ATOM   5748 O  OD2 . ASP   A 1 758 ? 7.450  48.163  33.910  1.00 28.21  ? 783  ASP   A OD2 1 
ATOM   5749 N  N   . PHE   A 1 759 ? 6.067  46.761  28.788  1.00 21.84  ? 784  PHE   A N   1 
ATOM   5750 C  CA  . PHE   A 1 759 ? 5.098  46.217  27.820  1.00 22.64  ? 784  PHE   A CA  1 
ATOM   5751 C  C   . PHE   A 1 759 ? 5.807  45.347  26.790  1.00 22.19  ? 784  PHE   A C   1 
ATOM   5752 O  O   . PHE   A 1 759 ? 5.381  44.230  26.490  1.00 21.30  ? 784  PHE   A O   1 
ATOM   5753 C  CB  . PHE   A 1 759 ? 4.336  47.344  27.109  1.00 23.68  ? 784  PHE   A CB  1 
ATOM   5754 C  CG  . PHE   A 1 759 ? 3.308  46.786  26.159  1.00 24.10  ? 784  PHE   A CG  1 
ATOM   5755 C  CD1 . PHE   A 1 759 ? 2.070  46.354  26.629  1.00 25.57  ? 784  PHE   A CD1 1 
ATOM   5756 C  CD2 . PHE   A 1 759 ? 3.559  46.721  24.799  1.00 25.32  ? 784  PHE   A CD2 1 
ATOM   5757 C  CE1 . PHE   A 1 759 ? 1.116  45.845  25.754  1.00 26.32  ? 784  PHE   A CE1 1 
ATOM   5758 C  CE2 . PHE   A 1 759 ? 2.615  46.191  23.927  1.00 26.31  ? 784  PHE   A CE2 1 
ATOM   5759 C  CZ  . PHE   A 1 759 ? 1.394  45.769  24.412  1.00 26.14  ? 784  PHE   A CZ  1 
ATOM   5760 N  N   . LEU   A 1 760 ? 6.938  45.855  26.262  1.00 21.82  ? 785  LEU   A N   1 
ATOM   5761 C  CA  . LEU   A 1 760 ? 7.681  45.098  25.274  1.00 22.46  ? 785  LEU   A CA  1 
ATOM   5762 C  C   . LEU   A 1 760 ? 8.177  43.762  25.835  1.00 21.81  ? 785  LEU   A C   1 
ATOM   5763 O  O   . LEU   A 1 760 ? 8.028  42.715  25.204  1.00 22.42  ? 785  LEU   A O   1 
ATOM   5764 C  CB  . LEU   A 1 760 ? 8.852  45.945  24.777  1.00 22.90  ? 785  LEU   A CB  1 
ATOM   5765 C  CG  . LEU   A 1 760 ? 9.470  45.504  23.475  1.00 24.86  ? 785  LEU   A CG  1 
ATOM   5766 C  CD1 . LEU   A 1 760 ? 8.472  45.482  22.327  1.00 22.05  ? 785  LEU   A CD1 1 
ATOM   5767 C  CD2 . LEU   A 1 760 ? 10.698 46.371  23.152  1.00 25.27  ? 785  LEU   A CD2 1 
ATOM   5768 N  N   . TYR   A 1 761 ? 8.718  43.781  27.065  1.00 20.64  ? 786  TYR   A N   1 
ATOM   5769 C  CA  . TYR   A 1 761 ? 9.160  42.547  27.676  1.00 20.82  ? 786  TYR   A CA  1 
ATOM   5770 C  C   . TYR   A 1 761 ? 7.977  41.585  27.900  1.00 21.41  ? 786  TYR   A C   1 
ATOM   5771 O  O   . TYR   A 1 761 ? 8.122  40.391  27.713  1.00 20.33  ? 786  TYR   A O   1 
ATOM   5772 C  CB  . TYR   A 1 761 ? 9.934  42.820  28.962  1.00 20.60  ? 786  TYR   A CB  1 
ATOM   5773 C  CG  . TYR   A 1 761 ? 10.222 41.557  29.693  1.00 20.95  ? 786  TYR   A CG  1 
ATOM   5774 C  CD1 . TYR   A 1 761 ? 11.085 40.611  29.163  1.00 22.55  ? 786  TYR   A CD1 1 
ATOM   5775 C  CD2 . TYR   A 1 761 ? 9.497  41.210  30.825  1.00 22.43  ? 786  TYR   A CD2 1 
ATOM   5776 C  CE1 . TYR   A 1 761 ? 11.281 39.388  29.776  1.00 24.22  ? 786  TYR   A CE1 1 
ATOM   5777 C  CE2 . TYR   A 1 761 ? 9.663  39.979  31.424  1.00 23.17  ? 786  TYR   A CE2 1 
ATOM   5778 C  CZ  . TYR   A 1 761 ? 10.611 39.102  30.944  1.00 24.94  ? 786  TYR   A CZ  1 
ATOM   5779 O  OH  . TYR   A 1 761 ? 10.756 37.874  31.535  1.00 27.25  ? 786  TYR   A OH  1 
ATOM   5780 N  N   . SER   A 1 762 ? 6.797  42.133  28.245  1.00 21.29  ? 787  SER   A N   1 
ATOM   5781 C  CA  . SER   A 1 762 ? 5.624  41.258  28.435  1.00 22.09  ? 787  SER   A CA  1 
ATOM   5782 C  C   . SER   A 1 762 ? 5.219  40.481  27.196  1.00 23.80  ? 787  SER   A C   1 
ATOM   5783 O  O   . SER   A 1 762 ? 4.573  39.439  27.331  1.00 27.23  ? 787  SER   A O   1 
ATOM   5784 C  CB  . SER   A 1 762 ? 4.437  42.053  28.979  1.00 22.22  ? 787  SER   A CB  1 
ATOM   5785 O  OG  . SER   A 1 762 ? 3.762  42.814  27.992  1.00 25.70  ? 787  SER   A OG  1 
ATOM   5786 N  N   . LYS   A 1 763 ? 5.551  40.969  25.988  1.00 20.42  ? 788  LYS   A N   1 
ATOM   5787 C  CA  . LYS   A 1 763 ? 5.187  40.276  24.753  1.00 19.42  ? 788  LYS   A CA  1 
ATOM   5788 C  C   . LYS   A 1 763 ? 6.251  39.200  24.358  1.00 19.42  ? 788  LYS   A C   1 
ATOM   5789 O  O   . LYS   A 1 763 ? 5.990  38.284  23.578  1.00 20.22  ? 788  LYS   A O   1 
ATOM   5790 C  CB  . LYS   A 1 763 ? 5.083  41.273  23.592  1.00 20.97  ? 788  LYS   A CB  1 
ATOM   5791 C  CG  . LYS   A 1 763 ? 3.865  42.238  23.634  1.00 23.86  ? 788  LYS   A CG  1 
ATOM   5792 C  CD  . LYS   A 1 763 ? 2.535  41.455  23.717  1.00 28.42  ? 788  LYS   A CD  1 
ATOM   5793 C  CE  . LYS   A 1 763 ? 1.306  42.335  23.650  1.00 35.14  ? 788  LYS   A CE  1 
ATOM   5794 N  NZ  . LYS   A 1 763 ? 0.064  41.514  23.618  1.00 39.13  ? 788  LYS   A NZ  1 
ATOM   5795 N  N   . TYR   A 1 764 ? 7.446  39.330  24.902  1.00 18.38  ? 789  TYR   A N   1 
ATOM   5796 C  CA  . TYR   A 1 764 ? 8.566  38.443  24.573  1.00 17.40  ? 789  TYR   A CA  1 
ATOM   5797 C  C   . TYR   A 1 764 ? 8.231  36.987  24.869  1.00 18.26  ? 789  TYR   A C   1 
ATOM   5798 O  O   . TYR   A 1 764 ? 8.525  36.143  24.038  1.00 17.34  ? 789  TYR   A O   1 
ATOM   5799 C  CB  . TYR   A 1 764 ? 9.771  38.898  25.373  1.00 17.15  ? 789  TYR   A CB  1 
ATOM   5800 C  CG  . TYR   A 1 764 ? 11.031 38.124  25.081  1.00 15.92  ? 789  TYR   A CG  1 
ATOM   5801 C  CD1 . TYR   A 1 764 ? 11.843 38.463  24.008  1.00 15.46  ? 789  TYR   A CD1 1 
ATOM   5802 C  CD2 . TYR   A 1 764 ? 11.424 37.080  25.899  1.00 15.98  ? 789  TYR   A CD2 1 
ATOM   5803 C  CE1 . TYR   A 1 764 ? 13.036 37.792  23.769  1.00 15.14  ? 789  TYR   A CE1 1 
ATOM   5804 C  CE2 . TYR   A 1 764 ? 12.603 36.382  25.651  1.00 16.03  ? 789  TYR   A CE2 1 
ATOM   5805 C  CZ  . TYR   A 1 764 ? 13.395 36.739  24.582  1.00 15.77  ? 789  TYR   A CZ  1 
ATOM   5806 O  OH  . TYR   A 1 764 ? 14.593 36.106  24.399  1.00 16.30  ? 789  TYR   A OH  1 
ATOM   5807 N  N   . GLN   A 1 765 ? 7.609  36.681  26.043  1.00 19.53  ? 790  GLN   A N   1 
ATOM   5808 C  CA  . GLN   A 1 765 ? 7.322  35.279  26.358  1.00 21.43  ? 790  GLN   A CA  1 
ATOM   5809 C  C   . GLN   A 1 765 ? 6.380  34.567  25.424  1.00 22.21  ? 790  GLN   A C   1 
ATOM   5810 O  O   . GLN   A 1 765 ? 6.433  33.329  25.370  1.00 25.82  ? 790  GLN   A O   1 
ATOM   5811 C  CB  . GLN   A 1 765 ? 6.802  35.108  27.803  1.00 25.96  ? 790  GLN   A CB  1 
ATOM   5812 C  CG  . GLN   A 1 765 ? 5.375  35.562  28.018  1.00 32.51  ? 790  GLN   A CG  1 
ATOM   5813 C  CD  . GLN   A 1 765 ? 4.740  34.912  29.242  1.00 40.39  ? 790  GLN   A CD  1 
ATOM   5814 O  OE1 . GLN   A 1 765 ? 4.929  33.716  29.534  1.00 44.23  ? 790  GLN   A OE1 1 
ATOM   5815 N  NE2 . GLN   A 1 765 ? 3.968  35.686  29.972  1.00 40.34  ? 790  GLN   A NE2 1 
ATOM   5816 N  N   . PHE   A 1 766 ? 5.556  35.294  24.697  1.00 19.69  ? 791  PHE   A N   1 
ATOM   5817 C  CA  . PHE   A 1 766 ? 4.596  34.663  23.795  1.00 20.80  ? 791  PHE   A CA  1 
ATOM   5818 C  C   . PHE   A 1 766 ? 5.135  34.519  22.396  1.00 19.47  ? 791  PHE   A C   1 
ATOM   5819 O  O   . PHE   A 1 766 ? 4.526  33.794  21.609  1.00 21.51  ? 791  PHE   A O   1 
ATOM   5820 C  CB  . PHE   A 1 766 ? 3.308  35.509  23.717  1.00 23.00  ? 791  PHE   A CB  1 
ATOM   5821 C  CG  . PHE   A 1 766 ? 2.684  35.722  25.074  1.00 27.61  ? 791  PHE   A CG  1 
ATOM   5822 C  CD1 . PHE   A 1 766 ? 2.002  34.699  25.706  1.00 30.68  ? 791  PHE   A CD1 1 
ATOM   5823 C  CD2 . PHE   A 1 766 ? 2.773  36.949  25.712  1.00 30.55  ? 791  PHE   A CD2 1 
ATOM   5824 C  CE1 . PHE   A 1 766 ? 1.411  34.903  26.956  1.00 32.09  ? 791  PHE   A CE1 1 
ATOM   5825 C  CE2 . PHE   A 1 766 ? 2.182  37.148  26.960  1.00 32.20  ? 791  PHE   A CE2 1 
ATOM   5826 C  CZ  . PHE   A 1 766 ? 1.525  36.119  27.577  1.00 31.70  ? 791  PHE   A CZ  1 
ATOM   5827 N  N   . SER   A 1 767 ? 6.236  35.203  22.053  1.00 16.54  ? 792  SER   A N   1 
ATOM   5828 C  CA  . SER   A 1 767 ? 6.653  35.227  20.669  1.00 15.45  ? 792  SER   A CA  1 
ATOM   5829 C  C   . SER   A 1 767 ? 7.228  33.914  20.223  1.00 15.39  ? 792  SER   A C   1 
ATOM   5830 O  O   . SER   A 1 767 ? 8.053  33.304  20.922  1.00 17.21  ? 792  SER   A O   1 
ATOM   5831 C  CB  . SER   A 1 767 ? 7.699  36.318  20.488  1.00 17.27  ? 792  SER   A CB  1 
ATOM   5832 O  OG  . SER   A 1 767 ? 8.027  36.403  19.107  1.00 16.83  ? 792  SER   A OG  1 
ATOM   5833 N  N   . LEU   A 1 768 ? 6.846  33.514  19.012  1.00 15.11  ? 793  LEU   A N   1 
ATOM   5834 C  CA  . LEU   A 1 768 ? 7.431  32.358  18.337  1.00 14.81  ? 793  LEU   A CA  1 
ATOM   5835 C  C   . LEU   A 1 768 ? 8.375  32.826  17.210  1.00 13.87  ? 793  LEU   A C   1 
ATOM   5836 O  O   . LEU   A 1 768 ? 8.937  32.004  16.506  1.00 14.03  ? 793  LEU   A O   1 
ATOM   5837 C  CB  . LEU   A 1 768 ? 6.345  31.449  17.772  1.00 15.62  ? 793  LEU   A CB  1 
ATOM   5838 C  CG  . LEU   A 1 768 ? 5.432  30.854  18.832  1.00 15.81  ? 793  LEU   A CG  1 
ATOM   5839 C  CD1 . LEU   A 1 768 ? 4.253  30.105  18.188  1.00 17.04  ? 793  LEU   A CD1 1 
ATOM   5840 C  CD2 . LEU   A 1 768 ? 6.213  29.872  19.716  1.00 17.54  ? 793  LEU   A CD2 1 
ATOM   5841 N  N   . SER   A 1 769 ? 8.549  34.137  17.031  1.00 14.30  ? 794  SER   A N   1 
ATOM   5842 C  CA  . SER   A 1 769 ? 9.364  34.681  15.950  1.00 13.71  ? 794  SER   A CA  1 
ATOM   5843 C  C   . SER   A 1 769 ? 10.781 34.972  16.410  1.00 13.27  ? 794  SER   A C   1 
ATOM   5844 O  O   . SER   A 1 769 ? 10.961 35.781  17.322  1.00 14.00  ? 794  SER   A O   1 
ATOM   5845 C  CB  . SER   A 1 769 ? 8.716  35.982  15.487  1.00 14.71  ? 794  SER   A CB  1 
ATOM   5846 O  OG  . SER   A 1 769 ? 9.607  36.770  14.710  1.00 14.54  ? 794  SER   A OG  1 
ATOM   5847 N  N   . SER   A 1 770 ? 11.775 34.367  15.745  1.00 13.14  ? 795  SER   A N   1 
ATOM   5848 C  CA  . SER   A 1 770 ? 13.154 34.645  16.150  1.00 12.86  ? 795  SER   A CA  1 
ATOM   5849 C  C   . SER   A 1 770 ? 13.499 36.115  15.880  1.00 13.80  ? 795  SER   A C   1 
ATOM   5850 O  O   . SER   A 1 770 ? 14.215 36.742  16.679  1.00 14.12  ? 795  SER   A O   1 
ATOM   5851 C  CB  . SER   A 1 770 ? 14.124 33.748  15.375  1.00 14.51  ? 795  SER   A CB  1 
ATOM   5852 O  OG  . SER   A 1 770 ? 13.964 32.401  15.785  1.00 15.40  ? 795  SER   A OG  1 
ATOM   5853 N  N   . THR   A 1 771 ? 13.005 36.702  14.749  1.00 13.15  ? 796  THR   A N   1 
ATOM   5854 C  CA  . THR   A 1 771 ? 13.262 38.124  14.516  1.00 13.16  ? 796  THR   A CA  1 
ATOM   5855 C  C   . THR   A 1 771 ? 12.650 38.993  15.588  1.00 13.63  ? 796  THR   A C   1 
ATOM   5856 O  O   . THR   A 1 771 ? 13.347 39.877  16.140  1.00 14.00  ? 796  THR   A O   1 
ATOM   5857 C  CB  . THR   A 1 771 ? 12.754 38.569  13.147  1.00 13.73  ? 796  THR   A CB  1 
ATOM   5858 O  OG1 . THR   A 1 771 ? 13.545 37.935  12.142  1.00 15.71  ? 796  THR   A OG1 1 
ATOM   5859 C  CG2 . THR   A 1 771 ? 12.788 40.081  12.995  1.00 15.10  ? 796  THR   A CG2 1 
ATOM   5860 N  N   . GLU   A 1 772 ? 11.372 38.749  15.947  1.00 13.23  ? 797  GLU   A N   1 
ATOM   5861 C  CA  . GLU   A 1 772 ? 10.760 39.597  16.948  1.00 13.79  ? 797  GLU   A CA  1 
ATOM   5862 C  C   . GLU   A 1 772 ? 11.497 39.477  18.281  1.00 13.85  ? 797  GLU   A C   1 
ATOM   5863 O  O   . GLU   A 1 772 ? 11.677 40.497  18.972  1.00 14.42  ? 797  GLU   A O   1 
ATOM   5864 C  CB  . GLU   A 1 772 ? 9.304  39.196  17.133  1.00 15.42  ? 797  GLU   A CB  1 
ATOM   5865 C  CG  . GLU   A 1 772 ? 8.510  40.187  17.956  1.00 17.38  ? 797  GLU   A CG  1 
ATOM   5866 C  CD  . GLU   A 1 772 ? 7.066  39.762  18.046  1.00 19.95  ? 797  GLU   A CD  1 
ATOM   5867 O  OE1 . GLU   A 1 772 ? 6.780  38.552  18.166  1.00 18.51  ? 797  GLU   A OE1 1 
ATOM   5868 O  OE2 . GLU   A 1 772 ? 6.205  40.668  18.008  1.00 22.58  ? 797  GLU   A OE2 1 
ATOM   5869 N  N   . LYS   A 1 773 ? 11.905 38.256  18.657  1.00 13.49  ? 798  LYS   A N   1 
ATOM   5870 C  CA  . LYS   A 1 773 ? 12.607 38.087  19.932  1.00 14.00  ? 798  LYS   A CA  1 
ATOM   5871 C  C   . LYS   A 1 773 ? 13.947 38.843  19.887  1.00 13.97  ? 798  LYS   A C   1 
ATOM   5872 O  O   . LYS   A 1 773 ? 14.327 39.492  20.881  1.00 14.70  ? 798  LYS   A O   1 
ATOM   5873 C  CB  . LYS   A 1 773 ? 12.800 36.605  20.237  1.00 14.21  ? 798  LYS   A CB  1 
ATOM   5874 C  CG  . LYS   A 1 773 ? 11.455 35.985  20.631  1.00 15.40  ? 798  LYS   A CG  1 
ATOM   5875 C  CD  . LYS   A 1 773 ? 11.515 34.481  20.806  1.00 16.62  ? 798  LYS   A CD  1 
ATOM   5876 C  CE  . LYS   A 1 773 ? 12.330 34.086  22.019  1.00 19.84  ? 798  LYS   A CE  1 
ATOM   5877 N  NZ  . LYS   A 1 773 ? 12.212 32.605  22.238  1.00 22.17  ? 798  LYS   A NZ  1 
ATOM   5878 N  N   . SER   A 1 774 ? 14.650 38.775  18.742  1.00 13.07  ? 799  SER   A N   1 
ATOM   5879 C  CA  A SER   A 1 774 ? 15.907 39.510  18.573  0.50 13.78  ? 799  SER   A CA  1 
ATOM   5880 C  CA  B SER   A 1 774 ? 15.908 39.505  18.601  0.50 13.82  ? 799  SER   A CA  1 
ATOM   5881 C  C   . SER   A 1 774 ? 15.664 41.009  18.669  1.00 14.41  ? 799  SER   A C   1 
ATOM   5882 O  O   . SER   A 1 774 ? 16.485 41.748  19.244  1.00 14.10  ? 799  SER   A O   1 
ATOM   5883 C  CB  A SER   A 1 774 ? 16.507 39.194  17.203  0.50 15.04  ? 799  SER   A CB  1 
ATOM   5884 C  CB  B SER   A 1 774 ? 16.561 39.156  17.266  0.50 15.20  ? 799  SER   A CB  1 
ATOM   5885 O  OG  A SER   A 1 774 ? 16.980 37.861  17.173  0.50 16.33  ? 799  SER   A OG  1 
ATOM   5886 O  OG  B SER   A 1 774 ? 17.741 39.922  17.082  0.50 16.74  ? 799  SER   A OG  1 
ATOM   5887 N  N   . GLN   A 1 775 ? 14.605 41.509  18.018  1.00 14.02  ? 800  GLN   A N   1 
ATOM   5888 C  CA  . GLN   A 1 775 ? 14.329 42.946  18.012  1.00 14.07  ? 800  GLN   A CA  1 
ATOM   5889 C  C   . GLN   A 1 775 ? 13.959 43.416  19.410  1.00 14.32  ? 800  GLN   A C   1 
ATOM   5890 O  O   . GLN   A 1 775 ? 14.398 44.499  19.823  1.00 14.91  ? 800  GLN   A O   1 
ATOM   5891 C  CB  . GLN   A 1 775 ? 13.171 43.238  17.059  1.00 13.84  ? 800  GLN   A CB  1 
ATOM   5892 C  CG  . GLN   A 1 775 ? 13.561 43.071  15.610  1.00 15.95  ? 800  GLN   A CG  1 
ATOM   5893 C  CD  . GLN   A 1 775 ? 12.339 43.099  14.715  1.00 15.56  ? 800  GLN   A CD  1 
ATOM   5894 O  OE1 . GLN   A 1 775 ? 11.305 42.573  15.053  1.00 17.03  ? 800  GLN   A OE1 1 
ATOM   5895 N  NE2 . GLN   A 1 775 ? 12.555 43.550  13.461  1.00 18.47  ? 800  GLN   A NE2 1 
ATOM   5896 N  N   . ILE   A 1 776 ? 13.202 42.600  20.171  1.00 14.18  ? 801  ILE   A N   1 
ATOM   5897 C  CA  . ILE   A 1 776 ? 12.870 42.987  21.547  1.00 13.90  ? 801  ILE   A CA  1 
ATOM   5898 C  C   . ILE   A 1 776 ? 14.150 43.000  22.376  1.00 13.61  ? 801  ILE   A C   1 
ATOM   5899 O  O   . ILE   A 1 776 ? 14.400 43.958  23.121  1.00 13.48  ? 801  ILE   A O   1 
ATOM   5900 C  CB  . ILE   A 1 776 ? 11.829 42.024  22.119  1.00 14.68  ? 801  ILE   A CB  1 
ATOM   5901 C  CG1 . ILE   A 1 776 ? 10.461 42.284  21.423  1.00 15.36  ? 801  ILE   A CG1 1 
ATOM   5902 C  CG2 . ILE   A 1 776 ? 11.705 42.256  23.638  1.00 16.60  ? 801  ILE   A CG2 1 
ATOM   5903 C  CD1 . ILE   A 1 776 ? 9.392  41.226  21.750  1.00 16.89  ? 801  ILE   A CD1 1 
ATOM   5904 N  N   . GLU   A 1 777 ? 15.010 41.945  22.221  1.00 13.41  ? 802  GLU   A N   1 
ATOM   5905 C  CA  . GLU   A 1 777 ? 16.248 41.932  23.019  1.00 13.55  ? 802  GLU   A CA  1 
ATOM   5906 C  C   . GLU   A 1 777 ? 17.077 43.184  22.730  1.00 14.59  ? 802  GLU   A C   1 
ATOM   5907 O  O   . GLU   A 1 777 ? 17.577 43.840  23.654  1.00 13.64  ? 802  GLU   A O   1 
ATOM   5908 C  CB  . GLU   A 1 777 ? 17.078 40.688  22.710  1.00 14.45  ? 802  GLU   A CB  1 
ATOM   5909 C  CG  . GLU   A 1 777 ? 16.434 39.417  23.258  1.00 14.33  ? 802  GLU   A CG  1 
ATOM   5910 C  CD  . GLU   A 1 777 ? 16.975 38.162  22.621  1.00 15.22  ? 802  GLU   A CD  1 
ATOM   5911 O  OE1 . GLU   A 1 777 ? 18.107 38.197  22.076  1.00 15.60  ? 802  GLU   A OE1 1 
ATOM   5912 O  OE2 . GLU   A 1 777 ? 16.275 37.125  22.685  1.00 15.46  ? 802  GLU   A OE2 1 
ATOM   5913 N  N   . PHE   A 1 778 ? 17.189 43.573  21.451  1.00 13.45  ? 803  PHE   A N   1 
ATOM   5914 C  CA  . PHE   A 1 778 ? 18.011 44.745  21.104  1.00 14.16  ? 803  PHE   A CA  1 
ATOM   5915 C  C   . PHE   A 1 778 ? 17.452 45.989  21.789  1.00 13.63  ? 803  PHE   A C   1 
ATOM   5916 O  O   . PHE   A 1 778 ? 18.179 46.806  22.372  1.00 13.95  ? 803  PHE   A O   1 
ATOM   5917 C  CB  . PHE   A 1 778 ? 17.976 44.956  19.566  1.00 14.51  ? 803  PHE   A CB  1 
ATOM   5918 C  CG  . PHE   A 1 778 ? 18.913 46.061  19.140  1.00 14.37  ? 803  PHE   A CG  1 
ATOM   5919 C  CD1 . PHE   A 1 778 ? 18.486 47.383  19.122  1.00 16.50  ? 803  PHE   A CD1 1 
ATOM   5920 C  CD2 . PHE   A 1 778 ? 20.238 45.779  18.778  1.00 16.53  ? 803  PHE   A CD2 1 
ATOM   5921 C  CE1 . PHE   A 1 778 ? 19.389 48.416  18.801  1.00 17.85  ? 803  PHE   A CE1 1 
ATOM   5922 C  CE2 . PHE   A 1 778 ? 21.113 46.806  18.442  1.00 17.84  ? 803  PHE   A CE2 1 
ATOM   5923 C  CZ  . PHE   A 1 778 ? 20.678 48.107  18.466  1.00 18.14  ? 803  PHE   A CZ  1 
ATOM   5924 N  N   . ALA   A 1 779 ? 16.113 46.179  21.664  1.00 13.56  ? 804  ALA   A N   1 
ATOM   5925 C  CA  . ALA   A 1 779 ? 15.484 47.357  22.227  1.00 13.91  ? 804  ALA   A CA  1 
ATOM   5926 C  C   . ALA   A 1 779 ? 15.622 47.391  23.728  1.00 14.18  ? 804  ALA   A C   1 
ATOM   5927 O  O   . ALA   A 1 779 ? 15.878 48.453  24.298  1.00 14.47  ? 804  ALA   A O   1 
ATOM   5928 C  CB  . ALA   A 1 779 ? 13.985 47.335  21.859  1.00 14.51  ? 804  ALA   A CB  1 
ATOM   5929 N  N   . LEU   A 1 780 ? 15.379 46.233  24.414  1.00 14.21  ? 805  LEU   A N   1 
ATOM   5930 C  CA  . LEU   A 1 780 ? 15.483 46.238  25.881  1.00 14.23  ? 805  LEU   A CA  1 
ATOM   5931 C  C   . LEU   A 1 780 ? 16.893 46.609  26.319  1.00 14.63  ? 805  LEU   A C   1 
ATOM   5932 O  O   . LEU   A 1 780 ? 17.051 47.296  27.309  1.00 14.84  ? 805  LEU   A O   1 
ATOM   5933 C  CB  . LEU   A 1 780 ? 15.088 44.893  26.460  1.00 13.94  ? 805  LEU   A CB  1 
ATOM   5934 C  CG  . LEU   A 1 780 ? 13.629 44.468  26.216  1.00 14.96  ? 805  LEU   A CG  1 
ATOM   5935 C  CD1 . LEU   A 1 780 ? 13.362 43.163  26.873  1.00 16.55  ? 805  LEU   A CD1 1 
ATOM   5936 C  CD2 . LEU   A 1 780 ? 12.599 45.538  26.648  1.00 15.97  ? 805  LEU   A CD2 1 
ATOM   5937 N  N   . CYS   A 1 781 ? 17.889 46.196  25.531  1.00 14.56  ? 806  CYS   A N   1 
ATOM   5938 C  CA  . CYS   A 1 781 ? 19.287 46.488  25.848  1.00 14.84  ? 806  CYS   A CA  1 
ATOM   5939 C  C   . CYS   A 1 781 ? 19.675 47.935  25.660  1.00 14.72  ? 806  CYS   A C   1 
ATOM   5940 O  O   . CYS   A 1 781 ? 20.793 48.293  26.046  1.00 14.30  ? 806  CYS   A O   1 
ATOM   5941 C  CB  . CYS   A 1 781 ? 20.222 45.594  25.050  1.00 14.94  ? 806  CYS   A CB  1 
ATOM   5942 S  SG  . CYS   A 1 781 ? 20.256 43.873  25.612  1.00 14.88  ? 806  CYS   A SG  1 
ATOM   5943 N  N   . ARG   A 1 782 ? 18.789 48.777  25.038  1.00 13.94  ? 807  ARG   A N   1 
ATOM   5944 C  CA  . ARG   A 1 782 ? 19.059 50.184  24.887  1.00 14.09  ? 807  ARG   A CA  1 
ATOM   5945 C  C   . ARG   A 1 782 ? 18.555 50.983  26.066  1.00 15.51  ? 807  ARG   A C   1 
ATOM   5946 O  O   . ARG   A 1 782 ? 18.804 52.188  26.116  1.00 16.26  ? 807  ARG   A O   1 
ATOM   5947 C  CB  . ARG   A 1 782 ? 18.440 50.790  23.614  1.00 14.75  ? 807  ARG   A CB  1 
ATOM   5948 C  CG  . ARG   A 1 782 ? 19.022 50.257  22.331  1.00 14.68  ? 807  ARG   A CG  1 
ATOM   5949 C  CD  . ARG   A 1 782 ? 20.555 50.434  22.265  1.00 15.75  ? 807  ARG   A CD  1 
ATOM   5950 N  NE  . ARG   A 1 782 ? 20.910 51.843  22.187  1.00 15.83  ? 807  ARG   A NE  1 
ATOM   5951 C  CZ  . ARG   A 1 782 ? 22.122 52.293  21.911  1.00 15.45  ? 807  ARG   A CZ  1 
ATOM   5952 N  NH1 . ARG   A 1 782 ? 23.151 51.447  21.805  1.00 14.48  ? 807  ARG   A NH1 1 
ATOM   5953 N  NH2 . ARG   A 1 782 ? 22.333 53.594  21.774  1.00 15.89  ? 807  ARG   A NH2 1 
ATOM   5954 N  N   . THR   A 1 783 ? 17.899 50.351  27.061  1.00 14.76  ? 808  THR   A N   1 
ATOM   5955 C  CA  . THR   A 1 783 ? 17.448 51.106  28.225  1.00 15.62  ? 808  THR   A CA  1 
ATOM   5956 C  C   . THR   A 1 783 ? 18.615 51.767  28.924  1.00 16.58  ? 808  THR   A C   1 
ATOM   5957 O  O   . THR   A 1 783 ? 19.746 51.253  28.930  1.00 16.12  ? 808  THR   A O   1 
ATOM   5958 C  CB  . THR   A 1 783 ? 16.734 50.208  29.242  1.00 16.84  ? 808  THR   A CB  1 
ATOM   5959 O  OG1 . THR   A 1 783 ? 16.205 51.020  30.304  1.00 18.24  ? 808  THR   A OG1 1 
ATOM   5960 C  CG2 . THR   A 1 783 ? 17.609 49.143  29.823  1.00 17.44  ? 808  THR   A CG2 1 
ATOM   5961 N  N   . GLN   A 1 784 ? 18.334 52.923  29.510  1.00 18.29  ? 809  GLN   A N   1 
ATOM   5962 C  CA  . GLN   A 1 784 ? 19.334 53.607  30.314  1.00 19.04  ? 809  GLN   A CA  1 
ATOM   5963 C  C   . GLN   A 1 784 ? 19.086 53.460  31.819  1.00 19.58  ? 809  GLN   A C   1 
ATOM   5964 O  O   . GLN   A 1 784 ? 19.750 54.116  32.625  1.00 20.93  ? 809  GLN   A O   1 
ATOM   5965 C  CB  . GLN   A 1 784 ? 19.476 55.068  29.889  1.00 23.00  ? 809  GLN   A CB  1 
ATOM   5966 C  CG  . GLN   A 1 784 ? 19.919 55.084  28.425  1.00 28.40  ? 809  GLN   A CG  1 
ATOM   5967 C  CD  . GLN   A 1 784 ? 20.232 56.453  27.895  1.00 34.93  ? 809  GLN   A CD  1 
ATOM   5968 O  OE1 . GLN   A 1 784 ? 20.904 56.596  26.850  1.00 37.25  ? 809  GLN   A OE1 1 
ATOM   5969 N  NE2 . GLN   A 1 784 ? 19.761 57.469  28.592  1.00 33.30  ? 809  GLN   A NE2 1 
ATOM   5970 N  N   . ASN   A 1 785 ? 18.279 52.472  32.202  1.00 17.07  ? 810  ASN   A N   1 
ATOM   5971 C  CA  . ASN   A 1 785 ? 18.007 52.118  33.585  1.00 18.52  ? 810  ASN   A CA  1 
ATOM   5972 C  C   . ASN   A 1 785 ? 18.972 50.979  33.927  1.00 19.82  ? 810  ASN   A C   1 
ATOM   5973 O  O   . ASN   A 1 785 ? 18.867 49.881  33.344  1.00 17.88  ? 810  ASN   A O   1 
ATOM   5974 C  CB  . ASN   A 1 785 ? 16.567 51.675  33.656  1.00 19.04  ? 810  ASN   A CB  1 
ATOM   5975 C  CG  . ASN   A 1 785 ? 16.169 51.243  35.012  1.00 24.05  ? 810  ASN   A CG  1 
ATOM   5976 O  OD1 . ASN   A 1 785 ? 16.852 50.489  35.705  1.00 23.42  ? 810  ASN   A OD1 1 
ATOM   5977 N  ND2 . ASN   A 1 785 ? 14.993 51.692  35.412  1.00 28.15  ? 810  ASN   A ND2 1 
ATOM   5978 N  N   . LYS   A 1 786 ? 19.941 51.238  34.770  1.00 19.92  ? 811  LYS   A N   1 
ATOM   5979 C  CA  . LYS   A 1 786 ? 20.968 50.235  35.051  1.00 19.54  ? 811  LYS   A CA  1 
ATOM   5980 C  C   . LYS   A 1 786 ? 20.441 49.021  35.784  1.00 19.74  ? 811  LYS   A C   1 
ATOM   5981 O  O   . LYS   A 1 786 ? 20.997 47.936  35.588  1.00 19.78  ? 811  LYS   A O   1 
ATOM   5982 C  CB  . LYS   A 1 786 ? 22.171 50.840  35.739  1.00 22.08  ? 811  LYS   A CB  1 
ATOM   5983 C  CG  . LYS   A 1 786 ? 22.891 51.830  34.835  1.00 24.30  ? 811  LYS   A CG  1 
ATOM   5984 C  CD  . LYS   A 1 786 ? 24.032 52.478  35.606  1.00 29.26  ? 811  LYS   A CD  1 
ATOM   5985 C  CE  . LYS   A 1 786 ? 24.607 53.672  34.900  1.00 34.62  ? 811  LYS   A CE  1 
ATOM   5986 N  NZ  . LYS   A 1 786 ? 25.785 54.198  35.655  1.00 39.93  ? 811  LYS   A NZ  1 
ATOM   5987 N  N   . GLU   A 1 787 ? 19.345 49.138  36.548  1.00 19.66  ? 812  GLU   A N   1 
ATOM   5988 C  CA  . GLU   A 1 787 ? 18.773 47.962  37.181  1.00 19.89  ? 812  GLU   A CA  1 
ATOM   5989 C  C   . GLU   A 1 787 ? 18.207 47.009  36.086  1.00 17.92  ? 812  GLU   A C   1 
ATOM   5990 O  O   . GLU   A 1 787 ? 18.330 45.789  36.216  1.00 17.83  ? 812  GLU   A O   1 
ATOM   5991 C  CB  . GLU   A 1 787 ? 17.656 48.388  38.144  1.00 23.96  ? 812  GLU   A CB  1 
ATOM   5992 C  CG  . GLU   A 1 787 ? 18.222 49.135  39.335  1.00 33.80  ? 812  GLU   A CG  1 
ATOM   5993 C  CD  . GLU   A 1 787 ? 17.302 49.167  40.539  1.00 45.20  ? 812  GLU   A CD  1 
ATOM   5994 O  OE1 . GLU   A 1 787 ? 16.088 48.918  40.370  1.00 46.97  ? 812  GLU   A OE1 1 
ATOM   5995 O  OE2 . GLU   A 1 787 ? 17.802 49.422  41.658  1.00 51.13  ? 812  GLU   A OE2 1 
ATOM   5996 N  N   . LYS   A 1 788 ? 17.580 47.579  35.040  1.00 16.79  ? 813  LYS   A N   1 
ATOM   5997 C  CA  . LYS   A 1 788 ? 17.043 46.772  33.930  1.00 16.42  ? 813  LYS   A CA  1 
ATOM   5998 C  C   . LYS   A 1 788 ? 18.184 46.143  33.118  1.00 16.30  ? 813  LYS   A C   1 
ATOM   5999 O  O   . LYS   A 1 788 ? 18.087 44.979  32.720  1.00 15.72  ? 813  LYS   A O   1 
ATOM   6000 C  CB  . LYS   A 1 788 ? 16.109 47.589  33.040  1.00 17.80  ? 813  LYS   A CB  1 
ATOM   6001 C  CG  . LYS   A 1 788 ? 14.780 47.819  33.775  1.00 20.27  ? 813  LYS   A CG  1 
ATOM   6002 C  CD  . LYS   A 1 788 ? 13.901 48.710  33.013  1.00 25.54  ? 813  LYS   A CD  1 
ATOM   6003 C  CE  . LYS   A 1 788 ? 12.492 48.708  33.565  1.00 28.69  ? 813  LYS   A CE  1 
ATOM   6004 N  NZ  . LYS   A 1 788 ? 12.446 49.484  34.821  1.00 31.59  ? 813  LYS   A NZ  1 
ATOM   6005 N  N   . LEU   A 1 789 ? 19.313 46.862  32.949  1.00 15.12  ? 814  LEU   A N   1 
ATOM   6006 C  CA  . LEU   A 1 789 ? 20.449 46.300  32.219  1.00 14.92  ? 814  LEU   A CA  1 
ATOM   6007 C  C   . LEU   A 1 789 ? 21.026 45.146  33.003  1.00 14.97  ? 814  LEU   A C   1 
ATOM   6008 O  O   . LEU   A 1 789 ? 21.322 44.100  32.425  1.00 14.71  ? 814  LEU   A O   1 
ATOM   6009 C  CB  . LEU   A 1 789 ? 21.524 47.365  32.012  1.00 14.15  ? 814  LEU   A CB  1 
ATOM   6010 C  CG  . LEU   A 1 789 ? 21.132 48.467  31.020  1.00 14.73  ? 814  LEU   A CG  1 
ATOM   6011 C  CD1 . LEU   A 1 789 ? 22.183 49.580  30.971  1.00 15.39  ? 814  LEU   A CD1 1 
ATOM   6012 C  CD2 . LEU   A 1 789 ? 20.918 47.896  29.620  1.00 16.01  ? 814  LEU   A CD2 1 
ATOM   6013 N  N   . GLN   A 1 790 ? 21.180 45.307  34.324  1.00 14.99  ? 815  GLN   A N   1 
ATOM   6014 C  CA  . GLN   A 1 790 ? 21.750 44.223  35.129  1.00 15.22  ? 815  GLN   A CA  1 
ATOM   6015 C  C   . GLN   A 1 790 ? 20.801 43.027  35.114  1.00 15.39  ? 815  GLN   A C   1 
ATOM   6016 O  O   . GLN   A 1 790 ? 21.258 41.893  35.080  1.00 15.85  ? 815  GLN   A O   1 
ATOM   6017 C  CB  . GLN   A 1 790 ? 21.941 44.708  36.578  1.00 15.71  ? 815  GLN   A CB  1 
ATOM   6018 C  CG  . GLN   A 1 790 ? 22.615 43.680  37.462  1.00 17.65  ? 815  GLN   A CG  1 
ATOM   6019 C  CD  . GLN   A 1 790 ? 24.010 43.382  37.019  1.00 19.41  ? 815  GLN   A CD  1 
ATOM   6020 O  OE1 . GLN   A 1 790 ? 24.818 44.277  36.765  1.00 18.89  ? 815  GLN   A OE1 1 
ATOM   6021 N  NE2 . GLN   A 1 790 ? 24.298 42.095  36.953  1.00 24.54  ? 815  GLN   A NE2 1 
ATOM   6022 N  N   . TRP   A 1 791 ? 19.481 43.278  35.098  1.00 14.69  ? 816  TRP   A N   1 
ATOM   6023 C  CA  . TRP   A 1 791 ? 18.498 42.208  35.056  1.00 14.77  ? 816  TRP   A CA  1 
ATOM   6024 C  C   . TRP   A 1 791 ? 18.640 41.425  33.759  1.00 15.19  ? 816  TRP   A C   1 
ATOM   6025 O  O   . TRP   A 1 791 ? 18.543 40.182  33.757  1.00 15.88  ? 816  TRP   A O   1 
ATOM   6026 C  CB  . TRP   A 1 791 ? 17.074 42.812  35.223  1.00 16.36  ? 816  TRP   A CB  1 
ATOM   6027 C  CG  . TRP   A 1 791 ? 15.984 41.783  35.289  1.00 18.05  ? 816  TRP   A CG  1 
ATOM   6028 C  CD1 . TRP   A 1 791 ? 15.436 41.251  36.422  1.00 20.66  ? 816  TRP   A CD1 1 
ATOM   6029 C  CD2 . TRP   A 1 791 ? 15.290 41.187  34.185  1.00 19.16  ? 816  TRP   A CD2 1 
ATOM   6030 N  NE1 . TRP   A 1 791 ? 14.415 40.387  36.089  1.00 21.18  ? 816  TRP   A NE1 1 
ATOM   6031 C  CE2 . TRP   A 1 791 ? 14.297 40.340  34.721  1.00 21.04  ? 816  TRP   A CE2 1 
ATOM   6032 C  CE3 . TRP   A 1 791 ? 15.358 41.346  32.790  1.00 20.95  ? 816  TRP   A CE3 1 
ATOM   6033 C  CZ2 . TRP   A 1 791 ? 13.440 39.591  33.911  1.00 22.73  ? 816  TRP   A CZ2 1 
ATOM   6034 C  CZ3 . TRP   A 1 791 ? 14.523 40.586  31.984  1.00 22.52  ? 816  TRP   A CZ3 1 
ATOM   6035 C  CH2 . TRP   A 1 791 ? 13.591 39.708  32.546  1.00 23.25  ? 816  TRP   A CH2 1 
ATOM   6036 N  N   . LEU   A 1 792 ? 18.838 42.133  32.628  1.00 13.71  ? 817  LEU   A N   1 
ATOM   6037 C  CA  . LEU   A 1 792 ? 19.003 41.412  31.338  1.00 13.32  ? 817  LEU   A CA  1 
ATOM   6038 C  C   . LEU   A 1 792 ? 20.217 40.506  31.388  1.00 13.98  ? 817  LEU   A C   1 
ATOM   6039 O  O   . LEU   A 1 792 ? 20.184 39.389  30.849  1.00 14.06  ? 817  LEU   A O   1 
ATOM   6040 C  CB  . LEU   A 1 792 ? 19.147 42.425  30.200  1.00 13.69  ? 817  LEU   A CB  1 
ATOM   6041 C  CG  . LEU   A 1 792 ? 17.857 43.162  29.895  1.00 14.61  ? 817  LEU   A CG  1 
ATOM   6042 C  CD1 . LEU   A 1 792 ? 18.157 44.406  29.042  1.00 14.96  ? 817  LEU   A CD1 1 
ATOM   6043 C  CD2 . LEU   A 1 792 ? 16.841 42.262  29.125  1.00 15.12  ? 817  LEU   A CD2 1 
ATOM   6044 N  N   . LEU   A 1 793 ? 21.314 40.999  31.968  1.00 14.28  ? 818  LEU   A N   1 
ATOM   6045 C  CA  . LEU   A 1 793 ? 22.521 40.151  32.076  1.00 13.23  ? 818  LEU   A CA  1 
ATOM   6046 C  C   . LEU   A 1 793 ? 22.254 38.978  33.001  1.00 14.46  ? 818  LEU   A C   1 
ATOM   6047 O  O   . LEU   A 1 793 ? 22.568 37.836  32.632  1.00 15.01  ? 818  LEU   A O   1 
ATOM   6048 C  CB  . LEU   A 1 793 ? 23.677 40.988  32.650  1.00 13.71  ? 818  LEU   A CB  1 
ATOM   6049 C  CG  . LEU   A 1 793 ? 24.143 42.113  31.736  1.00 14.32  ? 818  LEU   A CG  1 
ATOM   6050 C  CD1 . LEU   A 1 793 ? 25.150 43.005  32.492  1.00 16.07  ? 818  LEU   A CD1 1 
ATOM   6051 C  CD2 . LEU   A 1 793 ? 24.797 41.559  30.467  1.00 16.34  ? 818  LEU   A CD2 1 
ATOM   6052 N  N   . ASP   A 1 794 ? 21.682 39.233  34.183  1.00 15.13  ? 819  ASP   A N   1 
ATOM   6053 C  CA  . ASP   A 1 794 ? 21.440 38.126  35.132  1.00 15.89  ? 819  ASP   A CA  1 
ATOM   6054 C  C   . ASP   A 1 794 ? 20.488 37.095  34.548  1.00 15.81  ? 819  ASP   A C   1 
ATOM   6055 O  O   . ASP   A 1 794 ? 20.701 35.878  34.696  1.00 16.92  ? 819  ASP   A O   1 
ATOM   6056 C  CB  . ASP   A 1 794 ? 20.817 38.689  36.423  1.00 16.70  ? 819  ASP   A CB  1 
ATOM   6057 C  CG  . ASP   A 1 794 ? 21.787 39.480  37.284  1.00 20.39  ? 819  ASP   A CG  1 
ATOM   6058 O  OD1 . ASP   A 1 794 ? 22.992 39.253  37.175  1.00 22.37  ? 819  ASP   A OD1 1 
ATOM   6059 O  OD2 . ASP   A 1 794 ? 21.316 40.335  38.079  1.00 23.43  ? 819  ASP   A OD2 1 
ATOM   6060 N  N   . GLU   A 1 795 ? 19.436 37.563  33.887  1.00 14.73  ? 820  GLU   A N   1 
ATOM   6061 C  CA  . GLU   A 1 795 ? 18.416 36.632  33.420  1.00 14.93  ? 820  GLU   A CA  1 
ATOM   6062 C  C   . GLU   A 1 795 ? 18.832 35.844  32.203  1.00 14.74  ? 820  GLU   A C   1 
ATOM   6063 O  O   . GLU   A 1 795 ? 18.527 34.662  32.130  1.00 15.28  ? 820  GLU   A O   1 
ATOM   6064 C  CB  . GLU   A 1 795 ? 17.075 37.348  33.203  1.00 18.08  ? 820  GLU   A CB  1 
ATOM   6065 C  CG  . GLU   A 1 795 ? 16.562 37.861  34.548  1.00 23.54  ? 820  GLU   A CG  1 
ATOM   6066 C  CD  . GLU   A 1 795 ? 16.144 36.798  35.555  1.00 30.68  ? 820  GLU   A CD  1 
ATOM   6067 O  OE1 . GLU   A 1 795 ? 15.687 35.721  35.111  1.00 27.70  ? 820  GLU   A OE1 1 
ATOM   6068 O  OE2 . GLU   A 1 795 ? 16.289 37.035  36.783  1.00 33.06  ? 820  GLU   A OE2 1 
ATOM   6069 N  N   . SER   A 1 796 ? 19.532 36.472  31.256  1.00 14.19  ? 821  SER   A N   1 
ATOM   6070 C  CA  . SER   A 1 796 ? 20.018 35.695  30.113  1.00 14.11  ? 821  SER   A CA  1 
ATOM   6071 C  C   . SER   A 1 796 ? 21.131 34.769  30.539  1.00 15.41  ? 821  SER   A C   1 
ATOM   6072 O  O   . SER   A 1 796 ? 21.278 33.676  29.973  1.00 16.55  ? 821  SER   A O   1 
ATOM   6073 C  CB  . SER   A 1 796 ? 20.396 36.627  28.959  1.00 13.97  ? 821  SER   A CB  1 
ATOM   6074 O  OG  . SER   A 1 796 ? 21.491 37.478  29.302  1.00 16.14  ? 821  SER   A OG  1 
ATOM   6075 N  N   . PHE   A 1 797 ? 21.949 35.156  31.539  1.00 15.19  ? 822  PHE   A N   1 
ATOM   6076 C  CA  . PHE   A 1 797 ? 23.003 34.247  32.048  1.00 16.05  ? 822  PHE   A CA  1 
ATOM   6077 C  C   . PHE   A 1 797 ? 22.314 33.001  32.661  1.00 17.62  ? 822  PHE   A C   1 
ATOM   6078 O  O   . PHE   A 1 797 ? 22.781 31.868  32.433  1.00 18.98  ? 822  PHE   A O   1 
ATOM   6079 C  CB  . PHE   A 1 797 ? 23.810 35.009  33.139  1.00 17.87  ? 822  PHE   A CB  1 
ATOM   6080 C  CG  . PHE   A 1 797 ? 24.818 34.203  33.928  1.00 20.01  ? 822  PHE   A CG  1 
ATOM   6081 C  CD1 . PHE   A 1 797 ? 25.990 33.780  33.346  1.00 22.20  ? 822  PHE   A CD1 1 
ATOM   6082 C  CD2 . PHE   A 1 797 ? 24.630 33.960  35.281  1.00 22.08  ? 822  PHE   A CD2 1 
ATOM   6083 C  CE1 . PHE   A 1 797 ? 26.944 33.072  34.088  1.00 22.88  ? 822  PHE   A CE1 1 
ATOM   6084 C  CE2 . PHE   A 1 797 ? 25.581 33.242  36.018  1.00 24.32  ? 822  PHE   A CE2 1 
ATOM   6085 C  CZ  . PHE   A 1 797 ? 26.735 32.832  35.418  1.00 23.57  ? 822  PHE   A CZ  1 
ATOM   6086 N  N   . LYS   A 1 798 ? 21.213 33.204  33.390  1.00 16.41  ? 823  LYS   A N   1 
ATOM   6087 C  CA  . LYS   A 1 798 ? 20.486 32.101  34.049  1.00 16.95  ? 823  LYS   A CA  1 
ATOM   6088 C  C   . LYS   A 1 798 ? 19.770 31.220  33.033  1.00 18.06  ? 823  LYS   A C   1 
ATOM   6089 O  O   . LYS   A 1 798 ? 19.673 29.997  33.247  1.00 19.37  ? 823  LYS   A O   1 
ATOM   6090 C  CB  . LYS   A 1 798 ? 19.448 32.702  35.010  1.00 19.26  ? 823  LYS   A CB  1 
ATOM   6091 C  CG  . LYS   A 1 798 ? 18.663 31.667  35.785  1.00 23.53  ? 823  LYS   A CG  1 
ATOM   6092 C  CD  . LYS   A 1 798 ? 17.779 32.351  36.821  1.00 30.99  ? 823  LYS   A CD  1 
ATOM   6093 C  CE  . LYS   A 1 798 ? 16.945 31.416  37.668  1.00 37.03  ? 823  LYS   A CE  1 
ATOM   6094 N  NZ  . LYS   A 1 798 ? 16.188 32.197  38.704  1.00 38.90  ? 823  LYS   A NZ  1 
ATOM   6095 N  N   . GLY   A 1 799 ? 19.210 31.826  31.975  1.00 18.03  ? 824  GLY   A N   1 
ATOM   6096 C  CA  . GLY   A 1 799 ? 18.605 31.098  30.862  1.00 18.51  ? 824  GLY   A CA  1 
ATOM   6097 C  C   . GLY   A 1 799 ? 17.143 30.712  30.916  1.00 20.26  ? 824  GLY   A C   1 
ATOM   6098 O  O   . GLY   A 1 799 ? 16.650 30.059  29.977  1.00 22.53  ? 824  GLY   A O   1 
ATOM   6099 N  N   . ASP   A 1 800 ? 16.447 31.151  31.948  1.00 20.71  ? 825  ASP   A N   1 
ATOM   6100 C  CA  A ASP   A 1 800 ? 15.033 30.828  32.167  0.50 21.93  ? 825  ASP   A CA  1 
ATOM   6101 C  CA  B ASP   A 1 800 ? 15.028 30.806  32.094  0.50 21.87  ? 825  ASP   A CA  1 
ATOM   6102 C  C   . ASP   A 1 800 ? 14.129 31.771  31.350  1.00 22.02  ? 825  ASP   A C   1 
ATOM   6103 O  O   . ASP   A 1 800 ? 13.354 31.306  30.537  1.00 25.42  ? 825  ASP   A O   1 
ATOM   6104 C  CB  A ASP   A 1 800 ? 14.755 30.914  33.693  0.50 24.15  ? 825  ASP   A CB  1 
ATOM   6105 C  CB  B ASP   A 1 800 ? 14.628 30.720  33.572  0.50 23.96  ? 825  ASP   A CB  1 
ATOM   6106 C  CG  A ASP   A 1 800 ? 13.310 31.030  34.117  0.50 29.84  ? 825  ASP   A CG  1 
ATOM   6107 C  CG  B ASP   A 1 800 ? 15.210 29.521  34.280  0.50 28.74  ? 825  ASP   A CG  1 
ATOM   6108 O  OD1 A ASP   A 1 800 ? 12.463 30.379  33.493  0.50 30.84  ? 825  ASP   A OD1 1 
ATOM   6109 O  OD1 B ASP   A 1 800 ? 15.477 28.505  33.606  0.50 30.30  ? 825  ASP   A OD1 1 
ATOM   6110 O  OD2 A ASP   A 1 800 ? 13.036 31.766  35.095  0.50 33.41  ? 825  ASP   A OD2 1 
ATOM   6111 O  OD2 B ASP   A 1 800 ? 15.410 29.600  35.507  0.50 32.08  ? 825  ASP   A OD2 1 
ATOM   6112 N  N   . LYS   A 1 801 ? 14.196 33.076  31.632  1.00 20.87  ? 826  LYS   A N   1 
ATOM   6113 C  CA  . LYS   A 1 801 ? 13.325 34.059  30.958  1.00 21.10  ? 826  LYS   A CA  1 
ATOM   6114 C  C   . LYS   A 1 801 ? 13.831 34.421  29.582  1.00 19.27  ? 826  LYS   A C   1 
ATOM   6115 O  O   . LYS   A 1 801 ? 13.046 34.788  28.701  1.00 20.83  ? 826  LYS   A O   1 
ATOM   6116 C  CB  . LYS   A 1 801 ? 13.116 35.331  31.795  1.00 23.56  ? 826  LYS   A CB  1 
ATOM   6117 C  CG  . LYS   A 1 801 ? 12.462 35.073  33.163  1.00 29.71  ? 826  LYS   A CG  1 
ATOM   6118 C  CD  . LYS   A 1 801 ? 11.134 34.334  33.073  1.00 36.05  ? 826  LYS   A CD  1 
ATOM   6119 C  CE  . LYS   A 1 801 ? 10.374 34.342  34.397  1.00 40.87  ? 826  LYS   A CE  1 
ATOM   6120 N  NZ  . LYS   A 1 801 ? 8.986  33.805  34.239  1.00 43.92  ? 826  LYS   A NZ  1 
ATOM   6121 N  N   . ILE   A 1 802 ? 15.158 34.471  29.455  1.00 16.15  ? 827  ILE   A N   1 
ATOM   6122 C  CA  . ILE   A 1 802 ? 15.846 34.737  28.188  1.00 14.44  ? 827  ILE   A CA  1 
ATOM   6123 C  C   . ILE   A 1 802 ? 16.884 33.633  28.110  1.00 14.17  ? 827  ILE   A C   1 
ATOM   6124 O  O   . ILE   A 1 802 ? 17.629 33.436  29.071  1.00 15.20  ? 827  ILE   A O   1 
ATOM   6125 C  CB  . ILE   A 1 802 ? 16.504 36.135  28.161  1.00 15.29  ? 827  ILE   A CB  1 
ATOM   6126 C  CG1 . ILE   A 1 802 ? 15.414 37.259  28.303  1.00 17.03  ? 827  ILE   A CG1 1 
ATOM   6127 C  CG2 . ILE   A 1 802 ? 17.297 36.265  26.854  1.00 16.69  ? 827  ILE   A CG2 1 
ATOM   6128 C  CD1 . ILE   A 1 802 ? 16.052 38.640  28.545  1.00 18.79  ? 827  ILE   A CD1 1 
ATOM   6129 N  N   . LYS   A 1 803 ? 16.931 32.924  26.982  1.00 13.19  ? 828  LYS   A N   1 
ATOM   6130 C  CA  . LYS   A 1 803 ? 17.857 31.795  26.892  1.00 13.16  ? 828  LYS   A CA  1 
ATOM   6131 C  C   . LYS   A 1 803 ? 19.325 32.210  26.895  1.00 13.34  ? 828  LYS   A C   1 
ATOM   6132 O  O   . LYS   A 1 803 ? 19.678 33.244  26.307  1.00 13.99  ? 828  LYS   A O   1 
ATOM   6133 C  CB  . LYS   A 1 803 ? 17.571 30.964  25.643  1.00 13.84  ? 828  LYS   A CB  1 
ATOM   6134 C  CG  . LYS   A 1 803 ? 16.336 30.092  25.841  1.00 13.75  ? 828  LYS   A CG  1 
ATOM   6135 C  CD  . LYS   A 1 803 ? 16.052 29.249  24.583  1.00 15.28  ? 828  LYS   A CD  1 
ATOM   6136 C  CE  . LYS   A 1 803 ? 15.115 28.076  24.873  1.00 15.31  ? 828  LYS   A CE  1 
ATOM   6137 N  NZ  . LYS   A 1 803 ? 15.709 27.122  25.854  1.00 16.10  ? 828  LYS   A NZ  1 
ATOM   6138 N  N   . THR   A 1 804 ? 20.169 31.351  27.499  1.00 13.31  ? 829  THR   A N   1 
ATOM   6139 C  CA  . THR   A 1 804 ? 21.602 31.646  27.561  1.00 12.75  ? 829  THR   A CA  1 
ATOM   6140 C  C   . THR   A 1 804 ? 22.247 31.722  26.181  1.00 12.60  ? 829  THR   A C   1 
ATOM   6141 O  O   . THR   A 1 804 ? 23.283 32.392  26.021  1.00 12.98  ? 829  THR   A O   1 
ATOM   6142 C  CB  . THR   A 1 804 ? 22.285 30.648  28.474  1.00 14.66  ? 829  THR   A CB  1 
ATOM   6143 O  OG1 . THR   A 1 804 ? 21.621 30.684  29.748  1.00 15.69  ? 829  THR   A OG1 1 
ATOM   6144 C  CG2 . THR   A 1 804 ? 23.773 30.954  28.671  1.00 15.26  ? 829  THR   A CG2 1 
ATOM   6145 N  N   . GLN   A 1 805 ? 21.617 31.106  25.162  1.00 12.21  ? 830  GLN   A N   1 
ATOM   6146 C  CA  . GLN   A 1 805 ? 22.189 31.245  23.806  1.00 12.41  ? 830  GLN   A CA  1 
ATOM   6147 C  C   . GLN   A 1 805 ? 22.176 32.696  23.329  1.00 12.41  ? 830  GLN   A C   1 
ATOM   6148 O  O   . GLN   A 1 805 ? 22.903 33.042  22.394  1.00 13.17  ? 830  GLN   A O   1 
ATOM   6149 C  CB  . GLN   A 1 805 ? 21.411 30.354  22.800  1.00 13.01  ? 830  GLN   A CB  1 
ATOM   6150 C  CG  . GLN   A 1 805 ? 19.973 30.847  22.548  1.00 13.63  ? 830  GLN   A CG  1 
ATOM   6151 C  CD  . GLN   A 1 805 ? 19.213 29.943  21.623  1.00 13.55  ? 830  GLN   A CD  1 
ATOM   6152 O  OE1 . GLN   A 1 805 ? 19.742 28.957  21.078  1.00 13.37  ? 830  GLN   A OE1 1 
ATOM   6153 N  NE2 . GLN   A 1 805 ? 17.950 30.328  21.405  1.00 13.57  ? 830  GLN   A NE2 1 
ATOM   6154 N  N   . GLU   A 1 806 ? 21.346 33.560  23.971  1.00 12.71  ? 831  GLU   A N   1 
ATOM   6155 C  CA  . GLU   A 1 806 ? 21.337 34.991  23.651  1.00 13.08  ? 831  GLU   A CA  1 
ATOM   6156 C  C   . GLU   A 1 806 ? 22.286 35.822  24.509  1.00 13.50  ? 831  GLU   A C   1 
ATOM   6157 O  O   . GLU   A 1 806 ? 22.515 36.999  24.200  1.00 13.79  ? 831  GLU   A O   1 
ATOM   6158 C  CB  . GLU   A 1 806 ? 19.953 35.556  23.886  1.00 12.83  ? 831  GLU   A CB  1 
ATOM   6159 C  CG  . GLU   A 1 806 ? 18.898 34.900  22.992  1.00 13.36  ? 831  GLU   A CG  1 
ATOM   6160 C  CD  . GLU   A 1 806 ? 19.224 35.050  21.520  1.00 16.35  ? 831  GLU   A CD  1 
ATOM   6161 O  OE1 . GLU   A 1 806 ? 19.036 36.150  20.950  1.00 16.55  ? 831  GLU   A OE1 1 
ATOM   6162 O  OE2 . GLU   A 1 806 ? 19.719 34.065  20.935  1.00 19.29  ? 831  GLU   A OE2 1 
ATOM   6163 N  N   . PHE   A 1 807 ? 22.833 35.212  25.578  1.00 13.29  ? 832  PHE   A N   1 
ATOM   6164 C  CA  . PHE   A 1 807 ? 23.690 35.982  26.480  1.00 12.96  ? 832  PHE   A CA  1 
ATOM   6165 C  C   . PHE   A 1 807 ? 24.892 36.619  25.789  1.00 13.52  ? 832  PHE   A C   1 
ATOM   6166 O  O   . PHE   A 1 807 ? 25.160 37.795  26.035  1.00 13.25  ? 832  PHE   A O   1 
ATOM   6167 C  CB  . PHE   A 1 807 ? 24.126 35.100  27.690  1.00 13.35  ? 832  PHE   A CB  1 
ATOM   6168 C  CG  . PHE   A 1 807 ? 25.112 35.824  28.571  1.00 13.07  ? 832  PHE   A CG  1 
ATOM   6169 C  CD1 . PHE   A 1 807 ? 24.675 36.702  29.550  1.00 14.85  ? 832  PHE   A CD1 1 
ATOM   6170 C  CD2 . PHE   A 1 807 ? 26.471 35.689  28.356  1.00 12.91  ? 832  PHE   A CD2 1 
ATOM   6171 C  CE1 . PHE   A 1 807 ? 25.600 37.402  30.333  1.00 14.44  ? 832  PHE   A CE1 1 
ATOM   6172 C  CE2 . PHE   A 1 807 ? 27.380 36.407  29.101  1.00 13.88  ? 832  PHE   A CE2 1 
ATOM   6173 C  CZ  . PHE   A 1 807 ? 26.939 37.262  30.077  1.00 14.09  ? 832  PHE   A CZ  1 
ATOM   6174 N  N   . PRO   A 1 808 ? 25.630 35.966  24.885  1.00 12.65  ? 833  PRO   A N   1 
ATOM   6175 C  CA  . PRO   A 1 808 ? 26.788 36.653  24.295  1.00 12.92  ? 833  PRO   A CA  1 
ATOM   6176 C  C   . PRO   A 1 808 ? 26.375 37.932  23.573  1.00 13.75  ? 833  PRO   A C   1 
ATOM   6177 O  O   . PRO   A 1 808 ? 27.098 38.953  23.647  1.00 14.44  ? 833  PRO   A O   1 
ATOM   6178 C  CB  . PRO   A 1 808 ? 27.409 35.601  23.359  1.00 14.61  ? 833  PRO   A CB  1 
ATOM   6179 C  CG  . PRO   A 1 808 ? 26.945 34.237  24.023  1.00 15.03  ? 833  PRO   A CG  1 
ATOM   6180 C  CD  . PRO   A 1 808 ? 25.554 34.537  24.506  1.00 14.09  ? 833  PRO   A CD  1 
ATOM   6181 N  N   . GLN   A 1 809 ? 25.275 37.876  22.829  1.00 13.41  ? 834  GLN   A N   1 
ATOM   6182 C  CA  . GLN   A 1 809 ? 24.865 39.062  22.092  1.00 12.97  ? 834  GLN   A CA  1 
ATOM   6183 C  C   . GLN   A 1 809 ? 24.368 40.127  23.056  1.00 13.07  ? 834  GLN   A C   1 
ATOM   6184 O  O   . GLN   A 1 809 ? 24.715 41.308  22.875  1.00 13.28  ? 834  GLN   A O   1 
ATOM   6185 C  CB  . GLN   A 1 809 ? 23.795 38.708  21.088  1.00 15.07  ? 834  GLN   A CB  1 
ATOM   6186 C  CG  . GLN   A 1 809 ? 23.470 39.905  20.195  1.00 18.82  ? 834  GLN   A CG  1 
ATOM   6187 C  CD  . GLN   A 1 809 ? 22.558 39.501  19.082  1.00 27.60  ? 834  GLN   A CD  1 
ATOM   6188 O  OE1 . GLN   A 1 809 ? 21.642 38.658  19.251  1.00 27.17  ? 834  GLN   A OE1 1 
ATOM   6189 N  NE2 . GLN   A 1 809 ? 22.775 40.119  17.923  1.00 33.63  ? 834  GLN   A NE2 1 
ATOM   6190 N  N   . ILE   A 1 810 ? 23.581 39.747  24.071  1.00 12.41  ? 835  ILE   A N   1 
ATOM   6191 C  CA  . ILE   A 1 810 ? 23.104 40.718  25.032  1.00 11.92  ? 835  ILE   A CA  1 
ATOM   6192 C  C   . ILE   A 1 810 ? 24.262 41.377  25.779  1.00 13.10  ? 835  ILE   A C   1 
ATOM   6193 O  O   . ILE   A 1 810 ? 24.232 42.597  25.995  1.00 13.26  ? 835  ILE   A O   1 
ATOM   6194 C  CB  . ILE   A 1 810 ? 22.102 40.052  25.957  1.00 13.49  ? 835  ILE   A CB  1 
ATOM   6195 C  CG1 . ILE   A 1 810 ? 20.793 39.863  25.154  1.00 13.99  ? 835  ILE   A CG1 1 
ATOM   6196 C  CG2 . ILE   A 1 810 ? 21.883 40.837  27.271  1.00 14.77  ? 835  ILE   A CG2 1 
ATOM   6197 C  CD1 . ILE   A 1 810 ? 19.836 38.864  25.890  1.00 15.28  ? 835  ILE   A CD1 1 
ATOM   6198 N  N   . LEU   A 1 811 ? 25.294 40.605  26.145  1.00 13.01  ? 836  LEU   A N   1 
ATOM   6199 C  CA  . LEU   A 1 811 ? 26.433 41.194  26.856  1.00 11.59  ? 836  LEU   A CA  1 
ATOM   6200 C  C   . LEU   A 1 811 ? 27.121 42.231  25.960  1.00 12.33  ? 836  LEU   A C   1 
ATOM   6201 O  O   . LEU   A 1 811 ? 27.459 43.326  26.447  1.00 13.11  ? 836  LEU   A O   1 
ATOM   6202 C  CB  . LEU   A 1 811 ? 27.409 40.049  27.174  1.00 12.27  ? 836  LEU   A CB  1 
ATOM   6203 C  CG  . LEU   A 1 811 ? 28.620 40.517  27.926  1.00 12.62  ? 836  LEU   A CG  1 
ATOM   6204 C  CD1 . LEU   A 1 811 ? 28.274 40.820  29.372  1.00 13.43  ? 836  LEU   A CD1 1 
ATOM   6205 C  CD2 . LEU   A 1 811 ? 29.727 39.418  27.938  1.00 13.55  ? 836  LEU   A CD2 1 
ATOM   6206 N  N   . THR   A 1 812 ? 27.302 41.955  24.657  1.00 12.20  ? 837  THR   A N   1 
ATOM   6207 C  CA  . THR   A 1 812 ? 27.945 42.955  23.789  1.00 12.15  ? 837  THR   A CA  1 
ATOM   6208 C  C   . THR   A 1 812 ? 27.021 44.141  23.577  1.00 12.64  ? 837  THR   A C   1 
ATOM   6209 O  O   . THR   A 1 812 ? 27.502 45.284  23.552  1.00 13.18  ? 837  THR   A O   1 
ATOM   6210 C  CB  . THR   A 1 812 ? 28.259 42.323  22.460  1.00 14.18  ? 837  THR   A CB  1 
ATOM   6211 O  OG1 . THR   A 1 812 ? 29.295 41.360  22.700  1.00 17.93  ? 837  THR   A OG1 1 
ATOM   6212 C  CG2 . THR   A 1 812 ? 28.751 43.337  21.417  1.00 16.11  ? 837  THR   A CG2 1 
ATOM   6213 N  N   . LEU   A 1 813 ? 25.698 43.931  23.428  1.00 12.26  ? 838  LEU   A N   1 
ATOM   6214 C  CA  . LEU   A 1 813 ? 24.806 45.088  23.234  1.00 11.77  ? 838  LEU   A CA  1 
ATOM   6215 C  C   . LEU   A 1 813 ? 24.857 45.995  24.480  1.00 12.25  ? 838  LEU   A C   1 
ATOM   6216 O  O   . LEU   A 1 813 ? 24.840 47.231  24.339  1.00 13.24  ? 838  LEU   A O   1 
ATOM   6217 C  CB  . LEU   A 1 813 ? 23.370 44.628  23.015  1.00 12.15  ? 838  LEU   A CB  1 
ATOM   6218 C  CG  . LEU   A 1 813 ? 23.156 43.878  21.692  1.00 13.89  ? 838  LEU   A CG  1 
ATOM   6219 C  CD1 . LEU   A 1 813 ? 21.741 43.380  21.626  1.00 14.99  ? 838  LEU   A CD1 1 
ATOM   6220 C  CD2 . LEU   A 1 813 ? 23.449 44.793  20.479  1.00 15.16  ? 838  LEU   A CD2 1 
ATOM   6221 N  N   . ILE   A 1 814 ? 24.890 45.385  25.678  1.00 11.93  ? 839  ILE   A N   1 
ATOM   6222 C  CA  . ILE   A 1 814 ? 24.972 46.219  26.878  1.00 12.31  ? 839  ILE   A CA  1 
ATOM   6223 C  C   . ILE   A 1 814 ? 26.358 46.855  27.018  1.00 13.13  ? 839  ILE   A C   1 
ATOM   6224 O  O   . ILE   A 1 814 ? 26.475 48.006  27.408  1.00 13.94  ? 839  ILE   A O   1 
ATOM   6225 C  CB  . ILE   A 1 814 ? 24.516 45.393  28.096  1.00 13.12  ? 839  ILE   A CB  1 
ATOM   6226 C  CG1 . ILE   A 1 814 ? 23.047 45.038  27.891  1.00 13.02  ? 839  ILE   A CG1 1 
ATOM   6227 C  CG2 . ILE   A 1 814 ? 24.776 46.152  29.420  1.00 14.20  ? 839  ILE   A CG2 1 
ATOM   6228 C  CD1 . ILE   A 1 814 ? 22.438 44.180  28.990  1.00 14.74  ? 839  ILE   A CD1 1 
ATOM   6229 N  N   . GLY   A 1 815 ? 27.397 46.163  26.555  1.00 12.87  ? 840  GLY   A N   1 
ATOM   6230 C  CA  . GLY   A 1 815 ? 28.742 46.724  26.495  1.00 12.78  ? 840  GLY   A CA  1 
ATOM   6231 C  C   . GLY   A 1 815 ? 28.836 47.900  25.561  1.00 13.43  ? 840  GLY   A C   1 
ATOM   6232 O  O   . GLY   A 1 815 ? 29.792 48.670  25.628  1.00 13.66  ? 840  GLY   A O   1 
ATOM   6233 N  N   . ARG   A 1 816 ? 27.878 48.026  24.610  1.00 13.09  ? 841  ARG   A N   1 
ATOM   6234 C  CA  . ARG   A 1 816 ? 27.867 49.146  23.677  1.00 13.51  ? 841  ARG   A CA  1 
ATOM   6235 C  C   . ARG   A 1 816 ? 26.840 50.218  24.074  1.00 15.95  ? 841  ARG   A C   1 
ATOM   6236 O  O   . ARG   A 1 816 ? 26.779 51.264  23.445  1.00 17.38  ? 841  ARG   A O   1 
ATOM   6237 C  CB  . ARG   A 1 816 ? 27.604 48.643  22.262  1.00 14.11  ? 841  ARG   A CB  1 
ATOM   6238 C  CG  . ARG   A 1 816 ? 28.822 47.894  21.731  1.00 15.08  ? 841  ARG   A CG  1 
ATOM   6239 C  CD  . ARG   A 1 816 ? 28.396 47.157  20.472  1.00 17.71  ? 841  ARG   A CD  1 
ATOM   6240 N  NE  . ARG   A 1 816 ? 29.588 46.608  19.840  1.00 18.52  ? 841  ARG   A NE  1 
ATOM   6241 C  CZ  . ARG   A 1 816 ? 29.599 46.119  18.600  1.00 25.70  ? 841  ARG   A CZ  1 
ATOM   6242 N  NH1 . ARG   A 1 816 ? 30.738 45.727  18.049  1.00 27.34  ? 841  ARG   A NH1 1 
ATOM   6243 N  NH2 . ARG   A 1 816 ? 28.490 46.121  17.866  1.00 26.12  ? 841  ARG   A NH2 1 
ATOM   6244 N  N   . ASN   A 1 817 ? 26.089 50.010  25.152  1.00 13.90  ? 842  ASN   A N   1 
ATOM   6245 C  CA  . ASN   A 1 817 ? 25.095 51.000  25.598  1.00 13.56  ? 842  ASN   A CA  1 
ATOM   6246 C  C   . ASN   A 1 817 ? 25.844 52.171  26.189  1.00 16.38  ? 842  ASN   A C   1 
ATOM   6247 O  O   . ASN   A 1 817 ? 26.777 51.960  26.949  1.00 18.50  ? 842  ASN   A O   1 
ATOM   6248 C  CB  . ASN   A 1 817 ? 24.211 50.287  26.626  1.00 14.90  ? 842  ASN   A CB  1 
ATOM   6249 C  CG  . ASN   A 1 817 ? 23.154 51.147  27.215  1.00 15.38  ? 842  ASN   A CG  1 
ATOM   6250 O  OD1 . ASN   A 1 817 ? 23.473 52.165  27.839  1.00 18.43  ? 842  ASN   A OD1 1 
ATOM   6251 N  ND2 . ASN   A 1 817 ? 21.923 50.669  27.162  1.00 15.12  ? 842  ASN   A ND2 1 
ATOM   6252 N  N   . PRO   A 1 818 ? 25.507 53.397  25.795  1.00 17.06  ? 843  PRO   A N   1 
ATOM   6253 C  CA  . PRO   A 1 818 ? 26.291 54.567  26.267  1.00 18.87  ? 843  PRO   A CA  1 
ATOM   6254 C  C   . PRO   A 1 818 ? 26.245 54.836  27.747  1.00 22.24  ? 843  PRO   A C   1 
ATOM   6255 O  O   . PRO   A 1 818 ? 27.099 55.584  28.199  1.00 23.66  ? 843  PRO   A O   1 
ATOM   6256 C  CB  . PRO   A 1 818 ? 25.704 55.736  25.469  1.00 20.47  ? 843  PRO   A CB  1 
ATOM   6257 C  CG  . PRO   A 1 818 ? 24.388 55.307  25.024  1.00 20.18  ? 843  PRO   A CG  1 
ATOM   6258 C  CD  . PRO   A 1 818 ? 24.447 53.785  24.859  1.00 17.74  ? 843  PRO   A CD  1 
ATOM   6259 N  N   . VAL   A 1 819 ? 25.237 54.339  28.483  1.00 22.20  ? 844  VAL   A N   1 
ATOM   6260 C  CA  . VAL   A 1 819 ? 25.234 54.577  29.928  1.00 25.28  ? 844  VAL   A CA  1 
ATOM   6261 C  C   . VAL   A 1 819 ? 25.674 53.360  30.704  1.00 24.99  ? 844  VAL   A C   1 
ATOM   6262 O  O   . VAL   A 1 819 ? 26.365 53.499  31.719  1.00 26.12  ? 844  VAL   A O   1 
ATOM   6263 C  CB  . VAL   A 1 819 ? 23.926 55.154  30.493  1.00 28.21  ? 844  VAL   A CB  1 
ATOM   6264 C  CG1 . VAL   A 1 819 ? 23.445 56.346  29.698  1.00 29.51  ? 844  VAL   A CG1 1 
ATOM   6265 C  CG2 . VAL   A 1 819 ? 22.858 54.085  30.587  1.00 30.61  ? 844  VAL   A CG2 1 
ATOM   6266 N  N   . GLY   A 1 820 ? 25.308 52.194  30.229  1.00 23.36  ? 845  GLY   A N   1 
ATOM   6267 C  CA  . GLY   A 1 820 ? 25.550 50.982  30.979  1.00 23.52  ? 845  GLY   A CA  1 
ATOM   6268 C  C   . GLY   A 1 820 ? 26.730 50.154  30.551  1.00 21.04  ? 845  GLY   A C   1 
ATOM   6269 O  O   . GLY   A 1 820 ? 26.970 49.092  31.142  1.00 20.61  ? 845  GLY   A O   1 
ATOM   6270 N  N   . TYR   A 1 821 ? 27.551 50.660  29.595  1.00 17.89  ? 846  TYR   A N   1 
ATOM   6271 C  CA  . TYR   A 1 821 ? 28.684 49.845  29.152  1.00 17.03  ? 846  TYR   A CA  1 
ATOM   6272 C  C   . TYR   A 1 821 ? 29.602 49.292  30.253  1.00 17.82  ? 846  TYR   A C   1 
ATOM   6273 O  O   . TYR   A 1 821 ? 30.086 48.180  30.088  1.00 18.80  ? 846  TYR   A O   1 
ATOM   6274 C  CB  . TYR   A 1 821 ? 29.532 50.575  28.093  1.00 17.11  ? 846  TYR   A CB  1 
ATOM   6275 C  CG  . TYR   A 1 821 ? 30.238 51.805  28.626  1.00 15.79  ? 846  TYR   A CG  1 
ATOM   6276 C  CD1 . TYR   A 1 821 ? 31.499 51.714  29.187  1.00 16.52  ? 846  TYR   A CD1 1 
ATOM   6277 C  CD2 . TYR   A 1 821 ? 29.647 53.052  28.549  1.00 16.17  ? 846  TYR   A CD2 1 
ATOM   6278 C  CE1 . TYR   A 1 821 ? 32.143 52.834  29.712  1.00 16.40  ? 846  TYR   A CE1 1 
ATOM   6279 C  CE2 . TYR   A 1 821 ? 30.255 54.170  29.099  1.00 16.05  ? 846  TYR   A CE2 1 
ATOM   6280 C  CZ  . TYR   A 1 821 ? 31.518 54.060  29.655  1.00 16.71  ? 846  TYR   A CZ  1 
ATOM   6281 O  OH  . TYR   A 1 821 ? 32.146 55.139  30.230  1.00 18.74  ? 846  TYR   A OH  1 
ATOM   6282 N  N   . PRO   A 1 822 ? 29.881 49.974  31.401  1.00 15.72  ? 847  PRO   A N   1 
ATOM   6283 C  CA  . PRO   A 1 822 ? 30.761 49.347  32.403  1.00 15.17  ? 847  PRO   A CA  1 
ATOM   6284 C  C   . PRO   A 1 822 ? 30.206 48.042  32.950  1.00 16.97  ? 847  PRO   A C   1 
ATOM   6285 O  O   . PRO   A 1 822 ? 30.974 47.201  33.438  1.00 18.24  ? 847  PRO   A O   1 
ATOM   6286 C  CB  . PRO   A 1 822 ? 30.865 50.408  33.529  1.00 17.45  ? 847  PRO   A CB  1 
ATOM   6287 C  CG  . PRO   A 1 822 ? 30.517 51.721  32.828  1.00 17.30  ? 847  PRO   A CG  1 
ATOM   6288 C  CD  . PRO   A 1 822 ? 29.474 51.336  31.800  1.00 16.04  ? 847  PRO   A CD  1 
ATOM   6289 N  N   . LEU   A 1 823 ? 28.867 47.898  32.978  1.00 15.38  ? 848  LEU   A N   1 
ATOM   6290 C  CA  . LEU   A 1 823 ? 28.233 46.705  33.571  1.00 15.30  ? 848  LEU   A CA  1 
ATOM   6291 C  C   . LEU   A 1 823 ? 28.597 45.436  32.842  1.00 14.62  ? 848  LEU   A C   1 
ATOM   6292 O  O   . LEU   A 1 823 ? 28.615 44.366  33.470  1.00 15.06  ? 848  LEU   A O   1 
ATOM   6293 C  CB  . LEU   A 1 823 ? 26.690 46.828  33.551  1.00 15.54  ? 848  LEU   A CB  1 
ATOM   6294 C  CG  . LEU   A 1 823 ? 26.131 47.956  34.398  1.00 19.10  ? 848  LEU   A CG  1 
ATOM   6295 C  CD1 . LEU   A 1 823 ? 24.633 47.991  34.251  1.00 20.10  ? 848  LEU   A CD1 1 
ATOM   6296 C  CD2 . LEU   A 1 823 ? 26.512 47.757  35.846  1.00 21.51  ? 848  LEU   A CD2 1 
ATOM   6297 N  N   . ALA   A 1 824 ? 28.825 45.523  31.548  1.00 13.83  ? 849  ALA   A N   1 
ATOM   6298 C  CA  . ALA   A 1 824 ? 29.104 44.314  30.772  1.00 13.68  ? 849  ALA   A CA  1 
ATOM   6299 C  C   . ALA   A 1 824 ? 30.497 43.761  31.051  1.00 14.30  ? 849  ALA   A C   1 
ATOM   6300 O  O   . ALA   A 1 824 ? 30.631 42.586  31.411  1.00 13.71  ? 849  ALA   A O   1 
ATOM   6301 C  CB  . ALA   A 1 824 ? 28.874 44.588  29.281  1.00 14.64  ? 849  ALA   A CB  1 
ATOM   6302 N  N   . TRP   A 1 825 ? 31.522 44.615  30.972  1.00 14.46  ? 850  TRP   A N   1 
ATOM   6303 C  CA  . TRP   A 1 825 ? 32.872 44.201  31.328  1.00 13.97  ? 850  TRP   A CA  1 
ATOM   6304 C  C   . TRP   A 1 825 ? 32.911 43.734  32.779  1.00 14.23  ? 850  TRP   A C   1 
ATOM   6305 O  O   . TRP   A 1 825 ? 33.521 42.695  33.077  1.00 14.12  ? 850  TRP   A O   1 
ATOM   6306 C  CB  . TRP   A 1 825 ? 33.796 45.394  31.059  1.00 14.92  ? 850  TRP   A CB  1 
ATOM   6307 C  CG  . TRP   A 1 825 ? 35.212 45.356  31.571  1.00 14.18  ? 850  TRP   A CG  1 
ATOM   6308 C  CD1 . TRP   A 1 825 ? 35.875 46.403  32.141  1.00 14.97  ? 850  TRP   A CD1 1 
ATOM   6309 C  CD2 . TRP   A 1 825 ? 36.175 44.287  31.449  1.00 13.81  ? 850  TRP   A CD2 1 
ATOM   6310 N  NE1 . TRP   A 1 825 ? 37.183 46.055  32.387  1.00 14.33  ? 850  TRP   A NE1 1 
ATOM   6311 C  CE2 . TRP   A 1 825 ? 37.395 44.762  31.965  1.00 13.62  ? 850  TRP   A CE2 1 
ATOM   6312 C  CE3 . TRP   A 1 825 ? 36.126 42.979  30.954  1.00 14.11  ? 850  TRP   A CE3 1 
ATOM   6313 C  CZ2 . TRP   A 1 825 ? 38.537 43.976  32.035  1.00 13.59  ? 850  TRP   A CZ2 1 
ATOM   6314 C  CZ3 . TRP   A 1 825 ? 37.267 42.201  31.004  1.00 14.59  ? 850  TRP   A CZ3 1 
ATOM   6315 C  CH2 . TRP   A 1 825 ? 38.476 42.712  31.507  1.00 14.31  ? 850  TRP   A CH2 1 
ATOM   6316 N  N   . GLN   A 1 826 ? 32.207 44.415  33.679  1.00 14.65  ? 851  GLN   A N   1 
ATOM   6317 C  CA  . GLN   A 1 826 ? 32.146 43.975  35.047  1.00 15.81  ? 851  GLN   A CA  1 
ATOM   6318 C  C   . GLN   A 1 826 ? 31.544 42.562  35.195  1.00 15.14  ? 851  GLN   A C   1 
ATOM   6319 O  O   . GLN   A 1 826 ? 32.078 41.714  35.916  1.00 15.03  ? 851  GLN   A O   1 
ATOM   6320 C  CB  . GLN   A 1 826 ? 31.317 45.004  35.842  1.00 19.05  ? 851  GLN   A CB  1 
ATOM   6321 C  CG  . GLN   A 1 826 ? 31.167 44.711  37.272  1.00 21.30  ? 851  GLN   A CG  1 
ATOM   6322 C  CD  . GLN   A 1 826 ? 30.350 45.885  37.797  1.00 27.98  ? 851  GLN   A CD  1 
ATOM   6323 O  OE1 . GLN   A 1 826 ? 30.801 47.037  37.775  1.00 33.71  ? 851  GLN   A OE1 1 
ATOM   6324 N  NE2 . GLN   A 1 826 ? 29.096 45.657  38.152  1.00 27.31  ? 851  GLN   A NE2 1 
ATOM   6325 N  N   . PHE   A 1 827 ? 30.447 42.305  34.484  1.00 14.77  ? 852  PHE   A N   1 
ATOM   6326 C  CA  . PHE   A 1 827 ? 29.781 41.017  34.560  1.00 13.97  ? 852  PHE   A CA  1 
ATOM   6327 C  C   . PHE   A 1 827 ? 30.684 39.929  34.028  1.00 13.62  ? 852  PHE   A C   1 
ATOM   6328 O  O   . PHE   A 1 827 ? 30.746 38.826  34.607  1.00 14.08  ? 852  PHE   A O   1 
ATOM   6329 C  CB  . PHE   A 1 827 ? 28.492 41.062  33.722  1.00 14.11  ? 852  PHE   A CB  1 
ATOM   6330 C  CG  . PHE   A 1 827 ? 27.558 39.901  33.978  1.00 14.20  ? 852  PHE   A CG  1 
ATOM   6331 C  CD1 . PHE   A 1 827 ? 27.743 38.690  33.337  1.00 15.31  ? 852  PHE   A CD1 1 
ATOM   6332 C  CD2 . PHE   A 1 827 ? 26.578 39.993  34.948  1.00 15.79  ? 852  PHE   A CD2 1 
ATOM   6333 C  CE1 . PHE   A 1 827 ? 26.908 37.614  33.603  1.00 16.28  ? 852  PHE   A CE1 1 
ATOM   6334 C  CE2 . PHE   A 1 827 ? 25.733 38.919  35.209  1.00 16.33  ? 852  PHE   A CE2 1 
ATOM   6335 C  CZ  . PHE   A 1 827 ? 25.885 37.753  34.514  1.00 16.03  ? 852  PHE   A CZ  1 
ATOM   6336 N  N   . LEU   A 1 828 ? 31.382 40.199  32.910  1.00 12.95  ? 853  LEU   A N   1 
ATOM   6337 C  CA  . LEU   A 1 828 ? 32.290 39.209  32.358  1.00 14.06  ? 853  LEU   A CA  1 
ATOM   6338 C  C   . LEU   A 1 828 ? 33.378 38.819  33.366  1.00 15.09  ? 853  LEU   A C   1 
ATOM   6339 O  O   . LEU   A 1 828 ? 33.691 37.632  33.527  1.00 16.32  ? 853  LEU   A O   1 
ATOM   6340 C  CB  . LEU   A 1 828 ? 32.906 39.732  31.064  1.00 14.40  ? 853  LEU   A CB  1 
ATOM   6341 C  CG  . LEU   A 1 828 ? 33.822 38.765  30.357  1.00 15.74  ? 853  LEU   A CG  1 
ATOM   6342 C  CD1 . LEU   A 1 828 ? 33.102 37.478  29.996  1.00 17.69  ? 853  LEU   A CD1 1 
ATOM   6343 C  CD2 . LEU   A 1 828 ? 34.381 39.419  29.062  1.00 17.48  ? 853  LEU   A CD2 1 
ATOM   6344 N  N   . ARG   A 1 829 ? 33.976 39.828  34.031  1.00 15.27  ? 854  ARG   A N   1 
ATOM   6345 C  CA  . ARG   A 1 829 ? 35.029 39.508  35.024  1.00 15.14  ? 854  ARG   A CA  1 
ATOM   6346 C  C   . ARG   A 1 829 ? 34.484 38.707  36.191  1.00 16.64  ? 854  ARG   A C   1 
ATOM   6347 O  O   . ARG   A 1 829 ? 35.076 37.687  36.564  1.00 18.37  ? 854  ARG   A O   1 
ATOM   6348 C  CB  . ARG   A 1 829 ? 35.620 40.804  35.582  1.00 15.64  ? 854  ARG   A CB  1 
ATOM   6349 C  CG  . ARG   A 1 829 ? 36.386 41.639  34.568  1.00 17.05  ? 854  ARG   A CG  1 
ATOM   6350 C  CD  . ARG   A 1 829 ? 37.262 42.709  35.229  1.00 16.90  ? 854  ARG   A CD  1 
ATOM   6351 N  NE  . ARG   A 1 829 ? 36.571 43.395  36.340  1.00 20.46  ? 854  ARG   A NE  1 
ATOM   6352 C  CZ  . ARG   A 1 829 ? 35.835 44.485  36.220  1.00 20.03  ? 854  ARG   A CZ  1 
ATOM   6353 N  NH1 . ARG   A 1 829 ? 35.675 45.069  35.032  1.00 21.88  ? 854  ARG   A NH1 1 
ATOM   6354 N  NH2 . ARG   A 1 829 ? 35.231 44.997  37.276  1.00 22.96  ? 854  ARG   A NH2 1 
ATOM   6355 N  N   . LYS   A 1 830 ? 33.309 39.099  36.702  1.00 16.23  ? 855  LYS   A N   1 
ATOM   6356 C  CA  . LYS   A 1 830 ? 32.778 38.440  37.886  1.00 16.65  ? 855  LYS   A CA  1 
ATOM   6357 C  C   . LYS   A 1 830 ? 32.302 37.032  37.627  1.00 17.84  ? 855  LYS   A C   1 
ATOM   6358 O  O   . LYS   A 1 830 ? 32.381 36.174  38.501  1.00 18.22  ? 855  LYS   A O   1 
ATOM   6359 C  CB  . LYS   A 1 830 ? 31.614 39.293  38.441  1.00 17.17  ? 855  LYS   A CB  1 
ATOM   6360 C  CG  . LYS   A 1 830 ? 30.860 38.629  39.595  1.00 24.59  ? 855  LYS   A CG  1 
ATOM   6361 C  CD  . LYS   A 1 830 ? 29.894 39.598  40.268  1.00 30.92  ? 855  LYS   A CD  1 
ATOM   6362 C  CE  . LYS   A 1 830 ? 28.906 38.927  41.201  1.00 33.11  ? 855  LYS   A CE  1 
ATOM   6363 N  NZ  . LYS   A 1 830 ? 28.409 37.630  40.671  1.00 37.66  ? 855  LYS   A NZ  1 
ATOM   6364 N  N   . ASN   A 1 831 ? 31.770 36.782  36.445  1.00 16.04  ? 856  ASN   A N   1 
ATOM   6365 C  CA  . ASN   A 1 831 ? 31.159 35.498  36.086  1.00 14.06  ? 856  ASN   A CA  1 
ATOM   6366 C  C   . ASN   A 1 831 ? 31.999 34.714  35.107  1.00 14.06  ? 856  ASN   A C   1 
ATOM   6367 O  O   . ASN   A 1 831 ? 31.489 33.728  34.562  1.00 14.74  ? 856  ASN   A O   1 
ATOM   6368 C  CB  . ASN   A 1 831 ? 29.745 35.745  35.503  1.00 14.36  ? 856  ASN   A CB  1 
ATOM   6369 C  CG  . ASN   A 1 831 ? 28.881 36.358  36.579  1.00 17.00  ? 856  ASN   A CG  1 
ATOM   6370 O  OD1 . ASN   A 1 831 ? 28.452 35.672  37.541  1.00 19.01  ? 856  ASN   A OD1 1 
ATOM   6371 N  ND2 . ASN   A 1 831 ? 28.689 37.666  36.525  1.00 16.81  ? 856  ASN   A ND2 1 
ATOM   6372 N  N   . TRP   A 1 832 ? 33.289 35.051  34.976  1.00 14.21  ? 857  TRP   A N   1 
ATOM   6373 C  CA  . TRP   A 1 832 ? 34.157 34.402  34.013  1.00 14.65  ? 857  TRP   A CA  1 
ATOM   6374 C  C   . TRP   A 1 832 ? 34.130 32.867  34.086  1.00 15.90  ? 857  TRP   A C   1 
ATOM   6375 O  O   . TRP   A 1 832 ? 33.978 32.189  33.058  1.00 14.83  ? 857  TRP   A O   1 
ATOM   6376 C  CB  . TRP   A 1 832 ? 35.581 34.915  34.227  1.00 15.06  ? 857  TRP   A CB  1 
ATOM   6377 C  CG  . TRP   A 1 832 ? 36.572 34.282  33.293  1.00 14.45  ? 857  TRP   A CG  1 
ATOM   6378 C  CD1 . TRP   A 1 832 ? 37.461 33.295  33.587  1.00 14.79  ? 857  TRP   A CD1 1 
ATOM   6379 C  CD2 . TRP   A 1 832 ? 36.757 34.587  31.909  1.00 13.32  ? 857  TRP   A CD2 1 
ATOM   6380 N  NE1 . TRP   A 1 832 ? 38.179 32.949  32.474  1.00 14.51  ? 857  TRP   A NE1 1 
ATOM   6381 C  CE2 . TRP   A 1 832 ? 37.771 33.732  31.420  1.00 14.00  ? 857  TRP   A CE2 1 
ATOM   6382 C  CE3 . TRP   A 1 832 ? 36.139 35.469  31.027  1.00 13.72  ? 857  TRP   A CE3 1 
ATOM   6383 C  CZ2 . TRP   A 1 832 ? 38.195 33.756  30.096  1.00 14.40  ? 857  TRP   A CZ2 1 
ATOM   6384 C  CZ3 . TRP   A 1 832 ? 36.532 35.469  29.707  1.00 14.01  ? 857  TRP   A CZ3 1 
ATOM   6385 C  CH2 . TRP   A 1 832 ? 37.578 34.654  29.257  1.00 14.35  ? 857  TRP   A CH2 1 
ATOM   6386 N  N   . ASN   A 1 833 ? 34.305 32.307  35.307  1.00 15.58  ? 858  ASN   A N   1 
ATOM   6387 C  CA  . ASN   A 1 833 ? 34.400 30.851  35.374  1.00 16.21  ? 858  ASN   A CA  1 
ATOM   6388 C  C   . ASN   A 1 833 ? 33.186 30.133  34.876  1.00 15.80  ? 858  ASN   A C   1 
ATOM   6389 O  O   . ASN   A 1 833 ? 33.312 29.142  34.149  1.00 16.04  ? 858  ASN   A O   1 
ATOM   6390 C  CB  . ASN   A 1 833 ? 34.751 30.388  36.785  1.00 16.91  ? 858  ASN   A CB  1 
ATOM   6391 C  CG  . ASN   A 1 833 ? 36.176 30.680  37.125  1.00 19.43  ? 858  ASN   A CG  1 
ATOM   6392 O  OD1 . ASN   A 1 833 ? 37.010 31.166  36.324  1.00 19.66  ? 858  ASN   A OD1 1 
ATOM   6393 N  ND2 . ASN   A 1 833 ? 36.535 30.403  38.380  1.00 22.39  ? 858  ASN   A ND2 1 
ATOM   6394 N  N   . LYS   A 1 834 ? 32.027 30.629  35.223  1.00 15.67  ? 859  LYS   A N   1 
ATOM   6395 C  CA  . LYS   A 1 834 ? 30.784 30.001  34.780  1.00 15.90  ? 859  LYS   A CA  1 
ATOM   6396 C  C   . LYS   A 1 834 ? 30.575 30.192  33.283  1.00 15.21  ? 859  LYS   A C   1 
ATOM   6397 O  O   . LYS   A 1 834 ? 30.069 29.309  32.615  1.00 16.13  ? 859  LYS   A O   1 
ATOM   6398 C  CB  . LYS   A 1 834 ? 29.591 30.527  35.602  1.00 17.78  ? 859  LYS   A CB  1 
ATOM   6399 C  CG  . LYS   A 1 834 ? 29.606 29.960  37.019  1.00 23.68  ? 859  LYS   A CG  1 
ATOM   6400 C  CD  . LYS   A 1 834 ? 28.975 28.603  36.998  1.00 30.68  ? 859  LYS   A CD  1 
ATOM   6401 C  CE  . LYS   A 1 834 ? 28.964 27.853  38.318  1.00 35.64  ? 859  LYS   A CE  1 
ATOM   6402 N  NZ  . LYS   A 1 834 ? 28.262 26.551  38.125  1.00 38.61  ? 859  LYS   A NZ  1 
ATOM   6403 N  N   . LEU   A 1 835 ? 31.003 31.339  32.770  1.00 14.57  ? 860  LEU   A N   1 
ATOM   6404 C  CA  . LEU   A 1 835 ? 30.871 31.599  31.338  1.00 14.50  ? 860  LEU   A CA  1 
ATOM   6405 C  C   . LEU   A 1 835 ? 31.802 30.682  30.551  1.00 14.67  ? 860  LEU   A C   1 
ATOM   6406 O  O   . LEU   A 1 835 ? 31.390 30.131  29.521  1.00 13.58  ? 860  LEU   A O   1 
ATOM   6407 C  CB  . LEU   A 1 835 ? 31.159 33.071  31.044  1.00 15.36  ? 860  LEU   A CB  1 
ATOM   6408 C  CG  . LEU   A 1 835 ? 29.997 33.972  31.516  1.00 16.94  ? 860  LEU   A CG  1 
ATOM   6409 C  CD1 . LEU   A 1 835 ? 30.409 35.420  31.434  1.00 17.79  ? 860  LEU   A CD1 1 
ATOM   6410 C  CD2 . LEU   A 1 835 ? 28.719 33.694  30.706  1.00 17.57  ? 860  LEU   A CD2 1 
ATOM   6411 N  N   . VAL   A 1 836 ? 33.007 30.457  31.045  1.00 14.57  ? 861  VAL   A N   1 
ATOM   6412 C  CA  . VAL   A 1 836 ? 33.923 29.528  30.386  1.00 15.46  ? 861  VAL   A CA  1 
ATOM   6413 C  C   . VAL   A 1 836 ? 33.354 28.100  30.465  1.00 15.36  ? 861  VAL   A C   1 
ATOM   6414 O  O   . VAL   A 1 836 ? 33.408 27.352  29.488  1.00 14.99  ? 861  VAL   A O   1 
ATOM   6415 C  CB  . VAL   A 1 836 ? 35.296 29.615  31.065  1.00 18.95  ? 861  VAL   A CB  1 
ATOM   6416 C  CG1 . VAL   A 1 836 ? 36.151 28.367  30.789  1.00 20.46  ? 861  VAL   A CG1 1 
ATOM   6417 C  CG2 . VAL   A 1 836 ? 35.996 30.897  30.615  1.00 20.51  ? 861  VAL   A CG2 1 
ATOM   6418 N  N   . GLN   A 1 837 ? 32.817 27.726  31.623  1.00 14.97  ? 862  GLN   A N   1 
ATOM   6419 C  CA  . GLN   A 1 837 ? 32.238 26.375  31.741  1.00 14.94  ? 862  GLN   A CA  1 
ATOM   6420 C  C   . GLN   A 1 837 ? 31.079 26.186  30.729  1.00 15.96  ? 862  GLN   A C   1 
ATOM   6421 O  O   . GLN   A 1 837 ? 30.978 25.137  30.095  1.00 17.36  ? 862  GLN   A O   1 
ATOM   6422 C  CB  . GLN   A 1 837 ? 31.759 26.115  33.160  1.00 18.58  ? 862  GLN   A CB  1 
ATOM   6423 C  CG  . GLN   A 1 837 ? 31.013 24.791  33.346  1.00 26.04  ? 862  GLN   A CG  1 
ATOM   6424 C  CD  . GLN   A 1 837 ? 31.801 23.535  33.092  1.00 35.77  ? 862  GLN   A CD  1 
ATOM   6425 O  OE1 . GLN   A 1 837 ? 33.027 23.473  33.296  1.00 38.93  ? 862  GLN   A OE1 1 
ATOM   6426 N  NE2 . GLN   A 1 837 ? 31.083 22.482  32.668  1.00 36.21  ? 862  GLN   A NE2 1 
ATOM   6427 N  N   . LYS   A 1 838 ? 30.268 27.245  30.515  1.00 13.69  ? 863  LYS   A N   1 
ATOM   6428 C  CA  . LYS   A 1 838 ? 29.136 27.101  29.610  1.00 14.22  ? 863  LYS   A CA  1 
ATOM   6429 C  C   . LYS   A 1 838 ? 29.530 27.102  28.150  1.00 14.39  ? 863  LYS   A C   1 
ATOM   6430 O  O   . LYS   A 1 838 ? 28.992 26.301  27.365  1.00 14.78  ? 863  LYS   A O   1 
ATOM   6431 C  CB  . LYS   A 1 838 ? 28.157 28.252  29.861  1.00 14.59  ? 863  LYS   A CB  1 
ATOM   6432 C  CG  . LYS   A 1 838 ? 26.843 28.174  29.057  1.00 15.80  ? 863  LYS   A CG  1 
ATOM   6433 C  CD  . LYS   A 1 838 ? 25.860 27.184  29.688  1.00 17.53  ? 863  LYS   A CD  1 
ATOM   6434 C  CE  . LYS   A 1 838 ? 24.602 26.996  28.839  1.00 20.22  ? 863  LYS   A CE  1 
ATOM   6435 N  NZ  . LYS   A 1 838 ? 23.553 26.182  29.549  1.00 21.26  ? 863  LYS   A NZ  1 
ATOM   6436 N  N   . PHE   A 1 839 ? 30.459 28.013  27.767  1.00 13.83  ? 864  PHE   A N   1 
ATOM   6437 C  CA  . PHE   A 1 839 ? 30.730 28.238  26.359  1.00 13.27  ? 864  PHE   A CA  1 
ATOM   6438 C  C   . PHE   A 1 839 ? 32.082 27.688  25.858  1.00 13.05  ? 864  PHE   A C   1 
ATOM   6439 O  O   . PHE   A 1 839 ? 32.225 27.480  24.655  1.00 13.79  ? 864  PHE   A O   1 
ATOM   6440 C  CB  . PHE   A 1 839 ? 30.711 29.766  26.089  1.00 13.43  ? 864  PHE   A CB  1 
ATOM   6441 C  CG  . PHE   A 1 839 ? 29.327 30.364  26.174  1.00 13.71  ? 864  PHE   A CG  1 
ATOM   6442 C  CD1 . PHE   A 1 839 ? 28.487 30.343  25.078  1.00 14.73  ? 864  PHE   A CD1 1 
ATOM   6443 C  CD2 . PHE   A 1 839 ? 28.864 30.939  27.359  1.00 13.23  ? 864  PHE   A CD2 1 
ATOM   6444 C  CE1 . PHE   A 1 839 ? 27.205 30.872  25.149  1.00 14.97  ? 864  PHE   A CE1 1 
ATOM   6445 C  CE2 . PHE   A 1 839 ? 27.576 31.487  27.424  1.00 14.72  ? 864  PHE   A CE2 1 
ATOM   6446 C  CZ  . PHE   A 1 839 ? 26.744 31.434  26.325  1.00 14.09  ? 864  PHE   A CZ  1 
ATOM   6447 N  N   . GLU   A 1 840 ? 33.010 27.434  26.787  1.00 13.23  ? 865  GLU   A N   1 
ATOM   6448 C  CA  . GLU   A 1 840 ? 34.360 26.870  26.603  1.00 13.54  ? 865  GLU   A CA  1 
ATOM   6449 C  C   . GLU   A 1 840 ? 35.423 27.893  26.260  1.00 14.28  ? 865  GLU   A C   1 
ATOM   6450 O  O   . GLU   A 1 840 ? 35.255 28.760  25.382  1.00 13.99  ? 865  GLU   A O   1 
ATOM   6451 C  CB  . GLU   A 1 840 ? 34.427 25.742  25.577  1.00 15.36  ? 865  GLU   A CB  1 
ATOM   6452 C  CG  . GLU   A 1 840 ? 33.414 24.643  25.866  1.00 16.05  ? 865  GLU   A CG  1 
ATOM   6453 C  CD  . GLU   A 1 840 ? 33.813 23.393  25.121  1.00 16.65  ? 865  GLU   A CD  1 
ATOM   6454 O  OE1 . GLU   A 1 840 ? 33.550 23.326  23.899  1.00 16.71  ? 865  GLU   A OE1 1 
ATOM   6455 O  OE2 . GLU   A 1 840 ? 34.481 22.537  25.760  1.00 17.05  ? 865  GLU   A OE2 1 
ATOM   6456 N  N   . LEU   A 1 841 ? 36.609 27.690  26.853  1.00 14.30  ? 866  LEU   A N   1 
ATOM   6457 C  CA  . LEU   A 1 841 ? 37.772 28.501  26.492  1.00 15.25  ? 866  LEU   A CA  1 
ATOM   6458 C  C   . LEU   A 1 841 ? 38.113 28.258  25.035  1.00 14.93  ? 866  LEU   A C   1 
ATOM   6459 O  O   . LEU   A 1 841 ? 38.082 27.108  24.560  1.00 14.28  ? 866  LEU   A O   1 
ATOM   6460 C  CB  . LEU   A 1 841 ? 39.008 28.071  27.309  1.00 18.60  ? 866  LEU   A CB  1 
ATOM   6461 C  CG  . LEU   A 1 841 ? 39.041 28.530  28.728  1.00 21.82  ? 866  LEU   A CG  1 
ATOM   6462 C  CD1 . LEU   A 1 841 ? 40.170 27.783  29.465  1.00 23.97  ? 866  LEU   A CD1 1 
ATOM   6463 C  CD2 . LEU   A 1 841 ? 39.244 30.051  28.806  1.00 21.84  ? 866  LEU   A CD2 1 
ATOM   6464 N  N   . GLY   A 1 842 ? 38.372 29.329  24.312  1.00 13.98  ? 867  GLY   A N   1 
ATOM   6465 C  CA  . GLY   A 1 842 ? 38.724 29.229  22.909  1.00 13.95  ? 867  GLY   A CA  1 
ATOM   6466 C  C   . GLY   A 1 842 ? 37.552 29.335  21.958  1.00 13.93  ? 867  GLY   A C   1 
ATOM   6467 O  O   . GLY   A 1 842 ? 37.734 29.574  20.754  1.00 14.13  ? 867  GLY   A O   1 
ATOM   6468 N  N   . SER   A 1 843 ? 36.309 29.238  22.508  1.00 13.04  ? 868  SER   A N   1 
ATOM   6469 C  CA  . SER   A 1 843 ? 35.166 29.349  21.649  1.00 12.83  ? 868  SER   A CA  1 
ATOM   6470 C  C   . SER   A 1 843 ? 35.012 30.707  21.043  1.00 14.13  ? 868  SER   A C   1 
ATOM   6471 O  O   . SER   A 1 843 ? 35.417 31.717  21.642  1.00 13.54  ? 868  SER   A O   1 
ATOM   6472 C  CB  . SER   A 1 843 ? 33.888 29.026  22.431  1.00 14.02  ? 868  SER   A CB  1 
ATOM   6473 O  OG  . SER   A 1 843 ? 33.640 29.961  23.491  1.00 13.20  ? 868  SER   A OG  1 
ATOM   6474 N  N   . SER   A 1 844 ? 34.371 30.765  19.892  1.00 12.76  ? 869  SER   A N   1 
ATOM   6475 C  CA  . SER   A 1 844 ? 34.024 32.044  19.281  1.00 12.75  ? 869  SER   A CA  1 
ATOM   6476 C  C   . SER   A 1 844 ? 33.095 32.840  20.219  1.00 13.58  ? 869  SER   A C   1 
ATOM   6477 O  O   . SER   A 1 844 ? 33.223 34.058  20.288  1.00 14.34  ? 869  SER   A O   1 
ATOM   6478 C  CB  . SER   A 1 844 ? 33.344 31.783  17.925  1.00 15.94  ? 869  SER   A CB  1 
ATOM   6479 O  OG  . SER   A 1 844 ? 32.888 32.998  17.344  1.00 20.55  ? 869  SER   A OG  1 
ATOM   6480 N  N   . SER   A 1 845 ? 32.202 32.174  20.987  1.00 12.45  ? 870  SER   A N   1 
ATOM   6481 C  CA  . SER   A 1 845 ? 31.336 32.904  21.919  1.00 12.13  ? 870  SER   A CA  1 
ATOM   6482 C  C   . SER   A 1 845 ? 32.183 33.649  22.962  1.00 12.20  ? 870  SER   A C   1 
ATOM   6483 O  O   . SER   A 1 845 ? 31.934 34.847  23.211  1.00 13.21  ? 870  SER   A O   1 
ATOM   6484 C  CB  . SER   A 1 845 ? 30.408 31.947  22.646  1.00 14.04  ? 870  SER   A CB  1 
ATOM   6485 O  OG  . SER   A 1 845 ? 29.627 31.217  21.711  1.00 15.71  ? 870  SER   A OG  1 
ATOM   6486 N  N   . ILE   A 1 846 ? 33.154 32.976  23.595  1.00 12.08  ? 871  ILE   A N   1 
ATOM   6487 C  CA  . ILE   A 1 846 ? 34.004 33.671  24.577  1.00 12.22  ? 871  ILE   A CA  1 
ATOM   6488 C  C   . ILE   A 1 846 ? 34.797 34.786  23.886  1.00 12.93  ? 871  ILE   A C   1 
ATOM   6489 O  O   . ILE   A 1 846 ? 34.870 35.899  24.421  1.00 13.26  ? 871  ILE   A O   1 
ATOM   6490 C  CB  . ILE   A 1 846 ? 34.923 32.646  25.263  1.00 13.48  ? 871  ILE   A CB  1 
ATOM   6491 C  CG1 . ILE   A 1 846 ? 34.128 31.794  26.254  1.00 14.57  ? 871  ILE   A CG1 1 
ATOM   6492 C  CG2 . ILE   A 1 846 ? 36.115 33.372  25.987  1.00 15.58  ? 871  ILE   A CG2 1 
ATOM   6493 C  CD1 . ILE   A 1 846 ? 33.674 32.534  27.597  1.00 15.90  ? 871  ILE   A CD1 1 
ATOM   6494 N  N   . ALA   A 1 847 ? 35.285 34.554  22.651  1.00 12.36  ? 872  ALA   A N   1 
ATOM   6495 C  CA  . ALA   A 1 847 ? 36.019 35.596  21.944  1.00 12.91  ? 872  ALA   A CA  1 
ATOM   6496 C  C   . ALA   A 1 847 ? 35.166 36.825  21.721  1.00 14.14  ? 872  ALA   A C   1 
ATOM   6497 O  O   . ALA   A 1 847 ? 35.630 37.940  21.957  1.00 14.05  ? 872  ALA   A O   1 
ATOM   6498 C  CB  . ALA   A 1 847 ? 36.549 35.077  20.618  1.00 12.98  ? 872  ALA   A CB  1 
ATOM   6499 N  N   . HIS   A 1 848 ? 33.908 36.623  21.334  1.00 13.19  ? 873  HIS   A N   1 
ATOM   6500 C  CA  . HIS   A 1 848 ? 33.013 37.758  21.101  1.00 14.30  ? 873  HIS   A CA  1 
ATOM   6501 C  C   . HIS   A 1 848 ? 32.678 38.470  22.413  1.00 14.12  ? 873  HIS   A C   1 
ATOM   6502 O  O   . HIS   A 1 848 ? 32.443 39.688  22.393  1.00 13.91  ? 873  HIS   A O   1 
ATOM   6503 C  CB  . HIS   A 1 848 ? 31.733 37.276  20.370  1.00 17.29  ? 873  HIS   A CB  1 
ATOM   6504 C  CG  . HIS   A 1 848 ? 32.047 37.097  18.906  1.00 25.34  ? 873  HIS   A CG  1 
ATOM   6505 N  ND1 . HIS   A 1 848 ? 32.373 38.195  18.095  1.00 32.05  ? 873  HIS   A ND1 1 
ATOM   6506 C  CD2 . HIS   A 1 848 ? 32.269 35.966  18.198  1.00 29.10  ? 873  HIS   A CD2 1 
ATOM   6507 C  CE1 . HIS   A 1 848 ? 32.654 37.687  16.895  1.00 33.61  ? 873  HIS   A CE1 1 
ATOM   6508 N  NE2 . HIS   A 1 848 ? 32.598 36.350  16.907  1.00 32.26  ? 873  HIS   A NE2 1 
ATOM   6509 N  N   . MET   A 1 849 ? 32.592 37.751  23.528  1.00 13.17  ? 874  MET   A N   1 
ATOM   6510 C  CA  . MET   A 1 849 ? 32.319 38.405  24.813  1.00 13.37  ? 874  MET   A CA  1 
ATOM   6511 C  C   . MET   A 1 849 ? 33.506 39.236  25.240  1.00 14.42  ? 874  MET   A C   1 
ATOM   6512 O  O   . MET   A 1 849 ? 33.341 40.358  25.695  1.00 14.27  ? 874  MET   A O   1 
ATOM   6513 C  CB  . MET   A 1 849 ? 31.974 37.356  25.874  1.00 15.49  ? 874  MET   A CB  1 
ATOM   6514 C  CG  . MET   A 1 849 ? 30.660 36.745  25.544  1.00 17.09  ? 874  MET   A CG  1 
ATOM   6515 S  SD  . MET   A 1 849 ? 29.858 35.672  26.719  1.00 23.58  ? 874  MET   A SD  1 
ATOM   6516 C  CE  . MET   A 1 849 ? 30.381 34.008  26.160  1.00 19.17  ? 874  MET   A CE  1 
ATOM   6517 N  N   . VAL   A 1 850 ? 34.721 38.710  25.103  1.00 13.09  ? 875  VAL   A N   1 
ATOM   6518 C  CA  . VAL   A 1 850 ? 35.937 39.460  25.485  1.00 13.69  ? 875  VAL   A CA  1 
ATOM   6519 C  C   . VAL   A 1 850 ? 36.051 40.712  24.607  1.00 14.14  ? 875  VAL   A C   1 
ATOM   6520 O  O   . VAL   A 1 850 ? 36.179 41.843  25.130  1.00 15.89  ? 875  VAL   A O   1 
ATOM   6521 C  CB  . VAL   A 1 850 ? 37.157 38.535  25.313  1.00 13.30  ? 875  VAL   A CB  1 
ATOM   6522 C  CG1 . VAL   A 1 850 ? 38.473 39.319  25.404  1.00 14.28  ? 875  VAL   A CG1 1 
ATOM   6523 C  CG2 . VAL   A 1 850 ? 37.132 37.458  26.363  1.00 13.27  ? 875  VAL   A CG2 1 
ATOM   6524 N  N   . MET   A 1 851 ? 35.952 40.568  23.276  1.00 14.48  ? 876  MET   A N   1 
ATOM   6525 C  CA  . MET   A 1 851 ? 36.053 41.756  22.410  1.00 14.42  ? 876  MET   A CA  1 
ATOM   6526 C  C   . MET   A 1 851 ? 34.886 42.677  22.624  1.00 13.54  ? 876  MET   A C   1 
ATOM   6527 O  O   . MET   A 1 851 ? 35.050 43.918  22.644  1.00 14.00  ? 876  MET   A O   1 
ATOM   6528 C  CB  . MET   A 1 851 ? 36.012 41.353  20.915  1.00 17.25  ? 876  MET   A CB  1 
ATOM   6529 C  CG  . MET   A 1 851 ? 36.942 40.324  20.517  1.00 26.73  ? 876  MET   A CG  1 
ATOM   6530 S  SD  . MET   A 1 851 ? 38.656 40.754  20.709  1.00 33.65  ? 876  MET   A SD  1 
ATOM   6531 C  CE  . MET   A 1 851 ? 38.707 42.301  19.923  1.00 29.39  ? 876  MET   A CE  1 
ATOM   6532 N  N   . GLY   A 1 852 ? 33.674 42.142  22.733  1.00 13.41  ? 877  GLY   A N   1 
ATOM   6533 C  CA  . GLY   A 1 852 ? 32.467 42.963  22.797  1.00 13.23  ? 877  GLY   A CA  1 
ATOM   6534 C  C   . GLY   A 1 852 ? 32.443 43.906  23.963  1.00 13.91  ? 877  GLY   A C   1 
ATOM   6535 O  O   . GLY   A 1 852 ? 31.846 44.999  23.860  1.00 15.84  ? 877  GLY   A O   1 
ATOM   6536 N  N   . THR   A 1 853 ? 32.995 43.449  25.096  1.00 13.29  ? 878  THR   A N   1 
ATOM   6537 C  CA  . THR   A 1 853 ? 32.953 44.269  26.301  1.00 12.82  ? 878  THR   A CA  1 
ATOM   6538 C  C   . THR   A 1 853 ? 34.151 45.165  26.470  1.00 13.12  ? 878  THR   A C   1 
ATOM   6539 O  O   . THR   A 1 853 ? 34.087 46.009  27.382  1.00 14.44  ? 878  THR   A O   1 
ATOM   6540 C  CB  . THR   A 1 853 ? 32.814 43.400  27.528  1.00 13.36  ? 878  THR   A CB  1 
ATOM   6541 O  OG1 . THR   A 1 853 ? 33.957 42.529  27.654  1.00 14.79  ? 878  THR   A OG1 1 
ATOM   6542 C  CG2 . THR   A 1 853 ? 31.526 42.575  27.469  1.00 13.88  ? 878  THR   A CG2 1 
ATOM   6543 N  N   . THR   A 1 854 ? 35.226 45.021  25.672  1.00 12.04  ? 879  THR   A N   1 
ATOM   6544 C  CA  . THR   A 1 854 ? 36.433 45.789  25.932  1.00 12.99  ? 879  THR   A CA  1 
ATOM   6545 C  C   . THR   A 1 854 ? 36.988 46.527  24.759  1.00 13.23  ? 879  THR   A C   1 
ATOM   6546 O  O   . THR   A 1 854 ? 37.838 47.427  24.965  1.00 13.55  ? 879  THR   A O   1 
ATOM   6547 C  CB  . THR   A 1 854 ? 37.536 44.857  26.486  1.00 13.96  ? 879  THR   A CB  1 
ATOM   6548 O  OG1 . THR   A 1 854 ? 37.854 43.865  25.492  1.00 13.85  ? 879  THR   A OG1 1 
ATOM   6549 C  CG2 . THR   A 1 854 ? 37.124 44.145  27.794  1.00 14.02  ? 879  THR   A CG2 1 
ATOM   6550 N  N   . ASN   A 1 855 ? 36.590 46.193  23.519  1.00 12.86  ? 880  ASN   A N   1 
ATOM   6551 C  CA  . ASN   A 1 855 ? 37.287 46.763  22.377  1.00 12.61  ? 880  ASN   A CA  1 
ATOM   6552 C  C   . ASN   A 1 855 ? 36.906 48.160  21.974  1.00 13.57  ? 880  ASN   A C   1 
ATOM   6553 O  O   . ASN   A 1 855 ? 37.419 48.669  20.965  1.00 13.70  ? 880  ASN   A O   1 
ATOM   6554 C  CB  . ASN   A 1 855 ? 37.239 45.819  21.160  1.00 15.09  ? 880  ASN   A CB  1 
ATOM   6555 C  CG  . ASN   A 1 855 ? 35.926 45.803  20.481  1.00 16.67  ? 880  ASN   A CG  1 
ATOM   6556 O  OD1 . ASN   A 1 855 ? 34.962 46.461  20.851  1.00 16.01  ? 880  ASN   A OD1 1 
ATOM   6557 N  ND2 . ASN   A 1 855 ? 35.836 44.965  19.385  1.00 19.94  ? 880  ASN   A ND2 1 
ATOM   6558 N  N   . GLN   A 1 856 ? 36.077 48.821  22.797  1.00 12.75  ? 881  GLN   A N   1 
ATOM   6559 C  CA  . GLN   A 1 856 ? 35.770 50.220  22.583  1.00 11.99  ? 881  GLN   A CA  1 
ATOM   6560 C  C   . GLN   A 1 856 ? 36.398 51.101  23.680  1.00 12.54  ? 881  GLN   A C   1 
ATOM   6561 O  O   . GLN   A 1 856 ? 36.080 52.290  23.760  1.00 13.84  ? 881  GLN   A O   1 
ATOM   6562 C  CB  . GLN   A 1 856 ? 34.296 50.478  22.410  1.00 13.08  ? 881  GLN   A CB  1 
ATOM   6563 C  CG  . GLN   A 1 856 ? 33.792 49.786  21.132  1.00 13.05  ? 881  GLN   A CG  1 
ATOM   6564 C  CD  . GLN   A 1 856 ? 32.295 49.885  20.959  1.00 13.94  ? 881  GLN   A CD  1 
ATOM   6565 O  OE1 . GLN   A 1 856 ? 31.540 50.352  21.824  1.00 13.37  ? 881  GLN   A OE1 1 
ATOM   6566 N  NE2 . GLN   A 1 856 ? 31.833 49.425  19.783  1.00 14.53  ? 881  GLN   A NE2 1 
ATOM   6567 N  N   . PHE   A 1 857 ? 37.272 50.503  24.513  1.00 12.27  ? 882  PHE   A N   1 
ATOM   6568 C  CA  . PHE   A 1 857 ? 37.980 51.290  25.517  1.00 12.76  ? 882  PHE   A CA  1 
ATOM   6569 C  C   . PHE   A 1 857 ? 39.177 51.971  24.861  1.00 13.34  ? 882  PHE   A C   1 
ATOM   6570 O  O   . PHE   A 1 857 ? 39.771 51.452  23.875  1.00 13.97  ? 882  PHE   A O   1 
ATOM   6571 C  CB  . PHE   A 1 857 ? 38.489 50.393  26.667  1.00 13.45  ? 882  PHE   A CB  1 
ATOM   6572 C  CG  . PHE   A 1 857 ? 37.368 49.849  27.534  1.00 13.85  ? 882  PHE   A CG  1 
ATOM   6573 C  CD1 . PHE   A 1 857 ? 36.308 50.667  27.939  1.00 15.21  ? 882  PHE   A CD1 1 
ATOM   6574 C  CD2 . PHE   A 1 857 ? 37.430 48.559  28.024  1.00 15.29  ? 882  PHE   A CD2 1 
ATOM   6575 C  CE1 . PHE   A 1 857 ? 35.298 50.159  28.779  1.00 16.11  ? 882  PHE   A CE1 1 
ATOM   6576 C  CE2 . PHE   A 1 857 ? 36.454 48.083  28.893  1.00 16.19  ? 882  PHE   A CE2 1 
ATOM   6577 C  CZ  . PHE   A 1 857 ? 35.376 48.871  29.217  1.00 15.61  ? 882  PHE   A CZ  1 
ATOM   6578 N  N   . SER   A 1 858 ? 39.595 53.115  25.429  1.00 13.26  ? 883  SER   A N   1 
ATOM   6579 C  CA  . SER   A 1 858 ? 40.649 53.895  24.828  1.00 13.30  ? 883  SER   A CA  1 
ATOM   6580 C  C   . SER   A 1 858 ? 41.420 54.667  25.858  1.00 14.40  ? 883  SER   A C   1 
ATOM   6581 O  O   . SER   A 1 858 ? 42.008 55.691  25.502  1.00 15.21  ? 883  SER   A O   1 
ATOM   6582 C  CB  . SER   A 1 858 ? 40.100 54.862  23.766  1.00 14.20  ? 883  SER   A CB  1 
ATOM   6583 O  OG  . SER   A 1 858 ? 39.220 55.839  24.301  1.00 14.07  ? 883  SER   A OG  1 
ATOM   6584 N  N   . THR   A 1 859 ? 41.539 54.125  27.098  1.00 14.33  ? 884  THR   A N   1 
ATOM   6585 C  CA  . THR   A 1 859 ? 42.411 54.778  28.102  1.00 14.61  ? 884  THR   A CA  1 
ATOM   6586 C  C   . THR   A 1 859 ? 43.416 53.744  28.577  1.00 14.56  ? 884  THR   A C   1 
ATOM   6587 O  O   . THR   A 1 859 ? 43.176 52.532  28.537  1.00 13.96  ? 884  THR   A O   1 
ATOM   6588 C  CB  . THR   A 1 859 ? 41.620 55.320  29.297  1.00 16.97  ? 884  THR   A CB  1 
ATOM   6589 O  OG1 . THR   A 1 859 ? 41.100 54.220  30.053  1.00 16.37  ? 884  THR   A OG1 1 
ATOM   6590 C  CG2 . THR   A 1 859 ? 40.512 56.259  28.856  1.00 18.19  ? 884  THR   A CG2 1 
ATOM   6591 N  N   . ARG   A 1 860 ? 44.523 54.246  29.096  1.00 14.45  ? 885  ARG   A N   1 
ATOM   6592 C  CA  . ARG   A 1 860 ? 45.543 53.383  29.662  1.00 13.96  ? 885  ARG   A CA  1 
ATOM   6593 C  C   . ARG   A 1 860 ? 45.014 52.681  30.924  1.00 14.32  ? 885  ARG   A C   1 
ATOM   6594 O  O   . ARG   A 1 860 ? 45.432 51.550  31.169  1.00 14.23  ? 885  ARG   A O   1 
ATOM   6595 C  CB  . ARG   A 1 860 ? 46.783 54.205  30.025  1.00 16.47  ? 885  ARG   A CB  1 
ATOM   6596 C  CG  . ARG   A 1 860 ? 47.408 54.764  28.744  1.00 17.54  ? 885  ARG   A CG  1 
ATOM   6597 C  CD  . ARG   A 1 860 ? 48.360 55.941  28.970  1.00 20.45  ? 885  ARG   A CD  1 
ATOM   6598 N  NE  . ARG   A 1 860 ? 48.898 56.446  27.697  1.00 22.89  ? 885  ARG   A NE  1 
ATOM   6599 C  CZ  . ARG   A 1 860 ? 48.260 57.306  26.885  1.00 24.27  ? 885  ARG   A CZ  1 
ATOM   6600 N  NH1 . ARG   A 1 860 ? 47.084 57.806  27.229  1.00 25.62  ? 885  ARG   A NH1 1 
ATOM   6601 N  NH2 . ARG   A 1 860 ? 48.824 57.701  25.754  1.00 26.53  ? 885  ARG   A NH2 1 
ATOM   6602 N  N   . THR   A 1 861 ? 44.093 53.301  31.689  1.00 15.06  ? 886  THR   A N   1 
ATOM   6603 C  CA  . THR   A 1 861 ? 43.568 52.613  32.849  1.00 14.68  ? 886  THR   A CA  1 
ATOM   6604 C  C   . THR   A 1 861 ? 42.716 51.388  32.389  1.00 14.95  ? 886  THR   A C   1 
ATOM   6605 O  O   . THR   A 1 861 ? 42.801 50.319  32.995  1.00 14.47  ? 886  THR   A O   1 
ATOM   6606 C  CB  . THR   A 1 861 ? 42.724 53.559  33.696  1.00 15.97  ? 886  THR   A CB  1 
ATOM   6607 O  OG1 . THR   A 1 861 ? 43.621 54.560  34.173  1.00 16.24  ? 886  THR   A OG1 1 
ATOM   6608 C  CG2 . THR   A 1 861 ? 42.127 52.876  34.878  1.00 16.83  ? 886  THR   A CG2 1 
ATOM   6609 N  N   . ARG   A 1 862 ? 41.887 51.559  31.325  1.00 13.74  ? 887  ARG   A N   1 
ATOM   6610 C  CA  . ARG   A 1 862 ? 41.094 50.410  30.861  1.00 14.05  ? 887  ARG   A CA  1 
ATOM   6611 C  C   . ARG   A 1 862 ? 42.022 49.352  30.274  1.00 14.11  ? 887  ARG   A C   1 
ATOM   6612 O  O   . ARG   A 1 862 ? 41.770 48.155  30.471  1.00 14.07  ? 887  ARG   A O   1 
ATOM   6613 C  CB  . ARG   A 1 862 ? 40.086 50.852  29.778  1.00 14.28  ? 887  ARG   A CB  1 
ATOM   6614 C  CG  . ARG   A 1 862 ? 38.907 51.640  30.329  1.00 15.06  ? 887  ARG   A CG  1 
ATOM   6615 C  CD  . ARG   A 1 862 ? 38.011 50.810  31.216  1.00 15.17  ? 887  ARG   A CD  1 
ATOM   6616 N  NE  . ARG   A 1 862 ? 36.770 51.541  31.529  1.00 16.26  ? 887  ARG   A NE  1 
ATOM   6617 C  CZ  . ARG   A 1 862 ? 35.861 51.121  32.390  1.00 17.59  ? 887  ARG   A CZ  1 
ATOM   6618 N  NH1 . ARG   A 1 862 ? 36.016 49.951  33.018  1.00 16.06  ? 887  ARG   A NH1 1 
ATOM   6619 N  NH2 . ARG   A 1 862 ? 34.737 51.821  32.577  1.00 18.11  ? 887  ARG   A NH2 1 
ATOM   6620 N  N   . LEU   A 1 863 ? 43.090 49.745  29.567  1.00 13.56  ? 888  LEU   A N   1 
ATOM   6621 C  CA  . LEU   A 1 863 ? 44.022 48.745  29.012  1.00 13.88  ? 888  LEU   A CA  1 
ATOM   6622 C  C   . LEU   A 1 863 ? 44.621 47.901  30.137  1.00 14.98  ? 888  LEU   A C   1 
ATOM   6623 O  O   . LEU   A 1 863 ? 44.692 46.679  30.001  1.00 16.15  ? 888  LEU   A O   1 
ATOM   6624 C  CB  . LEU   A 1 863 ? 45.138 49.479  28.271  1.00 13.75  ? 888  LEU   A CB  1 
ATOM   6625 C  CG  . LEU   A 1 863 ? 46.255 48.575  27.736  1.00 14.97  ? 888  LEU   A CG  1 
ATOM   6626 C  CD1 . LEU   A 1 863 ? 45.722 47.583  26.747  1.00 16.80  ? 888  LEU   A CD1 1 
ATOM   6627 C  CD2 . LEU   A 1 863 ? 47.342 49.424  27.079  1.00 15.80  ? 888  LEU   A CD2 1 
ATOM   6628 N  N   . GLU   A 1 864 ? 45.019 48.541  31.274  1.00 14.14  ? 889  GLU   A N   1 
ATOM   6629 C  CA  . GLU   A 1 864 ? 45.563 47.753  32.362  1.00 13.92  ? 889  GLU   A CA  1 
ATOM   6630 C  C   . GLU   A 1 864 ? 44.517 46.890  33.025  1.00 14.12  ? 889  GLU   A C   1 
ATOM   6631 O  O   . GLU   A 1 864 ? 44.819 45.792  33.491  1.00 14.94  ? 889  GLU   A O   1 
ATOM   6632 C  CB  . GLU   A 1 864 ? 46.297 48.635  33.375  1.00 16.13  ? 889  GLU   A CB  1 
ATOM   6633 C  CG  . GLU   A 1 864 ? 47.127 47.859  34.381  1.00 17.01  ? 889  GLU   A CG  1 
ATOM   6634 C  CD  . GLU   A 1 864 ? 46.358 47.205  35.516  1.00 19.28  ? 889  GLU   A CD  1 
ATOM   6635 O  OE1 . GLU   A 1 864 ? 45.307 47.744  35.945  1.00 18.12  ? 889  GLU   A OE1 1 
ATOM   6636 O  OE2 . GLU   A 1 864 ? 46.801 46.126  35.989  1.00 20.40  ? 889  GLU   A OE2 1 
ATOM   6637 N  N   . GLU   A 1 865 ? 43.226 47.349  33.064  1.00 13.22  ? 890  GLU   A N   1 
ATOM   6638 C  CA  . GLU   A 1 865 ? 42.186 46.462  33.605  1.00 13.06  ? 890  GLU   A CA  1 
ATOM   6639 C  C   . GLU   A 1 865 ? 42.161 45.160  32.817  1.00 13.38  ? 890  GLU   A C   1 
ATOM   6640 O  O   . GLU   A 1 865 ? 42.043 44.097  33.399  1.00 14.11  ? 890  GLU   A O   1 
ATOM   6641 C  CB  . GLU   A 1 865 ? 40.771 47.078  33.534  1.00 13.40  ? 890  GLU   A CB  1 
ATOM   6642 C  CG  . GLU   A 1 865 ? 40.533 48.217  34.520  1.00 14.24  ? 890  GLU   A CG  1 
ATOM   6643 C  CD  . GLU   A 1 865 ? 39.153 48.834  34.424  1.00 14.57  ? 890  GLU   A CD  1 
ATOM   6644 O  OE1 . GLU   A 1 865 ? 38.380 48.426  33.529  1.00 14.50  ? 890  GLU   A OE1 1 
ATOM   6645 O  OE2 . GLU   A 1 865 ? 38.838 49.723  35.256  1.00 15.80  ? 890  GLU   A OE2 1 
ATOM   6646 N  N   . VAL   A 1 866 ? 42.207 45.276  31.491  1.00 13.52  ? 891  VAL   A N   1 
ATOM   6647 C  CA  . VAL   A 1 866 ? 42.136 44.088  30.646  1.00 13.13  ? 891  VAL   A CA  1 
ATOM   6648 C  C   . VAL   A 1 866 ? 43.392 43.241  30.802  1.00 14.02  ? 891  VAL   A C   1 
ATOM   6649 O  O   . VAL   A 1 866 ? 43.277 42.048  31.042  1.00 14.27  ? 891  VAL   A O   1 
ATOM   6650 C  CB  . VAL   A 1 866 ? 41.955 44.557  29.188  1.00 13.87  ? 891  VAL   A CB  1 
ATOM   6651 C  CG1 . VAL   A 1 866 ? 42.043 43.360  28.217  1.00 15.25  ? 891  VAL   A CG1 1 
ATOM   6652 C  CG2 . VAL   A 1 866 ? 40.589 45.242  29.050  1.00 14.83  ? 891  VAL   A CG2 1 
ATOM   6653 N  N   . LYS   A 1 867 ? 44.566 43.860  30.754  1.00 14.61  ? 892  LYS   A N   1 
ATOM   6654 C  CA  . LYS   A 1 867 ? 45.795 43.058  30.897  1.00 14.35  ? 892  LYS   A CA  1 
ATOM   6655 C  C   . LYS   A 1 867 ? 45.850 42.391  32.247  1.00 15.79  ? 892  LYS   A C   1 
ATOM   6656 O  O   . LYS   A 1 867 ? 46.200 41.209  32.347  1.00 16.99  ? 892  LYS   A O   1 
ATOM   6657 C  CB  . LYS   A 1 867 ? 47.005 43.941  30.701  1.00 15.90  ? 892  LYS   A CB  1 
ATOM   6658 C  CG  . LYS   A 1 867 ? 47.224 44.394  29.274  1.00 19.33  ? 892  LYS   A CG  1 
ATOM   6659 C  CD  . LYS   A 1 867 ? 48.507 45.238  29.286  1.00 26.84  ? 892  LYS   A CD  1 
ATOM   6660 C  CE  . LYS   A 1 867 ? 48.847 45.810  27.949  1.00 34.57  ? 892  LYS   A CE  1 
ATOM   6661 N  NZ  . LYS   A 1 867 ? 50.158 46.544  27.997  1.00 39.56  ? 892  LYS   A NZ  1 
ATOM   6662 N  N   . GLY   A 1 868 ? 45.544 43.159  33.293  1.00 15.78  ? 893  GLY   A N   1 
ATOM   6663 C  CA  . GLY   A 1 868 ? 45.632 42.623  34.647  1.00 15.98  ? 893  GLY   A CA  1 
ATOM   6664 C  C   . GLY   A 1 868 ? 44.631 41.520  34.896  1.00 16.25  ? 893  GLY   A C   1 
ATOM   6665 O  O   . GLY   A 1 868 ? 44.911 40.529  35.594  1.00 17.38  ? 893  GLY   A O   1 
ATOM   6666 N  N   . PHE   A 1 869 ? 43.374 41.716  34.426  1.00 14.98  ? 894  PHE   A N   1 
ATOM   6667 C  CA  . PHE   A 1 869 ? 42.357 40.678  34.637  1.00 14.59  ? 894  PHE   A CA  1 
ATOM   6668 C  C   . PHE   A 1 869 ? 42.771 39.384  33.946  1.00 15.31  ? 894  PHE   A C   1 
ATOM   6669 O  O   . PHE   A 1 869 ? 42.778 38.319  34.587  1.00 15.92  ? 894  PHE   A O   1 
ATOM   6670 C  CB  . PHE   A 1 869 ? 40.964 41.140  34.173  1.00 14.51  ? 894  PHE   A CB  1 
ATOM   6671 C  CG  . PHE   A 1 869 ? 39.956 40.036  34.327  1.00 15.17  ? 894  PHE   A CG  1 
ATOM   6672 C  CD1 . PHE   A 1 869 ? 39.548 39.635  35.579  1.00 17.10  ? 894  PHE   A CD1 1 
ATOM   6673 C  CD2 . PHE   A 1 869 ? 39.505 39.327  33.228  1.00 16.39  ? 894  PHE   A CD2 1 
ATOM   6674 C  CE1 . PHE   A 1 869 ? 38.667 38.568  35.727  1.00 17.04  ? 894  PHE   A CE1 1 
ATOM   6675 C  CE2 . PHE   A 1 869 ? 38.665 38.227  33.374  1.00 16.47  ? 894  PHE   A CE2 1 
ATOM   6676 C  CZ  . PHE   A 1 869 ? 38.237 37.869  34.622  1.00 16.64  ? 894  PHE   A CZ  1 
ATOM   6677 N  N   . PHE   A 1 870 ? 43.044 39.463  32.634  1.00 14.91  ? 895  PHE   A N   1 
ATOM   6678 C  CA  . PHE   A 1 870 ? 43.307 38.219  31.908  1.00 15.82  ? 895  PHE   A CA  1 
ATOM   6679 C  C   . PHE   A 1 870 ? 44.604 37.592  32.330  1.00 16.97  ? 895  PHE   A C   1 
ATOM   6680 O  O   . PHE   A 1 870 ? 44.648 36.358  32.418  1.00 17.33  ? 895  PHE   A O   1 
ATOM   6681 C  CB  . PHE   A 1 870 ? 43.186 38.444  30.402  1.00 15.62  ? 895  PHE   A CB  1 
ATOM   6682 C  CG  . PHE   A 1 870 ? 41.739 38.684  30.022  1.00 14.99  ? 895  PHE   A CG  1 
ATOM   6683 C  CD1 . PHE   A 1 870 ? 40.818 37.643  30.019  1.00 15.67  ? 895  PHE   A CD1 1 
ATOM   6684 C  CD2 . PHE   A 1 870 ? 41.308 39.937  29.637  1.00 15.41  ? 895  PHE   A CD2 1 
ATOM   6685 C  CE1 . PHE   A 1 870 ? 39.485 37.868  29.682  1.00 15.88  ? 895  PHE   A CE1 1 
ATOM   6686 C  CE2 . PHE   A 1 870 ? 39.976 40.166  29.286  1.00 16.04  ? 895  PHE   A CE2 1 
ATOM   6687 C  CZ  . PHE   A 1 870 ? 39.072 39.119  29.278  1.00 15.89  ? 895  PHE   A CZ  1 
ATOM   6688 N  N   . SER   A 1 871 ? 45.624 38.379  32.687  1.00 16.59  ? 896  SER   A N   1 
ATOM   6689 C  CA  . SER   A 1 871 ? 46.888 37.722  33.123  1.00 18.07  ? 896  SER   A CA  1 
ATOM   6690 C  C   . SER   A 1 871 ? 46.654 36.945  34.441  1.00 19.87  ? 896  SER   A C   1 
ATOM   6691 O  O   . SER   A 1 871 ? 47.202 35.845  34.614  1.00 21.83  ? 896  SER   A O   1 
ATOM   6692 C  CB  . SER   A 1 871 ? 48.036 38.716  33.203  1.00 21.41  ? 896  SER   A CB  1 
ATOM   6693 O  OG  . SER   A 1 871 ? 47.775 39.701  34.180  1.00 25.13  ? 896  SER   A OG  1 
ATOM   6694 N  N   . SER   A 1 872 ? 45.727 37.411  35.272  1.00 19.72  ? 897  SER   A N   1 
ATOM   6695 C  CA  . SER   A 1 872 ? 45.450 36.763  36.546  1.00 21.40  ? 897  SER   A CA  1 
ATOM   6696 C  C   . SER   A 1 872 ? 44.799 35.398  36.398  1.00 22.81  ? 897  SER   A C   1 
ATOM   6697 O  O   . SER   A 1 872 ? 44.808 34.613  37.355  1.00 23.92  ? 897  SER   A O   1 
ATOM   6698 C  CB  . SER   A 1 872 ? 44.593 37.677  37.411  1.00 23.63  ? 897  SER   A CB  1 
ATOM   6699 O  OG  . SER   A 1 872 ? 43.224 37.648  37.028  1.00 25.49  ? 897  SER   A OG  1 
ATOM   6700 N  N   . LEU   A 1 873 ? 44.257 35.084  35.232  1.00 21.71  ? 898  LEU   A N   1 
ATOM   6701 C  CA  . LEU   A 1 873 ? 43.578 33.805  35.010  1.00 21.85  ? 898  LEU   A CA  1 
ATOM   6702 C  C   . LEU   A 1 873 ? 44.528 32.641  34.818  1.00 22.68  ? 898  LEU   A C   1 
ATOM   6703 O  O   . LEU   A 1 873 ? 44.083 31.490  34.845  1.00 22.82  ? 898  LEU   A O   1 
ATOM   6704 C  CB  . LEU   A 1 873 ? 42.675 33.912  33.779  1.00 21.67  ? 898  LEU   A CB  1 
ATOM   6705 C  CG  . LEU   A 1 873 ? 41.629 34.983  33.895  1.00 22.12  ? 898  LEU   A CG  1 
ATOM   6706 C  CD1 . LEU   A 1 873 ? 40.876 35.081  32.590  1.00 21.78  ? 898  LEU   A CD1 1 
ATOM   6707 C  CD2 . LEU   A 1 873 ? 40.644 34.684  35.024  1.00 22.91  ? 898  LEU   A CD2 1 
ATOM   6708 N  N   . LYS   A 1 874 ? 45.813 32.924  34.524  1.00 23.46  ? 899  LYS   A N   1 
ATOM   6709 C  CA  . LYS   A 1 874 ? 46.793 31.867  34.268  1.00 24.00  ? 899  LYS   A CA  1 
ATOM   6710 C  C   . LYS   A 1 874 ? 46.260 30.833  33.218  1.00 25.02  ? 899  LYS   A C   1 
ATOM   6711 O  O   . LYS   A 1 874 ? 45.912 31.273  32.120  1.00 24.07  ? 899  LYS   A O   1 
ATOM   6712 C  CB  . LYS   A 1 874 ? 47.291 31.262  35.608  1.00 27.56  ? 899  LYS   A CB  1 
ATOM   6713 C  CG  . LYS   A 1 874 ? 47.961 32.335  36.439  1.00 32.78  ? 899  LYS   A CG  1 
ATOM   6714 C  CD  . LYS   A 1 874 ? 48.144 31.887  37.901  1.00 39.80  ? 899  LYS   A CD  1 
ATOM   6715 C  CE  . LYS   A 1 874 ? 49.092 32.808  38.644  1.00 46.06  ? 899  LYS   A CE  1 
ATOM   6716 N  NZ  . LYS   A 1 874 ? 49.111 32.516  40.108  1.00 50.31  ? 899  LYS   A NZ  1 
ATOM   6717 N  N   . GLU   A 1 875 ? 46.119 29.549  33.528  1.00 24.76  ? 900  GLU   A N   1 
ATOM   6718 C  CA  . GLU   A 1 875 ? 45.671 28.565  32.555  1.00 25.30  ? 900  GLU   A CA  1 
ATOM   6719 C  C   . GLU   A 1 875 ? 44.192 28.695  32.138  1.00 23.81  ? 900  GLU   A C   1 
ATOM   6720 O  O   . GLU   A 1 875 ? 43.783 28.070  31.161  1.00 25.15  ? 900  GLU   A O   1 
ATOM   6721 C  CB  . GLU   A 1 875 ? 45.958 27.146  33.075  1.00 30.22  ? 900  GLU   A CB  1 
ATOM   6722 C  CG  . GLU   A 1 875 ? 45.101 26.761  34.271  1.00 38.20  ? 900  GLU   A CG  1 
ATOM   6723 C  CD  . GLU   A 1 875 ? 45.598 27.194  35.639  1.00 47.82  ? 900  GLU   A CD  1 
ATOM   6724 O  OE1 . GLU   A 1 875 ? 46.745 27.687  35.738  1.00 48.04  ? 900  GLU   A OE1 1 
ATOM   6725 O  OE2 . GLU   A 1 875 ? 44.837 27.025  36.619  1.00 52.21  ? 900  GLU   A OE2 1 
ATOM   6726 N  N   . ASN   A 1 876 ? 43.403 29.463  32.898  1.00 22.93  ? 901  ASN   A N   1 
ATOM   6727 C  CA  . ASN   A 1 876 ? 41.980 29.607  32.590  1.00 23.16  ? 901  ASN   A CA  1 
ATOM   6728 C  C   . ASN   A 1 876 ? 41.692 30.848  31.716  1.00 20.83  ? 901  ASN   A C   1 
ATOM   6729 O  O   . ASN   A 1 876 ? 40.673 31.497  31.946  1.00 20.03  ? 901  ASN   A O   1 
ATOM   6730 C  CB  . ASN   A 1 876 ? 41.131 29.602  33.867  1.00 25.92  ? 901  ASN   A CB  1 
ATOM   6731 C  CG  . ASN   A 1 876 ? 39.692 29.239  33.572  1.00 30.83  ? 901  ASN   A CG  1 
ATOM   6732 O  OD1 . ASN   A 1 876 ? 39.419 28.460  32.667  1.00 32.47  ? 901  ASN   A OD1 1 
ATOM   6733 N  ND2 . ASN   A 1 876 ? 38.749 29.818  34.292  1.00 34.78  ? 901  ASN   A ND2 1 
ATOM   6734 N  N   . GLY   A 1 877 ? 42.586 31.194  30.787  1.00 19.47  ? 902  GLY   A N   1 
ATOM   6735 C  CA  . GLY   A 1 877 ? 42.275 32.297  29.862  1.00 18.52  ? 902  GLY   A CA  1 
ATOM   6736 C  C   . GLY   A 1 877 ? 43.358 33.302  29.545  1.00 17.62  ? 902  GLY   A C   1 
ATOM   6737 O  O   . GLY   A 1 877 ? 43.208 34.078  28.599  1.00 16.87  ? 902  GLY   A O   1 
ATOM   6738 N  N   . SER   A 1 878 ? 44.486 33.320  30.299  1.00 17.55  ? 903  SER   A N   1 
ATOM   6739 C  CA  . SER   A 1 878 ? 45.513 34.329  30.019  1.00 17.86  ? 903  SER   A CA  1 
ATOM   6740 C  C   . SER   A 1 878 ? 46.077 34.253  28.617  1.00 18.25  ? 903  SER   A C   1 
ATOM   6741 O  O   . SER   A 1 878 ? 46.573 35.239  28.110  1.00 19.33  ? 903  SER   A O   1 
ATOM   6742 C  CB  . SER   A 1 878 ? 46.645 34.241  31.036  1.00 18.97  ? 903  SER   A CB  1 
ATOM   6743 O  OG  . SER   A 1 878 ? 47.427 33.063  30.882  1.00 19.87  ? 903  SER   A OG  1 
ATOM   6744 N  N   . GLN   A 1 879 ? 46.052 33.058  28.017  1.00 18.49  ? 904  GLN   A N   1 
ATOM   6745 C  CA  . GLN   A 1 879 ? 46.672 32.845  26.717  1.00 18.37  ? 904  GLN   A CA  1 
ATOM   6746 C  C   . GLN   A 1 879 ? 45.685 32.855  25.554  1.00 17.73  ? 904  GLN   A C   1 
ATOM   6747 O  O   . GLN   A 1 879 ? 46.094 32.573  24.421  1.00 18.81  ? 904  GLN   A O   1 
ATOM   6748 C  CB  . GLN   A 1 879 ? 47.492 31.538  26.684  1.00 21.35  ? 904  GLN   A CB  1 
ATOM   6749 C  CG  . GLN   A 1 879 ? 48.562 31.447  27.800  1.00 24.37  ? 904  GLN   A CG  1 
ATOM   6750 C  CD  . GLN   A 1 879 ? 49.522 32.610  27.772  1.00 31.66  ? 904  GLN   A CD  1 
ATOM   6751 O  OE1 . GLN   A 1 879 ? 50.209 32.859  26.763  1.00 35.88  ? 904  GLN   A OE1 1 
ATOM   6752 N  NE2 . GLN   A 1 879 ? 49.596 33.364  28.872  1.00 32.67  ? 904  GLN   A NE2 1 
ATOM   6753 N  N   . LEU   A 1 880 ? 44.424 33.286  25.794  1.00 16.36  ? 905  LEU   A N   1 
ATOM   6754 C  CA  . LEU   A 1 880 ? 43.479 33.378  24.685  1.00 15.08  ? 905  LEU   A CA  1 
ATOM   6755 C  C   . LEU   A 1 880 ? 43.906 34.345  23.638  1.00 14.65  ? 905  LEU   A C   1 
ATOM   6756 O  O   . LEU   A 1 880 ? 44.356 35.462  23.933  1.00 15.43  ? 905  LEU   A O   1 
ATOM   6757 C  CB  . LEU   A 1 880 ? 42.140 33.856  25.215  1.00 15.45  ? 905  LEU   A CB  1 
ATOM   6758 C  CG  . LEU   A 1 880 ? 41.377 32.801  26.033  1.00 16.69  ? 905  LEU   A CG  1 
ATOM   6759 C  CD1 . LEU   A 1 880 ? 40.222 33.426  26.780  1.00 16.94  ? 905  LEU   A CD1 1 
ATOM   6760 C  CD2 . LEU   A 1 880 ? 40.903 31.633  25.135  1.00 18.16  ? 905  LEU   A CD2 1 
ATOM   6761 N  N   . ARG   A 1 881 ? 43.725 33.957  22.360  1.00 13.38  ? 906  ARG   A N   1 
ATOM   6762 C  CA  . ARG   A 1 881 ? 44.070 34.865  21.284  1.00 14.87  ? 906  ARG   A CA  1 
ATOM   6763 C  C   . ARG   A 1 881 ? 43.152 36.092  21.344  1.00 14.58  ? 906  ARG   A C   1 
ATOM   6764 O  O   . ARG   A 1 881 ? 43.618 37.182  21.017  1.00 15.42  ? 906  ARG   A O   1 
ATOM   6765 C  CB  . ARG   A 1 881 ? 43.930 34.166  19.933  1.00 16.67  ? 906  ARG   A CB  1 
ATOM   6766 C  CG  . ARG   A 1 881 ? 44.365 35.053  18.812  1.00 23.16  ? 906  ARG   A CG  1 
ATOM   6767 C  CD  . ARG   A 1 881 ? 44.521 34.291  17.519  1.00 26.65  ? 906  ARG   A CD  1 
ATOM   6768 N  NE  . ARG   A 1 881 ? 45.548 33.257  17.613  1.00 28.28  ? 906  ARG   A NE  1 
ATOM   6769 C  CZ  . ARG   A 1 881 ? 46.852 33.469  17.433  1.00 29.84  ? 906  ARG   A CZ  1 
ATOM   6770 N  NH1 . ARG   A 1 881 ? 47.705 32.470  17.525  1.00 27.69  ? 906  ARG   A NH1 1 
ATOM   6771 N  NH2 . ARG   A 1 881 ? 47.310 34.697  17.192  1.00 31.42  ? 906  ARG   A NH2 1 
ATOM   6772 N  N   . CYS   A 1 882 ? 41.878 35.921  21.739  1.00 14.55  ? 907  CYS   A N   1 
ATOM   6773 C  CA  . CYS   A 1 882 ? 40.984 37.104  21.739  1.00 14.09  ? 907  CYS   A CA  1 
ATOM   6774 C  C   . CYS   A 1 882 ? 41.481 38.154  22.738  1.00 14.84  ? 907  CYS   A C   1 
ATOM   6775 O  O   . CYS   A 1 882 ? 41.187 39.342  22.555  1.00 14.42  ? 907  CYS   A O   1 
ATOM   6776 C  CB  . CYS   A 1 882 ? 39.539 36.708  22.041  1.00 14.68  ? 907  CYS   A CB  1 
ATOM   6777 S  SG  . CYS   A 1 882 ? 39.299 35.890  23.653  1.00 15.31  ? 907  CYS   A SG  1 
ATOM   6778 N  N   . VAL   A 1 883 ? 42.150 37.737  23.803  1.00 14.57  ? 908  VAL   A N   1 
ATOM   6779 C  CA  . VAL   A 1 883 ? 42.638 38.672  24.809  1.00 15.32  ? 908  VAL   A CA  1 
ATOM   6780 C  C   . VAL   A 1 883 ? 43.760 39.505  24.195  1.00 15.32  ? 908  VAL   A C   1 
ATOM   6781 O  O   . VAL   A 1 883 ? 43.762 40.725  24.325  1.00 15.21  ? 908  VAL   A O   1 
ATOM   6782 C  CB  . VAL   A 1 883 ? 43.122 37.862  26.036  1.00 16.09  ? 908  VAL   A CB  1 
ATOM   6783 C  CG1 . VAL   A 1 883 ? 43.930 38.762  26.984  1.00 16.38  ? 908  VAL   A CG1 1 
ATOM   6784 C  CG2 . VAL   A 1 883 ? 41.925 37.251  26.769  1.00 16.70  ? 908  VAL   A CG2 1 
ATOM   6785 N  N   . GLN   A 1 884 ? 44.680 38.884  23.434  1.00 14.98  ? 909  GLN   A N   1 
ATOM   6786 C  CA  . GLN   A 1 884 ? 45.730 39.655  22.796  1.00 14.89  ? 909  GLN   A CA  1 
ATOM   6787 C  C   . GLN   A 1 884 ? 45.132 40.553  21.723  1.00 14.56  ? 909  GLN   A C   1 
ATOM   6788 O  O   . GLN   A 1 884 ? 45.589 41.705  21.531  1.00 15.04  ? 909  GLN   A O   1 
ATOM   6789 C  CB  . GLN   A 1 884 ? 46.805 38.764  22.203  1.00 16.92  ? 909  GLN   A CB  1 
ATOM   6790 C  CG  . GLN   A 1 884 ? 47.997 39.584  21.690  1.00 20.14  ? 909  GLN   A CG  1 
ATOM   6791 C  CD  . GLN   A 1 884 ? 48.719 40.374  22.780  1.00 23.99  ? 909  GLN   A CD  1 
ATOM   6792 O  OE1 . GLN   A 1 884 ? 48.691 40.028  23.996  1.00 24.68  ? 909  GLN   A OE1 1 
ATOM   6793 N  NE2 . GLN   A 1 884 ? 49.379 41.471  22.370  1.00 23.52  ? 909  GLN   A NE2 1 
ATOM   6794 N  N   . GLN   A 1 885 ? 44.099 40.077  21.005  1.00 14.60  ? 910  GLN   A N   1 
ATOM   6795 C  CA  . GLN   A 1 885 ? 43.460 40.896  19.994  1.00 13.64  ? 910  GLN   A CA  1 
ATOM   6796 C  C   . GLN   A 1 885 ? 42.820 42.127  20.630  1.00 13.99  ? 910  GLN   A C   1 
ATOM   6797 O  O   . GLN   A 1 885 ? 42.985 43.227  20.092  1.00 14.63  ? 910  GLN   A O   1 
ATOM   6798 C  CB  . GLN   A 1 885 ? 42.404 40.035  19.263  1.00 14.66  ? 910  GLN   A CB  1 
ATOM   6799 C  CG  . GLN   A 1 885 ? 41.685 40.755  18.143  1.00 20.42  ? 910  GLN   A CG  1 
ATOM   6800 C  CD  . GLN   A 1 885 ? 40.601 39.886  17.514  1.00 26.44  ? 910  GLN   A CD  1 
ATOM   6801 O  OE1 . GLN   A 1 885 ? 39.666 40.415  16.904  1.00 32.44  ? 910  GLN   A OE1 1 
ATOM   6802 N  NE2 . GLN   A 1 885 ? 40.667 38.567  17.701  1.00 27.60  ? 910  GLN   A NE2 1 
ATOM   6803 N  N   . THR   A 1 886 ? 42.077 41.946  21.752  1.00 13.58  ? 911  THR   A N   1 
ATOM   6804 C  CA  . THR   A 1 886 ? 41.458 43.142  22.343  1.00 13.31  ? 911  THR   A CA  1 
ATOM   6805 C  C   . THR   A 1 886 ? 42.495 44.077  22.960  1.00 13.87  ? 911  THR   A C   1 
ATOM   6806 O  O   . THR   A 1 886 ? 42.350 45.303  22.853  1.00 14.15  ? 911  THR   A O   1 
ATOM   6807 C  CB  . THR   A 1 886 ? 40.344 42.778  23.313  1.00 14.58  ? 911  THR   A CB  1 
ATOM   6808 O  OG1 . THR   A 1 886 ? 39.400 43.859  23.285  1.00 15.40  ? 911  THR   A OG1 1 
ATOM   6809 C  CG2 . THR   A 1 886 ? 40.833 42.498  24.753  1.00 15.32  ? 911  THR   A CG2 1 
ATOM   6810 N  N   . ILE   A 1 887 ? 43.597 43.549  23.506  1.00 14.23  ? 912  ILE   A N   1 
ATOM   6811 C  CA  . ILE   A 1 887 ? 44.660 44.421  24.039  1.00 14.87  ? 912  ILE   A CA  1 
ATOM   6812 C  C   . ILE   A 1 887 ? 45.213 45.269  22.889  1.00 15.40  ? 912  ILE   A C   1 
ATOM   6813 O  O   . ILE   A 1 887 ? 45.371 46.496  23.024  1.00 15.56  ? 912  ILE   A O   1 
ATOM   6814 C  CB  . ILE   A 1 887 ? 45.761 43.550  24.673  1.00 15.73  ? 912  ILE   A CB  1 
ATOM   6815 C  CG1 . ILE   A 1 887 ? 45.256 43.058  26.039  1.00 16.57  ? 912  ILE   A CG1 1 
ATOM   6816 C  CG2 . ILE   A 1 887 ? 47.100 44.308  24.808  1.00 17.33  ? 912  ILE   A CG2 1 
ATOM   6817 C  CD1 . ILE   A 1 887 ? 46.046 41.917  26.609  1.00 17.10  ? 912  ILE   A CD1 1 
ATOM   6818 N  N   . GLU   A 1 888 ? 45.517 44.628  21.735  1.00 14.71  ? 913  GLU   A N   1 
ATOM   6819 C  CA  . GLU   A 1 888 ? 46.095 45.392  20.624  1.00 15.18  ? 913  GLU   A CA  1 
ATOM   6820 C  C   . GLU   A 1 888 ? 45.071 46.390  20.048  1.00 14.62  ? 913  GLU   A C   1 
ATOM   6821 O  O   . GLU   A 1 888 ? 45.450 47.459  19.544  1.00 15.17  ? 913  GLU   A O   1 
ATOM   6822 C  CB  . GLU   A 1 888 ? 46.583 44.423  19.525  1.00 15.73  ? 913  GLU   A CB  1 
ATOM   6823 C  CG  . GLU   A 1 888 ? 47.800 43.712  20.054  1.00 16.19  ? 913  GLU   A CG  1 
ATOM   6824 C  CD  . GLU   A 1 888 ? 48.365 42.602  19.198  1.00 20.36  ? 913  GLU   A CD  1 
ATOM   6825 O  OE1 . GLU   A 1 888 ? 47.772 42.275  18.146  1.00 18.58  ? 913  GLU   A OE1 1 
ATOM   6826 O  OE2 . GLU   A 1 888 ? 49.448 42.077  19.576  1.00 21.98  ? 913  GLU   A OE2 1 
ATOM   6827 N  N   . THR   A 1 889 ? 43.783 46.028  20.095  1.00 14.62  ? 914  THR   A N   1 
ATOM   6828 C  CA  . THR   A 1 889 ? 42.742 46.941  19.644  1.00 13.86  ? 914  THR   A CA  1 
ATOM   6829 C  C   . THR   A 1 889 ? 42.687 48.162  20.574  1.00 13.47  ? 914  THR   A C   1 
ATOM   6830 O  O   . THR   A 1 889 ? 42.587 49.306  20.081  1.00 13.56  ? 914  THR   A O   1 
ATOM   6831 C  CB  . THR   A 1 889 ? 41.394 46.269  19.600  1.00 14.56  ? 914  THR   A CB  1 
ATOM   6832 O  OG1 . THR   A 1 889 ? 41.495 45.156  18.679  1.00 14.91  ? 914  THR   A OG1 1 
ATOM   6833 C  CG2 . THR   A 1 889 ? 40.314 47.213  19.122  1.00 15.51  ? 914  THR   A CG2 1 
ATOM   6834 N  N   . ILE   A 1 890 ? 42.711 47.936  21.898  1.00 13.16  ? 915  ILE   A N   1 
ATOM   6835 C  CA  . ILE   A 1 890 ? 42.683 49.073  22.825  1.00 12.94  ? 915  ILE   A CA  1 
ATOM   6836 C  C   . ILE   A 1 890 ? 43.925 49.917  22.688  1.00 13.50  ? 915  ILE   A C   1 
ATOM   6837 O  O   . ILE   A 1 890 ? 43.834 51.140  22.698  1.00 14.96  ? 915  ILE   A O   1 
ATOM   6838 C  CB  . ILE   A 1 890 ? 42.518 48.550  24.257  1.00 13.06  ? 915  ILE   A CB  1 
ATOM   6839 C  CG1 . ILE   A 1 890 ? 41.153 47.862  24.428  1.00 12.57  ? 915  ILE   A CG1 1 
ATOM   6840 C  CG2 . ILE   A 1 890 ? 42.637 49.680  25.260  1.00 13.65  ? 915  ILE   A CG2 1 
ATOM   6841 C  CD1 . ILE   A 1 890 ? 41.100 47.048  25.732  1.00 14.42  ? 915  ILE   A CD1 1 
ATOM   6842 N  N   . GLU   A 1 891 ? 45.096 49.284  22.437  1.00 13.54  ? 916  GLU   A N   1 
ATOM   6843 C  CA  . GLU   A 1 891 ? 46.317 50.067  22.245  1.00 13.90  ? 916  GLU   A CA  1 
ATOM   6844 C  C   . GLU   A 1 891 ? 46.171 50.961  21.031  1.00 14.51  ? 916  GLU   A C   1 
ATOM   6845 O  O   . GLU   A 1 891 ? 46.599 52.119  21.057  1.00 15.02  ? 916  GLU   A O   1 
ATOM   6846 C  CB  . GLU   A 1 891 ? 47.491 49.095  22.061  1.00 15.44  ? 916  GLU   A CB  1 
ATOM   6847 C  CG  . GLU   A 1 891 ? 47.926 48.573  23.425  1.00 16.86  ? 916  GLU   A CG  1 
ATOM   6848 C  CD  . GLU   A 1 891 ? 48.897 47.412  23.427  1.00 21.14  ? 916  GLU   A CD  1 
ATOM   6849 O  OE1 . GLU   A 1 891 ? 49.065 46.765  22.369  1.00 20.76  ? 916  GLU   A OE1 1 
ATOM   6850 O  OE2 . GLU   A 1 891 ? 49.421 47.089  24.516  1.00 24.84  ? 916  GLU   A OE2 1 
ATOM   6851 N  N   . GLU   A 1 892 ? 45.559 50.433  19.962  1.00 14.08  ? 917  GLU   A N   1 
ATOM   6852 C  CA  . GLU   A 1 892 ? 45.323 51.250  18.778  1.00 13.53  ? 917  GLU   A CA  1 
ATOM   6853 C  C   . GLU   A 1 892 ? 44.322 52.347  19.073  1.00 14.83  ? 917  GLU   A C   1 
ATOM   6854 O  O   . GLU   A 1 892 ? 44.484 53.463  18.604  1.00 14.77  ? 917  GLU   A O   1 
ATOM   6855 C  CB  . GLU   A 1 892 ? 44.814 50.379  17.617  1.00 14.75  ? 917  GLU   A CB  1 
ATOM   6856 C  CG  . GLU   A 1 892 ? 44.321 51.151  16.373  1.00 17.79  ? 917  GLU   A CG  1 
ATOM   6857 C  CD  . GLU   A 1 892 ? 45.370 52.008  15.671  1.00 18.68  ? 917  GLU   A CD  1 
ATOM   6858 O  OE1 . GLU   A 1 892 ? 46.583 51.780  15.884  1.00 19.13  ? 917  GLU   A OE1 1 
ATOM   6859 O  OE2 . GLU   A 1 892 ? 44.961 52.941  14.933  1.00 19.06  ? 917  GLU   A OE2 1 
ATOM   6860 N  N   . ASN   A 1 893 ? 43.263 52.034  19.825  1.00 14.15  ? 918  ASN   A N   1 
ATOM   6861 C  CA  . ASN   A 1 893 ? 42.257 53.082  20.137  1.00 14.02  ? 918  ASN   A CA  1 
ATOM   6862 C  C   . ASN   A 1 893 ? 42.893 54.212  20.928  1.00 13.49  ? 918  ASN   A C   1 
ATOM   6863 O  O   . ASN   A 1 893 ? 42.595 55.383  20.667  1.00 13.81  ? 918  ASN   A O   1 
ATOM   6864 C  CB  . ASN   A 1 893 ? 41.159 52.472  20.997  1.00 13.15  ? 918  ASN   A CB  1 
ATOM   6865 C  CG  . ASN   A 1 893 ? 40.274 51.485  20.285  1.00 14.08  ? 918  ASN   A CG  1 
ATOM   6866 O  OD1 . ASN   A 1 893 ? 40.142 51.495  19.047  1.00 14.07  ? 918  ASN   A OD1 1 
ATOM   6867 N  ND2 . ASN   A 1 893 ? 39.556 50.674  21.079  1.00 13.94  ? 918  ASN   A ND2 1 
ATOM   6868 N  N   . ILE   A 1 894 ? 43.783 53.874  21.876  1.00 13.24  ? 919  ILE   A N   1 
ATOM   6869 C  CA  . ILE   A 1 894 ? 44.468 54.922  22.660  1.00 13.84  ? 919  ILE   A CA  1 
ATOM   6870 C  C   . ILE   A 1 894 ? 45.309 55.808  21.738  1.00 15.83  ? 919  ILE   A C   1 
ATOM   6871 O  O   . ILE   A 1 894 ? 45.205 57.031  21.811  1.00 16.11  ? 919  ILE   A O   1 
ATOM   6872 C  CB  . ILE   A 1 894 ? 45.386 54.252  23.708  1.00 13.88  ? 919  ILE   A CB  1 
ATOM   6873 C  CG1 . ILE   A 1 894 ? 44.559 53.560  24.816  1.00 14.06  ? 919  ILE   A CG1 1 
ATOM   6874 C  CG2 . ILE   A 1 894 ? 46.302 55.295  24.398  1.00 16.03  ? 919  ILE   A CG2 1 
ATOM   6875 C  CD1 . ILE   A 1 894 ? 45.404 52.648  25.645  1.00 15.25  ? 919  ILE   A CD1 1 
ATOM   6876 N  N   . GLY   A 1 895 ? 46.129 55.192  20.886  1.00 15.15  ? 920  GLY   A N   1 
ATOM   6877 C  CA  . GLY   A 1 895 ? 46.982 55.968  20.003  1.00 14.41  ? 920  GLY   A CA  1 
ATOM   6878 C  C   . GLY   A 1 895 ? 46.188 56.764  19.004  1.00 14.84  ? 920  GLY   A C   1 
ATOM   6879 O  O   . GLY   A 1 895 ? 46.536 57.912  18.707  1.00 14.84  ? 920  GLY   A O   1 
ATOM   6880 N  N   . TRP   A 1 896 ? 45.134 56.160  18.434  1.00 14.48  ? 921  TRP   A N   1 
ATOM   6881 C  CA  . TRP   A 1 896 ? 44.330 56.848  17.422  1.00 13.57  ? 921  TRP   A CA  1 
ATOM   6882 C  C   . TRP   A 1 896 ? 43.623 58.055  18.045  1.00 14.33  ? 921  TRP   A C   1 
ATOM   6883 O  O   . TRP   A 1 896 ? 43.593 59.127  17.436  1.00 14.33  ? 921  TRP   A O   1 
ATOM   6884 C  CB  . TRP   A 1 896 ? 43.330 55.843  16.816  1.00 13.77  ? 921  TRP   A CB  1 
ATOM   6885 C  CG  . TRP   A 1 896 ? 42.516 56.369  15.681  1.00 14.44  ? 921  TRP   A CG  1 
ATOM   6886 C  CD1 . TRP   A 1 896 ? 42.746 56.150  14.348  1.00 15.48  ? 921  TRP   A CD1 1 
ATOM   6887 C  CD2 . TRP   A 1 896 ? 41.335 57.171  15.756  1.00 14.91  ? 921  TRP   A CD2 1 
ATOM   6888 N  NE1 . TRP   A 1 896 ? 41.779 56.766  13.602  1.00 15.90  ? 921  TRP   A NE1 1 
ATOM   6889 C  CE2 . TRP   A 1 896 ? 40.892 57.392  14.433  1.00 15.86  ? 921  TRP   A CE2 1 
ATOM   6890 C  CE3 . TRP   A 1 896 ? 40.548 57.646  16.817  1.00 15.41  ? 921  TRP   A CE3 1 
ATOM   6891 C  CZ2 . TRP   A 1 896 ? 39.710 58.089  14.147  1.00 16.90  ? 921  TRP   A CZ2 1 
ATOM   6892 C  CZ3 . TRP   A 1 896 ? 39.395 58.352  16.523  1.00 17.38  ? 921  TRP   A CZ3 1 
ATOM   6893 C  CH2 . TRP   A 1 896 ? 39.000 58.572  15.198  1.00 17.34  ? 921  TRP   A CH2 1 
ATOM   6894 N  N   A MET   A 1 897 ? 43.043 57.880  19.223  0.50 14.05  ? 922  MET   A N   1 
ATOM   6895 N  N   B MET   A 1 897 ? 43.063 57.887  19.240  0.50 14.28  ? 922  MET   A N   1 
ATOM   6896 C  CA  A MET   A 1 897 ? 42.338 59.005  19.844  0.50 14.51  ? 922  MET   A CA  1 
ATOM   6897 C  CA  B MET   A 1 897 ? 42.369 59.011  19.887  0.50 14.92  ? 922  MET   A CA  1 
ATOM   6898 C  C   A MET   A 1 897 ? 43.337 60.093  20.268  0.50 15.89  ? 922  MET   A C   1 
ATOM   6899 C  C   B MET   A 1 897 ? 43.353 60.096  20.256  0.50 16.03  ? 922  MET   A C   1 
ATOM   6900 O  O   A MET   A 1 897 ? 43.060 61.266  20.058  0.50 16.29  ? 922  MET   A O   1 
ATOM   6901 O  O   B MET   A 1 897 ? 43.070 61.266  20.040  0.50 16.37  ? 922  MET   A O   1 
ATOM   6902 C  CB  A MET   A 1 897 ? 41.451 58.530  21.008  0.50 15.50  ? 922  MET   A CB  1 
ATOM   6903 C  CB  B MET   A 1 897 ? 41.626 58.556  21.158  0.50 16.26  ? 922  MET   A CB  1 
ATOM   6904 C  CG  A MET   A 1 897 ? 40.522 59.587  21.518  0.50 15.25  ? 922  MET   A CG  1 
ATOM   6905 C  CG  B MET   A 1 897 ? 40.435 57.702  20.854  0.50 17.80  ? 922  MET   A CG  1 
ATOM   6906 S  SD  A MET   A 1 897 ? 39.283 60.145  20.324  0.50 13.98  ? 922  MET   A SD  1 
ATOM   6907 S  SD  B MET   A 1 897 ? 39.053 58.586  20.071  0.50 22.81  ? 922  MET   A SD  1 
ATOM   6908 C  CE  A MET   A 1 897 ? 37.914 59.031  20.627  0.50 16.13  ? 922  MET   A CE  1 
ATOM   6909 C  CE  B MET   A 1 897 ? 38.028 58.845  21.488  0.50 25.60  ? 922  MET   A CE  1 
ATOM   6910 N  N   . ASP   A 1 898 ? 44.533 59.720  20.770  1.00 15.34  ? 923  ASP   A N   1 
ATOM   6911 C  CA  . ASP   A 1 898 ? 45.532 60.765  21.138  1.00 15.94  ? 923  ASP   A CA  1 
ATOM   6912 C  C   . ASP   A 1 898 ? 45.940 61.551  19.905  1.00 18.00  ? 923  ASP   A C   1 
ATOM   6913 O  O   . ASP   A 1 898 ? 46.090 62.779  19.976  1.00 19.40  ? 923  ASP   A O   1 
ATOM   6914 C  CB  . ASP   A 1 898 ? 46.758 60.133  21.777  1.00 17.46  ? 923  ASP   A CB  1 
ATOM   6915 C  CG  . ASP   A 1 898 ? 46.527 59.713  23.218  1.00 20.52  ? 923  ASP   A CG  1 
ATOM   6916 O  OD1 . ASP   A 1 898 ? 45.497 60.121  23.798  1.00 22.76  ? 923  ASP   A OD1 1 
ATOM   6917 O  OD2 . ASP   A 1 898 ? 47.369 58.962  23.761  1.00 21.23  ? 923  ASP   A OD2 1 
ATOM   6918 N  N   . LYS   A 1 899 ? 46.102 60.864  18.768  1.00 15.81  ? 924  LYS   A N   1 
ATOM   6919 C  CA  A LYS   A 1 899 ? 46.528 61.561  17.561  0.50 16.76  ? 924  LYS   A CA  1 
ATOM   6920 C  CA  B LYS   A 1 899 ? 46.528 61.540  17.546  0.50 16.98  ? 924  LYS   A CA  1 
ATOM   6921 C  C   . LYS   A 1 899 ? 45.428 62.374  16.925  1.00 18.66  ? 924  LYS   A C   1 
ATOM   6922 O  O   . LYS   A 1 899 ? 45.704 63.449  16.400  1.00 20.56  ? 924  LYS   A O   1 
ATOM   6923 C  CB  A LYS   A 1 899 ? 47.091 60.575  16.539  0.50 17.89  ? 924  LYS   A CB  1 
ATOM   6924 C  CB  B LYS   A 1 899 ? 46.984 60.499  16.510  0.50 18.73  ? 924  LYS   A CB  1 
ATOM   6925 C  CG  A LYS   A 1 899 ? 47.594 61.281  15.296  0.50 19.08  ? 924  LYS   A CG  1 
ATOM   6926 C  CG  B LYS   A 1 899 ? 48.328 59.852  16.795  0.50 21.57  ? 924  LYS   A CG  1 
ATOM   6927 C  CD  A LYS   A 1 899 ? 48.306 60.356  14.364  0.50 20.03  ? 924  LYS   A CD  1 
ATOM   6928 C  CD  B LYS   A 1 899 ? 48.593 58.725  15.791  0.50 25.89  ? 924  LYS   A CD  1 
ATOM   6929 C  CE  A LYS   A 1 899 ? 48.766 61.131  13.147  0.50 22.41  ? 924  LYS   A CE  1 
ATOM   6930 C  CE  B LYS   A 1 899 ? 49.783 57.878  16.149  0.50 30.09  ? 924  LYS   A CE  1 
ATOM   6931 N  NZ  A LYS   A 1 899 ? 49.457 60.252  12.169  0.50 25.98  ? 924  LYS   A NZ  1 
ATOM   6932 N  NZ  B LYS   A 1 899 ? 49.742 56.577  15.426  0.50 33.46  ? 924  LYS   A NZ  1 
ATOM   6933 N  N   . ASN   A 1 900 ? 44.194 61.843  16.908  1.00 16.15  ? 925  ASN   A N   1 
ATOM   6934 C  CA  . ASN   A 1 900 ? 43.137 62.448  16.136  1.00 15.42  ? 925  ASN   A CA  1 
ATOM   6935 C  C   . ASN   A 1 900 ? 42.007 63.152  16.831  1.00 16.43  ? 925  ASN   A C   1 
ATOM   6936 O  O   . ASN   A 1 900 ? 41.291 63.852  16.136  1.00 16.21  ? 925  ASN   A O   1 
ATOM   6937 C  CB  . ASN   A 1 900 ? 42.523 61.322  15.251  1.00 15.58  ? 925  ASN   A CB  1 
ATOM   6938 C  CG  . ASN   A 1 900 ? 43.577 60.760  14.330  1.00 17.10  ? 925  ASN   A CG  1 
ATOM   6939 O  OD1 . ASN   A 1 900 ? 44.188 61.518  13.557  1.00 19.06  ? 925  ASN   A OD1 1 
ATOM   6940 N  ND2 . ASN   A 1 900 ? 43.809 59.457  14.379  1.00 17.10  ? 925  ASN   A ND2 1 
ATOM   6941 N  N   . PHE   A 1 901 ? 41.849 63.028  18.151  1.00 16.57  ? 926  PHE   A N   1 
ATOM   6942 C  CA  . PHE   A 1 901 ? 40.722 63.690  18.808  1.00 17.43  ? 926  PHE   A CA  1 
ATOM   6943 C  C   . PHE   A 1 901 ? 40.666 65.209  18.526  1.00 17.86  ? 926  PHE   A C   1 
ATOM   6944 O  O   . PHE   A 1 901 ? 39.630 65.722  18.076  1.00 18.52  ? 926  PHE   A O   1 
ATOM   6945 C  CB  . PHE   A 1 901 ? 40.780 63.441  20.333  1.00 17.30  ? 926  PHE   A CB  1 
ATOM   6946 C  CG  . PHE   A 1 901 ? 39.663 64.151  21.042  1.00 19.50  ? 926  PHE   A CG  1 
ATOM   6947 C  CD1 . PHE   A 1 901 ? 38.352 63.745  20.865  1.00 21.43  ? 926  PHE   A CD1 1 
ATOM   6948 C  CD2 . PHE   A 1 901 ? 39.920 65.242  21.846  1.00 22.37  ? 926  PHE   A CD2 1 
ATOM   6949 C  CE1 . PHE   A 1 901 ? 37.308 64.394  21.531  1.00 23.74  ? 926  PHE   A CE1 1 
ATOM   6950 C  CE2 . PHE   A 1 901 ? 38.871 65.900  22.492  1.00 23.73  ? 926  PHE   A CE2 1 
ATOM   6951 C  CZ  . PHE   A 1 901 ? 37.587 65.467  22.321  1.00 23.72  ? 926  PHE   A CZ  1 
ATOM   6952 N  N   A ASP   A 1 902 ? 41.764 65.931  18.789  0.50 17.70  ? 927  ASP   A N   1 
ATOM   6953 N  N   B ASP   A 1 902 ? 41.765 65.910  18.775  0.50 18.27  ? 927  ASP   A N   1 
ATOM   6954 C  CA  A ASP   A 1 902 ? 41.745 67.382  18.565  0.50 19.23  ? 927  ASP   A CA  1 
ATOM   6955 C  CA  B ASP   A 1 902 ? 41.797 67.355  18.565  0.50 20.36  ? 927  ASP   A CA  1 
ATOM   6956 C  C   A ASP   A 1 902 ? 41.566 67.718  17.102  0.50 19.28  ? 927  ASP   A C   1 
ATOM   6957 C  C   B ASP   A 1 902 ? 41.618 67.727  17.108  0.50 19.79  ? 927  ASP   A C   1 
ATOM   6958 O  O   A ASP   A 1 902 ? 40.868 68.674  16.772  0.50 19.57  ? 927  ASP   A O   1 
ATOM   6959 O  O   B ASP   A 1 902 ? 40.975 68.723  16.795  0.50 19.95  ? 927  ASP   A O   1 
ATOM   6960 C  CB  A ASP   A 1 902 ? 42.980 68.076  19.132  0.50 19.96  ? 927  ASP   A CB  1 
ATOM   6961 C  CB  B ASP   A 1 902 ? 43.082 67.941  19.143  0.50 23.04  ? 927  ASP   A CB  1 
ATOM   6962 C  CG  A ASP   A 1 902 ? 42.878 69.590  19.012  0.50 24.05  ? 927  ASP   A CG  1 
ATOM   6963 C  CG  B ASP   A 1 902 ? 43.034 67.989  20.653  0.50 31.51  ? 927  ASP   A CG  1 
ATOM   6964 O  OD1 A ASP   A 1 902 ? 41.924 70.164  19.569  0.50 25.03  ? 927  ASP   A OD1 1 
ATOM   6965 O  OD1 B ASP   A 1 902 ? 42.228 68.768  21.193  0.50 33.93  ? 927  ASP   A OD1 1 
ATOM   6966 O  OD2 A ASP   A 1 902 ? 43.700 70.175  18.308  0.50 27.40  ? 927  ASP   A OD2 1 
ATOM   6967 O  OD2 B ASP   A 1 902 ? 43.791 67.226  21.301  0.50 35.28  ? 927  ASP   A OD2 1 
ATOM   6968 N  N   . LYS   A 1 903 ? 42.157 66.908  16.195  1.00 18.11  ? 928  LYS   A N   1 
ATOM   6969 C  CA  . LYS   A 1 903 ? 41.982 67.139  14.755  1.00 16.91  ? 928  LYS   A CA  1 
ATOM   6970 C  C   . LYS   A 1 903 ? 40.503 67.022  14.393  1.00 16.17  ? 928  LYS   A C   1 
ATOM   6971 O  O   . LYS   A 1 903 ? 39.996 67.803  13.596  1.00 17.17  ? 928  LYS   A O   1 
ATOM   6972 C  CB  . LYS   A 1 903 ? 42.784 66.091  13.970  1.00 17.75  ? 928  LYS   A CB  1 
ATOM   6973 C  CG  . LYS   A 1 903 ? 44.281 66.311  14.128  1.00 21.35  ? 928  LYS   A CG  1 
ATOM   6974 C  CD  . LYS   A 1 903 ? 45.024 65.285  13.262  1.00 20.76  ? 928  LYS   A CD  1 
ATOM   6975 C  CE  . LYS   A 1 903 ? 46.501 65.216  13.569  1.00 26.58  ? 928  LYS   A CE  1 
ATOM   6976 N  NZ  . LYS   A 1 903 ? 47.174 66.429  13.054  1.00 29.63  ? 928  LYS   A NZ  1 
ATOM   6977 N  N   . ILE   A 1 904 ? 39.808 66.033  14.984  1.00 16.07  ? 929  ILE   A N   1 
ATOM   6978 C  CA  . ILE   A 1 904 ? 38.382 65.864  14.715  1.00 16.23  ? 929  ILE   A CA  1 
ATOM   6979 C  C   . ILE   A 1 904 ? 37.579 67.014  15.304  1.00 16.92  ? 929  ILE   A C   1 
ATOM   6980 O  O   . ILE   A 1 904 ? 36.685 67.510  14.664  1.00 18.28  ? 929  ILE   A O   1 
ATOM   6981 C  CB  . ILE   A 1 904 ? 37.931 64.506  15.260  1.00 15.80  ? 929  ILE   A CB  1 
ATOM   6982 C  CG1 . ILE   A 1 904 ? 38.546 63.391  14.377  1.00 15.79  ? 929  ILE   A CG1 1 
ATOM   6983 C  CG2 . ILE   A 1 904 ? 36.404 64.397  15.249  1.00 16.39  ? 929  ILE   A CG2 1 
ATOM   6984 C  CD1 . ILE   A 1 904 ? 38.265 61.999  14.984  1.00 17.93  ? 929  ILE   A CD1 1 
ATOM   6985 N  N   A ARG   A 1 905 ? 37.930 67.463  16.512  0.50 16.86  ? 930  ARG   A N   1 
ATOM   6986 N  N   B ARG   A 1 905 ? 37.952 67.465  16.509  0.50 16.97  ? 930  ARG   A N   1 
ATOM   6987 C  CA  A ARG   A 1 905 ? 37.231 68.595  17.137  0.50 17.69  ? 930  ARG   A CA  1 
ATOM   6988 C  CA  B ARG   A 1 905 ? 37.298 68.600  17.169  0.50 17.99  ? 930  ARG   A CA  1 
ATOM   6989 C  C   A ARG   A 1 905 ? 37.348 69.851  16.235  0.50 19.01  ? 930  ARG   A C   1 
ATOM   6990 C  C   B ARG   A 1 905 ? 37.366 69.846  16.255  0.50 19.23  ? 930  ARG   A C   1 
ATOM   6991 O  O   A ARG   A 1 905 ? 36.329 70.482  15.923  0.50 18.86  ? 930  ARG   A O   1 
ATOM   6992 O  O   B ARG   A 1 905 ? 36.337 70.476  15.979  0.50 19.24  ? 930  ARG   A O   1 
ATOM   6993 C  CB  A ARG   A 1 905 ? 37.844 68.862  18.521  0.50 19.00  ? 930  ARG   A CB  1 
ATOM   6994 C  CB  B ARG   A 1 905 ? 38.028 68.887  18.504  0.50 19.29  ? 930  ARG   A CB  1 
ATOM   6995 C  CG  A ARG   A 1 905 ? 37.216 70.049  19.271  0.50 20.61  ? 930  ARG   A CG  1 
ATOM   6996 C  CG  B ARG   A 1 905 ? 37.540 70.160  19.211  0.50 21.81  ? 930  ARG   A CG  1 
ATOM   6997 C  CD  A ARG   A 1 905 ? 37.641 70.071  20.726  0.50 22.33  ? 930  ARG   A CD  1 
ATOM   6998 C  CD  B ARG   A 1 905 ? 38.388 70.532  20.416  0.50 23.89  ? 930  ARG   A CD  1 
ATOM   6999 N  NE  A ARG   A 1 905 ? 39.093 70.134  20.871  0.50 24.58  ? 930  ARG   A NE  1 
ATOM   7000 N  NE  B ARG   A 1 905 ? 39.792 70.839  20.114  0.50 26.79  ? 930  ARG   A NE  1 
ATOM   7001 C  CZ  A ARG   A 1 905 ? 39.755 69.755  21.959  0.50 26.95  ? 930  ARG   A CZ  1 
ATOM   7002 C  CZ  B ARG   A 1 905 ? 40.215 71.988  19.584  0.50 29.11  ? 930  ARG   A CZ  1 
ATOM   7003 N  NH1 A ARG   A 1 905 ? 41.073 69.855  22.005  0.50 29.07  ? 930  ARG   A NH1 1 
ATOM   7004 N  NH1 B ARG   A 1 905 ? 39.344 72.922  19.225  0.50 28.67  ? 930  ARG   A NH1 1 
ATOM   7005 N  NH2 A ARG   A 1 905 ? 39.099 69.319  23.027  0.50 26.52  ? 930  ARG   A NH2 1 
ATOM   7006 N  NH2 B ARG   A 1 905 ? 41.509 72.202  19.393  0.50 30.31  ? 930  ARG   A NH2 1 
ATOM   7007 N  N   . VAL   A 1 906 ? 38.560 70.133  15.740  1.00 19.87  ? 931  VAL   A N   1 
ATOM   7008 C  CA  . VAL   A 1 906 ? 38.768 71.301  14.889  1.00 20.75  ? 931  VAL   A CA  1 
ATOM   7009 C  C   . VAL   A 1 906 ? 38.023 71.117  13.572  1.00 21.03  ? 931  VAL   A C   1 
ATOM   7010 O  O   . VAL   A 1 906 ? 37.318 72.027  13.111  1.00 22.71  ? 931  VAL   A O   1 
ATOM   7011 C  CB  . VAL   A 1 906 ? 40.285 71.509  14.629  1.00 22.45  ? 931  VAL   A CB  1 
ATOM   7012 C  CG1 . VAL   A 1 906 ? 40.524 72.544  13.525  1.00 23.92  ? 931  VAL   A CG1 1 
ATOM   7013 C  CG2 . VAL   A 1 906 ? 41.037 71.911  15.897  1.00 22.15  ? 931  VAL   A CG2 1 
ATOM   7014 N  N   . TRP   A 1 907 ? 38.110 69.894  12.969  1.00 18.71  ? 932  TRP   A N   1 
ATOM   7015 C  CA  . TRP   A 1 907 ? 37.416 69.639  11.713  1.00 19.07  ? 932  TRP   A CA  1 
ATOM   7016 C  C   . TRP   A 1 907 ? 35.905 69.850  11.854  1.00 20.99  ? 932  TRP   A C   1 
ATOM   7017 O  O   . TRP   A 1 907 ? 35.293 70.441  10.964  1.00 22.76  ? 932  TRP   A O   1 
ATOM   7018 C  CB  . TRP   A 1 907 ? 37.705 68.198  11.232  1.00 19.35  ? 932  TRP   A CB  1 
ATOM   7019 C  CG  . TRP   A 1 907 ? 37.182 67.905  9.860   1.00 20.26  ? 932  TRP   A CG  1 
ATOM   7020 C  CD1 . TRP   A 1 907 ? 37.827 68.128  8.681   1.00 21.09  ? 932  TRP   A CD1 1 
ATOM   7021 C  CD2 . TRP   A 1 907 ? 35.916 67.322  9.525   1.00 19.33  ? 932  TRP   A CD2 1 
ATOM   7022 N  NE1 . TRP   A 1 907 ? 37.053 67.685  7.626   1.00 20.34  ? 932  TRP   A NE1 1 
ATOM   7023 C  CE2 . TRP   A 1 907 ? 35.887 67.166  8.119   1.00 20.50  ? 932  TRP   A CE2 1 
ATOM   7024 C  CE3 . TRP   A 1 907 ? 34.847 66.815  10.285  1.00 20.12  ? 932  TRP   A CE3 1 
ATOM   7025 C  CZ2 . TRP   A 1 907 ? 34.788 66.641  7.450   1.00 20.86  ? 932  TRP   A CZ2 1 
ATOM   7026 C  CZ3 . TRP   A 1 907 ? 33.769 66.258  9.617   1.00 20.85  ? 932  TRP   A CZ3 1 
ATOM   7027 C  CH2 . TRP   A 1 907 ? 33.752 66.177  8.211   1.00 20.71  ? 932  TRP   A CH2 1 
ATOM   7028 N  N   . LEU   A 1 908 ? 35.303 69.357  12.942  1.00 19.80  ? 933  LEU   A N   1 
ATOM   7029 C  CA  . LEU   A 1 908 ? 33.856 69.516  13.131  1.00 21.44  ? 933  LEU   A CA  1 
ATOM   7030 C  C   . LEU   A 1 908 ? 33.465 70.970  13.262  1.00 25.90  ? 933  LEU   A C   1 
ATOM   7031 O  O   . LEU   A 1 908 ? 32.371 71.332  12.834  1.00 26.63  ? 933  LEU   A O   1 
ATOM   7032 C  CB  . LEU   A 1 908 ? 33.371 68.756  14.367  1.00 20.57  ? 933  LEU   A CB  1 
ATOM   7033 C  CG  . LEU   A 1 908 ? 33.367 67.212  14.215  1.00 21.41  ? 933  LEU   A CG  1 
ATOM   7034 C  CD1 . LEU   A 1 908 ? 33.282 66.549  15.585  1.00 21.13  ? 933  LEU   A CD1 1 
ATOM   7035 C  CD2 . LEU   A 1 908 ? 32.242 66.751  13.295  1.00 22.28  ? 933  LEU   A CD2 1 
ATOM   7036 N  N   . GLN   A 1 909 ? 34.324 71.781  13.880  1.00 28.42  ? 934  GLN   A N   1 
ATOM   7037 C  CA  . GLN   A 1 909 ? 34.026 73.199  14.037  1.00 32.79  ? 934  GLN   A CA  1 
ATOM   7038 C  C   . GLN   A 1 909 ? 34.134 73.936  12.732  1.00 37.13  ? 934  GLN   A C   1 
ATOM   7039 O  O   . GLN   A 1 909 ? 33.342 74.861  12.496  1.00 39.38  ? 934  GLN   A O   1 
ATOM   7040 C  CB  . GLN   A 1 909 ? 34.954 73.830  15.072  1.00 35.91  ? 934  GLN   A CB  1 
ATOM   7041 C  CG  . GLN   A 1 909 ? 34.429 73.639  16.473  1.00 43.18  ? 934  GLN   A CG  1 
ATOM   7042 C  CD  . GLN   A 1 909 ? 33.138 74.400  16.700  1.00 52.24  ? 934  GLN   A CD  1 
ATOM   7043 O  OE1 . GLN   A 1 909 ? 32.953 75.539  16.231  1.00 55.52  ? 934  GLN   A OE1 1 
ATOM   7044 N  NE2 . GLN   A 1 909 ? 32.220 73.789  17.424  1.00 52.85  ? 934  GLN   A NE2 1 
ATOM   7045 N  N   . SER   A 1 910 ? 35.121 73.571  11.892  1.00 38.76  ? 935  SER   A N   1 
ATOM   7046 C  CA  . SER   A 1 910 ? 35.376 74.225  10.606  1.00 41.26  ? 935  SER   A CA  1 
ATOM   7047 C  C   . SER   A 1 910 ? 34.315 73.863  9.573   1.00 42.96  ? 935  SER   A C   1 
ATOM   7048 O  O   . SER   A 1 910 ? 33.236 74.443  9.558   1.00 43.81  ? 935  SER   A O   1 
ATOM   7049 C  CB  . SER   A 1 910 ? 36.749 73.823  10.073  1.00 42.88  ? 935  SER   A CB  1 
ATOM   7050 O  OG  . SER   A 1 910 ? 37.758 74.001  11.054  1.00 45.75  ? 935  SER   A OG  1 
HETATM 7051 ZN ZN  . ZN    B 2 .   ? 31.296 26.108  8.466   1.00 13.32  2 1001 ZN    A ZN  1 
HETATM 7052 C  C1  . MLT   C 3 .   ? 28.170 29.534  12.293  1.00 24.77  ? 1002 MLT   A C1  1 
HETATM 7053 O  O1  . MLT   C 3 .   ? 27.209 30.190  11.837  1.00 27.09  ? 1002 MLT   A O1  1 
HETATM 7054 O  O2  . MLT   C 3 .   ? 28.497 29.452  13.492  1.00 25.28  ? 1002 MLT   A O2  1 
HETATM 7055 C  C2  . MLT   C 3 .   ? 29.040 28.757  11.300  1.00 21.62  ? 1002 MLT   A C2  1 
HETATM 7056 O  O3  . MLT   C 3 .   ? 28.767 29.208  9.977   1.00 21.69  ? 1002 MLT   A O3  1 
HETATM 7057 C  C3  . MLT   C 3 .   ? 28.762 27.248  11.448  1.00 17.71  ? 1002 MLT   A C3  1 
HETATM 7058 C  C4  . MLT   C 3 .   ? 29.564 26.450  10.437  1.00 15.41  ? 1002 MLT   A C4  1 
HETATM 7059 O  O4  . MLT   C 3 .   ? 28.971 25.638  9.717   1.00 14.61  ? 1002 MLT   A O4  1 
HETATM 7060 O  O5  . MLT   C 3 .   ? 30.797 26.668  10.343  1.00 14.21  ? 1002 MLT   A O5  1 
HETATM 7061 C  C1  . MLT   D 3 .   ? 23.748 -0.192  26.639  1.00 36.18  ? 1003 MLT   A C1  1 
HETATM 7062 O  O1  . MLT   D 3 .   ? 23.794 -1.428  26.752  1.00 36.55  ? 1003 MLT   A O1  1 
HETATM 7063 O  O2  . MLT   D 3 .   ? 24.720 0.549   26.513  1.00 36.45  ? 1003 MLT   A O2  1 
HETATM 7064 C  C2  . MLT   D 3 .   ? 22.388 0.475   26.836  1.00 35.00  ? 1003 MLT   A C2  1 
HETATM 7065 O  O3  . MLT   D 3 .   ? 22.436 1.831   26.411  1.00 35.70  ? 1003 MLT   A O3  1 
HETATM 7066 C  C3  . MLT   D 3 .   ? 22.054 0.384   28.330  1.00 32.95  ? 1003 MLT   A C3  1 
HETATM 7067 C  C4  . MLT   D 3 .   ? 20.643 0.863   28.590  1.00 32.31  ? 1003 MLT   A C4  1 
HETATM 7068 O  O4  . MLT   D 3 .   ? 20.481 1.664   29.537  1.00 30.25  ? 1003 MLT   A O4  1 
HETATM 7069 O  O5  . MLT   D 3 .   ? 19.711 0.427   27.846  1.00 32.06  ? 1003 MLT   A O5  1 
HETATM 7070 C  C1  . EDO   E 4 .   ? 15.963 44.564  7.837   1.00 20.76  ? 1004 EDO   A C1  1 
HETATM 7071 O  O1  . EDO   E 4 .   ? 16.634 43.313  8.010   1.00 18.63  ? 1004 EDO   A O1  1 
HETATM 7072 C  C2  . EDO   E 4 .   ? 14.568 44.445  8.416   1.00 22.99  ? 1004 EDO   A C2  1 
HETATM 7073 O  O2  . EDO   E 4 .   ? 13.795 43.708  7.464   1.00 21.44  ? 1004 EDO   A O2  1 
HETATM 7074 C  C1  . EDO   F 4 .   ? 36.220 18.099  24.885  1.00 16.57  ? 1005 EDO   A C1  1 
HETATM 7075 O  O1  . EDO   F 4 .   ? 37.506 18.372  24.346  1.00 16.39  ? 1005 EDO   A O1  1 
HETATM 7076 C  C2  . EDO   F 4 .   ? 35.318 19.310  24.619  1.00 17.45  ? 1005 EDO   A C2  1 
HETATM 7077 O  O2  . EDO   F 4 .   ? 35.923 20.482  25.161  1.00 17.95  ? 1005 EDO   A O2  1 
HETATM 7078 C  C1  . EDO   G 4 .   ? 0.989  21.583  18.122  1.00 31.09  ? 1006 EDO   A C1  1 
HETATM 7079 O  O1  . EDO   G 4 .   ? 1.254  21.470  19.521  1.00 30.80  ? 1006 EDO   A O1  1 
HETATM 7080 C  C2  . EDO   G 4 .   ? 1.799  22.721  17.526  1.00 31.18  ? 1006 EDO   A C2  1 
HETATM 7081 O  O2  . EDO   G 4 .   ? 1.278  23.946  17.965  1.00 32.05  ? 1006 EDO   A O2  1 
HETATM 7082 C  C1  . EDO   H 4 .   ? 31.255 24.715  15.475  1.00 21.01  ? 1007 EDO   A C1  1 
HETATM 7083 O  O1  . EDO   H 4 .   ? 30.959 25.779  16.378  1.00 21.65  ? 1007 EDO   A O1  1 
HETATM 7084 C  C2  . EDO   H 4 .   ? 30.253 24.852  14.329  1.00 20.03  ? 1007 EDO   A C2  1 
HETATM 7085 O  O2  . EDO   H 4 .   ? 28.887 24.690  14.780  1.00 17.82  ? 1007 EDO   A O2  1 
HETATM 7086 C  C1  . EDO   I 4 .   ? 33.477 26.072  19.140  1.00 23.25  ? 1008 EDO   A C1  1 
HETATM 7087 O  O1  . EDO   I 4 .   ? 33.437 26.517  20.484  1.00 22.42  ? 1008 EDO   A O1  1 
HETATM 7088 C  C2  . EDO   I 4 .   ? 34.197 27.116  18.287  1.00 23.16  ? 1008 EDO   A C2  1 
HETATM 7089 O  O2  . EDO   I 4 .   ? 33.479 28.378  18.301  1.00 22.77  ? 1008 EDO   A O2  1 
HETATM 7090 C  C1  . EDO   J 4 .   ? 30.354 46.169  4.079   1.00 33.72  ? 1009 EDO   A C1  1 
HETATM 7091 O  O1  . EDO   J 4 .   ? 31.543 46.350  4.844   1.00 32.90  ? 1009 EDO   A O1  1 
HETATM 7092 C  C2  . EDO   J 4 .   ? 29.251 47.018  4.630   1.00 34.35  ? 1009 EDO   A C2  1 
HETATM 7093 O  O2  . EDO   J 4 .   ? 28.800 46.495  5.885   1.00 35.27  ? 1009 EDO   A O2  1 
HETATM 7094 C  C1  . EDO   K 4 .   ? 39.983 53.797  15.780  1.00 22.39  ? 1010 EDO   A C1  1 
HETATM 7095 O  O1  . EDO   K 4 .   ? 40.188 53.053  14.589  1.00 23.08  ? 1010 EDO   A O1  1 
HETATM 7096 C  C2  . EDO   K 4 .   ? 38.707 54.583  15.594  1.00 22.20  ? 1010 EDO   A C2  1 
HETATM 7097 O  O2  . EDO   K 4 .   ? 37.629 53.656  15.544  1.00 22.38  ? 1010 EDO   A O2  1 
HETATM 7098 C  C1  . EDO   L 4 .   ? 26.839 48.107  8.625   1.00 33.25  ? 1011 EDO   A C1  1 
HETATM 7099 O  O1  . EDO   L 4 .   ? 27.586 47.332  9.555   1.00 32.94  ? 1011 EDO   A O1  1 
HETATM 7100 C  C2  . EDO   L 4 .   ? 25.427 48.405  9.115   1.00 34.37  ? 1011 EDO   A C2  1 
HETATM 7101 O  O2  . EDO   L 4 .   ? 24.813 47.204  9.540   1.00 35.55  ? 1011 EDO   A O2  1 
HETATM 7102 C  C1  . EDO   M 4 .   ? 42.900 62.569  23.333  1.00 27.25  ? 1012 EDO   A C1  1 
HETATM 7103 O  O1  . EDO   M 4 .   ? 42.918 61.248  23.862  1.00 24.32  ? 1012 EDO   A O1  1 
HETATM 7104 C  C2  . EDO   M 4 .   ? 43.315 63.563  24.396  1.00 30.26  ? 1012 EDO   A C2  1 
HETATM 7105 O  O2  . EDO   M 4 .   ? 42.355 63.452  25.442  1.00 32.22  ? 1012 EDO   A O2  1 
HETATM 7106 C  C1  . EDO   N 4 .   ? 25.778 37.639  3.586   1.00 39.93  ? 1013 EDO   A C1  1 
HETATM 7107 O  O1  . EDO   N 4 .   ? 25.964 37.050  4.864   1.00 39.40  ? 1013 EDO   A O1  1 
HETATM 7108 C  C2  . EDO   N 4 .   ? 25.457 39.086  3.736   1.00 39.65  ? 1013 EDO   A C2  1 
HETATM 7109 O  O2  . EDO   N 4 .   ? 26.477 39.746  4.472   1.00 39.71  ? 1013 EDO   A O2  1 
HETATM 7110 C  C1  . EDO   O 4 .   ? 22.963 47.546  14.291  1.00 32.74  ? 1014 EDO   A C1  1 
HETATM 7111 O  O1  . EDO   O 4 .   ? 22.113 48.608  13.976  1.00 33.37  ? 1014 EDO   A O1  1 
HETATM 7112 C  C2  . EDO   O 4 .   ? 24.118 48.140  14.929  1.00 31.17  ? 1014 EDO   A C2  1 
HETATM 7113 O  O2  . EDO   O 4 .   ? 23.892 48.069  16.295  1.00 26.99  ? 1014 EDO   A O2  1 
HETATM 7114 C  C1  . EDO   P 4 .   ? 19.879 50.041  -1.882  1.00 24.98  ? 1015 EDO   A C1  1 
HETATM 7115 O  O1  . EDO   P 4 .   ? 21.248 49.633  -1.977  1.00 21.15  ? 1015 EDO   A O1  1 
HETATM 7116 C  C2  . EDO   P 4 .   ? 19.598 50.997  -2.967  1.00 27.91  ? 1015 EDO   A C2  1 
HETATM 7117 O  O2  . EDO   P 4 .   ? 19.793 50.312  -4.187  1.00 30.10  ? 1015 EDO   A O2  1 
HETATM 7118 C  C1  . EDO   Q 4 .   ? 19.357 56.149  22.911  1.00 30.62  ? 1016 EDO   A C1  1 
HETATM 7119 O  O1  . EDO   Q 4 .   ? 20.746 56.067  22.573  1.00 31.52  ? 1016 EDO   A O1  1 
HETATM 7120 C  C2  . EDO   Q 4 .   ? 18.899 54.764  23.319  1.00 28.14  ? 1016 EDO   A C2  1 
HETATM 7121 O  O2  . EDO   Q 4 .   ? 18.907 53.919  22.168  1.00 24.17  ? 1016 EDO   A O2  1 
HETATM 7122 C  C1  . EDO   R 4 .   ? 31.765 28.403  14.846  1.00 29.33  ? 1017 EDO   A C1  1 
HETATM 7123 O  O1  . EDO   R 4 .   ? 31.799 28.374  16.287  1.00 26.24  ? 1017 EDO   A O1  1 
HETATM 7124 C  C2  . EDO   R 4 .   ? 31.670 29.833  14.362  1.00 31.22  ? 1017 EDO   A C2  1 
HETATM 7125 O  O2  . EDO   R 4 .   ? 30.602 30.517  15.036  1.00 32.22  ? 1017 EDO   A O2  1 
HETATM 7126 C  C1  . EDO   S 4 .   ? 20.276 25.127  27.489  1.00 32.00  ? 1018 EDO   A C1  1 
HETATM 7127 O  O1  . EDO   S 4 .   ? 21.552 24.995  28.070  1.00 31.57  ? 1018 EDO   A O1  1 
HETATM 7128 C  C2  . EDO   S 4 .   ? 19.232 24.273  28.199  1.00 32.78  ? 1018 EDO   A C2  1 
HETATM 7129 O  O2  . EDO   S 4 .   ? 19.193 24.567  29.603  1.00 33.22  ? 1018 EDO   A O2  1 
HETATM 7130 C  C1  . EDO   T 4 .   ? 46.792 29.413  16.664  1.00 35.54  ? 1019 EDO   A C1  1 
HETATM 7131 O  O1  . EDO   T 4 .   ? 47.744 30.228  17.332  1.00 35.83  ? 1019 EDO   A O1  1 
HETATM 7132 C  C2  . EDO   T 4 .   ? 45.611 30.189  16.165  1.00 36.01  ? 1019 EDO   A C2  1 
HETATM 7133 O  O2  . EDO   T 4 .   ? 44.487 29.627  16.804  1.00 37.86  ? 1019 EDO   A O2  1 
HETATM 7134 N  N1  . A1IMM U 5 .   ? 28.201 49.432  16.301  0.90 12.20  ? 1020 A1IMM A N1  1 
HETATM 7135 C  C4  . A1IMM U 5 .   ? 22.025 51.981  15.484  0.90 13.92  ? 1020 A1IMM A C4  1 
HETATM 7136 C  C5  . A1IMM U 5 .   ? 23.475 52.159  15.069  0.90 13.68  ? 1020 A1IMM A C5  1 
HETATM 7137 C  C6  . A1IMM U 5 .   ? 24.277 52.783  16.207  0.90 13.76  ? 1020 A1IMM A C6  1 
HETATM 7138 C  C7  . A1IMM U 5 .   ? 26.290 50.639  17.218  0.90 12.76  ? 1020 A1IMM A C7  1 
HETATM 7139 C  C8  . A1IMM U 5 .   ? 26.923 49.275  16.990  0.90 12.35  ? 1020 A1IMM A C8  1 
HETATM 7140 C  C10 . A1IMM U 5 .   ? 30.606 49.888  16.373  0.90 14.96  ? 1020 A1IMM A C10 1 
HETATM 7141 C  C13 . A1IMM U 5 .   ? 28.175 49.722  12.110  0.90 15.88  ? 1020 A1IMM A C13 1 
HETATM 7142 C  C15 . A1IMM U 5 .   ? 27.057 49.922  14.222  0.90 14.99  ? 1020 A1IMM A C15 1 
HETATM 7143 CL CL  . A1IMM U 5 .   ? 25.567 50.391  12.038  0.90 16.77  ? 1020 A1IMM A CL  1 
HETATM 7144 C  C14 . A1IMM U 5 .   ? 27.056 50.002  12.848  0.90 15.38  ? 1020 A1IMM A C14 1 
HETATM 7145 C  C12 . A1IMM U 5 .   ? 29.336 49.350  12.762  0.90 16.48  ? 1020 A1IMM A C12 1 
HETATM 7146 C  C16 . A1IMM U 5 .   ? 28.211 49.562  14.896  0.90 14.80  ? 1020 A1IMM A C16 1 
HETATM 7147 C  C11 . A1IMM U 5 .   ? 29.360 49.276  14.157  0.90 15.48  ? 1020 A1IMM A C11 1 
HETATM 7148 S  S   . A1IMM U 5 .   ? 30.835 48.798  14.962  0.90 16.58  ? 1020 A1IMM A S   1 
HETATM 7149 C  C9  . A1IMM U 5 .   ? 29.314 49.590  17.079  0.90 13.67  ? 1020 A1IMM A C9  1 
HETATM 7150 O  O3  . A1IMM U 5 .   ? 29.280 49.450  18.296  0.90 13.38  ? 1020 A1IMM A O3  1 
HETATM 7151 O  O2  . A1IMM U 5 .   ? 26.974 51.650  17.333  0.90 12.92  ? 1020 A1IMM A O2  1 
HETATM 7152 N  N   . A1IMM U 5 .   ? 24.950 50.659  17.221  0.90 12.40  ? 1020 A1IMM A N   1 
HETATM 7153 C  C1  . A1IMM U 5 .   ? 24.236 51.900  17.469  0.90 12.89  ? 1020 A1IMM A C1  1 
HETATM 7154 C  C   . A1IMM U 5 .   ? 24.875 52.662  18.636  0.90 14.10  ? 1020 A1IMM A C   1 
HETATM 7155 O  O1  . A1IMM U 5 .   ? 25.081 53.872  18.600  0.90 14.42  ? 1020 A1IMM A O1  1 
HETATM 7156 O  O   . A1IMM U 5 .   ? 25.119 51.896  19.663  0.90 13.60  ? 1020 A1IMM A O   1 
HETATM 7157 C  C3  . A1IMM U 5 .   ? 21.929 51.078  16.720  0.90 13.34  ? 1020 A1IMM A C3  1 
HETATM 7158 C  C2  . A1IMM U 5 .   ? 22.775 51.630  17.872  0.90 12.81  ? 1020 A1IMM A C2  1 
HETATM 7159 O  O   . HOH   V 6 .   ? 34.227 70.706  17.799  1.00 41.29  ? 1101 HOH   A O   1 
HETATM 7160 O  O   . HOH   V 6 .   ? 31.231 23.388  18.619  1.00 122.84 ? 1102 HOH   A O   1 
HETATM 7161 O  O   . HOH   V 6 .   ? 21.198 18.539  -9.255  1.00 32.41  ? 1103 HOH   A O   1 
HETATM 7162 O  O   . HOH   V 6 .   ? 26.668 67.406  24.743  1.00 33.66  ? 1104 HOH   A O   1 
HETATM 7163 O  O   . HOH   V 6 .   ? 54.066 28.614  -7.644  1.00 33.82  ? 1105 HOH   A O   1 
HETATM 7164 O  O   . HOH   V 6 .   ? 19.853 41.407  -0.877  1.00 43.58  ? 1106 HOH   A O   1 
HETATM 7165 O  O   . HOH   V 6 .   ? 6.514  25.672  21.947  1.00 29.43  ? 1107 HOH   A O   1 
HETATM 7166 O  O   . HOH   V 6 .   ? 40.524 52.479  10.345  1.00 40.02  ? 1108 HOH   A O   1 
HETATM 7167 O  O   . HOH   V 6 .   ? 47.737 38.654  25.728  1.00 31.57  ? 1109 HOH   A O   1 
HETATM 7168 O  O   . HOH   V 6 .   ? 48.237 18.108  8.302   1.00 38.13  ? 1110 HOH   A O   1 
HETATM 7169 O  O   . HOH   V 6 .   ? 11.553 18.248  22.052  1.00 28.99  ? 1111 HOH   A O   1 
HETATM 7170 O  O   . HOH   V 6 .   ? 48.722 61.051  -9.179  1.00 35.25  ? 1112 HOH   A O   1 
HETATM 7171 O  O   . HOH   V 6 .   ? 47.010 11.801  10.517  1.00 54.64  ? 1113 HOH   A O   1 
HETATM 7172 O  O   . HOH   V 6 .   ? 44.879 28.666  19.033  1.00 25.47  ? 1114 HOH   A O   1 
HETATM 7173 O  O   . HOH   V 6 .   ? 11.295 26.248  -5.354  1.00 50.65  ? 1115 HOH   A O   1 
HETATM 7174 O  O   . HOH   V 6 .   ? 14.355 27.781  -3.607  1.00 35.71  ? 1116 HOH   A O   1 
HETATM 7175 O  O   . HOH   V 6 .   ? 30.054 69.541  29.046  1.00 57.40  ? 1117 HOH   A O   1 
HETATM 7176 O  O   . HOH   V 6 .   ? 12.708 29.036  -0.127  1.00 39.33  ? 1118 HOH   A O   1 
HETATM 7177 O  O   . HOH   V 6 .   ? 1.220  48.961  11.386  1.00 47.09  ? 1119 HOH   A O   1 
HETATM 7178 O  O   . HOH   V 6 .   ? 7.487  38.126  28.573  1.00 26.95  ? 1120 HOH   A O   1 
HETATM 7179 O  O   . HOH   V 6 .   ? 42.810 40.555  -6.616  1.00 24.40  ? 1121 HOH   A O   1 
HETATM 7180 O  O   . HOH   V 6 .   ? 48.267 42.915  7.933   1.00 20.58  ? 1122 HOH   A O   1 
HETATM 7181 O  O   . HOH   V 6 .   ? 28.214 54.838  32.755  1.00 54.48  ? 1123 HOH   A O   1 
HETATM 7182 O  O   . HOH   V 6 .   ? 38.322 40.369  -10.922 1.00 42.59  ? 1124 HOH   A O   1 
HETATM 7183 O  O   . HOH   V 6 .   ? 39.449 -15.524 18.542  1.00 45.81  ? 1125 HOH   A O   1 
HETATM 7184 O  O   . HOH   V 6 .   ? 36.436 40.682  12.441  1.00 28.57  ? 1126 HOH   A O   1 
HETATM 7185 O  O   . HOH   V 6 .   ? 19.777 38.255  17.606  1.00 33.11  ? 1127 HOH   A O   1 
HETATM 7186 O  O   . HOH   V 6 .   ? 16.895 23.341  -8.656  1.00 30.20  ? 1128 HOH   A O   1 
HETATM 7187 O  O   . HOH   V 6 .   ? 31.451 23.854  11.205  1.00 14.37  ? 1129 HOH   A O   1 
HETATM 7188 O  O   . HOH   V 6 .   ? 53.077 23.164  -11.517 1.00 33.72  ? 1130 HOH   A O   1 
HETATM 7189 O  O   . HOH   V 6 .   ? 38.352 20.205  26.702  1.00 25.10  ? 1131 HOH   A O   1 
HETATM 7190 O  O   . HOH   V 6 .   ? 34.358 52.839  -14.113 1.00 30.49  ? 1132 HOH   A O   1 
HETATM 7191 O  O   . HOH   V 6 .   ? 14.112 29.245  -1.319  1.00 34.07  ? 1133 HOH   A O   1 
HETATM 7192 O  O   . HOH   V 6 .   ? 32.198 38.250  9.160   1.00 25.60  ? 1134 HOH   A O   1 
HETATM 7193 O  O   . HOH   V 6 .   ? 35.975 40.421  -2.096  1.00 34.12  ? 1135 HOH   A O   1 
HETATM 7194 O  O   . HOH   V 6 .   ? 27.668 34.864  5.271   1.00 28.41  ? 1136 HOH   A O   1 
HETATM 7195 O  O   . HOH   V 6 .   ? 11.329 32.772  13.293  1.00 14.53  ? 1137 HOH   A O   1 
HETATM 7196 O  O   . HOH   V 6 .   ? 21.331 23.336  30.451  1.00 28.17  ? 1138 HOH   A O   1 
HETATM 7197 O  O   . HOH   V 6 .   ? 14.631 34.676  -1.111  1.00 30.54  ? 1139 HOH   A O   1 
HETATM 7198 O  O   . HOH   V 6 .   ? 22.241 41.182  40.310  1.00 39.55  ? 1140 HOH   A O   1 
HETATM 7199 O  O   . HOH   V 6 .   ? 28.972 40.763  3.892   1.00 42.71  ? 1141 HOH   A O   1 
HETATM 7200 O  O   . HOH   V 6 .   ? 20.206 32.209  -11.366 1.00 41.91  ? 1142 HOH   A O   1 
HETATM 7201 O  O   . HOH   V 6 .   ? 41.728 69.373  12.031  1.00 20.77  ? 1143 HOH   A O   1 
HETATM 7202 O  O   . HOH   V 6 .   ? 19.453 53.193  -6.167  1.00 40.20  ? 1144 HOH   A O   1 
HETATM 7203 O  O   . HOH   V 6 .   ? 41.924 46.529  13.544  1.00 47.78  ? 1145 HOH   A O   1 
HETATM 7204 O  O   . HOH   V 6 .   ? 5.609  28.595  1.841   1.00 27.76  ? 1146 HOH   A O   1 
HETATM 7205 O  O   . HOH   V 6 .   ? 16.664 27.826  28.704  1.00 29.33  ? 1147 HOH   A O   1 
HETATM 7206 O  O   . HOH   V 6 .   ? 29.270 12.701  31.330  1.00 22.01  ? 1148 HOH   A O   1 
HETATM 7207 O  O   . HOH   V 6 .   ? 44.653 65.592  17.361  1.00 28.18  ? 1149 HOH   A O   1 
HETATM 7208 O  O   . HOH   V 6 .   ? 53.895 30.099  8.696   1.00 28.70  ? 1150 HOH   A O   1 
HETATM 7209 O  O   . HOH   V 6 .   ? 42.652 52.605  13.573  1.00 22.16  ? 1151 HOH   A O   1 
HETATM 7210 O  O   . HOH   V 6 .   ? 34.135 22.330  9.791   1.00 13.24  ? 1152 HOH   A O   1 
HETATM 7211 O  O   . HOH   V 6 .   ? 50.021 26.580  2.439   1.00 35.86  ? 1153 HOH   A O   1 
HETATM 7212 O  O   . HOH   V 6 .   ? 55.181 47.272  6.729   1.00 39.37  ? 1154 HOH   A O   1 
HETATM 7213 O  O   . HOH   V 6 .   ? 38.273 50.304  9.187   1.00 39.47  ? 1155 HOH   A O   1 
HETATM 7214 O  O   . HOH   V 6 .   ? 44.467 69.630  15.902  1.00 38.82  ? 1156 HOH   A O   1 
HETATM 7215 O  O   . HOH   V 6 .   ? 0.353  40.558  8.371   1.00 36.91  ? 1157 HOH   A O   1 
HETATM 7216 O  O   . HOH   V 6 .   ? 39.775 50.352  12.022  1.00 65.31  ? 1158 HOH   A O   1 
HETATM 7217 O  O   . HOH   V 6 .   ? 29.755 71.372  27.765  1.00 27.04  ? 1159 HOH   A O   1 
HETATM 7218 O  O   . HOH   V 6 .   ? 41.486 51.688  -4.393  1.00 16.09  ? 1160 HOH   A O   1 
HETATM 7219 O  O   . HOH   V 6 .   ? 28.475 21.826  -13.369 1.00 29.11  ? 1161 HOH   A O   1 
HETATM 7220 O  O   . HOH   V 6 .   ? 16.421 54.185  21.487  1.00 24.34  ? 1162 HOH   A O   1 
HETATM 7221 O  O   . HOH   V 6 .   ? 51.692 51.043  11.998  1.00 42.52  ? 1163 HOH   A O   1 
HETATM 7222 O  O   . HOH   V 6 .   ? 26.485 28.753  8.835   1.00 27.58  ? 1164 HOH   A O   1 
HETATM 7223 O  O   . HOH   V 6 .   ? 49.442 19.425  -9.647  1.00 43.33  ? 1165 HOH   A O   1 
HETATM 7224 O  O   . HOH   V 6 .   ? 20.105 4.065   4.141   1.00 33.50  ? 1166 HOH   A O   1 
HETATM 7225 O  O   . HOH   V 6 .   ? 45.492 45.119  37.991  1.00 21.00  ? 1167 HOH   A O   1 
HETATM 7226 O  O   . HOH   V 6 .   ? 23.825 36.478  6.223   1.00 32.42  ? 1168 HOH   A O   1 
HETATM 7227 O  O   . HOH   V 6 .   ? 1.657  41.202  19.294  1.00 51.03  ? 1169 HOH   A O   1 
HETATM 7228 O  O   . HOH   V 6 .   ? 41.872 -0.422  10.385  1.00 48.73  ? 1170 HOH   A O   1 
HETATM 7229 O  O   . HOH   V 6 .   ? 36.701 -4.886  10.834  1.00 38.85  ? 1171 HOH   A O   1 
HETATM 7230 O  O   . HOH   V 6 .   ? 32.823 0.313   7.135   1.00 35.39  ? 1172 HOH   A O   1 
HETATM 7231 O  O   . HOH   V 6 .   ? 59.133 37.439  -5.647  1.00 28.13  ? 1173 HOH   A O   1 
HETATM 7232 O  O   . HOH   V 6 .   ? 50.305 35.696  16.431  1.00 40.41  ? 1174 HOH   A O   1 
HETATM 7233 O  O   . HOH   V 6 .   ? 3.388  49.152  1.547   1.00 35.93  ? 1175 HOH   A O   1 
HETATM 7234 O  O   . HOH   V 6 .   ? 57.265 28.049  -3.432  1.00 41.14  ? 1176 HOH   A O   1 
HETATM 7235 O  O   . HOH   V 6 .   ? 22.579 44.758  -3.328  1.00 44.44  ? 1177 HOH   A O   1 
HETATM 7236 O  O   . HOH   V 6 .   ? 37.686 7.607   14.748  1.00 15.62  ? 1178 HOH   A O   1 
HETATM 7237 O  O   . HOH   V 6 .   ? 8.168  14.896  6.917   1.00 36.53  ? 1179 HOH   A O   1 
HETATM 7238 O  O   . HOH   V 6 .   ? 47.263 61.004  -2.440  1.00 23.17  ? 1180 HOH   A O   1 
HETATM 7239 O  O   . HOH   V 6 .   ? 35.492 -8.212  29.863  1.00 47.30  ? 1181 HOH   A O   1 
HETATM 7240 O  O   . HOH   V 6 .   ? 22.749 -3.478  25.510  1.00 32.67  ? 1182 HOH   A O   1 
HETATM 7241 O  O   . HOH   V 6 .   ? 18.942 41.395  38.358  1.00 27.57  ? 1183 HOH   A O   1 
HETATM 7242 O  O   . HOH   V 6 .   ? 55.439 45.918  -16.567 1.00 25.56  ? 1184 HOH   A O   1 
HETATM 7243 O  O   . HOH   V 6 .   ? 13.639 34.414  10.422  1.00 29.86  ? 1185 HOH   A O   1 
HETATM 7244 O  O   . HOH   V 6 .   ? 44.185 14.350  20.086  1.00 18.21  ? 1186 HOH   A O   1 
HETATM 7245 O  O   . HOH   V 6 .   ? 31.087 20.195  -12.391 1.00 26.69  ? 1187 HOH   A O   1 
HETATM 7246 O  O   . HOH   V 6 .   ? 6.671  27.518  22.336  1.00 30.32  ? 1188 HOH   A O   1 
HETATM 7247 O  O   . HOH   V 6 .   ? 46.912 59.891  -26.257 1.00 43.39  ? 1189 HOH   A O   1 
HETATM 7248 O  O   . HOH   V 6 .   ? 5.077  12.168  22.176  1.00 40.71  ? 1190 HOH   A O   1 
HETATM 7249 O  O   . HOH   V 6 .   ? 11.667 18.941  -5.352  1.00 35.02  ? 1191 HOH   A O   1 
HETATM 7250 O  O   . HOH   V 6 .   ? 16.313 38.922  12.856  1.00 40.57  ? 1192 HOH   A O   1 
HETATM 7251 O  O   . HOH   V 6 .   ? 20.798 42.683  -2.545  1.00 51.13  ? 1193 HOH   A O   1 
HETATM 7252 O  O   . HOH   V 6 .   ? 32.074 -2.484  15.665  1.00 34.44  ? 1194 HOH   A O   1 
HETATM 7253 O  O   . HOH   V 6 .   ? 24.250 49.043  -5.132  1.00 38.70  ? 1195 HOH   A O   1 
HETATM 7254 O  O   . HOH   V 6 .   ? 40.325 -15.107 25.456  1.00 29.71  ? 1196 HOH   A O   1 
HETATM 7255 O  O   . HOH   V 6 .   ? 43.541 53.259  -18.983 1.00 16.73  ? 1197 HOH   A O   1 
HETATM 7256 O  O   . HOH   V 6 .   ? 20.809 33.413  13.808  1.00 25.30  ? 1198 HOH   A O   1 
HETATM 7257 O  O   . HOH   V 6 .   ? 46.820 67.332  -4.601  1.00 42.21  ? 1199 HOH   A O   1 
HETATM 7258 O  O   . HOH   V 6 .   ? 5.999  33.589  14.902  1.00 20.43  ? 1200 HOH   A O   1 
HETATM 7259 O  O   . HOH   V 6 .   ? 26.905 46.673  -3.682  1.00 22.86  ? 1201 HOH   A O   1 
HETATM 7260 O  O   . HOH   V 6 .   ? 39.772 41.693  -17.985 1.00 25.07  ? 1202 HOH   A O   1 
HETATM 7261 O  O   . HOH   V 6 .   ? 45.494 -5.732  14.440  1.00 27.01  ? 1203 HOH   A O   1 
HETATM 7262 O  O   . HOH   V 6 .   ? 33.498 36.320  40.881  1.00 37.82  ? 1204 HOH   A O   1 
HETATM 7263 O  O   . HOH   V 6 .   ? 29.261 18.597  30.278  1.00 29.58  ? 1205 HOH   A O   1 
HETATM 7264 O  O   . HOH   V 6 .   ? 35.359 23.126  28.174  1.00 20.25  ? 1206 HOH   A O   1 
HETATM 7265 O  O   . HOH   V 6 .   ? 6.729  25.755  -0.961  1.00 32.02  ? 1207 HOH   A O   1 
HETATM 7266 O  O   . HOH   V 6 .   ? 7.753  6.253   28.891  1.00 29.27  ? 1208 HOH   A O   1 
HETATM 7267 O  O   . HOH   V 6 .   ? 41.237 -11.204 14.084  1.00 38.93  ? 1209 HOH   A O   1 
HETATM 7268 O  O   . HOH   V 6 .   ? 42.761 25.733  -11.682 1.00 37.38  ? 1210 HOH   A O   1 
HETATM 7269 O  O   . HOH   V 6 .   ? 45.173 60.049  26.416  1.00 30.42  ? 1211 HOH   A O   1 
HETATM 7270 O  O   . HOH   V 6 .   ? 14.827 13.737  5.377   1.00 16.56  ? 1212 HOH   A O   1 
HETATM 7271 O  O   . HOH   V 6 .   ? 10.432 34.512  28.451  1.00 30.38  ? 1213 HOH   A O   1 
HETATM 7272 O  O   . HOH   V 6 .   ? 9.331  37.412  2.248   1.00 44.13  ? 1214 HOH   A O   1 
HETATM 7273 O  O   . HOH   V 6 .   ? 50.019 16.131  -0.033  1.00 46.66  ? 1215 HOH   A O   1 
HETATM 7274 O  O   . HOH   V 6 .   ? 28.214 53.011  -11.405 1.00 39.78  ? 1216 HOH   A O   1 
HETATM 7275 O  O   . HOH   V 6 .   ? 32.040 64.869  28.914  1.00 24.80  ? 1217 HOH   A O   1 
HETATM 7276 O  O   . HOH   V 6 .   ? 27.069 31.798  21.364  1.00 20.21  ? 1218 HOH   A O   1 
HETATM 7277 O  O   . HOH   V 6 .   ? 39.724 31.084  36.402  1.00 44.73  ? 1219 HOH   A O   1 
HETATM 7278 O  O   . HOH   V 6 .   ? 40.818 69.220  5.136   1.00 45.31  ? 1220 HOH   A O   1 
HETATM 7279 O  O   . HOH   V 6 .   ? 13.976 57.731  28.401  1.00 36.14  ? 1221 HOH   A O   1 
HETATM 7280 O  O   . HOH   V 6 .   ? 43.637 49.773  35.614  1.00 16.01  ? 1222 HOH   A O   1 
HETATM 7281 O  O   . HOH   V 6 .   ? 39.130 30.062  -18.081 1.00 32.25  ? 1223 HOH   A O   1 
HETATM 7282 O  O   . HOH   V 6 .   ? 26.610 59.274  25.396  1.00 23.76  ? 1224 HOH   A O   1 
HETATM 7283 O  O   . HOH   V 6 .   ? 24.805 24.043  -10.524 1.00 28.22  ? 1225 HOH   A O   1 
HETATM 7284 O  O   . HOH   V 6 .   ? 22.332 46.320  9.237   1.00 37.62  ? 1226 HOH   A O   1 
HETATM 7285 O  O   . HOH   V 6 .   ? 10.309 61.916  5.409   1.00 49.17  ? 1227 HOH   A O   1 
HETATM 7286 O  O   . HOH   V 6 .   ? 16.979 40.563  11.923  1.00 33.90  ? 1228 HOH   A O   1 
HETATM 7287 O  O   . HOH   V 6 .   ? 37.925 74.854  13.559  1.00 44.94  ? 1229 HOH   A O   1 
HETATM 7288 O  O   . HOH   V 6 .   ? 38.975 14.139  30.415  1.00 24.50  ? 1230 HOH   A O   1 
HETATM 7289 O  O   . HOH   V 6 .   ? 18.396 6.223   36.640  1.00 34.28  ? 1231 HOH   A O   1 
HETATM 7290 O  O   . HOH   V 6 .   ? 5.314  29.285  14.598  1.00 14.66  ? 1232 HOH   A O   1 
HETATM 7291 O  O   . HOH   V 6 .   ? 21.747 58.064  24.805  1.00 53.85  ? 1233 HOH   A O   1 
HETATM 7292 O  O   . HOH   V 6 .   ? 48.672 36.777  4.434   1.00 14.89  ? 1234 HOH   A O   1 
HETATM 7293 O  O   . HOH   V 6 .   ? 17.544 46.705  -5.209  1.00 39.28  ? 1235 HOH   A O   1 
HETATM 7294 O  O   . HOH   V 6 .   ? 16.253 8.942   -0.829  1.00 31.07  ? 1236 HOH   A O   1 
HETATM 7295 O  O   . HOH   V 6 .   ? 7.567  62.719  12.185  1.00 43.73  ? 1237 HOH   A O   1 
HETATM 7296 O  O   . HOH   V 6 .   ? 15.345 52.657  -3.324  1.00 51.94  ? 1238 HOH   A O   1 
HETATM 7297 O  O   . HOH   V 6 .   ? 22.433 22.365  28.025  1.00 17.45  ? 1239 HOH   A O   1 
HETATM 7298 O  O   . HOH   V 6 .   ? 12.751 7.520   16.062  1.00 19.37  ? 1240 HOH   A O   1 
HETATM 7299 O  O   . HOH   V 6 .   ? 20.599 50.009  -7.012  1.00 48.98  ? 1241 HOH   A O   1 
HETATM 7300 O  O   . HOH   V 6 .   ? 31.077 57.517  29.704  1.00 32.22  ? 1242 HOH   A O   1 
HETATM 7301 O  O   . HOH   V 6 .   ? 48.778 16.622  11.721  1.00 33.04  ? 1243 HOH   A O   1 
HETATM 7302 O  O   . HOH   V 6 .   ? 14.913 33.352  11.646  1.00 25.24  ? 1244 HOH   A O   1 
HETATM 7303 O  O   . HOH   V 6 .   ? 22.524 17.293  32.949  1.00 34.18  ? 1245 HOH   A O   1 
HETATM 7304 O  O   . HOH   V 6 .   ? 48.613 61.500  2.247   1.00 34.62  ? 1246 HOH   A O   1 
HETATM 7305 O  O   . HOH   V 6 .   ? 16.381 33.752  33.458  1.00 23.02  ? 1247 HOH   A O   1 
HETATM 7306 O  O   . HOH   V 6 .   ? 24.310 5.039   11.817  1.00 16.51  ? 1248 HOH   A O   1 
HETATM 7307 O  O   . HOH   V 6 .   ? 38.620 21.457  1.500   1.00 15.79  ? 1249 HOH   A O   1 
HETATM 7308 O  O   . HOH   V 6 .   ? 45.691 5.001   17.569  1.00 28.01  ? 1250 HOH   A O   1 
HETATM 7309 O  O   . HOH   V 6 .   ? 50.190 2.587   22.403  1.00 42.09  ? 1251 HOH   A O   1 
HETATM 7310 O  O   . HOH   V 6 .   ? 24.350 45.482  16.740  1.00 30.99  ? 1252 HOH   A O   1 
HETATM 7311 O  O   . HOH   V 6 .   ? 31.591 61.641  25.767  1.00 17.00  ? 1253 HOH   A O   1 
HETATM 7312 O  O   . HOH   V 6 .   ? 23.195 59.499  1.823   1.00 26.45  ? 1254 HOH   A O   1 
HETATM 7313 O  O   . HOH   V 6 .   ? 39.757 18.259  29.890  1.00 32.99  ? 1255 HOH   A O   1 
HETATM 7314 O  O   . HOH   V 6 .   ? 29.269 24.898  25.104  1.00 14.02  ? 1256 HOH   A O   1 
HETATM 7315 O  O   . HOH   V 6 .   ? 54.318 39.820  -12.880 1.00 32.80  ? 1257 HOH   A O   1 
HETATM 7316 O  O   . HOH   V 6 .   ? 52.985 50.002  -0.158  1.00 15.24  ? 1258 HOH   A O   1 
HETATM 7317 O  O   . HOH   V 6 .   ? 33.173 47.891  36.901  1.00 30.63  ? 1259 HOH   A O   1 
HETATM 7318 O  O   . HOH   V 6 .   ? 22.292 34.626  -10.913 1.00 40.79  ? 1260 HOH   A O   1 
HETATM 7319 O  O   . HOH   V 6 .   ? 21.342 59.592  28.940  1.00 51.77  ? 1261 HOH   A O   1 
HETATM 7320 O  O   . HOH   V 6 .   ? 42.315 42.812  -7.095  1.00 23.70  ? 1262 HOH   A O   1 
HETATM 7321 O  O   . HOH   V 6 .   ? 14.861 28.835  21.178  1.00 19.49  ? 1263 HOH   A O   1 
HETATM 7322 O  O   . HOH   V 6 .   ? 38.411 52.398  -23.212 1.00 22.13  ? 1264 HOH   A O   1 
HETATM 7323 O  O   . HOH   V 6 .   ? 13.388 20.161  -7.064  1.00 26.19  ? 1265 HOH   A O   1 
HETATM 7324 O  O   . HOH   V 6 .   ? 21.308 0.919   31.966  1.00 64.54  ? 1266 HOH   A O   1 
HETATM 7325 O  O   . HOH   V 6 .   ? 32.349 43.674  -5.479  1.00 23.34  ? 1267 HOH   A O   1 
HETATM 7326 O  O   . HOH   V 6 .   ? 39.964 60.431  -18.974 1.00 27.96  ? 1268 HOH   A O   1 
HETATM 7327 O  O   . HOH   V 6 .   ? 3.705  55.697  8.460   1.00 54.11  ? 1269 HOH   A O   1 
HETATM 7328 O  O   . HOH   V 6 .   ? 8.811  13.102  11.463  1.00 28.72  ? 1270 HOH   A O   1 
HETATM 7329 O  O   . HOH   V 6 .   ? 32.425 44.850  6.874   1.00 32.39  ? 1271 HOH   A O   1 
HETATM 7330 O  O   . HOH   V 6 .   ? 32.321 25.368  22.683  1.00 19.28  ? 1272 HOH   A O   1 
HETATM 7331 O  O   . HOH   V 6 .   ? 45.112 67.145  6.010   1.00 26.89  ? 1273 HOH   A O   1 
HETATM 7332 O  O   . HOH   V 6 .   ? 34.801 40.000  -11.489 1.00 49.73  ? 1274 HOH   A O   1 
HETATM 7333 O  O   . HOH   V 6 .   ? 13.845 52.134  29.707  1.00 24.41  ? 1275 HOH   A O   1 
HETATM 7334 O  O   . HOH   V 6 .   ? 32.846 19.112  8.048   1.00 13.26  ? 1276 HOH   A O   1 
HETATM 7335 O  O   . HOH   V 6 .   ? 50.631 44.623  22.729  1.00 38.10  ? 1277 HOH   A O   1 
HETATM 7336 O  O   . HOH   V 6 .   ? 14.411 3.946   6.112   1.00 37.21  ? 1278 HOH   A O   1 
HETATM 7337 O  O   . HOH   V 6 .   ? 3.167  40.735  11.769  1.00 45.39  ? 1279 HOH   A O   1 
HETATM 7338 O  O   . HOH   V 6 .   ? 26.914 24.041  -13.104 1.00 62.20  ? 1280 HOH   A O   1 
HETATM 7339 O  O   . HOH   V 6 .   ? 10.939 35.404  12.802  1.00 17.24  ? 1281 HOH   A O   1 
HETATM 7340 O  O   . HOH   V 6 .   ? 48.748 -11.587 30.456  1.00 42.06  ? 1282 HOH   A O   1 
HETATM 7341 O  O   . HOH   V 6 .   ? 31.620 46.561  28.605  1.00 15.54  ? 1283 HOH   A O   1 
HETATM 7342 O  O   . HOH   V 6 .   ? 14.707 11.942  9.147   1.00 16.60  ? 1284 HOH   A O   1 
HETATM 7343 O  O   . HOH   V 6 .   ? 34.061 55.481  -15.166 1.00 41.60  ? 1285 HOH   A O   1 
HETATM 7344 O  O   . HOH   V 6 .   ? 24.884 39.797  38.993  1.00 36.94  ? 1286 HOH   A O   1 
HETATM 7345 O  O   . HOH   V 6 .   ? 49.470 35.125  33.381  1.00 31.19  ? 1287 HOH   A O   1 
HETATM 7346 O  O   . HOH   V 6 .   ? 44.120 14.235  23.388  1.00 16.65  ? 1288 HOH   A O   1 
HETATM 7347 O  O   . HOH   V 6 .   ? 55.348 25.274  -7.219  1.00 35.79  ? 1289 HOH   A O   1 
HETATM 7348 O  O   . HOH   V 6 .   ? 20.149 28.672  25.635  1.00 15.80  ? 1290 HOH   A O   1 
HETATM 7349 O  O   . HOH   V 6 .   ? 28.449 42.344  -6.995  1.00 42.65  ? 1291 HOH   A O   1 
HETATM 7350 O  O   . HOH   V 6 .   ? 43.592 12.583  0.629   1.00 23.28  ? 1292 HOH   A O   1 
HETATM 7351 O  O   . HOH   V 6 .   ? 51.055 -8.194  26.398  1.00 44.19  ? 1293 HOH   A O   1 
HETATM 7352 O  O   . HOH   V 6 .   ? 45.537 68.892  11.983  1.00 33.05  ? 1294 HOH   A O   1 
HETATM 7353 O  O   . HOH   V 6 .   ? 49.283 22.134  5.749   1.00 25.66  ? 1295 HOH   A O   1 
HETATM 7354 O  O   . HOH   V 6 .   ? 31.757 51.052  -20.649 1.00 31.90  ? 1296 HOH   A O   1 
HETATM 7355 O  O   . HOH   V 6 .   ? 10.882 11.266  11.376  1.00 25.43  ? 1297 HOH   A O   1 
HETATM 7356 O  O   . HOH   V 6 .   ? 46.501 34.931  39.416  1.00 42.00  ? 1298 HOH   A O   1 
HETATM 7357 O  O   . HOH   V 6 .   ? 43.243 14.208  12.572  1.00 16.22  ? 1299 HOH   A O   1 
HETATM 7358 O  O   . HOH   V 6 .   ? 21.861 67.510  5.940   1.00 35.50  ? 1300 HOH   A O   1 
HETATM 7359 O  O   . HOH   V 6 .   ? 31.356 29.336  -11.143 1.00 23.89  ? 1301 HOH   A O   1 
HETATM 7360 O  O   . HOH   V 6 .   ? 10.551 -6.850  20.790  1.00 46.02  ? 1302 HOH   A O   1 
HETATM 7361 O  O   . HOH   V 6 .   ? 2.436  22.885  21.681  1.00 55.40  ? 1303 HOH   A O   1 
HETATM 7362 O  O   . HOH   V 6 .   ? 49.327 57.873  22.272  1.00 24.72  ? 1304 HOH   A O   1 
HETATM 7363 O  O   . HOH   V 6 .   ? 29.560 20.462  31.753  1.00 48.76  ? 1305 HOH   A O   1 
HETATM 7364 O  O   . HOH   V 6 .   ? 45.086 12.391  13.257  1.00 23.22  ? 1306 HOH   A O   1 
HETATM 7365 O  O   . HOH   V 6 .   ? 40.422 5.460   10.712  1.00 17.48  ? 1307 HOH   A O   1 
HETATM 7366 O  O   . HOH   V 6 .   ? 48.773 45.873  16.195  1.00 26.88  ? 1308 HOH   A O   1 
HETATM 7367 O  O   . HOH   V 6 .   ? 49.553 28.746  15.986  1.00 22.37  ? 1309 HOH   A O   1 
HETATM 7368 O  O   . HOH   V 6 .   ? 36.816 67.614  -1.077  1.00 33.36  ? 1310 HOH   A O   1 
HETATM 7369 O  O   . HOH   V 6 .   ? 6.685  43.367  31.901  1.00 27.86  ? 1311 HOH   A O   1 
HETATM 7370 O  O   . HOH   V 6 .   ? 15.013 51.234  24.348  1.00 23.20  ? 1312 HOH   A O   1 
HETATM 7371 O  O   . HOH   V 6 .   ? 22.423 20.253  18.624  1.00 13.18  ? 1313 HOH   A O   1 
HETATM 7372 O  O   . HOH   V 6 .   ? 48.716 44.538  34.956  1.00 31.63  ? 1314 HOH   A O   1 
HETATM 7373 O  O   . HOH   V 6 .   ? 39.619 42.859  -8.014  1.00 53.64  ? 1315 HOH   A O   1 
HETATM 7374 O  O   . HOH   V 6 .   ? 5.198  49.634  33.755  1.00 38.82  ? 1316 HOH   A O   1 
HETATM 7375 O  O   . HOH   V 6 .   ? 47.800 15.053  2.197   1.00 33.55  ? 1317 HOH   A O   1 
HETATM 7376 O  O   . HOH   V 6 .   ? 45.503 30.375  22.978  1.00 27.54  ? 1318 HOH   A O   1 
HETATM 7377 O  O   . HOH   V 6 .   ? 45.992 26.579  -12.355 1.00 35.37  ? 1319 HOH   A O   1 
HETATM 7378 O  O   . HOH   V 6 .   ? 29.748 2.586   5.006   1.00 27.90  ? 1320 HOH   A O   1 
HETATM 7379 O  O   . HOH   V 6 .   ? 28.533 31.966  15.977  1.00 73.60  ? 1321 HOH   A O   1 
HETATM 7380 O  O   . HOH   V 6 .   ? 38.903 63.701  -9.959  1.00 32.07  ? 1322 HOH   A O   1 
HETATM 7381 O  O   . HOH   V 6 .   ? 36.763 54.793  24.680  1.00 13.65  ? 1323 HOH   A O   1 
HETATM 7382 O  O   . HOH   V 6 .   ? 28.346 1.506   32.309  1.00 23.67  ? 1324 HOH   A O   1 
HETATM 7383 O  O   . HOH   V 6 .   ? 33.285 38.437  13.920  1.00 50.50  ? 1325 HOH   A O   1 
HETATM 7384 O  O   . HOH   V 6 .   ? 29.595 25.193  18.630  1.00 20.72  ? 1326 HOH   A O   1 
HETATM 7385 O  O   . HOH   V 6 .   ? 40.724 46.999  0.370   1.00 19.03  ? 1327 HOH   A O   1 
HETATM 7386 O  O   . HOH   V 6 .   ? 55.133 44.714  9.701   1.00 35.45  ? 1328 HOH   A O   1 
HETATM 7387 O  O   . HOH   V 6 .   ? 48.318 50.326  17.351  1.00 21.58  ? 1329 HOH   A O   1 
HETATM 7388 O  O   . HOH   V 6 .   ? 17.958 27.857  32.767  1.00 40.32  ? 1330 HOH   A O   1 
HETATM 7389 O  O   . HOH   V 6 .   ? 49.752 35.248  -14.093 1.00 50.63  ? 1331 HOH   A O   1 
HETATM 7390 O  O   . HOH   V 6 .   ? 3.307  17.087  17.687  1.00 19.71  ? 1332 HOH   A O   1 
HETATM 7391 O  O   . HOH   V 6 .   ? 29.054 53.007  24.361  1.00 16.48  ? 1333 HOH   A O   1 
HETATM 7392 O  O   . HOH   V 6 .   ? 40.079 64.878  25.704  1.00 48.15  ? 1334 HOH   A O   1 
HETATM 7393 O  O   . HOH   V 6 .   ? 51.445 3.091   24.660  1.00 45.36  ? 1335 HOH   A O   1 
HETATM 7394 O  O   . HOH   V 6 .   ? 56.446 49.600  5.984   1.00 40.71  ? 1336 HOH   A O   1 
HETATM 7395 O  O   . HOH   V 6 .   ? 14.058 9.127   28.215  1.00 22.17  ? 1337 HOH   A O   1 
HETATM 7396 O  O   . HOH   V 6 .   ? 56.266 41.839  -9.786  1.00 13.79  ? 1338 HOH   A O   1 
HETATM 7397 O  O   . HOH   V 6 .   ? 33.859 46.623  38.939  1.00 38.68  ? 1339 HOH   A O   1 
HETATM 7398 O  O   . HOH   V 6 .   ? 43.226 26.786  8.947   1.00 14.79  ? 1340 HOH   A O   1 
HETATM 7399 O  O   . HOH   V 6 .   ? 24.072 56.551  -6.541  1.00 28.26  ? 1341 HOH   A O   1 
HETATM 7400 O  O   . HOH   V 6 .   ? 51.856 28.867  9.801   1.00 23.77  ? 1342 HOH   A O   1 
HETATM 7401 O  O   . HOH   V 6 .   ? 45.368 61.965  11.165  1.00 19.09  ? 1343 HOH   A O   1 
HETATM 7402 O  O   . HOH   V 6 .   ? 41.772 57.971  -25.753 1.00 26.25  ? 1344 HOH   A O   1 
HETATM 7403 O  O   . HOH   V 6 .   ? 49.741 -10.833 11.949  1.00 56.62  ? 1345 HOH   A O   1 
HETATM 7404 O  O   . HOH   V 6 .   ? 36.505 -8.283  15.496  1.00 39.35  ? 1346 HOH   A O   1 
HETATM 7405 O  O   . HOH   V 6 .   ? 11.347 26.542  20.718  1.00 21.01  ? 1347 HOH   A O   1 
HETATM 7406 O  O   . HOH   V 6 .   ? 24.874 54.923  21.112  1.00 18.06  ? 1348 HOH   A O   1 
HETATM 7407 O  O   . HOH   V 6 .   ? 55.800 53.083  3.875   1.00 33.13  ? 1349 HOH   A O   1 
HETATM 7408 O  O   . HOH   V 6 .   ? 3.840  38.480  29.755  1.00 39.62  ? 1350 HOH   A O   1 
HETATM 7409 O  O   . HOH   V 6 .   ? 33.711 38.080  -6.519  1.00 37.52  ? 1351 HOH   A O   1 
HETATM 7410 O  O   . HOH   V 6 .   ? 28.576 10.724  -4.443  1.00 23.69  ? 1352 HOH   A O   1 
HETATM 7411 O  O   . HOH   V 6 .   ? 46.323 66.242  10.177  1.00 23.86  ? 1353 HOH   A O   1 
HETATM 7412 O  O   . HOH   V 6 .   ? 33.435 21.161  22.272  1.00 17.01  ? 1354 HOH   A O   1 
HETATM 7413 O  O   . HOH   V 6 .   ? 41.615 9.648   5.935   1.00 23.79  ? 1355 HOH   A O   1 
HETATM 7414 O  O   . HOH   V 6 .   ? 41.268 37.273  38.868  1.00 44.61  ? 1356 HOH   A O   1 
HETATM 7415 O  O   . HOH   V 6 .   ? 32.698 23.228  29.228  1.00 20.66  ? 1357 HOH   A O   1 
HETATM 7416 O  O   . HOH   V 6 .   ? 7.349  54.193  25.571  1.00 25.97  ? 1358 HOH   A O   1 
HETATM 7417 O  O   . HOH   V 6 .   ? 6.680  28.037  6.436   1.00 17.20  ? 1359 HOH   A O   1 
HETATM 7418 O  O   . HOH   V 6 .   ? 3.108  34.182  10.211  1.00 29.30  ? 1360 HOH   A O   1 
HETATM 7419 O  O   . HOH   V 6 .   ? 15.657 65.889  3.281   1.00 42.76  ? 1361 HOH   A O   1 
HETATM 7420 O  O   . HOH   V 6 .   ? 34.338 54.676  31.767  1.00 30.29  ? 1362 HOH   A O   1 
HETATM 7421 O  O   . HOH   V 6 .   ? 53.771 53.359  1.069   1.00 26.87  ? 1363 HOH   A O   1 
HETATM 7422 O  O   . HOH   V 6 .   ? 45.435 -11.291 20.220  1.00 34.23  ? 1364 HOH   A O   1 
HETATM 7423 O  O   . HOH   V 6 .   ? 29.777 31.629  9.268   1.00 26.80  ? 1365 HOH   A O   1 
HETATM 7424 O  O   . HOH   V 6 .   ? 14.803 44.066  12.024  1.00 26.49  ? 1366 HOH   A O   1 
HETATM 7425 O  O   . HOH   V 6 .   ? 16.537 25.284  30.338  1.00 65.28  ? 1367 HOH   A O   1 
HETATM 7426 O  O   . HOH   V 6 .   ? 44.229 64.834  20.087  1.00 21.67  ? 1368 HOH   A O   1 
HETATM 7427 O  O   . HOH   V 6 .   ? 51.635 -9.176  17.602  1.00 47.75  ? 1369 HOH   A O   1 
HETATM 7428 O  O   . HOH   V 6 .   ? 32.031 52.450  -16.269 1.00 42.30  ? 1370 HOH   A O   1 
HETATM 7429 O  O   . HOH   V 6 .   ? 47.666 63.935  -11.814 1.00 37.19  ? 1371 HOH   A O   1 
HETATM 7430 O  O   . HOH   V 6 .   ? 8.041  22.911  0.273   1.00 30.76  ? 1372 HOH   A O   1 
HETATM 7431 O  O   . HOH   V 6 .   ? 2.049  51.362  8.398   1.00 37.11  ? 1373 HOH   A O   1 
HETATM 7432 O  O   . HOH   V 6 .   ? 47.923 16.441  -3.638  1.00 28.17  ? 1374 HOH   A O   1 
HETATM 7433 O  O   . HOH   V 6 .   ? 5.439  16.196  19.154  1.00 22.82  ? 1375 HOH   A O   1 
HETATM 7434 O  O   . HOH   V 6 .   ? 29.295 33.195  38.285  1.00 24.78  ? 1376 HOH   A O   1 
HETATM 7435 O  O   . HOH   V 6 .   ? 48.037 59.487  -16.049 1.00 18.68  ? 1377 HOH   A O   1 
HETATM 7436 O  O   . HOH   V 6 .   ? 7.230  16.314  28.391  1.00 45.21  ? 1378 HOH   A O   1 
HETATM 7437 O  O   . HOH   V 6 .   ? 42.739 30.532  10.110  1.00 15.68  ? 1379 HOH   A O   1 
HETATM 7438 O  O   . HOH   V 6 .   ? 5.927  42.846  16.400  1.00 25.78  ? 1380 HOH   A O   1 
HETATM 7439 O  O   . HOH   V 6 .   ? 3.467  35.818  13.235  1.00 25.67  ? 1381 HOH   A O   1 
HETATM 7440 O  O   . HOH   V 6 .   ? 48.805 52.884  22.456  1.00 29.25  ? 1382 HOH   A O   1 
HETATM 7441 O  O   . HOH   V 6 .   ? 35.919 21.164  21.288  1.00 14.82  ? 1383 HOH   A O   1 
HETATM 7442 O  O   . HOH   V 6 .   ? 24.777 -1.352  10.379  1.00 34.15  ? 1384 HOH   A O   1 
HETATM 7443 O  O   . HOH   V 6 .   ? 4.228  40.571  19.878  1.00 30.00  ? 1385 HOH   A O   1 
HETATM 7444 O  O   . HOH   V 6 .   ? 47.462 33.813  6.180   1.00 14.82  ? 1386 HOH   A O   1 
HETATM 7445 O  O   . HOH   V 6 .   ? 59.385 49.539  -9.660  1.00 17.77  ? 1387 HOH   A O   1 
HETATM 7446 O  O   . HOH   V 6 .   ? 37.256 44.275  17.165  1.00 43.37  ? 1388 HOH   A O   1 
HETATM 7447 O  O   . HOH   V 6 .   ? 39.281 9.057   -2.678  1.00 37.06  ? 1389 HOH   A O   1 
HETATM 7448 O  O   . HOH   V 6 .   ? 45.742 4.042   20.033  1.00 25.20  ? 1390 HOH   A O   1 
HETATM 7449 O  O   . HOH   V 6 .   ? 16.489 8.282   24.790  1.00 21.24  ? 1391 HOH   A O   1 
HETATM 7450 O  O   . HOH   V 6 .   ? 27.126 -1.275  20.525  1.00 20.79  ? 1392 HOH   A O   1 
HETATM 7451 O  O   . HOH   V 6 .   ? 18.200 46.511  10.699  1.00 22.21  ? 1393 HOH   A O   1 
HETATM 7452 O  O   . HOH   V 6 .   ? 25.214 19.754  15.961  1.00 12.77  ? 1394 HOH   A O   1 
HETATM 7453 O  O   . HOH   V 6 .   ? 37.555 20.174  3.486   1.00 19.70  ? 1395 HOH   A O   1 
HETATM 7454 O  O   . HOH   V 6 .   ? 9.205  41.413  13.759  1.00 20.27  ? 1396 HOH   A O   1 
HETATM 7455 O  O   . HOH   V 6 .   ? 5.964  15.403  11.839  1.00 18.77  ? 1397 HOH   A O   1 
HETATM 7456 O  O   . HOH   V 6 .   ? 20.177 39.820  21.360  1.00 25.34  ? 1398 HOH   A O   1 
HETATM 7457 O  O   . HOH   V 6 .   ? 18.622 54.465  -1.876  1.00 21.48  ? 1399 HOH   A O   1 
HETATM 7458 O  O   . HOH   V 6 .   ? 29.200 18.161  15.509  1.00 12.72  ? 1400 HOH   A O   1 
HETATM 7459 O  O   . HOH   V 6 .   ? -1.051 21.946  20.897  1.00 26.61  ? 1401 HOH   A O   1 
HETATM 7460 O  O   . HOH   V 6 .   ? 49.968 57.384  -25.654 1.00 34.74  ? 1402 HOH   A O   1 
HETATM 7461 O  O   . HOH   V 6 .   ? 37.356 -3.585  31.887  1.00 26.51  ? 1403 HOH   A O   1 
HETATM 7462 O  O   . HOH   V 6 .   ? 27.133 18.124  -13.091 1.00 34.31  ? 1404 HOH   A O   1 
HETATM 7463 O  O   . HOH   V 6 .   ? 29.665 67.780  -6.795  1.00 42.08  ? 1405 HOH   A O   1 
HETATM 7464 O  O   . HOH   V 6 .   ? 20.568 7.987   36.870  1.00 39.26  ? 1406 HOH   A O   1 
HETATM 7465 O  O   . HOH   V 6 .   ? 18.180 28.154  18.924  1.00 13.41  ? 1407 HOH   A O   1 
HETATM 7466 O  O   . HOH   V 6 .   ? 11.383 14.793  27.494  1.00 24.19  ? 1408 HOH   A O   1 
HETATM 7467 O  O   . HOH   V 6 .   ? 35.366 34.874  -7.558  1.00 20.22  ? 1409 HOH   A O   1 
HETATM 7468 O  O   . HOH   V 6 .   ? 38.317 9.926   31.864  1.00 20.47  ? 1410 HOH   A O   1 
HETATM 7469 O  O   . HOH   V 6 .   ? 52.006 29.981  12.309  1.00 22.88  ? 1411 HOH   A O   1 
HETATM 7470 O  O   . HOH   V 6 .   ? 37.119 20.544  -16.318 1.00 43.81  ? 1412 HOH   A O   1 
HETATM 7471 O  O   . HOH   V 6 .   ? 3.647  57.196  13.475  1.00 39.05  ? 1413 HOH   A O   1 
HETATM 7472 O  O   . HOH   V 6 .   ? 19.422 46.456  8.387   1.00 22.23  ? 1414 HOH   A O   1 
HETATM 7473 O  O   . HOH   V 6 .   ? 35.991 9.339   30.476  1.00 18.37  ? 1415 HOH   A O   1 
HETATM 7474 O  O   . HOH   V 6 .   ? 43.248 -7.879  31.238  1.00 58.41  ? 1416 HOH   A O   1 
HETATM 7475 O  O   . HOH   V 6 .   ? 40.304 33.253  21.784  1.00 14.94  ? 1417 HOH   A O   1 
HETATM 7476 O  O   . HOH   V 6 .   ? 32.180 47.573  24.869  1.00 20.67  ? 1418 HOH   A O   1 
HETATM 7477 O  O   . HOH   V 6 .   ? 38.443 36.103  -13.830 1.00 27.06  ? 1419 HOH   A O   1 
HETATM 7478 O  O   . HOH   V 6 .   ? 57.882 45.632  1.477   1.00 26.78  ? 1420 HOH   A O   1 
HETATM 7479 O  O   . HOH   V 6 .   ? 2.826  53.921  28.034  1.00 42.73  ? 1421 HOH   A O   1 
HETATM 7480 O  O   . HOH   V 6 .   ? 3.245  31.417  22.058  1.00 30.65  ? 1422 HOH   A O   1 
HETATM 7481 O  O   . HOH   V 6 .   ? 50.762 44.887  25.436  1.00 44.91  ? 1423 HOH   A O   1 
HETATM 7482 O  O   . HOH   V 6 .   ? 35.828 58.945  -17.459 1.00 33.59  ? 1424 HOH   A O   1 
HETATM 7483 O  O   . HOH   V 6 .   ? 14.208 31.443  20.767  1.00 23.08  ? 1425 HOH   A O   1 
HETATM 7484 O  O   . HOH   V 6 .   ? 9.191  52.495  -0.417  1.00 25.42  ? 1426 HOH   A O   1 
HETATM 7485 O  O   . HOH   V 6 .   ? 13.335 8.825   31.053  1.00 52.07  ? 1427 HOH   A O   1 
HETATM 7486 O  O   . HOH   V 6 .   ? 15.529 41.245  -3.004  1.00 33.95  ? 1428 HOH   A O   1 
HETATM 7487 O  O   . HOH   V 6 .   ? 44.869 57.091  -28.585 1.00 19.99  ? 1429 HOH   A O   1 
HETATM 7488 O  O   . HOH   V 6 .   ? 46.425 55.253  14.754  1.00 21.11  ? 1430 HOH   A O   1 
HETATM 7489 O  O   . HOH   V 6 .   ? 50.534 32.204  -10.189 1.00 27.57  ? 1431 HOH   A O   1 
HETATM 7490 O  O   . HOH   V 6 .   ? 9.403  43.944  -0.165  1.00 27.61  ? 1432 HOH   A O   1 
HETATM 7491 O  O   . HOH   V 6 .   ? 52.475 33.163  -8.644  1.00 22.96  ? 1433 HOH   A O   1 
HETATM 7492 O  O   . HOH   V 6 .   ? 34.462 11.334  4.388   1.00 14.94  ? 1434 HOH   A O   1 
HETATM 7493 O  O   . HOH   V 6 .   ? 51.011 10.370  17.246  1.00 35.67  ? 1435 HOH   A O   1 
HETATM 7494 O  O   . HOH   V 6 .   ? 33.254 19.778  28.383  1.00 25.97  ? 1436 HOH   A O   1 
HETATM 7495 O  O   . HOH   V 6 .   ? 13.504 46.559  11.940  1.00 16.42  ? 1437 HOH   A O   1 
HETATM 7496 O  O   . HOH   V 6 .   ? 36.724 35.984  37.947  1.00 44.51  ? 1438 HOH   A O   1 
HETATM 7497 O  O   . HOH   V 6 .   ? 11.368 16.440  23.764  1.00 29.19  ? 1439 HOH   A O   1 
HETATM 7498 O  O   . HOH   V 6 .   ? 15.695 51.812  1.260   1.00 20.46  ? 1440 HOH   A O   1 
HETATM 7499 O  O   . HOH   V 6 .   ? 28.437 62.337  -7.570  1.00 36.54  ? 1441 HOH   A O   1 
HETATM 7500 O  O   . HOH   V 6 .   ? 43.845 29.824  -15.245 1.00 30.36  ? 1442 HOH   A O   1 
HETATM 7501 O  O   . HOH   V 6 .   ? 16.912 28.957  -8.266  1.00 32.84  ? 1443 HOH   A O   1 
HETATM 7502 O  O   . HOH   V 6 .   ? 15.895 34.955  21.045  1.00 16.96  ? 1444 HOH   A O   1 
HETATM 7503 O  O   . HOH   V 6 .   ? 15.233 32.394  18.221  1.00 16.22  ? 1445 HOH   A O   1 
HETATM 7504 O  O   . HOH   V 6 .   ? 28.160 57.883  27.134  1.00 24.52  ? 1446 HOH   A O   1 
HETATM 7505 O  O   . HOH   V 6 .   ? 27.457 60.212  -10.326 1.00 42.39  ? 1447 HOH   A O   1 
HETATM 7506 O  O   . HOH   V 6 .   ? 38.470 38.649  -2.084  1.00 20.93  ? 1448 HOH   A O   1 
HETATM 7507 O  O   . HOH   V 6 .   ? 47.840 47.731  18.217  1.00 21.12  ? 1449 HOH   A O   1 
HETATM 7508 O  O   . HOH   V 6 .   ? 28.153 31.845  -8.860  1.00 23.99  ? 1450 HOH   A O   1 
HETATM 7509 O  O   . HOH   V 6 .   ? 58.823 52.125  -4.369  1.00 29.51  ? 1451 HOH   A O   1 
HETATM 7510 O  O   . HOH   V 6 .   ? 31.127 35.483  7.893   1.00 34.54  ? 1452 HOH   A O   1 
HETATM 7511 O  O   . HOH   V 6 .   ? 28.355 14.780  0.816   1.00 16.64  ? 1453 HOH   A O   1 
HETATM 7512 O  O   . HOH   V 6 .   ? 14.441 13.818  17.346  1.00 16.70  ? 1454 HOH   A O   1 
HETATM 7513 O  O   . HOH   V 6 .   ? 46.209 35.856  8.537   1.00 15.56  ? 1455 HOH   A O   1 
HETATM 7514 O  O   . HOH   V 6 .   ? 40.109 63.781  0.699   1.00 20.82  ? 1456 HOH   A O   1 
HETATM 7515 O  O   . HOH   V 6 .   ? 6.582  22.887  4.496   1.00 20.34  ? 1457 HOH   A O   1 
HETATM 7516 O  O   . HOH   V 6 .   ? 52.528 -2.978  9.483   1.00 40.54  ? 1458 HOH   A O   1 
HETATM 7517 O  O   . HOH   V 6 .   ? 6.101  55.940  4.758   1.00 25.84  ? 1459 HOH   A O   1 
HETATM 7518 O  O   . HOH   V 6 .   ? 41.164 62.462  -19.803 1.00 51.09  ? 1460 HOH   A O   1 
HETATM 7519 O  O   . HOH   V 6 .   ? 4.362  37.437  18.857  1.00 39.79  ? 1461 HOH   A O   1 
HETATM 7520 O  O   . HOH   V 6 .   ? 28.023 4.221   22.404  1.00 16.24  ? 1462 HOH   A O   1 
HETATM 7521 O  O   . HOH   V 6 .   ? 53.346 56.749  0.666   1.00 26.13  ? 1463 HOH   A O   1 
HETATM 7522 O  O   . HOH   V 6 .   ? 26.075 35.748  38.926  1.00 31.03  ? 1464 HOH   A O   1 
HETATM 7523 O  O   . HOH   V 6 .   ? 26.491 6.726   -1.658  1.00 50.52  ? 1465 HOH   A O   1 
HETATM 7524 O  O   . HOH   V 6 .   ? 12.620 24.076  16.854  1.00 14.44  ? 1466 HOH   A O   1 
HETATM 7525 O  O   . HOH   V 6 .   ? 58.275 54.043  -11.807 1.00 19.47  ? 1467 HOH   A O   1 
HETATM 7526 O  O   . HOH   V 6 .   ? 62.296 46.503  -7.191  1.00 18.00  ? 1468 HOH   A O   1 
HETATM 7527 O  O   . HOH   V 6 .   ? 36.557 68.725  23.904  1.00 37.47  ? 1469 HOH   A O   1 
HETATM 7528 O  O   . HOH   V 6 .   ? 17.323 38.947  38.474  1.00 32.52  ? 1470 HOH   A O   1 
HETATM 7529 O  O   . HOH   V 6 .   ? 25.212 23.802  20.312  1.00 13.95  ? 1471 HOH   A O   1 
HETATM 7530 O  O   . HOH   V 6 .   ? 14.670 6.333   28.829  1.00 24.38  ? 1472 HOH   A O   1 
HETATM 7531 O  O   . HOH   V 6 .   ? 42.050 52.475  -1.827  1.00 16.00  ? 1473 HOH   A O   1 
HETATM 7532 O  O   . HOH   V 6 .   ? 3.656  48.706  30.816  1.00 27.09  ? 1474 HOH   A O   1 
HETATM 7533 O  O   . HOH   V 6 .   ? 30.364 13.362  29.011  1.00 20.85  ? 1475 HOH   A O   1 
HETATM 7534 O  O   . HOH   V 6 .   ? 25.450 48.600  -2.584  1.00 19.38  ? 1476 HOH   A O   1 
HETATM 7535 O  O   . HOH   V 6 .   ? 50.309 24.180  6.630   1.00 36.35  ? 1477 HOH   A O   1 
HETATM 7536 O  O   . HOH   V 6 .   ? 28.332 27.403  33.589  1.00 24.12  ? 1478 HOH   A O   1 
HETATM 7537 O  O   . HOH   V 6 .   ? 26.640 16.362  16.535  1.00 13.68  ? 1479 HOH   A O   1 
HETATM 7538 O  O   . HOH   V 6 .   ? 2.277  27.664  16.441  1.00 20.11  ? 1480 HOH   A O   1 
HETATM 7539 O  O   . HOH   V 6 .   ? 22.104 12.048  -4.671  1.00 22.18  ? 1481 HOH   A O   1 
HETATM 7540 O  O   . HOH   V 6 .   ? 49.911 47.372  19.814  1.00 28.62  ? 1482 HOH   A O   1 
HETATM 7541 O  O   . HOH   V 6 .   ? 31.445 41.903  -2.950  1.00 22.16  ? 1483 HOH   A O   1 
HETATM 7542 O  O   . HOH   V 6 .   ? 42.829 63.748  -0.326  1.00 24.36  ? 1484 HOH   A O   1 
HETATM 7543 O  O   . HOH   V 6 .   ? 50.167 19.989  7.798   1.00 39.76  ? 1485 HOH   A O   1 
HETATM 7544 O  O   . HOH   V 6 .   ? 8.695  39.598  6.526   1.00 41.39  ? 1486 HOH   A O   1 
HETATM 7545 O  O   . HOH   V 6 .   ? 36.824 48.544  18.273  1.00 24.25  ? 1487 HOH   A O   1 
HETATM 7546 O  O   . HOH   V 6 .   ? 34.818 67.461  27.812  1.00 51.23  ? 1488 HOH   A O   1 
HETATM 7547 O  O   . HOH   V 6 .   ? 19.841 16.948  -7.802  1.00 37.92  ? 1489 HOH   A O   1 
HETATM 7548 O  O   . HOH   V 6 .   ? 47.479 6.715   11.370  1.00 48.62  ? 1490 HOH   A O   1 
HETATM 7549 O  O   . HOH   V 6 .   ? 14.760 24.769  -7.242  1.00 33.23  ? 1491 HOH   A O   1 
HETATM 7550 O  O   . HOH   V 6 .   ? 47.399 11.123  15.745  1.00 22.85  ? 1492 HOH   A O   1 
HETATM 7551 O  O   . HOH   V 6 .   ? 15.201 33.433  24.736  1.00 15.36  ? 1493 HOH   A O   1 
HETATM 7552 O  O   . HOH   V 6 .   ? 32.169 30.605  -17.874 1.00 33.20  ? 1494 HOH   A O   1 
HETATM 7553 O  O   . HOH   V 6 .   ? 9.769  33.414  0.034   1.00 45.66  ? 1495 HOH   A O   1 
HETATM 7554 O  O   . HOH   V 6 .   ? 4.194  38.317  21.478  1.00 28.52  ? 1496 HOH   A O   1 
HETATM 7555 O  O   . HOH   V 6 .   ? 57.203 56.344  -4.301  1.00 41.70  ? 1497 HOH   A O   1 
HETATM 7556 O  O   . HOH   V 6 .   ? 11.596 30.963  16.243  1.00 18.88  ? 1498 HOH   A O   1 
HETATM 7557 O  O   . HOH   V 6 .   ? 56.891 44.069  -14.950 1.00 23.18  ? 1499 HOH   A O   1 
HETATM 7558 O  O   . HOH   V 6 .   ? 36.046 54.260  -16.439 1.00 26.23  ? 1500 HOH   A O   1 
HETATM 7559 O  O   . HOH   V 6 .   ? 52.514 30.767  -7.380  1.00 25.71  ? 1501 HOH   A O   1 
HETATM 7560 O  O   . HOH   V 6 .   ? 13.823 -7.120  21.813  1.00 33.00  ? 1502 HOH   A O   1 
HETATM 7561 O  O   . HOH   V 6 .   ? 9.104  44.228  33.272  1.00 40.10  ? 1503 HOH   A O   1 
HETATM 7562 O  O   . HOH   V 6 .   ? 24.893 30.127  32.026  1.00 37.51  ? 1504 HOH   A O   1 
HETATM 7563 O  O   . HOH   V 6 .   ? 30.199 69.660  12.321  1.00 33.99  ? 1505 HOH   A O   1 
HETATM 7564 O  O   . HOH   V 6 .   ? 33.374 48.809  12.137  1.00 32.21  ? 1506 HOH   A O   1 
HETATM 7565 O  O   . HOH   V 6 .   ? 26.050 15.103  -9.292  1.00 29.29  ? 1507 HOH   A O   1 
HETATM 7566 O  O   . HOH   V 6 .   ? 34.703 35.025  -11.516 1.00 37.98  ? 1508 HOH   A O   1 
HETATM 7567 O  O   . HOH   V 6 .   ? 22.392 60.804  -5.550  1.00 38.95  ? 1509 HOH   A O   1 
HETATM 7568 O  O   . HOH   V 6 .   ? 21.331 47.491  -3.729  1.00 33.07  ? 1510 HOH   A O   1 
HETATM 7569 O  O   . HOH   V 6 .   ? 49.033 49.057  -19.639 1.00 29.23  ? 1511 HOH   A O   1 
HETATM 7570 O  O   . HOH   V 6 .   ? 4.899  55.974  22.277  1.00 31.18  ? 1512 HOH   A O   1 
HETATM 7571 O  O   . HOH   V 6 .   ? 47.606 13.762  -0.851  1.00 52.15  ? 1513 HOH   A O   1 
HETATM 7572 O  O   . HOH   V 6 .   ? 31.561 21.767  20.376  1.00 19.35  ? 1514 HOH   A O   1 
HETATM 7573 O  O   . HOH   V 6 .   ? 19.645 39.050  10.830  1.00 41.68  ? 1515 HOH   A O   1 
HETATM 7574 O  O   . HOH   V 6 .   ? 49.152 41.385  10.670  1.00 23.20  ? 1516 HOH   A O   1 
HETATM 7575 O  O   . HOH   V 6 .   ? 24.791 46.350  38.604  1.00 24.40  ? 1517 HOH   A O   1 
HETATM 7576 O  O   . HOH   V 6 .   ? 12.867 47.611  -5.850  1.00 50.04  ? 1518 HOH   A O   1 
HETATM 7577 O  O   . HOH   V 6 .   ? 22.255 66.570  12.812  1.00 24.26  ? 1519 HOH   A O   1 
HETATM 7578 O  O   . HOH   V 6 .   ? -2.077 47.951  26.174  1.00 42.91  ? 1520 HOH   A O   1 
HETATM 7579 O  O   . HOH   V 6 .   ? 4.982  42.708  12.238  1.00 34.65  ? 1521 HOH   A O   1 
HETATM 7580 O  O   . HOH   V 6 .   ? 33.707 50.251  -10.815 1.00 22.27  ? 1522 HOH   A O   1 
HETATM 7581 O  O   . HOH   V 6 .   ? 39.969 7.832   4.778   1.00 30.48  ? 1523 HOH   A O   1 
HETATM 7582 O  O   . HOH   V 6 .   ? 34.480 28.680  -9.784  1.00 20.08  ? 1524 HOH   A O   1 
HETATM 7583 O  O   . HOH   V 6 .   ? 47.796 2.573   21.066  1.00 30.61  ? 1525 HOH   A O   1 
HETATM 7584 O  O   . HOH   V 6 .   ? 37.371 10.842  13.012  1.00 14.18  ? 1526 HOH   A O   1 
HETATM 7585 O  O   . HOH   V 6 .   ? 20.882 47.222  21.889  1.00 16.03  ? 1527 HOH   A O   1 
HETATM 7586 O  O   . HOH   V 6 .   ? 35.094 24.228  -15.222 1.00 35.85  ? 1528 HOH   A O   1 
HETATM 7587 O  O   . HOH   V 6 .   ? 39.636 50.332  14.700  1.00 49.31  ? 1529 HOH   A O   1 
HETATM 7588 O  O   . HOH   V 6 .   ? 50.920 15.433  20.300  1.00 27.43  ? 1530 HOH   A O   1 
HETATM 7589 O  O   . HOH   V 6 .   ? 54.577 3.970   21.148  1.00 42.71  ? 1531 HOH   A O   1 
HETATM 7590 O  O   . HOH   V 6 .   ? 36.935 14.035  14.263  1.00 14.13  ? 1532 HOH   A O   1 
HETATM 7591 O  O   . HOH   V 6 .   ? 54.349 53.460  -5.408  1.00 16.18  ? 1533 HOH   A O   1 
HETATM 7592 O  O   . HOH   V 6 .   ? 24.139 35.343  21.443  1.00 15.40  ? 1534 HOH   A O   1 
HETATM 7593 O  O   . HOH   V 6 .   ? 34.678 47.898  -14.301 1.00 30.15  ? 1535 HOH   A O   1 
HETATM 7594 O  O   . HOH   V 6 .   ? 4.547  18.510  10.490  1.00 15.38  ? 1536 HOH   A O   1 
HETATM 7595 O  O   . HOH   V 6 .   ? 24.410 2.817   4.353   1.00 37.20  ? 1537 HOH   A O   1 
HETATM 7596 O  O   . HOH   V 6 .   ? 27.442 43.781  35.986  1.00 19.46  ? 1538 HOH   A O   1 
HETATM 7597 O  O   . HOH   V 6 .   ? 55.362 56.550  -11.426 1.00 17.01  ? 1539 HOH   A O   1 
HETATM 7598 O  O   . HOH   V 6 .   ? 45.480 17.106  -4.799  1.00 21.95  ? 1540 HOH   A O   1 
HETATM 7599 O  O   . HOH   V 6 .   ? 12.261 28.403  6.999   1.00 13.19  ? 1541 HOH   A O   1 
HETATM 7600 O  O   . HOH   V 6 .   ? 28.290 68.894  14.053  1.00 23.98  ? 1542 HOH   A O   1 
HETATM 7601 O  O   . HOH   V 6 .   ? 21.336 64.415  -0.913  1.00 34.87  ? 1543 HOH   A O   1 
HETATM 7602 O  O   . HOH   V 6 .   ? 22.250 0.636   13.558  1.00 29.56  ? 1544 HOH   A O   1 
HETATM 7603 O  O   . HOH   V 6 .   ? 34.314 -20.516 18.403  1.00 40.90  ? 1545 HOH   A O   1 
HETATM 7604 O  O   . HOH   V 6 .   ? 39.755 44.355  16.660  1.00 39.78  ? 1546 HOH   A O   1 
HETATM 7605 O  O   . HOH   V 6 .   ? 9.669  4.083   14.821  1.00 28.56  ? 1547 HOH   A O   1 
HETATM 7606 O  O   . HOH   V 6 .   ? 12.307 55.287  -0.143  1.00 30.94  ? 1548 HOH   A O   1 
HETATM 7607 O  O   . HOH   V 6 .   ? 21.695 35.005  37.146  1.00 25.79  ? 1549 HOH   A O   1 
HETATM 7608 O  O   . HOH   V 6 .   ? 55.465 31.303  -1.136  1.00 24.08  ? 1550 HOH   A O   1 
HETATM 7609 O  O   . HOH   V 6 .   ? 40.071 10.759  30.021  1.00 21.69  ? 1551 HOH   A O   1 
HETATM 7610 O  O   . HOH   V 6 .   ? 35.688 27.688  34.197  1.00 37.19  ? 1552 HOH   A O   1 
HETATM 7611 O  O   . HOH   V 6 .   ? 43.144 38.743  -10.850 1.00 20.40  ? 1553 HOH   A O   1 
HETATM 7612 O  O   . HOH   V 6 .   ? 48.522 52.246  13.938  1.00 27.51  ? 1554 HOH   A O   1 
HETATM 7613 O  O   . HOH   V 6 .   ? 41.214 36.046  14.606  1.00 34.42  ? 1555 HOH   A O   1 
HETATM 7614 O  O   . HOH   V 6 .   ? 36.832 1.233   33.997  1.00 34.40  ? 1556 HOH   A O   1 
HETATM 7615 O  O   . HOH   V 6 .   ? 33.719 60.945  -14.158 1.00 41.28  ? 1557 HOH   A O   1 
HETATM 7616 O  O   . HOH   V 6 .   ? 46.521 36.244  25.505  1.00 21.56  ? 1558 HOH   A O   1 
HETATM 7617 O  O   . HOH   V 6 .   ? 9.331  33.537  23.462  1.00 24.34  ? 1559 HOH   A O   1 
HETATM 7618 O  O   . HOH   V 6 .   ? 34.431 66.922  -8.018  1.00 46.25  ? 1560 HOH   A O   1 
HETATM 7619 O  O   . HOH   V 6 .   ? 33.547 42.269  38.220  1.00 35.09  ? 1561 HOH   A O   1 
HETATM 7620 O  O   . HOH   V 6 .   ? 47.389 40.416  36.869  1.00 30.13  ? 1562 HOH   A O   1 
HETATM 7621 O  O   . HOH   V 6 .   ? 15.012 4.183   31.333  1.00 31.72  ? 1563 HOH   A O   1 
HETATM 7622 O  O   . HOH   V 6 .   ? 4.337  61.019  17.982  1.00 40.93  ? 1564 HOH   A O   1 
HETATM 7623 O  O   . HOH   V 6 .   ? 20.640 23.123  -9.904  1.00 36.40  ? 1565 HOH   A O   1 
HETATM 7624 O  O   . HOH   V 6 .   ? 1.900  21.349  26.147  1.00 44.97  ? 1566 HOH   A O   1 
HETATM 7625 O  O   . HOH   V 6 .   ? 51.797 59.410  0.766   1.00 27.46  ? 1567 HOH   A O   1 
HETATM 7626 O  O   . HOH   V 6 .   ? 28.279 15.358  29.127  1.00 17.22  ? 1568 HOH   A O   1 
HETATM 7627 O  O   . HOH   V 6 .   ? 17.291 42.358  15.795  1.00 31.53  ? 1569 HOH   A O   1 
HETATM 7628 O  O   . HOH   V 6 .   ? 10.814 13.682  7.566   1.00 33.58  ? 1570 HOH   A O   1 
HETATM 7629 O  O   . HOH   V 6 .   ? 29.242 -6.665  25.811  1.00 46.69  ? 1571 HOH   A O   1 
HETATM 7630 O  O   . HOH   V 6 .   ? 13.360 9.355   -3.233  1.00 42.98  ? 1572 HOH   A O   1 
HETATM 7631 O  O   . HOH   V 6 .   ? 18.314 -3.200  11.961  1.00 40.13  ? 1573 HOH   A O   1 
HETATM 7632 O  O   . HOH   V 6 .   ? 23.366 48.561  22.373  1.00 14.65  ? 1574 HOH   A O   1 
HETATM 7633 O  O   . HOH   V 6 .   ? 45.418 -6.421  30.747  1.00 39.11  ? 1575 HOH   A O   1 
HETATM 7634 O  O   . HOH   V 6 .   ? 37.741 15.549  16.558  1.00 14.66  ? 1576 HOH   A O   1 
HETATM 7635 O  O   . HOH   V 6 .   ? 24.296 31.318  10.869  1.00 30.06  ? 1577 HOH   A O   1 
HETATM 7636 O  O   . HOH   V 6 .   ? 36.209 9.778   -6.061  1.00 44.87  ? 1578 HOH   A O   1 
HETATM 7637 O  O   . HOH   V 6 .   ? 47.487 28.682  19.648  1.00 36.67  ? 1579 HOH   A O   1 
HETATM 7638 O  O   . HOH   V 6 .   ? 58.419 35.067  -5.354  1.00 27.64  ? 1580 HOH   A O   1 
HETATM 7639 O  O   . HOH   V 6 .   ? 12.870 23.828  -3.689  1.00 23.07  ? 1581 HOH   A O   1 
HETATM 7640 O  O   . HOH   V 6 .   ? 29.636 3.374   34.430  1.00 28.88  ? 1582 HOH   A O   1 
HETATM 7641 O  O   . HOH   V 6 .   ? 15.661 35.089  12.496  1.00 31.32  ? 1583 HOH   A O   1 
HETATM 7642 O  O   . HOH   V 6 .   ? 9.933  31.229  20.932  1.00 18.82  ? 1584 HOH   A O   1 
HETATM 7643 O  O   . HOH   V 6 .   ? 38.098 55.851  -23.337 1.00 46.24  ? 1585 HOH   A O   1 
HETATM 7644 O  O   . HOH   V 6 .   ? 17.744 9.919   10.984  1.00 15.18  ? 1586 HOH   A O   1 
HETATM 7645 O  O   . HOH   V 6 .   ? 34.199 -4.353  35.096  1.00 39.91  ? 1587 HOH   A O   1 
HETATM 7646 O  O   . HOH   V 6 .   ? 19.844 63.885  15.503  1.00 41.69  ? 1588 HOH   A O   1 
HETATM 7647 O  O   . HOH   V 6 .   ? 31.844 28.680  -13.820 1.00 33.12  ? 1589 HOH   A O   1 
HETATM 7648 O  O   . HOH   V 6 .   ? 25.352 40.863  -7.536  1.00 55.91  ? 1590 HOH   A O   1 
HETATM 7649 O  O   . HOH   V 6 .   ? 28.733 64.414  -3.507  1.00 50.40  ? 1591 HOH   A O   1 
HETATM 7650 O  O   . HOH   V 6 .   ? 18.622 44.170  38.489  1.00 25.42  ? 1592 HOH   A O   1 
HETATM 7651 O  O   . HOH   V 6 .   ? 37.719 51.259  17.651  1.00 22.37  ? 1593 HOH   A O   1 
HETATM 7652 O  O   . HOH   V 6 .   ? 19.012 36.631  15.678  1.00 47.91  ? 1594 HOH   A O   1 
HETATM 7653 O  O   . HOH   V 6 .   ? 36.971 25.458  28.516  1.00 19.06  ? 1595 HOH   A O   1 
HETATM 7654 O  O   . HOH   V 6 .   ? 22.761 15.628  35.170  1.00 39.62  ? 1596 HOH   A O   1 
HETATM 7655 O  O   . HOH   V 6 .   ? 49.404 -12.325 20.970  1.00 33.01  ? 1597 HOH   A O   1 
HETATM 7656 O  O   . HOH   V 6 .   ? 45.931 40.182  17.814  1.00 20.76  ? 1598 HOH   A O   1 
HETATM 7657 O  O   . HOH   V 6 .   ? 13.790 8.708   25.556  1.00 18.94  ? 1599 HOH   A O   1 
HETATM 7658 O  O   . HOH   V 6 .   ? 53.077 54.042  7.550   1.00 36.95  ? 1600 HOH   A O   1 
HETATM 7659 O  O   . HOH   V 6 .   ? 30.435 16.882  31.089  1.00 26.32  ? 1601 HOH   A O   1 
HETATM 7660 O  O   . HOH   V 6 .   ? 19.287 41.559  19.346  1.00 20.09  ? 1602 HOH   A O   1 
HETATM 7661 O  O   . HOH   V 6 .   ? 15.349 63.705  1.275   1.00 34.84  ? 1603 HOH   A O   1 
HETATM 7662 O  O   . HOH   V 6 .   ? 55.894 -3.024  18.815  1.00 47.96  ? 1604 HOH   A O   1 
HETATM 7663 O  O   . HOH   V 6 .   ? 9.202  36.346  29.755  1.00 36.12  ? 1605 HOH   A O   1 
HETATM 7664 O  O   . HOH   V 6 .   ? 28.289 22.637  32.969  1.00 35.69  ? 1606 HOH   A O   1 
HETATM 7665 O  O   . HOH   V 6 .   ? 40.680 48.594  -2.144  1.00 22.58  ? 1607 HOH   A O   1 
HETATM 7666 O  O   . HOH   V 6 .   ? 32.098 43.531  19.167  1.00 42.68  ? 1608 HOH   A O   1 
HETATM 7667 O  O   . HOH   V 6 .   ? 41.272 4.565   7.118   1.00 73.46  ? 1609 HOH   A O   1 
HETATM 7668 O  O   . HOH   V 6 .   ? 36.774 53.580  12.795  1.00 23.58  ? 1610 HOH   A O   1 
HETATM 7669 O  O   . HOH   V 6 .   ? 41.430 20.039  27.119  1.00 39.85  ? 1611 HOH   A O   1 
HETATM 7670 O  O   . HOH   V 6 .   ? 18.761 34.254  10.103  1.00 23.91  ? 1612 HOH   A O   1 
HETATM 7671 O  O   . HOH   V 6 .   ? 48.435 62.340  -16.212 1.00 29.07  ? 1613 HOH   A O   1 
HETATM 7672 O  O   . HOH   V 6 .   ? 51.574 35.325  29.305  1.00 43.13  ? 1614 HOH   A O   1 
HETATM 7673 O  O   . HOH   V 6 .   ? 19.873 60.196  23.754  1.00 43.92  ? 1615 HOH   A O   1 
HETATM 7674 O  O   . HOH   V 6 .   ? 17.444 -0.289  29.366  1.00 37.29  ? 1616 HOH   A O   1 
HETATM 7675 O  O   . HOH   V 6 .   ? 23.331 57.133  22.192  1.00 44.70  ? 1617 HOH   A O   1 
HETATM 7676 O  O   . HOH   V 6 .   ? 34.385 15.424  18.016  1.00 13.84  ? 1618 HOH   A O   1 
HETATM 7677 O  O   . HOH   V 6 .   ? 44.873 54.765  36.694  1.00 16.18  ? 1619 HOH   A O   1 
HETATM 7678 O  O   . HOH   V 6 .   ? 12.551 56.425  31.204  1.00 46.83  ? 1620 HOH   A O   1 
HETATM 7679 O  O   . HOH   V 6 .   ? 32.917 11.023  -4.311  1.00 25.33  ? 1621 HOH   A O   1 
HETATM 7680 O  O   . HOH   V 6 .   ? 7.020  2.695   28.067  1.00 50.31  ? 1622 HOH   A O   1 
HETATM 7681 O  O   . HOH   V 6 .   ? 22.096 36.379  -4.846  1.00 23.38  ? 1623 HOH   A O   1 
HETATM 7682 O  O   . HOH   V 6 .   ? 25.173 -3.349  24.725  1.00 26.16  ? 1624 HOH   A O   1 
HETATM 7683 O  O   . HOH   V 6 .   ? 0.187  39.959  21.262  1.00 41.63  ? 1625 HOH   A O   1 
HETATM 7684 O  O   . HOH   V 6 .   ? 29.271 25.615  35.657  1.00 46.86  ? 1626 HOH   A O   1 
HETATM 7685 O  O   . HOH   V 6 .   ? 19.271 32.786  18.246  1.00 17.00  ? 1627 HOH   A O   1 
HETATM 7686 O  O   . HOH   V 6 .   ? 38.521 46.535  7.496   1.00 27.08  ? 1628 HOH   A O   1 
HETATM 7687 O  O   . HOH   V 6 .   ? 42.235 38.278  -8.149  1.00 22.12  ? 1629 HOH   A O   1 
HETATM 7688 O  O   . HOH   V 6 .   ? 21.134 10.318  5.553   1.00 16.10  ? 1630 HOH   A O   1 
HETATM 7689 O  O   . HOH   V 6 .   ? 23.765 36.545  37.448  1.00 32.14  ? 1631 HOH   A O   1 
HETATM 7690 O  O   . HOH   V 6 .   ? 11.382 11.064  6.993   1.00 33.98  ? 1632 HOH   A O   1 
HETATM 7691 O  O   . HOH   V 6 .   ? 14.514 33.831  36.861  1.00 42.75  ? 1633 HOH   A O   1 
HETATM 7692 O  O   . HOH   V 6 .   ? 46.021 63.819  -2.764  1.00 23.32  ? 1634 HOH   A O   1 
HETATM 7693 O  O   . HOH   V 6 .   ? 28.196 14.708  26.466  1.00 15.84  ? 1635 HOH   A O   1 
HETATM 7694 O  O   . HOH   V 6 .   ? 5.968  16.283  1.939   1.00 50.23  ? 1636 HOH   A O   1 
HETATM 7695 O  O   . HOH   V 6 .   ? 27.904 66.537  -10.836 1.00 49.10  ? 1637 HOH   A O   1 
HETATM 7696 O  O   . HOH   V 6 .   ? 34.419 13.327  7.343   1.00 14.87  ? 1638 HOH   A O   1 
HETATM 7697 O  O   . HOH   V 6 .   ? 26.667 16.906  32.851  1.00 22.67  ? 1639 HOH   A O   1 
HETATM 7698 O  O   . HOH   V 6 .   ? 46.194 19.613  8.076   1.00 23.02  ? 1640 HOH   A O   1 
HETATM 7699 O  O   . HOH   V 6 .   ? 7.358  11.605  5.182   1.00 44.51  ? 1641 HOH   A O   1 
HETATM 7700 O  O   . HOH   V 6 .   ? 50.636 62.288  -13.929 1.00 25.35  ? 1642 HOH   A O   1 
HETATM 7701 O  O   . HOH   V 6 .   ? 43.414 58.212  24.023  1.00 21.88  ? 1643 HOH   A O   1 
HETATM 7702 O  O   . HOH   V 6 .   ? 38.516 24.682  -16.906 1.00 41.39  ? 1644 HOH   A O   1 
HETATM 7703 O  O   . HOH   V 6 .   ? 56.764 35.533  0.962   1.00 29.34  ? 1645 HOH   A O   1 
HETATM 7704 O  O   . HOH   V 6 .   ? 54.397 32.630  -10.590 1.00 32.34  ? 1646 HOH   A O   1 
HETATM 7705 O  O   . HOH   V 6 .   ? 13.940 8.608   12.614  1.00 19.20  ? 1647 HOH   A O   1 
HETATM 7706 O  O   . HOH   V 6 .   ? 43.164 18.333  21.117  1.00 17.95  ? 1648 HOH   A O   1 
HETATM 7707 O  O   . HOH   V 6 .   ? 36.111 51.064  11.767  1.00 37.01  ? 1649 HOH   A O   1 
HETATM 7708 O  O   . HOH   V 6 .   ? 37.966 42.726  -10.134 1.00 35.68  ? 1650 HOH   A O   1 
HETATM 7709 O  O   . HOH   V 6 .   ? 34.005 40.517  18.095  1.00 50.05  ? 1651 HOH   A O   1 
HETATM 7710 O  O   . HOH   V 6 .   ? 33.912 -1.296  36.805  1.00 31.04  ? 1652 HOH   A O   1 
HETATM 7711 O  O   . HOH   V 6 .   ? 56.656 44.654  4.516   1.00 28.86  ? 1653 HOH   A O   1 
HETATM 7712 O  O   . HOH   V 6 .   ? 8.250  14.342  13.119  1.00 27.25  ? 1654 HOH   A O   1 
HETATM 7713 O  O   . HOH   V 6 .   ? 56.593 59.515  -16.687 1.00 41.54  ? 1655 HOH   A O   1 
HETATM 7714 O  O   . HOH   V 6 .   ? 8.694  13.836  0.920   1.00 39.06  ? 1656 HOH   A O   1 
HETATM 7715 O  O   . HOH   V 6 .   ? 10.546 39.412  5.423   1.00 30.31  ? 1657 HOH   A O   1 
HETATM 7716 O  O   . HOH   V 6 .   ? 20.923 53.938  25.384  1.00 26.38  ? 1658 HOH   A O   1 
HETATM 7717 O  O   . HOH   V 6 .   ? 4.498  45.439  6.148   1.00 49.64  ? 1659 HOH   A O   1 
HETATM 7718 O  O   . HOH   V 6 .   ? 3.697  25.083  13.680  1.00 15.36  ? 1660 HOH   A O   1 
HETATM 7719 O  O   . HOH   V 6 .   ? 50.475 32.568  16.878  1.00 43.28  ? 1661 HOH   A O   1 
HETATM 7720 O  O   . HOH   V 6 .   ? 3.437  50.841  6.057   1.00 37.72  ? 1662 HOH   A O   1 
HETATM 7721 O  O   . HOH   V 6 .   ? 55.493 60.263  -4.499  1.00 33.29  ? 1663 HOH   A O   1 
HETATM 7722 O  O   . HOH   V 6 .   ? 48.123 50.778  30.652  1.00 26.58  ? 1664 HOH   A O   1 
HETATM 7723 O  O   . HOH   V 6 .   ? 45.178 -9.449  22.309  1.00 29.03  ? 1665 HOH   A O   1 
HETATM 7724 O  O   . HOH   V 6 .   ? 33.057 -4.502  27.488  1.00 31.34  ? 1666 HOH   A O   1 
HETATM 7725 O  O   . HOH   V 6 .   ? 18.832 59.662  -2.321  1.00 59.80  ? 1667 HOH   A O   1 
HETATM 7726 O  O   . HOH   V 6 .   ? 42.494 19.389  29.332  1.00 55.34  ? 1668 HOH   A O   1 
HETATM 7727 O  O   . HOH   V 6 .   ? 12.961 52.508  32.641  1.00 31.48  ? 1669 HOH   A O   1 
HETATM 7728 O  O   . HOH   V 6 .   ? 41.420 33.154  17.189  1.00 20.78  ? 1670 HOH   A O   1 
HETATM 7729 O  O   . HOH   V 6 .   ? 5.614  31.960  7.557   1.00 27.23  ? 1671 HOH   A O   1 
HETATM 7730 O  O   . HOH   V 6 .   ? 17.350 43.497  10.762  1.00 25.30  ? 1672 HOH   A O   1 
HETATM 7731 O  O   . HOH   V 6 .   ? 1.304  20.318  23.931  1.00 65.83  ? 1673 HOH   A O   1 
HETATM 7732 O  O   . HOH   V 6 .   ? 7.315  5.412   19.525  1.00 44.03  ? 1674 HOH   A O   1 
HETATM 7733 O  O   . HOH   V 6 .   ? 30.516 11.218  -2.622  1.00 30.45  ? 1675 HOH   A O   1 
HETATM 7734 O  O   . HOH   V 6 .   ? 9.612  8.768   2.572   1.00 48.69  ? 1676 HOH   A O   1 
HETATM 7735 O  O   . HOH   V 6 .   ? 44.290 39.726  15.527  1.00 23.79  ? 1677 HOH   A O   1 
HETATM 7736 O  O   . HOH   V 6 .   ? 19.303 24.480  -8.004  1.00 21.22  ? 1678 HOH   A O   1 
HETATM 7737 O  O   . HOH   V 6 .   ? 40.655 16.401  17.292  1.00 15.81  ? 1679 HOH   A O   1 
HETATM 7738 O  O   . HOH   V 6 .   ? 38.737 64.414  27.692  1.00 46.39  ? 1680 HOH   A O   1 
HETATM 7739 O  O   . HOH   V 6 .   ? 27.244 47.420  39.422  1.00 33.41  ? 1681 HOH   A O   1 
HETATM 7740 O  O   . HOH   V 6 .   ? 39.595 66.715  -4.136  1.00 35.96  ? 1682 HOH   A O   1 
HETATM 7741 O  O   . HOH   V 6 .   ? 47.393 37.477  29.684  1.00 24.77  ? 1683 HOH   A O   1 
HETATM 7742 O  O   . HOH   V 6 .   ? 47.034 59.836  10.147  1.00 22.62  ? 1684 HOH   A O   1 
HETATM 7743 O  O   . HOH   V 6 .   ? 15.988 -1.892  27.759  1.00 33.13  ? 1685 HOH   A O   1 
HETATM 7744 O  O   . HOH   V 6 .   ? 53.564 34.359  -13.354 1.00 41.67  ? 1686 HOH   A O   1 
HETATM 7745 O  O   . HOH   V 6 .   ? 53.180 35.483  9.886   1.00 26.38  ? 1687 HOH   A O   1 
HETATM 7746 O  O   . HOH   V 6 .   ? 50.600 59.641  -8.038  1.00 28.73  ? 1688 HOH   A O   1 
HETATM 7747 O  O   . HOH   V 6 .   ? 42.164 16.199  19.683  1.00 14.35  ? 1689 HOH   A O   1 
HETATM 7748 O  O   . HOH   V 6 .   ? 21.112 -3.694  21.161  1.00 37.88  ? 1690 HOH   A O   1 
HETATM 7749 O  O   . HOH   V 6 .   ? 44.105 9.283   7.792   1.00 35.40  ? 1691 HOH   A O   1 
HETATM 7750 O  O   . HOH   V 6 .   ? 23.186 59.266  20.836  1.00 28.90  ? 1692 HOH   A O   1 
HETATM 7751 O  O   . HOH   V 6 .   ? 20.983 28.720  35.448  1.00 47.29  ? 1693 HOH   A O   1 
HETATM 7752 O  O   . HOH   V 6 .   ? 22.868 37.035  -7.584  1.00 27.71  ? 1694 HOH   A O   1 
HETATM 7753 O  O   . HOH   V 6 .   ? 9.685  48.305  35.693  1.00 36.87  ? 1695 HOH   A O   1 
HETATM 7754 O  O   . HOH   V 6 .   ? 8.346  58.625  4.843   1.00 45.15  ? 1696 HOH   A O   1 
HETATM 7755 O  O   . HOH   V 6 .   ? 24.015 65.021  18.511  1.00 25.29  ? 1697 HOH   A O   1 
HETATM 7756 O  O   . HOH   V 6 .   ? 3.139  42.864  16.471  1.00 35.02  ? 1698 HOH   A O   1 
HETATM 7757 O  O   . HOH   V 6 .   ? 59.139 43.155  1.844   1.00 57.98  ? 1699 HOH   A O   1 
HETATM 7758 O  O   . HOH   V 6 .   ? 51.282 23.233  -13.570 1.00 37.84  ? 1700 HOH   A O   1 
HETATM 7759 O  O   . HOH   V 6 .   ? 9.133  -3.464  27.238  1.00 33.40  ? 1701 HOH   A O   1 
HETATM 7760 O  O   . HOH   V 6 .   ? 39.222 54.448  32.207  1.00 29.27  ? 1702 HOH   A O   1 
HETATM 7761 O  O   . HOH   V 6 .   ? 31.048 24.045  -15.913 1.00 38.16  ? 1703 HOH   A O   1 
HETATM 7762 O  O   . HOH   V 6 .   ? 36.133 49.153  36.021  1.00 27.95  ? 1704 HOH   A O   1 
HETATM 7763 O  O   . HOH   V 6 .   ? 29.358 47.225  -6.757  1.00 21.51  ? 1705 HOH   A O   1 
HETATM 7764 O  O   . HOH   V 6 .   ? 33.071 -16.294 15.465  1.00 45.46  ? 1706 HOH   A O   1 
HETATM 7765 O  O   . HOH   V 6 .   ? 34.617 48.584  25.258  1.00 15.14  ? 1707 HOH   A O   1 
HETATM 7766 O  O   . HOH   V 6 .   ? 11.909 58.487  6.943   1.00 24.18  ? 1708 HOH   A O   1 
HETATM 7767 O  O   . HOH   V 6 .   ? 32.084 46.060  21.150  1.00 19.62  ? 1709 HOH   A O   1 
HETATM 7768 O  O   . HOH   V 6 .   ? 12.451 53.387  1.940   1.00 20.08  ? 1710 HOH   A O   1 
HETATM 7769 O  O   . HOH   V 6 .   ? 18.480 23.868  32.883  1.00 62.55  ? 1711 HOH   A O   1 
HETATM 7770 O  O   . HOH   V 6 .   ? 50.764 48.875  26.322  1.00 49.98  ? 1712 HOH   A O   1 
HETATM 7771 O  O   . HOH   V 6 .   ? 44.248 62.327  27.292  1.00 33.33  ? 1713 HOH   A O   1 
HETATM 7772 O  O   . HOH   V 6 .   ? 33.916 44.454  17.305  1.00 39.07  ? 1714 HOH   A O   1 
HETATM 7773 O  O   . HOH   V 6 .   ? 47.735 28.800  23.218  1.00 37.96  ? 1715 HOH   A O   1 
HETATM 7774 O  O   . HOH   V 6 .   ? 54.782 43.362  1.263   1.00 20.65  ? 1716 HOH   A O   1 
HETATM 7775 O  O   . HOH   V 6 .   ? 38.428 3.480   8.125   1.00 37.96  ? 1717 HOH   A O   1 
HETATM 7776 O  O   . HOH   V 6 .   ? 30.379 33.370  -11.552 1.00 40.87  ? 1718 HOH   A O   1 
HETATM 7777 O  O   . HOH   V 6 .   ? 51.964 -2.196  24.308  1.00 38.86  ? 1719 HOH   A O   1 
HETATM 7778 O  O   . HOH   V 6 .   ? 7.225  43.359  13.572  1.00 24.07  ? 1720 HOH   A O   1 
HETATM 7779 O  O   . HOH   V 6 .   ? 35.837 5.705   34.034  1.00 34.25  ? 1721 HOH   A O   1 
HETATM 7780 O  O   . HOH   V 6 .   ? 33.681 47.924  34.106  1.00 22.68  ? 1722 HOH   A O   1 
HETATM 7781 O  O   . HOH   V 6 .   ? 37.727 54.096  27.390  1.00 14.88  ? 1723 HOH   A O   1 
HETATM 7782 O  O   . HOH   V 6 .   ? 49.507 46.505  36.901  1.00 40.98  ? 1724 HOH   A O   1 
HETATM 7783 O  O   . HOH   V 6 .   ? 56.081 28.579  -1.169  1.00 32.35  ? 1725 HOH   A O   1 
HETATM 7784 O  O   . HOH   V 6 .   ? 34.418 33.614  37.872  1.00 23.61  ? 1726 HOH   A O   1 
HETATM 7785 O  O   . HOH   V 6 .   ? 25.336 2.633   35.400  1.00 32.27  ? 1727 HOH   A O   1 
HETATM 7786 O  O   . HOH   V 6 .   ? 37.766 -10.138 14.511  1.00 40.73  ? 1728 HOH   A O   1 
HETATM 7787 O  O   . HOH   V 6 .   ? 15.950 35.050  18.239  1.00 15.73  ? 1729 HOH   A O   1 
HETATM 7788 O  O   . HOH   V 6 .   ? 36.098 34.460  -13.646 1.00 24.35  ? 1730 HOH   A O   1 
HETATM 7789 O  O   . HOH   V 6 .   ? 15.519 56.723  20.792  1.00 29.54  ? 1731 HOH   A O   1 
HETATM 7790 O  O   . HOH   V 6 .   ? 12.919 26.521  28.380  1.00 37.96  ? 1732 HOH   A O   1 
HETATM 7791 O  O   . HOH   V 6 .   ? 50.091 53.410  -26.274 1.00 41.22  ? 1733 HOH   A O   1 
HETATM 7792 O  O   . HOH   V 6 .   ? 27.549 -7.375  22.488  1.00 66.18  ? 1734 HOH   A O   1 
HETATM 7793 O  O   . HOH   V 6 .   ? 9.666  -4.876  18.130  1.00 31.56  ? 1735 HOH   A O   1 
HETATM 7794 O  O   . HOH   V 6 .   ? 48.810 60.187  -23.106 1.00 33.33  ? 1736 HOH   A O   1 
HETATM 7795 O  O   . HOH   V 6 .   ? 26.855 24.998  18.451  1.00 15.27  ? 1737 HOH   A O   1 
HETATM 7796 O  O   . HOH   V 6 .   ? 46.452 14.599  4.207   1.00 40.62  ? 1738 HOH   A O   1 
HETATM 7797 O  O   . HOH   V 6 .   ? 37.037 73.779  20.733  1.00 39.96  ? 1739 HOH   A O   1 
HETATM 7798 O  O   . HOH   V 6 .   ? 4.630  41.638  7.500   1.00 37.38  ? 1740 HOH   A O   1 
HETATM 7799 O  O   . HOH   V 6 .   ? 52.287 61.274  -1.355  1.00 29.17  ? 1741 HOH   A O   1 
HETATM 7800 O  O   . HOH   V 6 .   ? 15.246 30.051  -5.103  1.00 42.98  ? 1742 HOH   A O   1 
HETATM 7801 O  O   . HOH   V 6 .   ? 22.959 7.525   11.806  1.00 15.09  ? 1743 HOH   A O   1 
HETATM 7802 O  O   . HOH   V 6 .   ? 10.785 -5.561  30.635  1.00 37.21  ? 1744 HOH   A O   1 
HETATM 7803 O  O   . HOH   V 6 .   ? 60.557 38.576  1.556   1.00 43.59  ? 1745 HOH   A O   1 
HETATM 7804 O  O   . HOH   V 6 .   ? 15.736 54.187  29.428  1.00 23.41  ? 1746 HOH   A O   1 
HETATM 7805 O  O   . HOH   V 6 .   ? 4.847  47.428  3.571   1.00 31.14  ? 1747 HOH   A O   1 
HETATM 7806 O  O   . HOH   V 6 .   ? 6.177  21.813  32.777  1.00 46.74  ? 1748 HOH   A O   1 
HETATM 7807 O  O   . HOH   V 6 .   ? 37.313 12.506  31.989  1.00 21.49  ? 1749 HOH   A O   1 
HETATM 7808 O  O   . HOH   V 6 .   ? 28.428 62.356  -4.845  1.00 35.87  ? 1750 HOH   A O   1 
HETATM 7809 O  O   . HOH   V 6 .   ? 15.500 -6.211  25.728  1.00 35.00  ? 1751 HOH   A O   1 
HETATM 7810 O  O   . HOH   V 6 .   ? 43.737 37.147  14.186  1.00 36.15  ? 1752 HOH   A O   1 
HETATM 7811 O  O   . HOH   V 6 .   ? 36.091 2.509   7.176   1.00 29.40  ? 1753 HOH   A O   1 
HETATM 7812 O  O   . HOH   V 6 .   ? 22.018 38.305  7.064   1.00 29.08  ? 1754 HOH   A O   1 
HETATM 7813 O  O   . HOH   V 6 .   ? 39.367 54.125  12.026  1.00 25.03  ? 1755 HOH   A O   1 
HETATM 7814 O  O   . HOH   V 6 .   ? 26.314 32.199  17.596  1.00 37.32  ? 1756 HOH   A O   1 
HETATM 7815 O  O   . HOH   V 6 .   ? 27.413 19.676  32.273  1.00 21.59  ? 1757 HOH   A O   1 
HETATM 7816 O  O   . HOH   V 6 .   ? 33.687 47.370  18.412  1.00 29.55  ? 1758 HOH   A O   1 
HETATM 7817 O  O   . HOH   V 6 .   ? 48.274 54.658  17.028  1.00 40.23  ? 1759 HOH   A O   1 
HETATM 7818 O  O   . HOH   V 6 .   ? 34.480 67.151  23.990  1.00 21.07  ? 1760 HOH   A O   1 
HETATM 7819 O  O   . HOH   V 6 .   ? 29.188 6.753   -1.232  1.00 46.23  ? 1761 HOH   A O   1 
HETATM 7820 O  O   . HOH   V 6 .   ? 47.159 45.202  -17.307 1.00 29.44  ? 1762 HOH   A O   1 
HETATM 7821 O  O   . HOH   V 6 .   ? 49.231 58.651  19.486  1.00 28.67  ? 1763 HOH   A O   1 
HETATM 7822 O  O   . HOH   V 6 .   ? 39.591 22.528  26.626  1.00 23.80  ? 1764 HOH   A O   1 
HETATM 7823 O  O   . HOH   V 6 .   ? 27.029 32.491  13.595  1.00 46.92  ? 1765 HOH   A O   1 
HETATM 7824 O  O   . HOH   V 6 .   ? 25.203 38.254  -6.701  1.00 25.98  ? 1766 HOH   A O   1 
HETATM 7825 O  O   . HOH   V 6 .   ? 52.571 64.046  -17.778 1.00 51.51  ? 1767 HOH   A O   1 
HETATM 7826 O  O   . HOH   V 6 .   ? 52.355 7.356   16.650  1.00 33.22  ? 1768 HOH   A O   1 
HETATM 7827 O  O   . HOH   V 6 .   ? 16.824 36.556  14.584  1.00 27.26  ? 1769 HOH   A O   1 
HETATM 7828 O  O   . HOH   V 6 .   ? 43.900 57.833  -8.777  1.00 24.68  ? 1770 HOH   A O   1 
HETATM 7829 O  O   . HOH   V 6 .   ? 52.570 20.286  3.084   1.00 35.89  ? 1771 HOH   A O   1 
HETATM 7830 O  O   . HOH   V 6 .   ? 36.483 -6.404  31.294  1.00 42.04  ? 1772 HOH   A O   1 
HETATM 7831 O  O   . HOH   V 6 .   ? 26.903 46.326  -6.358  1.00 41.48  ? 1773 HOH   A O   1 
HETATM 7832 O  O   . HOH   V 6 .   ? 15.955 66.414  15.482  1.00 30.41  ? 1774 HOH   A O   1 
HETATM 7833 O  O   . HOH   V 6 .   ? -4.219 51.487  18.254  1.00 37.24  ? 1775 HOH   A O   1 
HETATM 7834 O  O   . HOH   V 6 .   ? 25.492 -4.113  18.013  1.00 43.82  ? 1776 HOH   A O   1 
HETATM 7835 O  O   . HOH   V 6 .   ? 6.021  17.837  4.176   1.00 24.33  ? 1777 HOH   A O   1 
HETATM 7836 O  O   . HOH   V 6 .   ? 32.299 5.289   2.697   1.00 26.25  ? 1778 HOH   A O   1 
HETATM 7837 O  O   . HOH   V 6 .   ? 40.133 -1.698  34.613  1.00 28.46  ? 1779 HOH   A O   1 
HETATM 7838 O  O   . HOH   V 6 .   ? 43.756 62.050  -19.100 1.00 41.07  ? 1780 HOH   A O   1 
HETATM 7839 O  O   . HOH   V 6 .   ? 4.948  34.872  17.275  1.00 22.03  ? 1781 HOH   A O   1 
HETATM 7840 O  O   . HOH   V 6 .   ? 54.862 24.361  -0.025  1.00 50.67  ? 1782 HOH   A O   1 
HETATM 7841 O  O   . HOH   V 6 .   ? 20.531 68.771  8.872   1.00 36.42  ? 1783 HOH   A O   1 
HETATM 7842 O  O   . HOH   V 6 .   ? 45.582 39.979  -11.292 1.00 19.28  ? 1784 HOH   A O   1 
HETATM 7843 O  O   . HOH   V 6 .   ? 40.688 56.235  10.955  1.00 19.20  ? 1785 HOH   A O   1 
HETATM 7844 O  O   . HOH   V 6 .   ? 9.637  28.979  -0.061  1.00 38.95  ? 1786 HOH   A O   1 
HETATM 7845 O  O   . HOH   V 6 .   ? 49.277 42.173  33.842  1.00 40.86  ? 1787 HOH   A O   1 
HETATM 7846 O  O   . HOH   V 6 .   ? 51.747 16.386  23.051  1.00 32.77  ? 1788 HOH   A O   1 
HETATM 7847 O  O   . HOH   V 6 .   ? 40.765 7.632   7.679   1.00 23.69  ? 1789 HOH   A O   1 
HETATM 7848 O  O   . HOH   V 6 .   ? 6.280  -4.349  19.855  1.00 47.97  ? 1790 HOH   A O   1 
HETATM 7849 O  O   . HOH   V 6 .   ? 8.792  16.172  -3.043  1.00 25.28  ? 1791 HOH   A O   1 
HETATM 7850 O  O   . HOH   V 6 .   ? 31.384 29.461  20.016  1.00 16.15  ? 1792 HOH   A O   1 
HETATM 7851 O  O   . HOH   V 6 .   ? 50.404 -12.950 27.068  1.00 47.01  ? 1793 HOH   A O   1 
HETATM 7852 O  O   . HOH   V 6 .   ? 34.290 63.934  -11.101 1.00 42.93  ? 1794 HOH   A O   1 
HETATM 7853 O  O   . HOH   V 6 .   ? 22.635 28.407  31.268  1.00 38.82  ? 1795 HOH   A O   1 
HETATM 7854 O  O   . HOH   V 6 .   ? 1.506  55.718  13.373  1.00 56.49  ? 1796 HOH   A O   1 
HETATM 7855 O  O   . HOH   V 6 .   ? 45.410 60.660  -22.628 1.00 37.47  ? 1797 HOH   A O   1 
HETATM 7856 O  O   . HOH   V 6 .   ? 35.857 60.157  -14.979 1.00 36.36  ? 1798 HOH   A O   1 
HETATM 7857 O  O   . HOH   V 6 .   ? 2.182  38.102  12.457  1.00 30.53  ? 1799 HOH   A O   1 
HETATM 7858 O  O   . HOH   V 6 .   ? 27.306 49.878  -8.693  1.00 23.91  ? 1800 HOH   A O   1 
HETATM 7859 O  O   . HOH   V 6 .   ? 14.379 7.723   8.428   1.00 17.76  ? 1801 HOH   A O   1 
HETATM 7860 O  O   . HOH   V 6 .   ? 10.470 -0.868  12.522  1.00 40.38  ? 1802 HOH   A O   1 
HETATM 7861 O  O   . HOH   V 6 .   ? 51.903 49.250  7.671   1.00 24.82  ? 1803 HOH   A O   1 
HETATM 7862 O  O   . HOH   V 6 .   ? 37.841 18.800  -13.072 1.00 29.50  ? 1804 HOH   A O   1 
HETATM 7863 O  O   . HOH   V 6 .   ? 11.796 14.015  30.110  1.00 34.03  ? 1805 HOH   A O   1 
HETATM 7864 O  O   . HOH   V 6 .   ? 61.048 41.684  -4.417  1.00 16.95  ? 1806 HOH   A O   1 
HETATM 7865 O  O   . HOH   V 6 .   ? 10.030 23.153  -6.495  1.00 45.03  ? 1807 HOH   A O   1 
HETATM 7866 O  O   . HOH   V 6 .   ? 34.002 47.128  7.508   1.00 25.46  ? 1808 HOH   A O   1 
HETATM 7867 O  O   . HOH   V 6 .   ? 33.807 51.248  35.291  1.00 24.10  ? 1809 HOH   A O   1 
HETATM 7868 O  O   . HOH   V 6 .   ? 60.999 44.440  -6.227  1.00 20.45  ? 1810 HOH   A O   1 
HETATM 7869 O  O   . HOH   V 6 .   ? 51.077 40.406  -14.711 1.00 26.18  ? 1811 HOH   A O   1 
HETATM 7870 O  O   . HOH   V 6 .   ? 53.375 47.967  -19.070 1.00 20.54  ? 1812 HOH   A O   1 
HETATM 7871 O  O   . HOH   V 6 .   ? 49.734 26.460  19.042  1.00 53.27  ? 1813 HOH   A O   1 
HETATM 7872 O  O   . HOH   V 6 .   ? 35.565 31.386  -16.313 1.00 24.51  ? 1814 HOH   A O   1 
HETATM 7873 O  O   . HOH   V 6 .   ? 4.934  17.011  6.929   1.00 29.33  ? 1815 HOH   A O   1 
HETATM 7874 O  O   . HOH   V 6 .   ? 5.835  22.946  20.426  1.00 20.17  ? 1816 HOH   A O   1 
HETATM 7875 O  O   . HOH   V 6 .   ? 19.096 28.770  28.375  1.00 19.61  ? 1817 HOH   A O   1 
HETATM 7876 O  O   . HOH   V 6 .   ? 8.815  29.664  6.115   1.00 16.48  ? 1818 HOH   A O   1 
HETATM 7877 O  O   . HOH   V 6 .   ? 37.254 31.395  18.509  1.00 22.73  ? 1819 HOH   A O   1 
HETATM 7878 O  O   . HOH   V 6 .   ? 52.736 -0.017  22.530  1.00 45.45  ? 1820 HOH   A O   1 
HETATM 7879 O  O   . HOH   V 6 .   ? 16.741 54.150  -0.007  1.00 26.10  ? 1821 HOH   A O   1 
HETATM 7880 O  O   . HOH   V 6 .   ? 18.539 43.511  -3.171  1.00 33.65  ? 1822 HOH   A O   1 
HETATM 7881 O  O   . HOH   V 6 .   ? 58.072 55.592  -18.096 1.00 20.02  ? 1823 HOH   A O   1 
HETATM 7882 O  O   . HOH   V 6 .   ? 39.053 65.702  30.142  1.00 34.43  ? 1824 HOH   A O   1 
HETATM 7883 O  O   . HOH   V 6 .   ? 45.700 37.618  18.995  1.00 27.05  ? 1825 HOH   A O   1 
HETATM 7884 O  O   . HOH   V 6 .   ? 22.098 35.775  19.563  1.00 26.46  ? 1826 HOH   A O   1 
HETATM 7885 O  O   . HOH   V 6 .   ? 33.344 46.573  -9.569  1.00 28.93  ? 1827 HOH   A O   1 
HETATM 7886 O  O   . HOH   V 6 .   ? 14.021 48.994  37.252  1.00 41.17  ? 1828 HOH   A O   1 
HETATM 7887 O  O   . HOH   V 6 .   ? 6.733  6.991   26.427  1.00 24.64  ? 1829 HOH   A O   1 
HETATM 7888 O  O   . HOH   V 6 .   ? 35.825 8.682   34.393  1.00 45.34  ? 1830 HOH   A O   1 
HETATM 7889 O  O   . HOH   V 6 .   ? 39.154 40.868  -0.493  1.00 29.36  ? 1831 HOH   A O   1 
HETATM 7890 O  O   . HOH   V 6 .   ? 57.645 36.005  -13.495 1.00 35.20  ? 1832 HOH   A O   1 
HETATM 7891 O  O   . HOH   V 6 .   ? 7.280  37.345  3.516   1.00 42.39  ? 1833 HOH   A O   1 
HETATM 7892 O  O   . HOH   V 6 .   ? 33.504 19.117  30.500  1.00 33.53  ? 1834 HOH   A O   1 
HETATM 7893 O  O   . HOH   V 6 .   ? 14.912 15.888  33.561  1.00 39.54  ? 1835 HOH   A O   1 
HETATM 7894 O  O   . HOH   V 6 .   ? 28.303 69.797  21.576  1.00 31.43  ? 1836 HOH   A O   1 
HETATM 7895 O  O   . HOH   V 6 .   ? 38.375 60.625  29.026  1.00 27.29  ? 1837 HOH   A O   1 
HETATM 7896 O  O   . HOH   V 6 .   ? 46.912 60.115  -13.436 1.00 32.31  ? 1838 HOH   A O   1 
HETATM 7897 O  O   . HOH   V 6 .   ? 35.070 51.720  18.574  1.00 17.63  ? 1839 HOH   A O   1 
HETATM 7898 O  O   . HOH   V 6 .   ? 54.402 59.390  -19.424 1.00 28.86  ? 1840 HOH   A O   1 
HETATM 7899 O  O   . HOH   V 6 .   ? 14.686 28.457  28.474  1.00 37.01  ? 1841 HOH   A O   1 
HETATM 7900 O  O   . HOH   V 6 .   ? 46.590 38.313  -16.643 1.00 43.60  ? 1842 HOH   A O   1 
HETATM 7901 O  O   . HOH   V 6 .   ? 38.258 36.470  14.519  1.00 28.73  ? 1843 HOH   A O   1 
HETATM 7902 O  O   . HOH   V 6 .   ? 46.629 -13.632 20.341  1.00 59.45  ? 1844 HOH   A O   1 
HETATM 7903 O  O   . HOH   V 6 .   ? 8.453  3.651   17.114  1.00 32.88  ? 1845 HOH   A O   1 
HETATM 7904 O  O   . HOH   V 6 .   ? 46.391 48.994  38.387  1.00 18.81  ? 1846 HOH   A O   1 
HETATM 7905 O  O   . HOH   V 6 .   ? 31.142 35.335  -9.476  1.00 41.50  ? 1847 HOH   A O   1 
HETATM 7906 O  O   . HOH   V 6 .   ? 16.273 32.555  22.372  1.00 15.74  ? 1848 HOH   A O   1 
HETATM 7907 O  O   . HOH   V 6 .   ? 56.021 54.542  -0.777  1.00 50.12  ? 1849 HOH   A O   1 
HETATM 7908 O  O   . HOH   V 6 .   ? 41.113 49.926  16.743  1.00 33.41  ? 1850 HOH   A O   1 
HETATM 7909 O  O   . HOH   V 6 .   ? 27.077 52.843  -9.195  1.00 33.15  ? 1851 HOH   A O   1 
HETATM 7910 O  O   . HOH   V 6 .   ? 37.895 32.161  23.187  1.00 15.69  ? 1852 HOH   A O   1 
HETATM 7911 O  O   . HOH   V 6 .   ? 24.868 48.971  19.995  1.00 17.31  ? 1853 HOH   A O   1 
HETATM 7912 O  O   . HOH   V 6 .   ? 23.728 -3.769  13.598  1.00 55.12  ? 1854 HOH   A O   1 
HETATM 7913 O  O   . HOH   V 6 .   ? 12.650 13.123  -7.664  1.00 51.77  ? 1855 HOH   A O   1 
HETATM 7914 O  O   . HOH   V 6 .   ? 47.146 63.414  4.262   1.00 24.21  ? 1856 HOH   A O   1 
HETATM 7915 O  O   . HOH   V 6 .   ? 35.862 52.241  -20.814 1.00 26.19  ? 1857 HOH   A O   1 
HETATM 7916 O  O   . HOH   V 6 .   ? 45.840 26.594  25.701  1.00 50.33  ? 1858 HOH   A O   1 
HETATM 7917 O  O   . HOH   V 6 .   ? 14.157 49.996  12.112  1.00 14.81  ? 1859 HOH   A O   1 
HETATM 7918 O  O   . HOH   V 6 .   ? 22.050 64.413  3.741   1.00 27.15  ? 1860 HOH   A O   1 
HETATM 7919 O  O   . HOH   V 6 .   ? 44.779 30.506  28.841  1.00 22.24  ? 1861 HOH   A O   1 
HETATM 7920 O  O   . HOH   V 6 .   ? 20.127 9.776   -4.543  1.00 45.33  ? 1862 HOH   A O   1 
HETATM 7921 O  O   . HOH   V 6 .   ? 27.504 39.566  38.475  1.00 25.24  ? 1863 HOH   A O   1 
HETATM 7922 O  O   . HOH   V 6 .   ? 49.134 18.352  16.902  1.00 35.18  ? 1864 HOH   A O   1 
HETATM 7923 O  O   . HOH   V 6 .   ? 51.773 51.127  -22.748 1.00 30.50  ? 1865 HOH   A O   1 
HETATM 7924 O  O   . HOH   V 6 .   ? 30.058 35.210  41.181  1.00 60.05  ? 1866 HOH   A O   1 
HETATM 7925 O  O   . HOH   V 6 .   ? 44.308 5.662   35.560  1.00 40.40  ? 1867 HOH   A O   1 
HETATM 7926 O  O   . HOH   V 6 .   ? 49.992 25.019  -7.522  1.00 38.69  ? 1868 HOH   A O   1 
HETATM 7927 O  O   . HOH   V 6 .   ? 18.095 -5.377  20.943  1.00 63.12  ? 1869 HOH   A O   1 
HETATM 7928 O  O   . HOH   V 6 .   ? 45.977 57.683  13.377  1.00 21.84  ? 1870 HOH   A O   1 
HETATM 7929 O  O   . HOH   V 6 .   ? 51.880 -9.435  14.921  1.00 31.39  ? 1871 HOH   A O   1 
HETATM 7930 O  O   . HOH   V 6 .   ? 45.430 63.500  -16.836 1.00 44.14  ? 1872 HOH   A O   1 
HETATM 7931 O  O   . HOH   V 6 .   ? 44.676 42.786  -18.227 1.00 22.46  ? 1873 HOH   A O   1 
HETATM 7932 O  O   . HOH   V 6 .   ? 50.258 21.711  3.248   1.00 21.58  ? 1874 HOH   A O   1 
HETATM 7933 O  O   . HOH   V 6 .   ? 40.215 62.193  28.062  1.00 37.13  ? 1875 HOH   A O   1 
HETATM 7934 O  O   . HOH   V 6 .   ? 9.416  4.005   28.942  1.00 53.86  ? 1876 HOH   A O   1 
HETATM 7935 O  O   . HOH   V 6 .   ? 7.708  46.163  -2.735  1.00 41.36  ? 1877 HOH   A O   1 
HETATM 7936 O  O   . HOH   V 6 .   ? 12.939 31.917  25.047  1.00 24.45  ? 1878 HOH   A O   1 
HETATM 7937 O  O   . HOH   V 6 .   ? 11.240 50.798  -1.191  1.00 29.69  ? 1879 HOH   A O   1 
HETATM 7938 O  O   . HOH   V 6 .   ? 37.022 18.710  33.166  1.00 53.94  ? 1880 HOH   A O   1 
HETATM 7939 O  O   . HOH   V 6 .   ? 33.077 41.425  -8.814  1.00 50.54  ? 1881 HOH   A O   1 
HETATM 7940 O  O   . HOH   V 6 .   ? 35.854 20.168  28.464  1.00 39.38  ? 1882 HOH   A O   1 
HETATM 7941 O  O   . HOH   V 6 .   ? 11.253 41.166  0.792   1.00 40.98  ? 1883 HOH   A O   1 
HETATM 7942 O  O   . HOH   V 6 .   ? 17.448 30.775  17.959  1.00 14.41  ? 1884 HOH   A O   1 
HETATM 7943 O  O   . HOH   V 6 .   ? 17.320 3.347   35.134  1.00 38.93  ? 1885 HOH   A O   1 
HETATM 7944 O  O   . HOH   V 6 .   ? 29.326 27.067  -13.491 1.00 36.78  ? 1886 HOH   A O   1 
HETATM 7945 O  O   . HOH   V 6 .   ? 1.967  31.304  24.656  1.00 50.41  ? 1887 HOH   A O   1 
HETATM 7946 O  O   . HOH   V 6 .   ? 43.633 10.868  4.016   1.00 23.37  ? 1888 HOH   A O   1 
HETATM 7947 O  O   . HOH   V 6 .   ? 18.617 35.489  17.998  1.00 21.34  ? 1889 HOH   A O   1 
HETATM 7948 O  O   . HOH   V 6 .   ? 25.648 46.703  18.623  1.00 23.18  ? 1890 HOH   A O   1 
HETATM 7949 O  O   . HOH   V 6 .   ? 7.601  50.750  -3.681  1.00 49.55  ? 1891 HOH   A O   1 
HETATM 7950 O  O   . HOH   V 6 .   ? 29.802 44.805  15.352  1.00 44.58  ? 1892 HOH   A O   1 
HETATM 7951 O  O   . HOH   V 6 .   ? 35.475 25.151  32.848  1.00 35.07  ? 1893 HOH   A O   1 
HETATM 7952 O  O   . HOH   V 6 .   ? 21.810 61.790  2.654   1.00 22.43  ? 1894 HOH   A O   1 
HETATM 7953 O  O   . HOH   V 6 .   ? 36.296 43.706  -17.711 1.00 23.26  ? 1895 HOH   A O   1 
HETATM 7954 O  O   . HOH   V 6 .   ? 50.689 24.546  22.733  1.00 39.74  ? 1896 HOH   A O   1 
HETATM 7955 O  O   . HOH   V 6 .   ? 10.681 28.227  24.872  1.00 32.69  ? 1897 HOH   A O   1 
HETATM 7956 O  O   . HOH   V 6 .   ? 43.136 37.312  16.533  1.00 43.65  ? 1898 HOH   A O   1 
HETATM 7957 O  O   . HOH   V 6 .   ? 28.115 72.989  18.712  1.00 48.77  ? 1899 HOH   A O   1 
HETATM 7958 O  O   . HOH   V 6 .   ? 15.149 58.258  24.645  1.00 34.27  ? 1900 HOH   A O   1 
HETATM 7959 O  O   . HOH   V 6 .   ? 45.268 13.988  34.001  1.00 42.62  ? 1901 HOH   A O   1 
HETATM 7960 O  O   . HOH   V 6 .   ? 2.509  18.748  19.777  1.00 25.12  ? 1902 HOH   A O   1 
HETATM 7961 O  O   . HOH   V 6 .   ? 22.264 6.850   -0.886  1.00 47.56  ? 1903 HOH   A O   1 
HETATM 7962 O  O   . HOH   V 6 .   ? 37.301 38.882  15.843  1.00 48.15  ? 1904 HOH   A O   1 
HETATM 7963 O  O   . HOH   V 6 .   ? 27.462 37.381  -7.738  1.00 33.34  ? 1905 HOH   A O   1 
HETATM 7964 O  O   . HOH   V 6 .   ? 20.125 46.915  12.463  1.00 39.61  ? 1906 HOH   A O   1 
HETATM 7965 O  O   . HOH   V 6 .   ? 33.865 41.186  -3.692  1.00 40.78  ? 1907 HOH   A O   1 
HETATM 7966 O  O   . HOH   V 6 .   ? 48.672 58.068  -7.121  1.00 30.26  ? 1908 HOH   A O   1 
HETATM 7967 O  O   . HOH   V 6 .   ? 47.500 9.522   13.246  1.00 40.09  ? 1909 HOH   A O   1 
HETATM 7968 O  O   . HOH   V 6 .   ? 37.465 41.632  38.626  1.00 28.81  ? 1910 HOH   A O   1 
HETATM 7969 O  O   . HOH   V 6 .   ? 49.825 41.890  26.090  1.00 35.44  ? 1911 HOH   A O   1 
HETATM 7970 O  O   . HOH   V 6 .   ? 36.836 54.197  30.082  1.00 26.30  ? 1912 HOH   A O   1 
HETATM 7971 O  O   . HOH   V 6 .   ? 29.197 39.918  20.040  1.00 33.02  ? 1913 HOH   A O   1 
HETATM 7972 O  O   . HOH   V 6 .   ? 9.866  37.846  34.429  1.00 45.14  ? 1914 HOH   A O   1 
HETATM 7973 O  O   . HOH   V 6 .   ? 31.902 33.327  14.498  1.00 98.45  ? 1915 HOH   A O   1 
HETATM 7974 O  O   . HOH   V 6 .   ? 13.767 32.383  -4.511  1.00 40.63  ? 1916 HOH   A O   1 
HETATM 7975 O  O   . HOH   V 6 .   ? 29.834 30.437  17.967  1.00 27.93  ? 1917 HOH   A O   1 
HETATM 7976 O  O   . HOH   V 6 .   ? 15.709 56.677  28.496  1.00 27.94  ? 1918 HOH   A O   1 
HETATM 7977 O  O   . HOH   V 6 .   ? 26.669 30.977  7.348   1.00 38.46  ? 1919 HOH   A O   1 
HETATM 7978 O  O   . HOH   V 6 .   ? 7.181  20.240  0.795   1.00 27.73  ? 1920 HOH   A O   1 
HETATM 7979 O  O   . HOH   V 6 .   ? 7.928  41.665  5.615   1.00 41.36  ? 1921 HOH   A O   1 
HETATM 7980 O  O   . HOH   V 6 .   ? 21.596 38.555  -9.407  1.00 34.36  ? 1922 HOH   A O   1 
HETATM 7981 O  O   . HOH   V 6 .   ? 42.871 16.709  23.325  1.00 17.55  ? 1923 HOH   A O   1 
HETATM 7982 O  O   . HOH   V 6 .   ? 47.610 35.896  19.983  1.00 33.39  ? 1924 HOH   A O   1 
HETATM 7983 O  O   . HOH   V 6 .   ? 29.926 33.213  18.057  1.00 46.25  ? 1925 HOH   A O   1 
HETATM 7984 O  O   . HOH   V 6 .   ? 46.765 28.674  38.630  1.00 46.90  ? 1926 HOH   A O   1 
HETATM 7985 O  O   . HOH   V 6 .   ? -5.560 40.674  22.799  1.00 45.92  ? 1927 HOH   A O   1 
HETATM 7986 O  O   . HOH   V 6 .   ? 45.202 61.196  -10.622 1.00 50.45  ? 1928 HOH   A O   1 
HETATM 7987 O  O   . HOH   V 6 .   ? 25.118 48.946  -7.423  1.00 46.41  ? 1929 HOH   A O   1 
HETATM 7988 O  O   . HOH   V 6 .   ? 31.213 48.571  -16.824 1.00 58.21  ? 1930 HOH   A O   1 
HETATM 7989 O  O   . HOH   V 6 .   ? 38.372 5.770   33.577  1.00 46.78  ? 1931 HOH   A O   1 
HETATM 7990 O  O   . HOH   V 6 .   ? 38.717 6.429   1.866   1.00 39.50  ? 1932 HOH   A O   1 
HETATM 7991 O  O   . HOH   V 6 .   ? 48.678 21.953  25.159  1.00 46.78  ? 1933 HOH   A O   1 
HETATM 7992 O  O   . HOH   V 6 .   ? 25.989 4.460   3.635   1.00 49.30  ? 1934 HOH   A O   1 
HETATM 7993 O  O   . HOH   V 6 .   ? 46.461 -0.320  11.255  1.00 32.08  ? 1935 HOH   A O   1 
HETATM 7994 O  O   . HOH   V 6 .   ? 11.828 38.955  3.265   1.00 43.08  ? 1936 HOH   A O   1 
HETATM 7995 O  O   . HOH   V 6 .   ? -2.264 40.708  20.222  1.00 50.02  ? 1937 HOH   A O   1 
HETATM 7996 O  O   . HOH   V 6 .   ? 46.871 39.946  29.620  1.00 31.10  ? 1938 HOH   A O   1 
HETATM 7997 O  O   . HOH   V 6 .   ? 39.282 35.985  18.651  1.00 30.57  ? 1939 HOH   A O   1 
HETATM 7998 O  O   . HOH   V 6 .   ? 52.202 60.864  -22.369 1.00 53.53  ? 1940 HOH   A O   1 
HETATM 7999 O  O   . HOH   V 6 .   ? 31.916 32.378  37.760  1.00 20.59  ? 1941 HOH   A O   1 
HETATM 8000 O  O   . HOH   V 6 .   ? 11.644 8.267   5.168   1.00 31.21  ? 1942 HOH   A O   1 
HETATM 8001 O  O   . HOH   V 6 .   ? 6.824  55.189  31.932  1.00 25.25  ? 1943 HOH   A O   1 
HETATM 8002 O  O   . HOH   V 6 .   ? 44.948 11.686  6.458   1.00 36.57  ? 1944 HOH   A O   1 
HETATM 8003 O  O   . HOH   V 6 .   ? 28.386 66.593  3.125   1.00 44.65  ? 1945 HOH   A O   1 
HETATM 8004 O  O   . HOH   V 6 .   ? 29.246 14.078  -1.801  1.00 27.67  ? 1946 HOH   A O   1 
HETATM 8005 O  O   . HOH   V 6 .   ? 3.864  20.988  21.265  1.00 46.62  ? 1947 HOH   A O   1 
HETATM 8006 O  O   . HOH   V 6 .   ? 47.163 5.966   34.586  1.00 61.51  ? 1948 HOH   A O   1 
HETATM 8007 O  O   . HOH   V 6 .   ? 42.175 22.819  26.059  1.00 24.12  ? 1949 HOH   A O   1 
HETATM 8008 O  O   . HOH   V 6 .   ? 21.001 39.717  15.411  1.00 54.12  ? 1950 HOH   A O   1 
HETATM 8009 O  O   . HOH   V 6 .   ? 32.083 68.502  0.000   1.00 50.55  ? 1951 HOH   A O   1 
HETATM 8010 O  O   . HOH   V 6 .   ? 33.305 25.123  -16.289 1.00 47.30  ? 1952 HOH   A O   1 
HETATM 8011 O  O   . HOH   V 6 .   ? 42.190 25.436  31.569  1.00 53.08  ? 1953 HOH   A O   1 
HETATM 8012 O  O   . HOH   V 6 .   ? 50.341 20.745  16.118  1.00 36.95  ? 1954 HOH   A O   1 
HETATM 8013 O  O   . HOH   V 6 .   ? 1.511  29.692  14.996  1.00 32.80  ? 1955 HOH   A O   1 
HETATM 8014 O  O   . HOH   V 6 .   ? 9.493  16.647  27.844  1.00 27.65  ? 1956 HOH   A O   1 
HETATM 8015 O  O   . HOH   V 6 .   ? 40.304 1.809   8.527   1.00 52.43  ? 1957 HOH   A O   1 
HETATM 8016 O  O   . HOH   V 6 .   ? 31.953 41.122  19.668  1.00 34.51  ? 1958 HOH   A O   1 
HETATM 8017 O  O   . HOH   V 6 .   ? 30.271 10.973  34.567  1.00 50.01  ? 1959 HOH   A O   1 
HETATM 8018 O  O   . HOH   V 6 .   ? 28.711 42.867  4.025   1.00 47.78  ? 1960 HOH   A O   1 
HETATM 8019 O  O   . HOH   V 6 .   ? 49.568 41.456  -16.897 1.00 43.50  ? 1961 HOH   A O   1 
HETATM 8020 O  O   . HOH   V 6 .   ? 52.360 24.191  0.056   1.00 42.17  ? 1962 HOH   A O   1 
HETATM 8021 O  O   . HOH   V 6 .   ? 31.622 -17.876 17.288  1.00 51.29  ? 1963 HOH   A O   1 
HETATM 8022 O  O   . HOH   V 6 .   ? 17.504 30.649  -10.117 1.00 48.34  ? 1964 HOH   A O   1 
HETATM 8023 O  O   . HOH   V 6 .   ? 8.107  29.441  1.691   1.00 39.74  ? 1965 HOH   A O   1 
HETATM 8024 O  O   . HOH   V 6 .   ? 53.981 -0.399  20.223  1.00 42.58  ? 1966 HOH   A O   1 
HETATM 8025 O  O   . HOH   V 6 .   ? 50.764 53.695  14.706  1.00 51.53  ? 1967 HOH   A O   1 
HETATM 8026 O  O   . HOH   V 6 .   ? 46.033 16.284  -7.408  1.00 48.37  ? 1968 HOH   A O   1 
HETATM 8027 O  O   . HOH   V 6 .   ? 24.848 53.758  -7.818  1.00 33.81  ? 1969 HOH   A O   1 
HETATM 8028 O  O   . HOH   V 6 .   ? 33.820 49.495  17.348  1.00 23.23  ? 1970 HOH   A O   1 
HETATM 8029 O  O   . HOH   V 6 .   ? 33.699 33.390  12.473  1.00 46.32  ? 1971 HOH   A O   1 
HETATM 8030 O  O   . HOH   V 6 .   ? 43.232 17.790  25.918  1.00 27.49  ? 1972 HOH   A O   1 
HETATM 8031 O  O   . HOH   V 6 .   ? 22.175 -4.756  23.247  1.00 46.85  ? 1973 HOH   A O   1 
HETATM 8032 O  O   . HOH   V 6 .   ? 32.329 53.828  -18.655 1.00 73.41  ? 1974 HOH   A O   1 
HETATM 8033 O  O   . HOH   V 6 .   ? 26.255 33.087  6.826   1.00 42.17  ? 1975 HOH   A O   1 
HETATM 8034 O  O   . HOH   V 6 .   ? 37.155 57.818  30.405  1.00 34.99  ? 1976 HOH   A O   1 
HETATM 8035 O  O   . HOH   V 6 .   ? 29.479 49.735  36.790  1.00 45.34  ? 1977 HOH   A O   1 
HETATM 8036 O  O   . HOH   V 6 .   ? 39.234 -5.824  33.291  1.00 68.29  ? 1978 HOH   A O   1 
HETATM 8037 O  O   . HOH   V 6 .   ? 42.093 34.275  -15.847 1.00 38.95  ? 1979 HOH   A O   1 
HETATM 8038 O  O   . HOH   V 6 .   ? 24.579 5.851   1.818   1.00 46.42  ? 1980 HOH   A O   1 
HETATM 8039 O  O   . HOH   V 6 .   ? 34.345 34.633  14.696  1.00 52.54  ? 1981 HOH   A O   1 
HETATM 8040 O  O   . HOH   V 6 .   ? 53.001 51.358  6.728   1.00 38.57  ? 1982 HOH   A O   1 
HETATM 8041 O  O   . HOH   V 6 .   ? 31.870 59.904  30.289  1.00 55.78  ? 1983 HOH   A O   1 
HETATM 8042 O  O   . HOH   V 6 .   ? 24.307 41.939  5.213   1.00 46.83  ? 1984 HOH   A O   1 
HETATM 8043 O  O   . HOH   V 6 .   ? 35.880 33.890  16.758  1.00 41.78  ? 1985 HOH   A O   1 
HETATM 8044 O  O   . HOH   V 6 .   ? 51.695 22.934  -7.117  1.00 42.54  ? 1986 HOH   A O   1 
HETATM 8045 O  O   . HOH   V 6 .   ? 31.839 -6.774  26.773  1.00 39.85  ? 1987 HOH   A O   1 
HETATM 8046 O  O   . HOH   V 6 .   ? 22.377 47.525  38.432  1.00 41.63  ? 1988 HOH   A O   1 
HETATM 8047 O  O   . HOH   V 6 .   ? 50.223 24.815  10.226  1.00 26.61  ? 1989 HOH   A O   1 
HETATM 8048 O  O   . HOH   V 6 .   ? 29.426 43.090  40.023  1.00 56.80  ? 1990 HOH   A O   1 
HETATM 8049 O  O   . HOH   V 6 .   ? 4.757  43.801  14.584  1.00 57.19  ? 1991 HOH   A O   1 
HETATM 8050 O  O   . HOH   V 6 .   ? 43.263 58.131  27.144  1.00 24.51  ? 1992 HOH   A O   1 
HETATM 8051 O  O   . HOH   V 6 .   ? 49.043 21.607  14.135  1.00 25.50  ? 1993 HOH   A O   1 
HETATM 8052 O  O   . HOH   V 6 .   ? 20.533 27.389  30.341  1.00 48.28  ? 1994 HOH   A O   1 
HETATM 8053 O  O   . HOH   V 6 .   ? 50.240 24.108  20.096  1.00 52.61  ? 1995 HOH   A O   1 
HETATM 8054 O  O   . HOH   V 6 .   ? 23.029 40.896  7.114   1.00 53.99  ? 1996 HOH   A O   1 
HETATM 8055 O  O   . HOH   V 6 .   ? 38.282 33.725  37.796  1.00 63.56  ? 1997 HOH   A O   1 
HETATM 8056 O  O   . HOH   V 6 .   ? 36.881 49.939  13.996  1.00 69.01  ? 1998 HOH   A O   1 
HETATM 8057 O  O   . HOH   V 6 .   ? 34.472 20.637  32.815  1.00 45.00  ? 1999 HOH   A O   1 
HETATM 8058 O  O   . HOH   V 6 .   ? 26.964 46.389  12.572  1.00 58.70  ? 2000 HOH   A O   1 
HETATM 8059 O  O   . HOH   V 6 .   ? 5.287  30.979  9.869   1.00 23.05  ? 2001 HOH   A O   1 
HETATM 8060 O  O   . HOH   V 6 .   ? 53.810 59.250  -24.216 1.00 42.62  ? 2002 HOH   A O   1 
HETATM 8061 O  O   . HOH   V 6 .   ? 32.641 37.253  -8.679  1.00 36.29  ? 2003 HOH   A O   1 
HETATM 8062 O  O   . HOH   V 6 .   ? 8.869  7.777   17.448  1.00 35.21  ? 2004 HOH   A O   1 
HETATM 8063 O  O   . HOH   V 6 .   ? 3.649  43.792  8.485   1.00 47.77  ? 2005 HOH   A O   1 
HETATM 8064 O  O   . HOH   V 6 .   ? 49.906 18.502  13.047  1.00 58.46  ? 2006 HOH   A O   1 
HETATM 8065 O  O   . HOH   V 6 .   ? 55.689 41.743  -14.248 1.00 30.45  ? 2007 HOH   A O   1 
HETATM 8066 O  O   . HOH   V 6 .   ? 51.625 20.802  -8.362  1.00 47.76  ? 2008 HOH   A O   1 
HETATM 8067 O  O   . HOH   V 6 .   ? 53.177 -5.475  22.757  1.00 58.70  ? 2009 HOH   A O   1 
HETATM 8068 O  O   . HOH   V 6 .   ? 30.653 61.979  28.340  1.00 31.87  ? 2010 HOH   A O   1 
HETATM 8069 O  O   . HOH   V 6 .   ? 27.953 51.754  35.666  1.00 51.27  ? 2011 HOH   A O   1 
HETATM 8070 O  O   . HOH   V 6 .   ? 22.108 9.132   -2.772  1.00 45.19  ? 2012 HOH   A O   1 
HETATM 8071 O  O   . HOH   V 6 .   ? 39.394 40.440  -9.250  1.00 30.77  ? 2013 HOH   A O   1 
HETATM 8072 O  O   . HOH   V 6 .   ? 26.760 43.972  5.458   1.00 60.38  ? 2014 HOH   A O   1 
HETATM 8073 O  O   . HOH   V 6 .   ? 48.896 38.313  36.929  1.00 45.70  ? 2015 HOH   A O   1 
HETATM 8074 O  O   . HOH   V 6 .   ? 29.901 33.822  -8.070  1.00 35.34  ? 2016 HOH   A O   1 
HETATM 8075 O  O   . HOH   V 6 .   ? 31.241 41.088  -6.402  1.00 61.36  ? 2017 HOH   A O   1 
HETATM 8076 O  O   . HOH   V 6 .   ? 12.704 30.839  27.345  1.00 56.00  ? 2018 HOH   A O   1 
HETATM 8077 O  O   . HOH   V 6 .   ? 22.759 62.232  18.876  1.00 56.69  ? 2019 HOH   A O   1 
HETATM 8078 O  O   . HOH   V 6 .   ? 40.234 13.826  -9.810  1.00 61.46  ? 2020 HOH   A O   1 
HETATM 8079 O  O   . HOH   V 6 .   ? 22.534 63.484  16.697  1.00 36.33  ? 2021 HOH   A O   1 
HETATM 8080 O  O   . HOH   V 6 .   ? 31.675 36.442  11.070  1.00 67.11  ? 2022 HOH   A O   1 
HETATM 8081 O  O   . HOH   V 6 .   ? 27.093 45.166  15.031  1.00 62.89  ? 2023 HOH   A O   1 
HETATM 8082 O  O   . HOH   V 6 .   ? 44.276 50.741  -19.406 1.00 17.22  ? 2024 HOH   A O   1 
HETATM 8083 O  O   . HOH   V 6 .   ? 24.191 58.897  24.056  1.00 37.02  ? 2025 HOH   A O   1 
HETATM 8084 O  O   . HOH   V 6 .   ? 36.555 33.429  39.752  1.00 35.48  ? 2026 HOH   A O   1 
HETATM 8085 O  O   . HOH   V 6 .   ? 46.386 10.708  8.085   1.00 61.32  ? 2027 HOH   A O   1 
HETATM 8086 O  O   . HOH   V 6 .   ? 20.437 42.351  17.134  1.00 42.32  ? 2028 HOH   A O   1 
HETATM 8087 O  O   . HOH   V 6 .   ? 40.754 40.138  -7.461  1.00 47.41  ? 2029 HOH   A O   1 
HETATM 8088 O  O   . HOH   V 6 .   ? 46.008 32.923  -14.571 1.00 41.54  ? 2030 HOH   A O   1 
HETATM 8089 O  O   . HOH   V 6 .   ? 26.365 33.871  -10.390 1.00 49.32  ? 2031 HOH   A O   1 
HETATM 8090 O  O   . HOH   V 6 .   ? 32.538 69.787  9.196   1.00 43.43  ? 2032 HOH   A O   1 
HETATM 8091 O  O   . HOH   V 6 .   ? 20.064 46.222  15.102  1.00 63.48  ? 2033 HOH   A O   1 
HETATM 8092 O  O   . HOH   V 6 .   ? 50.741 33.680  14.644  1.00 32.21  ? 2034 HOH   A O   1 
HETATM 8093 O  O   . HOH   V 6 .   ? 57.211 56.979  -9.483  1.00 40.06  ? 2035 HOH   A O   1 
HETATM 8094 O  O   . HOH   V 6 .   ? 6.947  13.720  17.349  1.00 44.09  ? 2036 HOH   A O   1 
HETATM 8095 O  O   . HOH   V 6 .   ? 41.911 6.173   3.562   1.00 46.44  ? 2037 HOH   A O   1 
HETATM 8096 O  O   . HOH   V 6 .   ? 32.474 45.205  15.204  1.00 56.84  ? 2038 HOH   A O   1 
HETATM 8097 O  O   . HOH   V 6 .   ? 35.028 57.001  -16.507 1.00 48.09  ? 2039 HOH   A O   1 
HETATM 8098 O  O   . HOH   V 6 .   ? 31.464 45.589  -7.834  1.00 32.77  ? 2040 HOH   A O   1 
HETATM 8099 O  O   . HOH   V 6 .   ? 24.649 25.623  32.759  1.00 30.65  ? 2041 HOH   A O   1 
HETATM 8100 O  O   . HOH   V 6 .   ? 23.402 14.273  -8.477  1.00 31.56  ? 2042 HOH   A O   1 
HETATM 8101 O  O   . HOH   V 6 .   ? 12.345 63.332  1.615   1.00 49.89  ? 2043 HOH   A O   1 
HETATM 8102 O  O   . HOH   V 6 .   ? 7.263  9.321   18.653  1.00 65.13  ? 2044 HOH   A O   1 
HETATM 8103 O  O   . HOH   V 6 .   ? 29.870 41.905  6.517   1.00 66.05  ? 2045 HOH   A O   1 
HETATM 8104 O  O   . HOH   V 6 .   ? 22.557 4.217   2.977   1.00 49.80  ? 2046 HOH   A O   1 
HETATM 8105 O  O   . HOH   V 6 .   ? 20.683 60.535  -0.967  1.00 49.06  ? 2047 HOH   A O   1 
HETATM 8106 O  O   . HOH   V 6 .   ? 21.582 37.417  9.513   1.00 48.92  ? 2048 HOH   A O   1 
HETATM 8107 O  O   . HOH   V 6 .   ? 39.206 16.879  32.429  1.00 44.97  ? 2049 HOH   A O   1 
HETATM 8108 O  O   . HOH   V 6 .   ? 0.555  30.671  11.412  1.00 20.57  ? 2050 HOH   A O   1 
HETATM 8109 O  O   . HOH   V 6 .   ? 31.644 20.321  30.042  1.00 36.93  ? 2051 HOH   A O   1 
HETATM 8110 O  O   . HOH   V 6 .   ? 3.090  37.608  4.847   1.00 47.56  ? 2052 HOH   A O   1 
HETATM 8111 O  O   . HOH   V 6 .   ? 13.661 2.051   31.622  1.00 52.65  ? 2053 HOH   A O   1 
HETATM 8112 O  O   . HOH   V 6 .   ? 27.441 66.592  7.303   1.00 37.34  ? 2054 HOH   A O   1 
HETATM 8113 O  O   . HOH   V 6 .   ? 51.083 22.388  12.093  1.00 40.22  ? 2055 HOH   A O   1 
HETATM 8114 O  O   . HOH   V 6 .   ? 39.765 66.498  0.383   1.00 42.66  ? 2056 HOH   A O   1 
HETATM 8115 O  O   . HOH   V 6 .   ? 3.125  46.143  30.595  1.00 37.50  ? 2057 HOH   A O   1 
HETATM 8116 O  O   . HOH   V 6 .   ? 38.139 59.784  -20.825 1.00 48.48  ? 2058 HOH   A O   1 
HETATM 8117 O  O   . HOH   V 6 .   ? 42.492 40.763  38.474  1.00 30.03  ? 2059 HOH   A O   1 
HETATM 8118 O  O   . HOH   V 6 .   ? 46.100 67.974  16.986  1.00 42.29  ? 2060 HOH   A O   1 
HETATM 8119 O  O   . HOH   V 6 .   ? 22.959 43.417  16.717  1.00 40.54  ? 2061 HOH   A O   1 
HETATM 8120 O  O   . HOH   V 6 .   ? 48.929 48.385  30.730  1.00 39.28  ? 2062 HOH   A O   1 
HETATM 8121 O  O   . HOH   V 6 .   ? 35.885 38.087  17.939  1.00 47.91  ? 2063 HOH   A O   1 
HETATM 8122 O  O   . HOH   V 6 .   ? 48.932 61.596  -11.996 1.00 30.47  ? 2064 HOH   A O   1 
HETATM 8123 O  O   . HOH   V 6 .   ? 1.747  48.558  8.755   1.00 58.27  ? 2065 HOH   A O   1 
HETATM 8124 O  O   . HOH   V 6 .   ? 31.987 26.777  36.400  1.00 38.40  ? 2066 HOH   A O   1 
HETATM 8125 O  O   . HOH   V 6 .   ? 34.137 43.896  -9.765  1.00 39.75  ? 2067 HOH   A O   1 
HETATM 8126 O  O   . HOH   V 6 .   ? 52.211 54.242  11.906  1.00 63.57  ? 2068 HOH   A O   1 
HETATM 8127 O  O   . HOH   V 6 .   ? 43.943 70.691  9.093   1.00 48.46  ? 2069 HOH   A O   1 
HETATM 8128 O  O   . HOH   V 6 .   ? 55.227 31.379  1.621   1.00 35.06  ? 2070 HOH   A O   1 
HETATM 8129 O  O   . HOH   V 6 .   ? 12.613 31.224  -2.406  1.00 44.67  ? 2071 HOH   A O   1 
HETATM 8130 O  O   . HOH   V 6 .   ? 39.552 24.458  28.156  1.00 38.50  ? 2072 HOH   A O   1 
HETATM 8131 O  O   . HOH   V 6 .   ? 27.443 9.682   35.084  1.00 48.71  ? 2073 HOH   A O   1 
HETATM 8132 O  O   . HOH   V 6 .   ? 25.859 -5.097  15.724  1.00 54.95  ? 2074 HOH   A O   1 
HETATM 8133 O  O   . HOH   V 6 .   ? 26.315 34.217  20.172  1.00 21.74  ? 2075 HOH   A O   1 
HETATM 8134 O  O   . HOH   V 6 .   ? 43.741 29.291  24.460  1.00 53.24  ? 2076 HOH   A O   1 
HETATM 8135 O  O   . HOH   V 6 .   ? 60.346 52.133  -0.403  1.00 33.23  ? 2077 HOH   A O   1 
HETATM 8136 O  O   . HOH   V 6 .   ? 10.384 6.832   15.098  1.00 28.41  ? 2078 HOH   A O   1 
HETATM 8137 O  O   . HOH   V 6 .   ? 28.969 15.312  32.671  1.00 25.74  ? 2079 HOH   A O   1 
HETATM 8138 O  O   . HOH   V 6 .   ? 39.450 27.078  -17.852 1.00 50.47  ? 2080 HOH   A O   1 
HETATM 8139 O  O   . HOH   V 6 .   ? 45.452 63.757  -0.176  1.00 27.13  ? 2081 HOH   A O   1 
HETATM 8140 O  O   . HOH   V 6 .   ? 38.536 16.224  -12.619 1.00 39.10  ? 2082 HOH   A O   1 
HETATM 8141 O  O   . HOH   V 6 .   ? 49.368 30.212  32.109  1.00 46.44  ? 2083 HOH   A O   1 
HETATM 8142 O  O   . HOH   V 6 .   ? 47.118 38.765  -13.052 1.00 26.84  ? 2084 HOH   A O   1 
HETATM 8143 O  O   . HOH   V 6 .   ? 26.898 64.278  -7.945  1.00 57.32  ? 2085 HOH   A O   1 
HETATM 8144 O  O   . HOH   V 6 .   ? 34.890 72.901  19.713  1.00 51.98  ? 2086 HOH   A O   1 
HETATM 8145 O  O   . HOH   V 6 .   ? 44.861 7.718   10.229  1.00 40.46  ? 2087 HOH   A O   1 
HETATM 8146 O  O   . HOH   V 6 .   ? 35.722 42.288  16.928  1.00 46.50  ? 2088 HOH   A O   1 
HETATM 8147 O  O   . HOH   V 6 .   ? 30.322 24.185  21.186  1.00 23.08  ? 2089 HOH   A O   1 
HETATM 8148 O  O   . HOH   V 6 .   ? 34.918 47.315  9.874   1.00 54.67  ? 2090 HOH   A O   1 
HETATM 8149 O  O   . HOH   V 6 .   ? 10.127 57.460  26.360  1.00 44.05  ? 2091 HOH   A O   1 
HETATM 8150 O  O   . HOH   V 6 .   ? 25.043 32.709  15.484  1.00 42.45  ? 2092 HOH   A O   1 
HETATM 8151 O  O   . HOH   V 6 .   ? 19.601 36.419  11.203  1.00 46.24  ? 2093 HOH   A O   1 
HETATM 8152 O  O   . HOH   V 6 .   ? 42.442 6.038   9.057   1.00 27.35  ? 2094 HOH   A O   1 
HETATM 8153 O  O   . HOH   V 6 .   ? 13.743 54.734  32.791  1.00 56.73  ? 2095 HOH   A O   1 
HETATM 8154 O  O   . HOH   V 6 .   ? 49.716 12.449  14.988  1.00 30.31  ? 2096 HOH   A O   1 
HETATM 8155 O  O   . HOH   V 6 .   ? 14.467 8.445   1.097   1.00 46.17  ? 2097 HOH   A O   1 
HETATM 8156 O  O   . HOH   V 6 .   ? 50.846 22.789  17.901  1.00 52.62  ? 2098 HOH   A O   1 
HETATM 8157 O  O   . HOH   V 6 .   ? 34.168 21.912  -14.361 1.00 59.74  ? 2099 HOH   A O   1 
HETATM 8158 O  O   . HOH   V 6 .   ? 29.503 -2.257  8.552   1.00 53.72  ? 2100 HOH   A O   1 
HETATM 8159 O  O   . HOH   V 6 .   ? 10.975 3.832   31.118  1.00 60.15  ? 2101 HOH   A O   1 
HETATM 8160 O  O   . HOH   V 6 .   ? 42.208 48.170  15.378  1.00 44.88  ? 2102 HOH   A O   1 
HETATM 8161 O  O   . HOH   V 6 .   ? 38.175 72.522  24.592  1.00 83.97  ? 2103 HOH   A O   1 
HETATM 8162 O  O   . HOH   V 6 .   ? 49.296 62.277  6.200   1.00 42.30  ? 2104 HOH   A O   1 
HETATM 8163 O  O   . HOH   V 6 .   ? 12.352 28.450  22.426  1.00 28.45  ? 2105 HOH   A O   1 
HETATM 8164 O  O   . HOH   V 6 .   ? 51.524 24.291  2.846   1.00 29.18  ? 2106 HOH   A O   1 
HETATM 8165 O  O   . HOH   V 6 .   ? 59.082 36.561  -7.568  1.00 29.87  ? 2107 HOH   A O   1 
HETATM 8166 O  O   . HOH   V 6 .   ? 40.363 11.365  -8.932  1.00 44.85  ? 2108 HOH   A O   1 
HETATM 8167 O  O   . HOH   V 6 .   ? 8.616  11.078  1.105   1.00 56.79  ? 2109 HOH   A O   1 
HETATM 8168 O  O   . HOH   V 6 .   ? 7.108  11.839  18.710  1.00 41.58  ? 2110 HOH   A O   1 
HETATM 8169 O  O   . HOH   V 6 .   ? 10.077 49.896  -3.750  1.00 55.02  ? 2111 HOH   A O   1 
HETATM 8170 O  O   . HOH   V 6 .   ? 25.625 -3.071  21.879  1.00 32.66  ? 2112 HOH   A O   1 
HETATM 8171 O  O   . HOH   V 6 .   ? 26.775 -5.573  24.957  1.00 55.18  ? 2113 HOH   A O   1 
HETATM 8172 O  O   . HOH   V 6 .   ? 30.942 30.871  -15.468 1.00 41.28  ? 2114 HOH   A O   1 
HETATM 8173 O  O   . HOH   V 6 .   ? 49.199 42.293  36.439  1.00 52.37  ? 2115 HOH   A O   1 
HETATM 8174 O  O   . HOH   V 6 .   ? 47.325 63.712  10.513  1.00 28.02  ? 2116 HOH   A O   1 
HETATM 8175 O  O   . HOH   V 6 .   ? 36.976 67.084  -3.783  1.00 37.42  ? 2117 HOH   A O   1 
HETATM 8176 O  O   . HOH   V 6 .   ? 21.160 33.494  10.429  1.00 47.63  ? 2118 HOH   A O   1 
HETATM 8177 O  O   . HOH   V 6 .   ? 7.242  41.112  3.217   1.00 46.95  ? 2119 HOH   A O   1 
HETATM 8178 O  O   . HOH   V 6 .   ? 36.929 27.143  36.585  1.00 45.52  ? 2120 HOH   A O   1 
HETATM 8179 O  O   . HOH   V 6 .   ? 12.945 22.735  -6.221  1.00 30.73  ? 2121 HOH   A O   1 
HETATM 8180 O  O   . HOH   V 6 .   ? 16.263 1.178   31.529  1.00 41.66  ? 2122 HOH   A O   1 
HETATM 8181 O  O   . HOH   V 6 .   ? 42.622 61.595  29.175  1.00 62.89  ? 2123 HOH   A O   1 
HETATM 8182 O  O   . HOH   V 6 .   ? 8.421  33.021  2.256   1.00 42.01  ? 2124 HOH   A O   1 
HETATM 8183 O  O   . HOH   V 6 .   ? 18.510 66.011  15.072  1.00 40.70  ? 2125 HOH   A O   1 
HETATM 8184 O  O   . HOH   V 6 .   ? 24.587 -1.925  7.779   1.00 42.96  ? 2126 HOH   A O   1 
HETATM 8185 O  O   . HOH   V 6 .   ? 26.923 13.700  -11.309 1.00 43.41  ? 2127 HOH   A O   1 
HETATM 8186 O  O   . HOH   V 6 .   ? 28.405 41.980  37.760  1.00 26.58  ? 2128 HOH   A O   1 
HETATM 8187 O  O   . HOH   V 6 .   ? 46.761 40.434  -18.097 1.00 53.21  ? 2129 HOH   A O   1 
HETATM 8188 O  O   . HOH   V 6 .   ? 35.594 40.206  39.493  1.00 49.20  ? 2130 HOH   A O   1 
HETATM 8189 O  O   . HOH   V 6 .   ? 2.027  38.668  17.901  1.00 48.63  ? 2131 HOH   A O   1 
HETATM 8190 O  O   . HOH   V 6 .   ? 49.738 61.532  19.572  1.00 37.89  ? 2132 HOH   A O   1 
HETATM 8191 O  O   . HOH   V 6 .   ? 4.665  53.379  26.220  1.00 31.55  ? 2133 HOH   A O   1 
HETATM 8192 O  O   . HOH   V 6 .   ? 54.020 37.273  -14.043 1.00 38.21  ? 2134 HOH   A O   1 
HETATM 8193 O  O   . HOH   V 6 .   ? 8.687  29.283  22.546  1.00 31.95  ? 2135 HOH   A O   1 
HETATM 8194 O  O   . HOH   V 6 .   ? 10.559 33.246  26.270  1.00 50.00  ? 2136 HOH   A O   1 
HETATM 8195 O  O   . HOH   V 6 .   ? 35.198 54.256  -19.068 1.00 37.36  ? 2137 HOH   A O   1 
HETATM 8196 O  O   . HOH   V 6 .   ? 41.891 59.384  29.581  1.00 34.86  ? 2138 HOH   A O   1 
HETATM 8197 O  O   . HOH   V 6 .   ? 4.782  14.606  21.085  1.00 39.64  ? 2139 HOH   A O   1 
HETATM 8198 O  O   . HOH   V 6 .   ? 3.169  31.747  11.708  1.00 24.92  ? 2140 HOH   A O   1 
HETATM 8199 O  O   . HOH   V 6 .   ? 55.440 33.422  2.651   1.00 44.48  ? 2141 HOH   A O   1 
HETATM 8200 O  O   . HOH   V 6 .   ? 16.177 42.322  13.406  1.00 38.63  ? 2142 HOH   A O   1 
HETATM 8201 O  O   . HOH   V 6 .   ? 34.061 58.716  31.008  1.00 45.86  ? 2143 HOH   A O   1 
HETATM 8202 O  O   . HOH   V 6 .   ? 40.442 70.999  10.144  1.00 32.83  ? 2144 HOH   A O   1 
HETATM 8203 O  O   . HOH   V 6 .   ? 27.479 25.039  32.134  1.00 27.50  ? 2145 HOH   A O   1 
HETATM 8204 O  O   . HOH   V 6 .   ? 31.289 2.246   36.521  1.00 39.29  ? 2146 HOH   A O   1 
HETATM 8205 O  O   . HOH   V 6 .   ? 46.963 28.936  29.183  1.00 35.01  ? 2147 HOH   A O   1 
HETATM 8206 O  O   . HOH   V 6 .   ? 55.050 61.354  -1.626  1.00 44.93  ? 2148 HOH   A O   1 
HETATM 8207 O  O   . HOH   V 6 .   ? 48.700 62.064  8.601   1.00 40.57  ? 2149 HOH   A O   1 
HETATM 8208 O  O   . HOH   V 6 .   ? 49.918 51.237  19.320  1.00 47.23  ? 2150 HOH   A O   1 
HETATM 8209 O  O   . HOH   V 6 .   ? 32.306 2.839   4.253   1.00 51.98  ? 2151 HOH   A O   1 
HETATM 8210 O  O   . HOH   V 6 .   ? 25.752 69.384  17.875  1.00 31.10  ? 2152 HOH   A O   1 
HETATM 8211 O  O   . HOH   V 6 .   ? 49.799 36.649  30.878  1.00 33.68  ? 2153 HOH   A O   1 
HETATM 8212 O  O   . HOH   V 6 .   ? 52.735 32.328  13.423  1.00 37.72  ? 2154 HOH   A O   1 
HETATM 8213 O  O   . HOH   V 6 .   ? 37.673 46.701  16.465  1.00 37.15  ? 2155 HOH   A O   1 
HETATM 8214 O  O   . HOH   V 6 .   ? 51.760 16.901  16.146  1.00 50.74  ? 2156 HOH   A O   1 
HETATM 8215 O  O   . HOH   V 6 .   ? 1.470  38.167  22.284  1.00 40.14  ? 2157 HOH   A O   1 
HETATM 8216 O  O   . HOH   V 6 .   ? 17.426 -4.204  9.398   1.00 41.20  ? 2158 HOH   A O   1 
HETATM 8217 O  O   . HOH   V 6 .   ? 43.822 70.590  13.502  1.00 27.08  ? 2159 HOH   A O   1 
HETATM 8218 O  O   . HOH   V 6 .   ? 3.331  54.491  24.068  1.00 30.83  ? 2160 HOH   A O   1 
HETATM 8219 O  O   . HOH   V 6 .   ? 15.162 39.779  39.854  1.00 50.80  ? 2161 HOH   A O   1 
HETATM 8220 O  O   . HOH   V 6 .   ? 27.611 3.970   35.963  1.00 52.54  ? 2162 HOH   A O   1 
HETATM 8221 O  O   . HOH   V 6 .   ? -0.071 18.109  23.309  1.00 42.35  ? 2163 HOH   A O   1 
HETATM 8222 O  O   . HOH   V 6 .   ? 57.274 35.542  -1.743  1.00 43.79  ? 2164 HOH   A O   1 
HETATM 8223 O  O   . HOH   V 6 .   ? 17.551 53.491  -4.109  1.00 37.40  ? 2165 HOH   A O   1 
HETATM 8224 O  O   . HOH   V 6 .   ? 25.604 26.050  -11.874 1.00 39.52  ? 2166 HOH   A O   1 
HETATM 8225 O  O   . HOH   V 6 .   ? 14.555 45.646  37.196  1.00 45.95  ? 2167 HOH   A O   1 
HETATM 8226 O  O   . HOH   V 6 .   ? 19.465 -1.927  30.951  1.00 51.88  ? 2168 HOH   A O   1 
HETATM 8227 O  O   . HOH   V 6 .   ? 56.235 53.796  -3.431  1.00 32.58  ? 2169 HOH   A O   1 
HETATM 8228 O  O   . HOH   V 6 .   ? 51.546 15.924  12.965  1.00 56.12  ? 2170 HOH   A O   1 
HETATM 8229 O  O   . HOH   V 6 .   ? 24.691 42.023  40.855  1.00 48.63  ? 2171 HOH   A O   1 
HETATM 8230 O  O   . HOH   V 6 .   ? 47.190 66.164  4.099   1.00 42.98  ? 2172 HOH   A O   1 
HETATM 8231 O  O   . HOH   V 6 .   ? 14.132 11.342  6.564   1.00 18.07  ? 2173 HOH   A O   1 
HETATM 8232 O  O   . HOH   V 6 .   ? 51.434 14.444  15.652  1.00 46.92  ? 2174 HOH   A O   1 
HETATM 8233 O  O   . HOH   V 6 .   ? 10.551 60.618  8.729   1.00 58.52  ? 2175 HOH   A O   1 
HETATM 8234 O  O   . HOH   V 6 .   ? 39.573 33.272  19.053  1.00 21.89  ? 2176 HOH   A O   1 
HETATM 8235 O  O   . HOH   V 6 .   ? 59.853 57.581  -14.397 1.00 42.04  ? 2177 HOH   A O   1 
HETATM 8236 O  O   . HOH   V 6 .   ? 29.917 66.264  -2.363  1.00 46.38  ? 2178 HOH   A O   1 
HETATM 8237 O  O   . HOH   V 6 .   ? 5.233  30.034  23.204  1.00 43.23  ? 2179 HOH   A O   1 
HETATM 8238 O  O   . HOH   V 6 .   ? 15.132 9.509   10.320  1.00 16.30  ? 2180 HOH   A O   1 
HETATM 8239 O  O   . HOH   V 6 .   ? 23.781 63.610  20.866  1.00 40.97  ? 2181 HOH   A O   1 
HETATM 8240 O  O   . HOH   V 6 .   ? 18.276 51.259  -7.730  1.00 69.22  ? 2182 HOH   A O   1 
HETATM 8241 O  O   . HOH   V 6 .   ? 4.345  44.477  32.842  1.00 38.43  ? 2183 HOH   A O   1 
HETATM 8242 O  O   . HOH   V 6 .   ? 22.824 35.053  16.866  1.00 55.17  ? 2184 HOH   A O   1 
HETATM 8243 O  O   . HOH   V 6 .   ? 35.801 37.604  40.477  1.00 71.79  ? 2185 HOH   A O   1 
HETATM 8244 O  O   . HOH   V 6 .   ? 49.877 55.280  22.232  1.00 31.63  ? 2186 HOH   A O   1 
HETATM 8245 O  O   . HOH   V 6 .   ? 22.680 59.273  -7.775  1.00 52.64  ? 2187 HOH   A O   1 
HETATM 8246 O  O   . HOH   V 6 .   ? 13.824 52.068  -0.832  1.00 30.83  ? 2188 HOH   A O   1 
HETATM 8247 O  O   . HOH   V 6 .   ? 35.246 70.370  23.050  1.00 38.33  ? 2189 HOH   A O   1 
HETATM 8248 O  O   . HOH   V 6 .   ? 28.658 30.124  -11.082 1.00 32.06  ? 2190 HOH   A O   1 
HETATM 8249 O  O   . HOH   V 6 .   ? 7.301  15.080  -0.999  1.00 46.32  ? 2191 HOH   A O   1 
HETATM 8250 O  O   . HOH   V 6 .   ? 12.801 5.746   30.718  1.00 36.19  ? 2192 HOH   A O   1 
HETATM 8251 O  O   . HOH   V 6 .   ? 37.689 25.151  31.198  1.00 34.16  ? 2193 HOH   A O   1 
HETATM 8252 O  O   . HOH   V 6 .   ? 35.608 42.696  -11.371 1.00 36.35  ? 2194 HOH   A O   1 
HETATM 8253 O  O   . HOH   V 6 .   ? -3.090 24.818  18.063  1.00 36.69  ? 2195 HOH   A O   1 
HETATM 8254 O  O   . HOH   V 6 .   ? 57.742 56.319  -7.027  1.00 46.92  ? 2196 HOH   A O   1 
HETATM 8255 O  O   . HOH   V 6 .   ? 34.801 33.989  -15.789 1.00 54.99  ? 2197 HOH   A O   1 
HETATM 8256 O  O   . HOH   V 6 .   ? 2.430  46.100  7.634   1.00 66.08  ? 2198 HOH   A O   1 
HETATM 8257 O  O   . HOH   V 6 .   ? 38.510 3.510   34.915  1.00 49.67  ? 2199 HOH   A O   1 
HETATM 8258 O  O   . HOH   V 6 .   ? 3.991  31.635  14.501  1.00 19.78  ? 2200 HOH   A O   1 
HETATM 8259 O  O   . HOH   V 6 .   ? 32.022 46.261  41.546  1.00 65.47  ? 2201 HOH   A O   1 
HETATM 8260 O  O   . HOH   V 6 .   ? 20.396 66.991  11.042  1.00 33.89  ? 2202 HOH   A O   1 
HETATM 8261 O  O   . HOH   V 6 .   ? 49.117 52.894  25.784  1.00 41.29  ? 2203 HOH   A O   1 
HETATM 8262 O  O   . HOH   V 6 .   ? 37.190 13.582  34.733  1.00 50.56  ? 2204 HOH   A O   1 
HETATM 8263 O  O   . HOH   V 6 .   ? 27.268 1.538   34.498  1.00 46.16  ? 2205 HOH   A O   1 
HETATM 8264 O  O   . HOH   V 6 .   ? 32.231 35.116  -12.142 1.00 49.52  ? 2206 HOH   A O   1 
HETATM 8265 O  O   . HOH   V 6 .   ? 31.907 56.573  -16.111 1.00 57.87  ? 2207 HOH   A O   1 
HETATM 8266 O  O   . HOH   V 6 .   ? 7.865  31.134  3.908   1.00 24.95  ? 2208 HOH   A O   1 
HETATM 8267 O  O   . HOH   V 6 .   ? 26.439 70.394  15.508  1.00 38.94  ? 2209 HOH   A O   1 
HETATM 8268 O  O   . HOH   V 6 .   ? 25.494 16.297  -12.560 1.00 52.79  ? 2210 HOH   A O   1 
HETATM 8269 O  O   . HOH   V 6 .   ? 15.500 8.015   3.518   1.00 24.92  ? 2211 HOH   A O   1 
HETATM 8270 O  O   . HOH   V 6 .   ? 8.695  27.084  20.948  1.00 24.29  ? 2212 HOH   A O   1 
HETATM 8271 O  O   . HOH   V 6 .   ? 5.400  13.623  15.894  1.00 39.88  ? 2213 HOH   A O   1 
HETATM 8272 O  O   . HOH   V 6 .   ? 26.835 70.864  19.883  1.00 34.75  ? 2214 HOH   A O   1 
HETATM 8273 O  O   . HOH   V 6 .   ? 34.087 8.527   -4.497  1.00 40.10  ? 2215 HOH   A O   1 
HETATM 8274 O  O   . HOH   V 6 .   ? 7.350  55.920  23.393  1.00 40.21  ? 2216 HOH   A O   1 
HETATM 8275 O  O   . HOH   V 6 .   ? 37.079 5.306   0.197   1.00 49.30  ? 2217 HOH   A O   1 
HETATM 8276 O  O   . HOH   V 6 .   ? 12.390 61.003  24.104  1.00 42.48  ? 2218 HOH   A O   1 
HETATM 8277 O  O   . HOH   V 6 .   ? 47.215 61.829  0.105   1.00 36.22  ? 2219 HOH   A O   1 
HETATM 8278 O  O   . HOH   V 6 .   ? 44.227 27.197  -13.995 1.00 45.16  ? 2220 HOH   A O   1 
HETATM 8279 O  O   . HOH   V 6 .   ? 39.277 35.467  -16.200 1.00 43.31  ? 2221 HOH   A O   1 
HETATM 8280 O  O   . HOH   V 6 .   ? 14.861 67.891  13.159  1.00 50.18  ? 2222 HOH   A O   1 
HETATM 8281 O  O   . HOH   V 6 .   ? 37.381 -1.625  33.840  1.00 36.38  ? 2223 HOH   A O   1 
HETATM 8282 O  O   . HOH   V 6 .   ? 23.280 67.926  18.386  1.00 32.62  ? 2224 HOH   A O   1 
HETATM 8283 O  O   . HOH   V 6 .   ? 30.155 -0.087  5.580   1.00 45.78  ? 2225 HOH   A O   1 
HETATM 8284 O  O   . HOH   V 6 .   ? 15.956 44.498  39.393  1.00 45.55  ? 2226 HOH   A O   1 
HETATM 8285 O  O   . HOH   V 6 .   ? 25.638 34.294  17.447  1.00 36.02  ? 2227 HOH   A O   1 
HETATM 8286 O  O   . HOH   V 6 .   ? 48.440 63.054  -22.724 1.00 38.49  ? 2228 HOH   A O   1 
HETATM 8287 O  O   . HOH   V 6 .   ? 55.985 56.098  -19.741 1.00 39.19  ? 2229 HOH   A O   1 
HETATM 8288 O  O   . HOH   V 6 .   ? 35.103 11.266  34.613  1.00 43.85  ? 2230 HOH   A O   1 
HETATM 8289 O  O   . HOH   V 6 .   ? 26.134 28.764  33.990  1.00 43.77  ? 2231 HOH   A O   1 
HETATM 8290 O  O   . HOH   V 6 .   ? 45.488 10.004  11.597  1.00 38.21  ? 2232 HOH   A O   1 
HETATM 8291 O  O   . HOH   V 6 .   ? 23.436 -3.418  19.967  1.00 49.07  ? 2233 HOH   A O   1 
HETATM 8292 O  O   . HOH   V 6 .   ? 19.262 27.114  -8.918  1.00 30.12  ? 2234 HOH   A O   1 
HETATM 8293 O  O   . HOH   V 6 .   ? 5.754  20.667  3.129   1.00 21.88  ? 2235 HOH   A O   1 
HETATM 8294 O  O   . HOH   V 6 .   ? 52.537 26.119  9.832   1.00 28.00  ? 2236 HOH   A O   1 
HETATM 8295 O  O   . HOH   V 6 .   ? 22.379 10.436  -6.912  1.00 35.95  ? 2237 HOH   A O   1 
HETATM 8296 O  O   . HOH   V 6 .   ? 45.374 30.538  40.134  1.00 42.01  ? 2238 HOH   A O   1 
HETATM 8297 O  O   . HOH   V 6 .   ? 35.543 19.240  -14.220 1.00 43.12  ? 2239 HOH   A O   1 
HETATM 8298 O  O   . HOH   V 6 .   ? 33.119 11.562  -6.943  1.00 47.35  ? 2240 HOH   A O   1 
HETATM 8299 O  O   . HOH   V 6 .   ? 54.256 50.162  -23.024 1.00 35.41  ? 2241 HOH   A O   1 
HETATM 8300 O  O   . HOH   V 6 .   ? 11.176 42.667  34.561  1.00 46.04  ? 2242 HOH   A O   1 
HETATM 8301 O  O   . HOH   V 6 .   ? 49.808 49.913  -24.257 1.00 37.86  ? 2243 HOH   A O   1 
HETATM 8302 O  O   . HOH   V 6 .   ? 31.970 46.286  11.980  1.00 55.69  ? 2244 HOH   A O   1 
HETATM 8303 O  O   . HOH   V 6 .   ? 31.762 5.254   0.412   1.00 48.24  ? 2245 HOH   A O   1 
HETATM 8304 O  O   . HOH   V 6 .   ? 2.519  33.712  17.827  1.00 41.82  ? 2246 HOH   A O   1 
HETATM 8305 O  O   . HOH   V 6 .   ? 26.842 66.945  4.929   1.00 33.78  ? 2247 HOH   A O   1 
HETATM 8306 O  O   . HOH   V 6 .   ? 29.191 39.318  -7.980  1.00 51.14  ? 2248 HOH   A O   1 
HETATM 8307 O  O   . HOH   V 6 .   ? 35.334 -8.028  32.495  1.00 44.88  ? 2249 HOH   A O   1 
HETATM 8308 O  O   . HOH   V 6 .   ? 5.360  3.801   20.105  1.00 50.98  ? 2250 HOH   A O   1 
HETATM 8309 O  O   . HOH   V 6 .   ? 12.449 9.519   -0.389  1.00 53.27  ? 2251 HOH   A O   1 
HETATM 8310 O  O   . HOH   V 6 .   ? 21.623 65.323  15.436  1.00 35.66  ? 2252 HOH   A O   1 
HETATM 8311 O  O   . HOH   V 6 .   ? 52.112 28.848  17.030  1.00 46.93  ? 2253 HOH   A O   1 
HETATM 8312 O  O   . HOH   V 6 .   ? 26.568 36.502  -10.230 1.00 47.05  ? 2254 HOH   A O   1 
HETATM 8313 O  O   . HOH   V 6 .   ? 13.518 28.768  -6.625  1.00 49.99  ? 2255 HOH   A O   1 
HETATM 8314 O  O   . HOH   V 6 .   ? 23.417 43.568  7.654   1.00 43.96  ? 2256 HOH   A O   1 
HETATM 8315 O  O   . HOH   V 6 .   ? 14.579 55.251  -1.461  1.00 47.45  ? 2257 HOH   A O   1 
HETATM 8316 O  O   . HOH   V 6 .   ? 40.490 70.318  7.459   1.00 36.09  ? 2258 HOH   A O   1 
HETATM 8317 O  O   . HOH   V 6 .   ? 11.674 7.075   3.088   1.00 61.38  ? 2259 HOH   A O   1 
HETATM 8318 O  O   . HOH   V 6 .   ? 19.786 64.802  23.907  1.00 44.41  ? 2260 HOH   A O   1 
HETATM 8319 O  O   . HOH   V 6 .   ? 59.656 50.392  -2.328  1.00 24.80  ? 2261 HOH   A O   1 
HETATM 8320 O  O   . HOH   V 6 .   ? 43.942 21.002  27.326  1.00 43.80  ? 2262 HOH   A O   1 
HETATM 8321 O  O   . HOH   V 6 .   ? 43.018 29.111  26.978  1.00 36.10  ? 2263 HOH   A O   1 
HETATM 8322 O  O   . HOH   V 6 .   ? 59.040 36.178  2.187   1.00 48.83  ? 2264 HOH   A O   1 
HETATM 8323 O  O   . HOH   V 6 .   ? 50.409 45.049  -17.727 1.00 46.79  ? 2265 HOH   A O   1 
HETATM 8324 O  O   . HOH   V 6 .   ? 35.467 41.162  -15.500 1.00 54.80  ? 2266 HOH   A O   1 
HETATM 8325 O  O   . HOH   V 6 .   ? 14.720 27.494  -8.436  1.00 49.48  ? 2267 HOH   A O   1 
HETATM 8326 O  O   . HOH   V 6 .   ? 17.849 3.794   2.977   1.00 44.85  ? 2268 HOH   A O   1 
HETATM 8327 O  O   . HOH   V 6 .   ? 28.841 35.273  20.137  1.00 34.91  ? 2269 HOH   A O   1 
HETATM 8328 O  O   . HOH   V 6 .   ? 37.150 36.014  17.069  1.00 51.90  ? 2270 HOH   A O   1 
HETATM 8329 O  O   . HOH   V 6 .   ? 33.713 50.331  -13.457 1.00 32.57  ? 2271 HOH   A O   1 
HETATM 8330 O  O   . HOH   V 6 .   ? 26.786 8.656   -4.366  1.00 39.29  ? 2272 HOH   A O   1 
HETATM 8331 O  O   . HOH   V 6 .   ? 12.925 44.512  35.763  1.00 43.22  ? 2273 HOH   A O   1 
HETATM 8332 O  O   . HOH   V 6 .   ? 31.626 5.194   -2.045  1.00 52.53  ? 2274 HOH   A O   1 
HETATM 8333 O  O   . HOH   V 6 .   ? 42.773 24.691  27.867  1.00 64.27  ? 2275 HOH   A O   1 
HETATM 8334 O  O   . HOH   V 6 .   ? 20.143 11.994  -10.317 1.00 49.77  ? 2276 HOH   A O   1 
HETATM 8335 O  O   . HOH   V 6 .   ? 43.488 68.845  4.958   1.00 47.51  ? 2277 HOH   A O   1 
HETATM 8336 O  O   . HOH   V 6 .   ? 29.944 9.857   -6.704  1.00 44.88  ? 2278 HOH   A O   1 
HETATM 8337 O  O   . HOH   V 6 .   ? 6.040  40.744  32.415  1.00 34.99  ? 2279 HOH   A O   1 
HETATM 8338 O  O   . HOH   V 6 .   ? 61.455 39.057  -5.013  1.00 20.78  ? 2280 HOH   A O   1 
HETATM 8339 O  O   . HOH   V 6 .   ? 20.439 45.442  40.180  1.00 37.64  ? 2281 HOH   A O   1 
HETATM 8340 O  O   . HOH   V 6 .   ? 41.021 32.274  38.095  1.00 55.03  ? 2282 HOH   A O   1 
HETATM 8341 O  O   . HOH   V 6 .   ? 23.205 32.511  13.511  1.00 32.02  ? 2283 HOH   A O   1 
HETATM 8342 O  O   . HOH   V 6 .   ? 7.126  53.118  -5.003  1.00 64.78  ? 2284 HOH   A O   1 
HETATM 8343 O  O   . HOH   V 6 .   ? 14.586 42.383  40.145  1.00 47.47  ? 2285 HOH   A O   1 
HETATM 8344 O  O   . HOH   V 6 .   ? 46.401 58.344  -8.861  1.00 31.21  ? 2286 HOH   A O   1 
HETATM 8345 O  O   . HOH   V 6 .   ? 57.373 33.062  -1.628  1.00 40.07  ? 2287 HOH   A O   1 
HETATM 8346 O  O   . HOH   V 6 .   ? 19.394 43.769  15.329  1.00 44.61  ? 2288 HOH   A O   1 
HETATM 8347 O  O   . HOH   V 6 .   ? 50.894 51.152  22.196  1.00 46.64  ? 2289 HOH   A O   1 
HETATM 8348 O  O   . HOH   V 6 .   ? 54.040 28.651  13.617  1.00 39.25  ? 2290 HOH   A O   1 
HETATM 8349 O  O   . HOH   V 6 .   ? 22.789 30.258  36.752  1.00 51.49  ? 2291 HOH   A O   1 
HETATM 8350 O  O   . HOH   V 6 .   ? 10.262 54.673  -1.906  1.00 33.91  ? 2292 HOH   A O   1 
HETATM 8351 O  O   . HOH   V 6 .   ? 55.521 28.235  7.181   1.00 34.00  ? 2293 HOH   A O   1 
HETATM 8352 O  O   . HOH   V 6 .   ? 27.183 42.474  40.904  1.00 54.76  ? 2294 HOH   A O   1 
HETATM 8353 O  O   . HOH   V 6 .   ? 32.380 33.036  41.898  1.00 59.12  ? 2295 HOH   A O   1 
HETATM 8354 O  O   . HOH   V 6 .   ? 7.698  0.864   17.422  1.00 39.96  ? 2296 HOH   A O   1 
HETATM 8355 O  O   . HOH   V 6 .   ? 32.026 42.864  40.474  1.00 48.78  ? 2297 HOH   A O   1 
HETATM 8356 O  O   . HOH   V 6 .   ? 29.710 14.371  35.014  1.00 51.89  ? 2298 HOH   A O   1 
HETATM 8357 O  O   . HOH   V 6 .   ? 5.833  30.893  0.486   1.00 39.41  ? 2299 HOH   A O   1 
HETATM 8358 O  O   . HOH   V 6 .   ? 11.746 7.317   9.289   1.00 30.86  ? 2300 HOH   A O   1 
HETATM 8359 O  O   . HOH   V 6 .   ? 8.179  11.742  12.902  1.00 38.71  ? 2301 HOH   A O   1 
HETATM 8360 O  O   . HOH   V 6 .   ? 22.075 43.603  41.389  1.00 47.40  ? 2302 HOH   A O   1 
HETATM 8361 O  O   . HOH   V 6 .   ? 22.337 32.494  37.926  1.00 39.10  ? 2303 HOH   A O   1 
HETATM 8362 O  O   . HOH   V 6 .   ? 59.811 57.788  -17.990 1.00 30.49  ? 2304 HOH   A O   1 
HETATM 8363 O  O   . HOH   V 6 .   ? 34.577 48.457  14.586  1.00 42.26  ? 2305 HOH   A O   1 
HETATM 8364 O  O   . HOH   V 6 .   ? 18.434 67.398  12.899  1.00 48.99  ? 2306 HOH   A O   1 
HETATM 8365 O  O   . HOH   V 6 .   ? 8.848  19.031  -6.260  1.00 50.32  ? 2307 HOH   A O   1 
HETATM 8366 O  O   . HOH   V 6 .   ? 52.439 14.216  18.272  1.00 43.98  ? 2308 HOH   A O   1 
HETATM 8367 O  O   . HOH   V 6 .   ? 11.363 8.694   11.792  1.00 24.40  ? 2309 HOH   A O   1 
HETATM 8368 O  O   . HOH   V 6 .   ? 22.745 11.883  -9.049  1.00 39.87  ? 2310 HOH   A O   1 
HETATM 8369 O  O   . HOH   V 6 .   ? 27.311 50.422  38.173  1.00 43.54  ? 2311 HOH   A O   1 
HETATM 8370 O  O   . HOH   V 6 .   ? 17.866 57.132  -2.454  1.00 33.14  ? 2312 HOH   A O   1 
HETATM 8371 O  O   . HOH   V 6 .   ? 51.172 37.278  -14.940 1.00 40.26  ? 2313 HOH   A O   1 
HETATM 8372 O  O   . HOH   V 6 .   ? 8.530  56.932  -1.811  1.00 43.46  ? 2314 HOH   A O   1 
HETATM 8373 O  O   . HOH   V 6 .   ? 54.241 -8.585  14.099  1.00 47.52  ? 2315 HOH   A O   1 
HETATM 8374 O  O   . HOH   V 6 .   ? 7.092  11.125  15.302  1.00 52.10  ? 2316 HOH   A O   1 
HETATM 8375 O  O   . HOH   V 6 .   ? 33.371 58.799  -15.737 1.00 64.11  ? 2317 HOH   A O   1 
HETATM 8376 O  O   . HOH   V 6 .   ? 27.228 28.072  -11.817 1.00 33.05  ? 2318 HOH   A O   1 
HETATM 8377 O  O   . HOH   V 6 .   ? 14.542 8.841   5.873   1.00 21.71  ? 2319 HOH   A O   1 
HETATM 8378 O  O   . HOH   V 6 .   ? 24.117 44.195  4.802   1.00 54.14  ? 2320 HOH   A O   1 
HETATM 8379 O  O   . HOH   V 6 .   ? 34.672 4.725   1.321   1.00 43.86  ? 2321 HOH   A O   1 
HETATM 8380 O  O   . HOH   V 6 .   ? 54.620 26.208  11.662  1.00 38.11  ? 2322 HOH   A O   1 
HETATM 8381 O  O   . HOH   V 6 .   ? 53.519 22.351  13.145  1.00 42.26  ? 2323 HOH   A O   1 
HETATM 8382 O  O   . HOH   V 6 .   ? 1.564  32.250  15.809  1.00 44.68  ? 2324 HOH   A O   1 
HETATM 8383 O  O   . HOH   V 6 .   ? 53.492 24.341  4.925   1.00 46.11  ? 2325 HOH   A O   1 
HETATM 8384 O  O   . HOH   V 6 .   ? 44.368 73.100  13.486  1.00 39.97  ? 2326 HOH   A O   1 
HETATM 8385 O  O   . HOH   V 6 .   ? 15.904 5.334   3.134   1.00 33.73  ? 2327 HOH   A O   1 
HETATM 8386 O  O   . HOH   V 6 .   ? 9.204  7.698   13.001  1.00 31.15  ? 2328 HOH   A O   1 
HETATM 8387 O  O   . HOH   V 6 .   ? 54.355 25.598  7.431   1.00 42.09  ? 2329 HOH   A O   1 
HETATM 8388 O  O   . HOH   V 6 .   ? 7.155  9.535   13.245  1.00 40.77  ? 2330 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   . THR   A 45  ? 0.5553 0.6589 0.6375 0.0439  0.0265  0.1174  45   THR   A N   
2    C  CA  . THR   A 45  ? 0.5549 0.6541 0.6389 0.0462  0.0294  0.1168  45   THR   A CA  
3    C  C   . THR   A 45  ? 0.5394 0.6381 0.6213 0.0442  0.0278  0.1128  45   THR   A C   
4    O  O   . THR   A 45  ? 0.5526 0.6472 0.6301 0.0421  0.0268  0.1080  45   THR   A O   
5    C  CB  . THR   A 45  ? 0.5840 0.6742 0.6663 0.0479  0.0327  0.1147  45   THR   A CB  
6    O  OG1 . THR   A 45  ? 0.6072 0.6975 0.6907 0.0493  0.0339  0.1179  45   THR   A OG1 
7    C  CG2 . THR   A 45  ? 0.5893 0.6749 0.6737 0.0505  0.0361  0.1148  45   THR   A CG2 
8    N  N   . PRO   A 46  ? 0.5105 0.6131 0.5957 0.0449  0.0278  0.1147  46   PRO   A N   
9    C  CA  . PRO   A 46  ? 0.4848 0.5868 0.5682 0.0431  0.0265  0.1110  46   PRO   A CA  
10   C  C   . PRO   A 46  ? 0.4420 0.5350 0.5228 0.0438  0.0289  0.1067  46   PRO   A C   
11   O  O   . PRO   A 46  ? 0.4532 0.5411 0.5350 0.0464  0.0322  0.1076  46   PRO   A O   
12   C  CB  . PRO   A 46  ? 0.5024 0.6102 0.5907 0.0443  0.0266  0.1149  46   PRO   A CB  
13   C  CG  . PRO   A 46  ? 0.5142 0.6277 0.6066 0.0460  0.0268  0.1207  46   PRO   A CG  
14   C  CD  . PRO   A 46  ? 0.4987 0.6066 0.5897 0.0474  0.0290  0.1205  46   PRO   A CD  
15   N  N   . PHE   A 47  ? 0.3854 0.4763 0.4628 0.0415  0.0274  0.1022  47   PHE   A N   
16   C  CA  . PHE   A 47  ? 0.3286 0.4112 0.4031 0.0419  0.0293  0.0980  47   PHE   A CA  
17   C  C   . PHE   A 47  ? 0.3001 0.3810 0.3775 0.0442  0.0320  0.0993  47   PHE   A C   
18   O  O   . PHE   A 47  ? 0.3196 0.4054 0.3993 0.0440  0.0310  0.1006  47   PHE   A O   
19   C  CB  . PHE   A 47  ? 0.3018 0.3832 0.3721 0.0388  0.0268  0.0931  47   PHE   A CB  
20   C  CG  . PHE   A 47  ? 0.2717 0.3447 0.3386 0.0388  0.0284  0.0888  47   PHE   A CG  
21   C  CD1 . PHE   A 47  ? 0.2637 0.3323 0.3282 0.0387  0.0291  0.0873  47   PHE   A CD1 
22   C  CD2 . PHE   A 47  ? 0.2588 0.3284 0.3248 0.0388  0.0292  0.0863  47   PHE   A CD2 
23   C  CE1 . PHE   A 47  ? 0.2596 0.3209 0.3210 0.0385  0.0304  0.0834  47   PHE   A CE1 
24   C  CE2 . PHE   A 47  ? 0.2492 0.3114 0.3119 0.0387  0.0305  0.0824  47   PHE   A CE2 
25   C  CZ  . PHE   A 47  ? 0.2498 0.3079 0.3103 0.0385  0.0311  0.0810  47   PHE   A CZ  
26   N  N   . PRO   A 48  ? 0.2830 0.3573 0.3605 0.0465  0.0355  0.0990  48   PRO   A N   
27   C  CA  . PRO   A 48  ? 0.2871 0.3598 0.3674 0.0490  0.0385  0.1007  48   PRO   A CA  
28   C  C   . PRO   A 48  ? 0.3075 0.3765 0.3859 0.0483  0.0388  0.0971  48   PRO   A C   
29   O  O   . PRO   A 48  ? 0.3414 0.4062 0.4208 0.0503  0.0420  0.0974  48   PRO   A O   
30   C  CB  . PRO   A 48  ? 0.2956 0.3621 0.3762 0.0515  0.0422  0.1017  48   PRO   A CB  
31   C  CG  . PRO   A 48  ? 0.3081 0.3698 0.3840 0.0497  0.0413  0.0978  48   PRO   A CG  
32   C  CD  . PRO   A 48  ? 0.2779 0.3459 0.3529 0.0470  0.0372  0.0976  48   PRO   A CD  
33   N  N   . TRP   A 49  ? 0.2762 0.3466 0.3517 0.0454  0.0357  0.0937  49   TRP   A N   
34   C  CA  . TRP   A 49  ? 0.2635 0.3309 0.3372 0.0446  0.0358  0.0904  49   TRP   A CA  
35   C  C   . TRP   A 49  ? 0.2756 0.3484 0.3484 0.0418  0.0321  0.0891  49   TRP   A C   
36   O  O   . TRP   A 49  ? 0.2971 0.3714 0.3675 0.0397  0.0296  0.0876  49   TRP   A O   
37   C  CB  . TRP   A 49  ? 0.2518 0.3105 0.3209 0.0440  0.0370  0.0859  49   TRP   A CB  
38   C  CG  . TRP   A 49  ? 0.2465 0.3014 0.3136 0.0435  0.0375  0.0828  49   TRP   A CG  
39   C  CD1 . TRP   A 49  ? 0.2447 0.2980 0.3081 0.0410  0.0353  0.0786  49   TRP   A CD1 
40   C  CD2 . TRP   A 49  ? 0.2430 0.2954 0.3117 0.0454  0.0404  0.0837  49   TRP   A CD2 
41   N  NE1 . TRP   A 49  ? 0.2422 0.2924 0.3049 0.0412  0.0365  0.0769  49   TRP   A NE1 
42   C  CE2 . TRP   A 49  ? 0.2605 0.3098 0.3262 0.0439  0.0397  0.0799  49   TRP   A CE2 
43   C  CE3 . TRP   A 49  ? 0.2581 0.3103 0.3306 0.0484  0.0437  0.0874  49   TRP   A CE3 
44   C  CZ2 . TRP   A 49  ? 0.2825 0.3287 0.3486 0.0452  0.0421  0.0796  49   TRP   A CZ2 
45   C  CZ3 . TRP   A 49  ? 0.2841 0.3329 0.3569 0.0497  0.0462  0.0870  49   TRP   A CZ3 
46   C  CH2 . TRP   A 49  ? 0.2881 0.3341 0.3578 0.0480  0.0453  0.0832  49   TRP   A CH2 
47   N  N   . ASN   A 50  ? 0.2745 0.3501 0.3489 0.0417  0.0317  0.0896  50   ASN   A N   
48   C  CA  . ASN   A 50  ? 0.2889 0.3701 0.3629 0.0390  0.0283  0.0888  50   ASN   A CA  
49   C  C   . ASN   A 50  ? 0.3009 0.3789 0.3719 0.0374  0.0277  0.0848  50   ASN   A C   
50   O  O   . ASN   A 50  ? 0.3204 0.4029 0.3920 0.0358  0.0257  0.0848  50   ASN   A O   
51   C  CB  . ASN   A 50  ? 0.3359 0.4251 0.4148 0.0397  0.0278  0.0935  50   ASN   A CB  
52   C  CG  . ASN   A 50  ? 0.4280 0.5163 0.5100 0.0419  0.0305  0.0951  50   ASN   A CG  
53   O  OD1 . ASN   A 50  ? 0.4515 0.5328 0.5320 0.0433  0.0331  0.0931  50   ASN   A OD1 
54   N  ND2 . ASN   A 50  ? 0.4576 0.5530 0.5439 0.0423  0.0298  0.0990  50   ASN   A ND2 
55   N  N   . LYS   A 51  ? 0.2755 0.3458 0.3436 0.0380  0.0295  0.0815  51   LYS   A N   
56   C  CA  . LYS   A 51  ? 0.2436 0.3106 0.3089 0.0366  0.0290  0.0778  51   LYS   A CA  
57   C  C   . LYS   A 51  ? 0.2426 0.3046 0.3031 0.0348  0.0279  0.0734  51   LYS   A C   
58   O  O   . LYS   A 51  ? 0.2408 0.2994 0.3001 0.0354  0.0288  0.0730  51   LYS   A O   
59   C  CB  . LYS   A 51  ? 0.2679 0.3302 0.3340 0.0387  0.0323  0.0778  51   LYS   A CB  
60   C  CG  . LYS   A 51  ? 0.3394 0.4065 0.4105 0.0406  0.0337  0.0821  51   LYS   A CG  
61   C  CD  . LYS   A 51  ? 0.4321 0.4934 0.5034 0.0428  0.0373  0.0818  51   LYS   A CD  
62   C  CE  . LYS   A 51  ? 0.5166 0.5810 0.5931 0.0456  0.0399  0.0866  51   LYS   A CE  
63   N  NZ  . LYS   A 51  ? 0.5605 0.6189 0.6368 0.0476  0.0436  0.0860  51   LYS   A NZ  
64   N  N   . ILE   A 52  ? 0.2320 0.2937 0.2899 0.0327  0.0259  0.0702  52   ILE   A N   
65   C  CA  . ILE   A 52  ? 0.2373 0.2943 0.2909 0.0311  0.0249  0.0661  52   ILE   A CA  
66   C  C   . ILE   A 52  ? 0.2260 0.2754 0.2777 0.0323  0.0275  0.0642  52   ILE   A C   
67   O  O   . ILE   A 52  ? 0.2157 0.2611 0.2650 0.0320  0.0276  0.0623  52   ILE   A O   
68   C  CB  . ILE   A 52  ? 0.2604 0.3186 0.3118 0.0287  0.0224  0.0634  52   ILE   A CB  
69   C  CG1 . ILE   A 52  ? 0.3087 0.3735 0.3608 0.0269  0.0197  0.0645  52   ILE   A CG1 
70   C  CG2 . ILE   A 52  ? 0.2630 0.3155 0.3102 0.0274  0.0219  0.0590  52   ILE   A CG2 
71   C  CD1 . ILE   A 52  ? 0.3599 0.4249 0.4105 0.0261  0.0187  0.0641  52   ILE   A CD1 
72   N  N   . ARG   A 53  ? 0.2190 0.2664 0.2717 0.0336  0.0295  0.0647  53   ARG   A N   
73   C  CA  . ARG   A 53  ? 0.2129 0.2530 0.2638 0.0348  0.0322  0.0631  53   ARG   A CA  
74   C  C   . ARG   A 53  ? 0.2232 0.2617 0.2757 0.0370  0.0347  0.0656  53   ARG   A C   
75   O  O   . ARG   A 53  ? 0.2243 0.2673 0.2806 0.0384  0.0353  0.0694  53   ARG   A O   
76   C  CB  . ARG   A 53  ? 0.2129 0.2513 0.2642 0.0356  0.0338  0.0630  53   ARG   A CB  
77   C  CG  . ARG   A 53  ? 0.2316 0.2706 0.2808 0.0336  0.0316  0.0603  53   ARG   A CG  
78   C  CD  . ARG   A 53  ? 0.2101 0.2432 0.2547 0.0321  0.0309  0.0561  53   ARG   A CD  
79   N  NE  . ARG   A 53  ? 0.2149 0.2412 0.2574 0.0330  0.0335  0.0547  53   ARG   A NE  
80   C  CZ  . ARG   A 53  ? 0.2565 0.2804 0.2979 0.0330  0.0343  0.0535  53   ARG   A CZ  
81   N  NH1 . ARG   A 53  ? 0.2581 0.2862 0.3008 0.0323  0.0328  0.0539  53   ARG   A NH1 
82   N  NH2 . ARG   A 53  ? 0.2790 0.2964 0.3180 0.0336  0.0366  0.0521  53   ARG   A NH2 
83   N  N   . LEU   A 54  ? 0.2219 0.2538 0.2717 0.0372  0.0362  0.0637  54   LEU   A N   
84   C  CA  . LEU   A 54  ? 0.2273 0.2568 0.2782 0.0391  0.0389  0.0658  54   LEU   A CA  
85   C  C   . LEU   A 54  ? 0.2314 0.2593 0.2848 0.0416  0.0423  0.0681  54   LEU   A C   
86   O  O   . LEU   A 54  ? 0.2323 0.2586 0.2851 0.0416  0.0430  0.0671  54   LEU   A O   
87   C  CB  . LEU   A 54  ? 0.2361 0.2585 0.2830 0.0384  0.0397  0.0626  54   LEU   A CB  
88   C  CG  . LEU   A 54  ? 0.2479 0.2711 0.2926 0.0363  0.0369  0.0605  54   LEU   A CG  
89   C  CD1 . LEU   A 54  ? 0.2611 0.2772 0.3022 0.0356  0.0380  0.0576  54   LEU   A CD1 
90   C  CD2 . LEU   A 54  ? 0.2527 0.2809 0.3000 0.0367  0.0361  0.0633  54   LEU   A CD2 
91   N  N   . PRO   A 55  ? 0.2191 0.2465 0.2748 0.0438  0.0447  0.0712  55   PRO   A N   
92   C  CA  . PRO   A 55  ? 0.2289 0.2536 0.2866 0.0463  0.0486  0.0733  55   PRO   A CA  
93   C  C   . PRO   A 55  ? 0.2564 0.2726 0.3099 0.0461  0.0507  0.0699  55   PRO   A C   
94   O  O   . PRO   A 55  ? 0.2554 0.2672 0.3049 0.0444  0.0499  0.0666  55   PRO   A O   
95   C  CB  . PRO   A 55  ? 0.2327 0.2569 0.2925 0.0483  0.0506  0.0763  55   PRO   A CB  
96   C  CG  . PRO   A 55  ? 0.2344 0.2645 0.2951 0.0470  0.0474  0.0773  55   PRO   A CG  
97   C  CD  . PRO   A 55  ? 0.2066 0.2357 0.2633 0.0440  0.0444  0.0729  55   PRO   A CD  
98   N  N   . GLU   A 56  ? 0.2688 0.2830 0.3233 0.0476  0.0534  0.0707  56   GLU   A N   
99   C  CA  . GLU   A 56  ? 0.2977 0.3039 0.3481 0.0472  0.0555  0.0676  56   GLU   A CA  
100  C  C   . GLU   A 56  ? 0.3087 0.3081 0.3581 0.0489  0.0595  0.0682  56   GLU   A C   
101  O  O   . GLU   A 56  ? 0.3332 0.3253 0.3784 0.0483  0.0612  0.0654  56   GLU   A O   
102  C  CB  . GLU   A 56  ? 0.3502 0.3568 0.4014 0.0478  0.0566  0.0677  56   GLU   A CB  
103  C  CG  . GLU   A 56  ? 0.4474 0.4603 0.4995 0.0461  0.0529  0.0671  56   GLU   A CG  
104  C  CD  . GLU   A 56  ? 0.5757 0.5868 0.6266 0.0457  0.0535  0.0656  56   GLU   A CD  
105  O  OE1 . GLU   A 56  ? 0.6040 0.6169 0.6581 0.0476  0.0557  0.0683  56   GLU   A OE1 
106  O  OE2 . GLU   A 56  ? 0.5981 0.6064 0.6449 0.0436  0.0517  0.0620  56   GLU   A OE2 
107  N  N   . TYR   A 57  ? 0.2930 0.2944 0.3458 0.0509  0.0611  0.0717  57   TYR   A N   
108  C  CA  . TYR   A 57  ? 0.3087 0.3036 0.3610 0.0529  0.0654  0.0727  57   TYR   A CA  
109  C  C   . TYR   A 57  ? 0.3099 0.3004 0.3594 0.0522  0.0657  0.0715  57   TYR   A C   
110  O  O   . TYR   A 57  ? 0.3262 0.3113 0.3753 0.0538  0.0694  0.0724  57   TYR   A O   
111  C  CB  . TYR   A 57  ? 0.3134 0.3120 0.3713 0.0562  0.0680  0.0778  57   TYR   A CB  
112  C  CG  . TYR   A 57  ? 0.3215 0.3292 0.3838 0.0564  0.0652  0.0810  57   TYR   A CG  
113  C  CD1 . TYR   A 57  ? 0.3455 0.3539 0.4085 0.0567  0.0649  0.0825  57   TYR   A CD1 
114  C  CD2 . TYR   A 57  ? 0.3330 0.3484 0.3988 0.0563  0.0630  0.0828  57   TYR   A CD2 
115  C  CE1 . TYR   A 57  ? 0.3644 0.3810 0.4311 0.0568  0.0622  0.0855  57   TYR   A CE1 
116  C  CE2 . TYR   A 57  ? 0.3484 0.3720 0.4179 0.0563  0.0604  0.0859  57   TYR   A CE2 
117  C  CZ  . TYR   A 57  ? 0.3675 0.3918 0.4375 0.0566  0.0600  0.0872  57   TYR   A CZ  
118  O  OH  . TYR   A 57  ? 0.4030 0.4353 0.4765 0.0565  0.0575  0.0903  57   TYR   A OH  
119  N  N   . VAL   A 58  ? 0.2848 0.2771 0.3322 0.0497  0.0620  0.0692  58   VAL   A N   
120  C  CA  . VAL   A 58  ? 0.2677 0.2555 0.3122 0.0486  0.0622  0.0676  58   VAL   A CA  
121  C  C   . VAL   A 58  ? 0.2692 0.2539 0.3088 0.0456  0.0598  0.0629  58   VAL   A C   
122  O  O   . VAL   A 58  ? 0.2873 0.2768 0.3270 0.0441  0.0563  0.0617  58   VAL   A O   
123  C  CB  . VAL   A 58  ? 0.2785 0.2716 0.3253 0.0486  0.0601  0.0696  58   VAL   A CB  
124  C  CG1 . VAL   A 58  ? 0.2886 0.2765 0.3320 0.0473  0.0604  0.0676  58   VAL   A CG1 
125  C  CG2 . VAL   A 58  ? 0.2858 0.2826 0.3378 0.0516  0.0623  0.0746  58   VAL   A CG2 
126  N  N   . ILE   A 59  ? 0.2641 0.2408 0.2995 0.0449  0.0619  0.0604  59   ILE   A N   
127  C  CA  . ILE   A 59  ? 0.2827 0.2557 0.3134 0.0422  0.0602  0.0561  59   ILE   A CA  
128  C  C   . ILE   A 59  ? 0.2694 0.2379 0.2966 0.0405  0.0599  0.0539  59   ILE   A C   
129  O  O   . ILE   A 59  ? 0.2679 0.2306 0.2938 0.0412  0.0630  0.0542  59   ILE   A O   
130  C  CB  . ILE   A 59  ? 0.3253 0.2923 0.3537 0.0428  0.0633  0.0550  59   ILE   A CB  
131  C  CG1 . ILE   A 59  ? 0.3594 0.3311 0.3915 0.0446  0.0638  0.0573  59   ILE   A CG1 
132  C  CG2 . ILE   A 59  ? 0.3597 0.3220 0.3828 0.0401  0.0620  0.0508  59   ILE   A CG2 
133  C  CD1 . ILE   A 59  ? 0.3832 0.3609 0.4161 0.0432  0.0598  0.0564  59   ILE   A CD1 
134  N  N   . PRO   A 60  ? 0.2327 0.2031 0.2581 0.0380  0.0562  0.0513  60   PRO   A N   
135  C  CA  . PRO   A 60  ? 0.2269 0.1929 0.2489 0.0361  0.0558  0.0490  60   PRO   A CA  
136  C  C   . PRO   A 60  ? 0.2334 0.1921 0.2505 0.0345  0.0570  0.0458  60   PRO   A C   
137  O  O   . PRO   A 60  ? 0.2336 0.1919 0.2495 0.0342  0.0567  0.0446  60   PRO   A O   
138  C  CB  . PRO   A 60  ? 0.2347 0.2062 0.2571 0.0342  0.0515  0.0477  60   PRO   A CB  
139  C  CG  . PRO   A 60  ? 0.2303 0.2061 0.2538 0.0342  0.0496  0.0475  60   PRO   A CG  
140  C  CD  . PRO   A 60  ? 0.2374 0.2141 0.2640 0.0369  0.0524  0.0506  60   PRO   A CD  
141  N  N   . VAL   A 61  ? 0.2356 0.1885 0.2496 0.0334  0.0583  0.0444  61   VAL   A N   
142  C  CA  . VAL   A 61  ? 0.2660 0.2120 0.2748 0.0313  0.0590  0.0412  61   VAL   A CA  
143  C  C   . VAL   A 61  ? 0.2437 0.1893 0.2500 0.0285  0.0562  0.0387  61   VAL   A C   
144  O  O   . VAL   A 61  ? 0.2415 0.1847 0.2443 0.0263  0.0548  0.0359  61   VAL   A O   
145  C  CB  . VAL   A 61  ? 0.3422 0.2803 0.3487 0.0323  0.0637  0.0415  61   VAL   A CB  
146  C  CG1 . VAL   A 61  ? 0.3650 0.3018 0.3726 0.0329  0.0653  0.0432  61   VAL   A CG1 
147  C  CG2 . VAL   A 61  ? 0.3804 0.3112 0.3811 0.0298  0.0643  0.0381  61   VAL   A CG2 
148  N  N   . HIS   A 62  ? 0.2341 0.1823 0.2422 0.0284  0.0553  0.0397  62   HIS   A N   
149  C  CA  . HIS   A 62  ? 0.2252 0.1726 0.2311 0.0258  0.0531  0.0374  62   HIS   A CA  
150  C  C   . HIS   A 62  ? 0.2177 0.1709 0.2268 0.0262  0.0512  0.0390  62   HIS   A C   
151  O  O   . HIS   A 62  ? 0.2308 0.1856 0.2428 0.0282  0.0528  0.0418  62   HIS   A O   
152  C  CB  . HIS   A 62  ? 0.2374 0.1766 0.2394 0.0248  0.0560  0.0363  62   HIS   A CB  
153  C  CG  . HIS   A 62  ? 0.2520 0.1905 0.2521 0.0221  0.0539  0.0344  62   HIS   A CG  
154  N  ND1 . HIS   A 62  ? 0.2606 0.1986 0.2579 0.0195  0.0513  0.0315  62   HIS   A ND1 
155  C  CD2 . HIS   A 62  ? 0.2591 0.1980 0.2602 0.0219  0.0541  0.0353  62   HIS   A CD2 
156  C  CE1 . HIS   A 62  ? 0.2778 0.2159 0.2745 0.0177  0.0500  0.0308  62   HIS   A CE1 
157  N  NE2 . HIS   A 62  ? 0.2746 0.2132 0.2735 0.0191  0.0516  0.0329  62   HIS   A NE2 
158  N  N   . TYR   A 63  ? 0.2092 0.1656 0.2180 0.0242  0.0478  0.0373  63   TYR   A N   
159  C  CA  . TYR   A 63  ? 0.2023 0.1637 0.2137 0.0242  0.0459  0.0384  63   TYR   A CA  
160  C  C   . TYR   A 63  ? 0.2166 0.1755 0.2257 0.0219  0.0451  0.0365  63   TYR   A C   
161  O  O   . TYR   A 63  ? 0.2242 0.1803 0.2303 0.0198  0.0440  0.0339  63   TYR   A O   
162  C  CB  . TYR   A 63  ? 0.1915 0.1597 0.2047 0.0237  0.0423  0.0380  63   TYR   A CB  
163  C  CG  . TYR   A 63  ? 0.1843 0.1568 0.2003 0.0257  0.0423  0.0399  63   TYR   A CG  
164  C  CD1 . TYR   A 63  ? 0.1924 0.1635 0.2076 0.0260  0.0429  0.0393  63   TYR   A CD1 
165  C  CD2 . TYR   A 63  ? 0.1745 0.1531 0.1941 0.0268  0.0413  0.0423  63   TYR   A CD2 
166  C  CE1 . TYR   A 63  ? 0.1892 0.1647 0.2072 0.0276  0.0427  0.0411  63   TYR   A CE1 
167  C  CE2 . TYR   A 63  ? 0.1785 0.1616 0.2007 0.0283  0.0409  0.0441  63   TYR   A CE2 
168  C  CZ  . TYR   A 63  ? 0.1844 0.1660 0.2058 0.0286  0.0415  0.0434  63   TYR   A CZ  
169  O  OH  . TYR   A 63  ? 0.1955 0.1816 0.2196 0.0300  0.0411  0.0452  63   TYR   A OH  
170  N  N   A ASP   A 64  ? 0.2090 0.1688 0.2196 0.0222  0.0456  0.0380  64   ASP   A N   
171  N  N   B ASP   A 64  ? 0.2086 0.1685 0.2192 0.0222  0.0456  0.0380  64   ASP   A N   
172  C  CA  A ASP   A 64  ? 0.2109 0.1696 0.2200 0.0200  0.0444  0.0365  64   ASP   A CA  
173  C  CA  B ASP   A 64  ? 0.2099 0.1689 0.2192 0.0201  0.0444  0.0366  64   ASP   A CA  
174  C  C   A ASP   A 64  ? 0.2188 0.1846 0.2309 0.0202  0.0417  0.0374  64   ASP   A C   
175  C  C   B ASP   A 64  ? 0.2154 0.1815 0.2276 0.0203  0.0417  0.0374  64   ASP   A C   
176  O  O   A ASP   A 64  ? 0.2194 0.1884 0.2343 0.0220  0.0424  0.0400  64   ASP   A O   
177  O  O   B ASP   A 64  ? 0.2089 0.1785 0.2240 0.0221  0.0422  0.0400  64   ASP   A O   
178  C  CB  A ASP   A 64  ? 0.2338 0.1874 0.2419 0.0202  0.0474  0.0373  64   ASP   A CB  
179  C  CB  B ASP   A 64  ? 0.2354 0.1898 0.2439 0.0204  0.0473  0.0377  64   ASP   A CB  
180  C  CG  A ASP   A 64  ? 0.2706 0.2228 0.2769 0.0177  0.0462  0.0356  64   ASP   A CG  
181  C  CG  B ASP   A 64  ? 0.2990 0.2457 0.3040 0.0200  0.0502  0.0366  64   ASP   A CG  
182  O  OD1 A ASP   A 64  ? 0.2667 0.2228 0.2751 0.0177  0.0450  0.0366  64   ASP   A OD1 
183  O  OD1 B ASP   A 64  ? 0.3124 0.2560 0.3142 0.0177  0.0492  0.0339  64   ASP   A OD1 
184  O  OD2 A ASP   A 64  ? 0.3118 0.2592 0.3147 0.0156  0.0464  0.0333  64   ASP   A OD2 
185  O  OD2 B ASP   A 64  ? 0.3285 0.2721 0.3340 0.0219  0.0534  0.0385  64   ASP   A OD2 
186  N  N   . LEU   A 65  ? 0.2103 0.1789 0.2220 0.0184  0.0387  0.0354  65   LEU   A N   
187  C  CA  . LEU   A 65  ? 0.2106 0.1857 0.2248 0.0184  0.0363  0.0360  65   LEU   A CA  
188  C  C   . LEU   A 65  ? 0.2242 0.1992 0.2379 0.0166  0.0352  0.0349  65   LEU   A C   
189  O  O   . LEU   A 65  ? 0.2539 0.2270 0.2656 0.0146  0.0341  0.0326  65   LEU   A O   
190  C  CB  . LEU   A 65  ? 0.2088 0.1875 0.2233 0.0180  0.0337  0.0347  65   LEU   A CB  
191  C  CG  . LEU   A 65  ? 0.2203 0.1992 0.2351 0.0194  0.0344  0.0353  65   LEU   A CG  
192  C  CD1 . LEU   A 65  ? 0.2240 0.2065 0.2391 0.0187  0.0317  0.0338  65   LEU   A CD1 
193  C  CD2 . LEU   A 65  ? 0.2317 0.2134 0.2494 0.0217  0.0357  0.0384  65   LEU   A CD2 
194  N  N   . LEU   A 66  ? 0.1959 0.1732 0.2114 0.0172  0.0356  0.0367  66   LEU   A N   
195  C  CA  . LEU   A 66  ? 0.2084 0.1866 0.2238 0.0155  0.0344  0.0358  66   LEU   A CA  
196  C  C   . LEU   A 66  ? 0.2150 0.1999 0.2327 0.0157  0.0320  0.0363  66   LEU   A C   
197  O  O   . LEU   A 66  ? 0.2259 0.2142 0.2456 0.0174  0.0322  0.0384  66   LEU   A O   
198  C  CB  . LEU   A 66  ? 0.2149 0.1905 0.2304 0.0159  0.0366  0.0374  66   LEU   A CB  
199  C  CG  . LEU   A 66  ? 0.2373 0.2147 0.2533 0.0145  0.0356  0.0371  66   LEU   A CG  
200  C  CD1 . LEU   A 66  ? 0.2437 0.2190 0.2577 0.0119  0.0343  0.0343  66   LEU   A CD1 
201  C  CD2 . LEU   A 66  ? 0.2623 0.2368 0.2784 0.0151  0.0381  0.0389  66   LEU   A CD2 
202  N  N   . ILE   A 67  ? 0.2122 0.1990 0.2296 0.0141  0.0297  0.0343  67   ILE   A N   
203  C  CA  . ILE   A 67  ? 0.2194 0.2119 0.2386 0.0141  0.0276  0.0344  67   ILE   A CA  
204  C  C   . ILE   A 67  ? 0.2020 0.1955 0.2213 0.0126  0.0267  0.0335  67   ILE   A C   
205  O  O   . ILE   A 67  ? 0.2057 0.1967 0.2237 0.0109  0.0262  0.0317  67   ILE   A O   
206  C  CB  . ILE   A 67  ? 0.2541 0.2483 0.2729 0.0138  0.0257  0.0328  67   ILE   A CB  
207  C  CG1 . ILE   A 67  ? 0.2953 0.2885 0.3139 0.0151  0.0266  0.0334  67   ILE   A CG1 
208  C  CG2 . ILE   A 67  ? 0.2801 0.2799 0.3004 0.0136  0.0236  0.0327  67   ILE   A CG2 
209  C  CD1 . ILE   A 67  ? 0.3219 0.3195 0.3424 0.0167  0.0263  0.0353  67   ILE   A CD1 
210  N  N   . HIS   A 68  ? 0.2044 0.2018 0.2254 0.0130  0.0263  0.0348  68   HIS   A N   
211  C  CA  . HIS   A 68  ? 0.2121 0.2111 0.2334 0.0116  0.0253  0.0340  68   HIS   A CA  
212  C  C   . HIS   A 68  ? 0.2078 0.2121 0.2304 0.0118  0.0235  0.0340  68   HIS   A C   
213  O  O   . HIS   A 68  ? 0.2040 0.2112 0.2276 0.0128  0.0237  0.0357  68   HIS   A O   
214  C  CB  . HIS   A 68  ? 0.2356 0.2340 0.2575 0.0117  0.0269  0.0357  68   HIS   A CB  
215  C  CG  . HIS   A 68  ? 0.2486 0.2494 0.2712 0.0105  0.0259  0.0352  68   HIS   A CG  
216  N  ND1 . HIS   A 68  ? 0.2732 0.2758 0.2968 0.0109  0.0267  0.0369  68   HIS   A ND1 
217  C  CD2 . HIS   A 68  ? 0.2578 0.2599 0.2805 0.0090  0.0243  0.0333  68   HIS   A CD2 
218  C  CE1 . HIS   A 68  ? 0.2798 0.2843 0.3039 0.0096  0.0256  0.0359  68   HIS   A CE1 
219  N  NE2 . HIS   A 68  ? 0.2704 0.2749 0.2941 0.0085  0.0242  0.0338  68   HIS   A NE2 
220  N  N   . ALA   A 69  ? 0.2132 0.2187 0.2357 0.0107  0.0218  0.0320  69   ALA   A N   
221  C  CA  . ALA   A 69  ? 0.2148 0.2249 0.2383 0.0107  0.0203  0.0318  69   ALA   A CA  
222  C  C   . ALA   A 69  ? 0.2149 0.2265 0.2391 0.0096  0.0199  0.0313  69   ALA   A C   
223  O  O   . ALA   A 69  ? 0.2242 0.2339 0.2482 0.0084  0.0198  0.0301  69   ALA   A O   
224  C  CB  . ALA   A 69  ? 0.2328 0.2435 0.2559 0.0104  0.0188  0.0300  69   ALA   A CB  
225  N  N   . GLN   A 70  ? 0.2127 0.2278 0.2377 0.0099  0.0197  0.0322  70   GLN   A N   
226  C  CA  . GLN   A 70  ? 0.2331 0.2501 0.2589 0.0090  0.0195  0.0319  70   GLN   A CA  
227  C  C   . GLN   A 70  ? 0.2394 0.2594 0.2655 0.0087  0.0180  0.0306  70   GLN   A C   
228  O  O   . GLN   A 70  ? 0.2609 0.2836 0.2869 0.0093  0.0177  0.0312  70   GLN   A O   
229  C  CB  . GLN   A 70  ? 0.2635 0.2822 0.2896 0.0097  0.0205  0.0340  70   GLN   A CB  
230  C  CG  . GLN   A 70  ? 0.3028 0.3224 0.3295 0.0088  0.0208  0.0341  70   GLN   A CG  
231  C  CD  . GLN   A 70  ? 0.3318 0.3521 0.3586 0.0095  0.0221  0.0365  70   GLN   A CD  
232  O  OE1 . GLN   A 70  ? 0.3385 0.3620 0.3654 0.0101  0.0218  0.0376  70   GLN   A OE1 
233  N  NE2 . GLN   A 70  ? 0.3657 0.3832 0.3925 0.0094  0.0234  0.0373  70   GLN   A NE2 
234  N  N   . LEU   A 71  ? 0.2400 0.2593 0.2663 0.0078  0.0171  0.0288  71   LEU   A N   
235  C  CA  . LEU   A 71  ? 0.2698 0.2915 0.2964 0.0077  0.0159  0.0275  71   LEU   A CA  
236  C  C   . LEU   A 71  ? 0.3000 0.3248 0.3272 0.0074  0.0158  0.0276  71   LEU   A C   
237  O  O   . LEU   A 71  ? 0.3339 0.3607 0.3611 0.0075  0.0151  0.0267  71   LEU   A O   
238  C  CB  . LEU   A 71  ? 0.2762 0.2965 0.3029 0.0069  0.0149  0.0258  71   LEU   A CB  
239  C  CG  . LEU   A 71  ? 0.3262 0.3433 0.3517 0.0071  0.0147  0.0254  71   LEU   A CG  
240  C  CD1 . LEU   A 71  ? 0.3135 0.3302 0.3392 0.0064  0.0134  0.0237  71   LEU   A CD1 
241  C  CD2 . LEU   A 71  ? 0.3560 0.3734 0.3808 0.0082  0.0149  0.0261  71   LEU   A CD2 
242  N  N   . THR   A 72  ? 0.2891 0.3143 0.3168 0.0071  0.0168  0.0285  72   THR   A N   
243  C  CA  . THR   A 72  ? 0.3066 0.3347 0.3348 0.0069  0.0169  0.0287  72   THR   A CA  
244  C  C   . THR   A 72  ? 0.3091 0.3392 0.3363 0.0075  0.0172  0.0300  72   THR   A C   
245  O  O   . THR   A 72  ? 0.3439 0.3765 0.3709 0.0073  0.0171  0.0299  72   THR   A O   
246  C  CB  . THR   A 72  ? 0.3377 0.3653 0.3666 0.0062  0.0179  0.0293  72   THR   A CB  
247  O  OG1 . THR   A 72  ? 0.3579 0.3836 0.3863 0.0066  0.0189  0.0309  72   THR   A OG1 
248  C  CG2 . THR   A 72  ? 0.3498 0.3763 0.3799 0.0052  0.0175  0.0280  72   THR   A CG2 
249  N  N   . THR   A 73  ? 0.2737 0.3030 0.3004 0.0083  0.0175  0.0315  73   THR   A N   
250  C  CA  . THR   A 73  ? 0.2595 0.2912 0.2855 0.0089  0.0175  0.0330  73   THR   A CA  
251  C  C   . THR   A 73  ? 0.2554 0.2873 0.2809 0.0095  0.0168  0.0330  73   THR   A C   
252  O  O   . THR   A 73  ? 0.2578 0.2920 0.2827 0.0098  0.0165  0.0342  73   THR   A O   
253  C  CB  . THR   A 73  ? 0.2763 0.3076 0.3025 0.0094  0.0187  0.0353  73   THR   A CB  
254  O  OG1 . THR   A 73  ? 0.2610 0.2891 0.2873 0.0100  0.0192  0.0357  73   THR   A OG1 
255  C  CG2 . THR   A 73  ? 0.2872 0.3185 0.3137 0.0088  0.0196  0.0357  73   THR   A CG2 
256  N  N   . LEU   A 74  ? 0.2374 0.2669 0.2630 0.0096  0.0165  0.0319  74   LEU   A N   
257  C  CA  . LEU   A 74  ? 0.2503 0.2795 0.2755 0.0102  0.0159  0.0317  74   LEU   A CA  
258  C  C   . LEU   A 74  ? 0.2631 0.2919 0.2883 0.0113  0.0167  0.0339  74   LEU   A C   
259  O  O   . LEU   A 74  ? 0.2849 0.3143 0.3100 0.0119  0.0163  0.0343  74   LEU   A O   
260  C  CB  . LEU   A 74  ? 0.2622 0.2941 0.2868 0.0099  0.0148  0.0309  74   LEU   A CB  
261  C  CG  . LEU   A 74  ? 0.2897 0.3221 0.3143 0.0091  0.0143  0.0289  74   LEU   A CG  
262  C  CD1 . LEU   A 74  ? 0.3110 0.3458 0.3346 0.0087  0.0135  0.0282  74   LEU   A CD1 
263  C  CD2 . LEU   A 74  ? 0.2924 0.3223 0.3174 0.0089  0.0139  0.0273  74   LEU   A CD2 
264  N  N   . THR   A 75  ? 0.2543 0.2821 0.2800 0.0116  0.0179  0.0354  75   THR   A N   
265  C  CA  . THR   A 75  ? 0.2444 0.2714 0.2704 0.0127  0.0189  0.0376  75   THR   A CA  
266  C  C   . THR   A 75  ? 0.2270 0.2497 0.2528 0.0130  0.0197  0.0369  75   THR   A C   
267  O  O   . THR   A 75  ? 0.2296 0.2499 0.2551 0.0121  0.0197  0.0353  75   THR   A O   
268  C  CB  . THR   A 75  ? 0.2825 0.3101 0.3089 0.0129  0.0200  0.0396  75   THR   A CB  
269  O  OG1 . THR   A 75  ? 0.3266 0.3583 0.3528 0.0126  0.0193  0.0402  75   THR   A OG1 
270  C  CG2 . THR   A 75  ? 0.2903 0.3170 0.3173 0.0143  0.0213  0.0421  75   THR   A CG2 
271  N  N   . PHE   A 76  ? 0.1854 0.2068 0.2113 0.0142  0.0204  0.0382  76   PHE   A N   
272  C  CA  . PHE   A 76  ? 0.1809 0.1978 0.2064 0.0144  0.0216  0.0378  76   PHE   A CA  
273  C  C   . PHE   A 76  ? 0.1889 0.2049 0.2150 0.0158  0.0233  0.0404  76   PHE   A C   
274  O  O   . PHE   A 76  ? 0.1963 0.2155 0.2233 0.0168  0.0232  0.0424  76   PHE   A O   
275  C  CB  . PHE   A 76  ? 0.1769 0.1922 0.2016 0.0142  0.0208  0.0360  76   PHE   A CB  
276  C  CG  . PHE   A 76  ? 0.1685 0.1854 0.1935 0.0152  0.0205  0.0368  76   PHE   A CG  
277  C  CD1 . PHE   A 76  ? 0.1830 0.2038 0.2083 0.0150  0.0190  0.0365  76   PHE   A CD1 
278  C  CD2 . PHE   A 76  ? 0.1744 0.1888 0.1994 0.0164  0.0219  0.0378  76   PHE   A CD2 
279  C  CE1 . PHE   A 76  ? 0.1884 0.2108 0.2140 0.0158  0.0187  0.0372  76   PHE   A CE1 
280  C  CE2 . PHE   A 76  ? 0.1862 0.2023 0.2118 0.0173  0.0216  0.0386  76   PHE   A CE2 
281  C  CZ  . PHE   A 76  ? 0.1793 0.1994 0.2051 0.0169  0.0200  0.0384  76   PHE   A CZ  
282  N  N   . TRP   A 77  ? 0.1931 0.2047 0.2187 0.0160  0.0249  0.0405  77   TRP   A N   
283  C  CA  . TRP   A 77  ? 0.1952 0.2050 0.2213 0.0175  0.0270  0.0429  77   TRP   A CA  
284  C  C   . TRP   A 77  ? 0.2110 0.2160 0.2361 0.0178  0.0281  0.0420  77   TRP   A C   
285  O  O   . TRP   A 77  ? 0.2144 0.2168 0.2381 0.0165  0.0276  0.0396  77   TRP   A O   
286  C  CB  . TRP   A 77  ? 0.2220 0.2302 0.2482 0.0173  0.0283  0.0439  77   TRP   A CB  
287  C  CG  . TRP   A 77  ? 0.2484 0.2608 0.2755 0.0171  0.0276  0.0451  77   TRP   A CG  
288  C  CD1 . TRP   A 77  ? 0.2715 0.2868 0.2997 0.0183  0.0280  0.0479  77   TRP   A CD1 
289  C  CD2 . TRP   A 77  ? 0.2588 0.2731 0.2856 0.0156  0.0262  0.0435  77   TRP   A CD2 
290  N  NE1 . TRP   A 77  ? 0.2835 0.3022 0.3119 0.0174  0.0270  0.0481  77   TRP   A NE1 
291  C  CE2 . TRP   A 77  ? 0.2736 0.2917 0.3011 0.0158  0.0260  0.0454  77   TRP   A CE2 
292  C  CE3 . TRP   A 77  ? 0.2783 0.2915 0.3043 0.0140  0.0253  0.0409  77   TRP   A CE3 
293  C  CZ2 . TRP   A 77  ? 0.2999 0.3204 0.3273 0.0146  0.0250  0.0445  77   TRP   A CZ2 
294  C  CZ3 . TRP   A 77  ? 0.3021 0.3181 0.3284 0.0130  0.0242  0.0401  77   TRP   A CZ3 
295  C  CH2 . TRP   A 77  ? 0.3051 0.3245 0.3319 0.0133  0.0242  0.0419  77   TRP   A CH2 
296  N  N   . GLY   A 78  ? 0.1991 0.2032 0.2249 0.0194  0.0297  0.0439  78   GLY   A N   
297  C  CA  . GLY   A 78  ? 0.2009 0.2000 0.2254 0.0198  0.0312  0.0432  78   GLY   A CA  
298  C  C   . GLY   A 78  ? 0.1836 0.1800 0.2087 0.0215  0.0339  0.0457  78   GLY   A C   
299  O  O   . GLY   A 78  ? 0.2000 0.1993 0.2270 0.0228  0.0345  0.0484  78   GLY   A O   
300  N  N   . THR   A 79  ? 0.1962 0.1869 0.2196 0.0214  0.0357  0.0447  79   THR   A N   
301  C  CA  . THR   A 79  ? 0.1945 0.1818 0.2182 0.0232  0.0386  0.0467  79   THR   A CA  
302  C  C   . THR   A 79  ? 0.1870 0.1715 0.2095 0.0233  0.0391  0.0454  79   THR   A C   
303  O  O   . THR   A 79  ? 0.2103 0.1907 0.2302 0.0218  0.0390  0.0428  79   THR   A O   
304  C  CB  . THR   A 79  ? 0.2226 0.2046 0.2450 0.0228  0.0409  0.0469  79   THR   A CB  
305  O  OG1 . THR   A 79  ? 0.2386 0.2232 0.2620 0.0224  0.0403  0.0479  79   THR   A OG1 
306  C  CG2 . THR   A 79  ? 0.2231 0.2016 0.2460 0.0250  0.0442  0.0492  79   THR   A CG2 
307  N  N   . THR   A 80  ? 0.1778 0.1640 0.2019 0.0253  0.0399  0.0473  80   THR   A N   
308  C  CA  . THR   A 80  ? 0.1810 0.1646 0.2041 0.0257  0.0407  0.0464  80   THR   A CA  
309  C  C   . THR   A 80  ? 0.2062 0.1854 0.2295 0.0276  0.0443  0.0484  80   THR   A C   
310  O  O   . THR   A 80  ? 0.2176 0.1991 0.2434 0.0295  0.0454  0.0515  80   THR   A O   
311  C  CB  . THR   A 80  ? 0.2009 0.1901 0.2260 0.0265  0.0389  0.0472  80   THR   A CB  
312  O  OG1 . THR   A 80  ? 0.1939 0.1862 0.2184 0.0247  0.0358  0.0450  80   THR   A OG1 
313  C  CG2 . THR   A 80  ? 0.1913 0.1780 0.2158 0.0273  0.0401  0.0468  80   THR   A CG2 
314  N  N   . LYS   A 81  ? 0.2060 0.1789 0.2265 0.0271  0.0460  0.0466  81   LYS   A N   
315  C  CA  . LYS   A 81  ? 0.2236 0.1915 0.2440 0.0288  0.0498  0.0482  81   LYS   A CA  
316  C  C   . LYS   A 81  ? 0.2256 0.1921 0.2451 0.0292  0.0502  0.0473  81   LYS   A C   
317  O  O   . LYS   A 81  ? 0.2524 0.2167 0.2691 0.0274  0.0490  0.0444  81   LYS   A O   
318  C  CB  . LYS   A 81  ? 0.2513 0.2119 0.2684 0.0276  0.0519  0.0468  81   LYS   A CB  
319  C  CG  . LYS   A 81  ? 0.3132 0.2747 0.3306 0.0266  0.0513  0.0472  81   LYS   A CG  
320  C  CD  . LYS   A 81  ? 0.3813 0.3352 0.3954 0.0252  0.0535  0.0457  81   LYS   A CD  
321  C  CE  . LYS   A 81  ? 0.4833 0.4379 0.4976 0.0241  0.0529  0.0459  81   LYS   A CE  
322  N  NZ  . LYS   A 81  ? 0.5370 0.4847 0.5477 0.0221  0.0545  0.0439  81   LYS   A NZ  
323  N  N   . VAL   A 82  ? 0.2097 0.1779 0.2316 0.0316  0.0517  0.0498  82   VAL   A N   
324  C  CA  . VAL   A 82  ? 0.2208 0.1882 0.2422 0.0321  0.0522  0.0491  82   VAL   A CA  
325  C  C   . VAL   A 82  ? 0.2292 0.1917 0.2507 0.0342  0.0563  0.0508  82   VAL   A C   
326  O  O   . VAL   A 82  ? 0.2345 0.1988 0.2591 0.0365  0.0581  0.0541  82   VAL   A O   
327  C  CB  . VAL   A 82  ? 0.2421 0.2167 0.2662 0.0326  0.0495  0.0499  82   VAL   A CB  
328  C  CG1 . VAL   A 82  ? 0.2793 0.2597 0.3077 0.0347  0.0496  0.0537  82   VAL   A CG1 
329  C  CG2 . VAL   A 82  ? 0.2355 0.2089 0.2588 0.0329  0.0499  0.0489  82   VAL   A CG2 
330  N  N   . GLU   A 83  ? 0.2318 0.1875 0.2496 0.0334  0.0581  0.0486  83   GLU   A N   
331  C  CA  . GLU   A 83  ? 0.2297 0.1797 0.2469 0.0352  0.0624  0.0497  83   GLU   A CA  
332  C  C   . GLU   A 83  ? 0.2454 0.1986 0.2649 0.0370  0.0626  0.0511  83   GLU   A C   
333  O  O   . GLU   A 83  ? 0.2577 0.2126 0.2761 0.0357  0.0604  0.0491  83   GLU   A O   
334  C  CB  . GLU   A 83  ? 0.2651 0.2069 0.2770 0.0331  0.0639  0.0465  83   GLU   A CB  
335  C  CG  . GLU   A 83  ? 0.3479 0.2859 0.3574 0.0313  0.0641  0.0452  83   GLU   A CG  
336  C  CD  . GLU   A 83  ? 0.4889 0.4191 0.4928 0.0288  0.0651  0.0419  83   GLU   A CD  
337  O  OE1 . GLU   A 83  ? 0.5067 0.4348 0.5084 0.0266  0.0641  0.0402  83   GLU   A OE1 
338  O  OE2 . GLU   A 83  ? 0.5000 0.4263 0.5018 0.0290  0.0668  0.0409  83   GLU   A OE2 
339  N  N   . ILE   A 84  ? 0.2381 0.1928 0.2612 0.0399  0.0652  0.0546  84   ILE   A N   
340  C  CA  . ILE   A 84  ? 0.2406 0.1991 0.2666 0.0417  0.0655  0.0565  84   ILE   A CA  
341  C  C   . ILE   A 84  ? 0.2526 0.2064 0.2793 0.0443  0.0703  0.0585  84   ILE   A C   
342  O  O   . ILE   A 84  ? 0.2709 0.2192 0.2965 0.0450  0.0734  0.0592  84   ILE   A O   
343  C  CB  . ILE   A 84  ? 0.2365 0.2040 0.2676 0.0430  0.0632  0.0596  84   ILE   A CB  
344  C  CG1 . ILE   A 84  ? 0.2474 0.2150 0.2809 0.0448  0.0653  0.0629  84   ILE   A CG1 
345  C  CG2 . ILE   A 84  ? 0.2357 0.2084 0.2664 0.0406  0.0586  0.0578  84   ILE   A CG2 
346  C  CD1 . ILE   A 84  ? 0.2458 0.2217 0.2843 0.0464  0.0638  0.0665  84   ILE   A CD1 
347  N  N   . THR   A 85  ? 0.2664 0.2220 0.2948 0.0456  0.0710  0.0594  85   THR   A N   
348  C  CA  . THR   A 85  ? 0.2997 0.2527 0.3301 0.0486  0.0754  0.0622  85   THR   A CA  
349  C  C   . THR   A 85  ? 0.3124 0.2737 0.3482 0.0505  0.0742  0.0653  85   THR   A C   
350  O  O   . THR   A 85  ? 0.3124 0.2788 0.3486 0.0492  0.0707  0.0642  85   THR   A O   
351  C  CB  . THR   A 85  ? 0.3587 0.3035 0.3850 0.0483  0.0785  0.0598  85   THR   A CB  
352  O  OG1 . THR   A 85  ? 0.4130 0.3599 0.4382 0.0471  0.0763  0.0579  85   THR   A OG1 
353  C  CG2 . THR   A 85  ? 0.3634 0.2998 0.3841 0.0461  0.0798  0.0568  85   THR   A CG2 
354  N  N   . ALA   A 86  ? 0.3200 0.2823 0.3598 0.0536  0.0773  0.0693  86   ALA   A N   
355  C  CA  . ALA   A 86  ? 0.3312 0.3011 0.3763 0.0556  0.0767  0.0728  86   ALA   A CA  
356  C  C   . ALA   A 86  ? 0.3532 0.3193 0.3989 0.0577  0.0808  0.0737  86   ALA   A C   
357  O  O   . ALA   A 86  ? 0.3575 0.3164 0.4017 0.0591  0.0852  0.0741  86   ALA   A O   
358  C  CB  . ALA   A 86  ? 0.3354 0.3105 0.3853 0.0576  0.0768  0.0771  86   ALA   A CB  
359  N  N   . SER   A 87  ? 0.3443 0.3147 0.3918 0.0579  0.0796  0.0740  87   SER   A N   
360  C  CA  . SER   A 87  ? 0.3604 0.3282 0.4089 0.0600  0.0834  0.0752  87   SER   A CA  
361  C  C   . SER   A 87  ? 0.3827 0.3565 0.4380 0.0633  0.0851  0.0805  87   SER   A C   
362  O  O   . SER   A 87  ? 0.3917 0.3637 0.4486 0.0654  0.0885  0.0820  87   SER   A O   
363  C  CB  . SER   A 87  ? 0.3819 0.3507 0.4286 0.0583  0.0815  0.0725  87   SER   A CB  
364  O  OG  . SER   A 87  ? 0.3923 0.3703 0.4424 0.0576  0.0773  0.0736  87   SER   A OG  
365  N  N   . GLN   A 88  ? 0.3823 0.3635 0.4416 0.0637  0.0825  0.0833  88   GLN   A N   
366  C  CA  . GLN   A 88  ? 0.4015 0.3893 0.4673 0.0666  0.0835  0.0887  88   GLN   A CA  
367  C  C   . GLN   A 88  ? 0.4024 0.3907 0.4692 0.0672  0.0834  0.0905  88   GLN   A C   
368  O  O   . GLN   A 88  ? 0.4018 0.3900 0.4656 0.0647  0.0804  0.0880  88   GLN   A O   
369  C  CB  . GLN   A 88  ? 0.4331 0.4311 0.5023 0.0655  0.0789  0.0898  88   GLN   A CB  
370  C  CG  . GLN   A 88  ? 0.4849 0.4858 0.5557 0.0658  0.0788  0.0899  88   GLN   A CG  
371  C  CD  . GLN   A 88  ? 0.5268 0.5381 0.6013 0.0648  0.0744  0.0917  88   GLN   A CD  
372  O  OE1 . GLN   A 88  ? 0.5328 0.5500 0.6102 0.0649  0.0723  0.0943  88   GLN   A OE1 
373  N  NE2 . GLN   A 88  ? 0.5394 0.5531 0.6138 0.0638  0.0730  0.0904  88   GLN   A NE2 
374  N  N   . PRO   A 89  ? 0.3925 0.3821 0.4639 0.0704  0.0865  0.0952  89   PRO   A N   
375  C  CA  . PRO   A 89  ? 0.3873 0.3784 0.4600 0.0709  0.0860  0.0973  89   PRO   A CA  
376  C  C   . PRO   A 89  ? 0.3635 0.3642 0.4383 0.0692  0.0806  0.0982  89   PRO   A C   
377  O  O   . PRO   A 89  ? 0.3724 0.3804 0.4505 0.0692  0.0785  0.0998  89   PRO   A O   
378  C  CB  . PRO   A 89  ? 0.4028 0.3945 0.4808 0.0750  0.0903  0.1027  89   PRO   A CB  
379  C  CG  . PRO   A 89  ? 0.4110 0.3988 0.4891 0.0765  0.0939  0.1024  89   PRO   A CG  
380  C  CD  . PRO   A 89  ? 0.3875 0.3779 0.4634 0.0738  0.0904  0.0990  89   PRO   A CD  
381  N  N   . THR   A 90  ? 0.3250 0.3252 0.3971 0.0671  0.0782  0.0963  90   THR   A N   
382  C  CA  . THR   A 90  ? 0.3034 0.3119 0.3769 0.0654  0.0734  0.0970  90   THR   A CA  
383  C  C   . THR   A 90  ? 0.2954 0.3024 0.3675 0.0648  0.0729  0.0971  90   THR   A C   
384  O  O   . THR   A 90  ? 0.3153 0.3142 0.3836 0.0644  0.0751  0.0947  90   THR   A O   
385  C  CB  . THR   A 90  ? 0.3291 0.3389 0.3990 0.0620  0.0694  0.0925  90   THR   A CB  
386  O  OG1 . THR   A 90  ? 0.3219 0.3400 0.3936 0.0605  0.0650  0.0936  90   THR   A OG1 
387  C  CG2 . THR   A 90  ? 0.3476 0.3494 0.4114 0.0597  0.0694  0.0875  90   THR   A CG2 
388  N  N   . SER   A 91  ? 0.2785 0.2932 0.3536 0.0647  0.0701  0.0999  91   SER   A N   
389  C  CA  . SER   A 91  ? 0.2834 0.2976 0.3571 0.0638  0.0691  0.0999  91   SER   A CA  
390  C  C   . SER   A 91  ? 0.3004 0.3186 0.3716 0.0603  0.0641  0.0968  91   SER   A C   
391  O  O   . SER   A 91  ? 0.3105 0.3296 0.3807 0.0593  0.0626  0.0968  91   SER   A O   
392  C  CB  . SER   A 91  ? 0.3145 0.3342 0.3933 0.0662  0.0697  0.1055  91   SER   A CB  
393  O  OG  . SER   A 91  ? 0.3473 0.3629 0.4285 0.0696  0.0746  0.1084  91   SER   A OG  
394  N  N   . THR   A 92  ? 0.2956 0.3161 0.3657 0.0586  0.0617  0.0943  92   THR   A N   
395  C  CA  . THR   A 92  ? 0.3084 0.3332 0.3766 0.0556  0.0572  0.0918  92   THR   A CA  
396  C  C   . THR   A 92  ? 0.2952 0.3154 0.3590 0.0534  0.0563  0.0867  92   THR   A C   
397  O  O   . THR   A 92  ? 0.2947 0.3130 0.3584 0.0540  0.0576  0.0859  92   THR   A O   
398  C  CB  . THR   A 92  ? 0.3545 0.3884 0.4266 0.0557  0.0547  0.0946  92   THR   A CB  
399  O  OG1 . THR   A 92  ? 0.3913 0.4297 0.4681 0.0581  0.0559  0.0999  92   THR   A OG1 
400  C  CG2 . THR   A 92  ? 0.3678 0.4067 0.4381 0.0527  0.0502  0.0925  92   THR   A CG2 
401  N  N   . ILE   A 93  ? 0.2753 0.2938 0.3354 0.0509  0.0541  0.0834  93   ILE   A N   
402  C  CA  . ILE   A 93  ? 0.2645 0.2792 0.3203 0.0486  0.0528  0.0785  93   ILE   A CA  
403  C  C   . ILE   A 93  ? 0.2458 0.2666 0.3012 0.0462  0.0484  0.0771  93   ILE   A C   
404  O  O   . ILE   A 93  ? 0.2439 0.2677 0.2993 0.0452  0.0464  0.0775  93   ILE   A O   
405  C  CB  . ILE   A 93  ? 0.2739 0.2812 0.3258 0.0476  0.0540  0.0757  93   ILE   A CB  
406  C  CG1 . ILE   A 93  ? 0.3086 0.3094 0.3607 0.0499  0.0587  0.0772  93   ILE   A CG1 
407  C  CG2 . ILE   A 93  ? 0.2673 0.2710 0.3149 0.0450  0.0524  0.0708  93   ILE   A CG2 
408  C  CD1 . ILE   A 93  ? 0.3277 0.3229 0.3773 0.0494  0.0601  0.0762  93   ILE   A CD1 
409  N  N   . ILE   A 94  ? 0.2493 0.2717 0.3044 0.0453  0.0470  0.0756  94   ILE   A N   
410  C  CA  . ILE   A 94  ? 0.2367 0.2644 0.2911 0.0430  0.0430  0.0741  94   ILE   A CA  
411  C  C   . ILE   A 94  ? 0.2357 0.2586 0.2857 0.0408  0.0420  0.0692  94   ILE   A C   
412  O  O   . ILE   A 94  ? 0.2548 0.2728 0.3032 0.0410  0.0436  0.0674  94   ILE   A O   
413  C  CB  . ILE   A 94  ? 0.2540 0.2872 0.3111 0.0433  0.0420  0.0755  94   ILE   A CB  
414  C  CG1 . ILE   A 94  ? 0.2589 0.2967 0.3209 0.0458  0.0435  0.0806  94   ILE   A CG1 
415  C  CG2 . ILE   A 94  ? 0.2564 0.2948 0.3125 0.0407  0.0379  0.0739  94   ILE   A CG2 
416  C  CD1 . ILE   A 94  ? 0.2706 0.3136 0.3343 0.0457  0.0419  0.0833  94   ILE   A CD1 
417  N  N   . LEU   A 95  ? 0.2197 0.2442 0.2679 0.0388  0.0393  0.0674  95   LEU   A N   
418  C  CA  . LEU   A 95  ? 0.2331 0.2539 0.2775 0.0367  0.0380  0.0630  95   LEU   A CA  
419  C  C   . LEU   A 95  ? 0.2105 0.2359 0.2541 0.0345  0.0344  0.0617  95   LEU   A C   
420  O  O   . LEU   A 95  ? 0.2157 0.2470 0.2615 0.0346  0.0330  0.0640  95   LEU   A O   
421  C  CB  . LEU   A 95  ? 0.2567 0.2702 0.2983 0.0365  0.0399  0.0611  95   LEU   A CB  
422  C  CG  . LEU   A 95  ? 0.2529 0.2660 0.2940 0.0362  0.0398  0.0615  95   LEU   A CG  
423  C  CD1 . LEU   A 95  ? 0.2857 0.2920 0.3232 0.0350  0.0406  0.0584  95   LEU   A CD1 
424  C  CD2 . LEU   A 95  ? 0.2802 0.2945 0.3244 0.0385  0.0421  0.0656  95   LEU   A CD2 
425  N  N   . HIS   A 96  ? 0.1726 0.1956 0.2131 0.0326  0.0329  0.0579  96   HIS   A N   
426  C  CA  . HIS   A 96  ? 0.1749 0.2019 0.2146 0.0306  0.0297  0.0564  96   HIS   A CA  
427  C  C   . HIS   A 96  ? 0.1819 0.2082 0.2202 0.0295  0.0289  0.0554  96   HIS   A C   
428  O  O   . HIS   A 96  ? 0.1949 0.2162 0.2316 0.0295  0.0303  0.0542  96   HIS   A O   
429  C  CB  . HIS   A 96  ? 0.1756 0.2008 0.2129 0.0291  0.0284  0.0531  96   HIS   A CB  
430  C  CG  . HIS   A 96  ? 0.1632 0.1902 0.2018 0.0297  0.0285  0.0539  96   HIS   A CG  
431  N  ND1 . HIS   A 96  ? 0.1795 0.2021 0.2172 0.0304  0.0303  0.0528  96   HIS   A ND1 
432  C  CD2 . HIS   A 96  ? 0.1728 0.2056 0.2133 0.0294  0.0270  0.0553  96   HIS   A CD2 
433  C  CE1 . HIS   A 96  ? 0.1876 0.2134 0.2268 0.0306  0.0298  0.0537  96   HIS   A CE1 
434  N  NE2 . HIS   A 96  ? 0.1813 0.2133 0.2222 0.0300  0.0278  0.0552  96   HIS   A NE2 
435  N  N   . SER   A 97  ? 0.1740 0.2053 0.2128 0.0284  0.0267  0.0558  97   SER   A N   
436  C  CA  . SER   A 97  ? 0.1915 0.2226 0.2288 0.0272  0.0257  0.0547  97   SER   A CA  
437  C  C   . SER   A 97  ? 0.1889 0.2256 0.2263 0.0257  0.0230  0.0545  97   SER   A C   
438  O  O   . SER   A 97  ? 0.2061 0.2476 0.2454 0.0261  0.0224  0.0569  97   SER   A O   
439  C  CB  . SER   A 97  ? 0.1968 0.2278 0.2356 0.0285  0.0273  0.0574  97   SER   A CB  
440  O  OG  . SER   A 97  ? 0.2054 0.2359 0.2427 0.0273  0.0266  0.0562  97   SER   A OG  
441  N  N   . HIS   A 98  ? 0.1817 0.2177 0.2168 0.0239  0.0214  0.0517  98   HIS   A N   
442  C  CA  . HIS   A 98  ? 0.1834 0.2241 0.2182 0.0224  0.0191  0.0512  98   HIS   A CA  
443  C  C   . HIS   A 98  ? 0.1952 0.2355 0.2284 0.0212  0.0184  0.0497  98   HIS   A C   
444  O  O   . HIS   A 98  ? 0.1973 0.2336 0.2288 0.0206  0.0185  0.0471  98   HIS   A O   
445  C  CB  . HIS   A 98  ? 0.1913 0.2315 0.2248 0.0214  0.0179  0.0487  98   HIS   A CB  
446  C  CG  . HIS   A 98  ? 0.2349 0.2791 0.2676 0.0197  0.0157  0.0478  98   HIS   A CG  
447  N  ND1 . HIS   A 98  ? 0.2607 0.3102 0.2946 0.0194  0.0148  0.0501  98   HIS   A ND1 
448  C  CD2 . HIS   A 98  ? 0.2664 0.3098 0.2970 0.0181  0.0144  0.0449  98   HIS   A CD2 
449  C  CE1 . HIS   A 98  ? 0.2896 0.3410 0.3218 0.0176  0.0130  0.0484  98   HIS   A CE1 
450  N  NE2 . HIS   A 98  ? 0.2909 0.3387 0.3212 0.0169  0.0128  0.0453  98   HIS   A NE2 
451  N  N   . HIS   A 99  ? 0.1898 0.2340 0.2235 0.0208  0.0176  0.0515  99   HIS   A N   
452  C  CA  . HIS   A 99  ? 0.2086 0.2531 0.2410 0.0196  0.0170  0.0504  99   HIS   A CA  
453  C  C   . HIS   A 99  ? 0.2162 0.2566 0.2484 0.0202  0.0186  0.0503  99   HIS   A C   
454  O  O   . HIS   A 99  ? 0.2564 0.2959 0.2873 0.0192  0.0182  0.0487  99   HIS   A O   
455  C  CB  . HIS   A 99  ? 0.2277 0.2722 0.2581 0.0178  0.0154  0.0473  99   HIS   A CB  
456  C  CG  . HIS   A 99  ? 0.2955 0.3443 0.3256 0.0167  0.0137  0.0475  99   HIS   A CG  
457  N  ND1 . HIS   A 99  ? 0.3365 0.3851 0.3648 0.0153  0.0124  0.0447  99   HIS   A ND1 
458  C  CD2 . HIS   A 99  ? 0.3338 0.3870 0.3651 0.0169  0.0132  0.0501  99   HIS   A CD2 
459  C  CE1 . HIS   A 99  ? 0.3572 0.4099 0.3855 0.0145  0.0112  0.0457  99   HIS   A CE1 
460  N  NE2 . HIS   A 99  ? 0.3623 0.4181 0.3924 0.0153  0.0115  0.0489  99   HIS   A NE2 
461  N  N   . LEU   A 100 ? 0.1909 0.2292 0.2244 0.0219  0.0205  0.0522  100  LEU   A N   
462  C  CA  . LEU   A 100 ? 0.1882 0.2228 0.2216 0.0225  0.0222  0.0523  100  LEU   A CA  
463  C  C   . LEU   A 100 ? 0.2038 0.2410 0.2389 0.0235  0.0230  0.0559  100  LEU   A C   
464  O  O   . LEU   A 100 ? 0.2186 0.2586 0.2555 0.0246  0.0232  0.0585  100  LEU   A O   
465  C  CB  . LEU   A 100 ? 0.1896 0.2191 0.2229 0.0235  0.0241  0.0518  100  LEU   A CB  
466  C  CG  . LEU   A 100 ? 0.1956 0.2222 0.2272 0.0225  0.0233  0.0485  100  LEU   A CG  
467  C  CD1 . LEU   A 100 ? 0.2257 0.2474 0.2570 0.0236  0.0253  0.0483  100  LEU   A CD1 
468  C  CD2 . LEU   A 100 ? 0.2088 0.2340 0.2386 0.0209  0.0223  0.0458  100  LEU   A CD2 
469  N  N   . GLN   A 101 ? 0.1981 0.2344 0.2326 0.0231  0.0234  0.0560  101  GLN   A N   
470  C  CA  . GLN   A 101 ? 0.1972 0.2355 0.2331 0.0241  0.0243  0.0593  101  GLN   A CA  
471  C  C   . GLN   A 101 ? 0.1976 0.2312 0.2342 0.0256  0.0269  0.0603  101  GLN   A C   
472  O  O   . GLN   A 101 ? 0.2009 0.2303 0.2361 0.0250  0.0277  0.0586  101  GLN   A O   
473  C  CB  . GLN   A 101 ? 0.2419 0.2816 0.2766 0.0227  0.0233  0.0587  101  GLN   A CB  
474  C  CG  . GLN   A 101 ? 0.3560 0.4004 0.3898 0.0211  0.0210  0.0579  101  GLN   A CG  
475  C  CD  . GLN   A 101 ? 0.5300 0.5763 0.5628 0.0200  0.0204  0.0581  101  GLN   A CD  
476  O  OE1 . GLN   A 101 ? 0.5844 0.6291 0.6174 0.0204  0.0217  0.0592  101  GLN   A OE1 
477  N  NE2 . GLN   A 101 ? 0.5660 0.6158 0.5976 0.0184  0.0186  0.0570  101  GLN   A NE2 
478  N  N   . ILE   A 102 ? 0.1963 0.2304 0.2349 0.0275  0.0283  0.0632  102  ILE   A N   
479  C  CA  . ILE   A 102 ? 0.2129 0.2421 0.2520 0.0291  0.0311  0.0643  102  ILE   A CA  
480  C  C   . ILE   A 102 ? 0.2258 0.2552 0.2658 0.0298  0.0323  0.0669  102  ILE   A C   
481  O  O   . ILE   A 102 ? 0.2459 0.2801 0.2877 0.0306  0.0317  0.0700  102  ILE   A O   
482  C  CB  . ILE   A 102 ? 0.2317 0.2612 0.2729 0.0310  0.0323  0.0662  102  ILE   A CB  
483  C  CG1 . ILE   A 102 ? 0.2738 0.3028 0.3138 0.0301  0.0310  0.0634  102  ILE   A CG1 
484  C  CG2 . ILE   A 102 ? 0.2512 0.2752 0.2928 0.0328  0.0355  0.0674  102  ILE   A CG2 
485  C  CD1 . ILE   A 102 ? 0.3187 0.3487 0.3605 0.0315  0.0318  0.0649  102  ILE   A CD1 
486  N  N   . SER   A 103 ? 0.2129 0.2373 0.2515 0.0296  0.0337  0.0657  103  SER   A N   
487  C  CA  . SER   A 103 ? 0.2256 0.2499 0.2650 0.0303  0.0351  0.0683  103  SER   A CA  
488  C  C   . SER   A 103 ? 0.2355 0.2564 0.2763 0.0326  0.0381  0.0709  103  SER   A C   
489  O  O   . SER   A 103 ? 0.2519 0.2743 0.2943 0.0337  0.0391  0.0741  103  SER   A O   
490  C  CB  . SER   A 103 ? 0.2590 0.2802 0.2962 0.0286  0.0350  0.0659  103  SER   A CB  
491  O  OG  . SER   A 103 ? 0.2748 0.2898 0.3105 0.0283  0.0364  0.0634  103  SER   A OG  
492  N  N   . ARG   A 104 ? 0.2320 0.2482 0.2723 0.0332  0.0397  0.0696  104  ARG   A N   
493  C  CA  . ARG   A 104 ? 0.2521 0.2642 0.2936 0.0354  0.0431  0.0719  104  ARG   A CA  
494  C  C   . ARG   A 104 ? 0.2563 0.2650 0.2973 0.0360  0.0442  0.0705  104  ARG   A C   
495  O  O   . ARG   A 104 ? 0.2442 0.2509 0.2830 0.0343  0.0430  0.0669  104  ARG   A O   
496  C  CB  . ARG   A 104 ? 0.2889 0.2952 0.3286 0.0349  0.0450  0.0710  104  ARG   A CB  
497  C  CG  . ARG   A 104 ? 0.3710 0.3720 0.4114 0.0370  0.0488  0.0731  104  ARG   A CG  
498  C  CD  . ARG   A 104 ? 0.4808 0.4791 0.5210 0.0373  0.0506  0.0746  104  ARG   A CD  
499  N  NE  . ARG   A 104 ? 0.5608 0.5556 0.5981 0.0349  0.0501  0.0715  104  ARG   A NE  
500  C  CZ  . ARG   A 104 ? 0.6024 0.5918 0.6385 0.0348  0.0525  0.0715  104  ARG   A CZ  
501  N  NH1 . ARG   A 104 ? 0.6043 0.5906 0.6416 0.0370  0.0557  0.0744  104  ARG   A NH1 
502  N  NH2 . ARG   A 104 ? 0.6156 0.6025 0.6493 0.0325  0.0518  0.0687  104  ARG   A NH2 
503  N  N   . ALA   A 105 ? 0.2419 0.2501 0.2852 0.0384  0.0464  0.0733  105  ALA   A N   
504  C  CA  . ALA   A 105 ? 0.2430 0.2473 0.2858 0.0392  0.0480  0.0722  105  ALA   A CA  
505  C  C   . ALA   A 105 ? 0.2460 0.2455 0.2898 0.0415  0.0520  0.0746  105  ALA   A C   
506  O  O   . ALA   A 105 ? 0.2655 0.2678 0.3121 0.0433  0.0530  0.0785  105  ALA   A O   
507  C  CB  . ALA   A 105 ? 0.2416 0.2512 0.2865 0.0399  0.0466  0.0732  105  ALA   A CB  
508  N  N   . THR   A 106 ? 0.2533 0.2456 0.2947 0.0414  0.0543  0.0725  106  THR   A N   
509  C  CA  . THR   A 106 ? 0.2721 0.2587 0.3139 0.0435  0.0585  0.0744  106  THR   A CA  
510  C  C   . THR   A 106 ? 0.2623 0.2440 0.3028 0.0441  0.0606  0.0729  106  THR   A C   
511  O  O   . THR   A 106 ? 0.2549 0.2358 0.2932 0.0423  0.0589  0.0696  106  THR   A O   
512  C  CB  . THR   A 106 ? 0.3301 0.3110 0.3690 0.0421  0.0596  0.0727  106  THR   A CB  
513  O  OG1 . THR   A 106 ? 0.3809 0.3664 0.4205 0.0411  0.0574  0.0735  106  THR   A OG1 
514  C  CG2 . THR   A 106 ? 0.3474 0.3221 0.3864 0.0441  0.0640  0.0747  106  THR   A CG2 
515  N  N   . LEU   A 107 ? 0.2622 0.2408 0.3043 0.0467  0.0642  0.0755  107  LEU   A N   
516  C  CA  . LEU   A 107 ? 0.2718 0.2453 0.3127 0.0474  0.0668  0.0744  107  LEU   A CA  
517  C  C   . LEU   A 107 ? 0.2905 0.2551 0.3286 0.0476  0.0705  0.0736  107  LEU   A C   
518  O  O   . LEU   A 107 ? 0.2942 0.2573 0.3340 0.0495  0.0731  0.0766  107  LEU   A O   
519  C  CB  . LEU   A 107 ? 0.2793 0.2563 0.3243 0.0505  0.0683  0.0782  107  LEU   A CB  
520  C  CG  . LEU   A 107 ? 0.3179 0.2904 0.3620 0.0514  0.0709  0.0773  107  LEU   A CG  
521  C  CD1 . LEU   A 107 ? 0.3220 0.2963 0.3643 0.0493  0.0679  0.0739  107  LEU   A CD1 
522  C  CD2 . LEU   A 107 ? 0.3407 0.3164 0.3895 0.0548  0.0730  0.0817  107  LEU   A CD2 
523  N  N   . ARG   A 108 ? 0.2982 0.2567 0.3320 0.0456  0.0709  0.0697  108  ARG   A N   
524  C  CA  . ARG   A 108 ? 0.3144 0.2638 0.3450 0.0453  0.0746  0.0685  108  ARG   A CA  
525  C  C   . ARG   A 108 ? 0.3219 0.2661 0.3515 0.0467  0.0779  0.0683  108  ARG   A C   
526  O  O   . ARG   A 108 ? 0.3086 0.2546 0.3381 0.0465  0.0766  0.0671  108  ARG   A O   
527  C  CB  . ARG   A 108 ? 0.3369 0.2824 0.3629 0.0418  0.0729  0.0643  108  ARG   A CB  
528  C  CG  . ARG   A 108 ? 0.3914 0.3408 0.4178 0.0402  0.0701  0.0641  108  ARG   A CG  
529  C  CD  . ARG   A 108 ? 0.4428 0.3878 0.4648 0.0369  0.0690  0.0600  108  ARG   A CD  
530  N  NE  . ARG   A 108 ? 0.4884 0.4369 0.5108 0.0354  0.0665  0.0598  108  ARG   A NE  
531  C  CZ  . ARG   A 108 ? 0.5256 0.4735 0.5454 0.0324  0.0642  0.0566  108  ARG   A CZ  
532  N  NH1 . ARG   A 108 ? 0.5294 0.4732 0.5457 0.0305  0.0639  0.0533  108  ARG   A NH1 
533  N  NH2 . ARG   A 108 ? 0.5389 0.4902 0.5594 0.0313  0.0621  0.0568  108  ARG   A NH2 
534  N  N   . LYS   A 109 ? 0.3351 0.2725 0.3640 0.0483  0.0824  0.0696  109  LYS   A N   
535  C  CA  . LYS   A 109 ? 0.3764 0.3072 0.4037 0.0495  0.0864  0.0693  109  LYS   A CA  
536  C  C   . LYS   A 109 ? 0.4379 0.3591 0.4604 0.0480  0.0893  0.0671  109  LYS   A C   
537  O  O   . LYS   A 109 ? 0.4417 0.3620 0.4649 0.0483  0.0903  0.0687  109  LYS   A O   
538  C  CB  . LYS   A 109 ? 0.4234 0.3562 0.4555 0.0536  0.0895  0.0740  109  LYS   A CB  
539  C  CG  . LYS   A 109 ? 0.4903 0.4158 0.5209 0.0552  0.0943  0.0740  109  LYS   A CG  
540  C  CD  . LYS   A 109 ? 0.5318 0.4608 0.5680 0.0593  0.0968  0.0789  109  LYS   A CD  
541  C  CE  . LYS   A 109 ? 0.5627 0.4843 0.5978 0.0613  0.1021  0.0792  109  LYS   A CE  
542  N  NZ  . LYS   A 109 ? 0.5799 0.4935 0.6086 0.0586  0.1029  0.0744  109  LYS   A NZ  
543  N  N   . GLY   A 110 ? 0.4640 0.3786 0.4818 0.0461  0.0903  0.0636  110  GLY   A N   
544  C  CA  . GLY   A 110 ? 0.4981 0.4033 0.5109 0.0443  0.0931  0.0613  110  GLY   A CA  
545  C  C   . GLY   A 110 ? 0.5310 0.4356 0.5406 0.0405  0.0900  0.0582  110  GLY   A C   
546  O  O   . GLY   A 110 ? 0.5548 0.4663 0.5656 0.0391  0.0855  0.0573  110  GLY   A O   
547  N  N   . ARG   A 114 ? 0.5868 0.4643 0.5908 0.0428  0.1057  0.0622  114  ARG   A N   
548  C  CA  . ARG   A 114 ? 0.5835 0.4664 0.5930 0.0469  0.1067  0.0662  114  ARG   A CA  
549  C  C   . ARG   A 114 ? 0.5646 0.4591 0.5789 0.0474  0.1017  0.0677  114  ARG   A C   
550  O  O   . ARG   A 114 ? 0.5739 0.4737 0.5925 0.0503  0.1017  0.0705  114  ARG   A O   
551  C  CB  . ARG   A 114 ? 0.6071 0.4862 0.6149 0.0477  0.1090  0.0650  114  ARG   A CB  
552  N  N   . LEU   A 115 ? 0.5423 0.4408 0.5557 0.0446  0.0974  0.0658  115  LEU   A N   
553  C  CA  . LEU   A 115 ? 0.5212 0.4302 0.5385 0.0447  0.0927  0.0668  115  LEU   A CA  
554  C  C   . LEU   A 115 ? 0.4945 0.4096 0.5173 0.0479  0.0929  0.0717  115  LEU   A C   
555  O  O   . LEU   A 115 ? 0.4962 0.4088 0.5197 0.0489  0.0952  0.0738  115  LEU   A O   
556  C  CB  . LEU   A 115 ? 0.5337 0.4451 0.5489 0.0410  0.0884  0.0638  115  LEU   A CB  
557  C  CG  . LEU   A 115 ? 0.5606 0.4822 0.5792 0.0408  0.0836  0.0645  115  LEU   A CG  
558  C  CD1 . LEU   A 115 ? 0.5721 0.4971 0.5909 0.0407  0.0815  0.0630  115  LEU   A CD1 
559  C  CD2 . LEU   A 115 ? 0.5771 0.5002 0.5936 0.0375  0.0803  0.0619  115  LEU   A CD2 
560  N  N   . SER   A 116 ? 0.4564 0.3788 0.4831 0.0496  0.0910  0.0736  116  SER   A N   
561  C  CA  . SER   A 116 ? 0.4329 0.3627 0.4650 0.0523  0.0903  0.0781  116  SER   A CA  
562  C  C   . SER   A 116 ? 0.4215 0.3603 0.4552 0.0509  0.0851  0.0773  116  SER   A C   
563  O  O   . SER   A 116 ? 0.4210 0.3606 0.4531 0.0494  0.0831  0.0744  116  SER   A O   
564  C  CB  . SER   A 116 ? 0.4288 0.3585 0.4645 0.0562  0.0940  0.0820  116  SER   A CB  
565  O  OG  . SER   A 116 ? 0.4618 0.3949 0.4989 0.0569  0.0930  0.0817  116  SER   A OG  
566  N  N   . GLU   A 117 ? 0.4041 0.3492 0.4405 0.0511  0.0828  0.0795  117  GLU   A N   
567  C  CA  . GLU   A 117 ? 0.3848 0.3387 0.4230 0.0501  0.0781  0.0792  117  GLU   A CA  
568  C  C   . GLU   A 117 ? 0.3755 0.3363 0.4189 0.0529  0.0780  0.0840  117  GLU   A C   
569  O  O   . GLU   A 117 ? 0.3832 0.3429 0.4287 0.0551  0.0807  0.0876  117  GLU   A O   
570  C  CB  . GLU   A 117 ? 0.3913 0.3469 0.4280 0.0475  0.0753  0.0776  117  GLU   A CB  
571  C  CG  . GLU   A 117 ? 0.4649 0.4145 0.4966 0.0443  0.0748  0.0728  117  GLU   A CG  
572  C  CD  . GLU   A 117 ? 0.5033 0.4570 0.5340 0.0415  0.0709  0.0707  117  GLU   A CD  
573  O  OE1 . GLU   A 117 ? 0.4303 0.3904 0.4637 0.0419  0.0688  0.0729  117  GLU   A OE1 
574  O  OE2 . GLU   A 117 ? 0.5995 0.5497 0.6265 0.0388  0.0698  0.0668  117  GLU   A OE2 
575  N  N   . GLU   A 118 ? 0.3541 0.3224 0.3997 0.0528  0.0747  0.0844  118  GLU   A N   
576  C  CA  . GLU   A 118 ? 0.3526 0.3289 0.4030 0.0549  0.0737  0.0888  118  GLU   A CA  
577  C  C   . GLU   A 118 ? 0.3354 0.3193 0.3860 0.0527  0.0687  0.0875  118  GLU   A C   
578  O  O   . GLU   A 118 ? 0.3033 0.2878 0.3520 0.0509  0.0665  0.0842  118  GLU   A O   
579  C  CB  . GLU   A 118 ? 0.4210 0.3985 0.4741 0.0572  0.0752  0.0906  118  GLU   A CB  
580  C  CG  . GLU   A 118 ? 0.5473 0.5170 0.6000 0.0595  0.0804  0.0915  118  GLU   A CG  
581  C  CD  . GLU   A 118 ? 0.6680 0.6378 0.7223 0.0611  0.0819  0.0920  118  GLU   A CD  
582  O  OE1 . GLU   A 118 ? 0.7203 0.6823 0.7720 0.0615  0.0853  0.0903  118  GLU   A OE1 
583  O  OE2 . GLU   A 118 ? 0.6710 0.6488 0.7288 0.0618  0.0795  0.0939  118  GLU   A OE2 
584  N  N   . PRO   A 119 ? 0.3369 0.3266 0.3896 0.0528  0.0668  0.0901  119  PRO   A N   
585  C  CA  . PRO   A 119 ? 0.3325 0.3295 0.3853 0.0508  0.0622  0.0890  119  PRO   A CA  
586  C  C   . PRO   A 119 ? 0.3114 0.3142 0.3668 0.0516  0.0607  0.0901  119  PRO   A C   
587  O  O   . PRO   A 119 ? 0.3250 0.3291 0.3838 0.0543  0.0628  0.0937  119  PRO   A O   
588  C  CB  . PRO   A 119 ? 0.3522 0.3537 0.4071 0.0513  0.0615  0.0924  119  PRO   A CB  
589  C  CG  . PRO   A 119 ? 0.3619 0.3620 0.4199 0.0547  0.0651  0.0969  119  PRO   A CG  
590  C  CD  . PRO   A 119 ? 0.3445 0.3349 0.3998 0.0549  0.0688  0.0944  119  PRO   A CD  
591  N  N   . LEU   A 120 ? 0.2788 0.2847 0.3327 0.0493  0.0573  0.0872  120  LEU   A N   
592  C  CA  . LEU   A 120 ? 0.2787 0.2904 0.3349 0.0497  0.0556  0.0881  120  LEU   A CA  
593  C  C   . LEU   A 120 ? 0.3026 0.3227 0.3603 0.0486  0.0519  0.0895  120  LEU   A C   
594  O  O   . LEU   A 120 ? 0.3267 0.3474 0.3820 0.0464  0.0497  0.0873  120  LEU   A O   
595  C  CB  . LEU   A 120 ? 0.2702 0.2792 0.3236 0.0480  0.0546  0.0837  120  LEU   A CB  
596  C  CG  . LEU   A 120 ? 0.2847 0.2856 0.3362 0.0487  0.0580  0.0819  120  LEU   A CG  
597  C  CD1 . LEU   A 120 ? 0.2829 0.2809 0.3306 0.0462  0.0563  0.0770  120  LEU   A CD1 
598  C  CD2 . LEU   A 120 ? 0.3063 0.3079 0.3609 0.0515  0.0603  0.0849  120  LEU   A CD2 
599  N  N   . GLN   A 121 ? 0.2969 0.3234 0.3583 0.0500  0.0512  0.0930  121  GLN   A N   
600  C  CA  . GLN   A 121 ? 0.2971 0.3317 0.3595 0.0486  0.0475  0.0942  121  GLN   A CA  
601  C  C   . GLN   A 121 ? 0.3001 0.3364 0.3607 0.0465  0.0448  0.0906  121  GLN   A C   
602  O  O   . GLN   A 121 ? 0.2971 0.3316 0.3579 0.0471  0.0457  0.0896  121  GLN   A O   
603  C  CB  . GLN   A 121 ? 0.3498 0.3908 0.4169 0.0508  0.0477  0.0995  121  GLN   A CB  
604  C  CG  . GLN   A 121 ? 0.4315 0.4813 0.4998 0.0493  0.0439  0.1008  121  GLN   A CG  
605  C  CD  . GLN   A 121 ? 0.5476 0.6036 0.6206 0.0515  0.0442  0.1065  121  GLN   A CD  
606  O  OE1 . GLN   A 121 ? 0.5752 0.6295 0.6506 0.0540  0.0471  0.1099  121  GLN   A OE1 
607  N  NE2 . GLN   A 121 ? 0.5714 0.6350 0.6459 0.0504  0.0412  0.1077  121  GLN   A NE2 
608  N  N   . VAL   A 122 ? 0.2857 0.3256 0.3445 0.0440  0.0415  0.0889  122  VAL   A N   
609  C  CA  . VAL   A 122 ? 0.2731 0.3143 0.3300 0.0419  0.0390  0.0853  122  VAL   A CA  
610  C  C   . VAL   A 122 ? 0.2802 0.3295 0.3388 0.0410  0.0361  0.0871  122  VAL   A C   
611  O  O   . VAL   A 122 ? 0.3129 0.3665 0.3718 0.0404  0.0345  0.0889  122  VAL   A O   
612  C  CB  . VAL   A 122 ? 0.2774 0.3154 0.3303 0.0394  0.0377  0.0811  122  VAL   A CB  
613  C  CG1 . VAL   A 122 ? 0.2866 0.3255 0.3374 0.0373  0.0352  0.0775  122  VAL   A CG1 
614  C  CG2 . VAL   A 122 ? 0.2824 0.3125 0.3334 0.0399  0.0404  0.0794  122  VAL   A CG2 
615  N  N   . LEU   A 123 ? 0.2551 0.3064 0.3145 0.0410  0.0353  0.0867  123  LEU   A N   
616  C  CA  . LEU   A 123 ? 0.2570 0.3157 0.3175 0.0397  0.0323  0.0876  123  LEU   A CA  
617  C  C   . LEU   A 123 ? 0.2764 0.3339 0.3339 0.0374  0.0304  0.0831  123  LEU   A C   
618  O  O   . LEU   A 123 ? 0.2712 0.3228 0.3269 0.0375  0.0317  0.0801  123  LEU   A O   
619  C  CB  . LEU   A 123 ? 0.2745 0.3372 0.3391 0.0416  0.0331  0.0914  123  LEU   A CB  
620  C  CG  . LEU   A 123 ? 0.2987 0.3626 0.3670 0.0444  0.0355  0.0963  123  LEU   A CG  
621  C  CD1 . LEU   A 123 ? 0.3006 0.3687 0.3731 0.0461  0.0361  0.0996  123  LEU   A CD1 
622  C  CD2 . LEU   A 123 ? 0.3177 0.3863 0.3865 0.0438  0.0339  0.0989  123  LEU   A CD2 
623  N  N   . GLU   A 124 ? 0.2664 0.3292 0.3232 0.0353  0.0273  0.0826  124  GLU   A N   
624  C  CA  . GLU   A 124 ? 0.2693 0.3310 0.3234 0.0332  0.0256  0.0784  124  GLU   A CA  
625  C  C   . GLU   A 124 ? 0.2774 0.3449 0.3326 0.0322  0.0235  0.0793  124  GLU   A C   
626  O  O   . GLU   A 124 ? 0.2869 0.3605 0.3441 0.0321  0.0223  0.0825  124  GLU   A O   
627  C  CB  . GLU   A 124 ? 0.3136 0.3740 0.3642 0.0310  0.0240  0.0753  124  GLU   A CB  
628  C  CG  . GLU   A 124 ? 0.3900 0.4563 0.4405 0.0295  0.0217  0.0769  124  GLU   A CG  
629  C  CD  . GLU   A 124 ? 0.5051 0.5705 0.5521 0.0271  0.0200  0.0735  124  GLU   A CD  
630  O  OE1 . GLU   A 124 ? 0.4776 0.5377 0.5227 0.0269  0.0208  0.0704  124  GLU   A OE1 
631  O  OE2 . GLU   A 124 ? 0.5709 0.6412 0.6173 0.0255  0.0179  0.0741  124  GLU   A OE2 
632  N  N   . HIS   A 125 ? 0.2533 0.3191 0.3073 0.0314  0.0230  0.0765  125  HIS   A N   
633  C  CA  . HIS   A 125 ? 0.2503 0.3211 0.3048 0.0301  0.0209  0.0766  125  HIS   A CA  
634  C  C   . HIS   A 125 ? 0.2589 0.3272 0.3097 0.0277  0.0193  0.0720  125  HIS   A C   
635  O  O   . HIS   A 125 ? 0.2542 0.3189 0.3040 0.0278  0.0198  0.0695  125  HIS   A O   
636  C  CB  . HIS   A 125 ? 0.2788 0.3500 0.3360 0.0316  0.0222  0.0781  125  HIS   A CB  
637  C  CG  . HIS   A 125 ? 0.3621 0.4396 0.4205 0.0303  0.0200  0.0793  125  HIS   A CG  
638  N  ND1 . HIS   A 125 ? 0.3925 0.4708 0.4483 0.0278  0.0177  0.0761  125  HIS   A ND1 
639  C  CD2 . HIS   A 125 ? 0.3869 0.4702 0.4491 0.0312  0.0199  0.0834  125  HIS   A CD2 
640  C  CE1 . HIS   A 125 ? 0.4083 0.4925 0.4659 0.0271  0.0163  0.0782  125  HIS   A CE1 
641  N  NE2 . HIS   A 125 ? 0.4011 0.4888 0.4627 0.0290  0.0174  0.0826  125  HIS   A NE2 
642  N  N   . PRO   A 126 ? 0.2564 0.3266 0.3050 0.0258  0.0173  0.0708  126  PRO   A N   
643  C  CA  . PRO   A 126 ? 0.2616 0.3291 0.3067 0.0237  0.0160  0.0665  126  PRO   A CA  
644  C  C   . PRO   A 126 ? 0.2737 0.3421 0.3182 0.0226  0.0148  0.0647  126  PRO   A C   
645  O  O   . PRO   A 126 ? 0.2542 0.3184 0.2965 0.0220  0.0148  0.0612  126  PRO   A O   
646  C  CB  . PRO   A 126 ? 0.2806 0.3509 0.3240 0.0219  0.0143  0.0663  126  PRO   A CB  
647  C  CG  . PRO   A 126 ? 0.2946 0.3671 0.3402 0.0233  0.0152  0.0701  126  PRO   A CG  
648  C  CD  . PRO   A 126 ? 0.2677 0.3418 0.3168 0.0254  0.0165  0.0733  126  PRO   A CD  
649  N  N   . ARG   A 127 ? 0.2874 0.3610 0.3336 0.0222  0.0137  0.0668  127  ARG   A N   
650  C  CA  . ARG   A 127 ? 0.3088 0.3831 0.3544 0.0210  0.0126  0.0651  127  ARG   A CA  
651  C  C   . ARG   A 127 ? 0.2909 0.3608 0.3372 0.0226  0.0145  0.0642  127  ARG   A C   
652  O  O   . ARG   A 127 ? 0.3094 0.3766 0.3538 0.0217  0.0141  0.0611  127  ARG   A O   
653  C  CB  . ARG   A 127 ? 0.3681 0.4493 0.4157 0.0202  0.0112  0.0680  127  ARG   A CB  
654  C  CG  . ARG   A 127 ? 0.4769 0.5625 0.5229 0.0178  0.0089  0.0683  127  ARG   A CG  
655  C  CD  . ARG   A 127 ? 0.5706 0.6627 0.6183 0.0166  0.0073  0.0707  127  ARG   A CD  
656  N  NE  . ARG   A 127 ? 0.6532 0.7450 0.6991 0.0148  0.0061  0.0680  127  ARG   A NE  
657  C  CZ  . ARG   A 127 ? 0.7082 0.7997 0.7557 0.0155  0.0067  0.0682  127  ARG   A CZ  
658  N  NH1 . ARG   A 127 ? 0.7103 0.8019 0.7613 0.0181  0.0085  0.0709  127  ARG   A NH1 
659  N  NH2 . ARG   A 127 ? 0.7202 0.8113 0.7659 0.0137  0.0056  0.0657  127  ARG   A NH2 
660  N  N   . GLN   A 128 ? 0.2682 0.3370 0.3172 0.0250  0.0167  0.0667  128  GLN   A N   
661  C  CA  . GLN   A 128 ? 0.2554 0.3194 0.3046 0.0266  0.0188  0.0657  128  GLN   A CA  
662  C  C   . GLN   A 128 ? 0.2191 0.2763 0.2657 0.0268  0.0200  0.0627  128  GLN   A C   
663  O  O   . GLN   A 128 ? 0.2107 0.2631 0.2570 0.0279  0.0218  0.0616  128  GLN   A O   
664  C  CB  . GLN   A 128 ? 0.2783 0.3435 0.3314 0.0292  0.0211  0.0697  128  GLN   A CB  
665  C  CG  . GLN   A 128 ? 0.3315 0.4030 0.3876 0.0291  0.0202  0.0725  128  GLN   A CG  
666  C  CD  . GLN   A 128 ? 0.3621 0.4365 0.4225 0.0316  0.0220  0.0771  128  GLN   A CD  
667  O  OE1 . GLN   A 128 ? 0.4273 0.5079 0.4904 0.0313  0.0209  0.0800  128  GLN   A OE1 
668  N  NE2 . GLN   A 128 ? 0.3268 0.3970 0.3882 0.0339  0.0248  0.0781  128  GLN   A NE2 
669  N  N   . GLU   A 129 ? 0.2049 0.2616 0.2498 0.0258  0.0192  0.0617  129  GLU   A N   
670  C  CA  . GLU   A 129 ? 0.1892 0.2401 0.2318 0.0259  0.0201  0.0592  129  GLU   A CA  
671  C  C   . GLU   A 129 ? 0.1943 0.2413 0.2382 0.0281  0.0230  0.0606  129  GLU   A C   
672  O  O   . GLU   A 129 ? 0.1966 0.2379 0.2387 0.0283  0.0243  0.0584  129  GLU   A O   
673  C  CB  . GLU   A 129 ? 0.1893 0.2368 0.2292 0.0245  0.0193  0.0552  129  GLU   A CB  
674  C  CG  . GLU   A 129 ? 0.2227 0.2739 0.2612 0.0223  0.0167  0.0539  129  GLU   A CG  
675  C  CD  . GLU   A 129 ? 0.2492 0.2976 0.2852 0.0209  0.0157  0.0502  129  GLU   A CD  
676  O  OE1 . GLU   A 129 ? 0.2024 0.2460 0.2375 0.0215  0.0168  0.0486  129  GLU   A OE1 
677  O  OE2 . GLU   A 129 ? 0.2941 0.3451 0.3289 0.0192  0.0138  0.0490  129  GLU   A OE2 
678  N  N   . GLN   A 130 ? 0.1810 0.2309 0.2279 0.0297  0.0241  0.0645  130  GLN   A N   
679  C  CA  . GLN   A 130 ? 0.1980 0.2443 0.2463 0.0320  0.0271  0.0663  130  GLN   A CA  
680  C  C   . GLN   A 130 ? 0.2047 0.2519 0.2541 0.0329  0.0279  0.0688  130  GLN   A C   
681  O  O   . GLN   A 130 ? 0.2155 0.2675 0.2654 0.0320  0.0261  0.0701  130  GLN   A O   
682  C  CB  . GLN   A 130 ? 0.2058 0.2546 0.2573 0.0337  0.0283  0.0692  130  GLN   A CB  
683  C  CG  . GLN   A 130 ? 0.1883 0.2350 0.2386 0.0332  0.0282  0.0668  130  GLN   A CG  
684  C  CD  . GLN   A 130 ? 0.2200 0.2704 0.2735 0.0344  0.0288  0.0695  130  GLN   A CD  
685  O  OE1 . GLN   A 130 ? 0.2327 0.2878 0.2896 0.0356  0.0291  0.0733  130  GLN   A OE1 
686  N  NE2 . GLN   A 130 ? 0.2222 0.2707 0.2750 0.0342  0.0291  0.0678  130  GLN   A NE2 
687  N  N   . ILE   A 131 ? 0.2021 0.2442 0.2515 0.0345  0.0306  0.0692  131  ILE   A N   
688  C  CA  . ILE   A 131 ? 0.2143 0.2567 0.2653 0.0358  0.0320  0.0721  131  ILE   A CA  
689  C  C   . ILE   A 131 ? 0.2258 0.2661 0.2793 0.0385  0.0352  0.0748  131  ILE   A C   
690  O  O   . ILE   A 131 ? 0.2254 0.2622 0.2785 0.0391  0.0366  0.0735  131  ILE   A O   
691  C  CB  . ILE   A 131 ? 0.2328 0.2706 0.2812 0.0350  0.0324  0.0700  131  ILE   A CB  
692  C  CG1 . ILE   A 131 ? 0.2606 0.2911 0.3063 0.0349  0.0340  0.0667  131  ILE   A CG1 
693  C  CG2 . ILE   A 131 ? 0.2151 0.2560 0.2617 0.0327  0.0295  0.0683  131  ILE   A CG2 
694  C  CD1 . ILE   A 131 ? 0.2706 0.2959 0.3141 0.0344  0.0351  0.0652  131  ILE   A CD1 
695  N  N   . ALA   A 132 ? 0.2263 0.2690 0.2826 0.0403  0.0364  0.0788  132  ALA   A N   
696  C  CA  . ALA   A 132 ? 0.2451 0.2857 0.3041 0.0431  0.0397  0.0817  132  ALA   A CA  
697  C  C   . ALA   A 132 ? 0.2383 0.2751 0.2970 0.0441  0.0418  0.0828  132  ALA   A C   
698  O  O   . ALA   A 132 ? 0.2661 0.3059 0.3249 0.0435  0.0405  0.0840  132  ALA   A O   
699  C  CB  . ALA   A 132 ? 0.2484 0.2961 0.3119 0.0445  0.0394  0.0861  132  ALA   A CB  
700  N  N   . LEU   A 133 ? 0.2414 0.2714 0.2993 0.0455  0.0451  0.0821  133  LEU   A N   
701  C  CA  . LEU   A 133 ? 0.2543 0.2796 0.3117 0.0466  0.0476  0.0831  133  LEU   A CA  
702  C  C   . LEU   A 133 ? 0.2631 0.2881 0.3241 0.0498  0.0510  0.0872  133  LEU   A C   
703  O  O   . LEU   A 133 ? 0.2564 0.2787 0.3179 0.0510  0.0529  0.0870  133  LEU   A O   
704  C  CB  . LEU   A 133 ? 0.2625 0.2797 0.3158 0.0455  0.0489  0.0790  133  LEU   A CB  
705  C  CG  . LEU   A 133 ? 0.2818 0.2991 0.3317 0.0424  0.0458  0.0747  133  LEU   A CG  
706  C  CD1 . LEU   A 133 ? 0.2991 0.3086 0.3452 0.0414  0.0471  0.0710  133  LEU   A CD1 
707  C  CD2 . LEU   A 133 ? 0.2847 0.3063 0.3344 0.0410  0.0432  0.0750  133  LEU   A CD2 
708  N  N   . LEU   A 134 ? 0.2778 0.3054 0.3413 0.0512  0.0516  0.0910  134  LEU   A N   
709  C  CA  . LEU   A 134 ? 0.3009 0.3292 0.3684 0.0544  0.0547  0.0957  134  LEU   A CA  
710  C  C   . LEU   A 134 ? 0.2895 0.3107 0.3561 0.0559  0.0584  0.0962  134  LEU   A C   
711  O  O   . LEU   A 134 ? 0.2935 0.3141 0.3589 0.0551  0.0578  0.0962  134  LEU   A O   
712  C  CB  . LEU   A 134 ? 0.3274 0.3644 0.3987 0.0549  0.0527  0.1000  134  LEU   A CB  
713  C  CG  . LEU   A 134 ? 0.3774 0.4221 0.4493 0.0530  0.0485  0.0997  134  LEU   A CG  
714  C  CD1 . LEU   A 134 ? 0.3936 0.4465 0.4692 0.0536  0.0470  0.1044  134  LEU   A CD1 
715  C  CD2 . LEU   A 134 ? 0.4111 0.4564 0.4838 0.0531  0.0486  0.0987  134  LEU   A CD2 
716  N  N   . ALA   A 135 ? 0.2915 0.3073 0.3587 0.0580  0.0622  0.0968  135  ALA   A N   
717  C  CA  . ALA   A 135 ? 0.3045 0.3126 0.3705 0.0594  0.0662  0.0971  135  ALA   A CA  
718  C  C   . ALA   A 135 ? 0.3159 0.3265 0.3867 0.0628  0.0687  0.1028  135  ALA   A C   
719  O  O   . ALA   A 135 ? 0.3233 0.3397 0.3982 0.0644  0.0685  0.1060  135  ALA   A O   
720  C  CB  . ALA   A 135 ? 0.3155 0.3160 0.3791 0.0598  0.0692  0.0944  135  ALA   A CB  
721  N  N   . PRO   A 136 ? 0.3308 0.3368 0.4010 0.0638  0.0713  0.1040  136  PRO   A N   
722  C  CA  . PRO   A 136 ? 0.3355 0.3437 0.4104 0.0671  0.0738  0.1096  136  PRO   A CA  
723  C  C   . PRO   A 136 ? 0.3454 0.3501 0.4227 0.0702  0.0782  0.1119  136  PRO   A C   
724  O  O   . PRO   A 136 ? 0.3510 0.3580 0.4327 0.0733  0.0804  0.1169  136  PRO   A O   
725  C  CB  . PRO   A 136 ? 0.3626 0.3656 0.4352 0.0668  0.0753  0.1094  136  PRO   A CB  
726  C  CG  . PRO   A 136 ? 0.3750 0.3701 0.4420 0.0644  0.0758  0.1039  136  PRO   A CG  
727  C  CD  . PRO   A 136 ? 0.3429 0.3421 0.4085 0.0619  0.0718  0.1005  136  PRO   A CD  
728  N  N   . GLU   A 137 ? 0.3302 0.3293 0.4047 0.0697  0.0796  0.1083  137  GLU   A N   
729  C  CA  . GLU   A 137 ? 0.3309 0.3260 0.4072 0.0724  0.0839  0.1098  137  GLU   A CA  
730  C  C   . GLU   A 137 ? 0.3379 0.3308 0.4113 0.0707  0.0832  0.1056  137  GLU   A C   
731  O  O   . GLU   A 137 ? 0.3285 0.3204 0.3977 0.0675  0.0802  0.1011  137  GLU   A O   
732  C  CB  . GLU   A 137 ? 0.3676 0.3535 0.4425 0.0742  0.0891  0.1103  137  GLU   A CB  
733  C  CG  . GLU   A 137 ? 0.4215 0.3980 0.4898 0.0717  0.0900  0.1051  137  GLU   A CG  
734  C  CD  . GLU   A 137 ? 0.4801 0.4498 0.5474 0.0729  0.0937  0.1063  137  GLU   A CD  
735  O  OE1 . GLU   A 137 ? 0.5214 0.4952 0.5915 0.0739  0.0930  0.1097  137  GLU   A OE1 
736  O  OE2 . GLU   A 137 ? 0.4667 0.4269 0.5303 0.0728  0.0973  0.1039  137  GLU   A OE2 
737  N  N   . PRO   A 138 ? 0.3310 0.3238 0.4068 0.0728  0.0855  0.1070  138  PRO   A N   
738  C  CA  . PRO   A 138 ? 0.3376 0.3288 0.4107 0.0711  0.0846  0.1031  138  PRO   A CA  
739  C  C   . PRO   A 138 ? 0.3492 0.3304 0.4161 0.0693  0.0863  0.0981  138  PRO   A C   
740  O  O   . PRO   A 138 ? 0.3539 0.3276 0.4191 0.0703  0.0901  0.0982  138  PRO   A O   
741  C  CB  . PRO   A 138 ? 0.3494 0.3422 0.4268 0.0742  0.0875  0.1064  138  PRO   A CB  
742  C  CG  . PRO   A 138 ? 0.3507 0.3485 0.4339 0.0772  0.0888  0.1123  138  PRO   A CG  
743  C  CD  . PRO   A 138 ? 0.3309 0.3252 0.4121 0.0768  0.0892  0.1123  138  PRO   A CD  
744  N  N   . LEU   A 139 ? 0.3400 0.3209 0.4034 0.0664  0.0835  0.0938  139  LEU   A N   
745  C  CA  . LEU   A 139 ? 0.3484 0.3202 0.4059 0.0646  0.0849  0.0891  139  LEU   A CA  
746  C  C   . LEU   A 139 ? 0.3730 0.3392 0.4308 0.0669  0.0898  0.0898  139  LEU   A C   
747  O  O   . LEU   A 139 ? 0.3899 0.3609 0.4518 0.0689  0.0902  0.0925  139  LEU   A O   
748  C  CB  . LEU   A 139 ? 0.3278 0.3019 0.3824 0.0614  0.0807  0.0849  139  LEU   A CB  
749  C  CG  . LEU   A 139 ? 0.3284 0.3043 0.3804 0.0583  0.0767  0.0824  139  LEU   A CG  
750  C  CD1 . LEU   A 139 ? 0.3177 0.3024 0.3738 0.0587  0.0738  0.0856  139  LEU   A CD1 
751  C  CD2 . LEU   A 139 ? 0.3250 0.3016 0.3738 0.0554  0.0733  0.0781  139  LEU   A CD2 
752  N  N   . LEU   A 140 ? 0.3797 0.3360 0.4331 0.0666  0.0933  0.0874  140  LEU   A N   
753  C  CA  . LEU   A 140 ? 0.4005 0.3507 0.4534 0.0685  0.0981  0.0876  140  LEU   A CA  
754  C  C   . LEU   A 140 ? 0.4054 0.3542 0.4546 0.0662  0.0964  0.0835  140  LEU   A C   
755  O  O   . LEU   A 140 ? 0.3966 0.3436 0.4413 0.0629  0.0935  0.0794  140  LEU   A O   
756  C  CB  . LEU   A 140 ? 0.4251 0.3649 0.4743 0.0690  0.1027  0.0867  140  LEU   A CB  
757  C  CG  . LEU   A 140 ? 0.4761 0.4163 0.5285 0.0713  0.1047  0.0908  140  LEU   A CG  
758  C  CD1 . LEU   A 140 ? 0.5031 0.4324 0.5512 0.0712  0.1091  0.0893  140  LEU   A CD1 
759  C  CD2 . LEU   A 140 ? 0.4816 0.4270 0.5408 0.0754  0.1070  0.0963  140  LEU   A CD2 
760  N  N   . VAL   A 141 ? 0.4023 0.3528 0.4539 0.0679  0.0978  0.0848  141  VAL   A N   
761  C  CA  . VAL   A 141 ? 0.4024 0.3522 0.4511 0.0660  0.0963  0.0813  141  VAL   A CA  
762  C  C   . VAL   A 141 ? 0.3926 0.3319 0.4341 0.0638  0.0982  0.0767  141  VAL   A C   
763  O  O   . VAL   A 141 ? 0.3958 0.3272 0.4354 0.0651  0.1029  0.0770  141  VAL   A O   
764  C  CB  . VAL   A 141 ? 0.4370 0.3900 0.4900 0.0687  0.0984  0.0843  141  VAL   A CB  
765  C  CG1 . VAL   A 141 ? 0.4489 0.4000 0.4987 0.0670  0.0977  0.0809  141  VAL   A CG1 
766  C  CG2 . VAL   A 141 ? 0.4411 0.4053 0.5008 0.0701  0.0955  0.0885  141  VAL   A CG2 
767  N  N   . GLY   A 142 ? 0.3862 0.3256 0.4238 0.0605  0.0946  0.0726  142  GLY   A N   
768  C  CA  . GLY   A 142 ? 0.4008 0.3312 0.4315 0.0581  0.0958  0.0681  142  GLY   A CA  
769  C  C   . GLY   A 142 ? 0.4260 0.3506 0.4525 0.0560  0.0959  0.0659  142  GLY   A C   
770  O  O   . GLY   A 142 ? 0.4612 0.3787 0.4818 0.0536  0.0965  0.0621  142  GLY   A O   
771  N  N   . LEU   A 143 ? 0.4078 0.3353 0.4371 0.0569  0.0954  0.0683  143  LEU   A N   
772  C  CA  . LEU   A 143 ? 0.4074 0.3298 0.4330 0.0550  0.0955  0.0664  143  LEU   A CA  
773  C  C   . LEU   A 143 ? 0.3775 0.3052 0.4024 0.0521  0.0900  0.0644  143  LEU   A C   
774  O  O   . LEU   A 143 ? 0.3488 0.2852 0.3777 0.0525  0.0866  0.0661  143  LEU   A O   
775  C  CB  . LEU   A 143 ? 0.4218 0.3432 0.4504 0.0576  0.0986  0.0702  143  LEU   A CB  
776  C  CG  . LEU   A 143 ? 0.4698 0.3851 0.4991 0.0607  0.1047  0.0723  143  LEU   A CG  
777  C  CD1 . LEU   A 143 ? 0.4831 0.3970 0.5151 0.0631  0.1076  0.0758  143  LEU   A CD1 
778  C  CD2 . LEU   A 143 ? 0.5004 0.4051 0.5230 0.0589  0.1077  0.0684  143  LEU   A CD2 
779  N  N   . PRO   A 144 ? 0.3765 0.2990 0.3963 0.0491  0.0892  0.0609  144  PRO   A N   
780  C  CA  . PRO   A 144 ? 0.3560 0.2834 0.3753 0.0464  0.0841  0.0590  144  PRO   A CA  
781  C  C   . PRO   A 144 ? 0.3202 0.2522 0.3428 0.0472  0.0829  0.0616  144  PRO   A C   
782  O  O   . PRO   A 144 ? 0.3372 0.2657 0.3603 0.0486  0.0860  0.0635  144  PRO   A O   
783  C  CB  . PRO   A 144 ? 0.3837 0.3035 0.3965 0.0431  0.0841  0.0547  144  PRO   A CB  
784  C  CG  . PRO   A 144 ? 0.4053 0.3162 0.4157 0.0442  0.0894  0.0550  144  PRO   A CG  
785  C  CD  . PRO   A 144 ? 0.3960 0.3079 0.4104 0.0479  0.0928  0.0585  144  PRO   A CD  
786  N  N   . TYR   A 145 ? 0.2832 0.2234 0.3082 0.0463  0.0784  0.0618  145  TYR   A N   
787  C  CA  . TYR   A 145 ? 0.2762 0.2213 0.3037 0.0463  0.0765  0.0636  145  TYR   A CA  
788  C  C   . TYR   A 145 ? 0.2659 0.2141 0.2915 0.0432  0.0719  0.0605  145  TYR   A C   
789  O  O   . TYR   A 145 ? 0.2546 0.2037 0.2785 0.0416  0.0698  0.0580  145  TYR   A O   
790  C  CB  . TYR   A 145 ? 0.2717 0.2252 0.3050 0.0488  0.0755  0.0677  145  TYR   A CB  
791  C  CG  . TYR   A 145 ? 0.2876 0.2394 0.3239 0.0523  0.0798  0.0715  145  TYR   A CG  
792  C  CD1 . TYR   A 145 ? 0.3006 0.2506 0.3377 0.0540  0.0824  0.0723  145  TYR   A CD1 
793  C  CD2 . TYR   A 145 ? 0.2952 0.2476 0.3339 0.0539  0.0813  0.0747  145  TYR   A CD2 
794  C  CE1 . TYR   A 145 ? 0.3170 0.2655 0.3572 0.0574  0.0866  0.0760  145  TYR   A CE1 
795  C  CE2 . TYR   A 145 ? 0.3030 0.2539 0.3448 0.0573  0.0854  0.0785  145  TYR   A CE2 
796  C  CZ  . TYR   A 145 ? 0.3226 0.2716 0.3652 0.0591  0.0881  0.0792  145  TYR   A CZ  
797  O  OH  . TYR   A 145 ? 0.3478 0.2956 0.3939 0.0626  0.0923  0.0831  145  TYR   A OH  
798  N  N   . THR   A 146 ? 0.2507 0.2011 0.2768 0.0423  0.0703  0.0609  146  THR   A N   
799  C  CA  . THR   A 146 ? 0.2591 0.2130 0.2839 0.0395  0.0660  0.0584  146  THR   A CA  
800  C  C   . THR   A 146 ? 0.2494 0.2114 0.2781 0.0402  0.0635  0.0609  146  THR   A C   
801  O  O   . THR   A 146 ? 0.2529 0.2152 0.2832 0.0413  0.0648  0.0633  146  THR   A O   
802  C  CB  . THR   A 146 ? 0.2772 0.2252 0.2978 0.0370  0.0663  0.0555  146  THR   A CB  
803  O  OG1 . THR   A 146 ? 0.3215 0.2617 0.3380 0.0362  0.0687  0.0531  146  THR   A OG1 
804  C  CG2 . THR   A 146 ? 0.2669 0.2187 0.2864 0.0343  0.0620  0.0530  146  THR   A CG2 
805  N  N   . VAL   A 147 ? 0.2408 0.2093 0.2709 0.0396  0.0601  0.0605  147  VAL   A N   
806  C  CA  . VAL   A 147 ? 0.2388 0.2149 0.2719 0.0397  0.0573  0.0624  147  VAL   A CA  
807  C  C   . VAL   A 147 ? 0.2295 0.2058 0.2603 0.0370  0.0547  0.0597  147  VAL   A C   
808  O  O   . VAL   A 147 ? 0.2415 0.2162 0.2696 0.0349  0.0531  0.0563  147  VAL   A O   
809  C  CB  . VAL   A 147 ? 0.2814 0.2640 0.3166 0.0399  0.0549  0.0628  147  VAL   A CB  
810  C  CG1 . VAL   A 147 ? 0.3021 0.2924 0.3399 0.0396  0.0518  0.0644  147  VAL   A CG1 
811  C  CG2 . VAL   A 147 ? 0.2949 0.2777 0.3327 0.0426  0.0574  0.0656  147  VAL   A CG2 
812  N  N   . VAL   A 148 ? 0.2203 0.1985 0.2522 0.0370  0.0544  0.0613  148  VAL   A N   
813  C  CA  . VAL   A 148 ? 0.2216 0.2003 0.2517 0.0346  0.0522  0.0591  148  VAL   A CA  
814  C  C   . VAL   A 148 ? 0.2303 0.2169 0.2630 0.0346  0.0493  0.0607  148  VAL   A C   
815  O  O   . VAL   A 148 ? 0.2451 0.2348 0.2805 0.0363  0.0500  0.0641  148  VAL   A O   
816  C  CB  . VAL   A 148 ? 0.2359 0.2092 0.2646 0.0344  0.0546  0.0594  148  VAL   A CB  
817  C  CG1 . VAL   A 148 ? 0.2478 0.2218 0.2749 0.0319  0.0522  0.0572  148  VAL   A CG1 
818  C  CG2 . VAL   A 148 ? 0.2641 0.2291 0.2900 0.0344  0.0577  0.0579  148  VAL   A CG2 
819  N  N   . ILE   A 149 ? 0.2189 0.2088 0.2507 0.0326  0.0460  0.0583  149  ILE   A N   
820  C  CA  . ILE   A 149 ? 0.2125 0.2094 0.2461 0.0322  0.0432  0.0593  149  ILE   A CA  
821  C  C   . ILE   A 149 ? 0.2155 0.2130 0.2474 0.0299  0.0412  0.0569  149  ILE   A C   
822  O  O   . ILE   A 149 ? 0.2112 0.2065 0.2408 0.0281  0.0400  0.0537  149  ILE   A O   
823  C  CB  . ILE   A 149 ? 0.2141 0.2154 0.2486 0.0322  0.0413  0.0589  149  ILE   A CB  
824  C  CG1 . ILE   A 149 ? 0.2333 0.2344 0.2699 0.0346  0.0435  0.0614  149  ILE   A CG1 
825  C  CG2 . ILE   A 149 ? 0.2172 0.2259 0.2535 0.0317  0.0384  0.0600  149  ILE   A CG2 
826  C  CD1 . ILE   A 149 ? 0.2575 0.2619 0.2947 0.0345  0.0417  0.0606  149  ILE   A CD1 
827  N  N   . HIS   A 150 ? 0.2048 0.2055 0.2379 0.0299  0.0406  0.0587  150  HIS   A N   
828  C  CA  . HIS   A 150 ? 0.1988 0.2008 0.2307 0.0279  0.0387  0.0568  150  HIS   A CA  
829  C  C   . HIS   A 150 ? 0.1927 0.2015 0.2257 0.0275  0.0359  0.0573  150  HIS   A C   
830  O  O   . HIS   A 150 ? 0.1934 0.2065 0.2286 0.0288  0.0358  0.0602  150  HIS   A O   
831  C  CB  . HIS   A 150 ? 0.2133 0.2139 0.2454 0.0282  0.0402  0.0586  150  HIS   A CB  
832  C  CG  . HIS   A 150 ? 0.2454 0.2389 0.2760 0.0284  0.0430  0.0581  150  HIS   A CG  
833  N  ND1 . HIS   A 150 ? 0.2776 0.2673 0.3059 0.0263  0.0429  0.0553  150  HIS   A ND1 
834  C  CD2 . HIS   A 150 ? 0.2792 0.2691 0.3105 0.0302  0.0461  0.0602  150  HIS   A CD2 
835  C  CE1 . HIS   A 150 ? 0.2850 0.2685 0.3121 0.0268  0.0458  0.0555  150  HIS   A CE1 
836  N  NE2 . HIS   A 150 ? 0.2955 0.2787 0.3243 0.0292  0.0478  0.0584  150  HIS   A NE2 
837  N  N   . TYR   A 151 ? 0.1889 0.1988 0.2205 0.0255  0.0336  0.0543  151  TYR   A N   
838  C  CA  . TYR   A 151 ? 0.1853 0.2012 0.2177 0.0249  0.0311  0.0543  151  TYR   A CA  
839  C  C   . TYR   A 151 ? 0.1795 0.1961 0.2103 0.0228  0.0292  0.0517  151  TYR   A C   
840  O  O   . TYR   A 151 ? 0.1831 0.1959 0.2125 0.0217  0.0296  0.0495  151  TYR   A O   
841  C  CB  . TYR   A 151 ? 0.1888 0.2061 0.2215 0.0253  0.0303  0.0539  151  TYR   A CB  
842  C  CG  . TYR   A 151 ? 0.1806 0.1939 0.2113 0.0243  0.0301  0.0506  151  TYR   A CG  
843  C  CD1 . TYR   A 151 ? 0.1798 0.1876 0.2096 0.0249  0.0322  0.0501  151  TYR   A CD1 
844  C  CD2 . TYR   A 151 ? 0.1841 0.1990 0.2137 0.0226  0.0278  0.0480  151  TYR   A CD2 
845  C  CE1 . TYR   A 151 ? 0.1805 0.1847 0.2083 0.0237  0.0318  0.0471  151  TYR   A CE1 
846  C  CE2 . TYR   A 151 ? 0.1884 0.1997 0.2162 0.0216  0.0275  0.0451  151  TYR   A CE2 
847  C  CZ  . TYR   A 151 ? 0.1921 0.1983 0.2190 0.0221  0.0294  0.0447  151  TYR   A CZ  
848  O  OH  . TYR   A 151 ? 0.1865 0.1894 0.2114 0.0210  0.0289  0.0420  151  TYR   A OH  
849  N  N   . ALA   A 152 ? 0.1918 0.2137 0.2231 0.0222  0.0272  0.0517  152  ALA   A N   
850  C  CA  . ALA   A 152 ? 0.1994 0.2225 0.2295 0.0204  0.0254  0.0493  152  ALA   A CA  
851  C  C   . ALA   A 152 ? 0.1965 0.2231 0.2265 0.0198  0.0234  0.0483  152  ALA   A C   
852  O  O   . ALA   A 152 ? 0.1992 0.2287 0.2302 0.0207  0.0232  0.0501  152  ALA   A O   
853  C  CB  . ALA   A 152 ? 0.2090 0.2346 0.2393 0.0199  0.0252  0.0506  152  ALA   A CB  
854  N  N   . GLY   A 153 ? 0.1982 0.2247 0.2269 0.0184  0.0220  0.0456  153  GLY   A N   
855  C  CA  . GLY   A 153 ? 0.2010 0.2306 0.2294 0.0177  0.0202  0.0444  153  GLY   A CA  
856  C  C   . GLY   A 153 ? 0.1971 0.2274 0.2244 0.0161  0.0190  0.0422  153  GLY   A C   
857  O  O   . GLY   A 153 ? 0.1954 0.2242 0.2224 0.0156  0.0195  0.0416  153  GLY   A O   
858  N  N   . GLN   A 154 ? 0.1960 0.2288 0.2228 0.0154  0.0174  0.0409  154  GLN   A N   
859  C  CA  . GLN   A 154 ? 0.1873 0.2206 0.2131 0.0140  0.0164  0.0387  154  GLN   A CA  
860  C  C   . GLN   A 154 ? 0.1823 0.2138 0.2075 0.0137  0.0156  0.0364  154  GLN   A C   
861  O  O   . GLN   A 154 ? 0.1894 0.2215 0.2147 0.0141  0.0153  0.0367  154  GLN   A O   
862  C  CB  . GLN   A 154 ? 0.2400 0.2775 0.2654 0.0133  0.0154  0.0391  154  GLN   A CB  
863  C  CG  . GLN   A 154 ? 0.3070 0.3465 0.3327 0.0134  0.0159  0.0413  154  GLN   A CG  
864  C  CD  . GLN   A 154 ? 0.4160 0.4537 0.4414 0.0128  0.0166  0.0404  154  GLN   A CD  
865  O  OE1 . GLN   A 154 ? 0.4570 0.4944 0.4818 0.0118  0.0161  0.0382  154  GLN   A OE1 
866  N  NE2 . GLN   A 154 ? 0.4241 0.4607 0.4502 0.0135  0.0178  0.0422  154  GLN   A NE2 
867  N  N   . LEU   A 155 ? 0.1697 0.1993 0.1944 0.0129  0.0153  0.0342  155  LEU   A N   
868  C  CA  . LEU   A 155 ? 0.1815 0.2096 0.2056 0.0125  0.0145  0.0321  155  LEU   A CA  
869  C  C   . LEU   A 155 ? 0.1741 0.2050 0.1978 0.0122  0.0134  0.0318  155  LEU   A C   
870  O  O   . LEU   A 155 ? 0.1796 0.2134 0.2030 0.0117  0.0129  0.0321  155  LEU   A O   
871  C  CB  . LEU   A 155 ? 0.1937 0.2203 0.2176 0.0116  0.0142  0.0302  155  LEU   A CB  
872  C  CG  . LEU   A 155 ? 0.2229 0.2462 0.2470 0.0115  0.0151  0.0301  155  LEU   A CG  
873  C  CD1 . LEU   A 155 ? 0.2383 0.2612 0.2625 0.0105  0.0145  0.0283  155  LEU   A CD1 
874  C  CD2 . LEU   A 155 ? 0.2345 0.2545 0.2581 0.0120  0.0156  0.0299  155  LEU   A CD2 
875  N  N   . SER   A 156 ? 0.1621 0.1922 0.1856 0.0125  0.0129  0.0311  156  SER   A N   
876  C  CA  . SER   A 156 ? 0.1655 0.1981 0.1884 0.0121  0.0119  0.0308  156  SER   A CA  
877  C  C   . SER   A 156 ? 0.1627 0.1956 0.1849 0.0111  0.0110  0.0286  156  SER   A C   
878  O  O   . SER   A 156 ? 0.1711 0.2017 0.1932 0.0108  0.0110  0.0271  156  SER   A O   
879  C  CB  . SER   A 156 ? 0.1808 0.2121 0.2036 0.0126  0.0117  0.0305  156  SER   A CB  
880  O  OG  . SER   A 156 ? 0.1929 0.2269 0.2153 0.0121  0.0108  0.0305  156  SER   A OG  
881  N  N   . GLU   A 157 ? 0.1637 0.1994 0.1852 0.0104  0.0104  0.0286  157  GLU   A N   
882  C  CA  . GLU   A 157 ? 0.1658 0.2017 0.1864 0.0095  0.0098  0.0266  157  GLU   A CA  
883  C  C   . GLU   A 157 ? 0.1718 0.2072 0.1918 0.0094  0.0090  0.0255  157  GLU   A C   
884  O  O   . GLU   A 157 ? 0.1840 0.2195 0.2032 0.0087  0.0085  0.0239  157  GLU   A O   
885  C  CB  . GLU   A 157 ? 0.1990 0.2377 0.2187 0.0087  0.0097  0.0269  157  GLU   A CB  
886  C  CG  . GLU   A 157 ? 0.2325 0.2715 0.2528 0.0088  0.0105  0.0279  157  GLU   A CG  
887  C  CD  . GLU   A 157 ? 0.3032 0.3406 0.3239 0.0085  0.0108  0.0263  157  GLU   A CD  
888  O  OE1 . GLU   A 157 ? 0.3350 0.3719 0.3552 0.0081  0.0103  0.0245  157  GLU   A OE1 
889  O  OE2 . GLU   A 157 ? 0.3631 0.3997 0.3847 0.0088  0.0114  0.0269  157  GLU   A OE2 
890  N  N   . THR   A 158 ? 0.1530 0.1877 0.1734 0.0101  0.0090  0.0263  158  THR   A N   
891  C  CA  . THR   A 158 ? 0.1590 0.1928 0.1788 0.0100  0.0084  0.0253  158  THR   A CA  
892  C  C   . THR   A 158 ? 0.1672 0.1976 0.1872 0.0104  0.0085  0.0240  158  THR   A C   
893  O  O   . THR   A 158 ? 0.1700 0.1990 0.1903 0.0104  0.0089  0.0236  158  THR   A O   
894  C  CB  . THR   A 158 ? 0.1662 0.2013 0.1864 0.0105  0.0085  0.0271  158  THR   A CB  
895  O  OG1 . THR   A 158 ? 0.1687 0.2017 0.1898 0.0116  0.0094  0.0280  158  THR   A OG1 
896  C  CG2 . THR   A 158 ? 0.1768 0.2155 0.1971 0.0101  0.0084  0.0288  158  THR   A CG2 
897  N  N   . PHE   A 159 ? 0.1566 0.1856 0.1761 0.0106  0.0082  0.0234  159  PHE   A N   
898  C  CA  . PHE   A 159 ? 0.1556 0.1815 0.1751 0.0109  0.0082  0.0225  159  PHE   A CA  
899  C  C   . PHE   A 159 ? 0.1608 0.1850 0.1805 0.0117  0.0090  0.0236  159  PHE   A C   
900  O  O   . PHE   A 159 ? 0.1674 0.1889 0.1866 0.0118  0.0090  0.0228  159  PHE   A O   
901  C  CB  . PHE   A 159 ? 0.1543 0.1793 0.1730 0.0105  0.0074  0.0209  159  PHE   A CB  
902  C  CG  . PHE   A 159 ? 0.1686 0.1946 0.1869 0.0098  0.0069  0.0196  159  PHE   A CG  
903  C  CD1 . PHE   A 159 ? 0.2245 0.2495 0.2433 0.0096  0.0068  0.0186  159  PHE   A CD1 
904  C  CD2 . PHE   A 159 ? 0.1824 0.2103 0.2000 0.0093  0.0065  0.0194  159  PHE   A CD2 
905  C  CE1 . PHE   A 159 ? 0.2413 0.2670 0.2598 0.0092  0.0065  0.0175  159  PHE   A CE1 
906  C  CE2 . PHE   A 159 ? 0.1952 0.2236 0.2123 0.0087  0.0062  0.0181  159  PHE   A CE2 
907  C  CZ  . PHE   A 159 ? 0.2115 0.2387 0.2291 0.0087  0.0063  0.0172  159  PHE   A CZ  
908  N  N   . HIS   A 160 ? 0.1519 0.1776 0.1723 0.0122  0.0097  0.0255  160  HIS   A N   
909  C  CA  . HIS   A 160 ? 0.1502 0.1742 0.1709 0.0131  0.0107  0.0268  160  HIS   A CA  
910  C  C   . HIS   A 160 ? 0.1505 0.1747 0.1722 0.0137  0.0118  0.0284  160  HIS   A C   
911  O  O   . HIS   A 160 ? 0.1599 0.1860 0.1820 0.0134  0.0117  0.0288  160  HIS   A O   
912  C  CB  . HIS   A 160 ? 0.1547 0.1805 0.1757 0.0135  0.0107  0.0278  160  HIS   A CB  
913  C  CG  . HIS   A 160 ? 0.1750 0.2049 0.1969 0.0134  0.0104  0.0294  160  HIS   A CG  
914  N  ND1 . HIS   A 160 ? 0.1900 0.2225 0.2113 0.0124  0.0093  0.0287  160  HIS   A ND1 
915  C  CD2 . HIS   A 160 ? 0.1772 0.2090 0.2004 0.0142  0.0112  0.0317  160  HIS   A CD2 
916  C  CE1 . HIS   A 160 ? 0.2054 0.2412 0.2274 0.0123  0.0093  0.0305  160  HIS   A CE1 
917  N  NE2 . HIS   A 160 ? 0.1910 0.2267 0.2143 0.0135  0.0104  0.0325  160  HIS   A NE2 
918  N  N   . GLY   A 161 ? 0.1483 0.1703 0.1702 0.0146  0.0131  0.0294  161  GLY   A N   
919  C  CA  . GLY   A 161 ? 0.1498 0.1709 0.1724 0.0152  0.0144  0.0309  161  GLY   A CA  
920  C  C   . GLY   A 161 ? 0.1460 0.1644 0.1678 0.0145  0.0144  0.0294  161  GLY   A C   
921  O  O   . GLY   A 161 ? 0.1537 0.1699 0.1745 0.0139  0.0138  0.0276  161  GLY   A O   
922  N  N   . PHE   A 162 ? 0.1444 0.1631 0.1669 0.0146  0.0151  0.0304  162  PHE   A N   
923  C  CA  . PHE   A 162 ? 0.1511 0.1679 0.1731 0.0138  0.0151  0.0292  162  PHE   A CA  
924  C  C   . PHE   A 162 ? 0.1629 0.1829 0.1853 0.0130  0.0140  0.0287  162  PHE   A C   
925  O  O   . PHE   A 162 ? 0.1647 0.1874 0.1878 0.0132  0.0142  0.0301  162  PHE   A O   
926  C  CB  . PHE   A 162 ? 0.1546 0.1698 0.1770 0.0143  0.0167  0.0308  162  PHE   A CB  
927  C  CG  . PHE   A 162 ? 0.1590 0.1718 0.1810 0.0134  0.0171  0.0299  162  PHE   A CG  
928  C  CD1 . PHE   A 162 ? 0.1678 0.1789 0.1889 0.0123  0.0161  0.0278  162  PHE   A CD1 
929  C  CD2 . PHE   A 162 ? 0.1738 0.1858 0.1962 0.0137  0.0184  0.0313  162  PHE   A CD2 
930  C  CE1 . PHE   A 162 ? 0.1762 0.1851 0.1969 0.0114  0.0164  0.0272  162  PHE   A CE1 
931  C  CE2 . PHE   A 162 ? 0.1799 0.1896 0.2019 0.0128  0.0187  0.0305  162  PHE   A CE2 
932  C  CZ  . PHE   A 162 ? 0.1897 0.1979 0.2108 0.0116  0.0177  0.0284  162  PHE   A CZ  
933  N  N   . TYR   A 163 ? 0.1509 0.1708 0.1728 0.0122  0.0128  0.0268  163  TYR   A N   
934  C  CA  . TYR   A 163 ? 0.1459 0.1688 0.1680 0.0116  0.0118  0.0261  163  TYR   A CA  
935  C  C   . TYR   A 163 ? 0.1520 0.1744 0.1742 0.0108  0.0114  0.0248  163  TYR   A C   
936  O  O   . TYR   A 163 ? 0.1661 0.1859 0.1882 0.0105  0.0115  0.0240  163  TYR   A O   
937  C  CB  . TYR   A 163 ? 0.1488 0.1728 0.1704 0.0116  0.0109  0.0253  163  TYR   A CB  
938  C  CG  . TYR   A 163 ? 0.1406 0.1622 0.1615 0.0112  0.0102  0.0235  163  TYR   A CG  
939  C  CD1 . TYR   A 163 ? 0.1463 0.1654 0.1666 0.0116  0.0105  0.0235  163  TYR   A CD1 
940  C  CD2 . TYR   A 163 ? 0.1425 0.1646 0.1634 0.0106  0.0093  0.0220  163  TYR   A CD2 
941  C  CE1 . TYR   A 163 ? 0.1482 0.1653 0.1677 0.0113  0.0098  0.0220  163  TYR   A CE1 
942  C  CE2 . TYR   A 163 ? 0.1536 0.1739 0.1740 0.0103  0.0086  0.0206  163  TYR   A CE2 
943  C  CZ  . TYR   A 163 ? 0.1512 0.1691 0.1708 0.0106  0.0088  0.0206  163  TYR   A CZ  
944  O  OH  . TYR   A 163 ? 0.1578 0.1739 0.1767 0.0103  0.0080  0.0193  163  TYR   A OH  
945  N  N   . LYS   A 164 ? 0.1519 0.1769 0.1744 0.0104  0.0111  0.0246  164  LYS   A N   
946  C  CA  . LYS   A 164 ? 0.1576 0.1827 0.1806 0.0097  0.0108  0.0235  164  LYS   A CA  
947  C  C   . LYS   A 164 ? 0.1639 0.1888 0.1868 0.0094  0.0099  0.0218  164  LYS   A C   
948  O  O   . LYS   A 164 ? 0.1755 0.2014 0.1977 0.0095  0.0094  0.0214  164  LYS   A O   
949  C  CB  . LYS   A 164 ? 0.1888 0.2168 0.2121 0.0095  0.0111  0.0240  164  LYS   A CB  
950  C  CG  . LYS   A 164 ? 0.2046 0.2330 0.2286 0.0089  0.0111  0.0231  164  LYS   A CG  
951  C  CD  . LYS   A 164 ? 0.2743 0.3053 0.2981 0.0086  0.0115  0.0236  164  LYS   A CD  
952  C  CE  . LYS   A 164 ? 0.3686 0.4011 0.3915 0.0084  0.0110  0.0228  164  LYS   A CE  
953  N  NZ  . LYS   A 164 ? 0.4085 0.4434 0.4308 0.0079  0.0114  0.0232  164  LYS   A NZ  
954  N  N   . SER   A 165 ? 0.1477 0.1712 0.1711 0.0090  0.0096  0.0208  165  SER   A N   
955  C  CA  . SER   A 165 ? 0.1594 0.1829 0.1830 0.0088  0.0087  0.0194  165  SER   A CA  
956  C  C   . SER   A 165 ? 0.1781 0.2025 0.2030 0.0083  0.0087  0.0190  165  SER   A C   
957  O  O   . SER   A 165 ? 0.1807 0.2049 0.2063 0.0080  0.0093  0.0196  165  SER   A O   
958  C  CB  . SER   A 165 ? 0.1711 0.1920 0.1942 0.0087  0.0081  0.0188  165  SER   A CB  
959  O  OG  . SER   A 165 ? 0.1737 0.1946 0.1971 0.0085  0.0072  0.0176  165  SER   A OG  
960  N  N   . THR   A 166 ? 0.1651 0.1907 0.1905 0.0082  0.0084  0.0180  166  THR   A N   
961  C  CA  . THR   A 166 ? 0.1612 0.1879 0.1882 0.0079  0.0086  0.0177  166  THR   A CA  
962  C  C   . THR   A 166 ? 0.1719 0.1984 0.1997 0.0079  0.0078  0.0167  166  THR   A C   
963  O  O   . THR   A 166 ? 0.1770 0.2028 0.2039 0.0082  0.0073  0.0161  166  THR   A O   
964  C  CB  . THR   A 166 ? 0.2007 0.2296 0.2275 0.0079  0.0094  0.0179  166  THR   A CB  
965  O  OG1 . THR   A 166 ? 0.2264 0.2559 0.2525 0.0081  0.0092  0.0171  166  THR   A OG1 
966  C  CG2 . THR   A 166 ? 0.2124 0.2418 0.2383 0.0079  0.0101  0.0191  166  THR   A CG2 
967  N  N   . TYR   A 167 ? 0.1702 0.1975 0.1998 0.0076  0.0079  0.0166  167  TYR   A N   
968  C  CA  . TYR   A 167 ? 0.1759 0.2036 0.2068 0.0078  0.0074  0.0158  167  TYR   A CA  
969  C  C   . TYR   A 167 ? 0.1823 0.2118 0.2153 0.0077  0.0080  0.0160  167  TYR   A C   
970  O  O   . TYR   A 167 ? 0.1936 0.2236 0.2270 0.0072  0.0085  0.0166  167  TYR   A O   
971  C  CB  . TYR   A 167 ? 0.1888 0.2148 0.2196 0.0076  0.0062  0.0156  167  TYR   A CB  
972  C  CG  . TYR   A 167 ? 0.2054 0.2312 0.2375 0.0068  0.0058  0.0161  167  TYR   A CG  
973  C  CD1 . TYR   A 167 ? 0.2310 0.2553 0.2620 0.0062  0.0060  0.0166  167  TYR   A CD1 
974  C  CD2 . TYR   A 167 ? 0.2496 0.2765 0.2838 0.0066  0.0053  0.0160  167  TYR   A CD2 
975  C  CE1 . TYR   A 167 ? 0.2410 0.2650 0.2730 0.0053  0.0057  0.0170  167  TYR   A CE1 
976  C  CE2 . TYR   A 167 ? 0.2689 0.2959 0.3043 0.0056  0.0048  0.0165  167  TYR   A CE2 
977  C  CZ  . TYR   A 167 ? 0.2648 0.2902 0.2989 0.0049  0.0050  0.0169  167  TYR   A CZ  
978  O  OH  . TYR   A 167 ? 0.3342 0.3595 0.3693 0.0037  0.0045  0.0172  167  TYR   A OH  
979  N  N   . ARG   A 168 ? 0.1905 0.2208 0.2250 0.0080  0.0079  0.0155  168  ARG   A N   
980  C  CA  . ARG   A 168 ? 0.2086 0.2407 0.2455 0.0080  0.0086  0.0158  168  ARG   A CA  
981  C  C   . ARG   A 168 ? 0.2249 0.2573 0.2640 0.0077  0.0075  0.0160  168  ARG   A C   
982  O  O   . ARG   A 168 ? 0.2216 0.2533 0.2607 0.0080  0.0066  0.0156  168  ARG   A O   
983  C  CB  . ARG   A 168 ? 0.2614 0.2944 0.2985 0.0087  0.0096  0.0151  168  ARG   A CB  
984  C  CG  . ARG   A 168 ? 0.3649 0.3982 0.3999 0.0086  0.0107  0.0150  168  ARG   A CG  
985  C  CD  . ARG   A 168 ? 0.4455 0.4799 0.4808 0.0089  0.0122  0.0146  168  ARG   A CD  
986  N  NE  . ARG   A 168 ? 0.4956 0.5304 0.5288 0.0085  0.0131  0.0148  168  ARG   A NE  
987  C  CZ  . ARG   A 168 ? 0.5207 0.5566 0.5543 0.0081  0.0139  0.0154  168  ARG   A CZ  
988  N  NH1 . ARG   A 168 ? 0.5258 0.5627 0.5621 0.0081  0.0141  0.0159  168  ARG   A NH1 
989  N  NH2 . ARG   A 168 ? 0.5378 0.5742 0.5693 0.0078  0.0146  0.0156  168  ARG   A NH2 
990  N  N   . THR   A 169 ? 0.2466 0.2802 0.2876 0.0071  0.0076  0.0166  169  THR   A N   
991  C  CA  . THR   A 169 ? 0.2687 0.3031 0.3121 0.0067  0.0065  0.0170  169  THR   A CA  
992  C  C   . THR   A 169 ? 0.2889 0.3250 0.3346 0.0076  0.0069  0.0169  169  THR   A C   
993  O  O   . THR   A 169 ? 0.2603 0.2970 0.3060 0.0084  0.0083  0.0166  169  THR   A O   
994  C  CB  . THR   A 169 ? 0.2959 0.3311 0.3406 0.0055  0.0064  0.0177  169  THR   A CB  
995  O  OG1 . THR   A 169 ? 0.2950 0.3323 0.3415 0.0058  0.0078  0.0180  169  THR   A OG1 
996  C  CG2 . THR   A 169 ? 0.3060 0.3391 0.3483 0.0047  0.0064  0.0178  169  THR   A CG2 
997  N  N   . LYS   A 170 ? 0.3193 0.3560 0.3669 0.0075  0.0056  0.0173  170  LYS   A N   
998  C  CA  . LYS   A 170 ? 0.3551 0.3935 0.4053 0.0085  0.0060  0.0174  170  LYS   A CA  
999  C  C   . LYS   A 170 ? 0.3877 0.4285 0.4406 0.0088  0.0075  0.0179  170  LYS   A C   
1000 O  O   . LYS   A 170 ? 0.4009 0.4426 0.4552 0.0099  0.0088  0.0178  170  LYS   A O   
1001 C  CB  . LYS   A 170 ? 0.3830 0.4219 0.4350 0.0084  0.0043  0.0180  170  LYS   A CB  
1002 C  CG  . LYS   A 170 ? 0.4329 0.4728 0.4862 0.0069  0.0030  0.0189  170  LYS   A CG  
1003 C  CD  . LYS   A 170 ? 0.4784 0.5184 0.5324 0.0066  0.0011  0.0194  170  LYS   A CD  
1004 C  CE  . LYS   A 170 ? 0.5151 0.5566 0.5708 0.0049  -0.0002 0.0203  170  LYS   A CE  
1005 N  NZ  . LYS   A 170 ? 0.5248 0.5650 0.5785 0.0036  0.0001  0.0200  170  LYS   A NZ  
1006 N  N   . GLU   A 171 ? 0.3983 0.4397 0.4514 0.0077  0.0076  0.0184  171  GLU   A N   
1007 C  CA  . GLU   A 171 ? 0.3987 0.4422 0.4539 0.0076  0.0090  0.0189  171  GLU   A CA  
1008 C  C   . GLU   A 171 ? 0.4136 0.4563 0.4666 0.0081  0.0108  0.0182  171  GLU   A C   
1009 O  O   . GLU   A 171 ? 0.4315 0.4759 0.4861 0.0082  0.0122  0.0186  171  GLU   A O   
1010 C  CB  . GLU   A 171 ? 0.4068 0.4509 0.4630 0.0061  0.0081  0.0197  171  GLU   A CB  
1011 C  CG  . GLU   A 171 ? 0.4239 0.4691 0.4822 0.0054  0.0062  0.0204  171  GLU   A CG  
1012 C  CD  . GLU   A 171 ? 0.4643 0.5070 0.5200 0.0044  0.0045  0.0201  171  GLU   A CD  
1013 O  OE1 . GLU   A 171 ? 0.4351 0.4753 0.4874 0.0042  0.0048  0.0194  171  GLU   A OE1 
1014 O  OE2 . GLU   A 171 ? 0.4332 0.4765 0.4900 0.0037  0.0029  0.0205  171  GLU   A OE2 
1015 N  N   . GLY   A 172 ? 0.3965 0.4371 0.4461 0.0083  0.0108  0.0174  172  GLY   A N   
1016 C  CA  . GLY   A 172 ? 0.3814 0.4214 0.4286 0.0086  0.0123  0.0169  172  GLY   A CA  
1017 C  C   . GLY   A 172 ? 0.3688 0.4079 0.4136 0.0079  0.0124  0.0171  172  GLY   A C   
1018 O  O   . GLY   A 172 ? 0.3771 0.4160 0.4199 0.0080  0.0134  0.0167  172  GLY   A O   
1019 N  N   . GLU   A 173 ? 0.3442 0.3829 0.3892 0.0070  0.0114  0.0176  173  GLU   A N   
1020 C  CA  . GLU   A 173 ? 0.3341 0.3719 0.3772 0.0064  0.0116  0.0180  173  GLU   A CA  
1021 C  C   . GLU   A 173 ? 0.3152 0.3509 0.3552 0.0066  0.0111  0.0177  173  GLU   A C   
1022 O  O   . GLU   A 173 ? 0.3001 0.3345 0.3396 0.0066  0.0099  0.0174  173  GLU   A O   
1023 C  CB  . GLU   A 173 ? 0.3683 0.4058 0.4126 0.0053  0.0108  0.0187  173  GLU   A CB  
1024 C  CG  . GLU   A 173 ? 0.4533 0.4896 0.4957 0.0047  0.0112  0.0193  173  GLU   A CG  
1025 C  CD  . GLU   A 173 ? 0.5525 0.5872 0.5948 0.0036  0.0103  0.0196  173  GLU   A CD  
1026 O  OE1 . GLU   A 173 ? 0.5820 0.6172 0.6260 0.0030  0.0093  0.0196  173  GLU   A OE1 
1027 O  OE2 . GLU   A 173 ? 0.5801 0.6130 0.6204 0.0033  0.0105  0.0200  173  GLU   A OE2 
1028 N  N   . LEU   A 174 ? 0.3025 0.3380 0.3405 0.0067  0.0119  0.0178  174  LEU   A N   
1029 C  CA  . LEU   A 174 ? 0.3010 0.3350 0.3363 0.0068  0.0114  0.0178  174  LEU   A CA  
1030 C  C   . LEU   A 174 ? 0.2862 0.3188 0.3212 0.0063  0.0109  0.0185  174  LEU   A C   
1031 O  O   . LEU   A 174 ? 0.3189 0.3517 0.3545 0.0057  0.0115  0.0192  174  LEU   A O   
1032 C  CB  . LEU   A 174 ? 0.3266 0.3612 0.3601 0.0070  0.0124  0.0179  174  LEU   A CB  
1033 C  CG  . LEU   A 174 ? 0.3727 0.4063 0.4038 0.0072  0.0120  0.0181  174  LEU   A CG  
1034 C  CD1 . LEU   A 174 ? 0.3765 0.4093 0.4070 0.0075  0.0112  0.0172  174  LEU   A CD1 
1035 C  CD2 . LEU   A 174 ? 0.4031 0.4379 0.4326 0.0071  0.0129  0.0185  174  LEU   A CD2 
1036 N  N   . ARG   A 175 ? 0.2199 0.2506 0.2538 0.0063  0.0100  0.0183  175  ARG   A N   
1037 C  CA  . ARG   A 175 ? 0.1965 0.2252 0.2297 0.0058  0.0097  0.0188  175  ARG   A CA  
1038 C  C   . ARG   A 175 ? 0.1856 0.2131 0.2166 0.0063  0.0098  0.0190  175  ARG   A C   
1039 O  O   . ARG   A 175 ? 0.2038 0.2313 0.2339 0.0068  0.0093  0.0185  175  ARG   A O   
1040 C  CB  . ARG   A 175 ? 0.1994 0.2269 0.2332 0.0052  0.0085  0.0184  175  ARG   A CB  
1041 C  CG  . ARG   A 175 ? 0.2662 0.2952 0.3026 0.0046  0.0082  0.0184  175  ARG   A CG  
1042 C  CD  . ARG   A 175 ? 0.3342 0.3620 0.3707 0.0034  0.0081  0.0189  175  ARG   A CD  
1043 N  NE  . ARG   A 175 ? 0.3778 0.4075 0.4170 0.0026  0.0077  0.0190  175  ARG   A NE  
1044 C  CZ  . ARG   A 175 ? 0.4597 0.4891 0.4997 0.0017  0.0065  0.0189  175  ARG   A CZ  
1045 N  NH1 . ARG   A 175 ? 0.4789 0.5062 0.5172 0.0015  0.0055  0.0185  175  ARG   A NH1 
1046 N  NH2 . ARG   A 175 ? 0.4456 0.4771 0.4883 0.0010  0.0062  0.0193  175  ARG   A NH2 
1047 N  N   . ILE   A 176 ? 0.1796 0.2060 0.2098 0.0061  0.0104  0.0200  176  ILE   A N   
1048 C  CA  . ILE   A 176 ? 0.1915 0.2170 0.2200 0.0067  0.0106  0.0205  176  ILE   A CA  
1049 C  C   . ILE   A 176 ? 0.2005 0.2232 0.2282 0.0065  0.0105  0.0207  176  ILE   A C   
1050 O  O   . ILE   A 176 ? 0.2099 0.2314 0.2380 0.0058  0.0108  0.0210  176  ILE   A O   
1051 C  CB  . ILE   A 176 ? 0.2288 0.2556 0.2571 0.0069  0.0117  0.0217  176  ILE   A CB  
1052 C  CG1 . ILE   A 176 ? 0.2874 0.3168 0.3160 0.0069  0.0120  0.0214  176  ILE   A CG1 
1053 C  CG2 . ILE   A 176 ? 0.2552 0.2812 0.2820 0.0075  0.0120  0.0227  176  ILE   A CG2 
1054 C  CD1 . ILE   A 176 ? 0.3305 0.3613 0.3587 0.0070  0.0130  0.0226  176  ILE   A CD1 
1055 N  N   . LEU   A 177 ? 0.1765 0.1980 0.2029 0.0070  0.0101  0.0205  177  LEU   A N   
1056 C  CA  . LEU   A 177 ? 0.1717 0.1901 0.1970 0.0068  0.0103  0.0207  177  LEU   A CA  
1057 C  C   . LEU   A 177 ? 0.1603 0.1784 0.1844 0.0078  0.0109  0.0216  177  LEU   A C   
1058 O  O   . LEU   A 177 ? 0.1696 0.1899 0.1938 0.0083  0.0109  0.0219  177  LEU   A O   
1059 C  CB  . LEU   A 177 ? 0.1835 0.2004 0.2083 0.0064  0.0092  0.0196  177  LEU   A CB  
1060 C  CG  . LEU   A 177 ? 0.2080 0.2256 0.2324 0.0070  0.0084  0.0189  177  LEU   A CG  
1061 C  CD1 . LEU   A 177 ? 0.2223 0.2372 0.2453 0.0070  0.0080  0.0185  177  LEU   A CD1 
1062 C  CD2 . LEU   A 177 ? 0.2239 0.2435 0.2497 0.0068  0.0076  0.0181  177  LEU   A CD2 
1063 N  N   . ALA   A 178 ? 0.1546 0.1699 0.1778 0.0079  0.0115  0.0220  178  ALA   A N   
1064 C  CA  . ALA   A 178 ? 0.1608 0.1759 0.1832 0.0089  0.0121  0.0231  178  ALA   A CA  
1065 C  C   . ALA   A 178 ? 0.1579 0.1701 0.1791 0.0089  0.0120  0.0225  178  ALA   A C   
1066 O  O   . ALA   A 178 ? 0.1644 0.1738 0.1848 0.0082  0.0121  0.0219  178  ALA   A O   
1067 C  CB  . ALA   A 178 ? 0.1817 0.1961 0.2043 0.0093  0.0136  0.0246  178  ALA   A CB  
1068 N  N   . SER   A 179 ? 0.1446 0.1574 0.1653 0.0097  0.0118  0.0226  179  SER   A N   
1069 C  CA  . SER   A 179 ? 0.1471 0.1572 0.1665 0.0098  0.0117  0.0220  179  SER   A CA  
1070 C  C   . SER   A 179 ? 0.1470 0.1575 0.1662 0.0109  0.0124  0.0231  179  SER   A C   
1071 O  O   . SER   A 179 ? 0.1631 0.1762 0.1832 0.0115  0.0127  0.0244  179  SER   A O   
1072 C  CB  . SER   A 179 ? 0.1597 0.1704 0.1790 0.0092  0.0102  0.0205  179  SER   A CB  
1073 O  OG  . SER   A 179 ? 0.1793 0.1870 0.1971 0.0090  0.0100  0.0198  179  SER   A OG  
1074 N  N   . THR   A 180 ? 0.1441 0.1521 0.1622 0.0111  0.0127  0.0229  180  THR   A N   
1075 C  CA  . THR   A 180 ? 0.1416 0.1498 0.1597 0.0122  0.0136  0.0241  180  THR   A CA  
1076 C  C   . THR   A 180 ? 0.1450 0.1536 0.1626 0.0123  0.0127  0.0233  180  THR   A C   
1077 O  O   . THR   A 180 ? 0.1504 0.1574 0.1669 0.0116  0.0118  0.0218  180  THR   A O   
1078 C  CB  . THR   A 180 ? 0.1509 0.1554 0.1681 0.0127  0.0153  0.0249  180  THR   A CB  
1079 O  OG1 . THR   A 180 ? 0.1601 0.1611 0.1756 0.0118  0.0151  0.0234  180  THR   A OG1 
1080 C  CG2 . THR   A 180 ? 0.1508 0.1550 0.1687 0.0127  0.0164  0.0260  180  THR   A CG2 
1081 N  N   . GLN   A 181 ? 0.1461 0.1569 0.1644 0.0131  0.0130  0.0245  181  GLN   A N   
1082 C  CA  . GLN   A 181 ? 0.1463 0.1572 0.1640 0.0133  0.0125  0.0240  181  GLN   A CA  
1083 C  C   . GLN   A 181 ? 0.1534 0.1655 0.1720 0.0145  0.0136  0.0260  181  GLN   A C   
1084 O  O   . GLN   A 181 ? 0.1583 0.1739 0.1781 0.0147  0.0134  0.0272  181  GLN   A O   
1085 C  CB  . GLN   A 181 ? 0.1497 0.1631 0.1675 0.0127  0.0109  0.0230  181  GLN   A CB  
1086 C  CG  . GLN   A 181 ? 0.1521 0.1660 0.1695 0.0130  0.0106  0.0230  181  GLN   A CG  
1087 C  CD  . GLN   A 181 ? 0.1760 0.1864 0.1921 0.0130  0.0108  0.0220  181  GLN   A CD  
1088 O  OE1 . GLN   A 181 ? 0.1784 0.1863 0.1935 0.0123  0.0105  0.0208  181  GLN   A OE1 
1089 N  NE2 . GLN   A 181 ? 0.1849 0.1949 0.2008 0.0136  0.0114  0.0227  181  GLN   A NE2 
1090 N  N   . PHE   A 182 ? 0.1390 0.1482 0.1569 0.0151  0.0149  0.0264  182  PHE   A N   
1091 C  CA  . PHE   A 182 ? 0.1381 0.1484 0.1573 0.0164  0.0163  0.0286  182  PHE   A CA  
1092 C  C   . PHE   A 182 ? 0.1468 0.1577 0.1660 0.0168  0.0162  0.0288  182  PHE   A C   
1093 O  O   . PHE   A 182 ? 0.1569 0.1705 0.1776 0.0176  0.0167  0.0306  182  PHE   A O   
1094 C  CB  . PHE   A 182 ? 0.1419 0.1483 0.1606 0.0171  0.0183  0.0293  182  PHE   A CB  
1095 C  CG  . PHE   A 182 ? 0.1496 0.1553 0.1684 0.0167  0.0187  0.0295  182  PHE   A CG  
1096 C  CD1 . PHE   A 182 ? 0.1503 0.1597 0.1704 0.0165  0.0177  0.0300  182  PHE   A CD1 
1097 C  CD2 . PHE   A 182 ? 0.1700 0.1714 0.1876 0.0167  0.0202  0.0293  182  PHE   A CD2 
1098 C  CE1 . PHE   A 182 ? 0.1541 0.1629 0.1744 0.0162  0.0182  0.0303  182  PHE   A CE1 
1099 C  CE2 . PHE   A 182 ? 0.1838 0.1845 0.2016 0.0164  0.0206  0.0296  182  PHE   A CE2 
1100 C  CZ  . PHE   A 182 ? 0.1704 0.1748 0.1896 0.0161  0.0196  0.0301  182  PHE   A CZ  
1101 N  N   . GLU   A 183 ? 0.1408 0.1496 0.1585 0.0162  0.0156  0.0270  183  GLU   A N   
1102 C  CA  . GLU   A 183 ? 0.1411 0.1506 0.1588 0.0166  0.0157  0.0274  183  GLU   A CA  
1103 C  C   . GLU   A 183 ? 0.1474 0.1615 0.1663 0.0163  0.0143  0.0278  183  GLU   A C   
1104 O  O   . GLU   A 183 ? 0.1651 0.1804 0.1836 0.0153  0.0128  0.0265  183  GLU   A O   
1105 C  CB  . GLU   A 183 ? 0.1486 0.1546 0.1642 0.0160  0.0153  0.0255  183  GLU   A CB  
1106 C  CG  . GLU   A 183 ? 0.1501 0.1560 0.1658 0.0167  0.0161  0.0261  183  GLU   A CG  
1107 C  CD  . GLU   A 183 ? 0.1617 0.1643 0.1751 0.0160  0.0158  0.0244  183  GLU   A CD  
1108 O  OE1 . GLU   A 183 ? 0.1793 0.1808 0.1915 0.0150  0.0145  0.0227  183  GLU   A OE1 
1109 O  OE2 . GLU   A 183 ? 0.1572 0.1585 0.1702 0.0166  0.0168  0.0248  183  GLU   A OE2 
1110 N  N   . PRO   A 184 ? 0.1530 0.1696 0.1734 0.0170  0.0148  0.0295  184  PRO   A N   
1111 C  CA  . PRO   A 184 ? 0.1430 0.1587 0.1643 0.0183  0.0167  0.0313  184  PRO   A CA  
1112 C  C   . PRO   A 184 ? 0.1530 0.1697 0.1760 0.0194  0.0180  0.0335  184  PRO   A C   
1113 O  O   . PRO   A 184 ? 0.1600 0.1735 0.1829 0.0204  0.0199  0.0342  184  PRO   A O   
1114 C  CB  . PRO   A 184 ? 0.1598 0.1785 0.1821 0.0184  0.0162  0.0321  184  PRO   A CB  
1115 C  CG  . PRO   A 184 ? 0.1654 0.1880 0.1880 0.0173  0.0144  0.0318  184  PRO   A CG  
1116 C  CD  . PRO   A 184 ? 0.1530 0.1737 0.1740 0.0164  0.0134  0.0296  184  PRO   A CD  
1117 N  N   . THR   A 185 ? 0.1525 0.1734 0.1770 0.0193  0.0172  0.0348  185  THR   A N   
1118 C  CA  . THR   A 185 ? 0.1449 0.1674 0.1714 0.0205  0.0185  0.0375  185  THR   A CA  
1119 C  C   . THR   A 185 ? 0.1538 0.1772 0.1804 0.0201  0.0181  0.0376  185  THR   A C   
1120 O  O   . THR   A 185 ? 0.1529 0.1792 0.1812 0.0208  0.0185  0.0399  185  THR   A O   
1121 C  CB  . THR   A 185 ? 0.1649 0.1927 0.1936 0.0209  0.0181  0.0397  185  THR   A CB  
1122 O  OG1 . THR   A 185 ? 0.1701 0.2016 0.1985 0.0195  0.0160  0.0392  185  THR   A OG1 
1123 C  CG2 . THR   A 185 ? 0.1705 0.1979 0.1995 0.0213  0.0185  0.0399  185  THR   A CG2 
1124 N  N   . ALA   A 186 ? 0.1445 0.1654 0.1693 0.0191  0.0174  0.0354  186  ALA   A N   
1125 C  CA  . ALA   A 186 ? 0.1448 0.1667 0.1698 0.0186  0.0171  0.0355  186  ALA   A CA  
1126 C  C   . ALA   A 186 ? 0.1540 0.1721 0.1786 0.0192  0.0187  0.0357  186  ALA   A C   
1127 O  O   . ALA   A 186 ? 0.1547 0.1735 0.1795 0.0189  0.0185  0.0360  186  ALA   A O   
1128 C  CB  . ALA   A 186 ? 0.1492 0.1719 0.1729 0.0171  0.0152  0.0333  186  ALA   A CB  
1129 N  N   . ALA   A 187 ? 0.1491 0.1631 0.1730 0.0199  0.0203  0.0357  187  ALA   A N   
1130 C  CA  . ALA   A 187 ? 0.1512 0.1614 0.1745 0.0203  0.0220  0.0360  187  ALA   A CA  
1131 C  C   . ALA   A 187 ? 0.1611 0.1737 0.1865 0.0214  0.0230  0.0387  187  ALA   A C   
1132 O  O   . ALA   A 187 ? 0.1605 0.1719 0.1856 0.0211  0.0234  0.0387  187  ALA   A O   
1133 C  CB  . ALA   A 187 ? 0.1600 0.1655 0.1822 0.0210  0.0240  0.0358  187  ALA   A CB  
1134 N  N   . ARG   A 188 ? 0.1562 0.1725 0.1835 0.0223  0.0231  0.0408  188  ARG   A N   
1135 C  CA  . ARG   A 188 ? 0.1519 0.1713 0.1814 0.0234  0.0238  0.0438  188  ARG   A CA  
1136 C  C   . ARG   A 188 ? 0.1671 0.1896 0.1967 0.0224  0.0223  0.0438  188  ARG   A C   
1137 O  O   . ARG   A 188 ? 0.1712 0.1959 0.2023 0.0232  0.0229  0.0462  188  ARG   A O   
1138 C  CB  . ARG   A 188 ? 0.1630 0.1863 0.1946 0.0244  0.0238  0.0460  188  ARG   A CB  
1139 C  CG  . ARG   A 188 ? 0.1557 0.1832 0.1872 0.0231  0.0213  0.0451  188  ARG   A CG  
1140 C  CD  . ARG   A 188 ? 0.1611 0.1921 0.1944 0.0238  0.0212  0.0469  188  ARG   A CD  
1141 N  NE  . ARG   A 188 ? 0.1577 0.1856 0.1906 0.0244  0.0224  0.0462  188  ARG   A NE  
1142 C  CZ  . ARG   A 188 ? 0.1646 0.1949 0.1987 0.0248  0.0222  0.0472  188  ARG   A CZ  
1143 N  NH1 . ARG   A 188 ? 0.1697 0.2058 0.2055 0.0244  0.0208  0.0488  188  ARG   A NH1 
1144 N  NH2 . ARG   A 188 ? 0.1605 0.1876 0.1941 0.0254  0.0235  0.0466  188  ARG   A NH2 
1145 N  N   . MET   A 189 ? 0.1614 0.1844 0.1896 0.0208  0.0205  0.0414  189  MET   A N   
1146 C  CA  . MET   A 189 ? 0.1690 0.1944 0.1970 0.0198  0.0192  0.0410  189  MET   A CA  
1147 C  C   . MET   A 189 ? 0.1591 0.1809 0.1861 0.0194  0.0200  0.0398  189  MET   A C   
1148 O  O   . MET   A 189 ? 0.1675 0.1909 0.1944 0.0186  0.0193  0.0397  189  MET   A O   
1149 C  CB  . MET   A 189 ? 0.2075 0.2347 0.2344 0.0183  0.0171  0.0388  189  MET   A CB  
1150 C  CG  . MET   A 189 ? 0.2414 0.2731 0.2693 0.0183  0.0162  0.0400  189  MET   A CG  
1151 S  SD  . MET   A 189 ? 0.2184 0.2513 0.2446 0.0166  0.0141  0.0373  189  MET   A SD  
1152 C  CE  . MET   A 189 ? 0.2229 0.2573 0.2486 0.0156  0.0135  0.0369  189  MET   A CE  
1153 N  N   . ALA   A 190 ? 0.1555 0.1725 0.1815 0.0196  0.0213  0.0390  190  ALA   A N   
1154 C  CA  . ALA   A 190 ? 0.1661 0.1796 0.1910 0.0190  0.0219  0.0379  190  ALA   A CA  
1155 C  C   . ALA   A 190 ? 0.1679 0.1783 0.1932 0.0202  0.0243  0.0396  190  ALA   A C   
1156 O  O   . ALA   A 190 ? 0.1717 0.1805 0.1966 0.0198  0.0250  0.0397  190  ALA   A O   
1157 C  CB  . ALA   A 190 ? 0.1759 0.1860 0.1989 0.0179  0.0213  0.0351  190  ALA   A CB  
1158 N  N   . PHE   A 191 ? 0.1692 0.1785 0.1951 0.0215  0.0257  0.0409  191  PHE   A N   
1159 C  CA  . PHE   A 191 ? 0.1746 0.1808 0.2009 0.0229  0.0283  0.0428  191  PHE   A CA  
1160 C  C   . PHE   A 191 ? 0.1741 0.1821 0.2022 0.0246  0.0293  0.0451  191  PHE   A C   
1161 O  O   . PHE   A 191 ? 0.1783 0.1874 0.2063 0.0246  0.0285  0.0444  191  PHE   A O   
1162 C  CB  . PHE   A 191 ? 0.1791 0.1789 0.2030 0.0224  0.0298  0.0410  191  PHE   A CB  
1163 C  CG  . PHE   A 191 ? 0.1842 0.1819 0.2067 0.0220  0.0295  0.0392  191  PHE   A CG  
1164 C  CD1 . PHE   A 191 ? 0.1902 0.1883 0.2113 0.0204  0.0273  0.0367  191  PHE   A CD1 
1165 C  CD2 . PHE   A 191 ? 0.1960 0.1907 0.2182 0.0233  0.0316  0.0400  191  PHE   A CD2 
1166 C  CE1 . PHE   A 191 ? 0.1975 0.1937 0.2172 0.0200  0.0270  0.0351  191  PHE   A CE1 
1167 C  CE2 . PHE   A 191 ? 0.2049 0.1974 0.2255 0.0228  0.0314  0.0383  191  PHE   A CE2 
1168 C  CZ  . PHE   A 191 ? 0.2056 0.1990 0.2250 0.0212  0.0290  0.0359  191  PHE   A CZ  
1169 N  N   . PRO   A 192 ? 0.1580 0.1666 0.1879 0.0262  0.0311  0.0480  192  PRO   A N   
1170 C  CA  . PRO   A 192 ? 0.1740 0.1844 0.2060 0.0280  0.0322  0.0505  192  PRO   A CA  
1171 C  C   . PRO   A 192 ? 0.1855 0.1908 0.2163 0.0286  0.0341  0.0495  192  PRO   A C   
1172 O  O   . PRO   A 192 ? 0.1878 0.1875 0.2166 0.0283  0.0357  0.0482  192  PRO   A O   
1173 C  CB  . PRO   A 192 ? 0.1860 0.1973 0.2200 0.0295  0.0339  0.0537  192  PRO   A CB  
1174 C  CG  . PRO   A 192 ? 0.2093 0.2164 0.2415 0.0287  0.0347  0.0524  192  PRO   A CG  
1175 C  CD  . PRO   A 192 ? 0.1761 0.1835 0.2062 0.0265  0.0322  0.0492  192  PRO   A CD  
1176 N  N   . CYS   A 193 ? 0.1788 0.1859 0.2105 0.0293  0.0340  0.0500  193  CYS   A N   
1177 C  CA  . CYS   A 193 ? 0.1800 0.1822 0.2102 0.0297  0.0357  0.0488  193  CYS   A CA  
1178 C  C   . CYS   A 193 ? 0.1789 0.1837 0.2110 0.0309  0.0361  0.0503  193  CYS   A C   
1179 O  O   . CYS   A 193 ? 0.1768 0.1875 0.2112 0.0311  0.0345  0.0519  193  CYS   A O   
1180 C  CB  . CYS   A 193 ? 0.1890 0.1882 0.2160 0.0276  0.0342  0.0451  193  CYS   A CB  
1181 S  SG  . CYS   A 193 ? 0.1841 0.1885 0.2110 0.0259  0.0305  0.0433  193  CYS   A SG  
1182 N  N   . PHE   A 194 ? 0.1753 0.1757 0.2063 0.0316  0.0380  0.0497  194  PHE   A N   
1183 C  CA  . PHE   A 194 ? 0.1747 0.1772 0.2073 0.0326  0.0385  0.0508  194  PHE   A CA  
1184 C  C   . PHE   A 194 ? 0.1721 0.1750 0.2026 0.0307  0.0360  0.0479  194  PHE   A C   
1185 O  O   . PHE   A 194 ? 0.1696 0.1679 0.1974 0.0300  0.0365  0.0455  194  PHE   A O   
1186 C  CB  . PHE   A 194 ? 0.1807 0.1777 0.2127 0.0342  0.0420  0.0514  194  PHE   A CB  
1187 C  CG  . PHE   A 194 ? 0.1931 0.1892 0.2271 0.0362  0.0447  0.0544  194  PHE   A CG  
1188 C  CD1 . PHE   A 194 ? 0.2126 0.2044 0.2449 0.0358  0.0458  0.0537  194  PHE   A CD1 
1189 C  CD2 . PHE   A 194 ? 0.2123 0.2116 0.2501 0.0384  0.0463  0.0579  194  PHE   A CD2 
1190 C  CE1 . PHE   A 194 ? 0.2251 0.2156 0.2591 0.0377  0.0486  0.0565  194  PHE   A CE1 
1191 C  CE2 . PHE   A 194 ? 0.2341 0.2323 0.2738 0.0404  0.0489  0.0608  194  PHE   A CE2 
1192 C  CZ  . PHE   A 194 ? 0.2325 0.2262 0.2703 0.0400  0.0501  0.0601  194  PHE   A CZ  
1193 N  N   . ASP   A 195 ? 0.1590 0.1674 0.1906 0.0298  0.0332  0.0479  195  ASP   A N   
1194 C  CA  . ASP   A 195 ? 0.1524 0.1613 0.1819 0.0278  0.0307  0.0449  195  ASP   A CA  
1195 C  C   . ASP   A 195 ? 0.1600 0.1706 0.1899 0.0278  0.0301  0.0447  195  ASP   A C   
1196 O  O   . ASP   A 195 ? 0.1670 0.1823 0.1978 0.0270  0.0278  0.0447  195  ASP   A O   
1197 C  CB  . ASP   A 195 ? 0.1530 0.1662 0.1830 0.0266  0.0282  0.0447  195  ASP   A CB  
1198 C  CG  . ASP   A 195 ? 0.1545 0.1674 0.1823 0.0246  0.0258  0.0416  195  ASP   A CG  
1199 O  OD1 . ASP   A 195 ? 0.1570 0.1658 0.1824 0.0240  0.0260  0.0394  195  ASP   A OD1 
1200 O  OD2 . ASP   A 195 ? 0.1618 0.1785 0.1900 0.0236  0.0238  0.0415  195  ASP   A OD2 
1201 N  N   . GLU   A 196 ? 0.1545 0.1610 0.1835 0.0286  0.0322  0.0444  196  GLU   A N   
1202 C  CA  . GLU   A 196 ? 0.1708 0.1778 0.1996 0.0285  0.0319  0.0439  196  GLU   A CA  
1203 C  C   . GLU   A 196 ? 0.1834 0.1839 0.2088 0.0279  0.0331  0.0414  196  GLU   A C   
1204 O  O   . GLU   A 196 ? 0.1816 0.1774 0.2057 0.0284  0.0352  0.0413  196  GLU   A O   
1205 C  CB  . GLU   A 196 ? 0.1755 0.1849 0.2075 0.0304  0.0337  0.0469  196  GLU   A CB  
1206 C  CG  . GLU   A 196 ? 0.1985 0.2145 0.2340 0.0310  0.0327  0.0498  196  GLU   A CG  
1207 C  CD  . GLU   A 196 ? 0.2265 0.2457 0.2656 0.0329  0.0343  0.0531  196  GLU   A CD  
1208 O  OE1 . GLU   A 196 ? 0.2302 0.2463 0.2691 0.0340  0.0365  0.0533  196  GLU   A OE1 
1209 O  OE2 . GLU   A 196 ? 0.2331 0.2580 0.2750 0.0332  0.0333  0.0556  196  GLU   A OE2 
1210 N  N   . PRO   A 197 ? 0.1742 0.1741 0.1978 0.0268  0.0317  0.0394  197  PRO   A N   
1211 C  CA  . PRO   A 197 ? 0.1724 0.1663 0.1923 0.0258  0.0323  0.0368  197  PRO   A CA  
1212 C  C   . PRO   A 197 ? 0.1835 0.1722 0.2022 0.0269  0.0355  0.0371  197  PRO   A C   
1213 O  O   . PRO   A 197 ? 0.1818 0.1651 0.1970 0.0259  0.0360  0.0350  197  PRO   A O   
1214 C  CB  . PRO   A 197 ? 0.1843 0.1796 0.2030 0.0245  0.0300  0.0349  197  PRO   A CB  
1215 C  CG  . PRO   A 197 ? 0.1823 0.1835 0.2043 0.0252  0.0292  0.0369  197  PRO   A CG  
1216 C  CD  . PRO   A 197 ? 0.1717 0.1764 0.1963 0.0260  0.0293  0.0391  197  PRO   A CD  
1217 N  N   . ALA   A 198 ? 0.1715 0.1616 0.1928 0.0288  0.0375  0.0396  198  ALA   A N   
1218 C  CA  . ALA   A 198 ? 0.1910 0.1758 0.2110 0.0300  0.0409  0.0400  198  ALA   A CA  
1219 C  C   . ALA   A 198 ? 0.2088 0.1906 0.2291 0.0311  0.0434  0.0413  198  ALA   A C   
1220 O  O   . ALA   A 198 ? 0.2289 0.2054 0.2477 0.0320  0.0465  0.0414  198  ALA   A O   
1221 C  CB  . ALA   A 198 ? 0.2060 0.1936 0.2288 0.0316  0.0422  0.0422  198  ALA   A CB  
1222 N  N   . PHE   A 199 ? 0.1930 0.1775 0.2148 0.0310  0.0422  0.0421  199  PHE   A N   
1223 C  CA  . PHE   A 199 ? 0.2024 0.1836 0.2241 0.0319  0.0446  0.0431  199  PHE   A CA  
1224 C  C   . PHE   A 199 ? 0.2015 0.1776 0.2190 0.0298  0.0439  0.0401  199  PHE   A C   
1225 O  O   . PHE   A 199 ? 0.2042 0.1818 0.2219 0.0289  0.0423  0.0398  199  PHE   A O   
1226 C  CB  . PHE   A 199 ? 0.2023 0.1888 0.2275 0.0327  0.0437  0.0457  199  PHE   A CB  
1227 C  CG  . PHE   A 199 ? 0.2325 0.2238 0.2620 0.0349  0.0447  0.0492  199  PHE   A CG  
1228 C  CD1 . PHE   A 199 ? 0.2801 0.2688 0.3109 0.0370  0.0483  0.0513  199  PHE   A CD1 
1229 C  CD2 . PHE   A 199 ? 0.2656 0.2640 0.2979 0.0346  0.0421  0.0504  199  PHE   A CD2 
1230 C  CE1 . PHE   A 199 ? 0.2949 0.2885 0.3301 0.0391  0.0492  0.0549  199  PHE   A CE1 
1231 C  CE2 . PHE   A 199 ? 0.2811 0.2843 0.3174 0.0364  0.0429  0.0537  199  PHE   A CE2 
1232 C  CZ  . PHE   A 199 ? 0.2789 0.2800 0.3170 0.0387  0.0464  0.0561  199  PHE   A CZ  
1233 N  N   . LYS   A 200 ? 0.2052 0.1758 0.2191 0.0289  0.0449  0.0380  200  LYS   A N   
1234 C  CA  . LYS   A 200 ? 0.1972 0.1633 0.2071 0.0267  0.0440  0.0352  200  LYS   A CA  
1235 C  C   . LYS   A 200 ? 0.2098 0.1715 0.2187 0.0269  0.0464  0.0356  200  LYS   A C   
1236 O  O   . LYS   A 200 ? 0.2161 0.1757 0.2260 0.0289  0.0496  0.0376  200  LYS   A O   
1237 C  CB  . LYS   A 200 ? 0.2055 0.1671 0.2115 0.0254  0.0442  0.0328  200  LYS   A CB  
1238 C  CG  . LYS   A 200 ? 0.2009 0.1667 0.2076 0.0248  0.0416  0.0320  200  LYS   A CG  
1239 C  CD  . LYS   A 200 ? 0.2050 0.1661 0.2073 0.0231  0.0413  0.0294  200  LYS   A CD  
1240 C  CE  . LYS   A 200 ? 0.2032 0.1684 0.2061 0.0224  0.0384  0.0285  200  LYS   A CE  
1241 N  NZ  . LYS   A 200 ? 0.1971 0.1584 0.1959 0.0205  0.0376  0.0260  200  LYS   A NZ  
1242 N  N   . ALA   A 201 ? 0.2051 0.1654 0.2120 0.0250  0.0449  0.0339  201  ALA   A N   
1243 C  CA  . ALA   A 201 ? 0.2060 0.1622 0.2117 0.0249  0.0469  0.0341  201  ALA   A CA  
1244 C  C   . ALA   A 201 ? 0.2041 0.1578 0.2065 0.0222  0.0450  0.0314  201  ALA   A C   
1245 O  O   . ALA   A 201 ? 0.2059 0.1621 0.2077 0.0207  0.0420  0.0298  201  ALA   A O   
1246 C  CB  . ALA   A 201 ? 0.2234 0.1844 0.2331 0.0263  0.0466  0.0367  201  ALA   A CB  
1247 N  N   . SER   A 202 ? 0.2087 0.1572 0.2088 0.0214  0.0468  0.0309  202  SER   A N   
1248 C  CA  . SER   A 202 ? 0.2133 0.1602 0.2108 0.0188  0.0449  0.0286  202  SER   A CA  
1249 C  C   . SER   A 202 ? 0.2074 0.1586 0.2078 0.0189  0.0435  0.0298  202  SER   A C   
1250 O  O   . SER   A 202 ? 0.2156 0.1689 0.2189 0.0209  0.0449  0.0322  202  SER   A O   
1251 C  CB  . SER   A 202 ? 0.2328 0.1718 0.2260 0.0175  0.0474  0.0273  202  SER   A CB  
1252 O  OG  . SER   A 202 ? 0.2555 0.1920 0.2498 0.0191  0.0506  0.0292  202  SER   A OG  
1253 N  N   . PHE   A 203 ? 0.2035 0.1562 0.2031 0.0167  0.0407  0.0281  203  PHE   A N   
1254 C  CA  . PHE   A 203 ? 0.2087 0.1656 0.2108 0.0166  0.0392  0.0289  203  PHE   A CA  
1255 C  C   . PHE   A 203 ? 0.2140 0.1680 0.2138 0.0143  0.0387  0.0273  203  PHE   A C   
1256 O  O   . PHE   A 203 ? 0.2110 0.1633 0.2082 0.0122  0.0371  0.0251  203  PHE   A O   
1257 C  CB  . PHE   A 203 ? 0.2014 0.1649 0.2058 0.0165  0.0358  0.0286  203  PHE   A CB  
1258 C  CG  . PHE   A 203 ? 0.2018 0.1692 0.2087 0.0185  0.0359  0.0303  203  PHE   A CG  
1259 C  CD1 . PHE   A 203 ? 0.1988 0.1650 0.2045 0.0187  0.0361  0.0295  203  PHE   A CD1 
1260 C  CD2 . PHE   A 203 ? 0.1959 0.1684 0.2064 0.0200  0.0356  0.0325  203  PHE   A CD2 
1261 C  CE1 . PHE   A 203 ? 0.2058 0.1756 0.2140 0.0205  0.0362  0.0311  203  PHE   A CE1 
1262 C  CE2 . PHE   A 203 ? 0.2034 0.1796 0.2162 0.0217  0.0356  0.0341  203  PHE   A CE2 
1263 C  CZ  . PHE   A 203 ? 0.1956 0.1705 0.2074 0.0219  0.0359  0.0334  203  PHE   A CZ  
1264 N  N   . SER   A 204 ? 0.2070 0.1603 0.2077 0.0146  0.0399  0.0285  204  SER   A N   
1265 C  CA  . SER   A 204 ? 0.2157 0.1670 0.2147 0.0124  0.0393  0.0272  204  SER   A CA  
1266 C  C   . SER   A 204 ? 0.2160 0.1734 0.2184 0.0125  0.0372  0.0281  204  SER   A C   
1267 O  O   . SER   A 204 ? 0.2392 0.1988 0.2441 0.0143  0.0382  0.0303  204  SER   A O   
1268 C  CB  . SER   A 204 ? 0.2446 0.1902 0.2421 0.0125  0.0426  0.0279  204  SER   A CB  
1269 O  OG  . SER   A 204 ? 0.2638 0.2031 0.2575 0.0119  0.0445  0.0266  204  SER   A OG  
1270 N  N   . ILE   A 205 ? 0.2148 0.1747 0.2170 0.0107  0.0344  0.0265  205  ILE   A N   
1271 C  CA  . ILE   A 205 ? 0.2082 0.1740 0.2134 0.0109  0.0323  0.0271  205  ILE   A CA  
1272 C  C   . ILE   A 205 ? 0.2137 0.1788 0.2184 0.0090  0.0318  0.0264  205  ILE   A C   
1273 O  O   . ILE   A 205 ? 0.2123 0.1743 0.2146 0.0069  0.0313  0.0247  205  ILE   A O   
1274 C  CB  . ILE   A 205 ? 0.2167 0.1867 0.2226 0.0106  0.0295  0.0260  205  ILE   A CB  
1275 C  CG1 . ILE   A 205 ? 0.2382 0.2093 0.2450 0.0125  0.0302  0.0270  205  ILE   A CG1 
1276 C  CG2 . ILE   A 205 ? 0.2209 0.1966 0.2295 0.0104  0.0273  0.0263  205  ILE   A CG2 
1277 C  CD1 . ILE   A 205 ? 0.2576 0.2310 0.2643 0.0122  0.0280  0.0258  205  ILE   A CD1 
1278 N  N   . LYS   A 206 ? 0.2034 0.1716 0.2106 0.0098  0.0319  0.0280  206  LYS   A N   
1279 C  CA  . LYS   A 206 ? 0.2097 0.1781 0.2171 0.0083  0.0314  0.0277  206  LYS   A CA  
1280 C  C   . LYS   A 206 ? 0.1961 0.1708 0.2064 0.0087  0.0294  0.0283  206  LYS   A C   
1281 O  O   . LYS   A 206 ? 0.2010 0.1790 0.2133 0.0106  0.0296  0.0300  206  LYS   A O   
1282 C  CB  . LYS   A 206 ? 0.2404 0.2052 0.2474 0.0089  0.0343  0.0292  206  LYS   A CB  
1283 C  CG  . LYS   A 206 ? 0.2816 0.2394 0.2852 0.0081  0.0365  0.0284  206  LYS   A CG  
1284 C  CD  . LYS   A 206 ? 0.3656 0.3196 0.3691 0.0092  0.0397  0.0301  206  LYS   A CD  
1285 C  CE  . LYS   A 206 ? 0.4502 0.3969 0.4502 0.0088  0.0424  0.0294  206  LYS   A CE  
1286 N  NZ  . LYS   A 206 ? 0.4826 0.4285 0.4815 0.0095  0.0423  0.0287  206  LYS   A NZ  
1287 N  N   A ILE   A 207 ? 0.1996 0.1761 0.2100 0.0070  0.0275  0.0270  207  ILE   A N   
1288 N  N   B ILE   A 207 ? 0.1911 0.1677 0.2016 0.0069  0.0274  0.0269  207  ILE   A N   
1289 C  CA  A ILE   A 207 ? 0.2014 0.1837 0.2145 0.0072  0.0257  0.0273  207  ILE   A CA  
1290 C  CA  B ILE   A 207 ? 0.1829 0.1652 0.1959 0.0071  0.0255  0.0272  207  ILE   A CA  
1291 C  C   A ILE   A 207 ? 0.1951 0.1778 0.2088 0.0060  0.0257  0.0275  207  ILE   A C   
1292 C  C   B ILE   A 207 ? 0.1893 0.1723 0.2031 0.0060  0.0255  0.0274  207  ILE   A C   
1293 O  O   A ILE   A 207 ? 0.2066 0.1866 0.2188 0.0041  0.0255  0.0262  207  ILE   A O   
1294 O  O   B ILE   A 207 ? 0.2057 0.1866 0.2182 0.0040  0.0250  0.0260  207  ILE   A O   
1295 C  CB  A ILE   A 207 ? 0.2076 0.1925 0.2209 0.0065  0.0232  0.0257  207  ILE   A CB  
1296 C  CB  B ILE   A 207 ? 0.1735 0.1580 0.1865 0.0062  0.0230  0.0255  207  ILE   A CB  
1297 C  CG1 A ILE   A 207 ? 0.2350 0.2191 0.2474 0.0075  0.0232  0.0255  207  ILE   A CG1 
1298 C  CG1 B ILE   A 207 ? 0.1878 0.1719 0.2001 0.0074  0.0230  0.0253  207  ILE   A CG1 
1299 C  CG2 A ILE   A 207 ? 0.2039 0.1945 0.2197 0.0070  0.0217  0.0262  207  ILE   A CG2 
1300 C  CG2 B ILE   A 207 ? 0.1745 0.1646 0.1899 0.0063  0.0213  0.0256  207  ILE   A CG2 
1301 C  CD1 A ILE   A 207 ? 0.2559 0.2418 0.2681 0.0068  0.0210  0.0240  207  ILE   A CD1 
1302 C  CD1 B ILE   A 207 ? 0.1839 0.1715 0.1981 0.0095  0.0233  0.0270  207  ILE   A CD1 
1303 N  N   . ARG   A 208 ? 0.1916 0.1775 0.2073 0.0070  0.0259  0.0290  208  ARG   A N   
1304 C  CA  . ARG   A 208 ? 0.2021 0.1889 0.2186 0.0059  0.0259  0.0292  208  ARG   A CA  
1305 C  C   . ARG   A 208 ? 0.2169 0.2089 0.2352 0.0055  0.0236  0.0284  208  ARG   A C   
1306 O  O   . ARG   A 208 ? 0.2215 0.2171 0.2410 0.0068  0.0229  0.0290  208  ARG   A O   
1307 C  CB  . ARG   A 208 ? 0.2276 0.2148 0.2451 0.0072  0.0277  0.0314  208  ARG   A CB  
1308 C  CG  . ARG   A 208 ? 0.2560 0.2376 0.2719 0.0073  0.0302  0.0321  208  ARG   A CG  
1309 C  CD  . ARG   A 208 ? 0.2976 0.2794 0.3145 0.0087  0.0320  0.0345  208  ARG   A CD  
1310 N  NE  . ARG   A 208 ? 0.3230 0.2990 0.3382 0.0089  0.0347  0.0351  208  ARG   A NE  
1311 C  CZ  . ARG   A 208 ? 0.3736 0.3486 0.3895 0.0102  0.0367  0.0373  208  ARG   A CZ  
1312 N  NH1 . ARG   A 208 ? 0.3542 0.3338 0.3723 0.0114  0.0363  0.0391  208  ARG   A NH1 
1313 N  NH2 . ARG   A 208 ? 0.4002 0.3695 0.4145 0.0104  0.0393  0.0378  208  ARG   A NH2 
1314 N  N   . ARG   A 209 ? 0.2100 0.2022 0.2285 0.0037  0.0227  0.0273  209  ARG   A N   
1315 C  CA  . ARG   A 209 ? 0.2083 0.2049 0.2285 0.0032  0.0207  0.0265  209  ARG   A CA  
1316 C  C   . ARG   A 209 ? 0.2203 0.2178 0.2414 0.0017  0.0205  0.0263  209  ARG   A C   
1317 O  O   . ARG   A 209 ? 0.2319 0.2262 0.2520 0.0005  0.0216  0.0264  209  ARG   A O   
1318 C  CB  . ARG   A 209 ? 0.2298 0.2259 0.2491 0.0026  0.0191  0.0248  209  ARG   A CB  
1319 C  CG  . ARG   A 209 ? 0.2585 0.2505 0.2759 0.0006  0.0192  0.0238  209  ARG   A CG  
1320 C  CD  . ARG   A 209 ? 0.2950 0.2876 0.3121 -0.0007 0.0173  0.0222  209  ARG   A CD  
1321 N  NE  . ARG   A 209 ? 0.2471 0.2352 0.2619 -0.0026 0.0176  0.0214  209  ARG   A NE  
1322 C  CZ  . ARG   A 209 ? 0.2502 0.2377 0.2649 -0.0047 0.0171  0.0208  209  ARG   A CZ  
1323 N  NH1 . ARG   A 209 ? 0.2332 0.2244 0.2504 -0.0051 0.0164  0.0211  209  ARG   A NH1 
1324 N  NH2 . ARG   A 209 ? 0.2436 0.2266 0.2556 -0.0065 0.0175  0.0200  209  ARG   A NH2 
1325 N  N   . GLU   A 210 ? 0.2190 0.2207 0.2420 0.0016  0.0192  0.0260  210  GLU   A N   
1326 C  CA  . GLU   A 210 ? 0.2157 0.2187 0.2399 0.0002  0.0188  0.0257  210  GLU   A CA  
1327 C  C   . GLU   A 210 ? 0.2253 0.2267 0.2489 -0.0017 0.0176  0.0242  210  GLU   A C   
1328 O  O   . GLU   A 210 ? 0.2260 0.2271 0.2489 -0.0016 0.0165  0.0233  210  GLU   A O   
1329 C  CB  . GLU   A 210 ? 0.2400 0.2479 0.2664 0.0007  0.0179  0.0257  210  GLU   A CB  
1330 C  CG  . GLU   A 210 ? 0.2798 0.2898 0.3066 0.0022  0.0188  0.0271  210  GLU   A CG  
1331 C  CD  . GLU   A 210 ? 0.3318 0.3462 0.3603 0.0025  0.0179  0.0268  210  GLU   A CD  
1332 O  OE1 . GLU   A 210 ? 0.3327 0.3486 0.3626 0.0015  0.0177  0.0265  210  GLU   A OE1 
1333 O  OE2 . GLU   A 210 ? 0.3071 0.3234 0.3356 0.0037  0.0175  0.0269  210  GLU   A OE2 
1334 N  N   . PRO   A 211 ? 0.2223 0.2231 0.2463 -0.0035 0.0177  0.0241  211  PRO   A N   
1335 C  CA  . PRO   A 211 ? 0.2258 0.2255 0.2493 -0.0055 0.0164  0.0229  211  PRO   A CA  
1336 C  C   . PRO   A 211 ? 0.2270 0.2303 0.2521 -0.0054 0.0143  0.0220  211  PRO   A C   
1337 O  O   . PRO   A 211 ? 0.2483 0.2506 0.2726 -0.0066 0.0131  0.0211  211  PRO   A O   
1338 C  CB  . PRO   A 211 ? 0.2469 0.2467 0.2713 -0.0073 0.0168  0.0231  211  PRO   A CB  
1339 C  CG  . PRO   A 211 ? 0.2596 0.2577 0.2834 -0.0064 0.0189  0.0244  211  PRO   A CG  
1340 C  CD  . PRO   A 211 ? 0.2313 0.2318 0.2559 -0.0039 0.0191  0.0251  211  PRO   A CD  
1341 N  N   . ARG   A 212 ? 0.2278 0.2353 0.2552 -0.0041 0.0141  0.0224  212  ARG   A N   
1342 C  CA  . ARG   A 212 ? 0.2366 0.2473 0.2656 -0.0039 0.0124  0.0217  212  ARG   A CA  
1343 C  C   . ARG   A 212 ? 0.2385 0.2484 0.2662 -0.0029 0.0116  0.0211  212  ARG   A C   
1344 O  O   . ARG   A 212 ? 0.2587 0.2707 0.2874 -0.0028 0.0102  0.0205  212  ARG   A O   
1345 C  CB  . ARG   A 212 ? 0.2430 0.2580 0.2745 -0.0028 0.0126  0.0222  212  ARG   A CB  
1346 C  CG  . ARG   A 212 ? 0.2841 0.2997 0.3149 -0.0009 0.0135  0.0229  212  ARG   A CG  
1347 C  CD  . ARG   A 212 ? 0.2973 0.3167 0.3301 -0.0002 0.0139  0.0233  212  ARG   A CD  
1348 N  NE  . ARG   A 212 ? 0.3135 0.3331 0.3453 0.0012  0.0149  0.0242  212  ARG   A NE  
1349 C  CZ  . ARG   A 212 ? 0.3614 0.3832 0.3933 0.0024  0.0146  0.0240  212  ARG   A CZ  
1350 N  NH1 . ARG   A 212 ? 0.3541 0.3778 0.3870 0.0025  0.0135  0.0231  212  ARG   A NH1 
1351 N  NH2 . ARG   A 212 ? 0.3686 0.3907 0.3995 0.0035  0.0153  0.0249  212  ARG   A NH2 
1352 N  N   . HIS   A 213 ? 0.2102 0.2172 0.2357 -0.0020 0.0127  0.0214  213  HIS   A N   
1353 C  CA  . HIS   A 213 ? 0.2067 0.2130 0.2310 -0.0010 0.0121  0.0208  213  HIS   A CA  
1354 C  C   . HIS   A 213 ? 0.2206 0.2227 0.2424 -0.0020 0.0121  0.0202  213  HIS   A C   
1355 O  O   . HIS   A 213 ? 0.2366 0.2356 0.2570 -0.0031 0.0130  0.0203  213  HIS   A O   
1356 C  CB  . HIS   A 213 ? 0.2241 0.2307 0.2480 0.0009  0.0132  0.0217  213  HIS   A CB  
1357 C  CG  . HIS   A 213 ? 0.2507 0.2614 0.2766 0.0019  0.0132  0.0222  213  HIS   A CG  
1358 N  ND1 . HIS   A 213 ? 0.2758 0.2872 0.3019 0.0027  0.0145  0.0235  213  HIS   A ND1 
1359 C  CD2 . HIS   A 213 ? 0.2717 0.2856 0.2991 0.0021  0.0121  0.0217  213  HIS   A CD2 
1360 C  CE1 . HIS   A 213 ? 0.2891 0.3042 0.3167 0.0033  0.0141  0.0235  213  HIS   A CE1 
1361 N  NE2 . HIS   A 213 ? 0.2825 0.2990 0.3109 0.0030  0.0127  0.0224  213  HIS   A NE2 
1362 N  N   . LEU   A 214 ? 0.2090 0.2108 0.2299 -0.0017 0.0110  0.0195  214  LEU   A N   
1363 C  CA  . LEU   A 214 ? 0.2131 0.2108 0.2312 -0.0023 0.0111  0.0188  214  LEU   A CA  
1364 C  C   . LEU   A 214 ? 0.1921 0.1885 0.2091 -0.0005 0.0122  0.0193  214  LEU   A C   
1365 O  O   . LEU   A 214 ? 0.1991 0.1984 0.2174 0.0010  0.0118  0.0195  214  LEU   A O   
1366 C  CB  . LEU   A 214 ? 0.2270 0.2258 0.2452 -0.0031 0.0091  0.0178  214  LEU   A CB  
1367 C  CG  . LEU   A 214 ? 0.2580 0.2531 0.2733 -0.0037 0.0089  0.0171  214  LEU   A CG  
1368 C  CD1 . LEU   A 214 ? 0.2726 0.2636 0.2854 -0.0057 0.0094  0.0167  214  LEU   A CD1 
1369 C  CD2 . LEU   A 214 ? 0.2951 0.2920 0.3108 -0.0041 0.0068  0.0164  214  LEU   A CD2 
1370 N  N   . ALA   A 215 ? 0.1767 0.1688 0.1913 -0.0006 0.0136  0.0194  215  ALA   A N   
1371 C  CA  . ALA   A 215 ? 0.1759 0.1667 0.1894 0.0010  0.0147  0.0198  215  ALA   A CA  
1372 C  C   . ALA   A 215 ? 0.1830 0.1703 0.1939 0.0003  0.0143  0.0187  215  ALA   A C   
1373 O  O   . ALA   A 215 ? 0.2008 0.1848 0.2098 -0.0015 0.0145  0.0180  215  ALA   A O   
1374 C  CB  . ALA   A 215 ? 0.1881 0.1769 0.2013 0.0020  0.0170  0.0211  215  ALA   A CB  
1375 N  N   . ILE   A 216 ? 0.1731 0.1611 0.1838 0.0015  0.0140  0.0186  216  ILE   A N   
1376 C  CA  . ILE   A 216 ? 0.1771 0.1616 0.1851 0.0011  0.0141  0.0178  216  ILE   A CA  
1377 C  C   . ILE   A 216 ? 0.1732 0.1571 0.1810 0.0031  0.0156  0.0186  216  ILE   A C   
1378 O  O   . ILE   A 216 ? 0.1762 0.1632 0.1861 0.0046  0.0158  0.0197  216  ILE   A O   
1379 C  CB  . ILE   A 216 ? 0.1943 0.1802 0.2022 0.0003  0.0119  0.0167  216  ILE   A CB  
1380 C  CG1 . ILE   A 216 ? 0.1827 0.1731 0.1930 0.0017  0.0108  0.0169  216  ILE   A CG1 
1381 C  CG2 . ILE   A 216 ? 0.2100 0.1961 0.2180 -0.0018 0.0106  0.0160  216  ILE   A CG2 
1382 C  CD1 . ILE   A 216 ? 0.2082 0.1998 0.2184 0.0011  0.0087  0.0160  216  ILE   A CD1 
1383 N  N   . SER   A 217 ? 0.1631 0.1428 0.1683 0.0030  0.0166  0.0182  217  SER   A N   
1384 C  CA  . SER   A 217 ? 0.1815 0.1603 0.1865 0.0048  0.0182  0.0191  217  SER   A CA  
1385 C  C   . SER   A 217 ? 0.1707 0.1462 0.1730 0.0044  0.0183  0.0182  217  SER   A C   
1386 O  O   . SER   A 217 ? 0.1816 0.1566 0.1826 0.0029  0.0167  0.0169  217  SER   A O   
1387 C  CB  . SER   A 217 ? 0.1776 0.1542 0.1826 0.0056  0.0206  0.0204  217  SER   A CB  
1388 O  OG  . SER   A 217 ? 0.1789 0.1552 0.1843 0.0075  0.0223  0.0217  217  SER   A OG  
1389 N  N   . ASN   A 218 ? 0.1697 0.1431 0.1712 0.0058  0.0202  0.0189  218  ASN   A N   
1390 C  CA  . ASN   A 218 ? 0.1793 0.1495 0.1782 0.0055  0.0204  0.0180  218  ASN   A CA  
1391 C  C   . ASN   A 218 ? 0.1884 0.1536 0.1837 0.0033  0.0207  0.0166  218  ASN   A C   
1392 O  O   . ASN   A 218 ? 0.1974 0.1613 0.1907 0.0021  0.0196  0.0154  218  ASN   A O   
1393 C  CB  . ASN   A 218 ? 0.1849 0.1534 0.1837 0.0074  0.0229  0.0192  218  ASN   A CB  
1394 C  CG  . ASN   A 218 ? 0.1838 0.1573 0.1859 0.0093  0.0225  0.0206  218  ASN   A CG  
1395 O  OD1 . ASN   A 218 ? 0.1822 0.1580 0.1865 0.0103  0.0231  0.0219  218  ASN   A OD1 
1396 N  ND2 . ASN   A 218 ? 0.1834 0.1585 0.1856 0.0099  0.0216  0.0203  218  ASN   A ND2 
1397 N  N   . MET   A 219 ? 0.1946 0.1568 0.1890 0.0027  0.0224  0.0169  219  MET   A N   
1398 C  CA  . MET   A 219 ? 0.2057 0.1623 0.1962 0.0006  0.0232  0.0157  219  MET   A CA  
1399 C  C   . MET   A 219 ? 0.2050 0.1623 0.1957 -0.0016 0.0218  0.0151  219  MET   A C   
1400 O  O   . MET   A 219 ? 0.2015 0.1629 0.1952 -0.0011 0.0208  0.0158  219  MET   A O   
1401 C  CB  . MET   A 219 ? 0.2128 0.1646 0.2019 0.0015  0.0266  0.0165  219  MET   A CB  
1402 C  CG  . MET   A 219 ? 0.2188 0.1698 0.2078 0.0036  0.0283  0.0172  219  MET   A CG  
1403 S  SD  . MET   A 219 ? 0.2567 0.2048 0.2423 0.0026  0.0277  0.0156  219  MET   A SD  
1404 C  CE  . MET   A 219 ? 0.2866 0.2274 0.2672 0.0002  0.0295  0.0143  219  MET   A CE  
1405 N  N   . PRO   A 220 ? 0.2139 0.1669 0.2009 -0.0041 0.0217  0.0138  220  PRO   A N   
1406 C  CA  . PRO   A 220 ? 0.2177 0.1714 0.2049 -0.0063 0.0205  0.0133  220  PRO   A CA  
1407 C  C   . PRO   A 220 ? 0.2309 0.1845 0.2197 -0.0058 0.0220  0.0143  220  PRO   A C   
1408 O  O   . PRO   A 220 ? 0.2297 0.1805 0.2181 -0.0044 0.0247  0.0152  220  PRO   A O   
1409 C  CB  . PRO   A 220 ? 0.2384 0.1864 0.2207 -0.0090 0.0208  0.0119  220  PRO   A CB  
1410 C  CG  . PRO   A 220 ? 0.2385 0.1848 0.2188 -0.0083 0.0210  0.0114  220  PRO   A CG  
1411 C  CD  . PRO   A 220 ? 0.2167 0.1643 0.1994 -0.0051 0.0228  0.0127  220  PRO   A CD  
1412 N  N   . LEU   A 221 ? 0.2172 0.1740 0.2079 -0.0071 0.0203  0.0143  221  LEU   A N   
1413 C  CA  . LEU   A 221 ? 0.2315 0.1883 0.2235 -0.0072 0.0215  0.0151  221  LEU   A CA  
1414 C  C   . LEU   A 221 ? 0.2600 0.2106 0.2481 -0.0096 0.0230  0.0143  221  LEU   A C   
1415 O  O   . LEU   A 221 ? 0.2821 0.2313 0.2678 -0.0123 0.0216  0.0130  221  LEU   A O   
1416 C  CB  . LEU   A 221 ? 0.2349 0.1968 0.2298 -0.0081 0.0191  0.0152  221  LEU   A CB  
1417 C  CG  . LEU   A 221 ? 0.2677 0.2300 0.2640 -0.0086 0.0200  0.0160  221  LEU   A CG  
1418 C  CD1 . LEU   A 221 ? 0.2777 0.2418 0.2765 -0.0059 0.0216  0.0175  221  LEU   A CD1 
1419 C  CD2 . LEU   A 221 ? 0.2888 0.2557 0.2876 -0.0101 0.0175  0.0158  221  LEU   A CD2 
1420 N  N   . VAL   A 222 ? 0.2562 0.2029 0.2433 -0.0086 0.0261  0.0151  222  VAL   A N   
1421 C  CA  . VAL   A 222 ? 0.2891 0.2292 0.2721 -0.0109 0.0278  0.0142  222  VAL   A CA  
1422 C  C   . VAL   A 222 ? 0.3151 0.2552 0.2990 -0.0121 0.0283  0.0146  222  VAL   A C   
1423 O  O   . VAL   A 222 ? 0.3334 0.2693 0.3142 -0.0149 0.0287  0.0136  222  VAL   A O   
1424 C  CB  . VAL   A 222 ? 0.3166 0.2508 0.2968 -0.0096 0.0311  0.0143  222  VAL   A CB  
1425 C  CG1 . VAL   A 222 ? 0.3297 0.2634 0.3083 -0.0092 0.0305  0.0135  222  VAL   A CG1 
1426 C  CG2 . VAL   A 222 ? 0.3322 0.2675 0.3153 -0.0065 0.0334  0.0163  222  VAL   A CG2 
1427 N  N   . LYS   A 223 ? 0.2971 0.2418 0.2851 -0.0104 0.0281  0.0161  223  LYS   A N   
1428 C  CA  . LYS   A 223 ? 0.3072 0.2518 0.2961 -0.0114 0.0287  0.0166  223  LYS   A CA  
1429 C  C   . LYS   A 223 ? 0.2925 0.2435 0.2861 -0.0096 0.0277  0.0180  223  LYS   A C   
1430 O  O   . LYS   A 223 ? 0.2754 0.2295 0.2712 -0.0070 0.0276  0.0190  223  LYS   A O   
1431 C  CB  . LYS   A 223 ? 0.3462 0.2847 0.3330 -0.0108 0.0324  0.0173  223  LYS   A CB  
1432 C  CG  . LYS   A 223 ? 0.4306 0.3673 0.4171 -0.0125 0.0334  0.0175  223  LYS   A CG  
1433 C  CD  . LYS   A 223 ? 0.4974 0.4281 0.4821 -0.0115 0.0372  0.0184  223  LYS   A CD  
1434 C  CE  . LYS   A 223 ? 0.5638 0.4871 0.5434 -0.0145 0.0387  0.0168  223  LYS   A CE  
1435 N  NZ  . LYS   A 223 ? 0.5863 0.5030 0.5636 -0.0132 0.0428  0.0175  223  LYS   A NZ  
1436 N  N   . SER   A 224 ? 0.2873 0.2407 0.2826 -0.0110 0.0267  0.0182  224  SER   A N   
1437 C  CA  . SER   A 224 ? 0.2895 0.2486 0.2889 -0.0094 0.0260  0.0195  224  SER   A CA  
1438 C  C   . SER   A 224 ? 0.3092 0.2661 0.3085 -0.0102 0.0278  0.0203  224  SER   A C   
1439 O  O   . SER   A 224 ? 0.3349 0.2891 0.3324 -0.0129 0.0278  0.0194  224  SER   A O   
1440 C  CB  . SER   A 224 ? 0.2796 0.2441 0.2814 -0.0106 0.0230  0.0189  224  SER   A CB  
1441 O  OG  . SER   A 224 ? 0.2837 0.2501 0.2855 -0.0098 0.0213  0.0183  224  SER   A OG  
1442 N  N   . VAL   A 225 ? 0.2898 0.2476 0.2909 -0.0079 0.0295  0.0219  225  VAL   A N   
1443 C  CA  . VAL   A 225 ? 0.2994 0.2548 0.3005 -0.0082 0.0316  0.0229  225  VAL   A CA  
1444 C  C   . VAL   A 225 ? 0.2915 0.2525 0.2963 -0.0072 0.0308  0.0243  225  VAL   A C   
1445 O  O   . VAL   A 225 ? 0.2905 0.2554 0.2975 -0.0048 0.0303  0.0253  225  VAL   A O   
1446 C  CB  . VAL   A 225 ? 0.3342 0.2852 0.3339 -0.0061 0.0347  0.0241  225  VAL   A CB  
1447 C  CG1 . VAL   A 225 ? 0.3537 0.3019 0.3533 -0.0061 0.0371  0.0254  225  VAL   A CG1 
1448 C  CG2 . VAL   A 225 ? 0.3724 0.3177 0.3683 -0.0068 0.0357  0.0228  225  VAL   A CG2 
1449 N  N   . THR   A 226 ? 0.2898 0.2508 0.2951 -0.0089 0.0310  0.0244  226  THR   A N   
1450 C  CA  . THR   A 226 ? 0.2938 0.2597 0.3024 -0.0078 0.0306  0.0258  226  THR   A CA  
1451 C  C   . THR   A 226 ? 0.2948 0.2591 0.3036 -0.0055 0.0331  0.0278  226  THR   A C   
1452 O  O   . THR   A 226 ? 0.3091 0.2678 0.3157 -0.0057 0.0356  0.0281  226  THR   A O   
1453 C  CB  . THR   A 226 ? 0.3500 0.3162 0.3590 -0.0105 0.0301  0.0253  226  THR   A CB  
1454 O  OG1 . THR   A 226 ? 0.3799 0.3483 0.3890 -0.0124 0.0275  0.0237  226  THR   A OG1 
1455 C  CG2 . THR   A 226 ? 0.3661 0.3368 0.3782 -0.0096 0.0301  0.0267  226  THR   A CG2 
1456 N  N   . VAL   A 227 ? 0.2714 0.2405 0.2829 -0.0031 0.0327  0.0291  227  VAL   A N   
1457 C  CA  . VAL   A 227 ? 0.2760 0.2445 0.2882 -0.0008 0.0348  0.0313  227  VAL   A CA  
1458 C  C   . VAL   A 227 ? 0.2807 0.2538 0.2954 -0.0006 0.0344  0.0326  227  VAL   A C   
1459 O  O   . VAL   A 227 ? 0.3048 0.2807 0.3206 -0.0022 0.0327  0.0316  227  VAL   A O   
1460 C  CB  . VAL   A 227 ? 0.2807 0.2500 0.2931 0.0017  0.0351  0.0321  227  VAL   A CB  
1461 C  CG1 . VAL   A 227 ? 0.2996 0.2636 0.3092 0.0013  0.0360  0.0310  227  VAL   A CG1 
1462 C  CG2 . VAL   A 227 ? 0.2827 0.2580 0.2971 0.0024  0.0325  0.0317  227  VAL   A CG2 
1463 N  N   . ALA   A 228 ? 0.2832 0.2569 0.2990 0.0014  0.0359  0.0348  228  ALA   A N   
1464 C  CA  . ALA   A 228 ? 0.2910 0.2685 0.3087 0.0017  0.0358  0.0361  228  ALA   A CA  
1465 C  C   . ALA   A 228 ? 0.3004 0.2842 0.3202 0.0019  0.0333  0.0356  228  ALA   A C   
1466 O  O   . ALA   A 228 ? 0.2957 0.2815 0.3157 0.0026  0.0319  0.0348  228  ALA   A O   
1467 C  CB  . ALA   A 228 ? 0.3052 0.2823 0.3235 0.0040  0.0377  0.0387  228  ALA   A CB  
1468 N  N   . GLU   A 229 ? 0.3193 0.3060 0.3405 0.0012  0.0330  0.0361  229  GLU   A N   
1469 C  CA  . GLU   A 229 ? 0.3475 0.3400 0.3707 0.0015  0.0312  0.0359  229  GLU   A CA  
1470 C  C   . GLU   A 229 ? 0.3522 0.3467 0.3758 0.0004  0.0289  0.0338  229  GLU   A C   
1471 O  O   . GLU   A 229 ? 0.3738 0.3720 0.3983 0.0014  0.0276  0.0335  229  GLU   A O   
1472 C  CB  . GLU   A 229 ? 0.3797 0.3749 0.4035 0.0039  0.0313  0.0376  229  GLU   A CB  
1473 C  CG  . GLU   A 229 ? 0.4695 0.4633 0.4933 0.0049  0.0334  0.0400  229  GLU   A CG  
1474 C  CD  . GLU   A 229 ? 0.5671 0.5641 0.5918 0.0071  0.0335  0.0421  229  GLU   A CD  
1475 O  OE1 . GLU   A 229 ? 0.5847 0.5808 0.6091 0.0085  0.0339  0.0428  229  GLU   A OE1 
1476 O  OE2 . GLU   A 229 ? 0.5895 0.5900 0.6152 0.0072  0.0333  0.0432  229  GLU   A OE2 
1477 N  N   . GLY   A 230 ? 0.3421 0.3340 0.3649 -0.0017 0.0286  0.0323  230  GLY   A N   
1478 C  CA  . GLY   A 230 ? 0.3439 0.3376 0.3671 -0.0030 0.0266  0.0304  230  GLY   A CA  
1479 C  C   . GLY   A 230 ? 0.3332 0.3268 0.3557 -0.0022 0.0254  0.0295  230  GLY   A C   
1480 O  O   . GLY   A 230 ? 0.3669 0.3634 0.3904 -0.0026 0.0236  0.0283  230  GLY   A O   
1481 N  N   . LEU   A 231 ? 0.2795 0.2699 0.3003 -0.0010 0.0266  0.0300  231  LEU   A N   
1482 C  CA  . LEU   A 231 ? 0.2647 0.2547 0.2846 -0.0002 0.0257  0.0291  231  LEU   A CA  
1483 C  C   . LEU   A 231 ? 0.2590 0.2439 0.2765 -0.0016 0.0261  0.0279  231  LEU   A C   
1484 O  O   . LEU   A 231 ? 0.2683 0.2492 0.2844 -0.0028 0.0276  0.0281  231  LEU   A O   
1485 C  CB  . LEU   A 231 ? 0.2686 0.2590 0.2886 0.0022  0.0267  0.0306  231  LEU   A CB  
1486 C  CG  . LEU   A 231 ? 0.3173 0.3127 0.3393 0.0035  0.0263  0.0319  231  LEU   A CG  
1487 C  CD1 . LEU   A 231 ? 0.3525 0.3483 0.3745 0.0057  0.0271  0.0335  231  LEU   A CD1 
1488 C  CD2 . LEU   A 231 ? 0.3542 0.3540 0.3776 0.0030  0.0241  0.0306  231  LEU   A CD2 
1489 N  N   . ILE   A 232 ? 0.2352 0.2201 0.2519 -0.0016 0.0249  0.0267  232  ILE   A N   
1490 C  CA  . ILE   A 232 ? 0.2248 0.2048 0.2388 -0.0028 0.0252  0.0256  232  ILE   A CA  
1491 C  C   . ILE   A 232 ? 0.2241 0.2026 0.2370 -0.0009 0.0260  0.0259  232  ILE   A C   
1492 O  O   . ILE   A 232 ? 0.2231 0.2054 0.2374 0.0006  0.0249  0.0262  232  ILE   A O   
1493 C  CB  . ILE   A 232 ? 0.2467 0.2279 0.2604 -0.0047 0.0229  0.0238  232  ILE   A CB  
1494 C  CG1 . ILE   A 232 ? 0.2948 0.2776 0.3099 -0.0067 0.0223  0.0236  232  ILE   A CG1 
1495 C  CG2 . ILE   A 232 ? 0.2556 0.2319 0.2661 -0.0061 0.0231  0.0225  232  ILE   A CG2 
1496 C  CD1 . ILE   A 232 ? 0.3341 0.3195 0.3501 -0.0081 0.0200  0.0225  232  ILE   A CD1 
1497 N  N   . GLU   A 233 ? 0.2131 0.1864 0.2236 -0.0009 0.0278  0.0259  233  GLU   A N   
1498 C  CA  . GLU   A 233 ? 0.2173 0.1888 0.2267 0.0009  0.0288  0.0263  233  GLU   A CA  
1499 C  C   . GLU   A 233 ? 0.2331 0.2012 0.2399 -0.0006 0.0282  0.0244  233  GLU   A C   
1500 O  O   . GLU   A 233 ? 0.2506 0.2139 0.2547 -0.0024 0.0292  0.0236  233  GLU   A O   
1501 C  CB  . GLU   A 233 ? 0.2599 0.2277 0.2687 0.0021  0.0318  0.0279  233  GLU   A CB  
1502 C  CG  . GLU   A 233 ? 0.2780 0.2436 0.2859 0.0040  0.0332  0.0286  233  GLU   A CG  
1503 C  CD  . GLU   A 233 ? 0.3644 0.3261 0.3717 0.0051  0.0363  0.0303  233  GLU   A CD  
1504 O  OE1 . GLU   A 233 ? 0.3997 0.3554 0.4043 0.0041  0.0382  0.0296  233  GLU   A OE1 
1505 O  OE2 . GLU   A 233 ? 0.3300 0.2947 0.3397 0.0069  0.0369  0.0323  233  GLU   A OE2 
1506 N  N   . ASP   A 234 ? 0.2088 0.1793 0.2159 0.0000  0.0266  0.0238  234  ASP   A N   
1507 C  CA  . ASP   A 234 ? 0.2198 0.1875 0.2244 -0.0012 0.0258  0.0221  234  ASP   A CA  
1508 C  C   . ASP   A 234 ? 0.2340 0.1978 0.2368 0.0003  0.0280  0.0226  234  ASP   A C   
1509 O  O   . ASP   A 234 ? 0.2431 0.2091 0.2476 0.0027  0.0286  0.0240  234  ASP   A O   
1510 C  CB  . ASP   A 234 ? 0.2147 0.1871 0.2208 -0.0010 0.0232  0.0214  234  ASP   A CB  
1511 C  CG  . ASP   A 234 ? 0.2234 0.1993 0.2311 -0.0026 0.0210  0.0207  234  ASP   A CG  
1512 O  OD1 . ASP   A 234 ? 0.2324 0.2065 0.2394 -0.0046 0.0213  0.0204  234  ASP   A OD1 
1513 O  OD2 . ASP   A 234 ? 0.2336 0.2141 0.2434 -0.0019 0.0193  0.0207  234  ASP   A OD2 
1514 N  N   . HIS   A 235 ? 0.2151 0.1733 0.2144 -0.0011 0.0290  0.0215  235  HIS   A N   
1515 C  CA  . HIS   A 235 ? 0.2243 0.1785 0.2217 0.0003  0.0312  0.0218  235  HIS   A CA  
1516 C  C   . HIS   A 235 ? 0.2261 0.1795 0.2215 -0.0006 0.0299  0.0202  235  HIS   A C   
1517 O  O   . HIS   A 235 ? 0.2413 0.1928 0.2344 -0.0031 0.0286  0.0186  235  HIS   A O   
1518 C  CB  . HIS   A 235 ? 0.2453 0.1927 0.2396 -0.0008 0.0340  0.0216  235  HIS   A CB  
1519 C  CG  . HIS   A 235 ? 0.2949 0.2420 0.2907 -0.0002 0.0357  0.0232  235  HIS   A CG  
1520 N  ND1 . HIS   A 235 ? 0.3518 0.2927 0.3450 -0.0009 0.0385  0.0232  235  HIS   A ND1 
1521 C  CD2 . HIS   A 235 ? 0.3332 0.2853 0.3325 0.0011  0.0351  0.0247  235  HIS   A CD2 
1522 C  CE1 . HIS   A 235 ? 0.3485 0.2908 0.3439 0.0001  0.0395  0.0249  235  HIS   A CE1 
1523 N  NE2 . HIS   A 235 ? 0.3372 0.2862 0.3362 0.0013  0.0375  0.0258  235  HIS   A NE2 
1524 N  N   . PHE   A 236 ? 0.2079 0.1629 0.2042 0.0014  0.0298  0.0207  236  PHE   A N   
1525 C  CA  . PHE   A 236 ? 0.2127 0.1667 0.2070 0.0008  0.0287  0.0193  236  PHE   A CA  
1526 C  C   . PHE   A 236 ? 0.2216 0.1696 0.2128 0.0013  0.0315  0.0192  236  PHE   A C   
1527 O  O   . PHE   A 236 ? 0.2347 0.1811 0.2265 0.0031  0.0341  0.0207  236  PHE   A O   
1528 C  CB  . PHE   A 236 ? 0.1994 0.1592 0.1966 0.0025  0.0269  0.0198  236  PHE   A CB  
1529 C  CG  . PHE   A 236 ? 0.1934 0.1585 0.1932 0.0019  0.0244  0.0197  236  PHE   A CG  
1530 C  CD1 . PHE   A 236 ? 0.1992 0.1655 0.1985 0.0000  0.0220  0.0183  236  PHE   A CD1 
1531 C  CD2 . PHE   A 236 ? 0.1920 0.1608 0.1949 0.0032  0.0246  0.0212  236  PHE   A CD2 
1532 C  CE1 . PHE   A 236 ? 0.2099 0.1809 0.2118 -0.0005 0.0199  0.0183  236  PHE   A CE1 
1533 C  CE2 . PHE   A 236 ? 0.1989 0.1722 0.2040 0.0025  0.0225  0.0210  236  PHE   A CE2 
1534 C  CZ  . PHE   A 236 ? 0.2116 0.1861 0.2164 0.0008  0.0203  0.0196  236  PHE   A CZ  
1535 N  N   . ASP   A 237 ? 0.2219 0.1666 0.2097 -0.0003 0.0311  0.0176  237  ASP   A N   
1536 C  CA  . ASP   A 237 ? 0.2280 0.1666 0.2125 0.0000  0.0339  0.0173  237  ASP   A CA  
1537 C  C   . ASP   A 237 ? 0.2331 0.1735 0.2197 0.0031  0.0351  0.0188  237  ASP   A C   
1538 O  O   . ASP   A 237 ? 0.2307 0.1767 0.2204 0.0043  0.0332  0.0194  237  ASP   A O   
1539 C  CB  . ASP   A 237 ? 0.2597 0.1947 0.2400 -0.0025 0.0329  0.0153  237  ASP   A CB  
1540 C  CG  . ASP   A 237 ? 0.3502 0.2773 0.3259 -0.0035 0.0361  0.0145  237  ASP   A CG  
1541 O  OD1 . ASP   A 237 ? 0.3251 0.2494 0.3011 -0.0018 0.0392  0.0157  237  ASP   A OD1 
1542 O  OD2 . ASP   A 237 ? 0.3891 0.3127 0.3608 -0.0058 0.0355  0.0128  237  ASP   A OD2 
1543 N  N   . VAL   A 238 ? 0.2370 0.1724 0.2217 0.0041  0.0383  0.0192  238  VAL   A N   
1544 C  CA  . VAL   A 238 ? 0.2365 0.1734 0.2232 0.0070  0.0396  0.0208  238  VAL   A CA  
1545 C  C   . VAL   A 238 ? 0.2353 0.1738 0.2213 0.0068  0.0379  0.0197  238  VAL   A C   
1546 O  O   . VAL   A 238 ? 0.2423 0.1775 0.2247 0.0047  0.0372  0.0179  238  VAL   A O   
1547 C  CB  . VAL   A 238 ? 0.2441 0.1748 0.2290 0.0082  0.0439  0.0216  238  VAL   A CB  
1548 C  CG1 . VAL   A 238 ? 0.2687 0.1924 0.2482 0.0062  0.0452  0.0196  238  VAL   A CG1 
1549 C  CG2 . VAL   A 238 ? 0.2465 0.1797 0.2344 0.0114  0.0454  0.0237  238  VAL   A CG2 
1550 N  N   . THR   A 239 ? 0.2156 0.1594 0.2051 0.0089  0.0370  0.0210  239  THR   A N   
1551 C  CA  . THR   A 239 ? 0.2222 0.1674 0.2111 0.0090  0.0356  0.0202  239  THR   A CA  
1552 C  C   . THR   A 239 ? 0.2348 0.1748 0.2212 0.0098  0.0385  0.0202  239  THR   A C   
1553 O  O   . THR   A 239 ? 0.2442 0.1808 0.2304 0.0110  0.0417  0.0213  239  THR   A O   
1554 C  CB  . THR   A 239 ? 0.2138 0.1659 0.2070 0.0109  0.0340  0.0216  239  THR   A CB  
1555 O  OG1 . THR   A 239 ? 0.2208 0.1733 0.2162 0.0134  0.0364  0.0238  239  THR   A OG1 
1556 C  CG2 . THR   A 239 ? 0.2107 0.1679 0.2066 0.0104  0.0315  0.0218  239  THR   A CG2 
1557 N  N   . VAL   A 240 ? 0.2421 0.1820 0.2270 0.0093  0.0375  0.0191  240  VAL   A N   
1558 C  CA  . VAL   A 240 ? 0.2442 0.1809 0.2277 0.0106  0.0399  0.0195  240  VAL   A CA  
1559 C  C   . VAL   A 240 ? 0.2294 0.1710 0.2176 0.0136  0.0406  0.0219  240  VAL   A C   
1560 O  O   . VAL   A 240 ? 0.2331 0.1803 0.2250 0.0144  0.0389  0.0230  240  VAL   A O   
1561 C  CB  . VAL   A 240 ? 0.2575 0.1939 0.2386 0.0094  0.0382  0.0178  240  VAL   A CB  
1562 C  CG1 . VAL   A 240 ? 0.2874 0.2190 0.2637 0.0063  0.0376  0.0156  240  VAL   A CG1 
1563 C  CG2 . VAL   A 240 ? 0.2669 0.2102 0.2512 0.0096  0.0348  0.0180  240  VAL   A CG2 
1564 N  N   . LYS   A 241 ? 0.2283 0.1679 0.2164 0.0153  0.0432  0.0228  241  LYS   A N   
1565 C  CA  . LYS   A 241 ? 0.2299 0.1740 0.2222 0.0180  0.0439  0.0252  241  LYS   A CA  
1566 C  C   . LYS   A 241 ? 0.2219 0.1722 0.2165 0.0179  0.0406  0.0250  241  LYS   A C   
1567 O  O   . LYS   A 241 ? 0.2236 0.1728 0.2158 0.0167  0.0394  0.0234  241  LYS   A O   
1568 C  CB  . LYS   A 241 ? 0.2816 0.2219 0.2729 0.0194  0.0472  0.0259  241  LYS   A CB  
1569 C  CG  . LYS   A 241 ? 0.3461 0.2902 0.3418 0.0223  0.0486  0.0287  241  LYS   A CG  
1570 C  CD  . LYS   A 241 ? 0.3961 0.3352 0.3906 0.0238  0.0527  0.0296  241  LYS   A CD  
1571 C  CE  . LYS   A 241 ? 0.4608 0.4045 0.4603 0.0267  0.0540  0.0327  241  LYS   A CE  
1572 N  NZ  . LYS   A 241 ? 0.4803 0.4202 0.4794 0.0285  0.0578  0.0338  241  LYS   A NZ  
1573 N  N   . MET   A 242 ? 0.2080 0.1643 0.2066 0.0190  0.0392  0.0266  242  MET   A N   
1574 C  CA  . MET   A 242 ? 0.1997 0.1617 0.2002 0.0187  0.0361  0.0264  242  MET   A CA  
1575 C  C   . MET   A 242 ? 0.1924 0.1604 0.1974 0.0205  0.0357  0.0287  242  MET   A C   
1576 O  O   . MET   A 242 ? 0.1952 0.1633 0.2019 0.0218  0.0374  0.0306  242  MET   A O   
1577 C  CB  . MET   A 242 ? 0.1904 0.1533 0.1896 0.0165  0.0332  0.0244  242  MET   A CB  
1578 C  CG  . MET   A 242 ? 0.1992 0.1643 0.2002 0.0164  0.0325  0.0251  242  MET   A CG  
1579 S  SD  . MET   A 242 ? 0.2106 0.1762 0.2100 0.0138  0.0294  0.0228  242  MET   A SD  
1580 C  CE  . MET   A 242 ? 0.2049 0.1758 0.2081 0.0144  0.0283  0.0243  242  MET   A CE  
1581 N  N   . SER   A 243 ? 0.1841 0.1571 0.1908 0.0205  0.0333  0.0287  243  SER   A N   
1582 C  CA  . SER   A 243 ? 0.1712 0.1503 0.1818 0.0217  0.0325  0.0308  243  SER   A CA  
1583 C  C   . SER   A 243 ? 0.1698 0.1518 0.1816 0.0211  0.0308  0.0308  243  SER   A C   
1584 O  O   . SER   A 243 ? 0.1744 0.1554 0.1845 0.0194  0.0292  0.0289  243  SER   A O   
1585 C  CB  . SER   A 243 ? 0.1874 0.1702 0.1988 0.0215  0.0306  0.0304  243  SER   A CB  
1586 O  OG  . SER   A 243 ? 0.1923 0.1723 0.2024 0.0220  0.0321  0.0302  243  SER   A OG  
1587 N  N   . THR   A 244 ? 0.1660 0.1520 0.1809 0.0224  0.0311  0.0331  244  THR   A N   
1588 C  CA  . THR   A 244 ? 0.1636 0.1526 0.1798 0.0218  0.0297  0.0334  244  THR   A CA  
1589 C  C   . THR   A 244 ? 0.1678 0.1599 0.1837 0.0203  0.0266  0.0317  244  THR   A C   
1590 O  O   . THR   A 244 ? 0.1721 0.1647 0.1877 0.0193  0.0254  0.0308  244  THR   A O   
1591 C  CB  . THR   A 244 ? 0.1669 0.1605 0.1864 0.0234  0.0301  0.0362  244  THR   A CB  
1592 O  OG1 . THR   A 244 ? 0.1633 0.1607 0.1846 0.0241  0.0295  0.0372  244  THR   A OG1 
1593 C  CG2 . THR   A 244 ? 0.1773 0.1680 0.1975 0.0250  0.0332  0.0383  244  THR   A CG2 
1594 N  N   . TYR   A 245 ? 0.1545 0.1485 0.1705 0.0202  0.0255  0.0312  245  TYR   A N   
1595 C  CA  . TYR   A 245 ? 0.1588 0.1558 0.1747 0.0189  0.0227  0.0297  245  TYR   A CA  
1596 C  C   . TYR   A 245 ? 0.1680 0.1619 0.1814 0.0173  0.0217  0.0273  245  TYR   A C   
1597 O  O   . TYR   A 245 ? 0.1678 0.1639 0.1813 0.0163  0.0196  0.0261  245  TYR   A O   
1598 C  CB  . TYR   A 245 ? 0.1564 0.1564 0.1731 0.0191  0.0217  0.0298  245  TYR   A CB  
1599 C  CG  . TYR   A 245 ? 0.1512 0.1479 0.1658 0.0188  0.0220  0.0285  245  TYR   A CG  
1600 C  CD1 . TYR   A 245 ? 0.1544 0.1496 0.1670 0.0174  0.0204  0.0262  245  TYR   A CD1 
1601 C  CD2 . TYR   A 245 ? 0.1654 0.1609 0.1804 0.0200  0.0239  0.0296  245  TYR   A CD2 
1602 C  CE1 . TYR   A 245 ? 0.1584 0.1506 0.1690 0.0171  0.0206  0.0251  245  TYR   A CE1 
1603 C  CE2 . TYR   A 245 ? 0.1686 0.1609 0.1815 0.0197  0.0243  0.0284  245  TYR   A CE2 
1604 C  CZ  . TYR   A 245 ? 0.1593 0.1501 0.1699 0.0182  0.0226  0.0261  245  TYR   A CZ  
1605 O  OH  . TYR   A 245 ? 0.1729 0.1607 0.1813 0.0178  0.0229  0.0250  245  TYR   A OH  
1606 N  N   . LEU   A 246 ? 0.1654 0.1541 0.1766 0.0170  0.0231  0.0265  246  LEU   A N   
1607 C  CA  . LEU   A 246 ? 0.1682 0.1540 0.1769 0.0153  0.0221  0.0244  246  LEU   A CA  
1608 C  C   . LEU   A 246 ? 0.1683 0.1529 0.1768 0.0145  0.0222  0.0242  246  LEU   A C   
1609 O  O   . LEU   A 246 ? 0.1690 0.1517 0.1757 0.0130  0.0212  0.0226  246  LEU   A O   
1610 C  CB  . LEU   A 246 ? 0.1687 0.1495 0.1746 0.0150  0.0234  0.0235  246  LEU   A CB  
1611 C  CG  . LEU   A 246 ? 0.1693 0.1510 0.1750 0.0154  0.0229  0.0232  246  LEU   A CG  
1612 C  CD1 . LEU   A 246 ? 0.1857 0.1621 0.1887 0.0154  0.0249  0.0227  246  LEU   A CD1 
1613 C  CD2 . LEU   A 246 ? 0.1771 0.1607 0.1824 0.0141  0.0202  0.0216  246  LEU   A CD2 
1614 N  N   . VAL   A 247 ? 0.1624 0.1483 0.1727 0.0155  0.0234  0.0259  247  VAL   A N   
1615 C  CA  . VAL   A 247 ? 0.1638 0.1487 0.1739 0.0147  0.0235  0.0257  247  VAL   A CA  
1616 C  C   . VAL   A 247 ? 0.1609 0.1494 0.1719 0.0137  0.0210  0.0248  247  VAL   A C   
1617 O  O   . VAL   A 247 ? 0.1665 0.1592 0.1792 0.0141  0.0197  0.0252  247  VAL   A O   
1618 C  CB  . VAL   A 247 ? 0.1653 0.1514 0.1774 0.0162  0.0252  0.0280  247  VAL   A CB  
1619 C  CG1 . VAL   A 247 ? 0.1790 0.1650 0.1914 0.0154  0.0251  0.0281  247  VAL   A CG1 
1620 C  CG2 . VAL   A 247 ? 0.1926 0.1745 0.2038 0.0173  0.0281  0.0290  247  VAL   A CG2 
1621 N  N   . ALA   A 248 ? 0.1624 0.1494 0.1724 0.0122  0.0204  0.0236  248  ALA   A N   
1622 C  CA  . ALA   A 248 ? 0.1631 0.1534 0.1742 0.0113  0.0183  0.0228  248  ALA   A CA  
1623 C  C   . ALA   A 248 ? 0.1644 0.1536 0.1754 0.0102  0.0184  0.0226  248  ALA   A C   
1624 O  O   . ALA   A 248 ? 0.1723 0.1573 0.1814 0.0095  0.0195  0.0222  248  ALA   A O   
1625 C  CB  . ALA   A 248 ? 0.1672 0.1572 0.1771 0.0103  0.0165  0.0211  248  ALA   A CB  
1626 N  N   . PHE   A 249 ? 0.1580 0.1508 0.1707 0.0100  0.0172  0.0227  249  PHE   A N   
1627 C  CA  . PHE   A 249 ? 0.1638 0.1562 0.1767 0.0088  0.0170  0.0223  249  PHE   A CA  
1628 C  C   . PHE   A 249 ? 0.1675 0.1642 0.1822 0.0085  0.0153  0.0220  249  PHE   A C   
1629 O  O   . PHE   A 249 ? 0.1738 0.1739 0.1899 0.0094  0.0147  0.0225  249  PHE   A O   
1630 C  CB  . PHE   A 249 ? 0.1734 0.1643 0.1866 0.0093  0.0190  0.0238  249  PHE   A CB  
1631 C  CG  . PHE   A 249 ? 0.1754 0.1687 0.1902 0.0112  0.0200  0.0258  249  PHE   A CG  
1632 C  CD1 . PHE   A 249 ? 0.1779 0.1755 0.1947 0.0116  0.0194  0.0266  249  PHE   A CD1 
1633 C  CD2 . PHE   A 249 ? 0.1847 0.1761 0.1991 0.0124  0.0217  0.0268  249  PHE   A CD2 
1634 C  CE1 . PHE   A 249 ? 0.1790 0.1790 0.1972 0.0130  0.0201  0.0286  249  PHE   A CE1 
1635 C  CE2 . PHE   A 249 ? 0.1884 0.1823 0.2045 0.0141  0.0225  0.0288  249  PHE   A CE2 
1636 C  CZ  . PHE   A 249 ? 0.1695 0.1677 0.1874 0.0143  0.0216  0.0297  249  PHE   A CZ  
1637 N  N   . ILE   A 250 ? 0.1575 0.1540 0.1722 0.0071  0.0144  0.0211  250  ILE   A N   
1638 C  CA  . ILE   A 250 ? 0.1577 0.1579 0.1741 0.0067  0.0128  0.0206  250  ILE   A CA  
1639 C  C   . ILE   A 250 ? 0.1606 0.1609 0.1778 0.0057  0.0130  0.0207  250  ILE   A C   
1640 O  O   . ILE   A 250 ? 0.1694 0.1666 0.1852 0.0044  0.0133  0.0202  250  ILE   A O   
1641 C  CB  . ILE   A 250 ? 0.1600 0.1603 0.1760 0.0059  0.0111  0.0192  250  ILE   A CB  
1642 C  CG1 . ILE   A 250 ? 0.1709 0.1707 0.1859 0.0068  0.0110  0.0190  250  ILE   A CG1 
1643 C  CG2 . ILE   A 250 ? 0.1804 0.1845 0.1983 0.0058  0.0098  0.0188  250  ILE   A CG2 
1644 C  CD1 . ILE   A 250 ? 0.1852 0.1847 0.1995 0.0060  0.0094  0.0177  250  ILE   A CD1 
1645 N  N   . ILE   A 251 ? 0.1615 0.1651 0.1805 0.0060  0.0129  0.0213  251  ILE   A N   
1646 C  CA  . ILE   A 251 ? 0.1650 0.1692 0.1850 0.0050  0.0130  0.0214  251  ILE   A CA  
1647 C  C   . ILE   A 251 ? 0.1623 0.1698 0.1839 0.0047  0.0115  0.0207  251  ILE   A C   
1648 O  O   . ILE   A 251 ? 0.1670 0.1775 0.1896 0.0056  0.0113  0.0209  251  ILE   A O   
1649 C  CB  . ILE   A 251 ? 0.1804 0.1853 0.2011 0.0058  0.0145  0.0229  251  ILE   A CB  
1650 C  CG1 . ILE   A 251 ? 0.2249 0.2260 0.2440 0.0063  0.0162  0.0238  251  ILE   A CG1 
1651 C  CG2 . ILE   A 251 ? 0.2009 0.2064 0.2226 0.0048  0.0146  0.0231  251  ILE   A CG2 
1652 C  CD1 . ILE   A 251 ? 0.3027 0.3045 0.3217 0.0079  0.0167  0.0246  251  ILE   A CD1 
1653 N  N   . SER   A 252 ? 0.1546 0.1619 0.1766 0.0033  0.0106  0.0199  252  SER   A N   
1654 C  CA  . SER   A 252 ? 0.1639 0.1742 0.1875 0.0032  0.0092  0.0192  252  SER   A CA  
1655 C  C   . SER   A 252 ? 0.1743 0.1848 0.1989 0.0016  0.0085  0.0189  252  SER   A C   
1656 O  O   . SER   A 252 ? 0.1877 0.1961 0.2116 0.0006  0.0091  0.0191  252  SER   A O   
1657 C  CB  . SER   A 252 ? 0.1742 0.1839 0.1969 0.0034  0.0081  0.0184  252  SER   A CB  
1658 O  OG  . SER   A 252 ? 0.1807 0.1877 0.2021 0.0022  0.0075  0.0178  252  SER   A OG  
1659 N  N   . ASP   A 253 ? 0.1819 0.1948 0.2081 0.0015  0.0073  0.0183  253  ASP   A N   
1660 C  CA  A ASP   A 253 ? 0.1815 0.1955 0.2091 0.0001  0.0063  0.0181  253  ASP   A CA  
1661 C  CA  B ASP   A 253 ? 0.1903 0.2038 0.2177 0.0000  0.0063  0.0181  253  ASP   A CA  
1662 C  C   . ASP   A 253 ? 0.1840 0.1971 0.2110 -0.0005 0.0048  0.0174  253  ASP   A C   
1663 O  O   . ASP   A 253 ? 0.1901 0.2051 0.2188 -0.0013 0.0036  0.0173  253  ASP   A O   
1664 C  CB  A ASP   A 253 ? 0.1799 0.1979 0.2104 0.0007  0.0062  0.0183  253  ASP   A CB  
1665 C  CB  B ASP   A 253 ? 0.2187 0.2359 0.2490 0.0001  0.0064  0.0185  253  ASP   A CB  
1666 C  CG  A ASP   A 253 ? 0.1858 0.2055 0.2170 0.0019  0.0054  0.0178  253  ASP   A CG  
1667 C  CG  B ASP   A 253 ? 0.3201 0.3376 0.3507 0.0002  0.0078  0.0193  253  ASP   A CG  
1668 O  OD1 A ASP   A 253 ? 0.2300 0.2481 0.2595 0.0024  0.0051  0.0174  253  ASP   A OD1 
1669 O  OD1 B ASP   A 253 ? 0.3282 0.3431 0.3575 -0.0006 0.0086  0.0196  253  ASP   A OD1 
1670 O  OD2 A ASP   A 253 ? 0.2367 0.2592 0.2702 0.0021  0.0052  0.0178  253  ASP   A OD2 
1671 O  OD2 B ASP   A 253 ? 0.3695 0.3897 0.4017 0.0011  0.0084  0.0196  253  ASP   A OD2 
1672 N  N   . PHE   A 254 ? 0.1668 0.1774 0.1914 -0.0001 0.0047  0.0170  254  PHE   A N   
1673 C  CA  . PHE   A 254 ? 0.1584 0.1684 0.1823 -0.0005 0.0033  0.0164  254  PHE   A CA  
1674 C  C   . PHE   A 254 ? 0.1708 0.1797 0.1942 -0.0025 0.0022  0.0162  254  PHE   A C   
1675 O  O   . PHE   A 254 ? 0.1924 0.1990 0.2145 -0.0038 0.0028  0.0162  254  PHE   A O   
1676 C  CB  . PHE   A 254 ? 0.1727 0.1798 0.1939 0.0001  0.0036  0.0160  254  PHE   A CB  
1677 C  CG  . PHE   A 254 ? 0.1802 0.1884 0.2016 0.0019  0.0043  0.0161  254  PHE   A CG  
1678 C  CD1 . PHE   A 254 ? 0.1841 0.1956 0.2076 0.0029  0.0041  0.0162  254  PHE   A CD1 
1679 C  CD2 . PHE   A 254 ? 0.1878 0.1936 0.2070 0.0026  0.0051  0.0161  254  PHE   A CD2 
1680 C  CE1 . PHE   A 254 ? 0.2017 0.2140 0.2249 0.0043  0.0046  0.0163  254  PHE   A CE1 
1681 C  CE2 . PHE   A 254 ? 0.1815 0.1885 0.2009 0.0041  0.0055  0.0163  254  PHE   A CE2 
1682 C  CZ  . PHE   A 254 ? 0.1839 0.1942 0.2052 0.0048  0.0052  0.0164  254  PHE   A CZ  
1683 N  N   . GLU   A 255 ? 0.1474 0.1580 0.1719 -0.0028 0.0006  0.0160  255  GLU   A N   
1684 C  CA  . GLU   A 255 ? 0.1585 0.1680 0.1821 -0.0048 -0.0008 0.0158  255  GLU   A CA  
1685 C  C   . GLU   A 255 ? 0.1690 0.1751 0.1893 -0.0049 -0.0011 0.0152  255  GLU   A C   
1686 O  O   . GLU   A 255 ? 0.1593 0.1649 0.1789 -0.0034 -0.0005 0.0150  255  GLU   A O   
1687 C  CB  . GLU   A 255 ? 0.1590 0.1723 0.1856 -0.0049 -0.0025 0.0162  255  GLU   A CB  
1688 C  CG  . GLU   A 255 ? 0.1696 0.1862 0.1995 -0.0052 -0.0024 0.0168  255  GLU   A CG  
1689 C  CD  . GLU   A 255 ? 0.1974 0.2137 0.2273 -0.0076 -0.0032 0.0171  255  GLU   A CD  
1690 O  OE1 . GLU   A 255 ? 0.2021 0.2161 0.2296 -0.0092 -0.0042 0.0168  255  GLU   A OE1 
1691 O  OE2 . GLU   A 255 ? 0.2012 0.2197 0.2335 -0.0080 -0.0027 0.0177  255  GLU   A OE2 
1692 N  N   . SER   A 256 ? 0.1755 0.1796 0.1939 -0.0069 -0.0021 0.0149  256  SER   A N   
1693 C  CA  . SER   A 256 ? 0.1788 0.1796 0.1938 -0.0073 -0.0025 0.0143  256  SER   A CA  
1694 C  C   . SER   A 256 ? 0.1844 0.1852 0.1985 -0.0092 -0.0044 0.0142  256  SER   A C   
1695 O  O   . SER   A 256 ? 0.1929 0.1956 0.2086 -0.0107 -0.0055 0.0146  256  SER   A O   
1696 C  CB  . SER   A 256 ? 0.2002 0.1965 0.2119 -0.0076 -0.0007 0.0139  256  SER   A CB  
1697 O  OG  . SER   A 256 ? 0.2402 0.2349 0.2509 -0.0098 -0.0006 0.0138  256  SER   A OG  
1698 N  N   . VAL   A 257 ? 0.1742 0.1730 0.1859 -0.0092 -0.0050 0.0137  257  VAL   A N   
1699 C  CA  . VAL   A 257 ? 0.1830 0.1807 0.1927 -0.0111 -0.0068 0.0135  257  VAL   A CA  
1700 C  C   . VAL   A 257 ? 0.1854 0.1781 0.1905 -0.0116 -0.0058 0.0127  257  VAL   A C   
1701 O  O   . VAL   A 257 ? 0.1910 0.1821 0.1954 -0.0099 -0.0042 0.0124  257  VAL   A O   
1702 C  CB  . VAL   A 257 ? 0.1904 0.1914 0.2023 -0.0104 -0.0086 0.0141  257  VAL   A CB  
1703 C  CG1 . VAL   A 257 ? 0.1973 0.2031 0.2137 -0.0105 -0.0096 0.0150  257  VAL   A CG1 
1704 C  CG2 . VAL   A 257 ? 0.1929 0.1940 0.2052 -0.0079 -0.0078 0.0139  257  VAL   A CG2 
1705 N  N   . SER   A 258 ? 0.1853 0.1754 0.1872 -0.0141 -0.0068 0.0123  258  SER   A N   
1706 C  CA  A SER   A 258 ? 0.2026 0.1874 0.1998 -0.0147 -0.0057 0.0114  258  SER   A CA  
1707 C  CA  B SER   A 258 ? 0.2072 0.1921 0.2045 -0.0148 -0.0056 0.0114  258  SER   A CA  
1708 C  C   . SER   A 258 ? 0.2154 0.1987 0.2096 -0.0168 -0.0074 0.0111  258  SER   A C   
1709 O  O   . SER   A 258 ? 0.2230 0.2089 0.2184 -0.0183 -0.0096 0.0116  258  SER   A O   
1710 C  CB  A SER   A 258 ? 0.2144 0.1956 0.2095 -0.0159 -0.0038 0.0110  258  SER   A CB  
1711 C  CB  B SER   A 258 ? 0.2335 0.2147 0.2285 -0.0162 -0.0039 0.0110  258  SER   A CB  
1712 O  OG  A SER   A 258 ? 0.2071 0.1887 0.2019 -0.0186 -0.0050 0.0111  258  SER   A OG  
1713 O  OG  B SER   A 258 ? 0.2507 0.2334 0.2484 -0.0147 -0.0024 0.0114  258  SER   A OG  
1714 N  N   . LYS   A 259 ? 0.2009 0.1799 0.1912 -0.0168 -0.0064 0.0104  259  LYS   A N   
1715 C  CA  . LYS   A 259 ? 0.2143 0.1910 0.2008 -0.0188 -0.0077 0.0099  259  LYS   A CA  
1716 C  C   . LYS   A 259 ? 0.2386 0.2092 0.2203 -0.0190 -0.0054 0.0089  259  LYS   A C   
1717 O  O   . LYS   A 259 ? 0.2433 0.2128 0.2255 -0.0168 -0.0033 0.0088  259  LYS   A O   
1718 C  CB  . LYS   A 259 ? 0.2297 0.2091 0.2178 -0.0174 -0.0093 0.0104  259  LYS   A CB  
1719 C  CG  . LYS   A 259 ? 0.2703 0.2478 0.2546 -0.0193 -0.0109 0.0102  259  LYS   A CG  
1720 C  CD  . LYS   A 259 ? 0.3124 0.2935 0.2993 -0.0179 -0.0127 0.0110  259  LYS   A CD  
1721 C  CE  . LYS   A 259 ? 0.3742 0.3539 0.3577 -0.0198 -0.0145 0.0110  259  LYS   A CE  
1722 N  NZ  . LYS   A 259 ? 0.4093 0.3919 0.3950 -0.0180 -0.0157 0.0118  259  LYS   A NZ  
1723 N  N   . ILE   A 260 ? 0.2484 0.2151 0.2255 -0.0218 -0.0058 0.0082  260  ILE   A N   
1724 C  CA  . ILE   A 260 ? 0.2588 0.2193 0.2310 -0.0222 -0.0033 0.0071  260  ILE   A CA  
1725 C  C   . ILE   A 260 ? 0.2598 0.2181 0.2289 -0.0222 -0.0037 0.0067  260  ILE   A C   
1726 O  O   . ILE   A 260 ? 0.2774 0.2372 0.2457 -0.0238 -0.0061 0.0069  260  ILE   A O   
1727 C  CB  . ILE   A 260 ? 0.2937 0.2504 0.2620 -0.0257 -0.0031 0.0064  260  ILE   A CB  
1728 C  CG1 . ILE   A 260 ? 0.3422 0.3014 0.3136 -0.0263 -0.0034 0.0069  260  ILE   A CG1 
1729 C  CG2 . ILE   A 260 ? 0.3038 0.2535 0.2670 -0.0261 -0.0002 0.0053  260  ILE   A CG2 
1730 C  CD1 . ILE   A 260 ? 0.3855 0.3446 0.3592 -0.0240 -0.0010 0.0071  260  ILE   A CD1 
1731 N  N   . THR   A 261 ? 0.2459 0.2010 0.2134 -0.0204 -0.0012 0.0063  261  THR   A N   
1732 C  CA  . THR   A 261 ? 0.2477 0.2006 0.2121 -0.0203 -0.0013 0.0059  261  THR   A CA  
1733 C  C   . THR   A 261 ? 0.2746 0.2221 0.2329 -0.0235 -0.0012 0.0048  261  THR   A C   
1734 O  O   . THR   A 261 ? 0.2823 0.2272 0.2386 -0.0255 -0.0004 0.0043  261  THR   A O   
1735 C  CB  . THR   A 261 ? 0.2461 0.1969 0.2104 -0.0176 0.0015  0.0058  261  THR   A CB  
1736 O  OG1 . THR   A 261 ? 0.2497 0.1956 0.2114 -0.0181 0.0043  0.0052  261  THR   A OG1 
1737 C  CG2 . THR   A 261 ? 0.2591 0.2147 0.2289 -0.0146 0.0015  0.0067  261  THR   A CG2 
1738 N  N   . LYS   A 262 ? 0.2816 0.2271 0.2366 -0.0241 -0.0017 0.0045  262  LYS   A N   
1739 C  CA  . LYS   A 262 ? 0.2950 0.2350 0.2436 -0.0271 -0.0013 0.0034  262  LYS   A CA  
1740 C  C   . LYS   A 262 ? 0.3204 0.2544 0.2658 -0.0270 0.0024  0.0024  262  LYS   A C   
1741 O  O   . LYS   A 262 ? 0.3393 0.2685 0.2798 -0.0299 0.0032  0.0015  262  LYS   A O   
1742 C  CB  . LYS   A 262 ? 0.3412 0.2800 0.2871 -0.0270 -0.0019 0.0032  262  LYS   A CB  
1743 C  CG  . LYS   A 262 ? 0.4247 0.3685 0.3729 -0.0274 -0.0055 0.0042  262  LYS   A CG  
1744 C  CD  . LYS   A 262 ? 0.4857 0.4290 0.4326 -0.0261 -0.0056 0.0043  262  LYS   A CD  
1745 C  CE  . LYS   A 262 ? 0.5517 0.4996 0.5007 -0.0265 -0.0090 0.0053  262  LYS   A CE  
1746 N  NZ  . LYS   A 262 ? 0.5814 0.5355 0.5367 -0.0252 -0.0106 0.0064  262  LYS   A NZ  
1747 N  N   . SER   A 263 ? 0.2995 0.2336 0.2475 -0.0238 0.0048  0.0028  263  SER   A N   
1748 C  CA  . SER   A 263 ? 0.3040 0.2328 0.2497 -0.0233 0.0085  0.0022  263  SER   A CA  
1749 C  C   . SER   A 263 ? 0.3049 0.2338 0.2523 -0.0237 0.0093  0.0024  263  SER   A C   
1750 O  O   . SER   A 263 ? 0.3286 0.2532 0.2743 -0.0233 0.0124  0.0020  263  SER   A O   
1751 C  CB  . SER   A 263 ? 0.3194 0.2487 0.2675 -0.0198 0.0107  0.0028  263  SER   A CB  
1752 O  OG  . SER   A 263 ? 0.3476 0.2832 0.3018 -0.0174 0.0094  0.0039  263  SER   A OG  
1753 N  N   . GLY   A 264 ? 0.2814 0.2153 0.2323 -0.0244 0.0068  0.0030  264  GLY   A N   
1754 C  CA  . GLY   A 264 ? 0.2880 0.2222 0.2405 -0.0251 0.0074  0.0032  264  GLY   A CA  
1755 C  C   . GLY   A 264 ? 0.2790 0.2171 0.2371 -0.0219 0.0083  0.0043  264  GLY   A C   
1756 O  O   . GLY   A 264 ? 0.2943 0.2323 0.2536 -0.0221 0.0092  0.0045  264  GLY   A O   
1757 N  N   . VAL   A 265 ? 0.2666 0.2082 0.2279 -0.0191 0.0080  0.0050  265  VAL   A N   
1758 C  CA  . VAL   A 265 ? 0.2539 0.1993 0.2203 -0.0162 0.0088  0.0060  265  VAL   A CA  
1759 C  C   . VAL   A 265 ? 0.2341 0.1855 0.2048 -0.0164 0.0061  0.0067  265  VAL   A C   
1760 O  O   . VAL   A 265 ? 0.2374 0.1917 0.2088 -0.0170 0.0035  0.0068  265  VAL   A O   
1761 C  CB  . VAL   A 265 ? 0.2385 0.1854 0.2065 -0.0134 0.0094  0.0065  265  VAL   A CB  
1762 C  CG1 . VAL   A 265 ? 0.2335 0.1849 0.2067 -0.0106 0.0099  0.0076  265  VAL   A CG1 
1763 C  CG2 . VAL   A 265 ? 0.2630 0.2042 0.2271 -0.0130 0.0122  0.0059  265  VAL   A CG2 
1764 N  N   . LYS   A 266 ? 0.2256 0.1788 0.1992 -0.0158 0.0067  0.0073  266  LYS   A N   
1765 C  CA  . LYS   A 266 ? 0.2201 0.1789 0.1979 -0.0159 0.0045  0.0080  266  LYS   A CA  
1766 C  C   . LYS   A 266 ? 0.2162 0.1797 0.1983 -0.0128 0.0042  0.0088  266  LYS   A C   
1767 O  O   . LYS   A 266 ? 0.2233 0.1871 0.2071 -0.0108 0.0061  0.0093  266  LYS   A O   
1768 C  CB  . LYS   A 266 ? 0.2196 0.1785 0.1986 -0.0167 0.0053  0.0082  266  LYS   A CB  
1769 C  CG  . LYS   A 266 ? 0.2400 0.2045 0.2232 -0.0170 0.0030  0.0089  266  LYS   A CG  
1770 C  CD  . LYS   A 266 ? 0.2626 0.2269 0.2467 -0.0181 0.0038  0.0091  266  LYS   A CD  
1771 C  CE  . LYS   A 266 ? 0.2885 0.2583 0.2766 -0.0186 0.0016  0.0098  266  LYS   A CE  
1772 N  NZ  . LYS   A 266 ? 0.3375 0.3070 0.3263 -0.0199 0.0023  0.0100  266  LYS   A NZ  
1773 N  N   . VAL   A 267 ? 0.2042 0.1713 0.1880 -0.0126 0.0019  0.0090  267  VAL   A N   
1774 C  CA  . VAL   A 267 ? 0.1894 0.1607 0.1770 -0.0100 0.0015  0.0097  267  VAL   A CA  
1775 C  C   . VAL   A 267 ? 0.1896 0.1657 0.1813 -0.0099 0.0001  0.0103  267  VAL   A C   
1776 O  O   . VAL   A 267 ? 0.1992 0.1767 0.1911 -0.0118 -0.0018 0.0103  267  VAL   A O   
1777 C  CB  . VAL   A 267 ? 0.2089 0.1807 0.1956 -0.0097 0.0002  0.0095  267  VAL   A CB  
1778 C  CG1 . VAL   A 267 ? 0.2060 0.1818 0.1964 -0.0072 -0.0001 0.0101  267  VAL   A CG1 
1779 C  CG2 . VAL   A 267 ? 0.2233 0.1900 0.2058 -0.0099 0.0018  0.0088  267  VAL   A CG2 
1780 N  N   . SER   A 268 ? 0.1845 0.1635 0.1796 -0.0079 0.0009  0.0109  268  SER   A N   
1781 C  CA  . SER   A 268 ? 0.1752 0.1587 0.1742 -0.0077 -0.0002 0.0115  268  SER   A CA  
1782 C  C   . SER   A 268 ? 0.1850 0.1721 0.1871 -0.0053 -0.0002 0.0120  268  SER   A C   
1783 O  O   . SER   A 268 ? 0.1985 0.1847 0.2002 -0.0037 0.0012  0.0120  268  SER   A O   
1784 C  CB  . SER   A 268 ? 0.1868 0.1701 0.1867 -0.0080 0.0011  0.0118  268  SER   A CB  
1785 O  OG  . SER   A 268 ? 0.2128 0.1926 0.2098 -0.0104 0.0014  0.0114  268  SER   A OG  
1786 N  N   . VAL   A 269 ? 0.1683 0.1596 0.1735 -0.0051 -0.0018 0.0124  269  VAL   A N   
1787 C  CA  . VAL   A 269 ? 0.1605 0.1553 0.1689 -0.0031 -0.0017 0.0128  269  VAL   A CA  
1788 C  C   . VAL   A 269 ? 0.1612 0.1585 0.1723 -0.0029 -0.0012 0.0133  269  VAL   A C   
1789 O  O   . VAL   A 269 ? 0.1722 0.1704 0.1841 -0.0044 -0.0021 0.0135  269  VAL   A O   
1790 C  CB  . VAL   A 269 ? 0.1718 0.1690 0.1815 -0.0027 -0.0034 0.0129  269  VAL   A CB  
1791 C  CG1 . VAL   A 269 ? 0.1814 0.1820 0.1942 -0.0007 -0.0031 0.0132  269  VAL   A CG1 
1792 C  CG2 . VAL   A 269 ? 0.1761 0.1707 0.1830 -0.0027 -0.0037 0.0124  269  VAL   A CG2 
1793 N  N   . TYR   A 270 ? 0.1581 0.1565 0.1704 -0.0013 0.0001  0.0136  270  TYR   A N   
1794 C  CA  . TYR   A 270 ? 0.1622 0.1632 0.1771 -0.0010 0.0007  0.0142  270  TYR   A CA  
1795 C  C   . TYR   A 270 ? 0.1566 0.1611 0.1741 0.0006  0.0004  0.0144  270  TYR   A C   
1796 O  O   . TYR   A 270 ? 0.1606 0.1651 0.1776 0.0018  0.0007  0.0142  270  TYR   A O   
1797 C  CB  . TYR   A 270 ? 0.1645 0.1636 0.1785 -0.0004 0.0027  0.0145  270  TYR   A CB  
1798 C  CG  . TYR   A 270 ? 0.1578 0.1535 0.1696 -0.0020 0.0033  0.0144  270  TYR   A CG  
1799 C  CD1 . TYR   A 270 ? 0.1648 0.1565 0.1734 -0.0027 0.0037  0.0138  270  TYR   A CD1 
1800 C  CD2 . TYR   A 270 ? 0.1578 0.1541 0.1707 -0.0029 0.0037  0.0147  270  TYR   A CD2 
1801 C  CE1 . TYR   A 270 ? 0.1685 0.1565 0.1747 -0.0042 0.0046  0.0136  270  TYR   A CE1 
1802 C  CE2 . TYR   A 270 ? 0.1769 0.1697 0.1876 -0.0044 0.0045  0.0146  270  TYR   A CE2 
1803 C  CZ  . TYR   A 270 ? 0.1886 0.1772 0.1959 -0.0051 0.0049  0.0140  270  TYR   A CZ  
1804 O  OH  . TYR   A 270 ? 0.2170 0.2017 0.2218 -0.0069 0.0058  0.0137  270  TYR   A OH  
1805 N  N   . ALA   A 271 ? 0.1540 0.1615 0.1742 0.0005  0.0000  0.0147  271  ALA   A N   
1806 C  CA  . ALA   A 271 ? 0.1556 0.1663 0.1782 0.0019  0.0000  0.0148  271  ALA   A CA  
1807 C  C   . ALA   A 271 ? 0.1473 0.1607 0.1725 0.0017  0.0004  0.0153  271  ALA   A C   
1808 O  O   . ALA   A 271 ? 0.1472 0.1601 0.1725 0.0004  0.0002  0.0155  271  ALA   A O   
1809 C  CB  . ALA   A 271 ? 0.1719 0.1836 0.1952 0.0021  -0.0014 0.0146  271  ALA   A CB  
1810 N  N   . VAL   A 272 ? 0.1501 0.1660 0.1772 0.0029  0.0008  0.0154  272  VAL   A N   
1811 C  CA  . VAL   A 272 ? 0.1603 0.1787 0.1898 0.0028  0.0012  0.0159  272  VAL   A CA  
1812 C  C   . VAL   A 272 ? 0.1534 0.1732 0.1848 0.0018  -0.0001 0.0161  272  VAL   A C   
1813 O  O   . VAL   A 272 ? 0.1485 0.1682 0.1799 0.0017  -0.0013 0.0160  272  VAL   A O   
1814 C  CB  . VAL   A 272 ? 0.1652 0.1860 0.1962 0.0042  0.0020  0.0159  272  VAL   A CB  
1815 C  CG1 . VAL   A 272 ? 0.1839 0.2037 0.2131 0.0050  0.0032  0.0158  272  VAL   A CG1 
1816 C  CG2 . VAL   A 272 ? 0.1707 0.1924 0.2025 0.0049  0.0012  0.0155  272  VAL   A CG2 
1817 N  N   . PRO   A 273 ? 0.1540 0.1752 0.1871 0.0009  0.0001  0.0166  273  PRO   A N   
1818 C  CA  . PRO   A 273 ? 0.1523 0.1752 0.1875 -0.0002 -0.0013 0.0170  273  PRO   A CA  
1819 C  C   . PRO   A 273 ? 0.1579 0.1832 0.1953 0.0007  -0.0021 0.0172  273  PRO   A C   
1820 O  O   . PRO   A 273 ? 0.1632 0.1886 0.2008 -0.0001 -0.0036 0.0174  273  PRO   A O   
1821 C  CB  . PRO   A 273 ? 0.1664 0.1911 0.2036 -0.0008 -0.0005 0.0176  273  PRO   A CB  
1822 C  CG  . PRO   A 273 ? 0.1692 0.1915 0.2041 -0.0008 0.0009  0.0174  273  PRO   A CG  
1823 C  CD  . PRO   A 273 ? 0.1597 0.1811 0.1930 0.0009  0.0015  0.0169  273  PRO   A CD  
1824 N  N   . ASP   A 274 ? 0.1595 0.1863 0.1981 0.0023  -0.0012 0.0171  274  ASP   A N   
1825 C  CA  . ASP   A 274 ? 0.1612 0.1900 0.2021 0.0033  -0.0017 0.0173  274  ASP   A CA  
1826 C  C   . ASP   A 274 ? 0.1527 0.1797 0.1917 0.0037  -0.0026 0.0169  274  ASP   A C   
1827 O  O   . ASP   A 274 ? 0.1613 0.1897 0.2020 0.0044  -0.0032 0.0171  274  ASP   A O   
1828 C  CB  . ASP   A 274 ? 0.2057 0.2359 0.2477 0.0049  -0.0001 0.0171  274  ASP   A CB  
1829 C  CG  . ASP   A 274 ? 0.2865 0.3191 0.3310 0.0048  0.0009  0.0176  274  ASP   A CG  
1830 O  OD1 . ASP   A 274 ? 0.2613 0.2952 0.3075 0.0037  0.0002  0.0182  274  ASP   A OD1 
1831 O  OD2 . ASP   A 274 ? 0.3071 0.3402 0.3516 0.0058  0.0023  0.0173  274  ASP   A OD2 
1832 N  N   . LYS   A 275 ? 0.1529 0.1770 0.1886 0.0033  -0.0027 0.0163  275  LYS   A N   
1833 C  CA  . LYS   A 275 ? 0.1478 0.1700 0.1815 0.0036  -0.0035 0.0159  275  LYS   A CA  
1834 C  C   . LYS   A 275 ? 0.1390 0.1588 0.1703 0.0021  -0.0046 0.0158  275  LYS   A C   
1835 O  O   . LYS   A 275 ? 0.1420 0.1601 0.1715 0.0023  -0.0052 0.0155  275  LYS   A O   
1836 C  CB  . LYS   A 275 ? 0.1524 0.1731 0.1842 0.0048  -0.0023 0.0152  275  LYS   A CB  
1837 C  CG  . LYS   A 275 ? 0.1488 0.1716 0.1824 0.0061  -0.0012 0.0151  275  LYS   A CG  
1838 C  CD  . LYS   A 275 ? 0.1570 0.1785 0.1886 0.0071  -0.0004 0.0145  275  LYS   A CD  
1839 C  CE  . LYS   A 275 ? 0.1763 0.1995 0.2093 0.0081  0.0007  0.0143  275  LYS   A CE  
1840 N  NZ  . LYS   A 275 ? 0.2143 0.2364 0.2452 0.0088  0.0013  0.0136  275  LYS   A NZ  
1841 N  N   . ILE   A 276 ? 0.1385 0.1579 0.1696 0.0006  -0.0048 0.0161  276  ILE   A N   
1842 C  CA  . ILE   A 276 ? 0.1469 0.1636 0.1752 -0.0011 -0.0058 0.0159  276  ILE   A CA  
1843 C  C   . ILE   A 276 ? 0.1486 0.1662 0.1775 -0.0016 -0.0077 0.0163  276  ILE   A C   
1844 O  O   . ILE   A 276 ? 0.1583 0.1734 0.1844 -0.0026 -0.0085 0.0160  276  ILE   A O   
1845 C  CB  . ILE   A 276 ? 0.1506 0.1664 0.1783 -0.0028 -0.0055 0.0160  276  ILE   A CB  
1846 C  CG1 . ILE   A 276 ? 0.1665 0.1785 0.1905 -0.0043 -0.0058 0.0155  276  ILE   A CG1 
1847 C  CG2 . ILE   A 276 ? 0.1659 0.1849 0.1967 -0.0038 -0.0065 0.0168  276  ILE   A CG2 
1848 C  CD1 . ILE   A 276 ? 0.1747 0.1833 0.1956 -0.0033 -0.0045 0.0148  276  ILE   A CD1 
1849 N  N   . ASN   A 277 ? 0.1400 0.1611 0.1725 -0.0010 -0.0083 0.0170  277  ASN   A N   
1850 C  CA  . ASN   A 277 ? 0.1448 0.1670 0.1781 -0.0013 -0.0101 0.0177  277  ASN   A CA  
1851 C  C   . ASN   A 277 ? 0.1587 0.1792 0.1903 -0.0001 -0.0101 0.0172  277  ASN   A C   
1852 O  O   . ASN   A 277 ? 0.1832 0.2042 0.2149 -0.0003 -0.0116 0.0177  277  ASN   A O   
1853 C  CB  . ASN   A 277 ? 0.1629 0.1893 0.2007 -0.0008 -0.0106 0.0188  277  ASN   A CB  
1854 C  CG  . ASN   A 277 ? 0.1748 0.2027 0.2149 0.0014  -0.0091 0.0187  277  ASN   A CG  
1855 O  OD1 . ASN   A 277 ? 0.1778 0.2039 0.2161 0.0026  -0.0080 0.0179  277  ASN   A OD1 
1856 N  ND2 . ASN   A 277 ? 0.1704 0.2019 0.2145 0.0020  -0.0090 0.0196  277  ASN   A ND2 
1857 N  N   . GLN   A 278 ? 0.1380 0.1567 0.1679 0.0011  -0.0087 0.0163  278  GLN   A N   
1858 C  CA  . GLN   A 278 ? 0.1426 0.1594 0.1705 0.0020  -0.0086 0.0158  278  GLN   A CA  
1859 C  C   . GLN   A 278 ? 0.1453 0.1584 0.1692 0.0012  -0.0085 0.0151  278  GLN   A C   
1860 O  O   . GLN   A 278 ? 0.1657 0.1770 0.1878 0.0020  -0.0082 0.0146  278  GLN   A O   
1861 C  CB  . GLN   A 278 ? 0.1591 0.1765 0.1879 0.0039  -0.0071 0.0154  278  GLN   A CB  
1862 C  CG  . GLN   A 278 ? 0.1678 0.1884 0.2004 0.0049  -0.0069 0.0160  278  GLN   A CG  
1863 C  CD  . GLN   A 278 ? 0.1943 0.2150 0.2271 0.0065  -0.0053 0.0154  278  GLN   A CD  
1864 O  OE1 . GLN   A 278 ? 0.2258 0.2447 0.2565 0.0071  -0.0051 0.0148  278  GLN   A OE1 
1865 N  NE2 . GLN   A 278 ? 0.1717 0.1944 0.2066 0.0071  -0.0042 0.0155  278  GLN   A NE2 
1866 N  N   . ALA   A 279 ? 0.1448 0.1566 0.1673 -0.0004 -0.0086 0.0151  279  ALA   A N   
1867 C  CA  . ALA   A 279 ? 0.1594 0.1674 0.1780 -0.0011 -0.0080 0.0143  279  ALA   A CA  
1868 C  C   . ALA   A 279 ? 0.1734 0.1790 0.1892 -0.0025 -0.0093 0.0142  279  ALA   A C   
1869 O  O   . ALA   A 279 ? 0.1756 0.1778 0.1880 -0.0028 -0.0086 0.0136  279  ALA   A O   
1870 C  CB  . ALA   A 279 ? 0.1740 0.1809 0.1919 -0.0023 -0.0072 0.0143  279  ALA   A CB  
1871 N  N   . ASP   A 280 ? 0.1766 0.1841 0.1937 -0.0033 -0.0111 0.0149  280  ASP   A N   
1872 C  CA  . ASP   A 280 ? 0.1782 0.1834 0.1922 -0.0050 -0.0125 0.0149  280  ASP   A CA  
1873 C  C   . ASP   A 280 ? 0.1799 0.1827 0.1913 -0.0043 -0.0124 0.0144  280  ASP   A C   
1874 O  O   . ASP   A 280 ? 0.1893 0.1887 0.1969 -0.0056 -0.0125 0.0139  280  ASP   A O   
1875 C  CB  . ASP   A 280 ? 0.1955 0.2036 0.2115 -0.0061 -0.0147 0.0159  280  ASP   A CB  
1876 C  CG  . ASP   A 280 ? 0.2276 0.2334 0.2401 -0.0087 -0.0160 0.0159  280  ASP   A CG  
1877 O  OD1 . ASP   A 280 ? 0.2483 0.2517 0.2584 -0.0103 -0.0153 0.0152  280  ASP   A OD1 
1878 O  OD2 . ASP   A 280 ? 0.2855 0.2918 0.2975 -0.0091 -0.0177 0.0164  280  ASP   A OD2 
1879 N  N   . TYR   A 281 ? 0.1735 0.1776 0.1865 -0.0024 -0.0121 0.0145  281  TYR   A N   
1880 C  CA  . TYR   A 281 ? 0.1762 0.1780 0.1868 -0.0018 -0.0120 0.0141  281  TYR   A CA  
1881 C  C   . TYR   A 281 ? 0.1809 0.1792 0.1883 -0.0018 -0.0104 0.0131  281  TYR   A C   
1882 O  O   . TYR   A 281 ? 0.1868 0.1821 0.1908 -0.0026 -0.0105 0.0127  281  TYR   A O   
1883 C  CB  . TYR   A 281 ? 0.1773 0.1811 0.1902 0.0003  -0.0118 0.0143  281  TYR   A CB  
1884 C  CG  . TYR   A 281 ? 0.1944 0.1958 0.2049 0.0008  -0.0117 0.0139  281  TYR   A CG  
1885 C  CD1 . TYR   A 281 ? 0.2292 0.2301 0.2385 0.0001  -0.0133 0.0144  281  TYR   A CD1 
1886 C  CD2 . TYR   A 281 ? 0.1908 0.1905 0.1999 0.0017  -0.0101 0.0132  281  TYR   A CD2 
1887 C  CE1 . TYR   A 281 ? 0.2364 0.2348 0.2430 0.0004  -0.0132 0.0141  281  TYR   A CE1 
1888 C  CE2 . TYR   A 281 ? 0.2098 0.2073 0.2165 0.0021  -0.0100 0.0128  281  TYR   A CE2 
1889 C  CZ  . TYR   A 281 ? 0.2335 0.2302 0.2389 0.0014  -0.0115 0.0132  281  TYR   A CZ  
1890 O  OH  . TYR   A 281 ? 0.2460 0.2405 0.2490 0.0016  -0.0114 0.0129  281  TYR   A OH  
1891 N  N   . ALA   A 282 ? 0.1626 0.1615 0.1712 -0.0008 -0.0088 0.0129  282  ALA   A N   
1892 C  CA  . ALA   A 282 ? 0.1656 0.1616 0.1717 -0.0006 -0.0071 0.0123  282  ALA   A CA  
1893 C  C   . ALA   A 282 ? 0.1680 0.1611 0.1713 -0.0024 -0.0069 0.0120  282  ALA   A C   
1894 O  O   . ALA   A 282 ? 0.1773 0.1670 0.1776 -0.0026 -0.0059 0.0115  282  ALA   A O   
1895 C  CB  . ALA   A 282 ? 0.1824 0.1800 0.1907 0.0007  -0.0056 0.0123  282  ALA   A CB  
1896 N  N   . LEU   A 283 ? 0.1623 0.1564 0.1665 -0.0038 -0.0077 0.0123  283  LEU   A N   
1897 C  CA  . LEU   A 283 ? 0.1727 0.1636 0.1738 -0.0058 -0.0075 0.0119  283  LEU   A CA  
1898 C  C   . LEU   A 283 ? 0.1891 0.1772 0.1866 -0.0072 -0.0084 0.0116  283  LEU   A C   
1899 O  O   . LEU   A 283 ? 0.1955 0.1795 0.1893 -0.0079 -0.0073 0.0109  283  LEU   A O   
1900 C  CB  . LEU   A 283 ? 0.1779 0.1710 0.1809 -0.0073 -0.0085 0.0124  283  LEU   A CB  
1901 C  CG  . LEU   A 283 ? 0.1845 0.1743 0.1843 -0.0097 -0.0085 0.0120  283  LEU   A CG  
1902 C  CD1 . LEU   A 283 ? 0.2109 0.1972 0.2086 -0.0094 -0.0060 0.0114  283  LEU   A CD1 
1903 C  CD2 . LEU   A 283 ? 0.2101 0.2026 0.2121 -0.0113 -0.0097 0.0126  283  LEU   A CD2 
1904 N  N   . ASP   A 284 ? 0.1869 0.1771 0.1854 -0.0074 -0.0104 0.0121  284  ASP   A N   
1905 C  CA  A ASP   A 284 ? 0.1981 0.1858 0.1931 -0.0087 -0.0115 0.0119  284  ASP   A CA  
1906 C  CA  B ASP   A 284 ? 0.2069 0.1947 0.2020 -0.0087 -0.0115 0.0119  284  ASP   A CA  
1907 C  C   . ASP   A 284 ? 0.1957 0.1807 0.1884 -0.0075 -0.0101 0.0113  284  ASP   A C   
1908 O  O   . ASP   A 284 ? 0.2122 0.1932 0.2007 -0.0087 -0.0097 0.0107  284  ASP   A O   
1909 C  CB  A ASP   A 284 ? 0.2050 0.1958 0.2019 -0.0090 -0.0138 0.0128  284  ASP   A CB  
1910 C  CB  B ASP   A 284 ? 0.2405 0.2318 0.2381 -0.0087 -0.0138 0.0129  284  ASP   A CB  
1911 C  CG  A ASP   A 284 ? 0.2256 0.2183 0.2235 -0.0111 -0.0155 0.0135  284  ASP   A CG  
1912 C  CG  B ASP   A 284 ? 0.3208 0.3104 0.3154 -0.0098 -0.0152 0.0130  284  ASP   A CG  
1913 O  OD1 A ASP   A 284 ? 0.2120 0.2029 0.2082 -0.0127 -0.0150 0.0130  284  ASP   A OD1 
1914 O  OD1 B ASP   A 284 ? 0.3514 0.3396 0.3434 -0.0122 -0.0163 0.0130  284  ASP   A OD1 
1915 O  OD2 A ASP   A 284 ? 0.2830 0.2789 0.2832 -0.0111 -0.0174 0.0145  284  ASP   A OD2 
1916 O  OD2 B ASP   A 284 ? 0.3532 0.3428 0.3479 -0.0084 -0.0151 0.0131  284  ASP   A OD2 
1917 N  N   . ALA   A 285 ? 0.1820 0.1688 0.1772 -0.0052 -0.0094 0.0115  285  ALA   A N   
1918 C  CA  . ALA   A 285 ? 0.1826 0.1672 0.1760 -0.0040 -0.0082 0.0110  285  ALA   A CA  
1919 C  C   . ALA   A 285 ? 0.1929 0.1742 0.1839 -0.0042 -0.0060 0.0104  285  ALA   A C   
1920 O  O   . ALA   A 285 ? 0.1956 0.1735 0.1834 -0.0043 -0.0052 0.0099  285  ALA   A O   
1921 C  CB  . ALA   A 285 ? 0.1933 0.1809 0.1900 -0.0018 -0.0078 0.0113  285  ALA   A CB  
1922 N  N   . ALA   A 286 ? 0.1834 0.1654 0.1759 -0.0040 -0.0050 0.0105  286  ALA   A N   
1923 C  CA  . ALA   A 286 ? 0.1784 0.1573 0.1690 -0.0039 -0.0028 0.0101  286  ALA   A CA  
1924 C  C   . ALA   A 286 ? 0.1907 0.1652 0.1770 -0.0060 -0.0026 0.0095  286  ALA   A C   
1925 O  O   . ALA   A 286 ? 0.1986 0.1695 0.1822 -0.0058 -0.0008 0.0091  286  ALA   A O   
1926 C  CB  . ALA   A 286 ? 0.1844 0.1649 0.1774 -0.0034 -0.0019 0.0104  286  ALA   A CB  
1927 N  N   . VAL   A 287 ? 0.1884 0.1631 0.1740 -0.0080 -0.0042 0.0095  287  VAL   A N   
1928 C  CA  . VAL   A 287 ? 0.2044 0.1748 0.1854 -0.0103 -0.0041 0.0088  287  VAL   A CA  
1929 C  C   . VAL   A 287 ? 0.2112 0.1790 0.1889 -0.0105 -0.0043 0.0085  287  VAL   A C   
1930 O  O   . VAL   A 287 ? 0.2239 0.1872 0.1978 -0.0111 -0.0026 0.0078  287  VAL   A O   
1931 C  CB  . VAL   A 287 ? 0.2107 0.1825 0.1918 -0.0127 -0.0062 0.0091  287  VAL   A CB  
1932 C  CG1 . VAL   A 287 ? 0.2407 0.2083 0.2166 -0.0154 -0.0067 0.0084  287  VAL   A CG1 
1933 C  CG2 . VAL   A 287 ? 0.2186 0.1916 0.2019 -0.0129 -0.0056 0.0092  287  VAL   A CG2 
1934 N  N   . THR   A 288 ? 0.2014 0.1720 0.1806 -0.0099 -0.0061 0.0089  288  THR   A N   
1935 C  CA  . THR   A 288 ? 0.2030 0.1714 0.1793 -0.0100 -0.0063 0.0087  288  THR   A CA  
1936 C  C   . THR   A 288 ? 0.2061 0.1725 0.1817 -0.0083 -0.0040 0.0083  288  THR   A C   
1937 O  O   . THR   A 288 ? 0.2144 0.1768 0.1860 -0.0089 -0.0030 0.0078  288  THR   A O   
1938 C  CB  . THR   A 288 ? 0.2240 0.1963 0.2029 -0.0094 -0.0086 0.0095  288  THR   A CB  
1939 O  OG1 . THR   A 288 ? 0.2434 0.2178 0.2232 -0.0112 -0.0108 0.0100  288  THR   A OG1 
1940 C  CG2 . THR   A 288 ? 0.2475 0.2178 0.2236 -0.0095 -0.0090 0.0093  288  THR   A CG2 
1941 N  N   . LEU   A 289 ? 0.1981 0.1670 0.1772 -0.0061 -0.0030 0.0087  289  LEU   A N   
1942 C  CA  . LEU   A 289 ? 0.2075 0.1751 0.1864 -0.0044 -0.0009 0.0086  289  LEU   A CA  
1943 C  C   . LEU   A 289 ? 0.2095 0.1732 0.1860 -0.0047 0.0016  0.0082  289  LEU   A C   
1944 O  O   . LEU   A 289 ? 0.2068 0.1674 0.1809 -0.0043 0.0032  0.0079  289  LEU   A O   
1945 C  CB  . LEU   A 289 ? 0.2015 0.1733 0.1848 -0.0022 -0.0008 0.0092  289  LEU   A CB  
1946 C  CG  . LEU   A 289 ? 0.1995 0.1739 0.1844 -0.0016 -0.0025 0.0095  289  LEU   A CG  
1947 C  CD1 . LEU   A 289 ? 0.2092 0.1879 0.1985 -0.0001 -0.0027 0.0100  289  LEU   A CD1 
1948 C  CD2 . LEU   A 289 ? 0.2227 0.1951 0.2057 -0.0009 -0.0015 0.0093  289  LEU   A CD2 
1949 N  N   . LEU   A 290 ? 0.2019 0.1654 0.1789 -0.0055 0.0019  0.0082  290  LEU   A N   
1950 C  CA  . LEU   A 290 ? 0.2059 0.1653 0.1804 -0.0057 0.0044  0.0079  290  LEU   A CA  
1951 C  C   . LEU   A 290 ? 0.2344 0.1888 0.2036 -0.0077 0.0048  0.0070  290  LEU   A C   
1952 O  O   . LEU   A 290 ? 0.2423 0.1929 0.2091 -0.0073 0.0071  0.0067  290  LEU   A O   
1953 C  CB  . LEU   A 290 ? 0.2163 0.1761 0.1920 -0.0064 0.0047  0.0080  290  LEU   A CB  
1954 C  CG  . LEU   A 290 ? 0.2488 0.2052 0.2233 -0.0058 0.0077  0.0080  290  LEU   A CG  
1955 C  CD1 . LEU   A 290 ? 0.2482 0.2071 0.2262 -0.0031 0.0091  0.0088  290  LEU   A CD1 
1956 C  CD2 . LEU   A 290 ? 0.2769 0.2327 0.2516 -0.0071 0.0079  0.0079  290  LEU   A CD2 
1957 N  N   . GLU   A 291 ? 0.2308 0.1852 0.1983 -0.0098 0.0025  0.0067  291  GLU   A N   
1958 C  CA  . GLU   A 291 ? 0.2350 0.1848 0.1971 -0.0119 0.0026  0.0059  291  GLU   A CA  
1959 C  C   . GLU   A 291 ? 0.2453 0.1937 0.2059 -0.0109 0.0032  0.0058  291  GLU   A C   
1960 O  O   . GLU   A 291 ? 0.2674 0.2111 0.2239 -0.0115 0.0051  0.0051  291  GLU   A O   
1961 C  CB  . GLU   A 291 ? 0.2419 0.1930 0.2030 -0.0143 -0.0004 0.0059  291  GLU   A CB  
1962 C  CG  . GLU   A 291 ? 0.2635 0.2153 0.2254 -0.0159 -0.0010 0.0059  291  GLU   A CG  
1963 C  CD  . GLU   A 291 ? 0.2866 0.2405 0.2483 -0.0182 -0.0040 0.0061  291  GLU   A CD  
1964 O  OE1 . GLU   A 291 ? 0.3750 0.3304 0.3365 -0.0184 -0.0060 0.0065  291  GLU   A OE1 
1965 O  OE2 . GLU   A 291 ? 0.2629 0.2168 0.2246 -0.0200 -0.0045 0.0061  291  GLU   A OE2 
1966 N  N   . PHE   A 292 ? 0.2271 0.1795 0.1910 -0.0092 0.0020  0.0064  292  PHE   A N   
1967 C  CA  . PHE   A 292 ? 0.2284 0.1799 0.1913 -0.0081 0.0026  0.0064  292  PHE   A CA  
1968 C  C   . PHE   A 292 ? 0.2340 0.1830 0.1964 -0.0066 0.0058  0.0064  292  PHE   A C   
1969 O  O   . PHE   A 292 ? 0.2458 0.1909 0.2046 -0.0069 0.0072  0.0059  292  PHE   A O   
1970 C  CB  . PHE   A 292 ? 0.2245 0.1809 0.1914 -0.0065 0.0010  0.0072  292  PHE   A CB  
1971 C  CG  . PHE   A 292 ? 0.2230 0.1786 0.1893 -0.0052 0.0020  0.0072  292  PHE   A CG  
1972 C  CD1 . PHE   A 292 ? 0.2333 0.1895 0.2017 -0.0031 0.0040  0.0075  292  PHE   A CD1 
1973 C  CD2 . PHE   A 292 ? 0.2496 0.2034 0.2129 -0.0061 0.0010  0.0070  292  PHE   A CD2 
1974 C  CE1 . PHE   A 292 ? 0.2476 0.2029 0.2152 -0.0021 0.0051  0.0076  292  PHE   A CE1 
1975 C  CE2 . PHE   A 292 ? 0.2551 0.2079 0.2176 -0.0050 0.0021  0.0070  292  PHE   A CE2 
1976 C  CZ  . PHE   A 292 ? 0.2556 0.2092 0.2204 -0.0030 0.0042  0.0073  292  PHE   A CZ  
1977 N  N   . TYR   A 293 ? 0.2204 0.1715 0.1863 -0.0049 0.0070  0.0069  293  TYR   A N   
1978 C  CA  . TYR   A 293 ? 0.2137 0.1631 0.1798 -0.0033 0.0099  0.0072  293  TYR   A CA  
1979 C  C   . TYR   A 293 ? 0.2226 0.1664 0.1846 -0.0044 0.0122  0.0065  293  TYR   A C   
1980 O  O   . TYR   A 293 ? 0.2425 0.1832 0.2026 -0.0037 0.0145  0.0065  293  TYR   A O   
1981 C  CB  . TYR   A 293 ? 0.2036 0.1569 0.1744 -0.0015 0.0104  0.0080  293  TYR   A CB  
1982 C  CG  . TYR   A 293 ? 0.1928 0.1511 0.1675 0.0000  0.0089  0.0087  293  TYR   A CG  
1983 C  CD1 . TYR   A 293 ? 0.1958 0.1544 0.1704 0.0010  0.0092  0.0088  293  TYR   A CD1 
1984 C  CD2 . TYR   A 293 ? 0.1897 0.1522 0.1679 0.0004  0.0073  0.0091  293  TYR   A CD2 
1985 C  CE1 . TYR   A 293 ? 0.1856 0.1483 0.1635 0.0022  0.0081  0.0093  293  TYR   A CE1 
1986 C  CE2 . TYR   A 293 ? 0.1893 0.1560 0.1709 0.0017  0.0063  0.0096  293  TYR   A CE2 
1987 C  CZ  . TYR   A 293 ? 0.1865 0.1532 0.1678 0.0026  0.0066  0.0097  293  TYR   A CZ  
1988 O  OH  . TYR   A 293 ? 0.1864 0.1569 0.1706 0.0037  0.0057  0.0101  293  TYR   A OH  
1989 N  N   . GLU   A 294 ? 0.2349 0.1772 0.1954 -0.0063 0.0117  0.0060  294  GLU   A N   
1990 C  CA  . GLU   A 294 ? 0.2457 0.1820 0.2017 -0.0076 0.0141  0.0053  294  GLU   A CA  
1991 C  C   . GLU   A 294 ? 0.2716 0.2035 0.2226 -0.0089 0.0145  0.0044  294  GLU   A C   
1992 O  O   . GLU   A 294 ? 0.2917 0.2190 0.2398 -0.0086 0.0175  0.0041  294  GLU   A O   
1993 C  CB  . GLU   A 294 ? 0.2588 0.1941 0.2136 -0.0098 0.0132  0.0048  294  GLU   A CB  
1994 C  CG  . GLU   A 294 ? 0.2803 0.2190 0.2395 -0.0086 0.0133  0.0056  294  GLU   A CG  
1995 C  CD  . GLU   A 294 ? 0.3086 0.2454 0.2661 -0.0109 0.0129  0.0050  294  GLU   A CD  
1996 O  OE1 . GLU   A 294 ? 0.3504 0.2890 0.3076 -0.0129 0.0102  0.0048  294  GLU   A OE1 
1997 O  OE2 . GLU   A 294 ? 0.2977 0.2312 0.2541 -0.0109 0.0154  0.0049  294  GLU   A OE2 
1998 N  N   A ASP   A 295 ? 0.2690 0.2025 0.2190 -0.0102 0.0118  0.0042  295  ASP   A N   
1999 N  N   B ASP   A 295 ? 0.2767 0.2103 0.2268 -0.0102 0.0117  0.0042  295  ASP   A N   
2000 C  CA  A ASP   A 295 ? 0.2757 0.2053 0.2209 -0.0116 0.0120  0.0035  295  ASP   A CA  
2001 C  CA  B ASP   A 295 ? 0.2918 0.2218 0.2371 -0.0116 0.0116  0.0035  295  ASP   A CA  
2002 C  C   A ASP   A 295 ? 0.2836 0.2135 0.2298 -0.0093 0.0136  0.0039  295  ASP   A C   
2003 C  C   B ASP   A 295 ? 0.2968 0.2269 0.2427 -0.0096 0.0130  0.0039  295  ASP   A C   
2004 O  O   A ASP   A 295 ? 0.2948 0.2201 0.2374 -0.0094 0.0160  0.0035  295  ASP   A O   
2005 O  O   B ASP   A 295 ? 0.3123 0.2380 0.2538 -0.0104 0.0144  0.0033  295  ASP   A O   
2006 C  CB  A ASP   A 295 ? 0.2915 0.2231 0.2356 -0.0135 0.0084  0.0034  295  ASP   A CB  
2007 C  CB  B ASP   A 295 ? 0.3178 0.2504 0.2627 -0.0134 0.0080  0.0035  295  ASP   A CB  
2008 C  CG  A ASP   A 295 ? 0.3720 0.3002 0.3113 -0.0148 0.0084  0.0029  295  ASP   A CG  
2009 C  CG  B ASP   A 295 ? 0.4204 0.3525 0.3637 -0.0161 0.0063  0.0032  295  ASP   A CG  
2010 O  OD1 A ASP   A 295 ? 0.4016 0.3246 0.3355 -0.0170 0.0094  0.0019  295  ASP   A OD1 
2011 O  OD1 B ASP   A 295 ? 0.4574 0.3857 0.3983 -0.0171 0.0082  0.0025  295  ASP   A OD1 
2012 O  OD2 A ASP   A 295 ? 0.4005 0.3310 0.3413 -0.0135 0.0074  0.0034  295  ASP   A OD2 
2013 O  OD2 B ASP   A 295 ? 0.4627 0.3984 0.4074 -0.0170 0.0032  0.0036  295  ASP   A OD2 
2014 N  N   . TYR   A 296 ? 0.2817 0.2168 0.2326 -0.0073 0.0123  0.0048  296  TYR   A N   
2015 C  CA  . TYR   A 296 ? 0.2774 0.2133 0.2295 -0.0055 0.0134  0.0053  296  TYR   A CA  
2016 C  C   . TYR   A 296 ? 0.3040 0.2372 0.2560 -0.0039 0.0170  0.0056  296  TYR   A C   
2017 O  O   . TYR   A 296 ? 0.3219 0.2524 0.2717 -0.0035 0.0188  0.0054  296  TYR   A O   
2018 C  CB  . TYR   A 296 ? 0.2698 0.2117 0.2271 -0.0038 0.0115  0.0062  296  TYR   A CB  
2019 C  CG  . TYR   A 296 ? 0.2734 0.2164 0.2315 -0.0024 0.0119  0.0066  296  TYR   A CG  
2020 C  CD1 . TYR   A 296 ? 0.2783 0.2207 0.2342 -0.0034 0.0103  0.0063  296  TYR   A CD1 
2021 C  CD2 . TYR   A 296 ? 0.2834 0.2279 0.2444 -0.0003 0.0138  0.0073  296  TYR   A CD2 
2022 C  CE1 . TYR   A 296 ? 0.2842 0.2275 0.2408 -0.0022 0.0106  0.0067  296  TYR   A CE1 
2023 C  CE2 . TYR   A 296 ? 0.2939 0.2393 0.2555 0.0008  0.0142  0.0077  296  TYR   A CE2 
2024 C  CZ  . TYR   A 296 ? 0.2900 0.2347 0.2493 -0.0002 0.0126  0.0073  296  TYR   A CZ  
2025 O  OH  . TYR   A 296 ? 0.3141 0.2597 0.2741 0.0008  0.0130  0.0077  296  TYR   A OH  
2026 N  N   . PHE   A 297 ? 0.2805 0.2148 0.2352 -0.0029 0.0182  0.0060  297  PHE   A N   
2027 C  CA  . PHE   A 297 ? 0.2847 0.2170 0.2400 -0.0012 0.0216  0.0066  297  PHE   A CA  
2028 C  C   . PHE   A 297 ? 0.3067 0.2324 0.2572 -0.0024 0.0243  0.0058  297  PHE   A C   
2029 O  O   . PHE   A 297 ? 0.3348 0.2584 0.2856 -0.0009 0.0275  0.0063  297  PHE   A O   
2030 C  CB  . PHE   A 297 ? 0.2694 0.2056 0.2296 0.0005  0.0219  0.0077  297  PHE   A CB  
2031 C  CG  . PHE   A 297 ? 0.2671 0.2096 0.2321 0.0018  0.0197  0.0085  297  PHE   A CG  
2032 C  CD1 . PHE   A 297 ? 0.2785 0.2228 0.2445 0.0029  0.0195  0.0089  297  PHE   A CD1 
2033 C  CD2 . PHE   A 297 ? 0.2651 0.2116 0.2336 0.0020  0.0181  0.0089  297  PHE   A CD2 
2034 C  CE1 . PHE   A 297 ? 0.2704 0.2200 0.2405 0.0040  0.0178  0.0096  297  PHE   A CE1 
2035 C  CE2 . PHE   A 297 ? 0.2566 0.2085 0.2292 0.0033  0.0165  0.0096  297  PHE   A CE2 
2036 C  CZ  . PHE   A 297 ? 0.2525 0.2058 0.2257 0.0041  0.0163  0.0099  297  PHE   A CZ  
2037 N  N   . SER   A 298 ? 0.2980 0.2208 0.2445 -0.0051 0.0231  0.0046  298  SER   A N   
2038 C  CA  . SER   A 298 ? 0.3148 0.2311 0.2564 -0.0067 0.0255  0.0037  298  SER   A CA  
2039 C  C   . SER   A 298 ? 0.3169 0.2323 0.2604 -0.0055 0.0279  0.0042  298  SER   A C   
2040 O  O   . SER   A 298 ? 0.3396 0.2497 0.2802 -0.0055 0.0312  0.0039  298  SER   A O   
2041 C  CB  . SER   A 298 ? 0.3481 0.2594 0.2855 -0.0066 0.0281  0.0032  298  SER   A CB  
2042 O  OG  . SER   A 298 ? 0.4213 0.3326 0.3560 -0.0083 0.0258  0.0025  298  SER   A OG  
2043 N  N   . ILE   A 299 ? 0.2799 0.2006 0.2285 -0.0043 0.0264  0.0052  299  ILE   A N   
2044 C  CA  . ILE   A 299 ? 0.2780 0.1986 0.2290 -0.0031 0.0284  0.0059  299  ILE   A CA  
2045 C  C   . ILE   A 299 ? 0.2769 0.2007 0.2298 -0.0042 0.0258  0.0059  299  ILE   A C   
2046 O  O   . ILE   A 299 ? 0.2677 0.1972 0.2246 -0.0034 0.0233  0.0065  299  ILE   A O   
2047 C  CB  . ILE   A 299 ? 0.2948 0.2192 0.2508 0.0002  0.0298  0.0076  299  ILE   A CB  
2048 C  CG1 . ILE   A 299 ? 0.3221 0.2436 0.2767 0.0014  0.0326  0.0078  299  ILE   A CG1 
2049 C  CG2 . ILE   A 299 ? 0.3002 0.2250 0.2589 0.0013  0.0314  0.0085  299  ILE   A CG2 
2050 C  CD1 . ILE   A 299 ? 0.3550 0.2811 0.3147 0.0044  0.0334  0.0096  299  ILE   A CD1 
2051 N  N   . PRO   A 300 ? 0.2759 0.1962 0.2261 -0.0061 0.0263  0.0051  300  PRO   A N   
2052 C  CA  . PRO   A 300 ? 0.2731 0.1966 0.2252 -0.0074 0.0238  0.0051  300  PRO   A CA  
2053 C  C   . PRO   A 300 ? 0.2592 0.1878 0.2171 -0.0051 0.0236  0.0065  300  PRO   A C   
2054 O  O   . PRO   A 300 ? 0.2633 0.1916 0.2231 -0.0029 0.0262  0.0074  300  PRO   A O   
2055 C  CB  . PRO   A 300 ? 0.2999 0.2177 0.2478 -0.0096 0.0253  0.0041  300  PRO   A CB  
2056 C  CG  . PRO   A 300 ? 0.3235 0.2351 0.2657 -0.0107 0.0273  0.0031  300  PRO   A CG  
2057 C  CD  . PRO   A 300 ? 0.2830 0.1958 0.2277 -0.0076 0.0292  0.0041  300  PRO   A CD  
2058 N  N   . TYR   A 301 ? 0.2469 0.1803 0.2077 -0.0056 0.0207  0.0067  301  TYR   A N   
2059 C  CA  . TYR   A 301 ? 0.2417 0.1794 0.2074 -0.0039 0.0206  0.0078  301  TYR   A CA  
2060 C  C   . TYR   A 301 ? 0.2648 0.1988 0.2292 -0.0045 0.0229  0.0078  301  TYR   A C   
2061 O  O   . TYR   A 301 ? 0.2734 0.2038 0.2342 -0.0070 0.0226  0.0067  301  TYR   A O   
2062 C  CB  . TYR   A 301 ? 0.2237 0.1665 0.1920 -0.0047 0.0172  0.0078  301  TYR   A CB  
2063 C  CG  . TYR   A 301 ? 0.2130 0.1601 0.1859 -0.0034 0.0169  0.0089  301  TYR   A CG  
2064 C  CD1 . TYR   A 301 ? 0.2184 0.1698 0.1953 -0.0010 0.0169  0.0100  301  TYR   A CD1 
2065 C  CD2 . TYR   A 301 ? 0.2234 0.1705 0.1965 -0.0048 0.0163  0.0087  301  TYR   A CD2 
2066 C  CE1 . TYR   A 301 ? 0.2148 0.1702 0.1956 0.0001  0.0165  0.0109  301  TYR   A CE1 
2067 C  CE2 . TYR   A 301 ? 0.2192 0.1703 0.1964 -0.0037 0.0160  0.0097  301  TYR   A CE2 
2068 C  CZ  . TYR   A 301 ? 0.2209 0.1762 0.2018 -0.0013 0.0160  0.0107  301  TYR   A CZ  
2069 O  OH  . TYR   A 301 ? 0.2193 0.1784 0.2040 -0.0003 0.0157  0.0116  301  TYR   A OH  
2070 N  N   . PRO   A 302 ? 0.2545 0.1889 0.2215 -0.0023 0.0252  0.0090  302  PRO   A N   
2071 C  CA  . PRO   A 302 ? 0.2515 0.1810 0.2165 -0.0027 0.0280  0.0090  302  PRO   A CA  
2072 C  C   . PRO   A 302 ? 0.2676 0.1986 0.2344 -0.0034 0.0274  0.0093  302  PRO   A C   
2073 O  O   . PRO   A 302 ? 0.2877 0.2145 0.2528 -0.0037 0.0299  0.0093  302  PRO   A O   
2074 C  CB  . PRO   A 302 ? 0.2747 0.2040 0.2417 0.0003  0.0310  0.0104  302  PRO   A CB  
2075 C  CG  . PRO   A 302 ? 0.2725 0.2089 0.2446 0.0022  0.0290  0.0116  302  PRO   A CG  
2076 C  CD  . PRO   A 302 ? 0.2558 0.1939 0.2267 0.0006  0.0259  0.0104  302  PRO   A CD  
2077 N  N   . LEU   A 303 ? 0.2361 0.1730 0.2065 -0.0033 0.0245  0.0097  303  LEU   A N   
2078 C  CA  . LEU   A 303 ? 0.2345 0.1732 0.2070 -0.0038 0.0240  0.0101  303  LEU   A CA  
2079 C  C   . LEU   A 303 ? 0.2313 0.1700 0.2019 -0.0068 0.0215  0.0089  303  LEU   A C   
2080 O  O   . LEU   A 303 ? 0.2490 0.1882 0.2181 -0.0081 0.0195  0.0081  303  LEU   A O   
2081 C  CB  . LEU   A 303 ? 0.2291 0.1745 0.2070 -0.0016 0.0227  0.0114  303  LEU   A CB  
2082 C  CG  . LEU   A 303 ? 0.2361 0.1831 0.2164 0.0013  0.0243  0.0128  303  LEU   A CG  
2083 C  CD1 . LEU   A 303 ? 0.2418 0.1953 0.2270 0.0028  0.0229  0.0140  303  LEU   A CD1 
2084 C  CD2 . LEU   A 303 ? 0.2535 0.1962 0.2327 0.0024  0.0280  0.0135  303  LEU   A CD2 
2085 N  N   . PRO   A 304 ? 0.2360 0.1743 0.2069 -0.0081 0.0215  0.0089  304  PRO   A N   
2086 C  CA  . PRO   A 304 ? 0.2459 0.1843 0.2151 -0.0111 0.0191  0.0079  304  PRO   A CA  
2087 C  C   . PRO   A 304 ? 0.2382 0.1830 0.2110 -0.0111 0.0157  0.0082  304  PRO   A C   
2088 O  O   . PRO   A 304 ? 0.2456 0.1911 0.2172 -0.0135 0.0134  0.0075  304  PRO   A O   
2089 C  CB  . PRO   A 304 ? 0.2665 0.2028 0.2354 -0.0123 0.0203  0.0080  304  PRO   A CB  
2090 C  CG  . PRO   A 304 ? 0.2804 0.2140 0.2497 -0.0100 0.0239  0.0088  304  PRO   A CG  
2091 C  CD  . PRO   A 304 ? 0.2462 0.1833 0.2184 -0.0070 0.0239  0.0098  304  PRO   A CD  
2092 N  N   . LYS   A 305 ? 0.2185 0.1681 0.1957 -0.0086 0.0154  0.0093  305  LYS   A N   
2093 C  CA  . LYS   A 305 ? 0.2091 0.1646 0.1898 -0.0084 0.0126  0.0096  305  LYS   A CA  
2094 C  C   . LYS   A 305 ? 0.2082 0.1675 0.1920 -0.0057 0.0124  0.0104  305  LYS   A C   
2095 O  O   . LYS   A 305 ? 0.2086 0.1666 0.1925 -0.0039 0.0146  0.0110  305  LYS   A O   
2096 C  CB  . LYS   A 305 ? 0.2052 0.1633 0.1885 -0.0090 0.0120  0.0101  305  LYS   A CB  
2097 C  CG  . LYS   A 305 ? 0.2166 0.1757 0.2025 -0.0069 0.0140  0.0112  305  LYS   A CG  
2098 C  CD  . LYS   A 305 ? 0.1964 0.1614 0.1869 -0.0045 0.0131  0.0122  305  LYS   A CD  
2099 C  CE  . LYS   A 305 ? 0.2014 0.1674 0.1942 -0.0029 0.0149  0.0134  305  LYS   A CE  
2100 N  NZ  . LYS   A 305 ? 0.1874 0.1587 0.1839 -0.0008 0.0141  0.0143  305  LYS   A NZ  
2101 N  N   . GLN   A 306 ? 0.1991 0.1628 0.1851 -0.0056 0.0100  0.0104  306  GLN   A N   
2102 C  CA  . GLN   A 306 ? 0.1925 0.1600 0.1814 -0.0033 0.0095  0.0111  306  GLN   A CA  
2103 C  C   . GLN   A 306 ? 0.1923 0.1649 0.1848 -0.0033 0.0075  0.0114  306  GLN   A C   
2104 O  O   . GLN   A 306 ? 0.1974 0.1710 0.1897 -0.0048 0.0055  0.0110  306  GLN   A O   
2105 C  CB  . GLN   A 306 ? 0.1991 0.1657 0.1862 -0.0033 0.0087  0.0105  306  GLN   A CB  
2106 C  CG  . GLN   A 306 ? 0.2035 0.1741 0.1935 -0.0012 0.0082  0.0111  306  GLN   A CG  
2107 C  CD  . GLN   A 306 ? 0.2042 0.1745 0.1952 0.0009  0.0105  0.0119  306  GLN   A CD  
2108 O  OE1 . GLN   A 306 ? 0.2382 0.2103 0.2315 0.0017  0.0114  0.0127  306  GLN   A OE1 
2109 N  NE2 . GLN   A 306 ? 0.2342 0.2027 0.2238 0.0017  0.0116  0.0119  306  GLN   A NE2 
2110 N  N   . ASP   A 307 ? 0.1805 0.1562 0.1762 -0.0015 0.0081  0.0123  307  ASP   A N   
2111 C  CA  . ASP   A 307 ? 0.1662 0.1467 0.1652 -0.0013 0.0065  0.0126  307  ASP   A CA  
2112 C  C   . ASP   A 307 ? 0.1766 0.1603 0.1776 0.0004  0.0058  0.0128  307  ASP   A C   
2113 O  O   . ASP   A 307 ? 0.1890 0.1721 0.1897 0.0017  0.0069  0.0131  307  ASP   A O   
2114 C  CB  . ASP   A 307 ? 0.1673 0.1491 0.1684 -0.0008 0.0076  0.0133  307  ASP   A CB  
2115 C  CG  . ASP   A 307 ? 0.1939 0.1731 0.1935 -0.0027 0.0079  0.0131  307  ASP   A CG  
2116 O  OD1 . ASP   A 307 ? 0.2018 0.1794 0.1995 -0.0047 0.0067  0.0123  307  ASP   A OD1 
2117 O  OD2 . ASP   A 307 ? 0.2020 0.1805 0.2021 -0.0024 0.0095  0.0137  307  ASP   A OD2 
2118 N  N   . LEU   A 308 ? 0.1690 0.1561 0.1721 0.0002  0.0040  0.0128  308  LEU   A N   
2119 C  CA  . LEU   A 308 ? 0.1604 0.1508 0.1655 0.0017  0.0033  0.0129  308  LEU   A CA  
2120 C  C   . LEU   A 308 ? 0.1636 0.1577 0.1719 0.0020  0.0028  0.0134  308  LEU   A C   
2121 O  O   . LEU   A 308 ? 0.1704 0.1659 0.1797 0.0010  0.0016  0.0133  308  LEU   A O   
2122 C  CB  . LEU   A 308 ? 0.1586 0.1490 0.1629 0.0011  0.0016  0.0124  308  LEU   A CB  
2123 C  CG  . LEU   A 308 ? 0.1680 0.1548 0.1691 0.0007  0.0019  0.0119  308  LEU   A CG  
2124 C  CD1 . LEU   A 308 ? 0.1738 0.1572 0.1720 -0.0013 0.0017  0.0115  308  LEU   A CD1 
2125 C  CD2 . LEU   A 308 ? 0.1808 0.1686 0.1818 0.0011  0.0006  0.0117  308  LEU   A CD2 
2126 N  N   . ALA   A 309 ? 0.1483 0.1442 0.1581 0.0034  0.0039  0.0140  309  ALA   A N   
2127 C  CA  . ALA   A 309 ? 0.1454 0.1446 0.1580 0.0037  0.0037  0.0144  309  ALA   A CA  
2128 C  C   . ALA   A 309 ? 0.1428 0.1451 0.1570 0.0048  0.0033  0.0144  309  ALA   A C   
2129 O  O   . ALA   A 309 ? 0.1484 0.1509 0.1623 0.0059  0.0040  0.0146  309  ALA   A O   
2130 C  CB  . ALA   A 309 ? 0.1709 0.1697 0.1836 0.0040  0.0054  0.0151  309  ALA   A CB  
2131 N  N   . ALA   A 310 ? 0.1353 0.1402 0.1516 0.0047  0.0023  0.0143  310  ALA   A N   
2132 C  CA  . ALA   A 310 ? 0.1438 0.1513 0.1616 0.0056  0.0020  0.0142  310  ALA   A CA  
2133 C  C   . ALA   A 310 ? 0.1493 0.1592 0.1687 0.0062  0.0029  0.0147  310  ALA   A C   
2134 O  O   . ALA   A 310 ? 0.1515 0.1625 0.1723 0.0057  0.0029  0.0149  310  ALA   A O   
2135 C  CB  . ALA   A 310 ? 0.1457 0.1547 0.1649 0.0052  0.0006  0.0139  310  ALA   A CB  
2136 N  N   . ILE   A 311 ? 0.1381 0.1487 0.1573 0.0071  0.0037  0.0149  311  ILE   A N   
2137 C  CA  . ILE   A 311 ? 0.1397 0.1523 0.1599 0.0075  0.0046  0.0156  311  ILE   A CA  
2138 C  C   . ILE   A 311 ? 0.1506 0.1658 0.1720 0.0080  0.0043  0.0152  311  ILE   A C   
2139 O  O   . ILE   A 311 ? 0.1597 0.1749 0.1806 0.0083  0.0039  0.0148  311  ILE   A O   
2140 C  CB  . ILE   A 311 ? 0.1476 0.1596 0.1667 0.0082  0.0056  0.0163  311  ILE   A CB  
2141 C  CG1 . ILE   A 311 ? 0.1462 0.1549 0.1637 0.0080  0.0061  0.0164  311  ILE   A CG1 
2142 C  CG2 . ILE   A 311 ? 0.1555 0.1692 0.1756 0.0084  0.0066  0.0172  311  ILE   A CG2 
2143 C  CD1 . ILE   A 311 ? 0.1685 0.1755 0.1858 0.0071  0.0064  0.0166  311  ILE   A CD1 
2144 N  N   . PRO   A 312 ? 0.1461 0.1633 0.1691 0.0079  0.0047  0.0155  312  PRO   A N   
2145 C  CA  . PRO   A 312 ? 0.1458 0.1651 0.1698 0.0082  0.0046  0.0150  312  PRO   A CA  
2146 C  C   . PRO   A 312 ? 0.1542 0.1743 0.1771 0.0087  0.0050  0.0150  312  PRO   A C   
2147 O  O   . PRO   A 312 ? 0.1609 0.1818 0.1839 0.0090  0.0049  0.0144  312  PRO   A O   
2148 C  CB  . PRO   A 312 ? 0.1488 0.1697 0.1743 0.0080  0.0052  0.0154  312  PRO   A CB  
2149 C  CG  . PRO   A 312 ? 0.1612 0.1808 0.1870 0.0073  0.0049  0.0157  312  PRO   A CG  
2150 C  CD  . PRO   A 312 ? 0.1499 0.1671 0.1737 0.0073  0.0050  0.0159  312  PRO   A CD  
2151 N  N   . ASP   A 313 ? 0.1491 0.1689 0.1711 0.0089  0.0056  0.0158  313  ASP   A N   
2152 C  CA  . ASP   A 313 ? 0.1411 0.1620 0.1622 0.0092  0.0059  0.0160  313  ASP   A CA  
2153 C  C   . ASP   A 313 ? 0.1435 0.1628 0.1634 0.0094  0.0059  0.0165  313  ASP   A C   
2154 O  O   . ASP   A 313 ? 0.1492 0.1675 0.1691 0.0095  0.0064  0.0173  313  ASP   A O   
2155 C  CB  . ASP   A 313 ? 0.1552 0.1781 0.1765 0.0092  0.0067  0.0169  313  ASP   A CB  
2156 C  CG  . ASP   A 313 ? 0.1752 0.1996 0.1976 0.0089  0.0069  0.0164  313  ASP   A CG  
2157 O  OD1 . ASP   A 313 ? 0.1746 0.1998 0.1967 0.0089  0.0068  0.0157  313  ASP   A OD1 
2158 O  OD2 . ASP   A 313 ? 0.1896 0.2142 0.2129 0.0088  0.0072  0.0169  313  ASP   A OD2 
2159 N  N   . PHE   A 314 ? 0.1379 0.1568 0.1570 0.0096  0.0055  0.0160  314  PHE   A N   
2160 C  CA  . PHE   A 314 ? 0.1343 0.1516 0.1524 0.0098  0.0056  0.0164  314  PHE   A CA  
2161 C  C   . PHE   A 314 ? 0.1456 0.1638 0.1630 0.0099  0.0054  0.0161  314  PHE   A C   
2162 O  O   . PHE   A 314 ? 0.1589 0.1773 0.1761 0.0097  0.0048  0.0152  314  PHE   A O   
2163 C  CB  . PHE   A 314 ? 0.1354 0.1500 0.1531 0.0096  0.0051  0.0158  314  PHE   A CB  
2164 C  CG  . PHE   A 314 ? 0.1365 0.1490 0.1531 0.0098  0.0056  0.0163  314  PHE   A CG  
2165 C  CD1 . PHE   A 314 ? 0.1487 0.1600 0.1653 0.0099  0.0065  0.0170  314  PHE   A CD1 
2166 C  CD2 . PHE   A 314 ? 0.1341 0.1456 0.1497 0.0100  0.0055  0.0161  314  PHE   A CD2 
2167 C  CE1 . PHE   A 314 ? 0.1554 0.1644 0.1709 0.0101  0.0072  0.0176  314  PHE   A CE1 
2168 C  CE2 . PHE   A 314 ? 0.1511 0.1604 0.1657 0.0103  0.0062  0.0166  314  PHE   A CE2 
2169 C  CZ  . PHE   A 314 ? 0.1572 0.1653 0.1718 0.0104  0.0071  0.0173  314  PHE   A CZ  
2170 N  N   . GLN   A 315 ? 0.1434 0.1621 0.1604 0.0102  0.0058  0.0171  315  GLN   A N   
2171 C  CA  . GLN   A 315 ? 0.1363 0.1563 0.1528 0.0101  0.0056  0.0171  315  GLN   A CA  
2172 C  C   . GLN   A 315 ? 0.1487 0.1668 0.1642 0.0101  0.0051  0.0163  315  GLN   A C   
2173 O  O   . GLN   A 315 ? 0.1538 0.1721 0.1688 0.0098  0.0046  0.0154  315  GLN   A O   
2174 C  CB  . GLN   A 315 ? 0.1458 0.1677 0.1626 0.0103  0.0062  0.0187  315  GLN   A CB  
2175 C  CG  . GLN   A 315 ? 0.1403 0.1639 0.1565 0.0100  0.0058  0.0188  315  GLN   A CG  
2176 C  CD  . GLN   A 315 ? 0.1829 0.2092 0.1997 0.0100  0.0062  0.0205  315  GLN   A CD  
2177 O  OE1 . GLN   A 315 ? 0.1893 0.2168 0.2068 0.0102  0.0066  0.0214  315  GLN   A OE1 
2178 N  NE2 . GLN   A 315 ? 0.1652 0.1929 0.1818 0.0098  0.0060  0.0210  315  GLN   A NE2 
2179 N  N   . SER   A 316 ? 0.1478 0.1640 0.1630 0.0105  0.0055  0.0168  316  SER   A N   
2180 C  CA  . SER   A 316 ? 0.1487 0.1629 0.1628 0.0105  0.0052  0.0161  316  SER   A CA  
2181 C  C   . SER   A 316 ? 0.1547 0.1668 0.1686 0.0102  0.0045  0.0150  316  SER   A C   
2182 O  O   . SER   A 316 ? 0.1515 0.1643 0.1661 0.0100  0.0042  0.0147  316  SER   A O   
2183 C  CB  . SER   A 316 ? 0.1719 0.1847 0.1857 0.0110  0.0060  0.0171  316  SER   A CB  
2184 O  OG  . SER   A 316 ? 0.2148 0.2261 0.2287 0.0111  0.0066  0.0174  316  SER   A OG  
2185 N  N   . GLY   A 317 ? 0.1597 0.1695 0.1724 0.0102  0.0042  0.0146  317  GLY   A N   
2186 C  CA  . GLY   A 317 ? 0.1540 0.1620 0.1664 0.0098  0.0034  0.0137  317  GLY   A CA  
2187 C  C   . GLY   A 317 ? 0.1536 0.1600 0.1658 0.0096  0.0037  0.0140  317  GLY   A C   
2188 O  O   . GLY   A 317 ? 0.1449 0.1512 0.1576 0.0092  0.0032  0.0137  317  GLY   A O   
2189 N  N   . ALA   A 318 ? 0.1470 0.1521 0.1585 0.0099  0.0047  0.0147  318  ALA   A N   
2190 C  CA  . ALA   A 318 ? 0.1560 0.1587 0.1667 0.0096  0.0052  0.0149  318  ALA   A CA  
2191 C  C   . ALA   A 318 ? 0.1436 0.1454 0.1539 0.0102  0.0067  0.0158  318  ALA   A C   
2192 O  O   . ALA   A 318 ? 0.1547 0.1578 0.1654 0.0108  0.0071  0.0164  318  ALA   A O   
2193 C  CB  . ALA   A 318 ? 0.1587 0.1587 0.1677 0.0089  0.0044  0.0140  318  ALA   A CB  
2194 N  N   . MET   A 319 ? 0.1419 0.1414 0.1515 0.0100  0.0075  0.0161  319  MET   A N   
2195 C  CA  . MET   A 319 ? 0.1428 0.1410 0.1521 0.0107  0.0092  0.0171  319  MET   A CA  
2196 C  C   . MET   A 319 ? 0.1532 0.1472 0.1604 0.0101  0.0100  0.0168  319  MET   A C   
2197 O  O   . MET   A 319 ? 0.1708 0.1638 0.1776 0.0091  0.0093  0.0161  319  MET   A O   
2198 C  CB  . MET   A 319 ? 0.1498 0.1505 0.1609 0.0113  0.0099  0.0183  319  MET   A CB  
2199 C  CG  . MET   A 319 ? 0.1598 0.1591 0.1709 0.0121  0.0118  0.0197  319  MET   A CG  
2200 S  SD  . MET   A 319 ? 0.1576 0.1575 0.1688 0.0131  0.0125  0.0205  319  MET   A SD  
2201 C  CE  . MET   A 319 ? 0.1685 0.1644 0.1786 0.0138  0.0150  0.0214  319  MET   A CE  
2202 N  N   . GLU   A 320 ? 0.1459 0.1375 0.1519 0.0106  0.0114  0.0172  320  GLU   A N   
2203 C  CA  . GLU   A 320 ? 0.1437 0.1309 0.1472 0.0099  0.0122  0.0166  320  GLU   A CA  
2204 C  C   . GLU   A 320 ? 0.1644 0.1491 0.1673 0.0100  0.0139  0.0172  320  GLU   A C   
2205 O  O   . GLU   A 320 ? 0.1747 0.1554 0.1754 0.0097  0.0153  0.0169  320  GLU   A O   
2206 C  CB  . GLU   A 320 ? 0.1557 0.1409 0.1576 0.0103  0.0129  0.0165  320  GLU   A CB  
2207 C  CG  . GLU   A 320 ? 0.1652 0.1512 0.1684 0.0118  0.0148  0.0180  320  GLU   A CG  
2208 C  CD  . GLU   A 320 ? 0.1621 0.1520 0.1673 0.0126  0.0142  0.0187  320  GLU   A CD  
2209 O  OE1 . GLU   A 320 ? 0.1502 0.1431 0.1565 0.0122  0.0125  0.0182  320  GLU   A OE1 
2210 O  OE2 . GLU   A 320 ? 0.1675 0.1575 0.1731 0.0136  0.0156  0.0197  320  GLU   A OE2 
2211 N  N   . ASN   A 321 ? 0.1601 0.1469 0.1650 0.0102  0.0141  0.0180  321  ASN   A N   
2212 C  CA  . ASN   A 321 ? 0.1690 0.1534 0.1734 0.0104  0.0160  0.0187  321  ASN   A CA  
2213 C  C   . ASN   A 321 ? 0.1780 0.1576 0.1795 0.0091  0.0165  0.0176  321  ASN   A C   
2214 O  O   . ASN   A 321 ? 0.1805 0.1597 0.1810 0.0076  0.0149  0.0164  321  ASN   A O   
2215 C  CB  . ASN   A 321 ? 0.1582 0.1453 0.1647 0.0104  0.0156  0.0193  321  ASN   A CB  
2216 C  CG  . ASN   A 321 ? 0.1631 0.1551 0.1721 0.0111  0.0145  0.0199  321  ASN   A CG  
2217 O  OD1 . ASN   A 321 ? 0.1646 0.1587 0.1751 0.0124  0.0153  0.0213  321  ASN   A OD1 
2218 N  ND2 . ASN   A 321 ? 0.1578 0.1520 0.1675 0.0103  0.0127  0.0190  321  ASN   A ND2 
2219 N  N   . TRP   A 322 ? 0.1684 0.1442 0.1683 0.0095  0.0187  0.0181  322  TRP   A N   
2220 C  CA  . TRP   A 322 ? 0.1785 0.1490 0.1748 0.0081  0.0195  0.0169  322  TRP   A CA  
2221 C  C   . TRP   A 322 ? 0.1848 0.1540 0.1802 0.0064  0.0188  0.0162  322  TRP   A C   
2222 O  O   . TRP   A 322 ? 0.1909 0.1597 0.1871 0.0068  0.0201  0.0170  322  TRP   A O   
2223 C  CB  . TRP   A 322 ? 0.1861 0.1528 0.1812 0.0092  0.0224  0.0177  322  TRP   A CB  
2224 C  CG  . TRP   A 322 ? 0.1876 0.1494 0.1789 0.0084  0.0234  0.0166  322  TRP   A CG  
2225 C  CD1 . TRP   A 322 ? 0.2015 0.1612 0.1899 0.0065  0.0220  0.0150  322  TRP   A CD1 
2226 C  CD2 . TRP   A 322 ? 0.1960 0.1543 0.1861 0.0095  0.0262  0.0173  322  TRP   A CD2 
2227 N  NE1 . TRP   A 322 ? 0.2063 0.1613 0.1915 0.0063  0.0237  0.0145  322  TRP   A NE1 
2228 C  CE2 . TRP   A 322 ? 0.2003 0.1545 0.1866 0.0082  0.0264  0.0159  322  TRP   A CE2 
2229 C  CE3 . TRP   A 322 ? 0.2000 0.1588 0.1921 0.0116  0.0285  0.0191  322  TRP   A CE3 
2230 C  CZ2 . TRP   A 322 ? 0.2112 0.1610 0.1953 0.0089  0.0291  0.0160  322  TRP   A CZ2 
2231 C  CZ3 . TRP   A 322 ? 0.2077 0.1626 0.1981 0.0124  0.0311  0.0194  322  TRP   A CZ3 
2232 C  CH2 . TRP   A 322 ? 0.2104 0.1608 0.1968 0.0111  0.0314  0.0178  322  TRP   A CH2 
2233 N  N   . GLY   A 323 ? 0.1804 0.1491 0.1743 0.0047  0.0169  0.0149  323  GLY   A N   
2234 C  CA  . GLY   A 323 ? 0.1752 0.1432 0.1685 0.0029  0.0161  0.0143  323  GLY   A CA  
2235 C  C   . GLY   A 323 ? 0.1832 0.1562 0.1797 0.0029  0.0142  0.0145  323  GLY   A C   
2236 O  O   . GLY   A 323 ? 0.1805 0.1537 0.1769 0.0013  0.0130  0.0140  323  GLY   A O   
2237 N  N   . LEU   A 324 ? 0.1702 0.1473 0.1695 0.0046  0.0138  0.0153  324  LEU   A N   
2238 C  CA  . LEU   A 324 ? 0.1681 0.1498 0.1703 0.0047  0.0122  0.0156  324  LEU   A CA  
2239 C  C   . LEU   A 324 ? 0.1737 0.1590 0.1777 0.0059  0.0113  0.0158  324  LEU   A C   
2240 O  O   . LEU   A 324 ? 0.1625 0.1504 0.1685 0.0072  0.0118  0.0168  324  LEU   A O   
2241 C  CB  . LEU   A 324 ? 0.1668 0.1495 0.1708 0.0053  0.0135  0.0167  324  LEU   A CB  
2242 C  CG  . LEU   A 324 ? 0.1752 0.1626 0.1821 0.0055  0.0122  0.0170  324  LEU   A CG  
2243 C  CD1 . LEU   A 324 ? 0.1785 0.1669 0.1855 0.0039  0.0102  0.0160  324  LEU   A CD1 
2244 C  CD2 . LEU   A 324 ? 0.1822 0.1697 0.1902 0.0057  0.0135  0.0180  324  LEU   A CD2 
2245 N  N   . THR   A 325 ? 0.1671 0.1522 0.1701 0.0053  0.0099  0.0149  325  THR   A N   
2246 C  CA  . THR   A 325 ? 0.1555 0.1436 0.1598 0.0062  0.0089  0.0149  325  THR   A CA  
2247 C  C   . THR   A 325 ? 0.1545 0.1465 0.1613 0.0063  0.0076  0.0149  325  THR   A C   
2248 O  O   . THR   A 325 ? 0.1622 0.1544 0.1694 0.0052  0.0068  0.0146  325  THR   A O   
2249 C  CB  . THR   A 325 ? 0.1716 0.1579 0.1739 0.0057  0.0080  0.0140  325  THR   A CB  
2250 O  OG1 . THR   A 325 ? 0.1758 0.1617 0.1774 0.0042  0.0064  0.0132  325  THR   A OG1 
2251 C  CG2 . THR   A 325 ? 0.1829 0.1649 0.1824 0.0057  0.0097  0.0140  325  THR   A CG2 
2252 N  N   . THR   A 326 ? 0.1453 0.1405 0.1539 0.0074  0.0075  0.0154  326  THR   A N   
2253 C  CA  . THR   A 326 ? 0.1432 0.1420 0.1541 0.0076  0.0066  0.0155  326  THR   A CA  
2254 C  C   . THR   A 326 ? 0.1428 0.1435 0.1542 0.0079  0.0055  0.0150  326  THR   A C   
2255 O  O   . THR   A 326 ? 0.1485 0.1484 0.1590 0.0083  0.0056  0.0149  326  THR   A O   
2256 C  CB  . THR   A 326 ? 0.1506 0.1514 0.1630 0.0084  0.0077  0.0166  326  THR   A CB  
2257 O  OG1 . THR   A 326 ? 0.1588 0.1595 0.1708 0.0094  0.0086  0.0172  326  THR   A OG1 
2258 C  CG2 . THR   A 326 ? 0.1516 0.1508 0.1638 0.0080  0.0088  0.0171  326  THR   A CG2 
2259 N  N   . TYR   A 327 ? 0.1397 0.1428 0.1527 0.0077  0.0045  0.0147  327  TYR   A N   
2260 C  CA  . TYR   A 327 ? 0.1430 0.1474 0.1563 0.0079  0.0035  0.0141  327  TYR   A CA  
2261 C  C   . TYR   A 327 ? 0.1381 0.1455 0.1534 0.0082  0.0032  0.0141  327  TYR   A C   
2262 O  O   . TYR   A 327 ? 0.1426 0.1511 0.1591 0.0079  0.0032  0.0143  327  TYR   A O   
2263 C  CB  . TYR   A 327 ? 0.1427 0.1457 0.1554 0.0071  0.0022  0.0134  327  TYR   A CB  
2264 C  CG  . TYR   A 327 ? 0.1367 0.1363 0.1470 0.0065  0.0023  0.0132  327  TYR   A CG  
2265 C  CD1 . TYR   A 327 ? 0.1488 0.1463 0.1581 0.0057  0.0029  0.0134  327  TYR   A CD1 
2266 C  CD2 . TYR   A 327 ? 0.1489 0.1471 0.1577 0.0066  0.0020  0.0129  327  TYR   A CD2 
2267 C  CE1 . TYR   A 327 ? 0.1374 0.1315 0.1441 0.0052  0.0034  0.0132  327  TYR   A CE1 
2268 C  CE2 . TYR   A 327 ? 0.1497 0.1446 0.1560 0.0060  0.0023  0.0127  327  TYR   A CE2 
2269 C  CZ  . TYR   A 327 ? 0.1518 0.1445 0.1570 0.0054  0.0031  0.0128  327  TYR   A CZ  
2270 O  OH  . TYR   A 327 ? 0.1660 0.1550 0.1683 0.0048  0.0037  0.0125  327  TYR   A OH  
2271 N  N   . ARG   A 328 ? 0.1389 0.1477 0.1545 0.0087  0.0029  0.0138  328  ARG   A N   
2272 C  CA  . ARG   A 328 ? 0.1405 0.1516 0.1576 0.0088  0.0025  0.0135  328  ARG   A CA  
2273 C  C   . ARG   A 328 ? 0.1542 0.1649 0.1721 0.0083  0.0015  0.0131  328  ARG   A C   
2274 O  O   . ARG   A 328 ? 0.1555 0.1643 0.1723 0.0079  0.0008  0.0129  328  ARG   A O   
2275 C  CB  . ARG   A 328 ? 0.1580 0.1697 0.1748 0.0092  0.0023  0.0130  328  ARG   A CB  
2276 C  CG  . ARG   A 328 ? 0.1617 0.1750 0.1784 0.0095  0.0031  0.0134  328  ARG   A CG  
2277 C  CD  . ARG   A 328 ? 0.1665 0.1800 0.1825 0.0096  0.0028  0.0128  328  ARG   A CD  
2278 N  NE  . ARG   A 328 ? 0.1544 0.1696 0.1702 0.0096  0.0034  0.0132  328  ARG   A NE  
2279 C  CZ  . ARG   A 328 ? 0.1570 0.1740 0.1731 0.0095  0.0036  0.0129  328  ARG   A CZ  
2280 N  NH1 . ARG   A 328 ? 0.1643 0.1815 0.1811 0.0095  0.0035  0.0122  328  ARG   A NH1 
2281 N  NH2 . ARG   A 328 ? 0.1515 0.1701 0.1670 0.0093  0.0040  0.0134  328  ARG   A NH2 
2282 N  N   . GLU   A 329 ? 0.1458 0.1585 0.1655 0.0083  0.0015  0.0132  329  GLU   A N   
2283 C  CA  . GLU   A 329 ? 0.1395 0.1523 0.1603 0.0079  0.0005  0.0130  329  GLU   A CA  
2284 C  C   . GLU   A 329 ? 0.1518 0.1639 0.1722 0.0081  -0.0003 0.0126  329  GLU   A C   
2285 O  O   . GLU   A 329 ? 0.1579 0.1690 0.1781 0.0076  -0.0013 0.0126  329  GLU   A O   
2286 C  CB  . GLU   A 329 ? 0.1453 0.1606 0.1685 0.0081  0.0008  0.0132  329  GLU   A CB  
2287 C  CG  . GLU   A 329 ? 0.1549 0.1707 0.1786 0.0076  0.0014  0.0137  329  GLU   A CG  
2288 C  CD  . GLU   A 329 ? 0.1506 0.1689 0.1765 0.0077  0.0019  0.0139  329  GLU   A CD  
2289 O  OE1 . GLU   A 329 ? 0.1787 0.1983 0.2053 0.0084  0.0022  0.0135  329  GLU   A OE1 
2290 O  OE2 . GLU   A 329 ? 0.1782 0.1969 0.2049 0.0072  0.0021  0.0143  329  GLU   A OE2 
2291 N  N   . SER   A 330 ? 0.1352 0.1477 0.1553 0.0088  0.0001  0.0123  330  SER   A N   
2292 C  CA  . SER   A 330 ? 0.1441 0.1558 0.1637 0.0091  -0.0005 0.0119  330  SER   A CA  
2293 C  C   . SER   A 330 ? 0.1567 0.1660 0.1742 0.0087  -0.0011 0.0118  330  SER   A C   
2294 O  O   . SER   A 330 ? 0.1632 0.1716 0.1803 0.0088  -0.0018 0.0116  330  SER   A O   
2295 C  CB  . SER   A 330 ? 0.1525 0.1648 0.1718 0.0097  0.0002  0.0114  330  SER   A CB  
2296 O  OG  . SER   A 330 ? 0.1788 0.1908 0.1967 0.0096  0.0008  0.0115  330  SER   A OG  
2297 N  N   . ALA   A 331 ? 0.1559 0.1640 0.1720 0.0084  -0.0006 0.0120  331  ALA   A N   
2298 C  CA  . ALA   A 331 ? 0.1622 0.1678 0.1761 0.0081  -0.0008 0.0119  331  ALA   A CA  
2299 C  C   . ALA   A 331 ? 0.1637 0.1678 0.1770 0.0072  -0.0015 0.0121  331  ALA   A C   
2300 O  O   . ALA   A 331 ? 0.1700 0.1717 0.1812 0.0068  -0.0016 0.0119  331  ALA   A O   
2301 C  CB  . ALA   A 331 ? 0.1659 0.1709 0.1787 0.0084  0.0003  0.0121  331  ALA   A CB  
2302 N  N   . LEU   A 332 ? 0.1591 0.1644 0.1739 0.0068  -0.0019 0.0123  332  LEU   A N   
2303 C  CA  . LEU   A 332 ? 0.1526 0.1566 0.1667 0.0056  -0.0026 0.0124  332  LEU   A CA  
2304 C  C   . LEU   A 332 ? 0.1516 0.1572 0.1674 0.0051  -0.0039 0.0127  332  LEU   A C   
2305 O  O   . LEU   A 332 ? 0.1653 0.1697 0.1802 0.0040  -0.0049 0.0128  332  LEU   A O   
2306 C  CB  . LEU   A 332 ? 0.1580 0.1617 0.1720 0.0052  -0.0016 0.0127  332  LEU   A CB  
2307 C  CG  . LEU   A 332 ? 0.1664 0.1677 0.1787 0.0038  -0.0018 0.0126  332  LEU   A CG  
2308 C  CD1 . LEU   A 332 ? 0.1719 0.1699 0.1811 0.0036  -0.0016 0.0123  332  LEU   A CD1 
2309 C  CD2 . LEU   A 332 ? 0.1684 0.1694 0.1808 0.0035  -0.0007 0.0129  332  LEU   A CD2 
2310 N  N   . LEU   A 333 ? 0.1490 0.1573 0.1675 0.0058  -0.0037 0.0129  333  LEU   A N   
2311 C  CA  . LEU   A 333 ? 0.1589 0.1692 0.1798 0.0054  -0.0047 0.0133  333  LEU   A CA  
2312 C  C   . LEU   A 333 ? 0.1609 0.1721 0.1829 0.0060  -0.0056 0.0135  333  LEU   A C   
2313 O  O   . LEU   A 333 ? 0.1712 0.1829 0.1937 0.0071  -0.0049 0.0132  333  LEU   A O   
2314 C  CB  . LEU   A 333 ? 0.1541 0.1668 0.1773 0.0057  -0.0038 0.0136  333  LEU   A CB  
2315 C  CG  . LEU   A 333 ? 0.1492 0.1610 0.1714 0.0052  -0.0029 0.0136  333  LEU   A CG  
2316 C  CD1 . LEU   A 333 ? 0.1705 0.1847 0.1951 0.0055  -0.0021 0.0139  333  LEU   A CD1 
2317 C  CD2 . LEU   A 333 ? 0.1862 0.1964 0.2073 0.0036  -0.0037 0.0137  333  LEU   A CD2 
2318 N  N   . PHE   A 334 ? 0.1531 0.1645 0.1754 0.0052  -0.0070 0.0140  334  PHE   A N   
2319 C  CA  . PHE   A 334 ? 0.1651 0.1771 0.1884 0.0057  -0.0080 0.0144  334  PHE   A CA  
2320 C  C   . PHE   A 334 ? 0.1642 0.1792 0.1909 0.0057  -0.0088 0.0153  334  PHE   A C   
2321 O  O   . PHE   A 334 ? 0.1702 0.1859 0.1973 0.0044  -0.0098 0.0159  334  PHE   A O   
2322 C  CB  . PHE   A 334 ? 0.1702 0.1798 0.1907 0.0047  -0.0092 0.0144  334  PHE   A CB  
2323 C  CG  . PHE   A 334 ? 0.1864 0.1965 0.2076 0.0053  -0.0103 0.0149  334  PHE   A CG  
2324 C  CD1 . PHE   A 334 ? 0.2064 0.2156 0.2271 0.0065  -0.0096 0.0145  334  PHE   A CD1 
2325 C  CD2 . PHE   A 334 ? 0.2119 0.2231 0.2341 0.0044  -0.0119 0.0159  334  PHE   A CD2 
2326 C  CE1 . PHE   A 334 ? 0.2281 0.2377 0.2496 0.0071  -0.0104 0.0151  334  PHE   A CE1 
2327 C  CE2 . PHE   A 334 ? 0.2305 0.2424 0.2536 0.0050  -0.0129 0.0166  334  PHE   A CE2 
2328 C  CZ  . PHE   A 334 ? 0.2189 0.2299 0.2417 0.0064  -0.0121 0.0162  334  PHE   A CZ  
2329 N  N   . ASP   A 335 ? 0.1587 0.1754 0.1878 0.0071  -0.0084 0.0156  335  ASP   A N   
2330 C  CA  . ASP   A 335 ? 0.1624 0.1821 0.1952 0.0074  -0.0089 0.0167  335  ASP   A CA  
2331 C  C   . ASP   A 335 ? 0.1719 0.1915 0.2050 0.0078  -0.0101 0.0174  335  ASP   A C   
2332 O  O   . ASP   A 335 ? 0.1748 0.1934 0.2074 0.0090  -0.0095 0.0170  335  ASP   A O   
2333 C  CB  . ASP   A 335 ? 0.1756 0.1969 0.2107 0.0088  -0.0073 0.0165  335  ASP   A CB  
2334 C  CG  . ASP   A 335 ? 0.2310 0.2554 0.2702 0.0095  -0.0074 0.0176  335  ASP   A CG  
2335 O  OD1 . ASP   A 335 ? 0.2183 0.2436 0.2587 0.0093  -0.0088 0.0187  335  ASP   A OD1 
2336 O  OD2 . ASP   A 335 ? 0.2349 0.2607 0.2760 0.0103  -0.0060 0.0175  335  ASP   A OD2 
2337 N  N   . ALA   A 336 ? 0.1708 0.1912 0.2043 0.0066  -0.0119 0.0184  336  ALA   A N   
2338 C  CA  . ALA   A 336 ? 0.1906 0.2108 0.2240 0.0069  -0.0132 0.0192  336  ALA   A CA  
2339 C  C   . ALA   A 336 ? 0.2056 0.2276 0.2423 0.0087  -0.0127 0.0200  336  ALA   A C   
2340 O  O   . ALA   A 336 ? 0.2469 0.2681 0.2832 0.0093  -0.0133 0.0205  336  ALA   A O   
2341 C  CB  . ALA   A 336 ? 0.2157 0.2370 0.2492 0.0051  -0.0154 0.0203  336  ALA   A CB  
2342 N  N   . GLU   A 337 ? 0.1893 0.2134 0.2290 0.0097  -0.0114 0.0201  337  GLU   A N   
2343 C  CA  . GLU   A 337 ? 0.2026 0.2281 0.2454 0.0116  -0.0105 0.0208  337  GLU   A CA  
2344 C  C   . GLU   A 337 ? 0.2074 0.2310 0.2491 0.0129  -0.0084 0.0195  337  GLU   A C   
2345 O  O   . GLU   A 337 ? 0.2589 0.2825 0.3020 0.0144  -0.0077 0.0199  337  GLU   A O   
2346 C  CB  . GLU   A 337 ? 0.2344 0.2636 0.2816 0.0119  -0.0103 0.0220  337  GLU   A CB  
2347 C  CG  . GLU   A 337 ? 0.2838 0.3155 0.3330 0.0107  -0.0125 0.0237  337  GLU   A CG  
2348 C  CD  . GLU   A 337 ? 0.3540 0.3896 0.4078 0.0112  -0.0120 0.0249  337  GLU   A CD  
2349 O  OE1 . GLU   A 337 ? 0.3595 0.3955 0.4136 0.0109  -0.0108 0.0241  337  GLU   A OE1 
2350 O  OE2 . GLU   A 337 ? 0.3370 0.3752 0.3943 0.0118  -0.0128 0.0267  337  GLU   A OE2 
2351 N  N   . LYS   A 338 ? 0.1747 0.1969 0.2140 0.0124  -0.0074 0.0181  338  LYS   A N   
2352 C  CA  . LYS   A 338 ? 0.1750 0.1958 0.2133 0.0135  -0.0055 0.0169  338  LYS   A CA  
2353 C  C   . LYS   A 338 ? 0.1730 0.1908 0.2073 0.0129  -0.0053 0.0157  338  LYS   A C   
2354 O  O   . LYS   A 338 ? 0.1919 0.2086 0.2253 0.0137  -0.0040 0.0148  338  LYS   A O   
2355 C  CB  . LYS   A 338 ? 0.1953 0.2176 0.2349 0.0135  -0.0041 0.0165  338  LYS   A CB  
2356 C  CG  . LYS   A 338 ? 0.2710 0.2959 0.3147 0.0145  -0.0034 0.0175  338  LYS   A CG  
2357 C  CD  . LYS   A 338 ? 0.3453 0.3714 0.3898 0.0145  -0.0018 0.0169  338  LYS   A CD  
2358 C  CE  . LYS   A 338 ? 0.4190 0.4478 0.4677 0.0155  -0.0011 0.0180  338  LYS   A CE  
2359 N  NZ  . LYS   A 338 ? 0.4459 0.4740 0.4957 0.0171  -0.0003 0.0183  338  LYS   A NZ  
2360 N  N   . SER   A 339 ? 0.1659 0.1826 0.1980 0.0117  -0.0065 0.0156  339  SER   A N   
2361 C  CA  . SER   A 339 ? 0.1680 0.1822 0.1966 0.0113  -0.0062 0.0146  339  SER   A CA  
2362 C  C   . SER   A 339 ? 0.1803 0.1926 0.2076 0.0118  -0.0065 0.0146  339  SER   A C   
2363 O  O   . SER   A 339 ? 0.1961 0.2088 0.2243 0.0119  -0.0077 0.0155  339  SER   A O   
2364 C  CB  . SER   A 339 ? 0.1745 0.1877 0.2010 0.0098  -0.0072 0.0145  339  SER   A CB  
2365 O  OG  . SER   A 339 ? 0.1840 0.1982 0.2110 0.0094  -0.0064 0.0143  339  SER   A OG  
2366 N  N   . SER   A 340 ? 0.1760 0.1865 0.2012 0.0121  -0.0055 0.0136  340  SER   A N   
2367 C  CA  . SER   A 340 ? 0.1846 0.1931 0.2082 0.0125  -0.0057 0.0134  340  SER   A CA  
2368 C  C   . SER   A 340 ? 0.1892 0.1959 0.2102 0.0115  -0.0069 0.0136  340  SER   A C   
2369 O  O   . SER   A 340 ? 0.1900 0.1966 0.2099 0.0105  -0.0073 0.0134  340  SER   A O   
2370 C  CB  . SER   A 340 ? 0.2078 0.2152 0.2300 0.0129  -0.0041 0.0123  340  SER   A CB  
2371 O  OG  . SER   A 340 ? 0.1947 0.2016 0.2149 0.0120  -0.0039 0.0117  340  SER   A OG  
2372 N  N   . ALA   A 341 ? 0.1822 0.1874 0.2022 0.0118  -0.0073 0.0137  341  ALA   A N   
2373 C  CA  . ALA   A 341 ? 0.1886 0.1917 0.2057 0.0109  -0.0083 0.0137  341  ALA   A CA  
2374 C  C   . ALA   A 341 ? 0.1850 0.1866 0.1996 0.0105  -0.0073 0.0127  341  ALA   A C   
2375 O  O   . ALA   A 341 ? 0.1929 0.1934 0.2055 0.0095  -0.0078 0.0126  341  ALA   A O   
2376 C  CB  . ALA   A 341 ? 0.2066 0.2084 0.2232 0.0115  -0.0086 0.0141  341  ALA   A CB  
2377 N  N   . SER   A 342 ? 0.1905 0.1922 0.2053 0.0111  -0.0060 0.0119  342  SER   A N   
2378 C  CA  A SER   A 342 ? 0.2040 0.2048 0.2168 0.0107  -0.0051 0.0112  342  SER   A CA  
2379 C  CA  B SER   A 342 ? 0.1995 0.2002 0.2122 0.0107  -0.0051 0.0112  342  SER   A CA  
2380 C  C   . SER   A 342 ? 0.2066 0.2084 0.2196 0.0101  -0.0049 0.0112  342  SER   A C   
2381 O  O   . SER   A 342 ? 0.2034 0.2041 0.2146 0.0096  -0.0047 0.0110  342  SER   A O   
2382 C  CB  A SER   A 342 ? 0.2384 0.2395 0.2515 0.0112  -0.0038 0.0105  342  SER   A CB  
2383 C  CB  B SER   A 342 ? 0.2242 0.2250 0.2369 0.0112  -0.0038 0.0105  342  SER   A CB  
2384 O  OG  A SER   A 342 ? 0.2744 0.2752 0.2860 0.0108  -0.0030 0.0100  342  SER   A OG  
2385 O  OG  B SER   A 342 ? 0.2310 0.2336 0.2459 0.0117  -0.0032 0.0104  342  SER   A OG  
2386 N  N   . SER   A 343 ? 0.1997 0.2036 0.2151 0.0103  -0.0050 0.0115  343  SER   A N   
2387 C  CA  A SER   A 343 ? 0.2195 0.2243 0.2353 0.0097  -0.0048 0.0116  343  SER   A CA  
2388 C  CA  B SER   A 343 ? 0.2129 0.2176 0.2285 0.0097  -0.0048 0.0115  343  SER   A CA  
2389 C  C   . SER   A 343 ? 0.2162 0.2198 0.2306 0.0087  -0.0059 0.0119  343  SER   A C   
2390 O  O   . SER   A 343 ? 0.2255 0.2283 0.2386 0.0081  -0.0055 0.0118  343  SER   A O   
2391 C  CB  A SER   A 343 ? 0.2505 0.2577 0.2692 0.0100  -0.0047 0.0119  343  SER   A CB  
2392 C  CB  B SER   A 343 ? 0.2286 0.2356 0.2468 0.0101  -0.0043 0.0117  343  SER   A CB  
2393 O  OG  A SER   A 343 ? 0.2985 0.3067 0.3178 0.0106  -0.0034 0.0114  343  SER   A OG  
2394 O  OG  B SER   A 343 ? 0.2299 0.2379 0.2499 0.0100  -0.0054 0.0124  343  SER   A OG  
2395 N  N   . LYS   A 344 ? 0.2048 0.2081 0.2193 0.0084  -0.0071 0.0125  344  LYS   A N   
2396 C  CA  . LYS   A 344 ? 0.2154 0.2175 0.2283 0.0072  -0.0083 0.0128  344  LYS   A CA  
2397 C  C   . LYS   A 344 ? 0.2137 0.2129 0.2233 0.0068  -0.0078 0.0122  344  LYS   A C   
2398 O  O   . LYS   A 344 ? 0.2241 0.2219 0.2318 0.0059  -0.0076 0.0120  344  LYS   A O   
2399 C  CB  . LYS   A 344 ? 0.2537 0.2563 0.2674 0.0070  -0.0098 0.0136  344  LYS   A CB  
2400 C  CG  . LYS   A 344 ? 0.3431 0.3446 0.3549 0.0054  -0.0111 0.0140  344  LYS   A CG  
2401 C  CD  . LYS   A 344 ? 0.4134 0.4159 0.4262 0.0051  -0.0129 0.0151  344  LYS   A CD  
2402 C  CE  . LYS   A 344 ? 0.4860 0.4901 0.4999 0.0038  -0.0140 0.0157  344  LYS   A CE  
2403 N  NZ  . LYS   A 344 ? 0.5336 0.5392 0.5486 0.0032  -0.0159 0.0170  344  LYS   A NZ  
2404 N  N   . LEU   A 345 ? 0.1995 0.1977 0.2082 0.0075  -0.0075 0.0120  345  LEU   A N   
2405 C  CA  . LEU   A 345 ? 0.2071 0.2029 0.2130 0.0072  -0.0068 0.0115  345  LEU   A CA  
2406 C  C   . LEU   A 345 ? 0.1964 0.1924 0.2021 0.0073  -0.0055 0.0111  345  LEU   A C   
2407 O  O   . LEU   A 345 ? 0.1971 0.1912 0.2008 0.0067  -0.0050 0.0110  345  LEU   A O   
2408 C  CB  . LEU   A 345 ? 0.2161 0.2115 0.2218 0.0080  -0.0066 0.0114  345  LEU   A CB  
2409 C  CG  . LEU   A 345 ? 0.2482 0.2415 0.2515 0.0080  -0.0057 0.0109  345  LEU   A CG  
2410 C  CD1 . LEU   A 345 ? 0.2588 0.2497 0.2594 0.0071  -0.0062 0.0110  345  LEU   A CD1 
2411 C  CD2 . LEU   A 345 ? 0.2675 0.2606 0.2709 0.0087  -0.0055 0.0107  345  LEU   A CD2 
2412 N  N   . GLY   A 346 ? 0.1837 0.1817 0.1914 0.0080  -0.0047 0.0110  346  GLY   A N   
2413 C  CA  . GLY   A 346 ? 0.1774 0.1759 0.1851 0.0082  -0.0035 0.0109  346  GLY   A CA  
2414 C  C   . GLY   A 346 ? 0.1795 0.1776 0.1869 0.0075  -0.0034 0.0111  346  GLY   A C   
2415 O  O   . GLY   A 346 ? 0.1885 0.1857 0.1949 0.0074  -0.0024 0.0111  346  GLY   A O   
2416 N  N   . ILE   A 347 ? 0.1657 0.1648 0.1744 0.0071  -0.0042 0.0113  347  ILE   A N   
2417 C  CA  . ILE   A 347 ? 0.1695 0.1681 0.1778 0.0062  -0.0041 0.0115  347  ILE   A CA  
2418 C  C   . ILE   A 347 ? 0.1771 0.1725 0.1823 0.0053  -0.0042 0.0113  347  ILE   A C   
2419 O  O   . ILE   A 347 ? 0.1677 0.1616 0.1716 0.0050  -0.0032 0.0113  347  ILE   A O   
2420 C  CB  . ILE   A 347 ? 0.1732 0.1734 0.1833 0.0057  -0.0052 0.0119  347  ILE   A CB  
2421 C  CG1 . ILE   A 347 ? 0.1690 0.1722 0.1822 0.0065  -0.0048 0.0120  347  ILE   A CG1 
2422 C  CG2 . ILE   A 347 ? 0.1863 0.1853 0.1954 0.0044  -0.0053 0.0120  347  ILE   A CG2 
2423 C  CD1 . ILE   A 347 ? 0.1968 0.2019 0.2122 0.0063  -0.0059 0.0125  347  ILE   A CD1 
2424 N  N   . THR   A 348 ? 0.1696 0.1638 0.1736 0.0050  -0.0052 0.0113  348  THR   A N   
2425 C  CA  . THR   A 348 ? 0.1666 0.1576 0.1673 0.0040  -0.0053 0.0111  348  THR   A CA  
2426 C  C   . THR   A 348 ? 0.1607 0.1500 0.1598 0.0045  -0.0037 0.0108  348  THR   A C   
2427 O  O   . THR   A 348 ? 0.1828 0.1697 0.1799 0.0039  -0.0028 0.0107  348  THR   A O   
2428 C  CB  . THR   A 348 ? 0.1771 0.1675 0.1768 0.0036  -0.0067 0.0112  348  THR   A CB  
2429 O  OG1 . THR   A 348 ? 0.1973 0.1900 0.1993 0.0035  -0.0081 0.0118  348  THR   A OG1 
2430 C  CG2 . THR   A 348 ? 0.1995 0.1866 0.1956 0.0023  -0.0070 0.0111  348  THR   A CG2 
2431 N  N   . MET   A 349 ? 0.1619 0.1523 0.1620 0.0056  -0.0032 0.0108  349  MET   A N   
2432 C  CA  . MET   A 349 ? 0.1581 0.1474 0.1571 0.0061  -0.0017 0.0107  349  MET   A CA  
2433 C  C   . MET   A 349 ? 0.1646 0.1546 0.1645 0.0065  -0.0004 0.0110  349  MET   A C   
2434 O  O   . MET   A 349 ? 0.1768 0.1651 0.1753 0.0066  0.0009  0.0111  349  MET   A O   
2435 C  CB  . MET   A 349 ? 0.1649 0.1554 0.1647 0.0070  -0.0017 0.0107  349  MET   A CB  
2436 C  CG  . MET   A 349 ? 0.1803 0.1697 0.1790 0.0067  -0.0028 0.0105  349  MET   A CG  
2437 S  SD  . MET   A 349 ? 0.2261 0.2117 0.2211 0.0059  -0.0027 0.0104  349  MET   A SD  
2438 C  CE  . MET   A 349 ? 0.2362 0.2217 0.2309 0.0068  -0.0015 0.0103  349  MET   A CE  
2439 N  N   . THR   A 350 ? 0.1631 0.1557 0.1654 0.0068  -0.0006 0.0112  350  THR   A N   
2440 C  CA  . THR   A 350 ? 0.1563 0.1497 0.1595 0.0071  0.0006  0.0116  350  THR   A CA  
2441 C  C   . THR   A 350 ? 0.1625 0.1535 0.1642 0.0063  0.0011  0.0116  350  THR   A C   
2442 O  O   . THR   A 350 ? 0.1607 0.1504 0.1616 0.0066  0.0026  0.0119  350  THR   A O   
2443 C  CB  . THR   A 350 ? 0.1593 0.1559 0.1652 0.0075  0.0003  0.0117  350  THR   A CB  
2444 O  OG1 . THR   A 350 ? 0.1694 0.1677 0.1763 0.0081  0.0001  0.0116  350  THR   A OG1 
2445 C  CG2 . THR   A 350 ? 0.1570 0.1546 0.1638 0.0079  0.0015  0.0122  350  THR   A CG2 
2446 N  N   . VAL   A 351 ? 0.1600 0.1503 0.1611 0.0053  0.0000  0.0113  351  VAL   A N   
2447 C  CA  . VAL   A 351 ? 0.1619 0.1495 0.1611 0.0042  0.0004  0.0112  351  VAL   A CA  
2448 C  C   . VAL   A 351 ? 0.1656 0.1496 0.1617 0.0040  0.0014  0.0110  351  VAL   A C   
2449 O  O   . VAL   A 351 ? 0.1805 0.1622 0.1752 0.0039  0.0029  0.0111  351  VAL   A O   
2450 C  CB  . VAL   A 351 ? 0.1744 0.1621 0.1734 0.0028  -0.0013 0.0111  351  VAL   A CB  
2451 C  CG1 . VAL   A 351 ? 0.1951 0.1794 0.1913 0.0013  -0.0010 0.0108  351  VAL   A CG1 
2452 C  CG2 . VAL   A 351 ? 0.1784 0.1695 0.1807 0.0031  -0.0018 0.0114  351  VAL   A CG2 
2453 N  N   . ALA   A 352 ? 0.1695 0.1529 0.1645 0.0041  0.0007  0.0108  352  ALA   A N   
2454 C  CA  . ALA   A 352 ? 0.1723 0.1524 0.1643 0.0039  0.0018  0.0105  352  ALA   A CA  
2455 C  C   . ALA   A 352 ? 0.1718 0.1518 0.1644 0.0052  0.0038  0.0110  352  ALA   A C   
2456 O  O   . ALA   A 352 ? 0.1743 0.1514 0.1649 0.0051  0.0053  0.0110  352  ALA   A O   
2457 C  CB  . ALA   A 352 ? 0.1801 0.1599 0.1711 0.0039  0.0007  0.0103  352  ALA   A CB  
2458 N  N   . HIS   A 353 ? 0.1601 0.1435 0.1555 0.0063  0.0038  0.0114  353  HIS   A N   
2459 C  CA  . HIS   A 353 ? 0.1630 0.1472 0.1595 0.0074  0.0054  0.0121  353  HIS   A CA  
2460 C  C   . HIS   A 353 ? 0.1618 0.1453 0.1585 0.0075  0.0068  0.0126  353  HIS   A C   
2461 O  O   . HIS   A 353 ? 0.1712 0.1526 0.1669 0.0080  0.0086  0.0130  353  HIS   A O   
2462 C  CB  . HIS   A 353 ? 0.1671 0.1553 0.1663 0.0082  0.0048  0.0124  353  HIS   A CB  
2463 C  CG  . HIS   A 353 ? 0.1529 0.1426 0.1533 0.0092  0.0062  0.0132  353  HIS   A CG  
2464 N  ND1 . HIS   A 353 ? 0.1765 0.1668 0.1769 0.0096  0.0063  0.0133  353  HIS   A ND1 
2465 C  CD2 . HIS   A 353 ? 0.1594 0.1503 0.1612 0.0099  0.0074  0.0141  353  HIS   A CD2 
2466 C  CE1 . HIS   A 353 ? 0.1741 0.1660 0.1758 0.0104  0.0075  0.0143  353  HIS   A CE1 
2467 N  NE2 . HIS   A 353 ? 0.1710 0.1634 0.1737 0.0107  0.0082  0.0149  353  HIS   A NE2 
2468 N  N   . GLU   A 354 ? 0.1587 0.1436 0.1567 0.0072  0.0061  0.0126  354  GLU   A N   
2469 C  CA  . GLU   A 354 ? 0.1661 0.1502 0.1644 0.0073  0.0075  0.0131  354  GLU   A CA  
2470 C  C   . GLU   A 354 ? 0.1744 0.1540 0.1697 0.0064  0.0085  0.0127  354  GLU   A C   
2471 O  O   . GLU   A 354 ? 0.1817 0.1596 0.1766 0.0069  0.0104  0.0132  354  GLU   A O   
2472 C  CB  . GLU   A 354 ? 0.1693 0.1558 0.1696 0.0069  0.0065  0.0131  354  GLU   A CB  
2473 C  CG  . GLU   A 354 ? 0.1587 0.1493 0.1617 0.0077  0.0057  0.0134  354  GLU   A CG  
2474 C  CD  . GLU   A 354 ? 0.1874 0.1796 0.1915 0.0089  0.0069  0.0143  354  GLU   A CD  
2475 O  OE1 . GLU   A 354 ? 0.1979 0.1892 0.2020 0.0094  0.0085  0.0150  354  GLU   A OE1 
2476 O  OE2 . GLU   A 354 ? 0.1870 0.1813 0.1920 0.0093  0.0063  0.0142  354  GLU   A OE2 
2477 N  N   . LEU   A 355 ? 0.1772 0.1548 0.1702 0.0050  0.0073  0.0118  355  LEU   A N   
2478 C  CA  . LEU   A 355 ? 0.1780 0.1510 0.1676 0.0039  0.0082  0.0113  355  LEU   A CA  
2479 C  C   . LEU   A 355 ? 0.1818 0.1521 0.1695 0.0046  0.0099  0.0114  355  LEU   A C   
2480 O  O   . LEU   A 355 ? 0.1847 0.1515 0.1704 0.0044  0.0119  0.0114  355  LEU   A O   
2481 C  CB  . LEU   A 355 ? 0.1768 0.1486 0.1645 0.0021  0.0064  0.0105  355  LEU   A CB  
2482 C  CG  . LEU   A 355 ? 0.1899 0.1641 0.1795 0.0013  0.0050  0.0106  355  LEU   A CG  
2483 C  CD1 . LEU   A 355 ? 0.1947 0.1680 0.1825 -0.0006 0.0031  0.0100  355  LEU   A CD1 
2484 C  CD2 . LEU   A 355 ? 0.2073 0.1806 0.1974 0.0013  0.0066  0.0109  355  LEU   A CD2 
2485 N  N   . ALA   A 356 ? 0.1815 0.1534 0.1698 0.0053  0.0095  0.0115  356  ALA   A N   
2486 C  CA  . ALA   A 356 ? 0.1791 0.1488 0.1660 0.0061  0.0113  0.0118  356  ALA   A CA  
2487 C  C   . ALA   A 356 ? 0.1770 0.1469 0.1655 0.0075  0.0136  0.0128  356  ALA   A C   
2488 O  O   . ALA   A 356 ? 0.1809 0.1476 0.1676 0.0078  0.0157  0.0130  356  ALA   A O   
2489 C  CB  . ALA   A 356 ? 0.1761 0.1482 0.1642 0.0069  0.0105  0.0119  356  ALA   A CB  
2490 N  N   . HIS   A 357 ? 0.1651 0.1389 0.1569 0.0083  0.0132  0.0136  357  HIS   A N   
2491 C  CA  . HIS   A 357 ? 0.1662 0.1408 0.1598 0.0096  0.0151  0.0148  357  HIS   A CA  
2492 C  C   . HIS   A 357 ? 0.1752 0.1459 0.1671 0.0093  0.0169  0.0149  357  HIS   A C   
2493 O  O   . HIS   A 357 ? 0.1788 0.1491 0.1716 0.0105  0.0191  0.0160  357  HIS   A O   
2494 C  CB  . HIS   A 357 ? 0.1638 0.1431 0.1609 0.0102  0.0142  0.0156  357  HIS   A CB  
2495 C  CG  . HIS   A 357 ? 0.1504 0.1336 0.1497 0.0112  0.0136  0.0162  357  HIS   A CG  
2496 N  ND1 . HIS   A 357 ? 0.1534 0.1369 0.1532 0.0122  0.0149  0.0171  357  HIS   A ND1 
2497 C  CD2 . HIS   A 357 ? 0.1545 0.1416 0.1559 0.0111  0.0119  0.0161  357  HIS   A CD2 
2498 C  CE1 . HIS   A 357 ? 0.1627 0.1503 0.1647 0.0126  0.0139  0.0175  357  HIS   A CE1 
2499 N  NE2 . HIS   A 357 ? 0.1529 0.1425 0.1556 0.0119  0.0121  0.0169  357  HIS   A NE2 
2500 N  N   . GLN   A 358 ? 0.1701 0.1382 0.1597 0.0076  0.0162  0.0138  358  GLN   A N   
2501 C  CA  . GLN   A 358 ? 0.1824 0.1464 0.1700 0.0072  0.0181  0.0137  358  GLN   A CA  
2502 C  C   . GLN   A 358 ? 0.1920 0.1520 0.1773 0.0077  0.0206  0.0139  358  GLN   A C   
2503 O  O   . GLN   A 358 ? 0.1992 0.1565 0.1840 0.0083  0.0230  0.0144  358  GLN   A O   
2504 C  CB  . GLN   A 358 ? 0.1850 0.1468 0.1702 0.0050  0.0169  0.0125  358  GLN   A CB  
2505 C  CG  . GLN   A 358 ? 0.1803 0.1463 0.1680 0.0045  0.0143  0.0124  358  GLN   A CG  
2506 C  CD  . GLN   A 358 ? 0.1897 0.1590 0.1808 0.0057  0.0148  0.0135  358  GLN   A CD  
2507 O  OE1 . GLN   A 358 ? 0.1900 0.1575 0.1808 0.0054  0.0160  0.0138  358  GLN   A OE1 
2508 N  NE2 . GLN   A 358 ? 0.1835 0.1573 0.1777 0.0068  0.0138  0.0141  358  GLN   A NE2 
2509 N  N   . TRP   A 359 ? 0.1882 0.1478 0.1723 0.0077  0.0203  0.0135  359  TRP   A N   
2510 C  CA  . TRP   A 359 ? 0.1945 0.1505 0.1766 0.0084  0.0227  0.0136  359  TRP   A CA  
2511 C  C   . TRP   A 359 ? 0.1955 0.1552 0.1810 0.0104  0.0234  0.0151  359  TRP   A C   
2512 O  O   . TRP   A 359 ? 0.2047 0.1638 0.1913 0.0119  0.0259  0.0163  359  TRP   A O   
2513 C  CB  . TRP   A 359 ? 0.2070 0.1601 0.1852 0.0069  0.0217  0.0123  359  TRP   A CB  
2514 C  CG  . TRP   A 359 ? 0.2127 0.1615 0.1871 0.0047  0.0215  0.0110  359  TRP   A CG  
2515 C  CD1 . TRP   A 359 ? 0.2288 0.1719 0.1992 0.0039  0.0237  0.0103  359  TRP   A CD1 
2516 C  CD2 . TRP   A 359 ? 0.2072 0.1572 0.1813 0.0030  0.0189  0.0102  359  TRP   A CD2 
2517 N  NE1 . TRP   A 359 ? 0.2292 0.1698 0.1967 0.0016  0.0225  0.0092  359  TRP   A NE1 
2518 C  CE2 . TRP   A 359 ? 0.2349 0.1799 0.2047 0.0010  0.0195  0.0092  359  TRP   A CE2 
2519 C  CE3 . TRP   A 359 ? 0.2106 0.1655 0.1877 0.0029  0.0162  0.0103  359  TRP   A CE3 
2520 C  CZ2 . TRP   A 359 ? 0.2350 0.1800 0.2037 -0.0011 0.0173  0.0084  359  TRP   A CZ2 
2521 C  CZ3 . TRP   A 359 ? 0.2171 0.1720 0.1933 0.0010  0.0142  0.0096  359  TRP   A CZ3 
2522 C  CH2 . TRP   A 359 ? 0.2237 0.1739 0.1958 -0.0010 0.0147  0.0087  359  TRP   A CH2 
2523 N  N   . PHE   A 360 ? 0.1879 0.1516 0.1751 0.0105  0.0212  0.0150  360  PHE   A N   
2524 C  CA  . PHE   A 360 ? 0.1852 0.1527 0.1755 0.0121  0.0216  0.0163  360  PHE   A CA  
2525 C  C   . PHE   A 360 ? 0.1764 0.1485 0.1704 0.0130  0.0210  0.0175  360  PHE   A C   
2526 O  O   . PHE   A 360 ? 0.1783 0.1542 0.1741 0.0127  0.0189  0.0173  360  PHE   A O   
2527 C  CB  . PHE   A 360 ? 0.1858 0.1550 0.1759 0.0116  0.0197  0.0157  360  PHE   A CB  
2528 C  CG  . PHE   A 360 ? 0.2013 0.1664 0.1880 0.0111  0.0207  0.0150  360  PHE   A CG  
2529 C  CD1 . PHE   A 360 ? 0.2019 0.1659 0.1887 0.0123  0.0231  0.0159  360  PHE   A CD1 
2530 C  CD2 . PHE   A 360 ? 0.2243 0.1868 0.2077 0.0095  0.0193  0.0135  360  PHE   A CD2 
2531 C  CE1 . PHE   A 360 ? 0.2174 0.1777 0.2011 0.0119  0.0241  0.0152  360  PHE   A CE1 
2532 C  CE2 . PHE   A 360 ? 0.2401 0.1989 0.2202 0.0089  0.0202  0.0128  360  PHE   A CE2 
2533 C  CZ  . PHE   A 360 ? 0.2344 0.1918 0.2145 0.0101  0.0227  0.0136  360  PHE   A CZ  
2534 N  N   . GLY   A 361 ? 0.1826 0.1540 0.1777 0.0139  0.0230  0.0186  361  GLY   A N   
2535 C  CA  . GLY   A 361 ? 0.1829 0.1585 0.1815 0.0149  0.0228  0.0201  361  GLY   A CA  
2536 C  C   . GLY   A 361 ? 0.1798 0.1532 0.1783 0.0152  0.0244  0.0206  361  GLY   A C   
2537 O  O   . GLY   A 361 ? 0.1821 0.1573 0.1831 0.0166  0.0259  0.0223  361  GLY   A O   
2538 N  N   . ASN   A 362 ? 0.1755 0.1452 0.1711 0.0137  0.0241  0.0192  362  ASN   A N   
2539 C  CA  . ASN   A 362 ? 0.1763 0.1437 0.1716 0.0136  0.0256  0.0195  362  ASN   A CA  
2540 C  C   . ASN   A 362 ? 0.1893 0.1511 0.1820 0.0140  0.0286  0.0196  362  ASN   A C   
2541 O  O   . ASN   A 362 ? 0.2065 0.1677 0.2006 0.0154  0.0309  0.0211  362  ASN   A O   
2542 C  CB  . ASN   A 362 ? 0.1800 0.1465 0.1738 0.0118  0.0237  0.0180  362  ASN   A CB  
2543 C  CG  . ASN   A 362 ? 0.1824 0.1541 0.1788 0.0115  0.0211  0.0180  362  ASN   A CG  
2544 O  OD1 . ASN   A 362 ? 0.1774 0.1532 0.1763 0.0126  0.0204  0.0188  362  ASN   A OD1 
2545 N  ND2 . ASN   A 362 ? 0.1808 0.1524 0.1767 0.0101  0.0196  0.0171  362  ASN   A ND2 
2546 N  N   . LEU   A 363 ? 0.1890 0.1467 0.1780 0.0127  0.0287  0.0180  363  LEU   A N   
2547 C  CA  . LEU   A 363 ? 0.1954 0.1473 0.1814 0.0128  0.0317  0.0179  363  LEU   A CA  
2548 C  C   . LEU   A 363 ? 0.2051 0.1581 0.1931 0.0149  0.0337  0.0194  363  LEU   A C   
2549 O  O   . LEU   A 363 ? 0.2222 0.1729 0.2105 0.0163  0.0367  0.0206  363  LEU   A O   
2550 C  CB  . LEU   A 363 ? 0.2119 0.1599 0.1934 0.0108  0.0309  0.0159  363  LEU   A CB  
2551 C  CG  . LEU   A 363 ? 0.2356 0.1771 0.2132 0.0106  0.0339  0.0154  363  LEU   A CG  
2552 C  CD1 . LEU   A 363 ? 0.2530 0.1904 0.2290 0.0101  0.0357  0.0152  363  LEU   A CD1 
2553 C  CD2 . LEU   A 363 ? 0.2460 0.1845 0.2193 0.0086  0.0326  0.0135  363  LEU   A CD2 
2554 N  N   . VAL   A 364 ? 0.1899 0.1465 0.1793 0.0153  0.0321  0.0196  364  VAL   A N   
2555 C  CA  . VAL   A 364 ? 0.1909 0.1494 0.1825 0.0171  0.0337  0.0211  364  VAL   A CA  
2556 C  C   . VAL   A 364 ? 0.1902 0.1555 0.1861 0.0178  0.0316  0.0223  364  VAL   A C   
2557 O  O   . VAL   A 364 ? 0.2061 0.1740 0.2021 0.0167  0.0288  0.0213  364  VAL   A O   
2558 C  CB  . VAL   A 364 ? 0.2116 0.1681 0.2008 0.0167  0.0338  0.0202  364  VAL   A CB  
2559 C  CG1 . VAL   A 364 ? 0.2306 0.1902 0.2230 0.0186  0.0352  0.0221  364  VAL   A CG1 
2560 C  CG2 . VAL   A 364 ? 0.2243 0.1737 0.2089 0.0157  0.0360  0.0190  364  VAL   A CG2 
2561 N  N   . THR   A 365 ? 0.1887 0.1569 0.1881 0.0197  0.0330  0.0246  365  THR   A N   
2562 C  CA  . THR   A 365 ? 0.1812 0.1558 0.1845 0.0202  0.0312  0.0258  365  THR   A CA  
2563 C  C   . THR   A 365 ? 0.1886 0.1666 0.1947 0.0217  0.0321  0.0277  365  THR   A C   
2564 O  O   . THR   A 365 ? 0.1886 0.1645 0.1950 0.0231  0.0349  0.0289  365  THR   A O   
2565 C  CB  . THR   A 365 ? 0.1917 0.1673 0.1967 0.0208  0.0317  0.0270  365  THR   A CB  
2566 O  OG1 . THR   A 365 ? 0.1870 0.1588 0.1893 0.0194  0.0314  0.0253  365  THR   A OG1 
2567 C  CG2 . THR   A 365 ? 0.1847 0.1667 0.1932 0.0211  0.0297  0.0281  365  THR   A CG2 
2568 N  N   . MET   A 366 ? 0.1765 0.1598 0.1848 0.0216  0.0299  0.0281  366  MET   A N   
2569 C  CA  . MET   A 366 ? 0.1903 0.1773 0.2017 0.0229  0.0307  0.0302  366  MET   A CA  
2570 C  C   . MET   A 366 ? 0.1837 0.1724 0.1981 0.0247  0.0327  0.0328  366  MET   A C   
2571 O  O   . MET   A 366 ? 0.1802 0.1694 0.1952 0.0247  0.0323  0.0331  366  MET   A O   
2572 C  CB  . MET   A 366 ? 0.1945 0.1868 0.2076 0.0222  0.0281  0.0301  366  MET   A CB  
2573 C  CG  . MET   A 366 ? 0.1937 0.1906 0.2091 0.0220  0.0264  0.0309  366  MET   A CG  
2574 S  SD  . MET   A 366 ? 0.1876 0.1826 0.2006 0.0204  0.0243  0.0285  366  MET   A SD  
2575 C  CE  . MET   A 366 ? 0.1945 0.1916 0.2098 0.0212  0.0248  0.0303  366  MET   A CE  
2576 N  N   A GLU   A 367 ? 0.1791 0.1685 0.1955 0.0262  0.0349  0.0348  367  GLU   A N   
2577 N  N   B GLU   A 367 ? 0.1756 0.1651 0.1920 0.0262  0.0348  0.0347  367  GLU   A N   
2578 C  CA  A GLU   A 367 ? 0.1808 0.1722 0.2005 0.0281  0.0368  0.0376  367  GLU   A CA  
2579 C  CA  B GLU   A 367 ? 0.1743 0.1656 0.1940 0.0281  0.0368  0.0376  367  GLU   A CA  
2580 C  C   A GLU   A 367 ? 0.1867 0.1847 0.2097 0.0280  0.0346  0.0391  367  GLU   A C   
2581 C  C   B GLU   A 367 ? 0.1801 0.1782 0.2032 0.0282  0.0348  0.0393  367  GLU   A C   
2582 O  O   A GLU   A 367 ? 0.1935 0.1926 0.2180 0.0288  0.0351  0.0405  367  GLU   A O   
2583 O  O   B GLU   A 367 ? 0.1793 0.1787 0.2044 0.0291  0.0355  0.0410  367  GLU   A O   
2584 C  CB  A GLU   A 367 ? 0.2068 0.1983 0.2283 0.0298  0.0394  0.0396  367  GLU   A CB  
2585 C  CB  B GLU   A 367 ? 0.1904 0.1817 0.2117 0.0297  0.0394  0.0394  367  GLU   A CB  
2586 C  CG  A GLU   A 367 ? 0.2456 0.2384 0.2705 0.0320  0.0419  0.0427  367  GLU   A CG  
2587 C  CG  B GLU   A 367 ? 0.2416 0.2348 0.2665 0.0319  0.0418  0.0427  367  GLU   A CG  
2588 C  CD  A GLU   A 367 ? 0.3247 0.3249 0.3543 0.0328  0.0408  0.0456  367  GLU   A CD  
2589 C  CD  B GLU   A 367 ? 0.3175 0.3091 0.3436 0.0336  0.0449  0.0442  367  GLU   A CD  
2590 O  OE1 A GLU   A 367 ? 0.3525 0.3546 0.3846 0.0340  0.0416  0.0478  367  GLU   A OE1 
2591 O  OE1 B GLU   A 367 ? 0.3322 0.3272 0.3598 0.0336  0.0443  0.0448  367  GLU   A OE1 
2592 O  OE2 A GLU   A 367 ? 0.3588 0.3631 0.3896 0.0322  0.0391  0.0457  367  GLU   A OE2 
2593 O  OE2 B GLU   A 367 ? 0.3678 0.3544 0.3928 0.0348  0.0481  0.0446  367  GLU   A OE2 
2594 N  N   . TRP   A 368 ? 0.1754 0.1776 0.1992 0.0271  0.0323  0.0388  368  TRP   A N   
2595 C  CA  . TRP   A 368 ? 0.1675 0.1759 0.1940 0.0268  0.0302  0.0400  368  TRP   A CA  
2596 C  C   . TRP   A 368 ? 0.1769 0.1870 0.2019 0.0248  0.0273  0.0379  368  TRP   A C   
2597 O  O   . TRP   A 368 ? 0.1712 0.1787 0.1941 0.0242  0.0271  0.0362  368  TRP   A O   
2598 C  CB  . TRP   A 368 ? 0.1744 0.1876 0.2050 0.0283  0.0312  0.0434  368  TRP   A CB  
2599 C  CG  . TRP   A 368 ? 0.1696 0.1892 0.2028 0.0278  0.0291  0.0449  368  TRP   A CG  
2600 C  CD1 . TRP   A 368 ? 0.1870 0.2118 0.2219 0.0271  0.0275  0.0458  368  TRP   A CD1 
2601 C  CD2 . TRP   A 368 ? 0.1639 0.1854 0.1979 0.0277  0.0283  0.0456  368  TRP   A CD2 
2602 N  NE1 . TRP   A 368 ? 0.1771 0.2068 0.2135 0.0264  0.0255  0.0467  368  TRP   A NE1 
2603 C  CE2 . TRP   A 368 ? 0.1695 0.1972 0.2054 0.0269  0.0261  0.0468  368  TRP   A CE2 
2604 C  CE3 . TRP   A 368 ? 0.1644 0.1827 0.1974 0.0282  0.0292  0.0454  368  TRP   A CE3 
2605 C  CZ2 . TRP   A 368 ? 0.1714 0.2024 0.2084 0.0266  0.0249  0.0478  368  TRP   A CZ2 
2606 C  CZ3 . TRP   A 368 ? 0.1781 0.1997 0.2123 0.0279  0.0280  0.0464  368  TRP   A CZ3 
2607 C  CH2 . TRP   A 368 ? 0.1648 0.1926 0.2008 0.0271  0.0258  0.0475  368  TRP   A CH2 
2608 N  N   . TRP   A 369 ? 0.1663 0.1807 0.1925 0.0240  0.0251  0.0382  369  TRP   A N   
2609 C  CA  . TRP   A 369 ? 0.1586 0.1744 0.1834 0.0222  0.0225  0.0361  369  TRP   A CA  
2610 C  C   . TRP   A 369 ? 0.1648 0.1826 0.1898 0.0217  0.0217  0.0360  369  TRP   A C   
2611 O  O   . TRP   A 369 ? 0.1626 0.1799 0.1858 0.0202  0.0200  0.0339  369  TRP   A O   
2612 C  CB  . TRP   A 369 ? 0.1589 0.1788 0.1849 0.0216  0.0207  0.0367  369  TRP   A CB  
2613 C  CG  . TRP   A 369 ? 0.1524 0.1703 0.1781 0.0221  0.0214  0.0368  369  TRP   A CG  
2614 C  CD1 . TRP   A 369 ? 0.1680 0.1875 0.1959 0.0234  0.0227  0.0392  369  TRP   A CD1 
2615 C  CD2 . TRP   A 369 ? 0.1499 0.1638 0.1730 0.0213  0.0210  0.0345  369  TRP   A CD2 
2616 N  NE1 . TRP   A 369 ? 0.1644 0.1811 0.1911 0.0233  0.0231  0.0385  369  TRP   A NE1 
2617 C  CE2 . TRP   A 369 ? 0.1600 0.1733 0.1839 0.0221  0.0221  0.0356  369  TRP   A CE2 
2618 C  CE3 . TRP   A 369 ? 0.1632 0.1741 0.1835 0.0201  0.0199  0.0318  369  TRP   A CE3 
2619 C  CZ2 . TRP   A 369 ? 0.1603 0.1700 0.1821 0.0215  0.0220  0.0340  369  TRP   A CZ2 
2620 C  CZ3 . TRP   A 369 ? 0.1660 0.1737 0.1845 0.0195  0.0197  0.0303  369  TRP   A CZ3 
2621 C  CH2 . TRP   A 369 ? 0.1761 0.1833 0.1954 0.0202  0.0207  0.0314  369  TRP   A CH2 
2622 N  N   . ASN   A 370 ? 0.1584 0.1781 0.1857 0.0227  0.0232  0.0382  370  ASN   A N   
2623 C  CA  . ASN   A 370 ? 0.1593 0.1805 0.1868 0.0222  0.0227  0.0380  370  ASN   A CA  
2624 C  C   . ASN   A 370 ? 0.1715 0.1876 0.1956 0.0215  0.0228  0.0354  370  ASN   A C   
2625 O  O   . ASN   A 370 ? 0.1744 0.1911 0.1976 0.0204  0.0216  0.0343  370  ASN   A O   
2626 C  CB  . ASN   A 370 ? 0.1680 0.1917 0.1986 0.0236  0.0246  0.0409  370  ASN   A CB  
2627 C  CG  . ASN   A 370 ? 0.2277 0.2469 0.2580 0.0254  0.0276  0.0415  370  ASN   A CG  
2628 O  OD1 . ASN   A 370 ? 0.2290 0.2450 0.2583 0.0260  0.0286  0.0411  370  ASN   A OD1 
2629 N  ND2 . ASN   A 370 ? 0.2597 0.2786 0.2909 0.0261  0.0292  0.0424  370  ASN   A ND2 
2630 N  N   . ASP   A 371 ? 0.1676 0.1785 0.1897 0.0221  0.0243  0.0345  371  ASP   A N   
2631 C  CA  . ASP   A 371 ? 0.1642 0.1698 0.1827 0.0215  0.0246  0.0322  371  ASP   A CA  
2632 C  C   . ASP   A 371 ? 0.1695 0.1724 0.1854 0.0204  0.0231  0.0299  371  ASP   A C   
2633 O  O   . ASP   A 371 ? 0.1758 0.1738 0.1889 0.0201  0.0237  0.0284  371  ASP   A O   
2634 C  CB  . ASP   A 371 ? 0.1866 0.1880 0.2044 0.0228  0.0275  0.0327  371  ASP   A CB  
2635 C  CG  . ASP   A 371 ? 0.2160 0.2196 0.2361 0.0238  0.0290  0.0347  371  ASP   A CG  
2636 O  OD1 . ASP   A 371 ? 0.2191 0.2264 0.2403 0.0230  0.0275  0.0348  371  ASP   A OD1 
2637 O  OD2 . ASP   A 371 ? 0.2082 0.2097 0.2290 0.0253  0.0318  0.0361  371  ASP   A OD2 
2638 N  N   . LEU   A 372 ? 0.1588 0.1649 0.1756 0.0197  0.0212  0.0298  372  LEU   A N   
2639 C  CA  . LEU   A 372 ? 0.1598 0.1638 0.1745 0.0186  0.0197  0.0277  372  LEU   A CA  
2640 C  C   . LEU   A 372 ? 0.1647 0.1655 0.1765 0.0175  0.0188  0.0255  372  LEU   A C   
2641 O  O   . LEU   A 372 ? 0.1691 0.1668 0.1788 0.0169  0.0183  0.0240  372  LEU   A O   
2642 C  CB  . LEU   A 372 ? 0.1687 0.1771 0.1848 0.0179  0.0177  0.0278  372  LEU   A CB  
2643 C  CG  . LEU   A 372 ? 0.1621 0.1691 0.1765 0.0168  0.0161  0.0258  372  LEU   A CG  
2644 C  CD1 . LEU   A 372 ? 0.1628 0.1668 0.1765 0.0172  0.0171  0.0257  372  LEU   A CD1 
2645 C  CD2 . LEU   A 372 ? 0.1703 0.1814 0.1859 0.0160  0.0143  0.0258  372  LEU   A CD2 
2646 N  N   . TRP   A 373 ? 0.1686 0.1703 0.1803 0.0173  0.0186  0.0255  373  TRP   A N   
2647 C  CA  . TRP   A 373 ? 0.1637 0.1624 0.1727 0.0163  0.0177  0.0235  373  TRP   A CA  
2648 C  C   . TRP   A 373 ? 0.1793 0.1726 0.1856 0.0164  0.0191  0.0226  373  TRP   A C   
2649 O  O   . TRP   A 373 ? 0.1698 0.1604 0.1735 0.0154  0.0181  0.0209  373  TRP   A O   
2650 C  CB  . TRP   A 373 ? 0.1653 0.1657 0.1747 0.0161  0.0175  0.0237  373  TRP   A CB  
2651 C  CG  . TRP   A 373 ? 0.1694 0.1678 0.1786 0.0169  0.0197  0.0246  373  TRP   A CG  
2652 C  CD1 . TRP   A 373 ? 0.1681 0.1680 0.1796 0.0182  0.0216  0.0267  373  TRP   A CD1 
2653 C  CD2 . TRP   A 373 ? 0.1716 0.1657 0.1780 0.0166  0.0203  0.0234  373  TRP   A CD2 
2654 N  NE1 . TRP   A 373 ? 0.1848 0.1815 0.1951 0.0188  0.0236  0.0269  373  TRP   A NE1 
2655 C  CE2 . TRP   A 373 ? 0.1829 0.1761 0.1899 0.0177  0.0228  0.0248  373  TRP   A CE2 
2656 C  CE3 . TRP   A 373 ? 0.1971 0.1883 0.2004 0.0155  0.0191  0.0214  373  TRP   A CE3 
2657 C  CZ2 . TRP   A 373 ? 0.1971 0.1861 0.2015 0.0177  0.0241  0.0241  373  TRP   A CZ2 
2658 C  CZ3 . TRP   A 373 ? 0.2190 0.2063 0.2198 0.0154  0.0202  0.0208  373  TRP   A CZ3 
2659 C  CH2 . TRP   A 373 ? 0.2121 0.1983 0.2133 0.0164  0.0227  0.0221  373  TRP   A CH2 
2660 N  N   . LEU   A 374 ? 0.1745 0.1662 0.1812 0.0175  0.0214  0.0238  374  LEU   A N   
2661 C  CA  . LEU   A 374 ? 0.1802 0.1663 0.1838 0.0174  0.0228  0.0228  374  LEU   A CA  
2662 C  C   . LEU   A 374 ? 0.1832 0.1672 0.1850 0.0164  0.0216  0.0214  374  LEU   A C   
2663 O  O   . LEU   A 374 ? 0.1857 0.1655 0.1843 0.0156  0.0216  0.0200  374  LEU   A O   
2664 C  CB  . LEU   A 374 ? 0.1761 0.1607 0.1806 0.0189  0.0258  0.0245  374  LEU   A CB  
2665 C  CG  . LEU   A 374 ? 0.1881 0.1740 0.1942 0.0199  0.0274  0.0259  374  LEU   A CG  
2666 C  CD1 . LEU   A 374 ? 0.2015 0.1865 0.2091 0.0216  0.0303  0.0279  374  LEU   A CD1 
2667 C  CD2 . LEU   A 374 ? 0.1991 0.1811 0.2020 0.0193  0.0279  0.0246  374  LEU   A CD2 
2668 N  N   . ASN   A 375 ? 0.1763 0.1633 0.1801 0.0165  0.0206  0.0219  375  ASN   A N   
2669 C  CA  . ASN   A 375 ? 0.1575 0.1434 0.1601 0.0155  0.0193  0.0206  375  ASN   A CA  
2670 C  C   . ASN   A 375 ? 0.1723 0.1597 0.1744 0.0144  0.0168  0.0193  375  ASN   A C   
2671 O  O   . ASN   A 375 ? 0.1820 0.1668 0.1818 0.0133  0.0158  0.0178  375  ASN   A O   
2672 C  CB  . ASN   A 375 ? 0.1575 0.1465 0.1627 0.0160  0.0192  0.0218  375  ASN   A CB  
2673 C  CG  . ASN   A 375 ? 0.1934 0.1805 0.1990 0.0170  0.0215  0.0229  375  ASN   A CG  
2674 O  OD1 . ASN   A 375 ? 0.1889 0.1730 0.1935 0.0177  0.0236  0.0234  375  ASN   A OD1 
2675 N  ND2 . ASN   A 375 ? 0.1772 0.1659 0.1842 0.0171  0.0211  0.0235  375  ASN   A ND2 
2676 N  N   . GLU   A 376 ? 0.1604 0.1521 0.1646 0.0145  0.0157  0.0198  376  GLU   A N   
2677 C  CA  . GLU   A 376 ? 0.1649 0.1581 0.1690 0.0136  0.0135  0.0186  376  GLU   A CA  
2678 C  C   . GLU   A 376 ? 0.1693 0.1609 0.1715 0.0129  0.0127  0.0176  376  GLU   A C   
2679 O  O   . GLU   A 376 ? 0.1698 0.1606 0.1709 0.0121  0.0112  0.0163  376  GLU   A O   
2680 C  CB  . GLU   A 376 ? 0.1626 0.1607 0.1693 0.0137  0.0126  0.0194  376  GLU   A CB  
2681 C  CG  . GLU   A 376 ? 0.1581 0.1579 0.1665 0.0142  0.0130  0.0204  376  GLU   A CG  
2682 C  CD  . GLU   A 376 ? 0.1806 0.1786 0.1880 0.0136  0.0122  0.0193  376  GLU   A CD  
2683 O  OE1 . GLU   A 376 ? 0.1590 0.1553 0.1648 0.0127  0.0111  0.0178  376  GLU   A OE1 
2684 O  OE2 . GLU   A 376 ? 0.1760 0.1744 0.1843 0.0139  0.0128  0.0200  376  GLU   A OE2 
2685 N  N   . GLY   A 377 ? 0.1651 0.1566 0.1673 0.0134  0.0138  0.0182  377  GLY   A N   
2686 C  CA  . GLY   A 377 ? 0.1696 0.1593 0.1699 0.0128  0.0133  0.0172  377  GLY   A CA  
2687 C  C   . GLY   A 377 ? 0.1720 0.1571 0.1691 0.0122  0.0134  0.0161  377  GLY   A C   
2688 O  O   . GLY   A 377 ? 0.1763 0.1601 0.1717 0.0113  0.0120  0.0150  377  GLY   A O   
2689 N  N   . PHE   A 378 ? 0.1806 0.1631 0.1768 0.0125  0.0150  0.0164  378  PHE   A N   
2690 C  CA  . PHE   A 378 ? 0.1903 0.1683 0.1833 0.0117  0.0152  0.0154  378  PHE   A CA  
2691 C  C   . PHE   A 378 ? 0.1850 0.1630 0.1775 0.0107  0.0133  0.0144  378  PHE   A C   
2692 O  O   . PHE   A 378 ? 0.1870 0.1628 0.1772 0.0097  0.0123  0.0134  378  PHE   A O   
2693 C  CB  . PHE   A 378 ? 0.1981 0.1729 0.1900 0.0122  0.0176  0.0159  378  PHE   A CB  
2694 C  CG  . PHE   A 378 ? 0.2148 0.1863 0.2044 0.0124  0.0193  0.0158  378  PHE   A CG  
2695 C  CD1 . PHE   A 378 ? 0.2286 0.1965 0.2147 0.0112  0.0188  0.0145  378  PHE   A CD1 
2696 C  CD2 . PHE   A 378 ? 0.2316 0.2036 0.2228 0.0137  0.0216  0.0172  378  PHE   A CD2 
2697 C  CE1 . PHE   A 378 ? 0.2446 0.2092 0.2283 0.0112  0.0205  0.0145  378  PHE   A CE1 
2698 C  CE2 . PHE   A 378 ? 0.2474 0.2164 0.2366 0.0139  0.0234  0.0172  378  PHE   A CE2 
2699 C  CZ  . PHE   A 378 ? 0.2464 0.2116 0.2317 0.0126  0.0228  0.0158  378  PHE   A CZ  
2700 N  N   . ALA   A 379 ? 0.1706 0.1513 0.1654 0.0110  0.0129  0.0148  379  ALA   A N   
2701 C  CA  . ALA   A 379 ? 0.1651 0.1460 0.1597 0.0101  0.0111  0.0140  379  ALA   A CA  
2702 C  C   . ALA   A 379 ? 0.1715 0.1541 0.1664 0.0096  0.0091  0.0133  379  ALA   A C   
2703 O  O   . ALA   A 379 ? 0.1859 0.1672 0.1794 0.0087  0.0078  0.0125  379  ALA   A O   
2704 C  CB  . ALA   A 379 ? 0.1766 0.1602 0.1738 0.0106  0.0113  0.0147  379  ALA   A CB  
2705 N  N   . LYS   A 380 ? 0.1614 0.1468 0.1580 0.0102  0.0090  0.0138  380  LYS   A N   
2706 C  CA  . LYS   A 380 ? 0.1630 0.1498 0.1598 0.0098  0.0073  0.0131  380  LYS   A CA  
2707 C  C   . LYS   A 380 ? 0.1812 0.1648 0.1752 0.0092  0.0070  0.0124  380  LYS   A C   
2708 O  O   . LYS   A 380 ? 0.1930 0.1760 0.1862 0.0085  0.0055  0.0117  380  LYS   A O   
2709 C  CB  . LYS   A 380 ? 0.1669 0.1569 0.1656 0.0103  0.0074  0.0137  380  LYS   A CB  
2710 C  CG  . LYS   A 380 ? 0.2031 0.1942 0.2019 0.0099  0.0060  0.0130  380  LYS   A CG  
2711 C  CD  . LYS   A 380 ? 0.2090 0.2010 0.2085 0.0096  0.0045  0.0124  380  LYS   A CD  
2712 C  CE  . LYS   A 380 ? 0.2364 0.2312 0.2380 0.0099  0.0047  0.0129  380  LYS   A CE  
2713 N  NZ  . LYS   A 380 ? 0.2762 0.2719 0.2786 0.0096  0.0034  0.0123  380  LYS   A NZ  
2714 N  N   . PHE   A 381 ? 0.1803 0.1618 0.1729 0.0094  0.0084  0.0127  381  PHE   A N   
2715 C  CA  . PHE   A 381 ? 0.1821 0.1605 0.1718 0.0087  0.0082  0.0121  381  PHE   A CA  
2716 C  C   . PHE   A 381 ? 0.1876 0.1630 0.1749 0.0077  0.0076  0.0114  381  PHE   A C   
2717 O  O   . PHE   A 381 ? 0.1954 0.1695 0.1809 0.0069  0.0063  0.0108  381  PHE   A O   
2718 C  CB  . PHE   A 381 ? 0.1854 0.1621 0.1742 0.0092  0.0103  0.0126  381  PHE   A CB  
2719 C  CG  . PHE   A 381 ? 0.2200 0.1936 0.2057 0.0086  0.0102  0.0120  381  PHE   A CG  
2720 C  CD1 . PHE   A 381 ? 0.2372 0.2115 0.2227 0.0082  0.0086  0.0116  381  PHE   A CD1 
2721 C  CD2 . PHE   A 381 ? 0.2392 0.2090 0.2223 0.0084  0.0118  0.0120  381  PHE   A CD2 
2722 C  CE1 . PHE   A 381 ? 0.2495 0.2210 0.2321 0.0076  0.0086  0.0112  381  PHE   A CE1 
2723 C  CE2 . PHE   A 381 ? 0.2533 0.2203 0.2334 0.0078  0.0119  0.0115  381  PHE   A CE2 
2724 C  CZ  . PHE   A 381 ? 0.2433 0.2111 0.2231 0.0073  0.0101  0.0111  381  PHE   A CZ  
2725 N  N   . MET   A 382 ? 0.1886 0.1629 0.1757 0.0077  0.0085  0.0115  382  MET   A N   
2726 C  CA  . MET   A 382 ? 0.1952 0.1665 0.1797 0.0065  0.0080  0.0109  382  MET   A CA  
2727 C  C   . MET   A 382 ? 0.1987 0.1719 0.1841 0.0058  0.0057  0.0105  382  MET   A C   
2728 O  O   . MET   A 382 ? 0.2078 0.1789 0.1910 0.0045  0.0047  0.0100  382  MET   A O   
2729 C  CB  . MET   A 382 ? 0.2077 0.1773 0.1918 0.0065  0.0097  0.0111  382  MET   A CB  
2730 C  CG  . MET   A 382 ? 0.2219 0.1884 0.2041 0.0069  0.0121  0.0113  382  MET   A CG  
2731 S  SD  . MET   A 382 ? 0.2692 0.2310 0.2467 0.0058  0.0123  0.0105  382  MET   A SD  
2732 C  CE  . MET   A 382 ? 0.3026 0.2620 0.2774 0.0038  0.0109  0.0095  382  MET   A CE  
2733 N  N   . GLU   A 383 ? 0.1881 0.1650 0.1766 0.0065  0.0048  0.0108  383  GLU   A N   
2734 C  CA  . GLU   A 383 ? 0.1913 0.1700 0.1809 0.0059  0.0028  0.0105  383  GLU   A CA  
2735 C  C   . GLU   A 383 ? 0.2122 0.1895 0.1999 0.0053  0.0016  0.0101  383  GLU   A C   
2736 O  O   . GLU   A 383 ? 0.2314 0.2083 0.2184 0.0044  0.0001  0.0099  383  GLU   A O   
2737 C  CB  . GLU   A 383 ? 0.1977 0.1802 0.1905 0.0068  0.0023  0.0108  383  GLU   A CB  
2738 C  CG  . GLU   A 383 ? 0.1812 0.1660 0.1763 0.0075  0.0031  0.0112  383  GLU   A CG  
2739 C  CD  . GLU   A 383 ? 0.1997 0.1879 0.1973 0.0082  0.0027  0.0114  383  GLU   A CD  
2740 O  OE1 . GLU   A 383 ? 0.2125 0.2016 0.2106 0.0081  0.0015  0.0111  383  GLU   A OE1 
2741 O  OE2 . GLU   A 383 ? 0.2018 0.1919 0.2010 0.0088  0.0037  0.0120  383  GLU   A OE2 
2742 N  N   . PHE   A 384 ? 0.2083 0.1851 0.1954 0.0058  0.0021  0.0102  384  PHE   A N   
2743 C  CA  A PHE   A 384 ? 0.1994 0.1749 0.1847 0.0052  0.0010  0.0100  384  PHE   A CA  
2744 C  CA  B PHE   A 384 ? 0.2319 0.2074 0.2172 0.0053  0.0012  0.0100  384  PHE   A CA  
2745 C  C   . PHE   A 384 ? 0.2286 0.2003 0.2102 0.0042  0.0013  0.0096  384  PHE   A C   
2746 O  O   . PHE   A 384 ? 0.2327 0.2035 0.2128 0.0032  -0.0003 0.0095  384  PHE   A O   
2747 C  CB  A PHE   A 384 ? 0.1667 0.1430 0.1526 0.0060  0.0016  0.0101  384  PHE   A CB  
2748 C  CB  B PHE   A 384 ? 0.2469 0.2229 0.2326 0.0061  0.0021  0.0101  384  PHE   A CB  
2749 C  CG  A PHE   A 384 ? 0.1333 0.1132 0.1225 0.0068  0.0011  0.0103  384  PHE   A CG  
2750 C  CG  B PHE   A 384 ? 0.2829 0.2565 0.2660 0.0057  0.0020  0.0100  384  PHE   A CG  
2751 C  CD1 A PHE   A 384 ? 0.1383 0.1204 0.1297 0.0074  0.0021  0.0106  384  PHE   A CD1 
2752 C  CD1 B PHE   A 384 ? 0.3020 0.2760 0.2851 0.0055  0.0004  0.0099  384  PHE   A CD1 
2753 C  CD2 A PHE   A 384 ? 0.1338 0.1148 0.1238 0.0068  -0.0003 0.0101  384  PHE   A CD2 
2754 C  CD2 B PHE   A 384 ? 0.3145 0.2854 0.2953 0.0056  0.0035  0.0100  384  PHE   A CD2 
2755 C  CE1 A PHE   A 384 ? 0.1227 0.1078 0.1165 0.0080  0.0017  0.0107  384  PHE   A CE1 
2756 C  CE1 B PHE   A 384 ? 0.3186 0.2904 0.2993 0.0051  0.0003  0.0099  384  PHE   A CE1 
2757 C  CE2 A PHE   A 384 ? 0.1346 0.1185 0.1273 0.0074  -0.0005 0.0102  384  PHE   A CE2 
2758 C  CE2 B PHE   A 384 ? 0.3274 0.2962 0.3058 0.0052  0.0034  0.0098  384  PHE   A CE2 
2759 C  CZ  A PHE   A 384 ? 0.1246 0.1106 0.1191 0.0079  0.0005  0.0104  384  PHE   A CZ  
2760 C  CZ  B PHE   A 384 ? 0.3235 0.2926 0.3017 0.0049  0.0017  0.0098  384  PHE   A CZ  
2761 N  N   . VAL   A 385 ? 0.2117 0.1811 0.1917 0.0042  0.0031  0.0096  385  VAL   A N   
2762 C  CA  . VAL   A 385 ? 0.2211 0.1864 0.1971 0.0030  0.0036  0.0092  385  VAL   A CA  
2763 C  C   . VAL   A 385 ? 0.2317 0.1962 0.2065 0.0016  0.0022  0.0089  385  VAL   A C   
2764 O  O   . VAL   A 385 ? 0.2608 0.2234 0.2328 0.0003  0.0011  0.0086  385  VAL   A O   
2765 C  CB  . VAL   A 385 ? 0.2452 0.2080 0.2199 0.0034  0.0062  0.0092  385  VAL   A CB  
2766 C  CG1 . VAL   A 385 ? 0.2644 0.2225 0.2346 0.0020  0.0070  0.0086  385  VAL   A CG1 
2767 C  CG2 . VAL   A 385 ? 0.2587 0.2222 0.2343 0.0046  0.0075  0.0096  385  VAL   A CG2 
2768 N  N   . SER   A 386 ? 0.2122 0.1786 0.1893 0.0018  0.0022  0.0090  386  SER   A N   
2769 C  CA  . SER   A 386 ? 0.2086 0.1746 0.1850 0.0004  0.0010  0.0088  386  SER   A CA  
2770 C  C   . SER   A 386 ? 0.2232 0.1917 0.2010 0.0000  -0.0015 0.0090  386  SER   A C   
2771 O  O   . SER   A 386 ? 0.2359 0.2030 0.2115 -0.0016 -0.0029 0.0089  386  SER   A O   
2772 C  CB  . SER   A 386 ? 0.2083 0.1753 0.1866 0.0008  0.0019  0.0090  386  SER   A CB  
2773 O  OG  . SER   A 386 ? 0.2012 0.1723 0.1836 0.0021  0.0016  0.0094  386  SER   A OG  
2774 N  N   . VAL   A 387 ? 0.2153 0.1875 0.1968 0.0012  -0.0021 0.0094  387  VAL   A N   
2775 C  CA  . VAL   A 387 ? 0.2070 0.1817 0.1904 0.0010  -0.0042 0.0098  387  VAL   A CA  
2776 C  C   . VAL   A 387 ? 0.2288 0.2024 0.2102 0.0005  -0.0054 0.0099  387  VAL   A C   
2777 O  O   . VAL   A 387 ? 0.2317 0.2062 0.2133 -0.0003 -0.0073 0.0103  387  VAL   A O   
2778 C  CB  . VAL   A 387 ? 0.2006 0.1791 0.1880 0.0025  -0.0042 0.0101  387  VAL   A CB  
2779 C  CG1 . VAL   A 387 ? 0.2231 0.2041 0.2127 0.0025  -0.0061 0.0105  387  VAL   A CG1 
2780 C  CG2 . VAL   A 387 ? 0.2124 0.1918 0.2013 0.0026  -0.0032 0.0101  387  VAL   A CG2 
2781 N  N   . SER   A 388 ? 0.2269 0.1985 0.2065 0.0009  -0.0044 0.0097  388  SER   A N   
2782 C  CA  A SER   A 388 ? 0.2390 0.2090 0.2162 0.0004  -0.0054 0.0098  388  SER   A CA  
2783 C  CA  B SER   A 388 ? 0.2407 0.2110 0.2181 0.0004  -0.0055 0.0099  388  SER   A CA  
2784 C  C   . SER   A 388 ? 0.2646 0.2324 0.2385 -0.0015 -0.0065 0.0098  388  SER   A C   
2785 O  O   . SER   A 388 ? 0.2751 0.2429 0.2481 -0.0022 -0.0082 0.0102  388  SER   A O   
2786 C  CB  A SER   A 388 ? 0.2381 0.2060 0.2134 0.0009  -0.0038 0.0096  388  SER   A CB  
2787 C  CB  B SER   A 388 ? 0.2437 0.2122 0.2197 0.0011  -0.0041 0.0097  388  SER   A CB  
2788 O  OG  A SER   A 388 ? 0.2531 0.2232 0.2313 0.0024  -0.0031 0.0097  388  SER   A OG  
2789 O  OG  B SER   A 388 ? 0.2626 0.2284 0.2363 0.0007  -0.0022 0.0092  388  SER   A OG  
2790 N  N   . VAL   A 389 ? 0.2551 0.2209 0.2272 -0.0025 -0.0056 0.0093  389  VAL   A N   
2791 C  CA  . VAL   A 389 ? 0.2644 0.2278 0.2331 -0.0047 -0.0065 0.0091  389  VAL   A CA  
2792 C  C   . VAL   A 389 ? 0.2817 0.2475 0.2523 -0.0055 -0.0082 0.0095  389  VAL   A C   
2793 O  O   . VAL   A 389 ? 0.3093 0.2752 0.2786 -0.0071 -0.0101 0.0098  389  VAL   A O   
2794 C  CB  . VAL   A 389 ? 0.2853 0.2445 0.2504 -0.0054 -0.0043 0.0083  389  VAL   A CB  
2795 C  CG1 . VAL   A 389 ? 0.3008 0.2573 0.2620 -0.0079 -0.0052 0.0079  389  VAL   A CG1 
2796 C  CG2 . VAL   A 389 ? 0.2928 0.2494 0.2557 -0.0047 -0.0026 0.0080  389  VAL   A CG2 
2797 N  N   . THR   A 390 ? 0.2584 0.2263 0.2321 -0.0046 -0.0074 0.0094  390  THR   A N   
2798 C  CA  . THR   A 390 ? 0.2604 0.2304 0.2359 -0.0056 -0.0088 0.0097  390  THR   A CA  
2799 C  C   . THR   A 390 ? 0.2783 0.2523 0.2573 -0.0050 -0.0108 0.0107  390  THR   A C   
2800 O  O   . THR   A 390 ? 0.2905 0.2660 0.2701 -0.0063 -0.0125 0.0111  390  THR   A O   
2801 C  CB  . THR   A 390 ? 0.2525 0.2232 0.2300 -0.0049 -0.0072 0.0095  390  THR   A CB  
2802 O  OG1 . THR   A 390 ? 0.2486 0.2219 0.2296 -0.0027 -0.0065 0.0097  390  THR   A OG1 
2803 C  CG2 . THR   A 390 ? 0.2538 0.2203 0.2279 -0.0055 -0.0050 0.0087  390  THR   A CG2 
2804 N  N   . HIS   A 391 ? 0.2687 0.2447 0.2503 -0.0031 -0.0106 0.0109  391  HIS   A N   
2805 C  CA  . HIS   A 391 ? 0.2672 0.2469 0.2524 -0.0023 -0.0121 0.0118  391  HIS   A CA  
2806 C  C   . HIS   A 391 ? 0.2830 0.2622 0.2676 -0.0015 -0.0124 0.0121  391  HIS   A C   
2807 O  O   . HIS   A 391 ? 0.2914 0.2721 0.2784 0.0002  -0.0117 0.0121  391  HIS   A O   
2808 C  CB  . HIS   A 391 ? 0.2680 0.2506 0.2572 -0.0008 -0.0112 0.0118  391  HIS   A CB  
2809 C  CG  . HIS   A 391 ? 0.2702 0.2535 0.2603 -0.0016 -0.0110 0.0116  391  HIS   A CG  
2810 N  ND1 . HIS   A 391 ? 0.2670 0.2478 0.2550 -0.0020 -0.0094 0.0109  391  HIS   A ND1 
2811 C  CD2 . HIS   A 391 ? 0.2833 0.2695 0.2762 -0.0018 -0.0121 0.0122  391  HIS   A CD2 
2812 C  CE1 . HIS   A 391 ? 0.2767 0.2588 0.2662 -0.0027 -0.0096 0.0110  391  HIS   A CE1 
2813 N  NE2 . HIS   A 391 ? 0.2889 0.2744 0.2813 -0.0026 -0.0112 0.0118  391  HIS   A NE2 
2814 N  N   . PRO   A 392 ? 0.2985 0.2756 0.2799 -0.0027 -0.0134 0.0123  392  PRO   A N   
2815 C  CA  . PRO   A 392 ? 0.3096 0.2858 0.2901 -0.0020 -0.0135 0.0125  392  PRO   A CA  
2816 C  C   . PRO   A 392 ? 0.3206 0.2999 0.3047 -0.0006 -0.0146 0.0134  392  PRO   A C   
2817 O  O   . PRO   A 392 ? 0.3425 0.3214 0.3268 0.0005  -0.0140 0.0134  392  PRO   A O   
2818 C  CB  . PRO   A 392 ? 0.3310 0.3045 0.3072 -0.0039 -0.0146 0.0127  392  PRO   A CB  
2819 C  CG  . PRO   A 392 ? 0.3405 0.3146 0.3163 -0.0056 -0.0158 0.0129  392  PRO   A CG  
2820 C  CD  . PRO   A 392 ? 0.3047 0.2798 0.2827 -0.0050 -0.0144 0.0122  392  PRO   A CD  
2821 N  N   . GLU   A 393 ? 0.3156 0.2979 0.3028 -0.0006 -0.0158 0.0142  393  GLU   A N   
2822 C  CA  . GLU   A 393 ? 0.3364 0.3218 0.3274 0.0008  -0.0165 0.0151  393  GLU   A CA  
2823 C  C   . GLU   A 393 ? 0.3317 0.3179 0.3250 0.0027  -0.0148 0.0145  393  GLU   A C   
2824 O  O   . GLU   A 393 ? 0.3473 0.3347 0.3428 0.0039  -0.0149 0.0150  393  GLU   A O   
2825 C  CB  . GLU   A 393 ? 0.3753 0.3638 0.3692 0.0004  -0.0180 0.0161  393  GLU   A CB  
2826 C  CG  . GLU   A 393 ? 0.4167 0.4069 0.4130 0.0007  -0.0170 0.0155  393  GLU   A CG  
2827 C  CD  . GLU   A 393 ? 0.4211 0.4098 0.4151 -0.0010 -0.0167 0.0148  393  GLU   A CD  
2828 O  OE1 . GLU   A 393 ? 0.3590 0.3449 0.3491 -0.0025 -0.0170 0.0145  393  GLU   A OE1 
2829 O  OE2 . GLU   A 393 ? 0.4625 0.4527 0.4586 -0.0007 -0.0160 0.0145  393  GLU   A OE2 
2830 N  N   . LEU   A 394 ? 0.3048 0.2903 0.2978 0.0028  -0.0132 0.0135  394  LEU   A N   
2831 C  CA  . LEU   A 394 ? 0.2851 0.2716 0.2801 0.0043  -0.0117 0.0130  394  LEU   A CA  
2832 C  C   . LEU   A 394 ? 0.2997 0.2841 0.2928 0.0048  -0.0107 0.0126  394  LEU   A C   
2833 O  O   . LEU   A 394 ? 0.3211 0.3063 0.3158 0.0059  -0.0097 0.0122  394  LEU   A O   
2834 C  CB  . LEU   A 394 ? 0.2778 0.2647 0.2733 0.0042  -0.0104 0.0123  394  LEU   A CB  
2835 C  CG  . LEU   A 394 ? 0.2918 0.2808 0.2894 0.0037  -0.0111 0.0126  394  LEU   A CG  
2836 C  CD1 . LEU   A 394 ? 0.2870 0.2760 0.2847 0.0037  -0.0097 0.0120  394  LEU   A CD1 
2837 C  CD2 . LEU   A 394 ? 0.3017 0.2939 0.3032 0.0048  -0.0116 0.0132  394  LEU   A CD2 
2838 N  N   . LYS   A 395 ? 0.2943 0.2759 0.2839 0.0039  -0.0110 0.0125  395  LYS   A N   
2839 C  CA  . LYS   A 395 ? 0.3022 0.2817 0.2899 0.0042  -0.0100 0.0122  395  LYS   A CA  
2840 C  C   . LYS   A 395 ? 0.2988 0.2787 0.2873 0.0051  -0.0081 0.0114  395  LYS   A C   
2841 O  O   . LYS   A 395 ? 0.3131 0.2933 0.3024 0.0059  -0.0075 0.0113  395  LYS   A O   
2842 C  CB  . LYS   A 395 ? 0.3431 0.3231 0.3317 0.0050  -0.0108 0.0128  395  LYS   A CB  
2843 C  CG  . LYS   A 395 ? 0.4061 0.3864 0.3945 0.0043  -0.0128 0.0139  395  LYS   A CG  
2844 C  CD  . LYS   A 395 ? 0.5120 0.4894 0.4962 0.0029  -0.0133 0.0139  395  LYS   A CD  
2845 C  CE  . LYS   A 395 ? 0.5988 0.5764 0.5825 0.0024  -0.0153 0.0152  395  LYS   A CE  
2846 N  NZ  . LYS   A 395 ? 0.6476 0.6252 0.6323 0.0036  -0.0152 0.0157  395  LYS   A NZ  
2847 N  N   . VAL   A 396 ? 0.2798 0.2598 0.2684 0.0048  -0.0073 0.0110  396  VAL   A N   
2848 C  CA  . VAL   A 396 ? 0.2804 0.2615 0.2704 0.0056  -0.0057 0.0106  396  VAL   A CA  
2849 C  C   . VAL   A 396 ? 0.2848 0.2641 0.2730 0.0058  -0.0044 0.0103  396  VAL   A C   
2850 O  O   . VAL   A 396 ? 0.2768 0.2574 0.2664 0.0065  -0.0035 0.0102  396  VAL   A O   
2851 C  CB  . VAL   A 396 ? 0.2805 0.2623 0.2712 0.0054  -0.0050 0.0104  396  VAL   A CB  
2852 C  CG1 . VAL   A 396 ? 0.2748 0.2587 0.2677 0.0053  -0.0061 0.0107  396  VAL   A CG1 
2853 C  CG2 . VAL   A 396 ? 0.2913 0.2702 0.2789 0.0045  -0.0044 0.0102  396  VAL   A CG2 
2854 N  N   . GLY   A 397 ? 0.2732 0.2497 0.2583 0.0050  -0.0044 0.0103  397  GLY   A N   
2855 C  CA  . GLY   A 397 ? 0.2863 0.2612 0.2698 0.0052  -0.0032 0.0102  397  GLY   A CA  
2856 C  C   . GLY   A 397 ? 0.3032 0.2791 0.2879 0.0059  -0.0033 0.0102  397  GLY   A C   
2857 O  O   . GLY   A 397 ? 0.3293 0.3052 0.3140 0.0063  -0.0020 0.0101  397  GLY   A O   
2858 N  N   . ASP   A 398 ? 0.2936 0.2706 0.2796 0.0061  -0.0046 0.0105  398  ASP   A N   
2859 C  CA  . ASP   A 398 ? 0.2943 0.2719 0.2814 0.0067  -0.0046 0.0106  398  ASP   A CA  
2860 C  C   . ASP   A 398 ? 0.2727 0.2525 0.2621 0.0074  -0.0036 0.0102  398  ASP   A C   
2861 O  O   . ASP   A 398 ? 0.2767 0.2566 0.2665 0.0077  -0.0032 0.0101  398  ASP   A O   
2862 C  CB  . ASP   A 398 ? 0.3181 0.2965 0.3065 0.0070  -0.0061 0.0110  398  ASP   A CB  
2863 C  CG  . ASP   A 398 ? 0.4008 0.3773 0.3870 0.0064  -0.0074 0.0116  398  ASP   A CG  
2864 O  OD1 . ASP   A 398 ? 0.4017 0.3760 0.3850 0.0057  -0.0071 0.0115  398  ASP   A OD1 
2865 O  OD2 . ASP   A 398 ? 0.4181 0.3956 0.4057 0.0067  -0.0086 0.0123  398  ASP   A OD2 
2866 N  N   . TYR   A 399 ? 0.2543 0.2358 0.2453 0.0075  -0.0034 0.0101  399  TYR   A N   
2867 C  CA  . TYR   A 399 ? 0.2524 0.2363 0.2455 0.0080  -0.0026 0.0099  399  TYR   A CA  
2868 C  C   . TYR   A 399 ? 0.2551 0.2393 0.2480 0.0079  -0.0013 0.0098  399  TYR   A C   
2869 O  O   . TYR   A 399 ? 0.2651 0.2513 0.2595 0.0082  -0.0007 0.0097  399  TYR   A O   
2870 C  CB  . TYR   A 399 ? 0.2633 0.2492 0.2586 0.0082  -0.0030 0.0099  399  TYR   A CB  
2871 C  CG  . TYR   A 399 ? 0.2838 0.2699 0.2799 0.0083  -0.0043 0.0102  399  TYR   A CG  
2872 C  CD1 . TYR   A 399 ? 0.3138 0.2997 0.3104 0.0088  -0.0046 0.0102  399  TYR   A CD1 
2873 C  CD2 . TYR   A 399 ? 0.3000 0.2865 0.2965 0.0080  -0.0052 0.0105  399  TYR   A CD2 
2874 C  CE1 . TYR   A 399 ? 0.3330 0.3192 0.3305 0.0090  -0.0057 0.0107  399  TYR   A CE1 
2875 C  CE2 . TYR   A 399 ? 0.3226 0.3096 0.3201 0.0081  -0.0065 0.0110  399  TYR   A CE2 
2876 C  CZ  . TYR   A 399 ? 0.3450 0.3319 0.3432 0.0087  -0.0067 0.0112  399  TYR   A CZ  
2877 O  OH  . TYR   A 399 ? 0.4004 0.3881 0.4000 0.0090  -0.0078 0.0119  399  TYR   A OH  
2878 N  N   . PHE   A 400 ? 0.2500 0.2323 0.2409 0.0076  -0.0008 0.0099  400  PHE   A N   
2879 C  CA  . PHE   A 400 ? 0.2396 0.2224 0.2307 0.0077  0.0006  0.0101  400  PHE   A CA  
2880 C  C   . PHE   A 400 ? 0.2357 0.2199 0.2276 0.0079  0.0014  0.0102  400  PHE   A C   
2881 O  O   . PHE   A 400 ? 0.2435 0.2299 0.2370 0.0082  0.0022  0.0104  400  PHE   A O   
2882 C  CB  . PHE   A 400 ? 0.2400 0.2201 0.2286 0.0074  0.0013  0.0102  400  PHE   A CB  
2883 C  CG  . PHE   A 400 ? 0.2574 0.2379 0.2464 0.0077  0.0029  0.0106  400  PHE   A CG  
2884 C  CD1 . PHE   A 400 ? 0.2766 0.2586 0.2671 0.0080  0.0034  0.0108  400  PHE   A CD1 
2885 C  CD2 . PHE   A 400 ? 0.2670 0.2470 0.2553 0.0078  0.0040  0.0108  400  PHE   A CD2 
2886 C  CE1 . PHE   A 400 ? 0.2840 0.2666 0.2752 0.0085  0.0050  0.0114  400  PHE   A CE1 
2887 C  CE2 . PHE   A 400 ? 0.2691 0.2498 0.2582 0.0082  0.0056  0.0114  400  PHE   A CE2 
2888 C  CZ  . PHE   A 400 ? 0.2604 0.2425 0.2510 0.0086  0.0060  0.0117  400  PHE   A CZ  
2889 N  N   . PHE   A 401 ? 0.2431 0.2259 0.2338 0.0077  0.0012  0.0100  401  PHE   A N   
2890 C  CA  . PHE   A 401 ? 0.2407 0.2246 0.2319 0.0076  0.0020  0.0101  401  PHE   A CA  
2891 C  C   . PHE   A 401 ? 0.2264 0.2132 0.2198 0.0077  0.0019  0.0099  401  PHE   A C   
2892 O  O   . PHE   A 401 ? 0.2186 0.2069 0.2126 0.0075  0.0026  0.0101  401  PHE   A O   
2893 C  CB  . PHE   A 401 ? 0.2437 0.2256 0.2332 0.0073  0.0017  0.0099  401  PHE   A CB  
2894 C  CG  . PHE   A 401 ? 0.2403 0.2223 0.2304 0.0074  0.0008  0.0095  401  PHE   A CG  
2895 C  CD1 . PHE   A 401 ? 0.2628 0.2439 0.2527 0.0076  -0.0003 0.0095  401  PHE   A CD1 
2896 C  CD2 . PHE   A 401 ? 0.2518 0.2352 0.2429 0.0072  0.0011  0.0093  401  PHE   A CD2 
2897 C  CE1 . PHE   A 401 ? 0.2737 0.2550 0.2645 0.0078  -0.0009 0.0093  401  PHE   A CE1 
2898 C  CE2 . PHE   A 401 ? 0.2689 0.2521 0.2605 0.0073  0.0005  0.0089  401  PHE   A CE2 
2899 C  CZ  . PHE   A 401 ? 0.2756 0.2578 0.2671 0.0077  -0.0004 0.0090  401  PHE   A CZ  
2900 N  N   . GLY   A 402 ? 0.2151 0.2025 0.2095 0.0079  0.0010  0.0096  402  GLY   A N   
2901 C  CA  . GLY   A 402 ? 0.2182 0.2080 0.2142 0.0079  0.0011  0.0094  402  GLY   A CA  
2902 C  C   . GLY   A 402 ? 0.2141 0.2063 0.2114 0.0079  0.0018  0.0098  402  GLY   A C   
2903 O  O   . GLY   A 402 ? 0.2491 0.2435 0.2474 0.0076  0.0021  0.0098  402  GLY   A O   
2904 N  N   . LYS   A 403 ? 0.2109 0.2028 0.2081 0.0082  0.0020  0.0103  403  LYS   A N   
2905 C  CA  . LYS   A 403 ? 0.2222 0.2162 0.2208 0.0084  0.0028  0.0109  403  LYS   A CA  
2906 C  C   . LYS   A 403 ? 0.2308 0.2257 0.2294 0.0082  0.0037  0.0115  403  LYS   A C   
2907 O  O   . LYS   A 403 ? 0.2218 0.2195 0.2218 0.0082  0.0041  0.0120  403  LYS   A O   
2908 C  CB  . LYS   A 403 ? 0.2703 0.2630 0.2684 0.0087  0.0031  0.0112  403  LYS   A CB  
2909 C  CG  . LYS   A 403 ? 0.3163 0.3085 0.3146 0.0088  0.0022  0.0108  403  LYS   A CG  
2910 C  CD  . LYS   A 403 ? 0.3948 0.3896 0.3950 0.0089  0.0018  0.0107  403  LYS   A CD  
2911 C  CE  . LYS   A 403 ? 0.4769 0.4713 0.4775 0.0089  0.0010  0.0105  403  LYS   A CE  
2912 N  NZ  . LYS   A 403 ? 0.5191 0.5159 0.5215 0.0091  0.0009  0.0103  403  LYS   A NZ  
2913 N  N   . CYS   A 404 ? 0.2216 0.2144 0.2186 0.0081  0.0040  0.0114  404  CYS   A N   
2914 C  CA  . CYS   A 404 ? 0.2091 0.2028 0.2062 0.0078  0.0048  0.0120  404  CYS   A CA  
2915 C  C   . CYS   A 404 ? 0.2038 0.1993 0.2015 0.0071  0.0045  0.0117  404  CYS   A C   
2916 O  O   . CYS   A 404 ? 0.2181 0.2161 0.2170 0.0069  0.0050  0.0124  404  CYS   A O   
2917 C  CB  . CYS   A 404 ? 0.2083 0.1990 0.2035 0.0078  0.0052  0.0119  404  CYS   A CB  
2918 S  SG  . CYS   A 404 ? 0.2499 0.2377 0.2435 0.0083  0.0056  0.0120  404  CYS   A SG  
2919 N  N   . PHE   A 405 ? 0.2045 0.1990 0.2016 0.0068  0.0037  0.0108  405  PHE   A N   
2920 C  CA  . PHE   A 405 ? 0.2137 0.2097 0.2111 0.0061  0.0035  0.0104  405  PHE   A CA  
2921 C  C   . PHE   A 405 ? 0.2300 0.2291 0.2290 0.0059  0.0034  0.0106  405  PHE   A C   
2922 O  O   . PHE   A 405 ? 0.2514 0.2527 0.2509 0.0051  0.0036  0.0108  405  PHE   A O   
2923 C  CB  . PHE   A 405 ? 0.2265 0.2203 0.2229 0.0059  0.0029  0.0095  405  PHE   A CB  
2924 C  CG  . PHE   A 405 ? 0.2426 0.2338 0.2373 0.0057  0.0030  0.0094  405  PHE   A CG  
2925 C  CD1 . PHE   A 405 ? 0.2621 0.2538 0.2565 0.0053  0.0037  0.0099  405  PHE   A CD1 
2926 C  CD2 . PHE   A 405 ? 0.2623 0.2510 0.2559 0.0060  0.0025  0.0089  405  PHE   A CD2 
2927 C  CE1 . PHE   A 405 ? 0.2765 0.2659 0.2694 0.0050  0.0039  0.0098  405  PHE   A CE1 
2928 C  CE2 . PHE   A 405 ? 0.2748 0.2611 0.2668 0.0058  0.0026  0.0089  405  PHE   A CE2 
2929 C  CZ  . PHE   A 405 ? 0.2694 0.2560 0.2610 0.0053  0.0033  0.0093  405  PHE   A CZ  
2930 N  N   . ASP   A 406 ? 0.2335 0.2329 0.2333 0.0066  0.0032  0.0107  406  ASP   A N   
2931 C  CA  . ASP   A 406 ? 0.2431 0.2455 0.2444 0.0065  0.0032  0.0110  406  ASP   A CA  
2932 C  C   . ASP   A 406 ? 0.2480 0.2529 0.2503 0.0064  0.0039  0.0122  406  ASP   A C   
2933 O  O   . ASP   A 406 ? 0.2634 0.2711 0.2666 0.0057  0.0039  0.0126  406  ASP   A O   
2934 C  CB  . ASP   A 406 ? 0.2538 0.2561 0.2559 0.0072  0.0030  0.0110  406  ASP   A CB  
2935 C  CG  . ASP   A 406 ? 0.3448 0.3455 0.3465 0.0074  0.0023  0.0101  406  ASP   A CG  
2936 O  OD1 . ASP   A 406 ? 0.3426 0.3427 0.3437 0.0070  0.0022  0.0094  406  ASP   A OD1 
2937 O  OD2 . ASP   A 406 ? 0.3766 0.3769 0.3788 0.0080  0.0021  0.0101  406  ASP   A OD2 
2938 N  N   . ALA   A 407 ? 0.2286 0.2325 0.2309 0.0070  0.0045  0.0130  407  ALA   A N   
2939 C  CA  . ALA   A 407 ? 0.2260 0.2323 0.2296 0.0071  0.0053  0.0144  407  ALA   A CA  
2940 C  C   . ALA   A 407 ? 0.2236 0.2314 0.2272 0.0061  0.0053  0.0146  407  ALA   A C   
2941 O  O   . ALA   A 407 ? 0.2110 0.2221 0.2160 0.0057  0.0055  0.0156  407  ALA   A O   
2942 C  CB  . ALA   A 407 ? 0.2380 0.2423 0.2413 0.0080  0.0062  0.0150  407  ALA   A CB  
2943 N  N   . MET   A 408 ? 0.2100 0.2154 0.2120 0.0057  0.0052  0.0137  408  MET   A N   
2944 C  CA  . MET   A 408 ? 0.1962 0.2028 0.1981 0.0046  0.0053  0.0139  408  MET   A CA  
2945 C  C   . MET   A 408 ? 0.2357 0.2448 0.2380 0.0034  0.0047  0.0136  408  MET   A C   
2946 O  O   . MET   A 408 ? 0.2514 0.2629 0.2542 0.0023  0.0048  0.0142  408  MET   A O   
2947 C  CB  . MET   A 408 ? 0.1912 0.1945 0.1912 0.0043  0.0053  0.0130  408  MET   A CB  
2948 C  CG  . MET   A 408 ? 0.1916 0.1929 0.1912 0.0052  0.0060  0.0135  408  MET   A CG  
2949 S  SD  . MET   A 408 ? 0.2788 0.2762 0.2759 0.0047  0.0058  0.0125  408  MET   A SD  
2950 C  CE  . MET   A 408 ? 0.2544 0.2510 0.2513 0.0053  0.0070  0.0135  408  MET   A CE  
2951 N  N   . GLU   A 409 ? 0.2456 0.2543 0.2475 0.0034  0.0041  0.0127  409  GLU   A N   
2952 C  CA  . GLU   A 409 ? 0.2889 0.2997 0.2907 0.0021  0.0037  0.0122  409  GLU   A CA  
2953 C  C   . GLU   A 409 ? 0.3022 0.3172 0.3057 0.0017  0.0037  0.0136  409  GLU   A C   
2954 O  O   . GLU   A 409 ? 0.3337 0.3509 0.3371 0.0003  0.0036  0.0140  409  GLU   A O   
2955 C  CB  . GLU   A 409 ? 0.3354 0.3450 0.3368 0.0024  0.0033  0.0111  409  GLU   A CB  
2956 C  CG  . GLU   A 409 ? 0.4738 0.4837 0.4740 0.0010  0.0031  0.0101  409  GLU   A CG  
2957 C  CD  . GLU   A 409 ? 0.6201 0.6271 0.6186 0.0003  0.0032  0.0091  409  GLU   A CD  
2958 O  OE1 . GLU   A 409 ? 0.6569 0.6613 0.6550 0.0012  0.0033  0.0090  409  GLU   A OE1 
2959 O  OE2 . GLU   A 409 ? 0.6857 0.6932 0.6832 -0.0012 0.0033  0.0085  409  GLU   A OE2 
2960 N  N   . VAL   A 410 ? 0.2924 0.3084 0.2973 0.0029  0.0040  0.0146  410  VAL   A N   
2961 C  CA  . VAL   A 410 ? 0.2902 0.3101 0.2969 0.0028  0.0041  0.0163  410  VAL   A CA  
2962 C  C   . VAL   A 410 ? 0.2398 0.2614 0.2477 0.0028  0.0046  0.0178  410  VAL   A C   
2963 O  O   . VAL   A 410 ? 0.2145 0.2399 0.2235 0.0018  0.0045  0.0190  410  VAL   A O   
2964 C  CB  . VAL   A 410 ? 0.3350 0.3551 0.3429 0.0042  0.0043  0.0168  410  VAL   A CB  
2965 C  CG1 . VAL   A 410 ? 0.3747 0.3927 0.3815 0.0043  0.0039  0.0153  410  VAL   A CG1 
2966 C  CG2 . VAL   A 410 ? 0.3440 0.3622 0.3524 0.0057  0.0052  0.0175  410  VAL   A CG2 
2967 N  N   . ASP   A 411 ? 0.1916 0.2105 0.1991 0.0037  0.0053  0.0177  411  ASP   A N   
2968 C  CA  . ASP   A 411 ? 0.1865 0.2067 0.1953 0.0040  0.0062  0.0192  411  ASP   A CA  
2969 C  C   . ASP   A 411 ? 0.2074 0.2286 0.2158 0.0026  0.0060  0.0192  411  ASP   A C   
2970 O  O   . ASP   A 411 ? 0.2318 0.2547 0.2416 0.0027  0.0067  0.0207  411  ASP   A O   
2971 C  CB  . ASP   A 411 ? 0.1863 0.2027 0.1944 0.0055  0.0071  0.0190  411  ASP   A CB  
2972 C  CG  . ASP   A 411 ? 0.1957 0.2130 0.2054 0.0066  0.0084  0.0207  411  ASP   A CG  
2973 O  OD1 . ASP   A 411 ? 0.1880 0.2092 0.2000 0.0067  0.0086  0.0224  411  ASP   A OD1 
2974 O  OD2 . ASP   A 411 ? 0.1846 0.1988 0.1933 0.0073  0.0092  0.0204  411  ASP   A OD2 
2975 N  N   . ALA   A 412 ? 0.1990 0.2192 0.2057 0.0012  0.0052  0.0177  412  ALA   A N   
2976 C  CA  . ALA   A 412 ? 0.2124 0.2335 0.2185 -0.0004 0.0050  0.0176  412  ALA   A CA  
2977 C  C   . ALA   A 412 ? 0.2133 0.2392 0.2206 -0.0019 0.0044  0.0187  412  ALA   A C   
2978 O  O   . ALA   A 412 ? 0.2317 0.2590 0.2388 -0.0036 0.0042  0.0188  412  ALA   A O   
2979 C  CB  . ALA   A 412 ? 0.2372 0.2549 0.2408 -0.0013 0.0046  0.0156  412  ALA   A CB  
2980 N  N   . LEU   A 413 ? 0.2074 0.2357 0.2158 -0.0016 0.0041  0.0194  413  LEU   A N   
2981 C  CA  . LEU   A 413 ? 0.2240 0.2568 0.2333 -0.0032 0.0034  0.0203  413  LEU   A CA  
2982 C  C   . LEU   A 413 ? 0.2491 0.2861 0.2612 -0.0028 0.0037  0.0229  413  LEU   A C   
2983 O  O   . LEU   A 413 ? 0.2507 0.2872 0.2644 -0.0008 0.0046  0.0240  413  LEU   A O   
2984 C  CB  . LEU   A 413 ? 0.2169 0.2501 0.2257 -0.0031 0.0029  0.0198  413  LEU   A CB  
2985 C  CG  . LEU   A 413 ? 0.2371 0.2664 0.2433 -0.0035 0.0026  0.0174  413  LEU   A CG  
2986 C  CD1 . LEU   A 413 ? 0.2327 0.2622 0.2388 -0.0030 0.0024  0.0170  413  LEU   A CD1 
2987 C  CD2 . LEU   A 413 ? 0.2731 0.3021 0.2772 -0.0058 0.0022  0.0162  413  LEU   A CD2 
2988 N  N   . GLN   A 414 ? 0.2568 0.2980 0.2697 -0.0047 0.0030  0.0239  414  GLN   A N   
2989 C  CA  . GLN   A 414 ? 0.2819 0.3277 0.2978 -0.0046 0.0033  0.0266  414  GLN   A CA  
2990 C  C   . GLN   A 414 ? 0.2787 0.3266 0.2971 -0.0027 0.0038  0.0285  414  GLN   A C   
2991 O  O   . GLN   A 414 ? 0.3063 0.3558 0.3273 -0.0014 0.0047  0.0304  414  GLN   A O   
2992 C  CB  . GLN   A 414 ? 0.3168 0.3673 0.3329 -0.0073 0.0021  0.0275  414  GLN   A CB  
2993 C  CG  . GLN   A 414 ? 0.4119 0.4630 0.4260 -0.0090 0.0010  0.0263  414  GLN   A CG  
2994 C  CD  . GLN   A 414 ? 0.4678 0.5233 0.4815 -0.0120 -0.0002 0.0269  414  GLN   A CD  
2995 O  OE1 . GLN   A 414 ? 0.4442 0.5037 0.4588 -0.0126 -0.0010 0.0284  414  GLN   A OE1 
2996 N  NE2 . GLN   A 414 ? 0.4981 0.5524 0.5099 -0.0141 -0.0005 0.0257  414  GLN   A NE2 
2997 N  N   . SER   A 415 ? 0.2704 0.3181 0.2882 -0.0024 0.0033  0.0280  415  SER   A N   
2998 C  CA  . SER   A 415 ? 0.2778 0.3277 0.2979 -0.0007 0.0038  0.0299  415  SER   A CA  
2999 C  C   . SER   A 415 ? 0.2709 0.3164 0.2906 0.0015  0.0048  0.0290  415  SER   A C   
3000 O  O   . SER   A 415 ? 0.2761 0.3228 0.2972 0.0028  0.0051  0.0303  415  SER   A O   
3001 C  CB  . SER   A 415 ? 0.2801 0.3337 0.3003 -0.0020 0.0026  0.0305  415  SER   A CB  
3002 O  OG  . SER   A 415 ? 0.2869 0.3449 0.3075 -0.0043 0.0016  0.0316  415  SER   A OG  
3003 N  N   . SER   A 416 ? 0.2471 0.2877 0.2648 0.0021  0.0053  0.0271  416  SER   A N   
3004 C  CA  . SER   A 416 ? 0.2370 0.2736 0.2543 0.0041  0.0062  0.0264  416  SER   A CA  
3005 C  C   . SER   A 416 ? 0.2361 0.2742 0.2562 0.0058  0.0076  0.0288  416  SER   A C   
3006 O  O   . SER   A 416 ? 0.2714 0.3125 0.2933 0.0056  0.0079  0.0305  416  SER   A O   
3007 C  CB  . SER   A 416 ? 0.2200 0.2517 0.2352 0.0043  0.0066  0.0246  416  SER   A CB  
3008 O  OG  . SER   A 416 ? 0.2284 0.2564 0.2428 0.0059  0.0073  0.0238  416  SER   A OG  
3009 N  N   . HIS   A 417 ? 0.1984 0.2342 0.2186 0.0075  0.0084  0.0288  417  HIS   A N   
3010 C  CA  . HIS   A 417 ? 0.1858 0.2224 0.2084 0.0093  0.0100  0.0310  417  HIS   A CA  
3011 C  C   . HIS   A 417 ? 0.1827 0.2145 0.2041 0.0105  0.0115  0.0302  417  HIS   A C   
3012 O  O   . HIS   A 417 ? 0.1784 0.2060 0.1972 0.0104  0.0112  0.0280  417  HIS   A O   
3013 C  CB  . HIS   A 417 ? 0.1819 0.2195 0.2056 0.0103  0.0102  0.0320  417  HIS   A CB  
3014 C  CG  . HIS   A 417 ? 0.1749 0.2082 0.1964 0.0107  0.0101  0.0299  417  HIS   A CG  
3015 N  ND1 . HIS   A 417 ? 0.1799 0.2090 0.2007 0.0121  0.0114  0.0295  417  HIS   A ND1 
3016 C  CD2 . HIS   A 417 ? 0.1775 0.2102 0.1974 0.0098  0.0088  0.0283  417  HIS   A CD2 
3017 C  CE1 . HIS   A 417 ? 0.1980 0.2244 0.2169 0.0120  0.0108  0.0277  417  HIS   A CE1 
3018 N  NE2 . HIS   A 417 ? 0.1808 0.2092 0.1993 0.0107  0.0093  0.0270  417  HIS   A NE2 
3019 N  N   . PRO   A 418 ? 0.1759 0.2082 0.1992 0.0118  0.0131  0.0321  418  PRO   A N   
3020 C  CA  . PRO   A 418 ? 0.1734 0.2009 0.1953 0.0130  0.0147  0.0313  418  PRO   A CA  
3021 C  C   . PRO   A 418 ? 0.1688 0.1926 0.1892 0.0139  0.0151  0.0302  418  PRO   A C   
3022 O  O   . PRO   A 418 ? 0.1744 0.1998 0.1959 0.0142  0.0148  0.0309  418  PRO   A O   
3023 C  CB  . PRO   A 418 ? 0.1781 0.2076 0.2029 0.0144  0.0167  0.0339  418  PRO   A CB  
3024 C  CG  . PRO   A 418 ? 0.2035 0.2390 0.2310 0.0135  0.0157  0.0358  418  PRO   A CG  
3025 C  CD  . PRO   A 418 ? 0.1844 0.2218 0.2113 0.0123  0.0137  0.0350  418  PRO   A CD  
3026 N  N   . VAL   A 419 ? 0.1654 0.1841 0.1833 0.0142  0.0158  0.0287  419  VAL   A N   
3027 C  CA  . VAL   A 419 ? 0.1597 0.1746 0.1760 0.0148  0.0161  0.0276  419  VAL   A CA  
3028 C  C   . VAL   A 419 ? 0.1727 0.1884 0.1909 0.0163  0.0176  0.0295  419  VAL   A C   
3029 O  O   . VAL   A 419 ? 0.1788 0.1942 0.1969 0.0165  0.0172  0.0292  419  VAL   A O   
3030 C  CB  . VAL   A 419 ? 0.1737 0.1832 0.1870 0.0149  0.0168  0.0260  419  VAL   A CB  
3031 C  CG1 . VAL   A 419 ? 0.1982 0.2039 0.2099 0.0155  0.0175  0.0253  419  VAL   A CG1 
3032 C  CG2 . VAL   A 419 ? 0.1773 0.1857 0.1884 0.0135  0.0151  0.0241  419  VAL   A CG2 
3033 N  N   . SER   A 420 ? 0.1611 0.1779 0.1813 0.0174  0.0194  0.0314  420  SER   A N   
3034 C  CA  A SER   A 420 ? 0.1729 0.1909 0.1954 0.0190  0.0210  0.0336  420  SER   A CA  
3035 C  CA  B SER   A 420 ? 0.1803 0.1981 0.2028 0.0190  0.0211  0.0335  420  SER   A CA  
3036 C  C   . SER   A 420 ? 0.1866 0.2108 0.2127 0.0189  0.0205  0.0359  420  SER   A C   
3037 O  O   . SER   A 420 ? 0.1916 0.2181 0.2188 0.0186  0.0206  0.0368  420  SER   A O   
3038 C  CB  A SER   A 420 ? 0.1770 0.1917 0.1994 0.0204  0.0237  0.0343  420  SER   A CB  
3039 C  CB  B SER   A 420 ? 0.2036 0.2180 0.2258 0.0203  0.0238  0.0342  420  SER   A CB  
3040 O  OG  A SER   A 420 ? 0.1760 0.1850 0.1952 0.0204  0.0243  0.0324  420  SER   A OG  
3041 O  OG  B SER   A 420 ? 0.2303 0.2457 0.2550 0.0220  0.0257  0.0365  420  SER   A OG  
3042 N  N   . THR   A 421 ? 0.1804 0.2077 0.2080 0.0190  0.0198  0.0370  421  THR   A N   
3043 C  CA  . THR   A 421 ? 0.1819 0.2155 0.2127 0.0187  0.0189  0.0393  421  THR   A CA  
3044 C  C   . THR   A 421 ? 0.1930 0.2286 0.2258 0.0197  0.0194  0.0412  421  THR   A C   
3045 O  O   . THR   A 421 ? 0.1870 0.2195 0.2182 0.0200  0.0194  0.0400  421  THR   A O   
3046 C  CB  . THR   A 421 ? 0.1927 0.2284 0.2222 0.0165  0.0164  0.0378  421  THR   A CB  
3047 O  OG1 . THR   A 421 ? 0.2053 0.2471 0.2374 0.0157  0.0155  0.0398  421  THR   A OG1 
3048 C  CG2 . THR   A 421 ? 0.2026 0.2371 0.2302 0.0158  0.0150  0.0360  421  THR   A CG2 
3049 N  N   . PRO   A 422 ? 0.1876 0.2283 0.2239 0.0204  0.0197  0.0442  422  PRO   A N   
3050 C  CA  . PRO   A 422 ? 0.1848 0.2272 0.2232 0.0216  0.0204  0.0463  422  PRO   A CA  
3051 C  C   . PRO   A 422 ? 0.1869 0.2312 0.2244 0.0204  0.0183  0.0456  422  PRO   A C   
3052 O  O   . PRO   A 422 ? 0.2051 0.2526 0.2422 0.0185  0.0162  0.0450  422  PRO   A O   
3053 C  CB  . PRO   A 422 ? 0.1865 0.2346 0.2291 0.0224  0.0210  0.0499  422  PRO   A CB  
3054 C  CG  . PRO   A 422 ? 0.2102 0.2587 0.2530 0.0219  0.0212  0.0497  422  PRO   A CG  
3055 C  CD  . PRO   A 422 ? 0.1882 0.2332 0.2271 0.0201  0.0198  0.0461  422  PRO   A CD  
3056 N  N   . VAL   A 423 ? 0.1695 0.2117 0.2067 0.0213  0.0190  0.0457  423  VAL   A N   
3057 C  CA  . VAL   A 423 ? 0.1737 0.2179 0.2105 0.0204  0.0174  0.0454  423  VAL   A CA  
3058 C  C   . VAL   A 423 ? 0.1765 0.2215 0.2154 0.0221  0.0188  0.0479  423  VAL   A C   
3059 O  O   . VAL   A 423 ? 0.1819 0.2238 0.2215 0.0239  0.0212  0.0487  423  VAL   A O   
3060 C  CB  . VAL   A 423 ? 0.1841 0.2239 0.2173 0.0194  0.0165  0.0420  423  VAL   A CB  
3061 C  CG1 . VAL   A 423 ? 0.1990 0.2383 0.2301 0.0176  0.0149  0.0397  423  VAL   A CG1 
3062 C  CG2 . VAL   A 423 ? 0.1894 0.2232 0.2210 0.0206  0.0183  0.0409  423  VAL   A CG2 
3063 N  N   . GLU   A 424 ? 0.1733 0.2222 0.2131 0.0215  0.0175  0.0490  424  GLU   A N   
3064 C  CA  . GLU   A 424 ? 0.1980 0.2480 0.2400 0.0231  0.0187  0.0516  424  GLU   A CA  
3065 C  C   . GLU   A 424 ? 0.1883 0.2379 0.2289 0.0225  0.0178  0.0507  424  GLU   A C   
3066 O  O   . GLU   A 424 ? 0.2115 0.2579 0.2520 0.0237  0.0193  0.0509  424  GLU   A O   
3067 C  CB  . GLU   A 424 ? 0.2265 0.2830 0.2723 0.0235  0.0185  0.0553  424  GLU   A CB  
3068 C  CG  . GLU   A 424 ? 0.3650 0.4225 0.4133 0.0255  0.0201  0.0583  424  GLU   A CG  
3069 C  CD  . GLU   A 424 ? 0.5190 0.5811 0.5716 0.0270  0.0213  0.0624  424  GLU   A CD  
3070 O  OE1 . GLU   A 424 ? 0.5654 0.6250 0.6197 0.0293  0.0240  0.0638  424  GLU   A OE1 
3071 O  OE2 . GLU   A 424 ? 0.5777 0.6461 0.6322 0.0259  0.0195  0.0643  424  GLU   A OE2 
3072 N  N   . ASN   A 425 ? 0.1764 0.2293 0.2161 0.0206  0.0155  0.0501  425  ASN   A N   
3073 C  CA  . ASN   A 425 ? 0.1828 0.2359 0.2215 0.0200  0.0147  0.0496  425  ASN   A CA  
3074 C  C   . ASN   A 425 ? 0.1751 0.2235 0.2104 0.0190  0.0141  0.0459  425  ASN   A C   
3075 O  O   . ASN   A 425 ? 0.1693 0.2153 0.2030 0.0184  0.0138  0.0438  425  ASN   A O   
3076 C  CB  . ASN   A 425 ? 0.2032 0.2624 0.2428 0.0186  0.0128  0.0512  425  ASN   A CB  
3077 C  CG  . ASN   A 425 ? 0.2495 0.3103 0.2873 0.0163  0.0108  0.0492  425  ASN   A CG  
3078 O  OD1 . ASN   A 425 ? 0.2535 0.3108 0.2885 0.0154  0.0102  0.0461  425  ASN   A OD1 
3079 N  ND2 . ASN   A 425 ? 0.2806 0.3466 0.3198 0.0153  0.0097  0.0511  425  ASN   A ND2 
3080 N  N   . PRO   A 426 ? 0.1734 0.2208 0.2078 0.0189  0.0139  0.0453  426  PRO   A N   
3081 C  CA  . PRO   A 426 ? 0.1715 0.2146 0.2030 0.0181  0.0134  0.0421  426  PRO   A CA  
3082 C  C   . PRO   A 426 ? 0.1741 0.2176 0.2037 0.0163  0.0116  0.0397  426  PRO   A C   
3083 O  O   . PRO   A 426 ? 0.1647 0.2043 0.1924 0.0160  0.0116  0.0373  426  PRO   A O   
3084 C  CB  . PRO   A 426 ? 0.1823 0.2259 0.2138 0.0181  0.0133  0.0426  426  PRO   A CB  
3085 C  CG  . PRO   A 426 ? 0.1950 0.2399 0.2291 0.0199  0.0150  0.0459  426  PRO   A CG  
3086 C  CD  . PRO   A 426 ? 0.1784 0.2279 0.2144 0.0197  0.0143  0.0477  426  PRO   A CD  
3087 N  N   . ALA   A 427 ? 0.1702 0.2184 0.2002 0.0149  0.0102  0.0405  427  ALA   A N   
3088 C  CA  . ALA   A 427 ? 0.1810 0.2291 0.2089 0.0131  0.0087  0.0382  427  ALA   A CA  
3089 C  C   . ALA   A 427 ? 0.1720 0.2186 0.1997 0.0132  0.0090  0.0374  427  ALA   A C   
3090 O  O   . ALA   A 427 ? 0.1710 0.2145 0.1967 0.0125  0.0085  0.0349  427  ALA   A O   
3091 C  CB  . ALA   A 427 ? 0.1921 0.2452 0.2201 0.0116  0.0072  0.0391  427  ALA   A CB  
3092 N  N   . GLN   A 428 ? 0.1676 0.2161 0.1976 0.0142  0.0098  0.0397  428  GLN   A N   
3093 C  CA  . GLN   A 428 ? 0.1695 0.2164 0.1993 0.0144  0.0103  0.0392  428  GLN   A CA  
3094 C  C   . GLN   A 428 ? 0.1597 0.2009 0.1882 0.0154  0.0116  0.0374  428  GLN   A C   
3095 O  O   . GLN   A 428 ? 0.1652 0.2037 0.1921 0.0149  0.0114  0.0356  428  GLN   A O   
3096 C  CB  . GLN   A 428 ? 0.1857 0.2360 0.2186 0.0154  0.0113  0.0423  428  GLN   A CB  
3097 C  CG  . GLN   A 428 ? 0.2119 0.2683 0.2463 0.0142  0.0099  0.0442  428  GLN   A CG  
3098 C  CD  . GLN   A 428 ? 0.2447 0.3048 0.2826 0.0155  0.0109  0.0478  428  GLN   A CD  
3099 O  OE1 . GLN   A 428 ? 0.2131 0.2715 0.2526 0.0175  0.0128  0.0492  428  GLN   A OE1 
3100 N  NE2 . GLN   A 428 ? 0.2411 0.3064 0.2803 0.0142  0.0097  0.0493  428  GLN   A NE2 
3101 N  N   . ILE   A 429 ? 0.1613 0.2002 0.1901 0.0167  0.0128  0.0380  429  ILE   A N   
3102 C  CA  . ILE   A 429 ? 0.1550 0.1883 0.1821 0.0174  0.0139  0.0363  429  ILE   A CA  
3103 C  C   . ILE   A 429 ? 0.1567 0.1877 0.1813 0.0161  0.0125  0.0333  429  ILE   A C   
3104 O  O   . ILE   A 429 ? 0.1556 0.1830 0.1785 0.0159  0.0126  0.0315  429  ILE   A O   
3105 C  CB  . ILE   A 429 ? 0.1594 0.1913 0.1874 0.0188  0.0154  0.0375  429  ILE   A CB  
3106 C  CG1 . ILE   A 429 ? 0.1602 0.1938 0.1909 0.0204  0.0171  0.0405  429  ILE   A CG1 
3107 C  CG2 . ILE   A 429 ? 0.1650 0.1910 0.1908 0.0191  0.0163  0.0355  429  ILE   A CG2 
3108 C  CD1 . ILE   A 429 ? 0.1649 0.1977 0.1968 0.0218  0.0186  0.0422  429  ILE   A CD1 
3109 N  N   . ARG   A 430 ? 0.1485 0.1814 0.1727 0.0152  0.0113  0.0329  430  ARG   A N   
3110 C  CA  . ARG   A 430 ? 0.1415 0.1723 0.1636 0.0141  0.0102  0.0302  430  ARG   A CA  
3111 C  C   . ARG   A 430 ? 0.1576 0.1884 0.1785 0.0130  0.0092  0.0289  430  ARG   A C   
3112 O  O   . ARG   A 430 ? 0.1587 0.1863 0.1778 0.0126  0.0088  0.0267  430  ARG   A O   
3113 C  CB  . ARG   A 430 ? 0.1464 0.1795 0.1684 0.0133  0.0093  0.0302  430  ARG   A CB  
3114 C  CG  . ARG   A 430 ? 0.1655 0.1974 0.1881 0.0142  0.0102  0.0309  430  ARG   A CG  
3115 C  CD  . ARG   A 430 ? 0.1879 0.2217 0.2102 0.0134  0.0093  0.0306  430  ARG   A CD  
3116 N  NE  . ARG   A 430 ? 0.1621 0.2006 0.1854 0.0129  0.0087  0.0323  430  ARG   A NE  
3117 C  CZ  . ARG   A 430 ? 0.1737 0.2145 0.1986 0.0136  0.0092  0.0346  430  ARG   A CZ  
3118 N  NH1 . ARG   A 430 ? 0.1829 0.2216 0.2086 0.0149  0.0106  0.0355  430  ARG   A NH1 
3119 N  NH2 . ARG   A 430 ? 0.1663 0.2115 0.1918 0.0128  0.0085  0.0361  430  ARG   A NH2 
3120 N  N   . GLU   A 431 ? 0.1412 0.1754 0.1632 0.0126  0.0089  0.0301  431  GLU   A N   
3121 C  CA  . GLU   A 431 ? 0.1469 0.1810 0.1678 0.0115  0.0081  0.0289  431  GLU   A CA  
3122 C  C   . GLU   A 431 ? 0.1598 0.1901 0.1799 0.0122  0.0090  0.0281  431  GLU   A C   
3123 O  O   . GLU   A 431 ? 0.1741 0.2032 0.1928 0.0114  0.0084  0.0266  431  GLU   A O   
3124 C  CB  . GLU   A 431 ? 0.1451 0.1837 0.1673 0.0108  0.0077  0.0306  431  GLU   A CB  
3125 C  CG  . GLU   A 431 ? 0.1652 0.2074 0.1874 0.0096  0.0066  0.0310  431  GLU   A CG  
3126 C  CD  . GLU   A 431 ? 0.2019 0.2487 0.2251 0.0085  0.0058  0.0325  431  GLU   A CD  
3127 O  OE1 . GLU   A 431 ? 0.2251 0.2740 0.2505 0.0093  0.0065  0.0347  431  GLU   A OE1 
3128 O  OE2 . GLU   A 431 ? 0.1926 0.2411 0.2145 0.0067  0.0046  0.0316  431  GLU   A OE2 
3129 N  N   . MET   A 432 ? 0.1531 0.1813 0.1738 0.0137  0.0105  0.0290  432  MET   A N   
3130 C  CA  . MET   A 432 ? 0.1559 0.1801 0.1754 0.0142  0.0113  0.0281  432  MET   A CA  
3131 C  C   . MET   A 432 ? 0.1654 0.1857 0.1826 0.0137  0.0107  0.0257  432  MET   A C   
3132 O  O   . MET   A 432 ? 0.1589 0.1761 0.1746 0.0137  0.0110  0.0246  432  MET   A O   
3133 C  CB  . MET   A 432 ? 0.1637 0.1865 0.1843 0.0157  0.0133  0.0296  432  MET   A CB  
3134 C  CG  . MET   A 432 ? 0.1604 0.1870 0.1837 0.0164  0.0141  0.0322  432  MET   A CG  
3135 S  SD  . MET   A 432 ? 0.2034 0.2314 0.2268 0.0157  0.0138  0.0323  432  MET   A SD  
3136 C  CE  . MET   A 432 ? 0.1933 0.2155 0.2150 0.0167  0.0156  0.0313  432  MET   A CE  
3137 N  N   . PHE   A 433 ? 0.1588 0.1794 0.1757 0.0133  0.0099  0.0249  433  PHE   A N   
3138 C  CA  . PHE   A 433 ? 0.1675 0.1849 0.1825 0.0128  0.0093  0.0228  433  PHE   A CA  
3139 C  C   . PHE   A 433 ? 0.1925 0.2107 0.2066 0.0117  0.0079  0.0215  433  PHE   A C   
3140 O  O   . PHE   A 433 ? 0.2291 0.2491 0.2432 0.0109  0.0070  0.0210  433  PHE   A O   
3141 C  CB  . PHE   A 433 ? 0.1494 0.1667 0.1647 0.0129  0.0091  0.0227  433  PHE   A CB  
3142 C  CG  . PHE   A 433 ? 0.1593 0.1750 0.1751 0.0140  0.0106  0.0238  433  PHE   A CG  
3143 C  CD1 . PHE   A 433 ? 0.1670 0.1851 0.1846 0.0148  0.0115  0.0260  433  PHE   A CD1 
3144 C  CD2 . PHE   A 433 ? 0.1686 0.1803 0.1830 0.0141  0.0110  0.0228  433  PHE   A CD2 
3145 C  CE1 . PHE   A 433 ? 0.1746 0.1909 0.1927 0.0159  0.0131  0.0270  433  PHE   A CE1 
3146 C  CE2 . PHE   A 433 ? 0.1684 0.1781 0.1829 0.0150  0.0125  0.0237  433  PHE   A CE2 
3147 C  CZ  . PHE   A 433 ? 0.1608 0.1727 0.1773 0.0159  0.0137  0.0258  433  PHE   A CZ  
3148 N  N   . ASP   A 434 ? 0.1638 0.1810 0.1772 0.0115  0.0080  0.0212  434  ASP   A N   
3149 C  CA  . ASP   A 434 ? 0.1602 0.1782 0.1727 0.0104  0.0070  0.0201  434  ASP   A CA  
3150 C  C   . ASP   A 434 ? 0.1679 0.1825 0.1787 0.0103  0.0069  0.0190  434  ASP   A C   
3151 O  O   . ASP   A 434 ? 0.1696 0.1814 0.1798 0.0110  0.0077  0.0189  434  ASP   A O   
3152 C  CB  . ASP   A 434 ? 0.1714 0.1933 0.1852 0.0098  0.0068  0.0214  434  ASP   A CB  
3153 C  CG  . ASP   A 434 ? 0.1951 0.2173 0.2096 0.0103  0.0077  0.0227  434  ASP   A CG  
3154 O  OD1 . ASP   A 434 ? 0.1804 0.1995 0.1943 0.0112  0.0087  0.0225  434  ASP   A OD1 
3155 O  OD2 . ASP   A 434 ? 0.2077 0.2334 0.2234 0.0097  0.0076  0.0238  434  ASP   A OD2 
3156 N  N   . ASP   A 435 ? 0.1780 0.1927 0.1880 0.0094  0.0062  0.0180  435  ASP   A N   
3157 C  CA  . ASP   A 435 ? 0.1812 0.1927 0.1895 0.0093  0.0060  0.0169  435  ASP   A CA  
3158 C  C   . ASP   A 435 ? 0.1803 0.1910 0.1886 0.0098  0.0071  0.0177  435  ASP   A C   
3159 O  O   . ASP   A 435 ? 0.1878 0.1954 0.1946 0.0098  0.0072  0.0170  435  ASP   A O   
3160 C  CB  . ASP   A 435 ? 0.2199 0.2314 0.2273 0.0083  0.0051  0.0157  435  ASP   A CB  
3161 C  CG  . ASP   A 435 ? 0.3183 0.3297 0.3254 0.0080  0.0043  0.0146  435  ASP   A CG  
3162 O  OD1 . ASP   A 435 ? 0.2982 0.3088 0.3056 0.0086  0.0044  0.0146  435  ASP   A OD1 
3163 O  OD2 . ASP   A 435 ? 0.3633 0.3751 0.3698 0.0072  0.0038  0.0138  435  ASP   A OD2 
3164 N  N   . VAL   A 436 ? 0.1788 0.1924 0.1888 0.0100  0.0077  0.0194  436  VAL   A N   
3165 C  CA  . VAL   A 436 ? 0.1715 0.1843 0.1818 0.0105  0.0089  0.0203  436  VAL   A CA  
3166 C  C   . VAL   A 436 ? 0.1761 0.1860 0.1859 0.0117  0.0101  0.0206  436  VAL   A C   
3167 O  O   . VAL   A 436 ? 0.1822 0.1889 0.1905 0.0119  0.0108  0.0201  436  VAL   A O   
3168 C  CB  . VAL   A 436 ? 0.1881 0.2052 0.2006 0.0105  0.0094  0.0222  436  VAL   A CB  
3169 C  CG1 . VAL   A 436 ? 0.1831 0.1994 0.1962 0.0113  0.0109  0.0234  436  VAL   A CG1 
3170 C  CG2 . VAL   A 436 ? 0.2003 0.2198 0.2126 0.0090  0.0082  0.0218  436  VAL   A CG2 
3171 N  N   . SER   A 437 ? 0.1682 0.1790 0.1791 0.0123  0.0104  0.0213  437  SER   A N   
3172 C  CA  . SER   A 437 ? 0.1592 0.1668 0.1695 0.0132  0.0117  0.0214  437  SER   A CA  
3173 C  C   . SER   A 437 ? 0.1688 0.1724 0.1766 0.0128  0.0111  0.0196  437  SER   A C   
3174 O  O   . SER   A 437 ? 0.1845 0.1846 0.1907 0.0131  0.0121  0.0194  437  SER   A O   
3175 C  CB  . SER   A 437 ? 0.1724 0.1816 0.1842 0.0138  0.0121  0.0225  437  SER   A CB  
3176 O  OG  . SER   A 437 ? 0.1729 0.1857 0.1872 0.0144  0.0128  0.0245  437  SER   A OG  
3177 N  N   . TYR   A 438 ? 0.1701 0.1742 0.1775 0.0121  0.0096  0.0185  438  TYR   A N   
3178 C  CA  . TYR   A 438 ? 0.1719 0.1727 0.1773 0.0117  0.0089  0.0170  438  TYR   A CA  
3179 C  C   . TYR   A 438 ? 0.1678 0.1665 0.1714 0.0112  0.0084  0.0160  438  TYR   A C   
3180 O  O   . TYR   A 438 ? 0.1717 0.1671 0.1734 0.0112  0.0088  0.0156  438  TYR   A O   
3181 C  CB  . TYR   A 438 ? 0.1709 0.1731 0.1768 0.0112  0.0076  0.0163  438  TYR   A CB  
3182 C  CG  . TYR   A 438 ? 0.1613 0.1643 0.1683 0.0116  0.0079  0.0168  438  TYR   A CG  
3183 C  CD1 . TYR   A 438 ? 0.1697 0.1759 0.1787 0.0120  0.0084  0.0181  438  TYR   A CD1 
3184 C  CD2 . TYR   A 438 ? 0.1649 0.1659 0.1711 0.0114  0.0075  0.0160  438  TYR   A CD2 
3185 C  CE1 . TYR   A 438 ? 0.1707 0.1775 0.1806 0.0123  0.0088  0.0187  438  TYR   A CE1 
3186 C  CE2 . TYR   A 438 ? 0.1612 0.1630 0.1685 0.0117  0.0078  0.0165  438  TYR   A CE2 
3187 C  CZ  . TYR   A 438 ? 0.1716 0.1761 0.1806 0.0122  0.0084  0.0178  438  TYR   A CZ  
3188 O  OH  . TYR   A 438 ? 0.1885 0.1938 0.1985 0.0124  0.0088  0.0184  438  TYR   A OH  
3189 N  N   . ASP   A 439 ? 0.1658 0.1664 0.1698 0.0106  0.0075  0.0157  439  ASP   A N   
3190 C  CA  . ASP   A 439 ? 0.1710 0.1696 0.1733 0.0101  0.0069  0.0147  439  ASP   A CA  
3191 C  C   . ASP   A 439 ? 0.1731 0.1711 0.1749 0.0102  0.0079  0.0153  439  ASP   A C   
3192 O  O   . ASP   A 439 ? 0.1766 0.1715 0.1765 0.0101  0.0081  0.0148  439  ASP   A O   
3193 C  CB  . ASP   A 439 ? 0.1824 0.1828 0.1851 0.0094  0.0057  0.0140  439  ASP   A CB  
3194 C  CG  . ASP   A 439 ? 0.2369 0.2376 0.2400 0.0093  0.0048  0.0133  439  ASP   A CG  
3195 O  OD1 . ASP   A 439 ? 0.2405 0.2393 0.2430 0.0096  0.0047  0.0131  439  ASP   A OD1 
3196 O  OD2 . ASP   A 439 ? 0.2729 0.2755 0.2766 0.0089  0.0042  0.0130  439  ASP   A OD2 
3197 N  N   . LYS   A 440 ? 0.1754 0.1764 0.1790 0.0103  0.0085  0.0164  440  LYS   A N   
3198 C  CA  . LYS   A 440 ? 0.1672 0.1676 0.1705 0.0105  0.0096  0.0171  440  LYS   A CA  
3199 C  C   . LYS   A 440 ? 0.1854 0.1830 0.1878 0.0113  0.0111  0.0175  440  LYS   A C   
3200 O  O   . LYS   A 440 ? 0.1920 0.1868 0.1927 0.0113  0.0118  0.0172  440  LYS   A O   
3201 C  CB  . LYS   A 440 ? 0.1731 0.1775 0.1786 0.0103  0.0100  0.0184  440  LYS   A CB  
3202 C  CG  . LYS   A 440 ? 0.1790 0.1828 0.1844 0.0106  0.0112  0.0192  440  LYS   A CG  
3203 C  CD  . LYS   A 440 ? 0.1762 0.1844 0.1840 0.0103  0.0114  0.0206  440  LYS   A CD  
3204 C  CE  . LYS   A 440 ? 0.1734 0.1814 0.1816 0.0106  0.0128  0.0217  440  LYS   A CE  
3205 N  NZ  . LYS   A 440 ? 0.1764 0.1890 0.1870 0.0101  0.0127  0.0231  440  LYS   A NZ  
3206 N  N   . GLY   A 441 ? 0.1844 0.1823 0.1877 0.0119  0.0117  0.0181  441  GLY   A N   
3207 C  CA  . GLY   A 441 ? 0.1864 0.1811 0.1886 0.0126  0.0132  0.0184  441  GLY   A CA  
3208 C  C   . GLY   A 441 ? 0.1889 0.1793 0.1880 0.0121  0.0128  0.0169  441  GLY   A C   
3209 O  O   . GLY   A 441 ? 0.1855 0.1728 0.1828 0.0122  0.0140  0.0169  441  GLY   A O   
3210 N  N   . ALA   A 442 ? 0.1802 0.1703 0.1786 0.0114  0.0111  0.0158  442  ALA   A N   
3211 C  CA  . ALA   A 442 ? 0.1856 0.1720 0.1811 0.0108  0.0105  0.0146  442  ALA   A CA  
3212 C  C   . ALA   A 442 ? 0.1819 0.1670 0.1759 0.0104  0.0103  0.0142  442  ALA   A C   
3213 O  O   . ALA   A 442 ? 0.2018 0.1835 0.1933 0.0101  0.0108  0.0137  442  ALA   A O   
3214 C  CB  . ALA   A 442 ? 0.1894 0.1762 0.1849 0.0102  0.0086  0.0137  442  ALA   A CB  
3215 N  N   . CYS   A 443 ? 0.1800 0.1679 0.1755 0.0102  0.0098  0.0144  443  CYS   A N   
3216 C  CA  . CYS   A 443 ? 0.1869 0.1736 0.1810 0.0098  0.0096  0.0141  443  CYS   A CA  
3217 C  C   . CYS   A 443 ? 0.2031 0.1885 0.1965 0.0101  0.0114  0.0148  443  CYS   A C   
3218 O  O   . CYS   A 443 ? 0.2126 0.1951 0.2037 0.0098  0.0115  0.0143  443  CYS   A O   
3219 C  CB  . CYS   A 443 ? 0.2064 0.1961 0.2021 0.0094  0.0086  0.0140  443  CYS   A CB  
3220 S  SG  . CYS   A 443 ? 0.2522 0.2427 0.2482 0.0090  0.0067  0.0130  443  CYS   A SG  
3221 N  N   . ILE   A 444 ? 0.1836 0.1708 0.1790 0.0109  0.0129  0.0160  444  ILE   A N   
3222 C  CA  . ILE   A 444 ? 0.1966 0.1824 0.1915 0.0114  0.0148  0.0168  444  ILE   A CA  
3223 C  C   . ILE   A 444 ? 0.2068 0.1881 0.1990 0.0115  0.0159  0.0163  444  ILE   A C   
3224 O  O   . ILE   A 444 ? 0.2018 0.1803 0.1920 0.0115  0.0172  0.0162  444  ILE   A O   
3225 C  CB  . ILE   A 444 ? 0.2037 0.1931 0.2018 0.0122  0.0161  0.0185  444  ILE   A CB  
3226 C  CG1 . ILE   A 444 ? 0.2085 0.1986 0.2080 0.0130  0.0167  0.0192  444  ILE   A CG1 
3227 C  CG2 . ILE   A 444 ? 0.2034 0.1970 0.2036 0.0117  0.0149  0.0188  444  ILE   A CG2 
3228 C  CD1 . ILE   A 444 ? 0.2151 0.2087 0.2179 0.0140  0.0182  0.0212  444  ILE   A CD1 
3229 N  N   . LEU   A 445 ? 0.1967 0.1769 0.1884 0.0115  0.0155  0.0158  445  LEU   A N   
3230 C  CA  . LEU   A 445 ? 0.1998 0.1754 0.1884 0.0113  0.0164  0.0152  445  LEU   A CA  
3231 C  C   . LEU   A 445 ? 0.1900 0.1629 0.1755 0.0102  0.0151  0.0139  445  LEU   A C   
3232 O  O   . LEU   A 445 ? 0.2029 0.1719 0.1853 0.0099  0.0161  0.0135  445  LEU   A O   
3233 C  CB  . LEU   A 445 ? 0.1992 0.1746 0.1881 0.0113  0.0160  0.0150  445  LEU   A CB  
3234 C  CG  . LEU   A 445 ? 0.1969 0.1743 0.1884 0.0125  0.0175  0.0163  445  LEU   A CG  
3235 C  CD1 . LEU   A 445 ? 0.2022 0.1797 0.1941 0.0123  0.0169  0.0160  445  LEU   A CD1 
3236 C  CD2 . LEU   A 445 ? 0.2045 0.1790 0.1949 0.0132  0.0203  0.0169  445  LEU   A CD2 
3237 N  N   . ASN   A 446 ? 0.1957 0.1704 0.1817 0.0096  0.0129  0.0133  446  ASN   A N   
3238 C  CA  . ASN   A 446 ? 0.1998 0.1721 0.1831 0.0087  0.0116  0.0124  446  ASN   A CA  
3239 C  C   . ASN   A 446 ? 0.2175 0.1885 0.1995 0.0087  0.0126  0.0126  446  ASN   A C   
3240 O  O   . ASN   A 446 ? 0.2188 0.1862 0.1976 0.0081  0.0129  0.0121  446  ASN   A O   
3241 C  CB  . ASN   A 446 ? 0.1961 0.1710 0.1809 0.0084  0.0094  0.0121  446  ASN   A CB  
3242 C  CG  . ASN   A 446 ? 0.2416 0.2142 0.2239 0.0076  0.0081  0.0113  446  ASN   A CG  
3243 O  OD1 . ASN   A 446 ? 0.2472 0.2170 0.2270 0.0070  0.0076  0.0109  446  ASN   A OD1 
3244 N  ND2 . ASN   A 446 ? 0.2574 0.2311 0.2402 0.0075  0.0074  0.0113  446  ASN   A ND2 
3245 N  N   . MET   A 447 ? 0.2131 0.1871 0.1977 0.0092  0.0132  0.0134  447  MET   A N   
3246 C  CA  . MET   A 447 ? 0.2150 0.1881 0.1986 0.0092  0.0143  0.0137  447  MET   A CA  
3247 C  C   . MET   A 447 ? 0.2149 0.1848 0.1967 0.0095  0.0166  0.0140  447  MET   A C   
3248 O  O   . MET   A 447 ? 0.2350 0.2018 0.2139 0.0091  0.0172  0.0137  447  MET   A O   
3249 C  CB  . MET   A 447 ? 0.2303 0.2077 0.2174 0.0095  0.0144  0.0146  447  MET   A CB  
3250 C  CG  . MET   A 447 ? 0.2571 0.2343 0.2439 0.0095  0.0156  0.0151  447  MET   A CG  
3251 S  SD  . MET   A 447 ? 0.2249 0.2075 0.2156 0.0094  0.0151  0.0161  447  MET   A SD  
3252 C  CE  . MET   A 447 ? 0.2413 0.2272 0.2352 0.0105  0.0161  0.0174  447  MET   A CE  
3253 N  N   . LEU   A 448 ? 0.2111 0.1813 0.1941 0.0103  0.0180  0.0146  448  LEU   A N   
3254 C  CA  . LEU   A 448 ? 0.2218 0.1886 0.2030 0.0108  0.0205  0.0149  448  LEU   A CA  
3255 C  C   . LEU   A 448 ? 0.2317 0.1935 0.2083 0.0098  0.0203  0.0137  448  LEU   A C   
3256 O  O   . LEU   A 448 ? 0.2504 0.2086 0.2242 0.0096  0.0220  0.0135  448  LEU   A O   
3257 C  CB  . LEU   A 448 ? 0.2256 0.1939 0.2093 0.0119  0.0220  0.0159  448  LEU   A CB  
3258 C  CG  . LEU   A 448 ? 0.2424 0.2070 0.2245 0.0125  0.0249  0.0163  448  LEU   A CG  
3259 C  CD1 . LEU   A 448 ? 0.2520 0.2162 0.2341 0.0130  0.0268  0.0171  448  LEU   A CD1 
3260 C  CD2 . LEU   A 448 ? 0.2481 0.2141 0.2327 0.0136  0.0262  0.0173  448  LEU   A CD2 
3261 N  N   . ARG   A 449 ? 0.2127 0.1744 0.1887 0.0090  0.0183  0.0128  449  ARG   A N   
3262 C  CA  . ARG   A 449 ? 0.2229 0.1803 0.1947 0.0078  0.0177  0.0118  449  ARG   A CA  
3263 C  C   . ARG   A 449 ? 0.2330 0.1887 0.2021 0.0069  0.0169  0.0112  449  ARG   A C   
3264 O  O   . ARG   A 449 ? 0.2463 0.1978 0.2115 0.0062  0.0176  0.0107  449  ARG   A O   
3265 C  CB  . ARG   A 449 ? 0.2256 0.1842 0.1980 0.0072  0.0155  0.0112  449  ARG   A CB  
3266 C  CG  . ARG   A 449 ? 0.2399 0.1946 0.2081 0.0058  0.0147  0.0102  449  ARG   A CG  
3267 C  CD  . ARG   A 449 ? 0.2664 0.2229 0.2360 0.0054  0.0127  0.0100  449  ARG   A CD  
3268 N  NE  . ARG   A 449 ? 0.2694 0.2230 0.2355 0.0038  0.0115  0.0092  449  ARG   A NE  
3269 C  CZ  . ARG   A 449 ? 0.2840 0.2387 0.2500 0.0030  0.0089  0.0089  449  ARG   A CZ  
3270 N  NH1 . ARG   A 449 ? 0.2967 0.2546 0.2653 0.0036  0.0076  0.0092  449  ARG   A NH1 
3271 N  NH2 . ARG   A 449 ? 0.2985 0.2509 0.2616 0.0015  0.0078  0.0084  449  ARG   A NH2 
3272 N  N   . GLU   A 450 ? 0.2171 0.1757 0.1881 0.0070  0.0153  0.0114  450  GLU   A N   
3273 C  CA  . GLU   A 450 ? 0.2189 0.1757 0.1875 0.0063  0.0146  0.0111  450  GLU   A CA  
3274 C  C   . GLU   A 450 ? 0.2422 0.1970 0.2094 0.0065  0.0170  0.0114  450  GLU   A C   
3275 O  O   . GLU   A 450 ? 0.2490 0.2004 0.2124 0.0057  0.0172  0.0110  450  GLU   A O   
3276 C  CB  . GLU   A 450 ? 0.2343 0.1946 0.2054 0.0064  0.0128  0.0112  450  GLU   A CB  
3277 C  CG  . GLU   A 450 ? 0.2642 0.2262 0.2364 0.0061  0.0105  0.0108  450  GLU   A CG  
3278 C  CD  . GLU   A 450 ? 0.3236 0.2826 0.2924 0.0050  0.0090  0.0102  450  GLU   A CD  
3279 O  OE1 . GLU   A 450 ? 0.3312 0.2897 0.2994 0.0046  0.0083  0.0099  450  GLU   A OE1 
3280 O  OE2 . GLU   A 450 ? 0.3348 0.2922 0.3015 0.0045  0.0085  0.0101  450  GLU   A OE2 
3281 N  N   . TYR   A 451 ? 0.2357 0.1927 0.2058 0.0076  0.0188  0.0123  451  TYR   A N   
3282 C  CA  . TYR   A 451 ? 0.2542 0.2098 0.2236 0.0081  0.0212  0.0129  451  TYR   A CA  
3283 C  C   . TYR   A 451 ? 0.2587 0.2095 0.2245 0.0079  0.0234  0.0125  451  TYR   A C   
3284 O  O   . TYR   A 451 ? 0.2621 0.2095 0.2247 0.0075  0.0246  0.0123  451  TYR   A O   
3285 C  CB  . TYR   A 451 ? 0.2552 0.2150 0.2292 0.0094  0.0225  0.0142  451  TYR   A CB  
3286 C  CG  . TYR   A 451 ? 0.2475 0.2063 0.2215 0.0101  0.0253  0.0151  451  TYR   A CG  
3287 C  CD1 . TYR   A 451 ? 0.2654 0.2238 0.2385 0.0097  0.0257  0.0152  451  TYR   A CD1 
3288 C  CD2 . TYR   A 451 ? 0.2564 0.2149 0.2316 0.0112  0.0278  0.0159  451  TYR   A CD2 
3289 C  CE1 . TYR   A 451 ? 0.2754 0.2331 0.2489 0.0104  0.0284  0.0161  451  TYR   A CE1 
3290 C  CE2 . TYR   A 451 ? 0.2628 0.2203 0.2382 0.0120  0.0306  0.0169  451  TYR   A CE2 
3291 C  CZ  . TYR   A 451 ? 0.2824 0.2399 0.2572 0.0116  0.0309  0.0170  451  TYR   A CZ  
3292 O  OH  . TYR   A 451 ? 0.3216 0.2785 0.2970 0.0124  0.0338  0.0180  451  TYR   A OH  
3293 N  N   . LEU   A 452 ? 0.2512 0.2011 0.2171 0.0082  0.0240  0.0124  452  LEU   A N   
3294 C  CA  . LEU   A 452 ? 0.2553 0.2003 0.2176 0.0080  0.0262  0.0120  452  LEU   A CA  
3295 C  C   . LEU   A 452 ? 0.2630 0.2039 0.2203 0.0062  0.0249  0.0107  452  LEU   A C   
3296 O  O   . LEU   A 452 ? 0.2777 0.2139 0.2310 0.0056  0.0268  0.0101  452  LEU   A O   
3297 C  CB  . LEU   A 452 ? 0.2661 0.2116 0.2303 0.0088  0.0275  0.0124  452  LEU   A CB  
3298 C  CG  . LEU   A 452 ? 0.2870 0.2362 0.2559 0.0106  0.0291  0.0140  452  LEU   A CG  
3299 C  CD1 . LEU   A 452 ? 0.2900 0.2393 0.2604 0.0113  0.0301  0.0144  452  LEU   A CD1 
3300 C  CD2 . LEU   A 452 ? 0.3119 0.2595 0.2804 0.0114  0.0322  0.0147  452  LEU   A CD2 
3301 N  N   . SER   A 453 ? 0.2575 0.2002 0.2152 0.0054  0.0219  0.0102  453  SER   A N   
3302 C  CA  . SER   A 453 ? 0.2543 0.1947 0.2085 0.0037  0.0198  0.0092  453  SER   A CA  
3303 C  C   . SER   A 453 ? 0.2558 0.1964 0.2106 0.0035  0.0193  0.0089  453  SER   A C   
3304 O  O   . SER   A 453 ? 0.2603 0.2007 0.2164 0.0044  0.0213  0.0093  453  SER   A O   
3305 C  CB  . SER   A 453 ? 0.2752 0.2101 0.2237 0.0025  0.0210  0.0085  453  SER   A CB  
3306 O  OG  . SER   A 453 ? 0.2971 0.2283 0.2433 0.0024  0.0235  0.0082  453  SER   A OG  
3307 N  N   . ALA   A 454 ? 0.2495 0.1907 0.2035 0.0024  0.0165  0.0084  454  ALA   A N   
3308 C  CA  . ALA   A 454 ? 0.2563 0.1980 0.2111 0.0020  0.0158  0.0082  454  ALA   A CA  
3309 C  C   . ALA   A 454 ? 0.2678 0.2049 0.2192 0.0013  0.0179  0.0076  454  ALA   A C   
3310 O  O   . ALA   A 454 ? 0.2726 0.2103 0.2258 0.0019  0.0188  0.0078  454  ALA   A O   
3311 C  CB  . ALA   A 454 ? 0.2699 0.2124 0.2238 0.0007  0.0126  0.0078  454  ALA   A CB  
3312 N  N   . ASP   A 455 ? 0.2713 0.2038 0.2177 0.0001  0.0189  0.0070  455  ASP   A N   
3313 C  CA  . ASP   A 455 ? 0.2753 0.2029 0.2180 -0.0007 0.0212  0.0063  455  ASP   A CA  
3314 C  C   . ASP   A 455 ? 0.2793 0.2062 0.2239 0.0011  0.0247  0.0069  455  ASP   A C   
3315 O  O   . ASP   A 455 ? 0.2784 0.2036 0.2228 0.0012  0.0263  0.0068  455  ASP   A O   
3316 C  CB  . ASP   A 455 ? 0.2986 0.2211 0.2351 -0.0026 0.0214  0.0054  455  ASP   A CB  
3317 C  CG  . ASP   A 455 ? 0.3876 0.3104 0.3220 -0.0047 0.0180  0.0049  455  ASP   A CG  
3318 O  OD1 . ASP   A 455 ? 0.4375 0.3632 0.3745 -0.0048 0.0161  0.0050  455  ASP   A OD1 
3319 O  OD2 . ASP   A 455 ? 0.4288 0.3492 0.3593 -0.0061 0.0173  0.0045  455  ASP   A OD2 
3320 N  N   . ALA   A 456 ? 0.2666 0.1949 0.2130 0.0025  0.0260  0.0077  456  ALA   A N   
3321 C  CA  . ALA   A 456 ? 0.2616 0.1898 0.2102 0.0044  0.0294  0.0086  456  ALA   A CA  
3322 C  C   . ALA   A 456 ? 0.2565 0.1893 0.2105 0.0058  0.0289  0.0095  456  ALA   A C   
3323 O  O   . ALA   A 456 ? 0.2604 0.1923 0.2155 0.0068  0.0312  0.0100  456  ALA   A O   
3324 C  CB  . ALA   A 456 ? 0.2817 0.2111 0.2316 0.0054  0.0306  0.0093  456  ALA   A CB  
3325 N  N   . PHE   A 457 ? 0.2425 0.1802 0.1998 0.0059  0.0260  0.0098  457  PHE   A N   
3326 C  CA  . PHE   A 457 ? 0.2339 0.1761 0.1960 0.0070  0.0253  0.0106  457  PHE   A CA  
3327 C  C   . PHE   A 457 ? 0.2519 0.1923 0.2129 0.0063  0.0252  0.0101  457  PHE   A C   
3328 O  O   . PHE   A 457 ? 0.2459 0.1872 0.2093 0.0075  0.0266  0.0108  457  PHE   A O   
3329 C  CB  . PHE   A 457 ? 0.2343 0.1811 0.1991 0.0070  0.0222  0.0107  457  PHE   A CB  
3330 C  CG  . PHE   A 457 ? 0.2301 0.1818 0.1997 0.0080  0.0214  0.0116  457  PHE   A CG  
3331 C  CD1 . PHE   A 457 ? 0.2448 0.2002 0.2182 0.0095  0.0222  0.0128  457  PHE   A CD1 
3332 C  CD2 . PHE   A 457 ? 0.2403 0.1931 0.2105 0.0074  0.0196  0.0111  457  PHE   A CD2 
3333 C  CE1 . PHE   A 457 ? 0.2512 0.2111 0.2288 0.0103  0.0213  0.0135  457  PHE   A CE1 
3334 C  CE2 . PHE   A 457 ? 0.2426 0.1998 0.2170 0.0083  0.0188  0.0118  457  PHE   A CE2 
3335 C  CZ  . PHE   A 457 ? 0.2476 0.2083 0.2256 0.0097  0.0196  0.0130  457  PHE   A CZ  
3336 N  N   . LYS   A 458 ? 0.2502 0.1879 0.2074 0.0044  0.0236  0.0089  458  LYS   A N   
3337 C  CA  . LYS   A 458 ? 0.2521 0.1879 0.2079 0.0034  0.0234  0.0083  458  LYS   A CA  
3338 C  C   . LYS   A 458 ? 0.2622 0.1933 0.2157 0.0037  0.0269  0.0082  458  LYS   A C   
3339 O  O   . LYS   A 458 ? 0.2656 0.1969 0.2208 0.0042  0.0279  0.0086  458  LYS   A O   
3340 C  CB  . LYS   A 458 ? 0.2597 0.1934 0.2115 0.0011  0.0210  0.0071  458  LYS   A CB  
3341 C  CG  . LYS   A 458 ? 0.2878 0.2196 0.2380 -0.0003 0.0206  0.0065  458  LYS   A CG  
3342 C  CD  . LYS   A 458 ? 0.3063 0.2369 0.2530 -0.0027 0.0179  0.0056  458  LYS   A CD  
3343 C  CE  . LYS   A 458 ? 0.3625 0.2912 0.3073 -0.0044 0.0173  0.0049  458  LYS   A CE  
3344 N  NZ  . LYS   A 458 ? 0.3791 0.3067 0.3205 -0.0069 0.0146  0.0043  458  LYS   A NZ  
3345 N  N   . SER   A 459 ? 0.2681 0.1951 0.2181 0.0034  0.0290  0.0079  459  SER   A N   
3346 C  CA  . SER   A 459 ? 0.2710 0.1933 0.2189 0.0039  0.0328  0.0079  459  SER   A CA  
3347 C  C   . SER   A 459 ? 0.2642 0.1896 0.2173 0.0065  0.0348  0.0095  459  SER   A C   
3348 O  O   . SER   A 459 ? 0.2723 0.1955 0.2254 0.0070  0.0370  0.0097  459  SER   A O   
3349 C  CB  . SER   A 459 ? 0.3208 0.2385 0.2644 0.0035  0.0349  0.0074  459  SER   A CB  
3350 O  OG  . SER   A 459 ? 0.3738 0.2881 0.3121 0.0010  0.0333  0.0060  459  SER   A OG  
3351 N  N   . GLY   A 460 ? 0.2637 0.1940 0.2210 0.0080  0.0341  0.0106  460  GLY   A N   
3352 C  CA  . GLY   A 460 ? 0.2649 0.1989 0.2273 0.0103  0.0357  0.0124  460  GLY   A CA  
3353 C  C   . GLY   A 460 ? 0.2664 0.2032 0.2317 0.0105  0.0344  0.0127  460  GLY   A C   
3354 O  O   . GLY   A 460 ? 0.2695 0.2060 0.2366 0.0118  0.0367  0.0137  460  GLY   A O   
3355 N  N   . ILE   A 461 ? 0.2637 0.2029 0.2292 0.0092  0.0310  0.0119  461  ILE   A N   
3356 C  CA  . ILE   A 461 ? 0.2893 0.2313 0.2574 0.0092  0.0294  0.0121  461  ILE   A CA  
3357 C  C   . ILE   A 461 ? 0.2682 0.2057 0.2338 0.0087  0.0313  0.0117  461  ILE   A C   
3358 O  O   . ILE   A 461 ? 0.2622 0.2010 0.2305 0.0097  0.0323  0.0126  461  ILE   A O   
3359 C  CB  . ILE   A 461 ? 0.3152 0.2591 0.2827 0.0075  0.0255  0.0110  461  ILE   A CB  
3360 C  CG1 . ILE   A 461 ? 0.3523 0.3015 0.3232 0.0081  0.0233  0.0116  461  ILE   A CG1 
3361 C  CG2 . ILE   A 461 ? 0.3566 0.3005 0.3243 0.0067  0.0245  0.0107  461  ILE   A CG2 
3362 C  CD1 . ILE   A 461 ? 0.3394 0.2897 0.3094 0.0066  0.0202  0.0106  461  ILE   A CD1 
3363 N  N   . VAL   A 462 ? 0.2530 0.1852 0.2133 0.0069  0.0316  0.0103  462  VAL   A N   
3364 C  CA  . VAL   A 462 ? 0.2716 0.1989 0.2287 0.0058  0.0331  0.0095  462  VAL   A CA  
3365 C  C   . VAL   A 462 ? 0.2721 0.1967 0.2296 0.0075  0.0372  0.0104  462  VAL   A C   
3366 O  O   . VAL   A 462 ? 0.2782 0.2020 0.2366 0.0079  0.0384  0.0108  462  VAL   A O   
3367 C  CB  . VAL   A 462 ? 0.2974 0.2197 0.2484 0.0032  0.0325  0.0078  462  VAL   A CB  
3368 C  CG1 . VAL   A 462 ? 0.3116 0.2282 0.2587 0.0019  0.0345  0.0069  462  VAL   A CG1 
3369 C  CG2 . VAL   A 462 ? 0.3144 0.2398 0.2655 0.0016  0.0283  0.0071  462  VAL   A CG2 
3370 N  N   . GLN   A 463 ? 0.2647 0.1882 0.2220 0.0086  0.0394  0.0109  463  GLN   A N   
3371 C  CA  . GLN   A 463 ? 0.2620 0.1830 0.2201 0.0105  0.0435  0.0121  463  GLN   A CA  
3372 C  C   . GLN   A 463 ? 0.2586 0.1849 0.2227 0.0127  0.0437  0.0140  463  GLN   A C   
3373 O  O   . GLN   A 463 ? 0.2537 0.1782 0.2188 0.0138  0.0463  0.0149  463  GLN   A O   
3374 C  CB  . GLN   A 463 ? 0.2831 0.2027 0.2402 0.0113  0.0455  0.0124  463  GLN   A CB  
3375 C  CG  . GLN   A 463 ? 0.3933 0.3089 0.3502 0.0130  0.0503  0.0133  463  GLN   A CG  
3376 C  CD  . GLN   A 463 ? 0.4877 0.4083 0.4509 0.0158  0.0517  0.0158  463  GLN   A CD  
3377 O  OE1 . GLN   A 463 ? 0.4943 0.4213 0.4619 0.0165  0.0491  0.0168  463  GLN   A OE1 
3378 N  NE2 . GLN   A 463 ? 0.5182 0.4358 0.4818 0.0175  0.0558  0.0169  463  GLN   A NE2 
3379 N  N   . TYR   A 464 ? 0.2416 0.1743 0.2099 0.0133  0.0409  0.0148  464  TYR   A N   
3380 C  CA  . TYR   A 464 ? 0.2333 0.1714 0.2071 0.0151  0.0408  0.0167  464  TYR   A CA  
3381 C  C   . TYR   A 464 ? 0.2381 0.1761 0.2123 0.0146  0.0401  0.0165  464  TYR   A C   
3382 O  O   . TYR   A 464 ? 0.2411 0.1796 0.2178 0.0161  0.0420  0.0179  464  TYR   A O   
3383 C  CB  . TYR   A 464 ? 0.2319 0.1760 0.2088 0.0151  0.0377  0.0170  464  TYR   A CB  
3384 C  CG  . TYR   A 464 ? 0.2260 0.1762 0.2081 0.0164  0.0365  0.0186  464  TYR   A CG  
3385 C  CD1 . TYR   A 464 ? 0.2202 0.1737 0.2063 0.0185  0.0382  0.0207  464  TYR   A CD1 
3386 C  CD2 . TYR   A 464 ? 0.2228 0.1761 0.2061 0.0155  0.0335  0.0180  464  TYR   A CD2 
3387 C  CE1 . TYR   A 464 ? 0.2180 0.1775 0.2089 0.0194  0.0369  0.0222  464  TYR   A CE1 
3388 C  CE2 . TYR   A 464 ? 0.2117 0.1705 0.1995 0.0165  0.0325  0.0194  464  TYR   A CE2 
3389 C  CZ  . TYR   A 464 ? 0.2180 0.1800 0.2094 0.0184  0.0340  0.0215  464  TYR   A CZ  
3390 O  OH  . TYR   A 464 ? 0.2256 0.1934 0.2212 0.0191  0.0326  0.0228  464  TYR   A OH  
3391 N  N   . LEU   A 465 ? 0.2266 0.1640 0.1985 0.0125  0.0374  0.0149  465  LEU   A N   
3392 C  CA  . LEU   A 465 ? 0.2232 0.1607 0.1955 0.0119  0.0365  0.0146  465  LEU   A CA  
3393 C  C   . LEU   A 465 ? 0.2460 0.1776 0.2154 0.0117  0.0396  0.0144  465  LEU   A C   
3394 O  O   . LEU   A 465 ? 0.2597 0.1917 0.2311 0.0125  0.0406  0.0153  465  LEU   A O   
3395 C  CB  . LEU   A 465 ? 0.2260 0.1643 0.1965 0.0097  0.0330  0.0131  465  LEU   A CB  
3396 C  CG  . LEU   A 465 ? 0.2195 0.1637 0.1932 0.0098  0.0298  0.0133  465  LEU   A CG  
3397 C  CD1 . LEU   A 465 ? 0.2419 0.1858 0.2131 0.0075  0.0268  0.0117  465  LEU   A CD1 
3398 C  CD2 . LEU   A 465 ? 0.2211 0.1703 0.1995 0.0111  0.0291  0.0147  465  LEU   A CD2 
3399 N  N   . GLN   A 466 ? 0.2551 0.1808 0.2196 0.0107  0.0414  0.0132  466  GLN   A N   
3400 C  CA  . GLN   A 466 ? 0.2645 0.1838 0.2256 0.0103  0.0446  0.0127  466  GLN   A CA  
3401 C  C   . GLN   A 466 ? 0.2806 0.1997 0.2447 0.0130  0.0483  0.0147  466  GLN   A C   
3402 O  O   . GLN   A 466 ? 0.3077 0.2250 0.2724 0.0136  0.0501  0.0153  466  GLN   A O   
3403 C  CB  . GLN   A 466 ? 0.2937 0.2065 0.2485 0.0083  0.0457  0.0109  466  GLN   A CB  
3404 C  CG  . GLN   A 466 ? 0.3572 0.2695 0.3086 0.0053  0.0422  0.0091  466  GLN   A CG  
3405 C  CD  . GLN   A 466 ? 0.4648 0.3711 0.4097 0.0031  0.0428  0.0073  466  GLN   A CD  
3406 O  OE1 . GLN   A 466 ? 0.4637 0.3672 0.4068 0.0037  0.0451  0.0073  466  GLN   A OE1 
3407 N  NE2 . GLN   A 466 ? 0.4917 0.3965 0.4332 0.0003  0.0404  0.0058  466  GLN   A NE2 
3408 N  N   . LYS   A 467 ? 0.2617 0.1829 0.2281 0.0148  0.0494  0.0159  467  LYS   A N   
3409 C  CA  . LYS   A 467 ? 0.2699 0.1912 0.2393 0.0175  0.0531  0.0180  467  LYS   A CA  
3410 C  C   . LYS   A 467 ? 0.2670 0.1935 0.2418 0.0191  0.0525  0.0200  467  LYS   A C   
3411 O  O   . LYS   A 467 ? 0.2939 0.2190 0.2704 0.0209  0.0555  0.0215  467  LYS   A O   
3412 C  CB  . LYS   A 467 ? 0.2846 0.2081 0.2558 0.0188  0.0538  0.0190  467  LYS   A CB  
3413 C  CG  . LYS   A 467 ? 0.3577 0.2818 0.3325 0.0217  0.0575  0.0214  467  LYS   A CG  
3414 C  CD  . LYS   A 467 ? 0.4232 0.3474 0.3983 0.0227  0.0592  0.0221  467  LYS   A CD  
3415 C  CE  . LYS   A 467 ? 0.5097 0.4319 0.4868 0.0253  0.0639  0.0241  467  LYS   A CE  
3416 N  NZ  . LYS   A 467 ? 0.5524 0.4759 0.5308 0.0264  0.0653  0.0251  467  LYS   A NZ  
3417 N  N   . HIS   A 468 ? 0.2412 0.1738 0.2190 0.0187  0.0487  0.0201  468  HIS   A N   
3418 C  CA  . HIS   A 468 ? 0.2247 0.1628 0.2076 0.0202  0.0479  0.0220  468  HIS   A CA  
3419 C  C   . HIS   A 468 ? 0.2312 0.1696 0.2138 0.0189  0.0460  0.0212  468  HIS   A C   
3420 O  O   . HIS   A 468 ? 0.2266 0.1701 0.2132 0.0198  0.0446  0.0226  468  HIS   A O   
3421 C  CB  . HIS   A 468 ? 0.2349 0.1800 0.2219 0.0210  0.0455  0.0231  468  HIS   A CB  
3422 C  CG  . HIS   A 468 ? 0.2493 0.1945 0.2371 0.0223  0.0476  0.0241  468  HIS   A CG  
3423 N  ND1 . HIS   A 468 ? 0.2656 0.2117 0.2567 0.0247  0.0507  0.0265  468  HIS   A ND1 
3424 C  CD2 . HIS   A 468 ? 0.2559 0.2005 0.2418 0.0216  0.0471  0.0232  468  HIS   A CD2 
3425 C  CE1 . HIS   A 468 ? 0.2654 0.2113 0.2565 0.0254  0.0519  0.0270  468  HIS   A CE1 
3426 N  NE2 . HIS   A 468 ? 0.2611 0.2060 0.2491 0.0236  0.0499  0.0249  468  HIS   A NE2 
3427 N  N   . SER   A 469 ? 0.2267 0.1597 0.2044 0.0168  0.0459  0.0192  469  SER   A N   
3428 C  CA  . SER   A 469 ? 0.2322 0.1653 0.2095 0.0154  0.0443  0.0185  469  SER   A CA  
3429 C  C   . SER   A 469 ? 0.2352 0.1692 0.2156 0.0171  0.0461  0.0203  469  SER   A C   
3430 O  O   . SER   A 469 ? 0.2470 0.1774 0.2271 0.0185  0.0497  0.0213  469  SER   A O   
3431 C  CB  . SER   A 469 ? 0.2571 0.1834 0.2286 0.0130  0.0449  0.0163  469  SER   A CB  
3432 O  OG  . SER   A 469 ? 0.2625 0.1889 0.2313 0.0110  0.0421  0.0146  469  SER   A OG  
3433 N  N   . TYR   A 470 ? 0.2291 0.1679 0.2125 0.0170  0.0436  0.0208  470  TYR   A N   
3434 C  CA  . TYR   A 470 ? 0.2323 0.1728 0.2188 0.0184  0.0447  0.0226  470  TYR   A CA  
3435 C  C   . TYR   A 470 ? 0.2350 0.1788 0.2258 0.0212  0.0466  0.0252  470  TYR   A C   
3436 O  O   . TYR   A 470 ? 0.2438 0.1878 0.2368 0.0227  0.0485  0.0270  470  TYR   A O   
3437 C  CB  . TYR   A 470 ? 0.2294 0.1633 0.2126 0.0176  0.0472  0.0219  470  TYR   A CB  
3438 C  CG  . TYR   A 470 ? 0.2286 0.1599 0.2078 0.0146  0.0451  0.0194  470  TYR   A CG  
3439 C  CD1 . TYR   A 470 ? 0.2433 0.1785 0.2241 0.0135  0.0420  0.0191  470  TYR   A CD1 
3440 C  CD2 . TYR   A 470 ? 0.2402 0.1656 0.2142 0.0128  0.0458  0.0175  470  TYR   A CD2 
3441 C  CE1 . TYR   A 470 ? 0.2540 0.1874 0.2316 0.0108  0.0399  0.0170  470  TYR   A CE1 
3442 C  CE2 . TYR   A 470 ? 0.2693 0.1927 0.2398 0.0099  0.0437  0.0154  470  TYR   A CE2 
3443 C  CZ  . TYR   A 470 ? 0.2859 0.2136 0.2584 0.0090  0.0406  0.0152  470  TYR   A CZ  
3444 O  OH  . TYR   A 470 ? 0.3201 0.2463 0.2895 0.0062  0.0384  0.0134  470  TYR   A OH  
3445 N  N   . LYS   A 471 ? 0.2192 0.1662 0.2115 0.0218  0.0458  0.0257  471  LYS   A N   
3446 C  CA  . LYS   A 471 ? 0.2200 0.1709 0.2165 0.0243  0.0473  0.0283  471  LYS   A CA  
3447 C  C   . LYS   A 471 ? 0.2109 0.1686 0.2104 0.0243  0.0441  0.0286  471  LYS   A C   
3448 O  O   . LYS   A 471 ? 0.2081 0.1677 0.2068 0.0226  0.0409  0.0271  471  LYS   A O   
3449 C  CB  . LYS   A 471 ? 0.2581 0.2044 0.2529 0.0253  0.0508  0.0285  471  LYS   A CB  
3450 C  CG  . LYS   A 471 ? 0.2970 0.2361 0.2888 0.0255  0.0543  0.0283  471  LYS   A CG  
3451 C  CD  . LYS   A 471 ? 0.3923 0.3266 0.3820 0.0263  0.0578  0.0283  471  LYS   A CD  
3452 C  CE  . LYS   A 471 ? 0.4984 0.4260 0.4860 0.0270  0.0619  0.0285  471  LYS   A CE  
3453 N  NZ  . LYS   A 471 ? 0.5722 0.4930 0.5537 0.0243  0.0619  0.0256  471  LYS   A NZ  
3454 N  N   . ASN   A 472 ? 0.2032 0.1648 0.2063 0.0261  0.0450  0.0308  472  ASN   A N   
3455 C  CA  . ASN   A 472 ? 0.1983 0.1664 0.2042 0.0260  0.0422  0.0314  472  ASN   A CA  
3456 C  C   . ASN   A 472 ? 0.2035 0.1719 0.2096 0.0266  0.0431  0.0317  472  ASN   A C   
3457 O  O   . ASN   A 472 ? 0.2309 0.1960 0.2365 0.0278  0.0463  0.0325  472  ASN   A O   
3458 C  CB  . ASN   A 472 ? 0.1962 0.1704 0.2070 0.0275  0.0418  0.0340  472  ASN   A CB  
3459 C  CG  . ASN   A 472 ? 0.2035 0.1780 0.2145 0.0269  0.0407  0.0338  472  ASN   A CG  
3460 O  OD1 . ASN   A 472 ? 0.2071 0.1774 0.2167 0.0273  0.0428  0.0339  472  ASN   A OD1 
3461 N  ND2 . ASN   A 472 ? 0.1918 0.1709 0.2040 0.0260  0.0376  0.0335  472  ASN   A ND2 
3462 N  N   . THR   A 473 ? 0.1933 0.1654 0.1998 0.0256  0.0403  0.0309  473  THR   A N   
3463 C  CA  . THR   A 473 ? 0.1985 0.1710 0.2050 0.0258  0.0408  0.0310  473  THR   A CA  
3464 C  C   . THR   A 473 ? 0.2031 0.1826 0.2136 0.0262  0.0389  0.0325  473  THR   A C   
3465 O  O   . THR   A 473 ? 0.2173 0.2013 0.2298 0.0258  0.0366  0.0329  473  THR   A O   
3466 C  CB  . THR   A 473 ? 0.2107 0.1798 0.2128 0.0238  0.0392  0.0282  473  THR   A CB  
3467 O  OG1 . THR   A 473 ? 0.2082 0.1800 0.2103 0.0224  0.0358  0.0270  473  THR   A OG1 
3468 C  CG2 . THR   A 473 ? 0.2243 0.1861 0.2219 0.0231  0.0412  0.0266  473  THR   A CG2 
3469 N  N   . LYS   A 474 ? 0.1981 0.1785 0.2094 0.0268  0.0399  0.0332  474  LYS   A N   
3470 C  CA  . LYS   A 474 ? 0.2026 0.1890 0.2170 0.0268  0.0381  0.0343  474  LYS   A CA  
3471 C  C   . LYS   A 474 ? 0.2102 0.1946 0.2218 0.0256  0.0374  0.0325  474  LYS   A C   
3472 O  O   . LYS   A 474 ? 0.2109 0.1897 0.2188 0.0251  0.0388  0.0309  474  LYS   A O   
3473 C  CB  . LYS   A 474 ? 0.2564 0.2465 0.2751 0.0288  0.0402  0.0375  474  LYS   A CB  
3474 C  CG  . LYS   A 474 ? 0.3566 0.3422 0.3745 0.0301  0.0439  0.0382  474  LYS   A CG  
3475 C  CD  . LYS   A 474 ? 0.4640 0.4538 0.4867 0.0322  0.0460  0.0416  474  LYS   A CD  
3476 C  CE  . LYS   A 474 ? 0.5403 0.5328 0.5663 0.0336  0.0465  0.0438  474  LYS   A CE  
3477 N  NZ  . LYS   A 474 ? 0.5785 0.5777 0.6071 0.0327  0.0431  0.0446  474  LYS   A NZ  
3478 N  N   . ASN   A 475 ? 0.2375 0.2265 0.2508 0.0250  0.0355  0.0328  475  ASN   A N   
3479 C  CA  . ASN   A 475 ? 0.2546 0.2419 0.2654 0.0239  0.0349  0.0312  475  ASN   A CA  
3480 C  C   . ASN   A 475 ? 0.2776 0.2602 0.2864 0.0245  0.0377  0.0310  475  ASN   A C   
3481 O  O   . ASN   A 475 ? 0.2842 0.2624 0.2889 0.0234  0.0375  0.0289  475  ASN   A O   
3482 C  CB  . ASN   A 475 ? 0.2769 0.2697 0.2905 0.0236  0.0332  0.0321  475  ASN   A CB  
3483 C  CG  . ASN   A 475 ? 0.3087 0.3050 0.3228 0.0223  0.0301  0.0313  475  ASN   A CG  
3484 O  OD1 . ASN   A 475 ? 0.2935 0.2888 0.3066 0.0219  0.0290  0.0304  475  ASN   A OD1 
3485 N  ND2 . ASN   A 475 ? 0.3009 0.3007 0.3161 0.0215  0.0285  0.0314  475  ASN   A ND2 
3486 N  N   . GLU   A 476 ? 0.2793 0.2630 0.2909 0.0263  0.0404  0.0333  476  GLU   A N   
3487 C  CA  . GLU   A 476 ? 0.2869 0.2663 0.2968 0.0271  0.0435  0.0334  476  GLU   A CA  
3488 C  C   . GLU   A 476 ? 0.2841 0.2560 0.2891 0.0266  0.0451  0.0315  476  GLU   A C   
3489 O  O   . GLU   A 476 ? 0.3071 0.2745 0.3088 0.0262  0.0464  0.0303  476  GLU   A O   
3490 C  CB  . GLU   A 476 ? 0.3375 0.3195 0.3518 0.0293  0.0463  0.0366  476  GLU   A CB  
3491 C  CG  . GLU   A 476 ? 0.4488 0.4273 0.4621 0.0303  0.0497  0.0370  476  GLU   A CG  
3492 C  CD  . GLU   A 476 ? 0.5735 0.5565 0.5921 0.0324  0.0518  0.0403  476  GLU   A CD  
3493 O  OE1 . GLU   A 476 ? 0.5837 0.5712 0.6063 0.0334  0.0514  0.0425  476  GLU   A OE1 
3494 O  OE2 . GLU   A 476 ? 0.6025 0.5848 0.6213 0.0329  0.0537  0.0409  476  GLU   A OE2 
3495 N  N   . ASP   A 477 ? 0.2493 0.2196 0.2535 0.0264  0.0446  0.0309  477  ASP   A N   
3496 C  CA  . ASP   A 477 ? 0.2443 0.2076 0.2436 0.0256  0.0459  0.0290  477  ASP   A CA  
3497 C  C   . ASP   A 477 ? 0.2421 0.2030 0.2372 0.0234  0.0435  0.0263  477  ASP   A C   
3498 O  O   . ASP   A 477 ? 0.2570 0.2121 0.2478 0.0226  0.0449  0.0248  477  ASP   A O   
3499 C  CB  . ASP   A 477 ? 0.2434 0.2062 0.2431 0.0257  0.0456  0.0290  477  ASP   A CB  
3500 C  CG  . ASP   A 477 ? 0.2842 0.2489 0.2879 0.0279  0.0481  0.0318  477  ASP   A CG  
3501 O  OD1 . ASP   A 477 ? 0.3010 0.2628 0.3046 0.0294  0.0517  0.0329  477  ASP   A OD1 
3502 O  OD2 . ASP   A 477 ? 0.2552 0.2239 0.2618 0.0283  0.0468  0.0329  477  ASP   A OD2 
3503 N  N   . LEU   A 478 ? 0.2417 0.2069 0.2379 0.0223  0.0400  0.0257  478  LEU   A N   
3504 C  CA  . LEU   A 478 ? 0.2448 0.2081 0.2374 0.0204  0.0377  0.0234  478  LEU   A CA  
3505 C  C   . LEU   A 478 ? 0.2572 0.2189 0.2482 0.0202  0.0388  0.0232  478  LEU   A C   
3506 O  O   . LEU   A 478 ? 0.2710 0.2277 0.2575 0.0190  0.0390  0.0215  478  LEU   A O   
3507 C  CB  . LEU   A 478 ? 0.2444 0.2128 0.2390 0.0195  0.0341  0.0232  478  LEU   A CB  
3508 C  CG  . LEU   A 478 ? 0.2389 0.2059 0.2304 0.0177  0.0316  0.0210  478  LEU   A CG  
3509 C  CD1 . LEU   A 478 ? 0.2528 0.2145 0.2400 0.0165  0.0316  0.0193  478  LEU   A CD1 
3510 C  CD2 . LEU   A 478 ? 0.2458 0.2178 0.2396 0.0171  0.0285  0.0209  478  LEU   A CD2 
3511 N  N   . TRP   A 479 ? 0.2601 0.2256 0.2547 0.0215  0.0396  0.0250  479  TRP   A N   
3512 C  CA  . TRP   A 479 ? 0.2663 0.2303 0.2594 0.0213  0.0408  0.0248  479  TRP   A CA  
3513 C  C   . TRP   A 479 ? 0.2710 0.2289 0.2610 0.0218  0.0442  0.0245  479  TRP   A C   
3514 O  O   . TRP   A 479 ? 0.2794 0.2333 0.2654 0.0209  0.0447  0.0231  479  TRP   A O   
3515 C  CB  . TRP   A 479 ? 0.2696 0.2391 0.2674 0.0225  0.0412  0.0270  479  TRP   A CB  
3516 C  CG  . TRP   A 479 ? 0.2518 0.2279 0.2534 0.0222  0.0383  0.0278  479  TRP   A CG  
3517 C  CD1 . TRP   A 479 ? 0.2664 0.2481 0.2729 0.0234  0.0386  0.0302  479  TRP   A CD1 
3518 C  CD2 . TRP   A 479 ? 0.2393 0.2171 0.2401 0.0207  0.0348  0.0263  479  TRP   A CD2 
3519 N  NE1 . TRP   A 479 ? 0.2572 0.2436 0.2655 0.0226  0.0355  0.0302  479  TRP   A NE1 
3520 C  CE2 . TRP   A 479 ? 0.2403 0.2243 0.2452 0.0210  0.0333  0.0278  479  TRP   A CE2 
3521 C  CE3 . TRP   A 479 ? 0.2466 0.2212 0.2435 0.0191  0.0328  0.0240  479  TRP   A CE3 
3522 C  CZ2 . TRP   A 479 ? 0.2404 0.2272 0.2456 0.0198  0.0302  0.0268  479  TRP   A CZ2 
3523 C  CZ3 . TRP   A 479 ? 0.2516 0.2293 0.2493 0.0181  0.0297  0.0232  479  TRP   A CZ3 
3524 C  CH2 . TRP   A 479 ? 0.2389 0.2225 0.2406 0.0185  0.0285  0.0246  479  TRP   A CH2 
3525 N  N   . ASP   A 480 ? 0.2645 0.2212 0.2559 0.0234  0.0469  0.0258  480  ASP   A N   
3526 C  CA  . ASP   A 480 ? 0.2797 0.2301 0.2680 0.0239  0.0507  0.0256  480  ASP   A CA  
3527 C  C   . ASP   A 480 ? 0.2924 0.2367 0.2747 0.0219  0.0500  0.0229  480  ASP   A C   
3528 O  O   . ASP   A 480 ? 0.2973 0.2363 0.2754 0.0214  0.0519  0.0219  480  ASP   A O   
3529 C  CB  . ASP   A 480 ? 0.3136 0.2638 0.3045 0.0258  0.0533  0.0274  480  ASP   A CB  
3530 C  CG  . ASP   A 480 ? 0.3766 0.3320 0.3734 0.0281  0.0549  0.0304  480  ASP   A CG  
3531 O  OD1 . ASP   A 480 ? 0.3923 0.3505 0.3906 0.0282  0.0547  0.0311  480  ASP   A OD1 
3532 O  OD2 . ASP   A 480 ? 0.4192 0.3760 0.4190 0.0297  0.0563  0.0323  480  ASP   A OD2 
3533 N  N   . SER   A 481 ? 0.2866 0.2316 0.2682 0.0207  0.0473  0.0219  481  SER   A N   
3534 C  CA  . SER   A 481 ? 0.2893 0.2290 0.2654 0.0186  0.0464  0.0195  481  SER   A CA  
3535 C  C   . SER   A 481 ? 0.3105 0.2494 0.2836 0.0170  0.0444  0.0180  481  SER   A C   
3536 O  O   . SER   A 481 ? 0.3238 0.2571 0.2918 0.0157  0.0452  0.0164  481  SER   A O   
3537 C  CB  . SER   A 481 ? 0.2868 0.2282 0.2635 0.0177  0.0437  0.0189  481  SER   A CB  
3538 O  OG  . SER   A 481 ? 0.3102 0.2509 0.2886 0.0190  0.0458  0.0200  481  SER   A OG  
3539 N  N   . MET   A 482 ? 0.3063 0.2506 0.2823 0.0170  0.0418  0.0184  482  MET   A N   
3540 C  CA  . MET   A 482 ? 0.3357 0.2797 0.3093 0.0155  0.0397  0.0172  482  MET   A CA  
3541 C  C   . MET   A 482 ? 0.3671 0.3077 0.3383 0.0158  0.0423  0.0172  482  MET   A C   
3542 O  O   . MET   A 482 ? 0.3907 0.3274 0.3573 0.0142  0.0418  0.0157  482  MET   A O   
3543 C  CB  . MET   A 482 ? 0.3315 0.2820 0.3090 0.0155  0.0366  0.0177  482  MET   A CB  
3544 C  CG  . MET   A 482 ? 0.3798 0.3323 0.3580 0.0147  0.0338  0.0171  482  MET   A CG  
3545 S  SD  . MET   A 482 ? 0.4265 0.3753 0.3994 0.0123  0.0312  0.0147  482  MET   A SD  
3546 C  CE  . MET   A 482 ? 0.4626 0.4145 0.4376 0.0119  0.0285  0.0145  482  MET   A CE  
3547 N  N   . ALA   A 483 ? 0.3769 0.3186 0.3511 0.0177  0.0453  0.0190  483  ALA   A N   
3548 C  CA  . ALA   A 483 ? 0.4170 0.3556 0.3894 0.0181  0.0482  0.0192  483  ALA   A CA  
3549 C  C   . ALA   A 483 ? 0.4551 0.3863 0.4226 0.0179  0.0515  0.0183  483  ALA   A C   
3550 O  O   . ALA   A 483 ? 0.4825 0.4100 0.4472 0.0177  0.0537  0.0179  483  ALA   A O   
3551 C  CB  . ALA   A 483 ? 0.4153 0.3582 0.3930 0.0203  0.0502  0.0217  483  ALA   A CB  
3552 N  N   . SER   A 484 ? 0.4636 0.3924 0.4302 0.0178  0.0520  0.0179  484  SER   A N   
3553 C  CA  . SER   A 484 ? 0.4918 0.4132 0.4535 0.0174  0.0552  0.0169  484  SER   A CA  
3554 C  C   . SER   A 484 ? 0.5129 0.4291 0.4679 0.0147  0.0539  0.0144  484  SER   A C   
3555 O  O   . SER   A 484 ? 0.5443 0.4539 0.4944 0.0140  0.0566  0.0134  484  SER   A O   
3556 C  CB  . SER   A 484 ? 0.5269 0.4475 0.4896 0.0179  0.0559  0.0172  484  SER   A CB  
3557 O  OG  . SER   A 484 ? 0.5666 0.4882 0.5280 0.0160  0.0522  0.0158  484  SER   A OG  
3558 N  N   . ILE   A 485 ? 0.5002 0.4191 0.4547 0.0132  0.0501  0.0136  485  ILE   A N   
3559 C  CA  . ILE   A 485 ? 0.5097 0.4246 0.4583 0.0106  0.0483  0.0115  485  ILE   A CA  
3560 C  C   . ILE   A 485 ? 0.5327 0.4441 0.4775 0.0100  0.0498  0.0109  485  ILE   A C   
3561 O  O   . ILE   A 485 ? 0.5357 0.4506 0.4828 0.0107  0.0490  0.0117  485  ILE   A O   
3562 C  CB  . ILE   A 485 ? 0.5072 0.4267 0.4574 0.0095  0.0436  0.0110  485  ILE   A CB  
3563 C  CG1 . ILE   A 485 ? 0.5107 0.4331 0.4642 0.0100  0.0424  0.0115  485  ILE   A CG1 
3564 C  CG2 . ILE   A 485 ? 0.5158 0.4320 0.4604 0.0069  0.0414  0.0092  485  ILE   A CG2 
3565 C  CD1 . ILE   A 485 ? 0.5229 0.4399 0.4730 0.0093  0.0443  0.0107  485  ILE   A CD1 
3566 N  N   . GLY   A 488 ? 0.6139 0.5170 0.5589 0.0150  0.0637  0.0139  513  GLY   A N   
3567 C  CA  . GLY   A 488 ? 0.6142 0.5249 0.5661 0.0168  0.0625  0.0159  513  GLY   A CA  
3568 C  C   . GLY   A 488 ? 0.6148 0.5291 0.5667 0.0155  0.0586  0.0153  513  GLY   A C   
3569 O  O   . GLY   A 488 ? 0.6229 0.5357 0.5726 0.0149  0.0591  0.0150  513  GLY   A O   
3570 N  N   . GLY   A 489 ? 0.6030 0.5220 0.5576 0.0150  0.0548  0.0153  514  GLY   A N   
3571 C  CA  . GLY   A 489 ? 0.5938 0.5163 0.5488 0.0138  0.0510  0.0148  514  GLY   A CA  
3572 C  C   . GLY   A 489 ? 0.5769 0.5058 0.5375 0.0152  0.0503  0.0165  514  GLY   A C   
3573 O  O   . GLY   A 489 ? 0.5808 0.5111 0.5446 0.0170  0.0532  0.0182  514  GLY   A O   
3574 N  N   . VAL   A 490 ? 0.5476 0.4804 0.5095 0.0142  0.0466  0.0162  515  VAL   A N   
3575 C  CA  . VAL   A 490 ? 0.5125 0.4514 0.4793 0.0151  0.0455  0.0176  515  VAL   A CA  
3576 C  C   . VAL   A 490 ? 0.4746 0.4184 0.4470 0.0167  0.0457  0.0193  515  VAL   A C   
3577 O  O   . VAL   A 490 ? 0.4706 0.4148 0.4433 0.0165  0.0443  0.0189  515  VAL   A O   
3578 C  CB  . VAL   A 490 ? 0.5138 0.4546 0.4798 0.0135  0.0415  0.0166  515  VAL   A CB  
3579 C  CG1 . VAL   A 490 ? 0.5211 0.4683 0.4921 0.0141  0.0400  0.0178  515  VAL   A CG1 
3580 C  CG2 . VAL   A 490 ? 0.5199 0.4561 0.4804 0.0120  0.0414  0.0152  515  VAL   A CG2 
3581 N  N   . ASP   A 491 ? 0.4427 0.3900 0.4194 0.0183  0.0474  0.0212  516  ASP   A N   
3582 C  CA  . ASP   A 491 ? 0.4173 0.3696 0.3995 0.0198  0.0475  0.0231  516  ASP   A CA  
3583 C  C   . ASP   A 491 ? 0.3921 0.3502 0.3771 0.0190  0.0437  0.0232  516  ASP   A C   
3584 O  O   . ASP   A 491 ? 0.4089 0.3687 0.3940 0.0182  0.0424  0.0230  516  ASP   A O   
3585 C  CB  . ASP   A 491 ? 0.4249 0.3790 0.4107 0.0217  0.0509  0.0254  516  ASP   A CB  
3586 C  CG  . ASP   A 491 ? 0.4571 0.4154 0.4481 0.0234  0.0517  0.0275  516  ASP   A CG  
3587 O  OD1 . ASP   A 491 ? 0.4583 0.4134 0.4488 0.0246  0.0545  0.0280  516  ASP   A OD1 
3588 O  OD2 . ASP   A 491 ? 0.4619 0.4266 0.4572 0.0235  0.0495  0.0287  516  ASP   A OD2 
3589 N  N   . VAL   A 492 ? 0.3342 0.2948 0.3213 0.0192  0.0422  0.0234  517  VAL   A N   
3590 C  CA  . VAL   A 492 ? 0.3470 0.3119 0.3360 0.0184  0.0386  0.0230  517  VAL   A CA  
3591 C  C   . VAL   A 492 ? 0.3055 0.2767 0.3003 0.0197  0.0386  0.0253  517  VAL   A C   
3592 O  O   . VAL   A 492 ? 0.2774 0.2530 0.2743 0.0191  0.0359  0.0253  517  VAL   A O   
3593 C  CB  . VAL   A 492 ? 0.3983 0.3595 0.3843 0.0178  0.0379  0.0216  517  VAL   A CB  
3594 C  CG1 . VAL   A 492 ? 0.4069 0.3718 0.3949 0.0173  0.0349  0.0213  517  VAL   A CG1 
3595 C  CG2 . VAL   A 492 ? 0.4239 0.3792 0.4041 0.0163  0.0377  0.0195  517  VAL   A CG2 
3596 N  N   . LYS   A 493 ? 0.2877 0.2594 0.2850 0.0214  0.0415  0.0272  518  LYS   A N   
3597 C  CA  . LYS   A 493 ? 0.2671 0.2447 0.2698 0.0226  0.0414  0.0294  518  LYS   A CA  
3598 C  C   . LYS   A 493 ? 0.2426 0.2261 0.2487 0.0222  0.0397  0.0305  518  LYS   A C   
3599 O  O   . LYS   A 493 ? 0.2251 0.2132 0.2336 0.0218  0.0374  0.0310  518  LYS   A O   
3600 C  CB  . LYS   A 493 ? 0.2978 0.2746 0.3026 0.0247  0.0451  0.0315  518  LYS   A CB  
3601 C  CG  . LYS   A 493 ? 0.3225 0.3055 0.3329 0.0260  0.0451  0.0341  518  LYS   A CG  
3602 C  CD  . LYS   A 493 ? 0.3974 0.3788 0.4096 0.0283  0.0490  0.0362  518  LYS   A CD  
3603 C  CE  . LYS   A 493 ? 0.4883 0.4637 0.4968 0.0283  0.0501  0.0346  518  LYS   A CE  
3604 N  NZ  . LYS   A 493 ? 0.5079 0.4804 0.5173 0.0303  0.0542  0.0362  518  LYS   A NZ  
3605 N  N   . THR   A 494 ? 0.2333 0.2168 0.2393 0.0221  0.0409  0.0309  519  THR   A N   
3606 C  CA  . THR   A 494 ? 0.2385 0.2278 0.2478 0.0215  0.0393  0.0320  519  THR   A CA  
3607 C  C   . THR   A 494 ? 0.2251 0.2155 0.2328 0.0196  0.0357  0.0302  519  THR   A C   
3608 O  O   . THR   A 494 ? 0.2224 0.2178 0.2329 0.0191  0.0336  0.0309  519  THR   A O   
3609 C  CB  . THR   A 494 ? 0.2726 0.2614 0.2820 0.0217  0.0413  0.0327  519  THR   A CB  
3610 O  OG1 . THR   A 494 ? 0.3127 0.3011 0.3243 0.0237  0.0448  0.0347  519  THR   A OG1 
3611 C  CG2 . THR   A 494 ? 0.2875 0.2820 0.2999 0.0209  0.0396  0.0337  519  THR   A CG2 
3612 N  N   . MET   A 495 ? 0.2323 0.2176 0.2353 0.0186  0.0349  0.0279  520  MET   A N   
3613 C  CA  . MET   A 495 ? 0.2192 0.2050 0.2206 0.0170  0.0317  0.0261  520  MET   A CA  
3614 C  C   . MET   A 495 ? 0.2153 0.2036 0.2181 0.0169  0.0298  0.0261  520  MET   A C   
3615 O  O   . MET   A 495 ? 0.2049 0.1972 0.2095 0.0161  0.0276  0.0261  520  MET   A O   
3616 C  CB  . MET   A 495 ? 0.2305 0.2103 0.2266 0.0161  0.0314  0.0239  520  MET   A CB  
3617 C  CG  . MET   A 495 ? 0.2393 0.2192 0.2338 0.0146  0.0282  0.0222  520  MET   A CG  
3618 S  SD  . MET   A 495 ? 0.3321 0.3052 0.3206 0.0136  0.0278  0.0200  520  MET   A SD  
3619 C  CE  . MET   A 495 ? 0.3609 0.3339 0.3485 0.0128  0.0277  0.0198  520  MET   A CE  
3620 N  N   . MET   A 496 ? 0.2043 0.1900 0.2063 0.0177  0.0308  0.0259  521  MET   A N   
3621 C  CA  . MET   A 496 ? 0.1925 0.1800 0.1954 0.0175  0.0289  0.0256  521  MET   A CA  
3622 C  C   . MET   A 496 ? 0.1968 0.1901 0.2044 0.0183  0.0288  0.0277  521  MET   A C   
3623 O  O   . MET   A 496 ? 0.1921 0.1883 0.2008 0.0177  0.0267  0.0275  521  MET   A O   
3624 C  CB  . MET   A 496 ? 0.2142 0.1972 0.2144 0.0177  0.0296  0.0245  521  MET   A CB  
3625 C  CG  . MET   A 496 ? 0.2144 0.1924 0.2099 0.0165  0.0288  0.0224  521  MET   A CG  
3626 S  SD  . MET   A 496 ? 0.2410 0.2206 0.2355 0.0148  0.0252  0.0208  521  MET   A SD  
3627 C  CE  . MET   A 496 ? 0.2553 0.2375 0.2516 0.0148  0.0235  0.0207  521  MET   A CE  
3628 N  N   . ASN   A 497 ? 0.1941 0.1896 0.2045 0.0194  0.0309  0.0298  522  ASN   A N   
3629 C  CA  . ASN   A 497 ? 0.1971 0.1988 0.2121 0.0200  0.0305  0.0320  522  ASN   A CA  
3630 C  C   . ASN   A 497 ? 0.1862 0.1920 0.2022 0.0184  0.0280  0.0318  522  ASN   A C   
3631 O  O   . ASN   A 497 ? 0.1823 0.1926 0.2006 0.0180  0.0264  0.0326  522  ASN   A O   
3632 C  CB  . ASN   A 497 ? 0.2085 0.2116 0.2265 0.0216  0.0334  0.0346  522  ASN   A CB  
3633 C  CG  . ASN   A 497 ? 0.2442 0.2449 0.2626 0.0233  0.0357  0.0355  522  ASN   A CG  
3634 O  OD1 . ASN   A 497 ? 0.2583 0.2570 0.2751 0.0232  0.0350  0.0344  522  ASN   A OD1 
3635 N  ND2 . ASN   A 497 ? 0.2904 0.2909 0.3107 0.0250  0.0389  0.0374  522  ASN   A ND2 
3636 N  N   . THR   A 498 ? 0.1740 0.1781 0.1879 0.0174  0.0277  0.0306  523  THR   A N   
3637 C  CA  . THR   A 498 ? 0.1753 0.1829 0.1898 0.0158  0.0254  0.0303  523  THR   A CA  
3638 C  C   . THR   A 498 ? 0.1768 0.1843 0.1899 0.0147  0.0228  0.0286  523  THR   A C   
3639 O  O   . THR   A 498 ? 0.1811 0.1925 0.1956 0.0137  0.0210  0.0287  523  THR   A O   
3640 C  CB  . THR   A 498 ? 0.1842 0.1899 0.1968 0.0149  0.0255  0.0294  523  THR   A CB  
3641 O  OG1 . THR   A 498 ? 0.1915 0.1919 0.1998 0.0142  0.0249  0.0270  523  THR   A OG1 
3642 C  CG2 . THR   A 498 ? 0.1948 0.2004 0.2089 0.0160  0.0283  0.0311  523  THR   A CG2 
3643 N  N   . TRP   A 499 ? 0.1717 0.1747 0.1818 0.0149  0.0227  0.0269  524  TRP   A N   
3644 C  CA  . TRP   A 499 ? 0.1680 0.1708 0.1768 0.0140  0.0204  0.0253  524  TRP   A CA  
3645 C  C   . TRP   A 499 ? 0.1664 0.1715 0.1771 0.0146  0.0201  0.0261  524  TRP   A C   
3646 O  O   . TRP   A 499 ? 0.1761 0.1819 0.1863 0.0138  0.0182  0.0251  524  TRP   A O   
3647 C  CB  . TRP   A 499 ? 0.1693 0.1665 0.1741 0.0137  0.0202  0.0233  524  TRP   A CB  
3648 C  CG  . TRP   A 499 ? 0.1568 0.1517 0.1594 0.0128  0.0201  0.0224  524  TRP   A CG  
3649 C  CD1 . TRP   A 499 ? 0.1711 0.1624 0.1717 0.0132  0.0218  0.0222  524  TRP   A CD1 
3650 C  CD2 . TRP   A 499 ? 0.1665 0.1628 0.1687 0.0115  0.0183  0.0215  524  TRP   A CD2 
3651 N  NE1 . TRP   A 499 ? 0.1688 0.1593 0.1679 0.0122  0.0211  0.0214  524  TRP   A NE1 
3652 C  CE2 . TRP   A 499 ? 0.1647 0.1580 0.1647 0.0112  0.0189  0.0210  524  TRP   A CE2 
3653 C  CE3 . TRP   A 499 ? 0.1739 0.1732 0.1771 0.0106  0.0163  0.0212  524  TRP   A CE3 
3654 C  CZ2 . TRP   A 499 ? 0.1780 0.1714 0.1770 0.0100  0.0176  0.0201  524  TRP   A CZ2 
3655 C  CZ3 . TRP   A 499 ? 0.1752 0.1745 0.1774 0.0094  0.0151  0.0203  524  TRP   A CZ3 
3656 C  CH2 . TRP   A 499 ? 0.1922 0.1885 0.1923 0.0091  0.0158  0.0198  524  TRP   A CH2 
3657 N  N   . THR   A 500 ? 0.1744 0.1804 0.1872 0.0160  0.0219  0.0279  525  THR   A N   
3658 C  CA  . THR   A 500 ? 0.1675 0.1754 0.1821 0.0167  0.0218  0.0288  525  THR   A CA  
3659 C  C   . THR   A 500 ? 0.1824 0.1961 0.2011 0.0171  0.0219  0.0313  525  THR   A C   
3660 O  O   . THR   A 500 ? 0.1813 0.1976 0.2014 0.0171  0.0210  0.0319  525  THR   A O   
3661 C  CB  . THR   A 500 ? 0.1822 0.1860 0.1957 0.0179  0.0237  0.0288  525  THR   A CB  
3662 O  OG1 . THR   A 500 ? 0.1959 0.1984 0.2100 0.0191  0.0263  0.0301  525  THR   A OG1 
3663 C  CG2 . THR   A 500 ? 0.2009 0.1996 0.2104 0.0172  0.0230  0.0264  525  THR   A CG2 
3664 N  N   . LEU   A 501 ? 0.1945 0.2105 0.2151 0.0173  0.0229  0.0328  526  LEU   A N   
3665 C  CA  . LEU   A 501 ? 0.2069 0.2288 0.2317 0.0177  0.0231  0.0355  526  LEU   A CA  
3666 C  C   . LEU   A 501 ? 0.2228 0.2495 0.2488 0.0161  0.0212  0.0358  526  LEU   A C   
3667 O  O   . LEU   A 501 ? 0.2550 0.2870 0.2844 0.0161  0.0210  0.0382  526  LEU   A O   
3668 C  CB  . LEU   A 501 ? 0.2111 0.2330 0.2381 0.0195  0.0260  0.0377  526  LEU   A CB  
3669 C  CG  . LEU   A 501 ? 0.2310 0.2481 0.2567 0.0212  0.0282  0.0376  526  LEU   A CG  
3670 C  CD1 . LEU   A 501 ? 0.2425 0.2593 0.2703 0.0229  0.0313  0.0397  526  LEU   A CD1 
3671 C  CD2 . LEU   A 501 ? 0.2307 0.2494 0.2578 0.0218  0.0278  0.0384  526  LEU   A CD2 
3672 N  N   . GLN   A 502 ? 0.2104 0.2350 0.2336 0.0145  0.0198  0.0337  527  GLN   A N   
3673 C  CA  . GLN   A 502 ? 0.2249 0.2530 0.2485 0.0127  0.0180  0.0334  527  GLN   A CA  
3674 C  C   . GLN   A 502 ? 0.1988 0.2255 0.2200 0.0114  0.0159  0.0312  527  GLN   A C   
3675 O  O   . GLN   A 502 ? 0.1874 0.2093 0.2057 0.0116  0.0159  0.0292  527  GLN   A O   
3676 C  CB  . GLN   A 502 ? 0.2710 0.2969 0.2930 0.0119  0.0184  0.0325  527  GLN   A CB  
3677 C  CG  . GLN   A 502 ? 0.3387 0.3654 0.3627 0.0129  0.0205  0.0344  527  GLN   A CG  
3678 C  CD  . GLN   A 502 ? 0.3127 0.3377 0.3350 0.0119  0.0205  0.0334  527  GLN   A CD  
3679 O  OE1 . GLN   A 502 ? 0.3698 0.3985 0.3940 0.0109  0.0203  0.0345  527  GLN   A OE1 
3680 N  NE2 . GLN   A 502 ? 0.1998 0.2193 0.2186 0.0119  0.0208  0.0313  527  GLN   A NE2 
3681 N  N   . ARG   A 503 ? 0.1920 0.2227 0.2140 0.0100  0.0142  0.0314  528  ARG   A N   
3682 C  CA  . ARG   A 503 ? 0.1967 0.2258 0.2162 0.0087  0.0124  0.0292  528  ARG   A CA  
3683 C  C   . ARG   A 503 ? 0.1886 0.2146 0.2055 0.0076  0.0120  0.0272  528  ARG   A C   
3684 O  O   . ARG   A 503 ? 0.1941 0.2203 0.2114 0.0074  0.0127  0.0279  528  ARG   A O   
3685 C  CB  . ARG   A 503 ? 0.2093 0.2432 0.2300 0.0073  0.0108  0.0298  528  ARG   A CB  
3686 C  CG  . ARG   A 503 ? 0.2332 0.2704 0.2547 0.0056  0.0103  0.0304  528  ARG   A CG  
3687 C  CD  . ARG   A 503 ? 0.3066 0.3484 0.3288 0.0038  0.0086  0.0309  528  ARG   A CD  
3688 N  NE  . ARG   A 503 ? 0.3362 0.3819 0.3611 0.0046  0.0087  0.0332  528  ARG   A NE  
3689 C  CZ  . ARG   A 503 ? 0.3822 0.4328 0.4104 0.0048  0.0091  0.0359  528  ARG   A CZ  
3690 N  NH1 . ARG   A 503 ? 0.3917 0.4457 0.4222 0.0056  0.0092  0.0380  528  ARG   A NH1 
3691 N  NH2 . ARG   A 503 ? 0.3956 0.4478 0.4247 0.0040  0.0094  0.0367  528  ARG   A NH2 
3692 N  N   . GLY   A 504 ? 0.1859 0.2094 0.2003 0.0069  0.0108  0.0251  529  GLY   A N   
3693 C  CA  . GLY   A 504 ? 0.1916 0.2128 0.2037 0.0057  0.0101  0.0235  529  GLY   A CA  
3694 C  C   . GLY   A 504 ? 0.1830 0.1996 0.1932 0.0063  0.0110  0.0226  529  GLY   A C   
3695 O  O   . GLY   A 504 ? 0.1762 0.1903 0.1860 0.0077  0.0120  0.0227  529  GLY   A O   
3696 N  N   . PHE   A 505 ? 0.1608 0.1759 0.1693 0.0052  0.0105  0.0215  530  PHE   A N   
3697 C  CA  . PHE   A 505 ? 0.1697 0.1804 0.1760 0.0056  0.0112  0.0206  530  PHE   A CA  
3698 C  C   . PHE   A 505 ? 0.1670 0.1780 0.1728 0.0043  0.0111  0.0204  530  PHE   A C   
3699 O  O   . PHE   A 505 ? 0.1669 0.1808 0.1734 0.0029  0.0103  0.0205  530  PHE   A O   
3700 C  CB  . PHE   A 505 ? 0.1749 0.1818 0.1787 0.0057  0.0103  0.0187  530  PHE   A CB  
3701 C  CG  . PHE   A 505 ? 0.1682 0.1758 0.1713 0.0045  0.0088  0.0175  530  PHE   A CG  
3702 C  CD1 . PHE   A 505 ? 0.1857 0.1915 0.1871 0.0034  0.0083  0.0165  530  PHE   A CD1 
3703 C  CD2 . PHE   A 505 ? 0.1711 0.1809 0.1753 0.0043  0.0080  0.0175  530  PHE   A CD2 
3704 C  CE1 . PHE   A 505 ? 0.1799 0.1860 0.1806 0.0023  0.0072  0.0154  530  PHE   A CE1 
3705 C  CE2 . PHE   A 505 ? 0.1777 0.1879 0.1810 0.0031  0.0068  0.0164  530  PHE   A CE2 
3706 C  CZ  . PHE   A 505 ? 0.1897 0.1979 0.1913 0.0021  0.0065  0.0153  530  PHE   A CZ  
3707 N  N   . PRO   A 506 ? 0.1618 0.1695 0.1660 0.0046  0.0120  0.0201  531  PRO   A N   
3708 C  CA  . PRO   A 506 ? 0.1667 0.1745 0.1703 0.0034  0.0121  0.0200  531  PRO   A CA  
3709 C  C   . PRO   A 506 ? 0.1646 0.1694 0.1656 0.0024  0.0110  0.0182  531  PRO   A C   
3710 O  O   . PRO   A 506 ? 0.1689 0.1704 0.1679 0.0029  0.0104  0.0169  531  PRO   A O   
3711 C  CB  . PRO   A 506 ? 0.1761 0.1816 0.1793 0.0044  0.0138  0.0207  531  PRO   A CB  
3712 C  CG  . PRO   A 506 ? 0.1742 0.1762 0.1758 0.0057  0.0141  0.0200  531  PRO   A CG  
3713 C  CD  . PRO   A 506 ? 0.1657 0.1699 0.1688 0.0061  0.0133  0.0201  531  PRO   A CD  
3714 N  N   . LEU   A 507 ? 0.1629 0.1689 0.1639 0.0009  0.0107  0.0182  532  LEU   A N   
3715 C  CA  . LEU   A 507 ? 0.1654 0.1683 0.1639 -0.0001 0.0102  0.0168  532  LEU   A CA  
3716 C  C   . LEU   A 507 ? 0.1605 0.1612 0.1581 0.0002  0.0115  0.0173  532  LEU   A C   
3717 O  O   . LEU   A 507 ? 0.1641 0.1673 0.1634 0.0000  0.0124  0.0186  532  LEU   A O   
3718 C  CB  . LEU   A 507 ? 0.1827 0.1881 0.1816 -0.0021 0.0095  0.0166  532  LEU   A CB  
3719 C  CG  . LEU   A 507 ? 0.1997 0.2019 0.1962 -0.0032 0.0093  0.0154  532  LEU   A CG  
3720 C  CD1 . LEU   A 507 ? 0.2071 0.2052 0.2012 -0.0026 0.0086  0.0138  532  LEU   A CD1 
3721 C  CD2 . LEU   A 507 ? 0.2241 0.2288 0.2209 -0.0054 0.0089  0.0154  532  LEU   A CD2 
3722 N  N   . ILE   A 508 ? 0.1583 0.1545 0.1532 0.0007  0.0115  0.0162  533  ILE   A N   
3723 C  CA  . ILE   A 508 ? 0.1579 0.1513 0.1513 0.0009  0.0126  0.0164  533  ILE   A CA  
3724 C  C   . ILE   A 508 ? 0.1636 0.1553 0.1553 -0.0005 0.0120  0.0155  533  ILE   A C   
3725 O  O   . ILE   A 508 ? 0.1757 0.1652 0.1658 -0.0007 0.0110  0.0143  533  ILE   A O   
3726 C  CB  . ILE   A 508 ? 0.1730 0.1624 0.1642 0.0021  0.0129  0.0159  533  ILE   A CB  
3727 C  CG1 . ILE   A 508 ? 0.1797 0.1703 0.1724 0.0034  0.0134  0.0165  533  ILE   A CG1 
3728 C  CG2 . ILE   A 508 ? 0.1817 0.1681 0.1711 0.0022  0.0141  0.0160  533  ILE   A CG2 
3729 C  CD1 . ILE   A 508 ? 0.1860 0.1795 0.1812 0.0039  0.0151  0.0182  533  ILE   A CD1 
3730 N  N   . THR   A 509 ? 0.1656 0.1585 0.1578 -0.0015 0.0128  0.0162  534  THR   A N   
3731 C  CA  . THR   A 509 ? 0.1656 0.1567 0.1561 -0.0029 0.0124  0.0154  534  THR   A CA  
3732 C  C   . THR   A 509 ? 0.1722 0.1596 0.1605 -0.0026 0.0134  0.0154  534  THR   A C   
3733 O  O   . THR   A 509 ? 0.1779 0.1660 0.1670 -0.0021 0.0147  0.0165  534  THR   A O   
3734 C  CB  . THR   A 509 ? 0.1807 0.1755 0.1730 -0.0047 0.0124  0.0160  534  THR   A CB  
3735 O  OG1 . THR   A 509 ? 0.1935 0.1916 0.1874 -0.0051 0.0114  0.0159  534  THR   A OG1 
3736 C  CG2 . THR   A 509 ? 0.1974 0.1899 0.1876 -0.0063 0.0121  0.0151  534  THR   A CG2 
3737 N  N   . ILE   A 510 ? 0.1690 0.1524 0.1546 -0.0028 0.0128  0.0143  535  ILE   A N   
3738 C  CA  . ILE   A 510 ? 0.1740 0.1535 0.1571 -0.0025 0.0134  0.0142  535  ILE   A CA  
3739 C  C   . ILE   A 510 ? 0.1968 0.1750 0.1787 -0.0040 0.0135  0.0139  535  ILE   A C   
3740 O  O   . ILE   A 510 ? 0.2148 0.1926 0.1963 -0.0048 0.0126  0.0130  535  ILE   A O   
3741 C  CB  . ILE   A 510 ? 0.1877 0.1635 0.1685 -0.0015 0.0125  0.0133  535  ILE   A CB  
3742 C  CG1 . ILE   A 510 ? 0.1920 0.1689 0.1738 -0.0002 0.0124  0.0135  535  ILE   A CG1 
3743 C  CG2 . ILE   A 510 ? 0.2017 0.1733 0.1795 -0.0013 0.0130  0.0133  535  ILE   A CG2 
3744 C  CD1 . ILE   A 510 ? 0.1931 0.1702 0.1752 0.0006  0.0139  0.0145  535  ILE   A CD1 
3745 N  N   . THR   A 511 ? 0.1954 0.1729 0.1767 -0.0043 0.0147  0.0146  536  THR   A N   
3746 C  CA  . THR   A 511 ? 0.1995 0.1755 0.1796 -0.0058 0.0149  0.0143  536  THR   A CA  
3747 C  C   . THR   A 511 ? 0.2043 0.1763 0.1817 -0.0052 0.0157  0.0145  536  THR   A C   
3748 O  O   . THR   A 511 ? 0.2025 0.1747 0.1801 -0.0046 0.0170  0.0153  536  THR   A O   
3749 C  CB  . THR   A 511 ? 0.2161 0.1961 0.1986 -0.0071 0.0157  0.0153  536  THR   A CB  
3750 O  OG1 . THR   A 511 ? 0.2335 0.2177 0.2186 -0.0074 0.0150  0.0155  536  THR   A OG1 
3751 C  CG2 . THR   A 511 ? 0.2300 0.2087 0.2113 -0.0089 0.0159  0.0150  536  THR   A CG2 
3752 N  N   . VAL   A 512 ? 0.2167 0.1848 0.1914 -0.0054 0.0151  0.0137  537  VAL   A N   
3753 C  CA  . VAL   A 512 ? 0.2212 0.1852 0.1930 -0.0050 0.0156  0.0138  537  VAL   A CA  
3754 C  C   . VAL   A 512 ? 0.2362 0.1988 0.2069 -0.0063 0.0163  0.0139  537  VAL   A C   
3755 O  O   . VAL   A 512 ? 0.2496 0.2117 0.2201 -0.0074 0.0157  0.0134  537  VAL   A O   
3756 C  CB  . VAL   A 512 ? 0.2487 0.2095 0.2184 -0.0041 0.0143  0.0131  537  VAL   A CB  
3757 C  CG1 . VAL   A 512 ? 0.2765 0.2332 0.2429 -0.0037 0.0147  0.0134  537  VAL   A CG1 
3758 C  CG2 . VAL   A 512 ? 0.2576 0.2200 0.2285 -0.0029 0.0136  0.0130  537  VAL   A CG2 
3759 N  N   . ARG   A 513 ? 0.2248 0.1863 0.1944 -0.0064 0.0177  0.0147  538  ARG   A N   
3760 C  CA  . ARG   A 513 ? 0.2294 0.1892 0.1978 -0.0076 0.0185  0.0149  538  ARG   A CA  
3761 C  C   . ARG   A 513 ? 0.2245 0.1803 0.1896 -0.0069 0.0191  0.0151  538  ARG   A C   
3762 O  O   . ARG   A 513 ? 0.2305 0.1866 0.1956 -0.0065 0.0204  0.0158  538  ARG   A O   
3763 C  CB  . ARG   A 513 ? 0.2690 0.2326 0.2399 -0.0087 0.0197  0.0157  538  ARG   A CB  
3764 C  CG  . ARG   A 513 ? 0.3524 0.3197 0.3260 -0.0097 0.0188  0.0154  538  ARG   A CG  
3765 C  CD  . ARG   A 513 ? 0.4458 0.4179 0.4225 -0.0108 0.0196  0.0164  538  ARG   A CD  
3766 N  NE  . ARG   A 513 ? 0.5191 0.4947 0.4980 -0.0122 0.0186  0.0160  538  ARG   A NE  
3767 C  CZ  . ARG   A 513 ? 0.5737 0.5482 0.5517 -0.0126 0.0173  0.0149  538  ARG   A CZ  
3768 N  NH1 . ARG   A 513 ? 0.5407 0.5184 0.5203 -0.0141 0.0167  0.0147  538  ARG   A NH1 
3769 N  NH2 . ARG   A 513 ? 0.5988 0.5690 0.5742 -0.0116 0.0167  0.0140  538  ARG   A NH2 
3770 N  N   . GLY   A 514 ? 0.2470 0.1990 0.2094 -0.0067 0.0181  0.0146  539  GLY   A N   
3771 C  CA  . GLY   A 514 ? 0.2583 0.2065 0.2174 -0.0061 0.0184  0.0149  539  GLY   A CA  
3772 C  C   . GLY   A 514 ? 0.2539 0.2023 0.2127 -0.0048 0.0183  0.0149  539  GLY   A C   
3773 O  O   . GLY   A 514 ? 0.2664 0.2158 0.2262 -0.0041 0.0170  0.0145  539  GLY   A O   
3774 N  N   . ARG   A 515 ? 0.2329 0.1803 0.1904 -0.0046 0.0197  0.0154  540  ARG   A N   
3775 C  CA  . ARG   A 515 ? 0.2178 0.1650 0.1747 -0.0036 0.0199  0.0154  540  ARG   A CA  
3776 C  C   . ARG   A 515 ? 0.2095 0.1609 0.1700 -0.0031 0.0207  0.0156  540  ARG   A C   
3777 O  O   . ARG   A 515 ? 0.2092 0.1608 0.1698 -0.0022 0.0207  0.0155  540  ARG   A O   
3778 C  CB  . ARG   A 515 ? 0.2367 0.1806 0.1902 -0.0035 0.0214  0.0158  540  ARG   A CB  
3779 C  CG  . ARG   A 515 ? 0.2714 0.2110 0.2209 -0.0039 0.0205  0.0157  540  ARG   A CG  
3780 C  CD  . ARG   A 515 ? 0.2973 0.2339 0.2434 -0.0042 0.0223  0.0161  540  ARG   A CD  
3781 N  NE  . ARG   A 515 ? 0.3342 0.2703 0.2794 -0.0035 0.0233  0.0161  540  ARG   A NE  
3782 C  CZ  . ARG   A 515 ? 0.3489 0.2828 0.2917 -0.0036 0.0253  0.0163  540  ARG   A CZ  
3783 N  NH1 . ARG   A 515 ? 0.3862 0.3188 0.3278 -0.0044 0.0266  0.0168  540  ARG   A NH1 
3784 N  NH2 . ARG   A 515 ? 0.3561 0.2893 0.2980 -0.0030 0.0263  0.0162  540  ARG   A NH2 
3785 N  N   . ASN   A 516 ? 0.2025 0.1573 0.1661 -0.0038 0.0213  0.0160  541  ASN   A N   
3786 C  CA  . ASN   A 516 ? 0.1981 0.1571 0.1653 -0.0035 0.0221  0.0166  541  ASN   A CA  
3787 C  C   . ASN   A 516 ? 0.2031 0.1648 0.1726 -0.0032 0.0205  0.0161  541  ASN   A C   
3788 O  O   . ASN   A 516 ? 0.2066 0.1691 0.1768 -0.0040 0.0193  0.0156  541  ASN   A O   
3789 C  CB  . ASN   A 516 ? 0.1998 0.1615 0.1692 -0.0046 0.0232  0.0173  541  ASN   A CB  
3790 C  CG  . ASN   A 516 ? 0.2171 0.1833 0.1903 -0.0042 0.0243  0.0183  541  ASN   A CG  
3791 O  OD1 . ASN   A 516 ? 0.2278 0.1975 0.2038 -0.0042 0.0233  0.0183  541  ASN   A OD1 
3792 N  ND2 . ASN   A 516 ? 0.2387 0.2051 0.2122 -0.0039 0.0264  0.0192  541  ASN   A ND2 
3793 N  N   . VAL   A 517 ? 0.1917 0.1546 0.1622 -0.0020 0.0205  0.0161  542  VAL   A N   
3794 C  CA  . VAL   A 517 ? 0.1824 0.1480 0.1552 -0.0017 0.0191  0.0158  542  VAL   A CA  
3795 C  C   . VAL   A 517 ? 0.1838 0.1537 0.1602 -0.0014 0.0201  0.0167  542  VAL   A C   
3796 O  O   . VAL   A 517 ? 0.2013 0.1713 0.1780 -0.0004 0.0215  0.0173  542  VAL   A O   
3797 C  CB  . VAL   A 517 ? 0.1945 0.1576 0.1654 -0.0006 0.0182  0.0151  542  VAL   A CB  
3798 C  CG1 . VAL   A 517 ? 0.2090 0.1749 0.1822 -0.0002 0.0169  0.0148  542  VAL   A CG1 
3799 C  CG2 . VAL   A 517 ? 0.2108 0.1698 0.1782 -0.0009 0.0171  0.0145  542  VAL   A CG2 
3800 N  N   . HIS   A 518 ? 0.1682 0.1418 0.1472 -0.0023 0.0196  0.0169  543  HIS   A N   
3801 C  CA  . HIS   A 518 ? 0.1728 0.1512 0.1556 -0.0022 0.0203  0.0180  543  HIS   A CA  
3802 C  C   . HIS   A 518 ? 0.1748 0.1554 0.1593 -0.0016 0.0190  0.0177  543  HIS   A C   
3803 O  O   . HIS   A 518 ? 0.1775 0.1573 0.1611 -0.0020 0.0173  0.0166  543  HIS   A O   
3804 C  CB  . HIS   A 518 ? 0.1865 0.1678 0.1711 -0.0039 0.0202  0.0184  543  HIS   A CB  
3805 C  CG  . HIS   A 518 ? 0.2049 0.1916 0.1935 -0.0041 0.0208  0.0198  543  HIS   A CG  
3806 N  ND1 . HIS   A 518 ? 0.2276 0.2160 0.2177 -0.0041 0.0226  0.0212  543  HIS   A ND1 
3807 C  CD2 . HIS   A 518 ? 0.2223 0.2132 0.2137 -0.0044 0.0198  0.0201  543  HIS   A CD2 
3808 C  CE1 . HIS   A 518 ? 0.2547 0.2485 0.2487 -0.0043 0.0226  0.0225  543  HIS   A CE1 
3809 N  NE2 . HIS   A 518 ? 0.2523 0.2477 0.2471 -0.0045 0.0209  0.0219  543  HIS   A NE2 
3810 N  N   . MET   A 519 ? 0.1675 0.1505 0.1542 -0.0005 0.0199  0.0186  544  MET   A N   
3811 C  CA  . MET   A 519 ? 0.1744 0.1594 0.1627 0.0002  0.0188  0.0185  544  MET   A CA  
3812 C  C   . MET   A 519 ? 0.1820 0.1726 0.1744 0.0000  0.0193  0.0199  544  MET   A C   
3813 O  O   . MET   A 519 ? 0.1926 0.1848 0.1866 0.0004  0.0209  0.0212  544  MET   A O   
3814 C  CB  . MET   A 519 ? 0.1897 0.1722 0.1767 0.0017  0.0195  0.0183  544  MET   A CB  
3815 C  CG  . MET   A 519 ? 0.2063 0.1837 0.1893 0.0018  0.0188  0.0170  544  MET   A CG  
3816 S  SD  . MET   A 519 ? 0.2177 0.1914 0.1983 0.0032  0.0202  0.0170  544  MET   A SD  
3817 C  CE  . MET   A 519 ? 0.1932 0.1656 0.1729 0.0029  0.0225  0.0179  544  MET   A CE  
3818 N  N   . LYS   A 520 ? 0.1735 0.1670 0.1675 -0.0004 0.0178  0.0197  545  LYS   A N   
3819 C  CA  . LYS   A 520 ? 0.1718 0.1707 0.1696 -0.0005 0.0180  0.0211  545  LYS   A CA  
3820 C  C   . LYS   A 520 ? 0.1691 0.1691 0.1677 0.0002  0.0169  0.0208  545  LYS   A C   
3821 O  O   . LYS   A 520 ? 0.1753 0.1728 0.1718 0.0002  0.0156  0.0193  545  LYS   A O   
3822 C  CB  . LYS   A 520 ? 0.2115 0.2133 0.2102 -0.0026 0.0170  0.0212  545  LYS   A CB  
3823 C  CG  . LYS   A 520 ? 0.2774 0.2852 0.2798 -0.0032 0.0166  0.0226  545  LYS   A CG  
3824 C  CD  . LYS   A 520 ? 0.3198 0.3300 0.3224 -0.0056 0.0153  0.0222  545  LYS   A CD  
3825 C  CE  . LYS   A 520 ? 0.3628 0.3791 0.3690 -0.0061 0.0148  0.0238  545  LYS   A CE  
3826 N  NZ  . LYS   A 520 ? 0.3806 0.3992 0.3866 -0.0083 0.0132  0.0232  545  LYS   A NZ  
3827 N  N   . GLN   A 521 ? 0.1489 0.1527 0.1505 0.0010  0.0174  0.0223  546  GLN   A N   
3828 C  CA  . GLN   A 521 ? 0.1578 0.1633 0.1605 0.0015  0.0164  0.0221  546  GLN   A CA  
3829 C  C   . GLN   A 521 ? 0.1697 0.1811 0.1757 0.0005  0.0158  0.0235  546  GLN   A C   
3830 O  O   . GLN   A 521 ? 0.1764 0.1912 0.1848 0.0001  0.0166  0.0251  546  GLN   A O   
3831 C  CB  . GLN   A 521 ? 0.1670 0.1714 0.1701 0.0035  0.0175  0.0227  546  GLN   A CB  
3832 C  CG  . GLN   A 521 ? 0.1634 0.1703 0.1693 0.0044  0.0195  0.0248  546  GLN   A CG  
3833 C  CD  . GLN   A 521 ? 0.1734 0.1794 0.1799 0.0063  0.0206  0.0253  546  GLN   A CD  
3834 O  OE1 . GLN   A 521 ? 0.1810 0.1893 0.1890 0.0066  0.0197  0.0256  546  GLN   A OE1 
3835 N  NE2 . GLN   A 521 ? 0.1785 0.1809 0.1835 0.0075  0.0225  0.0254  546  GLN   A NE2 
3836 N  N   . GLU   A 522 ? 0.1686 0.1814 0.1747 0.0001  0.0143  0.0228  547  GLU   A N   
3837 C  CA  . GLU   A 522 ? 0.1751 0.1935 0.1841 -0.0009 0.0135  0.0241  547  GLU   A CA  
3838 C  C   . GLU   A 522 ? 0.1897 0.2084 0.1986 -0.0003 0.0124  0.0235  547  GLU   A C   
3839 O  O   . GLU   A 522 ? 0.1924 0.2070 0.1988 0.0001  0.0119  0.0218  547  GLU   A O   
3840 C  CB  . GLU   A 522 ? 0.2004 0.2206 0.2090 -0.0033 0.0125  0.0237  547  GLU   A CB  
3841 C  CG  . GLU   A 522 ? 0.2210 0.2381 0.2266 -0.0043 0.0111  0.0214  547  GLU   A CG  
3842 C  CD  . GLU   A 522 ? 0.2756 0.2925 0.2800 -0.0065 0.0107  0.0208  547  GLU   A CD  
3843 O  OE1 . GLU   A 522 ? 0.2439 0.2575 0.2466 -0.0066 0.0114  0.0203  547  GLU   A OE1 
3844 O  OE2 . GLU   A 522 ? 0.3255 0.3455 0.3305 -0.0084 0.0097  0.0208  547  GLU   A OE2 
3845 N  N   . HIS   A 523 ? 0.1837 0.2071 0.1953 -0.0004 0.0120  0.0249  548  HIS   A N   
3846 C  CA  . HIS   A 523 ? 0.1910 0.2147 0.2024 0.0000  0.0110  0.0243  548  HIS   A CA  
3847 C  C   . HIS   A 523 ? 0.2084 0.2309 0.2176 -0.0017 0.0095  0.0224  548  HIS   A C   
3848 O  O   . HIS   A 523 ? 0.2177 0.2424 0.2269 -0.0037 0.0088  0.0224  548  HIS   A O   
3849 C  CB  . HIS   A 523 ? 0.2046 0.2339 0.2194 0.0000  0.0109  0.0264  548  HIS   A CB  
3850 C  CG  . HIS   A 523 ? 0.2416 0.2721 0.2565 0.0002  0.0099  0.0261  548  HIS   A CG  
3851 N  ND1 . HIS   A 523 ? 0.3008 0.3365 0.3179 -0.0007 0.0090  0.0276  548  HIS   A ND1 
3852 C  CD2 . HIS   A 523 ? 0.2406 0.2676 0.2537 0.0012  0.0096  0.0247  548  HIS   A CD2 
3853 C  CE1 . HIS   A 523 ? 0.2963 0.3316 0.3129 -0.0002 0.0084  0.0269  548  HIS   A CE1 
3854 N  NE2 . HIS   A 523 ? 0.2697 0.3000 0.2842 0.0010  0.0088  0.0253  548  HIS   A NE2 
3855 N  N   . TYR   A 524 ? 0.1962 0.2151 0.2033 -0.0010 0.0090  0.0207  549  TYR   A N   
3856 C  CA  . TYR   A 524 ? 0.1974 0.2150 0.2025 -0.0023 0.0078  0.0190  549  TYR   A CA  
3857 C  C   . TYR   A 524 ? 0.2135 0.2351 0.2200 -0.0028 0.0069  0.0195  549  TYR   A C   
3858 O  O   . TYR   A 524 ? 0.2180 0.2400 0.2255 -0.0014 0.0070  0.0200  549  TYR   A O   
3859 C  CB  . TYR   A 524 ? 0.1928 0.2055 0.1955 -0.0012 0.0076  0.0173  549  TYR   A CB  
3860 C  CG  . TYR   A 524 ? 0.1917 0.2032 0.1927 -0.0023 0.0066  0.0156  549  TYR   A CG  
3861 C  CD1 . TYR   A 524 ? 0.2099 0.2229 0.2114 -0.0022 0.0059  0.0154  549  TYR   A CD1 
3862 C  CD2 . TYR   A 524 ? 0.2025 0.2114 0.2014 -0.0035 0.0064  0.0144  549  TYR   A CD2 
3863 C  CE1 . TYR   A 524 ? 0.2091 0.2208 0.2090 -0.0031 0.0052  0.0139  549  TYR   A CE1 
3864 C  CE2 . TYR   A 524 ? 0.2095 0.2170 0.2068 -0.0044 0.0057  0.0129  549  TYR   A CE2 
3865 C  CZ  . TYR   A 524 ? 0.2150 0.2239 0.2128 -0.0042 0.0051  0.0127  549  TYR   A CZ  
3866 O  OH  . TYR   A 524 ? 0.2233 0.2309 0.2196 -0.0051 0.0047  0.0112  549  TYR   A OH  
3867 N  N   . MET   A 525 ? 0.2320 0.2560 0.2383 -0.0049 0.0061  0.0194  550  MET   A N   
3868 C  CA  . MET   A 525 ? 0.2658 0.2933 0.2730 -0.0056 0.0052  0.0198  550  MET   A CA  
3869 C  C   . MET   A 525 ? 0.2717 0.2990 0.2769 -0.0078 0.0043  0.0184  550  MET   A C   
3870 O  O   . MET   A 525 ? 0.2753 0.3028 0.2796 -0.0096 0.0042  0.0181  550  MET   A O   
3871 C  CB  . MET   A 525 ? 0.3084 0.3414 0.3188 -0.0056 0.0053  0.0223  550  MET   A CB  
3872 C  CG  . MET   A 525 ? 0.3626 0.3992 0.3739 -0.0063 0.0044  0.0230  550  MET   A CG  
3873 S  SD  . MET   A 525 ? 0.4500 0.4932 0.4655 -0.0060 0.0046  0.0264  550  MET   A SD  
3874 C  CE  . MET   A 525 ? 0.4700 0.5165 0.4855 -0.0091 0.0039  0.0268  550  MET   A CE  
3875 N  N   . LYS   A 526 ? 0.2563 0.2834 0.2606 -0.0079 0.0037  0.0175  551  LYS   A N   
3876 C  CA  . LYS   A 526 ? 0.2706 0.2975 0.2728 -0.0101 0.0030  0.0161  551  LYS   A CA  
3877 C  C   . LYS   A 526 ? 0.3103 0.3428 0.3138 -0.0120 0.0023  0.0176  551  LYS   A C   
3878 O  O   . LYS   A 526 ? 0.3076 0.3436 0.3135 -0.0111 0.0022  0.0194  551  LYS   A O   
3879 C  CB  . LYS   A 526 ? 0.2636 0.2880 0.2643 -0.0094 0.0028  0.0146  551  LYS   A CB  
3880 C  CG  . LYS   A 526 ? 0.2829 0.3020 0.2822 -0.0079 0.0033  0.0132  551  LYS   A CG  
3881 C  CD  . LYS   A 526 ? 0.2951 0.3117 0.2931 -0.0074 0.0032  0.0117  551  LYS   A CD  
3882 C  CE  . LYS   A 526 ? 0.2914 0.3035 0.2885 -0.0058 0.0036  0.0107  551  LYS   A CE  
3883 N  NZ  . LYS   A 526 ? 0.3150 0.3245 0.3108 -0.0054 0.0035  0.0092  551  LYS   A NZ  
3884 N  N   . GLY   A 527 ? 0.3380 0.3711 0.3398 -0.0147 0.0018  0.0169  552  GLY   A N   
3885 C  CA  . GLY   A 527 ? 0.3757 0.4142 0.3784 -0.0169 0.0009  0.0183  552  GLY   A CA  
3886 C  C   . GLY   A 527 ? 0.4103 0.4529 0.4158 -0.0173 0.0009  0.0206  552  GLY   A C   
3887 O  O   . GLY   A 527 ? 0.4365 0.4771 0.4420 -0.0169 0.0016  0.0205  552  GLY   A O   
3888 N  N   . GLY   A 535 ? 0.4372 0.4862 0.4673 0.0005  0.0150  0.0377  560  GLY   A N   
3889 C  CA  . GLY   A 535 ? 0.4284 0.4769 0.4607 0.0031  0.0173  0.0395  560  GLY   A CA  
3890 C  C   . GLY   A 535 ? 0.4022 0.4440 0.4315 0.0049  0.0184  0.0376  560  GLY   A C   
3891 O  O   . GLY   A 535 ? 0.4298 0.4684 0.4586 0.0062  0.0204  0.0376  560  GLY   A O   
3892 N  N   . TYR   A 536 ? 0.3432 0.3827 0.3702 0.0048  0.0171  0.0358  561  TYR   A N   
3893 C  CA  . TYR   A 536 ? 0.3004 0.3340 0.3244 0.0062  0.0177  0.0339  561  TYR   A CA  
3894 C  C   . TYR   A 536 ? 0.2703 0.2987 0.2918 0.0068  0.0191  0.0327  561  TYR   A C   
3895 O  O   . TYR   A 536 ? 0.2962 0.3239 0.3164 0.0053  0.0187  0.0319  561  TYR   A O   
3896 C  CB  . TYR   A 536 ? 0.3080 0.3397 0.3290 0.0050  0.0156  0.0315  561  TYR   A CB  
3897 C  CG  . TYR   A 536 ? 0.3274 0.3630 0.3499 0.0044  0.0142  0.0321  561  TYR   A CG  
3898 C  CD1 . TYR   A 536 ? 0.3499 0.3905 0.3740 0.0025  0.0128  0.0330  561  TYR   A CD1 
3899 C  CD2 . TYR   A 536 ? 0.3466 0.3805 0.3685 0.0056  0.0140  0.0316  561  TYR   A CD2 
3900 C  CE1 . TYR   A 536 ? 0.3776 0.4215 0.4024 0.0018  0.0114  0.0335  561  TYR   A CE1 
3901 C  CE2 . TYR   A 536 ? 0.3672 0.4044 0.3901 0.0051  0.0127  0.0320  561  TYR   A CE2 
3902 C  CZ  . TYR   A 536 ? 0.3926 0.4347 0.4169 0.0032  0.0114  0.0329  561  TYR   A CZ  
3903 O  OH  . TYR   A 536 ? 0.4165 0.4618 0.4415 0.0025  0.0101  0.0334  561  TYR   A OH  
3904 N  N   . LEU   A 537 ? 0.2225 0.2472 0.2431 0.0087  0.0208  0.0326  562  LEU   A N   
3905 C  CA  . LEU   A 537 ? 0.2125 0.2318 0.2302 0.0091  0.0222  0.0314  562  LEU   A CA  
3906 C  C   . LEU   A 537 ? 0.1929 0.2075 0.2082 0.0104  0.0227  0.0302  562  LEU   A C   
3907 O  O   . LEU   A 537 ? 0.1957 0.2114 0.2128 0.0118  0.0235  0.0313  562  LEU   A O   
3908 C  CB  . LEU   A 537 ? 0.2535 0.2741 0.2735 0.0101  0.0246  0.0334  562  LEU   A CB  
3909 C  CG  . LEU   A 537 ? 0.3293 0.3456 0.3466 0.0099  0.0257  0.0324  562  LEU   A CG  
3910 C  CD1 . LEU   A 537 ? 0.3427 0.3600 0.3591 0.0077  0.0241  0.0314  562  LEU   A CD1 
3911 C  CD2 . LEU   A 537 ? 0.3604 0.3777 0.3801 0.0112  0.0285  0.0345  562  LEU   A CD2 
3912 N  N   . TRP   A 538 ? 0.1760 0.1856 0.1875 0.0100  0.0223  0.0280  563  TRP   A N   
3913 C  CA  . TRP   A 538 ? 0.1744 0.1793 0.1832 0.0110  0.0228  0.0268  563  TRP   A CA  
3914 C  C   . TRP   A 538 ? 0.1757 0.1755 0.1816 0.0114  0.0244  0.0260  563  TRP   A C   
3915 O  O   . TRP   A 538 ? 0.1914 0.1907 0.1964 0.0106  0.0245  0.0258  563  TRP   A O   
3916 C  CB  . TRP   A 538 ? 0.1717 0.1750 0.1782 0.0101  0.0204  0.0248  563  TRP   A CB  
3917 C  CG  . TRP   A 538 ? 0.1599 0.1670 0.1685 0.0098  0.0189  0.0252  563  TRP   A CG  
3918 C  CD1 . TRP   A 538 ? 0.1831 0.1900 0.1921 0.0107  0.0188  0.0252  563  TRP   A CD1 
3919 C  CD2 . TRP   A 538 ? 0.1493 0.1608 0.1596 0.0085  0.0173  0.0255  563  TRP   A CD2 
3920 N  NE1 . TRP   A 538 ? 0.1761 0.1872 0.1871 0.0101  0.0173  0.0256  563  TRP   A NE1 
3921 C  CE2 . TRP   A 538 ? 0.1605 0.1743 0.1721 0.0087  0.0164  0.0257  563  TRP   A CE2 
3922 C  CE3 . TRP   A 538 ? 0.1630 0.1766 0.1738 0.0070  0.0167  0.0256  563  TRP   A CE3 
3923 C  CZ2 . TRP   A 538 ? 0.1626 0.1806 0.1757 0.0074  0.0148  0.0260  563  TRP   A CZ2 
3924 C  CZ3 . TRP   A 538 ? 0.1764 0.1939 0.1884 0.0056  0.0151  0.0258  563  TRP   A CZ3 
3925 C  CH2 . TRP   A 538 ? 0.1656 0.1851 0.1786 0.0058  0.0142  0.0259  563  TRP   A CH2 
3926 N  N   . HIS   A 539 ? 0.1767 0.1724 0.1805 0.0124  0.0254  0.0254  564  HIS   A N   
3927 C  CA  . HIS   A 539 ? 0.1763 0.1664 0.1761 0.0124  0.0265  0.0242  564  HIS   A CA  
3928 C  C   . HIS   A 539 ? 0.1725 0.1601 0.1693 0.0114  0.0242  0.0221  564  HIS   A C   
3929 O  O   . HIS   A 539 ? 0.1847 0.1715 0.1811 0.0117  0.0235  0.0216  564  HIS   A O   
3930 C  CB  . HIS   A 539 ? 0.2002 0.1872 0.1992 0.0138  0.0290  0.0246  564  HIS   A CB  
3931 C  CG  . HIS   A 539 ? 0.2057 0.1944 0.2074 0.0149  0.0317  0.0267  564  HIS   A CG  
3932 N  ND1 . HIS   A 539 ? 0.2282 0.2130 0.2284 0.0160  0.0344  0.0269  564  HIS   A ND1 
3933 C  CD2 . HIS   A 539 ? 0.2097 0.2036 0.2155 0.0151  0.0319  0.0285  564  HIS   A CD2 
3934 C  CE1 . HIS   A 539 ? 0.2257 0.2133 0.2292 0.0170  0.0365  0.0290  564  HIS   A CE1 
3935 N  NE2 . HIS   A 539 ? 0.2245 0.2178 0.2316 0.0165  0.0351  0.0301  564  HIS   A NE2 
3936 N  N   . VAL   A 540 ? 0.1747 0.1613 0.1697 0.0102  0.0230  0.0212  565  VAL   A N   
3937 C  CA  . VAL   A 540 ? 0.1731 0.1580 0.1658 0.0093  0.0207  0.0195  565  VAL   A CA  
3938 C  C   . VAL   A 540 ? 0.1857 0.1652 0.1742 0.0090  0.0209  0.0183  565  VAL   A C   
3939 O  O   . VAL   A 540 ? 0.1860 0.1640 0.1730 0.0085  0.0215  0.0182  565  VAL   A O   
3940 C  CB  . VAL   A 540 ? 0.1790 0.1665 0.1727 0.0081  0.0190  0.0192  565  VAL   A CB  
3941 C  CG1 . VAL   A 540 ? 0.2057 0.1919 0.1977 0.0074  0.0168  0.0177  565  VAL   A CG1 
3942 C  CG2 . VAL   A 540 ? 0.1842 0.1771 0.1818 0.0080  0.0189  0.0206  565  VAL   A CG2 
3943 N  N   . PRO   A 541 ? 0.1915 0.1682 0.1779 0.0092  0.0204  0.0173  566  PRO   A N   
3944 C  CA  . PRO   A 541 ? 0.1919 0.1636 0.1740 0.0087  0.0203  0.0162  566  PRO   A CA  
3945 C  C   . PRO   A 541 ? 0.2085 0.1800 0.1894 0.0077  0.0180  0.0152  566  PRO   A C   
3946 O  O   . PRO   A 541 ? 0.2432 0.2149 0.2240 0.0074  0.0162  0.0145  566  PRO   A O   
3947 C  CB  . PRO   A 541 ? 0.2091 0.1787 0.1898 0.0090  0.0203  0.0157  566  PRO   A CB  
3948 C  CG  . PRO   A 541 ? 0.2446 0.2180 0.2287 0.0096  0.0196  0.0162  566  PRO   A CG  
3949 C  CD  . PRO   A 541 ? 0.2051 0.1831 0.1929 0.0098  0.0199  0.0174  566  PRO   A CD  
3950 N  N   . LEU   A 542 ? 0.1872 0.1585 0.1675 0.0071  0.0182  0.0153  567  LEU   A N   
3951 C  CA  . LEU   A 542 ? 0.1802 0.1510 0.1594 0.0062  0.0163  0.0146  567  LEU   A CA  
3952 C  C   . LEU   A 542 ? 0.1798 0.1463 0.1551 0.0058  0.0156  0.0137  567  LEU   A C   
3953 O  O   . LEU   A 542 ? 0.1931 0.1564 0.1658 0.0059  0.0168  0.0136  567  LEU   A O   
3954 C  CB  . LEU   A 542 ? 0.1876 0.1594 0.1674 0.0056  0.0168  0.0150  567  LEU   A CB  
3955 C  CG  . LEU   A 542 ? 0.1905 0.1670 0.1741 0.0056  0.0174  0.0161  567  LEU   A CG  
3956 C  CD1 . LEU   A 542 ? 0.1863 0.1634 0.1701 0.0048  0.0179  0.0165  567  LEU   A CD1 
3957 C  CD2 . LEU   A 542 ? 0.2011 0.1806 0.1868 0.0053  0.0156  0.0157  567  LEU   A CD2 
3958 N  N   . THR   A 543 ? 0.1773 0.1436 0.1521 0.0053  0.0135  0.0130  568  THR   A N   
3959 C  CA  . THR   A 543 ? 0.1893 0.1520 0.1607 0.0048  0.0126  0.0124  568  THR   A CA  
3960 C  C   . THR   A 543 ? 0.1776 0.1404 0.1488 0.0043  0.0113  0.0122  568  THR   A C   
3961 O  O   . THR   A 543 ? 0.1777 0.1434 0.1516 0.0042  0.0108  0.0122  568  THR   A O   
3962 C  CB  . THR   A 543 ? 0.2054 0.1677 0.1764 0.0050  0.0112  0.0119  568  THR   A CB  
3963 O  OG1 . THR   A 543 ? 0.2135 0.1789 0.1874 0.0052  0.0099  0.0118  568  THR   A OG1 
3964 C  CG2 . THR   A 543 ? 0.2250 0.1861 0.1952 0.0053  0.0124  0.0119  568  THR   A CG2 
3965 N  N   . PHE   A 544 ? 0.1813 0.1409 0.1494 0.0038  0.0109  0.0120  569  PHE   A N   
3966 C  CA  . PHE   A 544 ? 0.1763 0.1355 0.1441 0.0033  0.0098  0.0119  569  PHE   A CA  
3967 C  C   . PHE   A 544 ? 0.1717 0.1275 0.1361 0.0030  0.0087  0.0117  569  PHE   A C   
3968 O  O   . PHE   A 544 ? 0.1851 0.1383 0.1468 0.0028  0.0092  0.0117  569  PHE   A O   
3969 C  CB  . PHE   A 544 ? 0.1774 0.1372 0.1458 0.0029  0.0110  0.0122  569  PHE   A CB  
3970 C  CG  . PHE   A 544 ? 0.1852 0.1423 0.1509 0.0026  0.0125  0.0125  569  PHE   A CG  
3971 C  CD1 . PHE   A 544 ? 0.1950 0.1490 0.1577 0.0021  0.0121  0.0125  569  PHE   A CD1 
3972 C  CD2 . PHE   A 544 ? 0.2067 0.1644 0.1730 0.0029  0.0144  0.0130  569  PHE   A CD2 
3973 C  CE1 . PHE   A 544 ? 0.2117 0.1631 0.1717 0.0018  0.0135  0.0128  569  PHE   A CE1 
3974 C  CE2 . PHE   A 544 ? 0.2133 0.1684 0.1771 0.0027  0.0160  0.0133  569  PHE   A CE2 
3975 C  CZ  . PHE   A 544 ? 0.2145 0.1665 0.1752 0.0020  0.0156  0.0131  569  PHE   A CZ  
3976 N  N   . ILE   A 545 ? 0.1820 0.1377 0.1467 0.0029  0.0074  0.0117  570  ILE   A N   
3977 C  CA  . ILE   A 545 ? 0.1840 0.1369 0.1459 0.0025  0.0063  0.0118  570  ILE   A CA  
3978 C  C   . ILE   A 545 ? 0.1907 0.1432 0.1528 0.0023  0.0065  0.0120  570  ILE   A C   
3979 O  O   . ILE   A 545 ? 0.1908 0.1454 0.1553 0.0023  0.0070  0.0119  570  ILE   A O   
3980 C  CB  . ILE   A 545 ? 0.1955 0.1487 0.1578 0.0028  0.0043  0.0118  570  ILE   A CB  
3981 C  CG1 . ILE   A 545 ? 0.2048 0.1608 0.1706 0.0034  0.0037  0.0116  570  ILE   A CG1 
3982 C  CG2 . ILE   A 545 ? 0.2062 0.1591 0.1676 0.0028  0.0041  0.0116  570  ILE   A CG2 
3983 C  CD1 . ILE   A 545 ? 0.2495 0.2058 0.2159 0.0038  0.0019  0.0117  570  ILE   A CD1 
3984 N  N   . THR   A 546 ? 0.1930 0.1426 0.1523 0.0019  0.0059  0.0124  571  THR   A N   
3985 C  CA  . THR   A 546 ? 0.1948 0.1437 0.1541 0.0016  0.0061  0.0126  571  THR   A CA  
3986 C  C   . THR   A 546 ? 0.2070 0.1538 0.1647 0.0018  0.0046  0.0130  571  THR   A C   
3987 O  O   . THR   A 546 ? 0.2096 0.1557 0.1662 0.0019  0.0034  0.0133  571  THR   A O   
3988 C  CB  . THR   A 546 ? 0.2062 0.1532 0.1633 0.0010  0.0077  0.0128  571  THR   A CB  
3989 O  OG1 . THR   A 546 ? 0.2036 0.1474 0.1570 0.0007  0.0073  0.0132  571  THR   A OG1 
3990 C  CG2 . THR   A 546 ? 0.2020 0.1507 0.1603 0.0010  0.0094  0.0127  571  THR   A CG2 
3991 N  N   . SER   A 547 ? 0.2047 0.1505 0.1624 0.0016  0.0047  0.0133  572  SER   A N   
3992 C  CA  . SER   A 547 ? 0.2011 0.1448 0.1574 0.0018  0.0035  0.0139  572  SER   A CA  
3993 C  C   . SER   A 547 ? 0.2334 0.1744 0.1860 0.0014  0.0031  0.0146  572  SER   A C   
3994 O  O   . SER   A 547 ? 0.2459 0.1858 0.1975 0.0016  0.0016  0.0153  572  SER   A O   
3995 C  CB  . SER   A 547 ? 0.2176 0.1602 0.1742 0.0016  0.0040  0.0141  572  SER   A CB  
3996 O  OG  . SER   A 547 ? 0.2485 0.1895 0.2031 0.0009  0.0054  0.0142  572  SER   A OG  
3997 N  N   . LYS   A 548 ? 0.2195 0.1597 0.1702 0.0008  0.0043  0.0144  573  LYS   A N   
3998 C  CA  . LYS   A 548 ? 0.2205 0.1578 0.1671 0.0002  0.0042  0.0149  573  LYS   A CA  
3999 C  C   . LYS   A 548 ? 0.2301 0.1675 0.1755 0.0000  0.0039  0.0146  573  LYS   A C   
4000 O  O   . LYS   A 548 ? 0.2469 0.1819 0.1887 -0.0007 0.0035  0.0149  573  LYS   A O   
4001 C  CB  . LYS   A 548 ? 0.2539 0.1894 0.1985 -0.0005 0.0060  0.0149  573  LYS   A CB  
4002 C  CG  . LYS   A 548 ? 0.2998 0.2342 0.2445 -0.0006 0.0061  0.0154  573  LYS   A CG  
4003 C  CD  . LYS   A 548 ? 0.3881 0.3201 0.3301 -0.0013 0.0076  0.0156  573  LYS   A CD  
4004 C  CE  . LYS   A 548 ? 0.4736 0.4034 0.4141 -0.0016 0.0073  0.0164  573  LYS   A CE  
4005 N  NZ  . LYS   A 548 ? 0.5030 0.4340 0.4463 -0.0015 0.0080  0.0161  573  LYS   A NZ  
4006 N  N   . SER   A 549 ? 0.2214 0.1614 0.1695 0.0004  0.0042  0.0139  574  SER   A N   
4007 C  CA  . SER   A 549 ? 0.2062 0.1460 0.1531 0.0002  0.0042  0.0136  574  SER   A CA  
4008 C  C   . SER   A 549 ? 0.2255 0.1682 0.1756 0.0008  0.0034  0.0132  574  SER   A C   
4009 O  O   . SER   A 549 ? 0.2136 0.1586 0.1668 0.0013  0.0043  0.0128  574  SER   A O   
4010 C  CB  . SER   A 549 ? 0.2113 0.1501 0.1569 -0.0001 0.0064  0.0132  574  SER   A CB  
4011 O  OG  . SER   A 549 ? 0.2104 0.1486 0.1546 -0.0004 0.0066  0.0128  574  SER   A OG  
4012 N  N   . ASP   A 550 ? 0.2198 0.1625 0.1693 0.0007  0.0018  0.0133  575  ASP   A N   
4013 C  CA  . ASP   A 550 ? 0.2290 0.1743 0.1814 0.0013  0.0011  0.0130  575  ASP   A CA  
4014 C  C   . ASP   A 550 ? 0.2311 0.1760 0.1822 0.0009  0.0019  0.0124  575  ASP   A C   
4015 O  O   . ASP   A 550 ? 0.2444 0.1912 0.1975 0.0011  0.0013  0.0122  575  ASP   A O   
4016 C  CB  . ASP   A 550 ? 0.2452 0.1916 0.1988 0.0016  -0.0011 0.0135  575  ASP   A CB  
4017 C  CG  . ASP   A 550 ? 0.3128 0.2574 0.2632 0.0007  -0.0026 0.0140  575  ASP   A CG  
4018 O  OD1 . ASP   A 550 ? 0.3066 0.2489 0.2536 -0.0002 -0.0018 0.0138  575  ASP   A OD1 
4019 O  OD2 . ASP   A 550 ? 0.3598 0.3055 0.3112 0.0009  -0.0044 0.0147  575  ASP   A OD2 
4020 N  N   . MET   A 551 ? 0.2169 0.1592 0.1649 0.0002  0.0034  0.0123  576  MET   A N   
4021 C  CA  . MET   A 551 ? 0.2192 0.1609 0.1663 0.0000  0.0048  0.0117  576  MET   A CA  
4022 C  C   . MET   A 551 ? 0.2205 0.1652 0.1717 0.0010  0.0062  0.0115  576  MET   A C   
4023 O  O   . MET   A 551 ? 0.2257 0.1715 0.1786 0.0014  0.0068  0.0117  576  MET   A O   
4024 C  CB  . MET   A 551 ? 0.2212 0.1594 0.1643 -0.0007 0.0065  0.0116  576  MET   A CB  
4025 C  CG  . MET   A 551 ? 0.2282 0.1658 0.1710 -0.0006 0.0087  0.0111  576  MET   A CG  
4026 S  SD  . MET   A 551 ? 0.2495 0.1823 0.1868 -0.0016 0.0108  0.0110  576  MET   A SD  
4027 C  CE  . MET   A 551 ? 0.2594 0.1928 0.1987 -0.0007 0.0139  0.0107  576  MET   A CE  
4028 N  N   . VAL   A 552 ? 0.2115 0.1573 0.1640 0.0013  0.0066  0.0111  577  VAL   A N   
4029 C  CA  . VAL   A 552 ? 0.2097 0.1584 0.1658 0.0022  0.0080  0.0111  577  VAL   A CA  
4030 C  C   . VAL   A 552 ? 0.2181 0.1654 0.1731 0.0022  0.0105  0.0112  577  VAL   A C   
4031 O  O   . VAL   A 552 ? 0.2478 0.1926 0.2003 0.0019  0.0117  0.0110  577  VAL   A O   
4032 C  CB  . VAL   A 552 ? 0.2386 0.1890 0.1966 0.0025  0.0075  0.0108  577  VAL   A CB  
4033 C  CG1 . VAL   A 552 ? 0.2626 0.2160 0.2243 0.0034  0.0090  0.0109  577  VAL   A CG1 
4034 C  CG2 . VAL   A 552 ? 0.2734 0.2253 0.2327 0.0026  0.0051  0.0108  577  VAL   A CG2 
4035 N  N   . HIS   A 553 ? 0.1949 0.1434 0.1515 0.0025  0.0113  0.0115  578  HIS   A N   
4036 C  CA  . HIS   A 553 ? 0.2019 0.1497 0.1581 0.0026  0.0138  0.0118  578  HIS   A CA  
4037 C  C   . HIS   A 553 ? 0.2140 0.1650 0.1739 0.0035  0.0150  0.0121  578  HIS   A C   
4038 O  O   . HIS   A 553 ? 0.2230 0.1773 0.1862 0.0038  0.0140  0.0121  578  HIS   A O   
4039 C  CB  . HIS   A 553 ? 0.1961 0.1439 0.1523 0.0023  0.0140  0.0121  578  HIS   A CB  
4040 C  CG  . HIS   A 553 ? 0.2102 0.1547 0.1625 0.0015  0.0130  0.0121  578  HIS   A CG  
4041 N  ND1 . HIS   A 553 ? 0.2356 0.1765 0.1839 0.0009  0.0142  0.0121  578  HIS   A ND1 
4042 C  CD2 . HIS   A 553 ? 0.2184 0.1626 0.1702 0.0012  0.0108  0.0121  578  HIS   A CD2 
4043 C  CE1 . HIS   A 553 ? 0.2389 0.1776 0.1844 0.0002  0.0127  0.0121  578  HIS   A CE1 
4044 N  NE2 . HIS   A 553 ? 0.2316 0.1722 0.1791 0.0004  0.0106  0.0122  578  HIS   A NE2 
4045 N  N   . ARG   A 554 ? 0.2135 0.1634 0.1728 0.0038  0.0173  0.0123  579  ARG   A N   
4046 C  CA  A ARG   A 554 ? 0.2199 0.1728 0.1828 0.0047  0.0186  0.0128  579  ARG   A CA  
4047 C  CA  B ARG   A 554 ? 0.2099 0.1626 0.1726 0.0047  0.0186  0.0128  579  ARG   A CA  
4048 C  C   . ARG   A 554 ? 0.2113 0.1655 0.1758 0.0051  0.0207  0.0137  579  ARG   A C   
4049 O  O   . ARG   A 554 ? 0.2412 0.1927 0.2033 0.0048  0.0221  0.0138  579  ARG   A O   
4050 C  CB  A ARG   A 554 ? 0.2560 0.2071 0.2177 0.0050  0.0194  0.0125  579  ARG   A CB  
4051 C  CB  B ARG   A 554 ? 0.2144 0.1645 0.1751 0.0049  0.0199  0.0125  579  ARG   A CB  
4052 C  CG  A ARG   A 554 ? 0.2880 0.2391 0.2492 0.0047  0.0171  0.0119  579  ARG   A CG  
4053 C  CG  B ARG   A 554 ? 0.2344 0.1831 0.1932 0.0044  0.0179  0.0117  579  ARG   A CG  
4054 C  CD  A ARG   A 554 ? 0.3340 0.2835 0.2942 0.0048  0.0178  0.0115  579  ARG   A CD  
4055 C  CD  B ARG   A 554 ? 0.2546 0.1995 0.2101 0.0041  0.0192  0.0113  579  ARG   A CD  
4056 N  NE  A ARG   A 554 ? 0.3567 0.3051 0.3150 0.0040  0.0155  0.0109  579  ARG   A NE  
4057 N  NE  B ARG   A 554 ? 0.2763 0.2219 0.2338 0.0051  0.0216  0.0118  579  ARG   A NE  
4058 C  CZ  A ARG   A 554 ? 0.3460 0.2970 0.3068 0.0042  0.0137  0.0108  579  ARG   A CZ  
4059 C  CZ  B ARG   A 554 ? 0.2798 0.2265 0.2389 0.0056  0.0217  0.0118  579  ARG   A CZ  
4060 N  NH1 A ARG   A 554 ? 0.2653 0.2203 0.2303 0.0051  0.0139  0.0112  579  ARG   A NH1 
4061 N  NH1 B ARG   A 554 ? 0.2500 0.1975 0.2112 0.0067  0.0240  0.0125  579  ARG   A NH1 
4062 N  NH2 A ARG   A 554 ? 0.3712 0.3212 0.3303 0.0035  0.0117  0.0103  579  ARG   A NH2 
4063 N  NH2 B ARG   A 554 ? 0.2763 0.2235 0.2353 0.0051  0.0195  0.0112  579  ARG   A NH2 
4064 N  N   . PHE   A 555 ? 0.1910 0.1495 0.1598 0.0057  0.0210  0.0144  580  PHE   A N   
4065 C  CA  . PHE   A 555 ? 0.1942 0.1546 0.1652 0.0061  0.0230  0.0154  580  PHE   A CA  
4066 C  C   . PHE   A 555 ? 0.1932 0.1575 0.1683 0.0070  0.0235  0.0163  580  PHE   A C   
4067 O  O   . PHE   A 555 ? 0.2066 0.1742 0.1841 0.0069  0.0218  0.0162  580  PHE   A O   
4068 C  CB  . PHE   A 555 ? 0.2035 0.1657 0.1755 0.0053  0.0221  0.0156  580  PHE   A CB  
4069 C  CG  . PHE   A 555 ? 0.2040 0.1679 0.1779 0.0055  0.0243  0.0167  580  PHE   A CG  
4070 C  CD1 . PHE   A 555 ? 0.2161 0.1848 0.1944 0.0059  0.0247  0.0178  580  PHE   A CD1 
4071 C  CD2 . PHE   A 555 ? 0.2357 0.1968 0.2071 0.0052  0.0257  0.0168  580  PHE   A CD2 
4072 C  CE1 . PHE   A 555 ? 0.2091 0.1798 0.1894 0.0061  0.0266  0.0190  580  PHE   A CE1 
4073 C  CE2 . PHE   A 555 ? 0.2413 0.2042 0.2147 0.0054  0.0278  0.0180  580  PHE   A CE2 
4074 C  CZ  . PHE   A 555 ? 0.2109 0.1787 0.1889 0.0059  0.0282  0.0191  580  PHE   A CZ  
4075 N  N   . LEU   A 556 ? 0.1982 0.1626 0.1743 0.0079  0.0260  0.0172  581  LEU   A N   
4076 C  CA  . LEU   A 556 ? 0.1996 0.1680 0.1799 0.0089  0.0266  0.0183  581  LEU   A CA  
4077 C  C   . LEU   A 556 ? 0.2001 0.1731 0.1842 0.0089  0.0272  0.0196  581  LEU   A C   
4078 O  O   . LEU   A 556 ? 0.2186 0.1913 0.2030 0.0092  0.0292  0.0205  581  LEU   A O   
4079 C  CB  . LEU   A 556 ? 0.2034 0.1696 0.1831 0.0100  0.0291  0.0187  581  LEU   A CB  
4080 C  CG  . LEU   A 556 ? 0.2353 0.2053 0.2191 0.0112  0.0300  0.0200  581  LEU   A CG  
4081 C  CD1 . LEU   A 556 ? 0.2398 0.2118 0.2248 0.0111  0.0276  0.0195  581  LEU   A CD1 
4082 C  CD2 . LEU   A 556 ? 0.2553 0.2223 0.2382 0.0124  0.0328  0.0205  581  LEU   A CD2 
4083 N  N   . LEU   A 557 ? 0.1830 0.1603 0.1700 0.0086  0.0253  0.0198  582  LEU   A N   
4084 C  CA  . LEU   A 557 ? 0.1699 0.1518 0.1604 0.0082  0.0255  0.0211  582  LEU   A CA  
4085 C  C   . LEU   A 557 ? 0.1854 0.1711 0.1798 0.0094  0.0266  0.0227  582  LEU   A C   
4086 O  O   . LEU   A 557 ? 0.1964 0.1842 0.1923 0.0096  0.0253  0.0227  582  LEU   A O   
4087 C  CB  . LEU   A 557 ? 0.1664 0.1504 0.1574 0.0070  0.0230  0.0204  582  LEU   A CB  
4088 C  CG  . LEU   A 557 ? 0.1783 0.1672 0.1727 0.0063  0.0229  0.0216  582  LEU   A CG  
4089 C  CD1 . LEU   A 557 ? 0.1898 0.1779 0.1836 0.0057  0.0242  0.0221  582  LEU   A CD1 
4090 C  CD2 . LEU   A 557 ? 0.2096 0.2005 0.2045 0.0050  0.0205  0.0208  582  LEU   A CD2 
4091 N  N   . LYS   A 558 ? 0.1807 0.1672 0.1768 0.0102  0.0290  0.0242  583  LYS   A N   
4092 C  CA  . LYS   A 558 ? 0.1902 0.1803 0.1902 0.0115  0.0303  0.0260  583  LYS   A CA  
4093 C  C   . LYS   A 558 ? 0.2101 0.2061 0.2144 0.0111  0.0303  0.0279  583  LYS   A C   
4094 O  O   . LYS   A 558 ? 0.2360 0.2356 0.2440 0.0122  0.0313  0.0297  583  LYS   A O   
4095 C  CB  . LYS   A 558 ? 0.2468 0.2343 0.2464 0.0130  0.0336  0.0269  583  LYS   A CB  
4096 C  CG  . LYS   A 558 ? 0.2860 0.2674 0.2813 0.0133  0.0343  0.0254  583  LYS   A CG  
4097 C  CD  . LYS   A 558 ? 0.3057 0.2852 0.3012 0.0148  0.0378  0.0266  583  LYS   A CD  
4098 C  CE  . LYS   A 558 ? 0.3836 0.3564 0.3740 0.0147  0.0388  0.0249  583  LYS   A CE  
4099 N  NZ  . LYS   A 558 ? 0.4141 0.3843 0.4042 0.0161  0.0426  0.0259  583  LYS   A NZ  
4100 N  N   . THR   A 559 ? 0.1836 0.1806 0.1875 0.0097  0.0292  0.0275  584  THR   A N   
4101 C  CA  . THR   A 559 ? 0.1733 0.1755 0.1809 0.0090  0.0293  0.0292  584  THR   A CA  
4102 C  C   . THR   A 559 ? 0.1682 0.1726 0.1757 0.0071  0.0267  0.0283  584  THR   A C   
4103 O  O   . THR   A 559 ? 0.1696 0.1712 0.1742 0.0064  0.0249  0.0264  584  THR   A O   
4104 C  CB  . THR   A 559 ? 0.1782 0.1784 0.1849 0.0090  0.0315  0.0296  584  THR   A CB  
4105 O  OG1 . THR   A 559 ? 0.1722 0.1675 0.1743 0.0080  0.0307  0.0276  584  THR   A OG1 
4106 C  CG2 . THR   A 559 ? 0.1894 0.1875 0.1964 0.0110  0.0346  0.0306  584  THR   A CG2 
4107 N  N   . LYS   A 560 ? 0.1738 0.1834 0.1846 0.0061  0.0264  0.0297  585  LYS   A N   
4108 C  CA  . LYS   A 560 ? 0.1649 0.1765 0.1755 0.0041  0.0240  0.0289  585  LYS   A CA  
4109 C  C   . LYS   A 560 ? 0.1746 0.1817 0.1812 0.0029  0.0233  0.0270  585  LYS   A C   
4110 O  O   . LYS   A 560 ? 0.1787 0.1848 0.1835 0.0019  0.0214  0.0254  585  LYS   A O   
4111 C  CB  . LYS   A 560 ? 0.1894 0.2073 0.2040 0.0030  0.0240  0.0310  585  LYS   A CB  
4112 C  CG  . LYS   A 560 ? 0.2461 0.2662 0.2604 0.0007  0.0215  0.0301  585  LYS   A CG  
4113 C  CD  . LYS   A 560 ? 0.3267 0.3534 0.3449 -0.0006 0.0212  0.0321  585  LYS   A CD  
4114 C  CE  . LYS   A 560 ? 0.4029 0.4311 0.4200 -0.0032 0.0190  0.0310  585  LYS   A CE  
4115 N  NZ  . LYS   A 560 ? 0.4379 0.4730 0.4588 -0.0045 0.0181  0.0330  585  LYS   A NZ  
4116 N  N   . THR   A 561 ? 0.1745 0.1790 0.1798 0.0032  0.0251  0.0272  586  THR   A N   
4117 C  CA  . THR   A 561 ? 0.1713 0.1713 0.1727 0.0022  0.0246  0.0255  586  THR   A CA  
4118 C  C   . THR   A 561 ? 0.1646 0.1597 0.1633 0.0034  0.0265  0.0251  586  THR   A C   
4119 O  O   . THR   A 561 ? 0.1746 0.1700 0.1747 0.0048  0.0286  0.0264  586  THR   A O   
4120 C  CB  . THR   A 561 ? 0.1880 0.1900 0.1901 0.0003  0.0243  0.0258  586  THR   A CB  
4121 O  OG1 . THR   A 561 ? 0.1973 0.1991 0.2001 0.0008  0.0266  0.0271  586  THR   A OG1 
4122 C  CG2 . THR   A 561 ? 0.1935 0.2011 0.1988 -0.0010 0.0229  0.0266  586  THR   A CG2 
4123 N  N   . ASP   A 562 ? 0.1648 0.1552 0.1594 0.0028  0.0258  0.0235  587  ASP   A N   
4124 C  CA  . ASP   A 562 ? 0.1648 0.1503 0.1562 0.0034  0.0275  0.0231  587  ASP   A CA  
4125 C  C   . ASP   A 562 ? 0.1652 0.1471 0.1530 0.0022  0.0263  0.0217  587  ASP   A C   
4126 O  O   . ASP   A 562 ? 0.1677 0.1509 0.1558 0.0010  0.0245  0.0211  587  ASP   A O   
4127 C  CB  . ASP   A 562 ? 0.1704 0.1530 0.1603 0.0049  0.0280  0.0226  587  ASP   A CB  
4128 C  CG  . ASP   A 562 ? 0.1805 0.1599 0.1687 0.0059  0.0307  0.0230  587  ASP   A CG  
4129 O  OD1 . ASP   A 562 ? 0.1917 0.1692 0.1784 0.0054  0.0318  0.0231  587  ASP   A OD1 
4130 O  OD2 . ASP   A 562 ? 0.1945 0.1728 0.1828 0.0072  0.0318  0.0232  587  ASP   A OD2 
4131 N  N   . VAL   A 563 ? 0.1718 0.1490 0.1561 0.0025  0.0275  0.0212  588  VAL   A N   
4132 C  CA  . VAL   A 563 ? 0.1801 0.1536 0.1609 0.0014  0.0265  0.0201  588  VAL   A CA  
4133 C  C   . VAL   A 563 ? 0.2011 0.1694 0.1777 0.0021  0.0270  0.0192  588  VAL   A C   
4134 O  O   . VAL   A 563 ? 0.2071 0.1741 0.1832 0.0031  0.0289  0.0196  588  VAL   A O   
4135 C  CB  . VAL   A 563 ? 0.2107 0.1848 0.1919 0.0005  0.0278  0.0208  588  VAL   A CB  
4136 C  CG1 . VAL   A 563 ? 0.2469 0.2205 0.2284 0.0014  0.0306  0.0219  588  VAL   A CG1 
4137 C  CG2 . VAL   A 563 ? 0.2447 0.2148 0.2221 -0.0006 0.0270  0.0198  588  VAL   A CG2 
4138 N  N   . LEU   A 564 ? 0.1833 0.1485 0.1568 0.0015  0.0253  0.0180  589  LEU   A N   
4139 C  CA  . LEU   A 564 ? 0.1964 0.1565 0.1654 0.0017  0.0255  0.0173  589  LEU   A CA  
4140 C  C   . LEU   A 564 ? 0.2009 0.1583 0.1671 0.0006  0.0246  0.0168  589  LEU   A C   
4141 O  O   . LEU   A 564 ? 0.1956 0.1548 0.1633 -0.0002 0.0234  0.0167  589  LEU   A O   
4142 C  CB  . LEU   A 564 ? 0.2112 0.1698 0.1790 0.0023  0.0241  0.0164  589  LEU   A CB  
4143 C  CG  . LEU   A 564 ? 0.2200 0.1796 0.1883 0.0019  0.0215  0.0157  589  LEU   A CG  
4144 C  CD1 . LEU   A 564 ? 0.2333 0.1890 0.1977 0.0012  0.0202  0.0150  589  LEU   A CD1 
4145 C  CD2 . LEU   A 564 ? 0.2264 0.1868 0.1955 0.0027  0.0207  0.0153  589  LEU   A CD2 
4146 N  N   . ILE   A 565 ? 0.2051 0.1581 0.1673 0.0005  0.0254  0.0166  590  ILE   A N   
4147 C  CA  . ILE   A 565 ? 0.2127 0.1629 0.1720 -0.0005 0.0248  0.0163  590  ILE   A CA  
4148 C  C   . ILE   A 565 ? 0.2162 0.1627 0.1718 -0.0005 0.0231  0.0155  590  ILE   A C   
4149 O  O   . ILE   A 565 ? 0.2366 0.1805 0.1895 -0.0001 0.0237  0.0152  590  ILE   A O   
4150 C  CB  . ILE   A 565 ? 0.2283 0.1763 0.1856 -0.0007 0.0272  0.0169  590  ILE   A CB  
4151 C  CG1 . ILE   A 565 ? 0.2397 0.1916 0.2010 -0.0006 0.0291  0.0179  590  ILE   A CG1 
4152 C  CG2 . ILE   A 565 ? 0.2528 0.1979 0.2071 -0.0018 0.0266  0.0167  590  ILE   A CG2 
4153 C  CD1 . ILE   A 565 ? 0.2519 0.2077 0.2166 -0.0014 0.0281  0.0182  590  ILE   A CD1 
4154 N  N   . LEU   A 566 ? 0.2071 0.1537 0.1627 -0.0009 0.0210  0.0151  591  LEU   A N   
4155 C  CA  . LEU   A 566 ? 0.2103 0.1538 0.1627 -0.0009 0.0193  0.0145  591  LEU   A CA  
4156 C  C   . LEU   A 566 ? 0.2270 0.1664 0.1751 -0.0015 0.0199  0.0147  591  LEU   A C   
4157 O  O   . LEU   A 566 ? 0.2307 0.1695 0.1784 -0.0020 0.0212  0.0152  591  LEU   A O   
4158 C  CB  . LEU   A 566 ? 0.2063 0.1508 0.1599 -0.0011 0.0172  0.0143  591  LEU   A CB  
4159 C  CG  . LEU   A 566 ? 0.2245 0.1728 0.1820 -0.0006 0.0163  0.0140  591  LEU   A CG  
4160 C  CD1 . LEU   A 566 ? 0.2371 0.1861 0.1957 -0.0010 0.0147  0.0137  591  LEU   A CD1 
4161 C  CD2 . LEU   A 566 ? 0.2313 0.1794 0.1884 0.0001  0.0155  0.0136  591  LEU   A CD2 
4162 N  N   . PRO   A 567 ? 0.2196 0.1559 0.1641 -0.0016 0.0190  0.0144  592  PRO   A N   
4163 C  CA  . PRO   A 567 ? 0.2315 0.1637 0.1714 -0.0023 0.0196  0.0147  592  PRO   A CA  
4164 C  C   . PRO   A 567 ? 0.2409 0.1721 0.1801 -0.0028 0.0187  0.0150  592  PRO   A C   
4165 O  O   . PRO   A 567 ? 0.2656 0.1942 0.2020 -0.0035 0.0197  0.0154  592  PRO   A O   
4166 C  CB  . PRO   A 567 ? 0.2539 0.1837 0.1906 -0.0024 0.0182  0.0143  592  PRO   A CB  
4167 C  CG  . PRO   A 567 ? 0.2764 0.2089 0.2161 -0.0017 0.0168  0.0139  592  PRO   A CG  
4168 C  CD  . PRO   A 567 ? 0.2356 0.1721 0.1801 -0.0011 0.0175  0.0140  592  PRO   A CD  
4169 N  N   . GLU   A 568 ? 0.2349 0.1679 0.1764 -0.0026 0.0168  0.0149  593  GLU   A N   
4170 C  CA  . GLU   A 568 ? 0.2446 0.1766 0.1857 -0.0030 0.0159  0.0153  593  GLU   A CA  
4171 C  C   . GLU   A 568 ? 0.2420 0.1772 0.1872 -0.0027 0.0150  0.0150  593  GLU   A C   
4172 O  O   . GLU   A 568 ? 0.2382 0.1758 0.1856 -0.0021 0.0143  0.0146  593  GLU   A O   
4173 C  CB  . GLU   A 568 ? 0.3064 0.2357 0.2444 -0.0030 0.0139  0.0155  593  GLU   A CB  
4174 C  CG  . GLU   A 568 ? 0.3536 0.2796 0.2871 -0.0035 0.0144  0.0157  593  GLU   A CG  
4175 C  CD  . GLU   A 568 ? 0.3343 0.2580 0.2649 -0.0037 0.0123  0.0162  593  GLU   A CD  
4176 O  OE1 . GLU   A 568 ? 0.2817 0.2058 0.2119 -0.0035 0.0108  0.0160  593  GLU   A OE1 
4177 O  OE2 . GLU   A 568 ? 0.3393 0.2609 0.2679 -0.0042 0.0121  0.0169  593  GLU   A OE2 
4178 N  N   . GLU   A 569 ? 0.2469 0.1820 0.1927 -0.0032 0.0149  0.0152  594  GLU   A N   
4179 C  CA  . GLU   A 569 ? 0.2435 0.1811 0.1927 -0.0031 0.0141  0.0148  594  GLU   A CA  
4180 C  C   . GLU   A 569 ? 0.2434 0.1811 0.1930 -0.0023 0.0121  0.0146  594  GLU   A C   
4181 O  O   . GLU   A 569 ? 0.2511 0.1863 0.1981 -0.0021 0.0111  0.0150  594  GLU   A O   
4182 C  CB  . GLU   A 569 ? 0.2771 0.2137 0.2263 -0.0039 0.0145  0.0150  594  GLU   A CB  
4183 C  CG  . GLU   A 569 ? 0.3293 0.2665 0.2787 -0.0047 0.0165  0.0152  594  GLU   A CG  
4184 C  CD  . GLU   A 569 ? 0.4806 0.4179 0.4309 -0.0058 0.0170  0.0153  594  GLU   A CD  
4185 O  OE1 . GLU   A 569 ? 0.4739 0.4111 0.4250 -0.0058 0.0160  0.0149  594  GLU   A OE1 
4186 O  OE2 . GLU   A 569 ? 0.5569 0.4945 0.5072 -0.0066 0.0186  0.0156  594  GLU   A OE2 
4187 N  N   . VAL   A 570 ? 0.2224 0.1629 0.1751 -0.0020 0.0115  0.0141  595  VAL   A N   
4188 C  CA  . VAL   A 570 ? 0.2226 0.1636 0.1762 -0.0012 0.0098  0.0139  595  VAL   A CA  
4189 C  C   . VAL   A 570 ? 0.2438 0.1858 0.1997 -0.0012 0.0094  0.0135  595  VAL   A C   
4190 O  O   . VAL   A 570 ? 0.2763 0.2192 0.2333 -0.0020 0.0104  0.0133  595  VAL   A O   
4191 C  CB  . VAL   A 570 ? 0.2257 0.1692 0.1810 -0.0006 0.0095  0.0135  595  VAL   A CB  
4192 C  CG1 . VAL   A 570 ? 0.2320 0.1740 0.1848 -0.0006 0.0101  0.0137  595  VAL   A CG1 
4193 C  CG2 . VAL   A 570 ? 0.2349 0.1820 0.1935 -0.0008 0.0105  0.0131  595  VAL   A CG2 
4194 N  N   . GLU   A 571 ? 0.2418 0.1834 0.1981 -0.0005 0.0080  0.0135  596  GLU   A N   
4195 C  CA  . GLU   A 571 ? 0.2517 0.1939 0.2099 -0.0004 0.0077  0.0132  596  GLU   A CA  
4196 C  C   . GLU   A 571 ? 0.2608 0.2064 0.2220 -0.0003 0.0077  0.0124  596  GLU   A C   
4197 O  O   . GLU   A 571 ? 0.2785 0.2250 0.2412 -0.0007 0.0080  0.0119  596  GLU   A O   
4198 C  CB  . GLU   A 571 ? 0.2704 0.2107 0.2280 0.0005  0.0064  0.0137  596  GLU   A CB  
4199 C  CG  . GLU   A 571 ? 0.3661 0.3029 0.3209 0.0003  0.0064  0.0146  596  GLU   A CG  
4200 C  CD  . GLU   A 571 ? 0.4560 0.3912 0.4105 0.0013  0.0051  0.0154  596  GLU   A CD  
4201 O  OE1 . GLU   A 571 ? 0.5135 0.4467 0.4655 0.0014  0.0044  0.0164  596  GLU   A OE1 
4202 O  OE2 . GLU   A 571 ? 0.4640 0.4001 0.4207 0.0020  0.0047  0.0152  596  GLU   A OE2 
4203 N  N   . TRP   A 572 ? 0.2247 0.1722 0.1866 0.0002  0.0073  0.0123  597  TRP   A N   
4204 C  CA  . TRP   A 572 ? 0.2205 0.1714 0.1851 0.0003  0.0073  0.0118  597  TRP   A CA  
4205 C  C   . TRP   A 572 ? 0.2127 0.1647 0.1772 0.0007  0.0074  0.0119  597  TRP   A C   
4206 O  O   . TRP   A 572 ? 0.2067 0.1568 0.1690 0.0009  0.0072  0.0123  597  TRP   A O   
4207 C  CB  . TRP   A 572 ? 0.2314 0.1828 0.1975 0.0011  0.0061  0.0115  597  TRP   A CB  
4208 C  CG  . TRP   A 572 ? 0.2243 0.1744 0.1894 0.0020  0.0048  0.0120  597  TRP   A CG  
4209 C  CD1 . TRP   A 572 ? 0.2484 0.1959 0.2122 0.0024  0.0041  0.0126  597  TRP   A CD1 
4210 C  CD2 . TRP   A 572 ? 0.2105 0.1617 0.1758 0.0025  0.0040  0.0121  597  TRP   A CD2 
4211 N  NE1 . TRP   A 572 ? 0.2490 0.1964 0.2124 0.0031  0.0028  0.0131  597  TRP   A NE1 
4212 C  CE2 . TRP   A 572 ? 0.2280 0.1775 0.1921 0.0031  0.0027  0.0127  597  TRP   A CE2 
4213 C  CE3 . TRP   A 572 ? 0.2114 0.1648 0.1777 0.0026  0.0043  0.0118  597  TRP   A CE3 
4214 C  CZ2 . TRP   A 572 ? 0.2144 0.1644 0.1782 0.0035  0.0017  0.0130  597  TRP   A CZ2 
4215 C  CZ3 . TRP   A 572 ? 0.2194 0.1729 0.1852 0.0030  0.0034  0.0119  597  TRP   A CZ3 
4216 C  CH2 . TRP   A 572 ? 0.2209 0.1728 0.1855 0.0034  0.0020  0.0125  597  TRP   A CH2 
4217 N  N   . ILE   A 573 ? 0.2013 0.1565 0.1682 0.0006  0.0078  0.0116  598  ILE   A N   
4218 C  CA  . ILE   A 573 ? 0.1966 0.1531 0.1638 0.0010  0.0082  0.0117  598  ILE   A CA  
4219 C  C   . ILE   A 573 ? 0.1993 0.1589 0.1693 0.0015  0.0076  0.0113  598  ILE   A C   
4220 O  O   . ILE   A 573 ? 0.2201 0.1814 0.1918 0.0011  0.0075  0.0110  598  ILE   A O   
4221 C  CB  . ILE   A 573 ? 0.2120 0.1692 0.1792 0.0005  0.0098  0.0121  598  ILE   A CB  
4222 C  CG1 . ILE   A 573 ? 0.2100 0.1681 0.1775 0.0011  0.0104  0.0122  598  ILE   A CG1 
4223 C  CG2 . ILE   A 573 ? 0.2558 0.2157 0.2254 -0.0002 0.0105  0.0120  598  ILE   A CG2 
4224 C  CD1 . ILE   A 573 ? 0.2137 0.1713 0.1803 0.0008  0.0123  0.0128  598  ILE   A CD1 
4225 N  N   . LYS   A 574 ? 0.1795 0.1395 0.1496 0.0021  0.0071  0.0113  599  LYS   A N   
4226 C  CA  . LYS   A 574 ? 0.1828 0.1456 0.1555 0.0026  0.0065  0.0110  599  LYS   A CA  
4227 C  C   . LYS   A 574 ? 0.1770 0.1412 0.1503 0.0029  0.0072  0.0112  599  LYS   A C   
4228 O  O   . LYS   A 574 ? 0.1813 0.1437 0.1528 0.0032  0.0071  0.0113  599  LYS   A O   
4229 C  CB  . LYS   A 574 ? 0.2090 0.1709 0.1815 0.0032  0.0050  0.0108  599  LYS   A CB  
4230 C  CG  . LYS   A 574 ? 0.2103 0.1749 0.1854 0.0035  0.0044  0.0104  599  LYS   A CG  
4231 C  CD  . LYS   A 574 ? 0.2190 0.1852 0.1951 0.0040  0.0043  0.0104  599  LYS   A CD  
4232 C  CE  . LYS   A 574 ? 0.2168 0.1858 0.1956 0.0042  0.0039  0.0100  599  LYS   A CE  
4233 N  NZ  . LYS   A 574 ? 0.2168 0.1877 0.1967 0.0046  0.0040  0.0101  599  LYS   A NZ  
4234 N  N   . PHE   A 575 ? 0.1733 0.1405 0.1489 0.0028  0.0079  0.0113  600  PHE   A N   
4235 C  CA  . PHE   A 575 ? 0.1740 0.1427 0.1506 0.0033  0.0088  0.0117  600  PHE   A CA  
4236 C  C   . PHE   A 575 ? 0.1788 0.1493 0.1571 0.0039  0.0079  0.0114  600  PHE   A C   
4237 O  O   . PHE   A 575 ? 0.1877 0.1593 0.1671 0.0038  0.0068  0.0110  600  PHE   A O   
4238 C  CB  . PHE   A 575 ? 0.1782 0.1498 0.1569 0.0030  0.0100  0.0122  600  PHE   A CB  
4239 C  CG  . PHE   A 575 ? 0.1761 0.1462 0.1534 0.0027  0.0114  0.0127  600  PHE   A CG  
4240 C  CD1 . PHE   A 575 ? 0.1760 0.1442 0.1517 0.0019  0.0115  0.0126  600  PHE   A CD1 
4241 C  CD2 . PHE   A 575 ? 0.1749 0.1451 0.1523 0.0032  0.0129  0.0133  600  PHE   A CD2 
4242 C  CE1 . PHE   A 575 ? 0.1932 0.1599 0.1675 0.0017  0.0129  0.0131  600  PHE   A CE1 
4243 C  CE2 . PHE   A 575 ? 0.1887 0.1574 0.1648 0.0030  0.0144  0.0138  600  PHE   A CE2 
4244 C  CZ  . PHE   A 575 ? 0.1881 0.1552 0.1627 0.0022  0.0144  0.0137  600  PHE   A CZ  
4245 N  N   . ASN   A 576 ? 0.1729 0.1437 0.1513 0.0044  0.0084  0.0116  601  ASN   A N   
4246 C  CA  . ASN   A 576 ? 0.1808 0.1531 0.1607 0.0050  0.0078  0.0115  601  ASN   A CA  
4247 C  C   . ASN   A 576 ? 0.1900 0.1604 0.1685 0.0051  0.0064  0.0110  601  ASN   A C   
4248 O  O   . ASN   A 576 ? 0.1990 0.1706 0.1787 0.0052  0.0052  0.0107  601  ASN   A O   
4249 C  CB  . ASN   A 576 ? 0.1812 0.1573 0.1641 0.0049  0.0076  0.0115  601  ASN   A CB  
4250 C  CG  . ASN   A 576 ? 0.1853 0.1631 0.1697 0.0056  0.0076  0.0117  601  ASN   A CG  
4251 O  OD1 . ASN   A 576 ? 0.1987 0.1748 0.1820 0.0060  0.0076  0.0116  601  ASN   A OD1 
4252 N  ND2 . ASN   A 576 ? 0.1884 0.1698 0.1755 0.0055  0.0077  0.0120  601  ASN   A ND2 
4253 N  N   . VAL   A 577 ? 0.1882 0.1556 0.1640 0.0050  0.0064  0.0110  602  VAL   A N   
4254 C  CA  . VAL   A 577 ? 0.1872 0.1527 0.1614 0.0049  0.0050  0.0108  602  VAL   A CA  
4255 C  C   . VAL   A 577 ? 0.1973 0.1641 0.1728 0.0053  0.0041  0.0106  602  VAL   A C   
4256 O  O   . VAL   A 577 ? 0.2152 0.1822 0.1907 0.0054  0.0049  0.0107  602  VAL   A O   
4257 C  CB  . VAL   A 577 ? 0.1995 0.1615 0.1701 0.0045  0.0052  0.0109  602  VAL   A CB  
4258 C  CG1 . VAL   A 577 ? 0.2189 0.1792 0.1879 0.0042  0.0035  0.0109  602  VAL   A CG1 
4259 C  CG2 . VAL   A 577 ? 0.2202 0.1811 0.1897 0.0041  0.0062  0.0111  602  VAL   A CG2 
4260 N  N   . GLY   A 578 ? 0.2004 0.1681 0.1770 0.0054  0.0027  0.0105  603  GLY   A N   
4261 C  CA  . GLY   A 578 ? 0.2310 0.2002 0.2090 0.0057  0.0019  0.0103  603  GLY   A CA  
4262 C  C   . GLY   A 578 ? 0.2387 0.2109 0.2195 0.0061  0.0026  0.0103  603  GLY   A C   
4263 O  O   . GLY   A 578 ? 0.2671 0.2407 0.2492 0.0064  0.0021  0.0102  603  GLY   A O   
4264 N  N   . MET   A 579 ? 0.2215 0.1950 0.2032 0.0060  0.0036  0.0104  604  MET   A N   
4265 C  CA  . MET   A 579 ? 0.2163 0.1930 0.2007 0.0063  0.0042  0.0105  604  MET   A CA  
4266 C  C   . MET   A 579 ? 0.2332 0.2101 0.2177 0.0066  0.0049  0.0108  604  MET   A C   
4267 O  O   . MET   A 579 ? 0.2502 0.2294 0.2367 0.0070  0.0048  0.0109  604  MET   A O   
4268 C  CB  . MET   A 579 ? 0.2340 0.2128 0.2203 0.0064  0.0033  0.0101  604  MET   A CB  
4269 C  CG  . MET   A 579 ? 0.2599 0.2411 0.2478 0.0060  0.0038  0.0101  604  MET   A CG  
4270 S  SD  . MET   A 579 ? 0.2727 0.2567 0.2622 0.0061  0.0051  0.0109  604  MET   A SD  
4271 C  CE  . MET   A 579 ? 0.2500 0.2362 0.2415 0.0067  0.0045  0.0108  604  MET   A CE  
4272 N  N   . ASN   A 580 ? 0.2190 0.1934 0.2013 0.0066  0.0057  0.0110  605  ASN   A N   
4273 C  CA  . ASN   A 580 ? 0.2220 0.1960 0.2042 0.0069  0.0068  0.0113  605  ASN   A CA  
4274 C  C   . ASN   A 580 ? 0.2244 0.2003 0.2083 0.0073  0.0085  0.0120  605  ASN   A C   
4275 O  O   . ASN   A 580 ? 0.2579 0.2337 0.2421 0.0077  0.0096  0.0124  605  ASN   A O   
4276 C  CB  . ASN   A 580 ? 0.2385 0.2088 0.2174 0.0065  0.0071  0.0111  605  ASN   A CB  
4277 C  CG  . ASN   A 580 ? 0.2673 0.2364 0.2451 0.0062  0.0054  0.0106  605  ASN   A CG  
4278 O  OD1 . ASN   A 580 ? 0.2646 0.2348 0.2436 0.0063  0.0049  0.0105  605  ASN   A OD1 
4279 N  ND2 . ASN   A 580 ? 0.2814 0.2487 0.2573 0.0057  0.0043  0.0104  605  ASN   A ND2 
4280 N  N   . GLY   A 581 ? 0.2093 0.1868 0.1943 0.0071  0.0087  0.0122  606  GLY   A N   
4281 C  CA  . GLY   A 581 ? 0.1964 0.1763 0.1833 0.0074  0.0102  0.0131  606  GLY   A CA  
4282 C  C   . GLY   A 581 ? 0.1840 0.1679 0.1738 0.0073  0.0096  0.0134  606  GLY   A C   
4283 O  O   . GLY   A 581 ? 0.1872 0.1719 0.1773 0.0068  0.0083  0.0128  606  GLY   A O   
4284 N  N   . TYR   A 582 ? 0.1819 0.1686 0.1740 0.0078  0.0106  0.0144  607  TYR   A N   
4285 C  CA  . TYR   A 582 ? 0.1838 0.1745 0.1785 0.0077  0.0101  0.0149  607  TYR   A CA  
4286 C  C   . TYR   A 582 ? 0.1776 0.1706 0.1735 0.0070  0.0104  0.0154  607  TYR   A C   
4287 O  O   . TYR   A 582 ? 0.1748 0.1706 0.1727 0.0072  0.0113  0.0167  607  TYR   A O   
4288 C  CB  . TYR   A 582 ? 0.1712 0.1637 0.1678 0.0086  0.0110  0.0159  607  TYR   A CB  
4289 C  CG  . TYR   A 582 ? 0.1752 0.1715 0.1742 0.0084  0.0102  0.0162  607  TYR   A CG  
4290 C  CD1 . TYR   A 582 ? 0.1674 0.1637 0.1661 0.0082  0.0088  0.0152  607  TYR   A CD1 
4291 C  CD2 . TYR   A 582 ? 0.1781 0.1783 0.1796 0.0084  0.0108  0.0175  607  TYR   A CD2 
4292 C  CE1 . TYR   A 582 ? 0.1894 0.1891 0.1900 0.0079  0.0082  0.0155  607  TYR   A CE1 
4293 C  CE2 . TYR   A 582 ? 0.1817 0.1854 0.1849 0.0081  0.0100  0.0179  607  TYR   A CE2 
4294 C  CZ  . TYR   A 582 ? 0.1892 0.1925 0.1919 0.0078  0.0087  0.0168  607  TYR   A CZ  
4295 O  OH  . TYR   A 582 ? 0.1953 0.2021 0.1997 0.0074  0.0081  0.0171  607  TYR   A OH  
4296 N  N   . TYR   A 583 ? 0.1664 0.1581 0.1608 0.0061  0.0096  0.0146  608  TYR   A N   
4297 C  CA  . TYR   A 583 ? 0.1659 0.1594 0.1610 0.0052  0.0098  0.0149  608  TYR   A CA  
4298 C  C   . TYR   A 583 ? 0.1707 0.1626 0.1642 0.0043  0.0086  0.0137  608  TYR   A C   
4299 O  O   . TYR   A 583 ? 0.1842 0.1735 0.1762 0.0046  0.0079  0.0128  608  TYR   A O   
4300 C  CB  . TYR   A 583 ? 0.1715 0.1637 0.1659 0.0054  0.0112  0.0157  608  TYR   A CB  
4301 C  CG  . TYR   A 583 ? 0.1599 0.1476 0.1514 0.0056  0.0114  0.0149  608  TYR   A CG  
4302 C  CD1 . TYR   A 583 ? 0.1648 0.1504 0.1544 0.0048  0.0110  0.0142  608  TYR   A CD1 
4303 C  CD2 . TYR   A 583 ? 0.1738 0.1591 0.1641 0.0065  0.0121  0.0149  608  TYR   A CD2 
4304 C  CE1 . TYR   A 583 ? 0.1809 0.1625 0.1677 0.0049  0.0111  0.0137  608  TYR   A CE1 
4305 C  CE2 . TYR   A 583 ? 0.1736 0.1547 0.1608 0.0064  0.0123  0.0143  608  TYR   A CE2 
4306 C  CZ  . TYR   A 583 ? 0.1853 0.1647 0.1708 0.0057  0.0117  0.0138  608  TYR   A CZ  
4307 O  OH  . TYR   A 583 ? 0.2014 0.1768 0.1838 0.0056  0.0117  0.0133  608  TYR   A OH  
4308 N  N   A ILE   A 584 ? 0.1741 0.1676 0.1681 0.0032  0.0085  0.0138  609  ILE   A N   
4309 N  N   B ILE   A 584 ? 0.1725 0.1664 0.1667 0.0031  0.0084  0.0137  609  ILE   A N   
4310 C  CA  A ILE   A 584 ? 0.1677 0.1594 0.1602 0.0024  0.0078  0.0127  609  ILE   A CA  
4311 C  CA  B ILE   A 584 ? 0.1672 0.1597 0.1600 0.0021  0.0077  0.0127  609  ILE   A CA  
4312 C  C   A ILE   A 584 ? 0.1545 0.1447 0.1458 0.0017  0.0084  0.0128  609  ILE   A C   
4313 C  C   B ILE   A 584 ? 0.1634 0.1543 0.1550 0.0015  0.0083  0.0128  609  ILE   A C   
4314 O  O   A ILE   A 584 ? 0.1426 0.1341 0.1348 0.0018  0.0095  0.0139  609  ILE   A O   
4315 O  O   B ILE   A 584 ? 0.1600 0.1528 0.1528 0.0013  0.0092  0.0139  609  ILE   A O   
4316 C  CB  A ILE   A 584 ? 0.1771 0.1712 0.1706 0.0015  0.0070  0.0122  609  ILE   A CB  
4317 C  CB  B ILE   A 584 ? 0.1648 0.1606 0.1590 0.0010  0.0071  0.0125  609  ILE   A CB  
4318 C  CG1 A ILE   A 584 ? 0.1749 0.1726 0.1699 0.0004  0.0074  0.0131  609  ILE   A CG1 
4319 C  CG1 B ILE   A 584 ? 0.1848 0.1816 0.1798 0.0017  0.0064  0.0122  609  ILE   A CG1 
4320 C  CG2 A ILE   A 584 ? 0.1926 0.1878 0.1871 0.0023  0.0064  0.0121  609  ILE   A CG2 
4321 C  CG2 B ILE   A 584 ? 0.1612 0.1555 0.1539 -0.0002 0.0067  0.0115  609  ILE   A CG2 
4322 C  CD1 A ILE   A 584 ? 0.2097 0.2085 0.2045 -0.0009 0.0066  0.0123  609  ILE   A CD1 
4323 C  CD1 B ILE   A 584 ? 0.1922 0.1918 0.1881 0.0006  0.0058  0.0119  609  ILE   A CD1 
4324 N  N   . VAL   A 585 ? 0.1522 0.1398 0.1417 0.0012  0.0079  0.0119  610  VAL   A N   
4325 C  CA  . VAL   A 585 ? 0.1596 0.1453 0.1477 0.0006  0.0085  0.0120  610  VAL   A CA  
4326 C  C   . VAL   A 585 ? 0.1770 0.1625 0.1645 -0.0008 0.0082  0.0114  610  VAL   A C   
4327 O  O   . VAL   A 585 ? 0.1815 0.1655 0.1682 -0.0008 0.0074  0.0105  610  VAL   A O   
4328 C  CB  . VAL   A 585 ? 0.1695 0.1511 0.1552 0.0014  0.0086  0.0118  610  VAL   A CB  
4329 C  CG1 . VAL   A 585 ? 0.1922 0.1720 0.1764 0.0008  0.0094  0.0120  610  VAL   A CG1 
4330 C  CG2 . VAL   A 585 ? 0.1700 0.1512 0.1558 0.0026  0.0089  0.0122  610  VAL   A CG2 
4331 N  N   . HIS   A 586 ? 0.1659 0.1525 0.1536 -0.0019 0.0088  0.0119  611  HIS   A N   
4332 C  CA  . HIS   A 586 ? 0.1664 0.1521 0.1531 -0.0034 0.0087  0.0112  611  HIS   A CA  
4333 C  C   . HIS   A 586 ? 0.1732 0.1559 0.1581 -0.0036 0.0094  0.0114  611  HIS   A C   
4334 O  O   . HIS   A 586 ? 0.2007 0.1837 0.1859 -0.0030 0.0103  0.0123  611  HIS   A O   
4335 C  CB  . HIS   A 586 ? 0.1762 0.1660 0.1647 -0.0049 0.0089  0.0118  611  HIS   A CB  
4336 C  CG  . HIS   A 586 ? 0.1848 0.1738 0.1722 -0.0068 0.0089  0.0111  611  HIS   A CG  
4337 N  ND1 . HIS   A 586 ? 0.1876 0.1736 0.1731 -0.0071 0.0084  0.0098  611  HIS   A ND1 
4338 C  CD2 . HIS   A 586 ? 0.2017 0.1925 0.1895 -0.0085 0.0093  0.0116  611  HIS   A CD2 
4339 C  CE1 . HIS   A 586 ? 0.2128 0.1985 0.1974 -0.0090 0.0087  0.0094  611  HIS   A CE1 
4340 N  NE2 . HIS   A 586 ? 0.2088 0.1974 0.1948 -0.0099 0.0092  0.0105  611  HIS   A NE2 
4341 N  N   . TYR   A 587 ? 0.1819 0.1619 0.1651 -0.0042 0.0093  0.0106  612  TYR   A N   
4342 C  CA  . TYR   A 587 ? 0.1993 0.1762 0.1805 -0.0045 0.0099  0.0107  612  TYR   A CA  
4343 C  C   . TYR   A 587 ? 0.2137 0.1910 0.1947 -0.0064 0.0102  0.0105  612  TYR   A C   
4344 O  O   . TYR   A 587 ? 0.2288 0.2058 0.2095 -0.0072 0.0098  0.0096  612  TYR   A O   
4345 C  CB  . TYR   A 587 ? 0.1977 0.1704 0.1768 -0.0036 0.0093  0.0101  612  TYR   A CB  
4346 C  CG  . TYR   A 587 ? 0.1913 0.1635 0.1704 -0.0020 0.0088  0.0103  612  TYR   A CG  
4347 C  CD1 . TYR   A 587 ? 0.1872 0.1606 0.1675 -0.0013 0.0080  0.0099  612  TYR   A CD1 
4348 C  CD2 . TYR   A 587 ? 0.1904 0.1610 0.1684 -0.0012 0.0093  0.0109  612  TYR   A CD2 
4349 C  CE1 . TYR   A 587 ? 0.1898 0.1629 0.1701 0.0000  0.0076  0.0101  612  TYR   A CE1 
4350 C  CE2 . TYR   A 587 ? 0.1887 0.1587 0.1664 0.0000  0.0089  0.0110  612  TYR   A CE2 
4351 C  CZ  . TYR   A 587 ? 0.1914 0.1628 0.1704 0.0006  0.0080  0.0106  612  TYR   A CZ  
4352 O  OH  . TYR   A 587 ? 0.2240 0.1948 0.2027 0.0016  0.0075  0.0107  612  TYR   A OH  
4353 N  N   . GLU   A 588 ? 0.2160 0.1941 0.1972 -0.0072 0.0111  0.0113  613  GLU   A N   
4354 C  CA  . GLU   A 588 ? 0.2275 0.2061 0.2084 -0.0093 0.0114  0.0111  613  GLU   A CA  
4355 C  C   . GLU   A 588 ? 0.2595 0.2334 0.2378 -0.0096 0.0116  0.0104  613  GLU   A C   
4356 O  O   . GLU   A 588 ? 0.2647 0.2352 0.2413 -0.0082 0.0115  0.0102  613  GLU   A O   
4357 C  CB  . GLU   A 588 ? 0.2455 0.2271 0.2280 -0.0101 0.0123  0.0124  613  GLU   A CB  
4358 C  CG  . GLU   A 588 ? 0.2458 0.2324 0.2313 -0.0100 0.0121  0.0132  613  GLU   A CG  
4359 C  CD  . GLU   A 588 ? 0.2905 0.2810 0.2781 -0.0110 0.0129  0.0146  613  GLU   A CD  
4360 O  OE1 . GLU   A 588 ? 0.2969 0.2861 0.2840 -0.0110 0.0139  0.0151  613  GLU   A OE1 
4361 O  OE2 . GLU   A 588 ? 0.3062 0.3014 0.2963 -0.0117 0.0125  0.0152  613  GLU   A OE2 
4362 N  N   . ASP   A 589 ? 0.2748 0.2486 0.2525 -0.0116 0.0119  0.0100  614  ASP   A N   
4363 C  CA  . ASP   A 589 ? 0.2820 0.2514 0.2571 -0.0122 0.0123  0.0095  614  ASP   A CA  
4364 C  C   . ASP   A 589 ? 0.2815 0.2471 0.2551 -0.0110 0.0118  0.0086  614  ASP   A C   
4365 O  O   . ASP   A 589 ? 0.2897 0.2561 0.2638 -0.0110 0.0113  0.0079  614  ASP   A O   
4366 C  CB  . ASP   A 589 ? 0.3113 0.2794 0.2857 -0.0118 0.0132  0.0104  614  ASP   A CB  
4367 C  CG  . ASP   A 589 ? 0.3950 0.3670 0.3714 -0.0128 0.0138  0.0115  614  ASP   A CG  
4368 O  OD1 . ASP   A 589 ? 0.4090 0.3838 0.3865 -0.0147 0.0138  0.0114  614  ASP   A OD1 
4369 O  OD2 . ASP   A 589 ? 0.4409 0.4136 0.4179 -0.0117 0.0144  0.0124  614  ASP   A OD2 
4370 N  N   . ASP   A 590 ? 0.2888 0.2505 0.2605 -0.0099 0.0119  0.0088  615  ASP   A N   
4371 C  CA  . ASP   A 590 ? 0.3006 0.2590 0.2711 -0.0087 0.0114  0.0082  615  ASP   A CA  
4372 C  C   . ASP   A 590 ? 0.2969 0.2561 0.2684 -0.0067 0.0105  0.0084  615  ASP   A C   
4373 O  O   . ASP   A 590 ? 0.2955 0.2522 0.2661 -0.0055 0.0100  0.0083  615  ASP   A O   
4374 C  CB  . ASP   A 590 ? 0.3271 0.2810 0.2953 -0.0085 0.0119  0.0084  615  ASP   A CB  
4375 C  CG  . ASP   A 590 ? 0.4277 0.3808 0.3951 -0.0076 0.0120  0.0094  615  ASP   A CG  
4376 O  OD1 . ASP   A 590 ? 0.4555 0.4115 0.4241 -0.0073 0.0119  0.0099  615  ASP   A OD1 
4377 O  OD2 . ASP   A 590 ? 0.4578 0.4073 0.4231 -0.0073 0.0122  0.0098  615  ASP   A OD2 
4378 N  N   . GLY   A 591 ? 0.2767 0.2394 0.2498 -0.0064 0.0104  0.0089  616  GLY   A N   
4379 C  CA  . GLY   A 591 ? 0.2605 0.2238 0.2343 -0.0047 0.0096  0.0091  616  GLY   A CA  
4380 C  C   . GLY   A 591 ? 0.2453 0.2084 0.2196 -0.0039 0.0088  0.0085  616  GLY   A C   
4381 O  O   . GLY   A 591 ? 0.2472 0.2085 0.2210 -0.0026 0.0082  0.0086  616  GLY   A O   
4382 N  N   . TRP   A 592 ? 0.2431 0.2083 0.2186 -0.0049 0.0088  0.0078  617  TRP   A N   
4383 C  CA  . TRP   A 592 ? 0.2376 0.2026 0.2136 -0.0042 0.0083  0.0071  617  TRP   A CA  
4384 C  C   . TRP   A 592 ? 0.2539 0.2149 0.2285 -0.0038 0.0084  0.0067  617  TRP   A C   
4385 O  O   . TRP   A 592 ? 0.2640 0.2241 0.2389 -0.0025 0.0078  0.0066  617  TRP   A O   
4386 C  CB  . TRP   A 592 ? 0.2215 0.1896 0.1989 -0.0053 0.0083  0.0065  617  TRP   A CB  
4387 C  CG  . TRP   A 592 ? 0.2073 0.1793 0.1867 -0.0048 0.0079  0.0071  617  TRP   A CG  
4388 C  CD1 . TRP   A 592 ? 0.2110 0.1864 0.1917 -0.0057 0.0081  0.0077  617  TRP   A CD1 
4389 C  CD2 . TRP   A 592 ? 0.1979 0.1707 0.1783 -0.0032 0.0072  0.0072  617  TRP   A CD2 
4390 N  NE1 . TRP   A 592 ? 0.2034 0.1815 0.1857 -0.0047 0.0077  0.0082  617  TRP   A NE1 
4391 C  CE2 . TRP   A 592 ? 0.1956 0.1721 0.1777 -0.0032 0.0071  0.0079  617  TRP   A CE2 
4392 C  CE3 . TRP   A 592 ? 0.2021 0.1729 0.1823 -0.0018 0.0066  0.0070  617  TRP   A CE3 
4393 C  CZ2 . TRP   A 592 ? 0.1951 0.1729 0.1784 -0.0019 0.0066  0.0081  617  TRP   A CZ2 
4394 C  CZ3 . TRP   A 592 ? 0.1990 0.1715 0.1805 -0.0006 0.0060  0.0073  617  TRP   A CZ3 
4395 C  CH2 . TRP   A 592 ? 0.1997 0.1755 0.1826 -0.0007 0.0060  0.0078  617  TRP   A CH2 
4396 N  N   . ASP   A 593 ? 0.2514 0.2099 0.2243 -0.0048 0.0091  0.0066  618  ASP   A N   
4397 C  CA  . ASP   A 593 ? 0.2488 0.2031 0.2202 -0.0043 0.0094  0.0065  618  ASP   A CA  
4398 C  C   . ASP   A 593 ? 0.2564 0.2090 0.2273 -0.0026 0.0087  0.0074  618  ASP   A C   
4399 O  O   . ASP   A 593 ? 0.2752 0.2259 0.2460 -0.0014 0.0084  0.0075  618  ASP   A O   
4400 C  CB  . ASP   A 593 ? 0.2468 0.1989 0.2166 -0.0059 0.0104  0.0063  618  ASP   A CB  
4401 C  CG  . ASP   A 593 ? 0.3432 0.2956 0.3128 -0.0077 0.0111  0.0052  618  ASP   A CG  
4402 O  OD1 . ASP   A 593 ? 0.3511 0.3051 0.3218 -0.0075 0.0108  0.0045  618  ASP   A OD1 
4403 O  OD2 . ASP   A 593 ? 0.3776 0.3285 0.3459 -0.0093 0.0119  0.0049  618  ASP   A OD2 
4404 N  N   . SER   A 594 ? 0.2492 0.2025 0.2197 -0.0025 0.0086  0.0081  619  SER   A N   
4405 C  CA  A SER   A 594 ? 0.2511 0.2028 0.2207 -0.0012 0.0079  0.0090  619  SER   A CA  
4406 C  CA  B SER   A 594 ? 0.2590 0.2107 0.2286 -0.0012 0.0079  0.0090  619  SER   A CA  
4407 C  C   . SER   A 594 ? 0.2577 0.2108 0.2286 0.0002  0.0068  0.0091  619  SER   A C   
4408 O  O   . SER   A 594 ? 0.2745 0.2259 0.2450 0.0013  0.0061  0.0096  619  SER   A O   
4409 C  CB  A SER   A 594 ? 0.2661 0.2183 0.2348 -0.0016 0.0082  0.0096  619  SER   A CB  
4410 C  CB  B SER   A 594 ? 0.2969 0.2493 0.2657 -0.0017 0.0082  0.0096  619  SER   A CB  
4411 O  OG  A SER   A 594 ? 0.2687 0.2189 0.2358 -0.0027 0.0091  0.0098  619  SER   A OG  
4412 O  OG  B SER   A 594 ? 0.3415 0.2922 0.3089 -0.0006 0.0076  0.0103  619  SER   A OG  
4413 N  N   . LEU   A 595 ? 0.2405 0.1971 0.2132 0.0000  0.0067  0.0087  620  LEU   A N   
4414 C  CA  . LEU   A 595 ? 0.2241 0.1820 0.1981 0.0013  0.0057  0.0088  620  LEU   A CA  
4415 C  C   . LEU   A 595 ? 0.2267 0.1841 0.2016 0.0018  0.0055  0.0083  620  LEU   A C   
4416 O  O   . LEU   A 595 ? 0.2296 0.1869 0.2051 0.0030  0.0047  0.0087  620  LEU   A O   
4417 C  CB  . LEU   A 595 ? 0.2225 0.1840 0.1979 0.0010  0.0057  0.0087  620  LEU   A CB  
4418 C  CG  . LEU   A 595 ? 0.2378 0.1996 0.2124 0.0008  0.0061  0.0093  620  LEU   A CG  
4419 C  CD1 . LEU   A 595 ? 0.2471 0.2125 0.2235 0.0004  0.0065  0.0092  620  LEU   A CD1 
4420 C  CD2 . LEU   A 595 ? 0.2562 0.2167 0.2298 0.0019  0.0053  0.0098  620  LEU   A CD2 
4421 N  N   . THR   A 596 ? 0.2158 0.1728 0.1907 0.0009  0.0064  0.0076  621  THR   A N   
4422 C  CA  . THR   A 596 ? 0.2312 0.1870 0.2067 0.0014  0.0065  0.0071  621  THR   A CA  
4423 C  C   . THR   A 596 ? 0.2503 0.2027 0.2248 0.0025  0.0064  0.0078  621  THR   A C   
4424 O  O   . THR   A 596 ? 0.2580 0.2101 0.2336 0.0038  0.0059  0.0081  621  THR   A O   
4425 C  CB  . THR   A 596 ? 0.2562 0.2117 0.2313 -0.0001 0.0076  0.0061  621  THR   A CB  
4426 O  OG1 . THR   A 596 ? 0.2630 0.2220 0.2391 -0.0011 0.0076  0.0056  621  THR   A OG1 
4427 C  CG2 . THR   A 596 ? 0.2767 0.2303 0.2520 0.0004  0.0082  0.0055  621  THR   A CG2 
4428 N  N   . GLY   A 597 ? 0.2451 0.1953 0.2179 0.0020  0.0067  0.0083  622  GLY   A N   
4429 C  CA  . GLY   A 597 ? 0.2526 0.1995 0.2243 0.0030  0.0065  0.0092  622  GLY   A CA  
4430 C  C   . GLY   A 597 ? 0.2536 0.2013 0.2257 0.0043  0.0051  0.0102  622  GLY   A C   
4431 O  O   . GLY   A 597 ? 0.2701 0.2164 0.2426 0.0056  0.0046  0.0110  622  GLY   A O   
4432 N  N   . LEU   A 598 ? 0.2410 0.1908 0.2131 0.0041  0.0045  0.0103  623  LEU   A N   
4433 C  CA  . LEU   A 598 ? 0.2443 0.1948 0.2165 0.0050  0.0032  0.0112  623  LEU   A CA  
4434 C  C   . LEU   A 598 ? 0.2563 0.2085 0.2307 0.0061  0.0025  0.0112  623  LEU   A C   
4435 O  O   . LEU   A 598 ? 0.2715 0.2231 0.2462 0.0071  0.0016  0.0121  623  LEU   A O   
4436 C  CB  . LEU   A 598 ? 0.2562 0.2085 0.2279 0.0043  0.0031  0.0110  623  LEU   A CB  
4437 C  CG  . LEU   A 598 ? 0.3143 0.2668 0.2853 0.0049  0.0019  0.0118  623  LEU   A CG  
4438 C  CD1 . LEU   A 598 ? 0.3477 0.2972 0.3163 0.0050  0.0015  0.0128  623  LEU   A CD1 
4439 C  CD2 . LEU   A 598 ? 0.3236 0.2775 0.2940 0.0043  0.0022  0.0116  623  LEU   A CD2 
4440 N  N   . LEU   A 599 ? 0.2370 0.1913 0.2130 0.0058  0.0030  0.0102  624  LEU   A N   
4441 C  CA  . LEU   A 599 ? 0.2284 0.1844 0.2066 0.0067  0.0025  0.0101  624  LEU   A CA  
4442 C  C   . LEU   A 599 ? 0.2453 0.1992 0.2241 0.0077  0.0029  0.0104  624  LEU   A C   
4443 O  O   . LEU   A 599 ? 0.2501 0.2046 0.2304 0.0089  0.0022  0.0110  624  LEU   A O   
4444 C  CB  . LEU   A 599 ? 0.2213 0.1798 0.2008 0.0061  0.0031  0.0090  624  LEU   A CB  
4445 C  CG  . LEU   A 599 ? 0.2279 0.1888 0.2075 0.0055  0.0028  0.0088  624  LEU   A CG  
4446 C  CD1 . LEU   A 599 ? 0.2250 0.1884 0.2057 0.0047  0.0035  0.0079  624  LEU   A CD1 
4447 C  CD2 . LEU   A 599 ? 0.2433 0.2056 0.2238 0.0064  0.0016  0.0095  624  LEU   A CD2 
4448 N  N   . LYS   A 600 ? 0.2474 0.1987 0.2250 0.0071  0.0041  0.0100  625  LYS   A N   
4449 C  CA  . LYS   A 600 ? 0.2532 0.2022 0.2313 0.0081  0.0047  0.0103  625  LYS   A CA  
4450 C  C   . LYS   A 600 ? 0.2841 0.2312 0.2619 0.0092  0.0040  0.0119  625  LYS   A C   
4451 O  O   . LYS   A 600 ? 0.3076 0.2540 0.2867 0.0106  0.0040  0.0127  625  LYS   A O   
4452 C  CB  . LYS   A 600 ? 0.2801 0.2269 0.2570 0.0070  0.0064  0.0093  625  LYS   A CB  
4453 C  CG  . LYS   A 600 ? 0.3419 0.2908 0.3199 0.0063  0.0070  0.0079  625  LYS   A CG  
4454 C  CD  . LYS   A 600 ? 0.3552 0.3021 0.3319 0.0049  0.0086  0.0068  625  LYS   A CD  
4455 C  CE  . LYS   A 600 ? 0.3189 0.2682 0.2965 0.0041  0.0090  0.0055  625  LYS   A CE  
4456 N  NZ  . LYS   A 600 ? 0.3599 0.3069 0.3360 0.0028  0.0106  0.0043  625  LYS   A NZ  
4457 N  N   . GLY   A 601 ? 0.2966 0.2429 0.2724 0.0086  0.0034  0.0125  626  GLY   A N   
4458 C  CA  . GLY   A 601 ? 0.3163 0.2606 0.2912 0.0095  0.0027  0.0141  626  GLY   A CA  
4459 C  C   . GLY   A 601 ? 0.3245 0.2705 0.2997 0.0101  0.0009  0.0153  626  GLY   A C   
4460 O  O   . GLY   A 601 ? 0.3371 0.2823 0.3127 0.0111  0.0000  0.0168  626  GLY   A O   
4461 N  N   . THR   A 602 ? 0.3278 0.2759 0.3025 0.0092  0.0002  0.0148  627  THR   A N   
4462 C  CA  . THR   A 602 ? 0.3279 0.2772 0.3022 0.0094  -0.0014 0.0157  627  THR   A CA  
4463 C  C   . THR   A 602 ? 0.3068 0.2590 0.2820 0.0089  -0.0016 0.0147  627  THR   A C   
4464 O  O   . THR   A 602 ? 0.2981 0.2507 0.2718 0.0080  -0.0017 0.0144  627  THR   A O   
4465 C  CB  . THR   A 602 ? 0.3779 0.3254 0.3491 0.0086  -0.0018 0.0163  627  THR   A CB  
4466 O  OG1 . THR   A 602 ? 0.4104 0.3575 0.3803 0.0074  -0.0006 0.0152  627  THR   A OG1 
4467 C  CG2 . THR   A 602 ? 0.3920 0.3366 0.3621 0.0091  -0.0018 0.0177  627  THR   A CG2 
4468 N  N   . HIS   A 603 ? 0.2876 0.2418 0.2655 0.0095  -0.0015 0.0142  628  HIS   A N   
4469 C  CA  . HIS   A 603 ? 0.2729 0.2298 0.2517 0.0091  -0.0015 0.0132  628  HIS   A CA  
4470 C  C   . HIS   A 603 ? 0.2773 0.2354 0.2555 0.0089  -0.0028 0.0137  628  HIS   A C   
4471 O  O   . HIS   A 603 ? 0.2734 0.2329 0.2514 0.0082  -0.0026 0.0130  628  HIS   A O   
4472 C  CB  . HIS   A 603 ? 0.2825 0.2412 0.2641 0.0097  -0.0011 0.0126  628  HIS   A CB  
4473 C  CG  . HIS   A 603 ? 0.3094 0.2692 0.2929 0.0109  -0.0021 0.0136  628  HIS   A CG  
4474 N  ND1 . HIS   A 603 ? 0.3681 0.3266 0.3526 0.0120  -0.0021 0.0145  628  HIS   A ND1 
4475 C  CD2 . HIS   A 603 ? 0.3330 0.2954 0.3180 0.0111  -0.0032 0.0138  628  HIS   A CD2 
4476 C  CE1 . HIS   A 603 ? 0.3702 0.3307 0.3568 0.0129  -0.0031 0.0154  628  HIS   A CE1 
4477 N  NE2 . HIS   A 603 ? 0.3389 0.3017 0.3258 0.0123  -0.0038 0.0148  628  HIS   A NE2 
4478 N  N   . THR   A 604 ? 0.2832 0.2407 0.2610 0.0093  -0.0042 0.0150  629  THR   A N   
4479 C  CA  . THR   A 604 ? 0.2970 0.2555 0.2738 0.0089  -0.0054 0.0154  629  THR   A CA  
4480 C  C   . THR   A 604 ? 0.3150 0.2717 0.2885 0.0078  -0.0052 0.0153  629  THR   A C   
4481 O  O   . THR   A 604 ? 0.3339 0.2909 0.3060 0.0072  -0.0061 0.0155  629  THR   A O   
4482 C  CB  . THR   A 604 ? 0.3381 0.2972 0.3159 0.0096  -0.0071 0.0169  629  THR   A CB  
4483 O  OG1 . THR   A 604 ? 0.3704 0.3272 0.3469 0.0098  -0.0073 0.0181  629  THR   A OG1 
4484 C  CG2 . THR   A 604 ? 0.3473 0.3085 0.3286 0.0107  -0.0072 0.0170  629  THR   A CG2 
4485 N  N   . ALA   A 605 ? 0.3022 0.2571 0.2743 0.0074  -0.0040 0.0149  630  ALA   A N   
4486 C  CA  . ALA   A 605 ? 0.3072 0.2605 0.2764 0.0064  -0.0035 0.0147  630  ALA   A CA  
4487 C  C   . ALA   A 605 ? 0.3015 0.2564 0.2709 0.0059  -0.0029 0.0138  630  ALA   A C   
4488 O  O   . ALA   A 605 ? 0.3126 0.2664 0.2796 0.0051  -0.0026 0.0137  630  ALA   A O   
4489 C  CB  . ALA   A 605 ? 0.3166 0.2681 0.2850 0.0061  -0.0021 0.0144  630  ALA   A CB  
4490 N  N   . VAL   A 606 ? 0.2739 0.2312 0.2459 0.0062  -0.0026 0.0131  631  VAL   A N   
4491 C  CA  . VAL   A 606 ? 0.2598 0.2189 0.2324 0.0059  -0.0021 0.0124  631  VAL   A CA  
4492 C  C   . VAL   A 606 ? 0.2352 0.1966 0.2100 0.0065  -0.0031 0.0124  631  VAL   A C   
4493 O  O   . VAL   A 606 ? 0.2463 0.2082 0.2227 0.0072  -0.0038 0.0128  631  VAL   A O   
4494 C  CB  . VAL   A 606 ? 0.2630 0.2232 0.2365 0.0056  -0.0006 0.0116  631  VAL   A CB  
4495 C  CG1 . VAL   A 606 ? 0.2885 0.2466 0.2598 0.0049  0.0004  0.0117  631  VAL   A CG1 
4496 C  CG2 . VAL   A 606 ? 0.2616 0.2232 0.2376 0.0060  -0.0003 0.0111  631  VAL   A CG2 
4497 N  N   . SER   A 607 ? 0.2283 0.1908 0.2031 0.0062  -0.0031 0.0121  632  SER   A N   
4498 C  CA  . SER   A 607 ? 0.2148 0.1792 0.1914 0.0065  -0.0040 0.0121  632  SER   A CA  
4499 C  C   . SER   A 607 ? 0.2025 0.1692 0.1822 0.0071  -0.0035 0.0116  632  SER   A C   
4500 O  O   . SER   A 607 ? 0.2089 0.1760 0.1892 0.0071  -0.0024 0.0111  632  SER   A O   
4501 C  CB  . SER   A 607 ? 0.2309 0.1957 0.2067 0.0060  -0.0037 0.0118  632  SER   A CB  
4502 O  OG  . SER   A 607 ? 0.2402 0.2064 0.2172 0.0061  -0.0023 0.0111  632  SER   A OG  
4503 N  N   . SER   A 608 ? 0.2132 0.1816 0.1948 0.0076  -0.0044 0.0118  633  SER   A N   
4504 C  CA  A SER   A 608 ? 0.2044 0.1749 0.1887 0.0082  -0.0040 0.0114  633  SER   A CA  
4505 C  CA  B SER   A 608 ? 0.2117 0.1822 0.1960 0.0082  -0.0040 0.0114  633  SER   A CA  
4506 C  CA  C SER   A 608 ? 0.2098 0.1803 0.1941 0.0082  -0.0041 0.0114  633  SER   A CA  
4507 C  C   . SER   A 608 ? 0.2066 0.1785 0.1915 0.0078  -0.0028 0.0105  633  SER   A C   
4508 O  O   . SER   A 608 ? 0.2075 0.1802 0.1935 0.0079  -0.0020 0.0100  633  SER   A O   
4509 C  CB  A SER   A 608 ? 0.2105 0.1827 0.1966 0.0086  -0.0051 0.0117  633  SER   A CB  
4510 C  CB  B SER   A 608 ? 0.2378 0.2099 0.2240 0.0087  -0.0051 0.0118  633  SER   A CB  
4511 C  CB  C SER   A 608 ? 0.2285 0.2006 0.2145 0.0086  -0.0052 0.0118  633  SER   A CB  
4512 O  OG  A SER   A 608 ? 0.1951 0.1665 0.1813 0.0090  -0.0062 0.0127  633  SER   A OG  
4513 O  OG  B SER   A 608 ? 0.2616 0.2341 0.2469 0.0081  -0.0056 0.0118  633  SER   A OG  
4514 O  OG  C SER   A 608 ? 0.2448 0.2191 0.2335 0.0091  -0.0047 0.0113  633  SER   A OG  
4515 N  N   . ASN   A 609 ? 0.2091 0.1811 0.1929 0.0074  -0.0027 0.0105  634  ASN   A N   
4516 C  CA  . ASN   A 609 ? 0.2116 0.1851 0.1961 0.0072  -0.0016 0.0100  634  ASN   A CA  
4517 C  C   . ASN   A 609 ? 0.1949 0.1677 0.1785 0.0067  -0.0004 0.0098  634  ASN   A C   
4518 O  O   . ASN   A 609 ? 0.1907 0.1653 0.1756 0.0066  0.0004  0.0095  634  ASN   A O   
4519 C  CB  . ASN   A 609 ? 0.2258 0.1997 0.2099 0.0070  -0.0015 0.0101  634  ASN   A CB  
4520 C  CG  . ASN   A 609 ? 0.2596 0.2349 0.2452 0.0073  -0.0024 0.0101  634  ASN   A CG  
4521 O  OD1 . ASN   A 609 ? 0.2592 0.2357 0.2467 0.0078  -0.0030 0.0101  634  ASN   A OD1 
4522 N  ND2 . ASN   A 609 ? 0.2501 0.2254 0.2352 0.0070  -0.0024 0.0102  634  ASN   A ND2 
4523 N  N   . ASP   A 610 ? 0.1895 0.1598 0.1709 0.0065  -0.0005 0.0101  635  ASP   A N   
4524 C  CA  . ASP   A 610 ? 0.1814 0.1510 0.1620 0.0060  0.0005  0.0099  635  ASP   A CA  
4525 C  C   . ASP   A 610 ? 0.1864 0.1564 0.1683 0.0061  0.0007  0.0096  635  ASP   A C   
4526 O  O   . ASP   A 610 ? 0.1939 0.1649 0.1762 0.0056  0.0016  0.0093  635  ASP   A O   
4527 C  CB  . ASP   A 610 ? 0.1901 0.1568 0.1680 0.0057  0.0004  0.0104  635  ASP   A CB  
4528 C  CG  . ASP   A 610 ? 0.2219 0.1880 0.1984 0.0054  0.0010  0.0105  635  ASP   A CG  
4529 O  OD1 . ASP   A 610 ? 0.2190 0.1864 0.1962 0.0052  0.0021  0.0104  635  ASP   A OD1 
4530 O  OD2 . ASP   A 610 ? 0.2753 0.2399 0.2501 0.0053  0.0002  0.0108  635  ASP   A OD2 
4531 N  N   . ARG   A 611 ? 0.1856 0.1551 0.1681 0.0066  -0.0002 0.0097  636  ARG   A N   
4532 C  CA  . ARG   A 611 ? 0.1823 0.1519 0.1658 0.0067  0.0003  0.0093  636  ARG   A CA  
4533 C  C   . ARG   A 611 ? 0.1832 0.1555 0.1687 0.0066  0.0007  0.0087  636  ARG   A C   
4534 O  O   . ARG   A 611 ? 0.1903 0.1631 0.1760 0.0060  0.0016  0.0081  636  ARG   A O   
4535 C  CB  . ARG   A 611 ? 0.1840 0.1526 0.1681 0.0076  -0.0005 0.0097  636  ARG   A CB  
4536 C  CG  . ARG   A 611 ? 0.1893 0.1554 0.1716 0.0077  -0.0011 0.0105  636  ARG   A CG  
4537 C  CD  . ARG   A 611 ? 0.2116 0.1766 0.1945 0.0085  -0.0016 0.0111  636  ARG   A CD  
4538 N  NE  . ARG   A 611 ? 0.2098 0.1765 0.1946 0.0093  -0.0027 0.0116  636  ARG   A NE  
4539 C  CZ  . ARG   A 611 ? 0.2229 0.1896 0.2074 0.0095  -0.0040 0.0125  636  ARG   A CZ  
4540 N  NH1 . ARG   A 611 ? 0.2246 0.1898 0.2066 0.0088  -0.0044 0.0129  636  ARG   A NH1 
4541 N  NH2 . ARG   A 611 ? 0.2263 0.1946 0.2128 0.0102  -0.0048 0.0130  636  ARG   A NH2 
4542 N  N   . ALA   A 612 ? 0.1769 0.1511 0.1636 0.0070  0.0002  0.0088  637  ALA   A N   
4543 C  CA  . ALA   A 612 ? 0.1718 0.1487 0.1602 0.0068  0.0007  0.0083  637  ALA   A CA  
4544 C  C   . ALA   A 612 ? 0.1860 0.1640 0.1741 0.0060  0.0015  0.0082  637  ALA   A C   
4545 O  O   . ALA   A 612 ? 0.1918 0.1714 0.1807 0.0055  0.0021  0.0077  637  ALA   A O   
4546 C  CB  . ALA   A 612 ? 0.1734 0.1518 0.1630 0.0073  0.0001  0.0085  637  ALA   A CB  
4547 N  N   . SER   A 613 ? 0.1812 0.1584 0.1681 0.0058  0.0017  0.0086  638  SER   A N   
4548 C  CA  . SER   A 613 ? 0.1800 0.1585 0.1669 0.0051  0.0026  0.0087  638  SER   A CA  
4549 C  C   . SER   A 613 ? 0.1800 0.1581 0.1664 0.0043  0.0032  0.0084  638  SER   A C   
4550 O  O   . SER   A 613 ? 0.1854 0.1656 0.1726 0.0036  0.0037  0.0084  638  SER   A O   
4551 C  CB  . SER   A 613 ? 0.2055 0.1829 0.1911 0.0052  0.0030  0.0093  638  SER   A CB  
4552 O  OG  . SER   A 613 ? 0.2421 0.2168 0.2257 0.0050  0.0030  0.0094  638  SER   A OG  
4553 N  N   . LEU   A 614 ? 0.1708 0.1462 0.1558 0.0043  0.0030  0.0083  639  LEU   A N   
4554 C  CA  . LEU   A 614 ? 0.1756 0.1502 0.1600 0.0034  0.0037  0.0079  639  LEU   A CA  
4555 C  C   . LEU   A 614 ? 0.1788 0.1546 0.1642 0.0030  0.0038  0.0072  639  LEU   A C   
4556 O  O   . LEU   A 614 ? 0.1843 0.1610 0.1696 0.0018  0.0044  0.0069  639  LEU   A O   
4557 C  CB  . LEU   A 614 ? 0.1822 0.1533 0.1648 0.0036  0.0035  0.0080  639  LEU   A CB  
4558 C  CG  . LEU   A 614 ? 0.2009 0.1706 0.1820 0.0037  0.0035  0.0087  639  LEU   A CG  
4559 C  CD1 . LEU   A 614 ? 0.2132 0.1795 0.1925 0.0040  0.0031  0.0090  639  LEU   A CD1 
4560 C  CD2 . LEU   A 614 ? 0.2030 0.1733 0.1836 0.0027  0.0045  0.0088  639  LEU   A CD2 
4561 N  N   . ILE   A 615 ? 0.1757 0.1515 0.1619 0.0038  0.0033  0.0070  640  ILE   A N   
4562 C  CA  . ILE   A 615 ? 0.1744 0.1511 0.1614 0.0034  0.0036  0.0062  640  ILE   A CA  
4563 C  C   . ILE   A 615 ? 0.1893 0.1695 0.1774 0.0027  0.0038  0.0062  640  ILE   A C   
4564 O  O   . ILE   A 615 ? 0.1879 0.1690 0.1758 0.0014  0.0043  0.0057  640  ILE   A O   
4565 C  CB  . ILE   A 615 ? 0.1875 0.1641 0.1757 0.0047  0.0031  0.0062  640  ILE   A CB  
4566 C  CG1 . ILE   A 615 ? 0.2016 0.1751 0.1890 0.0055  0.0029  0.0064  640  ILE   A CG1 
4567 C  CG2 . ILE   A 615 ? 0.2015 0.1795 0.1906 0.0043  0.0036  0.0054  640  ILE   A CG2 
4568 C  CD1 . ILE   A 615 ? 0.2146 0.1885 0.2035 0.0068  0.0021  0.0068  640  ILE   A CD1 
4569 N  N   . ASN   A 616 ? 0.1798 0.1619 0.1690 0.0033  0.0034  0.0067  641  ASN   A N   
4570 C  CA  . ASN   A 616 ? 0.1840 0.1694 0.1743 0.0027  0.0036  0.0069  641  ASN   A CA  
4571 C  C   . ASN   A 616 ? 0.1868 0.1732 0.1767 0.0015  0.0041  0.0072  641  ASN   A C   
4572 O  O   . ASN   A 616 ? 0.1860 0.1745 0.1763 0.0003  0.0044  0.0070  641  ASN   A O   
4573 C  CB  . ASN   A 616 ? 0.1884 0.1751 0.1797 0.0036  0.0033  0.0076  641  ASN   A CB  
4574 C  CG  . ASN   A 616 ? 0.2129 0.2030 0.2056 0.0031  0.0036  0.0082  641  ASN   A CG  
4575 O  OD1 . ASN   A 616 ? 0.2148 0.2056 0.2074 0.0027  0.0041  0.0088  641  ASN   A OD1 
4576 N  ND2 . ASN   A 616 ? 0.2391 0.2314 0.2329 0.0031  0.0034  0.0081  641  ASN   A ND2 
4577 N  N   . ASN   A 617 ? 0.1755 0.1604 0.1645 0.0016  0.0044  0.0077  642  ASN   A N   
4578 C  CA  . ASN   A 617 ? 0.1804 0.1666 0.1694 0.0005  0.0049  0.0082  642  ASN   A CA  
4579 C  C   . ASN   A 617 ? 0.1827 0.1683 0.1707 -0.0009 0.0052  0.0075  642  ASN   A C   
4580 O  O   . ASN   A 617 ? 0.1855 0.1735 0.1741 -0.0022 0.0055  0.0077  642  ASN   A O   
4581 C  CB  . ASN   A 617 ? 0.1857 0.1703 0.1738 0.0010  0.0053  0.0088  642  ASN   A CB  
4582 C  CG  . ASN   A 617 ? 0.1986 0.1840 0.1875 0.0020  0.0054  0.0096  642  ASN   A CG  
4583 O  OD1 . ASN   A 617 ? 0.1943 0.1786 0.1825 0.0022  0.0059  0.0101  642  ASN   A OD1 
4584 N  ND2 . ASN   A 617 ? 0.1937 0.1809 0.1839 0.0026  0.0050  0.0096  642  ASN   A ND2 
4585 N  N   . ALA   A 618 ? 0.1883 0.1706 0.1749 -0.0008 0.0052  0.0067  643  ALA   A N   
4586 C  CA  . ALA   A 618 ? 0.1895 0.1707 0.1750 -0.0023 0.0057  0.0060  643  ALA   A CA  
4587 C  C   . ALA   A 618 ? 0.1979 0.1817 0.1840 -0.0034 0.0057  0.0055  643  ALA   A C   
4588 O  O   . ALA   A 618 ? 0.1921 0.1772 0.1778 -0.0052 0.0060  0.0054  643  ALA   A O   
4589 C  CB  . ALA   A 618 ? 0.1991 0.1764 0.1832 -0.0016 0.0058  0.0054  643  ALA   A CB  
4590 N  N   . PHE   A 619 ? 0.1974 0.1820 0.1844 -0.0025 0.0053  0.0052  644  PHE   A N   
4591 C  CA  . PHE   A 619 ? 0.2019 0.1887 0.1892 -0.0037 0.0054  0.0047  644  PHE   A CA  
4592 C  C   . PHE   A 619 ? 0.2062 0.1974 0.1949 -0.0044 0.0051  0.0056  644  PHE   A C   
4593 O  O   . PHE   A 619 ? 0.2225 0.2156 0.2109 -0.0061 0.0052  0.0054  644  PHE   A O   
4594 C  CB  . PHE   A 619 ? 0.1927 0.1791 0.1806 -0.0025 0.0052  0.0042  644  PHE   A CB  
4595 C  CG  . PHE   A 619 ? 0.1972 0.1798 0.1837 -0.0022 0.0057  0.0032  644  PHE   A CG  
4596 C  CD1 . PHE   A 619 ? 0.2074 0.1889 0.1925 -0.0037 0.0065  0.0022  644  PHE   A CD1 
4597 C  CD2 . PHE   A 619 ? 0.2052 0.1852 0.1918 -0.0006 0.0056  0.0035  644  PHE   A CD2 
4598 C  CE1 . PHE   A 619 ? 0.2085 0.1861 0.1924 -0.0033 0.0072  0.0014  644  PHE   A CE1 
4599 C  CE2 . PHE   A 619 ? 0.2008 0.1774 0.1864 -0.0002 0.0061  0.0029  644  PHE   A CE2 
4600 C  CZ  . PHE   A 619 ? 0.1971 0.1723 0.1814 -0.0015 0.0071  0.0018  644  PHE   A CZ  
4601 N  N   A GLN   A 620 ? 0.1920 0.1846 0.1821 -0.0032 0.0049  0.0067  645  GLN   A N   
4602 N  N   B GLN   A 620 ? 0.1879 0.1804 0.1779 -0.0033 0.0049  0.0067  645  GLN   A N   
4603 C  CA  A GLN   A 620 ? 0.1914 0.1880 0.1831 -0.0037 0.0048  0.0079  645  GLN   A CA  
4604 C  CA  B GLN   A 620 ? 0.1847 0.1812 0.1762 -0.0038 0.0048  0.0078  645  GLN   A CA  
4605 C  C   A GLN   A 620 ? 0.1937 0.1912 0.1849 -0.0055 0.0051  0.0082  645  GLN   A C   
4606 C  C   B GLN   A 620 ? 0.1911 0.1886 0.1823 -0.0054 0.0051  0.0082  645  GLN   A C   
4607 O  O   A GLN   A 620 ? 0.2047 0.2058 0.1969 -0.0066 0.0050  0.0089  645  GLN   A O   
4608 O  O   B GLN   A 620 ? 0.2019 0.2030 0.1941 -0.0066 0.0050  0.0090  645  GLN   A O   
4609 C  CB  A GLN   A 620 ? 0.2100 0.2073 0.2030 -0.0021 0.0048  0.0090  645  GLN   A CB  
4610 C  CB  B GLN   A 620 ? 0.1971 0.1943 0.1900 -0.0022 0.0048  0.0089  645  GLN   A CB  
4611 C  CG  A GLN   A 620 ? 0.2174 0.2150 0.2114 -0.0006 0.0045  0.0091  645  GLN   A CG  
4612 C  CG  B GLN   A 620 ? 0.2083 0.2055 0.2019 -0.0009 0.0044  0.0086  645  GLN   A CG  
4613 C  CD  A GLN   A 620 ? 0.2346 0.2341 0.2302 0.0004  0.0047  0.0104  645  GLN   A CD  
4614 C  CD  B GLN   A 620 ? 0.2256 0.2266 0.2205 -0.0015 0.0042  0.0090  645  GLN   A CD  
4615 O  OE1 A GLN   A 620 ? 0.2544 0.2573 0.2514 -0.0001 0.0049  0.0114  645  GLN   A OE1 
4616 O  OE1 B GLN   A 620 ? 0.2021 0.2039 0.1965 -0.0027 0.0041  0.0084  645  GLN   A OE1 
4617 N  NE2 A GLN   A 620 ? 0.1969 0.1947 0.1925 0.0019  0.0047  0.0104  645  GLN   A NE2 
4618 N  NE2 B GLN   A 620 ? 0.2386 0.2418 0.2353 -0.0006 0.0042  0.0102  645  GLN   A NE2 
4619 N  N   . LEU   A 621 ? 0.1939 0.1883 0.1837 -0.0056 0.0055  0.0078  646  LEU   A N   
4620 C  CA  . LEU   A 621 ? 0.1923 0.1873 0.1816 -0.0073 0.0059  0.0082  646  LEU   A CA  
4621 C  C   . LEU   A 621 ? 0.2118 0.2071 0.1999 -0.0094 0.0059  0.0072  646  LEU   A C   
4622 O  O   . LEU   A 621 ? 0.2064 0.2039 0.1946 -0.0112 0.0059  0.0077  646  LEU   A O   
4623 C  CB  . LEU   A 621 ? 0.1884 0.1798 0.1764 -0.0067 0.0063  0.0081  646  LEU   A CB  
4624 C  CG  . LEU   A 621 ? 0.2043 0.1958 0.1933 -0.0050 0.0065  0.0091  646  LEU   A CG  
4625 C  CD1 . LEU   A 621 ? 0.2295 0.2169 0.2167 -0.0043 0.0068  0.0089  646  LEU   A CD1 
4626 C  CD2 . LEU   A 621 ? 0.2103 0.2056 0.2011 -0.0054 0.0069  0.0105  646  LEU   A CD2 
4627 N  N   . VAL   A 622 ? 0.2216 0.2148 0.2084 -0.0094 0.0058  0.0059  647  VAL   A N   
4628 C  CA  . VAL   A 622 ? 0.2203 0.2136 0.2057 -0.0116 0.0060  0.0049  647  VAL   A CA  
4629 C  C   . VAL   A 622 ? 0.2288 0.2270 0.2155 -0.0128 0.0054  0.0057  647  VAL   A C   
4630 O  O   . VAL   A 622 ? 0.2308 0.2308 0.2169 -0.0152 0.0053  0.0057  647  VAL   A O   
4631 C  CB  . VAL   A 622 ? 0.2304 0.2206 0.2146 -0.0109 0.0062  0.0036  647  VAL   A CB  
4632 C  CG1 . VAL   A 622 ? 0.2516 0.2420 0.2341 -0.0132 0.0065  0.0024  647  VAL   A CG1 
4633 C  CG2 . VAL   A 622 ? 0.2399 0.2254 0.2228 -0.0098 0.0067  0.0030  647  VAL   A CG2 
4634 N  N   . SER   A 623 ? 0.2355 0.2361 0.2241 -0.0113 0.0050  0.0065  648  SER   A N   
4635 C  CA  . SER   A 623 ? 0.2563 0.2615 0.2463 -0.0121 0.0044  0.0074  648  SER   A CA  
4636 C  C   . SER   A 623 ? 0.2824 0.2914 0.2737 -0.0135 0.0043  0.0088  648  SER   A C   
4637 O  O   . SER   A 623 ? 0.3110 0.3236 0.3026 -0.0152 0.0038  0.0093  648  SER   A O   
4638 C  CB  . SER   A 623 ? 0.2852 0.2918 0.2771 -0.0100 0.0042  0.0080  648  SER   A CB  
4639 O  OG  . SER   A 623 ? 0.3054 0.3085 0.2962 -0.0088 0.0043  0.0068  648  SER   A OG  
4640 N  N   . ILE   A 624 ? 0.2458 0.2540 0.2378 -0.0127 0.0047  0.0096  649  ILE   A N   
4641 C  CA  . ILE   A 624 ? 0.2524 0.2641 0.2459 -0.0138 0.0047  0.0111  649  ILE   A CA  
4642 C  C   . ILE   A 624 ? 0.2684 0.2784 0.2603 -0.0156 0.0050  0.0106  649  ILE   A C   
4643 O  O   . ILE   A 624 ? 0.2932 0.3054 0.2864 -0.0162 0.0052  0.0119  649  ILE   A O   
4644 C  CB  . ILE   A 624 ? 0.2558 0.2689 0.2517 -0.0116 0.0050  0.0127  649  ILE   A CB  
4645 C  CG1 . ILE   A 624 ? 0.2482 0.2565 0.2429 -0.0100 0.0057  0.0121  649  ILE   A CG1 
4646 C  CG2 . ILE   A 624 ? 0.2621 0.2775 0.2598 -0.0102 0.0047  0.0134  649  ILE   A CG2 
4647 C  CD1 . ILE   A 624 ? 0.2517 0.2610 0.2483 -0.0084 0.0064  0.0136  649  ILE   A CD1 
4648 N  N   . GLY   A 625 ? 0.2692 0.2752 0.2584 -0.0165 0.0053  0.0088  650  GLY   A N   
4649 C  CA  . GLY   A 625 ? 0.2606 0.2646 0.2479 -0.0185 0.0057  0.0081  650  GLY   A CA  
4650 C  C   . GLY   A 625 ? 0.2678 0.2690 0.2549 -0.0175 0.0063  0.0084  650  GLY   A C   
4651 O  O   . GLY   A 625 ? 0.2958 0.2962 0.2819 -0.0192 0.0067  0.0083  650  GLY   A O   
4652 N  N   . LYS   A 626 ? 0.2388 0.2382 0.2266 -0.0149 0.0065  0.0087  651  LYS   A N   
4653 C  CA  . LYS   A 626 ? 0.2321 0.2286 0.2194 -0.0139 0.0072  0.0090  651  LYS   A CA  
4654 C  C   . LYS   A 626 ? 0.2387 0.2297 0.2235 -0.0134 0.0075  0.0075  651  LYS   A C   
4655 O  O   . LYS   A 626 ? 0.2523 0.2406 0.2362 -0.0131 0.0081  0.0076  651  LYS   A O   
4656 C  CB  . LYS   A 626 ? 0.2347 0.2319 0.2238 -0.0114 0.0073  0.0101  651  LYS   A CB  
4657 C  CG  . LYS   A 626 ? 0.2706 0.2728 0.2624 -0.0115 0.0073  0.0119  651  LYS   A CG  
4658 C  CD  . LYS   A 626 ? 0.3147 0.3176 0.3068 -0.0126 0.0080  0.0127  651  LYS   A CD  
4659 C  CE  . LYS   A 626 ? 0.3341 0.3418 0.3293 -0.0123 0.0082  0.0147  651  LYS   A CE  
4660 N  NZ  . LYS   A 626 ? 0.3420 0.3507 0.3378 -0.0133 0.0090  0.0156  651  LYS   A NZ  
4661 N  N   . LEU   A 627 ? 0.2221 0.2115 0.2060 -0.0131 0.0073  0.0064  652  LEU   A N   
4662 C  CA  . LEU   A 627 ? 0.2213 0.2057 0.2031 -0.0125 0.0077  0.0052  652  LEU   A CA  
4663 C  C   . LEU   A 627 ? 0.2261 0.2100 0.2066 -0.0139 0.0078  0.0038  652  LEU   A C   
4664 O  O   . LEU   A 627 ? 0.2501 0.2369 0.2316 -0.0140 0.0073  0.0039  652  LEU   A O   
4665 C  CB  . LEU   A 627 ? 0.2308 0.2134 0.2131 -0.0098 0.0074  0.0053  652  LEU   A CB  
4666 C  CG  . LEU   A 627 ? 0.2459 0.2236 0.2264 -0.0089 0.0078  0.0045  652  LEU   A CG  
4667 C  CD1 . LEU   A 627 ? 0.2581 0.2331 0.2373 -0.0094 0.0083  0.0048  652  LEU   A CD1 
4668 C  CD2 . LEU   A 627 ? 0.2512 0.2281 0.2326 -0.0065 0.0073  0.0048  652  LEU   A CD2 
4669 N  N   . SER   A 628 ? 0.2182 0.1981 0.1964 -0.0148 0.0085  0.0027  653  SER   A N   
4670 C  CA  . SER   A 628 ? 0.2240 0.2029 0.2007 -0.0162 0.0088  0.0013  653  SER   A CA  
4671 C  C   . SER   A 628 ? 0.2247 0.2020 0.2017 -0.0141 0.0088  0.0008  653  SER   A C   
4672 O  O   . SER   A 628 ? 0.2202 0.1958 0.1979 -0.0118 0.0087  0.0013  653  SER   A O   
4673 C  CB  . SER   A 628 ? 0.2565 0.2312 0.2305 -0.0178 0.0098  0.0002  653  SER   A CB  
4674 O  OG  . SER   A 628 ? 0.2830 0.2533 0.2563 -0.0159 0.0103  0.0001  653  SER   A OG  
4675 N  N   . ILE   A 629 ? 0.2161 0.1940 0.1924 -0.0150 0.0089  -0.0001 654  ILE   A N   
4676 C  CA  . ILE   A 629 ? 0.2167 0.1931 0.1934 -0.0131 0.0091  -0.0006 654  ILE   A CA  
4677 C  C   . ILE   A 629 ? 0.2278 0.1989 0.2033 -0.0120 0.0101  -0.0013 654  ILE   A C   
4678 O  O   . ILE   A 629 ? 0.2222 0.1921 0.1987 -0.0097 0.0100  -0.0010 654  ILE   A O   
4679 C  CB  . ILE   A 629 ? 0.2208 0.1987 0.1967 -0.0146 0.0093  -0.0016 654  ILE   A CB  
4680 C  CG1 . ILE   A 629 ? 0.2347 0.2113 0.2112 -0.0126 0.0095  -0.0020 654  ILE   A CG1 
4681 C  CG2 . ILE   A 629 ? 0.2378 0.2129 0.2107 -0.0172 0.0103  -0.0030 654  ILE   A CG2 
4682 C  CD1 . ILE   A 629 ? 0.2469 0.2260 0.2262 -0.0102 0.0086  -0.0008 654  ILE   A CD1 
4683 N  N   . GLU   A 630 ? 0.2254 0.1934 0.1986 -0.0135 0.0109  -0.0019 655  GLU   A N   
4684 C  CA  . GLU   A 630 ? 0.2250 0.1878 0.1970 -0.0124 0.0120  -0.0024 655  GLU   A CA  
4685 C  C   . GLU   A 630 ? 0.2282 0.1905 0.2016 -0.0102 0.0114  -0.0011 655  GLU   A C   
4686 O  O   . GLU   A 630 ? 0.2402 0.2001 0.2140 -0.0082 0.0116  -0.0010 655  GLU   A O   
4687 C  CB  . GLU   A 630 ? 0.2499 0.2095 0.2192 -0.0147 0.0131  -0.0033 655  GLU   A CB  
4688 C  CG  . GLU   A 630 ? 0.2615 0.2208 0.2288 -0.0171 0.0139  -0.0048 655  GLU   A CG  
4689 C  CD  . GLU   A 630 ? 0.2640 0.2273 0.2310 -0.0199 0.0132  -0.0047 655  GLU   A CD  
4690 O  OE1 . GLU   A 630 ? 0.2647 0.2321 0.2337 -0.0197 0.0119  -0.0034 655  GLU   A OE1 
4691 O  OE2 . GLU   A 630 ? 0.2853 0.2477 0.2498 -0.0225 0.0138  -0.0059 655  GLU   A OE2 
4692 N  N   . LYS   A 631 ? 0.2295 0.1942 0.2036 -0.0106 0.0106  -0.0001 656  LYS   A N   
4693 C  CA  . LYS   A 631 ? 0.2294 0.1934 0.2044 -0.0087 0.0101  0.0010  656  LYS   A CA  
4694 C  C   . LYS   A 631 ? 0.2229 0.1887 0.1999 -0.0065 0.0092  0.0016  656  LYS   A C   
4695 O  O   . LYS   A 631 ? 0.2242 0.1883 0.2016 -0.0047 0.0090  0.0023  656  LYS   A O   
4696 C  CB  . LYS   A 631 ? 0.2387 0.2046 0.2138 -0.0098 0.0098  0.0018  656  LYS   A CB  
4697 C  CG  . LYS   A 631 ? 0.3008 0.2640 0.2738 -0.0117 0.0107  0.0014  656  LYS   A CG  
4698 C  CD  . LYS   A 631 ? 0.4046 0.3630 0.3763 -0.0106 0.0113  0.0014  656  LYS   A CD  
4699 C  CE  . LYS   A 631 ? 0.4799 0.4357 0.4496 -0.0122 0.0122  0.0012  656  LYS   A CE  
4700 N  NZ  . LYS   A 631 ? 0.5150 0.4665 0.4839 -0.0107 0.0126  0.0017  656  LYS   A NZ  
4701 N  N   . ALA   A 632 ? 0.2023 0.1719 0.1807 -0.0068 0.0087  0.0016  657  ALA   A N   
4702 C  CA  . ALA   A 632 ? 0.2021 0.1733 0.1824 -0.0048 0.0079  0.0022  657  ALA   A CA  
4703 C  C   . ALA   A 632 ? 0.2020 0.1707 0.1822 -0.0036 0.0084  0.0016  657  ALA   A C   
4704 O  O   . ALA   A 632 ? 0.2118 0.1797 0.1930 -0.0017 0.0079  0.0022  657  ALA   A O   
4705 C  CB  . ALA   A 632 ? 0.2044 0.1801 0.1860 -0.0055 0.0074  0.0023  657  ALA   A CB  
4706 N  N   . LEU   A 633 ? 0.2069 0.1741 0.1858 -0.0047 0.0093  0.0004  658  LEU   A N   
4707 C  CA  . LEU   A 633 ? 0.2190 0.1834 0.1979 -0.0034 0.0100  -0.0001 658  LEU   A CA  
4708 C  C   . LEU   A 633 ? 0.2255 0.1861 0.2039 -0.0021 0.0104  0.0004  658  LEU   A C   
4709 O  O   . LEU   A 633 ? 0.2399 0.1995 0.2195 -0.0002 0.0102  0.0009  658  LEU   A O   
4710 C  CB  . LEU   A 633 ? 0.2180 0.1812 0.1953 -0.0050 0.0113  -0.0015 658  LEU   A CB  
4711 C  CG  . LEU   A 633 ? 0.2276 0.1945 0.2055 -0.0060 0.0109  -0.0019 658  LEU   A CG  
4712 C  CD1 . LEU   A 633 ? 0.2542 0.2195 0.2296 -0.0083 0.0122  -0.0034 658  LEU   A CD1 
4713 C  CD2 . LEU   A 633 ? 0.2426 0.2108 0.2225 -0.0040 0.0106  -0.0016 658  LEU   A CD2 
4714 N  N   . ASP   A 634 ? 0.2236 0.1823 0.2004 -0.0032 0.0108  0.0004  659  ASP   A N   
4715 C  CA  . ASP   A 634 ? 0.2227 0.1778 0.1989 -0.0020 0.0110  0.0011  659  ASP   A CA  
4716 C  C   . ASP   A 634 ? 0.2304 0.1868 0.2082 -0.0001 0.0097  0.0024  659  ASP   A C   
4717 O  O   . ASP   A 634 ? 0.2593 0.2137 0.2375 0.0015  0.0096  0.0031  659  ASP   A O   
4718 C  CB  . ASP   A 634 ? 0.2465 0.1998 0.2208 -0.0036 0.0115  0.0010  659  ASP   A CB  
4719 C  CG  . ASP   A 634 ? 0.3159 0.2667 0.2881 -0.0056 0.0129  -0.0003 659  ASP   A CG  
4720 O  OD1 . ASP   A 634 ? 0.3406 0.2900 0.3126 -0.0053 0.0139  -0.0012 659  ASP   A OD1 
4721 O  OD2 . ASP   A 634 ? 0.3779 0.3280 0.3486 -0.0073 0.0133  -0.0005 659  ASP   A OD2 
4722 N  N   . LEU   A 635 ? 0.2274 0.1873 0.2060 -0.0005 0.0087  0.0029  660  LEU   A N   
4723 C  CA  . LEU   A 635 ? 0.2316 0.1925 0.2113 0.0011  0.0075  0.0040  660  LEU   A CA  
4724 C  C   . LEU   A 635 ? 0.2387 0.2005 0.2202 0.0027  0.0071  0.0042  660  LEU   A C   
4725 O  O   . LEU   A 635 ? 0.2494 0.2102 0.2315 0.0042  0.0065  0.0051  660  LEU   A O   
4726 C  CB  . LEU   A 635 ? 0.2303 0.1945 0.2105 0.0003  0.0069  0.0044  660  LEU   A CB  
4727 C  CG  . LEU   A 635 ? 0.2326 0.1978 0.2136 0.0017  0.0058  0.0054  660  LEU   A CG  
4728 C  CD1 . LEU   A 635 ? 0.2529 0.2197 0.2336 0.0008  0.0057  0.0059  660  LEU   A CD1 
4729 C  CD2 . LEU   A 635 ? 0.2416 0.2094 0.2245 0.0026  0.0052  0.0054  660  LEU   A CD2 
4730 N  N   . SER   A 636 ? 0.2291 0.1926 0.2114 0.0023  0.0075  0.0034  661  SER   A N   
4731 C  CA  . SER   A 636 ? 0.2385 0.2030 0.2226 0.0037  0.0071  0.0035  661  SER   A CA  
4732 C  C   . SER   A 636 ? 0.2337 0.1952 0.2180 0.0052  0.0077  0.0038  661  SER   A C   
4733 O  O   . SER   A 636 ? 0.2386 0.2009 0.2247 0.0067  0.0071  0.0045  661  SER   A O   
4734 C  CB  . SER   A 636 ? 0.2310 0.1977 0.2156 0.0029  0.0075  0.0026  661  SER   A CB  
4735 O  OG  . SER   A 636 ? 0.2564 0.2209 0.2398 0.0022  0.0089  0.0015  661  SER   A OG  
4736 N  N   . LEU   A 637 ? 0.2323 0.1904 0.2151 0.0047  0.0087  0.0035  662  LEU   A N   
4737 C  CA  . LEU   A 637 ? 0.2376 0.1926 0.2207 0.0062  0.0095  0.0039  662  LEU   A CA  
4738 C  C   . LEU   A 637 ? 0.2350 0.1901 0.2193 0.0079  0.0082  0.0055  662  LEU   A C   
4739 O  O   . LEU   A 637 ? 0.2405 0.1944 0.2260 0.0095  0.0084  0.0062  662  LEU   A O   
4740 C  CB  . LEU   A 637 ? 0.2493 0.2004 0.2302 0.0053  0.0108  0.0034  662  LEU   A CB  
4741 C  CG  . LEU   A 637 ? 0.2831 0.2334 0.2626 0.0036  0.0123  0.0018  662  LEU   A CG  
4742 C  CD1 . LEU   A 637 ? 0.2980 0.2441 0.2751 0.0026  0.0137  0.0013  662  LEU   A CD1 
4743 C  CD2 . LEU   A 637 ? 0.3053 0.2551 0.2858 0.0045  0.0133  0.0012  662  LEU   A CD2 
4744 N  N   . TYR   A 638 ? 0.2245 0.1810 0.2083 0.0075  0.0069  0.0061  663  TYR   A N   
4745 C  CA  . TYR   A 638 ? 0.2296 0.1861 0.2141 0.0088  0.0056  0.0076  663  TYR   A CA  
4746 C  C   . TYR   A 638 ? 0.2297 0.1885 0.2166 0.0101  0.0048  0.0081  663  TYR   A C   
4747 O  O   . TYR   A 638 ? 0.2439 0.2027 0.2318 0.0114  0.0039  0.0094  663  TYR   A O   
4748 C  CB  . TYR   A 638 ? 0.2245 0.1819 0.2077 0.0081  0.0046  0.0081  663  TYR   A CB  
4749 C  CG  . TYR   A 638 ? 0.2096 0.1702 0.1940 0.0082  0.0034  0.0083  663  TYR   A CG  
4750 C  CD1 . TYR   A 638 ? 0.2209 0.1821 0.2061 0.0093  0.0021  0.0095  663  TYR   A CD1 
4751 C  CD2 . TYR   A 638 ? 0.2086 0.1717 0.1933 0.0073  0.0036  0.0075  663  TYR   A CD2 
4752 C  CE1 . TYR   A 638 ? 0.2247 0.1886 0.2109 0.0094  0.0011  0.0096  663  TYR   A CE1 
4753 C  CE2 . TYR   A 638 ? 0.2034 0.1693 0.1892 0.0076  0.0026  0.0077  663  TYR   A CE2 
4754 C  CZ  . TYR   A 638 ? 0.2127 0.1788 0.1992 0.0086  0.0015  0.0087  663  TYR   A CZ  
4755 O  OH  . TYR   A 638 ? 0.2085 0.1770 0.1960 0.0087  0.0006  0.0088  663  TYR   A OH  
4756 N  N   . LEU   A 639 ? 0.2137 0.1750 0.2017 0.0097  0.0050  0.0072  664  LEU   A N   
4757 C  CA  . LEU   A 639 ? 0.2077 0.1714 0.1980 0.0108  0.0043  0.0077  664  LEU   A CA  
4758 C  C   . LEU   A 639 ? 0.2143 0.1768 0.2063 0.0124  0.0048  0.0084  664  LEU   A C   
4759 O  O   . LEU   A 639 ? 0.2239 0.1883 0.2179 0.0135  0.0039  0.0092  664  LEU   A O   
4760 C  CB  . LEU   A 639 ? 0.2012 0.1674 0.1921 0.0100  0.0047  0.0066  664  LEU   A CB  
4761 C  CG  . LEU   A 639 ? 0.2035 0.1718 0.1936 0.0089  0.0040  0.0063  664  LEU   A CG  
4762 C  CD1 . LEU   A 639 ? 0.2115 0.1820 0.2020 0.0079  0.0047  0.0052  664  LEU   A CD1 
4763 C  CD2 . LEU   A 639 ? 0.2145 0.1847 0.2057 0.0096  0.0025  0.0073  664  LEU   A CD2 
4764 N  N   . LYS   A 640 ? 0.2185 0.1777 0.2096 0.0127  0.0061  0.0082  665  LYS   A N   
4765 C  CA  . LYS   A 640 ? 0.2433 0.2013 0.2363 0.0144  0.0067  0.0092  665  LYS   A CA  
4766 C  C   . LYS   A 640 ? 0.2720 0.2309 0.2663 0.0157  0.0050  0.0111  665  LYS   A C   
4767 O  O   . LYS   A 640 ? 0.2977 0.2574 0.2944 0.0172  0.0048  0.0122  665  LYS   A O   
4768 C  CB  . LYS   A 640 ? 0.2987 0.2527 0.2904 0.0145  0.0086  0.0088  665  LYS   A CB  
4769 C  CG  . LYS   A 640 ? 0.4195 0.3711 0.4089 0.0138  0.0084  0.0091  665  LYS   A CG  
4770 C  CD  . LYS   A 640 ? 0.5297 0.4771 0.5184 0.0144  0.0103  0.0091  665  LYS   A CD  
4771 C  CE  . LYS   A 640 ? 0.6044 0.5488 0.5904 0.0133  0.0107  0.0090  665  LYS   A CE  
4772 N  NZ  . LYS   A 640 ? 0.6493 0.5895 0.6349 0.0142  0.0124  0.0094  665  LYS   A NZ  
4773 N  N   . HIS   A 641 ? 0.2522 0.2113 0.2449 0.0149  0.0036  0.0116  666  HIS   A N   
4774 C  CA  . HIS   A 641 ? 0.2736 0.2335 0.2669 0.0157  0.0019  0.0134  666  HIS   A CA  
4775 C  C   . HIS   A 641 ? 0.2651 0.2280 0.2585 0.0150  0.0002  0.0134  666  HIS   A C   
4776 O  O   . HIS   A 641 ? 0.2787 0.2421 0.2720 0.0152  -0.0013 0.0147  666  HIS   A O   
4777 C  CB  . HIS   A 641 ? 0.3260 0.2829 0.3171 0.0155  0.0018  0.0141  666  HIS   A CB  
4778 C  CG  . HIS   A 641 ? 0.4204 0.3742 0.4116 0.0163  0.0035  0.0142  666  HIS   A CG  
4779 N  ND1 . HIS   A 641 ? 0.4770 0.4278 0.4657 0.0152  0.0049  0.0132  666  HIS   A ND1 
4780 C  CD2 . HIS   A 641 ? 0.4610 0.4141 0.4543 0.0180  0.0041  0.0153  666  HIS   A CD2 
4781 C  CE1 . HIS   A 641 ? 0.4872 0.4354 0.4765 0.0163  0.0063  0.0136  666  HIS   A CE1 
4782 N  NE2 . HIS   A 641 ? 0.4845 0.4339 0.4767 0.0181  0.0059  0.0149  666  HIS   A NE2 
4783 N  N   . GLU   A 642 ? 0.2366 0.2013 0.2302 0.0142  0.0006  0.0121  667  GLU   A N   
4784 C  CA  . GLU   A 642 ? 0.2303 0.1976 0.2240 0.0136  -0.0007 0.0121  667  GLU   A CA  
4785 C  C   . GLU   A 642 ? 0.2400 0.2096 0.2364 0.0146  -0.0016 0.0130  667  GLU   A C   
4786 O  O   . GLU   A 642 ? 0.2567 0.2268 0.2552 0.0155  -0.0008 0.0129  667  GLU   A O   
4787 C  CB  . GLU   A 642 ? 0.2260 0.1944 0.2190 0.0125  0.0000  0.0106  667  GLU   A CB  
4788 C  CG  . GLU   A 642 ? 0.2103 0.1811 0.2033 0.0119  -0.0010 0.0106  667  GLU   A CG  
4789 C  CD  . GLU   A 642 ? 0.2205 0.1903 0.2115 0.0114  -0.0021 0.0113  667  GLU   A CD  
4790 O  OE1 . GLU   A 642 ? 0.2150 0.1836 0.2040 0.0105  -0.0015 0.0108  667  GLU   A OE1 
4791 O  OE2 . GLU   A 642 ? 0.2151 0.1855 0.2065 0.0118  -0.0034 0.0123  667  GLU   A OE2 
4792 N  N   . THR   A 643 ? 0.2345 0.2055 0.2307 0.0143  -0.0033 0.0138  668  THR   A N   
4793 C  CA  . THR   A 643 ? 0.2277 0.2012 0.2263 0.0150  -0.0044 0.0147  668  THR   A CA  
4794 C  C   . THR   A 643 ? 0.2228 0.1985 0.2214 0.0142  -0.0050 0.0141  668  THR   A C   
4795 O  O   . THR   A 643 ? 0.2231 0.2011 0.2240 0.0146  -0.0056 0.0146  668  THR   A O   
4796 C  CB  . THR   A 643 ? 0.2620 0.2352 0.2604 0.0153  -0.0060 0.0165  668  THR   A CB  
4797 O  OG1 . THR   A 643 ? 0.2661 0.2383 0.2615 0.0140  -0.0068 0.0163  668  THR   A OG1 
4798 C  CG2 . THR   A 643 ? 0.2871 0.2582 0.2859 0.0164  -0.0054 0.0175  668  THR   A CG2 
4799 N  N   . GLU   A 644 ? 0.2105 0.1857 0.2068 0.0130  -0.0048 0.0132  669  GLU   A N   
4800 C  CA  . GLU   A 644 ? 0.2053 0.1822 0.2014 0.0122  -0.0055 0.0129  669  GLU   A CA  
4801 C  C   . GLU   A 644 ? 0.2091 0.1877 0.2062 0.0120  -0.0045 0.0117  669  GLU   A C   
4802 O  O   . GLU   A 644 ? 0.2036 0.1815 0.2002 0.0118  -0.0032 0.0108  669  GLU   A O   
4803 C  CB  . GLU   A 644 ? 0.2339 0.2093 0.2270 0.0112  -0.0059 0.0129  669  GLU   A CB  
4804 C  CG  . GLU   A 644 ? 0.2397 0.2135 0.2316 0.0113  -0.0071 0.0141  669  GLU   A CG  
4805 C  CD  . GLU   A 644 ? 0.2938 0.2692 0.2873 0.0117  -0.0086 0.0154  669  GLU   A CD  
4806 O  OE1 . GLU   A 644 ? 0.3133 0.2900 0.3066 0.0110  -0.0095 0.0153  669  GLU   A OE1 
4807 O  OE2 . GLU   A 644 ? 0.3110 0.2865 0.3062 0.0126  -0.0090 0.0164  669  GLU   A OE2 
4808 N  N   . ILE   A 645 ? 0.1958 0.1764 0.1940 0.0119  -0.0051 0.0118  670  ILE   A N   
4809 C  CA  . ILE   A 645 ? 0.1974 0.1798 0.1968 0.0118  -0.0042 0.0109  670  ILE   A CA  
4810 C  C   . ILE   A 645 ? 0.2025 0.1845 0.2002 0.0110  -0.0033 0.0100  670  ILE   A C   
4811 O  O   . ILE   A 645 ? 0.1986 0.1813 0.1969 0.0109  -0.0022 0.0092  670  ILE   A O   
4812 C  CB  . ILE   A 645 ? 0.1998 0.1844 0.2007 0.0117  -0.0050 0.0113  670  ILE   A CB  
4813 C  CG1 . ILE   A 645 ? 0.2059 0.1924 0.2082 0.0118  -0.0041 0.0105  670  ILE   A CG1 
4814 C  CG2 . ILE   A 645 ? 0.2173 0.2014 0.2162 0.0108  -0.0058 0.0114  670  ILE   A CG2 
4815 C  CD1 . ILE   A 645 ? 0.2098 0.1985 0.2138 0.0118  -0.0049 0.0110  670  ILE   A CD1 
4816 N  N   . MET   A 646 ? 0.2013 0.1825 0.1971 0.0103  -0.0036 0.0101  671  MET   A N   
4817 C  CA  . MET   A 646 ? 0.1863 0.1676 0.1810 0.0096  -0.0026 0.0094  671  MET   A CA  
4818 C  C   . MET   A 646 ? 0.1778 0.1580 0.1718 0.0094  -0.0016 0.0089  671  MET   A C   
4819 O  O   . MET   A 646 ? 0.1819 0.1634 0.1765 0.0091  -0.0008 0.0082  671  MET   A O   
4820 C  CB  . MET   A 646 ? 0.2016 0.1821 0.1945 0.0090  -0.0029 0.0096  671  MET   A CB  
4821 C  CG  . MET   A 646 ? 0.2518 0.2336 0.2454 0.0090  -0.0034 0.0098  671  MET   A CG  
4822 S  SD  . MET   A 646 ? 0.2718 0.2564 0.2673 0.0090  -0.0026 0.0093  671  MET   A SD  
4823 C  CE  . MET   A 646 ? 0.2938 0.2800 0.2919 0.0097  -0.0030 0.0094  671  MET   A CE  
4824 N  N   . PRO   A 647 ? 0.1803 0.1583 0.1732 0.0095  -0.0017 0.0091  672  PRO   A N   
4825 C  CA  . PRO   A 647 ? 0.1706 0.1475 0.1627 0.0091  -0.0007 0.0085  672  PRO   A CA  
4826 C  C   . PRO   A 647 ? 0.1767 0.1541 0.1703 0.0095  0.0000  0.0080  672  PRO   A C   
4827 O  O   . PRO   A 647 ? 0.1855 0.1630 0.1788 0.0089  0.0010  0.0072  672  PRO   A O   
4828 C  CB  . PRO   A 647 ? 0.1883 0.1625 0.1788 0.0092  -0.0009 0.0091  672  PRO   A CB  
4829 C  CG  . PRO   A 647 ? 0.1967 0.1709 0.1877 0.0099  -0.0023 0.0101  672  PRO   A CG  
4830 C  CD  . PRO   A 647 ? 0.1845 0.1608 0.1761 0.0096  -0.0027 0.0100  672  PRO   A CD  
4831 N  N   . VAL   A 648 ? 0.1781 0.1559 0.1735 0.0105  -0.0004 0.0085  673  VAL   A N   
4832 C  CA  . VAL   A 648 ? 0.1705 0.1487 0.1673 0.0109  0.0005  0.0079  673  VAL   A CA  
4833 C  C   . VAL   A 648 ? 0.1730 0.1535 0.1703 0.0103  0.0010  0.0072  673  VAL   A C   
4834 O  O   . VAL   A 648 ? 0.1836 0.1639 0.1804 0.0097  0.0021  0.0063  673  VAL   A O   
4835 C  CB  . VAL   A 648 ? 0.1874 0.1660 0.1862 0.0122  0.0000  0.0087  673  VAL   A CB  
4836 C  CG1 . VAL   A 648 ? 0.1960 0.1752 0.1963 0.0127  0.0012  0.0081  673  VAL   A CG1 
4837 C  CG2 . VAL   A 648 ? 0.2077 0.1840 0.2061 0.0129  -0.0003 0.0096  673  VAL   A CG2 
4838 N  N   . PHE   A 649 ? 0.1739 0.1564 0.1718 0.0103  0.0002  0.0075  674  PHE   A N   
4839 C  CA  . PHE   A 649 ? 0.1678 0.1526 0.1663 0.0097  0.0006  0.0070  674  PHE   A CA  
4840 C  C   . PHE   A 649 ? 0.1831 0.1680 0.1801 0.0086  0.0012  0.0065  674  PHE   A C   
4841 O  O   . PHE   A 649 ? 0.1853 0.1716 0.1825 0.0080  0.0018  0.0059  674  PHE   A O   
4842 C  CB  . PHE   A 649 ? 0.1723 0.1589 0.1719 0.0100  -0.0003 0.0075  674  PHE   A CB  
4843 C  CG  . PHE   A 649 ? 0.1817 0.1693 0.1832 0.0108  -0.0007 0.0079  674  PHE   A CG  
4844 C  CD1 . PHE   A 649 ? 0.1888 0.1756 0.1913 0.0116  -0.0004 0.0080  674  PHE   A CD1 
4845 C  CD2 . PHE   A 649 ? 0.1892 0.1786 0.1917 0.0108  -0.0013 0.0083  674  PHE   A CD2 
4846 C  CE1 . PHE   A 649 ? 0.1977 0.1858 0.2025 0.0124  -0.0008 0.0085  674  PHE   A CE1 
4847 C  CE2 . PHE   A 649 ? 0.2006 0.1912 0.2051 0.0115  -0.0017 0.0086  674  PHE   A CE2 
4848 C  CZ  . PHE   A 649 ? 0.1892 0.1793 0.1949 0.0123  -0.0014 0.0088  674  PHE   A CZ  
4849 N  N   . GLN   A 650 ? 0.1777 0.1613 0.1733 0.0083  0.0010  0.0068  675  GLN   A N   
4850 C  CA  . GLN   A 650 ? 0.1785 0.1623 0.1729 0.0072  0.0016  0.0064  675  GLN   A CA  
4851 C  C   . GLN   A 650 ? 0.1820 0.1648 0.1757 0.0066  0.0025  0.0056  675  GLN   A C   
4852 O  O   . GLN   A 650 ? 0.1876 0.1717 0.1810 0.0055  0.0030  0.0052  675  GLN   A O   
4853 C  CB  . GLN   A 650 ? 0.1944 0.1769 0.1874 0.0069  0.0014  0.0069  675  GLN   A CB  
4854 C  CG  . GLN   A 650 ? 0.2148 0.1986 0.2072 0.0059  0.0019  0.0069  675  GLN   A CG  
4855 C  CD  . GLN   A 650 ? 0.2520 0.2385 0.2457 0.0060  0.0019  0.0071  675  GLN   A CD  
4856 O  OE1 . GLN   A 650 ? 0.2943 0.2810 0.2885 0.0067  0.0014  0.0076  675  GLN   A OE1 
4857 N  NE2 . GLN   A 650 ? 0.2388 0.2275 0.2330 0.0052  0.0023  0.0069  675  GLN   A NE2 
4858 N  N   . GLY   A 651 ? 0.1800 0.1604 0.1735 0.0072  0.0027  0.0055  676  GLY   A N   
4859 C  CA  . GLY   A 651 ? 0.1829 0.1618 0.1755 0.0066  0.0037  0.0047  676  GLY   A CA  
4860 C  C   . GLY   A 651 ? 0.1877 0.1683 0.1812 0.0064  0.0043  0.0040  676  GLY   A C   
4861 O  O   . GLY   A 651 ? 0.1882 0.1688 0.1806 0.0051  0.0051  0.0032  676  GLY   A O   
4862 N  N   . LEU   A 652 ? 0.1714 0.1534 0.1667 0.0074  0.0039  0.0043  677  LEU   A N   
4863 C  CA  . LEU   A 652 ? 0.1692 0.1528 0.1652 0.0071  0.0045  0.0037  677  LEU   A CA  
4864 C  C   . LEU   A 652 ? 0.1797 0.1659 0.1753 0.0059  0.0044  0.0036  677  LEU   A C   
4865 O  O   . LEU   A 652 ? 0.1814 0.1684 0.1763 0.0049  0.0051  0.0029  677  LEU   A O   
4866 C  CB  . LEU   A 652 ? 0.1712 0.1561 0.1694 0.0084  0.0040  0.0043  677  LEU   A CB  
4867 C  CG  . LEU   A 652 ? 0.1955 0.1786 0.1947 0.0098  0.0040  0.0048  677  LEU   A CG  
4868 C  CD1 . LEU   A 652 ? 0.2056 0.1906 0.2072 0.0109  0.0035  0.0054  677  LEU   A CD1 
4869 C  CD2 . LEU   A 652 ? 0.2110 0.1917 0.2094 0.0098  0.0055  0.0040  677  LEU   A CD2 
4870 N  N   . ASN   A 653 ? 0.1620 0.1496 0.1579 0.0059  0.0035  0.0044  678  ASN   A N   
4871 C  CA  . ASN   A 653 ? 0.1725 0.1627 0.1684 0.0050  0.0035  0.0045  678  ASN   A CA  
4872 C  C   . ASN   A 653 ? 0.1759 0.1660 0.1703 0.0034  0.0040  0.0041  678  ASN   A C   
4873 O  O   . ASN   A 653 ? 0.1904 0.1830 0.1849 0.0025  0.0041  0.0041  678  ASN   A O   
4874 C  CB  . ASN   A 653 ? 0.1884 0.1794 0.1848 0.0054  0.0027  0.0055  678  ASN   A CB  
4875 C  CG  . ASN   A 653 ? 0.2280 0.2198 0.2258 0.0065  0.0022  0.0059  678  ASN   A CG  
4876 O  OD1 . ASN   A 653 ? 0.2339 0.2263 0.2328 0.0070  0.0023  0.0056  678  ASN   A OD1 
4877 N  ND2 . ASN   A 653 ? 0.2476 0.2393 0.2455 0.0070  0.0016  0.0066  678  ASN   A ND2 
4878 N  N   . GLU   A 654 ? 0.1742 0.1617 0.1672 0.0032  0.0043  0.0038  679  GLU   A N   
4879 C  CA  . GLU   A 654 ? 0.1752 0.1626 0.1668 0.0015  0.0048  0.0033  679  GLU   A CA  
4880 C  C   . GLU   A 654 ? 0.1750 0.1609 0.1654 0.0007  0.0057  0.0022  679  GLU   A C   
4881 O  O   . GLU   A 654 ? 0.2007 0.1877 0.1900 -0.0010 0.0060  0.0017  679  GLU   A O   
4882 C  CB  . GLU   A 654 ? 0.1868 0.1719 0.1772 0.0014  0.0048  0.0036  679  GLU   A CB  
4883 C  CG  . GLU   A 654 ? 0.2032 0.1891 0.1943 0.0022  0.0041  0.0046  679  GLU   A CG  
4884 C  CD  . GLU   A 654 ? 0.2645 0.2539 0.2566 0.0016  0.0039  0.0053  679  GLU   A CD  
4885 O  OE1 . GLU   A 654 ? 0.2382 0.2292 0.2299 0.0002  0.0041  0.0051  679  GLU   A OE1 
4886 O  OE2 . GLU   A 654 ? 0.2761 0.2664 0.2691 0.0026  0.0034  0.0060  679  GLU   A OE2 
4887 N  N   . LEU   A 655 ? 0.1672 0.1506 0.1576 0.0018  0.0062  0.0018  680  LEU   A N   
4888 C  CA  . LEU   A 655 ? 0.1768 0.1581 0.1658 0.0010  0.0074  0.0006  680  LEU   A CA  
4889 C  C   . LEU   A 655 ? 0.1800 0.1628 0.1695 0.0008  0.0078  0.0000  680  LEU   A C   
4890 O  O   . LEU   A 655 ? 0.1849 0.1673 0.1726 -0.0007 0.0087  -0.0010 680  LEU   A O   
4891 C  CB  . LEU   A 655 ? 0.1717 0.1494 0.1607 0.0024  0.0079  0.0005  680  LEU   A CB  
4892 C  CG  . LEU   A 655 ? 0.1947 0.1703 0.1829 0.0024  0.0077  0.0010  680  LEU   A CG  
4893 C  CD1 . LEU   A 655 ? 0.2043 0.1769 0.1930 0.0040  0.0081  0.0013  680  LEU   A CD1 
4894 C  CD2 . LEU   A 655 ? 0.2133 0.1876 0.1991 0.0004  0.0085  0.0002  680  LEU   A CD2 
4895 N  N   . ILE   A 656 ? 0.1698 0.1543 0.1613 0.0023  0.0073  0.0006  681  ILE   A N   
4896 C  CA  . ILE   A 656 ? 0.1611 0.1469 0.1529 0.0021  0.0079  0.0001  681  ILE   A CA  
4897 C  C   . ILE   A 656 ? 0.1685 0.1569 0.1593 0.0003  0.0077  -0.0002 681  ILE   A C   
4898 O  O   . ILE   A 656 ? 0.1672 0.1552 0.1566 -0.0008 0.0087  -0.0012 681  ILE   A O   
4899 C  CB  . ILE   A 656 ? 0.1633 0.1506 0.1577 0.0039  0.0073  0.0009  681  ILE   A CB  
4900 C  CG1 . ILE   A 656 ? 0.1851 0.1697 0.1803 0.0055  0.0077  0.0010  681  ILE   A CG1 
4901 C  CG2 . ILE   A 656 ? 0.1773 0.1665 0.1721 0.0036  0.0077  0.0005  681  ILE   A CG2 
4902 C  CD1 . ILE   A 656 ? 0.1978 0.1839 0.1956 0.0071  0.0070  0.0019  681  ILE   A CD1 
4903 N  N   . PRO   A 657 ? 0.1661 0.1571 0.1573 -0.0003 0.0067  0.0007  682  PRO   A N   
4904 C  CA  . PRO   A 657 ? 0.1627 0.1565 0.1531 -0.0021 0.0066  0.0006  682  PRO   A CA  
4905 C  C   . PRO   A 657 ? 0.1704 0.1628 0.1582 -0.0042 0.0074  -0.0005 682  PRO   A C   
4906 O  O   . PRO   A 657 ? 0.1795 0.1736 0.1662 -0.0058 0.0076  -0.0009 682  PRO   A O   
4907 C  CB  . PRO   A 657 ? 0.1745 0.1708 0.1660 -0.0021 0.0056  0.0019  682  PRO   A CB  
4908 C  CG  . PRO   A 657 ? 0.1787 0.1743 0.1720 0.0000  0.0051  0.0026  682  PRO   A CG  
4909 C  CD  . PRO   A 657 ? 0.1665 0.1583 0.1591 0.0008  0.0057  0.0019  682  PRO   A CD  
4910 N  N   . MET   A 658 ? 0.1625 0.1516 0.1491 -0.0043 0.0079  -0.0010 683  MET   A N   
4911 C  CA  . MET   A 658 ? 0.1754 0.1627 0.1592 -0.0065 0.0088  -0.0022 683  MET   A CA  
4912 C  C   . MET   A 658 ? 0.1789 0.1644 0.1613 -0.0070 0.0101  -0.0035 683  MET   A C   
4913 O  O   . MET   A 658 ? 0.1860 0.1722 0.1663 -0.0092 0.0104  -0.0042 683  MET   A O   
4914 C  CB  . MET   A 658 ? 0.1834 0.1671 0.1663 -0.0064 0.0092  -0.0024 683  MET   A CB  
4915 C  CG  . MET   A 658 ? 0.1881 0.1733 0.1722 -0.0060 0.0081  -0.0012 683  MET   A CG  
4916 S  SD  . MET   A 658 ? 0.2089 0.1898 0.1916 -0.0060 0.0087  -0.0015 683  MET   A SD  
4917 C  CE  . MET   A 658 ? 0.2074 0.1907 0.1918 -0.0052 0.0074  0.0001  683  MET   A CE  
4918 N  N   . TYR   A 659 ? 0.1792 0.1627 0.1627 -0.0049 0.0108  -0.0036 684  TYR   A N   
4919 C  CA  . TYR   A 659 ? 0.1728 0.1547 0.1551 -0.0052 0.0122  -0.0048 684  TYR   A CA  
4920 C  C   . TYR   A 659 ? 0.1757 0.1611 0.1586 -0.0056 0.0118  -0.0046 684  TYR   A C   
4921 O  O   . TYR   A 659 ? 0.1850 0.1696 0.1659 -0.0068 0.0129  -0.0057 684  TYR   A O   
4922 C  CB  . TYR   A 659 ? 0.1815 0.1598 0.1646 -0.0032 0.0134  -0.0051 684  TYR   A CB  
4923 C  CG  . TYR   A 659 ? 0.1760 0.1558 0.1622 -0.0007 0.0129  -0.0041 684  TYR   A CG  
4924 C  CD1 . TYR   A 659 ? 0.1805 0.1626 0.1678 -0.0004 0.0129  -0.0040 684  TYR   A CD1 
4925 C  CD2 . TYR   A 659 ? 0.1758 0.1544 0.1640 0.0012  0.0124  -0.0032 684  TYR   A CD2 
4926 C  CE1 . TYR   A 659 ? 0.1772 0.1605 0.1674 0.0017  0.0125  -0.0031 684  TYR   A CE1 
4927 C  CE2 . TYR   A 659 ? 0.1859 0.1658 0.1768 0.0033  0.0119  -0.0023 684  TYR   A CE2 
4928 C  CZ  . TYR   A 659 ? 0.1914 0.1737 0.1835 0.0035  0.0120  -0.0022 684  TYR   A CZ  
4929 O  OH  . TYR   A 659 ? 0.2215 0.2049 0.2163 0.0054  0.0114  -0.0013 684  TYR   A OH  
4930 N  N   . LYS   A 660 ? 0.1605 0.1495 0.1459 -0.0046 0.0103  -0.0032 685  LYS   A N   
4931 C  CA  . LYS   A 660 ? 0.1611 0.1535 0.1470 -0.0051 0.0099  -0.0029 685  LYS   A CA  
4932 C  C   . LYS   A 660 ? 0.1729 0.1671 0.1564 -0.0079 0.0097  -0.0033 685  LYS   A C   
4933 O  O   . LYS   A 660 ? 0.1842 0.1798 0.1666 -0.0089 0.0100  -0.0036 685  LYS   A O   
4934 C  CB  . LYS   A 660 ? 0.1556 0.1512 0.1444 -0.0036 0.0086  -0.0014 685  LYS   A CB  
4935 C  CG  . LYS   A 660 ? 0.1626 0.1569 0.1537 -0.0011 0.0085  -0.0009 685  LYS   A CG  
4936 C  CD  . LYS   A 660 ? 0.1790 0.1718 0.1704 -0.0001 0.0097  -0.0016 685  LYS   A CD  
4937 C  CE  . LYS   A 660 ? 0.1813 0.1769 0.1734 -0.0002 0.0096  -0.0013 685  LYS   A CE  
4938 N  NZ  . LYS   A 660 ? 0.1838 0.1777 0.1762 0.0006  0.0110  -0.0021 685  LYS   A NZ  
4939 N  N   . LEU   A 661 ? 0.1740 0.1683 0.1566 -0.0092 0.0092  -0.0031 686  LEU   A N   
4940 C  CA  . LEU   A 661 ? 0.1624 0.1583 0.1427 -0.0120 0.0090  -0.0034 686  LEU   A CA  
4941 C  C   . LEU   A 661 ? 0.1730 0.1653 0.1498 -0.0137 0.0106  -0.0053 686  LEU   A C   
4942 O  O   . LEU   A 661 ? 0.1787 0.1723 0.1535 -0.0157 0.0108  -0.0058 686  LEU   A O   
4943 C  CB  . LEU   A 661 ? 0.1663 0.1629 0.1464 -0.0131 0.0082  -0.0028 686  LEU   A CB  
4944 C  CG  . LEU   A 661 ? 0.1729 0.1729 0.1560 -0.0118 0.0068  -0.0009 686  LEU   A CG  
4945 C  CD1 . LEU   A 661 ? 0.1923 0.1930 0.1750 -0.0132 0.0063  -0.0004 686  LEU   A CD1 
4946 C  CD2 . LEU   A 661 ? 0.1826 0.1871 0.1671 -0.0119 0.0060  0.0003  686  LEU   A CD2 
4947 N  N   . MET   A 662 ? 0.1790 0.1668 0.1551 -0.0129 0.0118  -0.0062 687  MET   A N   
4948 C  CA  . MET   A 662 ? 0.1802 0.1640 0.1529 -0.0143 0.0136  -0.0080 687  MET   A CA  
4949 C  C   . MET   A 662 ? 0.1986 0.1821 0.1708 -0.0140 0.0147  -0.0088 687  MET   A C   
4950 O  O   . MET   A 662 ? 0.2021 0.1838 0.1709 -0.0161 0.0159  -0.0102 687  MET   A O   
4951 C  CB  . MET   A 662 ? 0.2032 0.1822 0.1758 -0.0129 0.0148  -0.0086 687  MET   A CB  
4952 C  CG  . MET   A 662 ? 0.2072 0.1859 0.1798 -0.0135 0.0140  -0.0081 687  MET   A CG  
4953 S  SD  . MET   A 662 ? 0.2388 0.2123 0.2120 -0.0112 0.0152  -0.0083 687  MET   A SD  
4954 C  CE  . MET   A 662 ? 0.2457 0.2202 0.2192 -0.0120 0.0138  -0.0073 687  MET   A CE  
4955 N  N   . GLU   A 663 ? 0.1845 0.1693 0.1597 -0.0115 0.0144  -0.0079 688  GLU   A N   
4956 C  CA  . GLU   A 663 ? 0.1842 0.1690 0.1593 -0.0110 0.0155  -0.0085 688  GLU   A CA  
4957 C  C   . GLU   A 663 ? 0.1956 0.1833 0.1687 -0.0133 0.0151  -0.0086 688  GLU   A C   
4958 O  O   . GLU   A 663 ? 0.2140 0.2006 0.1854 -0.0138 0.0164  -0.0096 688  GLU   A O   
4959 C  CB  . GLU   A 663 ? 0.1791 0.1658 0.1582 -0.0081 0.0148  -0.0072 688  GLU   A CB  
4960 C  CG  . GLU   A 663 ? 0.1907 0.1741 0.1715 -0.0056 0.0157  -0.0071 688  GLU   A CG  
4961 C  CD  . GLU   A 663 ? 0.1995 0.1849 0.1841 -0.0030 0.0149  -0.0058 688  GLU   A CD  
4962 O  OE1 . GLU   A 663 ? 0.2114 0.2007 0.1975 -0.0030 0.0135  -0.0048 688  GLU   A OE1 
4963 O  OE2 . GLU   A 663 ? 0.2041 0.1873 0.1903 -0.0010 0.0157  -0.0058 688  GLU   A OE2 
4964 N  N   . LYS   A 664 ? 0.1922 0.1837 0.1655 -0.0147 0.0133  -0.0076 689  LYS   A N   
4965 C  CA  . LYS   A 664 ? 0.2041 0.1989 0.1758 -0.0170 0.0126  -0.0074 689  LYS   A CA  
4966 C  C   . LYS   A 664 ? 0.2271 0.2212 0.1950 -0.0204 0.0127  -0.0083 689  LYS   A C   
4967 O  O   . LYS   A 664 ? 0.2495 0.2473 0.2164 -0.0226 0.0115  -0.0077 689  LYS   A O   
4968 C  CB  . LYS   A 664 ? 0.2101 0.2101 0.1849 -0.0162 0.0106  -0.0053 689  LYS   A CB  
4969 C  CG  . LYS   A 664 ? 0.1948 0.1952 0.1731 -0.0130 0.0106  -0.0045 689  LYS   A CG  
4970 C  CD  . LYS   A 664 ? 0.1910 0.1958 0.1723 -0.0121 0.0089  -0.0025 689  LYS   A CD  
4971 C  CE  . LYS   A 664 ? 0.2109 0.2158 0.1955 -0.0091 0.0089  -0.0018 689  LYS   A CE  
4972 N  NZ  . LYS   A 664 ? 0.2089 0.2105 0.1945 -0.0074 0.0093  -0.0022 689  LYS   A NZ  
4973 N  N   . ARG   A 665 ? 0.2007 0.1903 0.1666 -0.0210 0.0140  -0.0097 690  ARG   A N   
4974 C  CA  . ARG   A 665 ? 0.2118 0.2001 0.1739 -0.0244 0.0141  -0.0107 690  ARG   A CA  
4975 C  C   . ARG   A 665 ? 0.2322 0.2145 0.1908 -0.0250 0.0167  -0.0130 690  ARG   A C   
4976 O  O   . ARG   A 665 ? 0.2270 0.2063 0.1867 -0.0226 0.0182  -0.0134 690  ARG   A O   
4977 C  CB  . ARG   A 665 ? 0.2228 0.2113 0.1861 -0.0244 0.0132  -0.0099 690  ARG   A CB  
4978 C  CG  . ARG   A 665 ? 0.2051 0.1993 0.1716 -0.0239 0.0109  -0.0077 690  ARG   A CG  
4979 C  CD  . ARG   A 665 ? 0.2071 0.2054 0.1721 -0.0270 0.0097  -0.0072 690  ARG   A CD  
4980 N  NE  . ARG   A 665 ? 0.2134 0.2101 0.1753 -0.0301 0.0099  -0.0081 690  ARG   A NE  
4981 C  CZ  . ARG   A 665 ? 0.2370 0.2349 0.1999 -0.0306 0.0089  -0.0072 690  ARG   A CZ  
4982 N  NH1 . ARG   A 665 ? 0.2075 0.2082 0.1744 -0.0282 0.0078  -0.0054 690  ARG   A NH1 
4983 N  NH2 . ARG   A 665 ? 0.2473 0.2435 0.2072 -0.0335 0.0092  -0.0081 690  ARG   A NH2 
4984 N  N   . ASP   A 666 ? 0.2392 0.2197 0.1936 -0.0284 0.0172  -0.0142 691  ASP   A N   
4985 C  CA  . ASP   A 666 ? 0.2561 0.2304 0.2066 -0.0294 0.0199  -0.0165 691  ASP   A CA  
4986 C  C   . ASP   A 666 ? 0.2609 0.2313 0.2119 -0.0283 0.0206  -0.0168 691  ASP   A C   
4987 O  O   . ASP   A 666 ? 0.2825 0.2510 0.2309 -0.0308 0.0207  -0.0175 691  ASP   A O   
4988 C  CB  . ASP   A 666 ? 0.2762 0.2504 0.2217 -0.0339 0.0199  -0.0177 691  ASP   A CB  
4989 C  CG  . ASP   A 666 ? 0.3579 0.3253 0.2986 -0.0354 0.0228  -0.0202 691  ASP   A CG  
4990 O  OD1 . ASP   A 666 ? 0.3241 0.2876 0.2656 -0.0329 0.0249  -0.0209 691  ASP   A OD1 
4991 O  OD2 . ASP   A 666 ? 0.4172 0.3834 0.3536 -0.0393 0.0230  -0.0214 691  ASP   A OD2 
4992 N  N   . MET   A 667 ? 0.2368 0.2063 0.1916 -0.0246 0.0208  -0.0159 692  MET   A N   
4993 C  CA  . MET   A 667 ? 0.2455 0.2122 0.2016 -0.0231 0.0211  -0.0157 692  MET   A CA  
4994 C  C   . MET   A 667 ? 0.2561 0.2189 0.2139 -0.0199 0.0229  -0.0159 692  MET   A C   
4995 O  O   . MET   A 667 ? 0.2433 0.2058 0.2041 -0.0173 0.0224  -0.0148 692  MET   A O   
4996 C  CB  . MET   A 667 ? 0.2399 0.2113 0.1999 -0.0218 0.0185  -0.0136 692  MET   A CB  
4997 C  CG  . MET   A 667 ? 0.2276 0.2028 0.1865 -0.0247 0.0169  -0.0131 692  MET   A CG  
4998 S  SD  . MET   A 667 ? 0.2482 0.2286 0.2118 -0.0228 0.0143  -0.0106 692  MET   A SD  
4999 C  CE  . MET   A 667 ? 0.2687 0.2525 0.2302 -0.0268 0.0129  -0.0102 692  MET   A CE  
5000 N  N   . ASN   A 668 ? 0.2544 0.2141 0.2100 -0.0200 0.0251  -0.0173 693  ASN   A N   
5001 C  CA  . ASN   A 668 ? 0.2546 0.2112 0.2124 -0.0167 0.0268  -0.0173 693  ASN   A CA  
5002 C  C   . ASN   A 668 ? 0.2622 0.2147 0.2207 -0.0152 0.0277  -0.0172 693  ASN   A C   
5003 O  O   . ASN   A 668 ? 0.2611 0.2138 0.2234 -0.0120 0.0276  -0.0159 693  ASN   A O   
5004 C  CB  . ASN   A 668 ? 0.2980 0.2514 0.2530 -0.0174 0.0295  -0.0189 693  ASN   A CB  
5005 C  CG  . ASN   A 668 ? 0.3853 0.3346 0.3418 -0.0145 0.0318  -0.0191 693  ASN   A CG  
5006 O  OD1 . ASN   A 668 ? 0.4237 0.3751 0.3841 -0.0117 0.0314  -0.0179 693  ASN   A OD1 
5007 N  ND2 . ASN   A 668 ? 0.3891 0.3326 0.3430 -0.0150 0.0340  -0.0203 693  ASN   A ND2 
5008 N  N   . GLU   A 669 ? 0.2724 0.2211 0.2274 -0.0175 0.0288  -0.0184 694  GLU   A N   
5009 C  CA  . GLU   A 669 ? 0.2716 0.2160 0.2269 -0.0161 0.0299  -0.0183 694  GLU   A CA  
5010 C  C   . GLU   A 669 ? 0.2735 0.2208 0.2325 -0.0143 0.0276  -0.0164 694  GLU   A C   
5011 O  O   . GLU   A 669 ? 0.2814 0.2273 0.2432 -0.0113 0.0280  -0.0154 694  GLU   A O   
5012 C  CB  . GLU   A 669 ? 0.3077 0.2475 0.2581 -0.0193 0.0315  -0.0201 694  GLU   A CB  
5013 C  CG  . GLU   A 669 ? 0.3792 0.3155 0.3254 -0.0212 0.0339  -0.0222 694  GLU   A CG  
5014 C  CD  . GLU   A 669 ? 0.4444 0.3842 0.3879 -0.0245 0.0328  -0.0228 694  GLU   A CD  
5015 O  OE1 . GLU   A 669 ? 0.5048 0.4415 0.4445 -0.0263 0.0349  -0.0246 694  GLU   A OE1 
5016 O  OE2 . GLU   A 669 ? 0.3930 0.3386 0.3382 -0.0254 0.0300  -0.0216 694  GLU   A OE2 
5017 N  N   . VAL   A 670 ? 0.2543 0.2057 0.2134 -0.0161 0.0253  -0.0158 695  VAL   A N   
5018 C  CA  . VAL   A 670 ? 0.2508 0.2050 0.2130 -0.0146 0.0232  -0.0140 695  VAL   A CA  
5019 C  C   . VAL   A 670 ? 0.2439 0.2017 0.2103 -0.0117 0.0220  -0.0125 695  VAL   A C   
5020 O  O   . VAL   A 670 ? 0.2381 0.1957 0.2072 -0.0093 0.0214  -0.0113 695  VAL   A O   
5021 C  CB  . VAL   A 670 ? 0.2591 0.2168 0.2203 -0.0174 0.0213  -0.0137 695  VAL   A CB  
5022 C  CG1 . VAL   A 670 ? 0.2669 0.2279 0.2314 -0.0158 0.0192  -0.0118 695  VAL   A CG1 
5023 C  CG2 . VAL   A 670 ? 0.2725 0.2264 0.2297 -0.0202 0.0225  -0.0151 695  VAL   A CG2 
5024 N  N   . GLU   A 671 ? 0.2249 0.1854 0.1917 -0.0118 0.0218  -0.0126 696  GLU   A N   
5025 C  CA  . GLU   A 671 ? 0.2290 0.1927 0.1997 -0.0091 0.0208  -0.0113 696  GLU   A CA  
5026 C  C   . GLU   A 671 ? 0.2358 0.1963 0.2085 -0.0062 0.0222  -0.0110 696  GLU   A C   
5027 O  O   . GLU   A 671 ? 0.2354 0.1974 0.2114 -0.0039 0.0210  -0.0095 696  GLU   A O   
5028 C  CB  . GLU   A 671 ? 0.2372 0.2035 0.2075 -0.0099 0.0209  -0.0117 696  GLU   A CB  
5029 C  CG  . GLU   A 671 ? 0.2427 0.2120 0.2167 -0.0073 0.0200  -0.0104 696  GLU   A CG  
5030 C  CD  . GLU   A 671 ? 0.2883 0.2586 0.2617 -0.0077 0.0210  -0.0111 696  GLU   A CD  
5031 O  OE1 . GLU   A 671 ? 0.3307 0.3010 0.3009 -0.0103 0.0214  -0.0122 696  GLU   A OE1 
5032 O  OE2 . GLU   A 671 ? 0.2569 0.2278 0.2330 -0.0054 0.0213  -0.0105 696  GLU   A OE2 
5033 N  N   . THR   A 672 ? 0.2377 0.1937 0.2082 -0.0064 0.0247  -0.0123 697  THR   A N   
5034 C  CA  . THR   A 672 ? 0.2406 0.1935 0.2131 -0.0036 0.0263  -0.0119 697  THR   A CA  
5035 C  C   . THR   A 672 ? 0.2380 0.1891 0.2117 -0.0023 0.0258  -0.0110 697  THR   A C   
5036 O  O   . THR   A 672 ? 0.2413 0.1930 0.2184 0.0004  0.0253  -0.0095 697  THR   A O   
5037 C  CB  . THR   A 672 ? 0.2687 0.2168 0.2384 -0.0041 0.0294  -0.0136 697  THR   A CB  
5038 O  OG1 . THR   A 672 ? 0.2804 0.2306 0.2495 -0.0049 0.0297  -0.0142 697  THR   A OG1 
5039 C  CG2 . THR   A 672 ? 0.2936 0.2383 0.2655 -0.0011 0.0313  -0.0131 697  THR   A CG2 
5040 N  N   . GLN   A 673 ? 0.2293 0.1782 0.2001 -0.0043 0.0259  -0.0117 698  GLN   A N   
5041 C  CA  . GLN   A 673 ? 0.2301 0.1769 0.2016 -0.0033 0.0256  -0.0108 698  GLN   A CA  
5042 C  C   . GLN   A 673 ? 0.2387 0.1900 0.2133 -0.0022 0.0228  -0.0090 698  GLN   A C   
5043 O  O   . GLN   A 673 ? 0.2537 0.2041 0.2303 -0.0002 0.0224  -0.0078 698  GLN   A O   
5044 C  CB  . GLN   A 673 ? 0.2365 0.1804 0.2042 -0.0061 0.0262  -0.0120 698  GLN   A CB  
5045 C  CG  . GLN   A 673 ? 0.2703 0.2085 0.2348 -0.0069 0.0293  -0.0137 698  GLN   A CG  
5046 C  CD  . GLN   A 673 ? 0.4139 0.3493 0.3744 -0.0100 0.0298  -0.0150 698  GLN   A CD  
5047 O  OE1 . GLN   A 673 ? 0.4750 0.4124 0.4354 -0.0113 0.0281  -0.0144 698  GLN   A OE1 
5048 N  NE2 . GLN   A 673 ? 0.4508 0.3811 0.4078 -0.0114 0.0325  -0.0167 698  GLN   A NE2 
5049 N  N   . PHE   A 674 ? 0.2215 0.1772 0.1963 -0.0035 0.0211  -0.0089 699  PHE   A N   
5050 C  CA  . PHE   A 674 ? 0.2241 0.1837 0.2014 -0.0026 0.0187  -0.0073 699  PHE   A CA  
5051 C  C   . PHE   A 674 ? 0.2251 0.1863 0.2059 0.0002  0.0182  -0.0061 699  PHE   A C   
5052 O  O   . PHE   A 674 ? 0.2234 0.1851 0.2063 0.0019  0.0171  -0.0048 699  PHE   A O   
5053 C  CB  . PHE   A 674 ? 0.2123 0.1762 0.1891 -0.0046 0.0172  -0.0074 699  PHE   A CB  
5054 C  CG  . PHE   A 674 ? 0.2078 0.1753 0.1867 -0.0040 0.0151  -0.0058 699  PHE   A CG  
5055 C  CD1 . PHE   A 674 ? 0.2220 0.1924 0.2038 -0.0021 0.0139  -0.0047 699  PHE   A CD1 
5056 C  CD2 . PHE   A 674 ? 0.2156 0.1830 0.1936 -0.0052 0.0143  -0.0056 699  PHE   A CD2 
5057 C  CE1 . PHE   A 674 ? 0.2257 0.1989 0.2093 -0.0015 0.0122  -0.0034 699  PHE   A CE1 
5058 C  CE2 . PHE   A 674 ? 0.2204 0.1906 0.2002 -0.0044 0.0126  -0.0042 699  PHE   A CE2 
5059 C  CZ  . PHE   A 674 ? 0.2210 0.1941 0.2035 -0.0026 0.0116  -0.0032 699  PHE   A CZ  
5060 N  N   . LYS   A 675 ? 0.2163 0.1782 0.1978 0.0008  0.0190  -0.0065 700  LYS   A N   
5061 C  CA  . LYS   A 675 ? 0.2172 0.1806 0.2021 0.0034  0.0186  -0.0054 700  LYS   A CA  
5062 C  C   . LYS   A 675 ? 0.2306 0.1907 0.2169 0.0055  0.0196  -0.0047 700  LYS   A C   
5063 O  O   . LYS   A 675 ? 0.2279 0.1895 0.2170 0.0074  0.0184  -0.0032 700  LYS   A O   
5064 C  CB  . LYS   A 675 ? 0.2263 0.1909 0.2116 0.0034  0.0196  -0.0060 700  LYS   A CB  
5065 C  CG  . LYS   A 675 ? 0.2105 0.1790 0.1950 0.0016  0.0183  -0.0062 700  LYS   A CG  
5066 C  CD  . LYS   A 675 ? 0.2165 0.1857 0.2007 0.0013  0.0195  -0.0070 700  LYS   A CD  
5067 C  CE  . LYS   A 675 ? 0.2328 0.2066 0.2173 0.0002  0.0179  -0.0067 700  LYS   A CE  
5068 N  NZ  . LYS   A 675 ? 0.2387 0.2131 0.2224 -0.0004 0.0191  -0.0075 700  LYS   A NZ  
5069 N  N   . ALA   A 676 ? 0.2220 0.1776 0.2061 0.0051  0.0218  -0.0057 701  ALA   A N   
5070 C  CA  . ALA   A 676 ? 0.2246 0.1769 0.2099 0.0071  0.0229  -0.0049 701  ALA   A CA  
5071 C  C   . ALA   A 676 ? 0.2379 0.1903 0.2237 0.0075  0.0212  -0.0037 701  ALA   A C   
5072 O  O   . ALA   A 676 ? 0.2391 0.1913 0.2274 0.0097  0.0208  -0.0022 701  ALA   A O   
5073 C  CB  . ALA   A 676 ? 0.2390 0.1860 0.2213 0.0063  0.0257  -0.0064 701  ALA   A CB  
5074 N  N   . PHE   A 677 ? 0.2361 0.1889 0.2196 0.0054  0.0203  -0.0042 702  PHE   A N   
5075 C  CA  . PHE   A 677 ? 0.2310 0.1840 0.2147 0.0055  0.0187  -0.0032 702  PHE   A CA  
5076 C  C   . PHE   A 677 ? 0.2269 0.1840 0.2138 0.0070  0.0165  -0.0016 702  PHE   A C   
5077 O  O   . PHE   A 677 ? 0.2320 0.1886 0.2202 0.0085  0.0157  -0.0003 702  PHE   A O   
5078 C  CB  . PHE   A 677 ? 0.2419 0.1953 0.2229 0.0028  0.0182  -0.0041 702  PHE   A CB  
5079 C  CG  . PHE   A 677 ? 0.2758 0.2315 0.2575 0.0027  0.0162  -0.0030 702  PHE   A CG  
5080 C  CD1 . PHE   A 677 ? 0.3049 0.2584 0.2867 0.0037  0.0159  -0.0020 702  PHE   A CD1 
5081 C  CD2 . PHE   A 677 ? 0.2929 0.2529 0.2752 0.0018  0.0145  -0.0027 702  PHE   A CD2 
5082 C  CE1 . PHE   A 677 ? 0.3177 0.2731 0.3001 0.0037  0.0142  -0.0010 702  PHE   A CE1 
5083 C  CE2 . PHE   A 677 ? 0.3129 0.2746 0.2958 0.0019  0.0129  -0.0017 702  PHE   A CE2 
5084 C  CZ  . PHE   A 677 ? 0.3088 0.2682 0.2916 0.0028  0.0128  -0.0009 702  PHE   A CZ  
5085 N  N   . LEU   A 678 ? 0.2150 0.1758 0.2027 0.0066  0.0156  -0.0017 703  LEU   A N   
5086 C  CA  . LEU   A 678 ? 0.2075 0.1718 0.1978 0.0078  0.0136  -0.0004 703  LEU   A CA  
5087 C  C   . LEU   A 678 ? 0.2178 0.1818 0.2108 0.0102  0.0137  0.0008  703  LEU   A C   
5088 O  O   . LEU   A 678 ? 0.2201 0.1852 0.2147 0.0114  0.0123  0.0022  703  LEU   A O   
5089 C  CB  . LEU   A 678 ? 0.2038 0.1719 0.1944 0.0068  0.0130  -0.0008 703  LEU   A CB  
5090 C  CG  . LEU   A 678 ? 0.2048 0.1764 0.1980 0.0079  0.0111  0.0004  703  LEU   A CG  
5091 C  CD1 . LEU   A 678 ? 0.2300 0.2023 0.2230 0.0077  0.0096  0.0013  703  LEU   A CD1 
5092 C  CD2 . LEU   A 678 ? 0.2202 0.1951 0.2136 0.0070  0.0108  0.0000  703  LEU   A CD2 
5093 N  N   . ILE   A 679 ? 0.2106 0.1733 0.2043 0.0110  0.0155  0.0003  704  ILE   A N   
5094 C  CA  . ILE   A 679 ? 0.2190 0.1818 0.2158 0.0134  0.0156  0.0017  704  ILE   A CA  
5095 C  C   . ILE   A 679 ? 0.2292 0.1889 0.2260 0.0146  0.0159  0.0027  704  ILE   A C   
5096 O  O   . ILE   A 679 ? 0.2305 0.1914 0.2298 0.0162  0.0147  0.0043  704  ILE   A O   
5097 C  CB  . ILE   A 679 ? 0.2364 0.1983 0.2339 0.0141  0.0178  0.0010  704  ILE   A CB  
5098 C  CG1 . ILE   A 679 ? 0.2475 0.2128 0.2451 0.0131  0.0173  0.0003  704  ILE   A CG1 
5099 C  CG2 . ILE   A 679 ? 0.2609 0.2227 0.2618 0.0167  0.0182  0.0025  704  ILE   A CG2 
5100 C  CD1 . ILE   A 679 ? 0.2478 0.2175 0.2480 0.0138  0.0149  0.0016  704  ILE   A CD1 
5101 N  N   . ARG   A 680 ? 0.2351 0.1911 0.2293 0.0136  0.0173  0.0017  705  ARG   A N   
5102 C  CA  . ARG   A 680 ? 0.2537 0.2066 0.2478 0.0146  0.0177  0.0027  705  ARG   A CA  
5103 C  C   . ARG   A 680 ? 0.2602 0.2148 0.2545 0.0146  0.0152  0.0039  705  ARG   A C   
5104 O  O   . ARG   A 680 ? 0.2733 0.2275 0.2693 0.0162  0.0146  0.0056  705  ARG   A O   
5105 C  CB  . ARG   A 680 ? 0.3045 0.2530 0.2951 0.0130  0.0196  0.0012  705  ARG   A CB  
5106 C  CG  . ARG   A 680 ? 0.3890 0.3336 0.3790 0.0139  0.0204  0.0019  705  ARG   A CG  
5107 C  CD  . ARG   A 680 ? 0.4309 0.3707 0.4177 0.0126  0.0230  0.0002  705  ARG   A CD  
5108 N  NE  . ARG   A 680 ? 0.4877 0.4276 0.4713 0.0097  0.0225  -0.0012 705  ARG   A NE  
5109 C  CZ  . ARG   A 680 ? 0.5163 0.4563 0.4977 0.0076  0.0234  -0.0030 705  ARG   A CZ  
5110 N  NH1 . ARG   A 680 ? 0.5204 0.4608 0.4992 0.0051  0.0228  -0.0040 705  ARG   A NH1 
5111 N  NH2 . ARG   A 680 ? 0.5189 0.4583 0.5006 0.0080  0.0251  -0.0038 705  ARG   A NH2 
5112 N  N   . LEU   A 681 ? 0.2424 0.1991 0.2352 0.0128  0.0140  0.0032  706  LEU   A N   
5113 C  CA  . LEU   A 681 ? 0.2455 0.2037 0.2383 0.0125  0.0120  0.0042  706  LEU   A CA  
5114 C  C   . LEU   A 681 ? 0.2447 0.2056 0.2402 0.0141  0.0103  0.0058  706  LEU   A C   
5115 O  O   . LEU   A 681 ? 0.2588 0.2195 0.2546 0.0147  0.0091  0.0071  706  LEU   A O   
5116 C  CB  . LEU   A 681 ? 0.2457 0.2059 0.2368 0.0104  0.0113  0.0031  706  LEU   A CB  
5117 C  CG  . LEU   A 681 ? 0.2555 0.2172 0.2461 0.0099  0.0095  0.0039  706  LEU   A CG  
5118 C  CD1 . LEU   A 681 ? 0.2685 0.2269 0.2572 0.0096  0.0099  0.0041  706  LEU   A CD1 
5119 C  CD2 . LEU   A 681 ? 0.2592 0.2232 0.2486 0.0080  0.0091  0.0029  706  LEU   A CD2 
5120 N  N   . LEU   A 682 ? 0.2184 0.1818 0.2159 0.0146  0.0102  0.0057  707  LEU   A N   
5121 C  CA  . LEU   A 682 ? 0.2059 0.1723 0.2060 0.0159  0.0085  0.0072  707  LEU   A CA  
5122 C  C   . LEU   A 682 ? 0.2101 0.1763 0.2131 0.0179  0.0092  0.0083  707  LEU   A C   
5123 O  O   . LEU   A 682 ? 0.2151 0.1840 0.2205 0.0188  0.0079  0.0095  707  LEU   A O   
5124 C  CB  . LEU   A 682 ? 0.2063 0.1761 0.2070 0.0150  0.0078  0.0066  707  LEU   A CB  
5125 C  CG  . LEU   A 682 ? 0.2414 0.2121 0.2398 0.0132  0.0070  0.0058  707  LEU   A CG  
5126 C  CD1 . LEU   A 682 ? 0.2575 0.2315 0.2566 0.0126  0.0065  0.0053  707  LEU   A CD1 
5127 C  CD2 . LEU   A 682 ? 0.2700 0.2405 0.2677 0.0132  0.0055  0.0068  707  LEU   A CD2 
5128 N  N   . ARG   A 683 ? 0.2152 0.1782 0.2179 0.0186  0.0112  0.0080  708  ARG   A N   
5129 C  CA  . ARG   A 683 ? 0.2245 0.1873 0.2301 0.0206  0.0123  0.0091  708  ARG   A CA  
5130 C  C   . ARG   A 683 ? 0.2231 0.1872 0.2312 0.0221  0.0106  0.0114  708  ARG   A C   
5131 O  O   . ARG   A 683 ? 0.2244 0.1910 0.2356 0.0234  0.0103  0.0125  708  ARG   A O   
5132 C  CB  . ARG   A 683 ? 0.2501 0.2085 0.2545 0.0210  0.0149  0.0084  708  ARG   A CB  
5133 C  CG  . ARG   A 683 ? 0.2875 0.2455 0.2949 0.0231  0.0164  0.0094  708  ARG   A CG  
5134 C  CD  . ARG   A 683 ? 0.3655 0.3187 0.3716 0.0236  0.0193  0.0088  708  ARG   A CD  
5135 N  NE  . ARG   A 683 ? 0.4623 0.4153 0.4715 0.0258  0.0210  0.0097  708  ARG   A NE  
5136 C  CZ  . ARG   A 683 ? 0.5304 0.4793 0.5394 0.0268  0.0238  0.0095  708  ARG   A CZ  
5137 N  NH1 . ARG   A 683 ? 0.5305 0.4795 0.5426 0.0289  0.0255  0.0105  708  ARG   A NH1 
5138 N  NH2 . ARG   A 683 ? 0.5337 0.4782 0.5393 0.0258  0.0251  0.0084  708  ARG   A NH2 
5139 N  N   . ASP   A 684 ? 0.2216 0.1844 0.2283 0.0219  0.0096  0.0122  709  ASP   A N   
5140 C  CA  . ASP   A 684 ? 0.2418 0.2059 0.2507 0.0233  0.0079  0.0145  709  ASP   A CA  
5141 C  C   . ASP   A 684 ? 0.2402 0.2085 0.2506 0.0229  0.0057  0.0152  709  ASP   A C   
5142 O  O   . ASP   A 684 ? 0.2515 0.2220 0.2649 0.0242  0.0047  0.0169  709  ASP   A O   
5143 C  CB  . ASP   A 684 ? 0.2770 0.2387 0.2837 0.0229  0.0073  0.0152  709  ASP   A CB  
5144 C  CG  . ASP   A 684 ? 0.3408 0.2981 0.3464 0.0235  0.0094  0.0150  709  ASP   A CG  
5145 O  OD1 . ASP   A 684 ? 0.3500 0.3063 0.3573 0.0248  0.0114  0.0150  709  ASP   A OD1 
5146 O  OD2 . ASP   A 684 ? 0.3631 0.3180 0.3662 0.0227  0.0093  0.0149  709  ASP   A OD2 
5147 N  N   . LEU   A 685 ? 0.2153 0.1848 0.2237 0.0212  0.0049  0.0138  710  LEU   A N   
5148 C  CA  . LEU   A 685 ? 0.2236 0.1967 0.2331 0.0207  0.0029  0.0142  710  LEU   A CA  
5149 C  C   . LEU   A 685 ? 0.2201 0.1956 0.2323 0.0214  0.0036  0.0141  710  LEU   A C   
5150 O  O   . LEU   A 685 ? 0.2338 0.2121 0.2483 0.0219  0.0022  0.0153  710  LEU   A O   
5151 C  CB  . LEU   A 685 ? 0.2298 0.2031 0.2364 0.0189  0.0023  0.0129  710  LEU   A CB  
5152 C  CG  . LEU   A 685 ? 0.2472 0.2235 0.2542 0.0182  0.0003  0.0133  710  LEU   A CG  
5153 C  CD1 . LEU   A 685 ? 0.2528 0.2295 0.2603 0.0187  -0.0015 0.0151  710  LEU   A CD1 
5154 C  CD2 . LEU   A 685 ? 0.2452 0.2213 0.2495 0.0165  0.0001  0.0120  710  LEU   A CD2 
5155 N  N   . ILE   A 686 ? 0.2097 0.1841 0.2216 0.0214  0.0056  0.0127  711  ILE   A N   
5156 C  CA  . ILE   A 686 ? 0.2158 0.1921 0.2301 0.0221  0.0065  0.0125  711  ILE   A CA  
5157 C  C   . ILE   A 686 ? 0.2187 0.1957 0.2367 0.0241  0.0067  0.0145  711  ILE   A C   
5158 O  O   . ILE   A 686 ? 0.2190 0.1992 0.2398 0.0247  0.0058  0.0155  711  ILE   A O   
5159 C  CB  . ILE   A 686 ? 0.2115 0.1858 0.2243 0.0215  0.0089  0.0106  711  ILE   A CB  
5160 C  CG1 . ILE   A 686 ? 0.2172 0.1921 0.2272 0.0195  0.0085  0.0090  711  ILE   A CG1 
5161 C  CG2 . ILE   A 686 ? 0.2334 0.2089 0.2488 0.0226  0.0104  0.0106  711  ILE   A CG2 
5162 C  CD1 . ILE   A 686 ? 0.2323 0.2046 0.2399 0.0185  0.0106  0.0071  711  ILE   A CD1 
5163 N  N   . ASP   A 687 ? 0.2340 0.2081 0.2520 0.0252  0.0078  0.0152  712  ASP   A N   
5164 C  CA  . ASP   A 687 ? 0.2320 0.2065 0.2535 0.0274  0.0082  0.0173  712  ASP   A CA  
5165 C  C   . ASP   A 687 ? 0.2544 0.2322 0.2781 0.0277  0.0055  0.0195  712  ASP   A C   
5166 O  O   . ASP   A 687 ? 0.2799 0.2598 0.3073 0.0293  0.0054  0.0213  712  ASP   A O   
5167 C  CB  . ASP   A 687 ? 0.2501 0.2205 0.2706 0.0283  0.0099  0.0176  712  ASP   A CB  
5168 C  CG  . ASP   A 687 ? 0.2705 0.2375 0.2897 0.0284  0.0130  0.0158  712  ASP   A CG  
5169 O  OD1 . ASP   A 687 ? 0.2878 0.2560 0.3075 0.0281  0.0140  0.0146  712  ASP   A OD1 
5170 O  OD2 . ASP   A 687 ? 0.3112 0.2743 0.3287 0.0287  0.0145  0.0156  712  ASP   A OD2 
5171 N  N   . LYS   A 688 ? 0.2358 0.2138 0.2570 0.0263  0.0035  0.0195  713  LYS   A N   
5172 C  CA  . LYS   A 688 ? 0.2523 0.2330 0.2749 0.0263  0.0008  0.0214  713  LYS   A CA  
5173 C  C   . LYS   A 688 ? 0.2587 0.2434 0.2830 0.0257  -0.0005 0.0214  713  LYS   A C   
5174 O  O   . LYS   A 688 ? 0.2695 0.2568 0.2956 0.0258  -0.0025 0.0232  713  LYS   A O   
5175 C  CB  . LYS   A 688 ? 0.2973 0.2764 0.3163 0.0249  -0.0007 0.0212  713  LYS   A CB  
5176 C  CG  . LYS   A 688 ? 0.3639 0.3402 0.3822 0.0258  -0.0003 0.0224  713  LYS   A CG  
5177 C  CD  . LYS   A 688 ? 0.4106 0.3850 0.4251 0.0244  -0.0014 0.0219  713  LYS   A CD  
5178 C  CE  . LYS   A 688 ? 0.4679 0.4389 0.4815 0.0252  -0.0005 0.0227  713  LYS   A CE  
5179 N  NZ  . LYS   A 688 ? 0.5111 0.4799 0.5207 0.0237  -0.0012 0.0220  713  LYS   A NZ  
5180 N  N   . GLN   A 689 ? 0.2272 0.2124 0.2511 0.0250  0.0007  0.0195  714  GLN   A N   
5181 C  CA  . GLN   A 689 ? 0.2190 0.2077 0.2443 0.0243  -0.0005 0.0196  714  GLN   A CA  
5182 C  C   . GLN   A 689 ? 0.2301 0.2216 0.2598 0.0258  -0.0005 0.0212  714  GLN   A C   
5183 O  O   . GLN   A 689 ? 0.2548 0.2455 0.2865 0.0273  0.0015  0.0214  714  GLN   A O   
5184 C  CB  . GLN   A 689 ? 0.2072 0.1958 0.2308 0.0232  0.0006  0.0173  714  GLN   A CB  
5185 C  CG  . GLN   A 689 ? 0.2115 0.1978 0.2310 0.0217  0.0005  0.0157  714  GLN   A CG  
5186 C  CD  . GLN   A 689 ? 0.2330 0.2198 0.2510 0.0207  -0.0017 0.0164  714  GLN   A CD  
5187 O  OE1 . GLN   A 689 ? 0.2307 0.2201 0.2496 0.0201  -0.0032 0.0169  714  GLN   A OE1 
5188 N  NE2 . GLN   A 689 ? 0.2184 0.2027 0.2340 0.0204  -0.0020 0.0164  714  GLN   A NE2 
5189 N  N   . THR   A 690 ? 0.2218 0.2166 0.2531 0.0253  -0.0026 0.0224  715  THR   A N   
5190 C  CA  . THR   A 690 ? 0.2249 0.2231 0.2606 0.0264  -0.0028 0.0240  715  THR   A CA  
5191 C  C   . THR   A 690 ? 0.2213 0.2210 0.2575 0.0258  -0.0019 0.0226  715  THR   A C   
5192 O  O   . THR   A 690 ? 0.2116 0.2107 0.2449 0.0242  -0.0022 0.0209  715  THR   A O   
5193 C  CB  . THR   A 690 ? 0.2495 0.2506 0.2867 0.0259  -0.0056 0.0262  715  THR   A CB  
5194 O  OG1 . THR   A 690 ? 0.2443 0.2461 0.2789 0.0238  -0.0072 0.0251  715  THR   A OG1 
5195 C  CG2 . THR   A 690 ? 0.2639 0.2636 0.3006 0.0265  -0.0065 0.0278  715  THR   A CG2 
5196 N  N   . TRP   A 691 ? 0.2123 0.2141 0.2523 0.0270  -0.0009 0.0234  716  TRP   A N   
5197 C  CA  . TRP   A 691 ? 0.2097 0.2131 0.2504 0.0266  0.0000  0.0222  716  TRP   A CA  
5198 C  C   . TRP   A 691 ? 0.2253 0.2328 0.2684 0.0259  -0.0021 0.0236  716  TRP   A C   
5199 O  O   . TRP   A 691 ? 0.2387 0.2490 0.2857 0.0269  -0.0019 0.0249  716  TRP   A O   
5200 C  CB  . TRP   A 691 ? 0.2110 0.2140 0.2542 0.0284  0.0028  0.0222  716  TRP   A CB  
5201 C  CG  . TRP   A 691 ? 0.2194 0.2182 0.2595 0.0284  0.0050  0.0203  716  TRP   A CG  
5202 C  CD1 . TRP   A 691 ? 0.2439 0.2394 0.2816 0.0285  0.0051  0.0202  716  TRP   A CD1 
5203 C  CD2 . TRP   A 691 ? 0.2196 0.2168 0.2579 0.0280  0.0072  0.0182  716  TRP   A CD2 
5204 N  NE1 . TRP   A 691 ? 0.2534 0.2455 0.2882 0.0282  0.0073  0.0181  716  TRP   A NE1 
5205 C  CE2 . TRP   A 691 ? 0.2312 0.2244 0.2664 0.0279  0.0086  0.0169  716  TRP   A CE2 
5206 C  CE3 . TRP   A 691 ? 0.2332 0.2322 0.2724 0.0277  0.0082  0.0173  716  TRP   A CE3 
5207 C  CZ2 . TRP   A 691 ? 0.2382 0.2291 0.2708 0.0272  0.0108  0.0148  716  TRP   A CZ2 
5208 C  CZ3 . TRP   A 691 ? 0.2339 0.2306 0.2705 0.0271  0.0103  0.0152  716  TRP   A CZ3 
5209 C  CH2 . TRP   A 691 ? 0.2371 0.2299 0.2705 0.0269  0.0115  0.0140  716  TRP   A CH2 
5210 N  N   . THR   A 692 ? 0.2069 0.2144 0.2473 0.0242  -0.0042 0.0232  717  THR   A N   
5211 C  CA  . THR   A 692 ? 0.2131 0.2237 0.2546 0.0230  -0.0065 0.0243  717  THR   A CA  
5212 C  C   . THR   A 692 ? 0.2188 0.2285 0.2566 0.0210  -0.0074 0.0227  717  THR   A C   
5213 O  O   . THR   A 692 ? 0.2157 0.2228 0.2503 0.0206  -0.0064 0.0209  717  THR   A O   
5214 C  CB  . THR   A 692 ? 0.2308 0.2420 0.2729 0.0231  -0.0086 0.0265  717  THR   A CB  
5215 O  OG1 . THR   A 692 ? 0.2463 0.2545 0.2840 0.0220  -0.0094 0.0256  717  THR   A OG1 
5216 C  CG2 . THR   A 692 ? 0.2370 0.2488 0.2826 0.0252  -0.0078 0.0284  717  THR   A CG2 
5217 N  N   . ASP   A 693 ? 0.2302 0.2423 0.2683 0.0197  -0.0094 0.0234  718  ASP   A N   
5218 C  CA  . ASP   A 693 ? 0.2180 0.2291 0.2527 0.0178  -0.0104 0.0222  718  ASP   A CA  
5219 C  C   . ASP   A 693 ? 0.2380 0.2482 0.2704 0.0167  -0.0125 0.0230  718  ASP   A C   
5220 O  O   . ASP   A 693 ? 0.2551 0.2653 0.2854 0.0150  -0.0137 0.0225  718  ASP   A O   
5221 C  CB  . ASP   A 693 ? 0.2210 0.2346 0.2570 0.0169  -0.0107 0.0220  718  ASP   A CB  
5222 C  CG  . ASP   A 693 ? 0.2666 0.2806 0.3038 0.0176  -0.0086 0.0208  718  ASP   A CG  
5223 O  OD1 . ASP   A 693 ? 0.2553 0.2669 0.2909 0.0183  -0.0069 0.0196  718  ASP   A OD1 
5224 O  OD2 . ASP   A 693 ? 0.2813 0.2978 0.3208 0.0174  -0.0085 0.0211  718  ASP   A OD2 
5225 N  N   . GLU   A 694 ? 0.2475 0.2569 0.2802 0.0176  -0.0129 0.0242  719  GLU   A N   
5226 C  CA  . GLU   A 694 ? 0.2636 0.2722 0.2942 0.0166  -0.0149 0.0251  719  GLU   A CA  
5227 C  C   . GLU   A 694 ? 0.2841 0.2892 0.3099 0.0156  -0.0148 0.0235  719  GLU   A C   
5228 O  O   . GLU   A 694 ? 0.2721 0.2751 0.2965 0.0160  -0.0130 0.0220  719  GLU   A O   
5229 C  CB  . GLU   A 694 ? 0.2799 0.2887 0.3125 0.0181  -0.0151 0.0270  719  GLU   A CB  
5230 C  CG  . GLU   A 694 ? 0.2995 0.3121 0.3371 0.0191  -0.0156 0.0291  719  GLU   A CG  
5231 C  CD  . GLU   A 694 ? 0.3667 0.3796 0.4069 0.0210  -0.0154 0.0311  719  GLU   A CD  
5232 O  OE1 . GLU   A 694 ? 0.3643 0.3742 0.4022 0.0214  -0.0150 0.0309  719  GLU   A OE1 
5233 O  OE2 . GLU   A 694 ? 0.4372 0.4533 0.4819 0.0221  -0.0154 0.0329  719  GLU   A OE2 
5234 N  N   . GLY   A 695 ? 0.2982 0.3027 0.3215 0.0141  -0.0166 0.0240  720  GLY   A N   
5235 C  CA  . GLY   A 695 ? 0.3117 0.3130 0.3307 0.0132  -0.0165 0.0228  720  GLY   A CA  
5236 C  C   . GLY   A 695 ? 0.2953 0.2956 0.3115 0.0116  -0.0165 0.0213  720  GLY   A C   
5237 O  O   . GLY   A 695 ? 0.2959 0.2980 0.3133 0.0110  -0.0166 0.0210  720  GLY   A O   
5238 N  N   . SER   A 696 ? 0.3096 0.3069 0.3220 0.0110  -0.0161 0.0203  721  SER   A N   
5239 C  CA  . SER   A 696 ? 0.3129 0.3087 0.3223 0.0097  -0.0157 0.0189  721  SER   A CA  
5240 C  C   . SER   A 696 ? 0.3068 0.3028 0.3171 0.0103  -0.0138 0.0174  721  SER   A C   
5241 O  O   . SER   A 696 ? 0.3090 0.3056 0.3215 0.0117  -0.0127 0.0174  721  SER   A O   
5242 C  CB  . SER   A 696 ? 0.3452 0.3378 0.3507 0.0090  -0.0157 0.0184  721  SER   A CB  
5243 O  OG  . SER   A 696 ? 0.3685 0.3598 0.3742 0.0103  -0.0143 0.0179  721  SER   A OG  
5244 N  N   . VAL   A 697 ? 0.2853 0.2806 0.2938 0.0093  -0.0133 0.0163  722  VAL   A N   
5245 C  CA  . VAL   A 697 ? 0.2813 0.2769 0.2904 0.0098  -0.0116 0.0152  722  VAL   A CA  
5246 C  C   . VAL   A 697 ? 0.2725 0.2666 0.2809 0.0107  -0.0103 0.0145  722  VAL   A C   
5247 O  O   . VAL   A 697 ? 0.2557 0.2507 0.2658 0.0116  -0.0090 0.0139  722  VAL   A O   
5248 C  CB  . VAL   A 697 ? 0.3201 0.3151 0.3273 0.0086  -0.0114 0.0143  722  VAL   A CB  
5249 C  CG1 . VAL   A 697 ? 0.3242 0.3194 0.3317 0.0091  -0.0097 0.0133  722  VAL   A CG1 
5250 C  CG2 . VAL   A 697 ? 0.3415 0.3383 0.3500 0.0078  -0.0125 0.0149  722  VAL   A CG2 
5251 N  N   A SER   A 698 ? 0.2582 0.2499 0.2641 0.0105  -0.0105 0.0145  723  SER   A N   
5252 N  N   B SER   A 698 ? 0.2655 0.2573 0.2714 0.0105  -0.0105 0.0145  723  SER   A N   
5253 C  CA  A SER   A 698 ? 0.2411 0.2313 0.2462 0.0111  -0.0093 0.0139  723  SER   A CA  
5254 C  CA  B SER   A 698 ? 0.2555 0.2457 0.2607 0.0112  -0.0092 0.0139  723  SER   A CA  
5255 C  C   A SER   A 698 ? 0.2288 0.2196 0.2363 0.0124  -0.0090 0.0145  723  SER   A C   
5256 C  C   B SER   A 698 ? 0.2360 0.2268 0.2436 0.0124  -0.0090 0.0145  723  SER   A C   
5257 O  O   A SER   A 698 ? 0.2278 0.2184 0.2360 0.0131  -0.0076 0.0137  723  SER   A O   
5258 O  O   B SER   A 698 ? 0.2347 0.2253 0.2429 0.0131  -0.0075 0.0137  723  SER   A O   
5259 C  CB  A SER   A 698 ? 0.2301 0.2176 0.2320 0.0105  -0.0096 0.0139  723  SER   A CB  
5260 C  CB  B SER   A 698 ? 0.2681 0.2557 0.2701 0.0106  -0.0095 0.0138  723  SER   A CB  
5261 O  OG  A SER   A 698 ? 0.2355 0.2228 0.2372 0.0103  -0.0112 0.0151  723  SER   A OG  
5262 O  OG  B SER   A 698 ? 0.3129 0.2996 0.3127 0.0096  -0.0091 0.0131  723  SER   A OG  
5263 N  N   . GLU   A 699 ? 0.2321 0.2237 0.2410 0.0128  -0.0102 0.0158  724  GLU   A N   
5264 C  CA  . GLU   A 699 ? 0.2276 0.2198 0.2391 0.0142  -0.0098 0.0166  724  GLU   A CA  
5265 C  C   . GLU   A 699 ? 0.2150 0.2092 0.2293 0.0149  -0.0087 0.0162  724  GLU   A C   
5266 O  O   . GLU   A 699 ? 0.2000 0.1937 0.2155 0.0159  -0.0073 0.0159  724  GLU   A O   
5267 C  CB  . GLU   A 699 ? 0.2585 0.2517 0.2713 0.0144  -0.0115 0.0185  724  GLU   A CB  
5268 C  CG  . GLU   A 699 ? 0.3185 0.3093 0.3285 0.0139  -0.0123 0.0190  724  GLU   A CG  
5269 C  CD  . GLU   A 699 ? 0.4138 0.4056 0.4242 0.0136  -0.0144 0.0209  724  GLU   A CD  
5270 O  OE1 . GLU   A 699 ? 0.3705 0.3646 0.3822 0.0130  -0.0156 0.0215  724  GLU   A OE1 
5271 O  OE2 . GLU   A 699 ? 0.4786 0.4688 0.4879 0.0139  -0.0148 0.0217  724  GLU   A OE2 
5272 N  N   . ARG   A 700 ? 0.2057 0.2020 0.2210 0.0142  -0.0093 0.0162  725  ARG   A N   
5273 C  CA  . ARG   A 700 ? 0.1886 0.1869 0.2065 0.0148  -0.0082 0.0158  725  ARG   A CA  
5274 C  C   . ARG   A 700 ? 0.1951 0.1924 0.2118 0.0148  -0.0064 0.0142  725  ARG   A C   
5275 O  O   . ARG   A 700 ? 0.1812 0.1789 0.1993 0.0157  -0.0051 0.0139  725  ARG   A O   
5276 C  CB  . ARG   A 700 ? 0.2042 0.2047 0.2230 0.0140  -0.0092 0.0161  725  ARG   A CB  
5277 C  CG  . ARG   A 700 ? 0.2116 0.2136 0.2320 0.0138  -0.0110 0.0179  725  ARG   A CG  
5278 C  CD  . ARG   A 700 ? 0.2319 0.2364 0.2538 0.0130  -0.0119 0.0183  725  ARG   A CD  
5279 N  NE  . ARG   A 700 ? 0.2465 0.2528 0.2711 0.0137  -0.0106 0.0179  725  ARG   A NE  
5280 C  CZ  . ARG   A 700 ? 0.2957 0.3040 0.3215 0.0131  -0.0108 0.0179  725  ARG   A CZ  
5281 N  NH1 . ARG   A 700 ? 0.3113 0.3198 0.3358 0.0116  -0.0122 0.0181  725  ARG   A NH1 
5282 N  NH2 . ARG   A 700 ? 0.2875 0.2972 0.3155 0.0139  -0.0094 0.0175  725  ARG   A NH2 
5283 N  N   . MET   A 701 ? 0.1956 0.1916 0.2094 0.0138  -0.0064 0.0133  726  MET   A N   
5284 C  CA  . MET   A 701 ? 0.1890 0.1845 0.2018 0.0136  -0.0049 0.0120  726  MET   A CA  
5285 C  C   . MET   A 701 ? 0.1775 0.1711 0.1896 0.0142  -0.0039 0.0116  726  MET   A C   
5286 O  O   . MET   A 701 ? 0.1807 0.1744 0.1931 0.0144  -0.0024 0.0108  726  MET   A O   
5287 C  CB  . MET   A 701 ? 0.2002 0.1948 0.2104 0.0125  -0.0051 0.0115  726  MET   A CB  
5288 C  CG  . MET   A 701 ? 0.1980 0.1943 0.2088 0.0120  -0.0057 0.0117  726  MET   A CG  
5289 S  SD  . MET   A 701 ? 0.2509 0.2463 0.2591 0.0109  -0.0054 0.0110  726  MET   A SD  
5290 C  CE  . MET   A 701 ? 0.2657 0.2585 0.2713 0.0104  -0.0063 0.0113  726  MET   A CE  
5291 N  N   . LEU   A 702 ? 0.1869 0.1787 0.1979 0.0144  -0.0044 0.0122  727  LEU   A N   
5292 C  CA  . LEU   A 702 ? 0.1824 0.1721 0.1927 0.0149  -0.0034 0.0119  727  LEU   A CA  
5293 C  C   . LEU   A 702 ? 0.1831 0.1734 0.1960 0.0162  -0.0024 0.0122  727  LEU   A C   
5294 O  O   . LEU   A 702 ? 0.1844 0.1737 0.1970 0.0164  -0.0008 0.0112  727  LEU   A O   
5295 C  CB  . LEU   A 702 ? 0.2004 0.1883 0.2093 0.0149  -0.0043 0.0127  727  LEU   A CB  
5296 C  CG  . LEU   A 702 ? 0.1979 0.1833 0.2059 0.0154  -0.0033 0.0125  727  LEU   A CG  
5297 C  CD1 . LEU   A 702 ? 0.2047 0.1889 0.2106 0.0146  -0.0020 0.0110  727  LEU   A CD1 
5298 C  CD2 . LEU   A 702 ? 0.2244 0.2081 0.2308 0.0153  -0.0044 0.0134  727  LEU   A CD2 
5299 N  N   . ARG   A 703 ? 0.1748 0.1668 0.1903 0.0169  -0.0033 0.0135  728  ARG   A N   
5300 C  CA  . ARG   A 703 ? 0.1772 0.1699 0.1955 0.0182  -0.0022 0.0139  728  ARG   A CA  
5301 C  C   . ARG   A 703 ? 0.1790 0.1725 0.1978 0.0182  -0.0007 0.0127  728  ARG   A C   
5302 O  O   . ARG   A 703 ? 0.1725 0.1648 0.1916 0.0188  0.0011  0.0121  728  ARG   A O   
5303 C  CB  . ARG   A 703 ? 0.1857 0.1810 0.2070 0.0188  -0.0036 0.0156  728  ARG   A CB  
5304 C  CG  . ARG   A 703 ? 0.1823 0.1790 0.2071 0.0202  -0.0025 0.0163  728  ARG   A CG  
5305 C  CD  . ARG   A 703 ? 0.2163 0.2162 0.2442 0.0205  -0.0040 0.0180  728  ARG   A CD  
5306 N  NE  . ARG   A 703 ? 0.1985 0.1983 0.2266 0.0207  -0.0057 0.0197  728  ARG   A NE  
5307 C  CZ  . ARG   A 703 ? 0.2300 0.2307 0.2572 0.0195  -0.0078 0.0204  728  ARG   A CZ  
5308 N  NH1 . ARG   A 703 ? 0.2154 0.2174 0.2418 0.0182  -0.0085 0.0197  728  ARG   A NH1 
5309 N  NH2 . ARG   A 703 ? 0.2379 0.2382 0.2648 0.0196  -0.0092 0.0218  728  ARG   A NH2 
5310 N  N   . SER   A 704 ? 0.1703 0.1659 0.1893 0.0173  -0.0013 0.0124  729  SER   A N   
5311 C  CA  . SER   A 704 ? 0.1737 0.1704 0.1934 0.0173  0.0001  0.0115  729  SER   A CA  
5312 C  C   . SER   A 704 ? 0.1753 0.1702 0.1925 0.0167  0.0015  0.0100  729  SER   A C   
5313 O  O   . SER   A 704 ? 0.1765 0.1710 0.1940 0.0170  0.0032  0.0093  729  SER   A O   
5314 C  CB  . SER   A 704 ? 0.1779 0.1768 0.1978 0.0164  -0.0009 0.0115  729  SER   A CB  
5315 O  OG  . SER   A 704 ? 0.1938 0.1940 0.2142 0.0163  0.0003  0.0107  729  SER   A OG  
5316 N  N   . GLN   A 705 ? 0.1616 0.1551 0.1762 0.0158  0.0010  0.0095  730  GLN   A N   
5317 C  CA  . GLN   A 705 ? 0.1651 0.1572 0.1773 0.0150  0.0022  0.0082  730  GLN   A CA  
5318 C  C   . GLN   A 705 ? 0.1780 0.1675 0.1897 0.0156  0.0035  0.0079  730  GLN   A C   
5319 O  O   . GLN   A 705 ? 0.1842 0.1729 0.1950 0.0152  0.0050  0.0068  730  GLN   A O   
5320 C  CB  . GLN   A 705 ? 0.1786 0.1700 0.1885 0.0139  0.0013  0.0081  730  GLN   A CB  
5321 C  CG  . GLN   A 705 ? 0.2113 0.2016 0.2189 0.0129  0.0023  0.0069  730  GLN   A CG  
5322 C  CD  . GLN   A 705 ? 0.2942 0.2864 0.3019 0.0123  0.0029  0.0062  730  GLN   A CD  
5323 O  OE1 . GLN   A 705 ? 0.3480 0.3420 0.3558 0.0119  0.0022  0.0064  730  GLN   A OE1 
5324 N  NE2 . GLN   A 705 ? 0.2969 0.2887 0.3045 0.0123  0.0043  0.0054  730  GLN   A NE2 
5325 N  N   . LEU   A 706 ? 0.1666 0.1548 0.1789 0.0164  0.0030  0.0089  731  LEU   A N   
5326 C  CA  . LEU   A 706 ? 0.1733 0.1588 0.1852 0.0171  0.0044  0.0087  731  LEU   A CA  
5327 C  C   . LEU   A 706 ? 0.1729 0.1586 0.1868 0.0182  0.0059  0.0086  731  LEU   A C   
5328 O  O   . LEU   A 706 ? 0.1874 0.1708 0.2002 0.0181  0.0078  0.0076  731  LEU   A O   
5329 C  CB  . LEU   A 706 ? 0.1866 0.1709 0.1988 0.0179  0.0034  0.0100  731  LEU   A CB  
5330 C  CG  . LEU   A 706 ? 0.2124 0.1955 0.2221 0.0169  0.0023  0.0099  731  LEU   A CG  
5331 C  CD1 . LEU   A 706 ? 0.2134 0.1957 0.2237 0.0176  0.0012  0.0114  731  LEU   A CD1 
5332 C  CD2 . LEU   A 706 ? 0.2294 0.2101 0.2363 0.0159  0.0036  0.0085  731  LEU   A CD2 
5333 N  N   . LEU   A 707 ? 0.1699 0.1580 0.1868 0.0191  0.0054  0.0097  732  LEU   A N   
5334 C  CA  . LEU   A 707 ? 0.1688 0.1572 0.1880 0.0202  0.0071  0.0097  732  LEU   A CA  
5335 C  C   . LEU   A 707 ? 0.1762 0.1647 0.1940 0.0193  0.0085  0.0081  732  LEU   A C   
5336 O  O   . LEU   A 707 ? 0.1897 0.1766 0.2073 0.0197  0.0106  0.0073  732  LEU   A O   
5337 C  CB  . LEU   A 707 ? 0.1838 0.1752 0.2067 0.0213  0.0061  0.0113  732  LEU   A CB  
5338 C  CG  . LEU   A 707 ? 0.2057 0.1973 0.2303 0.0223  0.0047  0.0132  732  LEU   A CG  
5339 C  CD1 . LEU   A 707 ? 0.2198 0.2148 0.2480 0.0230  0.0036  0.0148  732  LEU   A CD1 
5340 C  CD2 . LEU   A 707 ? 0.2218 0.2103 0.2463 0.0235  0.0061  0.0135  732  LEU   A CD2 
5341 N  N   . LEU   A 708 ? 0.1765 0.1669 0.1933 0.0180  0.0075  0.0076  733  LEU   A N   
5342 C  CA  . LEU   A 708 ? 0.1764 0.1672 0.1918 0.0170  0.0087  0.0062  733  LEU   A CA  
5343 C  C   . LEU   A 708 ? 0.1915 0.1794 0.2037 0.0160  0.0099  0.0049  733  LEU   A C   
5344 O  O   . LEU   A 708 ? 0.2044 0.1912 0.2157 0.0158  0.0118  0.0038  733  LEU   A O   
5345 C  CB  . LEU   A 708 ? 0.1757 0.1690 0.1905 0.0159  0.0072  0.0062  733  LEU   A CB  
5346 C  CG  . LEU   A 708 ? 0.1872 0.1812 0.2004 0.0147  0.0082  0.0050  733  LEU   A CG  
5347 C  CD1 . LEU   A 708 ? 0.2015 0.1963 0.2164 0.0154  0.0097  0.0047  733  LEU   A CD1 
5348 C  CD2 . LEU   A 708 ? 0.1928 0.1891 0.2057 0.0138  0.0067  0.0052  733  LEU   A CD2 
5349 N  N   . LEU   A 709 ? 0.1759 0.1624 0.1863 0.0154  0.0090  0.0049  734  LEU   A N   
5350 C  CA  . LEU   A 709 ? 0.1799 0.1638 0.1873 0.0143  0.0101  0.0037  734  LEU   A CA  
5351 C  C   . LEU   A 709 ? 0.1929 0.1737 0.2003 0.0152  0.0121  0.0033  734  LEU   A C   
5352 O  O   . LEU   A 709 ? 0.2006 0.1798 0.2060 0.0143  0.0138  0.0020  734  LEU   A O   
5353 C  CB  . LEU   A 709 ? 0.1806 0.1635 0.1865 0.0138  0.0088  0.0041  734  LEU   A CB  
5354 C  CG  . LEU   A 709 ? 0.1937 0.1738 0.1967 0.0127  0.0098  0.0030  734  LEU   A CG  
5355 C  CD1 . LEU   A 709 ? 0.2098 0.1913 0.2108 0.0108  0.0099  0.0019  734  LEU   A CD1 
5356 C  CD2 . LEU   A 709 ? 0.2205 0.1992 0.2227 0.0127  0.0087  0.0036  734  LEU   A CD2 
5357 N  N   . ALA   A 710 ? 0.1863 0.1665 0.1959 0.0169  0.0120  0.0046  735  ALA   A N   
5358 C  CA  . ALA   A 710 ? 0.2058 0.1829 0.2157 0.0181  0.0141  0.0045  735  ALA   A CA  
5359 C  C   . ALA   A 710 ? 0.2164 0.1937 0.2271 0.0184  0.0161  0.0038  735  ALA   A C   
5360 O  O   . ALA   A 710 ? 0.2345 0.2087 0.2433 0.0181  0.0183  0.0026  735  ALA   A O   
5361 C  CB  . ALA   A 710 ? 0.2119 0.1890 0.2245 0.0199  0.0134  0.0063  735  ALA   A CB  
5362 N  N   . CYS   A 711 ? 0.2121 0.1927 0.2252 0.0189  0.0154  0.0044  736  CYS   A N   
5363 C  CA  . CYS   A 711 ? 0.2196 0.2004 0.2335 0.0193  0.0174  0.0038  736  CYS   A CA  
5364 C  C   . CYS   A 711 ? 0.2394 0.2195 0.2499 0.0173  0.0183  0.0019  736  CYS   A C   
5365 O  O   . CYS   A 711 ? 0.2502 0.2282 0.2596 0.0173  0.0207  0.0008  736  CYS   A O   
5366 C  CB  . CYS   A 711 ? 0.2038 0.1885 0.2211 0.0201  0.0163  0.0049  736  CYS   A CB  
5367 S  SG  . CYS   A 711 ? 0.2427 0.2283 0.2646 0.0226  0.0160  0.0072  736  CYS   A SG  
5368 N  N   . VAL   A 712 ? 0.2344 0.2162 0.2431 0.0157  0.0166  0.0015  737  VAL   A N   
5369 C  CA  . VAL   A 712 ? 0.2436 0.2251 0.2491 0.0136  0.0173  -0.0001 737  VAL   A CA  
5370 C  C   . VAL   A 712 ? 0.2526 0.2301 0.2550 0.0127  0.0190  -0.0014 737  VAL   A C   
5371 O  O   . VAL   A 712 ? 0.2772 0.2533 0.2770 0.0114  0.0206  -0.0028 737  VAL   A O   
5372 C  CB  . VAL   A 712 ? 0.2676 0.2518 0.2723 0.0123  0.0151  0.0001  737  VAL   A CB  
5373 C  CG1 . VAL   A 712 ? 0.2988 0.2824 0.2999 0.0100  0.0154  -0.0012 737  VAL   A CG1 
5374 C  CG2 . VAL   A 712 ? 0.2658 0.2537 0.2729 0.0128  0.0141  0.0009  737  VAL   A CG2 
5375 N  N   . HIS   A 713 ? 0.2512 0.2264 0.2534 0.0133  0.0188  -0.0009 738  HIS   A N   
5376 C  CA  . HIS   A 713 ? 0.2672 0.2383 0.2664 0.0124  0.0204  -0.0021 738  HIS   A CA  
5377 C  C   . HIS   A 713 ? 0.2870 0.2545 0.2869 0.0140  0.0229  -0.0022 738  HIS   A C   
5378 O  O   . HIS   A 713 ? 0.3010 0.2647 0.2989 0.0137  0.0242  -0.0028 738  HIS   A O   
5379 C  CB  . HIS   A 713 ? 0.2814 0.2517 0.2793 0.0117  0.0189  -0.0018 738  HIS   A CB  
5380 C  CG  . HIS   A 713 ? 0.3022 0.2754 0.2988 0.0098  0.0172  -0.0021 738  HIS   A CG  
5381 N  ND1 . HIS   A 713 ? 0.3532 0.3268 0.3472 0.0078  0.0178  -0.0034 738  HIS   A ND1 
5382 C  CD2 . HIS   A 713 ? 0.2747 0.2506 0.2724 0.0098  0.0150  -0.0011 738  HIS   A CD2 
5383 C  CE1 . HIS   A 713 ? 0.3420 0.3187 0.3359 0.0068  0.0159  -0.0031 738  HIS   A CE1 
5384 N  NE2 . HIS   A 713 ? 0.2843 0.2622 0.2802 0.0079  0.0143  -0.0017 738  HIS   A NE2 
5385 N  N   A ASN   A 714 ? 0.2808 0.2497 0.2837 0.0157  0.0237  -0.0014 739  ASN   A N   
5386 N  N   B ASN   A 714 ? 0.2822 0.2510 0.2850 0.0156  0.0237  -0.0015 739  ASN   A N   
5387 C  CA  A ASN   A 714 ? 0.2920 0.2584 0.2963 0.0175  0.0262  -0.0013 739  ASN   A CA  
5388 C  CA  B ASN   A 714 ? 0.2919 0.2575 0.2956 0.0173  0.0265  -0.0015 739  ASN   A CA  
5389 C  C   A ASN   A 714 ? 0.3047 0.2687 0.3106 0.0192  0.0266  0.0000  739  ASN   A C   
5390 C  C   B ASN   A 714 ? 0.3100 0.2733 0.3151 0.0189  0.0265  -0.0002 739  ASN   A C   
5391 O  O   A ASN   A 714 ? 0.3036 0.2641 0.3094 0.0203  0.0291  -0.0003 739  ASN   A O   
5392 O  O   B ASN   A 714 ? 0.3143 0.2733 0.3183 0.0195  0.0290  -0.0007 739  ASN   A O   
5393 C  CB  A ASN   A 714 ? 0.3246 0.2875 0.3253 0.0161  0.0290  -0.0033 739  ASN   A CB  
5394 C  CB  B ASN   A 714 ? 0.3173 0.2792 0.3170 0.0156  0.0291  -0.0036 739  ASN   A CB  
5395 C  CG  A ASN   A 714 ? 0.3558 0.3212 0.3548 0.0141  0.0286  -0.0045 739  ASN   A CG  
5396 C  CG  B ASN   A 714 ? 0.3504 0.3096 0.3511 0.0173  0.0322  -0.0038 739  ASN   A CG  
5397 O  OD1 A ASN   A 714 ? 0.3946 0.3597 0.3900 0.0118  0.0280  -0.0057 739  ASN   A OD1 
5398 O  OD1 B ASN   A 714 ? 0.3634 0.3249 0.3678 0.0191  0.0323  -0.0026 739  ASN   A OD1 
5399 N  ND2 A ASN   A 714 ? 0.3448 0.3130 0.3463 0.0151  0.0287  -0.0039 739  ASN   A ND2 
5400 N  ND2 B ASN   A 714 ? 0.3689 0.3231 0.3666 0.0166  0.0348  -0.0052 739  ASN   A ND2 
5401 N  N   . TYR   A 715 ? 0.3002 0.2662 0.3076 0.0197  0.0240  0.0014  740  TYR   A N   
5402 C  CA  . TYR   A 715 ? 0.2901 0.2544 0.2993 0.0214  0.0238  0.0029  740  TYR   A CA  
5403 C  C   . TYR   A 715 ? 0.3126 0.2779 0.3259 0.0239  0.0249  0.0044  740  TYR   A C   
5404 O  O   . TYR   A 715 ? 0.3098 0.2791 0.3261 0.0246  0.0234  0.0056  740  TYR   A O   
5405 C  CB  . TYR   A 715 ? 0.2767 0.2434 0.2865 0.0212  0.0208  0.0042  740  TYR   A CB  
5406 C  CG  . TYR   A 715 ? 0.2717 0.2369 0.2831 0.0228  0.0204  0.0059  740  TYR   A CG  
5407 C  CD1 . TYR   A 715 ? 0.2847 0.2454 0.2940 0.0229  0.0221  0.0054  740  TYR   A CD1 
5408 C  CD2 . TYR   A 715 ? 0.2617 0.2300 0.2764 0.0242  0.0184  0.0080  740  TYR   A CD2 
5409 C  CE1 . TYR   A 715 ? 0.2981 0.2574 0.3088 0.0244  0.0218  0.0071  740  TYR   A CE1 
5410 C  CE2 . TYR   A 715 ? 0.2781 0.2451 0.2941 0.0256  0.0179  0.0097  740  TYR   A CE2 
5411 C  CZ  . TYR   A 715 ? 0.2915 0.2541 0.3056 0.0258  0.0197  0.0093  740  TYR   A CZ  
5412 O  OH  . TYR   A 715 ? 0.3034 0.2648 0.3188 0.0272  0.0192  0.0111  740  TYR   A OH  
5413 N  N   . GLN   A 716 ? 0.3147 0.2763 0.3280 0.0251  0.0279  0.0042  741  GLN   A N   
5414 C  CA  . GLN   A 716 ? 0.3257 0.2880 0.3428 0.0274  0.0296  0.0054  741  GLN   A CA  
5415 C  C   . GLN   A 716 ? 0.3036 0.2695 0.3256 0.0294  0.0276  0.0081  741  GLN   A C   
5416 O  O   . GLN   A 716 ? 0.3095 0.2786 0.3346 0.0303  0.0277  0.0089  741  GLN   A O   
5417 C  CB  . GLN   A 716 ? 0.3601 0.3173 0.3764 0.0285  0.0332  0.0049  741  GLN   A CB  
5418 C  CG  . GLN   A 716 ? 0.4465 0.4010 0.4588 0.0266  0.0356  0.0022  741  GLN   A CG  
5419 C  CD  . GLN   A 716 ? 0.5455 0.5034 0.5590 0.0263  0.0357  0.0018  741  GLN   A CD  
5420 O  OE1 . GLN   A 716 ? 0.5588 0.5181 0.5695 0.0241  0.0347  0.0003  741  GLN   A OE1 
5421 N  NE2 . GLN   A 716 ? 0.5720 0.5315 0.5898 0.0287  0.0367  0.0033  741  GLN   A NE2 
5422 N  N   . PRO   A 717 ? 0.3049 0.2710 0.3276 0.0299  0.0258  0.0096  742  PRO   A N   
5423 C  CA  . PRO   A 717 ? 0.3039 0.2739 0.3311 0.0316  0.0237  0.0122  742  PRO   A CA  
5424 C  C   . PRO   A 717 ? 0.2980 0.2729 0.3265 0.0306  0.0213  0.0124  742  PRO   A C   
5425 O  O   . PRO   A 717 ? 0.3062 0.2845 0.3387 0.0319  0.0208  0.0140  742  PRO   A O   
5426 C  CB  . PRO   A 717 ? 0.3232 0.2921 0.3495 0.0315  0.0219  0.0133  742  PRO   A CB  
5427 C  CG  . PRO   A 717 ? 0.3365 0.3000 0.3594 0.0311  0.0243  0.0118  742  PRO   A CG  
5428 C  CD  . PRO   A 717 ? 0.3117 0.2743 0.3313 0.0291  0.0255  0.0091  742  PRO   A CD  
5429 N  N   . CYS   A 718 ? 0.2852 0.2605 0.3104 0.0283  0.0201  0.0107  743  CYS   A N   
5430 C  CA  . CYS   A 718 ? 0.2814 0.2609 0.3075 0.0274  0.0180  0.0108  743  CYS   A CA  
5431 C  C   . CYS   A 718 ? 0.2685 0.2491 0.2952 0.0273  0.0197  0.0098  743  CYS   A C   
5432 O  O   . CYS   A 718 ? 0.2657 0.2499 0.2955 0.0279  0.0188  0.0109  743  CYS   A O   
5433 C  CB  . CYS   A 718 ? 0.2879 0.2676 0.3105 0.0253  0.0160  0.0098  743  CYS   A CB  
5434 S  SG  . CYS   A 718 ? 0.3421 0.3217 0.3647 0.0254  0.0134  0.0113  743  CYS   A SG  
5435 N  N   . VAL   A 719 ? 0.2615 0.2389 0.2854 0.0267  0.0222  0.0079  744  VAL   A N   
5436 C  CA  . VAL   A 719 ? 0.2671 0.2452 0.2913 0.0266  0.0241  0.0069  744  VAL   A CA  
5437 C  C   . VAL   A 719 ? 0.2843 0.2639 0.3132 0.0289  0.0254  0.0086  744  VAL   A C   
5438 O  O   . VAL   A 719 ? 0.2850 0.2678 0.3162 0.0292  0.0251  0.0090  744  VAL   A O   
5439 C  CB  . VAL   A 719 ? 0.3008 0.2748 0.3208 0.0253  0.0267  0.0046  744  VAL   A CB  
5440 C  CG1 . VAL   A 719 ? 0.3101 0.2848 0.3303 0.0252  0.0287  0.0037  744  VAL   A CG1 
5441 C  CG2 . VAL   A 719 ? 0.3161 0.2894 0.3318 0.0229  0.0253  0.0031  744  VAL   A CG2 
5442 N  N   . GLN   A 720 ? 0.2896 0.2669 0.3202 0.0308  0.0266  0.0098  745  GLN   A N   
5443 C  CA  . GLN   A 720 ? 0.3052 0.2839 0.3405 0.0333  0.0280  0.0116  745  GLN   A CA  
5444 C  C   . GLN   A 720 ? 0.2866 0.2706 0.3262 0.0339  0.0253  0.0138  745  GLN   A C   
5445 O  O   . GLN   A 720 ? 0.2832 0.2700 0.3262 0.0349  0.0260  0.0147  745  GLN   A O   
5446 C  CB  . GLN   A 720 ? 0.3551 0.3302 0.3913 0.0351  0.0300  0.0126  745  GLN   A CB  
5447 C  CG  . GLN   A 720 ? 0.4735 0.4431 0.5057 0.0346  0.0334  0.0104  745  GLN   A CG  
5448 C  CD  . GLN   A 720 ? 0.6160 0.5853 0.6487 0.0350  0.0362  0.0094  745  GLN   A CD  
5449 O  OE1 . GLN   A 720 ? 0.6647 0.6362 0.7020 0.0370  0.0372  0.0111  745  GLN   A OE1 
5450 N  NE2 . GLN   A 720 ? 0.6452 0.6120 0.6734 0.0329  0.0376  0.0068  745  GLN   A NE2 
5451 N  N   . ARG   A 721 ? 0.2716 0.2570 0.3108 0.0331  0.0222  0.0146  746  ARG   A N   
5452 C  CA  . ARG   A 721 ? 0.2670 0.2571 0.3095 0.0333  0.0195  0.0166  746  ARG   A CA  
5453 C  C   . ARG   A 721 ? 0.2490 0.2421 0.2911 0.0319  0.0186  0.0156  746  ARG   A C   
5454 O  O   . ARG   A 721 ? 0.2522 0.2491 0.2980 0.0325  0.0180  0.0169  746  ARG   A O   
5455 C  CB  . ARG   A 721 ? 0.3195 0.3096 0.3605 0.0325  0.0167  0.0172  746  ARG   A CB  
5456 C  CG  . ARG   A 721 ? 0.4008 0.3951 0.4453 0.0330  0.0140  0.0196  746  ARG   A CG  
5457 C  CD  . ARG   A 721 ? 0.4666 0.4597 0.5115 0.0338  0.0129  0.0212  746  ARG   A CD  
5458 N  NE  . ARG   A 721 ? 0.5054 0.5026 0.5533 0.0340  0.0101  0.0235  746  ARG   A NE  
5459 C  CZ  . ARG   A 721 ? 0.5247 0.5218 0.5719 0.0337  0.0080  0.0248  746  ARG   A CZ  
5460 N  NH1 . ARG   A 721 ? 0.5267 0.5200 0.5705 0.0333  0.0083  0.0239  746  ARG   A NH1 
5461 N  NH2 . ARG   A 721 ? 0.5196 0.5205 0.5695 0.0337  0.0054  0.0269  746  ARG   A NH2 
5462 N  N   . ALA   A 722 ? 0.2370 0.2285 0.2748 0.0299  0.0187  0.0133  747  ALA   A N   
5463 C  CA  . ALA   A 722 ? 0.2249 0.2188 0.2620 0.0285  0.0179  0.0124  747  ALA   A CA  
5464 C  C   . ALA   A 722 ? 0.2415 0.2363 0.2805 0.0292  0.0204  0.0121  747  ALA   A C   
5465 O  O   . ALA   A 722 ? 0.2325 0.2306 0.2735 0.0290  0.0196  0.0126  747  ALA   A O   
5466 C  CB  . ALA   A 722 ? 0.2364 0.2284 0.2685 0.0263  0.0176  0.0102  747  ALA   A CB  
5467 N  N   . GLU   A 723 ? 0.2555 0.2468 0.2935 0.0301  0.0233  0.0113  748  GLU   A N   
5468 C  CA  . GLU   A 723 ? 0.2684 0.2598 0.3079 0.0309  0.0261  0.0109  748  GLU   A CA  
5469 C  C   . GLU   A 723 ? 0.2795 0.2745 0.3249 0.0329  0.0259  0.0134  748  GLU   A C   
5470 O  O   . GLU   A 723 ? 0.2897 0.2871 0.3370 0.0331  0.0266  0.0135  748  GLU   A O   
5471 C  CB  . GLU   A 723 ? 0.3158 0.3024 0.3534 0.0316  0.0295  0.0098  748  GLU   A CB  
5472 C  CG  . GLU   A 723 ? 0.3943 0.3775 0.4262 0.0294  0.0304  0.0071  748  GLU   A CG  
5473 C  CD  . GLU   A 723 ? 0.5367 0.5147 0.5662 0.0299  0.0338  0.0059  748  GLU   A CD  
5474 O  OE1 . GLU   A 723 ? 0.5675 0.5441 0.5998 0.0321  0.0354  0.0072  748  GLU   A OE1 
5475 O  OE2 . GLU   A 723 ? 0.5903 0.5655 0.6151 0.0279  0.0348  0.0036  748  GLU   A OE2 
5476 N  N   . GLY   A 724 ? 0.2840 0.2795 0.3321 0.0343  0.0248  0.0154  749  GLY   A N   
5477 C  CA  . GLY   A 724 ? 0.2716 0.2708 0.3254 0.0362  0.0244  0.0180  749  GLY   A CA  
5478 C  C   . GLY   A 724 ? 0.2575 0.2615 0.3131 0.0351  0.0215  0.0189  749  GLY   A C   
5479 O  O   . GLY   A 724 ? 0.2764 0.2836 0.3356 0.0358  0.0219  0.0199  749  GLY   A O   
5480 N  N   . TYR   A 725 ? 0.2374 0.2418 0.2902 0.0333  0.0186  0.0183  750  TYR   A N   
5481 C  CA  . TYR   A 725 ? 0.2422 0.2506 0.2961 0.0320  0.0160  0.0189  750  TYR   A CA  
5482 C  C   . TYR   A 725 ? 0.2391 0.2483 0.2921 0.0311  0.0173  0.0174  750  TYR   A C   
5483 O  O   . TYR   A 725 ? 0.2600 0.2728 0.3160 0.0311  0.0165  0.0184  750  TYR   A O   
5484 C  CB  . TYR   A 725 ? 0.2504 0.2582 0.3008 0.0302  0.0133  0.0182  750  TYR   A CB  
5485 C  CG  . TYR   A 725 ? 0.2561 0.2652 0.3082 0.0306  0.0109  0.0202  750  TYR   A CG  
5486 C  CD1 . TYR   A 725 ? 0.2777 0.2909 0.3332 0.0305  0.0088  0.0221  750  TYR   A CD1 
5487 C  CD2 . TYR   A 725 ? 0.2695 0.2757 0.3195 0.0307  0.0106  0.0202  750  TYR   A CD2 
5488 C  CE1 . TYR   A 725 ? 0.3038 0.3183 0.3605 0.0306  0.0064  0.0240  750  TYR   A CE1 
5489 C  CE2 . TYR   A 725 ? 0.2986 0.3058 0.3498 0.0310  0.0083  0.0221  750  TYR   A CE2 
5490 C  CZ  . TYR   A 725 ? 0.3267 0.3382 0.3813 0.0309  0.0062  0.0240  750  TYR   A CZ  
5491 O  OH  . TYR   A 725 ? 0.3825 0.3950 0.4378 0.0309  0.0038  0.0258  750  TYR   A OH  
5492 N  N   . PHE   A 726 ? 0.2265 0.2324 0.2753 0.0302  0.0190  0.0151  751  PHE   A N   
5493 C  CA  . PHE   A 726 ? 0.2265 0.2333 0.2742 0.0292  0.0201  0.0138  751  PHE   A CA  
5494 C  C   . PHE   A 726 ? 0.2452 0.2534 0.2966 0.0307  0.0224  0.0145  751  PHE   A C   
5495 O  O   . PHE   A 726 ? 0.2384 0.2496 0.2915 0.0303  0.0220  0.0148  751  PHE   A O   
5496 C  CB  . PHE   A 726 ? 0.2180 0.2212 0.2606 0.0279  0.0215  0.0113  751  PHE   A CB  
5497 C  CG  . PHE   A 726 ? 0.2095 0.2139 0.2505 0.0265  0.0219  0.0101  751  PHE   A CG  
5498 C  CD1 . PHE   A 726 ? 0.2033 0.2098 0.2430 0.0249  0.0196  0.0098  751  PHE   A CD1 
5499 C  CD2 . PHE   A 726 ? 0.2204 0.2239 0.2613 0.0269  0.0248  0.0093  751  PHE   A CD2 
5500 C  CE1 . PHE   A 726 ? 0.2208 0.2284 0.2591 0.0237  0.0199  0.0089  751  PHE   A CE1 
5501 C  CE2 . PHE   A 726 ? 0.2274 0.2323 0.2669 0.0256  0.0251  0.0083  751  PHE   A CE2 
5502 C  CZ  . PHE   A 726 ? 0.2256 0.2325 0.2638 0.0240  0.0226  0.0081  751  PHE   A CZ  
5503 N  N   . ARG   A 727 ? 0.2564 0.2624 0.3092 0.0325  0.0248  0.0150  752  ARG   A N   
5504 C  CA  . ARG   A 727 ? 0.2863 0.2933 0.3428 0.0343  0.0275  0.0158  752  ARG   A CA  
5505 C  C   . ARG   A 727 ? 0.2994 0.3114 0.3613 0.0351  0.0257  0.0183  752  ARG   A C   
5506 O  O   . ARG   A 727 ? 0.3088 0.3236 0.3729 0.0350  0.0263  0.0186  752  ARG   A O   
5507 C  CB  . ARG   A 727 ? 0.3160 0.3194 0.3730 0.0362  0.0302  0.0160  752  ARG   A CB  
5508 C  CG  . ARG   A 727 ? 0.3804 0.3842 0.4412 0.0382  0.0335  0.0169  752  ARG   A CG  
5509 C  CD  . ARG   A 727 ? 0.4582 0.4578 0.5189 0.0400  0.0363  0.0170  752  ARG   A CD  
5510 N  NE  . ARG   A 727 ? 0.5440 0.5446 0.6077 0.0414  0.0346  0.0193  752  ARG   A NE  
5511 C  CZ  . ARG   A 727 ? 0.5953 0.5927 0.6563 0.0413  0.0340  0.0189  752  ARG   A CZ  
5512 N  NH1 . ARG   A 727 ? 0.6019 0.5949 0.6572 0.0397  0.0350  0.0163  752  ARG   A NH1 
5513 N  NH2 . ARG   A 727 ? 0.6051 0.6036 0.6690 0.0426  0.0324  0.0213  752  ARG   A NH2 
5514 N  N   . LYS   A 728 ? 0.3061 0.3196 0.3700 0.0355  0.0232  0.0201  753  LYS   A N   
5515 C  CA  . LYS   A 728 ? 0.3193 0.3378 0.3882 0.0360  0.0212  0.0227  753  LYS   A CA  
5516 C  C   . LYS   A 728 ? 0.3050 0.3266 0.3734 0.0340  0.0190  0.0223  753  LYS   A C   
5517 O  O   . LYS   A 728 ? 0.3260 0.3513 0.3981 0.0343  0.0189  0.0235  753  LYS   A O   
5518 C  CB  . LYS   A 728 ? 0.3624 0.3815 0.4329 0.0367  0.0190  0.0246  753  LYS   A CB  
5519 C  CG  . LYS   A 728 ? 0.4487 0.4655 0.5211 0.0391  0.0214  0.0256  753  LYS   A CG  
5520 C  CD  . LYS   A 728 ? 0.5347 0.5520 0.6084 0.0397  0.0191  0.0276  753  LYS   A CD  
5521 C  CE  . LYS   A 728 ? 0.5898 0.6035 0.6638 0.0417  0.0215  0.0281  753  LYS   A CE  
5522 N  NZ  . LYS   A 728 ? 0.6220 0.6359 0.6965 0.0420  0.0191  0.0299  753  LYS   A NZ  
5523 N  N   . TRP   A 729 ? 0.2800 0.2999 0.3437 0.0321  0.0176  0.0205  754  TRP   A N   
5524 C  CA  . TRP   A 729 ? 0.2681 0.2902 0.3308 0.0302  0.0158  0.0199  754  TRP   A CA  
5525 C  C   . TRP   A 729 ? 0.2879 0.3106 0.3507 0.0301  0.0181  0.0190  754  TRP   A C   
5526 O  O   . TRP   A 729 ? 0.2994 0.3255 0.3649 0.0298  0.0175  0.0199  754  TRP   A O   
5527 C  CB  . TRP   A 729 ? 0.2753 0.2949 0.3328 0.0285  0.0143  0.0182  754  TRP   A CB  
5528 C  CG  . TRP   A 729 ? 0.2775 0.2990 0.3337 0.0266  0.0127  0.0176  754  TRP   A CG  
5529 C  CD1 . TRP   A 729 ? 0.2920 0.3162 0.3496 0.0257  0.0100  0.0188  754  TRP   A CD1 
5530 C  CD2 . TRP   A 729 ? 0.2744 0.2946 0.3269 0.0253  0.0134  0.0157  754  TRP   A CD2 
5531 N  NE1 . TRP   A 729 ? 0.2945 0.3191 0.3498 0.0241  0.0093  0.0178  754  TRP   A NE1 
5532 C  CE2 . TRP   A 729 ? 0.2927 0.3151 0.3450 0.0238  0.0113  0.0159  754  TRP   A CE2 
5533 C  CE3 . TRP   A 729 ? 0.2845 0.3020 0.3340 0.0251  0.0157  0.0139  754  TRP   A CE3 
5534 C  CZ2 . TRP   A 729 ? 0.2939 0.3160 0.3434 0.0224  0.0114  0.0146  754  TRP   A CZ2 
5535 C  CZ3 . TRP   A 729 ? 0.2881 0.3055 0.3346 0.0235  0.0156  0.0125  754  TRP   A CZ3 
5536 C  CH2 . TRP   A 729 ? 0.2931 0.3128 0.3397 0.0223  0.0135  0.0129  754  TRP   A CH2 
5537 N  N   . LYS   A 730 ? 0.2719 0.2912 0.3320 0.0304  0.0208  0.0172  755  LYS   A N   
5538 C  CA  . LYS   A 730 ? 0.2815 0.3009 0.3412 0.0301  0.0231  0.0162  755  LYS   A CA  
5539 C  C   . LYS   A 730 ? 0.3002 0.3224 0.3653 0.0319  0.0247  0.0179  755  LYS   A C   
5540 O  O   . LYS   A 730 ? 0.3020 0.3268 0.3686 0.0314  0.0249  0.0181  755  LYS   A O   
5541 C  CB  . LYS   A 730 ? 0.2889 0.3038 0.3443 0.0300  0.0257  0.0140  755  LYS   A CB  
5542 C  CG  . LYS   A 730 ? 0.3298 0.3444 0.3838 0.0295  0.0281  0.0127  755  LYS   A CG  
5543 C  CD  . LYS   A 730 ? 0.3676 0.3776 0.4165 0.0288  0.0301  0.0104  755  LYS   A CD  
5544 C  CE  . LYS   A 730 ? 0.4186 0.4277 0.4659 0.0284  0.0329  0.0091  755  LYS   A CE  
5545 N  NZ  . LYS   A 730 ? 0.4397 0.4481 0.4902 0.0305  0.0361  0.0098  755  LYS   A NZ  
5546 N  N   . GLU   A 731 ? 0.3125 0.3343 0.3806 0.0339  0.0258  0.0193  756  GLU   A N   
5547 C  CA  . GLU   A 731 ? 0.3226 0.3471 0.3963 0.0358  0.0275  0.0213  756  GLU   A CA  
5548 C  C   . GLU   A 731 ? 0.3430 0.3728 0.4210 0.0355  0.0248  0.0234  756  GLU   A C   
5549 O  O   . GLU   A 731 ? 0.3434 0.3762 0.4255 0.0363  0.0260  0.0246  756  GLU   A O   
5550 C  CB  . GLU   A 731 ? 0.3535 0.3762 0.4296 0.0382  0.0292  0.0224  756  GLU   A CB  
5551 C  CG  . GLU   A 731 ? 0.4266 0.4441 0.4989 0.0387  0.0329  0.0203  756  GLU   A CG  
5552 C  CD  . GLU   A 731 ? 0.5085 0.5233 0.5824 0.0409  0.0349  0.0212  756  GLU   A CD  
5553 O  OE1 . GLU   A 731 ? 0.5327 0.5493 0.6098 0.0420  0.0331  0.0234  756  GLU   A OE1 
5554 O  OE2 . GLU   A 731 ? 0.5315 0.5421 0.6030 0.0415  0.0384  0.0197  756  GLU   A OE2 
5555 N  N   . SER   A 732 ? 0.3444 0.3754 0.4215 0.0341  0.0214  0.0238  757  SER   A N   
5556 C  CA  . SER   A 732 ? 0.3533 0.3889 0.4335 0.0333  0.0186  0.0256  757  SER   A CA  
5557 C  C   . SER   A 732 ? 0.3580 0.3946 0.4361 0.0312  0.0179  0.0242  757  SER   A C   
5558 O  O   . SER   A 732 ? 0.3655 0.4054 0.4452 0.0301  0.0155  0.0253  757  SER   A O   
5559 C  CB  . SER   A 732 ? 0.3678 0.4038 0.4474 0.0326  0.0153  0.0265  757  SER   A CB  
5560 O  OG  . SER   A 732 ? 0.3923 0.4259 0.4667 0.0306  0.0138  0.0246  757  SER   A OG  
5561 N  N   . ASN   A 733 ? 0.3580 0.3917 0.4322 0.0307  0.0199  0.0220  758  ASN   A N   
5562 C  CA  . ASN   A 733 ? 0.3816 0.4156 0.4530 0.0288  0.0195  0.0206  758  ASN   A CA  
5563 C  C   . ASN   A 733 ? 0.4234 0.4573 0.4920 0.0270  0.0163  0.0202  758  ASN   A C   
5564 O  O   . ASN   A 733 ? 0.4268 0.4627 0.4953 0.0256  0.0149  0.0202  758  ASN   A O   
5565 C  CB  . ASN   A 733 ? 0.3903 0.4280 0.4654 0.0288  0.0201  0.0216  758  ASN   A CB  
5566 C  CG  . ASN   A 733 ? 0.4389 0.4763 0.5110 0.0272  0.0204  0.0200  758  ASN   A CG  
5567 O  OD1 . ASN   A 733 ? 0.4573 0.4915 0.5246 0.0264  0.0211  0.0181  758  ASN   A OD1 
5568 N  ND2 . ASN   A 733 ? 0.4440 0.4848 0.5185 0.0265  0.0197  0.0210  758  ASN   A ND2 
5569 N  N   . GLY   A 734 ? 0.4496 0.4811 0.5160 0.0270  0.0153  0.0198  759  GLY   A N   
5570 C  CA  . GLY   A 734 ? 0.4873 0.5182 0.5507 0.0254  0.0126  0.0194  759  GLY   A CA  
5571 C  C   . GLY   A 734 ? 0.5270 0.5612 0.5933 0.0249  0.0098  0.0213  759  GLY   A C   
5572 O  O   . GLY   A 734 ? 0.5373 0.5712 0.6012 0.0233  0.0076  0.0209  759  GLY   A O   
5573 N  N   . GLN   A 735 ? 0.5439 0.5812 0.6152 0.0260  0.0099  0.0233  760  GLN   A N   
5574 C  CA  . GLN   A 735 ? 0.5640 0.6046 0.6380 0.0252  0.0071  0.0252  760  GLN   A CA  
5575 C  C   . GLN   A 735 ? 0.5755 0.6146 0.6477 0.0250  0.0051  0.0255  760  GLN   A C   
5576 O  O   . GLN   A 735 ? 0.5898 0.6287 0.6595 0.0232  0.0028  0.0252  760  GLN   A O   
5577 C  CB  . GLN   A 735 ? 0.5824 0.6271 0.6625 0.0265  0.0077  0.0275  760  GLN   A CB  
5578 C  CG  . GLN   A 735 ? 0.6362 0.6834 0.7184 0.0261  0.0087  0.0276  760  GLN   A CG  
5579 C  CD  . GLN   A 735 ? 0.6868 0.7388 0.7746 0.0263  0.0076  0.0302  760  GLN   A CD  
5580 O  OE1 . GLN   A 735 ? 0.6926 0.7472 0.7811 0.0246  0.0060  0.0306  760  GLN   A OE1 
5581 N  NE2 . GLN   A 735 ? 0.7092 0.7627 0.8011 0.0283  0.0085  0.0320  760  GLN   A NE2 
5582 N  N   . LEU   A 736 ? 0.5671 0.6046 0.6400 0.0267  0.0062  0.0260  761  LEU   A N   
5583 C  CA  . LEU   A 736 ? 0.5687 0.6044 0.6402 0.0270  0.0048  0.0264  761  LEU   A CA  
5584 C  C   . LEU   A 736 ? 0.5433 0.5764 0.6096 0.0252  0.0031  0.0248  761  LEU   A C   
5585 O  O   . LEU   A 736 ? 0.5555 0.5859 0.6182 0.0247  0.0043  0.0227  761  LEU   A O   
5586 C  CB  . LEU   A 736 ? 0.5840 0.6168 0.6553 0.0290  0.0075  0.0260  761  LEU   A CB  
5587 C  CG  . LEU   A 736 ? 0.6216 0.6526 0.6925 0.0299  0.0067  0.0268  761  LEU   A CG  
5588 C  CD1 . LEU   A 736 ? 0.6335 0.6666 0.7096 0.0320  0.0075  0.0293  761  LEU   A CD1 
5589 C  CD2 . LEU   A 736 ? 0.6366 0.6628 0.7034 0.0302  0.0086  0.0248  761  LEU   A CD2 
5590 N  N   . SER   A 737 ? 0.5092 0.5432 0.5752 0.0241  0.0004  0.0258  762  SER   A N   
5591 C  CA  . SER   A 737 ? 0.4739 0.5053 0.5351 0.0226  -0.0011 0.0245  762  SER   A CA  
5592 C  C   . SER   A 737 ? 0.4250 0.4532 0.4843 0.0236  -0.0005 0.0241  762  SER   A C   
5593 O  O   . SER   A 737 ? 0.4364 0.4651 0.4981 0.0249  -0.0007 0.0257  762  SER   A O   
5594 C  CB  . SER   A 737 ? 0.4999 0.5332 0.5612 0.0210  -0.0041 0.0257  762  SER   A CB  
5595 O  OG  . SER   A 737 ? 0.5374 0.5721 0.5983 0.0193  -0.0048 0.0252  762  SER   A OG  
5596 N  N   . LEU   A 738 ? 0.3614 0.3863 0.4168 0.0232  0.0006  0.0221  763  LEU   A N   
5597 C  CA  . LEU   A 738 ? 0.3138 0.3353 0.3667 0.0239  0.0013  0.0214  763  LEU   A CA  
5598 C  C   . LEU   A 738 ? 0.2631 0.2835 0.3130 0.0225  -0.0011 0.0212  763  LEU   A C   
5599 O  O   . LEU   A 738 ? 0.2754 0.2964 0.3236 0.0209  -0.0022 0.0207  763  LEU   A O   
5600 C  CB  . LEU   A 738 ? 0.3241 0.3429 0.3738 0.0237  0.0033  0.0191  763  LEU   A CB  
5601 C  CG  . LEU   A 738 ? 0.3462 0.3651 0.3976 0.0248  0.0060  0.0187  763  LEU   A CG  
5602 C  CD1 . LEU   A 738 ? 0.3517 0.3684 0.3994 0.0239  0.0075  0.0164  763  LEU   A CD1 
5603 C  CD2 . LEU   A 738 ? 0.3605 0.3779 0.4135 0.0267  0.0075  0.0194  763  LEU   A CD2 
5604 N  N   . PRO   A 739 ? 0.2334 0.2516 0.2818 0.0230  -0.0014 0.0215  764  PRO   A N   
5605 C  CA  . PRO   A 739 ? 0.2114 0.2281 0.2563 0.0215  -0.0033 0.0210  764  PRO   A CA  
5606 C  C   . PRO   A 739 ? 0.2085 0.2232 0.2498 0.0204  -0.0025 0.0188  764  PRO   A C   
5607 O  O   . PRO   A 739 ? 0.2019 0.2149 0.2421 0.0210  -0.0005 0.0176  764  PRO   A O   
5608 C  CB  . PRO   A 739 ? 0.2258 0.2401 0.2700 0.0225  -0.0032 0.0215  764  PRO   A CB  
5609 C  CG  . PRO   A 739 ? 0.2373 0.2533 0.2860 0.0245  -0.0021 0.0232  764  PRO   A CG  
5610 C  CD  . PRO   A 739 ? 0.2317 0.2486 0.2816 0.0248  -0.0001 0.0222  764  PRO   A CD  
5611 N  N   . VAL   A 740 ? 0.2027 0.2176 0.2419 0.0188  -0.0040 0.0184  765  VAL   A N   
5612 C  CA  . VAL   A 740 ? 0.1895 0.2028 0.2255 0.0179  -0.0032 0.0167  765  VAL   A CA  
5613 C  C   . VAL   A 740 ? 0.1903 0.2005 0.2234 0.0181  -0.0024 0.0155  765  VAL   A C   
5614 O  O   . VAL   A 740 ? 0.1876 0.1967 0.2190 0.0179  -0.0009 0.0142  765  VAL   A O   
5615 C  CB  . VAL   A 740 ? 0.2094 0.2233 0.2438 0.0163  -0.0049 0.0165  765  VAL   A CB  
5616 C  CG1 . VAL   A 740 ? 0.2268 0.2392 0.2582 0.0155  -0.0040 0.0149  765  VAL   A CG1 
5617 C  CG2 . VAL   A 740 ? 0.2088 0.2257 0.2461 0.0159  -0.0056 0.0175  765  VAL   A CG2 
5618 N  N   . ASP   A 741 ? 0.1882 0.1970 0.2207 0.0184  -0.0033 0.0163  766  ASP   A N   
5619 C  CA  . ASP   A 741 ? 0.1810 0.1868 0.2105 0.0184  -0.0027 0.0153  766  ASP   A CA  
5620 C  C   . ASP   A 741 ? 0.1787 0.1830 0.2085 0.0195  -0.0005 0.0146  766  ASP   A C   
5621 O  O   . ASP   A 741 ? 0.1863 0.1883 0.2134 0.0191  0.0003  0.0135  766  ASP   A O   
5622 C  CB  . ASP   A 741 ? 0.1781 0.1828 0.2068 0.0183  -0.0042 0.0163  766  ASP   A CB  
5623 C  CG  . ASP   A 741 ? 0.1887 0.1940 0.2161 0.0170  -0.0062 0.0167  766  ASP   A CG  
5624 O  OD1 . ASP   A 741 ? 0.2106 0.2169 0.2375 0.0160  -0.0063 0.0161  766  ASP   A OD1 
5625 O  OD2 . ASP   A 741 ? 0.2184 0.2231 0.2451 0.0168  -0.0076 0.0177  766  ASP   A OD2 
5626 N  N   . VAL   A 742 ? 0.1804 0.1861 0.2134 0.0207  0.0005  0.0153  767  VAL   A N   
5627 C  CA  . VAL   A 742 ? 0.1737 0.1777 0.2068 0.0217  0.0029  0.0146  767  VAL   A CA  
5628 C  C   . VAL   A 742 ? 0.1659 0.1709 0.1992 0.0214  0.0044  0.0135  767  VAL   A C   
5629 O  O   . VAL   A 742 ? 0.1869 0.1904 0.2197 0.0219  0.0065  0.0126  767  VAL   A O   
5630 C  CB  . VAL   A 742 ? 0.1816 0.1859 0.2180 0.0235  0.0036  0.0161  767  VAL   A CB  
5631 C  CG1 . VAL   A 742 ? 0.1925 0.1962 0.2289 0.0237  0.0018  0.0175  767  VAL   A CG1 
5632 C  CG2 . VAL   A 742 ? 0.1924 0.2001 0.2328 0.0242  0.0036  0.0173  767  VAL   A CG2 
5633 N  N   . THR   A 743 ? 0.1657 0.1730 0.1994 0.0205  0.0034  0.0135  768  THR   A N   
5634 C  CA  . THR   A 743 ? 0.1756 0.1841 0.2098 0.0203  0.0047  0.0127  768  THR   A CA  
5635 C  C   . THR   A 743 ? 0.1887 0.1951 0.2194 0.0195  0.0061  0.0109  768  THR   A C   
5636 O  O   . THR   A 743 ? 0.1960 0.2023 0.2269 0.0198  0.0080  0.0102  768  THR   A O   
5637 C  CB  . THR   A 743 ? 0.1964 0.2077 0.2317 0.0194  0.0033  0.0133  768  THR   A CB  
5638 O  OG1 . THR   A 743 ? 0.2020 0.2155 0.2408 0.0202  0.0023  0.0150  768  THR   A OG1 
5639 C  CG2 . THR   A 743 ? 0.1983 0.2108 0.2339 0.0192  0.0046  0.0126  768  THR   A CG2 
5640 N  N   . LEU   A 744 ? 0.1787 0.1837 0.2064 0.0184  0.0052  0.0102  769  LEU   A N   
5641 C  CA  . LEU   A 744 ? 0.1873 0.1907 0.2120 0.0176  0.0065  0.0087  769  LEU   A CA  
5642 C  C   . LEU   A 744 ? 0.1896 0.1906 0.2137 0.0183  0.0084  0.0080  769  LEU   A C   
5643 O  O   . LEU   A 744 ? 0.1948 0.1953 0.2180 0.0180  0.0101  0.0070  769  LEU   A O   
5644 C  CB  . LEU   A 744 ? 0.2075 0.2097 0.2294 0.0165  0.0053  0.0083  769  LEU   A CB  
5645 C  CG  . LEU   A 744 ? 0.2174 0.2214 0.2387 0.0155  0.0041  0.0083  769  LEU   A CG  
5646 C  CD1 . LEU   A 744 ? 0.2215 0.2243 0.2405 0.0147  0.0030  0.0082  769  LEU   A CD1 
5647 C  CD2 . LEU   A 744 ? 0.2153 0.2201 0.2355 0.0148  0.0053  0.0074  769  LEU   A CD2 
5648 N  N   . ALA   A 745 ? 0.1872 0.1866 0.2120 0.0192  0.0083  0.0087  770  ALA   A N   
5649 C  CA  . ALA   A 745 ? 0.1916 0.1883 0.2159 0.0200  0.0104  0.0081  770  ALA   A CA  
5650 C  C   . ALA   A 745 ? 0.2055 0.2030 0.2323 0.0211  0.0122  0.0083  770  ALA   A C   
5651 O  O   . ALA   A 745 ? 0.2207 0.2163 0.2460 0.0210  0.0143  0.0071  770  ALA   A O   
5652 C  CB  . ALA   A 745 ? 0.1948 0.1899 0.2197 0.0209  0.0098  0.0091  770  ALA   A CB  
5653 N  N   . VAL   A 746 ? 0.1913 0.1916 0.2217 0.0220  0.0114  0.0098  771  VAL   A N   
5654 C  CA  . VAL   A 746 ? 0.1824 0.1837 0.2156 0.0233  0.0132  0.0102  771  VAL   A CA  
5655 C  C   . VAL   A 746 ? 0.1830 0.1849 0.2149 0.0223  0.0144  0.0089  771  VAL   A C   
5656 O  O   . VAL   A 746 ? 0.1907 0.1912 0.2224 0.0228  0.0168  0.0082  771  VAL   A O   
5657 C  CB  . VAL   A 746 ? 0.1954 0.1999 0.2329 0.0243  0.0117  0.0123  771  VAL   A CB  
5658 C  CG1 . VAL   A 746 ? 0.2154 0.2217 0.2561 0.0253  0.0135  0.0128  771  VAL   A CG1 
5659 C  CG2 . VAL   A 746 ? 0.2143 0.2180 0.2532 0.0254  0.0109  0.0137  771  VAL   A CG2 
5660 N  N   . PHE   A 747 ? 0.1759 0.1797 0.2069 0.0210  0.0129  0.0087  772  PHE   A N   
5661 C  CA  . PHE   A 747 ? 0.1752 0.1798 0.2049 0.0201  0.0139  0.0076  772  PHE   A CA  
5662 C  C   . PHE   A 747 ? 0.1842 0.1860 0.2099 0.0190  0.0153  0.0059  772  PHE   A C   
5663 O  O   . PHE   A 747 ? 0.1930 0.1943 0.2177 0.0187  0.0171  0.0049  772  PHE   A O   
5664 C  CB  . PHE   A 747 ? 0.1719 0.1790 0.2014 0.0189  0.0119  0.0079  772  PHE   A CB  
5665 C  CG  . PHE   A 747 ? 0.1858 0.1960 0.2189 0.0195  0.0108  0.0094  772  PHE   A CG  
5666 C  CD1 . PHE   A 747 ? 0.2053 0.2164 0.2419 0.0209  0.0115  0.0105  772  PHE   A CD1 
5667 C  CD2 . PHE   A 747 ? 0.1831 0.1952 0.2160 0.0184  0.0092  0.0097  772  PHE   A CD2 
5668 C  CE1 . PHE   A 747 ? 0.2167 0.2309 0.2566 0.0212  0.0104  0.0119  772  PHE   A CE1 
5669 C  CE2 . PHE   A 747 ? 0.2008 0.2156 0.2367 0.0187  0.0082  0.0109  772  PHE   A CE2 
5670 C  CZ  . PHE   A 747 ? 0.2074 0.2233 0.2468 0.0200  0.0088  0.0120  772  PHE   A CZ  
5671 N  N   . ALA   A 748 ? 0.1899 0.1898 0.2131 0.0183  0.0144  0.0054  773  ALA   A N   
5672 C  CA  . ALA   A 748 ? 0.1948 0.1922 0.2141 0.0171  0.0156  0.0038  773  ALA   A CA  
5673 C  C   . ALA   A 748 ? 0.2131 0.2078 0.2321 0.0178  0.0182  0.0031  773  ALA   A C   
5674 O  O   . ALA   A 748 ? 0.2223 0.2155 0.2385 0.0168  0.0198  0.0017  773  ALA   A O   
5675 C  CB  . ALA   A 748 ? 0.2000 0.1961 0.2171 0.0162  0.0143  0.0036  773  ALA   A CB  
5676 N  N   . VAL   A 749 ? 0.1990 0.1928 0.2205 0.0196  0.0187  0.0041  774  VAL   A N   
5677 C  CA  . VAL   A 749 ? 0.2095 0.2004 0.2310 0.0205  0.0215  0.0035  774  VAL   A CA  
5678 C  C   . VAL   A 749 ? 0.2157 0.2080 0.2389 0.0211  0.0232  0.0035  774  VAL   A C   
5679 O  O   . VAL   A 749 ? 0.2372 0.2272 0.2583 0.0207  0.0257  0.0022  774  VAL   A O   
5680 C  CB  . VAL   A 749 ? 0.2254 0.2153 0.2496 0.0224  0.0214  0.0050  774  VAL   A CB  
5681 C  CG1 . VAL   A 749 ? 0.2275 0.2149 0.2527 0.0239  0.0245  0.0049  774  VAL   A CG1 
5682 C  CG2 . VAL   A 749 ? 0.2441 0.2317 0.2658 0.0217  0.0204  0.0047  774  VAL   A CG2 
5683 N  N   . GLY   A 750 ? 0.2021 0.1980 0.2289 0.0219  0.0220  0.0049  775  GLY   A N   
5684 C  CA  . GLY   A 750 ? 0.2147 0.2121 0.2435 0.0225  0.0236  0.0051  775  GLY   A CA  
5685 C  C   . GLY   A 750 ? 0.2287 0.2260 0.2543 0.0208  0.0245  0.0035  775  GLY   A C   
5686 O  O   . GLY   A 750 ? 0.2455 0.2420 0.2710 0.0211  0.0270  0.0028  775  GLY   A O   
5687 N  N   . ALA   A 751 ? 0.2329 0.2312 0.2560 0.0191  0.0226  0.0030  776  ALA   A N   
5688 C  CA  . ALA   A 751 ? 0.2410 0.2397 0.2613 0.0174  0.0232  0.0018  776  ALA   A CA  
5689 C  C   . ALA   A 751 ? 0.2381 0.2333 0.2541 0.0162  0.0252  -0.0001 776  ALA   A C   
5690 O  O   . ALA   A 751 ? 0.2411 0.2366 0.2543 0.0146  0.0256  -0.0011 776  ALA   A O   
5691 C  CB  . ALA   A 751 ? 0.2587 0.2599 0.2781 0.0161  0.0207  0.0021  776  ALA   A CB  
5692 N  N   . GLN   A 752 ? 0.2348 0.2267 0.2501 0.0168  0.0264  -0.0005 777  GLN   A N   
5693 C  CA  . GLN   A 752 ? 0.2518 0.2397 0.2629 0.0156  0.0286  -0.0023 777  GLN   A CA  
5694 C  C   . GLN   A 752 ? 0.3035 0.2897 0.3139 0.0160  0.0317  -0.0032 777  GLN   A C   
5695 O  O   . GLN   A 752 ? 0.3387 0.3216 0.3451 0.0146  0.0336  -0.0049 777  GLN   A O   
5696 C  CB  . GLN   A 752 ? 0.2565 0.2411 0.2669 0.0162  0.0288  -0.0024 777  GLN   A CB  
5697 C  CG  . GLN   A 752 ? 0.2519 0.2378 0.2616 0.0153  0.0259  -0.0020 777  GLN   A CG  
5698 C  CD  . GLN   A 752 ? 0.3135 0.2990 0.3188 0.0127  0.0254  -0.0033 777  GLN   A CD  
5699 O  OE1 . GLN   A 752 ? 0.3642 0.3464 0.3660 0.0115  0.0268  -0.0047 777  GLN   A OE1 
5700 N  NE2 . GLN   A 752 ? 0.3106 0.2996 0.3161 0.0118  0.0234  -0.0029 777  GLN   A NE2 
5701 N  N   . SER   A 753 ? 0.2862 0.2742 0.3006 0.0177  0.0325  -0.0021 778  SER   A N   
5702 C  CA  . SER   A 753 ? 0.2925 0.2791 0.3064 0.0181  0.0356  -0.0029 778  SER   A CA  
5703 C  C   . SER   A 753 ? 0.2775 0.2677 0.2919 0.0173  0.0348  -0.0026 778  SER   A C   
5704 O  O   . SER   A 753 ? 0.2631 0.2570 0.2798 0.0173  0.0322  -0.0014 778  SER   A O   
5705 C  CB  . SER   A 753 ? 0.3084 0.2943 0.3266 0.0208  0.0375  -0.0017 778  SER   A CB  
5706 O  OG  . SER   A 753 ? 0.3020 0.2924 0.3252 0.0221  0.0359  0.0003  778  SER   A OG  
5707 N  N   . THR   A 754 ? 0.2801 0.2690 0.2924 0.0166  0.0373  -0.0038 779  THR   A N   
5708 C  CA  . THR   A 754 ? 0.2778 0.2700 0.2904 0.0158  0.0368  -0.0036 779  THR   A CA  
5709 C  C   . THR   A 754 ? 0.2715 0.2672 0.2898 0.0178  0.0362  -0.0016 779  THR   A C   
5710 O  O   . THR   A 754 ? 0.2606 0.2599 0.2802 0.0174  0.0340  -0.0007 779  THR   A O   
5711 C  CB  . THR   A 754 ? 0.3242 0.3140 0.3334 0.0148  0.0399  -0.0052 779  THR   A CB  
5712 O  OG1 . THR   A 754 ? 0.3551 0.3418 0.3587 0.0126  0.0402  -0.0069 779  THR   A OG1 
5713 C  CG2 . THR   A 754 ? 0.3287 0.3215 0.3380 0.0141  0.0397  -0.0049 779  THR   A CG2 
5714 N  N   . GLU   A 755 ? 0.2699 0.2646 0.2916 0.0201  0.0380  -0.0009 780  GLU   A N   
5715 C  CA  . GLU   A 755 ? 0.2711 0.2695 0.2984 0.0218  0.0373  0.0011  780  GLU   A CA  
5716 C  C   . GLU   A 755 ? 0.2530 0.2544 0.2827 0.0220  0.0337  0.0026  780  GLU   A C   
5717 O  O   . GLU   A 755 ? 0.2490 0.2541 0.2816 0.0221  0.0321  0.0038  780  GLU   A O   
5718 C  CB  . GLU   A 755 ? 0.3117 0.3087 0.3424 0.0242  0.0400  0.0019  780  GLU   A CB  
5719 C  CG  . GLU   A 755 ? 0.3859 0.3809 0.4152 0.0243  0.0437  0.0008  780  GLU   A CG  
5720 C  CD  . GLU   A 755 ? 0.4846 0.4782 0.5175 0.0269  0.0466  0.0016  780  GLU   A CD  
5721 O  OE1 . GLU   A 755 ? 0.4363 0.4305 0.4729 0.0286  0.0457  0.0032  780  GLU   A OE1 
5722 O  OE2 . GLU   A 755 ? 0.5256 0.5173 0.5575 0.0272  0.0500  0.0008  780  GLU   A OE2 
5723 N  N   . GLY   A 756 ? 0.2382 0.2376 0.2665 0.0218  0.0325  0.0024  781  GLY   A N   
5724 C  CA  . GLY   A 756 ? 0.2395 0.2412 0.2698 0.0220  0.0293  0.0037  781  GLY   A CA  
5725 C  C   . GLY   A 756 ? 0.2342 0.2380 0.2624 0.0201  0.0269  0.0034  781  GLY   A C   
5726 O  O   . GLY   A 756 ? 0.2332 0.2401 0.2638 0.0202  0.0248  0.0046  781  GLY   A O   
5727 N  N   . TRP   A 757 ? 0.2234 0.2255 0.2470 0.0183  0.0275  0.0018  782  TRP   A N   
5728 C  CA  . TRP   A 757 ? 0.2247 0.2288 0.2463 0.0165  0.0255  0.0016  782  TRP   A CA  
5729 C  C   . TRP   A 757 ? 0.2331 0.2405 0.2570 0.0166  0.0254  0.0024  782  TRP   A C   
5730 O  O   . TRP   A 757 ? 0.2193 0.2293 0.2447 0.0164  0.0232  0.0034  782  TRP   A O   
5731 C  CB  . TRP   A 757 ? 0.2217 0.2235 0.2382 0.0146  0.0266  -0.0002 782  TRP   A CB  
5732 C  CG  . TRP   A 757 ? 0.2225 0.2259 0.2367 0.0128  0.0244  -0.0003 782  TRP   A CG  
5733 C  CD1 . TRP   A 757 ? 0.2081 0.2106 0.2202 0.0119  0.0230  -0.0006 782  TRP   A CD1 
5734 C  CD2 . TRP   A 757 ? 0.2191 0.2253 0.2329 0.0118  0.0237  0.0000  782  TRP   A CD2 
5735 N  NE1 . TRP   A 757 ? 0.2069 0.2115 0.2174 0.0104  0.0214  -0.0004 782  TRP   A NE1 
5736 C  CE2 . TRP   A 757 ? 0.2151 0.2220 0.2266 0.0104  0.0218  0.0000  782  TRP   A CE2 
5737 C  CE3 . TRP   A 757 ? 0.2378 0.2460 0.2531 0.0121  0.0244  0.0005  782  TRP   A CE3 
5738 C  CZ2 . TRP   A 757 ? 0.2241 0.2336 0.2349 0.0092  0.0207  0.0004  782  TRP   A CZ2 
5739 C  CZ3 . TRP   A 757 ? 0.2381 0.2489 0.2526 0.0109  0.0232  0.0009  782  TRP   A CZ3 
5740 C  CH2 . TRP   A 757 ? 0.2448 0.2561 0.2570 0.0095  0.0214  0.0009  782  TRP   A CH2 
5741 N  N   . ASP   A 758 ? 0.2344 0.2413 0.2586 0.0171  0.0279  0.0020  783  ASP   A N   
5742 C  CA  . ASP   A 758 ? 0.2526 0.2625 0.2790 0.0172  0.0280  0.0028  783  ASP   A CA  
5743 C  C   . ASP   A 758 ? 0.2577 0.2705 0.2892 0.0186  0.0266  0.0046  783  ASP   A C   
5744 O  O   . ASP   A 758 ? 0.2454 0.2609 0.2782 0.0181  0.0251  0.0054  783  ASP   A O   
5745 C  CB  . ASP   A 758 ? 0.2754 0.2840 0.3013 0.0175  0.0313  0.0020  783  ASP   A CB  
5746 C  CG  . ASP   A 758 ? 0.3239 0.3302 0.3444 0.0156  0.0326  0.0002  783  ASP   A CG  
5747 O  OD1 . ASP   A 758 ? 0.3239 0.3306 0.3415 0.0140  0.0307  -0.0002 783  ASP   A OD1 
5748 O  OD2 . ASP   A 758 ? 0.3495 0.3536 0.3687 0.0158  0.0355  -0.0008 783  ASP   A OD2 
5749 N  N   . PHE   A 759 ? 0.2613 0.2732 0.2954 0.0202  0.0270  0.0053  784  PHE   A N   
5750 C  CA  . PHE   A 759 ? 0.2688 0.2837 0.3078 0.0214  0.0254  0.0072  784  PHE   A CA  
5751 C  C   . PHE   A 759 ? 0.2627 0.2790 0.3014 0.0205  0.0222  0.0078  784  PHE   A C   
5752 O  O   . PHE   A 759 ? 0.2498 0.2690 0.2907 0.0203  0.0207  0.0089  784  PHE   A O   
5753 C  CB  . PHE   A 759 ? 0.2813 0.2952 0.3232 0.0233  0.0264  0.0081  784  PHE   A CB  
5754 C  CG  . PHE   A 759 ? 0.2838 0.3011 0.3307 0.0244  0.0247  0.0102  784  PHE   A CG  
5755 C  CD1 . PHE   A 759 ? 0.3003 0.3202 0.3510 0.0252  0.0257  0.0113  784  PHE   A CD1 
5756 C  CD2 . PHE   A 759 ? 0.2988 0.3165 0.3465 0.0244  0.0221  0.0111  784  PHE   A CD2 
5757 C  CE1 . PHE   A 759 ? 0.3071 0.3304 0.3625 0.0260  0.0241  0.0133  784  PHE   A CE1 
5758 C  CE2 . PHE   A 759 ? 0.3089 0.3298 0.3609 0.0251  0.0205  0.0130  784  PHE   A CE2 
5759 C  CZ  . PHE   A 759 ? 0.3046 0.3283 0.3605 0.0258  0.0214  0.0141  784  PHE   A CZ  
5760 N  N   . LEU   A 760 ? 0.2598 0.2739 0.2955 0.0199  0.0213  0.0070  785  LEU   A N   
5761 C  CA  . LEU   A 760 ? 0.2677 0.2827 0.3028 0.0190  0.0186  0.0075  785  LEU   A CA  
5762 C  C   . LEU   A 760 ? 0.2594 0.2762 0.2931 0.0176  0.0176  0.0073  785  LEU   A C   
5763 O  O   . LEU   A 760 ? 0.2659 0.2848 0.3012 0.0174  0.0158  0.0083  785  LEU   A O   
5764 C  CB  . LEU   A 760 ? 0.2753 0.2875 0.3072 0.0186  0.0182  0.0066  785  LEU   A CB  
5765 C  CG  . LEU   A 760 ? 0.3001 0.3127 0.3318 0.0182  0.0156  0.0072  785  LEU   A CG  
5766 C  CD1 . LEU   A 760 ? 0.2628 0.2767 0.2983 0.0194  0.0144  0.0088  785  LEU   A CD1 
5767 C  CD2 . LEU   A 760 ? 0.3074 0.3170 0.3357 0.0176  0.0155  0.0062  785  LEU   A CD2 
5768 N  N   . TYR   A 761 ? 0.2459 0.2619 0.2766 0.0167  0.0190  0.0062  786  TYR   A N   
5769 C  CA  . TYR   A 761 ? 0.2479 0.2657 0.2775 0.0155  0.0183  0.0062  786  TYR   A CA  
5770 C  C   . TYR   A 761 ? 0.2533 0.2738 0.2863 0.0159  0.0183  0.0073  786  TYR   A C   
5771 O  O   . TYR   A 761 ? 0.2389 0.2612 0.2724 0.0153  0.0169  0.0079  786  TYR   A O   
5772 C  CB  . TYR   A 761 ? 0.2467 0.2633 0.2725 0.0143  0.0197  0.0049  786  TYR   A CB  
5773 C  CG  . TYR   A 761 ? 0.2508 0.2695 0.2759 0.0132  0.0192  0.0051  786  TYR   A CG  
5774 C  CD1 . TYR   A 761 ? 0.2710 0.2907 0.2953 0.0124  0.0171  0.0057  786  TYR   A CD1 
5775 C  CD2 . TYR   A 761 ? 0.2690 0.2887 0.2945 0.0131  0.0207  0.0051  786  TYR   A CD2 
5776 C  CE1 . TYR   A 761 ? 0.2916 0.3132 0.3156 0.0116  0.0167  0.0062  786  TYR   A CE1 
5777 C  CE2 . TYR   A 761 ? 0.2779 0.2996 0.3030 0.0123  0.0202  0.0056  786  TYR   A CE2 
5778 C  CZ  . TYR   A 761 ? 0.3002 0.3228 0.3244 0.0115  0.0182  0.0061  786  TYR   A CZ  
5779 O  OH  . TYR   A 761 ? 0.3290 0.3535 0.3530 0.0108  0.0178  0.0067  786  TYR   A OH  
5780 N  N   . SER   A 762 ? 0.2509 0.2717 0.2865 0.0171  0.0201  0.0076  787  SER   A N   
5781 C  CA  . SER   A 762 ? 0.2589 0.2825 0.2980 0.0175  0.0201  0.0087  787  SER   A CA  
5782 C  C   . SER   A 762 ? 0.2789 0.3045 0.3209 0.0177  0.0178  0.0101  787  SER   A C   
5783 O  O   . SER   A 762 ? 0.3208 0.3488 0.3649 0.0174  0.0173  0.0110  787  SER   A O   
5784 C  CB  . SER   A 762 ? 0.2597 0.2833 0.3013 0.0189  0.0226  0.0089  787  SER   A CB  
5785 O  OG  . SER   A 762 ? 0.3028 0.3263 0.3475 0.0203  0.0223  0.0098  787  SER   A OG  
5786 N  N   . LYS   A 763 ? 0.2364 0.2610 0.2785 0.0181  0.0163  0.0104  788  LYS   A N   
5787 C  CA  . LYS   A 763 ? 0.2225 0.2487 0.2668 0.0180  0.0140  0.0117  788  LYS   A CA  
5788 C  C   . LYS   A 763 ? 0.2233 0.2495 0.2652 0.0166  0.0122  0.0115  788  LYS   A C   
5789 O  O   . LYS   A 763 ? 0.2326 0.2601 0.2757 0.0162  0.0104  0.0123  788  LYS   A O   
5790 C  CB  . LYS   A 763 ? 0.2421 0.2673 0.2875 0.0190  0.0133  0.0121  788  LYS   A CB  
5791 C  CG  . LYS   A 763 ? 0.2773 0.3030 0.3262 0.0206  0.0148  0.0130  788  LYS   A CG  
5792 C  CD  . LYS   A 763 ? 0.3325 0.3617 0.3857 0.0209  0.0146  0.0144  788  LYS   A CD  
5793 C  CE  . LYS   A 763 ? 0.4159 0.4462 0.4732 0.0226  0.0159  0.0156  788  LYS   A CE  
5794 N  NZ  . LYS   A 763 ? 0.4637 0.4977 0.5252 0.0227  0.0154  0.0171  788  LYS   A NZ  
5795 N  N   . TYR   A 764 ? 0.2118 0.2363 0.2501 0.0159  0.0126  0.0103  789  TYR   A N   
5796 C  CA  . TYR   A 764 ? 0.2004 0.2246 0.2362 0.0147  0.0111  0.0102  789  TYR   A CA  
5797 C  C   . TYR   A 764 ? 0.2103 0.2365 0.2471 0.0141  0.0105  0.0108  789  TYR   A C   
5798 O  O   . TYR   A 764 ? 0.1986 0.2250 0.2353 0.0135  0.0089  0.0114  789  TYR   A O   
5799 C  CB  . TYR   A 764 ? 0.1990 0.2215 0.2311 0.0141  0.0119  0.0090  789  TYR   A CB  
5800 C  CG  . TYR   A 764 ? 0.1843 0.2066 0.2141 0.0131  0.0106  0.0089  789  TYR   A CG  
5801 C  CD1 . TYR   A 764 ? 0.1793 0.2002 0.2079 0.0130  0.0094  0.0088  789  TYR   A CD1 
5802 C  CD2 . TYR   A 764 ? 0.1850 0.2084 0.2137 0.0123  0.0107  0.0090  789  TYR   A CD2 
5803 C  CE1 . TYR   A 764 ? 0.1760 0.1966 0.2025 0.0122  0.0084  0.0088  789  TYR   A CE1 
5804 C  CE2 . TYR   A 764 ? 0.1863 0.2096 0.2132 0.0115  0.0097  0.0092  789  TYR   A CE2 
5805 C  CZ  . TYR   A 764 ? 0.1839 0.2057 0.2096 0.0115  0.0086  0.0090  789  TYR   A CZ  
5806 O  OH  . TYR   A 764 ? 0.1912 0.2130 0.2152 0.0108  0.0078  0.0092  789  TYR   A OH  
5807 N  N   . GLN   A 765 ? 0.2256 0.2531 0.2633 0.0141  0.0120  0.0108  790  GLN   A N   
5808 C  CA  . GLN   A 765 ? 0.2489 0.2781 0.2873 0.0134  0.0116  0.0115  790  GLN   A CA  
5809 C  C   . GLN   A 765 ? 0.2573 0.2880 0.2987 0.0134  0.0103  0.0127  790  GLN   A C   
5810 O  O   . GLN   A 765 ? 0.3028 0.3342 0.3441 0.0125  0.0095  0.0131  790  GLN   A O   
5811 C  CB  . GLN   A 765 ? 0.3058 0.3361 0.3445 0.0133  0.0135  0.0114  790  GLN   A CB  
5812 C  CG  . GLN   A 765 ? 0.3872 0.4187 0.4293 0.0143  0.0146  0.0118  790  GLN   A CG  
5813 C  CD  . GLN   A 765 ? 0.4862 0.5194 0.5291 0.0140  0.0161  0.0120  790  GLN   A CD  
5814 O  OE1 . GLN   A 765 ? 0.5346 0.5688 0.5770 0.0131  0.0155  0.0124  790  GLN   A OE1 
5815 N  NE2 . GLN   A 765 ? 0.4852 0.5185 0.5293 0.0148  0.0181  0.0118  790  GLN   A NE2 
5816 N  N   . PHE   A 766 ? 0.2243 0.2554 0.2682 0.0142  0.0100  0.0132  791  PHE   A N   
5817 C  CA  . PHE   A 766 ? 0.2368 0.2697 0.2837 0.0140  0.0086  0.0144  791  PHE   A CA  
5818 C  C   . PHE   A 766 ? 0.2208 0.2525 0.2666 0.0135  0.0065  0.0146  791  PHE   A C   
5819 O  O   . PHE   A 766 ? 0.2456 0.2785 0.2930 0.0130  0.0052  0.0155  791  PHE   A O   
5820 C  CB  . PHE   A 766 ? 0.2630 0.2974 0.3136 0.0152  0.0093  0.0151  791  PHE   A CB  
5821 C  CG  . PHE   A 766 ? 0.3207 0.3560 0.3724 0.0157  0.0116  0.0150  791  PHE   A CG  
5822 C  CD1 . PHE   A 766 ? 0.3584 0.3958 0.4117 0.0152  0.0119  0.0155  791  PHE   A CD1 
5823 C  CD2 . PHE   A 766 ? 0.3586 0.3926 0.4097 0.0168  0.0135  0.0142  791  PHE   A CD2 
5824 C  CE1 . PHE   A 766 ? 0.3756 0.4138 0.4299 0.0157  0.0141  0.0154  791  PHE   A CE1 
5825 C  CE2 . PHE   A 766 ? 0.3789 0.4136 0.4309 0.0172  0.0157  0.0140  791  PHE   A CE2 
5826 C  CZ  . PHE   A 766 ? 0.3714 0.4082 0.4249 0.0167  0.0161  0.0146  791  PHE   A CZ  
5827 N  N   . SER   A 767 ? 0.1853 0.2148 0.2283 0.0137  0.0064  0.0138  792  SER   A N   
5828 C  CA  . SER   A 767 ? 0.1721 0.2005 0.2143 0.0134  0.0046  0.0140  792  SER   A CA  
5829 C  C   . SER   A 767 ? 0.1721 0.2000 0.2127 0.0122  0.0034  0.0141  792  SER   A C   
5830 O  O   . SER   A 767 ? 0.1960 0.2233 0.2345 0.0117  0.0040  0.0135  792  SER   A O   
5831 C  CB  . SER   A 767 ? 0.1968 0.2228 0.2365 0.0139  0.0049  0.0131  792  SER   A CB  
5832 O  OG  . SER   A 767 ? 0.1918 0.2167 0.2308 0.0136  0.0032  0.0134  792  SER   A OG  
5833 N  N   . LEU   A 768 ? 0.1684 0.1963 0.2096 0.0116  0.0018  0.0147  793  LEU   A N   
5834 C  CA  . LEU   A 768 ? 0.1655 0.1924 0.2048 0.0104  0.0007  0.0148  793  LEU   A CA  
5835 C  C   . LEU   A 768 ? 0.1552 0.1798 0.1921 0.0104  -0.0003 0.0144  793  LEU   A C   
5836 O  O   . LEU   A 768 ? 0.1583 0.1815 0.1933 0.0095  -0.0011 0.0144  793  LEU   A O   
5837 C  CB  . LEU   A 768 ? 0.1747 0.2030 0.2159 0.0095  -0.0004 0.0157  793  LEU   A CB  
5838 C  CG  . LEU   A 768 ? 0.1755 0.2062 0.2191 0.0094  0.0005  0.0161  793  LEU   A CG  
5839 C  CD1 . LEU   A 768 ? 0.1897 0.2221 0.2356 0.0084  -0.0007 0.0172  793  LEU   A CD1 
5840 C  CD2 . LEU   A 768 ? 0.1983 0.2281 0.2399 0.0089  0.0015  0.0156  793  LEU   A CD2 
5841 N  N   . SER   A 769 ? 0.1609 0.1848 0.1977 0.0113  -0.0001 0.0141  794  SER   A N   
5842 C  CA  . SER   A 769 ? 0.1548 0.1766 0.1895 0.0113  -0.0010 0.0139  794  SER   A CA  
5843 C  C   . SER   A 769 ? 0.1506 0.1708 0.1826 0.0114  -0.0002 0.0129  794  SER   A C   
5844 O  O   . SER   A 769 ? 0.1598 0.1801 0.1919 0.0121  0.0011  0.0124  794  SER   A O   
5845 C  CB  . SER   A 769 ? 0.1668 0.1890 0.2033 0.0122  -0.0013 0.0143  794  SER   A CB  
5846 O  OG  . SER   A 769 ? 0.1660 0.1860 0.2003 0.0125  -0.0017 0.0139  794  SER   A OG  
5847 N  N   . SER   A 770 ? 0.1504 0.1688 0.1799 0.0107  -0.0008 0.0127  795  SER   A N   
5848 C  CA  . SER   A 770 ? 0.1482 0.1653 0.1753 0.0109  0.0000  0.0119  795  SER   A CA  
5849 C  C   . SER   A 770 ? 0.1606 0.1766 0.1871 0.0115  0.0001  0.0115  795  SER   A C   
5850 O  O   . SER   A 770 ? 0.1651 0.1808 0.1906 0.0118  0.0011  0.0109  795  SER   A O   
5851 C  CB  . SER   A 770 ? 0.1703 0.1859 0.1952 0.0101  -0.0006 0.0119  795  SER   A CB  
5852 O  OG  . SER   A 770 ? 0.1813 0.1975 0.2064 0.0096  -0.0004 0.0123  795  SER   A OG  
5853 N  N   . THR   A 771 ? 0.1524 0.1678 0.1795 0.0117  -0.0009 0.0119  796  THR   A N   
5854 C  CA  . THR   A 771 ? 0.1530 0.1673 0.1797 0.0125  -0.0007 0.0116  796  THR   A CA  
5855 C  C   . THR   A 771 ? 0.1581 0.1733 0.1865 0.0133  0.0007  0.0114  796  THR   A C   
5856 O  O   . THR   A 771 ? 0.1636 0.1778 0.1907 0.0136  0.0017  0.0106  796  THR   A O   
5857 C  CB  . THR   A 771 ? 0.1603 0.1739 0.1875 0.0126  -0.0020 0.0122  796  THR   A CB  
5858 O  OG1 . THR   A 771 ? 0.1866 0.1987 0.2115 0.0118  -0.0030 0.0122  796  THR   A OG1 
5859 C  CG2 . THR   A 771 ? 0.1779 0.1906 0.2053 0.0135  -0.0016 0.0121  796  THR   A CG2 
5860 N  N   . GLU   A 772 ? 0.1515 0.1687 0.1827 0.0137  0.0008  0.0120  797  GLU   A N   
5861 C  CA  . GLU   A 772 ? 0.1578 0.1756 0.1905 0.0146  0.0023  0.0118  797  GLU   A CA  
5862 C  C   . GLU   A 772 ? 0.1591 0.1768 0.1902 0.0142  0.0038  0.0108  797  GLU   A C   
5863 O  O   . GLU   A 772 ? 0.1669 0.1837 0.1973 0.0147  0.0051  0.0101  797  GLU   A O   
5864 C  CB  . GLU   A 772 ? 0.1764 0.1967 0.2126 0.0149  0.0023  0.0128  797  GLU   A CB  
5865 C  CG  . GLU   A 772 ? 0.2005 0.2213 0.2387 0.0161  0.0040  0.0128  797  GLU   A CG  
5866 C  CD  . GLU   A 772 ? 0.2309 0.2544 0.2729 0.0164  0.0038  0.0140  797  GLU   A CD  
5867 O  OE1 . GLU   A 772 ? 0.2119 0.2370 0.2545 0.0156  0.0032  0.0143  797  GLU   A OE1 
5868 O  OE2 . GLU   A 772 ? 0.2632 0.2872 0.3077 0.0176  0.0045  0.0146  797  GLU   A OE2 
5869 N  N   . LYS   A 773 ? 0.1547 0.1731 0.1849 0.0134  0.0036  0.0108  798  LYS   A N   
5870 C  CA  . LYS   A 773 ? 0.1615 0.1802 0.1902 0.0130  0.0048  0.0101  798  LYS   A CA  
5871 C  C   . LYS   A 773 ? 0.1628 0.1795 0.1886 0.0128  0.0050  0.0093  798  LYS   A C   
5872 O  O   . LYS   A 773 ? 0.1725 0.1889 0.1971 0.0127  0.0062  0.0085  798  LYS   A O   
5873 C  CB  . LYS   A 773 ? 0.1639 0.1836 0.1923 0.0123  0.0044  0.0105  798  LYS   A CB  
5874 C  CG  . LYS   A 773 ? 0.1774 0.1991 0.2086 0.0124  0.0046  0.0111  798  LYS   A CG  
5875 C  CD  . LYS   A 773 ? 0.1925 0.2152 0.2237 0.0116  0.0043  0.0116  798  LYS   A CD  
5876 C  CE  . LYS   A 773 ? 0.2339 0.2568 0.2633 0.0113  0.0053  0.0113  798  LYS   A CE  
5877 N  NZ  . LYS   A 773 ? 0.2629 0.2868 0.2927 0.0107  0.0051  0.0119  798  LYS   A NZ  
5878 N  N   . SER   A 774 ? 0.1521 0.1677 0.1768 0.0125  0.0038  0.0094  799  SER   A N   
5879 C  CA  A SER   A 774 ? 0.1624 0.1763 0.1846 0.0122  0.0039  0.0088  799  SER   A CA  
5880 C  CA  B SER   A 774 ? 0.1630 0.1769 0.1852 0.0122  0.0039  0.0087  799  SER   A CA  
5881 C  C   . SER   A 774 ? 0.1709 0.1836 0.1931 0.0128  0.0047  0.0082  799  SER   A C   
5882 O  O   . SER   A 774 ? 0.1679 0.1796 0.1881 0.0125  0.0055  0.0074  799  SER   A O   
5883 C  CB  A SER   A 774 ? 0.1792 0.1919 0.2004 0.0120  0.0026  0.0091  799  SER   A CB  
5884 C  CB  B SER   A 774 ? 0.1812 0.1940 0.2023 0.0120  0.0026  0.0091  799  SER   A CB  
5885 O  OG  A SER   A 774 ? 0.1954 0.2088 0.2161 0.0114  0.0021  0.0095  799  SER   A OG  
5886 O  OG  B SER   A 774 ? 0.2019 0.2133 0.2210 0.0117  0.0027  0.0085  799  SER   A OG  
5887 N  N   . GLN   A 775 ? 0.1654 0.1779 0.1896 0.0137  0.0045  0.0087  800  GLN   A N   
5888 C  CA  . GLN   A 775 ? 0.1664 0.1774 0.1908 0.0144  0.0054  0.0083  800  GLN   A CA  
5889 C  C   . GLN   A 775 ? 0.1695 0.1807 0.1940 0.0146  0.0072  0.0076  800  GLN   A C   
5890 O  O   . GLN   A 775 ? 0.1781 0.1876 0.2010 0.0146  0.0084  0.0068  800  GLN   A O   
5891 C  CB  . GLN   A 775 ? 0.1626 0.1739 0.1895 0.0154  0.0046  0.0094  800  GLN   A CB  
5892 C  CG  . GLN   A 775 ? 0.1897 0.2002 0.2160 0.0152  0.0029  0.0099  800  GLN   A CG  
5893 C  CD  . GLN   A 775 ? 0.1836 0.1951 0.2126 0.0159  0.0019  0.0112  800  GLN   A CD  
5894 O  OE1 . GLN   A 775 ? 0.2007 0.2142 0.2321 0.0161  0.0019  0.0118  800  GLN   A OE1 
5895 N  NE2 . GLN   A 775 ? 0.2211 0.2313 0.2494 0.0159  0.0008  0.0116  800  GLN   A NE2 
5896 N  N   . ILE   A 776 ? 0.1665 0.1798 0.1926 0.0147  0.0076  0.0080  801  ILE   A N   
5897 C  CA  . ILE   A 776 ? 0.1630 0.1764 0.1889 0.0147  0.0095  0.0073  801  ILE   A CA  
5898 C  C   . ILE   A 776 ? 0.1606 0.1733 0.1832 0.0135  0.0100  0.0063  801  ILE   A C   
5899 O  O   . ILE   A 776 ? 0.1599 0.1712 0.1809 0.0133  0.0115  0.0053  801  ILE   A O   
5900 C  CB  . ILE   A 776 ? 0.1712 0.1870 0.1996 0.0149  0.0098  0.0080  801  ILE   A CB  
5901 C  CG1 . ILE   A 776 ? 0.1783 0.1949 0.2102 0.0162  0.0095  0.0090  801  ILE   A CG1 
5902 C  CG2 . ILE   A 776 ? 0.1957 0.2116 0.2232 0.0147  0.0118  0.0072  801  ILE   A CG2 
5903 C  CD1 . ILE   A 776 ? 0.1959 0.2152 0.2306 0.0162  0.0094  0.0099  801  ILE   A CD1 
5904 N  N   . GLU   A 777 ? 0.1580 0.1717 0.1796 0.0127  0.0088  0.0066  802  GLU   A N   
5905 C  CA  . GLU   A 777 ? 0.1608 0.1744 0.1795 0.0115  0.0092  0.0059  802  GLU   A CA  
5906 C  C   . GLU   A 777 ? 0.1756 0.1868 0.1921 0.0112  0.0095  0.0050  802  GLU   A C   
5907 O  O   . GLU   A 777 ? 0.1645 0.1750 0.1788 0.0104  0.0106  0.0041  802  GLU   A O   
5908 C  CB  . GLU   A 777 ? 0.1720 0.1868 0.1901 0.0108  0.0079  0.0065  802  GLU   A CB  
5909 C  CG  . GLU   A 777 ? 0.1694 0.1862 0.1890 0.0108  0.0079  0.0072  802  GLU   A CG  
5910 C  CD  . GLU   A 777 ? 0.1802 0.1979 0.2000 0.0106  0.0066  0.0081  802  GLU   A CD  
5911 O  OE1 . GLU   A 777 ? 0.1859 0.2028 0.2041 0.0102  0.0059  0.0081  802  GLU   A OE1 
5912 O  OE2 . GLU   A 777 ? 0.1823 0.2012 0.2037 0.0107  0.0064  0.0087  802  GLU   A OE2 
5913 N  N   . PHE   A 778 ? 0.1614 0.1714 0.1783 0.0117  0.0085  0.0053  803  PHE   A N   
5914 C  CA  . PHE   A 778 ? 0.1719 0.1796 0.1867 0.0114  0.0088  0.0046  803  PHE   A CA  
5915 C  C   . PHE   A 778 ? 0.1658 0.1718 0.1802 0.0117  0.0106  0.0037  803  PHE   A C   
5916 O  O   . PHE   A 778 ? 0.1712 0.1757 0.1831 0.0108  0.0115  0.0027  803  PHE   A O   
5917 C  CB  . PHE   A 778 ? 0.1763 0.1829 0.1919 0.0120  0.0075  0.0052  803  PHE   A CB  
5918 C  CG  . PHE   A 778 ? 0.1760 0.1804 0.1895 0.0116  0.0077  0.0045  803  PHE   A CG  
5919 C  CD1 . PHE   A 778 ? 0.2037 0.2059 0.2171 0.0122  0.0088  0.0040  803  PHE   A CD1 
5920 C  CD2 . PHE   A 778 ? 0.2041 0.2085 0.2157 0.0107  0.0069  0.0045  803  PHE   A CD2 
5921 C  CE1 . PHE   A 778 ? 0.2224 0.2222 0.2335 0.0117  0.0091  0.0033  803  PHE   A CE1 
5922 C  CE2 . PHE   A 778 ? 0.2220 0.2243 0.2316 0.0101  0.0071  0.0039  803  PHE   A CE2 
5923 C  CZ  . PHE   A 778 ? 0.2266 0.2266 0.2359 0.0106  0.0082  0.0033  803  PHE   A CZ  
5924 N  N   . ALA   A 779 ? 0.1640 0.1701 0.1811 0.0130  0.0112  0.0042  804  ALA   A N   
5925 C  CA  . ALA   A 779 ? 0.1691 0.1734 0.1861 0.0136  0.0131  0.0035  804  ALA   A CA  
5926 C  C   . ALA   A 779 ? 0.1731 0.1775 0.1883 0.0127  0.0147  0.0025  804  ALA   A C   
5927 O  O   . ALA   A 779 ? 0.1783 0.1803 0.1913 0.0123  0.0163  0.0014  804  ALA   A O   
5928 C  CB  . ALA   A 779 ? 0.1751 0.1802 0.1959 0.0153  0.0134  0.0045  804  ALA   A CB  
5929 N  N   . LEU   A 780 ? 0.1724 0.1793 0.1884 0.0123  0.0144  0.0029  805  LEU   A N   
5930 C  CA  . LEU   A 780 ? 0.1732 0.1802 0.1872 0.0114  0.0159  0.0020  805  LEU   A CA  
5931 C  C   . LEU   A 780 ? 0.1799 0.1860 0.1901 0.0096  0.0159  0.0010  805  LEU   A C   
5932 O  O   . LEU   A 780 ? 0.1839 0.1885 0.1917 0.0087  0.0174  -0.0001 805  LEU   A O   
5933 C  CB  . LEU   A 780 ? 0.1681 0.1780 0.1835 0.0112  0.0155  0.0027  805  LEU   A CB  
5934 C  CG  . LEU   A 780 ? 0.1794 0.1906 0.1986 0.0127  0.0157  0.0037  805  LEU   A CG  
5935 C  CD1 . LEU   A 780 ? 0.1983 0.2121 0.2183 0.0123  0.0154  0.0043  805  LEU   A CD1 
5936 C  CD2 . LEU   A 780 ? 0.1923 0.2020 0.2125 0.0137  0.0179  0.0032  805  LEU   A CD2 
5937 N  N   . CYS   A 781 ? 0.1789 0.1856 0.1886 0.0091  0.0141  0.0015  806  CYS   A N   
5938 C  CA  . CYS   A 781 ? 0.1837 0.1899 0.1901 0.0074  0.0138  0.0008  806  CYS   A CA  
5939 C  C   . CYS   A 781 ? 0.1840 0.1871 0.1883 0.0070  0.0147  -0.0003 806  CYS   A C   
5940 O  O   . CYS   A 781 ? 0.1798 0.1824 0.1812 0.0054  0.0146  -0.0009 806  CYS   A O   
5941 C  CB  . CYS   A 781 ? 0.1843 0.1922 0.1910 0.0071  0.0118  0.0018  806  CYS   A CB  
5942 S  SG  . CYS   A 781 ? 0.1820 0.1934 0.1899 0.0069  0.0109  0.0029  806  CYS   A SG  
5943 N  N   . ARG   A 782 ? 0.1743 0.1753 0.1802 0.0085  0.0155  -0.0003 807  ARG   A N   
5944 C  CA  . ARG   A 782 ? 0.1780 0.1756 0.1819 0.0082  0.0167  -0.0014 807  ARG   A CA  
5945 C  C   . ARG   A 782 ? 0.1972 0.1927 0.1994 0.0079  0.0191  -0.0026 807  ARG   A C   
5946 O  O   . ARG   A 782 ? 0.2084 0.2008 0.2085 0.0074  0.0204  -0.0036 807  ARG   A O   
5947 C  CB  . ARG   A 782 ? 0.1861 0.1820 0.1922 0.0100  0.0165  -0.0007 807  ARG   A CB  
5948 C  CG  . ARG   A 782 ? 0.1846 0.1816 0.1916 0.0102  0.0143  0.0003  807  ARG   A CG  
5949 C  CD  . ARG   A 782 ? 0.1993 0.1959 0.2034 0.0084  0.0136  -0.0003 807  ARG   A CD  
5950 N  NE  . ARG   A 782 ? 0.2021 0.1953 0.2040 0.0080  0.0148  -0.0013 807  ARG   A NE  
5951 C  CZ  . ARG   A 782 ? 0.1984 0.1907 0.1980 0.0066  0.0143  -0.0018 807  ARG   A CZ  
5952 N  NH1 . ARG   A 782 ? 0.1855 0.1801 0.1845 0.0056  0.0127  -0.0013 807  ARG   A NH1 
5953 N  NH2 . ARG   A 782 ? 0.2057 0.1946 0.2034 0.0063  0.0154  -0.0027 807  ARG   A NH2 
5954 N  N   . THR   A 783 ? 0.1870 0.1842 0.1898 0.0079  0.0199  -0.0026 808  THR   A N   
5955 C  CA  . THR   A 783 ? 0.1992 0.1942 0.2000 0.0074  0.0224  -0.0038 808  THR   A CA  
5956 C  C   . THR   A 783 ? 0.2134 0.2067 0.2097 0.0051  0.0230  -0.0052 808  THR   A C   
5957 O  O   . THR   A 783 ? 0.2075 0.2026 0.2023 0.0035  0.0213  -0.0051 808  THR   A O   
5958 C  CB  . THR   A 783 ? 0.2136 0.2109 0.2153 0.0075  0.0231  -0.0036 808  THR   A CB  
5959 O  OG1 . THR   A 783 ? 0.2327 0.2276 0.2326 0.0072  0.0258  -0.0048 808  THR   A OG1 
5960 C  CG2 . THR   A 783 ? 0.2207 0.2209 0.2210 0.0058  0.0216  -0.0033 808  THR   A CG2 
5961 N  N   . GLN   A 784 ? 0.2371 0.2269 0.2311 0.0047  0.0254  -0.0066 809  GLN   A N   
5962 C  CA  . GLN   A 784 ? 0.2489 0.2366 0.2381 0.0022  0.0261  -0.0081 809  GLN   A CA  
5963 C  C   . GLN   A 784 ? 0.2565 0.2442 0.2431 0.0009  0.0278  -0.0091 809  GLN   A C   
5964 O  O   . GLN   A 784 ? 0.2758 0.2615 0.2581 -0.0014 0.0288  -0.0105 809  GLN   A O   
5965 C  CB  . GLN   A 784 ? 0.3011 0.2844 0.2885 0.0022  0.0276  -0.0092 809  GLN   A CB  
5966 C  CG  . GLN   A 784 ? 0.3686 0.3523 0.3581 0.0031  0.0257  -0.0082 809  GLN   A CG  
5967 C  CD  . GLN   A 784 ? 0.4534 0.4329 0.4411 0.0030  0.0268  -0.0090 809  GLN   A CD  
5968 O  OE1 . GLN   A 784 ? 0.4825 0.4621 0.4707 0.0030  0.0252  -0.0085 809  GLN   A OE1 
5969 N  NE2 . GLN   A 784 ? 0.4347 0.4104 0.4203 0.0028  0.0295  -0.0104 809  GLN   A NE2 
5970 N  N   . ASN   A 785 ? 0.2230 0.2135 0.2122 0.0019  0.0277  -0.0082 810  ASN   A N   
5971 C  CA  . ASN   A 785 ? 0.2419 0.2329 0.2290 0.0008  0.0290  -0.0088 810  ASN   A CA  
5972 C  C   . ASN   A 785 ? 0.2573 0.2523 0.2436 -0.0009 0.0266  -0.0080 810  ASN   A C   
5973 O  O   . ASN   A 785 ? 0.2305 0.2288 0.2201 0.0003  0.0247  -0.0065 810  ASN   A O   
5974 C  CB  . ASN   A 785 ? 0.2469 0.2388 0.2377 0.0030  0.0301  -0.0081 810  ASN   A CB  
5975 C  CG  . ASN   A 785 ? 0.3106 0.3032 0.2998 0.0021  0.0315  -0.0085 810  ASN   A CG  
5976 O  OD1 . ASN   A 785 ? 0.3025 0.2975 0.2898 0.0004  0.0303  -0.0084 810  ASN   A OD1 
5977 N  ND2 . ASN   A 785 ? 0.3628 0.3536 0.3531 0.0035  0.0341  -0.0090 810  ASN   A ND2 
5978 N  N   . LYS   A 786 ? 0.2601 0.2548 0.2421 -0.0035 0.0266  -0.0089 811  LYS   A N   
5979 C  CA  . LYS   A 786 ? 0.2542 0.2528 0.2355 -0.0051 0.0243  -0.0080 811  LYS   A CA  
5980 C  C   . LYS   A 786 ? 0.2552 0.2569 0.2378 -0.0047 0.0241  -0.0070 811  LYS   A C   
5981 O  O   . LYS   A 786 ? 0.2541 0.2594 0.2382 -0.0048 0.0220  -0.0056 811  LYS   A O   
5982 C  CB  . LYS   A 786 ? 0.2882 0.2860 0.2646 -0.0081 0.0242  -0.0090 811  LYS   A CB  
5983 C  CG  . LYS   A 786 ? 0.3175 0.3129 0.2930 -0.0085 0.0239  -0.0096 811  LYS   A CG  
5984 C  CD  . LYS   A 786 ? 0.3823 0.3769 0.3527 -0.0119 0.0239  -0.0107 811  LYS   A CD  
5985 C  CE  . LYS   A 786 ? 0.4518 0.4432 0.4206 -0.0126 0.0241  -0.0117 811  LYS   A CE  
5986 N  NZ  . LYS   A 786 ? 0.5206 0.5120 0.4847 -0.0161 0.0237  -0.0125 811  LYS   A NZ  
5987 N  N   . GLU   A 787 ? 0.2547 0.2551 0.2372 -0.0041 0.0263  -0.0076 812  GLU   A N   
5988 C  CA  . GLU   A 787 ? 0.2561 0.2595 0.2402 -0.0037 0.0261  -0.0066 812  GLU   A CA  
5989 C  C   . GLU   A 787 ? 0.2286 0.2344 0.2180 -0.0012 0.0246  -0.0049 812  GLU   A C   
5990 O  O   . GLU   A 787 ? 0.2258 0.2349 0.2167 -0.0012 0.0232  -0.0036 812  GLU   A O   
5991 C  CB  . GLU   A 787 ? 0.3087 0.3100 0.2918 -0.0034 0.0290  -0.0077 812  GLU   A CB  
5992 C  CG  . GLU   A 787 ? 0.4359 0.4350 0.4133 -0.0061 0.0304  -0.0094 812  GLU   A CG  
5993 C  CD  . GLU   A 787 ? 0.5813 0.5791 0.5571 -0.0063 0.0331  -0.0102 812  GLU   A CD  
5994 O  OE1 . GLU   A 787 ? 0.6025 0.6003 0.5818 -0.0040 0.0343  -0.0097 812  GLU   A OE1 
5995 O  OE2 . GLU   A 787 ? 0.6583 0.6552 0.6292 -0.0089 0.0339  -0.0113 812  GLU   A OE2 
5996 N  N   . LYS   A 788 ? 0.2139 0.2179 0.2060 0.0007  0.0250  -0.0049 813  LYS   A N   
5997 C  CA  . LYS   A 788 ? 0.2070 0.2131 0.2038 0.0028  0.0235  -0.0034 813  LYS   A CA  
5998 C  C   . LYS   A 788 ? 0.2047 0.2128 0.2019 0.0023  0.0209  -0.0024 813  LYS   A C   
5999 O  O   . LYS   A 788 ? 0.1955 0.2063 0.1953 0.0031  0.0194  -0.0011 813  LYS   A O   
6000 C  CB  . LYS   A 788 ? 0.2243 0.2281 0.2237 0.0048  0.0245  -0.0036 813  LYS   A CB  
6001 C  CG  . LYS   A 788 ? 0.2557 0.2585 0.2561 0.0058  0.0270  -0.0039 813  LYS   A CG  
6002 C  CD  . LYS   A 788 ? 0.3223 0.3229 0.3252 0.0078  0.0282  -0.0039 813  LYS   A CD  
6003 C  CE  . LYS   A 788 ? 0.3615 0.3620 0.3667 0.0092  0.0304  -0.0038 813  LYS   A CE  
6004 N  NZ  . LYS   A 788 ? 0.4004 0.3982 0.4018 0.0081  0.0331  -0.0054 813  LYS   A NZ  
6005 N  N   . LEU   A 789 ? 0.1911 0.1979 0.1855 0.0009  0.0204  -0.0031 814  LEU   A N   
6006 C  CA  . LEU   A 789 ? 0.1878 0.1966 0.1826 0.0004  0.0181  -0.0021 814  LEU   A CA  
6007 C  C   . LEU   A 789 ? 0.1875 0.1996 0.1816 -0.0007 0.0170  -0.0012 814  LEU   A C   
6008 O  O   . LEU   A 789 ? 0.1827 0.1973 0.1790 -0.0001 0.0154  0.0002  814  LEU   A O   
6009 C  CB  . LEU   A 789 ? 0.1797 0.1865 0.1714 -0.0011 0.0180  -0.0031 814  LEU   A CB  
6010 C  CG  . LEU   A 789 ? 0.1879 0.1914 0.1804 0.0002  0.0187  -0.0037 814  LEU   A CG  
6011 C  CD1 . LEU   A 789 ? 0.1981 0.1994 0.1873 -0.0016 0.0188  -0.0048 814  LEU   A CD1 
6012 C  CD2 . LEU   A 789 ? 0.2026 0.2071 0.1988 0.0020  0.0171  -0.0024 814  LEU   A CD2 
6013 N  N   . GLN   A 790 ? 0.1888 0.2010 0.1798 -0.0024 0.0180  -0.0019 815  GLN   A N   
6014 C  CA  . GLN   A 790 ? 0.1908 0.2064 0.1812 -0.0036 0.0170  -0.0008 815  GLN   A CA  
6015 C  C   . GLN   A 790 ? 0.1912 0.2087 0.1848 -0.0019 0.0169  0.0004  815  GLN   A C   
6016 O  O   . GLN   A 790 ? 0.1957 0.2161 0.1906 -0.0019 0.0155  0.0018  815  GLN   A O   
6017 C  CB  . GLN   A 790 ? 0.1987 0.2137 0.1848 -0.0058 0.0183  -0.0019 815  GLN   A CB  
6018 C  CG  . GLN   A 790 ? 0.2224 0.2409 0.2074 -0.0072 0.0172  -0.0007 815  GLN   A CG  
6019 C  CD  . GLN   A 790 ? 0.2439 0.2647 0.2288 -0.0081 0.0151  0.0005  815  GLN   A CD  
6020 O  OE1 . GLN   A 790 ? 0.2384 0.2580 0.2213 -0.0094 0.0148  -0.0003 815  GLN   A OE1 
6021 N  NE2 . GLN   A 790 ? 0.3071 0.3312 0.2941 -0.0075 0.0137  0.0023  815  GLN   A NE2 
6022 N  N   . TRP   A 791 ? 0.1823 0.1983 0.1776 -0.0005 0.0185  -0.0002 816  TRP   A N   
6023 C  CA  . TRP   A 791 ? 0.1817 0.1993 0.1802 0.0010  0.0184  0.0009  816  TRP   A CA  
6024 C  C   . TRP   A 791 ? 0.1854 0.2044 0.1872 0.0023  0.0166  0.0022  816  TRP   A C   
6025 O  O   . TRP   A 791 ? 0.1928 0.2141 0.1964 0.0027  0.0157  0.0035  816  TRP   A O   
6026 C  CB  . TRP   A 791 ? 0.2021 0.2177 0.2019 0.0022  0.0205  0.0001  816  TRP   A CB  
6027 C  CG  . TRP   A 791 ? 0.2218 0.2393 0.2249 0.0035  0.0207  0.0011  816  TRP   A CG  
6028 C  CD1 . TRP   A 791 ? 0.2546 0.2732 0.2572 0.0031  0.0218  0.0012  816  TRP   A CD1 
6029 C  CD2 . TRP   A 791 ? 0.2341 0.2525 0.2413 0.0053  0.0197  0.0021  816  TRP   A CD2 
6030 N  NE1 . TRP   A 791 ? 0.2595 0.2796 0.2658 0.0046  0.0217  0.0022  816  TRP   A NE1 
6031 C  CE2 . TRP   A 791 ? 0.2568 0.2768 0.2659 0.0059  0.0204  0.0028  816  TRP   A CE2 
6032 C  CE3 . TRP   A 791 ? 0.2563 0.2742 0.2656 0.0064  0.0185  0.0025  816  TRP   A CE3 
6033 C  CZ2 . TRP   A 791 ? 0.2764 0.2977 0.2895 0.0073  0.0197  0.0039  816  TRP   A CZ2 
6034 C  CZ3 . TRP   A 791 ? 0.2746 0.2937 0.2876 0.0078  0.0177  0.0036  816  TRP   A CZ3 
6035 C  CH2 . TRP   A 791 ? 0.2826 0.3034 0.2975 0.0082  0.0183  0.0043  816  TRP   A CH2 
6036 N  N   . LEU   A 792 ? 0.1671 0.1843 0.1695 0.0030  0.0161  0.0019  817  LEU   A N   
6037 C  CA  . LEU   A 792 ? 0.1609 0.1791 0.1661 0.0041  0.0144  0.0030  817  LEU   A CA  
6038 C  C   . LEU   A 792 ? 0.1687 0.1892 0.1732 0.0032  0.0129  0.0041  817  LEU   A C   
6039 O  O   . LEU   A 792 ? 0.1685 0.1905 0.1751 0.0039  0.0118  0.0053  817  LEU   A O   
6040 C  CB  . LEU   A 792 ? 0.1662 0.1821 0.1717 0.0047  0.0141  0.0025  817  LEU   A CB  
6041 C  CG  . LEU   A 792 ? 0.1779 0.1919 0.1851 0.0061  0.0154  0.0019  817  LEU   A CG  
6042 C  CD1 . LEU   A 792 ? 0.1836 0.1949 0.1900 0.0063  0.0155  0.0012  817  LEU   A CD1 
6043 C  CD2 . LEU   A 792 ? 0.1827 0.1981 0.1938 0.0077  0.0147  0.0031  817  LEU   A CD2 
6044 N  N   . LEU   A 793 ? 0.1734 0.1941 0.1749 0.0015  0.0128  0.0037  818  LEU   A N   
6045 C  CA  . LEU   A 793 ? 0.1595 0.1827 0.1605 0.0007  0.0114  0.0049  818  LEU   A CA  
6046 C  C   . LEU   A 793 ? 0.1741 0.1997 0.1755 0.0005  0.0114  0.0060  818  LEU   A C   
6047 O  O   . LEU   A 793 ? 0.1798 0.2072 0.1831 0.0011  0.0104  0.0074  818  LEU   A O   
6048 C  CB  . LEU   A 793 ? 0.1668 0.1899 0.1644 -0.0013 0.0113  0.0043  818  LEU   A CB  
6049 C  CG  . LEU   A 793 ? 0.1755 0.1962 0.1724 -0.0014 0.0111  0.0034  818  LEU   A CG  
6050 C  CD1 . LEU   A 793 ? 0.1990 0.2195 0.1922 -0.0037 0.0113  0.0026  818  LEU   A CD1 
6051 C  CD2 . LEU   A 793 ? 0.2000 0.2216 0.1990 -0.0005 0.0097  0.0046  818  LEU   A CD2 
6052 N  N   . ASP   A 794 ? 0.1832 0.2086 0.1830 -0.0002 0.0127  0.0053  819  ASP   A N   
6053 C  CA  . ASP   A 794 ? 0.1920 0.2198 0.1921 -0.0005 0.0128  0.0063  819  ASP   A CA  
6054 C  C   . ASP   A 794 ? 0.1896 0.2179 0.1932 0.0013  0.0127  0.0072  819  ASP   A C   
6055 O  O   . ASP   A 794 ? 0.2026 0.2330 0.2073 0.0015  0.0120  0.0087  819  ASP   A O   
6056 C  CB  . ASP   A 794 ? 0.2033 0.2303 0.2011 -0.0015 0.0145  0.0052  819  ASP   A CB  
6057 C  CG  . ASP   A 794 ? 0.2514 0.2783 0.2451 -0.0037 0.0146  0.0045  819  ASP   A CG  
6058 O  OD1 . ASP   A 794 ? 0.2761 0.3048 0.2690 -0.0046 0.0132  0.0054  819  ASP   A OD1 
6059 O  OD2 . ASP   A 794 ? 0.2913 0.3164 0.2825 -0.0046 0.0162  0.0030  819  ASP   A OD2 
6060 N  N   . GLU   A 795 ? 0.1760 0.2023 0.1814 0.0025  0.0134  0.0065  820  GLU   A N   
6061 C  CA  . GLU   A 795 ? 0.1773 0.2042 0.1859 0.0040  0.0133  0.0072  820  GLU   A CA  
6062 C  C   . GLU   A 795 ? 0.1740 0.2014 0.1846 0.0048  0.0118  0.0083  820  GLU   A C   
6063 O  O   . GLU   A 795 ? 0.1799 0.2086 0.1922 0.0052  0.0115  0.0094  820  GLU   A O   
6064 C  CB  . GLU   A 795 ? 0.2172 0.2425 0.2274 0.0050  0.0145  0.0063  820  GLU   A CB  
6065 C  CG  . GLU   A 795 ? 0.2871 0.3120 0.2953 0.0042  0.0164  0.0054  820  GLU   A CG  
6066 C  CD  . GLU   A 795 ? 0.3768 0.4037 0.3853 0.0039  0.0168  0.0062  820  GLU   A CD  
6067 O  OE1 . GLU   A 795 ? 0.3377 0.3659 0.3489 0.0048  0.0161  0.0074  820  GLU   A OE1 
6068 O  OE2 . GLU   A 795 ? 0.4077 0.4348 0.4136 0.0027  0.0178  0.0057  820  GLU   A OE2 
6069 N  N   . SER   A 796 ? 0.1676 0.1938 0.1778 0.0048  0.0110  0.0080  821  SER   A N   
6070 C  CA  . SER   A 796 ? 0.1659 0.1924 0.1776 0.0055  0.0097  0.0090  821  SER   A CA  
6071 C  C   . SER   A 796 ? 0.1820 0.2105 0.1929 0.0048  0.0091  0.0103  821  SER   A C   
6072 O  O   . SER   A 796 ? 0.1958 0.2249 0.2082 0.0055  0.0085  0.0114  821  SER   A O   
6073 C  CB  . SER   A 796 ? 0.1649 0.1895 0.1764 0.0058  0.0092  0.0083  821  SER   A CB  
6074 O  OG  . SER   A 796 ? 0.1933 0.2176 0.2023 0.0047  0.0092  0.0078  821  SER   A OG  
6075 N  N   . PHE   A 797 ? 0.1796 0.2092 0.1882 0.0035  0.0092  0.0102  822  PHE   A N   
6076 C  CA  . PHE   A 797 ? 0.1899 0.2219 0.1980 0.0029  0.0086  0.0117  822  PHE   A CA  
6077 C  C   . PHE   A 797 ? 0.2089 0.2423 0.2183 0.0034  0.0090  0.0127  822  PHE   A C   
6078 O  O   . PHE   A 797 ? 0.2253 0.2599 0.2359 0.0038  0.0084  0.0142  822  PHE   A O   
6079 C  CB  . PHE   A 797 ? 0.2136 0.2466 0.2187 0.0012  0.0087  0.0113  822  PHE   A CB  
6080 C  CG  . PHE   A 797 ? 0.2400 0.2760 0.2444 0.0003  0.0081  0.0130  822  PHE   A CG  
6081 C  CD1 . PHE   A 797 ? 0.2671 0.3043 0.2722 0.0004  0.0071  0.0143  822  PHE   A CD1 
6082 C  CD2 . PHE   A 797 ? 0.2661 0.3036 0.2691 -0.0007 0.0086  0.0133  822  PHE   A CD2 
6083 C  CE1 . PHE   A 797 ? 0.2747 0.3150 0.2795 -0.0003 0.0065  0.0160  822  PHE   A CE1 
6084 C  CE2 . PHE   A 797 ? 0.2938 0.3343 0.2961 -0.0016 0.0080  0.0150  822  PHE   A CE2 
6085 C  CZ  . PHE   A 797 ? 0.2834 0.3254 0.2868 -0.0013 0.0069  0.0164  822  PHE   A CZ  
6086 N  N   . LYS   A 798 ? 0.1938 0.2268 0.2031 0.0033  0.0100  0.0120  823  LYS   A N   
6087 C  CA  . LYS   A 798 ? 0.1999 0.2341 0.2102 0.0036  0.0105  0.0129  823  LYS   A CA  
6088 C  C   . LYS   A 798 ? 0.2132 0.2467 0.2264 0.0049  0.0103  0.0134  823  LYS   A C   
6089 O  O   . LYS   A 798 ? 0.2290 0.2636 0.2432 0.0052  0.0102  0.0147  823  LYS   A O   
6090 C  CB  . LYS   A 798 ? 0.2296 0.2633 0.2391 0.0032  0.0119  0.0117  823  LYS   A CB  
6091 C  CG  . LYS   A 798 ? 0.2828 0.3178 0.2933 0.0034  0.0126  0.0126  823  LYS   A CG  
6092 C  CD  . LYS   A 798 ? 0.3779 0.4124 0.3871 0.0028  0.0141  0.0114  823  LYS   A CD  
6093 C  CE  . LYS   A 798 ? 0.4537 0.4894 0.4638 0.0029  0.0149  0.0122  823  LYS   A CE  
6094 N  NZ  . LYS   A 798 ? 0.4782 0.5132 0.4866 0.0023  0.0166  0.0109  823  LYS   A NZ  
6095 N  N   . GLY   A 799 ? 0.2130 0.2447 0.2274 0.0056  0.0101  0.0125  824  GLY   A N   
6096 C  CA  . GLY   A 799 ? 0.2185 0.2494 0.2353 0.0066  0.0097  0.0129  824  GLY   A CA  
6097 C  C   . GLY   A 799 ? 0.2401 0.2709 0.2588 0.0072  0.0103  0.0128  824  GLY   A C   
6098 O  O   . GLY   A 799 ? 0.2684 0.2986 0.2890 0.0077  0.0097  0.0132  824  GLY   A O   
6099 N  N   . ASP   A 800 ? 0.2457 0.2770 0.2640 0.0069  0.0113  0.0122  825  ASP   A N   
6100 C  CA  A ASP   A 800 ? 0.2604 0.2920 0.2808 0.0073  0.0121  0.0122  825  ASP   A CA  
6101 C  CA  B ASP   A 800 ? 0.2597 0.2912 0.2802 0.0073  0.0121  0.0122  825  ASP   A CA  
6102 C  C   . ASP   A 800 ? 0.2615 0.2917 0.2834 0.0080  0.0122  0.0113  825  ASP   A C   
6103 O  O   . ASP   A 800 ? 0.3038 0.3340 0.3280 0.0086  0.0118  0.0117  825  ASP   A O   
6104 C  CB  A ASP   A 800 ? 0.2887 0.3213 0.3078 0.0067  0.0134  0.0121  825  ASP   A CB  
6105 C  CB  B ASP   A 800 ? 0.2861 0.3188 0.3056 0.0068  0.0134  0.0122  825  ASP   A CB  
6106 C  CG  A ASP   A 800 ? 0.3600 0.3928 0.3808 0.0070  0.0147  0.0117  825  ASP   A CG  
6107 C  CG  B ASP   A 800 ? 0.3464 0.3806 0.3652 0.0062  0.0132  0.0135  825  ASP   A CG  
6108 O  OD1 A ASP   A 800 ? 0.3718 0.4049 0.3952 0.0076  0.0144  0.0122  825  ASP   A OD1 
6109 O  OD1 B ASP   A 800 ? 0.3656 0.4000 0.3856 0.0066  0.0124  0.0145  825  ASP   A OD1 
6110 O  OD2 A ASP   A 800 ? 0.4058 0.4385 0.4252 0.0067  0.0160  0.0109  825  ASP   A OD2 
6111 O  OD2 B ASP   A 800 ? 0.3888 0.4241 0.4059 0.0055  0.0140  0.0135  825  ASP   A OD2 
6112 N  N   . LYS   A 801 ? 0.2477 0.2770 0.2684 0.0079  0.0129  0.0102  826  LYS   A N   
6113 C  CA  . LYS   A 801 ? 0.2504 0.2785 0.2726 0.0088  0.0132  0.0095  826  LYS   A CA  
6114 C  C   . LYS   A 801 ? 0.2277 0.2545 0.2501 0.0091  0.0119  0.0094  826  LYS   A C   
6115 O  O   . LYS   A 801 ? 0.2469 0.2731 0.2713 0.0099  0.0117  0.0094  826  LYS   A O   
6116 C  CB  . LYS   A 801 ? 0.2825 0.3096 0.3032 0.0086  0.0148  0.0083  826  LYS   A CB  
6117 C  CG  . LYS   A 801 ? 0.3601 0.3882 0.3805 0.0083  0.0164  0.0082  826  LYS   A CG  
6118 C  CD  . LYS   A 801 ? 0.4389 0.4683 0.4626 0.0090  0.0167  0.0090  826  LYS   A CD  
6119 C  CE  . LYS   A 801 ? 0.4998 0.5298 0.5233 0.0088  0.0186  0.0087  826  LYS   A CE  
6120 N  NZ  . LYS   A 801 ? 0.5368 0.5681 0.5639 0.0096  0.0190  0.0095  826  LYS   A NZ  
6121 N  N   . ILE   A 802 ? 0.1890 0.2155 0.2093 0.0086  0.0112  0.0094  827  ILE   A N   
6122 C  CA  . ILE   A 802 ? 0.1678 0.1931 0.1879 0.0088  0.0100  0.0094  827  ILE   A CA  
6123 C  C   . ILE   A 802 ? 0.1643 0.1904 0.1836 0.0083  0.0092  0.0103  827  ILE   A C   
6124 O  O   . ILE   A 802 ? 0.1775 0.2047 0.1952 0.0076  0.0095  0.0105  827  ILE   A O   
6125 C  CB  . ILE   A 802 ? 0.1796 0.2034 0.1977 0.0085  0.0103  0.0083  827  ILE   A CB  
6126 C  CG1 . ILE   A 802 ? 0.2018 0.2244 0.2207 0.0091  0.0115  0.0074  827  ILE   A CG1 
6127 C  CG2 . ILE   A 802 ? 0.1979 0.2206 0.2158 0.0087  0.0090  0.0085  827  ILE   A CG2 
6128 C  CD1 . ILE   A 802 ? 0.2255 0.2464 0.2420 0.0087  0.0121  0.0063  827  ILE   A CD1 
6129 N  N   . LYS   A 803 ? 0.1517 0.1774 0.1722 0.0087  0.0082  0.0110  828  LYS   A N   
6130 C  CA  . LYS   A 803 ? 0.1513 0.1776 0.1713 0.0085  0.0077  0.0120  828  LYS   A CA  
6131 C  C   . LYS   A 803 ? 0.1542 0.1804 0.1722 0.0080  0.0073  0.0120  828  LYS   A C   
6132 O  O   . LYS   A 803 ? 0.1631 0.1881 0.1803 0.0081  0.0070  0.0112  828  LYS   A O   
6133 C  CB  . LYS   A 803 ? 0.1597 0.1850 0.1810 0.0089  0.0069  0.0125  828  LYS   A CB  
6134 C  CG  . LYS   A 803 ? 0.1577 0.1837 0.1808 0.0090  0.0071  0.0129  828  LYS   A CG  
6135 C  CD  . LYS   A 803 ? 0.1772 0.2020 0.2012 0.0091  0.0063  0.0134  828  LYS   A CD  
6136 C  CE  . LYS   A 803 ? 0.1769 0.2024 0.2024 0.0090  0.0066  0.0140  828  LYS   A CE  
6137 N  NZ  . LYS   A 803 ? 0.1868 0.2133 0.2116 0.0087  0.0073  0.0149  828  LYS   A NZ  
6138 N  N   . THR   A 804 ? 0.1536 0.1811 0.1709 0.0077  0.0073  0.0130  829  THR   A N   
6139 C  CA  . THR   A 804 ? 0.1469 0.1750 0.1627 0.0072  0.0070  0.0133  829  THR   A CA  
6140 C  C   . THR   A 804 ? 0.1454 0.1720 0.1613 0.0076  0.0063  0.0134  829  THR   A C   
6141 O  O   . THR   A 804 ? 0.1507 0.1773 0.1653 0.0072  0.0060  0.0132  829  THR   A O   
6142 C  CB  . THR   A 804 ? 0.1705 0.2006 0.1859 0.0069  0.0071  0.0147  829  THR   A CB  
6143 O  OG1 . THR   A 804 ? 0.1833 0.2146 0.1983 0.0064  0.0079  0.0145  829  THR   A OG1 
6144 C  CG2 . THR   A 804 ? 0.1781 0.2094 0.1922 0.0062  0.0067  0.0153  829  THR   A CG2 
6145 N  N   . GLN   A 805 ? 0.1406 0.1658 0.1577 0.0083  0.0060  0.0135  830  GLN   A N   
6146 C  CA  . GLN   A 805 ? 0.1436 0.1672 0.1605 0.0086  0.0054  0.0135  830  GLN   A CA  
6147 C  C   . GLN   A 805 ? 0.1444 0.1667 0.1606 0.0085  0.0051  0.0123  830  GLN   A C   
6148 O  O   . GLN   A 805 ? 0.1546 0.1758 0.1702 0.0086  0.0046  0.0122  830  GLN   A O   
6149 C  CB  . GLN   A 805 ? 0.1513 0.1735 0.1694 0.0091  0.0051  0.0137  830  GLN   A CB  
6150 C  CG  . GLN   A 805 ? 0.1591 0.1806 0.1782 0.0092  0.0049  0.0129  830  GLN   A CG  
6151 C  CD  . GLN   A 805 ? 0.1581 0.1785 0.1783 0.0094  0.0046  0.0132  830  GLN   A CD  
6152 O  OE1 . GLN   A 805 ? 0.1562 0.1758 0.1761 0.0094  0.0045  0.0139  830  GLN   A OE1 
6153 N  NE2 . GLN   A 805 ? 0.1580 0.1783 0.1794 0.0094  0.0043  0.0127  830  GLN   A NE2 
6154 N  N   . GLU   A 806 ? 0.1481 0.1706 0.1643 0.0084  0.0055  0.0114  831  GLU   A N   
6155 C  CA  . GLU   A 806 ? 0.1534 0.1746 0.1689 0.0083  0.0055  0.0103  831  GLU   A CA  
6156 C  C   . GLU   A 806 ? 0.1592 0.1810 0.1727 0.0075  0.0059  0.0099  831  GLU   A C   
6157 O  O   . GLU   A 806 ? 0.1636 0.1842 0.1762 0.0073  0.0059  0.0090  831  GLU   A O   
6158 C  CB  . GLU   A 806 ? 0.1501 0.1709 0.1666 0.0087  0.0060  0.0096  831  GLU   A CB  
6159 C  CG  . GLU   A 806 ? 0.1562 0.1765 0.1747 0.0094  0.0055  0.0100  831  GLU   A CG  
6160 C  CD  . GLU   A 806 ? 0.1947 0.2134 0.2131 0.0096  0.0046  0.0101  831  GLU   A CD  
6161 O  OE1 . GLU   A 806 ? 0.1977 0.2151 0.2160 0.0099  0.0044  0.0094  831  GLU   A OE1 
6162 O  OE2 . GLU   A 806 ? 0.2321 0.2506 0.2504 0.0096  0.0041  0.0107  831  GLU   A OE2 
6163 N  N   . PHE   A 807 ? 0.1560 0.1799 0.1690 0.0068  0.0061  0.0105  832  PHE   A N   
6164 C  CA  . PHE   A 807 ? 0.1523 0.1769 0.1632 0.0057  0.0063  0.0102  832  PHE   A CA  
6165 C  C   . PHE   A 807 ? 0.1599 0.1840 0.1698 0.0053  0.0058  0.0101  832  PHE   A C   
6166 O  O   . PHE   A 807 ? 0.1573 0.1806 0.1656 0.0045  0.0060  0.0091  832  PHE   A O   
6167 C  CB  . PHE   A 807 ? 0.1565 0.1837 0.1670 0.0051  0.0065  0.0112  832  PHE   A CB  
6168 C  CG  . PHE   A 807 ? 0.1533 0.1817 0.1616 0.0037  0.0065  0.0110  832  PHE   A CG  
6169 C  CD1 . PHE   A 807 ? 0.1765 0.2046 0.1832 0.0028  0.0073  0.0099  832  PHE   A CD1 
6170 C  CD2 . PHE   A 807 ? 0.1511 0.1807 0.1589 0.0032  0.0058  0.0119  832  PHE   A CD2 
6171 C  CE1 . PHE   A 807 ? 0.1719 0.2008 0.1761 0.0012  0.0073  0.0096  832  PHE   A CE1 
6172 C  CE2 . PHE   A 807 ? 0.1636 0.1944 0.1694 0.0017  0.0057  0.0118  832  PHE   A CE2 
6173 C  CZ  . PHE   A 807 ? 0.1671 0.1974 0.1709 0.0006  0.0064  0.0105  832  PHE   A CZ  
6174 N  N   . PRO   A 808 ? 0.1487 0.1728 0.1592 0.0058  0.0051  0.0110  833  PRO   A N   
6175 C  CA  . PRO   A 808 ? 0.1526 0.1763 0.1621 0.0053  0.0047  0.0110  833  PRO   A CA  
6176 C  C   . PRO   A 808 ? 0.1641 0.1853 0.1730 0.0054  0.0048  0.0096  833  PRO   A C   
6177 O  O   . PRO   A 808 ? 0.1736 0.1943 0.1809 0.0045  0.0048  0.0090  833  PRO   A O   
6178 C  CB  . PRO   A 808 ? 0.1735 0.1974 0.1842 0.0060  0.0043  0.0122  833  PRO   A CB  
6179 C  CG  . PRO   A 808 ? 0.1779 0.2033 0.1898 0.0065  0.0046  0.0133  833  PRO   A CG  
6180 C  CD  . PRO   A 808 ? 0.1662 0.1909 0.1783 0.0066  0.0050  0.0123  833  PRO   A CD  
6181 N  N   . GLN   A 809 ? 0.1600 0.1795 0.1700 0.0064  0.0048  0.0092  834  GLN   A N   
6182 C  CA  . GLN   A 809 ? 0.1553 0.1725 0.1650 0.0066  0.0048  0.0082  834  GLN   A CA  
6183 C  C   . GLN   A 809 ? 0.1571 0.1738 0.1657 0.0061  0.0057  0.0071  834  GLN   A C   
6184 O  O   . GLN   A 809 ? 0.1607 0.1759 0.1680 0.0057  0.0059  0.0062  834  GLN   A O   
6185 C  CB  . GLN   A 809 ? 0.1818 0.1977 0.1931 0.0078  0.0045  0.0083  834  GLN   A CB  
6186 C  CG  . GLN   A 809 ? 0.2301 0.2438 0.2411 0.0081  0.0044  0.0075  834  GLN   A CG  
6187 C  CD  . GLN   A 809 ? 0.3411 0.3538 0.3536 0.0090  0.0038  0.0079  834  GLN   A CD  
6188 O  OE1 . GLN   A 809 ? 0.3349 0.3485 0.3489 0.0094  0.0037  0.0083  834  GLN   A OE1 
6189 N  NE2 . GLN   A 809 ? 0.4184 0.4292 0.4304 0.0093  0.0033  0.0077  834  GLN   A NE2 
6190 N  N   . ILE   A 810 ? 0.1482 0.1661 0.1573 0.0061  0.0063  0.0070  835  ILE   A N   
6191 C  CA  . ILE   A 810 ? 0.1426 0.1598 0.1506 0.0056  0.0074  0.0059  835  ILE   A CA  
6192 C  C   . ILE   A 810 ? 0.1583 0.1758 0.1636 0.0040  0.0076  0.0055  835  ILE   A C   
6193 O  O   . ILE   A 810 ? 0.1614 0.1772 0.1652 0.0034  0.0083  0.0043  835  ILE   A O   
6194 C  CB  . ILE   A 810 ? 0.1618 0.1802 0.1707 0.0058  0.0080  0.0061  835  ILE   A CB  
6195 C  CG1 . ILE   A 810 ? 0.1675 0.1850 0.1789 0.0073  0.0080  0.0063  835  ILE   A CG1 
6196 C  CG2 . ILE   A 810 ? 0.1787 0.1969 0.1858 0.0049  0.0093  0.0051  835  ILE   A CG2 
6197 C  CD1 . ILE   A 810 ? 0.1828 0.2020 0.1958 0.0076  0.0084  0.0068  835  ILE   A CD1 
6198 N  N   . LEU   A 811 ? 0.1565 0.1763 0.1614 0.0032  0.0069  0.0065  836  LEU   A N   
6199 C  CA  . LEU   A 811 ? 0.1391 0.1597 0.1416 0.0015  0.0069  0.0062  836  LEU   A CA  
6200 C  C   . LEU   A 811 ? 0.1493 0.1681 0.1509 0.0012  0.0066  0.0056  836  LEU   A C   
6201 O  O   . LEU   A 811 ? 0.1604 0.1781 0.1597 -0.0001 0.0071  0.0046  836  LEU   A O   
6202 C  CB  . LEU   A 811 ? 0.1465 0.1703 0.1495 0.0011  0.0061  0.0078  836  LEU   A CB  
6203 C  CG  . LEU   A 811 ? 0.1511 0.1765 0.1520 -0.0007 0.0058  0.0080  836  LEU   A CG  
6204 C  CD1 . LEU   A 811 ? 0.1618 0.1877 0.1606 -0.0020 0.0065  0.0073  836  LEU   A CD1 
6205 C  CD2 . LEU   A 811 ? 0.1614 0.1899 0.1633 -0.0008 0.0049  0.0099  836  LEU   A CD2 
6206 N  N   . THR   A 812 ? 0.1474 0.1655 0.1504 0.0023  0.0059  0.0062  837  THR   A N   
6207 C  CA  . THR   A 812 ? 0.1478 0.1641 0.1499 0.0020  0.0057  0.0056  837  THR   A CA  
6208 C  C   . THR   A 812 ? 0.1552 0.1684 0.1566 0.0024  0.0066  0.0042  837  THR   A C   
6209 O  O   . THR   A 812 ? 0.1632 0.1748 0.1629 0.0014  0.0069  0.0033  837  THR   A O   
6210 C  CB  . THR   A 812 ? 0.1730 0.1891 0.1766 0.0031  0.0049  0.0065  837  THR   A CB  
6211 O  OG1 . THR   A 812 ? 0.2195 0.2382 0.2235 0.0026  0.0044  0.0079  837  THR   A OG1 
6212 C  CG2 . THR   A 812 ? 0.1985 0.2123 0.2012 0.0030  0.0048  0.0060  837  THR   A CG2 
6213 N  N   . LEU   A 813 ? 0.1501 0.1625 0.1532 0.0037  0.0070  0.0041  838  LEU   A N   
6214 C  CA  . LEU   A 813 ? 0.1449 0.1546 0.1478 0.0042  0.0079  0.0030  838  LEU   A CA  
6215 C  C   . LEU   A 813 ? 0.1520 0.1608 0.1525 0.0029  0.0092  0.0018  838  LEU   A C   
6216 O  O   . LEU   A 813 ? 0.1659 0.1722 0.1650 0.0026  0.0100  0.0008  838  LEU   A O   
6217 C  CB  . LEU   A 813 ? 0.1489 0.1585 0.1542 0.0058  0.0081  0.0033  838  LEU   A CB  
6218 C  CG  . LEU   A 813 ? 0.1703 0.1800 0.1776 0.0069  0.0069  0.0043  838  LEU   A CG  
6219 C  CD1 . LEU   A 813 ? 0.1833 0.1934 0.1930 0.0081  0.0071  0.0047  838  LEU   A CD1 
6220 C  CD2 . LEU   A 813 ? 0.1873 0.1947 0.1942 0.0073  0.0066  0.0041  838  LEU   A CD2 
6221 N  N   . ILE   A 814 ? 0.1475 0.1584 0.1474 0.0021  0.0094  0.0020  839  ILE   A N   
6222 C  CA  . ILE   A 814 ? 0.1535 0.1635 0.1506 0.0006  0.0106  0.0008  839  ILE   A CA  
6223 C  C   . ILE   A 814 ? 0.1648 0.1748 0.1593 -0.0013 0.0103  0.0004  839  ILE   A C   
6224 O  O   . ILE   A 814 ? 0.1766 0.1844 0.1687 -0.0024 0.0113  -0.0009 839  ILE   A O   
6225 C  CB  . ILE   A 814 ? 0.1631 0.1752 0.1603 0.0003  0.0111  0.0011  839  ILE   A CB  
6226 C  CG1 . ILE   A 814 ? 0.1611 0.1728 0.1609 0.0021  0.0117  0.0012  839  ILE   A CG1 
6227 C  CG2 . ILE   A 814 ? 0.1781 0.1896 0.1719 -0.0017 0.0122  -0.0001 839  ILE   A CG2 
6228 C  CD1 . ILE   A 814 ? 0.1821 0.1957 0.1823 0.0020  0.0122  0.0016  839  ILE   A CD1 
6229 N  N   . GLY   A 815 ? 0.1605 0.1728 0.1557 -0.0016 0.0088  0.0016  840  GLY   A N   
6230 C  CA  . GLY   A 815 ? 0.1600 0.1725 0.1532 -0.0033 0.0083  0.0015  840  GLY   A CA  
6231 C  C   . GLY   A 815 ? 0.1695 0.1788 0.1620 -0.0032 0.0086  0.0006  840  GLY   A C   
6232 O  O   . GLY   A 815 ? 0.1732 0.1820 0.1637 -0.0048 0.0086  0.0001  840  GLY   A O   
6233 N  N   . ARG   A 816 ? 0.1653 0.1725 0.1596 -0.0012 0.0089  0.0005  841  ARG   A N   
6234 C  CA  . ARG   A 816 ? 0.1718 0.1759 0.1657 -0.0009 0.0093  -0.0002 841  ARG   A CA  
6235 C  C   . ARG   A 816 ? 0.2040 0.2049 0.1969 -0.0005 0.0110  -0.0015 841  ARG   A C   
6236 O  O   . ARG   A 816 ? 0.2234 0.2214 0.2157 -0.0003 0.0115  -0.0022 841  ARG   A O   
6237 C  CB  . ARG   A 816 ? 0.1786 0.1825 0.1750 0.0010  0.0083  0.0008  841  ARG   A CB  
6238 C  CG  . ARG   A 816 ? 0.1900 0.1962 0.1868 0.0005  0.0070  0.0019  841  ARG   A CG  
6239 C  CD  . ARG   A 816 ? 0.2226 0.2287 0.2217 0.0023  0.0062  0.0029  841  ARG   A CD  
6240 N  NE  . ARG   A 816 ? 0.2323 0.2398 0.2316 0.0019  0.0053  0.0038  841  ARG   A NE  
6241 C  CZ  . ARG   A 816 ? 0.3229 0.3300 0.3235 0.0030  0.0046  0.0045  841  ARG   A CZ  
6242 N  NH1 . ARG   A 816 ? 0.3434 0.3515 0.3440 0.0027  0.0041  0.0053  841  ARG   A NH1 
6243 N  NH2 . ARG   A 816 ? 0.3285 0.3339 0.3302 0.0044  0.0046  0.0045  841  ARG   A NH2 
6244 N  N   . ASN   A 817 ? 0.1781 0.1794 0.1708 -0.0006 0.0119  -0.0020 842  ASN   A N   
6245 C  CA  . ASN   A 817 ? 0.1750 0.1732 0.1669 -0.0002 0.0138  -0.0032 842  ASN   A CA  
6246 C  C   . ASN   A 817 ? 0.2128 0.2087 0.2008 -0.0023 0.0148  -0.0046 842  ASN   A C   
6247 O  O   . ASN   A 817 ? 0.2398 0.2375 0.2258 -0.0044 0.0144  -0.0047 842  ASN   A O   
6248 C  CB  . ASN   A 817 ? 0.1912 0.1910 0.1838 0.0002  0.0145  -0.0031 842  ASN   A CB  
6249 C  CG  . ASN   A 817 ? 0.1986 0.1955 0.1905 0.0006  0.0167  -0.0043 842  ASN   A CG  
6250 O  OD1 . ASN   A 817 ? 0.2390 0.2335 0.2278 -0.0008 0.0180  -0.0056 842  ASN   A OD1 
6251 N  ND2 . ASN   A 817 ? 0.1941 0.1916 0.1888 0.0025  0.0171  -0.0037 842  ASN   A ND2 
6252 N  N   . PRO   A 818 ? 0.2229 0.2150 0.2101 -0.0019 0.0161  -0.0056 843  PRO   A N   
6253 C  CA  . PRO   A 818 ? 0.2480 0.2374 0.2313 -0.0041 0.0171  -0.0070 843  PRO   A CA  
6254 C  C   . PRO   A 818 ? 0.2920 0.2809 0.2722 -0.0060 0.0185  -0.0082 843  PRO   A C   
6255 O  O   . PRO   A 818 ? 0.3116 0.2991 0.2883 -0.0084 0.0189  -0.0092 843  PRO   A O   
6256 C  CB  . PRO   A 818 ? 0.2696 0.2548 0.2532 -0.0028 0.0184  -0.0076 843  PRO   A CB  
6257 C  CG  . PRO   A 818 ? 0.2647 0.2502 0.2519 -0.0001 0.0187  -0.0067 843  PRO   A CG  
6258 C  CD  . PRO   A 818 ? 0.2315 0.2214 0.2212 0.0005  0.0167  -0.0053 843  PRO   A CD  
6259 N  N   . VAL   A 819 ? 0.2910 0.2805 0.2721 -0.0051 0.0194  -0.0082 844  VAL   A N   
6260 C  CA  . VAL   A 819 ? 0.3313 0.3202 0.3090 -0.0071 0.0208  -0.0094 844  VAL   A CA  
6261 C  C   . VAL   A 819 ? 0.3261 0.3194 0.3039 -0.0081 0.0194  -0.0085 844  VAL   A C   
6262 O  O   . VAL   A 819 ? 0.3414 0.3352 0.3157 -0.0107 0.0195  -0.0092 844  VAL   A O   
6263 C  CB  . VAL   A 819 ? 0.3695 0.3553 0.3471 -0.0059 0.0235  -0.0105 844  VAL   A CB  
6264 C  CG1 . VAL   A 819 ? 0.3873 0.3687 0.3652 -0.0046 0.0249  -0.0111 844  VAL   A CG1 
6265 C  CG2 . VAL   A 819 ? 0.3978 0.3861 0.3789 -0.0039 0.0233  -0.0093 844  VAL   A CG2 
6266 N  N   . GLY   A 820 ? 0.3033 0.2997 0.2847 -0.0063 0.0181  -0.0070 845  GLY   A N   
6267 C  CA  . GLY   A 820 ? 0.3038 0.3042 0.2856 -0.0070 0.0170  -0.0060 845  GLY   A CA  
6268 C  C   . GLY   A 820 ? 0.2709 0.2749 0.2536 -0.0076 0.0147  -0.0045 845  GLY   A C   
6269 O  O   . GLY   A 820 ? 0.2641 0.2716 0.2474 -0.0080 0.0138  -0.0035 845  GLY   A O   
6270 N  N   . TYR   A 821 ? 0.2313 0.2345 0.2139 -0.0079 0.0139  -0.0044 846  TYR   A N   
6271 C  CA  . TYR   A 821 ? 0.2188 0.2255 0.2026 -0.0083 0.0119  -0.0029 846  TYR   A CA  
6272 C  C   . TYR   A 821 ? 0.2282 0.2384 0.2103 -0.0106 0.0111  -0.0023 846  TYR   A C   
6273 O  O   . TYR   A 821 ? 0.2388 0.2525 0.2229 -0.0101 0.0097  -0.0007 846  TYR   A O   
6274 C  CB  . TYR   A 821 ? 0.2204 0.2258 0.2040 -0.0086 0.0113  -0.0030 846  TYR   A CB  
6275 C  CG  . TYR   A 821 ? 0.2056 0.2089 0.1853 -0.0112 0.0121  -0.0044 846  TYR   A CG  
6276 C  CD1 . TYR   A 821 ? 0.2147 0.2206 0.1925 -0.0137 0.0110  -0.0040 846  TYR   A CD1 
6277 C  CD2 . TYR   A 821 ? 0.2126 0.2114 0.1906 -0.0112 0.0138  -0.0061 846  TYR   A CD2 
6278 C  CE1 . TYR   A 821 ? 0.2151 0.2190 0.1890 -0.0164 0.0116  -0.0054 846  TYR   A CE1 
6279 C  CE2 . TYR   A 821 ? 0.2131 0.2096 0.1872 -0.0137 0.0147  -0.0075 846  TYR   A CE2 
6280 C  CZ  . TYR   A 821 ? 0.2213 0.2204 0.1932 -0.0164 0.0135  -0.0072 846  TYR   A CZ  
6281 O  OH  . TYR   A 821 ? 0.2491 0.2461 0.2170 -0.0192 0.0142  -0.0086 846  TYR   A OH  
6282 N  N   . PRO   A 822 ? 0.2032 0.2126 0.1815 -0.0130 0.0119  -0.0035 847  PRO   A N   
6283 C  CA  . PRO   A 822 ? 0.1954 0.2086 0.1722 -0.0151 0.0108  -0.0026 847  PRO   A CA  
6284 C  C   . PRO   A 822 ? 0.2166 0.2327 0.1953 -0.0140 0.0105  -0.0013 847  PRO   A C   
6285 O  O   . PRO   A 822 ? 0.2312 0.2514 0.2103 -0.0150 0.0092  0.0001  847  PRO   A O   
6286 C  CB  . PRO   A 822 ? 0.2267 0.2377 0.1987 -0.0179 0.0121  -0.0044 847  PRO   A CB  
6287 C  CG  . PRO   A 822 ? 0.2267 0.2328 0.1977 -0.0175 0.0135  -0.0061 847  PRO   A CG  
6288 C  CD  . PRO   A 822 ? 0.2097 0.2148 0.1848 -0.0141 0.0138  -0.0056 847  PRO   A CD  
6289 N  N   . LEU   A 823 ? 0.1966 0.2110 0.1767 -0.0121 0.0117  -0.0019 848  LEU   A N   
6290 C  CA  . LEU   A 823 ? 0.1943 0.2111 0.1761 -0.0112 0.0116  -0.0009 848  LEU   A CA  
6291 C  C   . LEU   A 823 ? 0.1834 0.2034 0.1687 -0.0097 0.0100  0.0012  848  LEU   A C   
6292 O  O   . LEU   A 823 ? 0.1877 0.2108 0.1739 -0.0097 0.0095  0.0025  848  LEU   A O   
6293 C  CB  . LEU   A 823 ? 0.1978 0.2120 0.1808 -0.0093 0.0133  -0.0017 848  LEU   A CB  
6294 C  CG  . LEU   A 823 ? 0.2451 0.2559 0.2248 -0.0104 0.0154  -0.0037 848  LEU   A CG  
6295 C  CD1 . LEU   A 823 ? 0.2578 0.2665 0.2395 -0.0082 0.0170  -0.0042 848  LEU   A CD1 
6296 C  CD2 . LEU   A 823 ? 0.2761 0.2885 0.2524 -0.0128 0.0156  -0.0039 848  LEU   A CD2 
6297 N  N   . ALA   A 824 ? 0.1730 0.1922 0.1603 -0.0084 0.0094  0.0016  849  ALA   A N   
6298 C  CA  . ALA   A 824 ? 0.1692 0.1909 0.1598 -0.0068 0.0081  0.0034  849  ALA   A CA  
6299 C  C   . ALA   A 824 ? 0.1759 0.2013 0.1662 -0.0082 0.0067  0.0049  849  ALA   A C   
6300 O  O   . ALA   A 824 ? 0.1669 0.1952 0.1587 -0.0078 0.0061  0.0065  849  ALA   A O   
6301 C  CB  . ALA   A 824 ? 0.1813 0.2009 0.1739 -0.0051 0.0079  0.0032  849  ALA   A CB  
6302 N  N   . TRP   A 825 ? 0.1786 0.2038 0.1670 -0.0099 0.0063  0.0045  850  TRP   A N   
6303 C  CA  . TRP   A 825 ? 0.1711 0.2002 0.1593 -0.0115 0.0050  0.0061  850  TRP   A CA  
6304 C  C   . TRP   A 825 ? 0.1741 0.2058 0.1607 -0.0130 0.0050  0.0066  850  TRP   A C   
6305 O  O   . TRP   A 825 ? 0.1710 0.2065 0.1591 -0.0130 0.0040  0.0086  850  TRP   A O   
6306 C  CB  . TRP   A 825 ? 0.1843 0.2122 0.1703 -0.0133 0.0048  0.0052  850  TRP   A CB  
6307 C  CG  . TRP   A 825 ? 0.1741 0.2057 0.1591 -0.0156 0.0036  0.0064  850  TRP   A CG  
6308 C  CD1 . TRP   A 825 ? 0.1852 0.2165 0.1669 -0.0184 0.0036  0.0055  850  TRP   A CD1 
6309 C  CD2 . TRP   A 825 ? 0.1670 0.2030 0.1545 -0.0153 0.0023  0.0089  850  TRP   A CD2 
6310 N  NE1 . TRP   A 825 ? 0.1757 0.2112 0.1577 -0.0200 0.0022  0.0072  850  TRP   A NE1 
6311 C  CE2 . TRP   A 825 ? 0.1645 0.2030 0.1501 -0.0180 0.0014  0.0094  850  TRP   A CE2 
6312 C  CE3 . TRP   A 825 ? 0.1691 0.2071 0.1600 -0.0131 0.0019  0.0108  850  TRP   A CE3 
6313 C  CZ2 . TRP   A 825 ? 0.1618 0.2051 0.1494 -0.0184 0.0001  0.0119  850  TRP   A CZ2 
6314 C  CZ3 . TRP   A 825 ? 0.1731 0.2154 0.1658 -0.0134 0.0008  0.0131  850  TRP   A CZ3 
6315 C  CH2 . TRP   A 825 ? 0.1691 0.2142 0.1603 -0.0159 -0.0001 0.0138  850  TRP   A CH2 
6316 N  N   . GLN   A 826 ? 0.1812 0.2107 0.1649 -0.0141 0.0061  0.0049  851  GLN   A N   
6317 C  CA  . GLN   A 826 ? 0.1957 0.2275 0.1777 -0.0156 0.0062  0.0054  851  GLN   A CA  
6318 C  C   . GLN   A 826 ? 0.1855 0.2194 0.1703 -0.0136 0.0060  0.0069  851  GLN   A C   
6319 O  O   . GLN   A 826 ? 0.1829 0.2204 0.1679 -0.0144 0.0051  0.0086  851  GLN   A O   
6320 C  CB  . GLN   A 826 ? 0.2390 0.2673 0.2174 -0.0168 0.0079  0.0030  851  GLN   A CB  
6321 C  CG  . GLN   A 826 ? 0.2679 0.2977 0.2438 -0.0185 0.0081  0.0031  851  GLN   A CG  
6322 C  CD  . GLN   A 826 ? 0.3551 0.3805 0.3276 -0.0194 0.0101  0.0005  851  GLN   A CD  
6323 O  OE1 . GLN   A 826 ? 0.4293 0.4524 0.3989 -0.0212 0.0105  -0.0009 851  GLN   A OE1 
6324 N  NE2 . GLN   A 826 ? 0.3469 0.3707 0.3199 -0.0180 0.0116  -0.0001 851  GLN   A NE2 
6325 N  N   . PHE   A 827 ? 0.1808 0.2124 0.1679 -0.0112 0.0068  0.0064  852  PHE   A N   
6326 C  CA  . PHE   A 827 ? 0.1693 0.2024 0.1590 -0.0095 0.0068  0.0077  852  PHE   A CA  
6327 C  C   . PHE   A 827 ? 0.1629 0.1993 0.1553 -0.0087 0.0054  0.0100  852  PHE   A C   
6328 O  O   . PHE   A 827 ? 0.1675 0.2066 0.1608 -0.0084 0.0050  0.0116  852  PHE   A O   
6329 C  CB  . PHE   A 827 ? 0.1715 0.2015 0.1632 -0.0072 0.0077  0.0067  852  PHE   A CB  
6330 C  CG  . PHE   A 827 ? 0.1716 0.2026 0.1654 -0.0057 0.0080  0.0076  852  PHE   A CG  
6331 C  CD1 . PHE   A 827 ? 0.1840 0.2168 0.1808 -0.0042 0.0072  0.0093  852  PHE   A CD1 
6332 C  CD2 . PHE   A 827 ? 0.1924 0.2227 0.1851 -0.0060 0.0093  0.0067  852  PHE   A CD2 
6333 C  CE1 . PHE   A 827 ? 0.1955 0.2291 0.1941 -0.0031 0.0075  0.0101  852  PHE   A CE1 
6334 C  CE2 . PHE   A 827 ? 0.1982 0.2295 0.1928 -0.0048 0.0096  0.0076  852  PHE   A CE2 
6335 C  CZ  . PHE   A 827 ? 0.1929 0.2258 0.1905 -0.0033 0.0086  0.0092  852  PHE   A CZ  
6336 N  N   . LEU   A 828 ? 0.1542 0.1901 0.1477 -0.0082 0.0048  0.0102  853  LEU   A N   
6337 C  CA  . LEU   A 828 ? 0.1666 0.2052 0.1626 -0.0074 0.0037  0.0124  853  LEU   A CA  
6338 C  C   . LEU   A 828 ? 0.1784 0.2213 0.1736 -0.0091 0.0028  0.0141  853  LEU   A C   
6339 O  O   . LEU   A 828 ? 0.1924 0.2381 0.1895 -0.0083 0.0023  0.0162  853  LEU   A O   
6340 C  CB  . LEU   A 828 ? 0.1710 0.2083 0.1679 -0.0069 0.0033  0.0122  853  LEU   A CB  
6341 C  CG  . LEU   A 828 ? 0.1863 0.2260 0.1858 -0.0058 0.0025  0.0143  853  LEU   A CG  
6342 C  CD1 . LEU   A 828 ? 0.2102 0.2498 0.2123 -0.0036 0.0028  0.0153  853  LEU   A CD1 
6343 C  CD2 . LEU   A 828 ? 0.2087 0.2467 0.2087 -0.0054 0.0024  0.0138  853  LEU   A CD2 
6344 N  N   . ARG   A 829 ? 0.1816 0.2249 0.1737 -0.0116 0.0026  0.0133  854  ARG   A N   
6345 C  CA  . ARG   A 829 ? 0.1789 0.2264 0.1700 -0.0136 0.0015  0.0150  854  ARG   A CA  
6346 C  C   . ARG   A 829 ? 0.1975 0.2467 0.1880 -0.0138 0.0017  0.0158  854  ARG   A C   
6347 O  O   . ARG   A 829 ? 0.2176 0.2707 0.2098 -0.0136 0.0009  0.0182  854  ARG   A O   
6348 C  CB  . ARG   A 829 ? 0.1865 0.2337 0.1739 -0.0165 0.0013  0.0137  854  ARG   A CB  
6349 C  CG  . ARG   A 829 ? 0.2047 0.2508 0.1924 -0.0169 0.0009  0.0132  854  ARG   A CG  
6350 C  CD  . ARG   A 829 ? 0.2037 0.2506 0.1878 -0.0202 0.0004  0.0125  854  ARG   A CD  
6351 N  NE  . ARG   A 829 ? 0.2508 0.2957 0.2309 -0.0221 0.0013  0.0106  854  ARG   A NE  
6352 C  CZ  . ARG   A 829 ? 0.2476 0.2878 0.2254 -0.0224 0.0026  0.0080  854  ARG   A CZ  
6353 N  NH1 . ARG   A 829 ? 0.2717 0.3088 0.2507 -0.0210 0.0031  0.0070  854  ARG   A NH1 
6354 N  NH2 . ARG   A 829 ? 0.2866 0.3250 0.2607 -0.0240 0.0036  0.0065  854  ARG   A NH2 
6355 N  N   . LYS   A 830 ? 0.1939 0.2403 0.1826 -0.0139 0.0029  0.0139  855  LYS   A N   
6356 C  CA  . LYS   A 830 ? 0.1990 0.2468 0.1867 -0.0143 0.0032  0.0145  855  LYS   A CA  
6357 C  C   . LYS   A 830 ? 0.2125 0.2615 0.2037 -0.0119 0.0033  0.0162  855  LYS   A C   
6358 O  O   . LYS   A 830 ? 0.2164 0.2682 0.2076 -0.0122 0.0030  0.0178  855  LYS   A O   
6359 C  CB  . LYS   A 830 ? 0.2077 0.2519 0.1926 -0.0149 0.0048  0.0119  855  LYS   A CB  
6360 C  CG  . LYS   A 830 ? 0.3018 0.3469 0.2858 -0.0151 0.0054  0.0122  855  LYS   A CG  
6361 C  CD  . LYS   A 830 ? 0.3842 0.4259 0.3648 -0.0162 0.0071  0.0097  855  LYS   A CD  
6362 C  CE  . LYS   A 830 ? 0.4120 0.4539 0.3923 -0.0158 0.0081  0.0098  855  LYS   A CE  
6363 N  NZ  . LYS   A 830 ? 0.4678 0.5108 0.4522 -0.0132 0.0079  0.0114  855  LYS   A NZ  
6364 N  N   . ASN   A 831 ? 0.1896 0.2364 0.1835 -0.0096 0.0037  0.0158  856  ASN   A N   
6365 C  CA  . ASN   A 831 ? 0.1633 0.2104 0.1602 -0.0073 0.0040  0.0170  856  ASN   A CA  
6366 C  C   . ASN   A 831 ? 0.1619 0.2105 0.1618 -0.0059 0.0032  0.0189  856  ASN   A C   
6367 O  O   . ASN   A 831 ? 0.1699 0.2179 0.1722 -0.0040 0.0035  0.0197  856  ASN   A O   
6368 C  CB  . ASN   A 831 ? 0.1683 0.2115 0.1659 -0.0058 0.0051  0.0151  856  ASN   A CB  
6369 C  CG  . ASN   A 831 ? 0.2030 0.2450 0.1979 -0.0070 0.0061  0.0136  856  ASN   A CG  
6370 O  OD1 . ASN   A 831 ? 0.2281 0.2715 0.2227 -0.0072 0.0065  0.0143  856  ASN   A OD1 
6371 N  ND2 . ASN   A 831 ? 0.2022 0.2416 0.1949 -0.0079 0.0067  0.0115  856  ASN   A ND2 
6372 N  N   . TRP   A 832 ? 0.1632 0.2139 0.1629 -0.0070 0.0022  0.0198  857  TRP   A N   
6373 C  CA  . TRP   A 832 ? 0.1675 0.2194 0.1699 -0.0057 0.0017  0.0216  857  TRP   A CA  
6374 C  C   . TRP   A 832 ? 0.1818 0.2356 0.1868 -0.0040 0.0018  0.0239  857  TRP   A C   
6375 O  O   . TRP   A 832 ? 0.1679 0.2202 0.1753 -0.0021 0.0022  0.0243  857  TRP   A O   
6376 C  CB  . TRP   A 832 ? 0.1718 0.2268 0.1735 -0.0074 0.0007  0.0227  857  TRP   A CB  
6377 C  CG  . TRP   A 832 ? 0.1626 0.2192 0.1673 -0.0061 0.0002  0.0246  857  TRP   A CG  
6378 C  CD1 . TRP   A 832 ? 0.1650 0.2254 0.1716 -0.0057 -0.0003 0.0275  857  TRP   A CD1 
6379 C  CD2 . TRP   A 832 ? 0.1487 0.2029 0.1546 -0.0049 0.0005  0.0240  857  TRP   A CD2 
6380 N  NE1 . TRP   A 832 ? 0.1605 0.2211 0.1697 -0.0043 -0.0002 0.0286  857  TRP   A NE1 
6381 C  CE2 . TRP   A 832 ? 0.1555 0.2122 0.1641 -0.0039 0.0002  0.0264  857  TRP   A CE2 
6382 C  CE3 . TRP   A 832 ? 0.1553 0.2055 0.1604 -0.0046 0.0010  0.0216  857  TRP   A CE3 
6383 C  CZ2 . TRP   A 832 ? 0.1605 0.2157 0.1708 -0.0026 0.0005  0.0265  857  TRP   A CZ2 
6384 C  CZ3 . TRP   A 832 ? 0.1590 0.2077 0.1656 -0.0033 0.0011  0.0217  857  TRP   A CZ3 
6385 C  CH2 . TRP   A 832 ? 0.1616 0.2128 0.1707 -0.0025 0.0008  0.0240  857  TRP   A CH2 
6386 N  N   . ASN   A 833 ? 0.1769 0.2338 0.1814 -0.0049 0.0015  0.0254  858  ASN   A N   
6387 C  CA  . ASN   A 833 ? 0.1835 0.2421 0.1904 -0.0033 0.0017  0.0278  858  ASN   A CA  
6388 C  C   . ASN   A 833 ? 0.1788 0.2344 0.1871 -0.0014 0.0027  0.0271  858  ASN   A C   
6389 O  O   . ASN   A 833 ? 0.1811 0.2364 0.1919 0.0004  0.0030  0.0284  858  ASN   A O   
6390 C  CB  . ASN   A 833 ? 0.1914 0.2538 0.1974 -0.0046 0.0012  0.0296  858  ASN   A CB  
6391 C  CG  . ASN   A 833 ? 0.2220 0.2884 0.2278 -0.0061 0.0000  0.0314  858  ASN   A CG  
6392 O  OD1 . ASN   A 833 ? 0.2246 0.2912 0.2313 -0.0062 -0.0005 0.0315  858  ASN   A OD1 
6393 N  ND2 . ASN   A 833 ? 0.2586 0.3286 0.2633 -0.0076 -0.0007 0.0330  858  ASN   A ND2 
6394 N  N   . LYS   A 834 ? 0.1785 0.2318 0.1852 -0.0019 0.0033  0.0250  859  LYS   A N   
6395 C  CA  . LYS   A 834 ? 0.1819 0.2325 0.1899 -0.0002 0.0042  0.0243  859  LYS   A CA  
6396 C  C   . LYS   A 834 ? 0.1737 0.2213 0.1831 0.0011  0.0044  0.0232  859  LYS   A C   
6397 O  O   . LYS   A 834 ? 0.1851 0.2313 0.1963 0.0027  0.0049  0.0236  859  LYS   A O   
6398 C  CB  . LYS   A 834 ? 0.2067 0.2560 0.2127 -0.0011 0.0049  0.0225  859  LYS   A CB  
6399 C  CG  . LYS   A 834 ? 0.2809 0.3329 0.2858 -0.0020 0.0049  0.0238  859  LYS   A CG  
6400 C  CD  . LYS   A 834 ? 0.3689 0.4208 0.3760 -0.0005 0.0055  0.0250  859  LYS   A CD  
6401 C  CE  . LYS   A 834 ? 0.4311 0.4856 0.4375 -0.0011 0.0056  0.0267  859  LYS   A CE  
6402 N  NZ  . LYS   A 834 ? 0.4682 0.5220 0.4768 0.0005  0.0063  0.0277  859  LYS   A NZ  
6403 N  N   . LEU   A 835 ? 0.1662 0.2128 0.1745 0.0004  0.0040  0.0220  860  LEU   A N   
6404 C  CA  . LEU   A 835 ? 0.1658 0.2097 0.1752 0.0015  0.0041  0.0210  860  LEU   A CA  
6405 C  C   . LEU   A 835 ? 0.1670 0.2118 0.1785 0.0027  0.0040  0.0229  860  LEU   A C   
6406 O  O   . LEU   A 835 ? 0.1535 0.1960 0.1664 0.0042  0.0044  0.0228  860  LEU   A O   
6407 C  CB  . LEU   A 835 ? 0.1777 0.2204 0.1853 0.0004  0.0039  0.0193  860  LEU   A CB  
6408 C  CG  . LEU   A 835 ? 0.1991 0.2396 0.2049 -0.0002 0.0044  0.0171  860  LEU   A CG  
6409 C  CD1 . LEU   A 835 ? 0.2109 0.2504 0.2146 -0.0016 0.0043  0.0156  860  LEU   A CD1 
6410 C  CD2 . LEU   A 835 ? 0.2075 0.2452 0.2148 0.0014  0.0050  0.0162  860  LEU   A CD2 
6411 N  N   . VAL   A 836 ? 0.1646 0.2127 0.1764 0.0021  0.0035  0.0248  861  VAL   A N   
6412 C  CA  . VAL   A 836 ? 0.1747 0.2239 0.1887 0.0034  0.0035  0.0269  861  VAL   A CA  
6413 C  C   . VAL   A 836 ? 0.1730 0.2218 0.1886 0.0048  0.0043  0.0282  861  VAL   A C   
6414 O  O   . VAL   A 836 ? 0.1685 0.2155 0.1857 0.0063  0.0049  0.0287  861  VAL   A O   
6415 C  CB  . VAL   A 836 ? 0.2175 0.2709 0.2316 0.0023  0.0028  0.0289  861  VAL   A CB  
6416 C  CG1 . VAL   A 836 ? 0.2351 0.2904 0.2519 0.0038  0.0031  0.0317  861  VAL   A CG1 
6417 C  CG2 . VAL   A 836 ? 0.2377 0.2910 0.2507 0.0011  0.0021  0.0278  861  VAL   A CG2 
6418 N  N   . GLN   A 837 ? 0.1679 0.2180 0.1829 0.0043  0.0044  0.0286  862  GLN   A N   
6419 C  CA  . GLN   A 837 ? 0.1671 0.2168 0.1836 0.0056  0.0051  0.0297  862  GLN   A CA  
6420 C  C   . GLN   A 837 ? 0.1813 0.2269 0.1982 0.0067  0.0058  0.0280  862  GLN   A C   
6421 O  O   . GLN   A 837 ? 0.1990 0.2432 0.2173 0.0080  0.0065  0.0289  862  GLN   A O   
6422 C  CB  . GLN   A 837 ? 0.2129 0.2646 0.2284 0.0047  0.0051  0.0302  862  GLN   A CB  
6423 C  CG  . GLN   A 837 ? 0.3072 0.3581 0.3240 0.0059  0.0060  0.0312  862  GLN   A CG  
6424 C  CD  . GLN   A 837 ? 0.4294 0.4814 0.4484 0.0073  0.0064  0.0339  862  GLN   A CD  
6425 O  OE1 . GLN   A 837 ? 0.4682 0.5231 0.4878 0.0072  0.0060  0.0358  862  GLN   A OE1 
6426 N  NE2 . GLN   A 837 ? 0.4354 0.4850 0.4555 0.0085  0.0074  0.0341  862  GLN   A NE2 
6427 N  N   . LYS   A 838 ? 0.1537 0.1973 0.1692 0.0060  0.0056  0.0256  863  LYS   A N   
6428 C  CA  . LYS   A 838 ? 0.1613 0.2015 0.1773 0.0069  0.0061  0.0242  863  LYS   A CA  
6429 C  C   . LYS   A 838 ? 0.1640 0.2020 0.1808 0.0077  0.0061  0.0239  863  LYS   A C   
6430 O  O   . LYS   A 838 ? 0.1694 0.2052 0.1871 0.0087  0.0066  0.0239  863  LYS   A O   
6431 C  CB  . LYS   A 838 ? 0.1669 0.2060 0.1815 0.0060  0.0060  0.0219  863  LYS   A CB  
6432 C  CG  . LYS   A 838 ? 0.1829 0.2190 0.1982 0.0068  0.0063  0.0205  863  LYS   A CG  
6433 C  CD  . LYS   A 838 ? 0.2045 0.2408 0.2206 0.0071  0.0069  0.0210  863  LYS   A CD  
6434 C  CE  . LYS   A 838 ? 0.2392 0.2728 0.2562 0.0077  0.0072  0.0199  863  LYS   A CE  
6435 N  NZ  . LYS   A 838 ? 0.2521 0.2860 0.2698 0.0078  0.0078  0.0202  863  LYS   A NZ  
6436 N  N   . PHE   A 839 ? 0.1570 0.1955 0.1731 0.0073  0.0056  0.0237  864  PHE   A N   
6437 C  CA  . PHE   A 839 ? 0.1505 0.1866 0.1669 0.0079  0.0056  0.0231  864  PHE   A CA  
6438 C  C   . PHE   A 839 ? 0.1471 0.1843 0.1646 0.0086  0.0058  0.0249  864  PHE   A C   
6439 O  O   . PHE   A 839 ? 0.1571 0.1920 0.1750 0.0094  0.0061  0.0247  864  PHE   A O   
6440 C  CB  . PHE   A 839 ? 0.1534 0.1886 0.1683 0.0070  0.0050  0.0213  864  PHE   A CB  
6441 C  CG  . PHE   A 839 ? 0.1577 0.1911 0.1719 0.0067  0.0050  0.0194  864  PHE   A CG  
6442 C  CD1 . PHE   A 839 ? 0.1715 0.2020 0.1861 0.0075  0.0051  0.0183  864  PHE   A CD1 
6443 C  CD2 . PHE   A 839 ? 0.1517 0.1863 0.1648 0.0057  0.0050  0.0187  864  PHE   A CD2 
6444 C  CE1 . PHE   A 839 ? 0.1751 0.2042 0.1895 0.0074  0.0052  0.0168  864  PHE   A CE1 
6445 C  CE2 . PHE   A 839 ? 0.1712 0.2041 0.1839 0.0057  0.0053  0.0171  864  PHE   A CE2 
6446 C  CZ  . PHE   A 839 ? 0.1639 0.1942 0.1774 0.0066  0.0053  0.0162  864  PHE   A CZ  
6447 N  N   . GLU   A 840 ? 0.1481 0.1887 0.1660 0.0082  0.0056  0.0267  865  GLU   A N   
6448 C  CA  . GLU   A 840 ? 0.1508 0.1935 0.1702 0.0088  0.0058  0.0290  865  GLU   A CA  
6449 C  C   . GLU   A 840 ? 0.1599 0.2038 0.1789 0.0080  0.0052  0.0289  865  GLU   A C   
6450 O  O   . GLU   A 840 ? 0.1573 0.1988 0.1754 0.0078  0.0050  0.0271  865  GLU   A O   
6451 C  CB  . GLU   A 840 ? 0.1742 0.2145 0.1950 0.0105  0.0069  0.0298  865  GLU   A CB  
6452 C  CG  . GLU   A 840 ? 0.1832 0.2222 0.2044 0.0111  0.0076  0.0300  865  GLU   A CG  
6453 C  CD  . GLU   A 840 ? 0.1909 0.2282 0.2134 0.0127  0.0089  0.0315  865  GLU   A CD  
6454 O  OE1 . GLU   A 840 ? 0.1929 0.2268 0.2151 0.0132  0.0094  0.0304  865  GLU   A OE1 
6455 O  OE2 . GLU   A 840 ? 0.1947 0.2344 0.2186 0.0133  0.0094  0.0338  865  GLU   A OE2 
6456 N  N   . LEU   A 841 ? 0.1585 0.2062 0.1786 0.0078  0.0050  0.0311  866  LEU   A N   
6457 C  CA  . LEU   A 841 ? 0.1700 0.2192 0.1902 0.0071  0.0044  0.0314  866  LEU   A CA  
6458 C  C   . LEU   A 841 ? 0.1666 0.2131 0.1877 0.0085  0.0053  0.0314  866  LEU   A C   
6459 O  O   . LEU   A 841 ? 0.1582 0.2035 0.1807 0.0100  0.0063  0.0325  866  LEU   A O   
6460 C  CB  . LEU   A 841 ? 0.2103 0.2644 0.2321 0.0068  0.0041  0.0343  866  LEU   A CB  
6461 C  CG  . LEU   A 841 ? 0.2503 0.3078 0.2708 0.0050  0.0031  0.0346  866  LEU   A CG  
6462 C  CD1 . LEU   A 841 ? 0.2754 0.3377 0.2979 0.0051  0.0028  0.0379  866  LEU   A CD1 
6463 C  CD2 . LEU   A 841 ? 0.2512 0.3088 0.2695 0.0030  0.0021  0.0327  866  LEU   A CD2 
6464 N  N   . GLY   A 842 ? 0.1553 0.2005 0.1754 0.0078  0.0049  0.0299  867  GLY   A N   
6465 C  CA  . GLY   A 842 ? 0.1556 0.1983 0.1763 0.0089  0.0056  0.0297  867  GLY   A CA  
6466 C  C   . GLY   A 842 ? 0.1573 0.1952 0.1766 0.0094  0.0060  0.0275  867  GLY   A C   
6467 O  O   . GLY   A 842 ? 0.1608 0.1962 0.1799 0.0099  0.0063  0.0268  867  GLY   A O   
6468 N  N   . SER   A 843 ? 0.1468 0.1836 0.1652 0.0092  0.0057  0.0264  868  SER   A N   
6469 C  CA  . SER   A 843 ? 0.1457 0.1786 0.1632 0.0095  0.0059  0.0245  868  SER   A CA  
6470 C  C   . SER   A 843 ? 0.1632 0.1944 0.1792 0.0088  0.0053  0.0226  868  SER   A C   
6471 O  O   . SER   A 843 ? 0.1554 0.1885 0.1707 0.0076  0.0046  0.0222  868  SER   A O   
6472 C  CB  . SER   A 843 ? 0.1610 0.1936 0.1782 0.0094  0.0058  0.0238  868  SER   A CB  
6473 O  OG  . SER   A 843 ? 0.1503 0.1847 0.1664 0.0081  0.0050  0.0230  868  SER   A OG  
6474 N  N   . SER   A 844 ? 0.1473 0.1750 0.1627 0.0093  0.0055  0.0214  869  SER   A N   
6475 C  CA  . SER   A 844 ? 0.1483 0.1741 0.1622 0.0087  0.0049  0.0196  869  SER   A CA  
6476 C  C   . SER   A 844 ? 0.1589 0.1852 0.1720 0.0078  0.0043  0.0183  869  SER   A C   
6477 O  O   . SER   A 844 ? 0.1689 0.1951 0.1809 0.0069  0.0039  0.0172  869  SER   A O   
6478 C  CB  . SER   A 844 ? 0.1900 0.2120 0.2035 0.0094  0.0052  0.0187  869  SER   A CB  
6479 O  OG  . SER   A 844 ? 0.2495 0.2696 0.2617 0.0089  0.0046  0.0171  869  SER   A OG  
6480 N  N   . SER   A 845 ? 0.1442 0.1710 0.1578 0.0080  0.0045  0.0184  870  SER   A N   
6481 C  CA  . SER   A 845 ? 0.1403 0.1676 0.1531 0.0072  0.0041  0.0172  870  SER   A CA  
6482 C  C   . SER   A 845 ? 0.1405 0.1705 0.1525 0.0059  0.0038  0.0175  870  SER   A C   
6483 O  O   . SER   A 845 ? 0.1539 0.1833 0.1645 0.0050  0.0036  0.0161  870  SER   A O   
6484 C  CB  . SER   A 845 ? 0.1640 0.1918 0.1776 0.0075  0.0045  0.0176  870  SER   A CB  
6485 O  OG  . SER   A 845 ? 0.1857 0.2111 0.1999 0.0085  0.0047  0.0174  870  SER   A OG  
6486 N  N   . ILE   A 846 ? 0.1378 0.1707 0.1505 0.0057  0.0038  0.0192  871  ILE   A N   
6487 C  CA  . ILE   A 846 ? 0.1388 0.1746 0.1507 0.0042  0.0034  0.0196  871  ILE   A CA  
6488 C  C   . ILE   A 846 ? 0.1484 0.1835 0.1594 0.0035  0.0030  0.0189  871  ILE   A C   
6489 O  O   . ILE   A 846 ? 0.1531 0.1885 0.1624 0.0021  0.0027  0.0179  871  ILE   A O   
6490 C  CB  . ILE   A 846 ? 0.1531 0.1925 0.1664 0.0044  0.0034  0.0220  871  ILE   A CB  
6491 C  CG1 . ILE   A 846 ? 0.1666 0.2069 0.1801 0.0046  0.0036  0.0225  871  ILE   A CG1 
6492 C  CG2 . ILE   A 846 ? 0.1789 0.2216 0.1915 0.0027  0.0027  0.0228  871  ILE   A CG2 
6493 C  CD1 . ILE   A 846 ? 0.1836 0.2252 0.1953 0.0030  0.0032  0.0216  871  ILE   A CD1 
6494 N  N   . ALA   A 847 ? 0.1413 0.1750 0.1531 0.0045  0.0032  0.0193  872  ALA   A N   
6495 C  CA  . ALA   A 847 ? 0.1488 0.1818 0.1599 0.0039  0.0030  0.0187  872  ALA   A CA  
6496 C  C   . ALA   A 847 ? 0.1660 0.1961 0.1753 0.0033  0.0029  0.0165  872  ALA   A C   
6497 O  O   . ALA   A 847 ? 0.1652 0.1956 0.1731 0.0020  0.0026  0.0158  872  ALA   A O   
6498 C  CB  . ALA   A 847 ? 0.1498 0.1813 0.1620 0.0051  0.0034  0.0195  872  ALA   A CB  
6499 N  N   . HIS   A 848 ? 0.1548 0.1824 0.1641 0.0042  0.0031  0.0155  873  HIS   A N   
6500 C  CA  . HIS   A 848 ? 0.1701 0.1950 0.1781 0.0039  0.0031  0.0136  873  HIS   A CA  
6501 C  C   . HIS   A 848 ? 0.1679 0.1939 0.1746 0.0026  0.0031  0.0128  873  HIS   A C   
6502 O  O   . HIS   A 848 ? 0.1663 0.1906 0.1715 0.0019  0.0032  0.0114  873  HIS   A O   
6503 C  CB  . HIS   A 848 ? 0.2086 0.2310 0.2173 0.0052  0.0033  0.0131  873  HIS   A CB  
6504 C  CG  . HIS   A 848 ? 0.3111 0.3316 0.3201 0.0060  0.0032  0.0132  873  HIS   A CG  
6505 N  ND1 . HIS   A 848 ? 0.3970 0.4156 0.4050 0.0057  0.0031  0.0124  873  HIS   A ND1 
6506 C  CD2 . HIS   A 848 ? 0.3586 0.3787 0.3685 0.0070  0.0034  0.0143  873  HIS   A CD2 
6507 C  CE1 . HIS   A 848 ? 0.4171 0.4343 0.4254 0.0065  0.0031  0.0129  873  HIS   A CE1 
6508 N  NE2 . HIS   A 848 ? 0.3995 0.4173 0.4089 0.0073  0.0034  0.0139  873  HIS   A NE2 
6509 N  N   . MET   A 849 ? 0.1550 0.1834 0.1621 0.0024  0.0031  0.0136  874  MET   A N   
6510 C  CA  . MET   A 849 ? 0.1578 0.1871 0.1633 0.0010  0.0032  0.0128  874  MET   A CA  
6511 C  C   . MET   A 849 ? 0.1710 0.2018 0.1749 -0.0008 0.0029  0.0129  874  MET   A C   
6512 O  O   . MET   A 849 ? 0.1702 0.1999 0.1721 -0.0020 0.0031  0.0115  874  MET   A O   
6513 C  CB  . MET   A 849 ? 0.1837 0.2152 0.1898 0.0011  0.0034  0.0138  874  MET   A CB  
6514 C  CG  . MET   A 849 ? 0.2041 0.2338 0.2113 0.0025  0.0038  0.0134  874  MET   A CG  
6515 S  SD  . MET   A 849 ? 0.2855 0.3170 0.2934 0.0027  0.0042  0.0141  874  MET   A SD  
6516 C  CE  . MET   A 849 ? 0.2284 0.2612 0.2387 0.0041  0.0041  0.0163  874  MET   A CE  
6517 N  N   . VAL   A 850 ? 0.1530 0.1864 0.1580 -0.0009 0.0024  0.0146  875  VAL   A N   
6518 C  CA  . VAL   A 850 ? 0.1604 0.1957 0.1641 -0.0028 0.0019  0.0149  875  VAL   A CA  
6519 C  C   . VAL   A 850 ? 0.1675 0.2000 0.1700 -0.0032 0.0020  0.0134  875  VAL   A C   
6520 O  O   . VAL   A 850 ? 0.1905 0.2224 0.1908 -0.0049 0.0020  0.0122  875  VAL   A O   
6521 C  CB  . VAL   A 850 ? 0.1536 0.1923 0.1594 -0.0024 0.0015  0.0173  875  VAL   A CB  
6522 C  CG1 . VAL   A 850 ? 0.1656 0.2064 0.1707 -0.0042 0.0009  0.0177  875  VAL   A CG1 
6523 C  CG2 . VAL   A 850 ? 0.1519 0.1936 0.1585 -0.0023 0.0014  0.0188  875  VAL   A CG2 
6524 N  N   . MET   A 851 ? 0.1721 0.2024 0.1757 -0.0017 0.0022  0.0133  876  MET   A N   
6525 C  CA  . MET   A 851 ? 0.1727 0.2002 0.1751 -0.0020 0.0023  0.0120  876  MET   A CA  
6526 C  C   . MET   A 851 ? 0.1630 0.1875 0.1639 -0.0022 0.0028  0.0100  876  MET   A C   
6527 O  O   . MET   A 851 ? 0.1700 0.1928 0.1690 -0.0034 0.0029  0.0088  876  MET   A O   
6528 C  CB  . MET   A 851 ? 0.2087 0.2342 0.2125 -0.0003 0.0024  0.0123  876  MET   A CB  
6529 C  CG  . MET   A 851 ? 0.3275 0.3551 0.3331 0.0004  0.0023  0.0142  876  MET   A CG  
6530 S  SD  . MET   A 851 ? 0.4141 0.4449 0.4198 -0.0012 0.0019  0.0154  876  MET   A SD  
6531 C  CE  . MET   A 851 ? 0.3618 0.3893 0.3655 -0.0021 0.0020  0.0136  876  MET   A CE  
6532 N  N   . GLY   A 852 ? 0.1614 0.1849 0.1630 -0.0010 0.0031  0.0097  877  GLY   A N   
6533 C  CA  . GLY   A 852 ? 0.1606 0.1811 0.1612 -0.0007 0.0037  0.0080  877  GLY   A CA  
6534 C  C   . GLY   A 852 ? 0.1700 0.1904 0.1683 -0.0025 0.0042  0.0069  877  GLY   A C   
6535 O  O   . GLY   A 852 ? 0.1958 0.2133 0.1928 -0.0026 0.0048  0.0054  877  GLY   A O   
6536 N  N   . THR   A 853 ? 0.1613 0.1847 0.1590 -0.0037 0.0039  0.0077  878  THR   A N   
6537 C  CA  . THR   A 853 ? 0.1562 0.1796 0.1514 -0.0056 0.0043  0.0066  878  THR   A CA  
6538 C  C   . THR   A 853 ? 0.1604 0.1844 0.1536 -0.0077 0.0040  0.0064  878  THR   A C   
6539 O  O   . THR   A 853 ? 0.1783 0.2015 0.1688 -0.0095 0.0045  0.0052  878  THR   A O   
6540 C  CB  . THR   A 853 ? 0.1621 0.1883 0.1573 -0.0061 0.0043  0.0074  878  THR   A CB  
6541 O  OG1 . THR   A 853 ? 0.1786 0.2086 0.1749 -0.0065 0.0033  0.0094  878  THR   A OG1 
6542 C  CG2 . THR   A 853 ? 0.1682 0.1938 0.1652 -0.0042 0.0047  0.0075  878  THR   A CG2 
6543 N  N   . THR   A 854 ? 0.1460 0.1713 0.1402 -0.0078 0.0033  0.0075  879  THR   A N   
6544 C  CA  . THR   A 854 ? 0.1582 0.1847 0.1508 -0.0100 0.0028  0.0075  879  THR   A CA  
6545 C  C   . THR   A 854 ? 0.1619 0.1864 0.1545 -0.0099 0.0028  0.0071  879  THR   A C   
6546 O  O   . THR   A 854 ? 0.1665 0.1912 0.1572 -0.0120 0.0026  0.0067  879  THR   A O   
6547 C  CB  . THR   A 854 ? 0.1684 0.1998 0.1621 -0.0108 0.0018  0.0096  879  THR   A CB  
6548 O  OG1 . THR   A 854 ? 0.1657 0.1982 0.1625 -0.0088 0.0015  0.0112  879  THR   A OG1 
6549 C  CG2 . THR   A 854 ? 0.1685 0.2022 0.1619 -0.0113 0.0018  0.0101  879  THR   A CG2 
6550 N  N   . ASN   A 855 ? 0.1571 0.1799 0.1516 -0.0078 0.0029  0.0073  880  ASN   A N   
6551 C  CA  . ASN   A 855 ? 0.1544 0.1758 0.1490 -0.0077 0.0028  0.0073  880  ASN   A CA  
6552 C  C   . ASN   A 855 ? 0.1685 0.1859 0.1611 -0.0082 0.0035  0.0055  880  ASN   A C   
6553 O  O   . ASN   A 855 ? 0.1706 0.1866 0.1632 -0.0081 0.0034  0.0055  880  ASN   A O   
6554 C  CB  . ASN   A 855 ? 0.1850 0.2063 0.1822 -0.0055 0.0026  0.0085  880  ASN   A CB  
6555 C  CG  . ASN   A 855 ? 0.2059 0.2240 0.2035 -0.0036 0.0031  0.0076  880  ASN   A CG  
6556 O  OD1 . ASN   A 855 ? 0.1987 0.2145 0.1951 -0.0037 0.0036  0.0062  880  ASN   A OD1 
6557 N  ND2 . ASN   A 855 ? 0.2468 0.2645 0.2463 -0.0019 0.0029  0.0085  880  ASN   A ND2 
6558 N  N   . GLN   A 856 ? 0.1595 0.1749 0.1501 -0.0089 0.0042  0.0040  881  GLN   A N   
6559 C  CA  . GLN   A 856 ? 0.1519 0.1634 0.1404 -0.0095 0.0051  0.0023  881  GLN   A CA  
6560 C  C   . GLN   A 856 ? 0.1598 0.1715 0.1451 -0.0124 0.0053  0.0014  881  GLN   A C   
6561 O  O   . GLN   A 856 ? 0.1782 0.1864 0.1613 -0.0133 0.0063  -0.0002 881  GLN   A O   
6562 C  CB  . GLN   A 856 ? 0.1667 0.1749 0.1554 -0.0078 0.0060  0.0013  881  GLN   A CB  
6563 C  CG  . GLN   A 856 ? 0.1656 0.1733 0.1570 -0.0053 0.0056  0.0021  881  GLN   A CG  
6564 C  CD  . GLN   A 856 ? 0.1775 0.1827 0.1696 -0.0036 0.0063  0.0014  881  GLN   A CD  
6565 O  OE1 . GLN   A 856 ? 0.1710 0.1749 0.1620 -0.0039 0.0073  0.0004  881  GLN   A OE1 
6566 N  NE2 . GLN   A 856 ? 0.1845 0.1889 0.1786 -0.0017 0.0059  0.0021  881  GLN   A NE2 
6567 N  N   . PHE   A 857 ? 0.1551 0.1709 0.1404 -0.0140 0.0045  0.0025  882  PHE   A N   
6568 C  CA  . PHE   A 857 ? 0.1621 0.1785 0.1443 -0.0171 0.0045  0.0018  882  PHE   A CA  
6569 C  C   . PHE   A 857 ? 0.1695 0.1861 0.1512 -0.0185 0.0040  0.0020  882  PHE   A C   
6570 O  O   . PHE   A 857 ? 0.1762 0.1943 0.1604 -0.0173 0.0033  0.0034  882  PHE   A O   
6571 C  CB  . PHE   A 857 ? 0.1692 0.1904 0.1515 -0.0184 0.0036  0.0031  882  PHE   A CB  
6572 C  CG  . PHE   A 857 ? 0.1744 0.1954 0.1566 -0.0175 0.0042  0.0027  882  PHE   A CG  
6573 C  CD1 . PHE   A 857 ? 0.1936 0.2106 0.1735 -0.0176 0.0056  0.0007  882  PHE   A CD1 
6574 C  CD2 . PHE   A 857 ? 0.1907 0.2156 0.1748 -0.0169 0.0034  0.0044  882  PHE   A CD2 
6575 C  CE1 . PHE   A 857 ? 0.2051 0.2221 0.1849 -0.0169 0.0062  0.0004  882  PHE   A CE1 
6576 C  CE2 . PHE   A 857 ? 0.2022 0.2271 0.1860 -0.0163 0.0039  0.0041  882  PHE   A CE2 
6577 C  CZ  . PHE   A 857 ? 0.1968 0.2177 0.1785 -0.0163 0.0053  0.0021  882  PHE   A CZ  
6578 N  N   . SER   A 858 ? 0.1701 0.1851 0.1484 -0.0212 0.0044  0.0007  883  SER   A N   
6579 C  CA  . SER   A 858 ? 0.1710 0.1857 0.1486 -0.0228 0.0041  0.0007  883  SER   A CA  
6580 C  C   . SER   A 858 ? 0.1858 0.2013 0.1600 -0.0265 0.0040  0.0000  883  SER   A C   
6581 O  O   . SER   A 858 ? 0.1973 0.2108 0.1697 -0.0281 0.0043  -0.0008 883  SER   A O   
6582 C  CB  . SER   A 858 ? 0.1844 0.1939 0.1614 -0.0215 0.0053  -0.0007 883  SER   A CB  
6583 O  OG  . SER   A 858 ? 0.1851 0.1902 0.1592 -0.0221 0.0067  -0.0027 883  SER   A OG  
6584 N  N   . THR   A 859 ? 0.1841 0.2029 0.1574 -0.0279 0.0034  0.0005  884  THR   A N   
6585 C  CA  . THR   A 859 ? 0.1883 0.2086 0.1582 -0.0319 0.0030  0.0001  884  THR   A CA  
6586 C  C   . THR   A 859 ? 0.1847 0.2116 0.1567 -0.0328 0.0012  0.0026  884  THR   A C   
6587 O  O   . THR   A 859 ? 0.1752 0.2050 0.1503 -0.0305 0.0006  0.0042  884  THR   A O   
6588 C  CB  . THR   A 859 ? 0.2204 0.2380 0.1864 -0.0335 0.0041  -0.0019 884  THR   A CB  
6589 O  OG1 . THR   A 859 ? 0.2115 0.2318 0.1787 -0.0324 0.0037  -0.0009 884  THR   A OG1 
6590 C  CG2 . THR   A 859 ? 0.2385 0.2495 0.2030 -0.0321 0.0061  -0.0041 884  THR   A CG2 
6591 N  N   . ARG   A 860 ? 0.1831 0.2125 0.1533 -0.0362 0.0003  0.0029  885  ARG   A N   
6592 C  CA  . ARG   A 860 ? 0.1742 0.2102 0.1461 -0.0374 -0.0014 0.0054  885  ARG   A CA  
6593 C  C   . ARG   A 860 ? 0.1784 0.2165 0.1493 -0.0378 -0.0017 0.0057  885  ARG   A C   
6594 O  O   . ARG   A 860 ? 0.1746 0.2178 0.1484 -0.0370 -0.0029 0.0081  885  ARG   A O   
6595 C  CB  . ARG   A 860 ? 0.2061 0.2441 0.1757 -0.0414 -0.0023 0.0055  885  ARG   A CB  
6596 C  CG  . ARG   A 860 ? 0.2195 0.2562 0.1907 -0.0409 -0.0021 0.0056  885  ARG   A CG  
6597 C  CD  . ARG   A 860 ? 0.2575 0.2939 0.2255 -0.0449 -0.0024 0.0048  885  ARG   A CD  
6598 N  NE  . ARG   A 860 ? 0.2884 0.3234 0.2580 -0.0442 -0.0022 0.0049  885  ARG   A NE  
6599 C  CZ  . ARG   A 860 ? 0.3083 0.3371 0.2766 -0.0431 -0.0006 0.0029  885  ARG   A CZ  
6600 N  NH1 . ARG   A 860 ? 0.3282 0.3518 0.2935 -0.0426 0.0008  0.0006  885  ARG   A NH1 
6601 N  NH2 . ARG   A 860 ? 0.3368 0.3648 0.3065 -0.0425 -0.0005 0.0032  885  ARG   A NH2 
6602 N  N   . THR   A 861 ? 0.1903 0.2243 0.1574 -0.0388 -0.0005 0.0034  886  THR   A N   
6603 C  CA  . THR   A 861 ? 0.1853 0.2212 0.1514 -0.0391 -0.0006 0.0037  886  THR   A CA  
6604 C  C   . THR   A 861 ? 0.1872 0.2236 0.1573 -0.0350 -0.0004 0.0048  886  THR   A C   
6605 O  O   . THR   A 861 ? 0.1791 0.2197 0.1509 -0.0345 -0.0013 0.0067  886  THR   A O   
6606 C  CB  . THR   A 861 ? 0.2049 0.2358 0.1659 -0.0409 0.0009  0.0009  886  THR   A CB  
6607 O  OG1 . THR   A 861 ? 0.2096 0.2406 0.1669 -0.0450 0.0006  0.0001  886  THR   A OG1 
6608 C  CG2 . THR   A 861 ? 0.2157 0.2482 0.1756 -0.0411 0.0010  0.0011  886  THR   A CG2 
6609 N  N   . ARG   A 862 ? 0.1727 0.2049 0.1444 -0.0321 0.0008  0.0038  887  ARG   A N   
6610 C  CA  . ARG   A 862 ? 0.1752 0.2079 0.1505 -0.0285 0.0010  0.0048  887  ARG   A CA  
6611 C  C   . ARG   A 862 ? 0.1730 0.2106 0.1524 -0.0272 -0.0004 0.0076  887  ARG   A C   
6612 O  O   . ARG   A 862 ? 0.1709 0.2111 0.1528 -0.0255 -0.0008 0.0092  887  ARG   A O   
6613 C  CB  . ARG   A 862 ? 0.1797 0.2071 0.1558 -0.0258 0.0023  0.0033  887  ARG   A CB  
6614 C  CG  . ARG   A 862 ? 0.1922 0.2149 0.1652 -0.0261 0.0040  0.0008  887  ARG   A CG  
6615 C  CD  . ARG   A 862 ? 0.1931 0.2168 0.1663 -0.0252 0.0043  0.0010  887  ARG   A CD  
6616 N  NE  . ARG   A 862 ? 0.2093 0.2281 0.1803 -0.0248 0.0062  -0.0012 887  ARG   A NE  
6617 C  CZ  . ARG   A 862 ? 0.2265 0.2451 0.1968 -0.0243 0.0069  -0.0016 887  ARG   A CZ  
6618 N  NH1 . ARG   A 862 ? 0.2051 0.2280 0.1769 -0.0242 0.0059  0.0001  887  ARG   A NH1 
6619 N  NH2 . ARG   A 862 ? 0.2352 0.2492 0.2038 -0.0237 0.0088  -0.0035 887  ARG   A NH2 
6620 N  N   . LEU   A 863 ? 0.1654 0.2041 0.1456 -0.0281 -0.0010 0.0083  888  LEU   A N   
6621 C  CA  . LEU   A 863 ? 0.1666 0.2099 0.1508 -0.0268 -0.0021 0.0111  888  LEU   A CA  
6622 C  C   . LEU   A 863 ? 0.1785 0.2275 0.1633 -0.0282 -0.0033 0.0132  888  LEU   A C   
6623 O  O   . LEU   A 863 ? 0.1912 0.2432 0.1794 -0.0261 -0.0037 0.0153  888  LEU   A O   
6624 C  CB  . LEU   A 863 ? 0.1647 0.2085 0.1492 -0.0282 -0.0025 0.0114  888  LEU   A CB  
6625 C  CG  . LEU   A 863 ? 0.1772 0.2260 0.1657 -0.0272 -0.0035 0.0143  888  LEU   A CG  
6626 C  CD1 . LEU   A 863 ? 0.1996 0.2473 0.1915 -0.0235 -0.0029 0.0151  888  LEU   A CD1 
6627 C  CD2 . LEU   A 863 ? 0.1877 0.2367 0.1760 -0.0289 -0.0038 0.0144  888  LEU   A CD2 
6628 N  N   . GLU   A 864 ? 0.1685 0.2188 0.1499 -0.0317 -0.0039 0.0127  889  GLU   A N   
6629 C  CA  . GLU   A 864 ? 0.1638 0.2196 0.1456 -0.0330 -0.0052 0.0149  889  GLU   A CA  
6630 C  C   . GLU   A 864 ? 0.1664 0.2219 0.1483 -0.0314 -0.0047 0.0149  889  GLU   A C   
6631 O  O   . GLU   A 864 ? 0.1744 0.2345 0.1586 -0.0308 -0.0056 0.0173  889  GLU   A O   
6632 C  CB  . GLU   A 864 ? 0.1924 0.2500 0.1704 -0.0374 -0.0060 0.0144  889  GLU   A CB  
6633 C  CG  . GLU   A 864 ? 0.2012 0.2654 0.1799 -0.0391 -0.0077 0.0172  889  GLU   A CG  
6634 C  CD  . GLU   A 864 ? 0.2300 0.2950 0.2074 -0.0391 -0.0077 0.0173  889  GLU   A CD  
6635 O  OE1 . GLU   A 864 ? 0.2181 0.2784 0.1919 -0.0394 -0.0064 0.0146  889  GLU   A OE1 
6636 O  OE2 . GLU   A 864 ? 0.2416 0.3119 0.2215 -0.0386 -0.0088 0.0201  889  GLU   A OE2 
6637 N  N   . GLU   A 865 ? 0.1574 0.2076 0.1371 -0.0306 -0.0033 0.0123  890  GLU   A N   
6638 C  CA  . GLU   A 865 ? 0.1553 0.2053 0.1356 -0.0288 -0.0027 0.0124  890  GLU   A CA  
6639 C  C   . GLU   A 865 ? 0.1570 0.2090 0.1421 -0.0254 -0.0029 0.0146  890  GLU   A C   
6640 O  O   . GLU   A 865 ? 0.1649 0.2198 0.1514 -0.0246 -0.0033 0.0162  890  GLU   A O   
6641 C  CB  . GLU   A 865 ? 0.1623 0.2064 0.1405 -0.0278 -0.0010 0.0096  890  GLU   A CB  
6642 C  CG  . GLU   A 865 ? 0.1755 0.2170 0.1485 -0.0308 -0.0003 0.0073  890  GLU   A CG  
6643 C  CD  . GLU   A 865 ? 0.1823 0.2179 0.1536 -0.0296 0.0016  0.0047  890  GLU   A CD  
6644 O  OE1 . GLU   A 865 ? 0.1810 0.2148 0.1553 -0.0264 0.0023  0.0047  890  GLU   A OE1 
6645 O  OE2 . GLU   A 865 ? 0.2001 0.2331 0.1671 -0.0319 0.0026  0.0027  890  GLU   A OE2 
6646 N  N   . VAL   A 866 ? 0.1589 0.2088 0.1461 -0.0235 -0.0025 0.0144  891  VAL   A N   
6647 C  CA  . VAL   A 866 ? 0.1522 0.2032 0.1436 -0.0203 -0.0025 0.0161  891  VAL   A CA  
6648 C  C   . VAL   A 866 ? 0.1606 0.2174 0.1548 -0.0206 -0.0037 0.0192  891  VAL   A C   
6649 O  O   . VAL   A 866 ? 0.1622 0.2213 0.1586 -0.0190 -0.0038 0.0211  891  VAL   A O   
6650 C  CB  . VAL   A 866 ? 0.1624 0.2096 0.1549 -0.0186 -0.0018 0.0150  891  VAL   A CB  
6651 C  CG1 . VAL   A 866 ? 0.1783 0.2265 0.1748 -0.0156 -0.0017 0.0168  891  VAL   A CG1 
6652 C  CG2 . VAL   A 866 ? 0.1771 0.2188 0.1675 -0.0179 -0.0006 0.0123  891  VAL   A CG2 
6653 N  N   . LYS   A 867 ? 0.1674 0.2265 0.1612 -0.0227 -0.0045 0.0199  892  LYS   A N   
6654 C  CA  . LYS   A 867 ? 0.1612 0.2262 0.1579 -0.0228 -0.0056 0.0231  892  LYS   A CA  
6655 C  C   . LYS   A 867 ? 0.1782 0.2473 0.1745 -0.0240 -0.0065 0.0247  892  LYS   A C   
6656 O  O   . LYS   A 867 ? 0.1912 0.2639 0.1906 -0.0224 -0.0068 0.0274  892  LYS   A O   
6657 C  CB  . LYS   A 867 ? 0.1803 0.2473 0.1765 -0.0253 -0.0064 0.0235  892  LYS   A CB  
6658 C  CG  . LYS   A 867 ? 0.2242 0.2883 0.2217 -0.0239 -0.0057 0.0228  892  LYS   A CG  
6659 C  CD  . LYS   A 867 ? 0.3187 0.3854 0.3156 -0.0267 -0.0066 0.0234  892  LYS   A CD  
6660 C  CE  . LYS   A 867 ? 0.4172 0.4813 0.4151 -0.0258 -0.0060 0.0227  892  LYS   A CE  
6661 N  NZ  . LYS   A 867 ? 0.4793 0.5467 0.4772 -0.0286 -0.0069 0.0237  892  LYS   A NZ  
6662 N  N   . GLY   A 868 ? 0.1797 0.2480 0.1719 -0.0268 -0.0067 0.0231  893  GLY   A N   
6663 C  CA  . GLY   A 868 ? 0.1812 0.2534 0.1724 -0.0283 -0.0076 0.0245  893  GLY   A CA  
6664 C  C   . GLY   A 868 ? 0.1846 0.2560 0.1770 -0.0257 -0.0069 0.0249  893  GLY   A C   
6665 O  O   . GLY   A 868 ? 0.1969 0.2726 0.1909 -0.0255 -0.0076 0.0274  893  GLY   A O   
6666 N  N   . PHE   A 869 ? 0.1705 0.2365 0.1621 -0.0240 -0.0055 0.0225  894  PHE   A N   
6667 C  CA  . PHE   A 869 ? 0.1654 0.2306 0.1583 -0.0216 -0.0048 0.0228  894  PHE   A CA  
6668 C  C   . PHE   A 869 ? 0.1721 0.2398 0.1697 -0.0188 -0.0049 0.0255  894  PHE   A C   
6669 O  O   . PHE   A 869 ? 0.1783 0.2491 0.1773 -0.0181 -0.0052 0.0276  894  PHE   A O   
6670 C  CB  . PHE   A 869 ? 0.1669 0.2261 0.1584 -0.0202 -0.0033 0.0199  894  PHE   A CB  
6671 C  CG  . PHE   A 869 ? 0.1749 0.2335 0.1681 -0.0178 -0.0026 0.0203  894  PHE   A CG  
6672 C  CD1 . PHE   A 869 ? 0.1993 0.2595 0.1909 -0.0188 -0.0027 0.0207  894  PHE   A CD1 
6673 C  CD2 . PHE   A 869 ? 0.1899 0.2467 0.1862 -0.0148 -0.0019 0.0206  894  PHE   A CD2 
6674 C  CE1 . PHE   A 869 ? 0.1981 0.2579 0.1913 -0.0167 -0.0021 0.0213  894  PHE   A CE1 
6675 C  CE2 . PHE   A 869 ? 0.1905 0.2471 0.1884 -0.0128 -0.0014 0.0213  894  PHE   A CE2 
6676 C  CZ  . PHE   A 869 ? 0.1927 0.2507 0.1891 -0.0137 -0.0014 0.0216  894  PHE   A CZ  
6677 N  N   . PHE   A 870 ? 0.1669 0.2330 0.1667 -0.0172 -0.0045 0.0254  895  PHE   A N   
6678 C  CA  . PHE   A 870 ? 0.1766 0.2441 0.1804 -0.0143 -0.0042 0.0277  895  PHE   A CA  
6679 C  C   . PHE   A 870 ? 0.1884 0.2618 0.1945 -0.0149 -0.0053 0.0310  895  PHE   A C   
6680 O  O   . PHE   A 870 ? 0.1913 0.2668 0.2002 -0.0131 -0.0051 0.0333  895  PHE   A O   
6681 C  CB  . PHE   A 870 ? 0.1748 0.2386 0.1800 -0.0124 -0.0034 0.0266  895  PHE   A CB  
6682 C  CG  . PHE   A 870 ? 0.1691 0.2275 0.1729 -0.0112 -0.0023 0.0240  895  PHE   A CG  
6683 C  CD1 . PHE   A 870 ? 0.1777 0.2350 0.1828 -0.0091 -0.0016 0.0243  895  PHE   A CD1 
6684 C  CD2 . PHE   A 870 ? 0.1765 0.2311 0.1778 -0.0121 -0.0020 0.0213  895  PHE   A CD2 
6685 C  CE1 . PHE   A 870 ? 0.1821 0.2350 0.1862 -0.0081 -0.0008 0.0220  895  PHE   A CE1 
6686 C  CE2 . PHE   A 870 ? 0.1863 0.2363 0.1867 -0.0109 -0.0010 0.0191  895  PHE   A CE2 
6687 C  CZ  . PHE   A 870 ? 0.1841 0.2334 0.1860 -0.0088 -0.0005 0.0195  895  PHE   A CZ  
6688 N  N   . SER   A 871 ? 0.1829 0.2594 0.1881 -0.0176 -0.0063 0.0315  896  SER   A N   
6689 C  CA  . SER   A 871 ? 0.1986 0.2814 0.2064 -0.0181 -0.0075 0.0351  896  SER   A CA  
6690 C  C   . SER   A 871 ? 0.2206 0.3066 0.2279 -0.0187 -0.0081 0.0367  896  SER   A C   
6691 O  O   . SER   A 871 ? 0.2430 0.3330 0.2536 -0.0174 -0.0083 0.0399  896  SER   A O   
6692 C  CB  . SER   A 871 ? 0.2403 0.3259 0.2472 -0.0210 -0.0086 0.0355  896  SER   A CB  
6693 O  OG  . SER   A 871 ? 0.2892 0.3742 0.2916 -0.0243 -0.0093 0.0336  896  SER   A OG  
6694 N  N   . SER   A 872 ? 0.2207 0.3043 0.2242 -0.0202 -0.0080 0.0345  897  SER   A N   
6695 C  CA  . SER   A 872 ? 0.2414 0.3277 0.2440 -0.0209 -0.0085 0.0358  897  SER   A CA  
6696 C  C   . SER   A 872 ? 0.2585 0.3443 0.2639 -0.0177 -0.0076 0.0371  897  SER   A C   
6697 O  O   . SER   A 872 ? 0.2714 0.3603 0.2770 -0.0179 -0.0080 0.0391  897  SER   A O   
6698 C  CB  . SER   A 872 ? 0.2723 0.3556 0.2698 -0.0233 -0.0083 0.0329  897  SER   A CB  
6699 O  OG  . SER   A 872 ? 0.2980 0.3758 0.2947 -0.0214 -0.0068 0.0304  897  SER   A OG  
6700 N  N   . LEU   A 873 ? 0.2453 0.3272 0.2526 -0.0149 -0.0063 0.0362  898  LEU   A N   
6701 C  CA  . LEU   A 873 ? 0.2465 0.3273 0.2562 -0.0120 -0.0053 0.0371  898  LEU   A CA  
6702 C  C   . LEU   A 873 ? 0.2543 0.3392 0.2681 -0.0103 -0.0054 0.0409  898  LEU   A C   
6703 O  O   . LEU   A 873 ? 0.2555 0.3402 0.2713 -0.0081 -0.0046 0.0421  898  LEU   A O   
6704 C  CB  . LEU   A 873 ? 0.2461 0.3212 0.2561 -0.0098 -0.0039 0.0348  898  LEU   A CB  
6705 C  CG  . LEU   A 873 ? 0.2544 0.3252 0.2608 -0.0110 -0.0035 0.0312  898  LEU   A CG  
6706 C  CD1 . LEU   A 873 ? 0.2515 0.3174 0.2588 -0.0089 -0.0024 0.0293  898  LEU   A CD1 
6707 C  CD2 . LEU   A 873 ? 0.2652 0.3356 0.2696 -0.0115 -0.0033 0.0306  898  LEU   A CD2 
6708 N  N   . LYS   A 874 ? 0.2624 0.3509 0.2780 -0.0110 -0.0062 0.0426  899  LYS   A N   
6709 C  CA  . LYS   A 874 ? 0.2665 0.3590 0.2864 -0.0092 -0.0061 0.0464  899  LYS   A CA  
6710 C  C   . LYS   A 874 ? 0.2798 0.3687 0.3023 -0.0056 -0.0043 0.0465  899  LYS   A C   
6711 O  O   . LYS   A 874 ? 0.2692 0.3538 0.2914 -0.0048 -0.0035 0.0443  899  LYS   A O   
6712 C  CB  . LYS   A 874 ? 0.3095 0.4077 0.3299 -0.0104 -0.0073 0.0494  899  LYS   A CB  
6713 C  CG  . LYS   A 874 ? 0.3753 0.4770 0.3931 -0.0141 -0.0091 0.0493  899  LYS   A CG  
6714 C  CD  . LYS   A 874 ? 0.4630 0.5693 0.4799 -0.0158 -0.0103 0.0516  899  LYS   A CD  
6715 C  CE  . LYS   A 874 ? 0.5414 0.6524 0.5564 -0.0195 -0.0122 0.0523  899  LYS   A CE  
6716 N  NZ  . LYS   A 874 ? 0.5944 0.7093 0.6077 -0.0215 -0.0135 0.0540  899  LYS   A NZ  
6717 N  N   . GLU   A 875 ? 0.2754 0.3655 0.3001 -0.0037 -0.0037 0.0488  900  GLU   A N   
6718 C  CA  . GLU   A 875 ? 0.2825 0.3691 0.3095 -0.0006 -0.0020 0.0489  900  GLU   A CA  
6719 C  C   . GLU   A 875 ? 0.2665 0.3471 0.2912 0.0001  -0.0011 0.0455  900  GLU   A C   
6720 O  O   . GLU   A 875 ? 0.2843 0.3612 0.3102 0.0023  0.0003  0.0450  900  GLU   A O   
6721 C  CB  . GLU   A 875 ? 0.3429 0.4325 0.3728 0.0011  -0.0015 0.0524  900  GLU   A CB  
6722 C  CG  . GLU   A 875 ? 0.4445 0.5345 0.4725 0.0004  -0.0019 0.0523  900  GLU   A CG  
6723 C  CD  . GLU   A 875 ? 0.5650 0.6603 0.5917 -0.0022 -0.0037 0.0538  900  GLU   A CD  
6724 O  OE1 . GLU   A 875 ? 0.5662 0.6654 0.5936 -0.0037 -0.0048 0.0552  900  GLU   A OE1 
6725 O  OE2 . GLU   A 875 ? 0.6211 0.7166 0.6460 -0.0029 -0.0039 0.0537  900  GLU   A OE2 
6726 N  N   . ASN   A 876 ? 0.2568 0.3362 0.2780 -0.0019 -0.0018 0.0432  901  ASN   A N   
6727 C  CA  . ASN   A 876 ? 0.2621 0.3363 0.2814 -0.0013 -0.0010 0.0402  901  ASN   A CA  
6728 C  C   . ASN   A 876 ? 0.2346 0.3051 0.2520 -0.0020 -0.0009 0.0371  901  ASN   A C   
6729 O  O   . ASN   A 876 ? 0.2263 0.2938 0.2410 -0.0028 -0.0008 0.0345  901  ASN   A O   
6730 C  CB  . ASN   A 876 ? 0.2978 0.3725 0.3146 -0.0026 -0.0014 0.0395  901  ASN   A CB  
6731 C  CG  . ASN   A 876 ? 0.3618 0.4319 0.3779 -0.0013 -0.0002 0.0374  901  ASN   A CG  
6732 O  OD1 . ASN   A 876 ? 0.3827 0.4504 0.4007 0.0009  0.0008  0.0377  901  ASN   A OD1 
6733 N  ND2 . ASN   A 876 ? 0.4132 0.4818 0.4264 -0.0027 -0.0004 0.0354  901  ASN   A ND2 
6734 N  N   . GLY   A 877 ? 0.2168 0.2875 0.2355 -0.0017 -0.0009 0.0375  902  GLY   A N   
6735 C  CA  . GLY   A 877 ? 0.2066 0.2735 0.2237 -0.0021 -0.0007 0.0347  902  GLY   A CA  
6736 C  C   . GLY   A 877 ? 0.1947 0.2632 0.2115 -0.0037 -0.0015 0.0348  902  GLY   A C   
6737 O  O   . GLY   A 877 ? 0.1866 0.2518 0.2025 -0.0036 -0.0011 0.0328  902  GLY   A O   
6738 N  N   . SER   A 878 ? 0.1918 0.2655 0.2094 -0.0051 -0.0025 0.0371  903  SER   A N   
6739 C  CA  . SER   A 878 ? 0.1954 0.2708 0.2126 -0.0069 -0.0032 0.0371  903  SER   A CA  
6740 C  C   . SER   A 878 ? 0.2000 0.2740 0.2196 -0.0052 -0.0024 0.0374  903  SER   A C   
6741 O  O   . SER   A 878 ? 0.2141 0.2875 0.2328 -0.0064 -0.0027 0.0364  903  SER   A O   
6742 C  CB  . SER   A 878 ? 0.2069 0.2886 0.2251 -0.0087 -0.0045 0.0398  903  SER   A CB  
6743 O  OG  . SER   A 878 ? 0.2159 0.3011 0.2380 -0.0068 -0.0042 0.0433  903  SER   A OG  
6744 N  N   . GLN   A 879 ? 0.2023 0.2757 0.2246 -0.0025 -0.0013 0.0390  904  GLN   A N   
6745 C  CA  . GLN   A 879 ? 0.2004 0.2726 0.2249 -0.0008 -0.0003 0.0396  904  GLN   A CA  
6746 C  C   . GLN   A 879 ? 0.1946 0.2607 0.2182 0.0008  0.0008  0.0372  904  GLN   A C   
6747 O  O   . GLN   A 879 ? 0.2083 0.2728 0.2334 0.0023  0.0018  0.0376  904  GLN   A O   
6748 C  CB  . GLN   A 879 ? 0.2358 0.3113 0.2642 0.0011  0.0004  0.0432  904  GLN   A CB  
6749 C  CG  . GLN   A 879 ? 0.2712 0.3535 0.3012 -0.0003 -0.0009 0.0462  904  GLN   A CG  
6750 C  CD  . GLN   A 879 ? 0.3629 0.4478 0.3924 -0.0026 -0.0020 0.0461  904  GLN   A CD  
6751 O  OE1 . GLN   A 879 ? 0.4159 0.5003 0.4469 -0.0020 -0.0014 0.0464  904  GLN   A OE1 
6752 N  NE2 . GLN   A 879 ? 0.3756 0.4631 0.4028 -0.0055 -0.0036 0.0457  904  GLN   A NE2 
6753 N  N   . LEU   A 880 ? 0.1793 0.2420 0.2001 0.0003  0.0007  0.0345  905  LEU   A N   
6754 C  CA  . LEU   A 880 ? 0.1652 0.2225 0.1851 0.0016  0.0016  0.0323  905  LEU   A CA  
6755 C  C   . LEU   A 880 ? 0.1607 0.2159 0.1799 0.0012  0.0017  0.0310  905  LEU   A C   
6756 O  O   . LEU   A 880 ? 0.1707 0.2272 0.1885 -0.0008 0.0008  0.0303  905  LEU   A O   
6757 C  CB  . LEU   A 880 ? 0.1717 0.2263 0.1889 0.0009  0.0013  0.0298  905  LEU   A CB  
6758 C  CG  . LEU   A 880 ? 0.1870 0.2422 0.2047 0.0017  0.0016  0.0306  905  LEU   A CG  
6759 C  CD1 . LEU   A 880 ? 0.1917 0.2452 0.2068 0.0005  0.0012  0.0284  905  LEU   A CD1 
6760 C  CD2 . LEU   A 880 ? 0.2060 0.2585 0.2254 0.0041  0.0028  0.0310  905  LEU   A CD2 
6761 N  N   . ARG   A 881 ? 0.1455 0.1974 0.1654 0.0030  0.0027  0.0306  906  ARG   A N   
6762 C  CA  . ARG   A 881 ? 0.1654 0.2151 0.1846 0.0027  0.0029  0.0294  906  ARG   A CA  
6763 C  C   . ARG   A 881 ? 0.1637 0.2103 0.1798 0.0014  0.0023  0.0265  906  ARG   A C   
6764 O  O   . ARG   A 881 ? 0.1749 0.2211 0.1899 0.0001  0.0019  0.0257  906  ARG   A O   
6765 C  CB  . ARG   A 881 ? 0.1891 0.2353 0.2091 0.0048  0.0042  0.0294  906  ARG   A CB  
6766 C  CG  . ARG   A 881 ? 0.2722 0.3163 0.2914 0.0045  0.0044  0.0284  906  ARG   A CG  
6767 C  CD  . ARG   A 881 ? 0.3170 0.3584 0.3372 0.0065  0.0058  0.0289  906  ARG   A CD  
6768 N  NE  . ARG   A 881 ? 0.3357 0.3802 0.3588 0.0076  0.0066  0.0317  906  ARG   A NE  
6769 C  CZ  . ARG   A 881 ? 0.3539 0.4012 0.3787 0.0073  0.0068  0.0334  906  ARG   A CZ  
6770 N  NH1 . ARG   A 881 ? 0.3248 0.3749 0.3525 0.0086  0.0077  0.0361  906  ARG   A NH1 
6771 N  NH2 . ARG   A 881 ? 0.3741 0.4218 0.3979 0.0058  0.0061  0.0325  906  ARG   A NH2 
6772 N  N   . CYS   A 882 ? 0.1645 0.2090 0.1794 0.0017  0.0023  0.0252  907  CYS   A N   
6773 C  CA  . CYS   A 882 ? 0.1606 0.2021 0.1729 0.0006  0.0019  0.0226  907  CYS   A CA  
6774 C  C   . CYS   A 882 ? 0.1698 0.2137 0.1805 -0.0018 0.0011  0.0222  907  CYS   A C   
6775 O  O   . CYS   A 882 ? 0.1660 0.2075 0.1746 -0.0029 0.0010  0.0203  907  CYS   A O   
6776 C  CB  . CYS   A 882 ? 0.1690 0.2083 0.1806 0.0014  0.0022  0.0214  907  CYS   A CB  
6777 S  SG  . CYS   A 882 ? 0.1756 0.2184 0.1877 0.0009  0.0019  0.0226  907  CYS   A SG  
6778 N  N   . VAL   A 883 ? 0.1646 0.2128 0.1761 -0.0027 0.0006  0.0240  908  VAL   A N   
6779 C  CA  . VAL   A 883 ? 0.1739 0.2245 0.1836 -0.0053 -0.0003 0.0237  908  VAL   A CA  
6780 C  C   . VAL   A 883 ? 0.1737 0.2250 0.1834 -0.0064 -0.0006 0.0239  908  VAL   A C   
6781 O  O   . VAL   A 883 ? 0.1735 0.2235 0.1808 -0.0082 -0.0009 0.0222  908  VAL   A O   
6782 C  CB  . VAL   A 883 ? 0.1818 0.2372 0.1925 -0.0059 -0.0009 0.0259  908  VAL   A CB  
6783 C  CG1 . VAL   A 883 ? 0.1849 0.2435 0.1940 -0.0089 -0.0020 0.0261  908  VAL   A CG1 
6784 C  CG2 . VAL   A 883 ? 0.1900 0.2444 0.2001 -0.0053 -0.0007 0.0253  908  VAL   A CG2 
6785 N  N   . GLN   A 884 ? 0.1680 0.2209 0.1803 -0.0052 -0.0003 0.0258  909  GLN   A N   
6786 C  CA  . GLN   A 884 ? 0.1665 0.2201 0.1790 -0.0062 -0.0004 0.0260  909  GLN   A CA  
6787 C  C   . GLN   A 884 ? 0.1647 0.2131 0.1754 -0.0059 0.0001  0.0236  909  GLN   A C   
6788 O  O   . GLN   A 884 ? 0.1715 0.2193 0.1807 -0.0075 -0.0002 0.0226  909  GLN   A O   
6789 C  CB  . GLN   A 884 ? 0.1902 0.2466 0.2061 -0.0048 0.0000  0.0287  909  GLN   A CB  
6790 C  CG  . GLN   A 884 ? 0.2304 0.2883 0.2467 -0.0061 -0.0002 0.0292  909  GLN   A CG  
6791 C  CD  . GLN   A 884 ? 0.2782 0.3400 0.2934 -0.0091 -0.0015 0.0296  909  GLN   A CD  
6792 O  OE1 . GLN   A 884 ? 0.2858 0.3508 0.3009 -0.0101 -0.0023 0.0306  909  GLN   A OE1 
6793 N  NE2 . GLN   A 884 ? 0.2726 0.3341 0.2868 -0.0108 -0.0018 0.0289  909  GLN   A NE2 
6794 N  N   . GLN   A 885 ? 0.1664 0.2110 0.1771 -0.0038 0.0008  0.0226  910  GLN   A N   
6795 C  CA  . GLN   A 885 ? 0.1564 0.1964 0.1656 -0.0035 0.0012  0.0205  910  GLN   A CA  
6796 C  C   . GLN   A 885 ? 0.1624 0.2005 0.1686 -0.0053 0.0009  0.0183  910  GLN   A C   
6797 O  O   . GLN   A 885 ? 0.1717 0.2076 0.1764 -0.0061 0.0009  0.0170  910  GLN   A O   
6798 C  CB  . GLN   A 885 ? 0.1701 0.2069 0.1798 -0.0012 0.0019  0.0200  910  GLN   A CB  
6799 C  CG  . GLN   A 885 ? 0.2452 0.2772 0.2535 -0.0006 0.0023  0.0181  910  GLN   A CG  
6800 C  CD  . GLN   A 885 ? 0.3222 0.3514 0.3309 0.0014  0.0028  0.0177  910  GLN   A CD  
6801 O  OE1 . GLN   A 885 ? 0.3998 0.4255 0.4072 0.0017  0.0029  0.0161  910  GLN   A OE1 
6802 N  NE2 . GLN   A 885 ? 0.3357 0.3666 0.3463 0.0025  0.0031  0.0193  910  GLN   A NE2 
6803 N  N   . THR   A 886 ? 0.1573 0.1961 0.1626 -0.0057 0.0006  0.0178  911  THR   A N   
6804 C  CA  . THR   A 886 ? 0.1556 0.1923 0.1580 -0.0074 0.0005  0.0157  911  THR   A CA  
6805 C  C   . THR   A 886 ? 0.1624 0.2012 0.1633 -0.0101 0.0000  0.0158  911  THR   A C   
6806 O  O   . THR   A 886 ? 0.1676 0.2037 0.1662 -0.0114 0.0001  0.0140  911  THR   A O   
6807 C  CB  . THR   A 886 ? 0.1720 0.2083 0.1737 -0.0072 0.0007  0.0150  911  THR   A CB  
6808 O  OG1 . THR   A 886 ? 0.1844 0.2169 0.1838 -0.0076 0.0011  0.0127  911  THR   A OG1 
6809 C  CG2 . THR   A 886 ? 0.1801 0.2206 0.1814 -0.0089 0.0000  0.0161  911  THR   A CG2 
6810 N  N   . ILE   A 887 ? 0.1649 0.2085 0.1673 -0.0110 -0.0007 0.0179  912  ILE   A N   
6811 C  CA  . ILE   A 887 ? 0.1726 0.2187 0.1737 -0.0138 -0.0014 0.0181  912  ILE   A CA  
6812 C  C   . ILE   A 887 ? 0.1801 0.2241 0.1810 -0.0140 -0.0011 0.0175  912  ILE   A C   
6813 O  O   . ILE   A 887 ? 0.1834 0.2258 0.1818 -0.0160 -0.0012 0.0160  912  ILE   A O   
6814 C  CB  . ILE   A 887 ? 0.1808 0.2328 0.1842 -0.0143 -0.0023 0.0210  912  ILE   A CB  
6815 C  CG1 . ILE   A 887 ? 0.1910 0.2450 0.1935 -0.0150 -0.0027 0.0213  912  ILE   A CG1 
6816 C  CG2 . ILE   A 887 ? 0.2001 0.2552 0.2032 -0.0168 -0.0030 0.0218  912  ILE   A CG2 
6817 C  CD1 . ILE   A 887 ? 0.1949 0.2545 0.2002 -0.0147 -0.0034 0.0243  912  ILE   A CD1 
6818 N  N   . GLU   A 888 ? 0.1706 0.2143 0.1740 -0.0118 -0.0007 0.0186  913  GLU   A N   
6819 C  CA  . GLU   A 888 ? 0.1773 0.2191 0.1806 -0.0120 -0.0004 0.0182  913  GLU   A CA  
6820 C  C   . GLU   A 888 ? 0.1728 0.2090 0.1736 -0.0118 0.0002  0.0155  913  GLU   A C   
6821 O  O   . GLU   A 888 ? 0.1809 0.2152 0.1803 -0.0129 0.0004  0.0146  913  GLU   A O   
6822 C  CB  . GLU   A 888 ? 0.1830 0.2254 0.1893 -0.0097 0.0002  0.0199  913  GLU   A CB  
6823 C  CG  . GLU   A 888 ? 0.1861 0.2342 0.1949 -0.0102 -0.0003 0.0226  913  GLU   A CG  
6824 C  CD  . GLU   A 888 ? 0.2374 0.2868 0.2495 -0.0079 0.0004  0.0247  913  GLU   A CD  
6825 O  OE1 . GLU   A 888 ? 0.2160 0.2616 0.2282 -0.0059 0.0013  0.0240  913  GLU   A OE1 
6826 O  OE2 . GLU   A 888 ? 0.2555 0.3098 0.2700 -0.0083 0.0001  0.0272  913  GLU   A OE2 
6827 N  N   . THR   A 889 ? 0.1738 0.2074 0.1742 -0.0102 0.0006  0.0145  914  THR   A N   
6828 C  CA  . THR   A 889 ? 0.1666 0.1951 0.1648 -0.0099 0.0012  0.0122  914  THR   A CA  
6829 C  C   . THR   A 889 ? 0.1630 0.1907 0.1582 -0.0124 0.0011  0.0107  914  THR   A C   
6830 O  O   . THR   A 889 ? 0.1658 0.1901 0.1592 -0.0131 0.0015  0.0092  914  THR   A O   
6831 C  CB  . THR   A 889 ? 0.1759 0.2025 0.1746 -0.0079 0.0015  0.0117  914  THR   A CB  
6832 O  OG1 . THR   A 889 ? 0.1795 0.2065 0.1806 -0.0058 0.0017  0.0130  914  THR   A OG1 
6833 C  CG2 . THR   A 889 ? 0.1902 0.2119 0.1871 -0.0075 0.0021  0.0096  914  THR   A CG2 
6834 N  N   . ILE   A 890 ? 0.1584 0.1888 0.1530 -0.0138 0.0007  0.0109  915  ILE   A N   
6835 C  CA  . ILE   A 890 ? 0.1570 0.1864 0.1483 -0.0165 0.0007  0.0094  915  ILE   A CA  
6836 C  C   . ILE   A 890 ? 0.1640 0.1946 0.1544 -0.0188 0.0003  0.0096  915  ILE   A C   
6837 O  O   . ILE   A 890 ? 0.1844 0.2118 0.1721 -0.0203 0.0008  0.0078  915  ILE   A O   
6838 C  CB  . ILE   A 890 ? 0.1577 0.1900 0.1484 -0.0175 0.0003  0.0098  915  ILE   A CB  
6839 C  CG1 . ILE   A 890 ? 0.1519 0.1825 0.1432 -0.0154 0.0009  0.0093  915  ILE   A CG1 
6840 C  CG2 . ILE   A 890 ? 0.1667 0.1982 0.1537 -0.0206 0.0004  0.0083  915  ILE   A CG2 
6841 C  CD1 . ILE   A 890 ? 0.1741 0.2084 0.1655 -0.0161 0.0004  0.0103  915  ILE   A CD1 
6842 N  N   . GLU   A 891 ? 0.1623 0.1971 0.1551 -0.0189 -0.0004 0.0118  916  GLU   A N   
6843 C  CA  . GLU   A 891 ? 0.1665 0.2027 0.1588 -0.0211 -0.0008 0.0121  916  GLU   A CA  
6844 C  C   . GLU   A 891 ? 0.1761 0.2077 0.1675 -0.0205 0.0000  0.0108  916  GLU   A C   
6845 O  O   . GLU   A 891 ? 0.1838 0.2139 0.1730 -0.0227 0.0001  0.0097  916  GLU   A O   
6846 C  CB  . GLU   A 891 ? 0.1831 0.2247 0.1788 -0.0207 -0.0015 0.0150  916  GLU   A CB  
6847 C  CG  . GLU   A 891 ? 0.1994 0.2459 0.1952 -0.0224 -0.0025 0.0164  916  GLU   A CG  
6848 C  CD  . GLU   A 891 ? 0.2505 0.3026 0.2502 -0.0215 -0.0031 0.0195  916  GLU   A CD  
6849 O  OE1 . GLU   A 891 ? 0.2448 0.2967 0.2472 -0.0191 -0.0026 0.0206  916  GLU   A OE1 
6850 O  OE2 . GLU   A 891 ? 0.2957 0.3525 0.2956 -0.0232 -0.0041 0.0209  916  GLU   A OE2 
6851 N  N   . GLU   A 892 ? 0.1709 0.2002 0.1640 -0.0176 0.0006  0.0109  917  GLU   A N   
6852 C  CA  . GLU   A 892 ? 0.1657 0.1905 0.1579 -0.0169 0.0013  0.0097  917  GLU   A CA  
6853 C  C   . GLU   A 892 ? 0.1848 0.2050 0.1739 -0.0175 0.0020  0.0073  917  GLU   A C   
6854 O  O   . GLU   A 892 ? 0.1856 0.2028 0.1729 -0.0185 0.0024  0.0062  917  GLU   A O   
6855 C  CB  . GLU   A 892 ? 0.1808 0.2043 0.1753 -0.0137 0.0017  0.0103  917  GLU   A CB  
6856 C  CG  . GLU   A 892 ? 0.2214 0.2399 0.2148 -0.0127 0.0024  0.0091  917  GLU   A CG  
6857 C  CD  . GLU   A 892 ? 0.2330 0.2510 0.2258 -0.0140 0.0025  0.0092  917  GLU   A CD  
6858 O  OE1 . GLU   A 892 ? 0.2370 0.2589 0.2310 -0.0153 0.0021  0.0106  917  GLU   A OE1 
6859 O  OE2 . GLU   A 892 ? 0.2397 0.2535 0.2309 -0.0138 0.0031  0.0078  917  GLU   A OE2 
6860 N  N   . ASN   A 893 ? 0.1766 0.1960 0.1651 -0.0169 0.0022  0.0065  918  ASN   A N   
6861 C  CA  . ASN   A 893 ? 0.1773 0.1923 0.1631 -0.0173 0.0031  0.0043  918  ASN   A CA  
6862 C  C   . ASN   A 893 ? 0.1717 0.1863 0.1544 -0.0206 0.0032  0.0033  918  ASN   A C   
6863 O  O   . ASN   A 893 ? 0.1780 0.1884 0.1584 -0.0212 0.0041  0.0016  918  ASN   A O   
6864 C  CB  . ASN   A 893 ? 0.1663 0.1813 0.1521 -0.0163 0.0032  0.0039  918  ASN   A CB  
6865 C  CG  . ASN   A 893 ? 0.1773 0.1919 0.1657 -0.0133 0.0033  0.0046  918  ASN   A CG  
6866 O  OD1 . ASN   A 893 ? 0.1775 0.1901 0.1669 -0.0117 0.0035  0.0047  918  ASN   A OD1 
6867 N  ND2 . ASN   A 893 ? 0.1749 0.1908 0.1639 -0.0126 0.0032  0.0048  918  ASN   A ND2 
6868 N  N   . ILE   A 894 ? 0.1671 0.1862 0.1497 -0.0227 0.0023  0.0043  919  ILE   A N   
6869 C  CA  . ILE   A 894 ? 0.1758 0.1949 0.1553 -0.0262 0.0022  0.0034  919  ILE   A CA  
6870 C  C   . ILE   A 894 ? 0.2016 0.2192 0.1806 -0.0272 0.0024  0.0032  919  ILE   A C   
6871 O  O   . ILE   A 894 ? 0.2074 0.2212 0.1833 -0.0289 0.0032  0.0014  919  ILE   A O   
6872 C  CB  . ILE   A 894 ? 0.1741 0.1991 0.1541 -0.0282 0.0009  0.0050  919  ILE   A CB  
6873 C  CG1 . ILE   A 894 ? 0.1763 0.2023 0.1558 -0.0278 0.0009  0.0049  919  ILE   A CG1 
6874 C  CG2 . ILE   A 894 ? 0.2022 0.2278 0.1790 -0.0323 0.0006  0.0043  919  ILE   A CG2 
6875 C  CD1 . ILE   A 894 ? 0.1887 0.2209 0.1696 -0.0290 -0.0005 0.0070  919  ILE   A CD1 
6876 N  N   . GLY   A 895 ? 0.1910 0.2115 0.1730 -0.0262 0.0017  0.0051  920  GLY   A N   
6877 C  CA  . GLY   A 895 ? 0.1822 0.2016 0.1639 -0.0272 0.0019  0.0051  920  GLY   A CA  
6878 C  C   . GLY   A 895 ? 0.1900 0.2035 0.1706 -0.0257 0.0030  0.0035  920  GLY   A C   
6879 O  O   . GLY   A 895 ? 0.1916 0.2023 0.1700 -0.0273 0.0036  0.0025  920  GLY   A O   
6880 N  N   . TRP   A 896 ? 0.1855 0.1971 0.1676 -0.0225 0.0034  0.0035  921  TRP   A N   
6881 C  CA  . TRP   A 896 ? 0.1760 0.1823 0.1573 -0.0209 0.0044  0.0023  921  TRP   A CA  
6882 C  C   . TRP   A 896 ? 0.1882 0.1901 0.1661 -0.0222 0.0054  0.0001  921  TRP   A C   
6883 O  O   . TRP   A 896 ? 0.1901 0.1881 0.1664 -0.0226 0.0062  -0.0009 921  TRP   A O   
6884 C  CB  . TRP   A 896 ? 0.1779 0.1837 0.1615 -0.0176 0.0044  0.0029  921  TRP   A CB  
6885 C  CG  . TRP   A 896 ? 0.1880 0.1891 0.1714 -0.0157 0.0051  0.0021  921  TRP   A CG  
6886 C  CD1 . TRP   A 896 ? 0.2010 0.2014 0.1857 -0.0141 0.0051  0.0029  921  TRP   A CD1 
6887 C  CD2 . TRP   A 896 ? 0.1961 0.1927 0.1778 -0.0150 0.0061  0.0005  921  TRP   A CD2 
6888 N  NE1 . TRP   A 896 ? 0.2082 0.2040 0.1921 -0.0127 0.0057  0.0020  921  TRP   A NE1 
6889 C  CE2 . TRP   A 896 ? 0.2089 0.2024 0.1911 -0.0131 0.0064  0.0006  921  TRP   A CE2 
6890 C  CE3 . TRP   A 896 ? 0.2036 0.1985 0.1834 -0.0157 0.0068  -0.0009 921  TRP   A CE3 
6891 C  CZ2 . TRP   A 896 ? 0.2238 0.2130 0.2052 -0.0118 0.0073  -0.0005 921  TRP   A CZ2 
6892 C  CZ3 . TRP   A 896 ? 0.2303 0.2207 0.2092 -0.0144 0.0078  -0.0020 921  TRP   A CZ3 
6893 C  CH2 . TRP   A 896 ? 0.2304 0.2181 0.2102 -0.0124 0.0080  -0.0017 921  TRP   A CH2 
6894 N  N   A MET   A 897 ? 0.1849 0.1874 0.1616 -0.0228 0.0056  -0.0005 922  MET   A N   
6895 N  N   B MET   A 897 ? 0.1878 0.1903 0.1645 -0.0229 0.0055  -0.0005 922  MET   A N   
6896 C  CA  A MET   A 897 ? 0.1933 0.1913 0.1667 -0.0240 0.0068  -0.0026 922  MET   A CA  
6897 C  CA  B MET   A 897 ? 0.1984 0.1966 0.1718 -0.0241 0.0068  -0.0027 922  MET   A CA  
6898 C  C   A MET   A 897 ? 0.2120 0.2094 0.1824 -0.0275 0.0070  -0.0035 922  MET   A C   
6899 C  C   B MET   A 897 ? 0.2137 0.2111 0.1841 -0.0275 0.0070  -0.0035 922  MET   A C   
6900 O  O   A MET   A 897 ? 0.2195 0.2121 0.1874 -0.0282 0.0082  -0.0050 922  MET   A O   
6901 O  O   B MET   A 897 ? 0.2205 0.2131 0.1884 -0.0282 0.0082  -0.0050 922  MET   A O   
6902 C  CB  A MET   A 897 ? 0.2059 0.2045 0.1787 -0.0237 0.0071  -0.0032 922  MET   A CB  
6903 C  CB  B MET   A 897 ? 0.2153 0.2144 0.1879 -0.0243 0.0070  -0.0032 922  MET   A CB  
6904 C  CG  A MET   A 897 ? 0.2054 0.1990 0.1752 -0.0242 0.0087  -0.0053 922  MET   A CG  
6905 C  CG  B MET   A 897 ? 0.2342 0.2330 0.2092 -0.0210 0.0071  -0.0028 922  MET   A CG  
6906 S  SD  A MET   A 897 ? 0.1907 0.1788 0.1614 -0.0210 0.0100  -0.0060 922  MET   A SD  
6907 S  SD  B MET   A 897 ? 0.2999 0.2924 0.2744 -0.0187 0.0087  -0.0042 922  MET   A SD  
6908 C  CE  A MET   A 897 ? 0.2168 0.2061 0.1899 -0.0181 0.0100  -0.0055 922  MET   A CE  
6909 C  CE  B MET   A 897 ? 0.3365 0.3273 0.3088 -0.0193 0.0099  -0.0057 922  MET   A CE  
6910 N  N   . ASP   A 898 ? 0.2033 0.2055 0.1740 -0.0298 0.0058  -0.0023 923  ASP   A N   
6911 C  CA  . ASP   A 898 ? 0.2120 0.2138 0.1798 -0.0335 0.0058  -0.0030 923  ASP   A CA  
6912 C  C   . ASP   A 898 ? 0.2391 0.2380 0.2069 -0.0332 0.0063  -0.0032 923  ASP   A C   
6913 O  O   . ASP   A 898 ? 0.2591 0.2543 0.2238 -0.0353 0.0073  -0.0047 923  ASP   A O   
6914 C  CB  . ASP   A 898 ? 0.2287 0.2370 0.1976 -0.0358 0.0042  -0.0014 923  ASP   A CB  
6915 C  CG  . ASP   A 898 ? 0.2672 0.2779 0.2346 -0.0373 0.0038  -0.0015 923  ASP   A CG  
6916 O  OD1 . ASP   A 898 ? 0.2977 0.3045 0.2626 -0.0371 0.0049  -0.0033 923  ASP   A OD1 
6917 O  OD2 . ASP   A 898 ? 0.2737 0.2902 0.2426 -0.0385 0.0023  0.0002  923  ASP   A OD2 
6918 N  N   . LYS   A 899 ? 0.2097 0.2100 0.1809 -0.0307 0.0058  -0.0017 924  LYS   A N   
6919 C  CA  A LYS   A 899 ? 0.2226 0.2204 0.1939 -0.0305 0.0063  -0.0017 924  LYS   A CA  
6920 C  CA  B LYS   A 899 ? 0.2253 0.2232 0.1966 -0.0304 0.0063  -0.0016 924  LYS   A CA  
6921 C  C   . LYS   A 899 ? 0.2492 0.2407 0.2190 -0.0287 0.0077  -0.0031 924  LYS   A C   
6922 O  O   . LYS   A 899 ? 0.2751 0.2631 0.2431 -0.0297 0.0085  -0.0039 924  LYS   A O   
6923 C  CB  A LYS   A 899 ? 0.2345 0.2357 0.2095 -0.0285 0.0055  0.0004  924  LYS   A CB  
6924 C  CB  B LYS   A 899 ? 0.2451 0.2462 0.2202 -0.0282 0.0055  0.0005  924  LYS   A CB  
6925 C  CG  A LYS   A 899 ? 0.2504 0.2491 0.2253 -0.0284 0.0059  0.0005  924  LYS   A CG  
6926 C  CG  B LYS   A 899 ? 0.2785 0.2857 0.2555 -0.0298 0.0042  0.0023  924  LYS   A CG  
6927 C  CD  A LYS   A 899 ? 0.2602 0.2623 0.2384 -0.0268 0.0053  0.0026  924  LYS   A CD  
6928 C  CD  B LYS   A 899 ? 0.3309 0.3408 0.3118 -0.0271 0.0038  0.0043  924  LYS   A CD  
6929 C  CE  A LYS   A 899 ? 0.2914 0.2907 0.2692 -0.0268 0.0059  0.0025  924  LYS   A CE  
6930 C  CE  B LYS   A 899 ? 0.3812 0.3974 0.3645 -0.0282 0.0027  0.0064  924  LYS   A CE  
6931 N  NZ  A LYS   A 899 ? 0.3346 0.3369 0.3155 -0.0253 0.0055  0.0045  924  LYS   A NZ  
6932 N  NZ  B LYS   A 899 ? 0.4219 0.4405 0.4088 -0.0252 0.0025  0.0082  924  LYS   A NZ  
6933 N  N   . ASN   A 900 ? 0.2175 0.2077 0.1884 -0.0260 0.0080  -0.0033 925  ASN   A N   
6934 C  CA  . ASN   A 900 ? 0.2102 0.1952 0.1806 -0.0238 0.0092  -0.0042 925  ASN   A CA  
6935 C  C   . ASN   A 900 ? 0.2251 0.2059 0.1933 -0.0237 0.0106  -0.0060 925  ASN   A C   
6936 O  O   . ASN   A 900 ? 0.2240 0.2003 0.1917 -0.0222 0.0117  -0.0066 925  ASN   A O   
6937 C  CB  . ASN   A 900 ? 0.2105 0.1969 0.1844 -0.0204 0.0086  -0.0029 925  ASN   A CB  
6938 C  CG  . ASN   A 900 ? 0.2282 0.2175 0.2041 -0.0202 0.0076  -0.0012 925  ASN   A CG  
6939 O  OD1 . ASN   A 900 ? 0.2538 0.2413 0.2289 -0.0209 0.0080  -0.0013 925  ASN   A OD1 
6940 N  ND2 . ASN   A 900 ? 0.2259 0.2196 0.2044 -0.0192 0.0066  0.0002  925  ASN   A ND2 
6941 N  N   . PHE   A 901 ? 0.2269 0.2089 0.1936 -0.0252 0.0107  -0.0067 926  PHE   A N   
6942 C  CA  . PHE   A 901 ? 0.2400 0.2177 0.2046 -0.0249 0.0123  -0.0084 926  PHE   A CA  
6943 C  C   . PHE   A 901 ? 0.2484 0.2202 0.2099 -0.0260 0.0140  -0.0099 926  PHE   A C   
6944 O  O   . PHE   A 901 ? 0.2582 0.2258 0.2198 -0.0239 0.0153  -0.0105 926  PHE   A O   
6945 C  CB  . PHE   A 901 ? 0.2382 0.2180 0.2009 -0.0271 0.0123  -0.0091 926  PHE   A CB  
6946 C  CG  . PHE   A 901 ? 0.2684 0.2437 0.2287 -0.0269 0.0142  -0.0109 926  PHE   A CG  
6947 C  CD1 . PHE   A 901 ? 0.2926 0.2666 0.2549 -0.0238 0.0148  -0.0108 926  PHE   A CD1 
6948 C  CD2 . PHE   A 901 ? 0.3073 0.2793 0.2633 -0.0299 0.0155  -0.0126 926  PHE   A CD2 
6949 C  CE1 . PHE   A 901 ? 0.3240 0.2938 0.2842 -0.0235 0.0167  -0.0123 926  PHE   A CE1 
6950 C  CE2 . PHE   A 901 ? 0.3269 0.2943 0.2806 -0.0296 0.0175  -0.0143 926  PHE   A CE2 
6951 C  CZ  . PHE   A 901 ? 0.3263 0.2928 0.2823 -0.0263 0.0182  -0.0141 926  PHE   A CZ  
6952 N  N   A ASP   A 902 ? 0.2474 0.2190 0.2063 -0.0293 0.0140  -0.0105 927  ASP   A N   
6953 N  N   B ASP   A 902 ? 0.2544 0.2262 0.2135 -0.0292 0.0140  -0.0104 927  ASP   A N   
6954 C  CA  A ASP   A 902 ? 0.2697 0.2355 0.2255 -0.0305 0.0158  -0.0120 927  ASP   A CA  
6955 C  CA  B ASP   A 902 ? 0.2840 0.2500 0.2398 -0.0306 0.0157  -0.0119 927  ASP   A CA  
6956 C  C   A ASP   A 902 ? 0.2706 0.2338 0.2281 -0.0281 0.0160  -0.0112 927  ASP   A C   
6957 C  C   B ASP   A 902 ? 0.2770 0.2403 0.2345 -0.0283 0.0160  -0.0112 927  ASP   A C   
6958 O  O   A ASP   A 902 ? 0.2765 0.2343 0.2326 -0.0272 0.0177  -0.0122 927  ASP   A O   
6959 O  O   B ASP   A 902 ? 0.2815 0.2392 0.2373 -0.0275 0.0177  -0.0122 927  ASP   A O   
6960 C  CB  A ASP   A 902 ? 0.2799 0.2460 0.2326 -0.0347 0.0157  -0.0127 927  ASP   A CB  
6961 C  CB  B ASP   A 902 ? 0.3185 0.2854 0.2715 -0.0348 0.0154  -0.0125 927  ASP   A CB  
6962 C  CG  A ASP   A 902 ? 0.3351 0.2946 0.2841 -0.0361 0.0177  -0.0144 927  ASP   A CG  
6963 C  CG  B ASP   A 902 ? 0.4266 0.3940 0.3766 -0.0374 0.0158  -0.0138 927  ASP   A CG  
6964 O  OD1 A ASP   A 902 ? 0.3497 0.3048 0.2966 -0.0357 0.0196  -0.0159 927  ASP   A OD1 
6965 O  OD1 B ASP   A 902 ? 0.4599 0.4222 0.4069 -0.0377 0.0178  -0.0156 927  ASP   A OD1 
6966 O  OD2 A ASP   A 902 ? 0.3780 0.3366 0.3265 -0.0373 0.0176  -0.0142 927  ASP   A OD2 
6967 O  OD2 B ASP   A 902 ? 0.4723 0.4452 0.4229 -0.0391 0.0142  -0.0129 927  ASP   A OD2 
6968 N  N   . LYS   A 903 ? 0.2536 0.2206 0.2141 -0.0270 0.0144  -0.0095 928  LYS   A N   
6969 C  CA  . LYS   A 903 ? 0.2385 0.2033 0.2005 -0.0248 0.0146  -0.0087 928  LYS   A CA  
6970 C  C   . LYS   A 903 ? 0.2296 0.1917 0.1930 -0.0214 0.0153  -0.0087 928  LYS   A C   
6971 O  O   . LYS   A 903 ? 0.2438 0.2016 0.2068 -0.0200 0.0163  -0.0089 928  LYS   A O   
6972 C  CB  . LYS   A 903 ? 0.2466 0.2162 0.2116 -0.0240 0.0128  -0.0068 928  LYS   A CB  
6973 C  CG  . LYS   A 903 ? 0.2916 0.2639 0.2557 -0.0272 0.0122  -0.0065 928  LYS   A CG  
6974 C  CD  . LYS   A 903 ? 0.2816 0.2584 0.2490 -0.0261 0.0107  -0.0045 928  LYS   A CD  
6975 C  CE  . LYS   A 903 ? 0.3540 0.3348 0.3213 -0.0290 0.0099  -0.0038 928  LYS   A CE  
6976 N  NZ  . LYS   A 903 ? 0.3944 0.3720 0.3596 -0.0309 0.0107  -0.0044 928  LYS   A NZ  
6977 N  N   . ILE   A 904 ? 0.2268 0.1917 0.1919 -0.0200 0.0147  -0.0084 929  ILE   A N   
6978 C  CA  . ILE   A 904 ? 0.2290 0.1919 0.1957 -0.0169 0.0153  -0.0083 929  ILE   A CA  
6979 C  C   . ILE   A 904 ? 0.2404 0.1981 0.2046 -0.0172 0.0175  -0.0099 929  ILE   A C   
6980 O  O   . ILE   A 904 ? 0.2585 0.2126 0.2233 -0.0150 0.0184  -0.0098 929  ILE   A O   
6981 C  CB  . ILE   A 904 ? 0.2213 0.1886 0.1904 -0.0157 0.0142  -0.0075 929  ILE   A CB  
6982 C  CG1 . ILE   A 904 ? 0.2189 0.1904 0.1907 -0.0148 0.0124  -0.0058 929  ILE   A CG1 
6983 C  CG2 . ILE   A 904 ? 0.2291 0.1944 0.1995 -0.0130 0.0150  -0.0076 929  ILE   A CG2 
6984 C  CD1 . ILE   A 904 ? 0.2438 0.2198 0.2178 -0.0139 0.0113  -0.0050 929  ILE   A CD1 
6985 N  N   A ARG   A 905 ? 0.2408 0.1978 0.2020 -0.0199 0.0183  -0.0113 930  ARG   A N   
6986 N  N   B ARG   A 905 ? 0.2422 0.1993 0.2034 -0.0199 0.0183  -0.0113 930  ARG   A N   
6987 C  CA  A ARG   A 905 ? 0.2541 0.2056 0.2124 -0.0204 0.0207  -0.0130 930  ARG   A CA  
6988 C  CA  B ARG   A 905 ? 0.2579 0.2095 0.2161 -0.0205 0.0206  -0.0130 930  ARG   A CA  
6989 C  C   A ARG   A 905 ? 0.2730 0.2194 0.2300 -0.0203 0.0220  -0.0133 930  ARG   A C   
6990 C  C   B ARG   A 905 ? 0.2758 0.2222 0.2327 -0.0203 0.0220  -0.0133 930  ARG   A C   
6991 O  O   A ARG   A 905 ? 0.2725 0.2146 0.2296 -0.0182 0.0236  -0.0135 930  ARG   A O   
6992 O  O   B ARG   A 905 ? 0.2773 0.2195 0.2344 -0.0183 0.0236  -0.0136 930  ARG   A O   
6993 C  CB  A ARG   A 905 ? 0.2717 0.2236 0.2266 -0.0239 0.0211  -0.0145 930  ARG   A CB  
6994 C  CB  B ARG   A 905 ? 0.2754 0.2275 0.2301 -0.0243 0.0210  -0.0145 930  ARG   A CB  
6995 C  CG  A ARG   A 905 ? 0.2952 0.2412 0.2465 -0.0249 0.0239  -0.0165 930  ARG   A CG  
6996 C  CG  B ARG   A 905 ? 0.3106 0.2567 0.2615 -0.0255 0.0237  -0.0165 930  ARG   A CG  
6997 C  CD  A ARG   A 905 ? 0.3179 0.2648 0.2659 -0.0282 0.0242  -0.0179 930  ARG   A CD  
6998 C  CD  B ARG   A 905 ? 0.3383 0.2845 0.2850 -0.0298 0.0240  -0.0180 930  ARG   A CD  
6999 N  NE  A ARG   A 905 ? 0.3461 0.2955 0.2922 -0.0317 0.0228  -0.0178 930  ARG   A NE  
7000 N  NE  B ARG   A 905 ? 0.3750 0.3226 0.3204 -0.0327 0.0229  -0.0178 930  ARG   A NE  
7001 C  CZ  A ARG   A 905 ? 0.3757 0.3284 0.3200 -0.0347 0.0220  -0.0182 930  ARG   A CZ  
7002 C  CZ  B ARG   A 905 ? 0.4066 0.3498 0.3498 -0.0339 0.0241  -0.0185 930  ARG   A CZ  
7003 N  NH1 A ARG   A 905 ? 0.4021 0.3573 0.3452 -0.0379 0.0207  -0.0180 930  ARG   A NH1 
7004 N  NH1 B ARG   A 905 ? 0.4033 0.3404 0.3456 -0.0323 0.0263  -0.0193 930  ARG   A NH1 
7005 N  NH2 A ARG   A 905 ? 0.3702 0.3237 0.3138 -0.0347 0.0224  -0.0189 930  ARG   A NH2 
7006 N  NH2 B ARG   A 905 ? 0.4215 0.3664 0.3636 -0.0368 0.0230  -0.0183 930  ARG   A NH2 
7007 N  N   . VAL   A 906 ? 0.2839 0.2310 0.2399 -0.0223 0.0212  -0.0131 931  VAL   A N   
7008 C  CA  . VAL   A 906 ? 0.2972 0.2395 0.2518 -0.0224 0.0224  -0.0133 931  VAL   A CA  
7009 C  C   . VAL   A 906 ? 0.3000 0.2415 0.2575 -0.0188 0.0220  -0.0118 931  VAL   A C   
7010 O  O   . VAL   A 906 ? 0.3231 0.2596 0.2800 -0.0174 0.0237  -0.0121 931  VAL   A O   
7011 C  CB  . VAL   A 906 ? 0.3186 0.2626 0.2718 -0.0254 0.0214  -0.0132 931  VAL   A CB  
7012 C  CG1 . VAL   A 906 ? 0.3389 0.2786 0.2912 -0.0252 0.0223  -0.0130 931  VAL   A CG1 
7013 C  CG2 . VAL   A 906 ? 0.3160 0.2601 0.2657 -0.0294 0.0218  -0.0147 931  VAL   A CG2 
7014 N  N   . TRP   A 907 ? 0.2679 0.2143 0.2288 -0.0172 0.0200  -0.0102 932  TRP   A N   
7015 C  CA  . TRP   A 907 ? 0.2717 0.2176 0.2352 -0.0140 0.0195  -0.0088 932  TRP   A CA  
7016 C  C   . TRP   A 907 ? 0.2966 0.2398 0.2611 -0.0114 0.0207  -0.0089 932  TRP   A C   
7017 O  O   . TRP   A 907 ? 0.3199 0.2599 0.2851 -0.0095 0.0214  -0.0083 932  TRP   A O   
7018 C  CB  . TRP   A 907 ? 0.2724 0.2239 0.2389 -0.0130 0.0172  -0.0073 932  TRP   A CB  
7019 C  CG  . TRP   A 907 ? 0.2832 0.2344 0.2520 -0.0103 0.0165  -0.0058 932  TRP   A CG  
7020 C  CD1 . TRP   A 907 ? 0.2940 0.2445 0.2627 -0.0102 0.0160  -0.0050 932  TRP   A CD1 
7021 C  CD2 . TRP   A 907 ? 0.2706 0.2222 0.2418 -0.0073 0.0161  -0.0050 932  TRP   A CD2 
7022 N  NE1 . TRP   A 907 ? 0.2838 0.2343 0.2547 -0.0075 0.0153  -0.0037 932  TRP   A NE1 
7023 C  CE2 . TRP   A 907 ? 0.2850 0.2364 0.2575 -0.0058 0.0152  -0.0036 932  TRP   A CE2 
7024 C  CE3 . TRP   A 907 ? 0.2798 0.2324 0.2524 -0.0060 0.0163  -0.0052 932  TRP   A CE3 
7025 C  CZ2 . TRP   A 907 ? 0.2887 0.2405 0.2635 -0.0031 0.0146  -0.0025 932  TRP   A CZ2 
7026 C  CZ3 . TRP   A 907 ? 0.2880 0.2412 0.2632 -0.0033 0.0157  -0.0040 932  TRP   A CZ3 
7027 C  CH2 . TRP   A 907 ? 0.2859 0.2388 0.2621 -0.0019 0.0148  -0.0026 932  TRP   A CH2 
7028 N  N   . LEU   A 908 ? 0.2810 0.2257 0.2458 -0.0113 0.0210  -0.0095 933  LEU   A N   
7029 C  CA  . LEU   A 908 ? 0.3021 0.2446 0.2681 -0.0088 0.0222  -0.0095 933  LEU   A CA  
7030 C  C   . LEU   A 908 ? 0.3614 0.2976 0.3250 -0.0090 0.0248  -0.0106 933  LEU   A C   
7031 O  O   . LEU   A 908 ? 0.3709 0.3047 0.3361 -0.0064 0.0258  -0.0100 933  LEU   A O   
7032 C  CB  . LEU   A 908 ? 0.2900 0.2351 0.2565 -0.0090 0.0222  -0.0101 933  LEU   A CB  
7033 C  CG  . LEU   A 908 ? 0.2976 0.2486 0.2672 -0.0080 0.0199  -0.0088 933  LEU   A CG  
7034 C  CD1 . LEU   A 908 ? 0.2933 0.2470 0.2624 -0.0092 0.0199  -0.0096 933  LEU   A CD1 
7035 C  CD2 . LEU   A 908 ? 0.3075 0.2589 0.2804 -0.0046 0.0193  -0.0074 933  LEU   A CD2 
7036 N  N   . GLN   A 909 ? 0.3953 0.3291 0.3553 -0.0120 0.0259  -0.0121 934  GLN   A N   
7037 C  CA  . GLN   A 909 ? 0.4537 0.3812 0.4110 -0.0124 0.0286  -0.0133 934  GLN   A CA  
7038 C  C   . GLN   A 909 ? 0.5096 0.4339 0.4672 -0.0112 0.0288  -0.0123 934  GLN   A C   
7039 O  O   . GLN   A 909 ? 0.5398 0.4593 0.4971 -0.0097 0.0309  -0.0124 934  GLN   A O   
7040 C  CB  . GLN   A 909 ? 0.4953 0.4210 0.4482 -0.0163 0.0296  -0.0153 934  GLN   A CB  
7041 C  CG  . GLN   A 909 ? 0.5876 0.5138 0.5393 -0.0172 0.0306  -0.0166 934  GLN   A CG  
7042 C  CD  . GLN   A 909 ? 0.7041 0.6253 0.6555 -0.0152 0.0333  -0.0172 934  GLN   A CD  
7043 O  OE1 . GLN   A 909 ? 0.7485 0.6638 0.6970 -0.0160 0.0358  -0.0183 934  GLN   A OE1 
7044 N  NE2 . GLN   A 909 ? 0.7100 0.6335 0.6644 -0.0126 0.0331  -0.0164 934  GLN   A NE2 
7045 N  N   . SER   A 910 ? 0.5292 0.4563 0.4874 -0.0120 0.0269  -0.0114 935  SER   A N   
7046 C  CA  . SER   A 910 ? 0.5617 0.4862 0.5200 -0.0112 0.0269  -0.0104 935  SER   A CA  
7047 C  C   . SER   A 910 ? 0.5818 0.5069 0.5436 -0.0075 0.0262  -0.0086 935  SER   A C   
7048 O  O   . SER   A 910 ? 0.5936 0.5151 0.5559 -0.0055 0.0278  -0.0084 935  SER   A O   
7049 C  CB  . SER   A 910 ? 0.5812 0.5089 0.5392 -0.0132 0.0251  -0.0100 935  SER   A CB  
7050 O  OG  . SER   A 910 ? 0.6183 0.5467 0.5735 -0.0168 0.0253  -0.0114 935  SER   A OG  
7051 ZN ZN  . ZN    B .   ? 0.1689 0.1635 0.1738 0.0118  0.0100  0.0167  1001 ZN    A ZN  
7052 C  C1  . MLT   C .   ? 0.3088 0.3140 0.3185 0.0105  0.0049  0.0147  1002 MLT   A C1  
7053 O  O1  . MLT   C .   ? 0.3386 0.3429 0.3478 0.0101  0.0039  0.0137  1002 MLT   A O1  
7054 O  O2  . MLT   C .   ? 0.3140 0.3218 0.3248 0.0107  0.0051  0.0153  1002 MLT   A O2  
7055 C  C2  . MLT   C .   ? 0.2701 0.2729 0.2786 0.0108  0.0059  0.0152  1002 MLT   A C2  
7056 O  O3  . MLT   C .   ? 0.2724 0.2725 0.2792 0.0104  0.0054  0.0143  1002 MLT   A O3  
7057 C  C3  . MLT   C .   ? 0.2208 0.2227 0.2296 0.0110  0.0068  0.0159  1002 MLT   A C3  
7058 C  C4  . MLT   C .   ? 0.1930 0.1921 0.2005 0.0113  0.0081  0.0163  1002 MLT   A C4  
7059 O  O4  . MLT   C .   ? 0.1842 0.1804 0.1904 0.0110  0.0084  0.0160  1002 MLT   A O4  
7060 O  O5  . MLT   C .   ? 0.1776 0.1772 0.1852 0.0119  0.0088  0.0170  1002 MLT   A O5  
7061 C  C1  . MLT   D .   ? 0.4546 0.4431 0.4769 0.0179  0.0360  0.0439  1003 MLT   A C1  
7062 O  O1  . MLT   D .   ? 0.4606 0.4456 0.4826 0.0184  0.0382  0.0453  1003 MLT   A O1  
7063 O  O2  . MLT   D .   ? 0.4570 0.4480 0.4802 0.0190  0.0353  0.0444  1003 MLT   A O2  
7064 C  C2  . MLT   D .   ? 0.4392 0.4294 0.4610 0.0157  0.0338  0.0417  1003 MLT   A C2  
7065 O  O3  . MLT   D .   ? 0.4473 0.4401 0.4690 0.0153  0.0316  0.0400  1003 MLT   A O3  
7066 C  C3  . MLT   D .   ? 0.4114 0.4057 0.4347 0.0159  0.0333  0.0432  1003 MLT   A C3  
7067 C  C4  . MLT   D .   ? 0.4030 0.3987 0.4260 0.0139  0.0317  0.0413  1003 MLT   A C4  
7068 O  O4  . MLT   D .   ? 0.3749 0.3754 0.3991 0.0138  0.0301  0.0414  1003 MLT   A O4  
7069 O  O5  . MLT   D .   ? 0.4014 0.3934 0.4231 0.0123  0.0320  0.0396  1003 MLT   A O5  
7070 C  C1  . EDO   E .   ? 0.2561 0.2578 0.2747 0.0141  -0.0040 0.0121  1004 EDO   A C1  
7071 O  O1  . EDO   E .   ? 0.2296 0.2316 0.2468 0.0131  -0.0041 0.0116  1004 EDO   A O1  
7072 C  C2  . EDO   E .   ? 0.2825 0.2865 0.3044 0.0147  -0.0039 0.0128  1004 EDO   A C2  
7073 O  O2  . EDO   E .   ? 0.2623 0.2673 0.2849 0.0143  -0.0056 0.0138  1004 EDO   A O2  
7074 C  C1  . EDO   F .   ? 0.1878 0.2247 0.2171 0.0185  0.0147  0.0410  1005 EDO   A C1  
7075 O  O1  . EDO   F .   ? 0.1847 0.2229 0.2151 0.0192  0.0151  0.0423  1005 EDO   A O1  
7076 C  C2  . EDO   F .   ? 0.2001 0.2358 0.2272 0.0170  0.0133  0.0380  1005 EDO   A C2  
7077 O  O2  . EDO   F .   ? 0.2052 0.2446 0.2323 0.0160  0.0118  0.0379  1005 EDO   A O2  
7078 C  C1  . EDO   G .   ? 0.3668 0.4008 0.4138 -0.0018 -0.0023 0.0197  1006 EDO   A C1  
7079 O  O1  . EDO   G .   ? 0.3628 0.3974 0.4102 -0.0006 -0.0004 0.0195  1006 EDO   A O1  
7080 C  C2  . EDO   G .   ? 0.3688 0.4016 0.4143 -0.0005 -0.0028 0.0191  1006 EDO   A C2  
7081 O  O2  . EDO   G .   ? 0.3779 0.4134 0.4264 0.0010  -0.0026 0.0195  1006 EDO   A O2  
7082 C  C1  . EDO   H .   ? 0.2576 0.2687 0.2721 0.0132  0.0099  0.0213  1007 EDO   A C1  
7083 O  O1  . EDO   H .   ? 0.2647 0.2785 0.2796 0.0126  0.0086  0.0208  1007 EDO   A O1  
7084 C  C2  . EDO   H .   ? 0.2469 0.2544 0.2598 0.0127  0.0094  0.0197  1007 EDO   A C2  
7085 O  O2  . EDO   H .   ? 0.2188 0.2264 0.2318 0.0121  0.0087  0.0190  1007 EDO   A O2  
7086 C  C1  . EDO   I .   ? 0.2806 0.3041 0.2986 0.0128  0.0087  0.0245  1008 EDO   A C1  
7087 O  O1  . EDO   I .   ? 0.2688 0.2957 0.2873 0.0120  0.0079  0.0248  1008 EDO   A O1  
7088 C  C2  . EDO   I .   ? 0.2799 0.3028 0.2973 0.0125  0.0083  0.0238  1008 EDO   A C2  
7089 O  O2  . EDO   I .   ? 0.2755 0.2980 0.2916 0.0115  0.0072  0.0220  1008 EDO   A O2  
7090 C  C1  . EDO   J .   ? 0.4321 0.4203 0.4286 0.0081  0.0000  0.0082  1009 EDO   A C1  
7091 O  O1  . EDO   J .   ? 0.4214 0.4109 0.4178 0.0075  0.0008  0.0080  1009 EDO   A O1  
7092 C  C2  . EDO   J .   ? 0.4398 0.4280 0.4372 0.0085  -0.0002 0.0079  1009 EDO   A C2  
7093 O  O2  . EDO   J .   ? 0.4503 0.4407 0.4493 0.0086  0.0000  0.0077  1009 EDO   A O2  
7094 C  C1  . EDO   K .   ? 0.2868 0.2893 0.2745 -0.0101 0.0047  0.0031  1010 EDO   A C1  
7095 O  O1  . EDO   K .   ? 0.2947 0.2977 0.2844 -0.0084 0.0043  0.0043  1010 EDO   A O1  
7096 C  C2  . EDO   K .   ? 0.2863 0.2844 0.2729 -0.0090 0.0055  0.0017  1010 EDO   A C2  
7097 O  O2  . EDO   K .   ? 0.2878 0.2863 0.2761 -0.0070 0.0054  0.0020  1010 EDO   A O2  
7098 C  C1  . EDO   L .   ? 0.4232 0.4151 0.4249 0.0092  0.0011  0.0065  1011 EDO   A C1  
7099 O  O1  . EDO   L .   ? 0.4187 0.4126 0.4204 0.0086  0.0015  0.0063  1011 EDO   A O1  
7100 C  C2  . EDO   L .   ? 0.4369 0.4290 0.4402 0.0101  0.0013  0.0064  1011 EDO   A C2  
7101 O  O2  . EDO   L .   ? 0.4506 0.4447 0.4554 0.0103  0.0009  0.0068  1011 EDO   A O2  
7102 C  C1  . EDO   M .   ? 0.3619 0.3523 0.3210 -0.0350 0.0097  -0.0086 1012 EDO   A C1  
7103 O  O1  . EDO   M .   ? 0.3223 0.3180 0.2838 -0.0342 0.0084  -0.0071 1012 EDO   A O1  
7104 C  C2  . EDO   M .   ? 0.4023 0.3908 0.3566 -0.0390 0.0104  -0.0103 1012 EDO   A C2  
7105 O  O2  . EDO   M .   ? 0.4281 0.4153 0.3806 -0.0389 0.0114  -0.0114 1012 EDO   A O2  
7106 C  C1  . EDO   N .   ? 0.5085 0.4999 0.5087 0.0084  -0.0024 0.0101  1013 EDO   A C1  
7107 O  O1  . EDO   N .   ? 0.5010 0.4939 0.5021 0.0086  -0.0014 0.0102  1013 EDO   A O1  
7108 C  C2  . EDO   N .   ? 0.5053 0.4961 0.5049 0.0086  -0.0024 0.0099  1013 EDO   A C2  
7109 O  O2  . EDO   N .   ? 0.5052 0.4977 0.5060 0.0089  -0.0017 0.0097  1013 EDO   A O2  
7110 C  C1  . EDO   O .   ? 0.4126 0.4110 0.4206 0.0105  0.0043  0.0050  1014 EDO   A C1  
7111 O  O1  . EDO   O .   ? 0.4212 0.4174 0.4294 0.0112  0.0046  0.0049  1014 EDO   A O1  
7112 C  C2  . EDO   O .   ? 0.3935 0.3915 0.3993 0.0093  0.0047  0.0043  1014 EDO   A C2  
7113 O  O2  . EDO   O .   ? 0.3405 0.3393 0.3459 0.0087  0.0057  0.0037  1014 EDO   A O2  
7114 C  C1  . EDO   P .   ? 0.3210 0.3049 0.3233 0.0129  -0.0088 0.0151  1015 EDO   A C1  
7115 O  O1  . EDO   P .   ? 0.2739 0.2563 0.2735 0.0120  -0.0081 0.0140  1015 EDO   A O1  
7116 C  C2  . EDO   P .   ? 0.3587 0.3412 0.3604 0.0133  -0.0096 0.0163  1015 EDO   A C2  
7117 O  O2  . EDO   P .   ? 0.3876 0.3693 0.3868 0.0121  -0.0109 0.0167  1015 EDO   A O2  
7118 C  C1  . EDO   Q .   ? 0.3944 0.3758 0.3932 0.0094  0.0218  -0.0042 1016 EDO   A C1  
7119 O  O1  . EDO   Q .   ? 0.4065 0.3882 0.4030 0.0076  0.0203  -0.0045 1016 EDO   A O1  
7120 C  C2  . EDO   Q .   ? 0.3609 0.3463 0.3619 0.0097  0.0207  -0.0034 1016 EDO   A C2  
7121 O  O2  . EDO   Q .   ? 0.3090 0.2969 0.3126 0.0106  0.0184  -0.0019 1016 EDO   A O2  
7122 C  C1  . EDO   R .   ? 0.3630 0.3755 0.3758 0.0118  0.0073  0.0188  1017 EDO   A C1  
7123 O  O1  . EDO   R .   ? 0.3223 0.3383 0.3364 0.0116  0.0071  0.0195  1017 EDO   A O1  
7124 C  C2  . EDO   R .   ? 0.3875 0.3995 0.3993 0.0112  0.0063  0.0175  1017 EDO   A C2  
7125 O  O2  . EDO   R .   ? 0.3999 0.4127 0.4118 0.0106  0.0054  0.0165  1017 EDO   A O2  
7126 C  C1  . EDO   S .   ? 0.3888 0.4175 0.4096 0.0087  0.0081  0.0184  1018 EDO   A C1  
7127 O  O1  . EDO   S .   ? 0.3831 0.4133 0.4031 0.0087  0.0081  0.0195  1018 EDO   A O1  
7128 C  C2  . EDO   S .   ? 0.3982 0.4275 0.4200 0.0086  0.0087  0.0188  1018 EDO   A C2  
7129 O  O2  . EDO   S .   ? 0.4032 0.4346 0.4245 0.0082  0.0091  0.0190  1018 EDO   A O2  
7130 C  C1  . EDO   T .   ? 0.4255 0.4700 0.4550 0.0133  0.0113  0.0376  1019 EDO   A C1  
7131 O  O1  . EDO   T .   ? 0.4271 0.4765 0.4578 0.0119  0.0101  0.0388  1019 EDO   A O1  
7132 C  C2  . EDO   T .   ? 0.4339 0.4742 0.4601 0.0124  0.0105  0.0344  1019 EDO   A C2  
7133 O  O2  . EDO   T .   ? 0.4579 0.4974 0.4831 0.0123  0.0099  0.0336  1019 EDO   A O2  
7134 N  N1  . A1IMM U .   ? 0.1556 0.1534 0.1547 0.0046  0.0057  0.0026  1020 A1IMM A N1  
7135 C  C4  . A1IMM U .   ? 0.1776 0.1684 0.1831 0.0110  0.0085  0.0026  1020 A1IMM A C4  
7136 C  C5  . A1IMM U .   ? 0.1755 0.1657 0.1787 0.0097  0.0079  0.0023  1020 A1IMM A C5  
7137 C  C6  . A1IMM U .   ? 0.1776 0.1670 0.1783 0.0081  0.0091  0.0010  1020 A1IMM A C6  
7138 C  C7  . A1IMM U .   ? 0.1634 0.1586 0.1629 0.0056  0.0075  0.0014  1020 A1IMM A C7  
7139 C  C8  . A1IMM U .   ? 0.1569 0.1550 0.1573 0.0054  0.0062  0.0024  1020 A1IMM A C8  
7140 C  C10 . A1IMM U .   ? 0.1910 0.1899 0.1876 0.0021  0.0054  0.0026  1020 A1IMM A C10 
7141 C  C13 . A1IMM U .   ? 0.2033 0.1967 0.2033 0.0069  0.0038  0.0042  1020 A1IMM A C13 
7142 C  C15 . A1IMM U .   ? 0.1915 0.1861 0.1921 0.0068  0.0051  0.0032  1020 A1IMM A C15 
7143 CL CL  . A1IMM U .   ? 0.2144 0.2061 0.2168 0.0091  0.0042  0.0043  1020 A1IMM A CL  
7144 C  C14 . A1IMM U .   ? 0.1968 0.1900 0.1976 0.0075  0.0044  0.0038  1020 A1IMM A C14 
7145 C  C12 . A1IMM U .   ? 0.2106 0.2058 0.2097 0.0057  0.0039  0.0042  1020 A1IMM A C12 
7146 C  C16 . A1IMM U .   ? 0.1888 0.1851 0.1883 0.0054  0.0051  0.0031  1020 A1IMM A C16 
7147 C  C11 . A1IMM U .   ? 0.1975 0.1943 0.1965 0.0049  0.0044  0.0037  1020 A1IMM A C11 
7148 S  S   . A1IMM U .   ? 0.2107 0.2103 0.2089 0.0033  0.0043  0.0039  1020 A1IMM A S   
7149 C  C9  . A1IMM U .   ? 0.1743 0.1733 0.1719 0.0030  0.0059  0.0023  1020 A1IMM A C9  
7150 O  O3  . A1IMM U .   ? 0.1704 0.1708 0.1674 0.0021  0.0063  0.0020  1020 A1IMM A O3  
7151 O  O2  . A1IMM U .   ? 0.1667 0.1602 0.1641 0.0045  0.0081  0.0007  1020 A1IMM A O2  
7152 N  N   . A1IMM U .   ? 0.1584 0.1531 0.1596 0.0070  0.0079  0.0016  1020 A1IMM A N   
7153 C  C1  . A1IMM U .   ? 0.1657 0.1577 0.1665 0.0074  0.0093  0.0008  1020 A1IMM A C1  
7154 C  C   . A1IMM U .   ? 0.1822 0.1732 0.1803 0.0058  0.0106  -0.0005 1020 A1IMM A C   
7155 O  O1  . A1IMM U .   ? 0.1878 0.1759 0.1841 0.0053  0.0117  -0.0013 1020 A1IMM A O1  
7156 O  O   . A1IMM U .   ? 0.1752 0.1686 0.1729 0.0048  0.0106  -0.0006 1020 A1IMM A O   
7157 C  C3  . A1IMM U .   ? 0.1693 0.1625 0.1750 0.0104  0.0088  0.0023  1020 A1IMM A C3  
7158 C  C2  . A1IMM U .   ? 0.1637 0.1563 0.1668 0.0088  0.0099  0.0011  1020 A1IMM A C2  
# 
