CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 2009011651121366

Job options:

ID        	=	 2009011651121366
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 10
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


data_5FT9
# 
_entry.id   5FT9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.308 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5FT9         
PDBE  EBI-65971    
WWPDB D_1290065971 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        5FT9 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2016-01-12 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Fernandez-Millan, P.' 1 
'Pinker, F.'           2 
'Schelcher, C.'        3 
'Gobert, A.'           4 
'Giege, P.'            5 
'Sauter, C.'           6 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Structures of Arabidopsis Nuclear Rnase P Alone and with tRNA Reveal Plasticities'              'To be Published' ?  ?    
? ?    ?      ?  ?         0353 ? ?        ?                         
1       'Crystallization and Crystallographic Analysis of an Arabidopsis Nuclear Proteinaceous Rnase P.' 
'Acta Crystallogr.,Sect.F' 71 1372 ? 2015 ACSFEN US 2053-230X ?    ? 26527263 10.1107/S2053230X15017033 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pinker, F.'           1  ? 
primary 'Schelcher, C.'        2  ? 
primary 'Fernandez-Millan, P.' 3  ? 
primary 'Gobert, A.'           4  ? 
primary 'Birck, C.'            5  ? 
primary 'Roblin, P.'           6  ? 
primary 'Giege, P.'            7  ? 
primary 'Sauter, C.'           8  ? 
1       'Pinker, F.'           9  ? 
1       'Giege, P.'            10 ? 
1       'Sauter, C.'           11 ? 
# 
_cell.entry_id           5FT9 
_cell.length_a           70.500 
_cell.length_b           72.800 
_cell.length_c           80.300 
_cell.angle_alpha        63.10 
_cell.angle_beta         72.20 
_cell.angle_gamma        78.40 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         5FT9 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
# 
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 'PROTEINACEOUS RNASE P 2' 60431.070 2 3.1.26.5 ? ? ? 
2 non-polymer syn 'ZINC ION'                65.409    2 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PROTEIN-ONLY RNASE P' 
# 
_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       
;MGAASDQHRSRRHDESSSRPNKKKKVSRNPETNLLFNLNSCSKSKDLSAALALYDAAITSSEVRLSQQHFQTLLYLCSAS
ITDISLQYLAIDRGFEIFDRMVSSGISPNEASVTSVARLAAAKGNGDYAFKVVKEFVSVGGVSIPRLRTYAPALLCFCEK
LEAEKGYEVEEHMEAAGIALEEAEISALLKVSAATGRENKVYRYLHKLREYVGCVSEETLKIIEEWFCGEKAGEVGDNGI
GSDVGMLREAVLNNGGGWHGHGWVGEGKWTVKKGNVSSTGRCLSCSEQLACVDTNEVETQKFVDSLVALAMDRKTKMNSC
ETNVVFSEFQDWLEKHGDYEAIVDGANIGLYQQNFVDGSFSLSQLESVMKELYRESGNNKWPLILLHKRRVKTLLENPTH
RNLVEEWISNGVLYATPPGSNDDWYWLYAAAKLKCLLVTNDEMRDHIFELLGSTFFQKWKERHQVRYTFVKGNLKLEMPS
PFSVVIQESEKGSWHFPVSCENNEESSRTWMCISRQSILDSPKSNGKIPLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGAASDQHRSRRHDESSSRPNKKKKVSRNPETNLLFNLNSCSKSKDLSAALALYDAAITSSEVRLSQQHFQTLLYLCSAS
ITDISLQYLAIDRGFEIFDRMVSSGISPNEASVTSVARLAAAKGNGDYAFKVVKEFVSVGGVSIPRLRTYAPALLCFCEK
LEAEKGYEVEEHMEAAGIALEEAEISALLKVSAATGRENKVYRYLHKLREYVGCVSEETLKIIEEWFCGEKAGEVGDNGI
GSDVGMLREAVLNNGGGWHGHGWVGEGKWTVKKGNVSSTGRCLSCSEQLACVDTNEVETQKFVDSLVALAMDRKTKMNSC
ETNVVFSEFQDWLEKHGDYEAIVDGANIGLYQQNFVDGSFSLSQLESVMKELYRESGNNKWPLILLHKRRVKTLLENPTH
RNLVEEWISNGVLYATPPGSNDDWYWLYAAAKLKCLLVTNDEMRDHIFELLGSTFFQKWKERHQVRYTFVKGNLKLEMPS
PFSVVIQESEKGSWHFPVSCENNEESSRTWMCISRQSILDSPKSNGKIPLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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   GLY n 
1 3   ALA n 
1 4   ALA n 
1 5   SER n 
1 6   ASP n 
1 7   GLN n 
1 8   HIS n 
1 9   ARG n 
1 10  SER n 
1 11  ARG n 
1 12  ARG n 
1 13  HIS n 
1 14  ASP n 
1 15  GLU n 
1 16  SER n 
1 17  SER n 
1 18  SER n 
1 19  ARG n 
1 20  PRO n 
1 21  ASN n 
1 22  LYS n 
1 23  LYS n 
1 24  LYS n 
1 25  LYS n 
1 26  VAL n 
1 27  SER n 
1 28  ARG n 
1 29  ASN n 
1 30  PRO n 
1 31  GLU n 
1 32  THR n 
1 33  ASN n 
1 34  LEU n 
1 35  LEU n 
1 36  PHE n 
1 37  ASN n 
1 38  LEU n 
1 39  ASN n 
1 40  SER n 
1 41  CYS n 
1 42  SER n 
1 43  LYS n 
1 44  SER n 
1 45  LYS n 
1 46  ASP n 
1 47  LEU n 
1 48  SER n 
1 49  ALA n 
1 50  ALA n 
1 51  LEU n 
1 52  ALA n 
1 53  LEU n 
1 54  TYR n 
1 55  ASP n 
1 56  ALA n 
1 57  ALA n 
1 58  ILE n 
1 59  THR n 
1 60  SER n 
1 61  SER n 
1 62  GLU n 
1 63  VAL n 
1 64  ARG n 
1 65  LEU n 
1 66  SER n 
1 67  GLN n 
1 68  GLN n 
1 69  HIS n 
1 70  PHE n 
1 71  GLN n 
1 72  THR n 
1 73  LEU n 
1 74  LEU n 
1 75  TYR n 
1 76  LEU n 
1 77  CYS n 
1 78  SER n 
1 79  ALA n 
1 80  SER n 
1 81  ILE n 
1 82  THR n 
1 83  ASP n 
1 84  ILE n 
1 85  SER n 
1 86  LEU n 
1 87  GLN n 
1 88  TYR n 
1 89  LEU n 
1 90  ALA n 
1 91  ILE n 
1 92  ASP n 
1 93  ARG n 
1 94  GLY n 
1 95  PHE n 
1 96  GLU n 
1 97  ILE n 
1 98  PHE n 
1 99  ASP n 
1 100 ARG n 
1 101 MET n 
1 102 VAL n 
1 103 SER n 
1 104 SER n 
1 105 GLY n 
1 106 ILE n 
1 107 SER n 
1 108 PRO n 
1 109 ASN n 
1 110 GLU n 
1 111 ALA n 
1 112 SER n 
1 113 VAL n 
1 114 THR n 
1 115 SER n 
1 116 VAL n 
1 117 ALA n 
1 118 ARG n 
1 119 LEU n 
1 120 ALA n 
1 121 ALA n 
1 122 ALA n 
1 123 LYS n 
1 124 GLY n 
1 125 ASN n 
1 126 GLY n 
1 127 ASP n 
1 128 TYR n 
1 129 ALA n 
1 130 PHE n 
1 131 LYS n 
1 132 VAL n 
1 133 VAL n 
1 134 LYS n 
1 135 GLU n 
1 136 PHE n 
1 137 VAL n 
1 138 SER n 
1 139 VAL n 
1 140 GLY n 
1 141 GLY n 
1 142 VAL n 
1 143 SER n 
1 144 ILE n 
1 145 PRO n 
1 146 ARG n 
1 147 LEU n 
1 148 ARG n 
1 149 THR n 
1 150 TYR n 
1 151 ALA n 
1 152 PRO n 
1 153 ALA n 
1 154 LEU n 
1 155 LEU n 
1 156 CYS n 
1 157 PHE n 
1 158 CYS n 
1 159 GLU n 
1 160 LYS n 
1 161 LEU n 
1 162 GLU n 
1 163 ALA n 
1 164 GLU n 
1 165 LYS n 
1 166 GLY n 
1 167 TYR n 
1 168 GLU n 
1 169 VAL n 
1 170 GLU n 
1 171 GLU n 
1 172 HIS n 
1 173 MET n 
1 174 GLU n 
1 175 ALA n 
1 176 ALA n 
1 177 GLY n 
1 178 ILE n 
1 179 ALA n 
1 180 LEU n 
1 181 GLU n 
1 182 GLU n 
1 183 ALA n 
1 184 GLU n 
1 185 ILE n 
1 186 SER n 
1 187 ALA n 
1 188 LEU n 
1 189 LEU n 
1 190 LYS n 
1 191 VAL n 
1 192 SER n 
1 193 ALA n 
1 194 ALA n 
1 195 THR n 
1 196 GLY n 
1 197 ARG n 
1 198 GLU n 
1 199 ASN n 
1 200 LYS n 
1 201 VAL n 
1 202 TYR n 
1 203 ARG n 
1 204 TYR n 
1 205 LEU n 
1 206 HIS n 
1 207 LYS n 
1 208 LEU n 
1 209 ARG n 
1 210 GLU n 
1 211 TYR n 
1 212 VAL n 
1 213 GLY n 
1 214 CYS n 
1 215 VAL n 
1 216 SER n 
1 217 GLU n 
1 218 GLU n 
1 219 THR n 
1 220 LEU n 
1 221 LYS n 
1 222 ILE n 
1 223 ILE n 
1 224 GLU n 
1 225 GLU n 
1 226 TRP n 
1 227 PHE n 
1 228 CYS n 
1 229 GLY n 
1 230 GLU n 
1 231 LYS n 
1 232 ALA n 
1 233 GLY n 
1 234 GLU n 
1 235 VAL n 
1 236 GLY n 
1 237 ASP n 
1 238 ASN n 
1 239 GLY n 
1 240 ILE n 
1 241 GLY n 
1 242 SER n 
1 243 ASP n 
1 244 VAL n 
1 245 GLY n 
1 246 MET n 
1 247 LEU n 
1 248 ARG n 
1 249 GLU n 
1 250 ALA n 
1 251 VAL n 
1 252 LEU n 
1 253 ASN n 
1 254 ASN n 
1 255 GLY n 
1 256 GLY n 
1 257 GLY n 
1 258 TRP n 
1 259 HIS n 
1 260 GLY n 
1 261 HIS n 
1 262 GLY n 
1 263 TRP n 
1 264 VAL n 
1 265 GLY n 
1 266 GLU n 
1 267 GLY n 
1 268 LYS n 
1 269 TRP n 
1 270 THR n 
1 271 VAL n 
1 272 LYS n 
1 273 LYS n 
1 274 GLY n 
1 275 ASN n 
1 276 VAL n 
1 277 SER n 
1 278 SER n 
1 279 THR n 
1 280 GLY n 
1 281 ARG n 
1 282 CYS n 
1 283 LEU n 
1 284 SER n 
1 285 CYS n 
1 286 SER n 
1 287 GLU n 
1 288 GLN n 
1 289 LEU n 
1 290 ALA n 
1 291 CYS n 
1 292 VAL n 
1 293 ASP n 
1 294 THR n 
1 295 ASN n 
1 296 GLU n 
1 297 VAL n 
1 298 GLU n 
1 299 THR n 
1 300 GLN n 
1 301 LYS n 
1 302 PHE n 
1 303 VAL n 
1 304 ASP n 
1 305 SER n 
1 306 LEU n 
1 307 VAL n 
1 308 ALA n 
1 309 LEU n 
1 310 ALA n 
1 311 MET n 
1 312 ASP n 
1 313 ARG n 
1 314 LYS n 
1 315 THR n 
1 316 LYS n 
1 317 MET n 
1 318 ASN n 
1 319 SER n 
1 320 CYS n 
1 321 GLU n 
1 322 THR n 
1 323 ASN n 
1 324 VAL n 
1 325 VAL n 
1 326 PHE n 
1 327 SER n 
1 328 GLU n 
1 329 PHE n 
1 330 GLN n 
1 331 ASP n 
1 332 TRP n 
1 333 LEU n 
1 334 GLU n 
1 335 LYS n 
1 336 HIS n 
1 337 GLY n 
1 338 ASP n 
1 339 TYR n 
1 340 GLU n 
1 341 ALA n 
1 342 ILE n 
1 343 VAL n 
1 344 ASP n 
1 345 GLY n 
1 346 ALA n 
1 347 ASN n 
1 348 ILE n 
1 349 GLY n 
1 350 LEU n 
1 351 TYR n 
1 352 GLN n 
1 353 GLN n 
1 354 ASN n 
1 355 PHE n 
1 356 VAL n 
1 357 ASP n 
1 358 GLY n 
1 359 SER n 
1 360 PHE n 
1 361 SER n 
1 362 LEU n 
1 363 SER n 
1 364 GLN n 
1 365 LEU n 
1 366 GLU n 
1 367 SER n 
1 368 VAL n 
1 369 MET n 
1 370 LYS n 
1 371 GLU n 
1 372 LEU n 
1 373 TYR n 
1 374 ARG n 
1 375 GLU n 
1 376 SER n 
1 377 GLY n 
1 378 ASN n 
1 379 ASN n 
1 380 LYS n 
1 381 TRP n 
1 382 PRO n 
1 383 LEU n 
1 384 ILE n 
1 385 LEU n 
1 386 LEU n 
1 387 HIS n 
1 388 LYS n 
1 389 ARG n 
1 390 ARG n 
1 391 VAL n 
1 392 LYS n 
1 393 THR n 
1 394 LEU n 
1 395 LEU n 
1 396 GLU n 
1 397 ASN n 
1 398 PRO n 
1 399 THR n 
1 400 HIS n 
1 401 ARG n 
1 402 ASN n 
1 403 LEU n 
1 404 VAL n 
1 405 GLU n 
1 406 GLU n 
1 407 TRP n 
1 408 ILE n 
1 409 SER n 
1 410 ASN n 
1 411 GLY n 
1 412 VAL n 
1 413 LEU n 
1 414 TYR n 
1 415 ALA n 
1 416 THR n 
1 417 PRO n 
1 418 PRO n 
1 419 GLY n 
1 420 SER n 
1 421 ASN n 
1 422 ASP n 
1 423 ASP n 
1 424 TRP n 
1 425 TYR n 
1 426 TRP n 
1 427 LEU n 
1 428 TYR n 
1 429 ALA n 
1 430 ALA n 
1 431 ALA n 
1 432 LYS n 
1 433 LEU n 
1 434 LYS n 
1 435 CYS n 
1 436 LEU n 
1 437 LEU n 
1 438 VAL n 
1 439 THR n 
1 440 ASN n 
1 441 ASP n 
1 442 GLU n 
1 443 MET n 
1 444 ARG n 
1 445 ASP n 
1 446 HIS n 
1 447 ILE n 
1 448 PHE n 
1 449 GLU n 
1 450 LEU n 
1 451 LEU n 
1 452 GLY n 
1 453 SER n 
1 454 THR n 
1 455 PHE n 
1 456 PHE n 
1 457 GLN n 
1 458 LYS n 
1 459 TRP n 
1 460 LYS n 
1 461 GLU n 
1 462 ARG n 
1 463 HIS n 
1 464 GLN n 
1 465 VAL n 
1 466 ARG n 
1 467 TYR n 
1 468 THR n 
1 469 PHE n 
1 470 VAL n 
1 471 LYS n 
1 472 GLY n 
1 473 ASN n 
1 474 LEU n 
1 475 LYS n 
1 476 LEU n 
1 477 GLU n 
1 478 MET n 
1 479 PRO n 
1 480 SER n 
1 481 PRO n 
1 482 PHE n 
1 483 SER n 
1 484 VAL n 
1 485 VAL n 
1 486 ILE n 
1 487 GLN n 
1 488 GLU n 
1 489 SER n 
1 490 GLU n 
1 491 LYS n 
1 492 GLY n 
1 493 SER n 
1 494 TRP n 
1 495 HIS n 
1 496 PHE n 
1 497 PRO n 
1 498 VAL n 
1 499 SER n 
1 500 CYS n 
1 501 GLU n 
1 502 ASN n 
1 503 ASN n 
1 504 GLU n 
1 505 GLU n 
1 506 SER n 
1 507 SER n 
1 508 ARG n 
1 509 THR n 
1 510 TRP n 
1 511 MET n 
1 512 CYS n 
1 513 ILE n 
1 514 SER n 
1 515 ARG n 
1 516 GLN n 
1 517 SER n 
1 518 ILE n 
1 519 LEU n 
1 520 ASP n 
1 521 SER n 
1 522 PRO n 
1 523 LYS n 
1 524 SER n 
1 525 ASN n 
1 526 GLY n 
1 527 LYS n 
1 528 ILE n 
1 529 PRO n 
1 530 LEU n 
1 531 GLU n 
1 532 HIS n 
1 533 HIS n 
1 534 HIS n 
1 535 HIS n 
1 536 HIS n 
1 537 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'THALE CRESS' 
_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      'ARABIDOPSIS THALIANA' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_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      'ESCHERICHIA COLI' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               'BL21(DE3)' 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               PET-28B 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PRRP2_ARATH 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          Q680B9 
_struct_ref.pdbx_db_isoform            ? 
# 
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 5FT9 A 3 ? 529 ? Q680B9 2 ? 528 ? 2 528 
2 1 5FT9 B 3 ? 529 ? Q680B9 2 ? 528 ? 2 528 
# 
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 5FT9 MET A 1   ? UNP Q680B9 ? ? 'expression tag' 0   1  
1 5FT9 GLY A 2   ? UNP Q680B9 ? ? 'expression tag' 1   2  
1 5FT9 LEU A 530 ? UNP Q680B9 ? ? 'expression tag' 529 3  
1 5FT9 GLU A 531 ? UNP Q680B9 ? ? 'expression tag' 530 4  
1 5FT9 HIS A 532 ? UNP Q680B9 ? ? 'expression tag' 531 5  
1 5FT9 HIS A 533 ? UNP Q680B9 ? ? 'expression tag' 532 6  
1 5FT9 HIS A 534 ? UNP Q680B9 ? ? 'expression tag' 533 7  
1 5FT9 HIS A 535 ? UNP Q680B9 ? ? 'expression tag' 534 8  
1 5FT9 HIS A 536 ? UNP Q680B9 ? ? 'expression tag' 535 9  
1 5FT9 HIS A 537 ? UNP Q680B9 ? ? 'expression tag' 536 10 
2 5FT9 MET B 1   ? UNP Q680B9 ? ? 'expression tag' 0   11 
2 5FT9 GLY B 2   ? UNP Q680B9 ? ? 'expression tag' 1   12 
2 5FT9 LEU B 530 ? UNP Q680B9 ? ? 'expression tag' 529 13 
2 5FT9 GLU B 531 ? UNP Q680B9 ? ? 'expression tag' 530 14 
2 5FT9 HIS B 532 ? UNP Q680B9 ? ? 'expression tag' 531 15 
2 5FT9 HIS B 533 ? UNP Q680B9 ? ? 'expression tag' 532 16 
2 5FT9 HIS B 534 ? UNP Q680B9 ? ? 'expression tag' 533 17 
2 5FT9 HIS B 535 ? UNP Q680B9 ? ? 'expression tag' 534 18 
2 5FT9 HIS B 536 ? UNP Q680B9 ? ? 'expression tag' 535 19 
2 5FT9 HIS B 537 ? UNP Q680B9 ? ? 'expression tag' 536 20 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
_exptl.entry_id          5FT9 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.9 
_exptl_crystal.density_percent_sol   57.4 
_exptl_crystal.description           NONE 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          MICROBATCH 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
;PRORP2 STOCK SOLUTION WAS PREPARED AT 2.5 MG/ML IN 50 MM HEPES-NA PH 7.5, 250 MM NACL, 5%(W/V) GLYCEROL, 1 MM TCEP. PRORP2 WAS CRYSTALLIZED AT 277 K IN 2 MICROLITER MICROBATCH DROPS SET UP UNDER PARAFIN OIL BY MIXING 1 VOLUME OF PRORP2 SOLUTION WITH 1 VOLUME OF CRYSTALLANT SOLUTION CONTAINING 200 MM SODIUM MALONATE PH 6, 20% (W/V) PEG 3350.
;
# 
_diffrn.id                               1 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.crystal_id                       1 
_diffrn.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 2M' 
_diffrn_detector.pdbx_collection_date   2013-02-23 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SLS BEAMLINE X06DA' 
_diffrn_source.pdbx_synchrotron_site       SLS 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_wavelength             1.0 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     5FT9 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             35.00 
_reflns.d_resolution_high            3.05 
_reflns.number_obs                   23923 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         92.4 
_reflns.pdbx_Rmerge_I_obs            0.12 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        8.70 
_reflns.B_iso_Wilson_estimate        93.61 
_reflns.pdbx_redundancy              3.5 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             3.05 
_reflns_shell.d_res_low              3.23 
_reflns_shell.percent_possible_all   98.2 
_reflns_shell.Rmerge_I_obs           1.50 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    0.80 
_reflns_shell.pdbx_redundancy        3.7 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 5FT9 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     23727 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.91 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             34.707 
_refine.ls_d_res_high                            3.050 
_refine.ls_percent_reflns_obs                    92.20 
_refine.ls_R_factor_obs                          0.2444 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2421 
_refine.ls_R_factor_R_free                       0.2897 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_number_reflns_R_free                  1126 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               145.9 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 4G26' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.69 
_refine.pdbx_overall_phase_error                 43.31 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        7442 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               7444 
_refine_hist.d_res_high                       3.050 
_refine_hist.d_res_low                        34.707 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.005  ? ? 7598  'X-RAY DIFFRACTION' ? 
f_angle_d          1.148  ? ? 10274 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 15.092 ? ? 2746  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.051  ? ? 1125  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 1315  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 3.0500 3.1888  3005 0.4094 98.00 0.4457 . . 157 . . 
'X-RAY DIFFRACTION' . 3.1888 3.3567  3047 0.3954 98.00 0.4433 . . 145 . . 
'X-RAY DIFFRACTION' . 3.3567 3.5669  2888 0.4158 95.00 0.4797 . . 131 . . 
'X-RAY DIFFRACTION' . 3.5669 3.8419  2168 0.3538 70.00 0.4782 . . 102 . . 
'X-RAY DIFFRACTION' . 3.8419 4.2280  2428 0.2740 79.00 0.3141 . . 119 . . 
'X-RAY DIFFRACTION' . 4.2280 4.8383  3025 0.1999 99.00 0.2637 . . 148 . . 
'X-RAY DIFFRACTION' . 4.8383 6.0904  3028 0.2126 99.00 0.2811 . . 156 . . 
'X-RAY DIFFRACTION' . 6.0904 34.7095 3012 0.1668 99.00 0.1985 . . 168 . . 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.details        ? 
_struct_ncs_oper.matrix[1][1]   -0.913800 
_struct_ncs_oper.matrix[1][2]   0.406200 
_struct_ncs_oper.matrix[1][3]   0.007688 
_struct_ncs_oper.matrix[2][1]   0.406200 
_struct_ncs_oper.matrix[2][2]   0.913800 
_struct_ncs_oper.matrix[2][3]   -0.005994 
_struct_ncs_oper.matrix[3][1]   -0.009460 
_struct_ncs_oper.matrix[3][2]   -0.002355 
_struct_ncs_oper.matrix[3][3]   -1.000000 
_struct_ncs_oper.vector[1]      14.62000 
_struct_ncs_oper.vector[2]      12.05000 
_struct_ncs_oper.vector[3]      64.25000 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 ? 1 
2 ? 2 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
# 
_struct.entry_id                  5FT9 
_struct.title                     'Arabidopsis thaliana nuclear protein-only RNase P 2 (PRORP2)' 
_struct.pdbx_descriptor           'PROTEINACEOUS RNASE P 2 (E.C.3.1.26.5)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        5FT9 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;HYDROLASE, PROTEINACEOUS RNASE P, PRORP, PPR, TRNA 5' MATURATION
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
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  1  ASN A 29  ? LYS A 45  ? ASN A 28  LYS A 44  1 ? 17 
HELX_P HELX_P2  2  ASP A 46  ? SER A 61  ? ASP A 45  SER A 60  1 ? 16 
HELX_P HELX_P3  3  GLN A 67  ? ASP A 83  ? GLN A 66  ASP A 82  1 ? 17 
HELX_P HELX_P4  4  LEU A 86  ? SER A 103 ? LEU A 85  SER A 102 1 ? 18 
HELX_P HELX_P5  5  ASN A 109 ? LYS A 123 ? ASN A 108 LYS A 122 1 ? 15 
HELX_P HELX_P6  6  ASN A 125 ? GLY A 140 ? ASN A 124 GLY A 139 1 ? 16 
HELX_P HELX_P7  7  ARG A 146 ? LYS A 160 ? ARG A 145 LYS A 159 1 ? 15 
HELX_P HELX_P8  8  GLU A 162 ? GLY A 177 ? GLU A 161 GLY A 176 1 ? 16 
HELX_P HELX_P9  9  GLU A 181 ? THR A 195 ? GLU A 180 THR A 194 1 ? 15 
HELX_P HELX_P10 10 ARG A 197 ? VAL A 212 ? ARG A 196 VAL A 211 1 ? 16 
HELX_P HELX_P11 11 SER A 216 ? CYS A 228 ? SER A 215 CYS A 227 1 ? 13 
HELX_P HELX_P12 12 GLY A 229 ? GLY A 236 ? GLY A 228 GLY A 235 1 ? 8  
HELX_P HELX_P13 13 ASP A 243 ? ASN A 254 ? ASP A 242 ASN A 253 1 ? 12 
HELX_P HELX_P14 14 ASN A 295 ? ASP A 312 ? ASN A 294 ASP A 311 1 ? 18 
HELX_P HELX_P15 15 ASN A 323 ? GLY A 337 ? ASN A 322 GLY A 336 1 ? 15 
HELX_P HELX_P16 16 GLY A 345 ? TYR A 351 ? GLY A 344 TYR A 350 1 ? 7  
HELX_P HELX_P17 17 SER A 361 ? GLY A 377 ? SER A 360 GLY A 376 1 ? 17 
HELX_P HELX_P18 18 LYS A 388 ? ASN A 397 ? LYS A 387 ASN A 396 1 ? 10 
HELX_P HELX_P19 19 ASN A 397 ? GLY A 411 ? ASN A 396 GLY A 410 1 ? 15 
HELX_P HELX_P20 20 ASP A 423 ? LEU A 433 ? ASP A 422 LEU A 432 1 ? 11 
HELX_P HELX_P21 21 ASP A 445 ? GLY A 452 ? ASP A 444 GLY A 451 1 ? 8  
HELX_P HELX_P22 22 SER A 453 ? HIS A 463 ? SER A 452 HIS A 462 1 ? 11 
HELX_P HELX_P23 23 ASN B 29  ? LYS B 45  ? ASN B 28  LYS B 44  1 ? 17 
HELX_P HELX_P24 24 ASP B 46  ? SER B 61  ? ASP B 45  SER B 60  1 ? 16 
HELX_P HELX_P25 25 SER B 66  ? ASP B 83  ? SER B 65  ASP B 82  1 ? 18 
HELX_P HELX_P26 26 LEU B 86  ? SER B 104 ? LEU B 85  SER B 103 1 ? 19 
HELX_P HELX_P27 27 ASN B 109 ? LYS B 123 ? ASN B 108 LYS B 122 1 ? 15 
HELX_P HELX_P28 28 ASN B 125 ? GLY B 140 ? ASN B 124 GLY B 139 1 ? 16 
HELX_P HELX_P29 29 ARG B 146 ? LYS B 160 ? ARG B 145 LYS B 159 1 ? 15 
HELX_P HELX_P30 30 GLU B 162 ? ALA B 176 ? GLU B 161 ALA B 175 1 ? 15 
HELX_P HELX_P31 31 GLU B 181 ? THR B 195 ? GLU B 180 THR B 194 1 ? 15 
HELX_P HELX_P32 32 ARG B 197 ? VAL B 212 ? ARG B 196 VAL B 211 1 ? 16 
HELX_P HELX_P33 33 SER B 216 ? CYS B 228 ? SER B 215 CYS B 227 1 ? 13 
HELX_P HELX_P34 34 GLY B 229 ? GLY B 236 ? GLY B 228 GLY B 235 1 ? 8  
HELX_P HELX_P35 35 ASP B 243 ? ASN B 254 ? ASP B 242 ASN B 253 1 ? 12 
HELX_P HELX_P36 36 ASN B 295 ? ASP B 312 ? ASN B 294 ASP B 311 1 ? 18 
HELX_P HELX_P37 37 ASN B 323 ? HIS B 336 ? ASN B 322 HIS B 335 1 ? 14 
HELX_P HELX_P38 38 GLY B 345 ? TYR B 351 ? GLY B 344 TYR B 350 1 ? 7  
HELX_P HELX_P39 39 SER B 361 ? GLY B 377 ? SER B 360 GLY B 376 1 ? 17 
HELX_P HELX_P40 40 LYS B 388 ? ASN B 397 ? LYS B 387 ASN B 396 1 ? 10 
HELX_P HELX_P41 41 ASN B 397 ? GLY B 411 ? ASN B 396 GLY B 410 1 ? 15 
HELX_P HELX_P42 42 TRP B 424 ? LYS B 434 ? TRP B 423 LYS B 433 1 ? 11 
HELX_P HELX_P43 43 ASP B 445 ? GLY B 452 ? ASP B 444 GLY B 451 1 ? 8  
HELX_P HELX_P44 44 SER B 453 ? HIS B 463 ? SER B 452 HIS B 462 1 ? 11 
# 
_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 
metalc1 metalc ? ? C ZN . ZN ? ? ? 1_555 A CYS 285 SG  ? ? A ZN 1001 A CYS 284 1_555 ? ? ? ? ? ? ? 2.364 ? 
metalc2 metalc ? ? C ZN . ZN ? ? ? 1_555 A CYS 512 SG  ? ? A ZN 1001 A CYS 511 1_555 ? ? ? ? ? ? ? 2.490 ? 
metalc3 metalc ? ? C ZN . ZN ? ? ? 1_555 A HIS 495 NE2 ? ? A ZN 1001 A HIS 494 1_555 ? ? ? ? ? ? ? 2.268 ? 
metalc4 metalc ? ? C ZN . ZN ? ? ? 1_555 A CYS 282 SG  ? ? A ZN 1001 A CYS 281 1_555 ? ? ? ? ? ? ? 2.421 ? 
metalc5 metalc ? ? D ZN . ZN ? ? ? 1_555 B CYS 282 SG  ? ? B ZN 1001 B CYS 281 1_555 ? ? ? ? ? ? ? 2.804 ? 
metalc6 metalc ? ? D ZN . ZN ? ? ? 1_555 B CYS 512 SG  ? ? B ZN 1001 B CYS 511 1_555 ? ? ? ? ? ? ? 2.313 ? 
metalc7 metalc ? ? D ZN . ZN ? ? ? 1_555 B HIS 495 NE2 ? ? B ZN 1001 B HIS 494 1_555 ? ? ? ? ? ? ? 2.290 ? 
metalc8 metalc ? ? D ZN . ZN ? ? ? 1_555 B CYS 285 SG  ? ? B ZN 1001 B CYS 284 1_555 ? ? ? ? ? ? ? 2.217 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  SER 61  A . ? SER 60  A GLU 62  A ? GLU 61  A 1 -15.65 
2  ALA 176 A . ? ALA 175 A GLY 177 A ? GLY 176 A 1 1.18   
3  GLY 239 A . ? GLY 238 A ILE 240 A ? ILE 239 A 1 -3.52  
4  SER 242 A . ? SER 241 A ASP 243 A ? ASP 242 A 1 0.91   
5  GLY 337 A . ? GLY 336 A ASP 338 A ? ASP 337 A 1 3.18   
6  TYR 351 A . ? TYR 350 A GLN 352 A ? GLN 351 A 1 -0.36  
7  SER 359 A . ? SER 358 A PHE 360 A ? PHE 359 A 1 14.15  
8  SER 420 A . ? SER 419 A ASN 421 A ? ASN 420 A 1 -8.78  
9  GLY 124 B . ? GLY 123 B ASN 125 B ? ASN 124 B 1 6.47   
10 ASN 238 B . ? ASN 237 B GLY 239 B ? GLY 238 B 1 -7.88  
11 ILE 240 B . ? ILE 239 B GLY 241 B ? GLY 240 B 1 5.56   
12 GLY 241 B . ? GLY 240 B SER 242 B ? SER 241 B 1 4.32   
13 GLY 337 B . ? GLY 336 B ASP 338 B ? ASP 337 B 1 4.86   
14 SER 420 B . ? SER 419 B ASN 421 B ? ASN 420 B 1 -10.39 
15 LYS 471 B . ? LYS 470 B GLY 472 B ? GLY 471 B 1 11.49  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 4 ? 
AB ? 6 ? 
BA ? 4 ? 
BB ? 2 ? 
BC ? 6 ? 
# 
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 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AB 1 2 ? parallel      
AB 2 3 ? parallel      
AB 3 4 ? parallel      
AB 4 5 ? parallel      
AB 5 6 ? anti-parallel 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BB 1 2 ? anti-parallel 
BC 1 2 ? parallel      
BC 2 3 ? parallel      
BC 3 4 ? parallel      
BC 4 5 ? parallel      
BC 5 6 ? 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 
AA 1 THR A 270 ? GLY A 274 ? THR A 269 GLY A 273 
AA 2 TRP A 510 ? SER A 514 ? TRP A 509 SER A 513 
AA 3 TRP A 494 ? PRO A 497 ? TRP A 493 PRO A 496 
AA 4 GLN A 487 ? GLU A 488 ? GLN A 486 GLU A 487 
AB 1 LEU A 413 ? THR A 416 ? LEU A 412 THR A 415 
AB 2 LEU A 383 ? HIS A 387 ? LEU A 382 HIS A 386 
AB 3 ALA A 341 ? ASP A 344 ? ALA A 340 ASP A 343 
AB 4 LEU A 436 ? VAL A 438 ? LEU A 435 VAL A 437 
AB 5 GLN A 464 ? THR A 468 ? GLN A 463 THR A 467 
AB 6 LYS A 475 ? GLU A 477 ? LYS A 474 GLU A 476 
BA 1 TRP B 269 ? GLY B 274 ? TRP B 268 GLY B 273 
BA 2 TRP B 510 ? ARG B 515 ? TRP B 509 ARG B 514 
BA 3 TRP B 494 ? PRO B 497 ? TRP B 493 PRO B 496 
BA 4 GLN B 487 ? GLU B 488 ? GLN B 486 GLU B 487 
BB 1 ARG B 281 ? CYS B 282 ? ARG B 280 CYS B 281 
BB 2 GLU B 287 ? GLN B 288 ? GLU B 286 GLN B 287 
BC 1 LEU B 413 ? THR B 416 ? LEU B 412 THR B 415 
BC 2 LEU B 383 ? HIS B 387 ? LEU B 382 HIS B 386 
BC 3 ALA B 341 ? ASP B 344 ? ALA B 340 ASP B 343 
BC 4 LEU B 436 ? VAL B 438 ? LEU B 435 VAL B 437 
BC 5 GLN B 464 ? VAL B 470 ? GLN B 463 VAL B 469 
BC 6 ASN B 473 ? GLU B 477 ? ASN B 472 GLU B 476 
# 
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 
AA 1 2 N GLY A 274 ? N GLY A 273 O TRP A 510 ? O TRP A 509 
AA 2 3 N ILE A 513 ? N ILE A 512 O TRP A 494 ? O TRP A 493 
AA 3 4 N HIS A 495 ? N HIS A 494 O GLN A 487 ? O GLN A 486 
AB 1 2 N TYR A 414 ? N TYR A 413 O ILE A 384 ? O ILE A 383 
AB 2 3 N LEU A 383 ? N LEU A 382 O ALA A 341 ? O ALA A 340 
AB 3 4 N ILE A 342 ? N ILE A 341 O LEU A 436 ? O LEU A 435 
AB 4 5 O LEU A 437 ? O LEU A 436 N VAL A 465 ? N VAL A 464 
AB 5 6 N THR A 468 ? N THR A 467 O LYS A 475 ? O LYS A 474 
BA 1 2 N GLY B 274 ? N GLY B 273 O TRP B 510 ? O TRP B 509 
BA 2 3 N ILE B 513 ? N ILE B 512 O TRP B 494 ? O TRP B 493 
BA 3 4 N HIS B 495 ? N HIS B 494 O GLN B 487 ? O GLN B 486 
BB 1 2 N CYS B 282 ? N CYS B 281 O GLU B 287 ? O GLU B 286 
BC 1 2 N TYR B 414 ? N TYR B 413 O ILE B 384 ? O ILE B 383 
BC 2 3 N LEU B 383 ? N LEU B 382 O ALA B 341 ? O ALA B 340 
BC 3 4 N ILE B 342 ? N ILE B 341 O LEU B 436 ? O LEU B 435 
BC 4 5 O LEU B 437 ? O LEU B 436 N VAL B 465 ? N VAL B 464 
BC 5 6 N VAL B 470 ? N VAL B 469 O ASN B 473 ? O ASN B 472 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 1001' 
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 1001' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1 AC1 5 CYS A 282 ? CYS A 281 . ? 1_555 ? 
2 AC1 5 SER A 284 ? SER A 283 . ? 1_555 ? 
3 AC1 5 CYS A 285 ? CYS A 284 . ? 1_555 ? 
4 AC1 5 HIS A 495 ? HIS A 494 . ? 1_555 ? 
5 AC1 5 CYS A 512 ? CYS A 511 . ? 1_555 ? 
6 AC2 4 CYS B 282 ? CYS B 281 . ? 1_555 ? 
7 AC2 4 CYS B 285 ? CYS B 284 . ? 1_555 ? 
8 AC2 4 HIS B 495 ? HIS B 494 . ? 1_555 ? 
9 AC2 4 CYS B 512 ? CYS B 511 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          5FT9 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    5FT9 
_atom_sites.fract_transf_matrix[1][1]   0.014184 
_atom_sites.fract_transf_matrix[1][2]   -0.002912 
_atom_sites.fract_transf_matrix[1][3]   -0.003672 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014023 
_atom_sites.fract_transf_matrix[2][3]   -0.006474 
_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]   0.014406 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
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   . ASN A 1 29  ? 53.375  71.856  1.496   1.00 225.35 ?  28   ASN A N   1 
ATOM   2    C  CA  . ASN A 1 29  ? 52.631  72.160  2.712   1.00 226.20 ?  28   ASN A CA  1 
ATOM   3    C  C   . ASN A 1 29  ? 53.283  71.468  3.906   1.00 222.60 ?  28   ASN A C   1 
ATOM   4    O  O   . ASN A 1 29  ? 53.539  70.266  3.865   1.00 228.85 ?  28   ASN A O   1 
ATOM   5    C  CB  . ASN A 1 29  ? 51.163  71.734  2.559   1.00 227.27 ?  28   ASN A CB  1 
ATOM   6    C  CG  . ASN A 1 29  ? 50.298  72.128  3.753   1.00 224.16 ?  28   ASN A CG  1 
ATOM   7    O  OD1 . ASN A 1 29  ? 50.656  71.899  4.908   1.00 226.50 ?  28   ASN A OD1 1 
ATOM   8    N  ND2 . ASN A 1 29  ? 49.147  72.727  3.471   1.00 221.98 ?  28   ASN A ND2 1 
ATOM   9    N  N   . PRO A 1 30  ? 53.569  72.236  4.971   1.00 203.63 ?  29   PRO A N   1 
ATOM   10   C  CA  . PRO A 1 30  ? 54.205  71.726  6.195   1.00 187.84 ?  29   PRO A CA  1 
ATOM   11   C  C   . PRO A 1 30  ? 53.364  70.670  6.914   1.00 175.44 ?  29   PRO A C   1 
ATOM   12   O  O   . PRO A 1 30  ? 53.911  69.683  7.407   1.00 172.02 ?  29   PRO A O   1 
ATOM   13   C  CB  . PRO A 1 30  ? 54.351  72.980  7.064   1.00 197.41 ?  29   PRO A CB  1 
ATOM   14   C  CG  . PRO A 1 30  ? 54.311  74.122  6.099   1.00 201.12 ?  29   PRO A CG  1 
ATOM   15   C  CD  . PRO A 1 30  ? 53.363  73.693  5.026   1.00 200.61 ?  29   PRO A CD  1 
ATOM   16   N  N   . GLU A 1 31  ? 52.053  70.889  6.975   1.00 185.75 ?  30   GLU A N   1 
ATOM   17   C  CA  . GLU A 1 31  ? 51.128  69.985  7.659   1.00 189.21 ?  30   GLU A CA  1 
ATOM   18   C  C   . GLU A 1 31  ? 51.027  68.627  6.967   1.00 192.50 ?  30   GLU A C   1 
ATOM   19   O  O   . GLU A 1 31  ? 50.925  67.595  7.629   1.00 199.69 ?  30   GLU A O   1 
ATOM   20   C  CB  . GLU A 1 31  ? 49.742  70.625  7.769   1.00 193.45 ?  30   GLU A CB  1 
ATOM   21   C  CG  . GLU A 1 31  ? 49.754  71.992  8.431   1.00 202.20 ?  30   GLU A CG  1 
ATOM   22   C  CD  . GLU A 1 31  ? 48.381  72.632  8.479   1.00 212.29 ?  30   GLU A CD  1 
ATOM   23   O  OE1 . GLU A 1 31  ? 47.485  72.182  7.734   1.00 216.26 ?  30   GLU A OE1 1 
ATOM   24   O  OE2 . GLU A 1 31  ? 48.199  73.595  9.254   1.00 219.76 ?  30   GLU A OE2 1 
ATOM   25   N  N   . THR A 1 32  ? 51.038  68.631  5.638   1.00 213.42 ?  31   THR A N   1 
ATOM   26   C  CA  . THR A 1 32  ? 50.929  67.396  4.868   1.00 212.02 ?  31   THR A CA  1 
ATOM   27   C  C   . THR A 1 32  ? 52.213  66.583  5.016   1.00 228.44 ?  31   THR A C   1 
ATOM   28   O  O   . THR A 1 32  ? 52.198  65.357  4.919   1.00 222.31 ?  31   THR A O   1 
ATOM   29   C  CB  . THR A 1 32  ? 50.658  67.668  3.375   1.00 207.91 ?  31   THR A CB  1 
ATOM   30   O  OG1 . THR A 1 32  ? 51.753  68.400  2.812   1.00 216.98 ?  31   THR A OG1 1 
ATOM   31   C  CG2 . THR A 1 32  ? 49.371  68.463  3.199   1.00 210.40 ?  31   THR A CG2 1 
ATOM   32   N  N   . ASN A 1 33  ? 53.321  67.280  5.247   1.00 262.65 ?  32   ASN A N   1 
ATOM   33   C  CA  . ASN A 1 33  ? 54.596  66.635  5.537   1.00 271.78 ?  32   ASN A CA  1 
ATOM   34   C  C   . ASN A 1 33  ? 54.540  65.956  6.899   1.00 259.25 ?  32   ASN A C   1 
ATOM   35   O  O   . ASN A 1 33  ? 55.126  64.893  7.104   1.00 260.70 ?  32   ASN A O   1 
ATOM   36   C  CB  . ASN A 1 33  ? 55.747  67.647  5.505   1.00 286.68 ?  32   ASN A CB  1 
ATOM   37   C  CG  . ASN A 1 33  ? 56.079  68.114  4.101   1.00 301.38 ?  32   ASN A CG  1 
ATOM   38   O  OD1 . ASN A 1 33  ? 55.278  67.967  3.178   1.00 306.76 ?  32   ASN A OD1 1 
ATOM   39   N  ND2 . ASN A 1 33  ? 57.269  68.683  3.934   1.00 306.96 ?  32   ASN A ND2 1 
ATOM   40   N  N   . LEU A 1 34  ? 53.836  66.594  7.828   1.00 219.63 ?  33   LEU A N   1 
ATOM   41   C  CA  . LEU A 1 34  ? 53.659  66.064  9.174   1.00 178.21 ?  33   LEU A CA  1 
ATOM   42   C  C   . LEU A 1 34  ? 52.805  64.802  9.197   1.00 162.70 ?  33   LEU A C   1 
ATOM   43   O  O   . LEU A 1 34  ? 53.063  63.895  9.981   1.00 175.05 ?  33   LEU A O   1 
ATOM   44   C  CB  . LEU A 1 34  ? 53.030  67.135  10.072  1.00 168.46 ?  33   LEU A CB  1 
ATOM   45   C  CG  . LEU A 1 34  ? 52.556  66.789  11.485  1.00 151.17 ?  33   LEU A CG  1 
ATOM   46   C  CD1 . LEU A 1 34  ? 52.755  67.993  12.386  1.00 149.02 ?  33   LEU A CD1 1 
ATOM   47   C  CD2 . LEU A 1 34  ? 51.091  66.372  11.495  1.00 127.87 ?  33   LEU A CD2 1 
ATOM   48   N  N   . LEU A 1 35  ? 51.790  64.748  8.340   1.00 152.96 ?  34   LEU A N   1 
ATOM   49   C  CA  . LEU A 1 35  ? 50.936  63.568  8.240   1.00 152.28 ?  34   LEU A CA  1 
ATOM   50   C  C   . LEU A 1 35  ? 51.703  62.388  7.650   1.00 155.03 ?  34   LEU A C   1 
ATOM   51   O  O   . LEU A 1 35  ? 51.448  61.235  7.996   1.00 156.53 ?  34   LEU A O   1 
ATOM   52   C  CB  . LEU A 1 35  ? 49.689  63.865  7.401   1.00 163.79 ?  34   LEU A CB  1 
ATOM   53   C  CG  . LEU A 1 35  ? 48.597  62.788  7.401   1.00 161.55 ?  34   LEU A CG  1 
ATOM   54   C  CD1 . LEU A 1 35  ? 47.215  63.423  7.453   1.00 165.62 ?  34   LEU A CD1 1 
ATOM   55   C  CD2 . LEU A 1 35  ? 48.718  61.874  6.184   1.00 160.67 ?  34   LEU A CD2 1 
ATOM   56   N  N   . PHE A 1 36  ? 52.627  62.684  6.742   1.00 156.69 ?  35   PHE A N   1 
ATOM   57   C  CA  . PHE A 1 36  ? 53.515  61.670  6.186   1.00 164.63 ?  35   PHE A CA  1 
ATOM   58   C  C   . PHE A 1 36  ? 54.422  61.099  7.274   1.00 187.00 ?  35   PHE A C   1 
ATOM   59   O  O   . PHE A 1 36  ? 54.601  59.884  7.364   1.00 192.04 ?  35   PHE A O   1 
ATOM   60   C  CB  . PHE A 1 36  ? 54.338  62.262  5.040   1.00 163.80 ?  35   PHE A CB  1 
ATOM   61   C  CG  . PHE A 1 36  ? 55.580  61.483  4.707   1.00 160.67 ?  35   PHE A CG  1 
ATOM   62   C  CD1 . PHE A 1 36  ? 55.518  60.368  3.885   1.00 155.54 ?  35   PHE A CD1 1 
ATOM   63   C  CD2 . PHE A 1 36  ? 56.818  61.890  5.182   1.00 171.06 ?  35   PHE A CD2 1 
ATOM   64   C  CE1 . PHE A 1 36  ? 56.661  59.658  3.567   1.00 162.72 ?  35   PHE A CE1 1 
ATOM   65   C  CE2 . PHE A 1 36  ? 57.965  61.185  4.868   1.00 175.78 ?  35   PHE A CE2 1 
ATOM   66   C  CZ  . PHE A 1 36  ? 57.888  60.068  4.059   1.00 172.88 ?  35   PHE A CZ  1 
ATOM   67   N  N   . ASN A 1 37  ? 54.987  61.980  8.098   1.00 200.38 ?  36   ASN A N   1 
ATOM   68   C  CA  . ASN A 1 37  ? 55.847  61.568  9.207   1.00 181.22 ?  36   ASN A CA  1 
ATOM   69   C  C   . ASN A 1 37  ? 55.094  60.814  10.308  1.00 162.34 ?  36   ASN A C   1 
ATOM   70   O  O   . ASN A 1 37  ? 55.617  59.855  10.874  1.00 165.19 ?  36   ASN A O   1 
ATOM   71   C  CB  . ASN A 1 37  ? 56.558  62.785  9.805   1.00 178.15 ?  36   ASN A CB  1 
ATOM   72   C  CG  . ASN A 1 37  ? 57.746  63.233  8.971   1.00 180.32 ?  36   ASN A CG  1 
ATOM   73   O  OD1 . ASN A 1 37  ? 58.342  62.438  8.244   1.00 179.18 ?  36   ASN A OD1 1 
ATOM   74   N  ND2 . ASN A 1 37  ? 58.101  64.509  9.080   1.00 181.56 ?  36   ASN A ND2 1 
ATOM   75   N  N   . LEU A 1 38  ? 53.876  61.256  10.619  1.00 145.63 ?  37   LEU A N   1 
ATOM   76   C  CA  . LEU A 1 38  ? 53.035  60.568  11.599  1.00 138.29 ?  37   LEU A CA  1 
ATOM   77   C  C   . LEU A 1 38  ? 52.674  59.171  11.126  1.00 139.10 ?  37   LEU A C   1 
ATOM   78   O  O   . LEU A 1 38  ? 52.711  58.216  11.901  1.00 117.49 ?  37   LEU A O   1 
ATOM   79   C  CB  . LEU A 1 38  ? 51.756  61.355  11.888  1.00 112.63 ?  37   LEU A CB  1 
ATOM   80   C  CG  . LEU A 1 38  ? 51.839  62.471  12.926  1.00 119.67 ?  37   LEU A CG  1 
ATOM   81   C  CD1 . LEU A 1 38  ? 50.451  62.787  13.462  1.00 119.16 ?  37   LEU A CD1 1 
ATOM   82   C  CD2 . LEU A 1 38  ? 52.784  62.085  14.055  1.00 111.96 ?  37   LEU A CD2 1 
ATOM   83   N  N   . ASN A 1 39  ? 52.309  59.062  9.851   1.00 151.14 ?  38   ASN A N   1 
ATOM   84   C  CA  . ASN A 1 39  ? 51.992  57.771  9.252   1.00 143.60 ?  38   ASN A CA  1 
ATOM   85   C  C   . ASN A 1 39  ? 53.241  56.915  9.093   1.00 143.00 ?  38   ASN A C   1 
ATOM   86   O  O   . ASN A 1 39  ? 53.177  55.692  9.192   1.00 141.99 ?  38   ASN A O   1 
ATOM   87   C  CB  . ASN A 1 39  ? 51.311  57.961  7.894   1.00 132.45 ?  38   ASN A CB  1 
ATOM   88   C  CG  . ASN A 1 39  ? 49.898  58.500  8.018   1.00 122.03 ?  38   ASN A CG  1 
ATOM   89   O  OD1 . ASN A 1 39  ? 49.466  58.915  9.093   1.00 118.69 ?  38   ASN A OD1 1 
ATOM   90   N  ND2 . ASN A 1 39  ? 49.170  58.501  6.909   1.00 131.19 ?  38   ASN A ND2 1 
ATOM   91   N  N   . SER A 1 40  ? 54.378  57.563  8.853   1.00 145.91 ?  39   SER A N   1 
ATOM   92   C  CA  . SER A 1 40  ? 55.657  56.864  8.774   1.00 144.25 ?  39   SER A CA  1 
ATOM   93   C  C   . SER A 1 40  ? 56.038  56.241  10.113  1.00 140.31 ?  39   SER A C   1 
ATOM   94   O  O   . SER A 1 40  ? 56.625  55.162  10.158  1.00 144.76 ?  39   SER A O   1 
ATOM   95   C  CB  . SER A 1 40  ? 56.763  57.807  8.310   1.00 154.38 ?  39   SER A CB  1 
ATOM   96   O  OG  . SER A 1 40  ? 58.038  57.283  8.635   1.00 162.63 ?  39   SER A OG  1 
ATOM   97   N  N   . CYS A 1 41  ? 55.732  56.943  11.200  1.00 139.11 ?  40   CYS A N   1 
ATOM   98   C  CA  . CYS A 1 41  ? 55.966  56.421  12.544  1.00 126.04 ?  40   CYS A CA  1 
ATOM   99   C  C   . CYS A 1 41  ? 55.024  55.266  12.870  1.00 117.72 ?  40   CYS A C   1 
ATOM   100  O  O   . CYS A 1 41  ? 55.446  54.248  13.417  1.00 117.37 ?  40   CYS A O   1 
ATOM   101  C  CB  . CYS A 1 41  ? 55.815  57.523  13.595  1.00 127.51 ?  40   CYS A CB  1 
ATOM   102  S  SG  . CYS A 1 41  ? 57.329  58.441  13.947  1.00 123.52 ?  40   CYS A SG  1 
ATOM   103  N  N   . SER A 1 42  ? 53.749  55.431  12.524  1.00 118.48 ?  41   SER A N   1 
ATOM   104  C  CA  . SER A 1 42  ? 52.720  54.435  12.823  1.00 106.58 ?  41   SER A CA  1 
ATOM   105  C  C   . SER A 1 42  ? 53.028  53.105  12.131  1.00 96.12  ?  41   SER A C   1 
ATOM   106  O  O   . SER A 1 42  ? 52.647  52.041  12.616  1.00 114.20 ?  41   SER A O   1 
ATOM   107  C  CB  . SER A 1 42  ? 51.339  54.947  12.416  1.00 100.05 ?  41   SER A CB  1 
ATOM   108  O  OG  . SER A 1 42  ? 50.326  54.021  12.764  1.00 92.97  ?  41   SER A OG  1 
ATOM   109  N  N   . LYS A 1 43  ? 53.681  53.177  10.976  1.00 99.51  ?  42   LYS A N   1 
ATOM   110  C  CA  . LYS A 1 43  ? 54.153  51.982  10.280  1.00 102.73 ?  42   LYS A CA  1 
ATOM   111  C  C   . LYS A 1 43  ? 55.106  51.175  11.168  1.00 102.73 ?  42   LYS A C   1 
ATOM   112  O  O   . LYS A 1 43  ? 54.936  49.970  11.340  1.00 103.70 ?  42   LYS A O   1 
ATOM   113  C  CB  . LYS A 1 43  ? 54.858  52.360  8.970   1.00 121.07 ?  42   LYS A CB  1 
ATOM   114  C  CG  . LYS A 1 43  ? 53.955  52.937  7.884   1.00 135.48 ?  42   LYS A CG  1 
ATOM   115  C  CD  . LYS A 1 43  ? 53.026  51.888  7.288   1.00 141.18 ?  42   LYS A CD  1 
ATOM   116  C  CE  . LYS A 1 43  ? 51.564  52.194  7.583   1.00 133.60 ?  42   LYS A CE  1 
ATOM   117  N  NZ  . LYS A 1 43  ? 51.144  53.527  7.064   1.00 139.97 ?  42   LYS A NZ  1 
ATOM   118  N  N   . SER A 1 44  ? 56.112  51.851  11.720  1.00 114.59 ?  43   SER A N   1 
ATOM   119  C  CA  . SER A 1 44  ? 57.117  51.217  12.577  1.00 130.46 ?  43   SER A CA  1 
ATOM   120  C  C   . SER A 1 44  ? 56.789  51.335  14.066  1.00 145.68 ?  43   SER A C   1 
ATOM   121  O  O   . SER A 1 44  ? 57.608  50.974  14.909  1.00 151.86 ?  43   SER A O   1 
ATOM   122  C  CB  . SER A 1 44  ? 58.501  51.816  12.307  1.00 130.38 ?  43   SER A CB  1 
ATOM   123  O  OG  . SER A 1 44  ? 58.519  53.203  12.579  1.00 132.55 ?  43   SER A OG  1 
ATOM   124  N  N   . LYS A 1 45  ? 55.614  51.889  14.365  1.00 149.94 ?  44   LYS A N   1 
ATOM   125  C  CA  . LYS A 1 45  ? 55.057  52.001  15.721  1.00 152.66 ?  44   LYS A CA  1 
ATOM   126  C  C   . LYS A 1 45  ? 56.006  52.664  16.733  1.00 157.74 ?  44   LYS A C   1 
ATOM   127  O  O   . LYS A 1 45  ? 56.046  52.289  17.904  1.00 173.24 ?  44   LYS A O   1 
ATOM   128  C  CB  . LYS A 1 45  ? 54.581  50.623  16.240  1.00 159.83 ?  44   LYS A CB  1 
ATOM   129  C  CG  . LYS A 1 45  ? 55.648  49.587  16.610  1.00 175.69 ?  44   LYS A CG  1 
ATOM   130  C  CD  . LYS A 1 45  ? 55.033  48.283  17.093  1.00 184.38 ?  44   LYS A CD  1 
ATOM   131  C  CE  . LYS A 1 45  ? 56.114  47.277  17.469  1.00 185.35 ?  44   LYS A CE  1 
ATOM   132  N  NZ  . LYS A 1 45  ? 55.541  45.988  17.946  1.00 180.77 ?  44   LYS A NZ  1 
ATOM   133  N  N   . ASP A 1 46  ? 56.746  53.673  16.284  1.00 143.58 ?  45   ASP A N   1 
ATOM   134  C  CA  . ASP A 1 46  ? 57.607  54.443  17.177  1.00 131.15 ?  45   ASP A CA  1 
ATOM   135  C  C   . ASP A 1 46  ? 56.803  55.615  17.737  1.00 118.27 ?  45   ASP A C   1 
ATOM   136  O  O   . ASP A 1 46  ? 56.883  56.731  17.229  1.00 113.18 ?  45   ASP A O   1 
ATOM   137  C  CB  . ASP A 1 46  ? 58.855  54.936  16.432  1.00 133.63 ?  45   ASP A CB  1 
ATOM   138  C  CG  . ASP A 1 46  ? 59.912  55.522  17.361  1.00 142.13 ?  45   ASP A CG  1 
ATOM   139  O  OD1 . ASP A 1 46  ? 59.556  56.227  18.329  1.00 143.60 ?  45   ASP A OD1 1 
ATOM   140  O  OD2 . ASP A 1 46  ? 61.113  55.282  17.112  1.00 145.83 ?  45   ASP A OD2 1 
ATOM   141  N  N   . LEU A 1 47  ? 56.040  55.357  18.795  1.00 115.21 ?  46   LEU A N   1 
ATOM   142  C  CA  . LEU A 1 47  ? 55.170  56.367  19.394  1.00 123.07 ?  46   LEU A CA  1 
ATOM   143  C  C   . LEU A 1 47  ? 55.966  57.500  20.054  1.00 143.21 ?  46   LEU A C   1 
ATOM   144  O  O   . LEU A 1 47  ? 55.508  58.645  20.107  1.00 148.80 ?  46   LEU A O   1 
ATOM   145  C  CB  . LEU A 1 47  ? 54.222  55.708  20.406  1.00 108.56 ?  46   LEU A CB  1 
ATOM   146  C  CG  . LEU A 1 47  ? 53.199  56.586  21.137  1.00 107.75 ?  46   LEU A CG  1 
ATOM   147  C  CD1 . LEU A 1 47  ? 52.211  57.209  20.161  1.00 107.66 ?  46   LEU A CD1 1 
ATOM   148  C  CD2 . LEU A 1 47  ? 52.456  55.783  22.185  1.00 107.20 ?  46   LEU A CD2 1 
ATOM   149  N  N   . SER A 1 48  ? 57.156  57.176  20.553  1.00 151.51 ?  47   SER A N   1 
ATOM   150  C  CA  . SER A 1 48  ? 58.017  58.165  21.199  1.00 155.45 ?  47   SER A CA  1 
ATOM   151  C  C   . SER A 1 48  ? 58.413  59.263  20.215  1.00 157.33 ?  47   SER A C   1 
ATOM   152  O  O   . SER A 1 48  ? 58.390  60.448  20.550  1.00 157.58 ?  47   SER A O   1 
ATOM   153  C  CB  . SER A 1 48  ? 59.263  57.501  21.787  1.00 155.28 ?  47   SER A CB  1 
ATOM   154  O  OG  . SER A 1 48  ? 60.012  56.839  20.784  1.00 162.64 ?  47   SER A OG  1 
ATOM   155  N  N   . ALA A 1 49  ? 58.788  58.859  19.005  1.00 149.08 ?  48   ALA A N   1 
ATOM   156  C  CA  . ALA A 1 49  ? 59.130  59.808  17.953  1.00 136.42 ?  48   ALA A CA  1 
ATOM   157  C  C   . ALA A 1 49  ? 57.885  60.568  17.502  1.00 128.39 ?  48   ALA A C   1 
ATOM   158  O  O   . ALA A 1 49  ? 57.935  61.775  17.270  1.00 132.65 ?  48   ALA A O   1 
ATOM   159  C  CB  . ALA A 1 49  ? 59.777  59.094  16.779  1.00 135.16 ?  48   ALA A CB  1 
ATOM   160  N  N   . ALA A 1 50  ? 56.771  59.851  17.374  1.00 121.16 ?  49   ALA A N   1 
ATOM   161  C  CA  . ALA A 1 50  ? 55.495  60.464  17.020  1.00 130.21 ?  49   ALA A CA  1 
ATOM   162  C  C   . ALA A 1 50  ? 55.084  61.487  18.074  1.00 139.09 ?  49   ALA A C   1 
ATOM   163  O  O   . ALA A 1 50  ? 54.478  62.508  17.756  1.00 151.53 ?  49   ALA A O   1 
ATOM   164  C  CB  . ALA A 1 50  ? 54.418  59.405  16.861  1.00 103.35 ?  49   ALA A CB  1 
ATOM   165  N  N   . LEU A 1 51  ? 55.418  61.198  19.328  1.00 139.77 ?  50   LEU A N   1 
ATOM   166  C  CA  . LEU A 1 51  ? 55.165  62.117  20.430  1.00 142.52 ?  50   LEU A CA  1 
ATOM   167  C  C   . LEU A 1 51  ? 55.964  63.406  20.281  1.00 157.58 ?  50   LEU A C   1 
ATOM   168  O  O   . LEU A 1 51  ? 55.434  64.496  20.487  1.00 168.97 ?  50   LEU A O   1 
ATOM   169  C  CB  . LEU A 1 51  ? 55.499  61.455  21.765  1.00 136.18 ?  50   LEU A CB  1 
ATOM   170  C  CG  . LEU A 1 51  ? 54.335  60.853  22.549  1.00 132.77 ?  50   LEU A CG  1 
ATOM   171  C  CD1 . LEU A 1 51  ? 54.715  60.703  24.013  1.00 135.54 ?  50   LEU A CD1 1 
ATOM   172  C  CD2 . LEU A 1 51  ? 53.085  61.707  22.398  1.00 133.91 ?  50   LEU A CD2 1 
ATOM   173  N  N   . ALA A 1 52  ? 57.242  63.270  19.938  1.00 158.18 ?  51   ALA A N   1 
ATOM   174  C  CA  . ALA A 1 52  ? 58.126  64.418  19.751  1.00 148.76 ?  51   ALA A CA  1 
ATOM   175  C  C   . ALA A 1 52  ? 57.639  65.320  18.617  1.00 158.28 ?  51   ALA A C   1 
ATOM   176  O  O   . ALA A 1 52  ? 57.705  66.545  18.719  1.00 162.33 ?  51   ALA A O   1 
ATOM   177  C  CB  . ALA A 1 52  ? 59.550  63.951  19.485  1.00 132.91 ?  51   ALA A CB  1 
ATOM   178  N  N   . LEU A 1 53  ? 57.168  64.710  17.532  1.00 159.51 ?  52   LEU A N   1 
ATOM   179  C  CA  . LEU A 1 53  ? 56.579  65.464  16.429  1.00 157.28 ?  52   LEU A CA  1 
ATOM   180  C  C   . LEU A 1 53  ? 55.306  66.176  16.872  1.00 148.74 ?  52   LEU A C   1 
ATOM   181  O  O   . LEU A 1 53  ? 55.071  67.326  16.508  1.00 162.52 ?  52   LEU A O   1 
ATOM   182  C  CB  . LEU A 1 53  ? 56.285  64.551  15.236  1.00 159.29 ?  52   LEU A CB  1 
ATOM   183  C  CG  . LEU A 1 53  ? 57.461  63.752  14.673  1.00 164.31 ?  52   LEU A CG  1 
ATOM   184  C  CD1 . LEU A 1 53  ? 57.076  63.066  13.373  1.00 153.33 ?  52   LEU A CD1 1 
ATOM   185  C  CD2 . LEU A 1 53  ? 58.669  64.653  14.469  1.00 176.04 ?  52   LEU A CD2 1 
ATOM   186  N  N   . TYR A 1 54  ? 54.484  65.477  17.648  1.00 132.85 ?  53   TYR A N   1 
ATOM   187  C  CA  . TYR A 1 54  ? 53.265  66.052  18.212  1.00 130.44 ?  53   TYR A CA  1 
ATOM   188  C  C   . TYR A 1 54  ? 53.532  67.215  19.169  1.00 135.83 ?  53   TYR A C   1 
ATOM   189  O  O   . TYR A 1 54  ? 52.862  68.243  19.095  1.00 137.85 ?  53   TYR A O   1 
ATOM   190  C  CB  . TYR A 1 54  ? 52.462  64.959  18.922  1.00 121.84 ?  53   TYR A CB  1 
ATOM   191  C  CG  . TYR A 1 54  ? 51.309  65.460  19.761  1.00 124.70 ?  53   TYR A CG  1 
ATOM   192  C  CD1 . TYR A 1 54  ? 50.198  66.055  19.177  1.00 117.79 ?  53   TYR A CD1 1 
ATOM   193  C  CD2 . TYR A 1 54  ? 51.317  65.299  21.142  1.00 127.90 ?  53   TYR A CD2 1 
ATOM   194  C  CE1 . TYR A 1 54  ? 49.140  66.504  19.950  1.00 119.74 ?  53   TYR A CE1 1 
ATOM   195  C  CE2 . TYR A 1 54  ? 50.265  65.741  21.921  1.00 125.87 ?  53   TYR A CE2 1 
ATOM   196  C  CZ  . TYR A 1 54  ? 49.178  66.340  21.322  1.00 126.85 ?  53   TYR A CZ  1 
ATOM   197  O  OH  . TYR A 1 54  ? 48.132  66.776  22.104  1.00 126.93 ?  53   TYR A OH  1 
ATOM   198  N  N   . ASP A 1 55  ? 54.498  67.048  20.067  1.00 139.98 ?  54   ASP A N   1 
ATOM   199  C  CA  . ASP A 1 55  ? 54.881  68.112  20.996  1.00 157.54 ?  54   ASP A CA  1 
ATOM   200  C  C   . ASP A 1 55  ? 55.449  69.317  20.244  1.00 169.77 ?  54   ASP A C   1 
ATOM   201  O  O   . ASP A 1 55  ? 55.161  70.466  20.579  1.00 180.54 ?  54   ASP A O   1 
ATOM   202  C  CB  . ASP A 1 55  ? 55.899  67.599  22.019  1.00 159.95 ?  54   ASP A CB  1 
ATOM   203  C  CG  . ASP A 1 55  ? 55.332  66.512  22.916  1.00 152.34 ?  54   ASP A CG  1 
ATOM   204  O  OD1 . ASP A 1 55  ? 54.183  66.663  23.385  1.00 147.76 ?  54   ASP A OD1 1 
ATOM   205  O  OD2 . ASP A 1 55  ? 56.040  65.512  23.160  1.00 145.77 ?  54   ASP A OD2 1 
ATOM   206  N  N   . ALA A 1 56  ? 56.269  69.035  19.236  1.00 169.85 ?  55   ALA A N   1 
ATOM   207  C  CA  . ALA A 1 56  ? 56.848  70.061  18.372  1.00 168.79 ?  55   ALA A CA  1 
ATOM   208  C  C   . ALA A 1 56  ? 55.778  70.762  17.537  1.00 168.69 ?  55   ALA A C   1 
ATOM   209  O  O   . ALA A 1 56  ? 55.876  71.958  17.269  1.00 175.29 ?  55   ALA A O   1 
ATOM   210  C  CB  . ALA A 1 56  ? 57.913  69.460  17.467  1.00 160.99 ?  55   ALA A CB  1 
ATOM   211  N  N   . ALA A 1 57  ? 54.762  70.005  17.132  1.00 163.59 ?  56   ALA A N   1 
ATOM   212  C  CA  . ALA A 1 57  ? 53.709  70.511  16.254  1.00 176.39 ?  56   ALA A CA  1 
ATOM   213  C  C   . ALA A 1 57  ? 52.876  71.603  16.914  1.00 189.28 ?  56   ALA A C   1 
ATOM   214  O  O   . ALA A 1 57  ? 52.497  72.580  16.267  1.00 204.97 ?  56   ALA A O   1 
ATOM   215  C  CB  . ALA A 1 57  ? 52.806  69.371  15.806  1.00 176.01 ?  56   ALA A CB  1 
ATOM   216  N  N   . ILE A 1 58  ? 52.572  71.427  18.195  1.00 185.77 ?  57   ILE A N   1 
ATOM   217  C  CA  . ILE A 1 58  ? 51.773  72.404  18.927  1.00 190.68 ?  57   ILE A CA  1 
ATOM   218  C  C   . ILE A 1 58  ? 52.525  73.733  19.040  1.00 216.46 ?  57   ILE A C   1 
ATOM   219  O  O   . ILE A 1 58  ? 51.913  74.791  19.154  1.00 240.66 ?  57   ILE A O   1 
ATOM   220  C  CB  . ILE A 1 58  ? 51.407  71.904  20.339  1.00 174.06 ?  57   ILE A CB  1 
ATOM   221  C  CG1 . ILE A 1 58  ? 51.083  70.410  20.317  1.00 159.20 ?  57   ILE A CG1 1 
ATOM   222  C  CG2 . ILE A 1 58  ? 50.233  72.686  20.898  1.00 177.71 ?  57   ILE A CG2 1 
ATOM   223  C  CD1 . ILE A 1 58  ? 51.039  69.773  21.689  1.00 157.90 ?  57   ILE A CD1 1 
ATOM   224  N  N   . THR A 1 59  ? 53.853  73.657  19.063  1.00 215.05 ?  58   THR A N   1 
ATOM   225  C  CA  . THR A 1 59  ? 54.734  74.826  19.116  1.00 206.72 ?  58   THR A CA  1 
ATOM   226  C  C   . THR A 1 59  ? 55.095  75.481  17.766  1.00 223.95 ?  58   THR A C   1 
ATOM   227  O  O   . THR A 1 59  ? 55.342  76.682  17.705  1.00 222.12 ?  58   THR A O   1 
ATOM   228  C  CB  . THR A 1 59  ? 56.055  74.461  19.828  1.00 172.10 ?  58   THR A CB  1 
ATOM   229  O  OG1 . THR A 1 59  ? 56.834  73.599  18.989  1.00 160.77 ?  58   THR A OG1 1 
ATOM   230  C  CG2 . THR A 1 59  ? 55.772  73.756  21.142  1.00 157.26 ?  58   THR A CG2 1 
ATOM   231  N  N   . SER A 1 60  ? 55.120  74.686  16.699  1.00 247.09 ?  59   SER A N   1 
ATOM   232  C  CA  . SER A 1 60  ? 55.822  75.036  15.452  1.00 253.73 ?  59   SER A CA  1 
ATOM   233  C  C   . SER A 1 60  ? 55.404  76.206  14.523  1.00 247.05 ?  59   SER A C   1 
ATOM   234  O  O   . SER A 1 60  ? 56.265  77.018  14.187  1.00 259.01 ?  59   SER A O   1 
ATOM   235  C  CB  . SER A 1 60  ? 55.866  73.775  14.581  1.00 249.04 ?  59   SER A CB  1 
ATOM   236  O  OG  . SER A 1 60  ? 54.697  73.661  13.793  1.00 246.83 ?  59   SER A OG  1 
ATOM   237  N  N   . SER A 1 61  ? 54.143  76.335  14.101  1.00 246.79 ?  60   SER A N   1 
ATOM   238  C  CA  . SER A 1 61  ? 53.877  77.322  13.026  1.00 244.76 ?  60   SER A CA  1 
ATOM   239  C  C   . SER A 1 61  ? 53.026  78.607  13.234  1.00 208.87 ?  60   SER A C   1 
ATOM   240  O  O   . SER A 1 61  ? 53.273  79.585  12.527  1.00 196.15 ?  60   SER A O   1 
ATOM   241  C  CB  . SER A 1 61  ? 53.252  76.576  11.836  1.00 227.62 ?  60   SER A CB  1 
ATOM   242  O  OG  . SER A 1 61  ? 54.126  75.582  11.333  1.00 213.87 ?  60   SER A OG  1 
ATOM   243  N  N   . GLU A 1 62  ? 52.048  78.660  14.141  1.00 204.09 ?  61   GLU A N   1 
ATOM   244  C  CA  . GLU A 1 62  ? 51.432  77.518  14.800  1.00 196.70 ?  61   GLU A CA  1 
ATOM   245  C  C   . GLU A 1 62  ? 50.597  76.697  13.821  1.00 187.48 ?  61   GLU A C   1 
ATOM   246  O  O   . GLU A 1 62  ? 49.941  77.249  12.937  1.00 180.59 ?  61   GLU A O   1 
ATOM   247  C  CB  . GLU A 1 62  ? 50.557  77.988  15.965  1.00 200.17 ?  61   GLU A CB  1 
ATOM   248  C  CG  . GLU A 1 62  ? 51.323  78.662  17.106  1.00 204.62 ?  61   GLU A CG  1 
ATOM   249  C  CD  . GLU A 1 62  ? 52.246  77.715  17.856  1.00 192.26 ?  61   GLU A CD  1 
ATOM   250  O  OE1 . GLU A 1 62  ? 52.464  76.582  17.383  1.00 178.61 ?  61   GLU A OE1 1 
ATOM   251  O  OE2 . GLU A 1 62  ? 52.761  78.106  18.924  1.00 188.33 ?  61   GLU A OE2 1 
ATOM   252  N  N   . VAL A 1 63  ? 50.631  75.379  13.977  1.00 187.09 ?  62   VAL A N   1 
ATOM   253  C  CA  . VAL A 1 63  ? 49.881  74.487  13.100  1.00 191.75 ?  62   VAL A CA  1 
ATOM   254  C  C   . VAL A 1 63  ? 48.464  74.232  13.602  1.00 193.03 ?  62   VAL A C   1 
ATOM   255  O  O   . VAL A 1 63  ? 48.240  74.117  14.809  1.00 186.18 ?  62   VAL A O   1 
ATOM   256  C  CB  . VAL A 1 63  ? 50.603  73.125  12.952  1.00 177.85 ?  62   VAL A CB  1 
ATOM   257  C  CG1 . VAL A 1 63  ? 49.825  72.187  12.046  1.00 165.54 ?  62   VAL A CG1 1 
ATOM   258  C  CG2 . VAL A 1 63  ? 51.995  73.318  12.408  1.00 183.39 ?  62   VAL A CG2 1 
ATOM   259  N  N   . ARG A 1 64  ? 47.510  74.156  12.674  1.00 196.31 ?  63   ARG A N   1 
ATOM   260  C  CA  . ARG A 1 64  ? 46.213  73.578  12.990  1.00 196.29 ?  63   ARG A CA  1 
ATOM   261  C  C   . ARG A 1 64  ? 46.276  72.139  12.516  1.00 195.15 ?  63   ARG A C   1 
ATOM   262  O  O   . ARG A 1 64  ? 46.676  71.864  11.383  1.00 206.79 ?  63   ARG A O   1 
ATOM   263  C  CB  . ARG A 1 64  ? 45.054  74.313  12.313  1.00 205.11 ?  63   ARG A CB  1 
ATOM   264  C  CG  . ARG A 1 64  ? 44.455  75.458  13.118  1.00 209.64 ?  63   ARG A CG  1 
ATOM   265  C  CD  . ARG A 1 64  ? 43.259  76.064  12.392  1.00 219.08 ?  63   ARG A CD  1 
ATOM   266  N  NE  . ARG A 1 64  ? 42.079  76.148  13.251  1.00 215.83 ?  63   ARG A NE  1 
ATOM   267  C  CZ  . ARG A 1 64  ? 40.875  76.541  12.842  1.00 214.59 ?  63   ARG A CZ  1 
ATOM   268  N  NH1 . ARG A 1 64  ? 40.676  76.888  11.577  1.00 211.99 ?  63   ARG A NH1 1 
ATOM   269  N  NH2 . ARG A 1 64  ? 39.864  76.586  13.700  1.00 214.26 ?  63   ARG A NH2 1 
ATOM   270  N  N   . LEU A 1 65  ? 45.874  71.224  13.388  1.00 181.79 ?  64   LEU A N   1 
ATOM   271  C  CA  . LEU A 1 65  ? 46.022  69.799  13.127  1.00 155.44 ?  64   LEU A CA  1 
ATOM   272  C  C   . LEU A 1 65  ? 44.712  69.204  12.634  1.00 166.90 ?  64   LEU A C   1 
ATOM   273  O  O   . LEU A 1 65  ? 43.671  69.347  13.273  1.00 176.88 ?  64   LEU A O   1 
ATOM   274  C  CB  . LEU A 1 65  ? 46.520  69.070  14.378  1.00 143.94 ?  64   LEU A CB  1 
ATOM   275  C  CG  . LEU A 1 65  ? 47.972  69.318  14.820  1.00 143.89 ?  64   LEU A CG  1 
ATOM   276  C  CD1 . LEU A 1 65  ? 48.189  70.712  15.419  1.00 157.44 ?  64   LEU A CD1 1 
ATOM   277  C  CD2 . LEU A 1 65  ? 48.434  68.252  15.795  1.00 126.38 ?  64   LEU A CD2 1 
ATOM   278  N  N   . SER A 1 66  ? 44.772  68.533  11.490  1.00 170.64 ?  65   SER A N   1 
ATOM   279  C  CA  . SER A 1 66  ? 43.573  67.979  10.892  1.00 167.87 ?  65   SER A CA  1 
ATOM   280  C  C   . SER A 1 66  ? 43.203  66.764  11.725  1.00 127.17 ?  65   SER A C   1 
ATOM   281  O  O   . SER A 1 66  ? 44.040  66.229  12.446  1.00 123.76 ?  65   SER A O   1 
ATOM   282  C  CB  . SER A 1 66  ? 43.813  67.603  9.429   1.00 167.33 ?  65   SER A CB  1 
ATOM   283  O  OG  . SER A 1 66  ? 42.608  67.240  8.775   1.00 171.19 ?  65   SER A OG  1 
ATOM   284  N  N   . GLN A 1 67  ? 41.947  66.340  11.638  1.00 126.21 ?  66   GLN A N   1 
ATOM   285  C  CA  . GLN A 1 67  ? 41.457  65.234  12.453  1.00 120.98 ?  66   GLN A CA  1 
ATOM   286  C  C   . GLN A 1 67  ? 42.254  63.948  12.253  1.00 116.51 ?  66   GLN A C   1 
ATOM   287  O  O   . GLN A 1 67  ? 42.396  63.175  13.189  1.00 128.99 ?  66   GLN A O   1 
ATOM   288  C  CB  . GLN A 1 67  ? 39.972  64.990  12.177  1.00 143.43 ?  66   GLN A CB  1 
ATOM   289  C  CG  . GLN A 1 67  ? 39.077  66.147  12.618  1.00 165.21 ?  66   GLN A CG  1 
ATOM   290  C  CD  . GLN A 1 67  ? 39.022  67.284  11.606  1.00 196.52 ?  66   GLN A CD  1 
ATOM   291  O  OE1 . GLN A 1 67  ? 39.573  67.181  10.510  1.00 212.05 ?  66   GLN A OE1 1 
ATOM   292  N  NE2 . GLN A 1 67  ? 38.350  68.373  11.971  1.00 206.47 ?  66   GLN A NE2 1 
ATOM   293  N  N   . GLN A 1 68  ? 42.800  63.742  11.056  1.00 117.83 ?  67   GLN A N   1 
ATOM   294  C  CA  . GLN A 1 68  ? 43.657  62.583  10.780  1.00 119.08 ?  67   GLN A CA  1 
ATOM   295  C  C   . GLN A 1 68  ? 44.864  62.504  11.713  1.00 130.39 ?  67   GLN A C   1 
ATOM   296  O  O   . GLN A 1 68  ? 45.306  61.409  12.060  1.00 128.81 ?  67   GLN A O   1 
ATOM   297  C  CB  . GLN A 1 68  ? 44.136  62.577  9.324   1.00 117.43 ?  67   GLN A CB  1 
ATOM   298  C  CG  . GLN A 1 68  ? 43.124  62.024  8.324   1.00 130.56 ?  67   GLN A CG  1 
ATOM   299  C  CD  . GLN A 1 68  ? 42.210  63.083  7.745   1.00 146.51 ?  67   GLN A CD  1 
ATOM   300  O  OE1 . GLN A 1 68  ? 41.668  63.919  8.467   1.00 156.34 ?  67   GLN A OE1 1 
ATOM   301  N  NE2 . GLN A 1 68  ? 42.038  63.055  6.428   1.00 149.91 ?  67   GLN A NE2 1 
ATOM   302  N  N   . HIS A 1 69  ? 45.413  63.659  12.085  1.00 139.24 ?  68   HIS A N   1 
ATOM   303  C  CA  . HIS A 1 69  ? 46.592  63.717  12.952  1.00 140.72 ?  68   HIS A CA  1 
ATOM   304  C  C   . HIS A 1 69  ? 46.615  62.873  14.220  1.00 138.47 ?  68   HIS A C   1 
ATOM   305  O  O   . HIS A 1 69  ? 47.478  62.011  14.385  1.00 152.87 ?  68   HIS A O   1 
ATOM   306  C  CB  . HIS A 1 69  ? 47.003  65.165  13.223  1.00 153.55 ?  68   HIS A CB  1 
ATOM   307  C  CG  . HIS A 1 69  ? 47.288  65.962  11.988  1.00 165.93 ?  68   HIS A CG  1 
ATOM   308  N  ND1 . HIS A 1 69  ? 47.882  67.204  12.033  1.00 171.58 ?  68   HIS A ND1 1 
ATOM   309  C  CD2 . HIS A 1 69  ? 47.068  65.698  10.678  1.00 175.51 ?  68   HIS A CD2 1 
ATOM   310  C  CE1 . HIS A 1 69  ? 48.012  67.673  10.805  1.00 184.89 ?  68   HIS A CE1 1 
ATOM   311  N  NE2 . HIS A 1 69  ? 47.527  66.779  9.964   1.00 185.31 ?  68   HIS A NE2 1 
ATOM   312  N  N   . PHE A 1 70  ? 45.688  63.146  15.127  1.00 133.38 ?  69   PHE A N   1 
ATOM   313  C  CA  . PHE A 1 70  ? 45.575  62.323  16.333  1.00 149.44 ?  69   PHE A CA  1 
ATOM   314  C  C   . PHE A 1 70  ? 44.600  61.062  16.268  1.00 152.71 ?  69   PHE A C   1 
ATOM   315  O  O   . PHE A 1 70  ? 44.398  60.241  17.164  1.00 154.52 ?  69   PHE A O   1 
ATOM   316  C  CB  . PHE A 1 70  ? 44.899  63.112  17.434  1.00 153.44 ?  69   PHE A CB  1 
ATOM   317  C  CG  . PHE A 1 70  ? 43.535  63.582  17.064  1.00 140.58 ?  69   PHE A CG  1 
ATOM   318  C  CD1 . PHE A 1 70  ? 42.426  62.789  17.283  1.00 138.01 ?  69   PHE A CD1 1 
ATOM   319  C  CD2 . PHE A 1 70  ? 43.364  64.825  16.476  1.00 141.20 ?  69   PHE A CD2 1 
ATOM   320  C  CE1 . PHE A 1 70  ? 41.163  63.231  16.929  1.00 149.33 ?  69   PHE A CE1 1 
ATOM   321  C  CE2 . PHE A 1 70  ? 42.109  65.274  16.120  1.00 158.46 ?  69   PHE A CE2 1 
ATOM   322  C  CZ  . PHE A 1 70  ? 41.005  64.477  16.345  1.00 164.13 ?  69   PHE A CZ  1 
ATOM   323  N  N   . GLN A 1 71  ? 44.078  60.946  15.051  1.00 138.35 ?  70   GLN A N   1 
ATOM   324  C  CA  . GLN A 1 71  ? 43.347  59.746  14.681  1.00 128.03 ?  70   GLN A CA  1 
ATOM   325  C  C   . GLN A 1 71  ? 44.575  58.847  14.716  1.00 111.16 ?  70   GLN A C   1 
ATOM   326  O  O   . GLN A 1 71  ? 44.619  57.875  15.463  1.00 117.85 ?  70   GLN A O   1 
ATOM   327  C  CB  . GLN A 1 71  ? 42.649  59.638  13.319  1.00 144.15 ?  70   GLN A CB  1 
ATOM   328  C  CG  . GLN A 1 71  ? 41.347  60.422  13.175  1.00 154.27 ?  70   GLN A CG  1 
ATOM   329  C  CD  . GLN A 1 71  ? 40.164  59.775  13.864  1.00 169.11 ?  70   GLN A CD  1 
ATOM   330  O  OE1 . GLN A 1 71  ? 39.526  58.879  13.312  1.00 176.50 ?  70   GLN A OE1 1 
ATOM   331  N  NE2 . GLN A 1 71  ? 39.855  60.237  15.072  1.00 177.10 ?  70   GLN A NE2 1 
ATOM   332  N  N   . THR A 1 72  ? 45.592  59.222  13.944  1.00 99.41  ?  71   THR A N   1 
ATOM   333  C  CA  . THR A 1 72  ? 46.840  58.467  13.855  1.00 98.07  ?  71   THR A CA  1 
ATOM   334  C  C   . THR A 1 72  ? 47.463  58.288  15.228  1.00 123.98 ?  71   THR A C   1 
ATOM   335  O  O   . THR A 1 72  ? 48.005  57.232  15.553  1.00 110.22 ?  71   THR A O   1 
ATOM   336  C  CB  . THR A 1 72  ? 47.875  59.165  12.941  1.00 101.89 ?  71   THR A CB  1 
ATOM   337  O  OG1 . THR A 1 72  ? 47.365  59.263  11.607  1.00 106.14 ?  71   THR A OG1 1 
ATOM   338  C  CG2 . THR A 1 72  ? 49.197  58.402  12.929  1.00 100.93 ?  71   THR A CG2 1 
ATOM   339  N  N   . LEU A 1 73  ? 47.369  59.334  16.038  1.00 126.02 ?  72   LEU A N   1 
ATOM   340  C  CA  . LEU A 1 73  ? 47.964  59.320  17.359  1.00 124.67 ?  72   LEU A CA  1 
ATOM   341  C  C   . LEU A 1 73  ? 47.235  58.368  18.301  1.00 120.85 ?  72   LEU A C   1 
ATOM   342  O  O   . LEU A 1 73  ? 47.865  57.511  18.918  1.00 135.82 ?  72   LEU A O   1 
ATOM   343  C  CB  . LEU A 1 73  ? 47.979  60.737  17.934  1.00 127.17 ?  72   LEU A CB  1 
ATOM   344  C  CG  . LEU A 1 73  ? 49.364  61.232  18.346  1.00 125.64 ?  72   LEU A CG  1 
ATOM   345  C  CD1 . LEU A 1 73  ? 50.355  61.047  17.207  1.00 120.50 ?  72   LEU A CD1 1 
ATOM   346  C  CD2 . LEU A 1 73  ? 49.289  62.681  18.764  1.00 136.29 ?  72   LEU A CD2 1 
ATOM   347  N  N   . LEU A 1 74  ? 45.914  58.500  18.391  1.00 109.60 ?  73   LEU A N   1 
ATOM   348  C  CA  . LEU A 1 74  ? 45.121  57.621  19.253  1.00 104.43 ?  73   LEU A CA  1 
ATOM   349  C  C   . LEU A 1 74  ? 45.191  56.167  18.806  1.00 99.59  ?  73   LEU A C   1 
ATOM   350  O  O   . LEU A 1 74  ? 45.210  55.250  19.628  1.00 92.63  ?  73   LEU A O   1 
ATOM   351  C  CB  . LEU A 1 74  ? 43.660  58.062  19.303  1.00 102.15 ?  73   LEU A CB  1 
ATOM   352  C  CG  . LEU A 1 74  ? 43.252  59.094  20.350  1.00 102.64 ?  73   LEU A CG  1 
ATOM   353  C  CD1 . LEU A 1 74  ? 44.024  60.392  20.213  1.00 113.69 ?  73   LEU A CD1 1 
ATOM   354  C  CD2 . LEU A 1 74  ? 41.763  59.337  20.242  1.00 101.07 ?  73   LEU A CD2 1 
ATOM   355  N  N   . TYR A 1 75  ? 45.216  55.963  17.495  1.00 107.51 ?  74   TYR A N   1 
ATOM   356  C  CA  . TYR A 1 75  ? 45.322  54.623  16.949  1.00 118.34 ?  74   TYR A CA  1 
ATOM   357  C  C   . TYR A 1 75  ? 46.664  54.027  17.358  1.00 118.04 ?  74   TYR A C   1 
ATOM   358  O  O   . TYR A 1 75  ? 46.750  52.857  17.727  1.00 126.09 ?  74   TYR A O   1 
ATOM   359  C  CB  . TYR A 1 75  ? 45.166  54.646  15.422  1.00 120.16 ?  74   TYR A CB  1 
ATOM   360  C  CG  . TYR A 1 75  ? 43.812  55.142  14.942  1.00 128.08 ?  74   TYR A CG  1 
ATOM   361  C  CD1 . TYR A 1 75  ? 42.746  55.293  15.824  1.00 130.84 ?  74   TYR A CD1 1 
ATOM   362  C  CD2 . TYR A 1 75  ? 43.619  55.518  13.617  1.00 138.78 ?  74   TYR A CD2 1 
ATOM   363  C  CE1 . TYR A 1 75  ? 41.518  55.760  15.393  1.00 141.43 ?  74   TYR A CE1 1 
ATOM   364  C  CE2 . TYR A 1 75  ? 42.391  55.987  13.177  1.00 150.71 ?  74   TYR A CE2 1 
ATOM   365  C  CZ  . TYR A 1 75  ? 41.346  56.105  14.072  1.00 150.33 ?  74   TYR A CZ  1 
ATOM   366  O  OH  . TYR A 1 75  ? 40.124  56.567  13.640  1.00 156.33 ?  74   TYR A OH  1 
ATOM   367  N  N   . LEU A 1 76  ? 47.704  54.851  17.322  1.00 85.83  ?  75   LEU A N   1 
ATOM   368  C  CA  . LEU A 1 76  ? 49.034  54.420  17.728  1.00 85.63  ?  75   LEU A CA  1 
ATOM   369  C  C   . LEU A 1 76  ? 49.115  54.149  19.228  1.00 87.43  ?  75   LEU A C   1 
ATOM   370  O  O   . LEU A 1 76  ? 49.873  53.285  19.666  1.00 98.10  ?  75   LEU A O   1 
ATOM   371  C  CB  . LEU A 1 76  ? 50.078  55.464  17.324  1.00 94.00  ?  75   LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 76  ? 51.532  54.988  17.295  1.00 104.26 ?  75   LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 76  ? 51.652  53.692  16.513  1.00 105.03 ?  75   LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 76  ? 52.430  56.054  16.692  1.00 93.66  ?  75   LEU A CD2 1 
ATOM   375  N  N   . CYS A 1 77  ? 48.339  54.893  20.012  1.00 88.25  ?  76   CYS A N   1 
ATOM   376  C  CA  . CYS A 1 77  ? 48.330  54.722  21.464  1.00 93.34  ?  76   CYS A CA  1 
ATOM   377  C  C   . CYS A 1 77  ? 47.799  53.354  21.887  1.00 106.17 ?  76   CYS A C   1 
ATOM   378  O  O   . CYS A 1 77  ? 48.352  52.718  22.783  1.00 96.95  ?  76   CYS A O   1 
ATOM   379  C  CB  . CYS A 1 77  ? 47.503  55.825  22.126  1.00 84.51  ?  76   CYS A CB  1 
ATOM   380  S  SG  . CYS A 1 77  ? 48.314  57.439  22.177  1.00 98.68  ?  76   CYS A SG  1 
ATOM   381  N  N   . SER A 1 78  ? 46.721  52.911  21.246  1.00 120.98 ?  77   SER A N   1 
ATOM   382  C  CA  . SER A 1 78  ? 46.151  51.596  21.521  1.00 111.47 ?  77   SER A CA  1 
ATOM   383  C  C   . SER A 1 78  ? 47.037  50.484  20.993  1.00 111.70 ?  77   SER A C   1 
ATOM   384  O  O   . SER A 1 78  ? 47.183  49.441  21.627  1.00 123.61 ?  77   SER A O   1 
ATOM   385  C  CB  . SER A 1 78  ? 44.769  51.471  20.901  1.00 107.06 ?  77   SER A CB  1 
ATOM   386  O  OG  . SER A 1 78  ? 43.936  52.515  21.337  1.00 109.01 ?  77   SER A OG  1 
ATOM   387  N  N   . ALA A 1 79  ? 47.620  50.718  19.823  1.00 86.25  ?  78   ALA A N   1 
ATOM   388  C  CA  . ALA A 1 79  ? 48.583  49.797  19.241  1.00 85.64  ?  78   ALA A CA  1 
ATOM   389  C  C   . ALA A 1 79  ? 49.761  49.615  20.188  1.00 99.02  ?  78   ALA A C   1 
ATOM   390  O  O   . ALA A 1 79  ? 50.393  48.561  20.216  1.00 102.97 ?  78   ALA A O   1 
ATOM   391  C  CB  . ALA A 1 79  ? 49.051  50.304  17.890  1.00 96.00  ?  78   ALA A CB  1 
ATOM   392  N  N   . SER A 1 80  ? 50.051  50.665  20.951  1.00 110.30 ?  79   SER A N   1 
ATOM   393  C  CA  . SER A 1 80  ? 51.130  50.655  21.934  1.00 116.84 ?  79   SER A CA  1 
ATOM   394  C  C   . SER A 1 80  ? 50.802  49.814  23.170  1.00 103.02 ?  79   SER A C   1 
ATOM   395  O  O   . SER A 1 80  ? 51.704  49.268  23.811  1.00 92.01  ?  79   SER A O   1 
ATOM   396  C  CB  . SER A 1 80  ? 51.463  52.084  22.355  1.00 114.92 ?  79   SER A CB  1 
ATOM   397  O  OG  . SER A 1 80  ? 51.423  52.951  21.240  1.00 101.85 ?  79   SER A OG  1 
ATOM   398  N  N   . ILE A 1 81  ? 49.514  49.714  23.491  1.00 92.88  ?  80   ILE A N   1 
ATOM   399  C  CA  . ILE A 1 81  ? 49.055  49.052  24.711  1.00 86.29  ?  80   ILE A CA  1 
ATOM   400  C  C   . ILE A 1 81  ? 49.588  47.634  24.823  1.00 88.04  ?  80   ILE A C   1 
ATOM   401  O  O   . ILE A 1 81  ? 50.082  47.233  25.877  1.00 93.59  ?  80   ILE A O   1 
ATOM   402  C  CB  . ILE A 1 81  ? 47.521  49.014  24.783  1.00 86.76  ?  80   ILE A CB  1 
ATOM   403  C  CG1 . ILE A 1 81  ? 46.966  50.437  24.791  1.00 106.81 ?  80   ILE A CG1 1 
ATOM   404  C  CG2 . ILE A 1 81  ? 47.060  48.263  26.020  1.00 81.32  ?  80   ILE A CG2 1 
ATOM   405  C  CD1 . ILE A 1 81  ? 45.486  50.514  25.056  1.00 121.45 ?  80   ILE A CD1 1 
ATOM   406  N  N   . THR A 1 82  ? 49.492  46.883  23.732  1.00 87.35  ?  81   THR A N   1 
ATOM   407  C  CA  . THR A 1 82  ? 49.957  45.503  23.718  1.00 100.72 ?  81   THR A CA  1 
ATOM   408  C  C   . THR A 1 82  ? 51.466  45.436  23.987  1.00 109.06 ?  81   THR A C   1 
ATOM   409  O  O   . THR A 1 82  ? 51.950  44.494  24.619  1.00 107.20 ?  81   THR A O   1 
ATOM   410  C  CB  . THR A 1 82  ? 49.622  44.799  22.388  1.00 112.28 ?  81   THR A CB  1 
ATOM   411  O  OG1 . THR A 1 82  ? 50.227  43.502  22.369  1.00 133.81 ?  81   THR A OG1 1 
ATOM   412  C  CG2 . THR A 1 82  ? 50.127  45.599  21.198  1.00 113.64 ?  81   THR A CG2 1 
ATOM   413  N  N   . ASP A 1 83  ? 52.207  46.429  23.504  1.00 120.26 ?  82   ASP A N   1 
ATOM   414  C  CA  . ASP A 1 83  ? 53.638  46.496  23.773  1.00 126.20 ?  82   ASP A CA  1 
ATOM   415  C  C   . ASP A 1 83  ? 53.864  46.986  25.198  1.00 129.45 ?  82   ASP A C   1 
ATOM   416  O  O   . ASP A 1 83  ? 53.000  47.637  25.780  1.00 126.18 ?  82   ASP A O   1 
ATOM   417  C  CB  . ASP A 1 83  ? 54.349  47.411  22.777  1.00 134.07 ?  82   ASP A CB  1 
ATOM   418  C  CG  . ASP A 1 83  ? 55.862  47.303  22.867  1.00 144.59 ?  82   ASP A CG  1 
ATOM   419  O  OD1 . ASP A 1 83  ? 56.457  47.936  23.768  1.00 142.51 ?  82   ASP A OD1 1 
ATOM   420  O  OD2 . ASP A 1 83  ? 56.455  46.577  22.040  1.00 152.51 ?  82   ASP A OD2 1 
ATOM   421  N  N   . ILE A 1 84  ? 55.024  46.671  25.762  1.00 142.21 ?  83   ILE A N   1 
ATOM   422  C  CA  . ILE A 1 84  ? 55.340  47.111  27.115  1.00 148.40 ?  83   ILE A CA  1 
ATOM   423  C  C   . ILE A 1 84  ? 56.286  48.313  27.127  1.00 142.07 ?  83   ILE A C   1 
ATOM   424  O  O   . ILE A 1 84  ? 56.107  49.241  27.917  1.00 146.53 ?  83   ILE A O   1 
ATOM   425  C  CB  . ILE A 1 84  ? 55.960  45.962  27.953  1.00 131.60 ?  83   ILE A CB  1 
ATOM   426  C  CG1 . ILE A 1 84  ? 57.065  45.243  27.175  1.00 135.14 ?  83   ILE A CG1 1 
ATOM   427  C  CG2 . ILE A 1 84  ? 54.884  44.986  28.396  1.00 127.86 ?  83   ILE A CG2 1 
ATOM   428  C  CD1 . ILE A 1 84  ? 58.440  45.408  27.787  1.00 140.02 ?  83   ILE A CD1 1 
ATOM   429  N  N   . SER A 1 85  ? 57.270  48.320  26.234  1.00 126.18 ?  84   SER A N   1 
ATOM   430  C  CA  . SER A 1 85  ? 58.303  49.348  26.276  1.00 123.98 ?  84   SER A CA  1 
ATOM   431  C  C   . SER A 1 85  ? 57.769  50.736  25.907  1.00 114.87 ?  84   SER A C   1 
ATOM   432  O  O   . SER A 1 85  ? 58.463  51.741  26.076  1.00 98.33  ?  84   SER A O   1 
ATOM   433  C  CB  . SER A 1 85  ? 59.455  48.968  25.340  1.00 125.83 ?  84   SER A CB  1 
ATOM   434  O  OG  . SER A 1 85  ? 60.538  49.875  25.456  1.00 136.69 ?  84   SER A OG  1 
ATOM   435  N  N   . LEU A 1 86  ? 56.529  50.791  25.430  1.00 111.21 ?  85   LEU A N   1 
ATOM   436  C  CA  . LEU A 1 86  ? 55.901  52.056  25.051  1.00 110.41 ?  85   LEU A CA  1 
ATOM   437  C  C   . LEU A 1 86  ? 54.551  52.325  25.721  1.00 117.40 ?  85   LEU A C   1 
ATOM   438  O  O   . LEU A 1 86  ? 54.002  53.418  25.604  1.00 132.10 ?  85   LEU A O   1 
ATOM   439  C  CB  . LEU A 1 86  ? 55.731  52.117  23.530  1.00 115.49 ?  85   LEU A CB  1 
ATOM   440  C  CG  . LEU A 1 86  ? 57.000  51.984  22.683  1.00 117.84 ?  85   LEU A CG  1 
ATOM   441  C  CD1 . LEU A 1 86  ? 56.620  52.022  21.222  1.00 113.98 ?  85   LEU A CD1 1 
ATOM   442  C  CD2 . LEU A 1 86  ? 58.020  53.071  23.000  1.00 130.18 ?  85   LEU A CD2 1 
ATOM   443  N  N   . GLN A 1 87  ? 54.010  51.324  26.405  1.00 122.03 ?  86   GLN A N   1 
ATOM   444  C  CA  . GLN A 1 87  ? 52.654  51.408  26.945  1.00 125.08 ?  86   GLN A CA  1 
ATOM   445  C  C   . GLN A 1 87  ? 52.399  52.553  27.930  1.00 111.69 ?  86   GLN A C   1 
ATOM   446  O  O   . GLN A 1 87  ? 51.385  53.245  27.824  1.00 103.96 ?  86   GLN A O   1 
ATOM   447  C  CB  . GLN A 1 87  ? 52.287  50.095  27.644  1.00 139.14 ?  86   GLN A CB  1 
ATOM   448  C  CG  . GLN A 1 87  ? 50.802  49.957  27.950  1.00 134.64 ?  86   GLN A CG  1 
ATOM   449  C  CD  . GLN A 1 87  ? 50.488  48.705  28.744  1.00 125.36 ?  86   GLN A CD  1 
ATOM   450  O  OE1 . GLN A 1 87  ? 50.569  48.705  29.970  1.00 122.82 ?  86   GLN A OE1 1 
ATOM   451  N  NE2 . GLN A 1 87  ? 50.130  47.633  28.051  1.00 121.99 ?  86   GLN A NE2 1 
ATOM   452  N  N   . TYR A 1 88  ? 53.312  52.754  28.876  1.00 105.33 ?  87   TYR A N   1 
ATOM   453  C  CA  . TYR A 1 88  ? 53.066  53.680  29.977  1.00 105.63 ?  87   TYR A CA  1 
ATOM   454  C  C   . TYR A 1 88  ? 52.840  55.126  29.554  1.00 127.66 ?  87   TYR A C   1 
ATOM   455  O  O   . TYR A 1 88  ? 51.949  55.791  30.079  1.00 138.35 ?  87   TYR A O   1 
ATOM   456  C  CB  . TYR A 1 88  ? 54.228  53.650  30.971  1.00 105.51 ?  87   TYR A CB  1 
ATOM   457  C  CG  . TYR A 1 88  ? 55.565  54.072  30.406  1.00 108.19 ?  87   TYR A CG  1 
ATOM   458  C  CD1 . TYR A 1 88  ? 56.303  53.218  29.601  1.00 108.38 ?  87   TYR A CD1 1 
ATOM   459  C  CD2 . TYR A 1 88  ? 56.076  55.340  30.659  1.00 112.02 ?  87   TYR A CD2 1 
ATOM   460  C  CE1 . TYR A 1 88  ? 57.525  53.603  29.087  1.00 113.90 ?  87   TYR A CE1 1 
ATOM   461  C  CE2 . TYR A 1 88  ? 57.295  55.737  30.143  1.00 114.44 ?  87   TYR A CE2 1 
ATOM   462  C  CZ  . TYR A 1 88  ? 58.016  54.862  29.357  1.00 110.01 ?  87   TYR A CZ  1 
ATOM   463  O  OH  . TYR A 1 88  ? 59.233  55.241  28.838  1.00 103.13 ?  87   TYR A OH  1 
ATOM   464  N  N   . LEU A 1 89  ? 53.642  55.615  28.616  1.00 137.09 ?  88   LEU A N   1 
ATOM   465  C  CA  . LEU A 1 89  ? 53.450  56.959  28.081  1.00 135.85 ?  88   LEU A CA  1 
ATOM   466  C  C   . LEU A 1 89  ? 52.134  57.085  27.306  1.00 122.21 ?  88   LEU A C   1 
ATOM   467  O  O   . LEU A 1 89  ? 51.474  58.126  27.355  1.00 126.84 ?  88   LEU A O   1 
ATOM   468  C  CB  . LEU A 1 89  ? 54.644  57.361  27.212  1.00 148.13 ?  88   LEU A CB  1 
ATOM   469  C  CG  . LEU A 1 89  ? 55.004  56.540  25.980  1.00 149.71 ?  88   LEU A CG  1 
ATOM   470  C  CD1 . LEU A 1 89  ? 54.423  57.192  24.745  1.00 166.36 ?  88   LEU A CD1 1 
ATOM   471  C  CD2 . LEU A 1 89  ? 56.512  56.411  25.858  1.00 138.46 ?  88   LEU A CD2 1 
ATOM   472  N  N   . ALA A 1 90  ? 51.754  56.015  26.613  1.00 111.06 ?  89   ALA A N   1 
ATOM   473  C  CA  . ALA A 1 90  ? 50.538  56.005  25.806  1.00 109.50 ?  89   ALA A CA  1 
ATOM   474  C  C   . ALA A 1 90  ? 49.315  56.264  26.677  1.00 113.20 ?  89   ALA A C   1 
ATOM   475  O  O   . ALA A 1 90  ? 48.371  56.921  26.241  1.00 122.36 ?  89   ALA A O   1 
ATOM   476  C  CB  . ALA A 1 90  ? 50.388  54.679  25.071  1.00 100.33 ?  89   ALA A CB  1 
ATOM   477  N  N   . ILE A 1 91  ? 49.333  55.729  27.897  1.00 100.75 ?  90   ILE A N   1 
ATOM   478  C  CA  . ILE A 1 91  ? 48.247  55.921  28.856  1.00 98.45  ?  90   ILE A CA  1 
ATOM   479  C  C   . ILE A 1 91  ? 48.228  57.396  29.242  1.00 111.91 ?  90   ILE A C   1 
ATOM   480  O  O   . ILE A 1 91  ? 47.176  58.023  29.215  1.00 133.06 ?  90   ILE A O   1 
ATOM   481  C  CB  . ILE A 1 91  ? 48.395  55.040  30.116  1.00 104.08 ?  90   ILE A CB  1 
ATOM   482  C  CG1 . ILE A 1 91  ? 48.331  53.556  29.761  1.00 98.98  ?  90   ILE A CG1 1 
ATOM   483  C  CG2 . ILE A 1 91  ? 47.277  55.347  31.082  1.00 99.82  ?  90   ILE A CG2 1 
ATOM   484  C  CD1 . ILE A 1 91  ? 49.445  52.755  30.428  1.00 91.52  ?  90   ILE A CD1 1 
ATOM   485  N  N   . ASP A 1 92  ? 49.388  57.936  29.628  1.00 115.23 ?  91   ASP A N   1 
ATOM   486  C  CA  . ASP A 1 92  ? 49.493  59.336  30.061  1.00 123.99 ?  91   ASP A CA  1 
ATOM   487  C  C   . ASP A 1 92  ? 49.121  60.301  28.949  1.00 126.27 ?  91   ASP A C   1 
ATOM   488  O  O   . ASP A 1 92  ? 48.360  61.251  29.151  1.00 124.69 ?  91   ASP A O   1 
ATOM   489  C  CB  . ASP A 1 92  ? 50.911  59.661  30.524  1.00 127.21 ?  91   ASP A CB  1 
ATOM   490  C  CG  . ASP A 1 92  ? 51.007  59.827  32.025  1.00 146.23 ?  91   ASP A CG  1 
ATOM   491  O  OD1 . ASP A 1 92  ? 49.972  60.143  32.659  1.00 155.45 ?  91   ASP A OD1 1 
ATOM   492  O  OD2 . ASP A 1 92  ? 52.116  59.643  32.572  1.00 155.56 ?  91   ASP A OD2 1 
ATOM   493  N  N   . ARG A 1 93  ? 49.662  60.039  27.766  1.00 121.42 ?  92   ARG A N   1 
ATOM   494  C  CA  . ARG A 1 93  ? 49.418  60.887  26.603  1.00 116.83 ?  92   ARG A CA  1 
ATOM   495  C  C   . ARG A 1 93  ? 48.039  60.688  25.981  1.00 112.63 ?  92   ARG A C   1 
ATOM   496  O  O   . ARG A 1 93  ? 47.408  61.650  25.555  1.00 120.29 ?  92   ARG A O   1 
ATOM   497  C  CB  . ARG A 1 93  ? 50.518  60.676  25.567  1.00 123.94 ?  92   ARG A CB  1 
ATOM   498  C  CG  . ARG A 1 93  ? 51.774  61.424  25.968  1.00 132.50 ?  92   ARG A CG  1 
ATOM   499  C  CD  . ARG A 1 93  ? 51.594  62.905  25.611  1.00 139.21 ?  92   ARG A CD  1 
ATOM   500  N  NE  . ARG A 1 93  ? 52.053  63.783  26.681  1.00 150.28 ?  92   ARG A NE  1 
ATOM   501  C  CZ  . ARG A 1 93  ? 53.301  64.230  26.792  1.00 154.02 ?  92   ARG A CZ  1 
ATOM   502  N  NH1 . ARG A 1 93  ? 54.228  63.821  25.942  1.00 148.43 ?  92   ARG A NH1 1 
ATOM   503  N  NH2 . ARG A 1 93  ? 53.633  65.056  27.774  1.00 155.38 ?  92   ARG A NH2 1 
ATOM   504  N  N   . GLY A 1 94  ? 47.566  59.450  25.935  1.00 108.80 ?  93   GLY A N   1 
ATOM   505  C  CA  . GLY A 1 94  ? 46.332  59.143  25.234  1.00 102.88 ?  93   GLY A CA  1 
ATOM   506  C  C   . GLY A 1 94  ? 45.096  59.946  25.601  1.00 98.46  ?  93   GLY A C   1 
ATOM   507  O  O   . GLY A 1 94  ? 44.334  60.353  24.726  1.00 94.85  ?  93   GLY A O   1 
ATOM   508  N  N   . PHE A 1 95  ? 44.891  60.177  26.891  1.00 119.08 ?  94   PHE A N   1 
ATOM   509  C  CA  . PHE A 1 95  ? 43.728  60.933  27.344  1.00 135.46 ?  94   PHE A CA  1 
ATOM   510  C  C   . PHE A 1 95  ? 43.809  62.416  26.993  1.00 142.68 ?  94   PHE A C   1 
ATOM   511  O  O   . PHE A 1 95  ? 42.848  62.989  26.482  1.00 144.07 ?  94   PHE A O   1 
ATOM   512  C  CB  . PHE A 1 95  ? 43.546  60.758  28.851  1.00 147.61 ?  94   PHE A CB  1 
ATOM   513  C  CG  . PHE A 1 95  ? 43.274  59.343  29.257  1.00 145.37 ?  94   PHE A CG  1 
ATOM   514  C  CD1 . PHE A 1 95  ? 42.021  58.784  29.085  1.00 146.95 ?  94   PHE A CD1 1 
ATOM   515  C  CD2 . PHE A 1 95  ? 44.283  58.567  29.793  1.00 145.14 ?  94   PHE A CD2 1 
ATOM   516  C  CE1 . PHE A 1 95  ? 41.782  57.479  29.449  1.00 151.94 ?  94   PHE A CE1 1 
ATOM   517  C  CE2 . PHE A 1 95  ? 44.053  57.265  30.156  1.00 151.13 ?  94   PHE A CE2 1 
ATOM   518  C  CZ  . PHE A 1 95  ? 42.802  56.720  29.987  1.00 151.72 ?  94   PHE A CZ  1 
ATOM   519  N  N   . GLU A 1 96  ? 44.940  63.043  27.306  1.00 151.94 ?  95   GLU A N   1 
ATOM   520  C  CA  . GLU A 1 96  ? 45.137  64.461  27.011  1.00 160.26 ?  95   GLU A CA  1 
ATOM   521  C  C   . GLU A 1 96  ? 45.152  64.728  25.502  1.00 148.19 ?  95   GLU A C   1 
ATOM   522  O  O   . GLU A 1 96  ? 44.551  65.694  25.033  1.00 144.98 ?  95   GLU A O   1 
ATOM   523  C  CB  . GLU A 1 96  ? 46.424  64.978  27.664  1.00 180.64 ?  95   GLU A CB  1 
ATOM   524  C  CG  . GLU A 1 96  ? 47.652  64.106  27.464  1.00 193.07 ?  95   GLU A CG  1 
ATOM   525  C  CD  . GLU A 1 96  ? 48.880  64.677  28.145  1.00 210.15 ?  95   GLU A CD  1 
ATOM   526  O  OE1 . GLU A 1 96  ? 48.723  65.543  29.029  1.00 218.77 ?  95   GLU A OE1 1 
ATOM   527  O  OE2 . GLU A 1 96  ? 50.003  64.262  27.801  1.00 214.64 ?  95   GLU A OE2 1 
ATOM   528  N  N   . ILE A 1 97  ? 45.847  63.872  24.754  1.00 144.64 ?  96   ILE A N   1 
ATOM   529  C  CA  . ILE A 1 97  ? 45.909  63.974  23.294  1.00 136.06 ?  96   ILE A CA  1 
ATOM   530  C  C   . ILE A 1 97  ? 44.512  63.868  22.701  1.00 130.55 ?  96   ILE A C   1 
ATOM   531  O  O   . ILE A 1 97  ? 44.148  64.615  21.794  1.00 132.84 ?  96   ILE A O   1 
ATOM   532  C  CB  . ILE A 1 97  ? 46.802  62.881  22.678  1.00 130.39 ?  96   ILE A CB  1 
ATOM   533  C  CG1 . ILE A 1 97  ? 48.271  63.136  23.016  1.00 157.83 ?  96   ILE A CG1 1 
ATOM   534  C  CG2 . ILE A 1 97  ? 46.624  62.827  21.171  1.00 109.88 ?  96   ILE A CG2 1 
ATOM   535  C  CD1 . ILE A 1 97  ? 49.214  62.125  22.405  1.00 163.97 ?  96   ILE A CD1 1 
ATOM   536  N  N   . PHE A 1 98  ? 43.738  62.928  23.231  1.00 131.30 ?  97   PHE A N   1 
ATOM   537  C  CA  . PHE A 1 98  ? 42.366  62.710  22.796  1.00 127.45 ?  97   PHE A CA  1 
ATOM   538  C  C   . PHE A 1 98  ? 41.561  63.983  22.989  1.00 126.68 ?  97   PHE A C   1 
ATOM   539  O  O   . PHE A 1 98  ? 40.910  64.465  22.072  1.00 123.71 ?  97   PHE A O   1 
ATOM   540  C  CB  . PHE A 1 98  ? 41.741  61.558  23.588  1.00 129.04 ?  97   PHE A CB  1 
ATOM   541  C  CG  . PHE A 1 98  ? 40.245  61.467  23.471  1.00 120.73 ?  97   PHE A CG  1 
ATOM   542  C  CD1 . PHE A 1 98  ? 39.655  60.828  22.396  1.00 103.37 ?  97   PHE A CD1 1 
ATOM   543  C  CD2 . PHE A 1 98  ? 39.427  62.011  24.450  1.00 128.61 ?  97   PHE A CD2 1 
ATOM   544  C  CE1 . PHE A 1 98  ? 38.283  60.735  22.293  1.00 102.57 ?  97   PHE A CE1 1 
ATOM   545  C  CE2 . PHE A 1 98  ? 38.054  61.925  24.353  1.00 128.23 ?  97   PHE A CE2 1 
ATOM   546  C  CZ  . PHE A 1 98  ? 37.480  61.282  23.272  1.00 113.90 ?  97   PHE A CZ  1 
ATOM   547  N  N   . ASP A 1 99  ? 41.656  64.547  24.184  1.00 141.37 ?  98   ASP A N   1 
ATOM   548  C  CA  . ASP A 1 99  ? 40.879  65.721  24.549  1.00 155.47 ?  98   ASP A CA  1 
ATOM   549  C  C   . ASP A 1 99  ? 41.285  66.965  23.757  1.00 161.17 ?  98   ASP A C   1 
ATOM   550  O  O   . ASP A 1 99  ? 40.496  67.902  23.613  1.00 153.48 ?  98   ASP A O   1 
ATOM   551  C  CB  . ASP A 1 99  ? 41.003  65.977  26.051  1.00 155.00 ?  98   ASP A CB  1 
ATOM   552  C  CG  . ASP A 1 99  ? 40.015  65.156  26.857  1.00 148.96 ?  98   ASP A CG  1 
ATOM   553  O  OD1 . ASP A 1 99  ? 38.981  64.748  26.284  1.00 150.21 ?  98   ASP A OD1 1 
ATOM   554  O  OD2 . ASP A 1 99  ? 40.271  64.905  28.054  1.00 144.29 ?  98   ASP A OD2 1 
ATOM   555  N  N   . ARG A 1 100 ? 42.518  66.978  23.257  1.00 170.27 ?  99   ARG A N   1 
ATOM   556  C  CA  . ARG A 1 100 ? 42.987  68.076  22.418  1.00 184.69 ?  99   ARG A CA  1 
ATOM   557  C  C   . ARG A 1 100 ? 42.251  68.487  21.139  1.00 201.49 ?  99   ARG A C   1 
ATOM   558  O  O   . ARG A 1 100 ? 41.921  69.658  20.966  1.00 225.17 ?  99   ARG A O   1 
ATOM   559  C  CB  . ARG A 1 100 ? 44.494  67.945  22.164  1.00 180.45 ?  99   ARG A CB  1 
ATOM   560  C  CG  . ARG A 1 100 ? 45.110  69.072  21.338  1.00 181.82 ?  99   ARG A CG  1 
ATOM   561  C  CD  . ARG A 1 100 ? 45.042  70.407  22.070  1.00 181.31 ?  99   ARG A CD  1 
ATOM   562  N  NE  . ARG A 1 100 ? 45.607  70.331  23.415  1.00 184.47 ?  99   ARG A NE  1 
ATOM   563  C  CZ  . ARG A 1 100 ? 46.890  70.531  23.704  1.00 178.87 ?  99   ARG A CZ  1 
ATOM   564  N  NH1 . ARG A 1 100 ? 47.754  70.821  22.740  1.00 172.44 ?  99   ARG A NH1 1 
ATOM   565  N  NH2 . ARG A 1 100 ? 47.311  70.441  24.958  1.00 176.22 ?  99   ARG A NH2 1 
ATOM   566  N  N   . MET A 1 101 ? 42.010  67.533  20.241  1.00 194.12 ?  100  MET A N   1 
ATOM   567  C  CA  . MET A 1 101 ? 41.096  67.803  19.099  1.00 200.84 ?  100  MET A CA  1 
ATOM   568  C  C   . MET A 1 101 ? 39.494  67.493  19.169  1.00 172.69 ?  100  MET A C   1 
ATOM   569  O  O   . MET A 1 101 ? 38.609  67.830  18.382  1.00 181.96 ?  100  MET A O   1 
ATOM   570  C  CB  . MET A 1 101 ? 41.409  66.841  17.948  1.00 200.00 ?  100  MET A CB  1 
ATOM   571  C  CG  . MET A 1 101 ? 40.624  67.011  16.668  1.00 198.68 ?  100  MET A CG  1 
ATOM   572  S  SD  . MET A 1 101 ? 40.991  68.575  15.848  1.00 406.58 ?  100  MET A SD  1 
ATOM   573  C  CE  . MET A 1 101 ? 42.609  68.232  15.155  1.00 173.35 ?  100  MET A CE  1 
ATOM   574  N  N   . VAL A 1 102 ? 39.236  66.929  20.347  1.00 155.27 ?  101  VAL A N   1 
ATOM   575  C  CA  . VAL A 1 102 ? 37.861  66.712  20.785  1.00 147.15 ?  101  VAL A CA  1 
ATOM   576  C  C   . VAL A 1 102 ? 37.494  68.182  20.988  1.00 167.04 ?  101  VAL A C   1 
ATOM   577  O  O   . VAL A 1 102 ? 36.368  68.588  20.701  1.00 178.58 ?  101  VAL A O   1 
ATOM   578  C  CB  . VAL A 1 102 ? 37.445  65.882  22.024  1.00 136.73 ?  101  VAL A CB  1 
ATOM   579  C  CG1 . VAL A 1 102 ? 35.964  66.033  22.300  1.00 129.62 ?  101  VAL A CG1 1 
ATOM   580  C  CG2 . VAL A 1 102 ? 37.762  64.420  21.803  1.00 142.96 ?  101  VAL A CG2 1 
ATOM   581  N  N   . SER A 1 103 ? 38.454  68.982  21.450  1.00 178.48 ?  102  SER A N   1 
ATOM   582  C  CA  . SER A 1 103 ? 38.236  70.411  21.680  1.00 192.44 ?  102  SER A CA  1 
ATOM   583  C  C   . SER A 1 103 ? 37.815  71.119  20.390  1.00 194.01 ?  102  SER A C   1 
ATOM   584  O  O   . SER A 1 103 ? 37.098  72.123  20.425  1.00 184.36 ?  102  SER A O   1 
ATOM   585  C  CB  . SER A 1 103 ? 39.492  71.069  22.259  1.00 196.88 ?  102  SER A CB  1 
ATOM   586  O  OG  . SER A 1 103 ? 39.316  72.461  22.446  1.00 195.62 ?  102  SER A OG  1 
ATOM   587  N  N   . SER A 1 104 ? 38.272  70.591  19.257  1.00 198.68 ?  103  SER A N   1 
ATOM   588  C  CA  . SER A 1 104 ? 37.929  71.130  17.940  1.00 205.11 ?  103  SER A CA  1 
ATOM   589  C  C   . SER A 1 104 ? 36.433  71.062  17.631  1.00 208.56 ?  103  SER A C   1 
ATOM   590  O  O   . SER A 1 104 ? 35.947  71.741  16.725  1.00 210.41 ?  103  SER A O   1 
ATOM   591  C  CB  . SER A 1 104 ? 38.699  70.381  16.852  1.00 197.92 ?  103  SER A CB  1 
ATOM   592  O  OG  . SER A 1 104 ? 40.092  70.421  17.091  1.00 187.76 ?  103  SER A OG  1 
ATOM   593  N  N   . GLY A 1 105 ? 35.709  70.246  18.389  1.00 206.10 ?  104  GLY A N   1 
ATOM   594  C  CA  . GLY A 1 105 ? 34.273  70.125  18.223  1.00 199.91 ?  104  GLY A CA  1 
ATOM   595  C  C   . GLY A 1 105 ? 33.823  69.017  17.289  1.00 183.41 ?  104  GLY A C   1 
ATOM   596  O  O   . GLY A 1 105 ? 32.628  68.874  17.034  1.00 182.02 ?  104  GLY A O   1 
ATOM   597  N  N   . ILE A 1 106 ? 34.762  68.234  16.769  1.00 173.96 ?  105  ILE A N   1 
ATOM   598  C  CA  . ILE A 1 106 ? 34.376  67.084  15.967  1.00 182.35 ?  105  ILE A CA  1 
ATOM   599  C  C   . ILE A 1 106 ? 33.902  65.968  16.885  1.00 181.84 ?  105  ILE A C   1 
ATOM   600  O  O   . ILE A 1 106 ? 34.591  65.615  17.846  1.00 185.16 ?  105  ILE A O   1 
ATOM   601  C  CB  . ILE A 1 106 ? 35.528  66.563  15.063  1.00 179.93 ?  105  ILE A CB  1 
ATOM   602  C  CG1 . ILE A 1 106 ? 35.156  65.190  14.482  1.00 176.36 ?  105  ILE A CG1 1 
ATOM   603  C  CG2 . ILE A 1 106 ? 36.851  66.511  15.821  1.00 158.98 ?  105  ILE A CG2 1 
ATOM   604  C  CD1 . ILE A 1 106 ? 36.274  64.465  13.769  1.00 157.27 ?  105  ILE A CD1 1 
ATOM   605  N  N   . SER A 1 107 ? 32.716  65.431  16.605  1.00 178.62 ?  106  SER A N   1 
ATOM   606  C  CA  . SER A 1 107 ? 32.217  64.313  17.388  1.00 181.76 ?  106  SER A CA  1 
ATOM   607  C  C   . SER A 1 107 ? 33.226  63.214  17.140  1.00 181.28 ?  106  SER A C   1 
ATOM   608  O  O   . SER A 1 107 ? 33.532  62.906  15.990  1.00 181.45 ?  106  SER A O   1 
ATOM   609  C  CB  . SER A 1 107 ? 30.805  63.896  16.973  1.00 182.31 ?  106  SER A CB  1 
ATOM   610  O  OG  . SER A 1 107 ? 30.303  62.871  17.817  1.00 172.84 ?  106  SER A OG  1 
ATOM   611  N  N   . PRO A 1 108 ? 33.755  62.628  18.221  1.00 174.18 ?  107  PRO A N   1 
ATOM   612  C  CA  . PRO A 1 108 ? 34.913  61.743  18.112  1.00 164.84 ?  107  PRO A CA  1 
ATOM   613  C  C   . PRO A 1 108 ? 34.614  60.576  17.187  1.00 165.98 ?  107  PRO A C   1 
ATOM   614  O  O   . PRO A 1 108 ? 33.450  60.223  16.995  1.00 171.86 ?  107  PRO A O   1 
ATOM   615  C  CB  . PRO A 1 108 ? 35.134  61.289  19.560  1.00 156.94 ?  107  PRO A CB  1 
ATOM   616  C  CG  . PRO A 1 108 ? 33.773  61.394  20.183  1.00 158.10 ?  107  PRO A CG  1 
ATOM   617  C  CD  . PRO A 1 108 ? 33.203  62.637  19.587  1.00 168.60 ?  107  PRO A CD  1 
ATOM   618  N  N   . ASN A 1 109 ? 35.654  60.014  16.590  1.00 159.59 ?  108  ASN A N   1 
ATOM   619  C  CA  . ASN A 1 109 ? 35.476  58.912  15.669  1.00 141.34 ?  108  ASN A CA  1 
ATOM   620  C  C   . ASN A 1 109 ? 35.168  57.628  16.423  1.00 134.22 ?  108  ASN A C   1 
ATOM   621  O  O   . ASN A 1 109 ? 35.611  57.451  17.554  1.00 136.34 ?  108  ASN A O   1 
ATOM   622  C  CB  . ASN A 1 109 ? 36.730  58.753  14.807  1.00 136.98 ?  108  ASN A CB  1 
ATOM   623  C  CG  . ASN A 1 109 ? 36.589  57.672  13.767  1.00 141.58 ?  108  ASN A CG  1 
ATOM   624  O  OD1 . ASN A 1 109 ? 35.480  57.333  13.354  1.00 150.39 ?  108  ASN A OD1 1 
ATOM   625  N  ND2 . ASN A 1 109 ? 37.715  57.120  13.334  1.00 138.13 ?  108  ASN A ND2 1 
ATOM   626  N  N   . GLU A 1 110 ? 34.400  56.743  15.794  1.00 137.19 ?  109  GLU A N   1 
ATOM   627  C  CA  . GLU A 1 110 ? 34.071  55.446  16.377  1.00 127.92 ?  109  GLU A CA  1 
ATOM   628  C  C   . GLU A 1 110 ? 35.329  54.680  16.757  1.00 113.70 ?  109  GLU A C   1 
ATOM   629  O  O   . GLU A 1 110 ? 35.419  54.098  17.837  1.00 105.14 ?  109  GLU A O   1 
ATOM   630  C  CB  . GLU A 1 110 ? 33.212  54.633  15.397  1.00 142.25 ?  109  GLU A CB  1 
ATOM   631  C  CG  . GLU A 1 110 ? 32.795  53.237  15.872  1.00 155.86 ?  109  GLU A CG  1 
ATOM   632  C  CD  . GLU A 1 110 ? 33.845  52.170  15.569  1.00 157.12 ?  109  GLU A CD  1 
ATOM   633  O  OE1 . GLU A 1 110 ? 34.498  52.257  14.508  1.00 169.19 ?  109  GLU A OE1 1 
ATOM   634  O  OE2 . GLU A 1 110 ? 34.022  51.243  16.384  1.00 140.68 ?  109  GLU A OE2 1 
ATOM   635  N  N   . ALA A 1 111 ? 36.304  54.698  15.859  1.00 107.25 ?  110  ALA A N   1 
ATOM   636  C  CA  . ALA A 1 111 ? 37.581  54.046  16.099  1.00 102.74 ?  110  ALA A CA  1 
ATOM   637  C  C   . ALA A 1 111 ? 38.348  54.698  17.251  1.00 108.22 ?  110  ALA A C   1 
ATOM   638  O  O   . ALA A 1 111 ? 38.956  54.009  18.070  1.00 102.36 ?  110  ALA A O   1 
ATOM   639  C  CB  . ALA A 1 111 ? 38.415  54.057  14.830  1.00 105.03 ?  110  ALA A CB  1 
ATOM   640  N  N   . SER A 1 112 ? 38.310  56.027  17.316  1.00 120.48 ?  111  SER A N   1 
ATOM   641  C  CA  . SER A 1 112 ? 39.050  56.771  18.337  1.00 123.50 ?  111  SER A CA  1 
ATOM   642  C  C   . SER A 1 112 ? 38.482  56.525  19.732  1.00 116.81 ?  111  SER A C   1 
ATOM   643  O  O   . SER A 1 112 ? 39.230  56.419  20.703  1.00 124.97 ?  111  SER A O   1 
ATOM   644  C  CB  . SER A 1 112 ? 39.056  58.268  18.033  1.00 135.12 ?  111  SER A CB  1 
ATOM   645  O  OG  . SER A 1 112 ? 37.745  58.766  17.871  1.00 153.17 ?  111  SER A OG  1 
ATOM   646  N  N   . VAL A 1 113 ? 37.159  56.457  19.835  1.00 102.43 ?  112  VAL A N   1 
ATOM   647  C  CA  . VAL A 1 113 ? 36.512  56.215  21.118  1.00 102.77 ?  112  VAL A CA  1 
ATOM   648  C  C   . VAL A 1 113 ? 36.894  54.829  21.641  1.00 114.54 ?  112  VAL A C   1 
ATOM   649  O  O   . VAL A 1 113 ? 37.020  54.624  22.847  1.00 126.78 ?  112  VAL A O   1 
ATOM   650  C  CB  . VAL A 1 113 ? 34.979  56.351  21.013  1.00 93.98  ?  112  VAL A CB  1 
ATOM   651  C  CG1 . VAL A 1 113 ? 34.303  55.942  22.318  1.00 87.86  ?  112  VAL A CG1 1 
ATOM   652  C  CG2 . VAL A 1 113 ? 34.615  57.772  20.669  1.00 94.83  ?  112  VAL A CG2 1 
ATOM   653  N  N   . THR A 1 114 ? 37.090  53.880  20.731  1.00 110.87 ?  113  THR A N   1 
ATOM   654  C  CA  . THR A 1 114 ? 37.587  52.566  21.122  1.00 106.03 ?  113  THR A CA  1 
ATOM   655  C  C   . THR A 1 114 ? 39.005  52.684  21.663  1.00 107.37 ?  113  THR A C   1 
ATOM   656  O  O   . THR A 1 114 ? 39.368  52.023  22.635  1.00 105.78 ?  113  THR A O   1 
ATOM   657  C  CB  . THR A 1 114 ? 37.585  51.583  19.942  1.00 98.15  ?  113  THR A CB  1 
ATOM   658  O  OG1 . THR A 1 114 ? 36.299  51.598  19.315  1.00 114.81 ?  113  THR A OG1 1 
ATOM   659  C  CG2 . THR A 1 114 ? 37.900  50.172  20.410  1.00 81.71  ?  113  THR A CG2 1 
ATOM   660  N  N   . SER A 1 115 ? 39.796  53.541  21.026  1.00 104.49 ?  114  SER A N   1 
ATOM   661  C  CA  . SER A 1 115 ? 41.192  53.735  21.394  1.00 102.51 ?  114  SER A CA  1 
ATOM   662  C  C   . SER A 1 115 ? 41.390  54.268  22.816  1.00 113.13 ?  114  SER A C   1 
ATOM   663  O  O   . SER A 1 115 ? 42.200  53.734  23.577  1.00 121.11 ?  114  SER A O   1 
ATOM   664  C  CB  . SER A 1 115 ? 41.868  54.667  20.388  1.00 98.00  ?  114  SER A CB  1 
ATOM   665  O  OG  . SER A 1 115 ? 41.864  54.090  19.094  1.00 99.50  ?  114  SER A OG  1 
ATOM   666  N  N   . VAL A 1 116 ? 40.656  55.319  23.170  1.00 113.16 ?  115  VAL A N   1 
ATOM   667  C  CA  . VAL A 1 116 ? 40.726  55.872  24.520  1.00 119.36 ?  115  VAL A CA  1 
ATOM   668  C  C   . VAL A 1 116 ? 40.145  54.885  25.533  1.00 130.36 ?  115  VAL A C   1 
ATOM   669  O  O   . VAL A 1 116 ? 40.621  54.791  26.667  1.00 137.97 ?  115  VAL A O   1 
ATOM   670  C  CB  . VAL A 1 116 ? 39.996  57.236  24.615  1.00 120.56 ?  115  VAL A CB  1 
ATOM   671  C  CG1 . VAL A 1 116 ? 38.552  57.122  24.151  1.00 118.09 ?  115  VAL A CG1 1 
ATOM   672  C  CG2 . VAL A 1 116 ? 40.070  57.796  26.029  1.00 135.21 ?  115  VAL A CG2 1 
ATOM   673  N  N   . ALA A 1 117 ? 39.123  54.143  25.114  1.00 127.37 ?  116  ALA A N   1 
ATOM   674  C  CA  . ALA A 1 117 ? 38.523  53.118  25.961  1.00 111.23 ?  116  ALA A CA  1 
ATOM   675  C  C   . ALA A 1 117 ? 39.545  52.040  26.308  1.00 93.59  ?  116  ALA A C   1 
ATOM   676  O  O   . ALA A 1 117 ? 39.639  51.618  27.460  1.00 90.26  ?  116  ALA A O   1 
ATOM   677  C  CB  . ALA A 1 117 ? 37.309  52.502  25.282  1.00 112.01 ?  116  ALA A CB  1 
ATOM   678  N  N   . ARG A 1 118 ? 40.312  51.605  25.311  1.00 90.37  ?  117  ARG A N   1 
ATOM   679  C  CA  . ARG A 1 118 ? 41.370  50.626  25.541  1.00 101.19 ?  117  ARG A CA  1 
ATOM   680  C  C   . ARG A 1 118 ? 42.421  51.175  26.496  1.00 106.83 ?  117  ARG A C   1 
ATOM   681  O  O   . ARG A 1 118 ? 42.848  50.477  27.411  1.00 112.46 ?  117  ARG A O   1 
ATOM   682  C  CB  . ARG A 1 118 ? 42.040  50.203  24.232  1.00 113.22 ?  117  ARG A CB  1 
ATOM   683  C  CG  . ARG A 1 118 ? 41.158  49.430  23.272  1.00 110.42 ?  117  ARG A CG  1 
ATOM   684  C  CD  . ARG A 1 118 ? 41.985  48.855  22.132  1.00 117.57 ?  117  ARG A CD  1 
ATOM   685  N  NE  . ARG A 1 118 ? 41.160  48.127  21.174  1.00 140.68 ?  117  ARG A NE  1 
ATOM   686  C  CZ  . ARG A 1 118 ? 40.869  46.834  21.272  1.00 159.03 ?  117  ARG A CZ  1 
ATOM   687  N  NH1 . ARG A 1 118 ? 41.337  46.122  22.289  1.00 172.93 ?  117  ARG A NH1 1 
ATOM   688  N  NH2 . ARG A 1 118 ? 40.109  46.253  20.353  1.00 157.37 ?  117  ARG A NH2 1 
ATOM   689  N  N   . LEU A 1 119 ? 42.846  52.416  26.266  1.00 109.73 ?  118  LEU A N   1 
ATOM   690  C  CA  . LEU A 1 119 ? 43.849  53.062  27.114  1.00 111.95 ?  118  LEU A CA  1 
ATOM   691  C  C   . LEU A 1 119 ? 43.395  53.153  28.566  1.00 105.93 ?  118  LEU A C   1 
ATOM   692  O  O   . LEU A 1 119 ? 44.165  52.880  29.490  1.00 79.57  ?  118  LEU A O   1 
ATOM   693  C  CB  . LEU A 1 119 ? 44.168  54.464  26.594  1.00 104.73 ?  118  LEU A CB  1 
ATOM   694  C  CG  . LEU A 1 119 ? 44.937  54.572  25.278  1.00 96.53  ?  118  LEU A CG  1 
ATOM   695  C  CD1 . LEU A 1 119 ? 44.856  55.988  24.749  1.00 96.47  ?  118  LEU A CD1 1 
ATOM   696  C  CD2 . LEU A 1 119 ? 46.388  54.153  25.463  1.00 80.59  ?  118  LEU A CD2 1 
ATOM   697  N  N   . ALA A 1 120 ? 42.133  53.523  28.751  1.00 109.83 ?  119  ALA A N   1 
ATOM   698  C  CA  . ALA A 1 120 ? 41.541  53.610  30.075  1.00 106.55 ?  119  ALA A CA  1 
ATOM   699  C  C   . ALA A 1 120 ? 41.506  52.235  30.726  1.00 111.94 ?  119  ALA A C   1 
ATOM   700  O  O   . ALA A 1 120 ? 42.030  52.036  31.822  1.00 105.32 ?  119  ALA A O   1 
ATOM   701  C  CB  . ALA A 1 120 ? 40.146  54.208  29.987  1.00 82.26  ?  119  ALA A CB  1 
ATOM   702  N  N   . ALA A 1 121 ? 40.884  51.289  30.034  1.00 114.82 ?  120  ALA A N   1 
ATOM   703  C  CA  . ALA A 1 121 ? 40.713  49.940  30.549  1.00 105.93 ?  120  ALA A CA  1 
ATOM   704  C  C   . ALA A 1 121 ? 42.046  49.252  30.827  1.00 104.26 ?  120  ALA A C   1 
ATOM   705  O  O   . ALA A 1 121 ? 42.155  48.449  31.756  1.00 102.78 ?  120  ALA A O   1 
ATOM   706  C  CB  . ALA A 1 121 ? 39.895  49.114  29.569  1.00 98.71  ?  120  ALA A CB  1 
ATOM   707  N  N   . ALA A 1 122 ? 43.059  49.584  30.031  1.00 105.85 ?  121  ALA A N   1 
ATOM   708  C  CA  . ALA A 1 122 ? 44.361  48.930  30.124  1.00 112.79 ?  121  ALA A CA  1 
ATOM   709  C  C   . ALA A 1 122 ? 44.974  49.078  31.506  1.00 122.24 ?  121  ALA A C   1 
ATOM   710  O  O   . ALA A 1 122 ? 45.586  48.149  32.028  1.00 129.23 ?  121  ALA A O   1 
ATOM   711  C  CB  . ALA A 1 122 ? 45.312  49.482  29.071  1.00 110.81 ?  121  ALA A CB  1 
ATOM   712  N  N   . LYS A 1 123 ? 44.807  50.253  32.096  1.00 126.04 ?  122  LYS A N   1 
ATOM   713  C  CA  . LYS A 1 123 ? 45.329  50.498  33.431  1.00 133.18 ?  122  LYS A CA  1 
ATOM   714  C  C   . LYS A 1 123 ? 44.315  51.097  34.393  1.00 121.72 ?  122  LYS A C   1 
ATOM   715  O  O   . LYS A 1 123 ? 44.251  52.312  34.576  1.00 114.86 ?  122  LYS A O   1 
ATOM   716  C  CB  . LYS A 1 123 ? 46.573  51.385  33.361  1.00 149.80 ?  122  LYS A CB  1 
ATOM   717  C  CG  . LYS A 1 123 ? 47.746  50.726  32.657  1.00 151.37 ?  122  LYS A CG  1 
ATOM   718  C  CD  . LYS A 1 123 ? 48.397  49.669  33.532  1.00 143.49 ?  122  LYS A CD  1 
ATOM   719  C  CE  . LYS A 1 123 ? 49.208  48.677  32.718  1.00 132.78 ?  122  LYS A CE  1 
ATOM   720  N  NZ  . LYS A 1 123 ? 50.644  49.078  32.628  1.00 114.49 ?  122  LYS A NZ  1 
ATOM   721  N  N   . GLY A 1 124 ? 43.495  50.222  34.966  1.00 121.21 ?  123  GLY A N   1 
ATOM   722  C  CA  . GLY A 1 124 ? 42.580  50.592  36.028  1.00 133.48 ?  123  GLY A CA  1 
ATOM   723  C  C   . GLY A 1 124 ? 41.262  51.226  35.660  1.00 130.18 ?  123  GLY A C   1 
ATOM   724  O  O   . GLY A 1 124 ? 40.198  50.669  35.928  1.00 99.55  ?  123  GLY A O   1 
ATOM   725  N  N   . ASN A 1 125 ? 41.328  52.406  35.060  1.00 152.98 ?  124  ASN A N   1 
ATOM   726  C  CA  . ASN A 1 125 ? 40.129  53.202  34.841  1.00 168.88 ?  124  ASN A CA  1 
ATOM   727  C  C   . ASN A 1 125 ? 39.227  52.612  33.767  1.00 169.55 ?  124  ASN A C   1 
ATOM   728  O  O   . ASN A 1 125 ? 39.126  53.151  32.673  1.00 171.30 ?  124  ASN A O   1 
ATOM   729  C  CB  . ASN A 1 125 ? 40.497  54.640  34.478  1.00 170.75 ?  124  ASN A CB  1 
ATOM   730  C  CG  . ASN A 1 125 ? 39.328  55.593  34.627  1.00 168.61 ?  124  ASN A CG  1 
ATOM   731  O  OD1 . ASN A 1 125 ? 38.171  55.175  34.679  1.00 162.01 ?  124  ASN A OD1 1 
ATOM   732  N  ND2 . ASN A 1 125 ? 39.625  56.885  34.695  1.00 175.53 ?  124  ASN A ND2 1 
ATOM   733  N  N   . GLY A 1 126 ? 38.563  51.508  34.089  1.00 163.18 ?  125  GLY A N   1 
ATOM   734  C  CA  . GLY A 1 126 ? 37.558  50.961  33.200  1.00 158.42 ?  125  GLY A CA  1 
ATOM   735  C  C   . GLY A 1 126 ? 36.357  51.862  33.004  1.00 152.94 ?  125  GLY A C   1 
ATOM   736  O  O   . GLY A 1 126 ? 35.789  51.931  31.916  1.00 176.61 ?  125  GLY A O   1 
ATOM   737  N  N   . ASP A 1 127 ? 35.979  52.557  34.070  1.00 139.62 ?  126  ASP A N   1 
ATOM   738  C  CA  . ASP A 1 127 ? 34.785  53.395  34.066  1.00 136.81 ?  126  ASP A CA  1 
ATOM   739  C  C   . ASP A 1 127 ? 34.780  54.591  33.097  1.00 156.97 ?  126  ASP A C   1 
ATOM   740  O  O   . ASP A 1 127 ? 33.732  55.071  32.661  1.00 166.68 ?  126  ASP A O   1 
ATOM   741  C  CB  . ASP A 1 127 ? 34.565  53.987  35.455  1.00 141.49 ?  126  ASP A CB  1 
ATOM   742  C  CG  . ASP A 1 127 ? 33.295  54.796  35.538  1.00 168.68 ?  126  ASP A CG  1 
ATOM   743  O  OD1 . ASP A 1 127 ? 32.583  54.874  34.514  1.00 181.38 ?  126  ASP A OD1 1 
ATOM   744  O  OD2 . ASP A 1 127 ? 33.002  55.344  36.620  1.00 174.37 -1 126  ASP A OD2 1 
ATOM   745  N  N   . TYR A 1 128 ? 35.981  55.038  32.748  1.00 153.85 ?  127  TYR A N   1 
ATOM   746  C  CA  . TYR A 1 128 ? 36.145  56.112  31.777  1.00 151.22 ?  127  TYR A CA  1 
ATOM   747  C  C   . TYR A 1 128 ? 35.797  55.465  30.444  1.00 150.51 ?  127  TYR A C   1 
ATOM   748  O  O   . TYR A 1 128 ? 35.065  56.035  29.634  1.00 156.50 ?  127  TYR A O   1 
ATOM   749  C  CB  . TYR A 1 128 ? 37.556  56.701  31.705  1.00 152.40 ?  127  TYR A CB  1 
ATOM   750  C  CG  . TYR A 1 128 ? 37.789  57.751  30.632  1.00 157.74 ?  127  TYR A CG  1 
ATOM   751  C  CD1 . TYR A 1 128 ? 37.341  59.057  30.780  1.00 164.60 ?  127  TYR A CD1 1 
ATOM   752  C  CD2 . TYR A 1 128 ? 38.461  57.422  29.462  1.00 159.85 ?  127  TYR A CD2 1 
ATOM   753  C  CE1 . TYR A 1 128 ? 37.557  60.004  29.798  1.00 172.94 ?  127  TYR A CE1 1 
ATOM   754  C  CE2 . TYR A 1 128 ? 38.684  58.361  28.475  1.00 165.96 ?  127  TYR A CE2 1 
ATOM   755  C  CZ  . TYR A 1 128 ? 38.228  59.651  28.646  1.00 172.77 ?  127  TYR A CZ  1 
ATOM   756  O  OH  . TYR A 1 128 ? 38.447  60.591  27.664  1.00 181.79 ?  127  TYR A OH  1 
ATOM   757  N  N   . ALA A 1 129 ? 36.303  54.251  30.247  1.00 139.75 ?  128  ALA A N   1 
ATOM   758  C  CA  . ALA A 1 129 ? 36.087  53.509  29.013  1.00 123.69 ?  128  ALA A CA  1 
ATOM   759  C  C   . ALA A 1 129 ? 34.592  53.347  28.780  1.00 121.05 ?  128  ALA A C   1 
ATOM   760  O  O   . ALA A 1 129 ? 34.119  53.486  27.653  1.00 130.97 ?  128  ALA A O   1 
ATOM   761  C  CB  . ALA A 1 129 ? 36.770  52.149  29.035  1.00 111.10 ?  128  ALA A CB  1 
ATOM   762  N  N   . PHE A 1 130 ? 33.854  53.034  29.840  1.00 109.09 ?  129  PHE A N   1 
ATOM   763  C  CA  . PHE A 1 130 ? 32.404  52.917  29.742  1.00 112.18 ?  129  PHE A CA  1 
ATOM   764  C  C   . PHE A 1 130 ? 31.758  54.265  29.446  1.00 120.93 ?  129  PHE A C   1 
ATOM   765  O  O   . PHE A 1 130 ? 30.954  54.384  28.525  1.00 130.79 ?  129  PHE A O   1 
ATOM   766  C  CB  . PHE A 1 130 ? 31.817  52.344  31.035  1.00 118.29 ?  129  PHE A CB  1 
ATOM   767  C  CG  . PHE A 1 130 ? 30.387  51.862  30.908  1.00 131.35 ?  129  PHE A CG  1 
ATOM   768  C  CD1 . PHE A 1 130 ? 29.764  51.762  29.672  1.00 131.04 ?  129  PHE A CD1 1 
ATOM   769  C  CD2 . PHE A 1 130 ? 29.660  51.532  32.041  1.00 145.82 ?  129  PHE A CD2 1 
ATOM   770  C  CE1 . PHE A 1 130 ? 28.453  51.317  29.571  1.00 133.60 ?  129  PHE A CE1 1 
ATOM   771  C  CE2 . PHE A 1 130 ? 28.351  51.096  31.946  1.00 147.27 ?  129  PHE A CE2 1 
ATOM   772  C  CZ  . PHE A 1 130 ? 27.745  50.990  30.710  1.00 141.03 ?  129  PHE A CZ  1 
ATOM   773  N  N   . LYS A 1 131 ? 32.137  55.285  30.209  1.00 125.13 ?  130  LYS A N   1 
ATOM   774  C  CA  . LYS A 1 131 ? 31.436  56.566  30.151  1.00 138.29 ?  130  LYS A CA  1 
ATOM   775  C  C   . LYS A 1 131 ? 31.571  57.258  28.796  1.00 141.66 ?  130  LYS A C   1 
ATOM   776  O  O   . LYS A 1 131 ? 30.605  57.826  28.290  1.00 139.65 ?  130  LYS A O   1 
ATOM   777  C  CB  . LYS A 1 131 ? 31.925  57.499  31.261  1.00 129.82 ?  130  LYS A CB  1 
ATOM   778  C  CG  . LYS A 1 131 ? 30.976  58.656  31.535  1.00 126.36 ?  130  LYS A CG  1 
ATOM   779  C  CD  . LYS A 1 131 ? 31.573  59.661  32.501  1.00 131.75 ?  130  LYS A CD  1 
ATOM   780  C  CE  . LYS A 1 131 ? 30.672  60.876  32.649  1.00 139.14 ?  130  LYS A CE  1 
ATOM   781  N  NZ  . LYS A 1 131 ? 31.206  61.846  33.645  1.00 141.20 1  130  LYS A NZ  1 
ATOM   782  N  N   . VAL A 1 132 ? 32.755  57.187  28.197  1.00 135.08 ?  131  VAL A N   1 
ATOM   783  C  CA  . VAL A 1 132 ? 32.982  57.823  26.905  1.00 132.08 ?  131  VAL A CA  1 
ATOM   784  C  C   . VAL A 1 132 ? 32.153  57.162  25.793  1.00 130.38 ?  131  VAL A C   1 
ATOM   785  O  O   . VAL A 1 132 ? 31.667  57.846  24.889  1.00 144.69 ?  131  VAL A O   1 
ATOM   786  C  CB  . VAL A 1 132 ? 34.490  57.807  26.536  1.00 171.81 ?  131  VAL A CB  1 
ATOM   787  C  CG1 . VAL A 1 132 ? 35.035  56.386  26.488  1.00 157.95 ?  131  VAL A CG1 1 
ATOM   788  C  CG2 . VAL A 1 132 ? 34.742  58.534  25.218  1.00 180.08 ?  131  VAL A CG2 1 
ATOM   789  N  N   . VAL A 1 133 ? 31.983  55.843  25.865  1.00 114.50 ?  132  VAL A N   1 
ATOM   790  C  CA  . VAL A 1 133 ? 31.189  55.103  24.881  1.00 114.12 ?  132  VAL A CA  1 
ATOM   791  C  C   . VAL A 1 133 ? 29.694  55.420  24.999  1.00 109.75 ?  132  VAL A C   1 
ATOM   792  O  O   . VAL A 1 133 ? 28.997  55.561  23.991  1.00 100.32 ?  132  VAL A O   1 
ATOM   793  C  CB  . VAL A 1 133 ? 31.408  53.584  25.001  1.00 113.08 ?  132  VAL A CB  1 
ATOM   794  C  CG1 . VAL A 1 133 ? 30.537  52.858  24.011  1.00 102.06 ?  132  VAL A CG1 1 
ATOM   795  C  CG2 . VAL A 1 133 ? 32.857  53.246  24.729  1.00 126.38 ?  132  VAL A CG2 1 
ATOM   796  N  N   . LYS A 1 134 ? 29.200  55.519  26.231  1.00 112.92 ?  133  LYS A N   1 
ATOM   797  C  CA  . LYS A 1 134 ? 27.797  55.871  26.461  1.00 123.51 ?  133  LYS A CA  1 
ATOM   798  C  C   . LYS A 1 134 ? 27.464  57.259  25.912  1.00 142.17 ?  133  LYS A C   1 
ATOM   799  O  O   . LYS A 1 134 ? 26.430  57.458  25.281  1.00 145.82 ?  133  LYS A O   1 
ATOM   800  C  CB  . LYS A 1 134 ? 27.466  55.832  27.956  1.00 126.27 ?  133  LYS A CB  1 
ATOM   801  C  CG  . LYS A 1 134 ? 27.852  54.562  28.687  1.00 121.33 ?  133  LYS A CG  1 
ATOM   802  C  CD  . LYS A 1 134 ? 27.253  54.533  30.097  1.00 126.42 ?  133  LYS A CD  1 
ATOM   803  C  CE  . LYS A 1 134 ? 25.772  54.889  30.098  1.00 133.46 ?  133  LYS A CE  1 
ATOM   804  N  NZ  . LYS A 1 134 ? 25.293  55.239  31.469  1.00 129.16 1  133  LYS A NZ  1 
ATOM   805  N  N   . GLU A 1 135 ? 28.346  58.215  26.175  1.00 158.81 ?  134  GLU A N   1 
ATOM   806  C  CA  . GLU A 1 135 ? 28.233  59.570  25.652  1.00 158.59 ?  134  GLU A CA  1 
ATOM   807  C  C   . GLU A 1 135 ? 28.312  59.552  24.116  1.00 144.39 ?  134  GLU A C   1 
ATOM   808  O  O   . GLU A 1 135 ? 27.684  60.355  23.416  1.00 132.77 ?  134  GLU A O   1 
ATOM   809  C  CB  . GLU A 1 135 ? 29.336  60.427  26.275  1.00 157.55 ?  134  GLU A CB  1 
ATOM   810  C  CG  . GLU A 1 135 ? 29.012  60.897  27.689  1.00 156.73 ?  134  GLU A CG  1 
ATOM   811  C  CD  . GLU A 1 135 ? 30.020  61.892  28.228  1.00 156.87 ?  134  GLU A CD  1 
ATOM   812  O  OE1 . GLU A 1 135 ? 31.204  61.811  27.837  1.00 152.07 ?  134  GLU A OE1 1 
ATOM   813  O  OE2 . GLU A 1 135 ? 29.623  62.770  29.023  1.00 167.97 -1 134  GLU A OE2 1 
ATOM   814  N  N   . PHE A 1 136 ? 29.084  58.601  23.605  1.00 147.86 ?  135  PHE A N   1 
ATOM   815  C  CA  . PHE A 1 136 ? 29.250  58.424  22.170  1.00 150.08 ?  135  PHE A CA  1 
ATOM   816  C  C   . PHE A 1 136 ? 28.017  57.894  21.457  1.00 156.52 ?  135  PHE A C   1 
ATOM   817  O  O   . PHE A 1 136 ? 27.612  58.432  20.429  1.00 165.11 ?  135  PHE A O   1 
ATOM   818  C  CB  . PHE A 1 136 ? 30.420  57.485  21.898  1.00 150.14 ?  135  PHE A CB  1 
ATOM   819  C  CG  . PHE A 1 136 ? 30.773  57.376  20.451  1.00 159.69 ?  135  PHE A CG  1 
ATOM   820  C  CD1 . PHE A 1 136 ? 31.399  58.418  19.795  1.00 171.47 ?  135  PHE A CD1 1 
ATOM   821  C  CD2 . PHE A 1 136 ? 30.473  56.226  19.741  1.00 159.14 ?  135  PHE A CD2 1 
ATOM   822  C  CE1 . PHE A 1 136 ? 31.721  58.311  18.460  1.00 171.09 ?  135  PHE A CE1 1 
ATOM   823  C  CE2 . PHE A 1 136 ? 30.794  56.116  18.407  1.00 158.21 ?  135  PHE A CE2 1 
ATOM   824  C  CZ  . PHE A 1 136 ? 31.417  57.160  17.765  1.00 163.98 ?  135  PHE A CZ  1 
ATOM   825  N  N   . VAL A 1 137 ? 27.430  56.832  21.998  1.00 157.69 ?  136  VAL A N   1 
ATOM   826  C  CA  . VAL A 1 137 ? 26.262  56.211  21.384  1.00 164.33 ?  136  VAL A CA  1 
ATOM   827  C  C   . VAL A 1 137 ? 25.077  57.178  21.433  1.00 168.47 ?  136  VAL A C   1 
ATOM   828  O  O   . VAL A 1 137 ? 24.124  57.052  20.662  1.00 166.44 ?  136  VAL A O   1 
ATOM   829  C  CB  . VAL A 1 137 ? 25.900  54.874  22.071  1.00 155.58 ?  136  VAL A CB  1 
ATOM   830  C  CG1 . VAL A 1 137 ? 25.348  55.115  23.471  1.00 157.29 ?  136  VAL A CG1 1 
ATOM   831  C  CG2 . VAL A 1 137 ? 24.912  54.086  21.229  1.00 152.65 ?  136  VAL A CG2 1 
ATOM   832  N  N   . SER A 1 138 ? 25.156  58.152  22.336  1.00 166.87 ?  137  SER A N   1 
ATOM   833  C  CA  . SER A 1 138 ? 24.131  59.179  22.472  1.00 173.50 ?  137  SER A CA  1 
ATOM   834  C  C   . SER A 1 138 ? 24.010  60.022  21.205  1.00 179.94 ?  137  SER A C   1 
ATOM   835  O  O   . SER A 1 138 ? 22.908  60.405  20.816  1.00 189.21 ?  137  SER A O   1 
ATOM   836  C  CB  . SER A 1 138 ? 24.434  60.075  23.674  1.00 185.03 ?  137  SER A CB  1 
ATOM   837  O  OG  . SER A 1 138 ? 24.878  59.307  24.778  1.00 179.76 ?  137  SER A OG  1 
ATOM   838  N  N   . VAL A 1 139 ? 25.144  60.316  20.573  1.00 188.25 ?  138  VAL A N   1 
ATOM   839  C  CA  . VAL A 1 139 ? 25.160  61.140  19.366  1.00 202.68 ?  138  VAL A CA  1 
ATOM   840  C  C   . VAL A 1 139 ? 24.348  60.500  18.240  1.00 217.09 ?  138  VAL A C   1 
ATOM   841  O  O   . VAL A 1 139 ? 23.370  61.077  17.763  1.00 242.20 ?  138  VAL A O   1 
ATOM   842  C  CB  . VAL A 1 139 ? 26.600  61.392  18.873  1.00 195.56 ?  138  VAL A CB  1 
ATOM   843  C  CG1 . VAL A 1 139 ? 26.583  62.162  17.561  1.00 203.00 ?  138  VAL A CG1 1 
ATOM   844  C  CG2 . VAL A 1 139 ? 27.398  62.141  19.926  1.00 187.93 ?  138  VAL A CG2 1 
ATOM   845  N  N   . GLY A 1 140 ? 24.759  59.308  17.817  1.00 210.03 ?  139  GLY A N   1 
ATOM   846  C  CA  . GLY A 1 140 ? 23.974  58.520  16.885  1.00 199.49 ?  139  GLY A CA  1 
ATOM   847  C  C   . GLY A 1 140 ? 23.977  58.972  15.436  1.00 196.00 ?  139  GLY A C   1 
ATOM   848  O  O   . GLY A 1 140 ? 23.493  58.249  14.563  1.00 183.81 ?  139  GLY A O   1 
ATOM   849  N  N   . GLY A 1 141 ? 24.521  60.155  15.168  1.00 200.93 ?  140  GLY A N   1 
ATOM   850  C  CA  . GLY A 1 141 ? 24.538  60.672  13.812  1.00 201.48 ?  140  GLY A CA  1 
ATOM   851  C  C   . GLY A 1 141 ? 25.438  59.828  12.936  1.00 194.32 ?  140  GLY A C   1 
ATOM   852  O  O   . GLY A 1 141 ? 25.015  59.319  11.900  1.00 197.47 ?  140  GLY A O   1 
ATOM   853  N  N   . VAL A 1 142 ? 26.686  59.670  13.359  1.00 186.91 ?  141  VAL A N   1 
ATOM   854  C  CA  . VAL A 1 142 ? 27.597  58.739  12.706  1.00 180.31 ?  141  VAL A CA  1 
ATOM   855  C  C   . VAL A 1 142 ? 28.300  57.959  13.812  1.00 168.00 ?  141  VAL A C   1 
ATOM   856  O  O   . VAL A 1 142 ? 29.520  57.794  13.805  1.00 160.27 ?  141  VAL A O   1 
ATOM   857  C  CB  . VAL A 1 142 ? 28.631  59.450  11.798  1.00 179.38 ?  141  VAL A CB  1 
ATOM   858  C  CG1 . VAL A 1 142 ? 29.289  58.447  10.857  1.00 172.66 ?  141  VAL A CG1 1 
ATOM   859  C  CG2 . VAL A 1 142 ? 27.973  60.554  10.981  1.00 178.61 ?  141  VAL A CG2 1 
ATOM   860  N  N   . SER A 1 143 ? 27.513  57.495  14.776  1.00 167.33 ?  142  SER A N   1 
ATOM   861  C  CA  . SER A 1 143 ? 28.046  56.760  15.913  1.00 177.44 ?  142  SER A CA  1 
ATOM   862  C  C   . SER A 1 143 ? 28.637  55.432  15.455  1.00 181.23 ?  142  SER A C   1 
ATOM   863  O  O   . SER A 1 143 ? 29.805  55.136  15.723  1.00 171.79 ?  142  SER A O   1 
ATOM   864  C  CB  . SER A 1 143 ? 26.954  56.532  16.963  1.00 176.82 ?  142  SER A CB  1 
ATOM   865  O  OG  . SER A 1 143 ? 25.870  55.796  16.422  1.00 169.98 ?  142  SER A OG  1 
ATOM   866  N  N   . ILE A 1 144 ? 27.820  54.654  14.749  1.00 193.24 ?  143  ILE A N   1 
ATOM   867  C  CA  . ILE A 1 144 ? 28.204  53.334  14.257  1.00 187.00 ?  143  ILE A CA  1 
ATOM   868  C  C   . ILE A 1 144 ? 28.794  52.491  15.396  1.00 176.25 ?  143  ILE A C   1 
ATOM   869  O  O   . ILE A 1 144 ? 29.914  51.990  15.285  1.00 176.50 ?  143  ILE A O   1 
ATOM   870  C  CB  . ILE A 1 144 ? 29.224  53.442  13.089  1.00 180.50 ?  143  ILE A CB  1 
ATOM   871  C  CG1 . ILE A 1 144 ? 28.868  54.607  12.159  1.00 189.88 ?  143  ILE A CG1 1 
ATOM   872  C  CG2 . ILE A 1 144 ? 29.331  52.124  12.317  1.00 175.28 ?  143  ILE A CG2 1 
ATOM   873  C  CD1 . ILE A 1 144 ? 27.624  54.376  11.317  1.00 193.67 ?  143  ILE A CD1 1 
ATOM   874  N  N   . PRO A 1 145 ? 28.057  52.365  16.514  1.00 166.09 ?  144  PRO A N   1 
ATOM   875  C  CA  . PRO A 1 145 ? 28.647  51.752  17.707  1.00 147.93 ?  144  PRO A CA  1 
ATOM   876  C  C   . PRO A 1 145 ? 29.033  50.289  17.510  1.00 132.20 ?  144  PRO A C   1 
ATOM   877  O  O   . PRO A 1 145 ? 28.164  49.435  17.345  1.00 134.72 ?  144  PRO A O   1 
ATOM   878  C  CB  . PRO A 1 145 ? 27.530  51.883  18.741  1.00 145.93 ?  144  PRO A CB  1 
ATOM   879  C  CG  . PRO A 1 145 ? 26.279  51.844  17.927  1.00 155.20 ?  144  PRO A CG  1 
ATOM   880  C  CD  . PRO A 1 145 ? 26.624  52.659  16.714  1.00 162.84 ?  144  PRO A CD  1 
ATOM   881  N  N   . ARG A 1 146 ? 30.330  50.005  17.526  1.00 124.83 ?  145  ARG A N   1 
ATOM   882  C  CA  . ARG A 1 146 ? 30.801  48.645  17.304  1.00 121.33 ?  145  ARG A CA  1 
ATOM   883  C  C   . ARG A 1 146 ? 31.033  47.976  18.656  1.00 124.23 ?  145  ARG A C   1 
ATOM   884  O  O   . ARG A 1 146 ? 31.308  48.647  19.649  1.00 119.24 ?  145  ARG A O   1 
ATOM   885  C  CB  . ARG A 1 146 ? 32.076  48.615  16.458  1.00 114.30 ?  145  ARG A CB  1 
ATOM   886  C  CG  . ARG A 1 146 ? 32.423  47.221  15.958  1.00 106.70 ?  145  ARG A CG  1 
ATOM   887  C  CD  . ARG A 1 146 ? 33.719  47.174  15.171  1.00 110.05 ?  145  ARG A CD  1 
ATOM   888  N  NE  . ARG A 1 146 ? 33.620  47.829  13.870  1.00 132.97 ?  145  ARG A NE  1 
ATOM   889  C  CZ  . ARG A 1 146 ? 34.624  47.914  13.001  1.00 139.85 ?  145  ARG A CZ  1 
ATOM   890  N  NH1 . ARG A 1 146 ? 35.804  47.383  13.296  1.00 131.46 ?  145  ARG A NH1 1 
ATOM   891  N  NH2 . ARG A 1 146 ? 34.448  48.527  11.837  1.00 144.47 ?  145  ARG A NH2 1 
ATOM   892  N  N   . LEU A 1 147 ? 30.878  46.658  18.701  1.00 131.09 ?  146  LEU A N   1 
ATOM   893  C  CA  . LEU A 1 147 ? 31.138  45.890  19.914  1.00 124.74 ?  146  LEU A CA  1 
ATOM   894  C  C   . LEU A 1 147 ? 32.539  46.118  20.481  1.00 118.82 ?  146  LEU A C   1 
ATOM   895  O  O   . LEU A 1 147 ? 32.716  46.183  21.695  1.00 121.19 ?  146  LEU A O   1 
ATOM   896  C  CB  . LEU A 1 147 ? 30.932  44.399  19.644  1.00 130.99 ?  146  LEU A CB  1 
ATOM   897  C  CG  . LEU A 1 147 ? 31.163  43.456  20.826  1.00 121.89 ?  146  LEU A CG  1 
ATOM   898  C  CD1 . LEU A 1 147 ? 29.982  42.514  21.000  1.00 123.32 ?  146  LEU A CD1 1 
ATOM   899  C  CD2 . LEU A 1 147 ? 32.456  42.671  20.648  1.00 103.11 ?  146  LEU A CD2 1 
ATOM   900  N  N   . ARG A 1 148 ? 33.529  46.247  19.603  1.00 118.50 ?  147  ARG A N   1 
ATOM   901  C  CA  . ARG A 1 148 ? 34.913  46.435  20.032  1.00 114.30 ?  147  ARG A CA  1 
ATOM   902  C  C   . ARG A 1 148 ? 35.096  47.709  20.862  1.00 114.28 ?  147  ARG A C   1 
ATOM   903  O  O   . ARG A 1 148 ? 36.028  47.794  21.657  1.00 105.75 ?  147  ARG A O   1 
ATOM   904  C  CB  . ARG A 1 148 ? 35.854  46.450  18.831  1.00 118.22 ?  147  ARG A CB  1 
ATOM   905  C  CG  . ARG A 1 148 ? 35.795  47.716  18.009  1.00 132.25 ?  147  ARG A CG  1 
ATOM   906  C  CD  . ARG A 1 148 ? 36.796  47.667  16.876  1.00 139.58 ?  147  ARG A CD  1 
ATOM   907  N  NE  . ARG A 1 148 ? 36.569  48.762  15.941  1.00 140.23 ?  147  ARG A NE  1 
ATOM   908  C  CZ  . ARG A 1 148 ? 37.188  49.935  16.002  1.00 133.18 ?  147  ARG A CZ  1 
ATOM   909  N  NH1 . ARG A 1 148 ? 38.086  50.161  16.949  1.00 150.64 ?  147  ARG A NH1 1 
ATOM   910  N  NH2 . ARG A 1 148 ? 36.913  50.878  15.112  1.00 114.53 ?  147  ARG A NH2 1 
ATOM   911  N  N   . THR A 1 149 ? 34.245  48.711  20.641  1.00 117.36 ?  148  THR A N   1 
ATOM   912  C  CA  . THR A 1 149 ? 34.242  49.917  21.472  1.00 122.51 ?  148  THR A CA  1 
ATOM   913  C  C   . THR A 1 149 ? 33.765  49.590  22.887  1.00 125.53 ?  148  THR A C   1 
ATOM   914  O  O   . THR A 1 149 ? 34.386  49.985  23.872  1.00 134.52 ?  148  THR A O   1 
ATOM   915  C  CB  . THR A 1 149 ? 33.342  51.031  20.892  1.00 126.57 ?  148  THR A CB  1 
ATOM   916  O  OG1 . THR A 1 149 ? 32.013  50.902  21.413  1.00 129.23 ?  148  THR A OG1 1 
ATOM   917  C  CG2 . THR A 1 149 ? 33.303  50.964  19.380  1.00 132.54 ?  148  THR A CG2 1 
ATOM   918  N  N   . TYR A 1 150 ? 32.629  48.900  22.968  1.00 111.42 ?  149  TYR A N   1 
ATOM   919  C  CA  . TYR A 1 150 ? 32.058  48.426  24.229  1.00 99.89  ?  149  TYR A CA  1 
ATOM   920  C  C   . TYR A 1 150 ? 32.976  47.455  24.973  1.00 106.33 ?  149  TYR A C   1 
ATOM   921  O  O   . TYR A 1 150 ? 32.873  47.295  26.190  1.00 98.93  ?  149  TYR A O   1 
ATOM   922  C  CB  . TYR A 1 150 ? 30.720  47.735  23.969  1.00 102.42 ?  149  TYR A CB  1 
ATOM   923  C  CG  . TYR A 1 150 ? 29.515  48.643  23.891  1.00 109.09 ?  149  TYR A CG  1 
ATOM   924  C  CD1 . TYR A 1 150 ? 29.353  49.705  24.766  1.00 108.61 ?  149  TYR A CD1 1 
ATOM   925  C  CD2 . TYR A 1 150 ? 28.529  48.427  22.935  1.00 108.25 ?  149  TYR A CD2 1 
ATOM   926  C  CE1 . TYR A 1 150 ? 28.233  50.528  24.687  1.00 102.17 ?  149  TYR A CE1 1 
ATOM   927  C  CE2 . TYR A 1 150 ? 27.417  49.241  22.849  1.00 100.74 ?  149  TYR A CE2 1 
ATOM   928  C  CZ  . TYR A 1 150 ? 27.275  50.291  23.724  1.00 98.63  ?  149  TYR A CZ  1 
ATOM   929  O  OH  . TYR A 1 150 ? 26.166  51.098  23.633  1.00 107.66 ?  149  TYR A OH  1 
ATOM   930  N  N   . ALA A 1 151 ? 33.856  46.792  24.228  1.00 119.16 ?  150  ALA A N   1 
ATOM   931  C  CA  . ALA A 1 151 ? 34.643  45.674  24.752  1.00 114.76 ?  150  ALA A CA  1 
ATOM   932  C  C   . ALA A 1 151 ? 35.575  46.026  25.919  1.00 112.49 ?  150  ALA A C   1 
ATOM   933  O  O   . ALA A 1 151 ? 35.480  45.391  26.968  1.00 114.23 ?  150  ALA A O   1 
ATOM   934  C  CB  . ALA A 1 151 ? 35.449  45.021  23.621  1.00 122.27 ?  150  ALA A CB  1 
ATOM   935  N  N   . PRO A 1 152 ? 36.468  47.030  25.760  1.00 114.11 ?  151  PRO A N   1 
ATOM   936  C  CA  . PRO A 1 152 ? 37.423  47.268  26.850  1.00 103.44 ?  151  PRO A CA  1 
ATOM   937  C  C   . PRO A 1 152 ? 36.732  47.686  28.138  1.00 99.86  ?  151  PRO A C   1 
ATOM   938  O  O   . PRO A 1 152 ? 37.222  47.380  29.223  1.00 116.60 ?  151  PRO A O   1 
ATOM   939  C  CB  . PRO A 1 152 ? 38.305  48.403  26.313  1.00 106.49 ?  151  PRO A CB  1 
ATOM   940  C  CG  . PRO A 1 152 ? 38.058  48.438  24.845  1.00 115.01 ?  151  PRO A CG  1 
ATOM   941  C  CD  . PRO A 1 152 ? 36.640  48.020  24.683  1.00 117.14 ?  151  PRO A CD  1 
ATOM   942  N  N   . ALA A 1 153 ? 35.600  48.368  28.009  1.00 88.18  ?  152  ALA A N   1 
ATOM   943  C  CA  . ALA A 1 153 ? 34.826  48.783  29.172  1.00 105.15 ?  152  ALA A CA  1 
ATOM   944  C  C   . ALA A 1 153 ? 34.383  47.572  29.986  1.00 113.61 ?  152  ALA A C   1 
ATOM   945  O  O   . ALA A 1 153 ? 34.562  47.531  31.204  1.00 112.61 ?  152  ALA A O   1 
ATOM   946  C  CB  . ALA A 1 153 ? 33.620  49.606  28.745  1.00 104.94 ?  152  ALA A CB  1 
ATOM   947  N  N   . LEU A 1 154 ? 33.814  46.583  29.307  1.00 115.97 ?  153  LEU A N   1 
ATOM   948  C  CA  . LEU A 1 154 ? 33.361  45.371  29.976  1.00 111.27 ?  153  LEU A CA  1 
ATOM   949  C  C   . LEU A 1 154 ? 34.507  44.522  30.531  1.00 109.35 ?  153  LEU A C   1 
ATOM   950  O  O   . LEU A 1 154 ? 34.432  44.057  31.666  1.00 116.94 ?  153  LEU A O   1 
ATOM   951  C  CB  . LEU A 1 154 ? 32.495  44.542  29.022  1.00 105.81 ?  153  LEU A CB  1 
ATOM   952  C  CG  . LEU A 1 154 ? 31.959  43.207  29.543  1.00 91.45  ?  153  LEU A CG  1 
ATOM   953  C  CD1 . LEU A 1 154 ? 30.519  42.998  29.117  1.00 69.80  ?  153  LEU A CD1 1 
ATOM   954  C  CD2 . LEU A 1 154 ? 32.827  42.074  29.020  1.00 95.18  ?  153  LEU A CD2 1 
ATOM   955  N  N   . LEU A 1 155 ? 35.566  44.328  29.749  1.00 98.44  ?  154  LEU A N   1 
ATOM   956  C  CA  . LEU A 1 155 ? 36.676  43.473  30.177  1.00 98.21  ?  154  LEU A CA  1 
ATOM   957  C  C   . LEU A 1 155 ? 37.355  43.986  31.440  1.00 107.73 ?  154  LEU A C   1 
ATOM   958  O  O   . LEU A 1 155 ? 37.690  43.209  32.336  1.00 114.51 ?  154  LEU A O   1 
ATOM   959  C  CB  . LEU A 1 155 ? 37.723  43.327  29.070  1.00 92.86  ?  154  LEU A CB  1 
ATOM   960  C  CG  . LEU A 1 155 ? 37.544  42.158  28.099  1.00 96.20  ?  154  LEU A CG  1 
ATOM   961  C  CD1 . LEU A 1 155 ? 36.245  42.270  27.323  1.00 103.36 ?  154  LEU A CD1 1 
ATOM   962  C  CD2 . LEU A 1 155 ? 38.742  42.048  27.160  1.00 85.19  ?  154  LEU A CD2 1 
ATOM   963  N  N   . CYS A 1 156 ? 37.562  45.294  31.504  1.00 102.75 ?  155  CYS A N   1 
ATOM   964  C  CA  . CYS A 1 156 ? 38.191  45.897  32.663  1.00 103.46 ?  155  CYS A CA  1 
ATOM   965  C  C   . CYS A 1 156 ? 37.289  45.742  33.887  1.00 100.84 ?  155  CYS A C   1 
ATOM   966  O  O   . CYS A 1 156 ? 37.764  45.401  34.966  1.00 100.07 ?  155  CYS A O   1 
ATOM   967  C  CB  . CYS A 1 156 ? 38.509  47.366  32.394  1.00 115.24 ?  155  CYS A CB  1 
ATOM   968  S  SG  . CYS A 1 156 ? 39.523  48.150  33.656  1.00 98.80  ?  155  CYS A SG  1 
ATOM   969  N  N   . PHE A 1 157 ? 35.993  45.995  33.719  1.00 101.25 ?  156  PHE A N   1 
ATOM   970  C  CA  . PHE A 1 157 ? 35.024  45.798  34.800  1.00 117.81 ?  156  PHE A CA  1 
ATOM   971  C  C   . PHE A 1 157 ? 34.953  44.345  35.260  1.00 109.47 ?  156  PHE A C   1 
ATOM   972  O  O   . PHE A 1 157 ? 34.676  44.057  36.424  1.00 105.33 ?  156  PHE A O   1 
ATOM   973  C  CB  . PHE A 1 157 ? 33.634  46.262  34.366  1.00 126.56 ?  156  PHE A CB  1 
ATOM   974  C  CG  . PHE A 1 157 ? 33.477  47.749  34.345  1.00 140.28 ?  156  PHE A CG  1 
ATOM   975  C  CD1 . PHE A 1 157 ? 34.384  48.559  35.010  1.00 157.05 ?  156  PHE A CD1 1 
ATOM   976  C  CD2 . PHE A 1 157 ? 32.424  48.341  33.666  1.00 148.62 ?  156  PHE A CD2 1 
ATOM   977  C  CE1 . PHE A 1 157 ? 34.249  49.933  34.996  1.00 176.30 ?  156  PHE A CE1 1 
ATOM   978  C  CE2 . PHE A 1 157 ? 32.282  49.715  33.649  1.00 164.35 ?  156  PHE A CE2 1 
ATOM   979  C  CZ  . PHE A 1 157 ? 33.194  50.511  34.315  1.00 172.30 ?  156  PHE A CZ  1 
ATOM   980  N  N   . CYS A 1 158 ? 35.189  43.434  34.326  1.00 105.21 ?  157  CYS A N   1 
ATOM   981  C  CA  . CYS A 1 158 ? 35.192  42.011  34.621  1.00 107.63 ?  157  CYS A CA  1 
ATOM   982  C  C   . CYS A 1 158 ? 36.415  41.599  35.439  1.00 105.03 ?  157  CYS A C   1 
ATOM   983  O  O   . CYS A 1 158 ? 36.315  40.823  36.394  1.00 88.87  ?  157  CYS A O   1 
ATOM   984  C  CB  . CYS A 1 158 ? 35.122  41.205  33.327  1.00 106.53 ?  157  CYS A CB  1 
ATOM   985  S  SG  . CYS A 1 158 ? 33.428  40.934  32.761  1.00 138.50 ?  157  CYS A SG  1 
ATOM   986  N  N   . GLU A 1 159 ? 37.577  42.099  35.034  1.00 114.96 ?  158  GLU A N   1 
ATOM   987  C  CA  . GLU A 1 159 ? 38.823  41.794  35.720  1.00 121.25 ?  158  GLU A CA  1 
ATOM   988  C  C   . GLU A 1 159 ? 38.829  42.352  37.152  1.00 139.22 ?  158  GLU A C   1 
ATOM   989  O  O   . GLU A 1 159 ? 39.407  41.751  38.059  1.00 153.48 ?  158  GLU A O   1 
ATOM   990  C  CB  . GLU A 1 159 ? 40.002  42.342  34.911  1.00 116.54 ?  158  GLU A CB  1 
ATOM   991  C  CG  . GLU A 1 159 ? 41.376  42.033  35.481  1.00 135.36 ?  158  GLU A CG  1 
ATOM   992  C  CD  . GLU A 1 159 ? 41.834  40.611  35.199  1.00 151.56 ?  158  GLU A CD  1 
ATOM   993  O  OE1 . GLU A 1 159 ? 40.979  39.711  35.051  1.00 149.64 ?  158  GLU A OE1 1 
ATOM   994  O  OE2 . GLU A 1 159 ? 43.061  40.393  35.123  1.00 167.18 ?  158  GLU A OE2 1 
ATOM   995  N  N   . LYS A 1 160 ? 38.190  43.504  37.344  1.00 132.13 ?  159  LYS A N   1 
ATOM   996  C  CA  . LYS A 1 160 ? 38.084  44.144  38.659  1.00 110.10 ?  159  LYS A CA  1 
ATOM   997  C  C   . LYS A 1 160 ? 36.933  43.575  39.495  1.00 99.45  ?  159  LYS A C   1 
ATOM   998  O  O   . LYS A 1 160 ? 36.700  44.017  40.622  1.00 118.36 ?  159  LYS A O   1 
ATOM   999  C  CB  . LYS A 1 160 ? 37.928  45.662  38.502  1.00 106.74 ?  159  LYS A CB  1 
ATOM   1000 C  CG  . LYS A 1 160 ? 39.244  46.405  38.292  1.00 100.70 ?  159  LYS A CG  1 
ATOM   1001 C  CD  . LYS A 1 160 ? 39.025  47.813  37.748  1.00 97.50  ?  159  LYS A CD  1 
ATOM   1002 C  CE  . LYS A 1 160 ? 38.088  48.625  38.628  1.00 98.16  ?  159  LYS A CE  1 
ATOM   1003 N  NZ  . LYS A 1 160 ? 37.852  49.990  38.073  1.00 97.98  ?  159  LYS A NZ  1 
ATOM   1004 N  N   . LEU A 1 161 ? 36.203  42.624  38.915  1.00 87.88  ?  160  LEU A N   1 
ATOM   1005 C  CA  . LEU A 1 161 ? 35.123  41.898  39.591  1.00 85.73  ?  160  LEU A CA  1 
ATOM   1006 C  C   . LEU A 1 161 ? 33.902  42.764  39.901  1.00 86.52  ?  160  LEU A C   1 
ATOM   1007 O  O   . LEU A 1 161 ? 33.113  42.434  40.787  1.00 88.83  ?  160  LEU A O   1 
ATOM   1008 C  CB  . LEU A 1 161 ? 35.628  41.233  40.880  1.00 81.87  ?  160  LEU A CB  1 
ATOM   1009 C  CG  . LEU A 1 161 ? 36.379  39.898  40.778  1.00 83.54  ?  160  LEU A CG  1 
ATOM   1010 C  CD1 . LEU A 1 161 ? 37.699  40.040  40.047  1.00 78.17  ?  160  LEU A CD1 1 
ATOM   1011 C  CD2 . LEU A 1 161 ? 36.596  39.294  42.157  1.00 97.69  ?  160  LEU A CD2 1 
ATOM   1012 N  N   . GLU A 1 162 ? 33.740  43.862  39.171  1.00 93.33  ?  161  GLU A N   1 
ATOM   1013 C  CA  . GLU A 1 162 ? 32.528  44.667  39.300  1.00 111.87 ?  161  GLU A CA  1 
ATOM   1014 C  C   . GLU A 1 162 ? 31.422  44.026  38.470  1.00 123.89 ?  161  GLU A C   1 
ATOM   1015 O  O   . GLU A 1 162 ? 31.307  44.282  37.271  1.00 127.18 ?  161  GLU A O   1 
ATOM   1016 C  CB  . GLU A 1 162 ? 32.775  46.109  38.847  1.00 124.97 ?  161  GLU A CB  1 
ATOM   1017 C  CG  . GLU A 1 162 ? 34.189  46.621  39.114  1.00 137.10 ?  161  GLU A CG  1 
ATOM   1018 C  CD  . GLU A 1 162 ? 34.209  47.825  40.040  1.00 154.75 ?  161  GLU A CD  1 
ATOM   1019 O  OE1 . GLU A 1 162 ? 33.119  48.287  40.441  1.00 154.21 ?  161  GLU A OE1 1 
ATOM   1020 O  OE2 . GLU A 1 162 ? 35.314  48.306  40.373  1.00 165.75 ?  161  GLU A OE2 1 
ATOM   1021 N  N   . ALA A 1 163 ? 30.607  43.195  39.116  1.00 132.74 ?  162  ALA A N   1 
ATOM   1022 C  CA  . ALA A 1 163 ? 29.634  42.363  38.411  1.00 130.18 ?  162  ALA A CA  1 
ATOM   1023 C  C   . ALA A 1 163 ? 28.478  43.164  37.821  1.00 123.30 ?  162  ALA A C   1 
ATOM   1024 O  O   . ALA A 1 163 ? 28.190  43.060  36.632  1.00 101.32 ?  162  ALA A O   1 
ATOM   1025 C  CB  . ALA A 1 163 ? 29.101  41.286  39.347  1.00 130.98 ?  162  ALA A CB  1 
ATOM   1026 N  N   . GLU A 1 164 ? 27.821  43.958  38.661  1.00 124.72 ?  163  GLU A N   1 
ATOM   1027 C  CA  . GLU A 1 164 ? 26.660  44.751  38.255  1.00 135.36 ?  163  GLU A CA  1 
ATOM   1028 C  C   . GLU A 1 164 ? 27.026  45.776  37.189  1.00 129.05 ?  163  GLU A C   1 
ATOM   1029 O  O   . GLU A 1 164 ? 26.189  46.164  36.374  1.00 120.02 ?  163  GLU A O   1 
ATOM   1030 C  CB  . GLU A 1 164 ? 26.028  45.445  39.467  1.00 152.11 ?  163  GLU A CB  1 
ATOM   1031 C  CG  . GLU A 1 164 ? 24.946  44.626  40.168  1.00 156.15 ?  163  GLU A CG  1 
ATOM   1032 C  CD  . GLU A 1 164 ? 25.464  43.311  40.725  1.00 156.75 ?  163  GLU A CD  1 
ATOM   1033 O  OE1 . GLU A 1 164 ? 26.650  43.252  41.115  1.00 151.58 ?  163  GLU A OE1 1 
ATOM   1034 O  OE2 . GLU A 1 164 ? 24.681  42.337  40.780  1.00 160.88 ?  163  GLU A OE2 1 
ATOM   1035 N  N   . LYS A 1 165 ? 28.266  46.251  37.239  1.00 142.84 ?  164  LYS A N   1 
ATOM   1036 C  CA  . LYS A 1 165 ? 28.782  47.165  36.228  1.00 145.71 ?  164  LYS A CA  1 
ATOM   1037 C  C   . LYS A 1 165 ? 28.852  46.472  34.866  1.00 142.57 ?  164  LYS A C   1 
ATOM   1038 O  O   . LYS A 1 165 ? 28.456  47.035  33.846  1.00 150.90 ?  164  LYS A O   1 
ATOM   1039 C  CB  . LYS A 1 165 ? 30.167  47.679  36.636  1.00 144.33 ?  164  LYS A CB  1 
ATOM   1040 C  CG  . LYS A 1 165 ? 30.137  48.693  37.762  1.00 140.96 ?  164  LYS A CG  1 
ATOM   1041 C  CD  . LYS A 1 165 ? 29.195  49.836  37.439  1.00 141.69 ?  164  LYS A CD  1 
ATOM   1042 C  CE  . LYS A 1 165 ? 29.033  50.769  38.620  1.00 147.88 ?  164  LYS A CE  1 
ATOM   1043 N  NZ  . LYS A 1 165 ? 28.485  50.054  39.804  1.00 151.80 ?  164  LYS A NZ  1 
ATOM   1044 N  N   . GLY A 1 166 ? 29.370  45.246  34.874  1.00 126.55 ?  165  GLY A N   1 
ATOM   1045 C  CA  . GLY A 1 166 ? 29.480  44.424  33.682  1.00 114.98 ?  165  GLY A CA  1 
ATOM   1046 C  C   . GLY A 1 166 ? 28.130  44.056  33.085  1.00 105.39 ?  165  GLY A C   1 
ATOM   1047 O  O   . GLY A 1 166 ? 27.972  43.983  31.868  1.00 109.23 ?  165  GLY A O   1 
ATOM   1048 N  N   . TYR A 1 167 ? 27.163  43.783  33.950  1.00 97.41  ?  166  TYR A N   1 
ATOM   1049 C  CA  . TYR A 1 167 ? 25.827  43.436  33.510  1.00 106.88 ?  166  TYR A CA  1 
ATOM   1050 C  C   . TYR A 1 167 ? 25.193  44.656  32.846  1.00 117.61 ?  166  TYR A C   1 
ATOM   1051 O  O   . TYR A 1 167 ? 24.471  44.537  31.855  1.00 120.69 ?  166  TYR A O   1 
ATOM   1052 C  CB  . TYR A 1 167 ? 24.978  42.940  34.689  1.00 114.02 ?  166  TYR A CB  1 
ATOM   1053 C  CG  . TYR A 1 167 ? 25.457  41.632  35.294  1.00 128.48 ?  166  TYR A CG  1 
ATOM   1054 C  CD1 . TYR A 1 167 ? 26.628  41.019  34.855  1.00 127.02 ?  166  TYR A CD1 1 
ATOM   1055 C  CD2 . TYR A 1 167 ? 24.761  41.034  36.336  1.00 140.50 ?  166  TYR A CD2 1 
ATOM   1056 C  CE1 . TYR A 1 167 ? 27.075  39.837  35.416  1.00 125.95 ?  166  TYR A CE1 1 
ATOM   1057 C  CE2 . TYR A 1 167 ? 25.203  39.851  36.905  1.00 146.55 ?  166  TYR A CE2 1 
ATOM   1058 C  CZ  . TYR A 1 167 ? 26.364  39.260  36.440  1.00 136.55 ?  166  TYR A CZ  1 
ATOM   1059 O  OH  . TYR A 1 167 ? 26.816  38.085  36.993  1.00 135.90 ?  166  TYR A OH  1 
ATOM   1060 N  N   . GLU A 1 168 ? 25.473  45.830  33.407  1.00 127.63 ?  167  GLU A N   1 
ATOM   1061 C  CA  . GLU A 1 168 ? 24.952  47.101  32.902  1.00 126.44 ?  167  GLU A CA  1 
ATOM   1062 C  C   . GLU A 1 168 ? 25.474  47.450  31.508  1.00 132.64 ?  167  GLU A C   1 
ATOM   1063 O  O   . GLU A 1 168 ? 24.709  47.925  30.669  1.00 148.30 ?  167  GLU A O   1 
ATOM   1064 C  CB  . GLU A 1 168 ? 25.279  48.234  33.879  1.00 125.47 ?  167  GLU A CB  1 
ATOM   1065 C  CG  . GLU A 1 168 ? 24.760  49.595  33.445  1.00 130.46 ?  167  GLU A CG  1 
ATOM   1066 C  CD  . GLU A 1 168 ? 24.956  50.661  34.504  1.00 135.04 ?  167  GLU A CD  1 
ATOM   1067 O  OE1 . GLU A 1 168 ? 24.847  50.338  35.707  1.00 135.88 ?  167  GLU A OE1 1 
ATOM   1068 O  OE2 . GLU A 1 168 ? 25.213  51.826  34.134  1.00 132.50 ?  167  GLU A OE2 1 
ATOM   1069 N  N   . VAL A 1 169 ? 26.769  47.254  31.262  1.00 119.86 ?  168  VAL A N   1 
ATOM   1070 C  CA  . VAL A 1 169 ? 27.304  47.519  29.928  1.00 123.08 ?  168  VAL A CA  1 
ATOM   1071 C  C   . VAL A 1 169 ? 26.707  46.528  28.924  1.00 124.35 ?  168  VAL A C   1 
ATOM   1072 O  O   . VAL A 1 169 ? 26.359  46.917  27.815  1.00 129.05 ?  168  VAL A O   1 
ATOM   1073 C  CB  . VAL A 1 169 ? 28.864  47.488  29.885  1.00 102.80 ?  168  VAL A CB  1 
ATOM   1074 C  CG1 . VAL A 1 169 ? 29.414  46.167  30.350  1.00 104.86 ?  168  VAL A CG1 1 
ATOM   1075 C  CG2 . VAL A 1 169 ? 29.373  47.811  28.487  1.00 76.60  ?  168  VAL A CG2 1 
ATOM   1076 N  N   . GLU A 1 170 ? 26.545  45.269  29.332  1.00 122.72 ?  169  GLU A N   1 
ATOM   1077 C  CA  . GLU A 1 170 ? 25.945  44.241  28.475  1.00 127.95 ?  169  GLU A CA  1 
ATOM   1078 C  C   . GLU A 1 170 ? 24.538  44.665  28.057  1.00 129.08 ?  169  GLU A C   1 
ATOM   1079 O  O   . GLU A 1 170 ? 24.153  44.527  26.894  1.00 129.16 ?  169  GLU A O   1 
ATOM   1080 C  CB  . GLU A 1 170 ? 25.894  42.879  29.186  1.00 130.84 ?  169  GLU A CB  1 
ATOM   1081 C  CG  . GLU A 1 170 ? 24.859  41.905  28.599  1.00 133.70 ?  169  GLU A CG  1 
ATOM   1082 C  CD  . GLU A 1 170 ? 24.665  40.631  29.423  1.00 129.41 ?  169  GLU A CD  1 
ATOM   1083 O  OE1 . GLU A 1 170 ? 25.656  39.921  29.684  1.00 118.55 ?  169  GLU A OE1 1 
ATOM   1084 O  OE2 . GLU A 1 170 ? 23.513  40.336  29.807  1.00 129.78 ?  169  GLU A OE2 1 
ATOM   1085 N  N   . GLU A 1 171 ? 23.779  45.175  29.024  1.00 131.91 ?  170  GLU A N   1 
ATOM   1086 C  CA  . GLU A 1 171 ? 22.418  45.652  28.796  1.00 154.71 ?  170  GLU A CA  1 
ATOM   1087 C  C   . GLU A 1 171 ? 22.402  46.750  27.727  1.00 165.70 ?  170  GLU A C   1 
ATOM   1088 O  O   . GLU A 1 171 ? 21.503  46.795  26.886  1.00 190.19 ?  170  GLU A O   1 
ATOM   1089 C  CB  . GLU A 1 171 ? 21.807  46.152  30.113  1.00 171.38 ?  170  GLU A CB  1 
ATOM   1090 C  CG  . GLU A 1 171 ? 20.298  46.383  30.079  1.00 183.92 ?  170  GLU A CG  1 
ATOM   1091 C  CD  . GLU A 1 171 ? 19.621  45.998  31.385  1.00 191.21 ?  170  GLU A CD  1 
ATOM   1092 O  OE1 . GLU A 1 171 ? 20.148  45.111  32.090  1.00 186.81 ?  170  GLU A OE1 1 
ATOM   1093 O  OE2 . GLU A 1 171 ? 18.558  46.572  31.703  1.00 198.35 ?  170  GLU A OE2 1 
ATOM   1094 N  N   . HIS A 1 172 ? 23.382  47.648  27.779  1.00 149.75 ?  171  HIS A N   1 
ATOM   1095 C  CA  . HIS A 1 172 ? 23.513  48.694  26.766  1.00 136.93 ?  171  HIS A CA  1 
ATOM   1096 C  C   . HIS A 1 172 ? 23.973  48.113  25.431  1.00 123.85 ?  171  HIS A C   1 
ATOM   1097 O  O   . HIS A 1 172 ? 23.539  48.550  24.367  1.00 137.88 ?  171  HIS A O   1 
ATOM   1098 C  CB  . HIS A 1 172 ? 24.494  49.776  27.218  1.00 136.55 ?  171  HIS A CB  1 
ATOM   1099 C  CG  . HIS A 1 172 ? 23.833  51.037  27.681  1.00 146.51 ?  171  HIS A CG  1 
ATOM   1100 N  ND1 . HIS A 1 172 ? 23.386  51.212  28.972  1.00 154.45 ?  171  HIS A ND1 1 
ATOM   1101 C  CD2 . HIS A 1 172 ? 23.540  52.182  27.022  1.00 152.35 ?  171  HIS A CD2 1 
ATOM   1102 C  CE1 . HIS A 1 172 ? 22.847  52.413  29.090  1.00 163.47 ?  171  HIS A CE1 1 
ATOM   1103 N  NE2 . HIS A 1 172 ? 22.928  53.022  27.920  1.00 163.51 ?  171  HIS A NE2 1 
ATOM   1104 N  N   . MET A 1 173 ? 24.858  47.125  25.505  1.00 118.32 ?  172  MET A N   1 
ATOM   1105 C  CA  . MET A 1 173 ? 25.354  46.427  24.325  1.00 112.10 ?  172  MET A CA  1 
ATOM   1106 C  C   . MET A 1 173 ? 24.242  45.755  23.534  1.00 141.67 ?  172  MET A C   1 
ATOM   1107 O  O   . MET A 1 173 ? 24.234  45.800  22.309  1.00 141.98 ?  172  MET A O   1 
ATOM   1108 C  CB  . MET A 1 173 ? 26.396  45.391  24.726  1.00 107.23 ?  172  MET A CB  1 
ATOM   1109 C  CG  . MET A 1 173 ? 27.656  45.995  25.309  1.00 98.53  ?  172  MET A CG  1 
ATOM   1110 S  SD  . MET A 1 173 ? 28.898  44.761  25.692  1.00 135.03 ?  172  MET A SD  1 
ATOM   1111 C  CE  . MET A 1 173 ? 29.534  44.427  24.057  1.00 70.49  ?  172  MET A CE  1 
ATOM   1112 N  N   . GLU A 1 174 ? 23.339  45.081  24.234  1.00 167.61 ?  173  GLU A N   1 
ATOM   1113 C  CA  . GLU A 1 174 ? 22.205  44.427  23.593  1.00 169.65 ?  173  GLU A CA  1 
ATOM   1114 C  C   . GLU A 1 174 ? 21.259  45.468  22.984  1.00 156.46 ?  173  GLU A C   1 
ATOM   1115 O  O   . GLU A 1 174 ? 20.722  45.278  21.894  1.00 160.29 ?  173  GLU A O   1 
ATOM   1116 C  CB  . GLU A 1 174 ? 21.481  43.518  24.602  1.00 181.95 ?  173  GLU A CB  1 
ATOM   1117 C  CG  . GLU A 1 174 ? 20.204  44.082  25.220  1.00 196.46 ?  173  GLU A CG  1 
ATOM   1118 C  CD  . GLU A 1 174 ? 20.011  43.641  26.656  1.00 203.07 ?  173  GLU A CD  1 
ATOM   1119 O  OE1 . GLU A 1 174 ? 20.778  42.768  27.117  1.00 202.80 ?  173  GLU A OE1 1 
ATOM   1120 O  OE2 . GLU A 1 174 ? 19.091  44.164  27.321  1.00 204.67 ?  173  GLU A OE2 1 
ATOM   1121 N  N   . ALA A 1 175 ? 21.097  46.580  23.693  1.00 137.63 ?  174  ALA A N   1 
ATOM   1122 C  CA  . ALA A 1 175 ? 20.190  47.660  23.311  1.00 145.69 ?  174  ALA A CA  1 
ATOM   1123 C  C   . ALA A 1 175 ? 20.529  48.419  22.027  1.00 159.62 ?  174  ALA A C   1 
ATOM   1124 O  O   . ALA A 1 175 ? 19.632  48.759  21.256  1.00 162.38 ?  174  ALA A O   1 
ATOM   1125 C  CB  . ALA A 1 175 ? 20.084  48.650  24.460  1.00 146.94 ?  174  ALA A CB  1 
ATOM   1126 N  N   . ALA A 1 176 ? 21.811  48.689  21.799  1.00 166.57 ?  175  ALA A N   1 
ATOM   1127 C  CA  . ALA A 1 176 ? 22.231  49.511  20.654  1.00 168.74 ?  175  ALA A CA  1 
ATOM   1128 C  C   . ALA A 1 176 ? 21.981  48.941  19.234  1.00 166.59 ?  175  ALA A C   1 
ATOM   1129 O  O   . ALA A 1 176 ? 21.397  49.652  18.415  1.00 176.37 ?  175  ALA A O   1 
ATOM   1130 C  CB  . ALA A 1 176 ? 23.720  49.885  20.810  1.00 164.31 ?  175  ALA A CB  1 
ATOM   1131 N  N   . GLY A 1 177 ? 22.387  47.709  18.909  1.00 140.66 ?  176  GLY A N   1 
ATOM   1132 C  CA  . GLY A 1 177 ? 23.055  46.790  19.806  1.00 133.24 ?  176  GLY A CA  1 
ATOM   1133 C  C   . GLY A 1 177 ? 23.680  45.581  19.142  1.00 134.73 ?  176  GLY A C   1 
ATOM   1134 O  O   . GLY A 1 177 ? 23.011  44.833  18.435  1.00 133.27 ?  176  GLY A O   1 
ATOM   1135 N  N   . ILE A 1 178 ? 24.977  45.401  19.358  1.00 135.61 ?  177  ILE A N   1 
ATOM   1136 C  CA  . ILE A 1 178 ? 25.694  44.254  18.812  1.00 148.82 ?  177  ILE A CA  1 
ATOM   1137 C  C   . ILE A 1 178 ? 25.648  43.132  19.840  1.00 140.86 ?  177  ILE A C   1 
ATOM   1138 O  O   . ILE A 1 178 ? 25.833  43.365  21.036  1.00 129.71 ?  177  ILE A O   1 
ATOM   1139 C  CB  . ILE A 1 178 ? 27.151  44.582  18.430  1.00 166.52 ?  177  ILE A CB  1 
ATOM   1140 C  CG1 . ILE A 1 178 ? 27.180  45.667  17.350  1.00 180.36 ?  177  ILE A CG1 1 
ATOM   1141 C  CG2 . ILE A 1 178 ? 27.867  43.331  17.926  1.00 167.44 ?  177  ILE A CG2 1 
ATOM   1142 C  CD1 . ILE A 1 178 ? 28.497  45.770  16.598  1.00 183.52 ?  177  ILE A CD1 1 
ATOM   1143 N  N   . ALA A 1 179 ? 25.400  41.913  19.373  1.00 146.67 ?  178  ALA A N   1 
ATOM   1144 C  CA  . ALA A 1 179 ? 25.413  40.759  20.258  1.00 142.00 ?  178  ALA A CA  1 
ATOM   1145 C  C   . ALA A 1 179 ? 26.847  40.332  20.523  1.00 123.83 ?  178  ALA A C   1 
ATOM   1146 O  O   . ALA A 1 179 ? 27.757  40.651  19.757  1.00 118.23 ?  178  ALA A O   1 
ATOM   1147 C  CB  . ALA A 1 179 ? 24.612  39.608  19.655  1.00 158.81 ?  178  ALA A CB  1 
ATOM   1148 N  N   . LEU A 1 180 ? 27.025  39.565  21.592  1.00 114.76 ?  179  LEU A N   1 
ATOM   1149 C  CA  . LEU A 1 180 ? 28.342  39.302  22.152  1.00 98.43  ?  179  LEU A CA  1 
ATOM   1150 C  C   . LEU A 1 180 ? 29.101  38.184  21.456  1.00 97.88  ?  179  LEU A C   1 
ATOM   1151 O  O   . LEU A 1 180 ? 28.542  37.137  21.139  1.00 120.24 ?  179  LEU A O   1 
ATOM   1152 C  CB  . LEU A 1 180 ? 28.198  38.946  23.630  1.00 98.21  ?  179  LEU A CB  1 
ATOM   1153 C  CG  . LEU A 1 180 ? 27.501  39.965  24.531  1.00 108.90 ?  179  LEU A CG  1 
ATOM   1154 C  CD1 . LEU A 1 180 ? 27.109  39.313  25.844  1.00 114.82 ?  179  LEU A CD1 1 
ATOM   1155 C  CD2 . LEU A 1 180 ? 28.376  41.177  24.771  1.00 113.67 ?  179  LEU A CD2 1 
ATOM   1156 N  N   . GLU A 1 181 ? 30.381  38.429  21.203  1.00 96.87  ?  180  GLU A N   1 
ATOM   1157 C  CA  . GLU A 1 181 ? 31.270  37.387  20.716  1.00 111.71 ?  180  GLU A CA  1 
ATOM   1158 C  C   . GLU A 1 181 ? 31.736  36.580  21.928  1.00 101.65 ?  180  GLU A C   1 
ATOM   1159 O  O   . GLU A 1 181 ? 31.415  36.934  23.058  1.00 94.66  ?  180  GLU A O   1 
ATOM   1160 C  CB  . GLU A 1 181 ? 32.441  37.981  19.930  1.00 130.31 ?  180  GLU A CB  1 
ATOM   1161 C  CG  . GLU A 1 181 ? 32.132  38.153  18.438  1.00 140.42 ?  180  GLU A CG  1 
ATOM   1162 C  CD  . GLU A 1 181 ? 33.258  38.817  17.663  1.00 150.75 ?  180  GLU A CD  1 
ATOM   1163 O  OE1 . GLU A 1 181 ? 34.437  38.630  18.039  1.00 166.29 ?  180  GLU A OE1 1 
ATOM   1164 O  OE2 . GLU A 1 181 ? 32.961  39.510  16.664  1.00 151.44 ?  180  GLU A OE2 1 
ATOM   1165 N  N   . GLU A 1 182 ? 32.459  35.488  21.698  1.00 108.18 ?  181  GLU A N   1 
ATOM   1166 C  CA  . GLU A 1 182 ? 32.808  34.544  22.768  1.00 109.05 ?  181  GLU A CA  1 
ATOM   1167 C  C   . GLU A 1 182 ? 33.580  35.180  23.922  1.00 105.77 ?  181  GLU A C   1 
ATOM   1168 O  O   . GLU A 1 182 ? 33.237  34.979  25.086  1.00 116.16 ?  181  GLU A O   1 
ATOM   1169 C  CB  . GLU A 1 182 ? 33.616  33.373  22.199  1.00 119.55 ?  181  GLU A CB  1 
ATOM   1170 C  CG  . GLU A 1 182 ? 34.131  32.402  23.253  1.00 114.51 ?  181  GLU A CG  1 
ATOM   1171 C  CD  . GLU A 1 182 ? 35.495  31.838  22.919  1.00 115.16 ?  181  GLU A CD  1 
ATOM   1172 O  OE1 . GLU A 1 182 ? 36.000  32.093  21.804  1.00 107.40 ?  181  GLU A OE1 1 
ATOM   1173 O  OE2 . GLU A 1 182 ? 36.068  31.145  23.782  1.00 127.12 ?  181  GLU A OE2 1 
ATOM   1174 N  N   . ALA A 1 183 ? 34.629  35.926  23.590  1.00 101.24 ?  182  ALA A N   1 
ATOM   1175 C  CA  . ALA A 1 183 ? 35.491  36.565  24.585  1.00 98.51  ?  182  ALA A CA  1 
ATOM   1176 C  C   . ALA A 1 183 ? 34.719  37.357  25.637  1.00 81.00  ?  182  ALA A C   1 
ATOM   1177 O  O   . ALA A 1 183 ? 35.044  37.312  26.823  1.00 73.10  ?  182  ALA A O   1 
ATOM   1178 C  CB  . ALA A 1 183 ? 36.492  37.469  23.894  1.00 99.17  ?  182  ALA A CB  1 
ATOM   1179 N  N   . GLU A 1 184 ? 33.709  38.096  25.194  1.00 80.39  ?  183  GLU A N   1 
ATOM   1180 C  CA  . GLU A 1 184 ? 32.916  38.918  26.100  1.00 91.00  ?  183  GLU A CA  1 
ATOM   1181 C  C   . GLU A 1 184 ? 32.044  38.058  27.010  1.00 100.36 ?  183  GLU A C   1 
ATOM   1182 O  O   . GLU A 1 184 ? 31.918  38.344  28.199  1.00 111.64 ?  183  GLU A O   1 
ATOM   1183 C  CB  . GLU A 1 184 ? 32.058  39.913  25.315  1.00 94.24  ?  183  GLU A CB  1 
ATOM   1184 C  CG  . GLU A 1 184 ? 32.846  41.045  24.643  1.00 113.64 ?  183  GLU A CG  1 
ATOM   1185 C  CD  . GLU A 1 184 ? 33.501  40.614  23.337  1.00 129.93 ?  183  GLU A CD  1 
ATOM   1186 O  OE1 . GLU A 1 184 ? 32.892  39.796  22.621  1.00 153.77 ?  183  GLU A OE1 1 
ATOM   1187 O  OE2 . GLU A 1 184 ? 34.609  41.102  23.013  1.00 116.82 ?  183  GLU A OE2 1 
ATOM   1188 N  N   . ILE A 1 185 ? 31.439  37.009  26.461  1.00 94.96  ?  184  ILE A N   1 
ATOM   1189 C  CA  . ILE A 1 185 ? 30.596  36.138  27.278  1.00 100.98 ?  184  ILE A CA  1 
ATOM   1190 C  C   . ILE A 1 185 ? 31.398  35.358  28.314  1.00 107.12 ?  184  ILE A C   1 
ATOM   1191 O  O   . ILE A 1 185 ? 30.985  35.239  29.465  1.00 119.86 ?  184  ILE A O   1 
ATOM   1192 C  CB  . ILE A 1 185 ? 29.813  35.130  26.416  1.00 115.30 ?  184  ILE A CB  1 
ATOM   1193 C  CG1 . ILE A 1 185 ? 29.296  35.800  25.141  1.00 119.22 ?  184  ILE A CG1 1 
ATOM   1194 C  CG2 . ILE A 1 185 ? 28.675  34.506  27.221  1.00 123.53 ?  184  ILE A CG2 1 
ATOM   1195 C  CD1 . ILE A 1 185 ? 28.254  34.985  24.395  1.00 113.73 ?  184  ILE A CD1 1 
ATOM   1196 N  N   . SER A 1 186 ? 32.555  34.847  27.906  1.00 100.94 ?  185  SER A N   1 
ATOM   1197 C  CA  . SER A 1 186 ? 33.405  34.064  28.799  1.00 97.86  ?  185  SER A CA  1 
ATOM   1198 C  C   . SER A 1 186 ? 33.893  34.917  29.970  1.00 102.86 ?  185  SER A C   1 
ATOM   1199 O  O   . SER A 1 186 ? 33.933  34.453  31.111  1.00 104.94 ?  185  SER A O   1 
ATOM   1200 C  CB  . SER A 1 186 ? 34.582  33.455  28.025  1.00 94.16  ?  185  SER A CB  1 
ATOM   1201 O  OG  . SER A 1 186 ? 35.599  34.404  27.760  1.00 105.33 ?  185  SER A OG  1 
ATOM   1202 N  N   . ALA A 1 187 ? 34.253  36.166  29.682  1.00 95.55  ?  186  ALA A N   1 
ATOM   1203 C  CA  . ALA A 1 187 ? 34.676  37.107  30.712  1.00 81.94  ?  186  ALA A CA  1 
ATOM   1204 C  C   . ALA A 1 187 ? 33.527  37.390  31.678  1.00 92.62  ?  186  ALA A C   1 
ATOM   1205 O  O   . ALA A 1 187 ? 33.727  37.502  32.888  1.00 113.90 ?  186  ALA A O   1 
ATOM   1206 C  CB  . ALA A 1 187 ? 35.178  38.402  30.080  1.00 70.10  ?  186  ALA A CB  1 
ATOM   1207 N  N   . LEU A 1 188 ? 32.328  37.521  31.120  1.00 83.15  ?  187  LEU A N   1 
ATOM   1208 C  CA  . LEU A 1 188 ? 31.104  37.701  31.893  1.00 86.70  ?  187  LEU A CA  1 
ATOM   1209 C  C   . LEU A 1 188 ? 30.782  36.472  32.729  1.00 90.12  ?  187  LEU A C   1 
ATOM   1210 O  O   . LEU A 1 188 ? 30.254  36.582  33.836  1.00 103.45 ?  187  LEU A O   1 
ATOM   1211 C  CB  . LEU A 1 188 ? 29.941  38.017  30.960  1.00 101.65 ?  187  LEU A CB  1 
ATOM   1212 C  CG  . LEU A 1 188 ? 29.864  39.472  30.513  1.00 109.76 ?  187  LEU A CG  1 
ATOM   1213 C  CD1 . LEU A 1 188 ? 28.736  39.666  29.517  1.00 110.21 ?  187  LEU A CD1 1 
ATOM   1214 C  CD2 . LEU A 1 188 ? 29.668  40.359  31.732  1.00 118.11 ?  187  LEU A CD2 1 
ATOM   1215 N  N   . LEU A 1 189 ? 31.066  35.299  32.175  1.00 89.79  ?  188  LEU A N   1 
ATOM   1216 C  CA  . LEU A 1 189 ? 30.876  34.049  32.899  1.00 102.72 ?  188  LEU A CA  1 
ATOM   1217 C  C   . LEU A 1 189 ? 31.819  33.962  34.093  1.00 115.67 ?  188  LEU A C   1 
ATOM   1218 O  O   . LEU A 1 189 ? 31.411  33.571  35.186  1.00 124.38 ?  188  LEU A O   1 
ATOM   1219 C  CB  . LEU A 1 189 ? 31.091  32.852  31.971  1.00 93.23  ?  188  LEU A CB  1 
ATOM   1220 C  CG  . LEU A 1 189 ? 30.940  31.467  32.603  1.00 79.02  ?  188  LEU A CG  1 
ATOM   1221 C  CD1 . LEU A 1 189 ? 29.489  31.036  32.551  1.00 78.84  ?  188  LEU A CD1 1 
ATOM   1222 C  CD2 . LEU A 1 189 ? 31.833  30.448  31.915  1.00 62.80  ?  188  LEU A CD2 1 
ATOM   1223 N  N   . LYS A 1 190 ? 33.072  34.355  33.876  1.00 113.54 ?  189  LYS A N   1 
ATOM   1224 C  CA  . LYS A 1 190 ? 34.110  34.307  34.909  1.00 103.48 ?  189  LYS A CA  1 
ATOM   1225 C  C   . LYS A 1 190 ? 33.709  35.072  36.168  1.00 103.45 ?  189  LYS A C   1 
ATOM   1226 O  O   . LYS A 1 190 ? 33.860  34.572  37.281  1.00 112.87 ?  189  LYS A O   1 
ATOM   1227 C  CB  . LYS A 1 190 ? 35.425  34.871  34.361  1.00 85.95  ?  189  LYS A CB  1 
ATOM   1228 C  CG  . LYS A 1 190 ? 36.506  35.073  35.397  1.00 75.56  ?  189  LYS A CG  1 
ATOM   1229 C  CD  . LYS A 1 190 ? 37.727  35.764  34.803  1.00 92.05  ?  189  LYS A CD  1 
ATOM   1230 C  CE  . LYS A 1 190 ? 38.769  34.762  34.326  1.00 97.14  ?  189  LYS A CE  1 
ATOM   1231 N  NZ  . LYS A 1 190 ? 40.088  35.416  34.075  1.00 94.43  ?  189  LYS A NZ  1 
ATOM   1232 N  N   . VAL A 1 191 ? 33.163  36.267  35.978  1.00 100.89 ?  190  VAL A N   1 
ATOM   1233 C  CA  . VAL A 1 191 ? 32.801  37.134  37.090  1.00 101.00 ?  190  VAL A CA  1 
ATOM   1234 C  C   . VAL A 1 191 ? 31.654  36.553  37.904  1.00 109.59 ?  190  VAL A C   1 
ATOM   1235 O  O   . VAL A 1 191 ? 31.697  36.546  39.136  1.00 124.54 ?  190  VAL A O   1 
ATOM   1236 C  CB  . VAL A 1 191 ? 32.412  38.529  36.589  1.00 91.78  ?  190  VAL A CB  1 
ATOM   1237 C  CG1 . VAL A 1 191 ? 31.940  39.404  37.747  1.00 84.65  ?  190  VAL A CG1 1 
ATOM   1238 C  CG2 . VAL A 1 191 ? 33.591  39.156  35.895  1.00 92.86  ?  190  VAL A CG2 1 
ATOM   1239 N  N   . SER A 1 192 ? 30.630  36.065  37.212  1.00 102.50 ?  191  SER A N   1 
ATOM   1240 C  CA  . SER A 1 192 ? 29.482  35.464  37.877  1.00 105.93 ?  191  SER A CA  1 
ATOM   1241 C  C   . SER A 1 192 ? 29.935  34.275  38.717  1.00 101.71 ?  191  SER A C   1 
ATOM   1242 O  O   . SER A 1 192 ? 29.400  34.025  39.798  1.00 79.09  ?  191  SER A O   1 
ATOM   1243 C  CB  . SER A 1 192 ? 28.425  35.037  36.857  1.00 97.04  ?  191  SER A CB  1 
ATOM   1244 O  OG  . SER A 1 192 ? 27.719  36.157  36.354  1.00 96.26  ?  191  SER A OG  1 
ATOM   1245 N  N   . ALA A 1 193 ? 30.938  33.559  38.215  1.00 93.55  ?  192  ALA A N   1 
ATOM   1246 C  CA  . ALA A 1 193 ? 31.532  32.438  38.932  1.00 89.79  ?  192  ALA A CA  1 
ATOM   1247 C  C   . ALA A 1 193 ? 32.267  32.892  40.180  1.00 91.60  ?  192  ALA A C   1 
ATOM   1248 O  O   . ALA A 1 193 ? 32.097  32.308  41.249  1.00 101.69 ?  192  ALA A O   1 
ATOM   1249 C  CB  . ALA A 1 193 ? 32.480  31.674  38.019  1.00 89.88  ?  192  ALA A CB  1 
ATOM   1250 N  N   . ALA A 1 194 ? 33.086  33.930  40.034  1.00 91.75  ?  193  ALA A N   1 
ATOM   1251 C  CA  . ALA A 1 194 ? 33.878  34.466  41.140  1.00 97.75  ?  193  ALA A CA  1 
ATOM   1252 C  C   . ALA A 1 194 ? 33.004  35.117  42.213  1.00 89.78  ?  193  ALA A C   1 
ATOM   1253 O  O   . ALA A 1 194 ? 33.260  34.965  43.409  1.00 104.85 ?  193  ALA A O   1 
ATOM   1254 C  CB  . ALA A 1 194 ? 34.902  35.457  40.622  1.00 78.07  ?  193  ALA A CB  1 
ATOM   1255 N  N   . THR A 1 195 ? 31.976  35.844  41.782  1.00 82.75  ?  194  THR A N   1 
ATOM   1256 C  CA  . THR A 1 195 ? 31.029  36.454  42.712  1.00 94.22  ?  194  THR A CA  1 
ATOM   1257 C  C   . THR A 1 195 ? 30.013  35.428  43.220  1.00 96.53  ?  194  THR A C   1 
ATOM   1258 O  O   . THR A 1 195 ? 29.146  35.760  44.026  1.00 116.35 ?  194  THR A O   1 
ATOM   1259 C  CB  . THR A 1 195 ? 30.278  37.645  42.079  1.00 102.21 ?  194  THR A CB  1 
ATOM   1260 O  OG1 . THR A 1 195 ? 29.595  37.213  40.898  1.00 113.97 ?  194  THR A OG1 1 
ATOM   1261 C  CG2 . THR A 1 195 ? 31.247  38.758  41.724  1.00 85.01  ?  194  THR A CG2 1 
ATOM   1262 N  N   . GLY A 1 196 ? 30.129  34.188  42.747  1.00 86.33  ?  195  GLY A N   1 
ATOM   1263 C  CA  . GLY A 1 196 ? 29.248  33.113  43.170  1.00 99.53  ?  195  GLY A CA  1 
ATOM   1264 C  C   . GLY A 1 196 ? 27.778  33.313  42.842  1.00 118.88 ?  195  GLY A C   1 
ATOM   1265 O  O   . GLY A 1 196 ? 26.906  32.950  43.633  1.00 133.84 ?  195  GLY A O   1 
ATOM   1266 N  N   . ARG A 1 197 ? 27.495  33.875  41.669  1.00 122.20 ?  196  ARG A N   1 
ATOM   1267 C  CA  . ARG A 1 197 ? 26.113  34.006  41.212  1.00 120.96 ?  196  ARG A CA  1 
ATOM   1268 C  C   . ARG A 1 197 ? 25.676  32.765  40.438  1.00 119.66 ?  196  ARG A C   1 
ATOM   1269 O  O   . ARG A 1 197 ? 26.111  32.543  39.310  1.00 119.40 ?  196  ARG A O   1 
ATOM   1270 C  CB  . ARG A 1 197 ? 25.960  35.239  40.316  1.00 113.32 ?  196  ARG A CB  1 
ATOM   1271 C  CG  . ARG A 1 197 ? 26.278  36.568  40.988  1.00 106.33 ?  196  ARG A CG  1 
ATOM   1272 C  CD  . ARG A 1 197 ? 25.324  36.886  42.119  1.00 126.00 ?  196  ARG A CD  1 
ATOM   1273 N  NE  . ARG A 1 197 ? 23.942  36.995  41.665  1.00 133.48 ?  196  ARG A NE  1 
ATOM   1274 C  CZ  . ARG A 1 197 ? 23.420  38.086  41.110  1.00 139.43 ?  196  ARG A CZ  1 
ATOM   1275 N  NH1 . ARG A 1 197 ? 24.164  39.172  40.937  1.00 135.88 ?  196  ARG A NH1 1 
ATOM   1276 N  NH2 . ARG A 1 197 ? 22.151  38.093  40.726  1.00 145.94 ?  196  ARG A NH2 1 
ATOM   1277 N  N   . GLU A 1 198 ? 24.824  31.951  41.056  1.00 125.87 ?  197  GLU A N   1 
ATOM   1278 C  CA  . GLU A 1 198 ? 24.443  30.666  40.474  1.00 134.36 ?  197  GLU A CA  1 
ATOM   1279 C  C   . GLU A 1 198 ? 23.616  30.850  39.195  1.00 141.74 ?  197  GLU A C   1 
ATOM   1280 O  O   . GLU A 1 198 ? 23.935  30.273  38.157  1.00 146.59 ?  197  GLU A O   1 
ATOM   1281 C  CB  . GLU A 1 198 ? 23.695  29.767  41.477  1.00 145.75 ?  197  GLU A CB  1 
ATOM   1282 C  CG  . GLU A 1 198 ? 22.415  30.350  42.094  1.00 155.82 ?  197  GLU A CG  1 
ATOM   1283 C  CD  . GLU A 1 198 ? 22.672  31.349  43.216  1.00 159.37 ?  197  GLU A CD  1 
ATOM   1284 O  OE1 . GLU A 1 198 ? 23.660  32.110  43.145  1.00 156.29 ?  197  GLU A OE1 1 
ATOM   1285 O  OE2 . GLU A 1 198 ? 21.868  31.378  44.172  1.00 165.18 ?  197  GLU A OE2 1 
ATOM   1286 N  N   . ASN A 1 199 ? 22.558  31.653  39.275  1.00 137.12 ?  198  ASN A N   1 
ATOM   1287 C  CA  . ASN A 1 199 ? 21.634  31.829  38.160  1.00 125.44 ?  198  ASN A CA  1 
ATOM   1288 C  C   . ASN A 1 199 ? 22.276  32.510  36.961  1.00 130.29 ?  198  ASN A C   1 
ATOM   1289 O  O   . ASN A 1 199 ? 21.956  32.204  35.814  1.00 145.23 ?  198  ASN A O   1 
ATOM   1290 C  CB  . ASN A 1 199 ? 20.409  32.623  38.607  1.00 134.06 ?  198  ASN A CB  1 
ATOM   1291 C  CG  . ASN A 1 199 ? 19.486  31.813  39.492  1.00 160.55 ?  198  ASN A CG  1 
ATOM   1292 O  OD1 . ASN A 1 199 ? 19.788  30.672  39.845  1.00 164.42 ?  198  ASN A OD1 1 
ATOM   1293 N  ND2 . ASN A 1 199 ? 18.354  32.400  39.859  1.00 179.32 ?  198  ASN A ND2 1 
ATOM   1294 N  N   . LYS A 1 200 ? 23.175  33.447  37.233  1.00 120.31 ?  199  LYS A N   1 
ATOM   1295 C  CA  . LYS A 1 200 ? 23.876  34.145  36.167  1.00 113.26 ?  199  LYS A CA  1 
ATOM   1296 C  C   . LYS A 1 200 ? 24.836  33.239  35.395  1.00 104.60 ?  199  LYS A C   1 
ATOM   1297 O  O   . LYS A 1 200 ? 24.945  33.354  34.177  1.00 110.88 ?  199  LYS A O   1 
ATOM   1298 C  CB  . LYS A 1 200 ? 24.626  35.351  36.728  1.00 114.52 ?  199  LYS A CB  1 
ATOM   1299 C  CG  . LYS A 1 200 ? 24.215  36.664  36.086  1.00 111.74 ?  199  LYS A CG  1 
ATOM   1300 C  CD  . LYS A 1 200 ? 22.722  36.923  36.202  1.00 113.72 ?  199  LYS A CD  1 
ATOM   1301 C  CE  . LYS A 1 200 ? 22.342  38.181  35.431  1.00 111.19 ?  199  LYS A CE  1 
ATOM   1302 N  NZ  . LYS A 1 200 ? 20.920  38.578  35.628  1.00 112.52 ?  199  LYS A NZ  1 
ATOM   1303 N  N   . VAL A 1 201 ? 25.526  32.341  36.092  1.00 94.35  ?  200  VAL A N   1 
ATOM   1304 C  CA  . VAL A 1 201 ? 26.394  31.379  35.416  1.00 93.21  ?  200  VAL A CA  1 
ATOM   1305 C  C   . VAL A 1 201 ? 25.562  30.477  34.508  1.00 94.47  ?  200  VAL A C   1 
ATOM   1306 O  O   . VAL A 1 201 ? 25.983  30.132  33.402  1.00 85.12  ?  200  VAL A O   1 
ATOM   1307 C  CB  . VAL A 1 201 ? 27.194  30.511  36.419  1.00 87.03  ?  200  VAL A CB  1 
ATOM   1308 C  CG1 . VAL A 1 201 ? 27.984  29.436  35.696  1.00 81.13  ?  200  VAL A CG1 1 
ATOM   1309 C  CG2 . VAL A 1 201 ? 28.121  31.370  37.250  1.00 74.09  ?  200  VAL A CG2 1 
ATOM   1310 N  N   . TYR A 1 202 ? 24.366  30.128  34.970  1.00 102.96 ?  201  TYR A N   1 
ATOM   1311 C  CA  . TYR A 1 202 ? 23.455  29.299  34.190  1.00 106.99 ?  201  TYR A CA  1 
ATOM   1312 C  C   . TYR A 1 202 ? 23.077  30.025  32.905  1.00 115.25 ?  201  TYR A C   1 
ATOM   1313 O  O   . TYR A 1 202 ? 23.190  29.462  31.817  1.00 129.79 ?  201  TYR A O   1 
ATOM   1314 C  CB  . TYR A 1 202 ? 22.207  28.954  35.008  1.00 105.78 ?  201  TYR A CB  1 
ATOM   1315 C  CG  . TYR A 1 202 ? 21.219  28.033  34.319  1.00 111.38 ?  201  TYR A CG  1 
ATOM   1316 C  CD1 . TYR A 1 202 ? 21.522  26.695  34.088  1.00 100.48 ?  201  TYR A CD1 1 
ATOM   1317 C  CD2 . TYR A 1 202 ? 19.969  28.498  33.924  1.00 124.46 ?  201  TYR A CD2 1 
ATOM   1318 C  CE1 . TYR A 1 202 ? 20.612  25.851  33.464  1.00 103.20 ?  201  TYR A CE1 1 
ATOM   1319 C  CE2 . TYR A 1 202 ? 19.055  27.662  33.301  1.00 119.94 ?  201  TYR A CE2 1 
ATOM   1320 C  CZ  . TYR A 1 202 ? 19.381  26.341  33.074  1.00 112.19 ?  201  TYR A CZ  1 
ATOM   1321 O  OH  . TYR A 1 202 ? 18.467  25.515  32.457  1.00 111.47 ?  201  TYR A OH  1 
ATOM   1322 N  N   . ARG A 1 203 ? 22.668  31.286  33.031  1.00 105.06 ?  202  ARG A N   1 
ATOM   1323 C  CA  . ARG A 1 203 ? 22.268  32.086  31.874  1.00 96.66  ?  202  ARG A CA  1 
ATOM   1324 C  C   . ARG A 1 203 ? 23.393  32.228  30.855  1.00 87.26  ?  202  ARG A C   1 
ATOM   1325 O  O   . ARG A 1 203 ? 23.183  32.048  29.655  1.00 103.42 ?  202  ARG A O   1 
ATOM   1326 C  CB  . ARG A 1 203 ? 21.816  33.478  32.318  1.00 97.24  ?  202  ARG A CB  1 
ATOM   1327 C  CG  . ARG A 1 203 ? 21.524  34.433  31.173  1.00 99.57  ?  202  ARG A CG  1 
ATOM   1328 C  CD  . ARG A 1 203 ? 21.082  35.795  31.683  1.00 114.60 ?  202  ARG A CD  1 
ATOM   1329 N  NE  . ARG A 1 203 ? 19.925  35.708  32.570  1.00 142.06 ?  202  ARG A NE  1 
ATOM   1330 C  CZ  . ARG A 1 203 ? 18.683  36.029  32.216  1.00 151.34 ?  202  ARG A CZ  1 
ATOM   1331 N  NH1 . ARG A 1 203 ? 18.434  36.468  30.989  1.00 154.40 ?  202  ARG A NH1 1 
ATOM   1332 N  NH2 . ARG A 1 203 ? 17.691  35.918  33.090  1.00 144.63 ?  202  ARG A NH2 1 
ATOM   1333 N  N   . TYR A 1 204 ? 24.586  32.551  31.342  1.00 74.07  ?  203  TYR A N   1 
ATOM   1334 C  CA  . TYR A 1 204 ? 25.732  32.790  30.470  1.00 80.67  ?  203  TYR A CA  1 
ATOM   1335 C  C   . TYR A 1 204 ? 26.295  31.505  29.865  1.00 80.79  ?  203  TYR A C   1 
ATOM   1336 O  O   . TYR A 1 204 ? 26.921  31.543  28.806  1.00 101.98 ?  203  TYR A O   1 
ATOM   1337 C  CB  . TYR A 1 204 ? 26.827  33.567  31.207  1.00 95.80  ?  203  TYR A CB  1 
ATOM   1338 C  CG  . TYR A 1 204 ? 26.423  34.999  31.490  1.00 104.42 ?  203  TYR A CG  1 
ATOM   1339 C  CD1 . TYR A 1 204 ? 25.273  35.536  30.920  1.00 116.00 ?  203  TYR A CD1 1 
ATOM   1340 C  CD2 . TYR A 1 204 ? 27.199  35.821  32.294  1.00 94.76  ?  203  TYR A CD2 1 
ATOM   1341 C  CE1 . TYR A 1 204 ? 24.891  36.836  31.168  1.00 115.97 ?  203  TYR A CE1 1 
ATOM   1342 C  CE2 . TYR A 1 204 ? 26.827  37.126  32.541  1.00 107.04 ?  203  TYR A CE2 1 
ATOM   1343 C  CZ  . TYR A 1 204 ? 25.671  37.626  31.973  1.00 120.93 ?  203  TYR A CZ  1 
ATOM   1344 O  OH  . TYR A 1 204 ? 25.286  38.924  32.209  1.00 145.00 ?  203  TYR A OH  1 
ATOM   1345 N  N   . LEU A 1 205 ? 26.121  30.377  30.544  1.00 69.17  ?  204  LEU A N   1 
ATOM   1346 C  CA  . LEU A 1 205 ? 26.486  29.104  29.927  1.00 82.97  ?  204  LEU A CA  1 
ATOM   1347 C  C   . LEU A 1 205 ? 25.567  28.815  28.742  1.00 90.02  ?  204  LEU A C   1 
ATOM   1348 O  O   . LEU A 1 205 ? 26.007  28.301  27.716  1.00 87.24  ?  204  LEU A O   1 
ATOM   1349 C  CB  . LEU A 1 205 ? 26.435  27.953  30.929  1.00 87.03  ?  204  LEU A CB  1 
ATOM   1350 C  CG  . LEU A 1 205 ? 27.617  27.832  31.890  1.00 94.16  ?  204  LEU A CG  1 
ATOM   1351 C  CD1 . LEU A 1 205 ? 27.371  26.705  32.881  1.00 97.26  ?  204  LEU A CD1 1 
ATOM   1352 C  CD2 . LEU A 1 205 ? 28.924  27.626  31.128  1.00 85.33  ?  204  LEU A CD2 1 
ATOM   1353 N  N   . HIS A 1 206 ? 24.287  29.142  28.895  1.00 95.04  ?  205  HIS A N   1 
ATOM   1354 C  CA  . HIS A 1 206 ? 23.326  29.018  27.803  1.00 91.53  ?  205  HIS A CA  1 
ATOM   1355 C  C   . HIS A 1 206 ? 23.605  30.039  26.719  1.00 104.37 ?  205  HIS A C   1 
ATOM   1356 O  O   . HIS A 1 206 ? 23.419  29.769  25.534  1.00 122.98 ?  205  HIS A O   1 
ATOM   1357 C  CB  . HIS A 1 206 ? 21.895  29.184  28.303  1.00 91.99  ?  205  HIS A CB  1 
ATOM   1358 C  CG  . HIS A 1 206 ? 21.308  27.932  28.868  1.00 99.73  ?  205  HIS A CG  1 
ATOM   1359 N  ND1 . HIS A 1 206 ? 21.957  26.717  28.812  1.00 91.42  ?  205  HIS A ND1 1 
ATOM   1360 C  CD2 . HIS A 1 206 ? 20.124  27.698  29.481  1.00 114.76 ?  205  HIS A CD2 1 
ATOM   1361 C  CE1 . HIS A 1 206 ? 21.203  25.792  29.379  1.00 106.75 ?  205  HIS A CE1 1 
ATOM   1362 N  NE2 . HIS A 1 206 ? 20.085  26.361  29.792  1.00 120.17 ?  205  HIS A NE2 1 
ATOM   1363 N  N   . LYS A 1 207 ? 24.051  31.217  27.138  1.00 102.90 ?  206  LYS A N   1 
ATOM   1364 C  CA  . LYS A 1 207 ? 24.421  32.261  26.200  1.00 96.67  ?  206  LYS A CA  1 
ATOM   1365 C  C   . LYS A 1 207 ? 25.557  31.746  25.327  1.00 89.14  ?  206  LYS A C   1 
ATOM   1366 O  O   . LYS A 1 207 ? 25.562  31.942  24.115  1.00 104.67 ?  206  LYS A O   1 
ATOM   1367 C  CB  . LYS A 1 207 ? 24.842  33.531  26.943  1.00 101.49 ?  206  LYS A CB  1 
ATOM   1368 C  CG  . LYS A 1 207 ? 24.250  34.816  26.398  1.00 109.71 ?  206  LYS A CG  1 
ATOM   1369 C  CD  . LYS A 1 207 ? 22.761  34.897  26.686  1.00 116.48 ?  206  LYS A CD  1 
ATOM   1370 C  CE  . LYS A 1 207 ? 22.200  36.248  26.282  1.00 127.89 ?  206  LYS A CE  1 
ATOM   1371 N  NZ  . LYS A 1 207 ? 20.740  36.348  26.552  1.00 133.75 ?  206  LYS A NZ  1 
ATOM   1372 N  N   . LEU A 1 208 ? 26.495  31.043  25.951  1.00 72.49  ?  207  LEU A N   1 
ATOM   1373 C  CA  . LEU A 1 208 ? 27.612  30.439  25.239  1.00 76.87  ?  207  LEU A CA  1 
ATOM   1374 C  C   . LEU A 1 208 ? 27.163  29.384  24.244  1.00 91.40  ?  207  LEU A C   1 
ATOM   1375 O  O   . LEU A 1 208 ? 27.710  29.287  23.148  1.00 105.78 ?  207  LEU A O   1 
ATOM   1376 C  CB  . LEU A 1 208 ? 28.604  29.812  26.220  1.00 87.27  ?  207  LEU A CB  1 
ATOM   1377 C  CG  . LEU A 1 208 ? 29.657  30.717  26.853  1.00 85.85  ?  207  LEU A CG  1 
ATOM   1378 C  CD1 . LEU A 1 208 ? 30.607  29.876  27.687  1.00 94.12  ?  207  LEU A CD1 1 
ATOM   1379 C  CD2 . LEU A 1 208 ? 30.414  31.482  25.783  1.00 84.50  ?  207  LEU A CD2 1 
ATOM   1380 N  N   . ARG A 1 209 ? 26.182  28.580  24.636  1.00 101.07 ?  208  ARG A N   1 
ATOM   1381 C  CA  . ARG A 1 209 ? 25.684  27.517  23.772  1.00 107.41 ?  208  ARG A CA  1 
ATOM   1382 C  C   . ARG A 1 209 ? 25.096  28.092  22.495  1.00 125.06 ?  208  ARG A C   1 
ATOM   1383 O  O   . ARG A 1 209 ? 25.341  27.589  21.398  1.00 157.22 ?  208  ARG A O   1 
ATOM   1384 C  CB  . ARG A 1 209 ? 24.603  26.700  24.474  1.00 96.68  ?  208  ARG A CB  1 
ATOM   1385 C  CG  . ARG A 1 209 ? 24.061  25.578  23.615  1.00 93.68  ?  208  ARG A CG  1 
ATOM   1386 C  CD  . ARG A 1 209 ? 22.694  25.088  24.065  1.00 99.22  ?  208  ARG A CD  1 
ATOM   1387 N  NE  . ARG A 1 209 ? 21.646  26.063  23.768  1.00 100.47 ?  208  ARG A NE  1 
ATOM   1388 C  CZ  . ARG A 1 209 ? 21.155  26.944  24.630  1.00 107.37 ?  208  ARG A CZ  1 
ATOM   1389 N  NH1 . ARG A 1 209 ? 21.614  26.990  25.869  1.00 118.16 ?  208  ARG A NH1 1 
ATOM   1390 N  NH2 . ARG A 1 209 ? 20.198  27.780  24.248  1.00 108.03 ?  208  ARG A NH2 1 
ATOM   1391 N  N   . GLU A 1 210 ? 24.330  29.167  22.659  1.00 110.28 ?  209  GLU A N   1 
ATOM   1392 C  CA  . GLU A 1 210 ? 23.593  29.786  21.566  1.00 97.42  ?  209  GLU A CA  1 
ATOM   1393 C  C   . GLU A 1 210 ? 24.496  30.435  20.515  1.00 106.57 ?  209  GLU A C   1 
ATOM   1394 O  O   . GLU A 1 210 ? 24.155  30.468  19.329  1.00 118.96 ?  209  GLU A O   1 
ATOM   1395 C  CB  . GLU A 1 210 ? 22.625  30.831  22.123  1.00 84.69  ?  209  GLU A CB  1 
ATOM   1396 C  CG  . GLU A 1 210 ? 21.427  31.102  21.234  1.00 111.26 ?  209  GLU A CG  1 
ATOM   1397 C  CD  . GLU A 1 210 ? 20.289  31.753  21.987  1.00 127.05 ?  209  GLU A CD  1 
ATOM   1398 O  OE1 . GLU A 1 210 ? 20.459  32.015  23.196  1.00 118.37 ?  209  GLU A OE1 1 
ATOM   1399 O  OE2 . GLU A 1 210 ? 19.226  31.995  21.374  1.00 138.31 ?  209  GLU A OE2 1 
ATOM   1400 N  N   . TYR A 1 211 ? 25.639  30.959  20.950  1.00 107.15 ?  210  TYR A N   1 
ATOM   1401 C  CA  . TYR A 1 211 ? 26.490  31.745  20.062  1.00 105.94 ?  210  TYR A CA  1 
ATOM   1402 C  C   . TYR A 1 211 ? 27.866  31.122  19.814  1.00 102.30 ?  210  TYR A C   1 
ATOM   1403 O  O   . TYR A 1 211 ? 28.653  31.655  19.035  1.00 97.06  ?  210  TYR A O   1 
ATOM   1404 C  CB  . TYR A 1 211 ? 26.660  33.161  20.624  1.00 107.34 ?  210  TYR A CB  1 
ATOM   1405 C  CG  . TYR A 1 211 ? 25.355  33.923  20.748  1.00 118.73 ?  210  TYR A CG  1 
ATOM   1406 C  CD1 . TYR A 1 211 ? 24.570  33.807  21.888  1.00 123.12 ?  210  TYR A CD1 1 
ATOM   1407 C  CD2 . TYR A 1 211 ? 24.907  34.753  19.728  1.00 125.95 ?  210  TYR A CD2 1 
ATOM   1408 C  CE1 . TYR A 1 211 ? 23.378  34.493  22.010  1.00 123.16 ?  210  TYR A CE1 1 
ATOM   1409 C  CE2 . TYR A 1 211 ? 23.714  35.445  19.843  1.00 132.73 ?  210  TYR A CE2 1 
ATOM   1410 C  CZ  . TYR A 1 211 ? 22.955  35.310  20.987  1.00 131.50 ?  210  TYR A CZ  1 
ATOM   1411 O  OH  . TYR A 1 211 ? 21.767  35.994  21.113  1.00 139.75 ?  210  TYR A OH  1 
ATOM   1412 N  N   . VAL A 1 212 ? 28.169  30.019  20.497  1.00 110.73 ?  211  VAL A N   1 
ATOM   1413 C  CA  . VAL A 1 212 ? 29.384  29.237  20.228  1.00 112.18 ?  211  VAL A CA  1 
ATOM   1414 C  C   . VAL A 1 212 ? 29.099  27.738  20.333  1.00 116.77 ?  211  VAL A C   1 
ATOM   1415 O  O   . VAL A 1 212 ? 28.261  27.314  21.132  1.00 114.97 ?  211  VAL A O   1 
ATOM   1416 C  CB  . VAL A 1 212 ? 30.549  29.580  21.202  1.00 135.21 ?  211  VAL A CB  1 
ATOM   1417 C  CG1 . VAL A 1 212 ? 31.867  29.004  20.687  1.00 123.32 ?  211  VAL A CG1 1 
ATOM   1418 C  CG2 . VAL A 1 212 ? 30.679  31.085  21.424  1.00 138.07 ?  211  VAL A CG2 1 
ATOM   1419 N  N   . GLY A 1 213 ? 29.805  26.937  19.542  1.00 121.31 ?  212  GLY A N   1 
ATOM   1420 C  CA  . GLY A 1 213 ? 29.660  25.495  19.616  1.00 123.42 ?  212  GLY A CA  1 
ATOM   1421 C  C   . GLY A 1 213 ? 30.831  24.866  20.343  1.00 119.76 ?  212  GLY A C   1 
ATOM   1422 O  O   . GLY A 1 213 ? 30.753  24.590  21.539  1.00 108.07 ?  212  GLY A O   1 
ATOM   1423 N  N   . CYS A 1 214 ? 31.925  24.647  19.622  1.00 130.67 ?  213  CYS A N   1 
ATOM   1424 C  CA  . CYS A 1 214 ? 33.160  24.201  20.249  1.00 132.62 ?  213  CYS A CA  1 
ATOM   1425 C  C   . CYS A 1 214 ? 33.827  25.419  20.871  1.00 139.95 ?  213  CYS A C   1 
ATOM   1426 O  O   . CYS A 1 214 ? 33.969  26.456  20.226  1.00 146.71 ?  213  CYS A O   1 
ATOM   1427 C  CB  . CYS A 1 214 ? 34.083  23.513  19.240  1.00 128.52 ?  213  CYS A CB  1 
ATOM   1428 S  SG  . CYS A 1 214 ? 34.354  24.438  17.712  1.00 309.50 ?  213  CYS A SG  1 
ATOM   1429 N  N   . VAL A 1 215 ? 34.220  25.293  22.133  1.00 137.20 ?  214  VAL A N   1 
ATOM   1430 C  CA  . VAL A 1 215 ? 34.721  26.432  22.891  1.00 118.94 ?  214  VAL A CA  1 
ATOM   1431 C  C   . VAL A 1 215 ? 36.240  26.448  22.955  1.00 116.82 ?  214  VAL A C   1 
ATOM   1432 O  O   . VAL A 1 215 ? 36.894  25.424  22.759  1.00 115.09 ?  214  VAL A O   1 
ATOM   1433 C  CB  . VAL A 1 215 ? 34.165  26.435  24.324  1.00 106.01 ?  214  VAL A CB  1 
ATOM   1434 C  CG1 . VAL A 1 215 ? 34.046  27.854  24.835  1.00 104.55 ?  214  VAL A CG1 1 
ATOM   1435 C  CG2 . VAL A 1 215 ? 32.811  25.744  24.364  1.00 113.71 ?  214  VAL A CG2 1 
ATOM   1436 N  N   . SER A 1 216 ? 36.793  27.625  23.218  1.00 122.38 ?  215  SER A N   1 
ATOM   1437 C  CA  . SER A 1 216 ? 38.234  27.794  23.330  1.00 121.16 ?  215  SER A CA  1 
ATOM   1438 C  C   . SER A 1 216 ? 38.757  27.202  24.628  1.00 117.16 ?  215  SER A C   1 
ATOM   1439 O  O   . SER A 1 216 ? 37.986  26.880  25.529  1.00 121.06 ?  215  SER A O   1 
ATOM   1440 C  CB  . SER A 1 216 ? 38.610  29.272  23.251  1.00 114.38 ?  215  SER A CB  1 
ATOM   1441 O  OG  . SER A 1 216 ? 38.084  29.986  24.354  1.00 106.99 ?  215  SER A OG  1 
ATOM   1442 N  N   . GLU A 1 217 ? 40.076  27.057  24.703  1.00 125.06 ?  216  GLU A N   1 
ATOM   1443 C  CA  . GLU A 1 217 ? 40.750  26.499  25.874  1.00 145.99 ?  216  GLU A CA  1 
ATOM   1444 C  C   . GLU A 1 217 ? 40.649  27.399  27.104  1.00 150.52 ?  216  GLU A C   1 
ATOM   1445 O  O   . GLU A 1 217 ? 40.481  26.917  28.223  1.00 138.16 ?  216  GLU A O   1 
ATOM   1446 C  CB  . GLU A 1 217 ? 42.225  26.248  25.558  1.00 157.35 ?  216  GLU A CB  1 
ATOM   1447 C  CG  . GLU A 1 217 ? 42.477  25.195  24.497  1.00 169.41 ?  216  GLU A CG  1 
ATOM   1448 C  CD  . GLU A 1 217 ? 42.683  23.819  25.090  1.00 180.83 ?  216  GLU A CD  1 
ATOM   1449 O  OE1 . GLU A 1 217 ? 42.108  23.543  26.165  1.00 190.72 ?  216  GLU A OE1 1 
ATOM   1450 O  OE2 . GLU A 1 217 ? 43.430  23.018  24.489  1.00 180.10 ?  216  GLU A OE2 1 
ATOM   1451 N  N   . GLU A 1 218 ? 40.776  28.707  26.890  1.00 156.60 ?  217  GLU A N   1 
ATOM   1452 C  CA  . GLU A 1 218 ? 40.716  29.676  27.979  1.00 149.39 ?  217  GLU A CA  1 
ATOM   1453 C  C   . GLU A 1 218 ? 39.367  29.650  28.687  1.00 136.70 ?  217  GLU A C   1 
ATOM   1454 O  O   . GLU A 1 218 ? 39.300  29.612  29.916  1.00 140.76 ?  217  GLU A O   1 
ATOM   1455 C  CB  . GLU A 1 218 ? 40.997  31.090  27.456  1.00 155.75 ?  217  GLU A CB  1 
ATOM   1456 C  CG  . GLU A 1 218 ? 42.376  31.283  26.832  1.00 155.44 ?  217  GLU A CG  1 
ATOM   1457 C  CD  . GLU A 1 218 ? 42.426  30.891  25.366  1.00 150.33 ?  217  GLU A CD  1 
ATOM   1458 O  OE1 . GLU A 1 218 ? 41.358  30.586  24.793  1.00 153.12 ?  217  GLU A OE1 1 
ATOM   1459 O  OE2 . GLU A 1 218 ? 43.533  30.891  24.786  1.00 145.03 ?  217  GLU A OE2 1 
ATOM   1460 N  N   . THR A 1 219 ? 38.296  29.654  27.901  1.00 123.68 ?  218  THR A N   1 
ATOM   1461 C  CA  . THR A 1 219 ? 36.943  29.534  28.433  1.00 116.90 ?  218  THR A CA  1 
ATOM   1462 C  C   . THR A 1 219 ? 36.731  28.194  29.128  1.00 110.61 ?  218  THR A C   1 
ATOM   1463 O  O   . THR A 1 219 ? 36.057  28.113  30.154  1.00 114.86 ?  218  THR A O   1 
ATOM   1464 C  CB  . THR A 1 219 ? 35.887  29.706  27.328  1.00 123.12 ?  218  THR A CB  1 
ATOM   1465 O  OG1 . THR A 1 219 ? 36.187  30.882  26.566  1.00 133.28 ?  218  THR A OG1 1 
ATOM   1466 C  CG2 . THR A 1 219 ? 34.499  29.856  27.935  1.00 119.19 ?  218  THR A CG2 1 
ATOM   1467 N  N   . LEU A 1 220 ? 37.312  27.148  28.555  1.00 106.02 ?  219  LEU A N   1 
ATOM   1468 C  CA  . LEU A 1 220 ? 37.153  25.794  29.067  1.00 110.61 ?  219  LEU A CA  1 
ATOM   1469 C  C   . LEU A 1 220 ? 37.647  25.706  30.509  1.00 120.95 ?  219  LEU A C   1 
ATOM   1470 O  O   . LEU A 1 220 ? 37.033  25.039  31.344  1.00 120.02 ?  219  LEU A O   1 
ATOM   1471 C  CB  . LEU A 1 220 ? 37.908  24.804  28.184  1.00 114.47 ?  219  LEU A CB  1 
ATOM   1472 C  CG  . LEU A 1 220 ? 37.640  23.323  28.435  1.00 122.55 ?  219  LEU A CG  1 
ATOM   1473 C  CD1 . LEU A 1 220 ? 36.231  22.983  27.965  1.00 113.79 ?  219  LEU A CD1 1 
ATOM   1474 C  CD2 . LEU A 1 220 ? 38.677  22.458  27.743  1.00 130.60 ?  219  LEU A CD2 1 
ATOM   1475 N  N   . LYS A 1 221 ? 38.760  26.384  30.790  1.00 124.83 ?  220  LYS A N   1 
ATOM   1476 C  CA  . LYS A 1 221 ? 39.326  26.440  32.139  1.00 103.96 ?  220  LYS A CA  1 
ATOM   1477 C  C   . LYS A 1 221 ? 38.401  27.202  33.086  1.00 81.45  ?  220  LYS A C   1 
ATOM   1478 O  O   . LYS A 1 221 ? 38.237  26.818  34.239  1.00 81.99  ?  220  LYS A O   1 
ATOM   1479 C  CB  . LYS A 1 221 ? 40.717  27.087  32.127  1.00 101.79 ?  220  LYS A CB  1 
ATOM   1480 C  CG  . LYS A 1 221 ? 41.777  26.296  31.365  1.00 122.40 ?  220  LYS A CG  1 
ATOM   1481 C  CD  . LYS A 1 221 ? 43.171  26.890  31.557  1.00 135.65 ?  220  LYS A CD  1 
ATOM   1482 C  CE  . LYS A 1 221 ? 44.232  26.120  30.770  1.00 142.82 ?  220  LYS A CE  1 
ATOM   1483 N  NZ  . LYS A 1 221 ? 44.032  26.211  29.295  1.00 138.20 ?  220  LYS A NZ  1 
ATOM   1484 N  N   . ILE A 1 222 ? 37.806  28.285  32.593  1.00 70.66  ?  221  ILE A N   1 
ATOM   1485 C  CA  . ILE A 1 222 ? 36.839  29.059  33.369  1.00 75.44  ?  221  ILE A CA  1 
ATOM   1486 C  C   . ILE A 1 222 ? 35.620  28.223  33.761  1.00 86.66  ?  221  ILE A C   1 
ATOM   1487 O  O   . ILE A 1 222 ? 35.173  28.256  34.910  1.00 82.07  ?  221  ILE A O   1 
ATOM   1488 C  CB  . ILE A 1 222 ? 36.374  30.308  32.588  1.00 66.14  ?  221  ILE A CB  1 
ATOM   1489 C  CG1 . ILE A 1 222 ? 37.514  31.325  32.501  1.00 63.61  ?  221  ILE A CG1 1 
ATOM   1490 C  CG2 . ILE A 1 222 ? 35.175  30.955  33.264  1.00 63.77  ?  221  ILE A CG2 1 
ATOM   1491 C  CD1 . ILE A 1 222 ? 37.293  32.420  31.475  1.00 61.29  ?  221  ILE A CD1 1 
ATOM   1492 N  N   . ILE A 1 223 ? 35.090  27.476  32.797  1.00 97.55  ?  222  ILE A N   1 
ATOM   1493 C  CA  . ILE A 1 223 ? 33.982  26.555  33.038  1.00 85.58  ?  222  ILE A CA  1 
ATOM   1494 C  C   . ILE A 1 223 ? 34.361  25.469  34.041  1.00 73.05  ?  222  ILE A C   1 
ATOM   1495 O  O   . ILE A 1 223 ? 33.575  25.126  34.922  1.00 74.02  ?  222  ILE A O   1 
ATOM   1496 C  CB  . ILE A 1 223 ? 33.509  25.898  31.725  1.00 96.10  ?  222  ILE A CB  1 
ATOM   1497 C  CG1 . ILE A 1 223 ? 33.115  26.973  30.711  1.00 102.74 ?  222  ILE A CG1 1 
ATOM   1498 C  CG2 . ILE A 1 223 ? 32.329  24.976  31.982  1.00 95.68  ?  222  ILE A CG2 1 
ATOM   1499 C  CD1 . ILE A 1 223 ? 33.261  26.535  29.270  1.00 112.38 ?  222  ILE A CD1 1 
ATOM   1500 N  N   . GLU A 1 224 ? 35.568  24.931  33.897  1.00 75.49  ?  223  GLU A N   1 
ATOM   1501 C  CA  . GLU A 1 224 ? 36.052  23.868  34.771  1.00 86.46  ?  223  GLU A CA  1 
ATOM   1502 C  C   . GLU A 1 224 ? 36.164  24.329  36.229  1.00 111.20 ?  223  GLU A C   1 
ATOM   1503 O  O   . GLU A 1 224 ? 35.765  23.611  37.149  1.00 107.93 ?  223  GLU A O   1 
ATOM   1504 C  CB  . GLU A 1 224 ? 37.406  23.361  34.265  1.00 79.04  ?  223  GLU A CB  1 
ATOM   1505 C  CG  . GLU A 1 224 ? 37.865  22.052  34.883  1.00 109.17 ?  223  GLU A CG  1 
ATOM   1506 C  CD  . GLU A 1 224 ? 39.225  21.617  34.373  1.00 129.16 ?  223  GLU A CD  1 
ATOM   1507 O  OE1 . GLU A 1 224 ? 39.823  22.365  33.570  1.00 129.55 ?  223  GLU A OE1 1 
ATOM   1508 O  OE2 . GLU A 1 224 ? 39.692  20.527  34.767  1.00 136.39 ?  223  GLU A OE2 1 
ATOM   1509 N  N   . GLU A 1 225 ? 36.681  25.541  36.428  1.00 130.62 ?  224  GLU A N   1 
ATOM   1510 C  CA  . GLU A 1 225 ? 36.898  26.090  37.769  1.00 127.57 ?  224  GLU A CA  1 
ATOM   1511 C  C   . GLU A 1 225 ? 35.592  26.358  38.504  1.00 113.64 ?  224  GLU A C   1 
ATOM   1512 O  O   . GLU A 1 225 ? 35.539  26.248  39.727  1.00 124.78 ?  224  GLU A O   1 
ATOM   1513 C  CB  . GLU A 1 225 ? 37.725  27.376  37.711  1.00 143.11 ?  224  GLU A CB  1 
ATOM   1514 C  CG  . GLU A 1 225 ? 39.205  27.160  37.428  1.00 162.57 ?  224  GLU A CG  1 
ATOM   1515 C  CD  . GLU A 1 225 ? 40.000  28.453  37.480  1.00 180.56 ?  224  GLU A CD  1 
ATOM   1516 O  OE1 . GLU A 1 225 ? 39.377  29.529  37.600  1.00 185.88 ?  224  GLU A OE1 1 
ATOM   1517 O  OE2 . GLU A 1 225 ? 41.245  28.394  37.399  1.00 189.52 ?  224  GLU A OE2 1 
ATOM   1518 N  N   . TRP A 1 226 ? 34.558  26.760  37.771  1.00 87.57  ?  225  TRP A N   1 
ATOM   1519 C  CA  . TRP A 1 226 ? 33.250  26.978  38.381  1.00 89.17  ?  225  TRP A CA  1 
ATOM   1520 C  C   . TRP A 1 226 ? 32.610  25.697  38.925  1.00 102.27 ?  225  TRP A C   1 
ATOM   1521 O  O   . TRP A 1 226 ? 32.130  25.682  40.058  1.00 118.48 ?  225  TRP A O   1 
ATOM   1522 C  CB  . TRP A 1 226 ? 32.282  27.616  37.392  1.00 86.50  ?  225  TRP A CB  1 
ATOM   1523 C  CG  . TRP A 1 226 ? 30.852  27.392  37.796  1.00 100.90 ?  225  TRP A CG  1 
ATOM   1524 C  CD1 . TRP A 1 226 ? 29.987  26.477  37.266  1.00 104.14 ?  225  TRP A CD1 1 
ATOM   1525 C  CD2 . TRP A 1 226 ? 30.122  28.084  38.819  1.00 115.46 ?  225  TRP A CD2 1 
ATOM   1526 N  NE1 . TRP A 1 226 ? 28.768  26.557  37.893  1.00 102.13 ?  225  TRP A NE1 1 
ATOM   1527 C  CE2 . TRP A 1 226 ? 28.821  27.542  38.849  1.00 110.34 ?  225  TRP A CE2 1 
ATOM   1528 C  CE3 . TRP A 1 226 ? 30.439  29.117  39.711  1.00 126.96 ?  225  TRP A CE3 1 
ATOM   1529 C  CZ2 . TRP A 1 226 ? 27.838  27.989  39.732  1.00 107.72 ?  225  TRP A CZ2 1 
ATOM   1530 C  CZ3 . TRP A 1 226 ? 29.460  29.562  40.590  1.00 131.14 ?  225  TRP A CZ3 1 
ATOM   1531 C  CH2 . TRP A 1 226 ? 28.177  28.997  40.593  1.00 118.93 ?  225  TRP A CH2 1 
ATOM   1532 N  N   . PHE A 1 227 ? 32.584  24.634  38.121  1.00 92.86  ?  226  PHE A N   1 
ATOM   1533 C  CA  . PHE A 1 227 ? 31.934  23.393  38.549  1.00 109.50 ?  226  PHE A CA  1 
ATOM   1534 C  C   . PHE A 1 227 ? 32.655  22.746  39.728  1.00 119.28 ?  226  PHE A C   1 
ATOM   1535 O  O   . PHE A 1 227 ? 32.025  22.173  40.617  1.00 127.00 ?  226  PHE A O   1 
ATOM   1536 C  CB  . PHE A 1 227 ? 31.830  22.393  37.390  1.00 107.81 ?  226  PHE A CB  1 
ATOM   1537 C  CG  . PHE A 1 227 ? 30.716  22.696  36.425  1.00 110.03 ?  226  PHE A CG  1 
ATOM   1538 C  CD1 . PHE A 1 227 ? 29.391  22.635  36.835  1.00 109.54 ?  226  PHE A CD1 1 
ATOM   1539 C  CD2 . PHE A 1 227 ? 30.989  23.033  35.111  1.00 109.04 ?  226  PHE A CD2 1 
ATOM   1540 C  CE1 . PHE A 1 227 ? 28.359  22.916  35.955  1.00 98.02  ?  226  PHE A CE1 1 
ATOM   1541 C  CE2 . PHE A 1 227 ? 29.961  23.314  34.225  1.00 105.00 ?  226  PHE A CE2 1 
ATOM   1542 C  CZ  . PHE A 1 227 ? 28.644  23.255  34.650  1.00 100.71 ?  226  PHE A CZ  1 
ATOM   1543 N  N   . CYS A 1 228 ? 33.978  22.840  39.734  1.00 116.12 ?  227  CYS A N   1 
ATOM   1544 C  CA  . CYS A 1 228 ? 34.764  22.377  40.870  1.00 133.00 ?  227  CYS A CA  1 
ATOM   1545 C  C   . CYS A 1 228 ? 34.647  23.333  42.058  1.00 139.75 ?  227  CYS A C   1 
ATOM   1546 O  O   . CYS A 1 228 ? 35.046  23.002  43.178  1.00 148.75 ?  227  CYS A O   1 
ATOM   1547 C  CB  . CYS A 1 228 ? 36.226  22.198  40.464  1.00 143.26 ?  227  CYS A CB  1 
ATOM   1548 S  SG  . CYS A 1 228 ? 36.458  20.946  39.192  1.00 111.12 ?  227  CYS A SG  1 
ATOM   1549 N  N   . GLY A 1 229 ? 34.107  24.522  41.802  1.00 133.91 ?  228  GLY A N   1 
ATOM   1550 C  CA  . GLY A 1 229 ? 33.930  25.503  42.851  1.00 129.95 ?  228  GLY A CA  1 
ATOM   1551 C  C   . GLY A 1 229 ? 32.936  24.993  43.871  1.00 137.79 ?  228  GLY A C   1 
ATOM   1552 O  O   . GLY A 1 229 ? 31.863  24.496  43.526  1.00 140.79 ?  228  GLY A O   1 
ATOM   1553 N  N   . GLU A 1 230 ? 33.303  25.125  45.140  1.00 145.65 ?  229  GLU A N   1 
ATOM   1554 C  CA  . GLU A 1 230 ? 32.476  24.650  46.234  1.00 157.04 ?  229  GLU A CA  1 
ATOM   1555 C  C   . GLU A 1 230 ? 31.116  25.332  46.215  1.00 149.87 ?  229  GLU A C   1 
ATOM   1556 O  O   . GLU A 1 230 ? 30.100  24.692  46.480  1.00 151.81 ?  229  GLU A O   1 
ATOM   1557 C  CB  . GLU A 1 230 ? 33.181  24.874  47.577  1.00 169.16 ?  229  GLU A CB  1 
ATOM   1558 C  CG  . GLU A 1 230 ? 34.382  23.950  47.802  1.00 173.36 ?  229  GLU A CG  1 
ATOM   1559 C  CD  . GLU A 1 230 ? 35.060  24.177  49.142  1.00 173.63 ?  229  GLU A CD  1 
ATOM   1560 O  OE1 . GLU A 1 230 ? 34.578  25.033  49.914  1.00 172.50 ?  229  GLU A OE1 1 
ATOM   1561 O  OE2 . GLU A 1 230 ? 36.071  23.496  49.426  1.00 171.56 ?  229  GLU A OE2 1 
ATOM   1562 N  N   . LYS A 1 231 ? 31.099  26.615  45.859  1.00 140.69 ?  230  LYS A N   1 
ATOM   1563 C  CA  . LYS A 1 231 ? 29.852  27.368  45.777  1.00 145.80 ?  230  LYS A CA  1 
ATOM   1564 C  C   . LYS A 1 231 ? 28.887  26.697  44.818  1.00 143.99 ?  230  LYS A C   1 
ATOM   1565 O  O   . LYS A 1 231 ? 27.707  26.556  45.116  1.00 136.31 ?  230  LYS A O   1 
ATOM   1566 C  CB  . LYS A 1 231 ? 30.112  28.808  45.330  1.00 146.96 ?  230  LYS A CB  1 
ATOM   1567 C  CG  . LYS A 1 231 ? 28.859  29.679  45.269  1.00 157.60 ?  230  LYS A CG  1 
ATOM   1568 C  CD  . LYS A 1 231 ? 28.231  29.849  46.647  1.00 174.83 ?  230  LYS A CD  1 
ATOM   1569 C  CE  . LYS A 1 231 ? 27.122  30.895  46.636  1.00 173.29 ?  230  LYS A CE  1 
ATOM   1570 N  NZ  . LYS A 1 231 ? 26.065  30.584  45.633  1.00 162.15 ?  230  LYS A NZ  1 
ATOM   1571 N  N   . ALA A 1 232 ? 29.398  26.277  43.667  1.00 144.01 ?  231  ALA A N   1 
ATOM   1572 C  CA  . ALA A 1 232 ? 28.573  25.622  42.663  1.00 143.00 ?  231  ALA A CA  1 
ATOM   1573 C  C   . ALA A 1 232 ? 28.024  24.291  43.158  1.00 147.57 ?  231  ALA A C   1 
ATOM   1574 O  O   . ALA A 1 232 ? 26.853  23.979  42.958  1.00 147.87 ?  231  ALA A O   1 
ATOM   1575 C  CB  . ALA A 1 232 ? 29.367  25.408  41.396  1.00 141.82 ?  231  ALA A CB  1 
ATOM   1576 N  N   . GLY A 1 233 ? 28.885  23.508  43.799  1.00 148.69 ?  232  GLY A N   1 
ATOM   1577 C  CA  . GLY A 1 233 ? 28.500  22.200  44.293  1.00 140.66 ?  232  GLY A CA  1 
ATOM   1578 C  C   . GLY A 1 233 ? 27.471  22.206  45.405  1.00 135.87 ?  232  GLY A C   1 
ATOM   1579 O  O   . GLY A 1 233 ? 26.496  21.456  45.361  1.00 118.00 ?  232  GLY A O   1 
ATOM   1580 N  N   . GLU A 1 234 ? 27.694  23.043  46.413  1.00 155.18 ?  233  GLU A N   1 
ATOM   1581 C  CA  . GLU A 1 234 ? 26.804  23.086  47.565  1.00 171.77 ?  233  GLU A CA  1 
ATOM   1582 C  C   . GLU A 1 234 ? 25.432  23.664  47.228  1.00 176.59 ?  233  GLU A C   1 
ATOM   1583 O  O   . GLU A 1 234 ? 24.408  23.074  47.567  1.00 176.71 ?  233  GLU A O   1 
ATOM   1584 C  CB  . GLU A 1 234 ? 27.448  23.908  48.687  1.00 177.16 ?  233  GLU A CB  1 
ATOM   1585 C  CG  . GLU A 1 234 ? 28.824  23.410  49.111  1.00 182.95 ?  233  GLU A CG  1 
ATOM   1586 C  CD  . GLU A 1 234 ? 29.580  24.413  49.962  1.00 184.88 ?  233  GLU A CD  1 
ATOM   1587 O  OE1 . GLU A 1 234 ? 28.997  25.459  50.317  1.00 194.85 ?  233  GLU A OE1 1 
ATOM   1588 O  OE2 . GLU A 1 234 ? 30.761  24.154  50.277  1.00 178.18 ?  233  GLU A OE2 1 
ATOM   1589 N  N   . VAL A 1 235 ? 25.414  24.817  46.562  1.00 183.90 ?  234  VAL A N   1 
ATOM   1590 C  CA  . VAL A 1 235 ? 24.167  25.557  46.371  1.00 191.85 ?  234  VAL A CA  1 
ATOM   1591 C  C   . VAL A 1 235 ? 23.466  25.050  45.113  1.00 188.16 ?  234  VAL A C   1 
ATOM   1592 O  O   . VAL A 1 235 ? 22.270  25.278  44.927  1.00 200.18 ?  234  VAL A O   1 
ATOM   1593 C  CB  . VAL A 1 235 ? 24.388  27.087  46.283  1.00 197.24 ?  234  VAL A CB  1 
ATOM   1594 C  CG1 . VAL A 1 235 ? 24.826  27.491  44.889  1.00 199.85 ?  234  VAL A CG1 1 
ATOM   1595 C  CG2 . VAL A 1 235 ? 23.108  27.818  46.646  1.00 195.84 ?  234  VAL A CG2 1 
ATOM   1596 N  N   . GLY A 1 236 ? 24.237  24.390  44.247  1.00 180.85 ?  235  GLY A N   1 
ATOM   1597 C  CA  . GLY A 1 236 ? 23.798  23.993  42.917  1.00 169.70 ?  235  GLY A CA  1 
ATOM   1598 C  C   . GLY A 1 236 ? 22.431  23.351  42.866  1.00 181.59 ?  235  GLY A C   1 
ATOM   1599 O  O   . GLY A 1 236 ? 21.669  23.570  41.931  1.00 154.91 ?  235  GLY A O   1 
ATOM   1600 N  N   . ASP A 1 237 ? 22.135  22.536  43.873  1.00 213.38 ?  236  ASP A N   1 
ATOM   1601 C  CA  . ASP A 1 237 ? 20.803  21.973  44.044  1.00 232.67 ?  236  ASP A CA  1 
ATOM   1602 C  C   . ASP A 1 237 ? 19.744  23.068  44.045  1.00 234.92 ?  236  ASP A C   1 
ATOM   1603 O  O   . ASP A 1 237 ? 19.836  24.044  44.786  1.00 243.72 ?  236  ASP A O   1 
ATOM   1604 C  CB  . ASP A 1 237 ? 20.721  21.153  45.339  1.00 238.82 ?  236  ASP A CB  1 
ATOM   1605 C  CG  . ASP A 1 237 ? 20.774  22.016  46.588  1.00 237.01 ?  236  ASP A CG  1 
ATOM   1606 O  OD1 . ASP A 1 237 ? 21.857  22.544  46.906  1.00 236.28 ?  236  ASP A OD1 1 
ATOM   1607 O  OD2 . ASP A 1 237 ? 19.729  22.168  47.253  1.00 234.36 ?  236  ASP A OD2 1 
ATOM   1608 N  N   . ASN A 1 238 ? 18.743  22.909  43.191  1.00 226.58 ?  237  ASN A N   1 
ATOM   1609 C  CA  . ASN A 1 238 ? 17.626  23.837  43.164  1.00 218.31 ?  237  ASN A CA  1 
ATOM   1610 C  C   . ASN A 1 238 ? 16.336  23.100  42.850  1.00 213.21 ?  237  ASN A C   1 
ATOM   1611 O  O   . ASN A 1 238 ? 16.343  22.076  42.165  1.00 199.11 ?  237  ASN A O   1 
ATOM   1612 C  CB  . ASN A 1 238 ? 17.873  24.953  42.147  1.00 216.77 ?  237  ASN A CB  1 
ATOM   1613 C  CG  . ASN A 1 238 ? 17.005  26.169  42.399  1.00 217.89 ?  237  ASN A CG  1 
ATOM   1614 O  OD1 . ASN A 1 238 ? 15.792  26.054  42.575  1.00 221.98 ?  237  ASN A OD1 1 
ATOM   1615 N  ND2 . ASN A 1 238 ? 17.624  27.344  42.426  1.00 211.33 ?  237  ASN A ND2 1 
ATOM   1616 N  N   . GLY A 1 239 ? 15.227  23.622  43.357  1.00 220.64 ?  238  GLY A N   1 
ATOM   1617 C  CA  . GLY A 1 239 ? 13.951  22.960  43.193  1.00 222.84 ?  238  GLY A CA  1 
ATOM   1618 C  C   . GLY A 1 239 ? 12.864  23.835  42.593  1.00 235.52 ?  238  GLY A C   1 
ATOM   1619 O  O   . GLY A 1 239 ? 12.511  24.835  43.217  1.00 231.82 ?  238  GLY A O   1 
ATOM   1620 N  N   . ILE A 1 240 ? 12.320  23.520  41.408  1.00 251.61 ?  239  ILE A N   1 
ATOM   1621 C  CA  . ILE A 1 240 ? 12.678  22.414  40.492  1.00 270.65 ?  239  ILE A CA  1 
ATOM   1622 C  C   . ILE A 1 240 ? 12.930  21.042  41.142  1.00 290.06 ?  239  ILE A C   1 
ATOM   1623 O  O   . ILE A 1 240 ? 12.082  20.541  41.883  1.00 297.59 ?  239  ILE A O   1 
ATOM   1624 C  CB  . ILE A 1 240 ? 13.908  22.794  39.628  1.00 190.39 ?  239  ILE A CB  1 
ATOM   1625 C  CG1 . ILE A 1 240 ? 13.979  24.311  39.445  1.00 188.24 ?  239  ILE A CG1 1 
ATOM   1626 C  CG2 . ILE A 1 240 ? 13.832  22.117  38.259  1.00 182.45 ?  239  ILE A CG2 1 
ATOM   1627 C  CD1 . ILE A 1 240 ? 15.081  24.773  38.525  1.00 182.47 ?  239  ILE A CD1 1 
ATOM   1628 N  N   . GLY A 1 241 ? 14.088  20.442  40.868  1.00 299.02 ?  240  GLY A N   1 
ATOM   1629 C  CA  . GLY A 1 241 ? 14.387  19.095  41.331  1.00 298.44 ?  240  GLY A CA  1 
ATOM   1630 C  C   . GLY A 1 241 ? 13.589  18.055  40.563  1.00 296.00 ?  240  GLY A C   1 
ATOM   1631 O  O   . GLY A 1 241 ? 13.995  16.899  40.432  1.00 298.73 ?  240  GLY A O   1 
ATOM   1632 N  N   . SER A 1 242 ? 12.443  18.494  40.055  1.00 258.83 ?  241  SER A N   1 
ATOM   1633 C  CA  . SER A 1 242 ? 11.505  17.683  39.305  1.00 228.46 ?  241  SER A CA  1 
ATOM   1634 C  C   . SER A 1 242 ? 10.951  18.568  38.185  1.00 192.10 ?  241  SER A C   1 
ATOM   1635 O  O   . SER A 1 242 ? 10.962  19.794  38.310  1.00 180.58 ?  241  SER A O   1 
ATOM   1636 C  CB  . SER A 1 242 ? 10.394  17.152  40.225  1.00 223.18 ?  241  SER A CB  1 
ATOM   1637 O  OG  . SER A 1 242 ? 9.744   18.205  40.913  1.00 207.96 ?  241  SER A OG  1 
ATOM   1638 N  N   . ASP A 1 243 ? 10.494  17.975  37.084  1.00 161.93 ?  242  ASP A N   1 
ATOM   1639 C  CA  . ASP A 1 243 ? 10.469  16.531  36.882  1.00 142.06 ?  242  ASP A CA  1 
ATOM   1640 C  C   . ASP A 1 243 ? 11.002  16.173  35.502  1.00 151.64 ?  242  ASP A C   1 
ATOM   1641 O  O   . ASP A 1 243 ? 10.843  16.939  34.553  1.00 163.51 ?  242  ASP A O   1 
ATOM   1642 C  CB  . ASP A 1 243 ? 9.049   15.998  37.074  1.00 139.00 ?  242  ASP A CB  1 
ATOM   1643 C  CG  . ASP A 1 243 ? 7.999   16.932  36.517  1.00 128.94 ?  242  ASP A CG  1 
ATOM   1644 O  OD1 . ASP A 1 243 ? 8.253   18.153  36.479  1.00 120.93 ?  242  ASP A OD1 1 
ATOM   1645 O  OD2 . ASP A 1 243 ? 6.903   16.456  36.162  1.00 132.59 ?  242  ASP A OD2 1 
ATOM   1646 N  N   . VAL A 1 244 ? 11.641  15.011  35.402  1.00 149.27 ?  243  VAL A N   1 
ATOM   1647 C  CA  . VAL A 1 244 ? 12.219  14.548  34.143  1.00 143.59 ?  243  VAL A CA  1 
ATOM   1648 C  C   . VAL A 1 244 ? 11.195  14.467  33.010  1.00 155.99 ?  243  VAL A C   1 
ATOM   1649 O  O   . VAL A 1 244 ? 11.546  14.669  31.852  1.00 170.91 ?  243  VAL A O   1 
ATOM   1650 C  CB  . VAL A 1 244 ? 12.902  13.175  34.308  1.00 134.57 ?  243  VAL A CB  1 
ATOM   1651 C  CG1 . VAL A 1 244 ? 14.162  13.298  35.152  1.00 141.30 ?  243  VAL A CG1 1 
ATOM   1652 C  CG2 . VAL A 1 244 ? 11.927  12.164  34.912  1.00 134.68 ?  243  VAL A CG2 1 
ATOM   1653 N  N   . GLY A 1 245 ? 9.939   14.170  33.338  1.00 149.52 ?  244  GLY A N   1 
ATOM   1654 C  CA  . GLY A 1 245 ? 8.876   14.127  32.344  1.00 147.40 ?  244  GLY A CA  1 
ATOM   1655 C  C   . GLY A 1 245 ? 8.665   15.453  31.629  1.00 145.17 ?  244  GLY A C   1 
ATOM   1656 O  O   . GLY A 1 245 ? 8.612   15.505  30.398  1.00 139.26 ?  244  GLY A O   1 
ATOM   1657 N  N   . MET A 1 246 ? 8.534   16.524  32.407  1.00 143.34 ?  245  MET A N   1 
ATOM   1658 C  CA  . MET A 1 246 ? 8.400   17.875  31.866  1.00 132.83 ?  245  MET A CA  1 
ATOM   1659 C  C   . MET A 1 246 ? 9.672   18.287  31.139  1.00 113.17 ?  245  MET A C   1 
ATOM   1660 O  O   . MET A 1 246 ? 9.625   18.925  30.089  1.00 114.00 ?  245  MET A O   1 
ATOM   1661 C  CB  . MET A 1 246 ? 8.092   18.882  32.974  1.00 141.26 ?  245  MET A CB  1 
ATOM   1662 C  CG  . MET A 1 246 ? 8.178   20.336  32.523  1.00 141.41 ?  245  MET A CG  1 
ATOM   1663 S  SD  . MET A 1 246 ? 7.988   21.533  33.861  1.00 272.19 ?  245  MET A SD  1 
ATOM   1664 C  CE  . MET A 1 246 ? 9.391   21.127  34.900  1.00 126.82 ?  245  MET A CE  1 
ATOM   1665 N  N   . LEU A 1 247 ? 10.809  17.925  31.723  1.00 100.23 ?  246  LEU A N   1 
ATOM   1666 C  CA  . LEU A 1 247 ? 12.118  18.246  31.164  1.00 103.27 ?  246  LEU A CA  1 
ATOM   1667 C  C   . LEU A 1 247 ? 12.368  17.628  29.791  1.00 99.53  ?  246  LEU A C   1 
ATOM   1668 O  O   . LEU A 1 247 ? 12.860  18.306  28.896  1.00 91.62  ?  246  LEU A O   1 
ATOM   1669 C  CB  . LEU A 1 247 ? 13.227  17.825  32.128  1.00 108.65 ?  246  LEU A CB  1 
ATOM   1670 C  CG  . LEU A 1 247 ? 13.736  18.872  33.124  1.00 106.13 ?  246  LEU A CG  1 
ATOM   1671 C  CD1 . LEU A 1 247 ? 12.609  19.570  33.878  1.00 99.90  ?  246  LEU A CD1 1 
ATOM   1672 C  CD2 . LEU A 1 247 ? 14.718  18.234  34.092  1.00 116.93 ?  246  LEU A CD2 1 
ATOM   1673 N  N   . ARG A 1 248 ? 12.073  16.342  29.627  1.00 116.37 ?  247  ARG A N   1 
ATOM   1674 C  CA  . ARG A 1 248 ? 12.290  15.694  28.334  1.00 120.98 ?  247  ARG A CA  1 
ATOM   1675 C  C   . ARG A 1 248 ? 11.387  16.310  27.264  1.00 114.48 ?  247  ARG A C   1 
ATOM   1676 O  O   . ARG A 1 248 ? 11.794  16.477  26.115  1.00 105.46 ?  247  ARG A O   1 
ATOM   1677 C  CB  . ARG A 1 248 ? 12.045  14.182  28.422  1.00 120.34 ?  247  ARG A CB  1 
ATOM   1678 C  CG  . ARG A 1 248 ? 13.141  13.408  29.141  1.00 118.19 ?  247  ARG A CG  1 
ATOM   1679 C  CD  . ARG A 1 248 ? 12.818  11.924  29.215  1.00 122.77 ?  247  ARG A CD  1 
ATOM   1680 N  NE  . ARG A 1 248 ? 12.762  11.306  27.893  1.00 138.90 ?  247  ARG A NE  1 
ATOM   1681 C  CZ  . ARG A 1 248 ? 12.337  10.066  27.660  1.00 153.93 ?  247  ARG A CZ  1 
ATOM   1682 N  NH1 . ARG A 1 248 ? 11.923  9.305   28.664  1.00 156.03 ?  247  ARG A NH1 1 
ATOM   1683 N  NH2 . ARG A 1 248 ? 12.321  9.586   26.422  1.00 159.45 ?  247  ARG A NH2 1 
ATOM   1684 N  N   . GLU A 1 249 ? 10.169  16.668  27.657  1.00 114.56 ?  248  GLU A N   1 
ATOM   1685 C  CA  . GLU A 1 249 ? 9.251   17.359  26.762  1.00 108.18 ?  248  GLU A CA  1 
ATOM   1686 C  C   . GLU A 1 249 ? 9.740   18.764  26.429  1.00 115.21 ?  248  GLU A C   1 
ATOM   1687 O  O   . GLU A 1 249 ? 9.635   19.215  25.287  1.00 129.96 ?  248  GLU A O   1 
ATOM   1688 C  CB  . GLU A 1 249 ? 7.852   17.419  27.383  1.00 113.29 ?  248  GLU A CB  1 
ATOM   1689 C  CG  . GLU A 1 249 ? 6.860   18.290  26.624  1.00 128.15 ?  248  GLU A CG  1 
ATOM   1690 C  CD  . GLU A 1 249 ? 6.558   19.595  27.336  1.00 140.80 ?  248  GLU A CD  1 
ATOM   1691 O  OE1 . GLU A 1 249 ? 6.264   19.556  28.548  1.00 153.62 ?  248  GLU A OE1 1 
ATOM   1692 O  OE2 . GLU A 1 249 ? 6.602   20.658  26.682  1.00 140.28 ?  248  GLU A OE2 1 
ATOM   1693 N  N   . ALA A 1 250 ? 10.289  19.448  27.429  1.00 112.17 ?  249  ALA A N   1 
ATOM   1694 C  CA  . ALA A 1 250 ? 10.810  20.796  27.236  1.00 93.21  ?  249  ALA A CA  1 
ATOM   1695 C  C   . ALA A 1 250 ? 12.153  20.805  26.510  1.00 95.38  ?  249  ALA A C   1 
ATOM   1696 O  O   . ALA A 1 250 ? 12.421  21.712  25.722  1.00 107.12 ?  249  ALA A O   1 
ATOM   1697 C  CB  . ALA A 1 250 ? 10.932  21.511  28.574  1.00 93.68  ?  249  ALA A CB  1 
ATOM   1698 N  N   . VAL A 1 251 ? 13.000  19.811  26.775  1.00 102.97 ?  250  VAL A N   1 
ATOM   1699 C  CA  . VAL A 1 251 ? 14.284  19.726  26.079  1.00 94.24  ?  250  VAL A CA  1 
ATOM   1700 C  C   . VAL A 1 251 ? 14.050  19.459  24.599  1.00 102.79 ?  250  VAL A C   1 
ATOM   1701 O  O   . VAL A 1 251 ? 14.754  20.000  23.759  1.00 109.04 ?  250  VAL A O   1 
ATOM   1702 C  CB  . VAL A 1 251 ? 15.247  18.648  26.673  1.00 120.68 ?  250  VAL A CB  1 
ATOM   1703 C  CG1 . VAL A 1 251 ? 14.769  17.238  26.398  1.00 136.74 ?  250  VAL A CG1 1 
ATOM   1704 C  CG2 . VAL A 1 251 ? 16.650  18.826  26.105  1.00 97.22  ?  250  VAL A CG2 1 
ATOM   1705 N  N   . LEU A 1 252 ? 13.060  18.628  24.288  1.00 108.00 ?  251  LEU A N   1 
ATOM   1706 C  CA  . LEU A 1 252 ? 12.747  18.279  22.910  1.00 111.89 ?  251  LEU A CA  1 
ATOM   1707 C  C   . LEU A 1 252 ? 12.303  19.490  22.102  1.00 108.81 ?  251  LEU A C   1 
ATOM   1708 O  O   . LEU A 1 252 ? 12.734  19.678  20.965  1.00 104.69 ?  251  LEU A O   1 
ATOM   1709 C  CB  . LEU A 1 252 ? 11.658  17.205  22.869  1.00 124.69 ?  251  LEU A CB  1 
ATOM   1710 C  CG  . LEU A 1 252 ? 11.295  16.637  21.496  1.00 93.57  ?  251  LEU A CG  1 
ATOM   1711 C  CD1 . LEU A 1 252 ? 12.454  15.831  20.922  1.00 92.08  ?  251  LEU A CD1 1 
ATOM   1712 C  CD2 . LEU A 1 252 ? 10.040  15.791  21.590  1.00 97.45  ?  251  LEU A CD2 1 
ATOM   1713 N  N   . ASN A 1 253 ? 11.472  20.328  22.713  1.00 101.05 ?  252  ASN A N   1 
ATOM   1714 C  CA  . ASN A 1 253 ? 10.822  21.428  22.008  1.00 102.34 ?  252  ASN A CA  1 
ATOM   1715 C  C   . ASN A 1 253 ? 11.845  22.463  21.523  1.00 107.94 ?  252  ASN A C   1 
ATOM   1716 O  O   . ASN A 1 253 ? 11.625  23.151  20.529  1.00 110.82 ?  252  ASN A O   1 
ATOM   1717 C  CB  . ASN A 1 253 ? 9.784   22.080  22.927  1.00 103.21 ?  252  ASN A CB  1 
ATOM   1718 C  CG  . ASN A 1 253 ? 8.825   23.003  22.193  1.00 109.64 ?  252  ASN A CG  1 
ATOM   1719 O  OD1 . ASN A 1 253 ? 9.076   23.432  21.071  1.00 111.30 ?  252  ASN A OD1 1 
ATOM   1720 N  ND2 . ASN A 1 253 ? 7.711   23.319  22.843  1.00 116.62 ?  252  ASN A ND2 1 
ATOM   1721 N  N   . ASN A 1 254 ? 12.981  22.543  22.207  1.00 127.85 ?  253  ASN A N   1 
ATOM   1722 C  CA  . ASN A 1 254 ? 13.998  23.541  21.889  1.00 139.58 ?  253  ASN A CA  1 
ATOM   1723 C  C   . ASN A 1 254 ? 15.101  22.985  20.987  1.00 133.39 ?  253  ASN A C   1 
ATOM   1724 O  O   . ASN A 1 254 ? 16.190  23.558  20.892  1.00 132.62 ?  253  ASN A O   1 
ATOM   1725 C  CB  . ASN A 1 254 ? 14.610  24.092  23.176  1.00 143.57 ?  253  ASN A CB  1 
ATOM   1726 C  CG  . ASN A 1 254 ? 13.617  24.884  23.997  1.00 148.70 ?  253  ASN A CG  1 
ATOM   1727 O  OD1 . ASN A 1 254 ? 12.709  25.513  23.455  1.00 150.33 ?  253  ASN A OD1 1 
ATOM   1728 N  ND2 . ASN A 1 254 ? 13.780  24.854  25.314  1.00 149.45 ?  253  ASN A ND2 1 
ATOM   1729 N  N   . GLY A 1 255 ? 14.808  21.885  20.301  1.00 137.80 ?  254  GLY A N   1 
ATOM   1730 C  CA  . GLY A 1 255 ? 15.832  21.183  19.552  1.00 117.58 ?  254  GLY A CA  1 
ATOM   1731 C  C   . GLY A 1 255 ? 16.382  20.084  20.434  1.00 117.18 ?  254  GLY A C   1 
ATOM   1732 O  O   . GLY A 1 255 ? 15.784  19.749  21.443  1.00 115.21 ?  254  GLY A O   1 
ATOM   1733 N  N   . GLY A 1 256 ? 17.488  19.477  20.030  1.00 127.16 ?  255  GLY A N   1 
ATOM   1734 C  CA  . GLY A 1 256 ? 18.119  18.455  20.844  1.00 129.39 ?  255  GLY A CA  1 
ATOM   1735 C  C   . GLY A 1 256 ? 18.768  19.003  22.103  1.00 129.92 ?  255  GLY A C   1 
ATOM   1736 O  O   . GLY A 1 256 ? 18.814  18.334  23.135  1.00 132.85 ?  255  GLY A O   1 
ATOM   1737 N  N   . GLY A 1 257 ? 19.256  20.235  22.008  1.00 132.72 ?  256  GLY A N   1 
ATOM   1738 C  CA  . GLY A 1 257 ? 20.231  20.789  22.937  1.00 129.29 ?  256  GLY A CA  1 
ATOM   1739 C  C   . GLY A 1 257 ? 19.929  21.108  24.393  1.00 116.42 ?  256  GLY A C   1 
ATOM   1740 O  O   . GLY A 1 257 ? 20.766  20.838  25.252  1.00 116.14 ?  256  GLY A O   1 
ATOM   1741 N  N   . TRP A 1 258 ? 18.779  21.702  24.692  1.00 110.11 ?  257  TRP A N   1 
ATOM   1742 C  CA  . TRP A 1 258 ? 18.634  22.329  26.002  1.00 104.73 ?  257  TRP A CA  1 
ATOM   1743 C  C   . TRP A 1 258 ? 17.204  22.496  26.511  1.00 112.88 ?  257  TRP A C   1 
ATOM   1744 O  O   . TRP A 1 258 ? 16.249  22.493  25.735  1.00 111.17 ?  257  TRP A O   1 
ATOM   1745 C  CB  . TRP A 1 258 ? 19.300  23.699  25.967  1.00 112.28 ?  257  TRP A CB  1 
ATOM   1746 C  CG  . TRP A 1 258 ? 18.701  24.591  24.928  1.00 127.93 ?  257  TRP A CG  1 
ATOM   1747 C  CD1 . TRP A 1 258 ? 18.961  24.580  23.588  1.00 129.89 ?  257  TRP A CD1 1 
ATOM   1748 C  CD2 . TRP A 1 258 ? 17.729  25.619  25.139  1.00 136.68 ?  257  TRP A CD2 1 
ATOM   1749 N  NE1 . TRP A 1 258 ? 18.216  25.541  22.954  1.00 133.06 ?  257  TRP A NE1 1 
ATOM   1750 C  CE2 . TRP A 1 258 ? 17.450  26.195  23.885  1.00 139.99 ?  257  TRP A CE2 1 
ATOM   1751 C  CE3 . TRP A 1 258 ? 17.070  26.113  26.268  1.00 144.52 ?  257  TRP A CE3 1 
ATOM   1752 C  CZ2 . TRP A 1 258 ? 16.543  27.237  23.727  1.00 151.59 ?  257  TRP A CZ2 1 
ATOM   1753 C  CZ3 . TRP A 1 258 ? 16.169  27.148  26.111  1.00 147.54 ?  257  TRP A CZ3 1 
ATOM   1754 C  CH2 . TRP A 1 258 ? 15.913  27.700  24.850  1.00 149.50 ?  257  TRP A CH2 1 
ATOM   1755 N  N   . HIS A 1 259 ? 17.082  22.666  27.828  1.00 120.59 ?  258  HIS A N   1 
ATOM   1756 C  CA  . HIS A 1 259 ? 15.826  23.050  28.466  1.00 123.97 ?  258  HIS A CA  1 
ATOM   1757 C  C   . HIS A 1 259 ? 16.040  24.339  29.261  1.00 115.95 ?  258  HIS A C   1 
ATOM   1758 O  O   . HIS A 1 259 ? 17.067  24.511  29.917  1.00 107.72 ?  258  HIS A O   1 
ATOM   1759 C  CB  . HIS A 1 259 ? 15.308  21.932  29.377  1.00 132.01 ?  258  HIS A CB  1 
ATOM   1760 C  CG  . HIS A 1 259 ? 16.146  21.707  30.598  1.00 134.81 ?  258  HIS A CG  1 
ATOM   1761 N  ND1 . HIS A 1 259 ? 16.078  22.524  31.707  1.00 135.00 ?  258  HIS A ND1 1 
ATOM   1762 C  CD2 . HIS A 1 259 ? 17.077  20.766  30.880  1.00 126.79 ?  258  HIS A CD2 1 
ATOM   1763 C  CE1 . HIS A 1 259 ? 16.924  22.090  32.623  1.00 128.60 ?  258  HIS A CE1 1 
ATOM   1764 N  NE2 . HIS A 1 259 ? 17.545  21.026  32.146  1.00 123.15 ?  258  HIS A NE2 1 
ATOM   1765 N  N   . GLY A 1 260 ? 15.068  25.240  29.197  1.00 120.14 ?  259  GLY A N   1 
ATOM   1766 C  CA  . GLY A 1 260 ? 15.213  26.562  29.776  1.00 134.05 ?  259  GLY A CA  1 
ATOM   1767 C  C   . GLY A 1 260 ? 15.037  26.665  31.281  1.00 145.53 ?  259  GLY A C   1 
ATOM   1768 O  O   . GLY A 1 260 ? 15.556  27.589  31.905  1.00 146.39 ?  259  GLY A O   1 
ATOM   1769 N  N   . HIS A 1 261 ? 14.308  25.716  31.860  1.00 153.71 ?  260  HIS A N   1 
ATOM   1770 C  CA  . HIS A 1 261 ? 13.740  25.873  33.201  1.00 154.64 ?  260  HIS A CA  1 
ATOM   1771 C  C   . HIS A 1 261 ? 14.733  26.142  34.339  1.00 134.61 ?  260  HIS A C   1 
ATOM   1772 O  O   . HIS A 1 261 ? 14.416  26.897  35.256  1.00 133.78 ?  260  HIS A O   1 
ATOM   1773 C  CB  . HIS A 1 261 ? 12.899  24.641  33.538  1.00 163.37 ?  260  HIS A CB  1 
ATOM   1774 C  CG  . HIS A 1 261 ? 11.605  24.575  32.784  1.00 170.68 ?  260  HIS A CG  1 
ATOM   1775 N  ND1 . HIS A 1 261 ? 11.071  23.393  32.319  1.00 174.05 ?  260  HIS A ND1 1 
ATOM   1776 C  CD2 . HIS A 1 261 ? 10.738  25.549  32.418  1.00 173.84 ?  260  HIS A CD2 1 
ATOM   1777 C  CE1 . HIS A 1 261 ? 9.932   23.641  31.697  1.00 176.07 ?  260  HIS A CE1 1 
ATOM   1778 N  NE2 . HIS A 1 261 ? 9.706   24.941  31.743  1.00 176.47 ?  260  HIS A NE2 1 
ATOM   1779 N  N   . GLY A 1 262 ? 15.916  25.537  34.304  1.00 123.38 ?  261  GLY A N   1 
ATOM   1780 C  CA  . GLY A 1 262 ? 16.898  25.823  35.338  1.00 119.55 ?  261  GLY A CA  1 
ATOM   1781 C  C   . GLY A 1 262 ? 17.847  24.699  35.709  1.00 124.37 ?  261  GLY A C   1 
ATOM   1782 O  O   . GLY A 1 262 ? 18.269  23.917  34.858  1.00 122.12 ?  261  GLY A O   1 
ATOM   1783 N  N   . TRP A 1 263 ? 18.211  24.656  36.989  1.00 129.98 ?  262  TRP A N   1 
ATOM   1784 C  CA  . TRP A 1 263 ? 19.106  23.638  37.535  1.00 132.01 ?  262  TRP A CA  1 
ATOM   1785 C  C   . TRP A 1 263 ? 18.363  22.357  37.896  1.00 143.43 ?  262  TRP A C   1 
ATOM   1786 O  O   . TRP A 1 263 ? 17.168  22.380  38.198  1.00 148.56 ?  262  TRP A O   1 
ATOM   1787 C  CB  . TRP A 1 263 ? 19.821  24.155  38.781  1.00 132.12 ?  262  TRP A CB  1 
ATOM   1788 C  CG  . TRP A 1 263 ? 20.646  25.376  38.569  1.00 127.24 ?  262  TRP A CG  1 
ATOM   1789 C  CD1 . TRP A 1 263 ? 20.263  26.671  38.765  1.00 132.29 ?  262  TRP A CD1 1 
ATOM   1790 C  CD2 . TRP A 1 263 ? 22.009  25.420  38.132  1.00 118.07 ?  262  TRP A CD2 1 
ATOM   1791 N  NE1 . TRP A 1 263 ? 21.306  27.520  38.472  1.00 129.07 ?  262  TRP A NE1 1 
ATOM   1792 C  CE2 . TRP A 1 263 ? 22.388  26.777  38.081  1.00 125.59 ?  262  TRP A CE2 1 
ATOM   1793 C  CE3 . TRP A 1 263 ? 22.945  24.444  37.776  1.00 107.83 ?  262  TRP A CE3 1 
ATOM   1794 C  CZ2 . TRP A 1 263 ? 23.664  27.180  37.687  1.00 115.22 ?  262  TRP A CZ2 1 
ATOM   1795 C  CZ3 . TRP A 1 263 ? 24.210  24.847  37.385  1.00 104.20 ?  262  TRP A CZ3 1 
ATOM   1796 C  CH2 . TRP A 1 263 ? 24.558  26.203  37.343  1.00 105.34 ?  262  TRP A CH2 1 
ATOM   1797 N  N   . VAL A 1 264 ? 19.077  21.237  37.870  1.00 150.30 ?  263  VAL A N   1 
ATOM   1798 C  CA  . VAL A 1 264 ? 18.469  19.952  38.184  1.00 162.29 ?  263  VAL A CA  1 
ATOM   1799 C  C   . VAL A 1 264 ? 19.259  19.184  39.247  1.00 162.73 ?  263  VAL A C   1 
ATOM   1800 O  O   . VAL A 1 264 ? 20.491  19.229  39.283  1.00 151.25 ?  263  VAL A O   1 
ATOM   1801 C  CB  . VAL A 1 264 ? 18.328  19.084  36.915  1.00 170.98 ?  263  VAL A CB  1 
ATOM   1802 C  CG1 . VAL A 1 264 ? 19.689  18.754  36.341  1.00 172.78 ?  263  VAL A CG1 1 
ATOM   1803 C  CG2 . VAL A 1 264 ? 17.543  17.813  37.213  1.00 178.12 ?  263  VAL A CG2 1 
ATOM   1804 N  N   . GLY A 1 265 ? 18.532  18.505  40.129  1.00 175.23 ?  264  GLY A N   1 
ATOM   1805 C  CA  . GLY A 1 265 ? 19.124  17.548  41.042  1.00 173.67 ?  264  GLY A CA  1 
ATOM   1806 C  C   . GLY A 1 265 ? 19.774  18.159  42.261  1.00 162.39 ?  264  GLY A C   1 
ATOM   1807 O  O   . GLY A 1 265 ? 19.663  19.356  42.511  1.00 145.98 ?  264  GLY A O   1 
ATOM   1808 N  N   . GLU A 1 266 ? 20.452  17.313  43.027  1.00 165.84 ?  265  GLU A N   1 
ATOM   1809 C  CA  . GLU A 1 266 ? 21.113  17.739  44.251  1.00 170.58 ?  265  GLU A CA  1 
ATOM   1810 C  C   . GLU A 1 266 ? 22.544  17.218  44.311  1.00 158.30 ?  265  GLU A C   1 
ATOM   1811 O  O   . GLU A 1 266 ? 22.889  16.238  43.646  1.00 151.06 ?  265  GLU A O   1 
ATOM   1812 C  CB  . GLU A 1 266 ? 20.327  17.254  45.468  1.00 179.03 ?  265  GLU A CB  1 
ATOM   1813 C  CG  . GLU A 1 266 ? 18.893  17.750  45.510  1.00 170.77 ?  265  GLU A CG  1 
ATOM   1814 C  CD  . GLU A 1 266 ? 18.038  16.956  46.466  1.00 168.56 ?  265  GLU A CD  1 
ATOM   1815 O  OE1 . GLU A 1 266 ? 18.575  16.034  47.113  1.00 172.63 ?  265  GLU A OE1 1 
ATOM   1816 O  OE2 . GLU A 1 266 ? 16.827  17.244  46.555  1.00 170.72 ?  265  GLU A OE2 1 
ATOM   1817 N  N   . GLY A 1 267 ? 23.367  17.867  45.125  1.00 148.12 ?  266  GLY A N   1 
ATOM   1818 C  CA  . GLY A 1 267 ? 24.703  17.377  45.397  1.00 142.85 ?  266  GLY A CA  1 
ATOM   1819 C  C   . GLY A 1 267 ? 25.801  18.077  44.630  1.00 131.40 ?  266  GLY A C   1 
ATOM   1820 O  O   . GLY A 1 267 ? 25.566  19.078  43.958  1.00 140.71 ?  266  GLY A O   1 
ATOM   1821 N  N   . LYS A 1 268 ? 27.008  17.532  44.730  1.00 122.47 ?  267  LYS A N   1 
ATOM   1822 C  CA  . LYS A 1 268 ? 28.186  18.123  44.107  1.00 113.65 ?  267  LYS A CA  1 
ATOM   1823 C  C   . LYS A 1 268 ? 28.420  17.610  42.691  1.00 106.16 ?  267  LYS A C   1 
ATOM   1824 O  O   . LYS A 1 268 ? 27.898  16.563  42.309  1.00 99.57  ?  267  LYS A O   1 
ATOM   1825 C  CB  . LYS A 1 268 ? 29.417  17.853  44.970  1.00 121.46 ?  267  LYS A CB  1 
ATOM   1826 C  CG  . LYS A 1 268 ? 29.327  18.470  46.363  1.00 149.19 ?  267  LYS A CG  1 
ATOM   1827 C  CD  . LYS A 1 268 ? 30.462  18.021  47.278  1.00 161.62 ?  267  LYS A CD  1 
ATOM   1828 C  CE  . LYS A 1 268 ? 31.813  18.558  46.827  1.00 154.79 ?  267  LYS A CE  1 
ATOM   1829 N  NZ  . LYS A 1 268 ? 32.469  17.696  45.801  1.00 156.92 ?  267  LYS A NZ  1 
ATOM   1830 N  N   . TRP A 1 269 ? 29.195  18.373  41.918  1.00 117.93 ?  268  TRP A N   1 
ATOM   1831 C  CA  . TRP A 1 269 ? 29.503  18.044  40.524  1.00 116.87 ?  268  TRP A CA  1 
ATOM   1832 C  C   . TRP A 1 269 ? 30.685  17.098  40.357  1.00 115.54 ?  268  TRP A C   1 
ATOM   1833 O  O   . TRP A 1 269 ? 31.644  17.146  41.125  1.00 125.81 ?  268  TRP A O   1 
ATOM   1834 C  CB  . TRP A 1 269 ? 29.806  19.312  39.727  1.00 113.69 ?  268  TRP A CB  1 
ATOM   1835 C  CG  . TRP A 1 269 ? 28.655  20.244  39.571  1.00 124.22 ?  268  TRP A CG  1 
ATOM   1836 C  CD1 . TRP A 1 269 ? 28.511  21.473  40.144  1.00 131.59 ?  268  TRP A CD1 1 
ATOM   1837 C  CD2 . TRP A 1 269 ? 27.462  20.010  38.809  1.00 131.63 ?  268  TRP A CD2 1 
ATOM   1838 N  NE1 . TRP A 1 269 ? 27.310  22.028  39.770  1.00 132.96 ?  268  TRP A NE1 1 
ATOM   1839 C  CE2 . TRP A 1 269 ? 26.651  21.152  38.960  1.00 137.33 ?  268  TRP A CE2 1 
ATOM   1840 C  CE3 . TRP A 1 269 ? 27.011  18.951  38.021  1.00 123.64 ?  268  TRP A CE3 1 
ATOM   1841 C  CZ2 . TRP A 1 269 ? 25.407  21.260  38.331  1.00 134.08 ?  268  TRP A CZ2 1 
ATOM   1842 C  CZ3 . TRP A 1 269 ? 25.774  19.063  37.410  1.00 119.32 ?  268  TRP A CZ3 1 
ATOM   1843 C  CH2 . TRP A 1 269 ? 24.988  20.208  37.568  1.00 122.78 ?  268  TRP A CH2 1 
ATOM   1844 N  N   . THR A 1 270 ? 30.608  16.248  39.339  1.00 119.13 ?  269  THR A N   1 
ATOM   1845 C  CA  . THR A 1 270 ? 31.732  15.412  38.931  1.00 138.19 ?  269  THR A CA  1 
ATOM   1846 C  C   . THR A 1 270 ? 32.130  15.790  37.505  1.00 137.48 ?  269  THR A C   1 
ATOM   1847 O  O   . THR A 1 270 ? 31.296  15.772  36.600  1.00 137.69 ?  269  THR A O   1 
ATOM   1848 C  CB  . THR A 1 270 ? 31.399  13.906  39.013  1.00 141.55 ?  269  THR A CB  1 
ATOM   1849 O  OG1 . THR A 1 270 ? 30.359  13.590  38.082  1.00 146.94 ?  269  THR A OG1 1 
ATOM   1850 C  CG2 . THR A 1 270 ? 30.943  13.527  40.417  1.00 136.21 ?  269  THR A CG2 1 
ATOM   1851 N  N   . VAL A 1 271 ? 33.402  16.122  37.302  1.00 136.61 ?  270  VAL A N   1 
ATOM   1852 C  CA  . VAL A 1 271 ? 33.872  16.614  36.004  1.00 142.30 ?  270  VAL A CA  1 
ATOM   1853 C  C   . VAL A 1 271 ? 34.750  15.594  35.271  1.00 159.23 ?  270  VAL A C   1 
ATOM   1854 O  O   . VAL A 1 271 ? 35.721  15.081  35.823  1.00 175.75 ?  270  VAL A O   1 
ATOM   1855 C  CB  . VAL A 1 271 ? 34.659  17.943  36.157  1.00 102.23 ?  270  VAL A CB  1 
ATOM   1856 C  CG1 . VAL A 1 271 ? 35.648  17.861  37.316  1.00 125.46 ?  270  VAL A CG1 1 
ATOM   1857 C  CG2 . VAL A 1 271 ? 35.368  18.308  34.861  1.00 92.02  ?  270  VAL A CG2 1 
ATOM   1858 N  N   . LYS A 1 272 ? 34.396  15.301  34.022  1.00 160.81 ?  271  LYS A N   1 
ATOM   1859 C  CA  . LYS A 1 272 ? 35.174  14.377  33.200  1.00 157.24 ?  271  LYS A CA  1 
ATOM   1860 C  C   . LYS A 1 272 ? 35.460  14.961  31.809  1.00 158.86 ?  271  LYS A C   1 
ATOM   1861 O  O   . LYS A 1 272 ? 34.573  15.525  31.170  1.00 161.79 ?  271  LYS A O   1 
ATOM   1862 C  CB  . LYS A 1 272 ? 34.426  13.044  33.063  1.00 147.62 ?  271  LYS A CB  1 
ATOM   1863 C  CG  . LYS A 1 272 ? 34.424  12.178  34.321  1.00 150.98 ?  271  LYS A CG  1 
ATOM   1864 C  CD  . LYS A 1 272 ? 33.409  11.039  34.210  1.00 148.92 ?  271  LYS A CD  1 
ATOM   1865 C  CE  . LYS A 1 272 ? 33.335  10.209  35.487  1.00 142.84 ?  271  LYS A CE  1 
ATOM   1866 N  NZ  . LYS A 1 272 ? 32.308  9.129   35.412  1.00 129.32 ?  271  LYS A NZ  1 
ATOM   1867 N  N   . LYS A 1 273 ? 36.705  14.834  31.353  1.00 156.98 ?  272  LYS A N   1 
ATOM   1868 C  CA  . LYS A 1 273 ? 37.095  15.258  30.005  1.00 148.47 ?  272  LYS A CA  1 
ATOM   1869 C  C   . LYS A 1 273 ? 37.384  14.038  29.124  1.00 154.75 ?  272  LYS A C   1 
ATOM   1870 O  O   . LYS A 1 273 ? 38.345  13.307  29.370  1.00 153.80 ?  272  LYS A O   1 
ATOM   1871 C  CB  . LYS A 1 273 ? 38.318  16.185  30.053  1.00 136.12 ?  272  LYS A CB  1 
ATOM   1872 C  CG  . LYS A 1 273 ? 38.154  17.395  30.971  1.00 126.79 ?  272  LYS A CG  1 
ATOM   1873 C  CD  . LYS A 1 273 ? 39.446  18.207  31.096  1.00 127.74 ?  272  LYS A CD  1 
ATOM   1874 C  CE  . LYS A 1 273 ? 40.625  17.360  31.585  1.00 136.37 ?  272  LYS A CE  1 
ATOM   1875 N  NZ  . LYS A 1 273 ? 40.473  16.834  32.976  1.00 134.52 ?  272  LYS A NZ  1 
ATOM   1876 N  N   . GLY A 1 274 ? 36.559  13.819  28.102  1.00 160.43 ?  273  GLY A N   1 
ATOM   1877 C  CA  . GLY A 1 274 ? 36.645  12.603  27.310  1.00 166.51 ?  273  GLY A CA  1 
ATOM   1878 C  C   . GLY A 1 274 ? 36.252  12.745  25.850  1.00 166.48 ?  273  GLY A C   1 
ATOM   1879 O  O   . GLY A 1 274 ? 35.568  13.691  25.472  1.00 165.21 ?  273  GLY A O   1 
ATOM   1880 N  N   . ASN A 1 275 ? 36.699  11.802  25.026  1.00 173.16 ?  274  ASN A N   1 
ATOM   1881 C  CA  . ASN A 1 275 ? 36.238  11.703  23.645  1.00 170.57 ?  274  ASN A CA  1 
ATOM   1882 C  C   . ASN A 1 275 ? 34.816  11.148  23.583  1.00 174.96 ?  274  ASN A C   1 
ATOM   1883 O  O   . ASN A 1 275 ? 34.241  10.787  24.608  1.00 173.40 ?  274  ASN A O   1 
ATOM   1884 C  CB  . ASN A 1 275 ? 37.180  10.819  22.823  1.00 161.98 ?  274  ASN A CB  1 
ATOM   1885 C  CG  . ASN A 1 275 ? 38.438  11.547  22.390  1.00 160.04 ?  274  ASN A CG  1 
ATOM   1886 O  OD1 . ASN A 1 275 ? 38.593  11.906  21.220  1.00 157.62 ?  274  ASN A OD1 1 
ATOM   1887 N  ND2 . ASN A 1 275 ? 39.340  11.781  23.336  1.00 163.46 ?  274  ASN A ND2 1 
ATOM   1888 N  N   . VAL A 1 276 ? 34.256  11.066  22.379  1.00 173.49 ?  275  VAL A N   1 
ATOM   1889 C  CA  . VAL A 1 276 ? 32.919  10.508  22.202  1.00 172.69 ?  275  VAL A CA  1 
ATOM   1890 C  C   . VAL A 1 276 ? 32.895  9.454   21.101  1.00 189.05 ?  275  VAL A C   1 
ATOM   1891 O  O   . VAL A 1 276 ? 33.742  9.453   20.204  1.00 199.71 ?  275  VAL A O   1 
ATOM   1892 C  CB  . VAL A 1 276 ? 31.881  11.599  21.865  1.00 162.07 ?  275  VAL A CB  1 
ATOM   1893 C  CG1 . VAL A 1 276 ? 31.604  12.473  23.076  1.00 155.23 ?  275  VAL A CG1 1 
ATOM   1894 C  CG2 . VAL A 1 276 ? 32.351  12.434  20.684  1.00 162.93 ?  275  VAL A CG2 1 
ATOM   1895 N  N   . SER A 1 277 ? 31.908  8.567   21.174  1.00 208.02 ?  276  SER A N   1 
ATOM   1896 C  CA  . SER A 1 277 ? 31.788  7.457   20.233  1.00 216.36 ?  276  SER A CA  1 
ATOM   1897 C  C   . SER A 1 277 ? 31.360  7.910   18.844  1.00 209.44 ?  276  SER A C   1 
ATOM   1898 O  O   . SER A 1 277 ? 30.975  9.062   18.638  1.00 211.20 ?  276  SER A O   1 
ATOM   1899 C  CB  . SER A 1 277 ? 30.795  6.415   20.753  1.00 222.72 ?  276  SER A CB  1 
ATOM   1900 O  OG  . SER A 1 277 ? 29.460  6.867   20.615  1.00 223.29 ?  276  SER A OG  1 
ATOM   1901 N  N   . SER A 1 278 ? 31.449  6.989   17.892  1.00 200.87 ?  277  SER A N   1 
ATOM   1902 C  CA  . SER A 1 278 ? 30.908  7.194   16.557  1.00 187.40 ?  277  SER A CA  1 
ATOM   1903 C  C   . SER A 1 278 ? 29.394  7.389   16.617  1.00 179.12 ?  277  SER A C   1 
ATOM   1904 O  O   . SER A 1 278 ? 28.838  8.204   15.883  1.00 170.75 ?  277  SER A O   1 
ATOM   1905 C  CB  . SER A 1 278 ? 31.265  6.014   15.653  1.00 190.98 ?  277  SER A CB  1 
ATOM   1906 O  OG  . SER A 1 278 ? 32.668  5.814   15.603  1.00 194.02 ?  277  SER A OG  1 
ATOM   1907 N  N   . THR A 1 279 ? 28.736  6.641   17.501  1.00 179.07 ?  278  THR A N   1 
ATOM   1908 C  CA  . THR A 1 279 ? 27.303  6.805   17.742  1.00 167.73 ?  278  THR A CA  1 
ATOM   1909 C  C   . THR A 1 279 ? 27.040  8.103   18.501  1.00 163.61 ?  278  THR A C   1 
ATOM   1910 O  O   . THR A 1 279 ? 25.901  8.552   18.619  1.00 147.54 ?  278  THR A O   1 
ATOM   1911 C  CB  . THR A 1 279 ? 26.722  5.621   18.549  1.00 161.47 ?  278  THR A CB  1 
ATOM   1912 O  OG1 . THR A 1 279 ? 27.311  4.396   18.099  1.00 170.82 ?  278  THR A OG1 1 
ATOM   1913 C  CG2 . THR A 1 279 ? 25.206  5.540   18.394  1.00 159.33 ?  278  THR A CG2 1 
ATOM   1914 N  N   . GLY A 1 280 ? 28.113  8.703   19.005  1.00 186.38 ?  279  GLY A N   1 
ATOM   1915 C  CA  . GLY A 1 280 ? 28.038  9.963   19.721  1.00 198.42 ?  279  GLY A CA  1 
ATOM   1916 C  C   . GLY A 1 280 ? 27.711  9.769   21.185  1.00 197.57 ?  279  GLY A C   1 
ATOM   1917 O  O   . GLY A 1 280 ? 27.227  10.681  21.852  1.00 190.69 ?  279  GLY A O   1 
ATOM   1918 N  N   . ARG A 1 281 ? 27.999  8.574   21.687  1.00 189.53 ?  280  ARG A N   1 
ATOM   1919 C  CA  . ARG A 1 281 ? 27.819  8.258   23.096  1.00 176.84 ?  280  ARG A CA  1 
ATOM   1920 C  C   . ARG A 1 281 ? 29.032  8.736   23.884  1.00 162.72 ?  280  ARG A C   1 
ATOM   1921 O  O   . ARG A 1 281 ? 30.166  8.404   23.540  1.00 160.84 ?  280  ARG A O   1 
ATOM   1922 C  CB  . ARG A 1 281 ? 27.613  6.749   23.283  1.00 182.89 ?  280  ARG A CB  1 
ATOM   1923 C  CG  . ARG A 1 281 ? 27.094  6.325   24.652  1.00 178.16 ?  280  ARG A CG  1 
ATOM   1924 C  CD  . ARG A 1 281 ? 27.285  4.825   24.867  1.00 174.42 ?  280  ARG A CD  1 
ATOM   1925 N  NE  . ARG A 1 281 ? 28.699  4.477   24.984  1.00 175.05 ?  280  ARG A NE  1 
ATOM   1926 C  CZ  . ARG A 1 281 ? 29.251  3.933   26.063  1.00 173.80 ?  280  ARG A CZ  1 
ATOM   1927 N  NH1 . ARG A 1 281 ? 28.505  3.652   27.121  1.00 176.28 ?  280  ARG A NH1 1 
ATOM   1928 N  NH2 . ARG A 1 281 ? 30.548  3.657   26.081  1.00 170.57 ?  280  ARG A NH2 1 
ATOM   1929 N  N   . CYS A 1 282 ? 28.805  9.529   24.927  1.00 152.53 ?  281  CYS A N   1 
ATOM   1930 C  CA  . CYS A 1 282 ? 29.917  10.004  25.741  1.00 143.11 ?  281  CYS A CA  1 
ATOM   1931 C  C   . CYS A 1 282 ? 30.452  8.841   26.561  1.00 136.76 ?  281  CYS A C   1 
ATOM   1932 O  O   . CYS A 1 282 ? 29.719  8.236   27.344  1.00 132.43 ?  281  CYS A O   1 
ATOM   1933 C  CB  . CYS A 1 282 ? 29.496  11.157  26.652  1.00 151.22 ?  281  CYS A CB  1 
ATOM   1934 S  SG  . CYS A 1 282 ? 30.822  11.784  27.725  1.00 138.88 ?  281  CYS A SG  1 
ATOM   1935 N  N   . LEU A 1 283 ? 31.728  8.530   26.365  1.00 146.88 ?  282  LEU A N   1 
ATOM   1936 C  CA  . LEU A 1 283 ? 32.351  7.371   26.992  1.00 171.38 ?  282  LEU A CA  1 
ATOM   1937 C  C   . LEU A 1 283 ? 32.272  7.418   28.516  1.00 189.99 ?  282  LEU A C   1 
ATOM   1938 O  O   . LEU A 1 283 ? 32.120  6.383   29.170  1.00 216.56 ?  282  LEU A O   1 
ATOM   1939 C  CB  . LEU A 1 283 ? 33.810  7.261   26.552  1.00 169.11 ?  282  LEU A CB  1 
ATOM   1940 C  CG  . LEU A 1 283 ? 34.037  7.191   25.043  1.00 161.67 ?  282  LEU A CG  1 
ATOM   1941 C  CD1 . LEU A 1 283 ? 35.516  7.035   24.742  1.00 161.83 ?  282  LEU A CD1 1 
ATOM   1942 C  CD2 . LEU A 1 283 ? 33.233  6.052   24.426  1.00 166.58 ?  282  LEU A CD2 1 
ATOM   1943 N  N   . SER A 1 284 ? 32.370  8.622   29.070  1.00 169.79 ?  283  SER A N   1 
ATOM   1944 C  CA  . SER A 1 284 ? 32.384  8.808   30.516  1.00 157.31 ?  283  SER A CA  1 
ATOM   1945 C  C   . SER A 1 284 ? 31.054  8.481   31.204  1.00 166.67 ?  283  SER A C   1 
ATOM   1946 O  O   . SER A 1 284 ? 31.038  7.760   32.200  1.00 176.70 ?  283  SER A O   1 
ATOM   1947 C  CB  . SER A 1 284 ? 32.795  10.242  30.847  1.00 131.91 ?  283  SER A CB  1 
ATOM   1948 O  OG  . SER A 1 284 ? 31.822  11.162  30.395  1.00 127.78 ?  283  SER A OG  1 
ATOM   1949 N  N   . CYS A 1 285 ? 29.944  9.002   30.682  1.00 150.96 ?  284  CYS A N   1 
ATOM   1950 C  CA  . CYS A 1 285 ? 28.656  8.841   31.361  1.00 137.61 ?  284  CYS A CA  1 
ATOM   1951 C  C   . CYS A 1 285 ? 27.670  7.954   30.596  1.00 151.02 ?  284  CYS A C   1 
ATOM   1952 O  O   . CYS A 1 285 ? 26.533  7.771   31.031  1.00 155.98 ?  284  CYS A O   1 
ATOM   1953 C  CB  . CYS A 1 285 ? 28.011  10.205  31.633  1.00 115.97 ?  284  CYS A CB  1 
ATOM   1954 S  SG  . CYS A 1 285 ? 27.492  11.131  30.170  1.00 136.32 ?  284  CYS A SG  1 
ATOM   1955 N  N   . SER A 1 286 ? 28.104  7.425   29.454  1.00 159.54 ?  285  SER A N   1 
ATOM   1956 C  CA  . SER A 1 286 ? 27.317  6.469   28.673  1.00 170.18 ?  285  SER A CA  1 
ATOM   1957 C  C   . SER A 1 286 ? 26.012  7.038   28.121  1.00 159.56 ?  285  SER A C   1 
ATOM   1958 O  O   . SER A 1 286 ? 25.066  6.293   27.864  1.00 169.30 ?  285  SER A O   1 
ATOM   1959 C  CB  . SER A 1 286 ? 27.011  5.226   29.513  1.00 193.10 ?  285  SER A CB  1 
ATOM   1960 O  OG  . SER A 1 286 ? 28.205  4.597   29.943  1.00 205.71 ?  285  SER A OG  1 
ATOM   1961 N  N   . GLU A 1 287 ? 25.960  8.353   27.945  1.00 137.47 ?  286  GLU A N   1 
ATOM   1962 C  CA  . GLU A 1 287 ? 24.800  8.988   27.333  1.00 136.30 ?  286  GLU A CA  1 
ATOM   1963 C  C   . GLU A 1 287 ? 25.204  9.567   25.992  1.00 137.11 ?  286  GLU A C   1 
ATOM   1964 O  O   . GLU A 1 287 ? 26.288  10.138  25.863  1.00 135.94 ?  286  GLU A O   1 
ATOM   1965 C  CB  . GLU A 1 287 ? 24.216  10.081  28.227  1.00 139.00 ?  286  GLU A CB  1 
ATOM   1966 C  CG  . GLU A 1 287 ? 23.096  9.607   29.138  1.00 139.57 ?  286  GLU A CG  1 
ATOM   1967 C  CD  . GLU A 1 287 ? 23.596  9.195   30.506  1.00 146.62 ?  286  GLU A CD  1 
ATOM   1968 O  OE1 . GLU A 1 287 ? 24.592  9.786   30.974  1.00 160.77 ?  286  GLU A OE1 1 
ATOM   1969 O  OE2 . GLU A 1 287 ? 22.988  8.291   31.118  1.00 139.34 ?  286  GLU A OE2 1 
ATOM   1970 N  N   . GLN A 1 288 ? 24.361  9.391   24.981  1.00 140.73 ?  287  GLN A N   1 
ATOM   1971 C  CA  . GLN A 1 288 ? 24.691  9.942   23.676  1.00 140.97 ?  287  GLN A CA  1 
ATOM   1972 C  C   . GLN A 1 288 ? 24.140  11.344  23.434  1.00 148.08 ?  287  GLN A C   1 
ATOM   1973 O  O   . GLN A 1 288 ? 23.039  11.692  23.873  1.00 84.88  ?  287  GLN A O   1 
ATOM   1974 C  CB  . GLN A 1 288 ? 24.232  9.016   22.548  1.00 135.82 ?  287  GLN A CB  1 
ATOM   1975 C  CG  . GLN A 1 288 ? 22.741  8.839   22.423  1.00 144.42 ?  287  GLN A CG  1 
ATOM   1976 C  CD  . GLN A 1 288 ? 22.379  8.069   21.176  1.00 164.25 ?  287  GLN A CD  1 
ATOM   1977 O  OE1 . GLN A 1 288 ? 23.184  7.293   20.659  1.00 169.53 ?  287  GLN A OE1 1 
ATOM   1978 N  NE2 . GLN A 1 288 ? 21.164  8.276   20.684  1.00 176.16 ?  287  GLN A NE2 1 
ATOM   1979 N  N   . LEU A 1 289 ? 24.945  12.152  22.756  1.00 137.12 ?  288  LEU A N   1 
ATOM   1980 C  CA  . LEU A 1 289 ? 24.585  13.533  22.481  1.00 140.07 ?  288  LEU A CA  1 
ATOM   1981 C  C   . LEU A 1 289 ? 23.446  13.652  21.481  1.00 149.35 ?  288  LEU A C   1 
ATOM   1982 O  O   . LEU A 1 289 ? 23.373  12.882  20.522  1.00 171.42 ?  288  LEU A O   1 
ATOM   1983 C  CB  . LEU A 1 289 ? 25.807  14.276  21.952  1.00 140.39 ?  288  LEU A CB  1 
ATOM   1984 C  CG  . LEU A 1 289 ? 26.922  14.351  22.997  1.00 134.03 ?  288  LEU A CG  1 
ATOM   1985 C  CD1 . LEU A 1 289 ? 28.197  14.960  22.433  1.00 139.07 ?  288  LEU A CD1 1 
ATOM   1986 C  CD2 . LEU A 1 289 ? 26.438  15.133  24.189  1.00 141.07 ?  288  LEU A CD2 1 
ATOM   1987 N  N   . ALA A 1 290 ? 22.563  14.617  21.701  1.00 130.12 ?  289  ALA A N   1 
ATOM   1988 C  CA  . ALA A 1 290 ? 21.397  14.786  20.849  1.00 114.29 ?  289  ALA A CA  1 
ATOM   1989 C  C   . ALA A 1 290 ? 21.876  15.338  19.511  1.00 116.60 ?  289  ALA A C   1 
ATOM   1990 O  O   . ALA A 1 290 ? 22.975  15.882  19.407  1.00 115.98 ?  289  ALA A O   1 
ATOM   1991 C  CB  . ALA A 1 290 ? 20.328  15.687  21.444  1.00 103.91 ?  289  ALA A CB  1 
ATOM   1992 N  N   . CYS A 1 291 ? 21.057  15.156  18.482  1.00 212.25 ?  290  CYS A N   1 
ATOM   1993 C  CA  . CYS A 1 291 ? 21.349  15.694  17.161  1.00 152.37 ?  290  CYS A CA  1 
ATOM   1994 C  C   . CYS A 1 291 ? 21.150  17.205  17.182  1.00 179.89 ?  290  CYS A C   1 
ATOM   1995 O  O   . CYS A 1 291 ? 20.214  17.699  17.810  1.00 154.91 ?  290  CYS A O   1 
ATOM   1996 C  CB  . CYS A 1 291 ? 20.456  15.046  16.096  1.00 148.06 ?  290  CYS A CB  1 
ATOM   1997 S  SG  . CYS A 1 291 ? 20.995  15.320  14.384  1.00 180.38 ?  290  CYS A SG  1 
ATOM   1998 N  N   . VAL A 1 292 ? 22.028  17.937  16.507  1.00 175.33 ?  291  VAL A N   1 
ATOM   1999 C  CA  . VAL A 1 292 ? 21.849  19.377  16.366  1.00 199.56 ?  291  VAL A CA  1 
ATOM   2000 C  C   . VAL A 1 292 ? 20.540  19.639  15.637  1.00 217.70 ?  291  VAL A C   1 
ATOM   2001 O  O   . VAL A 1 292 ? 20.237  18.990  14.643  1.00 241.93 ?  291  VAL A O   1 
ATOM   2002 C  CB  . VAL A 1 292 ? 23.028  20.040  15.599  1.00 198.79 ?  291  VAL A CB  1 
ATOM   2003 C  CG1 . VAL A 1 292 ? 23.343  19.288  14.310  1.00 190.92 ?  291  VAL A CG1 1 
ATOM   2004 C  CG2 . VAL A 1 292 ? 22.745  21.515  15.323  1.00 196.44 ?  291  VAL A CG2 1 
ATOM   2005 N  N   . ASP A 1 293 ? 19.745  20.565  16.156  1.00 209.74 ?  292  ASP A N   1 
ATOM   2006 C  CA  . ASP A 1 293 ? 18.548  20.993  15.452  1.00 200.73 ?  292  ASP A CA  1 
ATOM   2007 C  C   . ASP A 1 293 ? 18.694  22.470  15.151  1.00 192.33 ?  292  ASP A C   1 
ATOM   2008 O  O   . ASP A 1 293 ? 18.818  23.301  16.051  1.00 200.21 ?  292  ASP A O   1 
ATOM   2009 C  CB  . ASP A 1 293 ? 17.284  20.718  16.268  1.00 206.43 ?  292  ASP A CB  1 
ATOM   2010 C  CG  . ASP A 1 293 ? 16.907  19.247  16.290  1.00 202.79 ?  292  ASP A CG  1 
ATOM   2011 O  OD1 . ASP A 1 293 ? 17.382  18.494  15.413  1.00 195.66 ?  292  ASP A OD1 1 
ATOM   2012 O  OD2 . ASP A 1 293 ? 16.130  18.842  17.181  1.00 206.94 ?  292  ASP A OD2 1 
ATOM   2013 N  N   . THR A 1 294 ? 18.686  22.781  13.862  1.00 177.97 ?  293  THR A N   1 
ATOM   2014 C  CA  . THR A 1 294 ? 18.983  24.119  13.390  1.00 164.43 ?  293  THR A CA  1 
ATOM   2015 C  C   . THR A 1 294 ? 17.856  25.085  13.776  1.00 160.34 ?  293  THR A C   1 
ATOM   2016 O  O   . THR A 1 294 ? 16.683  24.709  13.795  1.00 155.18 ?  293  THR A O   1 
ATOM   2017 C  CB  . THR A 1 294 ? 19.219  24.080  11.860  1.00 150.32 ?  293  THR A CB  1 
ATOM   2018 O  OG1 . THR A 1 294 ? 20.336  23.232  11.557  1.00 135.52 ?  293  THR A OG1 1 
ATOM   2019 C  CG2 . THR A 1 294 ? 19.457  25.446  11.306  1.00 150.23 ?  293  THR A CG2 1 
ATOM   2020 N  N   . ASN A 1 295 ? 18.220  26.329  14.077  1.00 162.97 ?  294  ASN A N   1 
ATOM   2021 C  CA  . ASN A 1 295 ? 17.271  27.299  14.620  1.00 168.03 ?  294  ASN A CA  1 
ATOM   2022 C  C   . ASN A 1 295 ? 16.206  27.706  13.611  1.00 169.64 ?  294  ASN A C   1 
ATOM   2023 O  O   . ASN A 1 295 ? 16.515  28.047  12.473  1.00 170.40 ?  294  ASN A O   1 
ATOM   2024 C  CB  . ASN A 1 295 ? 18.014  28.535  15.132  1.00 181.57 ?  294  ASN A CB  1 
ATOM   2025 C  CG  . ASN A 1 295 ? 17.129  29.448  15.966  1.00 196.00 ?  294  ASN A CG  1 
ATOM   2026 O  OD1 . ASN A 1 295 ? 16.207  28.993  16.641  1.00 201.76 ?  294  ASN A OD1 1 
ATOM   2027 N  ND2 . ASN A 1 295 ? 17.406  30.747  15.918  1.00 199.38 ?  294  ASN A ND2 1 
ATOM   2028 N  N   . GLU A 1 296 ? 14.950  27.656  14.044  1.00 176.42 ?  295  GLU A N   1 
ATOM   2029 C  CA  . GLU A 1 296 ? 13.806  27.950  13.182  1.00 175.60 ?  295  GLU A CA  1 
ATOM   2030 C  C   . GLU A 1 296 ? 13.896  29.330  12.538  1.00 167.21 ?  295  GLU A C   1 
ATOM   2031 O  O   . GLU A 1 296 ? 13.746  29.458  11.324  1.00 164.99 ?  295  GLU A O   1 
ATOM   2032 C  CB  . GLU A 1 296 ? 12.501  27.823  13.968  1.00 186.60 ?  295  GLU A CB  1 
ATOM   2033 C  CG  . GLU A 1 296 ? 12.245  26.423  14.502  1.00 194.46 ?  295  GLU A CG  1 
ATOM   2034 C  CD  . GLU A 1 296 ? 12.260  25.369  13.410  1.00 191.57 ?  295  GLU A CD  1 
ATOM   2035 O  OE1 . GLU A 1 296 ? 11.753  25.647  12.303  1.00 199.54 ?  295  GLU A OE1 1 
ATOM   2036 O  OE2 . GLU A 1 296 ? 12.787  24.263  13.658  1.00 185.30 ?  295  GLU A OE2 1 
ATOM   2037 N  N   . VAL A 1 297 ? 14.127  30.359  13.349  1.00 164.23 ?  296  VAL A N   1 
ATOM   2038 C  CA  . VAL A 1 297 ? 14.234  31.723  12.833  1.00 163.60 ?  296  VAL A CA  1 
ATOM   2039 C  C   . VAL A 1 297 ? 15.387  31.799  11.838  1.00 174.26 ?  296  VAL A C   1 
ATOM   2040 O  O   . VAL A 1 297 ? 15.342  32.563  10.876  1.00 182.79 ?  296  VAL A O   1 
ATOM   2041 C  CB  . VAL A 1 297 ? 14.428  32.765  13.963  1.00 170.34 ?  296  VAL A CB  1 
ATOM   2042 C  CG1 . VAL A 1 297 ? 15.726  32.525  14.721  1.00 169.95 ?  296  VAL A CG1 1 
ATOM   2043 C  CG2 . VAL A 1 297 ? 14.392  34.178  13.401  1.00 168.79 ?  296  VAL A CG2 1 
ATOM   2044 N  N   . GLU A 1 298 ? 16.421  31.000  12.079  1.00 153.77 ?  297  GLU A N   1 
ATOM   2045 C  CA  . GLU A 1 298 ? 17.543  30.912  11.159  1.00 162.72 ?  297  GLU A CA  1 
ATOM   2046 C  C   . GLU A 1 298 ? 17.142  30.194  9.865   1.00 173.19 ?  297  GLU A C   1 
ATOM   2047 O  O   . GLU A 1 298 ? 17.575  30.585  8.782   1.00 172.92 ?  297  GLU A O   1 
ATOM   2048 C  CB  . GLU A 1 298 ? 18.729  30.210  11.826  1.00 153.17 ?  297  GLU A CB  1 
ATOM   2049 C  CG  . GLU A 1 298 ? 19.360  30.989  12.980  1.00 155.91 ?  297  GLU A CG  1 
ATOM   2050 C  CD  . GLU A 1 298 ? 19.833  32.375  12.579  1.00 160.12 ?  297  GLU A CD  1 
ATOM   2051 O  OE1 . GLU A 1 298 ? 19.029  33.331  12.651  1.00 161.74 ?  297  GLU A OE1 1 
ATOM   2052 O  OE2 . GLU A 1 298 ? 21.015  32.512  12.201  1.00 158.18 ?  297  GLU A OE2 1 
ATOM   2053 N  N   . THR A 1 299 ? 16.306  29.160  9.976   1.00 173.98 ?  298  THR A N   1 
ATOM   2054 C  CA  . THR A 1 299 ? 15.848  28.430  8.793   1.00 169.15 ?  298  THR A CA  1 
ATOM   2055 C  C   . THR A 1 299 ? 15.145  29.337  7.800   1.00 175.67 ?  298  THR A C   1 
ATOM   2056 O  O   . THR A 1 299 ? 15.487  29.360  6.619   1.00 179.89 ?  298  THR A O   1 
ATOM   2057 C  CB  . THR A 1 299 ? 14.846  27.298  9.138   1.00 176.69 ?  298  THR A CB  1 
ATOM   2058 O  OG1 . THR A 1 299 ? 13.712  27.848  9.820   1.00 184.99 ?  298  THR A OG1 1 
ATOM   2059 C  CG2 . THR A 1 299 ? 15.471  26.242  9.995   1.00 166.77 ?  298  THR A CG2 1 
ATOM   2060 N  N   . GLN A 1 300 ? 14.168  30.092  8.291   1.00 172.39 ?  299  GLN A N   1 
ATOM   2061 C  CA  . GLN A 1 300 ? 13.388  30.980  7.441   1.00 173.37 ?  299  GLN A CA  1 
ATOM   2062 C  C   . GLN A 1 300 ? 14.258  32.058  6.805   1.00 182.63 ?  299  GLN A C   1 
ATOM   2063 O  O   . GLN A 1 300 ? 14.079  32.395  5.636   1.00 188.49 ?  299  GLN A O   1 
ATOM   2064 C  CB  . GLN A 1 300 ? 12.242  31.621  8.226   1.00 168.34 ?  299  GLN A CB  1 
ATOM   2065 C  CG  . GLN A 1 300 ? 11.302  32.475  7.374   1.00 174.18 ?  299  GLN A CG  1 
ATOM   2066 C  CD  . GLN A 1 300 ? 10.458  31.660  6.401   1.00 175.66 ?  299  GLN A CD  1 
ATOM   2067 O  OE1 . GLN A 1 300 ? 10.956  31.156  5.393   1.00 175.90 ?  299  GLN A OE1 1 
ATOM   2068 N  NE2 . GLN A 1 300 ? 9.170   31.536  6.700   1.00 180.63 ?  299  GLN A NE2 1 
ATOM   2069 N  N   . LYS A 1 301 ? 15.206  32.592  7.568   1.00 177.44 ?  300  LYS A N   1 
ATOM   2070 C  CA  . LYS A 1 301 ? 16.070  33.649  7.053   1.00 184.91 ?  300  LYS A CA  1 
ATOM   2071 C  C   . LYS A 1 301 ? 16.995  33.140  5.953   1.00 190.32 ?  300  LYS A C   1 
ATOM   2072 O  O   . LYS A 1 301 ? 17.351  33.885  5.039   1.00 201.04 ?  300  LYS A O   1 
ATOM   2073 C  CB  . LYS A 1 301 ? 16.894  34.273  8.181   1.00 190.69 ?  300  LYS A CB  1 
ATOM   2074 C  CG  . LYS A 1 301 ? 17.621  35.543  7.769   1.00 199.66 ?  300  LYS A CG  1 
ATOM   2075 C  CD  . LYS A 1 301 ? 16.666  36.521  7.096   1.00 208.44 ?  300  LYS A CD  1 
ATOM   2076 C  CE  . LYS A 1 301 ? 15.594  37.004  8.063   1.00 216.49 ?  300  LYS A CE  1 
ATOM   2077 N  NZ  . LYS A 1 301 ? 14.534  37.792  7.376   1.00 215.42 ?  300  LYS A NZ  1 
ATOM   2078 N  N   . PHE A 1 302 ? 17.387  31.874  6.046   1.00 194.58 ?  301  PHE A N   1 
ATOM   2079 C  CA  . PHE A 1 302 ? 18.175  31.254  4.991   1.00 174.03 ?  301  PHE A CA  1 
ATOM   2080 C  C   . PHE A 1 302 ? 17.304  31.044  3.751   1.00 152.05 ?  301  PHE A C   1 
ATOM   2081 O  O   . PHE A 1 302 ? 17.727  31.314  2.626   1.00 138.25 ?  301  PHE A O   1 
ATOM   2082 C  CB  . PHE A 1 302 ? 18.762  29.927  5.469   1.00 168.28 ?  301  PHE A CB  1 
ATOM   2083 C  CG  . PHE A 1 302 ? 19.812  29.362  4.558   1.00 162.40 ?  301  PHE A CG  1 
ATOM   2084 C  CD1 . PHE A 1 302 ? 19.468  28.634  3.429   1.00 147.04 ?  301  PHE A CD1 1 
ATOM   2085 C  CD2 . PHE A 1 302 ? 21.155  29.556  4.840   1.00 163.49 ?  301  PHE A CD2 1 
ATOM   2086 C  CE1 . PHE A 1 302 ? 20.444  28.120  2.597   1.00 140.76 ?  301  PHE A CE1 1 
ATOM   2087 C  CE2 . PHE A 1 302 ? 22.135  29.042  4.011   1.00 158.94 ?  301  PHE A CE2 1 
ATOM   2088 C  CZ  . PHE A 1 302 ? 21.778  28.324  2.889   1.00 147.83 ?  301  PHE A CZ  1 
ATOM   2089 N  N   . VAL A 1 303 ? 16.085  30.559  3.976   1.00 154.73 ?  302  VAL A N   1 
ATOM   2090 C  CA  . VAL A 1 303 ? 15.100  30.380  2.912   1.00 160.77 ?  302  VAL A CA  1 
ATOM   2091 C  C   . VAL A 1 303 ? 14.779  31.695  2.212   1.00 169.74 ?  302  VAL A C   1 
ATOM   2092 O  O   . VAL A 1 303 ? 14.812  31.776  0.987   1.00 169.31 ?  302  VAL A O   1 
ATOM   2093 C  CB  . VAL A 1 303 ? 13.790  29.763  3.451   1.00 159.73 ?  302  VAL A CB  1 
ATOM   2094 C  CG1 . VAL A 1 303 ? 12.710  29.762  2.375   1.00 154.65 ?  302  VAL A CG1 1 
ATOM   2095 C  CG2 . VAL A 1 303 ? 14.039  28.356  3.973   1.00 161.84 ?  302  VAL A CG2 1 
ATOM   2096 N  N   . ASP A 1 304 ? 14.482  32.724  2.997   1.00 170.72 ?  303  ASP A N   1 
ATOM   2097 C  CA  . ASP A 1 304 ? 14.159  34.038  2.452   1.00 177.94 ?  303  ASP A CA  1 
ATOM   2098 C  C   . ASP A 1 304 ? 15.307  34.591  1.615   1.00 192.65 ?  303  ASP A C   1 
ATOM   2099 O  O   . ASP A 1 304 ? 15.081  35.214  0.576   1.00 188.96 ?  303  ASP A O   1 
ATOM   2100 C  CB  . ASP A 1 304 ? 13.811  35.020  3.578   1.00 191.19 ?  303  ASP A CB  1 
ATOM   2101 C  CG  . ASP A 1 304 ? 12.492  34.692  4.255   1.00 182.77 ?  303  ASP A CG  1 
ATOM   2102 O  OD1 . ASP A 1 304 ? 12.021  33.542  4.123   1.00 177.51 ?  303  ASP A OD1 1 
ATOM   2103 O  OD2 . ASP A 1 304 ? 11.928  35.584  4.923   1.00 153.63 ?  303  ASP A OD2 1 
ATOM   2104 N  N   . SER A 1 305 ? 16.535  34.355  2.066   1.00 203.30 ?  304  SER A N   1 
ATOM   2105 C  CA  . SER A 1 305 ? 17.713  34.867  1.375   1.00 208.11 ?  304  SER A CA  1 
ATOM   2106 C  C   . SER A 1 305 ? 17.862  34.279  -0.029  1.00 190.88 ?  304  SER A C   1 
ATOM   2107 O  O   . SER A 1 305 ? 18.054  35.014  -0.997  1.00 192.60 ?  304  SER A O   1 
ATOM   2108 C  CB  . SER A 1 305 ? 18.973  34.583  2.196   1.00 223.05 ?  304  SER A CB  1 
ATOM   2109 O  OG  . SER A 1 305 ? 20.117  35.168  1.598   1.00 235.84 ?  304  SER A OG  1 
ATOM   2110 N  N   . LEU A 1 306 ? 17.768  32.958  -0.140  1.00 185.43 ?  305  LEU A N   1 
ATOM   2111 C  CA  . LEU A 1 306 ? 17.896  32.300  -1.439  1.00 153.84 ?  305  LEU A CA  1 
ATOM   2112 C  C   . LEU A 1 306 ? 16.721  32.614  -2.368  1.00 147.09 ?  305  LEU A C   1 
ATOM   2113 O  O   . LEU A 1 306 ? 16.909  32.842  -3.563  1.00 124.43 ?  305  LEU A O   1 
ATOM   2114 C  CB  . LEU A 1 306 ? 18.065  30.784  -1.248  1.00 148.56 ?  305  LEU A CB  1 
ATOM   2115 C  CG  . LEU A 1 306 ? 17.024  29.923  -0.521  1.00 134.77 ?  305  LEU A CG  1 
ATOM   2116 C  CD1 . LEU A 1 306 ? 15.858  29.526  -1.411  1.00 127.58 ?  305  LEU A CD1 1 
ATOM   2117 C  CD2 . LEU A 1 306 ? 17.685  28.675  0.061   1.00 127.28 ?  305  LEU A CD2 1 
ATOM   2118 N  N   . VAL A 1 307 ? 15.519  32.662  -1.803  1.00 159.99 ?  306  VAL A N   1 
ATOM   2119 C  CA  . VAL A 1 307 ? 14.311  32.976  -2.559  1.00 166.04 ?  306  VAL A CA  1 
ATOM   2120 C  C   . VAL A 1 307 ? 14.367  34.360  -3.208  1.00 185.37 ?  306  VAL A C   1 
ATOM   2121 O  O   . VAL A 1 307 ? 13.941  34.535  -4.349  1.00 193.29 ?  306  VAL A O   1 
ATOM   2122 C  CB  . VAL A 1 307 ? 13.050  32.880  -1.657  1.00 141.05 ?  306  VAL A CB  1 
ATOM   2123 C  CG1 . VAL A 1 307 ? 11.849  33.544  -2.312  1.00 140.65 ?  306  VAL A CG1 1 
ATOM   2124 C  CG2 . VAL A 1 307 ? 12.744  31.430  -1.316  1.00 126.83 ?  306  VAL A CG2 1 
ATOM   2125 N  N   . ALA A 1 308 ? 14.903  35.338  -2.484  1.00 200.46 ?  307  ALA A N   1 
ATOM   2126 C  CA  . ALA A 1 308 ? 14.989  36.708  -2.990  1.00 219.59 ?  307  ALA A CA  1 
ATOM   2127 C  C   . ALA A 1 308 ? 15.848  36.811  -4.248  1.00 226.75 ?  307  ALA A C   1 
ATOM   2128 O  O   . ALA A 1 308 ? 15.512  37.541  -5.183  1.00 230.93 ?  307  ALA A O   1 
ATOM   2129 C  CB  . ALA A 1 308 ? 15.529  37.627  -1.911  1.00 229.93 ?  307  ALA A CB  1 
ATOM   2130 N  N   . LEU A 1 309 ? 16.961  36.085  -4.261  1.00 230.14 ?  308  LEU A N   1 
ATOM   2131 C  CA  . LEU A 1 309 ? 17.856  36.068  -5.414  1.00 228.45 ?  308  LEU A CA  1 
ATOM   2132 C  C   . LEU A 1 309 ? 17.231  35.314  -6.583  1.00 217.86 ?  308  LEU A C   1 
ATOM   2133 O  O   . LEU A 1 309 ? 17.635  35.476  -7.735  1.00 219.33 ?  308  LEU A O   1 
ATOM   2134 C  CB  . LEU A 1 309 ? 19.201  35.441  -5.049  1.00 230.07 ?  308  LEU A CB  1 
ATOM   2135 C  CG  . LEU A 1 309 ? 20.333  35.702  -6.046  1.00 230.59 ?  308  LEU A CG  1 
ATOM   2136 C  CD1 . LEU A 1 309 ? 20.563  37.198  -6.190  1.00 233.16 ?  308  LEU A CD1 1 
ATOM   2137 C  CD2 . LEU A 1 309 ? 21.611  34.997  -5.622  1.00 230.10 ?  308  LEU A CD2 1 
ATOM   2138 N  N   . ALA A 1 310 ? 16.242  34.484  -6.274  1.00 194.59 ?  309  ALA A N   1 
ATOM   2139 C  CA  . ALA A 1 310 ? 15.587  33.658  -7.276  1.00 170.64 ?  309  ALA A CA  1 
ATOM   2140 C  C   . ALA A 1 310 ? 14.627  34.446  -8.159  1.00 160.99 ?  309  ALA A C   1 
ATOM   2141 O  O   . ALA A 1 310 ? 14.659  34.315  -9.379  1.00 169.38 ?  309  ALA A O   1 
ATOM   2142 C  CB  . ALA A 1 310 ? 14.849  32.524  -6.598  1.00 169.30 ?  309  ALA A CB  1 
ATOM   2143 N  N   . MET A 1 311 ? 13.786  35.272  -7.545  1.00 151.16 ?  310  MET A N   1 
ATOM   2144 C  CA  . MET A 1 311 ? 12.840  36.102  -8.289  1.00 177.74 ?  310  MET A CA  1 
ATOM   2145 C  C   . MET A 1 311 ? 13.517  37.072  -9.272  1.00 186.67 ?  310  MET A C   1 
ATOM   2146 O  O   . MET A 1 311 ? 12.887  37.539  -10.228 1.00 185.27 ?  310  MET A O   1 
ATOM   2147 C  CB  . MET A 1 311 ? 11.950  36.875  -7.311  1.00 189.34 ?  310  MET A CB  1 
ATOM   2148 C  CG  . MET A 1 311 ? 11.068  35.981  -6.444  1.00 187.84 ?  310  MET A CG  1 
ATOM   2149 S  SD  . MET A 1 311 ? 9.930   34.970  -7.421  1.00 193.49 ?  310  MET A SD  1 
ATOM   2150 C  CE  . MET A 1 311 ? 9.040   34.104  -6.132  1.00 136.02 ?  310  MET A CE  1 
ATOM   2151 N  N   . ASP A 1 312 ? 14.790  37.380  -9.035  1.00 185.46 ?  311  ASP A N   1 
ATOM   2152 C  CA  . ASP A 1 312 ? 15.541  38.243  -9.945  1.00 185.22 ?  311  ASP A CA  1 
ATOM   2153 C  C   . ASP A 1 312 ? 16.455  37.445  -10.874 1.00 176.60 ?  311  ASP A C   1 
ATOM   2154 O  O   . ASP A 1 312 ? 16.891  36.343  -10.541 1.00 173.97 ?  311  ASP A O   1 
ATOM   2155 C  CB  . ASP A 1 312 ? 16.365  39.264  -9.165  1.00 195.08 ?  311  ASP A CB  1 
ATOM   2156 C  CG  . ASP A 1 312 ? 16.493  40.584  -9.899  1.00 206.44 ?  311  ASP A CG  1 
ATOM   2157 O  OD1 . ASP A 1 312 ? 16.556  40.564  -11.148 1.00 205.43 ?  311  ASP A OD1 1 
ATOM   2158 O  OD2 . ASP A 1 312 ? 16.522  41.640  -9.230  1.00 211.94 ?  311  ASP A OD2 1 
ATOM   2159 N  N   . ASN A 1 323 ? 11.765  33.746  -10.501 1.00 183.40 ?  322  ASN A N   1 
ATOM   2160 C  CA  . ASN A 1 323 ? 10.774  34.178  -11.478 1.00 189.56 ?  322  ASN A CA  1 
ATOM   2161 C  C   . ASN A 1 323 ? 9.424   33.507  -11.251 1.00 213.32 ?  322  ASN A C   1 
ATOM   2162 O  O   . ASN A 1 323 ? 9.198   32.885  -10.213 1.00 213.05 ?  322  ASN A O   1 
ATOM   2163 C  CB  . ASN A 1 323 ? 11.271  33.895  -12.898 1.00 167.96 ?  322  ASN A CB  1 
ATOM   2164 C  CG  . ASN A 1 323 ? 12.442  34.776  -13.294 1.00 157.27 ?  322  ASN A CG  1 
ATOM   2165 O  OD1 . ASN A 1 323 ? 12.261  35.824  -13.917 1.00 166.43 ?  322  ASN A OD1 1 
ATOM   2166 N  ND2 . ASN A 1 323 ? 13.650  34.357  -12.933 1.00 136.98 ?  322  ASN A ND2 1 
ATOM   2167 N  N   . VAL A 1 324 ? 8.526   33.649  -12.223 1.00 232.59 ?  323  VAL A N   1 
ATOM   2168 C  CA  . VAL A 1 324 ? 7.212   33.015  -12.160 1.00 229.52 ?  323  VAL A CA  1 
ATOM   2169 C  C   . VAL A 1 324 ? 7.370   31.495  -12.207 1.00 218.08 ?  323  VAL A C   1 
ATOM   2170 O  O   . VAL A 1 324 ? 6.528   30.755  -11.695 1.00 226.98 ?  323  VAL A O   1 
ATOM   2171 C  CB  . VAL A 1 324 ? 6.287   33.502  -13.304 1.00 230.62 ?  323  VAL A CB  1 
ATOM   2172 C  CG1 . VAL A 1 324 ? 6.831   33.080  -14.664 1.00 225.61 ?  323  VAL A CG1 1 
ATOM   2173 C  CG2 . VAL A 1 324 ? 4.861   32.998  -13.104 1.00 232.75 ?  323  VAL A CG2 1 
ATOM   2174 N  N   . VAL A 1 325 ? 8.461   31.038  -12.815 1.00 199.57 ?  324  VAL A N   1 
ATOM   2175 C  CA  . VAL A 1 325 ? 8.787   29.619  -12.852 1.00 174.74 ?  324  VAL A CA  1 
ATOM   2176 C  C   . VAL A 1 325 ? 9.100   29.121  -11.441 1.00 168.66 ?  324  VAL A C   1 
ATOM   2177 O  O   . VAL A 1 325 ? 8.771   27.990  -11.077 1.00 160.71 ?  324  VAL A O   1 
ATOM   2178 C  CB  . VAL A 1 325 ? 9.977   29.335  -13.797 1.00 159.29 ?  324  VAL A CB  1 
ATOM   2179 C  CG1 . VAL A 1 325 ? 9.543   29.485  -15.245 1.00 155.07 ?  324  VAL A CG1 1 
ATOM   2180 C  CG2 . VAL A 1 325 ? 11.150  30.262  -13.492 1.00 153.48 ?  324  VAL A CG2 1 
ATOM   2181 N  N   . PHE A 1 326 ? 9.757   29.973  -10.661 1.00 172.12 ?  325  PHE A N   1 
ATOM   2182 C  CA  . PHE A 1 326 ? 10.062  29.664  -9.275  1.00 167.46 ?  325  PHE A CA  1 
ATOM   2183 C  C   . PHE A 1 326 ? 8.823   29.812  -8.393  1.00 168.72 ?  325  PHE A C   1 
ATOM   2184 O  O   . PHE A 1 326 ? 8.651   29.076  -7.422  1.00 161.97 ?  325  PHE A O   1 
ATOM   2185 C  CB  . PHE A 1 326 ? 11.189  30.553  -8.763  1.00 168.51 ?  325  PHE A CB  1 
ATOM   2186 C  CG  . PHE A 1 326 ? 11.514  30.327  -7.324  1.00 167.57 ?  325  PHE A CG  1 
ATOM   2187 C  CD1 . PHE A 1 326 ? 12.127  29.152  -6.919  1.00 155.42 ?  325  PHE A CD1 1 
ATOM   2188 C  CD2 . PHE A 1 326 ? 11.213  31.286  -6.376  1.00 180.76 ?  325  PHE A CD2 1 
ATOM   2189 C  CE1 . PHE A 1 326 ? 12.425  28.934  -5.598  1.00 159.89 ?  325  PHE A CE1 1 
ATOM   2190 C  CE2 . PHE A 1 326 ? 11.509  31.074  -5.054  1.00 186.53 ?  325  PHE A CE2 1 
ATOM   2191 C  CZ  . PHE A 1 326 ? 12.119  29.895  -4.662  1.00 179.62 ?  325  PHE A CZ  1 
ATOM   2192 N  N   . SER A 1 327 ? 7.973   30.779  -8.729  1.00 175.80 ?  326  SER A N   1 
ATOM   2193 C  CA  . SER A 1 327 ? 6.683   30.940  -8.065  1.00 192.61 ?  326  SER A CA  1 
ATOM   2194 C  C   . SER A 1 327 ? 5.848   29.675  -8.244  1.00 199.63 ?  326  SER A C   1 
ATOM   2195 O  O   . SER A 1 327 ? 5.114   29.271  -7.341  1.00 200.42 ?  326  SER A O   1 
ATOM   2196 C  CB  . SER A 1 327 ? 5.936   32.160  -8.614  1.00 198.27 ?  326  SER A CB  1 
ATOM   2197 O  OG  . SER A 1 327 ? 4.579   32.164  -8.205  1.00 195.48 ?  326  SER A OG  1 
ATOM   2198 N  N   . GLU A 1 328 ? 5.966   29.059  -9.418  1.00 207.05 ?  327  GLU A N   1 
ATOM   2199 C  CA  . GLU A 1 328 ? 5.326   27.775  -9.679  1.00 200.89 ?  327  GLU A CA  1 
ATOM   2200 C  C   . GLU A 1 328 ? 5.892   26.709  -8.750  1.00 187.19 ?  327  GLU A C   1 
ATOM   2201 O  O   . GLU A 1 328 ? 5.149   25.905  -8.192  1.00 184.27 ?  327  GLU A O   1 
ATOM   2202 C  CB  . GLU A 1 328 ? 5.506   27.351  -11.142 1.00 204.64 ?  327  GLU A CB  1 
ATOM   2203 C  CG  . GLU A 1 328 ? 4.648   28.124  -12.136 1.00 206.10 ?  327  GLU A CG  1 
ATOM   2204 C  CD  . GLU A 1 328 ? 4.691   27.531  -13.534 1.00 200.38 ?  327  GLU A CD  1 
ATOM   2205 O  OE1 . GLU A 1 328 ? 5.602   26.722  -13.817 1.00 191.52 ?  327  GLU A OE1 1 
ATOM   2206 O  OE2 . GLU A 1 328 ? 3.811   27.877  -14.350 1.00 204.45 ?  327  GLU A OE2 1 
ATOM   2207 N  N   . PHE A 1 329 ? 7.210   26.729  -8.569  1.00 176.25 ?  328  PHE A N   1 
ATOM   2208 C  CA  . PHE A 1 329 ? 7.891   25.752  -7.726  1.00 162.94 ?  328  PHE A CA  1 
ATOM   2209 C  C   . PHE A 1 329 ? 7.467   25.846  -6.262  1.00 162.12 ?  328  PHE A C   1 
ATOM   2210 O  O   . PHE A 1 329 ? 7.236   24.823  -5.616  1.00 158.21 ?  328  PHE A O   1 
ATOM   2211 C  CB  . PHE A 1 329 ? 9.402   25.926  -7.829  1.00 150.57 ?  328  PHE A CB  1 
ATOM   2212 C  CG  . PHE A 1 329 ? 10.179  24.808  -7.208  1.00 146.68 ?  328  PHE A CG  1 
ATOM   2213 C  CD1 . PHE A 1 329 ? 9.659   23.524  -7.163  1.00 145.91 ?  328  PHE A CD1 1 
ATOM   2214 C  CD2 . PHE A 1 329 ? 11.417  25.041  -6.647  1.00 146.75 ?  328  PHE A CD2 1 
ATOM   2215 C  CE1 . PHE A 1 329 ? 10.371  22.491  -6.585  1.00 137.35 ?  328  PHE A CE1 1 
ATOM   2216 C  CE2 . PHE A 1 329 ? 12.134  24.013  -6.068  1.00 144.21 ?  328  PHE A CE2 1 
ATOM   2217 C  CZ  . PHE A 1 329 ? 11.609  22.735  -6.037  1.00 134.65 ?  328  PHE A CZ  1 
ATOM   2218 N  N   . GLN A 1 330 ? 7.381   27.067  -5.739  1.00 165.95 ?  329  GLN A N   1 
ATOM   2219 C  CA  . GLN A 1 330 ? 6.941   27.281  -4.362  1.00 178.40 ?  329  GLN A CA  1 
ATOM   2220 C  C   . GLN A 1 330 ? 5.554   26.691  -4.154  1.00 192.34 ?  329  GLN A C   1 
ATOM   2221 O  O   . GLN A 1 330 ? 5.313   25.947  -3.200  1.00 193.74 ?  329  GLN A O   1 
ATOM   2222 C  CB  . GLN A 1 330 ? 6.928   28.771  -4.013  1.00 183.31 ?  329  GLN A CB  1 
ATOM   2223 C  CG  . GLN A 1 330 ? 8.290   29.442  -3.923  1.00 171.04 ?  329  GLN A CG  1 
ATOM   2224 C  CD  . GLN A 1 330 ? 8.177   30.951  -3.800  1.00 171.17 ?  329  GLN A CD  1 
ATOM   2225 O  OE1 . GLN A 1 330 ? 7.258   31.560  -4.346  1.00 163.30 ?  329  GLN A OE1 1 
ATOM   2226 N  NE2 . GLN A 1 330 ? 9.081   31.555  -3.039  1.00 183.81 ?  329  GLN A NE2 1 
ATOM   2227 N  N   . ASP A 1 331 ? 4.649   27.040  -5.061  1.00 207.27 ?  330  ASP A N   1 
ATOM   2228 C  CA  . ASP A 1 331 ? 3.283   26.541  -5.037  1.00 205.81 ?  330  ASP A CA  1 
ATOM   2229 C  C   . ASP A 1 331 ? 3.279   25.029  -5.231  1.00 198.40 ?  330  ASP A C   1 
ATOM   2230 O  O   . ASP A 1 331 ? 2.508   24.314  -4.595  1.00 197.78 ?  330  ASP A O   1 
ATOM   2231 C  CB  . ASP A 1 331 ? 2.439   27.222  -6.115  1.00 210.90 ?  330  ASP A CB  1 
ATOM   2232 C  CG  . ASP A 1 331 ? 2.409   28.733  -5.971  1.00 213.97 ?  330  ASP A CG  1 
ATOM   2233 O  OD1 . ASP A 1 331 ? 2.649   29.238  -4.853  1.00 213.13 ?  330  ASP A OD1 1 
ATOM   2234 O  OD2 . ASP A 1 331 ? 2.143   29.418  -6.982  1.00 214.80 ?  330  ASP A OD2 1 
ATOM   2235 N  N   . TRP A 1 332 ? 4.148   24.555  -6.120  1.00 190.62 ?  331  TRP A N   1 
ATOM   2236 C  CA  . TRP A 1 332 ? 4.216   23.139  -6.469  1.00 179.33 ?  331  TRP A CA  1 
ATOM   2237 C  C   . TRP A 1 332 ? 4.582   22.243  -5.296  1.00 163.59 ?  331  TRP A C   1 
ATOM   2238 O  O   . TRP A 1 332 ? 3.952   21.211  -5.071  1.00 154.93 ?  331  TRP A O   1 
ATOM   2239 C  CB  . TRP A 1 332 ? 5.248   22.923  -7.581  1.00 173.60 ?  331  TRP A CB  1 
ATOM   2240 C  CG  . TRP A 1 332 ? 5.307   21.515  -8.078  1.00 176.19 ?  331  TRP A CG  1 
ATOM   2241 C  CD1 . TRP A 1 332 ? 4.560   20.960  -9.079  1.00 184.26 ?  331  TRP A CD1 1 
ATOM   2242 C  CD2 . TRP A 1 332 ? 6.116   20.463  -7.558  1.00 169.91 ?  331  TRP A CD2 1 
ATOM   2243 N  NE1 . TRP A 1 332 ? 4.883   19.634  -9.232  1.00 186.70 ?  331  TRP A NE1 1 
ATOM   2244 C  CE2 . TRP A 1 332 ? 5.844   19.299  -8.294  1.00 174.98 ?  331  TRP A CE2 1 
ATOM   2245 C  CE3 . TRP A 1 332 ? 7.070   20.387  -6.531  1.00 162.63 ?  331  TRP A CE3 1 
ATOM   2246 C  CZ2 . TRP A 1 332 ? 6.466   18.083  -8.057  1.00 168.27 ?  331  TRP A CZ2 1 
ATOM   2247 C  CZ3 . TRP A 1 332 ? 7.692   19.183  -6.289  1.00 159.07 ?  331  TRP A CZ3 1 
ATOM   2248 C  CH2 . TRP A 1 332 ? 7.390   18.047  -7.047  1.00 159.15 ?  331  TRP A CH2 1 
ATOM   2249 N  N   . LEU A 1 333 ? 5.593   22.652  -4.541  1.00 156.36 ?  332  LEU A N   1 
ATOM   2250 C  CA  . LEU A 1 333 ? 6.116   21.826  -3.465  1.00 149.48 ?  332  LEU A CA  1 
ATOM   2251 C  C   . LEU A 1 333 ? 5.071   21.695  -2.346  1.00 156.33 ?  332  LEU A C   1 
ATOM   2252 O  O   . LEU A 1 333 ? 4.874   20.610  -1.796  1.00 154.85 ?  332  LEU A O   1 
ATOM   2253 C  CB  . LEU A 1 333 ? 7.438   22.426  -2.952  1.00 142.68 ?  332  LEU A CB  1 
ATOM   2254 C  CG  . LEU A 1 333 ? 8.369   21.730  -1.939  1.00 134.21 ?  332  LEU A CG  1 
ATOM   2255 C  CD1 . LEU A 1 333 ? 9.819   22.087  -2.237  1.00 118.72 ?  332  LEU A CD1 1 
ATOM   2256 C  CD2 . LEU A 1 333 ? 8.051   22.000  -0.469  1.00 142.76 ?  332  LEU A CD2 1 
ATOM   2257 N  N   . GLU A 1 334 ? 4.391   22.795  -2.030  1.00 162.61 ?  333  GLU A N   1 
ATOM   2258 C  CA  . GLU A 1 334 ? 3.366   22.793  -0.988  1.00 168.10 ?  333  GLU A CA  1 
ATOM   2259 C  C   . GLU A 1 334 ? 2.255   21.799  -1.318  1.00 179.97 ?  333  GLU A C   1 
ATOM   2260 O  O   . GLU A 1 334 ? 1.774   21.086  -0.435  1.00 188.75 ?  333  GLU A O   1 
ATOM   2261 C  CB  . GLU A 1 334 ? 2.791   24.198  -0.783  1.00 168.75 ?  333  GLU A CB  1 
ATOM   2262 C  CG  . GLU A 1 334 ? 3.606   25.078  0.171   1.00 172.34 ?  333  GLU A CG  1 
ATOM   2263 C  CD  . GLU A 1 334 ? 3.569   24.588  1.616   1.00 178.64 ?  333  GLU A CD  1 
ATOM   2264 O  OE1 . GLU A 1 334 ? 4.269   23.599  1.933   1.00 174.05 ?  333  GLU A OE1 1 
ATOM   2265 O  OE2 . GLU A 1 334 ? 2.850   25.202  2.436   1.00 184.03 ?  333  GLU A OE2 1 
ATOM   2266 N  N   . LYS A 1 335 ? 1.839   21.776  -2.581  1.00 184.48 ?  334  LYS A N   1 
ATOM   2267 C  CA  . LYS A 1 335 ? 0.838   20.830  -3.048  1.00 190.77 ?  334  LYS A CA  1 
ATOM   2268 C  C   . LYS A 1 335 ? 1.357   19.401  -2.891  1.00 190.88 ?  334  LYS A C   1 
ATOM   2269 O  O   . LYS A 1 335 ? 0.645   18.523  -2.414  1.00 197.59 ?  334  LYS A O   1 
ATOM   2270 C  CB  . LYS A 1 335 ? 0.460   21.118  -4.509  1.00 191.78 ?  334  LYS A CB  1 
ATOM   2271 C  CG  . LYS A 1 335 ? -0.057  22.527  -4.752  1.00 191.92 ?  334  LYS A CG  1 
ATOM   2272 C  CD  . LYS A 1 335 ? -0.368  22.753  -6.231  1.00 185.56 ?  334  LYS A CD  1 
ATOM   2273 C  CE  . LYS A 1 335 ? -1.630  22.018  -6.661  1.00 185.22 ?  334  LYS A CE  1 
ATOM   2274 N  NZ  . LYS A 1 335 ? -2.839  22.510  -5.939  1.00 193.56 ?  334  LYS A NZ  1 
ATOM   2275 N  N   . HIS A 1 336 ? 2.594   19.168  -3.315  1.00 187.80 ?  335  HIS A N   1 
ATOM   2276 C  CA  . HIS A 1 336 ? 3.123   17.806  -3.377  1.00 188.28 ?  335  HIS A CA  1 
ATOM   2277 C  C   . HIS A 1 336 ? 3.792   17.318  -2.086  1.00 197.18 ?  335  HIS A C   1 
ATOM   2278 O  O   . HIS A 1 336 ? 4.351   16.220  -2.059  1.00 194.88 ?  335  HIS A O   1 
ATOM   2279 C  CB  . HIS A 1 336 ? 4.116   17.689  -4.540  1.00 180.81 ?  335  HIS A CB  1 
ATOM   2280 C  CG  . HIS A 1 336 ? 3.472   17.723  -5.892  1.00 181.53 ?  335  HIS A CG  1 
ATOM   2281 N  ND1 . HIS A 1 336 ? 2.808   18.827  -6.374  1.00 189.67 ?  335  HIS A ND1 1 
ATOM   2282 C  CD2 . HIS A 1 336 ? 3.396   16.780  -6.860  1.00 176.40 ?  335  HIS A CD2 1 
ATOM   2283 C  CE1 . HIS A 1 336 ? 2.351   18.568  -7.588  1.00 188.97 ?  335  HIS A CE1 1 
ATOM   2284 N  NE2 . HIS A 1 336 ? 2.695   17.330  -7.904  1.00 182.13 ?  335  HIS A NE2 1 
ATOM   2285 N  N   . GLY A 1 337 ? 3.717   18.114  -1.021  1.00 208.42 ?  336  GLY A N   1 
ATOM   2286 C  CA  . GLY A 1 337 ? 4.400   17.781  0.218   1.00 214.56 ?  336  GLY A CA  1 
ATOM   2287 C  C   . GLY A 1 337 ? 3.923   16.490  0.856   1.00 223.44 ?  336  GLY A C   1 
ATOM   2288 O  O   . GLY A 1 337 ? 2.758   16.114  0.715   1.00 238.98 ?  336  GLY A O   1 
ATOM   2289 N  N   . ASP A 1 338 ? 4.808   15.824  1.593   1.00 201.33 ?  337  ASP A N   1 
ATOM   2290 C  CA  . ASP A 1 338 ? 6.154   16.315  1.854   1.00 179.77 ?  337  ASP A CA  1 
ATOM   2291 C  C   . ASP A 1 338 ? 7.203   15.225  1.611   1.00 162.22 ?  337  ASP A C   1 
ATOM   2292 O  O   . ASP A 1 338 ? 6.916   14.034  1.749   1.00 154.45 ?  337  ASP A O   1 
ATOM   2293 C  CB  . ASP A 1 338 ? 6.243   16.843  3.283   1.00 195.85 ?  337  ASP A CB  1 
ATOM   2294 C  CG  . ASP A 1 338 ? 5.120   17.808  3.615   1.00 199.96 ?  337  ASP A CG  1 
ATOM   2295 O  OD1 . ASP A 1 338 ? 4.025   17.345  3.994   1.00 200.64 ?  337  ASP A OD1 1 
ATOM   2296 O  OD2 . ASP A 1 338 ? 5.331   19.033  3.490   1.00 194.52 ?  337  ASP A OD2 1 
ATOM   2297 N  N   . TYR A 1 339 ? 8.422   15.633  1.271   1.00 159.06 ?  338  TYR A N   1 
ATOM   2298 C  CA  . TYR A 1 339 ? 9.486   14.671  0.989   1.00 157.33 ?  338  TYR A CA  1 
ATOM   2299 C  C   . TYR A 1 339 ? 10.507  14.586  2.110   1.00 155.55 ?  338  TYR A C   1 
ATOM   2300 O  O   . TYR A 1 339 ? 11.036  15.596  2.576   1.00 162.30 ?  338  TYR A O   1 
ATOM   2301 C  CB  . TYR A 1 339 ? 10.212  15.018  -0.316  1.00 158.30 ?  338  TYR A CB  1 
ATOM   2302 C  CG  . TYR A 1 339 ? 9.361   14.962  -1.561  1.00 164.31 ?  338  TYR A CG  1 
ATOM   2303 C  CD1 . TYR A 1 339 ? 8.471   15.982  -1.869  1.00 169.10 ?  338  TYR A CD1 1 
ATOM   2304 C  CD2 . TYR A 1 339 ? 9.463   13.891  -2.439  1.00 159.67 ?  338  TYR A CD2 1 
ATOM   2305 C  CE1 . TYR A 1 339 ? 7.698   15.928  -3.012  1.00 170.38 ?  338  TYR A CE1 1 
ATOM   2306 C  CE2 . TYR A 1 339 ? 8.700   13.830  -3.580  1.00 162.68 ?  338  TYR A CE2 1 
ATOM   2307 C  CZ  . TYR A 1 339 ? 7.818   14.850  -3.863  1.00 170.79 ?  338  TYR A CZ  1 
ATOM   2308 O  OH  . TYR A 1 339 ? 7.053   14.792  -5.004  1.00 176.75 ?  338  TYR A OH  1 
ATOM   2309 N  N   . GLU A 1 340 ? 10.766  13.354  2.534   1.00 139.85 ?  339  GLU A N   1 
ATOM   2310 C  CA  . GLU A 1 340 ? 11.733  13.060  3.581   1.00 136.90 ?  339  GLU A CA  1 
ATOM   2311 C  C   . GLU A 1 340 ? 13.179  13.306  3.149   1.00 129.59 ?  339  GLU A C   1 
ATOM   2312 O  O   . GLU A 1 340 ? 14.024  13.639  3.973   1.00 128.79 ?  339  GLU A O   1 
ATOM   2313 C  CB  . GLU A 1 340 ? 11.576  11.616  4.064   1.00 137.81 ?  339  GLU A CB  1 
ATOM   2314 C  CG  . GLU A 1 340 ? 10.293  11.328  4.827   1.00 151.30 ?  339  GLU A CG  1 
ATOM   2315 C  CD  . GLU A 1 340 ? 10.460  11.537  6.316   1.00 168.22 ?  339  GLU A CD  1 
ATOM   2316 O  OE1 . GLU A 1 340 ? 11.499  11.104  6.851   1.00 174.36 ?  339  GLU A OE1 1 
ATOM   2317 O  OE2 . GLU A 1 340 ? 9.549   12.106  6.956   1.00 176.55 ?  339  GLU A OE2 1 
ATOM   2318 N  N   . ALA A 1 341 ? 13.474  13.115  1.868   1.00 124.22 ?  340  ALA A N   1 
ATOM   2319 C  CA  . ALA A 1 341 ? 14.811  13.403  1.356   1.00 124.27 ?  340  ALA A CA  1 
ATOM   2320 C  C   . ALA A 1 341 ? 14.744  14.021  -0.035  1.00 118.41 ?  340  ALA A C   1 
ATOM   2321 O  O   . ALA A 1 341 ? 13.743  13.879  -0.732  1.00 129.31 ?  340  ALA A O   1 
ATOM   2322 C  CB  . ALA A 1 341 ? 15.652  12.145  1.335   1.00 128.43 ?  340  ALA A CB  1 
ATOM   2323 N  N   . ILE A 1 342 ? 15.817  14.697  -0.439  1.00 108.65 ?  341  ILE A N   1 
ATOM   2324 C  CA  . ILE A 1 342 ? 15.874  15.314  -1.761  1.00 115.57 ?  341  ILE A CA  1 
ATOM   2325 C  C   . ILE A 1 342 ? 17.253  15.139  -2.402  1.00 118.39 ?  341  ILE A C   1 
ATOM   2326 O  O   . ILE A 1 342 ? 18.276  15.236  -1.724  1.00 110.43 ?  341  ILE A O   1 
ATOM   2327 C  CB  . ILE A 1 342 ? 15.501  16.817  -1.667  1.00 97.39  ?  341  ILE A CB  1 
ATOM   2328 C  CG1 . ILE A 1 342 ? 13.980  16.978  -1.687  1.00 99.24  ?  341  ILE A CG1 1 
ATOM   2329 C  CG2 . ILE A 1 342 ? 16.125  17.623  -2.792  1.00 95.09  ?  341  ILE A CG2 1 
ATOM   2330 C  CD1 . ILE A 1 342 ? 13.472  18.100  -0.836  1.00 102.18 ?  341  ILE A CD1 1 
ATOM   2331 N  N   . VAL A 1 343 ? 17.272  14.878  -3.710  1.00 122.02 ?  342  VAL A N   1 
ATOM   2332 C  CA  . VAL A 1 343 ? 18.512  14.552  -4.411  1.00 107.56 ?  342  VAL A CA  1 
ATOM   2333 C  C   . VAL A 1 343 ? 18.897  15.597  -5.448  1.00 105.73 ?  342  VAL A C   1 
ATOM   2334 O  O   . VAL A 1 343 ? 18.049  16.111  -6.179  1.00 87.32  ?  342  VAL A O   1 
ATOM   2335 C  CB  . VAL A 1 343 ? 18.421  13.183  -5.128  1.00 102.23 ?  342  VAL A CB  1 
ATOM   2336 C  CG1 . VAL A 1 343 ? 19.813  12.614  -5.379  1.00 87.31  ?  342  VAL A CG1 1 
ATOM   2337 C  CG2 . VAL A 1 343 ? 17.567  12.204  -4.330  1.00 95.62  ?  342  VAL A CG2 1 
ATOM   2338 N  N   . ASP A 1 344 ? 20.193  15.881  -5.517  1.00 118.29 ?  343  ASP A N   1 
ATOM   2339 C  CA  . ASP A 1 344 ? 20.740  16.764  -6.536  1.00 113.22 ?  343  ASP A CA  1 
ATOM   2340 C  C   . ASP A 1 344 ? 20.990  15.949  -7.795  1.00 102.45 ?  343  ASP A C   1 
ATOM   2341 O  O   . ASP A 1 344 ? 22.001  15.254  -7.905  1.00 103.43 ?  343  ASP A O   1 
ATOM   2342 C  CB  . ASP A 1 344 ? 22.024  17.446  -6.043  1.00 111.55 ?  343  ASP A CB  1 
ATOM   2343 C  CG  . ASP A 1 344 ? 22.702  18.280  -7.119  1.00 115.23 ?  343  ASP A CG  1 
ATOM   2344 O  OD1 . ASP A 1 344 ? 22.067  18.578  -8.150  1.00 130.63 ?  343  ASP A OD1 1 
ATOM   2345 O  OD2 . ASP A 1 344 ? 23.869  18.669  -6.920  1.00 109.37 ?  343  ASP A OD2 1 
ATOM   2346 N  N   . GLY A 1 345 ? 20.047  16.025  -8.728  1.00 93.57  ?  344  GLY A N   1 
ATOM   2347 C  CA  . GLY A 1 345 ? 20.094  15.217  -9.929  1.00 102.27 ?  344  GLY A CA  1 
ATOM   2348 C  C   . GLY A 1 345 ? 21.384  15.318  -10.716 1.00 98.62  ?  344  GLY A C   1 
ATOM   2349 O  O   . GLY A 1 345 ? 21.977  14.301  -11.074 1.00 79.74  ?  344  GLY A O   1 
ATOM   2350 N  N   . ALA A 1 346 ? 21.839  16.545  -10.946 1.00 99.34  ?  345  ALA A N   1 
ATOM   2351 C  CA  . ALA A 1 346 ? 23.041  16.781  -11.742 1.00 112.86 ?  345  ALA A CA  1 
ATOM   2352 C  C   . ALA A 1 346 ? 24.247  16.071  -11.141 1.00 120.44 ?  345  ALA A C   1 
ATOM   2353 O  O   . ALA A 1 346 ? 24.947  15.326  -11.826 1.00 109.58 ?  345  ALA A O   1 
ATOM   2354 C  CB  . ALA A 1 346 ? 23.313  18.279  -11.864 1.00 127.13 ?  345  ALA A CB  1 
ATOM   2355 N  N   . ASN A 1 347 ? 24.458  16.291  -9.848  1.00 133.56 ?  346  ASN A N   1 
ATOM   2356 C  CA  . ASN A 1 347 ? 25.610  15.762  -9.127  1.00 130.10 ?  346  ASN A CA  1 
ATOM   2357 C  C   . ASN A 1 347 ? 25.792  14.248  -9.261  1.00 109.31 ?  346  ASN A C   1 
ATOM   2358 O  O   . ASN A 1 347 ? 26.902  13.769  -9.490  1.00 104.31 ?  346  ASN A O   1 
ATOM   2359 C  CB  . ASN A 1 347 ? 25.506  16.146  -7.651  1.00 143.06 ?  346  ASN A CB  1 
ATOM   2360 C  CG  . ASN A 1 347 ? 26.680  15.656  -6.842  1.00 154.65 ?  346  ASN A CG  1 
ATOM   2361 O  OD1 . ASN A 1 347 ? 26.524  14.832  -5.943  1.00 183.72 ?  346  ASN A OD1 1 
ATOM   2362 N  ND2 . ASN A 1 347 ? 27.870  16.145  -7.168  1.00 137.93 ?  346  ASN A ND2 1 
ATOM   2363 N  N   . ILE A 1 348 ? 24.699  13.507  -9.113  1.00 102.60 ?  347  ILE A N   1 
ATOM   2364 C  CA  . ILE A 1 348 ? 24.725  12.048  -9.185  1.00 108.26 ?  347  ILE A CA  1 
ATOM   2365 C  C   . ILE A 1 348 ? 25.198  11.521  -10.534 1.00 95.65  ?  347  ILE A C   1 
ATOM   2366 O  O   . ILE A 1 348 ? 26.151  10.743  -10.617 1.00 82.23  ?  347  ILE A O   1 
ATOM   2367 C  CB  . ILE A 1 348 ? 23.329  11.459  -8.904  1.00 102.87 ?  347  ILE A CB  1 
ATOM   2368 C  CG1 . ILE A 1 348 ? 22.664  12.160  -7.711  1.00 109.26 ?  347  ILE A CG1 1 
ATOM   2369 C  CG2 . ILE A 1 348 ? 23.429  9.942   -8.696  1.00 83.32  ?  347  ILE A CG2 1 
ATOM   2370 C  CD1 . ILE A 1 348 ? 23.323  11.884  -6.404  1.00 110.52 ?  347  ILE A CD1 1 
ATOM   2371 N  N   . GLY A 1 349 ? 24.524  11.974  -11.585 1.00 93.84  ?  348  GLY A N   1 
ATOM   2372 C  CA  . GLY A 1 349 ? 24.760  11.496  -12.931 1.00 87.39  ?  348  GLY A CA  1 
ATOM   2373 C  C   . GLY A 1 349 ? 26.140  11.700  -13.521 1.00 98.51  ?  348  GLY A C   1 
ATOM   2374 O  O   . GLY A 1 349 ? 26.614  10.840  -14.264 1.00 102.97 ?  348  GLY A O   1 
ATOM   2375 N  N   . LEU A 1 350 ? 26.792  12.818  -13.214 1.00 106.73 ?  349  LEU A N   1 
ATOM   2376 C  CA  . LEU A 1 350 ? 28.104  13.064  -13.798 1.00 104.94 ?  349  LEU A CA  1 
ATOM   2377 C  C   . LEU A 1 350 ? 29.201  12.422  -12.958 1.00 98.37  ?  349  LEU A C   1 
ATOM   2378 O  O   . LEU A 1 350 ? 30.283  12.124  -13.460 1.00 84.65  ?  349  LEU A O   1 
ATOM   2379 C  CB  . LEU A 1 350 ? 28.335  14.564  -13.960 1.00 97.43  ?  349  LEU A CB  1 
ATOM   2380 C  CG  . LEU A 1 350 ? 27.392  15.195  -14.992 1.00 108.65 ?  349  LEU A CG  1 
ATOM   2381 C  CD1 . LEU A 1 350 ? 26.451  16.204  -14.358 1.00 103.79 ?  349  LEU A CD1 1 
ATOM   2382 C  CD2 . LEU A 1 350 ? 28.181  15.835  -16.126 1.00 131.64 ?  349  LEU A CD2 1 
ATOM   2383 N  N   . TYR A 1 351 ? 28.901  12.193  -11.683 1.00 97.86  ?  350  TYR A N   1 
ATOM   2384 C  CA  . TYR A 1 351 ? 29.760  11.405  -10.808 1.00 107.76 ?  350  TYR A CA  1 
ATOM   2385 C  C   . TYR A 1 351 ? 29.638  9.983   -11.321 1.00 126.54 ?  350  TYR A C   1 
ATOM   2386 O  O   . TYR A 1 351 ? 28.521  9.532   -11.546 1.00 145.71 ?  350  TYR A O   1 
ATOM   2387 C  CB  . TYR A 1 351 ? 29.315  11.511  -9.347  1.00 113.20 ?  350  TYR A CB  1 
ATOM   2388 C  CG  . TYR A 1 351 ? 30.273  10.926  -8.328  1.00 128.76 ?  350  TYR A CG  1 
ATOM   2389 C  CD1 . TYR A 1 351 ? 30.364  9.552   -8.132  1.00 124.92 ?  350  TYR A CD1 1 
ATOM   2390 C  CD2 . TYR A 1 351 ? 31.063  11.751  -7.534  1.00 139.31 ?  350  TYR A CD2 1 
ATOM   2391 C  CE1 . TYR A 1 351 ? 31.230  9.017   -7.192  1.00 122.02 ?  350  TYR A CE1 1 
ATOM   2392 C  CE2 . TYR A 1 351 ? 31.931  11.224  -6.590  1.00 133.40 ?  350  TYR A CE2 1 
ATOM   2393 C  CZ  . TYR A 1 351 ? 32.011  9.859   -6.423  1.00 124.79 ?  350  TYR A CZ  1 
ATOM   2394 O  OH  . TYR A 1 351 ? 32.875  9.341   -5.484  1.00 112.19 ?  350  TYR A OH  1 
ATOM   2395 N  N   . GLN A 1 352 ? 30.736  9.268   -11.539 1.00 129.29 ?  351  GLN A N   1 
ATOM   2396 C  CA  . GLN A 1 352 ? 32.103  9.720   -11.338 1.00 121.85 ?  351  GLN A CA  1 
ATOM   2397 C  C   . GLN A 1 352 ? 32.885  9.661   -12.642 1.00 128.95 ?  351  GLN A C   1 
ATOM   2398 O  O   . GLN A 1 352 ? 34.108  9.796   -12.663 1.00 134.48 ?  351  GLN A O   1 
ATOM   2399 C  CB  . GLN A 1 352 ? 32.849  8.765   -10.402 1.00 123.13 ?  351  GLN A CB  1 
ATOM   2400 C  CG  . GLN A 1 352 ? 34.086  9.337   -9.732  1.00 134.87 ?  351  GLN A CG  1 
ATOM   2401 C  CD  . GLN A 1 352 ? 34.660  8.402   -8.678  1.00 134.67 ?  351  GLN A CD  1 
ATOM   2402 O  OE1 . GLN A 1 352 ? 34.104  7.336   -8.409  1.00 128.49 ?  351  GLN A OE1 1 
ATOM   2403 N  NE2 . GLN A 1 352 ? 35.776  8.799   -8.076  1.00 132.63 ?  351  GLN A NE2 1 
ATOM   2404 N  N   . GLN A 1 353 ? 32.154  9.442   -13.731 1.00 134.69 ?  352  GLN A N   1 
ATOM   2405 C  CA  . GLN A 1 353 ? 32.825  9.349   -15.047 1.00 133.76 ?  352  GLN A CA  1 
ATOM   2406 C  C   . GLN A 1 353 ? 33.247  10.668  -15.633 1.00 133.16 ?  352  GLN A C   1 
ATOM   2407 O  O   . GLN A 1 353 ? 32.672  11.701  -15.288 1.00 118.61 ?  352  GLN A O   1 
ATOM   2408 C  CB  . GLN A 1 353 ? 31.874  8.642   -16.003 1.00 126.65 ?  352  GLN A CB  1 
ATOM   2409 C  CG  . GLN A 1 353 ? 30.651  9.432   -16.356 1.00 109.39 ?  352  GLN A CG  1 
ATOM   2410 C  CD  . GLN A 1 353 ? 29.666  9.444   -15.213 1.00 96.61  ?  352  GLN A CD  1 
ATOM   2411 O  OE1 . GLN A 1 353 ? 29.911  8.856   -14.160 1.00 113.83 ?  352  GLN A OE1 1 
ATOM   2412 N  NE2 . GLN A 1 353 ? 28.530  10.100  -15.421 1.00 86.39  ?  352  GLN A NE2 1 
ATOM   2413 N  N   . ASN A 1 354 ? 34.280  10.636  -16.466 1.00 149.37 ?  353  ASN A N   1 
ATOM   2414 C  CA  . ASN A 1 354 ? 34.893  11.821  -17.048 1.00 154.88 ?  353  ASN A CA  1 
ATOM   2415 C  C   . ASN A 1 354 ? 34.110  12.629  -18.074 1.00 156.09 ?  353  ASN A C   1 
ATOM   2416 O  O   . ASN A 1 354 ? 33.137  12.136  -18.636 1.00 142.68 ?  353  ASN A O   1 
ATOM   2417 C  CB  . ASN A 1 354 ? 36.133  11.196  -17.688 1.00 163.64 ?  353  ASN A CB  1 
ATOM   2418 C  CG  . ASN A 1 354 ? 37.268  12.183  -17.848 1.00 171.16 ?  353  ASN A CG  1 
ATOM   2419 O  OD1 . ASN A 1 354 ? 37.057  13.346  -18.187 1.00 176.06 ?  353  ASN A OD1 1 
ATOM   2420 N  ND2 . ASN A 1 354 ? 38.485  11.724  -17.584 1.00 173.13 ?  353  ASN A ND2 1 
ATOM   2421 N  N   . PHE A 1 355 ? 34.528  13.872  -18.308 1.00 172.81 ?  354  PHE A N   1 
ATOM   2422 C  CA  . PHE A 1 355 ? 33.828  14.759  -19.236 1.00 164.94 ?  354  PHE A CA  1 
ATOM   2423 C  C   . PHE A 1 355 ? 34.072  14.369  -20.693 1.00 166.25 ?  354  PHE A C   1 
ATOM   2424 O  O   . PHE A 1 355 ? 34.542  15.164  -21.507 1.00 149.82 ?  354  PHE A O   1 
ATOM   2425 C  CB  . PHE A 1 355 ? 34.246  16.212  -19.009 1.00 180.33 ?  354  PHE A CB  1 
ATOM   2426 C  CG  . PHE A 1 355 ? 33.429  16.920  -17.964 1.00 199.94 ?  354  PHE A CG  1 
ATOM   2427 C  CD1 . PHE A 1 355 ? 32.249  16.362  -17.495 1.00 204.63 ?  354  PHE A CD1 1 
ATOM   2428 C  CD2 . PHE A 1 355 ? 33.834  18.148  -17.458 1.00 204.09 ?  354  PHE A CD2 1 
ATOM   2429 C  CE1 . PHE A 1 355 ? 31.491  17.012  -16.535 1.00 201.80 ?  354  PHE A CE1 1 
ATOM   2430 C  CE2 . PHE A 1 355 ? 33.079  18.804  -16.498 1.00 205.25 ?  354  PHE A CE2 1 
ATOM   2431 C  CZ  . PHE A 1 355 ? 31.906  18.234  -16.037 1.00 203.99 ?  354  PHE A CZ  1 
ATOM   2432 N  N   . VAL A 1 356 ? 33.729  13.122  -20.995 1.00 183.33 ?  355  VAL A N   1 
ATOM   2433 C  CA  . VAL A 1 356 ? 33.880  12.519  -22.316 1.00 190.84 ?  355  VAL A CA  1 
ATOM   2434 C  C   . VAL A 1 356 ? 32.906  12.986  -23.429 1.00 152.78 ?  355  VAL A C   1 
ATOM   2435 O  O   . VAL A 1 356 ? 33.377  13.281  -24.530 1.00 158.74 ?  355  VAL A O   1 
ATOM   2436 C  CB  . VAL A 1 356 ? 33.784  10.973  -22.218 1.00 159.89 ?  355  VAL A CB  1 
ATOM   2437 C  CG1 . VAL A 1 356 ? 34.177  10.326  -23.535 1.00 162.63 ?  355  VAL A CG1 1 
ATOM   2438 C  CG2 . VAL A 1 356 ? 34.663  10.452  -21.086 1.00 160.71 ?  355  VAL A CG2 1 
ATOM   2439 N  N   . ASP A 1 357 ? 31.586  13.076  -23.192 1.00 129.78 ?  356  ASP A N   1 
ATOM   2440 C  CA  . ASP A 1 357 ? 30.960  13.438  -21.907 1.00 136.41 ?  356  ASP A CA  1 
ATOM   2441 C  C   . ASP A 1 357 ? 30.831  12.360  -20.834 1.00 148.02 ?  356  ASP A C   1 
ATOM   2442 O  O   . ASP A 1 357 ? 30.725  12.698  -19.653 1.00 153.16 ?  356  ASP A O   1 
ATOM   2443 C  CB  . ASP A 1 357 ? 29.558  13.999  -22.144 1.00 131.40 ?  356  ASP A CB  1 
ATOM   2444 C  CG  . ASP A 1 357 ? 28.701  13.082  -22.977 1.00 141.92 ?  356  ASP A CG  1 
ATOM   2445 O  OD1 . ASP A 1 357 ? 29.067  12.838  -24.144 1.00 140.24 ?  356  ASP A OD1 1 
ATOM   2446 O  OD2 . ASP A 1 357 ? 27.691  12.566  -22.455 1.00 151.83 ?  356  ASP A OD2 1 
ATOM   2447 N  N   . GLY A 1 358 ? 30.802  11.087  -21.219 1.00 142.14 ?  357  GLY A N   1 
ATOM   2448 C  CA  . GLY A 1 358 ? 30.667  10.002  -20.256 1.00 135.44 ?  357  GLY A CA  1 
ATOM   2449 C  C   . GLY A 1 358 ? 29.364  9.976   -19.473 1.00 125.63 ?  357  GLY A C   1 
ATOM   2450 O  O   . GLY A 1 358 ? 29.026  8.972   -18.843 1.00 125.31 ?  357  GLY A O   1 
ATOM   2451 N  N   . SER A 1 359 ? 28.629  11.081  -19.520 1.00 120.27 ?  358  SER A N   1 
ATOM   2452 C  CA  . SER A 1 359 ? 27.326  11.175  -18.892 1.00 121.25 ?  358  SER A CA  1 
ATOM   2453 C  C   . SER A 1 359 ? 26.390  10.317  -19.736 1.00 148.39 ?  358  SER A C   1 
ATOM   2454 O  O   . SER A 1 359 ? 26.660  10.097  -20.918 1.00 166.87 ?  358  SER A O   1 
ATOM   2455 C  CB  . SER A 1 359 ? 26.875  12.638  -18.820 1.00 126.14 ?  358  SER A CB  1 
ATOM   2456 O  OG  . SER A 1 359 ? 26.931  13.254  -20.095 1.00 144.20 ?  358  SER A OG  1 
ATOM   2457 N  N   . PHE A 1 360 ? 25.294  9.828   -19.167 1.00 140.27 ?  359  PHE A N   1 
ATOM   2458 C  CA  . PHE A 1 360 ? 24.747  10.268  -17.892 1.00 118.71 ?  359  PHE A CA  1 
ATOM   2459 C  C   . PHE A 1 360 ? 24.249  9.047   -17.138 1.00 125.41 ?  359  PHE A C   1 
ATOM   2460 O  O   . PHE A 1 360 ? 23.464  8.265   -17.676 1.00 143.97 ?  359  PHE A O   1 
ATOM   2461 C  CB  . PHE A 1 360 ? 23.630  11.281  -18.152 1.00 102.81 ?  359  PHE A CB  1 
ATOM   2462 C  CG  . PHE A 1 360 ? 22.945  11.778  -16.922 1.00 86.92  ?  359  PHE A CG  1 
ATOM   2463 C  CD1 . PHE A 1 360 ? 23.440  12.863  -16.229 1.00 94.10  ?  359  PHE A CD1 1 
ATOM   2464 C  CD2 . PHE A 1 360 ? 21.782  11.178  -16.479 1.00 86.87  ?  359  PHE A CD2 1 
ATOM   2465 C  CE1 . PHE A 1 360 ? 22.794  13.332  -15.105 1.00 98.12  ?  359  PHE A CE1 1 
ATOM   2466 C  CE2 . PHE A 1 360 ? 21.134  11.638  -15.356 1.00 90.54  ?  359  PHE A CE2 1 
ATOM   2467 C  CZ  . PHE A 1 360 ? 21.641  12.717  -14.666 1.00 93.80  ?  359  PHE A CZ  1 
ATOM   2468 N  N   . SER A 1 361 ? 24.707  8.863   -15.904 1.00 109.96 ?  360  SER A N   1 
ATOM   2469 C  CA  . SER A 1 361 ? 24.421  7.616   -15.206 1.00 102.10 ?  360  SER A CA  1 
ATOM   2470 C  C   . SER A 1 361 ? 23.116  7.648   -14.433 1.00 89.91  ?  360  SER A C   1 
ATOM   2471 O  O   . SER A 1 361 ? 23.084  7.998   -13.256 1.00 90.44  ?  360  SER A O   1 
ATOM   2472 C  CB  . SER A 1 361 ? 25.565  7.261   -14.256 1.00 80.16  ?  360  SER A CB  1 
ATOM   2473 O  OG  . SER A 1 361 ? 26.598  6.583   -14.951 1.00 102.77 ?  360  SER A OG  1 
ATOM   2474 N  N   . LEU A 1 362 ? 22.044  7.251   -15.115 1.00 94.09  ?  361  LEU A N   1 
ATOM   2475 C  CA  . LEU A 1 362 ? 20.761  7.005   -14.473 1.00 99.66  ?  361  LEU A CA  1 
ATOM   2476 C  C   . LEU A 1 362 ? 20.913  5.764   -13.605 1.00 108.20 ?  361  LEU A C   1 
ATOM   2477 O  O   . LEU A 1 362 ? 20.145  5.541   -12.671 1.00 115.43 ?  361  LEU A O   1 
ATOM   2478 C  CB  . LEU A 1 362 ? 19.641  6.835   -15.504 1.00 102.16 ?  361  LEU A CB  1 
ATOM   2479 C  CG  . LEU A 1 362 ? 18.222  6.688   -14.945 1.00 113.12 ?  361  LEU A CG  1 
ATOM   2480 C  CD1 . LEU A 1 362 ? 17.234  7.435   -15.813 1.00 108.83 ?  361  LEU A CD1 1 
ATOM   2481 C  CD2 . LEU A 1 362 ? 17.823  5.220   -14.850 1.00 132.55 ?  361  LEU A CD2 1 
ATOM   2482 N  N   . SER A 1 363 ? 21.904  4.947   -13.946 1.00 105.50 ?  362  SER A N   1 
ATOM   2483 C  CA  . SER A 1 363 ? 22.227  3.765   -13.164 1.00 112.30 ?  362  SER A CA  1 
ATOM   2484 C  C   . SER A 1 363 ? 22.569  4.180   -11.742 1.00 127.42 ?  362  SER A C   1 
ATOM   2485 O  O   . SER A 1 363 ? 22.129  3.558   -10.775 1.00 139.68 ?  362  SER A O   1 
ATOM   2486 C  CB  . SER A 1 363 ? 23.399  3.004   -13.785 1.00 100.95 ?  362  SER A CB  1 
ATOM   2487 O  OG  . SER A 1 363 ? 24.476  3.875   -14.088 1.00 83.67  ?  362  SER A OG  1 
ATOM   2488 N  N   . GLN A 1 364 ? 23.351  5.248   -11.626 1.00 120.76 ?  363  GLN A N   1 
ATOM   2489 C  CA  . GLN A 1 364 ? 23.726  5.789   -10.325 1.00 112.97 ?  363  GLN A CA  1 
ATOM   2490 C  C   . GLN A 1 364 ? 22.585  6.544   -9.649  1.00 84.70  ?  363  GLN A C   1 
ATOM   2491 O  O   . GLN A 1 364 ? 22.472  6.540   -8.428  1.00 93.39  ?  363  GLN A O   1 
ATOM   2492 C  CB  . GLN A 1 364 ? 24.947  6.688   -10.473 1.00 84.26  ?  363  GLN A CB  1 
ATOM   2493 C  CG  . GLN A 1 364 ? 26.235  5.906   -10.654 1.00 85.49  ?  363  GLN A CG  1 
ATOM   2494 C  CD  . GLN A 1 364 ? 27.427  6.804   -10.870 1.00 94.66  ?  363  GLN A CD  1 
ATOM   2495 O  OE1 . GLN A 1 364 ? 28.404  6.423   -11.518 1.00 93.37  ?  363  GLN A OE1 1 
ATOM   2496 N  NE2 . GLN A 1 364 ? 27.362  8.006   -10.314 1.00 94.85  ?  363  GLN A NE2 1 
ATOM   2497 N  N   . LEU A 1 365 ? 21.763  7.220   -10.443 1.00 82.91  ?  364  LEU A N   1 
ATOM   2498 C  CA  . LEU A 1 365 ? 20.543  7.849   -9.941  1.00 91.69  ?  364  LEU A CA  1 
ATOM   2499 C  C   . LEU A 1 365 ? 19.540  6.830   -9.405  1.00 108.63 ?  364  LEU A C   1 
ATOM   2500 O  O   . LEU A 1 365 ? 18.912  7.043   -8.369  1.00 92.75  ?  364  LEU A O   1 
ATOM   2501 C  CB  . LEU A 1 365 ? 19.874  8.677   -11.035 1.00 94.51  ?  364  LEU A CB  1 
ATOM   2502 C  CG  . LEU A 1 365 ? 20.175  10.173  -11.019 1.00 107.63 ?  364  LEU A CG  1 
ATOM   2503 C  CD1 . LEU A 1 365 ? 21.421  10.472  -11.836 1.00 121.74 ?  364  LEU A CD1 1 
ATOM   2504 C  CD2 . LEU A 1 365 ? 18.978  10.958  -11.528 1.00 106.50 ?  364  LEU A CD2 1 
ATOM   2505 N  N   . GLU A 1 366 ? 19.369  5.738   -10.144 1.00 128.74 ?  365  GLU A N   1 
ATOM   2506 C  CA  . GLU A 1 366 ? 18.408  4.706   -9.779  1.00 133.77 ?  365  GLU A CA  1 
ATOM   2507 C  C   . GLU A 1 366 ? 18.852  4.037   -8.486  1.00 142.72 ?  365  GLU A C   1 
ATOM   2508 O  O   . GLU A 1 366 ? 18.023  3.658   -7.657  1.00 157.39 ?  365  GLU A O   1 
ATOM   2509 C  CB  . GLU A 1 366 ? 18.256  3.672   -10.901 1.00 137.81 ?  365  GLU A CB  1 
ATOM   2510 C  CG  . GLU A 1 366 ? 16.911  2.952   -10.904 1.00 141.31 ?  365  GLU A CG  1 
ATOM   2511 C  CD  . GLU A 1 366 ? 16.827  1.861   -11.954 1.00 135.61 ?  365  GLU A CD  1 
ATOM   2512 O  OE1 . GLU A 1 366 ? 17.816  1.665   -12.693 1.00 133.22 ?  365  GLU A OE1 1 
ATOM   2513 O  OE2 . GLU A 1 366 ? 15.768  1.206   -12.040 1.00 135.79 ?  365  GLU A OE2 1 
ATOM   2514 N  N   . SER A 1 367 ? 20.165  3.901   -8.322  1.00 117.31 ?  366  SER A N   1 
ATOM   2515 C  CA  . SER A 1 367 ? 20.734  3.287   -7.128  1.00 110.76 ?  366  SER A CA  1 
ATOM   2516 C  C   . SER A 1 367 ? 20.392  4.063   -5.859  1.00 123.12 ?  366  SER A C   1 
ATOM   2517 O  O   . SER A 1 367 ? 19.921  3.471   -4.889  1.00 139.92 ?  366  SER A O   1 
ATOM   2518 C  CB  . SER A 1 367 ? 22.252  3.155   -7.260  1.00 93.43  ?  366  SER A CB  1 
ATOM   2519 O  OG  . SER A 1 367 ? 22.605  2.331   -8.355  1.00 93.20  ?  366  SER A OG  1 
ATOM   2520 N  N   . VAL A 1 368 ? 20.607  5.380   -5.868  1.00 114.57 ?  367  VAL A N   1 
ATOM   2521 C  CA  . VAL A 1 368 ? 20.354  6.196   -4.676  1.00 112.34 ?  367  VAL A CA  1 
ATOM   2522 C  C   . VAL A 1 368 ? 18.884  6.105   -4.279  1.00 112.11 ?  367  VAL A C   1 
ATOM   2523 O  O   . VAL A 1 368 ? 18.556  6.124   -3.095  1.00 131.32 ?  367  VAL A O   1 
ATOM   2524 C  CB  . VAL A 1 368 ? 20.773  7.698   -4.854  1.00 97.10  ?  367  VAL A CB  1 
ATOM   2525 C  CG1 . VAL A 1 368 ? 22.208  7.821   -5.349  1.00 90.04  ?  367  VAL A CG1 1 
ATOM   2526 C  CG2 . VAL A 1 368 ? 19.826  8.448   -5.768  1.00 101.32 ?  367  VAL A CG2 1 
ATOM   2527 N  N   . MET A 1 369 ? 18.005  5.993   -5.268  1.00 97.16  ?  368  MET A N   1 
ATOM   2528 C  CA  . MET A 1 369 ? 16.587  5.818   -5.004  1.00 109.88 ?  368  MET A CA  1 
ATOM   2529 C  C   . MET A 1 369 ? 16.327  4.490   -4.298  1.00 121.54 ?  368  MET A C   1 
ATOM   2530 O  O   . MET A 1 369 ? 15.506  4.415   -3.384  1.00 119.77 ?  368  MET A O   1 
ATOM   2531 C  CB  . MET A 1 369 ? 15.797  5.893   -6.307  1.00 125.67 ?  368  MET A CB  1 
ATOM   2532 C  CG  . MET A 1 369 ? 15.851  7.248   -6.989  1.00 123.50 ?  368  MET A CG  1 
ATOM   2533 S  SD  . MET A 1 369 ? 14.423  8.263   -6.558  1.00 134.31 ?  368  MET A SD  1 
ATOM   2534 C  CE  . MET A 1 369 ? 13.098  7.147   -7.013  1.00 139.86 ?  368  MET A CE  1 
ATOM   2535 N  N   . LYS A 1 370 ? 17.040  3.450   -4.722  1.00 137.87 ?  369  LYS A N   1 
ATOM   2536 C  CA  . LYS A 1 370 ? 16.873  2.118   -4.149  1.00 159.78 ?  369  LYS A CA  1 
ATOM   2537 C  C   . LYS A 1 370 ? 17.320  2.050   -2.687  1.00 175.46 ?  369  LYS A C   1 
ATOM   2538 O  O   . LYS A 1 370 ? 16.587  1.545   -1.835  1.00 199.62 ?  369  LYS A O   1 
ATOM   2539 C  CB  . LYS A 1 370 ? 17.637  1.080   -4.976  1.00 166.39 ?  369  LYS A CB  1 
ATOM   2540 C  CG  . LYS A 1 370 ? 16.983  0.723   -6.306  1.00 165.65 ?  369  LYS A CG  1 
ATOM   2541 C  CD  . LYS A 1 370 ? 17.720  -0.429  -6.980  1.00 166.37 ?  369  LYS A CD  1 
ATOM   2542 C  CE  . LYS A 1 370 ? 18.170  -0.062  -8.386  1.00 166.54 ?  369  LYS A CE  1 
ATOM   2543 N  NZ  . LYS A 1 370 ? 19.612  -0.374  -8.600  1.00 160.91 ?  369  LYS A NZ  1 
ATOM   2544 N  N   . GLU A 1 371 ? 18.515  2.553   -2.396  1.00 165.35 ?  370  GLU A N   1 
ATOM   2545 C  CA  . GLU A 1 371 ? 19.047  2.498   -1.036  1.00 156.54 ?  370  GLU A CA  1 
ATOM   2546 C  C   . GLU A 1 371 ? 18.261  3.397   -0.090  1.00 146.16 ?  370  GLU A C   1 
ATOM   2547 O  O   . GLU A 1 371 ? 18.037  3.049   1.070   1.00 165.75 ?  370  GLU A O   1 
ATOM   2548 C  CB  . GLU A 1 371 ? 20.525  2.891   -1.015  1.00 150.52 ?  370  GLU A CB  1 
ATOM   2549 C  CG  . GLU A 1 371 ? 21.167  2.901   0.373   1.00 154.52 ?  370  GLU A CG  1 
ATOM   2550 C  CD  . GLU A 1 371 ? 21.099  1.555   1.076   1.00 154.04 ?  370  GLU A CD  1 
ATOM   2551 O  OE1 . GLU A 1 371 ? 21.508  0.545   0.468   1.00 150.03 ?  370  GLU A OE1 1 
ATOM   2552 O  OE2 . GLU A 1 371 ? 20.660  1.509   2.246   1.00 154.83 ?  370  GLU A OE2 1 
ATOM   2553 N  N   . LEU A 1 372 ? 17.850  4.557   -0.586  1.00 115.45 ?  371  LEU A N   1 
ATOM   2554 C  CA  . LEU A 1 372 ? 17.158  5.524   0.253   1.00 128.78 ?  371  LEU A CA  1 
ATOM   2555 C  C   . LEU A 1 372 ? 15.806  5.001   0.716   1.00 144.09 ?  371  LEU A C   1 
ATOM   2556 O  O   . LEU A 1 372 ? 15.438  5.187   1.875   1.00 157.50 ?  371  LEU A O   1 
ATOM   2557 C  CB  . LEU A 1 372 ? 16.980  6.853   -0.478  1.00 125.59 ?  371  LEU A CB  1 
ATOM   2558 C  CG  . LEU A 1 372 ? 16.456  8.033   0.345   1.00 125.17 ?  371  LEU A CG  1 
ATOM   2559 C  CD1 . LEU A 1 372 ? 17.042  9.315   -0.213  1.00 120.41 ?  371  LEU A CD1 1 
ATOM   2560 C  CD2 . LEU A 1 372 ? 14.926  8.116   0.369   1.00 129.27 ?  371  LEU A CD2 1 
ATOM   2561 N  N   . TYR A 1 373 ? 15.072  4.357   -0.186  1.00 144.29 ?  372  TYR A N   1 
ATOM   2562 C  CA  . TYR A 1 373 ? 13.738  3.862   0.135   1.00 163.92 ?  372  TYR A CA  1 
ATOM   2563 C  C   . TYR A 1 373 ? 13.782  2.916   1.343   1.00 184.17 ?  372  TYR A C   1 
ATOM   2564 O  O   . TYR A 1 373 ? 12.960  3.034   2.249   1.00 192.97 ?  372  TYR A O   1 
ATOM   2565 C  CB  . TYR A 1 373 ? 13.103  3.167   -1.074  1.00 168.13 ?  372  TYR A CB  1 
ATOM   2566 C  CG  . TYR A 1 373 ? 11.667  2.735   -0.843  1.00 177.07 ?  372  TYR A CG  1 
ATOM   2567 C  CD1 . TYR A 1 373 ? 10.628  3.646   -0.996  1.00 180.98 ?  372  TYR A CD1 1 
ATOM   2568 C  CD2 . TYR A 1 373 ? 11.347  1.437   -0.464  1.00 185.18 ?  372  TYR A CD2 1 
ATOM   2569 C  CE1 . TYR A 1 373 ? 9.311   3.280   -0.787  1.00 191.69 ?  372  TYR A CE1 1 
ATOM   2570 C  CE2 . TYR A 1 373 ? 10.025  1.060   -0.249  1.00 191.53 ?  372  TYR A CE2 1 
ATOM   2571 C  CZ  . TYR A 1 373 ? 9.013   1.988   -0.413  1.00 191.15 ?  372  TYR A CZ  1 
ATOM   2572 O  OH  . TYR A 1 373 ? 7.700   1.629   -0.204  1.00 189.52 ?  372  TYR A OH  1 
ATOM   2573 N  N   . ARG A 1 374 ? 14.733  1.983   1.361   1.00 189.06 ?  373  ARG A N   1 
ATOM   2574 C  CA  . ARG A 1 374 ? 14.830  1.051   2.485   1.00 198.08 ?  373  ARG A CA  1 
ATOM   2575 C  C   . ARG A 1 374 ? 15.308  1.767   3.753   1.00 194.04 ?  373  ARG A C   1 
ATOM   2576 O  O   . ARG A 1 374 ? 14.885  1.426   4.856   1.00 207.35 ?  373  ARG A O   1 
ATOM   2577 C  CB  . ARG A 1 374 ? 15.759  -0.129  2.157   1.00 203.88 ?  373  ARG A CB  1 
ATOM   2578 C  CG  . ARG A 1 374 ? 17.245  0.200   2.122   1.00 203.20 ?  373  ARG A CG  1 
ATOM   2579 C  CD  . ARG A 1 374 ? 18.094  -0.965  2.618   1.00 214.31 ?  373  ARG A CD  1 
ATOM   2580 N  NE  . ARG A 1 374 ? 17.751  -1.348  3.986   1.00 222.46 ?  373  ARG A NE  1 
ATOM   2581 C  CZ  . ARG A 1 374 ? 18.423  -2.243  4.704   1.00 228.00 ?  373  ARG A CZ  1 
ATOM   2582 N  NH1 . ARG A 1 374 ? 19.483  -2.849  4.188   1.00 226.32 ?  373  ARG A NH1 1 
ATOM   2583 N  NH2 . ARG A 1 374 ? 18.037  -2.531  5.941   1.00 234.82 ?  373  ARG A NH2 1 
ATOM   2584 N  N   . GLU A 1 375 ? 16.190  2.752   3.596   1.00 176.83 ?  374  GLU A N   1 
ATOM   2585 C  CA  . GLU A 1 375 ? 16.654  3.549   4.729   1.00 172.90 ?  374  GLU A CA  1 
ATOM   2586 C  C   . GLU A 1 375 ? 15.528  4.433   5.267   1.00 183.50 ?  374  GLU A C   1 
ATOM   2587 O  O   . GLU A 1 375 ? 15.282  4.479   6.472   1.00 199.00 ?  374  GLU A O   1 
ATOM   2588 C  CB  . GLU A 1 375 ? 17.866  4.402   4.336   1.00 157.90 ?  374  GLU A CB  1 
ATOM   2589 C  CG  . GLU A 1 375 ? 19.206  3.834   4.790   1.00 151.00 ?  374  GLU A CG  1 
ATOM   2590 C  CD  . GLU A 1 375 ? 19.389  3.901   6.297   1.00 155.71 ?  374  GLU A CD  1 
ATOM   2591 O  OE1 . GLU A 1 375 ? 18.750  4.764   6.935   1.00 153.34 ?  374  GLU A OE1 1 
ATOM   2592 O  OE2 . GLU A 1 375 ? 20.173  3.096   6.846   1.00 160.85 ?  374  GLU A OE2 1 
ATOM   2593 N  N   . SER A 1 376 ? 14.847  5.123   4.357   1.00 176.58 ?  375  SER A N   1 
ATOM   2594 C  CA  . SER A 1 376 ? 13.670  5.932   4.677   1.00 179.98 ?  375  SER A CA  1 
ATOM   2595 C  C   . SER A 1 376 ? 12.503  5.075   5.154   1.00 192.12 ?  375  SER A C   1 
ATOM   2596 O  O   . SER A 1 376 ? 11.669  5.523   5.944   1.00 184.08 ?  375  SER A O   1 
ATOM   2597 C  CB  . SER A 1 376 ? 13.235  6.767   3.467   1.00 173.36 ?  375  SER A CB  1 
ATOM   2598 O  OG  . SER A 1 376 ? 12.727  5.945   2.430   1.00 166.53 ?  375  SER A OG  1 
ATOM   2599 N  N   . GLY A 1 377 ? 12.459  3.838   4.672   1.00 202.97 ?  376  GLY A N   1 
ATOM   2600 C  CA  . GLY A 1 377 ? 11.350  2.937   4.920   1.00 191.79 ?  376  GLY A CA  1 
ATOM   2601 C  C   . GLY A 1 377 ? 10.265  3.015   3.861   1.00 183.24 ?  376  GLY A C   1 
ATOM   2602 O  O   . GLY A 1 377 ? 10.380  3.745   2.880   1.00 172.58 ?  376  GLY A O   1 
ATOM   2603 N  N   . ASN A 1 378 ? 9.190   2.270   4.086   1.00 207.18 ?  377  ASN A N   1 
ATOM   2604 C  CA  . ASN A 1 378 ? 8.134   2.068   3.093   1.00 226.38 ?  377  ASN A CA  1 
ATOM   2605 C  C   . ASN A 1 378 ? 7.181   3.223   2.785   1.00 230.88 ?  377  ASN A C   1 
ATOM   2606 O  O   . ASN A 1 378 ? 6.176   3.017   2.101   1.00 236.95 ?  377  ASN A O   1 
ATOM   2607 C  CB  . ASN A 1 378 ? 7.287   0.869   3.526   1.00 242.95 ?  377  ASN A CB  1 
ATOM   2608 C  CG  . ASN A 1 378 ? 8.072   -0.429  3.523   1.00 250.44 ?  377  ASN A CG  1 
ATOM   2609 O  OD1 . ASN A 1 378 ? 8.221   -1.078  2.488   1.00 253.05 ?  377  ASN A OD1 1 
ATOM   2610 N  ND2 . ASN A 1 378 ? 8.581   -0.813  4.686   1.00 252.25 ?  377  ASN A ND2 1 
ATOM   2611 N  N   . ASN A 1 379 ? 7.468   4.429   3.262   1.00 228.98 ?  378  ASN A N   1 
ATOM   2612 C  CA  . ASN A 1 379 ? 6.471   5.495   3.147   1.00 232.15 ?  378  ASN A CA  1 
ATOM   2613 C  C   . ASN A 1 379 ? 6.738   6.565   2.080   1.00 212.37 ?  378  ASN A C   1 
ATOM   2614 O  O   . ASN A 1 379 ? 5.826   6.945   1.346   1.00 209.98 ?  378  ASN A O   1 
ATOM   2615 C  CB  . ASN A 1 379 ? 6.287   6.173   4.511   1.00 249.38 ?  378  ASN A CB  1 
ATOM   2616 C  CG  . ASN A 1 379 ? 7.584   6.724   5.068   1.00 254.07 ?  378  ASN A CG  1 
ATOM   2617 O  OD1 . ASN A 1 379 ? 8.671   6.367   4.611   1.00 256.34 ?  378  ASN A OD1 1 
ATOM   2618 N  ND2 . ASN A 1 379 ? 7.477   7.595   6.065   1.00 253.63 ?  378  ASN A ND2 1 
ATOM   2619 N  N   . LYS A 1 380 ? 7.979   7.035   1.984   1.00 196.24 ?  379  LYS A N   1 
ATOM   2620 C  CA  . LYS A 1 380 ? 8.307   8.184   1.134   1.00 176.43 ?  379  LYS A CA  1 
ATOM   2621 C  C   . LYS A 1 380 ? 9.429   7.948   0.122   1.00 169.78 ?  379  LYS A C   1 
ATOM   2622 O  O   . LYS A 1 380 ? 10.360  7.178   0.358   1.00 164.25 ?  379  LYS A O   1 
ATOM   2623 C  CB  . LYS A 1 380 ? 8.642   9.402   2.001   1.00 166.91 ?  379  LYS A CB  1 
ATOM   2624 C  CG  . LYS A 1 380 ? 7.444   9.945   2.770   1.00 163.39 ?  379  LYS A CG  1 
ATOM   2625 C  CD  . LYS A 1 380 ? 6.355   10.420  1.812   1.00 150.71 ?  379  LYS A CD  1 
ATOM   2626 C  CE  . LYS A 1 380 ? 5.126   10.932  2.552   1.00 147.76 ?  379  LYS A CE  1 
ATOM   2627 N  NZ  . LYS A 1 380 ? 4.411   9.854   3.295   1.00 145.91 ?  379  LYS A NZ  1 
ATOM   2628 N  N   . TRP A 1 381 ? 9.309   8.631   -1.012  1.00 169.31 ?  380  TRP A N   1 
ATOM   2629 C  CA  . TRP A 1 381 ? 10.263  8.539   -2.107  1.00 164.34 ?  380  TRP A CA  1 
ATOM   2630 C  C   . TRP A 1 381 ? 10.984  9.879   -2.241  1.00 143.27 ?  380  TRP A C   1 
ATOM   2631 O  O   . TRP A 1 381 ? 10.393  10.933  -1.995  1.00 144.11 ?  380  TRP A O   1 
ATOM   2632 C  CB  . TRP A 1 381 ? 9.545   8.197   -3.412  1.00 183.01 ?  380  TRP A CB  1 
ATOM   2633 C  CG  . TRP A 1 381 ? 9.205   6.752   -3.587  1.00 201.93 ?  380  TRP A CG  1 
ATOM   2634 C  CD1 . TRP A 1 381 ? 7.980   6.174   -3.432  1.00 212.88 ?  380  TRP A CD1 1 
ATOM   2635 C  CD2 . TRP A 1 381 ? 10.096  5.706   -3.981  1.00 202.62 ?  380  TRP A CD2 1 
ATOM   2636 N  NE1 . TRP A 1 381 ? 8.055   4.828   -3.691  1.00 212.74 ?  380  TRP A NE1 1 
ATOM   2637 C  CE2 . TRP A 1 381 ? 9.343   4.516   -4.032  1.00 206.94 ?  380  TRP A CE2 1 
ATOM   2638 C  CE3 . TRP A 1 381 ? 11.457  5.659   -4.289  1.00 197.66 ?  380  TRP A CE3 1 
ATOM   2639 C  CZ2 . TRP A 1 381 ? 9.910   3.293   -4.380  1.00 207.73 ?  380  TRP A CZ2 1 
ATOM   2640 C  CZ3 . TRP A 1 381 ? 12.016  4.447   -4.634  1.00 195.25 ?  380  TRP A CZ3 1 
ATOM   2641 C  CH2 . TRP A 1 381 ? 11.245  3.279   -4.676  1.00 202.03 ?  380  TRP A CH2 1 
ATOM   2642 N  N   . PRO A 1 382 ? 12.266  9.848   -2.638  1.00 122.72 ?  381  PRO A N   1 
ATOM   2643 C  CA  . PRO A 1 382 ? 13.055  11.082  -2.688  1.00 115.03 ?  381  PRO A CA  1 
ATOM   2644 C  C   . PRO A 1 382 ? 12.921  11.826  -4.013  1.00 125.28 ?  381  PRO A C   1 
ATOM   2645 O  O   . PRO A 1 382 ? 13.073  11.234  -5.081  1.00 144.89 ?  381  PRO A O   1 
ATOM   2646 C  CB  . PRO A 1 382 ? 14.485  10.579  -2.492  1.00 101.42 ?  381  PRO A CB  1 
ATOM   2647 C  CG  . PRO A 1 382 ? 14.479  9.201   -3.088  1.00 98.00  ?  381  PRO A CG  1 
ATOM   2648 C  CD  . PRO A 1 382 ? 13.063  8.665   -3.009  1.00 108.50 ?  381  PRO A CD  1 
ATOM   2649 N  N   . LEU A 1 383 ? 12.633  13.120  -3.934  1.00 112.81 ?  382  LEU A N   1 
ATOM   2650 C  CA  . LEU A 1 383 ? 12.499  13.945  -5.128  1.00 112.10 ?  382  LEU A CA  1 
ATOM   2651 C  C   . LEU A 1 383 ? 13.854  14.199  -5.786  1.00 115.23 ?  382  LEU A C   1 
ATOM   2652 O  O   . LEU A 1 383 ? 14.857  14.387  -5.099  1.00 123.10 ?  382  LEU A O   1 
ATOM   2653 C  CB  . LEU A 1 383 ? 11.812  15.267  -4.776  1.00 103.53 ?  382  LEU A CB  1 
ATOM   2654 C  CG  . LEU A 1 383 ? 11.636  16.316  -5.871  1.00 98.17  ?  382  LEU A CG  1 
ATOM   2655 C  CD1 . LEU A 1 383 ? 10.336  17.042  -5.653  1.00 98.86  ?  382  LEU A CD1 1 
ATOM   2656 C  CD2 . LEU A 1 383 ? 12.783  17.305  -5.857  1.00 101.28 ?  382  LEU A CD2 1 
ATOM   2657 N  N   . ILE A 1 384 ? 13.875  14.212  -7.117  1.00 103.55 ?  383  ILE A N   1 
ATOM   2658 C  CA  . ILE A 1 384 ? 15.103  14.476  -7.859  1.00 98.81  ?  383  ILE A CA  1 
ATOM   2659 C  C   . ILE A 1 384 ? 14.951  15.695  -8.758  1.00 112.24 ?  383  ILE A C   1 
ATOM   2660 O  O   . ILE A 1 384 ? 13.994  15.794  -9.528  1.00 122.20 ?  383  ILE A O   1 
ATOM   2661 C  CB  . ILE A 1 384 ? 15.525  13.280  -8.729  1.00 91.36  ?  383  ILE A CB  1 
ATOM   2662 C  CG1 . ILE A 1 384 ? 15.430  11.973  -7.947  1.00 88.56  ?  383  ILE A CG1 1 
ATOM   2663 C  CG2 . ILE A 1 384 ? 16.940  13.468  -9.230  1.00 101.38 ?  383  ILE A CG2 1 
ATOM   2664 C  CD1 . ILE A 1 384 ? 15.385  10.751  -8.832  1.00 86.26  ?  383  ILE A CD1 1 
ATOM   2665 N  N   . LEU A 1 385 ? 15.905  16.616  -8.667  1.00 115.88 ?  384  LEU A N   1 
ATOM   2666 C  CA  . LEU A 1 385 ? 15.896  17.799  -9.520  1.00 113.83 ?  384  LEU A CA  1 
ATOM   2667 C  C   . LEU A 1 385 ? 16.983  17.765  -10.582 1.00 104.77 ?  384  LEU A C   1 
ATOM   2668 O  O   . LEU A 1 385 ? 18.180  17.748  -10.281 1.00 83.39  ?  384  LEU A O   1 
ATOM   2669 C  CB  . LEU A 1 385 ? 16.017  19.066  -8.676  1.00 129.26 ?  384  LEU A CB  1 
ATOM   2670 C  CG  . LEU A 1 385 ? 14.682  19.424  -8.023  1.00 132.32 ?  384  LEU A CG  1 
ATOM   2671 C  CD1 . LEU A 1 385 ? 14.884  20.124  -6.705  1.00 124.89 ?  384  LEU A CD1 1 
ATOM   2672 C  CD2 . LEU A 1 385 ? 13.854  20.287  -8.960  1.00 128.51 ?  384  LEU A CD2 1 
ATOM   2673 N  N   . LEU A 1 386 ? 16.531  17.757  -11.832 1.00 115.40 ?  385  LEU A N   1 
ATOM   2674 C  CA  . LEU A 1 386 ? 17.404  17.705  -12.991 1.00 122.51 ?  385  LEU A CA  1 
ATOM   2675 C  C   . LEU A 1 386 ? 16.918  18.717  -14.017 1.00 126.41 ?  385  LEU A C   1 
ATOM   2676 O  O   . LEU A 1 386 ? 15.724  19.024  -14.082 1.00 102.45 ?  385  LEU A O   1 
ATOM   2677 C  CB  . LEU A 1 386 ? 17.415  16.300  -13.596 1.00 108.15 ?  385  LEU A CB  1 
ATOM   2678 C  CG  . LEU A 1 386 ? 18.643  15.427  -13.350 1.00 87.83  ?  385  LEU A CG  1 
ATOM   2679 C  CD1 . LEU A 1 386 ? 18.405  14.020  -13.869 1.00 83.16  ?  385  LEU A CD1 1 
ATOM   2680 C  CD2 . LEU A 1 386 ? 19.867  16.040  -13.996 1.00 79.02  ?  385  LEU A CD2 1 
ATOM   2681 N  N   . HIS A 1 387 ? 17.843  19.246  -14.807 1.00 136.61 ?  386  HIS A N   1 
ATOM   2682 C  CA  . HIS A 1 387 ? 17.490  20.234  -15.813 1.00 148.77 ?  386  HIS A CA  1 
ATOM   2683 C  C   . HIS A 1 387 ? 16.633  19.591  -16.895 1.00 139.36 ?  386  HIS A C   1 
ATOM   2684 O  O   . HIS A 1 387 ? 16.690  18.379  -17.097 1.00 145.96 ?  386  HIS A O   1 
ATOM   2685 C  CB  . HIS A 1 387 ? 18.738  20.861  -16.421 1.00 164.19 ?  386  HIS A CB  1 
ATOM   2686 C  CG  . HIS A 1 387 ? 18.484  22.179  -17.080 1.00 187.64 ?  386  HIS A CG  1 
ATOM   2687 N  ND1 . HIS A 1 387 ? 18.105  22.291  -18.401 1.00 202.83 ?  386  HIS A ND1 1 
ATOM   2688 C  CD2 . HIS A 1 387 ? 18.549  23.442  -16.599 1.00 195.58 ?  386  HIS A CD2 1 
ATOM   2689 C  CE1 . HIS A 1 387 ? 17.949  23.567  -18.705 1.00 209.79 ?  386  HIS A CE1 1 
ATOM   2690 N  NE2 . HIS A 1 387 ? 18.214  24.287  -17.629 1.00 207.99 ?  386  HIS A NE2 1 
ATOM   2691 N  N   . LYS A 1 388 ? 15.838  20.399  -17.588 1.00 124.81 ?  387  LYS A N   1 
ATOM   2692 C  CA  . LYS A 1 388 ? 15.069  19.895  -18.719 1.00 107.05 ?  387  LYS A CA  1 
ATOM   2693 C  C   . LYS A 1 388 ? 15.981  19.323  -19.788 1.00 114.45 ?  387  LYS A C   1 
ATOM   2694 O  O   . LYS A 1 388 ? 15.642  18.320  -20.412 1.00 130.97 ?  387  LYS A O   1 
ATOM   2695 C  CB  . LYS A 1 388 ? 14.192  20.987  -19.325 1.00 98.23  ?  387  LYS A CB  1 
ATOM   2696 C  CG  . LYS A 1 388 ? 13.098  21.473  -18.407 1.00 102.59 ?  387  LYS A CG  1 
ATOM   2697 C  CD  . LYS A 1 388 ? 12.203  22.458  -19.125 1.00 118.33 ?  387  LYS A CD  1 
ATOM   2698 C  CE  . LYS A 1 388 ? 11.390  21.756  -20.189 1.00 112.39 ?  387  LYS A CE  1 
ATOM   2699 N  NZ  . LYS A 1 388 ? 10.508  20.738  -19.562 1.00 108.85 ?  387  LYS A NZ  1 
ATOM   2700 N  N   . ARG A 1 389 ? 17.130  19.959  -20.001 1.00 105.36 ?  388  ARG A N   1 
ATOM   2701 C  CA  . ARG A 1 389 ? 18.116  19.428  -20.935 1.00 112.40 ?  388  ARG A CA  1 
ATOM   2702 C  C   . ARG A 1 389 ? 18.467  17.982  -20.605 1.00 103.28 ?  388  ARG A C   1 
ATOM   2703 O  O   . ARG A 1 389 ? 18.446  17.119  -21.478 1.00 108.08 ?  388  ARG A O   1 
ATOM   2704 C  CB  . ARG A 1 389 ? 19.381  20.274  -20.971 1.00 127.02 ?  388  ARG A CB  1 
ATOM   2705 C  CG  . ARG A 1 389 ? 20.213  19.934  -22.194 1.00 147.90 ?  388  ARG A CG  1 
ATOM   2706 C  CD  . ARG A 1 389 ? 21.424  20.829  -22.331 1.00 165.09 ?  388  ARG A CD  1 
ATOM   2707 N  NE  . ARG A 1 389 ? 21.045  22.237  -22.283 1.00 174.76 ?  388  ARG A NE  1 
ATOM   2708 C  CZ  . ARG A 1 389 ? 21.004  23.036  -23.345 1.00 178.80 ?  388  ARG A CZ  1 
ATOM   2709 N  NH1 . ARG A 1 389 ? 21.333  22.568  -24.545 1.00 175.41 ?  388  ARG A NH1 1 
ATOM   2710 N  NH2 . ARG A 1 389 ? 20.645  24.307  -23.209 1.00 183.84 ?  388  ARG A NH2 1 
ATOM   2711 N  N   . ARG A 1 390 ? 18.809  17.724  -19.350 1.00 103.35 ?  389  ARG A N   1 
ATOM   2712 C  CA  . ARG A 1 390 ? 19.115  16.366  -18.920 1.00 109.89 ?  389  ARG A CA  1 
ATOM   2713 C  C   . ARG A 1 390 ? 17.892  15.460  -19.016 1.00 106.31 ?  389  ARG A C   1 
ATOM   2714 O  O   . ARG A 1 390 ? 17.994  14.306  -19.432 1.00 111.80 ?  389  ARG A O   1 
ATOM   2715 C  CB  . ARG A 1 390 ? 19.620  16.369  -17.481 1.00 120.04 ?  389  ARG A CB  1 
ATOM   2716 C  CG  . ARG A 1 390 ? 21.047  16.822  -17.273 1.00 126.28 ?  389  ARG A CG  1 
ATOM   2717 C  CD  . ARG A 1 390 ? 22.010  15.773  -17.792 1.00 114.49 ?  389  ARG A CD  1 
ATOM   2718 N  NE  . ARG A 1 390 ? 23.396  16.127  -17.513 1.00 114.82 ?  389  ARG A NE  1 
ATOM   2719 C  CZ  . ARG A 1 390 ? 24.160  16.831  -18.335 1.00 117.19 ?  389  ARG A CZ  1 
ATOM   2720 N  NH1 . ARG A 1 390 ? 23.664  17.248  -19.488 1.00 125.33 ?  389  ARG A NH1 1 
ATOM   2721 N  NH2 . ARG A 1 390 ? 25.412  17.115  -18.003 1.00 108.99 ?  389  ARG A NH2 1 
ATOM   2722 N  N   . VAL A 1 391 ? 16.737  15.994  -18.635 1.00 98.26  ?  390  VAL A N   1 
ATOM   2723 C  CA  . VAL A 1 391 ? 15.498  15.232  -18.660 1.00 103.44 ?  390  VAL A CA  1 
ATOM   2724 C  C   . VAL A 1 391 ? 15.072  14.890  -20.091 1.00 119.39 ?  390  VAL A C   1 
ATOM   2725 O  O   . VAL A 1 391 ? 14.664  13.761  -20.370 1.00 124.53 ?  390  VAL A O   1 
ATOM   2726 C  CB  . VAL A 1 391 ? 14.371  16.003  -17.938 1.00 97.66  ?  390  VAL A CB  1 
ATOM   2727 C  CG1 . VAL A 1 391 ? 12.999  15.470  -18.318 1.00 100.59 ?  390  VAL A CG1 1 
ATOM   2728 C  CG2 . VAL A 1 391 ? 14.578  15.939  -16.429 1.00 89.48  ?  390  VAL A CG2 1 
ATOM   2729 N  N   . LYS A 1 392 ? 15.200  15.851  -21.001 1.00 121.73 ?  391  LYS A N   1 
ATOM   2730 C  CA  . LYS A 1 392 ? 14.797  15.641  -22.390 1.00 110.65 ?  391  LYS A CA  1 
ATOM   2731 C  C   . LYS A 1 392 ? 15.674  14.605  -23.086 1.00 103.33 ?  391  LYS A C   1 
ATOM   2732 O  O   . LYS A 1 392 ? 15.164  13.738  -23.791 1.00 129.43 ?  391  LYS A O   1 
ATOM   2733 C  CB  . LYS A 1 392 ? 14.824  16.958  -23.169 1.00 107.47 ?  391  LYS A CB  1 
ATOM   2734 C  CG  . LYS A 1 392 ? 13.591  17.820  -22.953 1.00 110.14 ?  391  LYS A CG  1 
ATOM   2735 C  CD  . LYS A 1 392 ? 13.507  18.941  -23.975 1.00 113.76 ?  391  LYS A CD  1 
ATOM   2736 C  CE  . LYS A 1 392 ? 12.367  19.890  -23.639 1.00 122.76 ?  391  LYS A CE  1 
ATOM   2737 N  NZ  . LYS A 1 392 ? 11.076  19.168  -23.468 1.00 124.96 ?  391  LYS A NZ  1 
ATOM   2738 N  N   . THR A 1 393 ? 16.988  14.699  -22.891 1.00 78.72  ?  392  THR A N   1 
ATOM   2739 C  CA  . THR A 1 393 ? 17.928  13.733  -23.463 1.00 77.65  ?  392  THR A CA  1 
ATOM   2740 C  C   . THR A 1 393 ? 17.655  12.339  -22.916 1.00 105.22 ?  392  THR A C   1 
ATOM   2741 O  O   . THR A 1 393 ? 17.803  11.337  -23.616 1.00 91.47  ?  392  THR A O   1 
ATOM   2742 C  CB  . THR A 1 393 ? 19.387  14.118  -23.182 1.00 98.11  ?  392  THR A CB  1 
ATOM   2743 O  OG1 . THR A 1 393 ? 19.677  15.373  -23.808 1.00 102.91 ?  392  THR A OG1 1 
ATOM   2744 C  CG2 . THR A 1 393 ? 20.337  13.063  -23.729 1.00 89.62  ?  392  THR A CG2 1 
ATOM   2745 N  N   . LEU A 1 394 ? 17.270  12.282  -21.647 1.00 112.38 ?  393  LEU A N   1 
ATOM   2746 C  CA  . LEU A 1 394 ? 16.870  11.025  -21.030 1.00 110.28 ?  393  LEU A CA  1 
ATOM   2747 C  C   . LEU A 1 394 ? 15.567  10.497  -21.638 1.00 98.27  ?  393  LEU A C   1 
ATOM   2748 O  O   . LEU A 1 394 ? 15.425  9.297   -21.859 1.00 97.09  ?  393  LEU A O   1 
ATOM   2749 C  CB  . LEU A 1 394 ? 16.724  11.207  -19.520 1.00 116.82 ?  393  LEU A CB  1 
ATOM   2750 C  CG  . LEU A 1 394 ? 17.895  10.650  -18.710 1.00 121.02 ?  393  LEU A CG  1 
ATOM   2751 C  CD1 . LEU A 1 394 ? 17.963  9.153   -18.871 1.00 128.73 ?  393  LEU A CD1 1 
ATOM   2752 C  CD2 . LEU A 1 394 ? 19.213  11.288  -19.149 1.00 122.07 ?  393  LEU A CD2 1 
ATOM   2753 N  N   . LEU A 1 395 ? 14.627  11.399  -21.910 1.00 80.24  ?  394  LEU A N   1 
ATOM   2754 C  CA  . LEU A 1 395 ? 13.377  11.058  -22.585 1.00 89.87  ?  394  LEU A CA  1 
ATOM   2755 C  C   . LEU A 1 395 ? 13.623  10.521  -23.995 1.00 116.53 ?  394  LEU A C   1 
ATOM   2756 O  O   . LEU A 1 395 ? 12.911  9.637   -24.474 1.00 109.54 ?  394  LEU A O   1 
ATOM   2757 C  CB  . LEU A 1 395 ? 12.456  12.277  -22.659 1.00 100.13 ?  394  LEU A CB  1 
ATOM   2758 C  CG  . LEU A 1 395 ? 11.653  12.648  -21.410 1.00 96.84  ?  394  LEU A CG  1 
ATOM   2759 C  CD1 . LEU A 1 395 ? 10.581  13.682  -21.744 1.00 105.14 ?  394  LEU A CD1 1 
ATOM   2760 C  CD2 . LEU A 1 395 ? 11.041  11.416  -20.755 1.00 88.24  ?  394  LEU A CD2 1 
ATOM   2761 N  N   . GLU A 1 396 ? 14.630  11.082  -24.657 1.00 135.29 ?  395  GLU A N   1 
ATOM   2762 C  CA  . GLU A 1 396 ? 14.977  10.703  -26.021 1.00 132.30 ?  395  GLU A CA  1 
ATOM   2763 C  C   . GLU A 1 396 ? 15.480  9.266   -26.082 1.00 136.71 ?  395  GLU A C   1 
ATOM   2764 O  O   . GLU A 1 396 ? 15.244  8.565   -27.061 1.00 150.80 ?  395  GLU A O   1 
ATOM   2765 C  CB  . GLU A 1 396 ? 16.039  11.649  -26.581 1.00 125.19 ?  395  GLU A CB  1 
ATOM   2766 C  CG  . GLU A 1 396 ? 15.492  12.911  -27.230 1.00 118.35 ?  395  GLU A CG  1 
ATOM   2767 C  CD  . GLU A 1 396 ? 16.596  13.869  -27.631 1.00 123.78 ?  395  GLU A CD  1 
ATOM   2768 O  OE1 . GLU A 1 396 ? 17.727  13.401  -27.891 1.00 126.04 ?  395  GLU A OE1 1 
ATOM   2769 O  OE2 . GLU A 1 396 ? 16.336  15.089  -27.681 1.00 125.79 ?  395  GLU A OE2 1 
ATOM   2770 N  N   . ASN A 1 397 ? 16.178  8.828   -25.038 1.00 125.90 ?  396  ASN A N   1 
ATOM   2771 C  CA  . ASN A 1 397 ? 16.639  7.448   -24.979 1.00 117.57 ?  396  ASN A CA  1 
ATOM   2772 C  C   . ASN A 1 397 ? 15.451  6.518   -24.767 1.00 116.40 ?  396  ASN A C   1 
ATOM   2773 O  O   . ASN A 1 397 ? 14.666  6.712   -23.840 1.00 111.85 ?  396  ASN A O   1 
ATOM   2774 C  CB  . ASN A 1 397 ? 17.675  7.257   -23.869 1.00 114.26 ?  396  ASN A CB  1 
ATOM   2775 C  CG  . ASN A 1 397 ? 18.444  5.948   -24.005 1.00 107.91 ?  396  ASN A CG  1 
ATOM   2776 O  OD1 . ASN A 1 397 ? 17.859  4.866   -24.058 1.00 106.38 ?  396  ASN A OD1 1 
ATOM   2777 N  ND2 . ASN A 1 397 ? 19.765  6.047   -24.060 1.00 101.33 ?  396  ASN A ND2 1 
ATOM   2778 N  N   . PRO A 1 398 ? 15.311  5.511   -25.642 1.00 125.53 ?  397  PRO A N   1 
ATOM   2779 C  CA  . PRO A 1 398 ? 14.183  4.573   -25.629 1.00 132.93 ?  397  PRO A CA  1 
ATOM   2780 C  C   . PRO A 1 398 ? 14.183  3.687   -24.389 1.00 125.04 ?  397  PRO A C   1 
ATOM   2781 O  O   . PRO A 1 398 ? 13.117  3.383   -23.847 1.00 133.36 ?  397  PRO A O   1 
ATOM   2782 C  CB  . PRO A 1 398 ? 14.405  3.741   -26.893 1.00 148.99 ?  397  PRO A CB  1 
ATOM   2783 C  CG  . PRO A 1 398 ? 15.873  3.843   -27.161 1.00 143.42 ?  397  PRO A CG  1 
ATOM   2784 C  CD  . PRO A 1 398 ? 16.251  5.229   -26.741 1.00 128.16 ?  397  PRO A CD  1 
ATOM   2785 N  N   . THR A 1 399 ? 15.375  3.287   -23.954 1.00 123.18 ?  398  THR A N   1 
ATOM   2786 C  CA  . THR A 1 399 ? 15.550  2.444   -22.775 1.00 133.03 ?  398  THR A CA  1 
ATOM   2787 C  C   . THR A 1 399 ? 14.940  3.083   -21.528 1.00 125.81 ?  398  THR A C   1 
ATOM   2788 O  O   . THR A 1 399 ? 14.108  2.486   -20.839 1.00 118.75 ?  398  THR A O   1 
ATOM   2789 C  CB  . THR A 1 399 ? 17.053  2.175   -22.494 1.00 87.39  ?  398  THR A CB  1 
ATOM   2790 O  OG1 . THR A 1 399 ? 17.716  1.734   -23.686 1.00 85.57  ?  398  THR A OG1 1 
ATOM   2791 C  CG2 . THR A 1 399 ? 17.228  1.153   -21.380 1.00 98.60  ?  398  THR A CG2 1 
ATOM   2792 N  N   . HIS A 1 400 ? 15.366  4.314   -21.261 1.00 117.75 ?  399  HIS A N   1 
ATOM   2793 C  CA  . HIS A 1 400 ? 15.035  5.016   -20.028 1.00 110.41 ?  399  HIS A CA  1 
ATOM   2794 C  C   . HIS A 1 400 ? 13.653  5.676   -19.996 1.00 118.31 ?  399  HIS A C   1 
ATOM   2795 O  O   . HIS A 1 400 ? 13.115  5.916   -18.917 1.00 132.18 ?  399  HIS A O   1 
ATOM   2796 C  CB  . HIS A 1 400 ? 16.102  6.082   -19.762 1.00 103.43 ?  399  HIS A CB  1 
ATOM   2797 C  CG  . HIS A 1 400 ? 17.508  5.582   -19.915 1.00 107.43 ?  399  HIS A CG  1 
ATOM   2798 N  ND1 . HIS A 1 400 ? 17.893  4.319   -19.529 1.00 119.82 ?  399  HIS A ND1 1 
ATOM   2799 C  CD2 . HIS A 1 400 ? 18.616  6.181   -20.416 1.00 93.93  ?  399  HIS A CD2 1 
ATOM   2800 C  CE1 . HIS A 1 400 ? 19.184  4.158   -19.780 1.00 115.40 ?  399  HIS A CE1 1 
ATOM   2801 N  NE2 . HIS A 1 400 ? 19.643  5.272   -20.317 1.00 95.26  ?  399  HIS A NE2 1 
ATOM   2802 N  N   . ARG A 1 401 ? 13.085  5.958   -21.167 1.00 113.01 ?  400  ARG A N   1 
ATOM   2803 C  CA  . ARG A 1 401 ? 11.912  6.835   -21.267 1.00 119.35 ?  400  ARG A CA  1 
ATOM   2804 C  C   . ARG A 1 401 ? 10.723  6.446   -20.382 1.00 138.44 ?  400  ARG A C   1 
ATOM   2805 O  O   . ARG A 1 401 ? 10.106  7.313   -19.757 1.00 144.36 ?  400  ARG A O   1 
ATOM   2806 C  CB  . ARG A 1 401 ? 11.440  6.926   -22.720 1.00 120.23 ?  400  ARG A CB  1 
ATOM   2807 C  CG  . ARG A 1 401 ? 10.268  7.878   -22.904 1.00 120.37 ?  400  ARG A CG  1 
ATOM   2808 C  CD  . ARG A 1 401 ? 10.063  8.289   -24.350 1.00 114.57 ?  400  ARG A CD  1 
ATOM   2809 N  NE  . ARG A 1 401 ? 9.042   9.327   -24.492 1.00 119.97 ?  400  ARG A NE  1 
ATOM   2810 C  CZ  . ARG A 1 401 ? 7.743   9.138   -24.274 1.00 131.72 ?  400  ARG A CZ  1 
ATOM   2811 N  NH1 . ARG A 1 401 ? 7.287   7.940   -23.933 1.00 124.07 ?  400  ARG A NH1 1 
ATOM   2812 N  NH2 . ARG A 1 401 ? 6.893   10.145  -24.417 1.00 146.47 ?  400  ARG A NH2 1 
ATOM   2813 N  N   . ASN A 1 402 ? 10.399  5.158   -20.324 1.00 155.79 ?  401  ASN A N   1 
ATOM   2814 C  CA  . ASN A 1 402 ? 9.271   4.709   -19.509 1.00 169.06 ?  401  ASN A CA  1 
ATOM   2815 C  C   . ASN A 1 402 ? 9.500   4.973   -18.023 1.00 167.23 ?  401  ASN A C   1 
ATOM   2816 O  O   . ASN A 1 402 ? 8.582   5.370   -17.306 1.00 170.57 ?  401  ASN A O   1 
ATOM   2817 C  CB  . ASN A 1 402 ? 8.986   3.221   -19.742 1.00 178.86 ?  401  ASN A CB  1 
ATOM   2818 C  CG  . ASN A 1 402 ? 10.185  2.340   -19.450 1.00 180.15 ?  401  ASN A CG  1 
ATOM   2819 O  OD1 . ASN A 1 402 ? 11.324  2.701   -19.744 1.00 184.19 ?  401  ASN A OD1 1 
ATOM   2820 N  ND2 . ASN A 1 402 ? 9.932   1.173   -18.868 1.00 176.21 ?  401  ASN A ND2 1 
ATOM   2821 N  N   . LEU A 1 403 ? 10.730  4.754   -17.569 1.00 155.91 ?  402  LEU A N   1 
ATOM   2822 C  CA  . LEU A 1 403 ? 11.069  4.918   -16.161 1.00 134.07 ?  402  LEU A CA  1 
ATOM   2823 C  C   . LEU A 1 403 ? 11.045  6.381   -15.712 1.00 118.90 ?  402  LEU A C   1 
ATOM   2824 O  O   . LEU A 1 403 ? 10.443  6.712   -14.688 1.00 119.62 ?  402  LEU A O   1 
ATOM   2825 C  CB  . LEU A 1 403 ? 12.448  4.311   -15.889 1.00 128.60 ?  402  LEU A CB  1 
ATOM   2826 C  CG  . LEU A 1 403 ? 13.058  4.501   -14.500 1.00 127.24 ?  402  LEU A CG  1 
ATOM   2827 C  CD1 . LEU A 1 403 ? 12.114  3.974   -13.426 1.00 137.32 ?  402  LEU A CD1 1 
ATOM   2828 C  CD2 . LEU A 1 403 ? 14.411  3.814   -14.411 1.00 117.57 ?  402  LEU A CD2 1 
ATOM   2829 N  N   . VAL A 1 404 ? 11.684  7.255   -16.485 1.00 107.43 ?  403  VAL A N   1 
ATOM   2830 C  CA  . VAL A 1 404 ? 11.776  8.669   -16.123 1.00 106.64 ?  403  VAL A CA  1 
ATOM   2831 C  C   . VAL A 1 404 ? 10.409  9.338   -16.143 1.00 122.68 ?  403  VAL A C   1 
ATOM   2832 O  O   . VAL A 1 404 ? 10.093  10.152  -15.274 1.00 125.59 ?  403  VAL A O   1 
ATOM   2833 C  CB  . VAL A 1 404 ? 12.731  9.439   -17.056 1.00 96.18  ?  403  VAL A CB  1 
ATOM   2834 C  CG1 . VAL A 1 404 ? 12.785  10.914  -16.677 1.00 83.61  ?  403  VAL A CG1 1 
ATOM   2835 C  CG2 . VAL A 1 404 ? 14.118  8.824   -17.020 1.00 82.32  ?  403  VAL A CG2 1 
ATOM   2836 N  N   . GLU A 1 405 ? 9.595   8.985   -17.132 1.00 135.64 ?  404  GLU A N   1 
ATOM   2837 C  CA  . GLU A 1 405 ? 8.248   9.529   -17.225 1.00 162.87 ?  404  GLU A CA  1 
ATOM   2838 C  C   . GLU A 1 405 ? 7.431   9.077   -16.019 1.00 165.47 ?  404  GLU A C   1 
ATOM   2839 O  O   . GLU A 1 405 ? 6.610   9.833   -15.496 1.00 166.52 ?  404  GLU A O   1 
ATOM   2840 C  CB  . GLU A 1 405 ? 7.574   9.101   -18.533 1.00 176.91 ?  404  GLU A CB  1 
ATOM   2841 C  CG  . GLU A 1 405 ? 6.102   9.501   -18.646 1.00 194.47 ?  404  GLU A CG  1 
ATOM   2842 C  CD  . GLU A 1 405 ? 5.850   10.955  -18.273 1.00 199.55 ?  404  GLU A CD  1 
ATOM   2843 O  OE1 . GLU A 1 405 ? 6.602   11.833  -18.746 1.00 204.47 ?  404  GLU A OE1 1 
ATOM   2844 O  OE2 . GLU A 1 405 ? 4.902   11.221  -17.501 1.00 195.71 ?  404  GLU A OE2 1 
ATOM   2845 N  N   . GLU A 1 406 ? 7.679   7.849   -15.572 1.00 156.90 ?  405  GLU A N   1 
ATOM   2846 C  CA  . GLU A 1 406 ? 6.999   7.313   -14.401 1.00 161.19 ?  405  GLU A CA  1 
ATOM   2847 C  C   . GLU A 1 406 ? 7.291   8.187   -13.186 1.00 158.43 ?  405  GLU A C   1 
ATOM   2848 O  O   . GLU A 1 406 ? 6.406   8.468   -12.382 1.00 178.11 ?  405  GLU A O   1 
ATOM   2849 C  CB  . GLU A 1 406 ? 7.426   5.868   -14.138 1.00 174.38 ?  405  GLU A CB  1 
ATOM   2850 C  CG  . GLU A 1 406 ? 6.642   5.177   -13.029 1.00 198.13 ?  405  GLU A CG  1 
ATOM   2851 C  CD  . GLU A 1 406 ? 5.252   4.754   -13.473 1.00 208.76 ?  405  GLU A CD  1 
ATOM   2852 O  OE1 . GLU A 1 406 ? 5.147   4.045   -14.496 1.00 207.73 ?  405  GLU A OE1 1 
ATOM   2853 O  OE2 . GLU A 1 406 ? 4.267   5.124   -12.798 1.00 213.12 ?  405  GLU A OE2 1 
ATOM   2854 N  N   . TRP A 1 407 ? 8.538   8.624   -13.064 1.00 144.06 ?  406  TRP A N   1 
ATOM   2855 C  CA  . TRP A 1 407 ? 8.931   9.519   -11.982 1.00 124.17 ?  406  TRP A CA  1 
ATOM   2856 C  C   . TRP A 1 407 ? 8.244   10.871  -12.092 1.00 116.87 ?  406  TRP A C   1 
ATOM   2857 O  O   . TRP A 1 407 ? 7.713   11.383  -11.110 1.00 117.53 ?  406  TRP A O   1 
ATOM   2858 C  CB  . TRP A 1 407 ? 10.448  9.694   -11.966 1.00 108.07 ?  406  TRP A CB  1 
ATOM   2859 C  CG  . TRP A 1 407 ? 11.152  8.452   -11.548 1.00 103.05 ?  406  TRP A CG  1 
ATOM   2860 C  CD1 . TRP A 1 407 ? 10.576  7.304   -11.085 1.00 113.82 ?  406  TRP A CD1 1 
ATOM   2861 C  CD2 . TRP A 1 407 ? 12.565  8.216   -11.564 1.00 95.67  ?  406  TRP A CD2 1 
ATOM   2862 N  NE1 . TRP A 1 407 ? 11.544  6.371   -10.802 1.00 116.23 ?  406  TRP A NE1 1 
ATOM   2863 C  CE2 . TRP A 1 407 ? 12.770  6.904   -11.088 1.00 100.87 ?  406  TRP A CE2 1 
ATOM   2864 C  CE3 . TRP A 1 407 ? 13.672  8.985   -11.929 1.00 91.47  ?  406  TRP A CE3 1 
ATOM   2865 C  CZ2 . TRP A 1 407 ? 14.046  6.347   -10.970 1.00 90.44  ?  406  TRP A CZ2 1 
ATOM   2866 C  CZ3 . TRP A 1 407 ? 14.937  8.426   -11.812 1.00 89.96  ?  406  TRP A CZ3 1 
ATOM   2867 C  CH2 . TRP A 1 407 ? 15.112  7.120   -11.335 1.00 86.64  ?  406  TRP A CH2 1 
ATOM   2868 N  N   . ILE A 1 408 ? 8.242   11.436  -13.295 1.00 112.74 ?  407  ILE A N   1 
ATOM   2869 C  CA  . ILE A 1 408 ? 7.640   12.745  -13.529 1.00 114.12 ?  407  ILE A CA  1 
ATOM   2870 C  C   . ILE A 1 408 ? 6.140   12.733  -13.230 1.00 122.06 ?  407  ILE A C   1 
ATOM   2871 O  O   . ILE A 1 408 ? 5.608   13.681  -12.651 1.00 124.39 ?  407  ILE A O   1 
ATOM   2872 C  CB  . ILE A 1 408 ? 7.864   13.215  -14.981 1.00 108.44 ?  407  ILE A CB  1 
ATOM   2873 C  CG1 . ILE A 1 408 ? 9.358   13.240  -15.306 1.00 90.95  ?  407  ILE A CG1 1 
ATOM   2874 C  CG2 . ILE A 1 408 ? 7.213   14.575  -15.217 1.00 96.70  ?  407  ILE A CG2 1 
ATOM   2875 C  CD1 . ILE A 1 408 ? 9.706   14.026  -16.549 1.00 89.76  ?  407  ILE A CD1 1 
ATOM   2876 N  N   . SER A 1 409 ? 5.461   11.665  -13.636 1.00 133.61 ?  408  SER A N   1 
ATOM   2877 C  CA  . SER A 1 409 ? 4.027   11.542  -13.393 1.00 150.73 ?  408  SER A CA  1 
ATOM   2878 C  C   . SER A 1 409 ? 3.752   11.329  -11.907 1.00 151.31 ?  408  SER A C   1 
ATOM   2879 O  O   . SER A 1 409 ? 2.805   11.892  -11.357 1.00 146.01 ?  408  SER A O   1 
ATOM   2880 C  CB  . SER A 1 409 ? 3.429   10.397  -14.214 1.00 169.89 ?  408  SER A CB  1 
ATOM   2881 O  OG  . SER A 1 409 ? 4.015   9.155   -13.870 1.00 174.96 ?  408  SER A OG  1 
ATOM   2882 N  N   . ASN A 1 410 ? 4.580   10.506  -11.267 1.00 161.54 ?  409  ASN A N   1 
ATOM   2883 C  CA  . ASN A 1 410 ? 4.468   10.258  -9.831  1.00 169.01 ?  409  ASN A CA  1 
ATOM   2884 C  C   . ASN A 1 410 ? 4.763   11.503  -8.997  1.00 172.00 ?  409  ASN A C   1 
ATOM   2885 O  O   . ASN A 1 410 ? 4.097   11.762  -7.993  1.00 181.23 ?  409  ASN A O   1 
ATOM   2886 C  CB  . ASN A 1 410 ? 5.411   9.127   -9.403  1.00 156.45 ?  409  ASN A CB  1 
ATOM   2887 C  CG  . ASN A 1 410 ? 4.889   7.748   -9.774  1.00 144.73 ?  409  ASN A CG  1 
ATOM   2888 O  OD1 . ASN A 1 410 ? 3.680   7.526   -9.855  1.00 141.05 ?  409  ASN A OD1 1 
ATOM   2889 N  ND2 . ASN A 1 410 ? 5.805   6.810   -9.992  1.00 134.05 ?  409  ASN A ND2 1 
ATOM   2890 N  N   . GLY A 1 411 ? 5.767   12.268  -9.415  1.00 156.58 ?  410  GLY A N   1 
ATOM   2891 C  CA  . GLY A 1 411 ? 6.190   13.438  -8.669  1.00 141.05 ?  410  GLY A CA  1 
ATOM   2892 C  C   . GLY A 1 411 ? 7.543   13.202  -8.028  1.00 128.12 ?  410  GLY A C   1 
ATOM   2893 O  O   . GLY A 1 411 ? 7.948   13.920  -7.116  1.00 135.74 ?  410  GLY A O   1 
ATOM   2894 N  N   . VAL A 1 412 ? 8.237   12.175  -8.503  1.00 112.73 ?  411  VAL A N   1 
ATOM   2895 C  CA  . VAL A 1 412 ? 9.540   11.809  -7.966  1.00 109.87 ?  411  VAL A CA  1 
ATOM   2896 C  C   . VAL A 1 412 ? 10.645  12.495  -8.772  1.00 103.78 ?  411  VAL A C   1 
ATOM   2897 O  O   . VAL A 1 412 ? 11.823  12.445  -8.414  1.00 95.21  ?  411  VAL A O   1 
ATOM   2898 C  CB  . VAL A 1 412 ? 9.741   10.282  -7.974  1.00 122.80 ?  411  VAL A CB  1 
ATOM   2899 C  CG1 . VAL A 1 412 ? 10.868  9.893   -7.041  1.00 122.71 ?  411  VAL A CG1 1 
ATOM   2900 C  CG2 . VAL A 1 412 ? 8.465   9.587   -7.540  1.00 131.86 ?  411  VAL A CG2 1 
ATOM   2901 N  N   . LEU A 1 413 ? 10.263  13.107  -9.888  1.00 109.33 ?  412  LEU A N   1 
ATOM   2902 C  CA  . LEU A 1 413 ? 11.202  13.895  -10.675 1.00 104.11 ?  412  LEU A CA  1 
ATOM   2903 C  C   . LEU A 1 413 ? 10.629  15.278  -10.999 1.00 100.96 ?  412  LEU A C   1 
ATOM   2904 O  O   . LEU A 1 413 ? 9.425   15.426  -11.222 1.00 101.37 ?  412  LEU A O   1 
ATOM   2905 C  CB  . LEU A 1 413 ? 11.584  13.161  -11.960 1.00 106.56 ?  412  LEU A CB  1 
ATOM   2906 C  CG  . LEU A 1 413 ? 12.852  13.710  -12.614 1.00 107.86 ?  412  LEU A CG  1 
ATOM   2907 C  CD1 . LEU A 1 413 ? 14.075  12.981  -12.110 1.00 108.05 ?  412  LEU A CD1 1 
ATOM   2908 C  CD2 . LEU A 1 413 ? 12.762  13.619  -14.125 1.00 118.69 ?  412  LEU A CD2 1 
ATOM   2909 N  N   . TYR A 1 414 ? 11.492  16.290  -10.988 1.00 101.19 ?  413  TYR A N   1 
ATOM   2910 C  CA  . TYR A 1 414 ? 11.105  17.640  -11.386 1.00 108.98 ?  413  TYR A CA  1 
ATOM   2911 C  C   . TYR A 1 414 ? 12.152  18.230  -12.328 1.00 113.42 ?  413  TYR A C   1 
ATOM   2912 O  O   . TYR A 1 414 ? 13.354  18.054  -12.128 1.00 102.95 ?  413  TYR A O   1 
ATOM   2913 C  CB  . TYR A 1 414 ? 10.922  18.530  -10.154 1.00 125.97 ?  413  TYR A CB  1 
ATOM   2914 C  CG  . TYR A 1 414 ? 10.266  19.875  -10.406 1.00 129.44 ?  413  TYR A CG  1 
ATOM   2915 C  CD1 . TYR A 1 414 ? 11.001  20.958  -10.880 1.00 125.98 ?  413  TYR A CD1 1 
ATOM   2916 C  CD2 . TYR A 1 414 ? 8.918   20.071  -10.134 1.00 132.69 ?  413  TYR A CD2 1 
ATOM   2917 C  CE1 . TYR A 1 414 ? 10.405  22.192  -11.096 1.00 126.48 ?  413  TYR A CE1 1 
ATOM   2918 C  CE2 . TYR A 1 414 ? 8.313   21.302  -10.347 1.00 138.20 ?  413  TYR A CE2 1 
ATOM   2919 C  CZ  . TYR A 1 414 ? 9.061   22.359  -10.828 1.00 127.03 ?  413  TYR A CZ  1 
ATOM   2920 O  OH  . TYR A 1 414 ? 8.465   23.583  -11.040 1.00 115.53 ?  413  TYR A OH  1 
ATOM   2921 N  N   . ALA A 1 415 ? 11.687  18.946  -13.343 1.00 133.33 ?  414  ALA A N   1 
ATOM   2922 C  CA  . ALA A 1 415 ? 12.574  19.509  -14.348 1.00 134.03 ?  414  ALA A CA  1 
ATOM   2923 C  C   . ALA A 1 415 ? 12.807  20.993  -14.097 1.00 135.21 ?  414  ALA A C   1 
ATOM   2924 O  O   . ALA A 1 415 ? 11.898  21.808  -14.254 1.00 139.94 ?  414  ALA A O   1 
ATOM   2925 C  CB  . ALA A 1 415 ? 12.007  19.288  -15.739 1.00 137.45 ?  414  ALA A CB  1 
ATOM   2926 N  N   . THR A 1 416 ? 14.023  21.341  -13.693 1.00 123.30 ?  415  THR A N   1 
ATOM   2927 C  CA  . THR A 1 416 ? 14.377  22.741  -13.522 1.00 118.65 ?  415  THR A CA  1 
ATOM   2928 C  C   . THR A 1 416 ? 14.438  23.409  -14.894 1.00 125.93 ?  415  THR A C   1 
ATOM   2929 O  O   . THR A 1 416 ? 15.051  22.879  -15.819 1.00 123.33 ?  415  THR A O   1 
ATOM   2930 C  CB  . THR A 1 416 ? 15.722  22.899  -12.787 1.00 99.71  ?  415  THR A CB  1 
ATOM   2931 O  OG1 . THR A 1 416 ? 16.777  22.351  -13.584 1.00 96.41  ?  415  THR A OG1 1 
ATOM   2932 C  CG2 . THR A 1 416 ? 15.687  22.165  -11.464 1.00 101.10 ?  415  THR A CG2 1 
ATOM   2933 N  N   . PRO A 1 417 ? 13.805  24.584  -15.026 1.00 136.78 ?  416  PRO A N   1 
ATOM   2934 C  CA  . PRO A 1 417 ? 13.734  25.291  -16.312 1.00 146.62 ?  416  PRO A CA  1 
ATOM   2935 C  C   . PRO A 1 417 ? 15.079  25.889  -16.743 1.00 151.07 ?  416  PRO A C   1 
ATOM   2936 O  O   . PRO A 1 417 ? 16.005  25.925  -15.934 1.00 152.85 ?  416  PRO A O   1 
ATOM   2937 C  CB  . PRO A 1 417 ? 12.706  26.398  -16.031 1.00 151.99 ?  416  PRO A CB  1 
ATOM   2938 C  CG  . PRO A 1 417 ? 11.928  25.910  -14.847 1.00 145.15 ?  416  PRO A CG  1 
ATOM   2939 C  CD  . PRO A 1 417 ? 12.952  25.219  -14.010 1.00 138.35 ?  416  PRO A CD  1 
ATOM   2940 N  N   . PRO A 1 418 ? 15.190  26.336  -18.009 1.00 146.00 ?  417  PRO A N   1 
ATOM   2941 C  CA  . PRO A 1 418 ? 16.450  26.879  -18.531 1.00 148.56 ?  417  PRO A CA  1 
ATOM   2942 C  C   . PRO A 1 418 ? 16.853  28.217  -17.894 1.00 168.86 ?  417  PRO A C   1 
ATOM   2943 O  O   . PRO A 1 418 ? 16.026  28.891  -17.272 1.00 172.01 ?  417  PRO A O   1 
ATOM   2944 C  CB  . PRO A 1 418 ? 16.155  27.044  -20.027 1.00 139.82 ?  417  PRO A CB  1 
ATOM   2945 C  CG  . PRO A 1 418 ? 14.679  27.220  -20.090 1.00 143.68 ?  417  PRO A CG  1 
ATOM   2946 C  CD  . PRO A 1 418 ? 14.179  26.237  -19.076 1.00 140.95 ?  417  PRO A CD  1 
ATOM   2947 N  N   . GLY A 1 419 ? 18.122  28.584  -18.050 1.00 174.93 ?  418  GLY A N   1 
ATOM   2948 C  CA  . GLY A 1 419 ? 18.625  29.853  -17.555 1.00 173.51 ?  418  GLY A CA  1 
ATOM   2949 C  C   . GLY A 1 419 ? 19.020  29.813  -16.090 1.00 181.45 ?  418  GLY A C   1 
ATOM   2950 O  O   . GLY A 1 419 ? 19.562  30.784  -15.559 1.00 185.38 ?  418  GLY A O   1 
ATOM   2951 N  N   . SER A 1 420 ? 18.751  28.687  -15.438 1.00 191.26 ?  419  SER A N   1 
ATOM   2952 C  CA  . SER A 1 420 ? 19.018  28.541  -14.014 1.00 198.74 ?  419  SER A CA  1 
ATOM   2953 C  C   . SER A 1 420 ? 18.943  27.077  -13.584 1.00 205.56 ?  419  SER A C   1 
ATOM   2954 O  O   . SER A 1 420 ? 18.066  26.359  -14.062 1.00 212.89 ?  419  SER A O   1 
ATOM   2955 C  CB  . SER A 1 420 ? 18.020  29.370  -13.199 1.00 197.78 ?  419  SER A CB  1 
ATOM   2956 O  OG  . SER A 1 420 ? 16.715  28.825  -13.273 1.00 196.40 ?  419  SER A OG  1 
ATOM   2957 N  N   . ASN A 1 421 ? 19.828  26.604  -12.697 1.00 200.08 ?  420  ASN A N   1 
ATOM   2958 C  CA  . ASN A 1 421 ? 21.023  27.285  -12.181 1.00 182.24 ?  420  ASN A CA  1 
ATOM   2959 C  C   . ASN A 1 421 ? 21.819  26.189  -11.465 1.00 183.65 ?  420  ASN A C   1 
ATOM   2960 O  O   . ASN A 1 421 ? 21.591  25.001  -11.706 1.00 184.53 ?  420  ASN A O   1 
ATOM   2961 C  CB  . ASN A 1 421 ? 20.665  28.414  -11.201 1.00 161.53 ?  420  ASN A CB  1 
ATOM   2962 C  CG  . ASN A 1 421 ? 21.843  29.309  -10.869 1.00 157.34 ?  420  ASN A CG  1 
ATOM   2963 O  OD1 . ASN A 1 421 ? 22.981  28.854  -10.782 1.00 153.27 ?  420  ASN A OD1 1 
ATOM   2964 N  ND2 . ASN A 1 421 ? 21.569  30.596  -10.678 1.00 166.42 ?  420  ASN A ND2 1 
ATOM   2965 N  N   . ASP A 1 422 ? 22.745  26.567  -10.584 1.00 183.78 ?  421  ASP A N   1 
ATOM   2966 C  CA  . ASP A 1 422 ? 23.395  25.598  -9.702  1.00 170.87 ?  421  ASP A CA  1 
ATOM   2967 C  C   . ASP A 1 422 ? 22.350  25.424  -8.612  1.00 161.74 ?  421  ASP A C   1 
ATOM   2968 O  O   . ASP A 1 422 ? 22.572  25.755  -7.446  1.00 141.42 ?  421  ASP A O   1 
ATOM   2969 C  CB  . ASP A 1 422 ? 24.731  26.095  -9.150  1.00 159.72 ?  421  ASP A CB  1 
ATOM   2970 C  CG  . ASP A 1 422 ? 25.519  25.002  -8.440  1.00 145.52 ?  421  ASP A CG  1 
ATOM   2971 O  OD1 . ASP A 1 422 ? 24.906  24.174  -7.733  1.00 132.77 ?  421  ASP A OD1 1 
ATOM   2972 O  OD2 . ASP A 1 422 ? 26.759  24.971  -8.593  1.00 149.31 ?  421  ASP A OD2 1 
ATOM   2973 N  N   . ASP A 1 423 ? 21.212  24.878  -9.029  1.00 169.96 ?  422  ASP A N   1 
ATOM   2974 C  CA  . ASP A 1 423 ? 19.913  25.189  -8.450  1.00 167.14 ?  422  ASP A CA  1 
ATOM   2975 C  C   . ASP A 1 423 ? 19.796  25.124  -6.943  1.00 162.81 ?  422  ASP A C   1 
ATOM   2976 O  O   . ASP A 1 423 ? 20.263  24.195  -6.284  1.00 147.74 ?  422  ASP A O   1 
ATOM   2977 C  CB  . ASP A 1 423 ? 18.855  24.260  -9.048  1.00 167.77 ?  422  ASP A CB  1 
ATOM   2978 C  CG  . ASP A 1 423 ? 18.659  24.478  -10.532 1.00 162.07 ?  422  ASP A CG  1 
ATOM   2979 O  OD1 . ASP A 1 423 ? 18.427  25.638  -10.936 1.00 156.02 ?  422  ASP A OD1 1 
ATOM   2980 O  OD2 . ASP A 1 423 ? 18.744  23.488  -11.291 1.00 161.36 ?  422  ASP A OD2 1 
ATOM   2981 N  N   . TRP A 1 424 ? 19.143  26.150  -6.420  1.00 175.66 ?  423  TRP A N   1 
ATOM   2982 C  CA  . TRP A 1 424 ? 18.750  26.190  -5.035  1.00 190.50 ?  423  TRP A CA  1 
ATOM   2983 C  C   . TRP A 1 424 ? 17.448  25.415  -4.932  1.00 176.93 ?  423  TRP A C   1 
ATOM   2984 O  O   . TRP A 1 424 ? 16.928  25.201  -3.840  1.00 179.93 ?  423  TRP A O   1 
ATOM   2985 C  CB  . TRP A 1 424 ? 18.570  27.632  -4.572  1.00 216.52 ?  423  TRP A CB  1 
ATOM   2986 C  CG  . TRP A 1 424 ? 17.630  28.390  -5.459  1.00 240.22 ?  423  TRP A CG  1 
ATOM   2987 C  CD1 . TRP A 1 424 ? 16.286  28.546  -5.284  1.00 250.99 ?  423  TRP A CD1 1 
ATOM   2988 C  CD2 . TRP A 1 424 ? 17.957  29.071  -6.690  1.00 251.31 ?  423  TRP A CD2 1 
ATOM   2989 N  NE1 . TRP A 1 424 ? 15.759  29.291  -6.316  1.00 255.24 ?  423  TRP A NE1 1 
ATOM   2990 C  CE2 . TRP A 1 424 ? 16.754  29.618  -7.179  1.00 258.50 ?  423  TRP A CE2 1 
ATOM   2991 C  CE3 . TRP A 1 424 ? 19.142  29.264  -7.397  1.00 254.14 ?  423  TRP A CE3 1 
ATOM   2992 C  CZ2 . TRP A 1 424 ? 16.719  30.358  -8.372  1.00 265.20 ?  423  TRP A CZ2 1 
ATOM   2993 C  CZ3 . TRP A 1 424 ? 19.092  30.000  -8.574  1.00 262.42 ?  423  TRP A CZ3 1 
ATOM   2994 C  CH2 . TRP A 1 424 ? 17.890  30.537  -9.047  1.00 268.25 ?  423  TRP A CH2 1 
ATOM   2995 N  N   . TYR A 1 425 ? 16.931  25.007  -6.092  1.00 161.91 ?  424  TYR A N   1 
ATOM   2996 C  CA  . TYR A 1 425 ? 15.700  24.229  -6.181  1.00 149.93 ?  424  TYR A CA  1 
ATOM   2997 C  C   . TYR A 1 425 ? 15.693  23.080  -5.181  1.00 139.37 ?  424  TYR A C   1 
ATOM   2998 O  O   . TYR A 1 425 ? 14.707  22.867  -4.484  1.00 139.82 ?  424  TYR A O   1 
ATOM   2999 C  CB  . TYR A 1 425 ? 15.492  23.706  -7.617  1.00 145.57 ?  424  TYR A CB  1 
ATOM   3000 C  CG  . TYR A 1 425 ? 14.973  24.752  -8.594  1.00 133.64 ?  424  TYR A CG  1 
ATOM   3001 C  CD1 . TYR A 1 425 ? 15.792  25.778  -9.051  1.00 127.26 ?  424  TYR A CD1 1 
ATOM   3002 C  CD2 . TYR A 1 425 ? 13.664  24.703  -9.067  1.00 121.10 ?  424  TYR A CD2 1 
ATOM   3003 C  CE1 . TYR A 1 425 ? 15.319  26.732  -9.943  1.00 122.98 ?  424  TYR A CE1 1 
ATOM   3004 C  CE2 . TYR A 1 425 ? 13.184  25.653  -9.957  1.00 118.40 ?  424  TYR A CE2 1 
ATOM   3005 C  CZ  . TYR A 1 425 ? 14.017  26.662  -10.392 1.00 119.29 ?  424  TYR A CZ  1 
ATOM   3006 O  OH  . TYR A 1 425 ? 13.551  27.609  -11.275 1.00 114.82 ?  424  TYR A OH  1 
ATOM   3007 N  N   . TRP A 1 426 ? 16.801  22.353  -5.097  1.00 138.54 ?  425  TRP A N   1 
ATOM   3008 C  CA  . TRP A 1 426 ? 16.934  21.313  -4.082  1.00 143.11 ?  425  TRP A CA  1 
ATOM   3009 C  C   . TRP A 1 426 ? 17.357  21.875  -2.725  1.00 144.93 ?  425  TRP A C   1 
ATOM   3010 O  O   . TRP A 1 426 ? 16.906  21.391  -1.688  1.00 145.93 ?  425  TRP A O   1 
ATOM   3011 C  CB  . TRP A 1 426 ? 17.910  20.222  -4.552  1.00 136.78 ?  425  TRP A CB  1 
ATOM   3012 C  CG  . TRP A 1 426 ? 19.271  20.711  -4.947  1.00 138.80 ?  425  TRP A CG  1 
ATOM   3013 C  CD1 . TRP A 1 426 ? 20.299  21.052  -4.122  1.00 141.51 ?  425  TRP A CD1 1 
ATOM   3014 C  CD2 . TRP A 1 426 ? 19.748  20.898  -6.283  1.00 145.37 ?  425  TRP A CD2 1 
ATOM   3015 N  NE1 . TRP A 1 426 ? 21.390  21.446  -4.861  1.00 133.83 ?  425  TRP A NE1 1 
ATOM   3016 C  CE2 . TRP A 1 426 ? 21.077  21.357  -6.190  1.00 141.73 ?  425  TRP A CE2 1 
ATOM   3017 C  CE3 . TRP A 1 426 ? 19.180  20.720  -7.547  1.00 166.76 ?  425  TRP A CE3 1 
ATOM   3018 C  CZ2 . TRP A 1 426 ? 21.844  21.646  -7.316  1.00 163.42 ?  425  TRP A CZ2 1 
ATOM   3019 C  CZ3 . TRP A 1 426 ? 19.943  21.005  -8.663  1.00 182.88 ?  425  TRP A CZ3 1 
ATOM   3020 C  CH2 . TRP A 1 426 ? 21.260  21.466  -8.541  1.00 188.86 ?  425  TRP A CH2 1 
ATOM   3021 N  N   . LEU A 1 427 ? 18.207  22.897  -2.731  1.00 133.66 ?  426  LEU A N   1 
ATOM   3022 C  CA  . LEU A 1 427 ? 18.613  23.546  -1.489  1.00 113.08 ?  426  LEU A CA  1 
ATOM   3023 C  C   . LEU A 1 427 ? 17.401  24.160  -0.789  1.00 119.98 ?  426  LEU A C   1 
ATOM   3024 O  O   . LEU A 1 427 ? 17.226  23.992  0.416   1.00 134.97 ?  426  LEU A O   1 
ATOM   3025 C  CB  . LEU A 1 427 ? 19.672  24.618  -1.748  1.00 110.78 ?  426  LEU A CB  1 
ATOM   3026 C  CG  . LEU A 1 427 ? 21.123  24.153  -1.918  1.00 114.99 ?  426  LEU A CG  1 
ATOM   3027 C  CD1 . LEU A 1 427 ? 22.056  25.333  -2.183  1.00 105.13 ?  426  LEU A CD1 1 
ATOM   3028 C  CD2 . LEU A 1 427 ? 21.610  23.352  -0.716  1.00 124.62 ?  426  LEU A CD2 1 
ATOM   3029 N  N   . TYR A 1 428 ? 16.567  24.866  -1.550  1.00 106.13 ?  427  TYR A N   1 
ATOM   3030 C  CA  . TYR A 1 428 ? 15.325  25.430  -1.025  1.00 117.28 ?  427  TYR A CA  1 
ATOM   3031 C  C   . TYR A 1 428 ? 14.421  24.330  -0.507  1.00 140.69 ?  427  TYR A C   1 
ATOM   3032 O  O   . TYR A 1 428 ? 13.902  24.416  0.602   1.00 175.56 ?  427  TYR A O   1 
ATOM   3033 C  CB  . TYR A 1 428 ? 14.590  26.238  -2.101  1.00 112.89 ?  427  TYR A CB  1 
ATOM   3034 C  CG  . TYR A 1 428 ? 13.137  26.558  -1.782  1.00 120.04 ?  427  TYR A CG  1 
ATOM   3035 C  CD1 . TYR A 1 428 ? 12.800  27.663  -1.009  1.00 125.98 ?  427  TYR A CD1 1 
ATOM   3036 C  CD2 . TYR A 1 428 ? 12.103  25.759  -2.263  1.00 122.92 ?  427  TYR A CD2 1 
ATOM   3037 C  CE1 . TYR A 1 428 ? 11.474  27.964  -0.721  1.00 130.83 ?  427  TYR A CE1 1 
ATOM   3038 C  CE2 . TYR A 1 428 ? 10.774  26.051  -1.977  1.00 124.92 ?  427  TYR A CE2 1 
ATOM   3039 C  CZ  . TYR A 1 428 ? 10.466  27.155  -1.207  1.00 128.02 ?  427  TYR A CZ  1 
ATOM   3040 O  OH  . TYR A 1 428 ? 9.149   27.448  -0.922  1.00 128.73 ?  427  TYR A OH  1 
ATOM   3041 N  N   . ALA A 1 429 ? 14.244  23.291  -1.315  1.00 125.52 ?  428  ALA A N   1 
ATOM   3042 C  CA  . ALA A 1 429 ? 13.344  22.205  -0.965  1.00 121.54 ?  428  ALA A CA  1 
ATOM   3043 C  C   . ALA A 1 429 ? 13.861  21.435  0.251   1.00 130.47 ?  428  ALA A C   1 
ATOM   3044 O  O   . ALA A 1 429 ? 13.084  21.039  1.120   1.00 130.31 ?  428  ALA A O   1 
ATOM   3045 C  CB  . ALA A 1 429 ? 13.151  21.282  -2.150  1.00 111.86 ?  428  ALA A CB  1 
ATOM   3046 N  N   . ALA A 1 430 ? 15.173  21.237  0.325   1.00 105.24 ?  429  ALA A N   1 
ATOM   3047 C  CA  . ALA A 1 430 ? 15.753  20.555  1.476   1.00 106.38 ?  429  ALA A CA  1 
ATOM   3048 C  C   . ALA A 1 430 ? 15.552  21.385  2.746   1.00 132.30 ?  429  ALA A C   1 
ATOM   3049 O  O   . ALA A 1 430 ? 15.133  20.861  3.779   1.00 125.45 ?  429  ALA A O   1 
ATOM   3050 C  CB  . ALA A 1 430 ? 17.234  20.276  1.246   1.00 104.45 ?  429  ALA A CB  1 
ATOM   3051 N  N   . ALA A 1 431 ? 15.843  22.680  2.655   1.00 129.04 ?  430  ALA A N   1 
ATOM   3052 C  CA  . ALA A 1 431 ? 15.724  23.594  3.789   1.00 126.52 ?  430  ALA A CA  1 
ATOM   3053 C  C   . ALA A 1 431 ? 14.272  23.836  4.188   1.00 131.67 ?  430  ALA A C   1 
ATOM   3054 O  O   . ALA A 1 431 ? 13.953  23.894  5.377   1.00 130.48 ?  430  ALA A O   1 
ATOM   3055 C  CB  . ALA A 1 431 ? 16.403  24.914  3.470   1.00 116.55 ?  430  ALA A CB  1 
ATOM   3056 N  N   . LYS A 1 432 ? 13.402  23.995  3.193   1.00 117.35 ?  431  LYS A N   1 
ATOM   3057 C  CA  . LYS A 1 432 ? 11.986  24.263  3.437   1.00 133.45 ?  431  LYS A CA  1 
ATOM   3058 C  C   . LYS A 1 432 ? 11.334  23.087  4.156   1.00 144.41 ?  431  LYS A C   1 
ATOM   3059 O  O   . LYS A 1 432 ? 10.463  23.267  5.009   1.00 156.29 ?  431  LYS A O   1 
ATOM   3060 C  CB  . LYS A 1 432 ? 11.252  24.550  2.126   1.00 124.35 ?  431  LYS A CB  1 
ATOM   3061 C  CG  . LYS A 1 432 ? 9.850   25.115  2.296   1.00 135.98 ?  431  LYS A CG  1 
ATOM   3062 C  CD  . LYS A 1 432 ? 9.891   26.539  2.831   1.00 153.84 ?  431  LYS A CD  1 
ATOM   3063 C  CE  . LYS A 1 432 ? 8.500   27.150  2.896   1.00 165.71 ?  431  LYS A CE  1 
ATOM   3064 N  NZ  . LYS A 1 432 ? 8.540   28.565  3.361   1.00 172.25 ?  431  LYS A NZ  1 
ATOM   3065 N  N   . LEU A 1 433 ? 11.771  21.881  3.809   1.00 139.88 ?  432  LEU A N   1 
ATOM   3066 C  CA  . LEU A 1 433 ? 11.251  20.669  4.429   1.00 144.06 ?  432  LEU A CA  1 
ATOM   3067 C  C   . LEU A 1 433 ? 12.101  20.278  5.627   1.00 140.52 ?  432  LEU A C   1 
ATOM   3068 O  O   . LEU A 1 433 ? 11.764  19.341  6.355   1.00 126.34 ?  432  LEU A O   1 
ATOM   3069 C  CB  . LEU A 1 433 ? 11.212  19.514  3.423   1.00 146.59 ?  432  LEU A CB  1 
ATOM   3070 C  CG  . LEU A 1 433 ? 10.021  19.430  2.466   1.00 134.01 ?  432  LEU A CG  1 
ATOM   3071 C  CD1 . LEU A 1 433 ? 8.702   19.390  3.213   1.00 140.03 ?  432  LEU A CD1 1 
ATOM   3072 C  CD2 . LEU A 1 433 ? 10.053  20.597  1.523   1.00 121.06 ?  432  LEU A CD2 1 
ATOM   3073 N  N   . LYS A 1 434 ? 13.215  20.988  5.804   1.00 150.34 ?  433  LYS A N   1 
ATOM   3074 C  CA  . LYS A 1 434 ? 14.168  20.712  6.875   1.00 147.84 ?  433  LYS A CA  1 
ATOM   3075 C  C   . LYS A 1 434 ? 14.624  19.261  6.803   1.00 147.99 ?  433  LYS A C   1 
ATOM   3076 O  O   . LYS A 1 434 ? 14.965  18.640  7.813   1.00 153.81 ?  433  LYS A O   1 
ATOM   3077 C  CB  . LYS A 1 434 ? 13.550  21.039  8.234   1.00 146.24 ?  433  LYS A CB  1 
ATOM   3078 C  CG  . LYS A 1 434 ? 13.446  22.531  8.486   1.00 150.47 ?  433  LYS A CG  1 
ATOM   3079 C  CD  . LYS A 1 434 ? 12.668  22.840  9.747   1.00 156.07 ?  433  LYS A CD  1 
ATOM   3080 C  CE  . LYS A 1 434 ? 11.222  22.398  9.604   1.00 158.58 ?  433  LYS A CE  1 
ATOM   3081 N  NZ  . LYS A 1 434 ? 10.372  22.929  10.702  1.00 161.50 ?  433  LYS A NZ  1 
ATOM   3082 N  N   . CYS A 1 435 ? 14.609  18.730  5.585   1.00 133.96 ?  434  CYS A N   1 
ATOM   3083 C  CA  . CYS A 1 435 ? 14.899  17.327  5.345   1.00 130.39 ?  434  CYS A CA  1 
ATOM   3084 C  C   . CYS A 1 435 ? 16.338  17.105  4.900   1.00 121.98 ?  434  CYS A C   1 
ATOM   3085 O  O   . CYS A 1 435 ? 17.175  18.003  4.994   1.00 111.93 ?  434  CYS A O   1 
ATOM   3086 C  CB  . CYS A 1 435 ? 13.928  16.763  4.302   1.00 137.25 ?  434  CYS A CB  1 
ATOM   3087 S  SG  . CYS A 1 435 ? 14.174  17.383  2.627   1.00 125.53 ?  434  CYS A SG  1 
ATOM   3088 N  N   . LEU A 1 436 ? 16.606  15.908  4.388   1.00 123.71 ?  435  LEU A N   1 
ATOM   3089 C  CA  . LEU A 1 436 ? 17.950  15.537  3.967   1.00 125.12 ?  435  LEU A CA  1 
ATOM   3090 C  C   . LEU A 1 436 ? 18.265  16.077  2.580   1.00 118.43 ?  435  LEU A C   1 
ATOM   3091 O  O   . LEU A 1 436 ? 17.368  16.305  1.773   1.00 114.60 ?  435  LEU A O   1 
ATOM   3092 C  CB  . LEU A 1 436 ? 18.123  14.012  3.984   1.00 126.08 ?  435  LEU A CB  1 
ATOM   3093 C  CG  . LEU A 1 436 ? 18.273  13.269  5.317   1.00 131.55 ?  435  LEU A CG  1 
ATOM   3094 C  CD1 . LEU A 1 436 ? 16.979  13.244  6.121   1.00 138.47 ?  435  LEU A CD1 1 
ATOM   3095 C  CD2 . LEU A 1 436 ? 18.772  11.850  5.067   1.00 125.80 ?  435  LEU A CD2 1 
ATOM   3096 N  N   . LEU A 1 437 ? 19.549  16.297  2.320   1.00 115.97 ?  436  LEU A N   1 
ATOM   3097 C  CA  . LEU A 1 437 ? 20.020  16.668  0.991   1.00 119.89 ?  436  LEU A CA  1 
ATOM   3098 C  C   . LEU A 1 437 ? 21.087  15.684  0.536   1.00 132.77 ?  436  LEU A C   1 
ATOM   3099 O  O   . LEU A 1 437 ? 21.957  15.302  1.319   1.00 160.16 ?  436  LEU A O   1 
ATOM   3100 C  CB  . LEU A 1 437 ? 20.576  18.091  0.979   1.00 118.69 ?  436  LEU A CB  1 
ATOM   3101 C  CG  . LEU A 1 437 ? 21.002  18.610  -0.396  1.00 111.00 ?  436  LEU A CG  1 
ATOM   3102 C  CD1 . LEU A 1 437 ? 19.822  19.231  -1.120  1.00 106.75 ?  436  LEU A CD1 1 
ATOM   3103 C  CD2 . LEU A 1 437 ? 22.147  19.604  -0.280  1.00 115.76 ?  436  LEU A CD2 1 
ATOM   3104 N  N   . VAL A 1 438 ? 21.024  15.272  -0.726  1.00 106.65 ?  437  VAL A N   1 
ATOM   3105 C  CA  . VAL A 1 438 ? 22.027  14.362  -1.262  1.00 94.81  ?  437  VAL A CA  1 
ATOM   3106 C  C   . VAL A 1 438 ? 22.812  15.036  -2.371  1.00 110.04 ?  437  VAL A C   1 
ATOM   3107 O  O   . VAL A 1 438 ? 22.285  15.301  -3.450  1.00 117.64 ?  437  VAL A O   1 
ATOM   3108 C  CB  . VAL A 1 438 ? 21.409  13.078  -1.811  1.00 93.67  ?  437  VAL A CB  1 
ATOM   3109 C  CG1 . VAL A 1 438 ? 22.484  12.012  -1.955  1.00 93.79  ?  437  VAL A CG1 1 
ATOM   3110 C  CG2 . VAL A 1 438 ? 20.295  12.589  -0.899  1.00 96.60  ?  437  VAL A CG2 1 
ATOM   3111 N  N   . THR A 1 439 ? 24.076  15.324  -2.094  1.00 110.34 ?  438  THR A N   1 
ATOM   3112 C  CA  . THR A 1 439 ? 24.922  16.047  -3.032  1.00 115.31 ?  438  THR A CA  1 
ATOM   3113 C  C   . THR A 1 439 ? 26.363  15.791  -2.652  1.00 120.47 ?  438  THR A C   1 
ATOM   3114 O  O   . THR A 1 439 ? 26.664  15.499  -1.497  1.00 119.50 ?  438  THR A O   1 
ATOM   3115 C  CB  . THR A 1 439 ? 24.651  17.567  -3.027  1.00 120.45 ?  438  THR A CB  1 
ATOM   3116 O  OG1 . THR A 1 439 ? 23.243  17.817  -3.071  1.00 144.83 ?  438  THR A OG1 1 
ATOM   3117 C  CG2 . THR A 1 439 ? 25.307  18.233  -4.217  1.00 107.51 ?  438  THR A CG2 1 
ATOM   3118 N  N   . ASN A 1 440 ? 27.254  15.866  -3.629  1.00 124.68 ?  439  ASN A N   1 
ATOM   3119 C  CA  . ASN A 1 440 ? 28.661  15.695  -3.352  1.00 129.24 ?  439  ASN A CA  1 
ATOM   3120 C  C   . ASN A 1 440 ? 29.351  17.062  -3.352  1.00 114.71 ?  439  ASN A C   1 
ATOM   3121 O  O   . ASN A 1 440 ? 30.573  17.154  -3.215  1.00 102.29 ?  439  ASN A O   1 
ATOM   3122 C  CB  . ASN A 1 440 ? 29.276  14.769  -4.404  1.00 135.27 ?  439  ASN A CB  1 
ATOM   3123 C  CG  . ASN A 1 440 ? 30.222  13.756  -3.810  1.00 130.88 ?  439  ASN A CG  1 
ATOM   3124 O  OD1 . ASN A 1 440 ? 29.937  13.166  -2.769  1.00 118.20 ?  439  ASN A OD1 1 
ATOM   3125 N  ND2 . ASN A 1 440 ? 31.349  13.537  -4.474  1.00 142.28 ?  439  ASN A ND2 1 
ATOM   3126 N  N   . ASP A 1 441 ? 28.560  18.126  -3.485  1.00 110.89 ?  440  ASP A N   1 
ATOM   3127 C  CA  . ASP A 1 441 ? 29.122  19.470  -3.565  1.00 137.10 ?  440  ASP A CA  1 
ATOM   3128 C  C   . ASP A 1 441 ? 29.550  19.995  -2.206  1.00 160.89 ?  440  ASP A C   1 
ATOM   3129 O  O   . ASP A 1 441 ? 28.719  20.213  -1.323  1.00 162.50 ?  440  ASP A O   1 
ATOM   3130 C  CB  . ASP A 1 441 ? 28.113  20.444  -4.187  1.00 149.10 ?  440  ASP A CB  1 
ATOM   3131 C  CG  . ASP A 1 441 ? 28.418  20.760  -5.638  1.00 143.43 ?  440  ASP A CG  1 
ATOM   3132 O  OD1 . ASP A 1 441 ? 29.614  20.826  -5.997  1.00 133.48 ?  440  ASP A OD1 1 
ATOM   3133 O  OD2 . ASP A 1 441 ? 27.460  20.953  -6.418  1.00 140.01 ?  440  ASP A OD2 1 
ATOM   3134 N  N   . GLU A 1 442 ? 30.849  20.216  -2.049  1.00 176.74 ?  441  GLU A N   1 
ATOM   3135 C  CA  . GLU A 1 442 ? 31.358  20.931  -0.892  1.00 194.58 ?  441  GLU A CA  1 
ATOM   3136 C  C   . GLU A 1 442 ? 30.846  22.361  -0.988  1.00 190.28 ?  441  GLU A C   1 
ATOM   3137 O  O   . GLU A 1 442 ? 30.627  23.021  0.028   1.00 200.88 ?  441  GLU A O   1 
ATOM   3138 C  CB  . GLU A 1 442 ? 32.890  20.872  -0.831  1.00 216.96 ?  441  GLU A CB  1 
ATOM   3139 C  CG  . GLU A 1 442 ? 33.619  21.656  -1.924  1.00 234.11 ?  441  GLU A CG  1 
ATOM   3140 C  CD  . GLU A 1 442 ? 33.401  21.103  -3.321  1.00 236.44 ?  441  GLU A CD  1 
ATOM   3141 O  OE1 . GLU A 1 442 ? 32.925  19.955  -3.448  1.00 237.94 ?  441  GLU A OE1 1 
ATOM   3142 O  OE2 . GLU A 1 442 ? 33.705  21.821  -4.296  1.00 236.73 ?  441  GLU A OE2 1 
ATOM   3143 N  N   . MET A 1 443 ? 30.688  22.815  -2.235  1.00 177.21 ?  442  MET A N   1 
ATOM   3144 C  CA  . MET A 1 443 ? 30.177  24.140  -2.601  1.00 154.79 ?  442  MET A CA  1 
ATOM   3145 C  C   . MET A 1 443 ? 30.927  25.289  -1.909  1.00 134.27 ?  442  MET A C   1 
ATOM   3146 O  O   . MET A 1 443 ? 30.343  26.330  -1.610  1.00 137.75 ?  442  MET A O   1 
ATOM   3147 C  CB  . MET A 1 443 ? 28.651  24.236  -2.386  1.00 150.00 ?  442  MET A CB  1 
ATOM   3148 C  CG  . MET A 1 443 ? 28.108  24.146  -0.969  1.00 147.33 ?  442  MET A CG  1 
ATOM   3149 S  SD  . MET A 1 443 ? 26.314  23.902  -0.935  1.00 206.41 ?  442  MET A SD  1 
ATOM   3150 C  CE  . MET A 1 443 ? 26.159  22.251  -1.597  1.00 103.51 ?  442  MET A CE  1 
ATOM   3151 N  N   . ARG A 1 444 ? 32.229  25.108  -1.686  1.00 145.86 ?  443  ARG A N   1 
ATOM   3152 C  CA  . ARG A 1 444 ? 33.040  26.150  -1.063  1.00 162.74 ?  443  ARG A CA  1 
ATOM   3153 C  C   . ARG A 1 444 ? 33.473  27.136  -2.148  1.00 185.46 ?  443  ARG A C   1 
ATOM   3154 O  O   . ARG A 1 444 ? 34.638  27.221  -2.535  1.00 187.66 ?  443  ARG A O   1 
ATOM   3155 C  CB  . ARG A 1 444 ? 34.254  25.556  -0.327  1.00 157.18 ?  443  ARG A CB  1 
ATOM   3156 C  CG  . ARG A 1 444 ? 35.163  24.656  -1.163  1.00 153.04 ?  443  ARG A CG  1 
ATOM   3157 C  CD  . ARG A 1 444 ? 36.532  24.473  -0.517  1.00 157.93 ?  443  ARG A CD  1 
ATOM   3158 N  NE  . ARG A 1 444 ? 37.138  25.750  -0.143  1.00 165.37 ?  443  ARG A NE  1 
ATOM   3159 C  CZ  . ARG A 1 444 ? 38.437  26.024  -0.230  1.00 166.79 ?  443  ARG A CZ  1 
ATOM   3160 N  NH1 . ARG A 1 444 ? 39.285  25.112  -0.688  1.00 167.05 ?  443  ARG A NH1 1 
ATOM   3161 N  NH2 . ARG A 1 444 ? 38.890  27.216  0.136   1.00 171.23 ?  443  ARG A NH2 1 
ATOM   3162 N  N   . ASP A 1 445 ? 32.498  27.905  -2.619  1.00 194.94 ?  444  ASP A N   1 
ATOM   3163 C  CA  . ASP A 1 445 ? 32.719  28.888  -3.667  1.00 195.56 ?  444  ASP A CA  1 
ATOM   3164 C  C   . ASP A 1 445 ? 32.147  30.236  -3.243  1.00 213.19 ?  444  ASP A C   1 
ATOM   3165 O  O   . ASP A 1 445 ? 31.258  30.308  -2.397  1.00 215.76 ?  444  ASP A O   1 
ATOM   3166 C  CB  . ASP A 1 445 ? 32.080  28.415  -4.978  1.00 182.86 ?  444  ASP A CB  1 
ATOM   3167 C  CG  . ASP A 1 445 ? 32.211  29.431  -6.097  1.00 181.75 ?  444  ASP A CG  1 
ATOM   3168 O  OD1 . ASP A 1 445 ? 31.423  30.400  -6.115  1.00 181.44 ?  444  ASP A OD1 1 
ATOM   3169 O  OD2 . ASP A 1 445 ? 33.095  29.256  -6.961  1.00 181.71 ?  444  ASP A OD2 1 
ATOM   3170 N  N   . HIS A 1 446 ? 32.660  31.294  -3.863  1.00 231.57 ?  445  HIS A N   1 
ATOM   3171 C  CA  . HIS A 1 446 ? 32.393  32.675  -3.472  1.00 244.39 ?  445  HIS A CA  1 
ATOM   3172 C  C   . HIS A 1 446 ? 30.906  33.011  -3.463  1.00 237.45 ?  445  HIS A C   1 
ATOM   3173 O  O   . HIS A 1 446 ? 30.415  33.664  -2.540  1.00 242.24 ?  445  HIS A O   1 
ATOM   3174 C  CB  . HIS A 1 446 ? 33.136  33.620  -4.418  1.00 255.15 ?  445  HIS A CB  1 
ATOM   3175 C  CG  . HIS A 1 446 ? 34.557  33.219  -4.671  1.00 263.82 ?  445  HIS A CG  1 
ATOM   3176 N  ND1 . HIS A 1 446 ? 35.500  33.135  -3.669  1.00 268.10 ?  445  HIS A ND1 1 
ATOM   3177 C  CD2 . HIS A 1 446 ? 35.188  32.853  -5.812  1.00 266.52 ?  445  HIS A CD2 1 
ATOM   3178 C  CE1 . HIS A 1 446 ? 36.655  32.752  -4.184  1.00 270.02 ?  445  HIS A CE1 1 
ATOM   3179 N  NE2 . HIS A 1 446 ? 36.492  32.573  -5.483  1.00 270.97 ?  445  HIS A NE2 1 
ATOM   3180 N  N   . ILE A 1 447 ? 30.201  32.580  -4.504  1.00 221.73 ?  446  ILE A N   1 
ATOM   3181 C  CA  . ILE A 1 447 ? 28.764  32.808  -4.609  1.00 215.62 ?  446  ILE A CA  1 
ATOM   3182 C  C   . ILE A 1 447 ? 28.048  32.138  -3.442  1.00 213.63 ?  446  ILE A C   1 
ATOM   3183 O  O   . ILE A 1 447 ? 27.198  32.739  -2.785  1.00 204.01 ?  446  ILE A O   1 
ATOM   3184 C  CB  . ILE A 1 447 ? 28.183  32.273  -5.943  1.00 133.84 ?  446  ILE A CB  1 
ATOM   3185 C  CG1 . ILE A 1 447 ? 28.577  33.164  -7.132  1.00 137.28 ?  446  ILE A CG1 1 
ATOM   3186 C  CG2 . ILE A 1 447 ? 26.666  32.252  -5.884  1.00 123.88 ?  446  ILE A CG2 1 
ATOM   3187 C  CD1 . ILE A 1 447 ? 30.053  33.184  -7.499  1.00 138.68 ?  446  ILE A CD1 1 
ATOM   3188 N  N   . PHE A 1 448 ? 28.411  30.885  -3.191  1.00 220.89 ?  447  PHE A N   1 
ATOM   3189 C  CA  . PHE A 1 448 ? 27.871  30.118  -2.075  1.00 223.64 ?  447  PHE A CA  1 
ATOM   3190 C  C   . PHE A 1 448 ? 28.340  30.632  -0.714  1.00 262.41 ?  447  PHE A C   1 
ATOM   3191 O  O   . PHE A 1 448 ? 27.539  30.796  0.206   1.00 265.57 ?  447  PHE A O   1 
ATOM   3192 C  CB  . PHE A 1 448 ? 28.250  28.644  -2.218  1.00 220.08 ?  447  PHE A CB  1 
ATOM   3193 C  CG  . PHE A 1 448 ? 27.673  27.986  -3.439  1.00 207.28 ?  447  PHE A CG  1 
ATOM   3194 C  CD1 . PHE A 1 448 ? 26.357  27.554  -3.455  1.00 200.09 ?  447  PHE A CD1 1 
ATOM   3195 C  CD2 . PHE A 1 448 ? 28.451  27.793  -4.570  1.00 201.11 ?  447  PHE A CD2 1 
ATOM   3196 C  CE1 . PHE A 1 448 ? 25.825  26.948  -4.578  1.00 194.72 ?  447  PHE A CE1 1 
ATOM   3197 C  CE2 . PHE A 1 448 ? 27.927  27.188  -5.692  1.00 194.41 ?  447  PHE A CE2 1 
ATOM   3198 C  CZ  . PHE A 1 448 ? 26.612  26.764  -5.697  1.00 192.58 ?  447  PHE A CZ  1 
ATOM   3199 N  N   . GLU A 1 449 ? 29.641  30.886  -0.600  1.00 301.87 ?  448  GLU A N   1 
ATOM   3200 C  CA  . GLU A 1 449 ? 30.252  31.273  0.671   1.00 334.24 ?  448  GLU A CA  1 
ATOM   3201 C  C   . GLU A 1 449 ? 29.843  32.667  1.155   1.00 360.33 ?  448  GLU A C   1 
ATOM   3202 O  O   . GLU A 1 449 ? 29.893  32.938  2.351   1.00 384.66 ?  448  GLU A O   1 
ATOM   3203 C  CB  . GLU A 1 449 ? 31.779  31.180  0.583   1.00 340.45 ?  448  GLU A CB  1 
ATOM   3204 C  CG  . GLU A 1 449 ? 32.462  31.189  1.942   1.00 343.59 ?  448  GLU A CG  1 
ATOM   3205 C  CD  . GLU A 1 449 ? 31.878  30.154  2.888   1.00 339.34 ?  448  GLU A CD  1 
ATOM   3206 O  OE1 . GLU A 1 449 ? 31.712  28.988  2.469   1.00 331.90 ?  448  GLU A OE1 1 
ATOM   3207 O  OE2 . GLU A 1 449 ? 31.577  30.509  4.047   1.00 342.28 ?  448  GLU A OE2 1 
ATOM   3208 N  N   . LEU A 1 450 ? 29.508  33.571  0.239   1.00 316.82 ?  449  LEU A N   1 
ATOM   3209 C  CA  . LEU A 1 450 ? 28.998  34.873  0.659   1.00 278.36 ?  449  LEU A CA  1 
ATOM   3210 C  C   . LEU A 1 450 ? 27.723  34.640  1.467   1.00 252.59 ?  449  LEU A C   1 
ATOM   3211 O  O   . LEU A 1 450 ? 27.540  35.222  2.538   1.00 251.16 ?  449  LEU A O   1 
ATOM   3212 C  CB  . LEU A 1 450 ? 28.740  35.792  -0.537  1.00 267.21 ?  449  LEU A CB  1 
ATOM   3213 C  CG  . LEU A 1 450 ? 29.755  36.926  -0.719  1.00 255.32 ?  449  LEU A CG  1 
ATOM   3214 C  CD1 . LEU A 1 450 ? 29.704  37.897  0.455   1.00 252.53 ?  449  LEU A CD1 1 
ATOM   3215 C  CD2 . LEU A 1 450 ? 31.161  36.372  -0.889  1.00 249.10 ?  449  LEU A CD2 1 
ATOM   3216 N  N   . LEU A 1 451 ? 26.851  33.777  0.954   1.00 231.41 ?  450  LEU A N   1 
ATOM   3217 C  CA  . LEU A 1 451 ? 25.693  33.324  1.718   1.00 209.58 ?  450  LEU A CA  1 
ATOM   3218 C  C   . LEU A 1 451 ? 26.139  32.395  2.840   1.00 205.96 ?  450  LEU A C   1 
ATOM   3219 O  O   . LEU A 1 451 ? 25.582  32.420  3.939   1.00 202.66 ?  450  LEU A O   1 
ATOM   3220 C  CB  . LEU A 1 451 ? 24.678  32.616  0.822   1.00 187.41 ?  450  LEU A CB  1 
ATOM   3221 C  CG  . LEU A 1 451 ? 23.466  33.449  0.404   1.00 179.63 ?  450  LEU A CG  1 
ATOM   3222 C  CD1 . LEU A 1 451 ? 23.875  34.525  -0.592  1.00 185.89 ?  450  LEU A CD1 1 
ATOM   3223 C  CD2 . LEU A 1 451 ? 22.353  32.565  -0.156  1.00 156.78 ?  450  LEU A CD2 1 
ATOM   3224 N  N   . GLY A 1 452 ? 27.141  31.569  2.542   1.00 212.13 ?  451  GLY A N   1 
ATOM   3225 C  CA  . GLY A 1 452 ? 27.634  30.576  3.477   1.00 217.36 ?  451  GLY A CA  1 
ATOM   3226 C  C   . GLY A 1 452 ? 28.134  31.230  4.744   1.00 228.61 ?  451  GLY A C   1 
ATOM   3227 O  O   . GLY A 1 452 ? 28.858  32.220  4.706   1.00 246.17 ?  451  GLY A O   1 
ATOM   3228 N  N   . SER A 1 453 ? 27.747  30.676  5.881   1.00 221.57 ?  452  SER A N   1 
ATOM   3229 C  CA  . SER A 1 453 ? 28.034  31.324  7.148   1.00 214.96 ?  452  SER A CA  1 
ATOM   3230 C  C   . SER A 1 453 ? 28.510  30.347  8.211   1.00 190.78 ?  452  SER A C   1 
ATOM   3231 O  O   . SER A 1 453 ? 29.280  29.426  7.943   1.00 182.63 ?  452  SER A O   1 
ATOM   3232 C  CB  . SER A 1 453 ? 26.787  32.054  7.647   1.00 231.19 ?  452  SER A CB  1 
ATOM   3233 O  OG  . SER A 1 453 ? 25.611  31.302  7.378   1.00 226.62 ?  452  SER A OG  1 
ATOM   3234 N  N   . THR A 1 454 ? 28.053  30.590  9.432   1.00 182.65 ?  453  THR A N   1 
ATOM   3235 C  CA  . THR A 1 454 ? 28.266  29.689  10.549  1.00 175.45 ?  453  THR A CA  1 
ATOM   3236 C  C   . THR A 1 454 ? 27.068  28.745  10.581  1.00 164.78 ?  453  THR A C   1 
ATOM   3237 O  O   . THR A 1 454 ? 27.179  27.566  10.926  1.00 165.69 ?  453  THR A O   1 
ATOM   3238 C  CB  . THR A 1 454 ? 28.400  30.453  11.864  1.00 180.13 ?  453  THR A CB  1 
ATOM   3239 O  OG1 . THR A 1 454 ? 27.186  31.170  12.129  1.00 178.65 ?  453  THR A OG1 1 
ATOM   3240 C  CG2 . THR A 1 454 ? 29.559  31.441  11.776  1.00 186.04 ?  453  THR A CG2 1 
ATOM   3241 N  N   . PHE A 1 455 ? 25.923  29.293  10.184  1.00 173.10 ?  454  PHE A N   1 
ATOM   3242 C  CA  . PHE A 1 455 ? 24.675  28.553  10.043  1.00 171.46 ?  454  PHE A CA  1 
ATOM   3243 C  C   . PHE A 1 455 ? 24.822  27.494  8.950   1.00 163.62 ?  454  PHE A C   1 
ATOM   3244 O  O   . PHE A 1 455 ? 24.316  26.380  9.084   1.00 170.03 ?  454  PHE A O   1 
ATOM   3245 C  CB  . PHE A 1 455 ? 23.520  29.517  9.733   1.00 177.13 ?  454  PHE A CB  1 
ATOM   3246 C  CG  . PHE A 1 455 ? 22.201  28.840  9.458   1.00 177.24 ?  454  PHE A CG  1 
ATOM   3247 C  CD1 . PHE A 1 455 ? 21.863  27.642  10.064  1.00 176.66 ?  454  PHE A CD1 1 
ATOM   3248 C  CD2 . PHE A 1 455 ? 21.293  29.414  8.587   1.00 177.63 ?  454  PHE A CD2 1 
ATOM   3249 C  CE1 . PHE A 1 455 ? 20.661  27.031  9.795   1.00 174.96 ?  454  PHE A CE1 1 
ATOM   3250 C  CE2 . PHE A 1 455 ? 20.082  28.806  8.325   1.00 168.20 ?  454  PHE A CE2 1 
ATOM   3251 C  CZ  . PHE A 1 455 ? 19.764  27.616  8.927   1.00 164.31 ?  454  PHE A CZ  1 
ATOM   3252 N  N   . PHE A 1 456 ? 25.517  27.841  7.871   1.00 156.46 ?  455  PHE A N   1 
ATOM   3253 C  CA  . PHE A 1 456 ? 25.637  26.935  6.730   1.00 156.90 ?  455  PHE A CA  1 
ATOM   3254 C  C   . PHE A 1 456 ? 26.328  25.614  7.058   1.00 129.91 ?  455  PHE A C   1 
ATOM   3255 O  O   . PHE A 1 456 ? 25.846  24.549  6.667   1.00 132.49 ?  455  PHE A O   1 
ATOM   3256 C  CB  . PHE A 1 456 ? 26.387  27.625  5.600   1.00 158.51 ?  455  PHE A CB  1 
ATOM   3257 C  CG  . PHE A 1 456 ? 26.107  27.046  4.249   1.00 159.00 ?  455  PHE A CG  1 
ATOM   3258 C  CD1 . PHE A 1 456 ? 24.806  26.867  3.826   1.00 148.16 ?  455  PHE A CD1 1 
ATOM   3259 C  CD2 . PHE A 1 456 ? 27.148  26.725  3.378   1.00 154.67 ?  455  PHE A CD2 1 
ATOM   3260 C  CE1 . PHE A 1 456 ? 24.537  26.333  2.580   1.00 132.68 ?  455  PHE A CE1 1 
ATOM   3261 C  CE2 . PHE A 1 456 ? 26.880  26.202  2.127   1.00 125.59 ?  455  PHE A CE2 1 
ATOM   3262 C  CZ  . PHE A 1 456 ? 25.566  26.007  1.734   1.00 116.73 ?  455  PHE A CZ  1 
ATOM   3263 N  N   . GLN A 1 457 ? 27.427  25.689  7.801   1.00 133.68 ?  456  GLN A N   1 
ATOM   3264 C  CA  . GLN A 1 457 ? 28.141  24.507  8.260   1.00 140.29 ?  456  GLN A CA  1 
ATOM   3265 C  C   . GLN A 1 457 ? 27.296  23.689  9.232   1.00 145.95 ?  456  GLN A C   1 
ATOM   3266 O  O   . GLN A 1 457 ? 27.417  22.470  9.291   1.00 142.18 ?  456  GLN A O   1 
ATOM   3267 C  CB  . GLN A 1 457 ? 29.476  24.904  8.892   1.00 166.96 ?  456  GLN A CB  1 
ATOM   3268 C  CG  . GLN A 1 457 ? 30.638  24.987  7.907   1.00 186.80 ?  456  GLN A CG  1 
ATOM   3269 C  CD  . GLN A 1 457 ? 30.280  25.706  6.612   1.00 185.12 ?  456  GLN A CD  1 
ATOM   3270 O  OE1 . GLN A 1 457 ? 29.614  26.744  6.621   1.00 191.96 ?  456  GLN A OE1 1 
ATOM   3271 N  NE2 . GLN A 1 457 ? 30.732  25.157  5.490   1.00 166.54 ?  456  GLN A NE2 1 
ATOM   3272 N  N   . LYS A 1 458 ? 26.461  24.368  10.013  1.00 160.04 ?  457  LYS A N   1 
ATOM   3273 C  CA  . LYS A 1 458 ? 25.558  23.681  10.932  1.00 165.33 ?  457  LYS A CA  1 
ATOM   3274 C  C   . LYS A 1 458 ? 24.526  22.890  10.143  1.00 157.36 ?  457  LYS A C   1 
ATOM   3275 O  O   . LYS A 1 458 ? 24.283  21.712  10.415  1.00 162.11 ?  457  LYS A O   1 
ATOM   3276 C  CB  . LYS A 1 458 ? 24.848  24.676  11.852  1.00 165.81 ?  457  LYS A CB  1 
ATOM   3277 C  CG  . LYS A 1 458 ? 25.743  25.378  12.854  1.00 167.72 ?  457  LYS A CG  1 
ATOM   3278 C  CD  . LYS A 1 458 ? 25.039  26.594  13.439  1.00 174.48 ?  457  LYS A CD  1 
ATOM   3279 C  CE  . LYS A 1 458 ? 23.653  26.240  13.964  1.00 173.21 ?  457  LYS A CE  1 
ATOM   3280 N  NZ  . LYS A 1 458 ? 22.885  27.455  14.364  1.00 181.37 ?  457  LYS A NZ  1 
ATOM   3281 N  N   . TRP A 1 459 ? 23.941  23.547  9.150   1.00 143.61 ?  458  TRP A N   1 
ATOM   3282 C  CA  . TRP A 1 459 ? 22.931  22.928  8.313   1.00 135.30 ?  458  TRP A CA  1 
ATOM   3283 C  C   . TRP A 1 459 ? 23.499  21.796  7.466   1.00 132.54 ?  458  TRP A C   1 
ATOM   3284 O  O   . TRP A 1 459 ? 22.834  20.781  7.258   1.00 135.00 ?  458  TRP A O   1 
ATOM   3285 C  CB  . TRP A 1 459 ? 22.292  23.973  7.405   1.00 137.93 ?  458  TRP A CB  1 
ATOM   3286 C  CG  . TRP A 1 459 ? 21.007  23.525  6.795   1.00 138.38 ?  458  TRP A CG  1 
ATOM   3287 C  CD1 . TRP A 1 459 ? 19.776  23.496  7.384   1.00 123.05 ?  458  TRP A CD1 1 
ATOM   3288 C  CD2 . TRP A 1 459 ? 20.834  22.999  5.474   1.00 127.90 ?  458  TRP A CD2 1 
ATOM   3289 N  NE1 . TRP A 1 459 ? 18.843  23.007  6.500   1.00 120.01 ?  458  TRP A NE1 1 
ATOM   3290 C  CE2 . TRP A 1 459 ? 19.469  22.691  5.325   1.00 126.74 ?  458  TRP A CE2 1 
ATOM   3291 C  CE3 . TRP A 1 459 ? 21.703  22.768  4.403   1.00 130.37 ?  458  TRP A CE3 1 
ATOM   3292 C  CZ2 . TRP A 1 459 ? 18.954  22.158  4.145   1.00 127.17 ?  458  TRP A CZ2 1 
ATOM   3293 C  CZ3 . TRP A 1 459 ? 21.190  22.242  3.237   1.00 110.51 ?  458  TRP A CZ3 1 
ATOM   3294 C  CH2 . TRP A 1 459 ? 19.828  21.943  3.116   1.00 115.23 ?  458  TRP A CH2 1 
ATOM   3295 N  N   . LYS A 1 460 ? 24.725  21.967  6.976   1.00 121.88 ?  459  LYS A N   1 
ATOM   3296 C  CA  . LYS A 1 460 ? 25.355  20.931  6.156   1.00 118.90 ?  459  LYS A CA  1 
ATOM   3297 C  C   . LYS A 1 460 ? 25.613  19.643  6.939   1.00 140.28 ?  459  LYS A C   1 
ATOM   3298 O  O   . LYS A 1 460 ? 25.285  18.563  6.463   1.00 142.39 ?  459  LYS A O   1 
ATOM   3299 C  CB  . LYS A 1 460 ? 26.659  21.451  5.532   1.00 119.29 ?  459  LYS A CB  1 
ATOM   3300 C  CG  . LYS A 1 460 ? 26.442  22.348  4.311   1.00 117.04 ?  459  LYS A CG  1 
ATOM   3301 C  CD  . LYS A 1 460 ? 27.748  22.843  3.695   1.00 118.04 ?  459  LYS A CD  1 
ATOM   3302 C  CE  . LYS A 1 460 ? 28.748  21.717  3.482   1.00 117.37 ?  459  LYS A CE  1 
ATOM   3303 N  NZ  . LYS A 1 460 ? 30.109  22.255  3.183   1.00 119.89 ?  459  LYS A NZ  1 
ATOM   3304 N  N   . GLU A 1 461 ? 26.167  19.754  8.142   1.00 153.80 ?  460  GLU A N   1 
ATOM   3305 C  CA  . GLU A 1 461 ? 26.379  18.583  8.987   1.00 171.43 ?  460  GLU A CA  1 
ATOM   3306 C  C   . GLU A 1 461 ? 25.021  18.006  9.356   1.00 172.68 ?  460  GLU A C   1 
ATOM   3307 O  O   . GLU A 1 461 ? 24.856  16.794  9.472   1.00 186.14 ?  460  GLU A O   1 
ATOM   3308 C  CB  . GLU A 1 461 ? 27.191  18.939  10.236  1.00 188.34 ?  460  GLU A CB  1 
ATOM   3309 C  CG  . GLU A 1 461 ? 28.453  19.734  9.954   1.00 197.74 ?  460  GLU A CG  1 
ATOM   3310 C  CD  . GLU A 1 461 ? 29.544  18.967  9.205   1.00 202.35 ?  460  GLU A CD  1 
ATOM   3311 O  OE1 . GLU A 1 461 ? 29.323  17.829  8.741   1.00 201.61 ?  460  GLU A OE1 1 
ATOM   3312 O  OE2 . GLU A 1 461 ? 30.630  19.552  9.021   1.00 204.41 ?  460  GLU A OE2 1 
ATOM   3313 N  N   . ARG A 1 462 ? 24.047  18.892  9.514   1.00 150.12 ?  461  ARG A N   1 
ATOM   3314 C  CA  . ARG A 1 462 ? 22.687  18.499  9.851   1.00 142.05 ?  461  ARG A CA  1 
ATOM   3315 C  C   . ARG A 1 462 ? 21.985  17.710  8.733   1.00 135.43 ?  461  ARG A C   1 
ATOM   3316 O  O   . ARG A 1 462 ? 21.239  16.774  9.018   1.00 126.71 ?  461  ARG A O   1 
ATOM   3317 C  CB  . ARG A 1 462 ? 21.870  19.741  10.220  1.00 146.93 ?  461  ARG A CB  1 
ATOM   3318 C  CG  . ARG A 1 462 ? 20.400  19.496  10.531  1.00 150.16 ?  461  ARG A CG  1 
ATOM   3319 C  CD  . ARG A 1 462 ? 20.207  18.535  11.686  1.00 157.01 ?  461  ARG A CD  1 
ATOM   3320 N  NE  . ARG A 1 462 ? 18.795  18.219  11.893  1.00 170.58 ?  461  ARG A NE  1 
ATOM   3321 C  CZ  . ARG A 1 462 ? 18.165  17.175  11.361  1.00 178.88 ?  461  ARG A CZ  1 
ATOM   3322 N  NH1 . ARG A 1 462 ? 18.819  16.319  10.587  1.00 178.58 ?  461  ARG A NH1 1 
ATOM   3323 N  NH2 . ARG A 1 462 ? 16.876  16.986  11.606  1.00 182.98 ?  461  ARG A NH2 1 
ATOM   3324 N  N   . HIS A 1 463 ? 22.198  18.087  7.472   1.00 138.14 ?  462  HIS A N   1 
ATOM   3325 C  CA  . HIS A 1 463 ? 21.330  17.587  6.400   1.00 128.61 ?  462  HIS A CA  1 
ATOM   3326 C  C   . HIS A 1 463 ? 21.997  16.939  5.176   1.00 132.65 ?  462  HIS A C   1 
ATOM   3327 O  O   . HIS A 1 463 ? 21.340  16.212  4.427   1.00 129.95 ?  462  HIS A O   1 
ATOM   3328 C  CB  . HIS A 1 463 ? 20.442  18.736  5.929   1.00 113.83 ?  462  HIS A CB  1 
ATOM   3329 C  CG  . HIS A 1 463 ? 19.302  19.018  6.854   1.00 117.45 ?  462  HIS A CG  1 
ATOM   3330 N  ND1 . HIS A 1 463 ? 18.618  20.214  6.854   1.00 122.76 ?  462  HIS A ND1 1 
ATOM   3331 C  CD2 . HIS A 1 463 ? 18.717  18.252  7.804   1.00 119.80 ?  462  HIS A CD2 1 
ATOM   3332 C  CE1 . HIS A 1 463 ? 17.670  20.179  7.772   1.00 121.37 ?  462  HIS A CE1 1 
ATOM   3333 N  NE2 . HIS A 1 463 ? 17.706  18.997  8.361   1.00 125.01 ?  462  HIS A NE2 1 
ATOM   3334 N  N   . GLN A 1 464 ? 23.285  17.190  4.967   1.00 131.88 ?  463  GLN A N   1 
ATOM   3335 C  CA  . GLN A 1 464 ? 23.946  16.729  3.743   1.00 125.27 ?  463  GLN A CA  1 
ATOM   3336 C  C   . GLN A 1 464 ? 24.350  15.256  3.774   1.00 132.33 ?  463  GLN A C   1 
ATOM   3337 O  O   . GLN A 1 464 ? 24.913  14.765  4.757   1.00 134.21 ?  463  GLN A O   1 
ATOM   3338 C  CB  . GLN A 1 464 ? 25.174  17.585  3.440   1.00 122.09 ?  463  GLN A CB  1 
ATOM   3339 C  CG  . GLN A 1 464 ? 25.360  17.868  1.959   1.00 111.32 ?  463  GLN A CG  1 
ATOM   3340 C  CD  . GLN A 1 464 ? 26.679  18.543  1.661   1.00 125.83 ?  463  GLN A CD  1 
ATOM   3341 O  OE1 . GLN A 1 464 ? 27.531  18.681  2.539   1.00 135.83 ?  463  GLN A OE1 1 
ATOM   3342 N  NE2 . GLN A 1 464 ? 26.860  18.964  0.416   1.00 129.24 ?  463  GLN A NE2 1 
ATOM   3343 N  N   . VAL A 1 465 ? 24.064  14.572  2.669   1.00 125.98 ?  464  VAL A N   1 
ATOM   3344 C  CA  . VAL A 1 465 ? 24.401  13.166  2.486   1.00 121.39 ?  464  VAL A CA  1 
ATOM   3345 C  C   . VAL A 1 465 ? 25.508  13.051  1.445   1.00 102.90 ?  464  VAL A C   1 
ATOM   3346 O  O   . VAL A 1 465 ? 25.561  13.839  0.506   1.00 128.56 ?  464  VAL A O   1 
ATOM   3347 C  CB  . VAL A 1 465 ? 23.176  12.355  2.035   1.00 103.10 ?  464  VAL A CB  1 
ATOM   3348 C  CG1 . VAL A 1 465 ? 23.522  10.882  1.894   1.00 103.64 ?  464  VAL A CG1 1 
ATOM   3349 C  CG2 . VAL A 1 465 ? 22.035  12.530  3.019   1.00 105.25 ?  464  VAL A CG2 1 
ATOM   3350 N  N   . ARG A 1 466 ? 26.411  12.095  1.626   1.00 111.23 ?  465  ARG A N   1 
ATOM   3351 C  CA  . ARG A 1 466 ? 27.550  11.964  0.729   1.00 124.53 ?  465  ARG A CA  1 
ATOM   3352 C  C   . ARG A 1 466 ? 27.611  10.537  0.196   1.00 133.21 ?  465  ARG A C   1 
ATOM   3353 O  O   . ARG A 1 466 ? 27.174  9.605   0.870   1.00 141.66 ?  465  ARG A O   1 
ATOM   3354 C  CB  . ARG A 1 466 ? 28.842  12.299  1.461   1.00 139.65 ?  465  ARG A CB  1 
ATOM   3355 C  CG  . ARG A 1 466 ? 28.834  13.652  2.137   1.00 138.26 ?  465  ARG A CG  1 
ATOM   3356 C  CD  . ARG A 1 466 ? 30.234  14.091  2.499   1.00 151.90 ?  465  ARG A CD  1 
ATOM   3357 N  NE  . ARG A 1 466 ? 30.216  15.324  3.281   1.00 174.63 ?  465  ARG A NE  1 
ATOM   3358 C  CZ  . ARG A 1 466 ? 30.045  16.542  2.779   1.00 179.85 ?  465  ARG A CZ  1 
ATOM   3359 N  NH1 . ARG A 1 466 ? 29.870  16.714  1.475   1.00 182.41 ?  465  ARG A NH1 1 
ATOM   3360 N  NH2 . ARG A 1 466 ? 30.046  17.593  3.589   1.00 176.90 ?  465  ARG A NH2 1 
ATOM   3361 N  N   . TYR A 1 467 ? 28.141  10.353  -1.009  1.00 129.51 ?  466  TYR A N   1 
ATOM   3362 C  CA  . TYR A 1 467 ? 28.221  9.011   -1.570  1.00 121.21 ?  466  TYR A CA  1 
ATOM   3363 C  C   . TYR A 1 467 ? 29.582  8.738   -2.199  1.00 119.68 ?  466  TYR A C   1 
ATOM   3364 O  O   . TYR A 1 467 ? 30.287  9.663   -2.604  1.00 119.69 ?  466  TYR A O   1 
ATOM   3365 C  CB  . TYR A 1 467 ? 27.111  8.792   -2.601  1.00 120.97 ?  466  TYR A CB  1 
ATOM   3366 C  CG  . TYR A 1 467 ? 27.115  9.764   -3.759  1.00 132.93 ?  466  TYR A CG  1 
ATOM   3367 C  CD1 . TYR A 1 467 ? 27.885  9.520   -4.890  1.00 144.39 ?  466  TYR A CD1 1 
ATOM   3368 C  CD2 . TYR A 1 467 ? 26.357  10.925  -3.722  1.00 131.89 ?  466  TYR A CD2 1 
ATOM   3369 C  CE1 . TYR A 1 467 ? 27.895  10.398  -5.952  1.00 141.27 ?  466  TYR A CE1 1 
ATOM   3370 C  CE2 . TYR A 1 467 ? 26.363  11.813  -4.780  1.00 138.42 ?  466  TYR A CE2 1 
ATOM   3371 C  CZ  . TYR A 1 467 ? 27.133  11.544  -5.894  1.00 142.48 ?  466  TYR A CZ  1 
ATOM   3372 O  OH  . TYR A 1 467 ? 27.143  12.424  -6.954  1.00 147.17 ?  466  TYR A OH  1 
ATOM   3373 N  N   . THR A 1 468 ? 29.951  7.462   -2.254  1.00 123.53 ?  467  THR A N   1 
ATOM   3374 C  CA  . THR A 1 468 ? 31.116  7.029   -3.016  1.00 136.14 ?  467  THR A CA  1 
ATOM   3375 C  C   . THR A 1 468 ? 30.744  5.827   -3.884  1.00 143.80 ?  467  THR A C   1 
ATOM   3376 O  O   . THR A 1 468 ? 29.991  4.954   -3.454  1.00 155.97 ?  467  THR A O   1 
ATOM   3377 C  CB  . THR A 1 468 ? 32.300  6.661   -2.101  1.00 142.72 ?  467  THR A CB  1 
ATOM   3378 O  OG1 . THR A 1 468 ? 32.587  7.758   -1.230  1.00 156.25 ?  467  THR A OG1 1 
ATOM   3379 C  CG2 . THR A 1 468 ? 33.543  6.336   -2.923  1.00 138.59 ?  467  THR A CG2 1 
ATOM   3380 N  N   . PHE A 1 469 ? 31.271  5.791   -5.103  1.00 138.60 ?  468  PHE A N   1 
ATOM   3381 C  CA  . PHE A 1 469 ? 30.943  4.747   -6.060  1.00 128.97 ?  468  PHE A CA  1 
ATOM   3382 C  C   . PHE A 1 469 ? 32.222  4.085   -6.562  1.00 147.16 ?  468  PHE A C   1 
ATOM   3383 O  O   . PHE A 1 469 ? 33.066  4.749   -7.160  1.00 154.96 ?  468  PHE A O   1 
ATOM   3384 C  CB  . PHE A 1 469 ? 30.173  5.341   -7.233  1.00 120.82 ?  468  PHE A CB  1 
ATOM   3385 C  CG  . PHE A 1 469 ? 28.683  5.320   -7.066  1.00 113.45 ?  468  PHE A CG  1 
ATOM   3386 C  CD1 . PHE A 1 469 ? 27.972  4.143   -7.190  1.00 117.86 ?  468  PHE A CD1 1 
ATOM   3387 C  CD2 . PHE A 1 469 ? 27.991  6.485   -6.789  1.00 105.62 ?  468  PHE A CD2 1 
ATOM   3388 C  CE1 . PHE A 1 469 ? 26.597  4.134   -7.042  1.00 110.72 ?  468  PHE A CE1 1 
ATOM   3389 C  CE2 . PHE A 1 469 ? 26.619  6.479   -6.638  1.00 92.83  ?  468  PHE A CE2 1 
ATOM   3390 C  CZ  . PHE A 1 469 ? 25.923  5.306   -6.768  1.00 92.16  ?  468  PHE A CZ  1 
ATOM   3391 N  N   . VAL A 1 470 ? 32.377  2.788   -6.322  1.00 155.02 ?  469  VAL A N   1 
ATOM   3392 C  CA  . VAL A 1 470 ? 33.508  2.052   -6.888  1.00 160.24 ?  469  VAL A CA  1 
ATOM   3393 C  C   . VAL A 1 470 ? 33.083  0.692   -7.435  1.00 172.12 ?  469  VAL A C   1 
ATOM   3394 O  O   . VAL A 1 470 ? 32.718  -0.197  -6.670  1.00 169.98 ?  469  VAL A O   1 
ATOM   3395 C  CB  . VAL A 1 470 ? 34.628  1.854   -5.847  1.00 151.33 ?  469  VAL A CB  1 
ATOM   3396 C  CG1 . VAL A 1 470 ? 35.531  3.076   -5.792  1.00 144.85 ?  469  VAL A CG1 1 
ATOM   3397 C  CG2 . VAL A 1 470 ? 34.034  1.569   -4.481  1.00 142.48 ?  469  VAL A CG2 1 
ATOM   3398 N  N   . LYS A 1 471 ? 33.111  0.561   -8.764  1.00 193.10 ?  470  LYS A N   1 
ATOM   3399 C  CA  . LYS A 1 471 ? 32.952  -0.710  -9.486  1.00 192.52 ?  470  LYS A CA  1 
ATOM   3400 C  C   . LYS A 1 471 ? 31.803  -1.541  -8.916  1.00 184.25 ?  470  LYS A C   1 
ATOM   3401 O  O   . LYS A 1 471 ? 31.818  -2.771  -8.943  1.00 198.27 ?  470  LYS A O   1 
ATOM   3402 C  CB  . LYS A 1 471 ? 34.274  -1.494  -9.450  1.00 192.13 ?  470  LYS A CB  1 
ATOM   3403 C  CG  . LYS A 1 471 ? 34.374  -2.732  -10.367 1.00 192.24 ?  470  LYS A CG  1 
ATOM   3404 C  CD  . LYS A 1 471 ? 33.977  -2.463  -11.813 1.00 180.30 ?  470  LYS A CD  1 
ATOM   3405 C  CE  . LYS A 1 471 ? 34.053  -3.748  -12.632 1.00 175.36 ?  470  LYS A CE  1 
ATOM   3406 N  NZ  . LYS A 1 471 ? 33.537  -3.573  -14.014 1.00 171.77 ?  470  LYS A NZ  1 
ATOM   3407 N  N   . GLY A 1 472 ? 30.807  -0.840  -8.387  1.00 164.66 ?  471  GLY A N   1 
ATOM   3408 C  CA  . GLY A 1 472 ? 29.651  -1.468  -7.783  1.00 162.89 ?  471  GLY A CA  1 
ATOM   3409 C  C   . GLY A 1 472 ? 28.531  -0.480  -7.539  1.00 162.13 ?  471  GLY A C   1 
ATOM   3410 O  O   . GLY A 1 472 ? 28.145  0.289   -8.421  1.00 100.55 ?  471  GLY A O   1 
ATOM   3411 N  N   . ASN A 1 473 ? 28.028  -0.506  -6.310  1.00 154.99 ?  472  ASN A N   1 
ATOM   3412 C  CA  . ASN A 1 473 ? 26.959  0.374   -5.870  1.00 151.69 ?  472  ASN A CA  1 
ATOM   3413 C  C   . ASN A 1 473 ? 27.347  1.181   -4.641  1.00 131.99 ?  472  ASN A C   1 
ATOM   3414 O  O   . ASN A 1 473 ? 28.374  0.931   -4.024  1.00 136.92 ?  472  ASN A O   1 
ATOM   3415 C  CB  . ASN A 1 473 ? 25.671  -0.413  -5.630  1.00 180.02 ?  472  ASN A CB  1 
ATOM   3416 C  CG  . ASN A 1 473 ? 24.951  -0.755  -6.929  1.00 199.05 ?  472  ASN A CG  1 
ATOM   3417 O  OD1 . ASN A 1 473 ? 24.074  -0.011  -7.379  1.00 204.63 ?  472  ASN A OD1 1 
ATOM   3418 N  ND2 . ASN A 1 473 ? 25.319  -1.878  -7.538  1.00 206.31 ?  472  ASN A ND2 1 
ATOM   3419 N  N   . LEU A 1 474 ? 26.508  2.153   -4.310  1.00 119.09 ?  473  LEU A N   1 
ATOM   3420 C  CA  . LEU A 1 474 ? 26.802  3.174   -3.316  1.00 113.55 ?  473  LEU A CA  1 
ATOM   3421 C  C   . LEU A 1 474 ? 26.819  2.742   -1.856  1.00 117.15 ?  473  LEU A C   1 
ATOM   3422 O  O   . LEU A 1 474 ? 25.973  1.979   -1.397  1.00 109.35 ?  473  LEU A O   1 
ATOM   3423 C  CB  . LEU A 1 474 ? 25.794  4.316   -3.456  1.00 102.11 ?  473  LEU A CB  1 
ATOM   3424 C  CG  . LEU A 1 474 ? 24.320  3.901   -3.417  1.00 99.94  ?  473  LEU A CG  1 
ATOM   3425 C  CD1 . LEU A 1 474 ? 23.730  3.966   -2.022  1.00 102.70 ?  473  LEU A CD1 1 
ATOM   3426 C  CD2 . LEU A 1 474 ? 23.538  4.779   -4.340  1.00 96.25  ?  473  LEU A CD2 1 
ATOM   3427 N  N   . LYS A 1 475 ? 27.833  3.236   -1.154  1.00 131.57 ?  474  LYS A N   1 
ATOM   3428 C  CA  . LYS A 1 475 ? 27.896  3.218   0.301   1.00 143.82 ?  474  LYS A CA  1 
ATOM   3429 C  C   . LYS A 1 475 ? 27.544  4.649   0.713   1.00 127.17 ?  474  LYS A C   1 
ATOM   3430 O  O   . LYS A 1 475 ? 28.159  5.601   0.228   1.00 108.92 ?  474  LYS A O   1 
ATOM   3431 C  CB  . LYS A 1 475 ? 29.286  2.808   0.811   1.00 154.62 ?  474  LYS A CB  1 
ATOM   3432 C  CG  . LYS A 1 475 ? 29.349  2.338   2.276   1.00 155.42 ?  474  LYS A CG  1 
ATOM   3433 C  CD  . LYS A 1 475 ? 29.231  0.819   2.426   1.00 160.81 ?  474  LYS A CD  1 
ATOM   3434 C  CE  . LYS A 1 475 ? 29.219  0.390   3.896   1.00 175.75 ?  474  LYS A CE  1 
ATOM   3435 N  NZ  . LYS A 1 475 ? 28.047  0.887   4.665   1.00 177.75 ?  474  LYS A NZ  1 
ATOM   3436 N  N   . LEU A 1 476 ? 26.520  4.805   1.548   1.00 143.25 ?  475  LEU A N   1 
ATOM   3437 C  CA  . LEU A 1 476 ? 26.014  6.131   1.912   1.00 143.86 ?  475  LEU A CA  1 
ATOM   3438 C  C   . LEU A 1 476 ? 26.566  6.683   3.228   1.00 149.79 ?  475  LEU A C   1 
ATOM   3439 O  O   . LEU A 1 476 ? 26.417  6.070   4.287   1.00 151.62 ?  475  LEU A O   1 
ATOM   3440 C  CB  . LEU A 1 476 ? 24.484  6.120   1.994   1.00 127.98 ?  475  LEU A CB  1 
ATOM   3441 C  CG  . LEU A 1 476 ? 23.720  6.408   0.706   1.00 105.34 ?  475  LEU A CG  1 
ATOM   3442 C  CD1 . LEU A 1 476 ? 22.260  6.691   1.004   1.00 105.33 ?  475  LEU A CD1 1 
ATOM   3443 C  CD2 . LEU A 1 476 ? 24.360  7.582   -0.005  1.00 102.32 ?  475  LEU A CD2 1 
ATOM   3444 N  N   . GLU A 1 477 ? 27.220  7.839   3.146   1.00 138.39 ?  476  GLU A N   1 
ATOM   3445 C  CA  . GLU A 1 477 ? 27.627  8.564   4.341   1.00 123.80 ?  476  GLU A CA  1 
ATOM   3446 C  C   . GLU A 1 477 ? 26.447  9.428   4.773   1.00 120.70 ?  476  GLU A C   1 
ATOM   3447 O  O   . GLU A 1 477 ? 25.709  9.945   3.941   1.00 116.85 ?  476  GLU A O   1 
ATOM   3448 C  CB  . GLU A 1 477 ? 28.869  9.417   4.069   1.00 122.39 ?  476  GLU A CB  1 
ATOM   3449 C  CG  . GLU A 1 477 ? 29.335  10.275  5.246   1.00 143.84 ?  476  GLU A CG  1 
ATOM   3450 C  CD  . GLU A 1 477 ? 30.040  9.472   6.331   1.00 160.38 ?  476  GLU A CD  1 
ATOM   3451 O  OE1 . GLU A 1 477 ? 30.922  8.658   5.990   1.00 172.49 ?  476  GLU A OE1 1 
ATOM   3452 O  OE2 . GLU A 1 477 ? 29.715  9.655   7.525   1.00 152.79 ?  476  GLU A OE2 1 
ATOM   3453 N  N   . MET A 1 478 ? 26.281  9.593   6.078   1.00 127.46 ?  477  MET A N   1 
ATOM   3454 C  CA  . MET A 1 478 ? 25.095  10.238  6.628   1.00 124.84 ?  477  MET A CA  1 
ATOM   3455 C  C   . MET A 1 478 ? 25.459  11.425  7.504   1.00 127.52 ?  477  MET A C   1 
ATOM   3456 O  O   . MET A 1 478 ? 26.583  11.513  7.996   1.00 134.74 ?  477  MET A O   1 
ATOM   3457 C  CB  . MET A 1 478 ? 24.279  9.227   7.437   1.00 128.85 ?  477  MET A CB  1 
ATOM   3458 C  CG  . MET A 1 478 ? 23.615  8.151   6.604   1.00 119.82 ?  477  MET A CG  1 
ATOM   3459 S  SD  . MET A 1 478 ? 22.529  8.863   5.356   1.00 146.01 ?  477  MET A SD  1 
ATOM   3460 C  CE  . MET A 1 478 ? 21.027  9.111   6.298   1.00 117.21 ?  477  MET A CE  1 
ATOM   3461 N  N   . PRO A 1 479 ? 24.512  12.356  7.688   1.00 128.97 ?  478  PRO A N   1 
ATOM   3462 C  CA  . PRO A 1 479 ? 24.715  13.402  8.689   1.00 140.83 ?  478  PRO A CA  1 
ATOM   3463 C  C   . PRO A 1 479 ? 24.930  12.789  10.067  1.00 160.04 ?  478  PRO A C   1 
ATOM   3464 O  O   . PRO A 1 479 ? 24.281  11.795  10.394  1.00 173.94 ?  478  PRO A O   1 
ATOM   3465 C  CB  . PRO A 1 479 ? 23.407  14.199  8.622   1.00 136.05 ?  478  PRO A CB  1 
ATOM   3466 C  CG  . PRO A 1 479 ? 22.406  13.233  8.061   1.00 131.75 ?  478  PRO A CG  1 
ATOM   3467 C  CD  . PRO A 1 479 ? 23.194  12.473  7.044   1.00 122.04 ?  478  PRO A CD  1 
ATOM   3468 N  N   . SER A 1 480 ? 25.837  13.364  10.851  1.00 124.15 ?  479  SER A N   1 
ATOM   3469 C  CA  . SER A 1 480 ? 26.184  12.803  12.153  1.00 129.57 ?  479  SER A CA  1 
ATOM   3470 C  C   . SER A 1 480 ? 24.956  12.735  13.058  1.00 134.74 ?  479  SER A C   1 
ATOM   3471 O  O   . SER A 1 480 ? 24.182  13.690  13.132  1.00 146.27 ?  479  SER A O   1 
ATOM   3472 C  CB  . SER A 1 480 ? 27.290  13.632  12.815  1.00 120.60 ?  479  SER A CB  1 
ATOM   3473 O  OG  . SER A 1 480 ? 27.752  13.028  14.010  1.00 110.28 ?  479  SER A OG  1 
ATOM   3474 N  N   . PRO A 1 481 ? 24.768  11.596  13.743  1.00 117.62 ?  480  PRO A N   1 
ATOM   3475 C  CA  . PRO A 1 481 ? 23.610  11.439  14.628  1.00 115.81 ?  480  PRO A CA  1 
ATOM   3476 C  C   . PRO A 1 481 ? 23.639  12.410  15.809  1.00 115.63 ?  480  PRO A C   1 
ATOM   3477 O  O   . PRO A 1 481 ? 22.585  12.687  16.385  1.00 92.45  ?  480  PRO A O   1 
ATOM   3478 C  CB  . PRO A 1 481 ? 23.729  9.986   15.100  1.00 113.19 ?  480  PRO A CB  1 
ATOM   3479 C  CG  . PRO A 1 481 ? 25.186  9.671   14.975  1.00 103.22 ?  480  PRO A CG  1 
ATOM   3480 C  CD  . PRO A 1 481 ? 25.615  10.391  13.729  1.00 98.26  ?  480  PRO A CD  1 
ATOM   3481 N  N   . PHE A 1 482 ? 24.823  12.924  16.146  1.00 128.73 ?  481  PHE A N   1 
ATOM   3482 C  CA  . PHE A 1 482 ? 24.990  13.816  17.293  1.00 115.04 ?  481  PHE A CA  1 
ATOM   3483 C  C   . PHE A 1 482 ? 25.584  15.168  16.905  1.00 114.23 ?  481  PHE A C   1 
ATOM   3484 O  O   . PHE A 1 482 ? 26.389  15.271  15.980  1.00 121.97 ?  481  PHE A O   1 
ATOM   3485 C  CB  . PHE A 1 482 ? 25.879  13.158  18.353  1.00 99.64  ?  481  PHE A CB  1 
ATOM   3486 C  CG  . PHE A 1 482 ? 27.338  13.076  17.967  1.00 92.14  ?  481  PHE A CG  1 
ATOM   3487 C  CD1 . PHE A 1 482 ? 27.789  12.092  17.102  1.00 105.27 ?  481  PHE A CD1 1 
ATOM   3488 C  CD2 . PHE A 1 482 ? 28.261  13.971  18.484  1.00 80.07  ?  481  PHE A CD2 1 
ATOM   3489 C  CE1 . PHE A 1 482 ? 29.133  12.008  16.756  1.00 103.17 ?  481  PHE A CE1 1 
ATOM   3490 C  CE2 . PHE A 1 482 ? 29.604  13.891  18.139  1.00 83.01  ?  481  PHE A CE2 1 
ATOM   3491 C  CZ  . PHE A 1 482 ? 30.039  12.910  17.276  1.00 88.29  ?  481  PHE A CZ  1 
ATOM   3492 N  N   . SER A 1 483 ? 25.176  16.200  17.631  1.00 119.34 ?  482  SER A N   1 
ATOM   3493 C  CA  . SER A 1 483 ? 25.705  17.547  17.457  1.00 143.25 ?  482  SER A CA  1 
ATOM   3494 C  C   . SER A 1 483 ? 27.132  17.706  17.970  1.00 145.50 ?  482  SER A C   1 
ATOM   3495 O  O   . SER A 1 483 ? 27.530  17.059  18.937  1.00 156.86 ?  482  SER A O   1 
ATOM   3496 C  CB  . SER A 1 483 ? 24.813  18.553  18.179  1.00 174.90 ?  482  SER A CB  1 
ATOM   3497 O  OG  . SER A 1 483 ? 24.856  18.353  19.581  1.00 193.94 ?  482  SER A OG  1 
ATOM   3498 N  N   . VAL A 1 484 ? 27.896  18.579  17.326  1.00 142.51 ?  483  VAL A N   1 
ATOM   3499 C  CA  . VAL A 1 484 ? 29.141  19.049  17.913  1.00 128.29 ?  483  VAL A CA  1 
ATOM   3500 C  C   . VAL A 1 484 ? 28.896  20.466  18.410  1.00 119.27 ?  483  VAL A C   1 
ATOM   3501 O  O   . VAL A 1 484 ? 29.182  21.444  17.720  1.00 117.84 ?  483  VAL A O   1 
ATOM   3502 C  CB  . VAL A 1 484 ? 30.313  19.021  16.921  1.00 116.80 ?  483  VAL A CB  1 
ATOM   3503 C  CG1 . VAL A 1 484 ? 31.583  19.515  17.591  1.00 108.50 ?  483  VAL A CG1 1 
ATOM   3504 C  CG2 . VAL A 1 484 ? 30.513  17.617  16.378  1.00 123.14 ?  483  VAL A CG2 1 
ATOM   3505 N  N   . VAL A 1 485 ? 28.328  20.561  19.605  1.00 119.24 ?  484  VAL A N   1 
ATOM   3506 C  CA  . VAL A 1 485 ? 27.946  21.841  20.185  1.00 125.59 ?  484  VAL A CA  1 
ATOM   3507 C  C   . VAL A 1 485 ? 27.716  21.636  21.687  1.00 127.41 ?  484  VAL A C   1 
ATOM   3508 O  O   . VAL A 1 485 ? 27.609  20.496  22.145  1.00 129.37 ?  484  VAL A O   1 
ATOM   3509 C  CB  . VAL A 1 485 ? 26.673  22.407  19.498  1.00 115.36 ?  484  VAL A CB  1 
ATOM   3510 C  CG1 . VAL A 1 485 ? 25.455  21.591  19.876  1.00 113.92 ?  484  VAL A CG1 1 
ATOM   3511 C  CG2 . VAL A 1 485 ? 26.460  23.876  19.836  1.00 122.12 ?  484  VAL A CG2 1 
ATOM   3512 N  N   . ILE A 1 486 ? 27.663  22.723  22.454  1.00 116.66 ?  485  ILE A N   1 
ATOM   3513 C  CA  . ILE A 1 486 ? 27.290  22.644  23.861  1.00 107.40 ?  485  ILE A CA  1 
ATOM   3514 C  C   . ILE A 1 486 ? 25.885  22.051  23.988  1.00 116.40 ?  485  ILE A C   1 
ATOM   3515 O  O   . ILE A 1 486 ? 24.936  22.534  23.368  1.00 112.58 ?  485  ILE A O   1 
ATOM   3516 C  CB  . ILE A 1 486 ? 27.335  24.029  24.543  1.00 105.33 ?  485  ILE A CB  1 
ATOM   3517 C  CG1 . ILE A 1 486 ? 28.769  24.565  24.579  1.00 104.11 ?  485  ILE A CG1 1 
ATOM   3518 C  CG2 . ILE A 1 486 ? 26.787  23.952  25.956  1.00 109.40 ?  485  ILE A CG2 1 
ATOM   3519 C  CD1 . ILE A 1 486 ? 28.882  26.003  25.064  1.00 93.59  ?  485  ILE A CD1 1 
ATOM   3520 N  N   . GLN A 1 487 ? 25.761  20.993  24.783  1.00 130.58 ?  486  GLN A N   1 
ATOM   3521 C  CA  . GLN A 1 487 ? 24.484  20.313  24.952  1.00 131.89 ?  486  GLN A CA  1 
ATOM   3522 C  C   . GLN A 1 487 ? 24.115  20.255  26.439  1.00 116.36 ?  486  GLN A C   1 
ATOM   3523 O  O   . GLN A 1 487 ? 24.994  20.127  27.293  1.00 91.31  ?  486  GLN A O   1 
ATOM   3524 C  CB  . GLN A 1 487 ? 24.546  18.908  24.335  1.00 147.72 ?  486  GLN A CB  1 
ATOM   3525 C  CG  . GLN A 1 487 ? 23.197  18.220  24.180  1.00 158.72 ?  486  GLN A CG  1 
ATOM   3526 C  CD  . GLN A 1 487 ? 22.948  17.151  25.223  1.00 162.30 ?  486  GLN A CD  1 
ATOM   3527 O  OE1 . GLN A 1 487 ? 23.871  16.460  25.655  1.00 172.61 ?  486  GLN A OE1 1 
ATOM   3528 N  NE2 . GLN A 1 487 ? 21.692  17.007  25.633  1.00 158.83 ?  486  GLN A NE2 1 
ATOM   3529 N  N   . GLU A 1 488 ? 22.824  20.398  26.740  1.00 129.33 ?  487  GLU A N   1 
ATOM   3530 C  CA  . GLU A 1 488 ? 22.309  20.303  28.110  1.00 135.77 ?  487  GLU A CA  1 
ATOM   3531 C  C   . GLU A 1 488 ? 21.303  19.160  28.251  1.00 133.69 ?  487  GLU A C   1 
ATOM   3532 O  O   . GLU A 1 488 ? 20.470  18.953  27.367  1.00 158.29 ?  487  GLU A O   1 
ATOM   3533 C  CB  . GLU A 1 488 ? 21.651  21.621  28.534  1.00 142.31 ?  487  GLU A CB  1 
ATOM   3534 C  CG  . GLU A 1 488 ? 21.500  21.801  30.047  1.00 141.73 ?  487  GLU A CG  1 
ATOM   3535 C  CD  . GLU A 1 488 ? 20.144  22.372  30.443  1.00 135.76 ?  487  GLU A CD  1 
ATOM   3536 O  OE1 . GLU A 1 488 ? 19.514  23.065  29.618  1.00 130.12 ?  487  GLU A OE1 1 
ATOM   3537 O  OE2 . GLU A 1 488 ? 19.714  22.141  31.591  1.00 133.20 ?  487  GLU A OE2 1 
ATOM   3538 N  N   . SER A 1 489 ? 21.372  18.428  29.360  1.00 103.72 ?  488  SER A N   1 
ATOM   3539 C  CA  . SER A 1 489 ? 20.545  17.238  29.540  1.00 124.64 ?  488  SER A CA  1 
ATOM   3540 C  C   . SER A 1 489 ? 19.603  17.405  30.730  1.00 128.45 ?  488  SER A C   1 
ATOM   3541 O  O   . SER A 1 489 ? 19.846  18.240  31.600  1.00 114.95 ?  488  SER A O   1 
ATOM   3542 C  CB  . SER A 1 489 ? 21.422  16.001  29.726  1.00 81.31  ?  488  SER A CB  1 
ATOM   3543 O  OG  . SER A 1 489 ? 20.657  14.811  29.637  1.00 99.07  ?  488  SER A OG  1 
ATOM   3544 N  N   . GLU A 1 490 ? 18.515  16.638  30.760  1.00 140.85 ?  489  GLU A N   1 
ATOM   3545 C  CA  . GLU A 1 490 ? 17.562  16.754  31.862  1.00 144.40 ?  489  GLU A CA  1 
ATOM   3546 C  C   . GLU A 1 490 ? 18.135  16.177  33.156  1.00 137.29 ?  489  GLU A C   1 
ATOM   3547 O  O   . GLU A 1 490 ? 17.812  16.640  34.246  1.00 141.60 ?  489  GLU A O   1 
ATOM   3548 C  CB  . GLU A 1 490 ? 16.240  16.055  31.511  1.00 150.84 ?  489  GLU A CB  1 
ATOM   3549 C  CG  . GLU A 1 490 ? 16.350  14.570  31.181  1.00 157.70 ?  489  GLU A CG  1 
ATOM   3550 C  CD  . GLU A 1 490 ? 16.748  14.306  29.740  1.00 160.88 ?  489  GLU A CD  1 
ATOM   3551 O  OE1 . GLU A 1 490 ? 17.006  15.279  29.002  1.00 156.36 ?  489  GLU A OE1 1 
ATOM   3552 O  OE2 . GLU A 1 490 ? 16.799  13.121  29.345  1.00 172.92 ?  489  GLU A OE2 1 
ATOM   3553 N  N   . LYS A 1 491 ? 18.984  15.163  33.025  1.00 127.06 ?  490  LYS A N   1 
ATOM   3554 C  CA  . LYS A 1 491 ? 19.773  14.656  34.136  1.00 127.36 ?  490  LYS A CA  1 
ATOM   3555 C  C   . LYS A 1 491 ? 21.107  15.372  34.030  1.00 142.00 ?  490  LYS A C   1 
ATOM   3556 O  O   . LYS A 1 491 ? 21.809  15.173  33.050  1.00 149.51 ?  490  LYS A O   1 
ATOM   3557 C  CB  . LYS A 1 491 ? 19.927  13.131  34.071  1.00 136.48 ?  490  LYS A CB  1 
ATOM   3558 C  CG  . LYS A 1 491 ? 20.223  12.578  32.679  1.00 142.43 ?  490  LYS A CG  1 
ATOM   3559 C  CD  . LYS A 1 491 ? 20.620  11.104  32.713  1.00 149.29 ?  490  LYS A CD  1 
ATOM   3560 C  CE  . LYS A 1 491 ? 19.433  10.193  33.011  1.00 151.83 ?  490  LYS A CE  1 
ATOM   3561 N  NZ  . LYS A 1 491 ? 19.800  8.749   32.914  1.00 147.37 ?  490  LYS A NZ  1 
ATOM   3562 N  N   . GLY A 1 492 ? 21.472  16.192  35.014  1.00 150.28 ?  491  GLY A N   1 
ATOM   3563 C  CA  . GLY A 1 492 ? 22.648  17.038  34.865  1.00 139.42 ?  491  GLY A CA  1 
ATOM   3564 C  C   . GLY A 1 492 ? 22.294  17.944  33.702  1.00 119.34 ?  491  GLY A C   1 
ATOM   3565 O  O   . GLY A 1 492 ? 21.478  18.848  33.861  1.00 104.54 ?  491  GLY A O   1 
ATOM   3566 N  N   . SER A 1 493 ? 22.914  17.749  32.541  1.00 117.80 ?  492  SER A N   1 
ATOM   3567 C  CA  . SER A 1 493 ? 24.302  17.331  32.375  1.00 110.76 ?  492  SER A CA  1 
ATOM   3568 C  C   . SER A 1 493 ? 24.879  18.312  31.376  1.00 95.35  ?  492  SER A C   1 
ATOM   3569 O  O   . SER A 1 493 ? 24.162  18.759  30.480  1.00 99.70  ?  492  SER A O   1 
ATOM   3570 C  CB  . SER A 1 493 ? 24.448  15.897  31.858  1.00 131.46 ?  492  SER A CB  1 
ATOM   3571 O  OG  . SER A 1 493 ? 24.089  14.944  32.839  1.00 140.83 ?  492  SER A OG  1 
ATOM   3572 N  N   . TRP A 1 494 ? 26.151  18.657  31.499  1.00 89.31  ?  493  TRP A N   1 
ATOM   3573 C  CA  . TRP A 1 494 ? 26.724  19.608  30.554  1.00 96.11  ?  493  TRP A CA  1 
ATOM   3574 C  C   . TRP A 1 494 ? 27.882  19.017  29.763  1.00 98.85  ?  493  TRP A C   1 
ATOM   3575 O  O   . TRP A 1 494 ? 28.832  18.471  30.329  1.00 114.49 ?  493  TRP A O   1 
ATOM   3576 C  CB  . TRP A 1 494 ? 27.152  20.878  31.283  1.00 96.39  ?  493  TRP A CB  1 
ATOM   3577 C  CG  . TRP A 1 494 ? 25.975  21.717  31.645  1.00 99.61  ?  493  TRP A CG  1 
ATOM   3578 C  CD1 . TRP A 1 494 ? 25.065  21.484  32.639  1.00 109.72 ?  493  TRP A CD1 1 
ATOM   3579 C  CD2 . TRP A 1 494 ? 25.569  22.928  31.004  1.00 89.97  ?  493  TRP A CD2 1 
ATOM   3580 N  NE1 . TRP A 1 494 ? 24.116  22.480  32.652  1.00 99.23  ?  493  TRP A NE1 1 
ATOM   3581 C  CE2 . TRP A 1 494 ? 24.405  23.378  31.659  1.00 95.78  ?  493  TRP A CE2 1 
ATOM   3582 C  CE3 . TRP A 1 494 ? 26.079  23.676  29.941  1.00 71.17  ?  493  TRP A CE3 1 
ATOM   3583 C  CZ2 . TRP A 1 494 ? 23.746  24.545  31.282  1.00 96.18  ?  493  TRP A CZ2 1 
ATOM   3584 C  CZ3 . TRP A 1 494 ? 25.425  24.829  29.571  1.00 76.20  ?  493  TRP A CZ3 1 
ATOM   3585 C  CH2 . TRP A 1 494 ? 24.273  25.255  30.239  1.00 86.49  ?  493  TRP A CH2 1 
ATOM   3586 N  N   . HIS A 1 495 ? 27.784  19.129  28.442  1.00 76.68  ?  494  HIS A N   1 
ATOM   3587 C  CA  . HIS A 1 495 ? 28.808  18.599  27.558  1.00 70.65  ?  494  HIS A CA  1 
ATOM   3588 C  C   . HIS A 1 495 ? 29.394  19.696  26.678  1.00 82.58  ?  494  HIS A C   1 
ATOM   3589 O  O   . HIS A 1 495 ? 28.658  20.455  26.050  1.00 92.84  ?  494  HIS A O   1 
ATOM   3590 C  CB  . HIS A 1 495 ? 28.229  17.476  26.709  1.00 72.18  ?  494  HIS A CB  1 
ATOM   3591 C  CG  . HIS A 1 495 ? 27.919  16.231  27.485  1.00 82.48  ?  494  HIS A CG  1 
ATOM   3592 N  ND1 . HIS A 1 495 ? 26.684  15.991  28.048  1.00 81.76  ?  494  HIS A ND1 1 
ATOM   3593 C  CD2 . HIS A 1 495 ? 28.683  15.153  27.780  1.00 91.44  ?  494  HIS A CD2 1 
ATOM   3594 C  CE1 . HIS A 1 495 ? 26.701  14.820  28.660  1.00 93.62  ?  494  HIS A CE1 1 
ATOM   3595 N  NE2 . HIS A 1 495 ? 27.902  14.291  28.512  1.00 98.32  ?  494  HIS A NE2 1 
ATOM   3596 N  N   . PHE A 1 496 ? 30.720  19.801  26.667  1.00 74.28  ?  495  PHE A N   1 
ATOM   3597 C  CA  . PHE A 1 496 ? 31.388  20.862  25.923  1.00 81.70  ?  495  PHE A CA  1 
ATOM   3598 C  C   . PHE A 1 496 ? 32.421  20.295  24.964  1.00 100.35 ?  495  PHE A C   1 
ATOM   3599 O  O   . PHE A 1 496 ? 33.368  19.649  25.395  1.00 103.73 ?  495  PHE A O   1 
ATOM   3600 C  CB  . PHE A 1 496 ? 32.061  21.855  26.880  1.00 87.84  ?  495  PHE A CB  1 
ATOM   3601 C  CG  . PHE A 1 496 ? 31.147  22.382  27.946  1.00 101.55 ?  495  PHE A CG  1 
ATOM   3602 C  CD1 . PHE A 1 496 ? 31.007  21.710  29.155  1.00 113.63 ?  495  PHE A CD1 1 
ATOM   3603 C  CD2 . PHE A 1 496 ? 30.416  23.541  27.738  1.00 97.48  ?  495  PHE A CD2 1 
ATOM   3604 C  CE1 . PHE A 1 496 ? 30.159  22.187  30.139  1.00 114.85 ?  495  PHE A CE1 1 
ATOM   3605 C  CE2 . PHE A 1 496 ? 29.564  24.022  28.715  1.00 108.93 ?  495  PHE A CE2 1 
ATOM   3606 C  CZ  . PHE A 1 496 ? 29.437  23.343  29.919  1.00 119.57 ?  495  PHE A CZ  1 
ATOM   3607 N  N   . PRO A 1 497 ? 32.242  20.535  23.658  1.00 105.04 ?  496  PRO A N   1 
ATOM   3608 C  CA  . PRO A 1 497 ? 33.266  20.174  22.673  1.00 104.52 ?  496  PRO A CA  1 
ATOM   3609 C  C   . PRO A 1 497 ? 34.408  21.187  22.690  1.00 107.76 ?  496  PRO A C   1 
ATOM   3610 O  O   . PRO A 1 497 ? 34.223  22.281  23.217  1.00 109.13 ?  496  PRO A O   1 
ATOM   3611 C  CB  . PRO A 1 497 ? 32.504  20.214  21.349  1.00 96.76  ?  496  PRO A CB  1 
ATOM   3612 C  CG  . PRO A 1 497 ? 31.429  21.223  21.578  1.00 91.98  ?  496  PRO A CG  1 
ATOM   3613 C  CD  . PRO A 1 497 ? 31.031  21.084  23.022  1.00 97.36  ?  496  PRO A CD  1 
ATOM   3614 N  N   . VAL A 1 498 ? 35.563  20.839  22.135  1.00 116.20 ?  497  VAL A N   1 
ATOM   3615 C  CA  . VAL A 1 498 ? 36.693  21.764  22.142  1.00 129.56 ?  497  VAL A CA  1 
ATOM   3616 C  C   . VAL A 1 498 ? 37.207  22.038  20.723  1.00 138.18 ?  497  VAL A C   1 
ATOM   3617 O  O   . VAL A 1 498 ? 37.166  21.169  19.851  1.00 144.27 ?  497  VAL A O   1 
ATOM   3618 C  CB  . VAL A 1 498 ? 37.847  21.233  23.030  1.00 133.23 ?  497  VAL A CB  1 
ATOM   3619 C  CG1 . VAL A 1 498 ? 38.562  20.075  22.359  1.00 140.49 ?  497  VAL A CG1 1 
ATOM   3620 C  CG2 . VAL A 1 498 ? 38.833  22.346  23.358  1.00 130.60 ?  497  VAL A CG2 1 
ATOM   3621 N  N   . SER A 1 499 ? 37.674  23.264  20.498  1.00 138.54 ?  498  SER A N   1 
ATOM   3622 C  CA  . SER A 1 499 ? 38.220  23.663  19.205  1.00 123.14 ?  498  SER A CA  1 
ATOM   3623 C  C   . SER A 1 499 ? 39.551  22.968  18.930  1.00 109.90 ?  498  SER A C   1 
ATOM   3624 O  O   . SER A 1 499 ? 39.605  21.964  18.218  1.00 106.17 ?  498  SER A O   1 
ATOM   3625 C  CB  . SER A 1 499 ? 38.395  25.183  19.143  1.00 114.77 ?  498  SER A CB  1 
ATOM   3626 O  OG  . SER A 1 499 ? 37.166  25.848  19.387  1.00 116.08 ?  498  SER A OG  1 
ATOM   3627 N  N   . SER A 1 506 ? 37.626  12.600  14.248  1.00 172.69 ?  505  SER A N   1 
ATOM   3628 C  CA  . SER A 1 506 ? 38.479  13.769  14.429  1.00 176.69 ?  505  SER A CA  1 
ATOM   3629 C  C   . SER A 1 506 ? 39.128  13.761  15.808  1.00 190.80 ?  505  SER A C   1 
ATOM   3630 O  O   . SER A 1 506 ? 39.899  14.661  16.149  1.00 191.04 ?  505  SER A O   1 
ATOM   3631 C  CB  . SER A 1 506 ? 37.671  15.055  14.233  1.00 171.79 ?  505  SER A CB  1 
ATOM   3632 O  OG  . SER A 1 506 ? 36.743  15.246  15.288  1.00 163.90 ?  505  SER A OG  1 
ATOM   3633 N  N   . SER A 1 507 ? 38.817  12.720  16.578  1.00 215.14 ?  506  SER A N   1 
ATOM   3634 C  CA  . SER A 1 507 ? 39.272  12.555  17.957  1.00 211.70 ?  506  SER A CA  1 
ATOM   3635 C  C   . SER A 1 507 ? 39.053  13.828  18.767  1.00 208.80 ?  506  SER A C   1 
ATOM   3636 O  O   . SER A 1 507 ? 39.964  14.320  19.433  1.00 221.91 ?  506  SER A O   1 
ATOM   3637 C  CB  . SER A 1 507 ? 40.755  12.171  17.989  1.00 211.30 ?  506  SER A CB  1 
ATOM   3638 O  OG  . SER A 1 507 ? 40.980  10.926  17.353  1.00 211.68 ?  506  SER A OG  1 
ATOM   3639 N  N   . ARG A 1 508 ? 37.831  14.346  18.717  1.00 192.81 ?  507  ARG A N   1 
ATOM   3640 C  CA  . ARG A 1 508 ? 37.495  15.581  19.412  1.00 168.42 ?  507  ARG A CA  1 
ATOM   3641 C  C   . ARG A 1 508 ? 37.437  15.361  20.915  1.00 154.36 ?  507  ARG A C   1 
ATOM   3642 O  O   . ARG A 1 508 ? 37.018  14.300  21.374  1.00 158.78 ?  507  ARG A O   1 
ATOM   3643 C  CB  . ARG A 1 508 ? 36.172  16.137  18.893  1.00 155.96 ?  507  ARG A CB  1 
ATOM   3644 C  CG  . ARG A 1 508 ? 35.802  17.487  19.467  1.00 152.75 ?  507  ARG A CG  1 
ATOM   3645 C  CD  . ARG A 1 508 ? 34.500  17.968  18.883  1.00 154.49 ?  507  ARG A CD  1 
ATOM   3646 N  NE  . ARG A 1 508 ? 34.632  18.216  17.450  1.00 159.23 ?  507  ARG A NE  1 
ATOM   3647 C  CZ  . ARG A 1 508 ? 35.065  19.359  16.928  1.00 167.43 ?  507  ARG A CZ  1 
ATOM   3648 N  NH1 . ARG A 1 508 ? 35.397  20.371  17.719  1.00 164.39 ?  507  ARG A NH1 1 
ATOM   3649 N  NH2 . ARG A 1 508 ? 35.159  19.494  15.612  1.00 177.40 ?  507  ARG A NH2 1 
ATOM   3650 N  N   . THR A 1 509 ? 37.832  16.372  21.681  1.00 135.52 ?  508  THR A N   1 
ATOM   3651 C  CA  . THR A 1 509 ? 37.780  16.277  23.134  1.00 132.72 ?  508  THR A CA  1 
ATOM   3652 C  C   . THR A 1 509 ? 36.562  16.999  23.700  1.00 120.77 ?  508  THR A C   1 
ATOM   3653 O  O   . THR A 1 509 ? 36.236  18.112  23.290  1.00 117.39 ?  508  THR A O   1 
ATOM   3654 C  CB  . THR A 1 509 ? 39.053  16.854  23.781  1.00 135.11 ?  508  THR A CB  1 
ATOM   3655 O  OG1 . THR A 1 509 ? 40.209  16.324  23.122  1.00 137.58 ?  508  THR A OG1 1 
ATOM   3656 C  CG2 . THR A 1 509 ? 39.115  16.503  25.258  1.00 139.07 ?  508  THR A CG2 1 
ATOM   3657 N  N   . TRP A 1 510 ? 35.911  16.365  24.668  1.00 115.01 ?  509  TRP A N   1 
ATOM   3658 C  CA  . TRP A 1 510 ? 34.689  16.902  25.248  1.00 113.14 ?  509  TRP A CA  1 
ATOM   3659 C  C   . TRP A 1 510 ? 34.849  17.068  26.758  1.00 115.85 ?  509  TRP A C   1 
ATOM   3660 O  O   . TRP A 1 510 ? 35.812  16.573  27.346  1.00 124.81 ?  509  TRP A O   1 
ATOM   3661 C  CB  . TRP A 1 510 ? 33.495  15.987  24.948  1.00 112.34 ?  509  TRP A CB  1 
ATOM   3662 C  CG  . TRP A 1 510 ? 32.957  16.047  23.535  1.00 109.20 ?  509  TRP A CG  1 
ATOM   3663 C  CD1 . TRP A 1 510 ? 33.513  15.495  22.415  1.00 112.52 ?  509  TRP A CD1 1 
ATOM   3664 C  CD2 . TRP A 1 510 ? 31.736  16.668  23.109  1.00 98.56  ?  509  TRP A CD2 1 
ATOM   3665 N  NE1 . TRP A 1 510 ? 32.722  15.746  21.319  1.00 103.70 ?  509  TRP A NE1 1 
ATOM   3666 C  CE2 . TRP A 1 510 ? 31.624  16.463  21.719  1.00 98.76  ?  509  TRP A CE2 1 
ATOM   3667 C  CE3 . TRP A 1 510 ? 30.730  17.382  23.768  1.00 90.56  ?  509  TRP A CE3 1 
ATOM   3668 C  CZ2 . TRP A 1 510 ? 30.548  16.949  20.976  1.00 99.75  ?  509  TRP A CZ2 1 
ATOM   3669 C  CZ3 . TRP A 1 510 ? 29.664  17.862  23.031  1.00 89.58  ?  509  TRP A CZ3 1 
ATOM   3670 C  CH2 . TRP A 1 510 ? 29.581  17.645  21.650  1.00 96.07  ?  509  TRP A CH2 1 
ATOM   3671 N  N   . MET A 1 511 ? 33.906  17.773  27.378  1.00 110.23 ?  510  MET A N   1 
ATOM   3672 C  CA  . MET A 1 511 ? 33.833  17.867  28.835  1.00 109.73 ?  510  MET A CA  1 
ATOM   3673 C  C   . MET A 1 511 ? 32.501  17.298  29.311  1.00 89.51  ?  510  MET A C   1 
ATOM   3674 O  O   . MET A 1 511 ? 31.461  17.590  28.735  1.00 91.25  ?  510  MET A O   1 
ATOM   3675 C  CB  . MET A 1 511 ? 33.987  19.319  29.305  1.00 118.90 ?  510  MET A CB  1 
ATOM   3676 C  CG  . MET A 1 511 ? 35.353  19.664  29.890  1.00 121.18 ?  510  MET A CG  1 
ATOM   3677 S  SD  . MET A 1 511 ? 35.351  21.209  30.833  1.00 150.34 ?  510  MET A SD  1 
ATOM   3678 C  CE  . MET A 1 511 ? 34.229  20.804  32.167  1.00 75.36  ?  510  MET A CE  1 
ATOM   3679 N  N   . CYS A 1 512 ? 32.528  16.509  30.376  1.00 76.83  ?  511  CYS A N   1 
ATOM   3680 C  CA  . CYS A 1 512 ? 31.311  15.881  30.873  1.00 98.35  ?  511  CYS A CA  1 
ATOM   3681 C  C   . CYS A 1 512 ? 30.974  16.378  32.270  1.00 110.98 ?  511  CYS A C   1 
ATOM   3682 O  O   . CYS A 1 512 ? 31.847  16.513  33.127  1.00 106.53 ?  511  CYS A O   1 
ATOM   3683 C  CB  . CYS A 1 512 ? 31.452  14.358  30.881  1.00 110.11 ?  511  CYS A CB  1 
ATOM   3684 S  SG  . CYS A 1 512 ? 29.985  13.468  31.460  1.00 180.05 ?  511  CYS A SG  1 
ATOM   3685 N  N   . ILE A 1 513 ? 29.703  16.694  32.480  1.00 115.46 ?  512  ILE A N   1 
ATOM   3686 C  CA  . ILE A 1 513 ? 29.251  17.166  33.776  1.00 118.74 ?  512  ILE A CA  1 
ATOM   3687 C  C   . ILE A 1 513 ? 28.118  16.280  34.301  1.00 137.08 ?  512  ILE A C   1 
ATOM   3688 O  O   . ILE A 1 513 ? 27.080  16.115  33.661  1.00 146.13 ?  512  ILE A O   1 
ATOM   3689 C  CB  . ILE A 1 513 ? 28.835  18.647  33.696  1.00 111.00 ?  512  ILE A CB  1 
ATOM   3690 C  CG1 . ILE A 1 513 ? 30.032  19.529  34.049  1.00 101.20 ?  512  ILE A CG1 1 
ATOM   3691 C  CG2 . ILE A 1 513 ? 27.703  18.956  34.643  1.00 126.55 ?  512  ILE A CG2 1 
ATOM   3692 C  CD1 . ILE A 1 513 ? 31.036  19.667  32.945  1.00 74.06  ?  512  ILE A CD1 1 
ATOM   3693 N  N   . SER A 1 514 ? 28.346  15.693  35.470  1.00 145.32 ?  513  SER A N   1 
ATOM   3694 C  CA  . SER A 1 514 ? 27.414  14.745  36.062  1.00 162.77 ?  513  SER A CA  1 
ATOM   3695 C  C   . SER A 1 514 ? 27.112  15.102  37.512  1.00 171.65 ?  513  SER A C   1 
ATOM   3696 O  O   . SER A 1 514 ? 28.005  15.495  38.261  1.00 182.60 ?  513  SER A O   1 
ATOM   3697 C  CB  . SER A 1 514 ? 27.968  13.320  35.979  1.00 172.05 ?  513  SER A CB  1 
ATOM   3698 O  OG  . SER A 1 514 ? 27.154  12.424  36.715  1.00 180.50 ?  513  SER A OG  1 
ATOM   3699 N  N   . ARG A 1 515 ? 25.849  14.973  37.898  1.00 165.58 ?  514  ARG A N   1 
ATOM   3700 C  CA  . ARG A 1 515 ? 25.458  15.176  39.283  1.00 152.04 ?  514  ARG A CA  1 
ATOM   3701 C  C   . ARG A 1 515 ? 25.041  13.802  39.854  1.00 158.69 ?  514  ARG A C   1 
ATOM   3702 O  O   . ARG A 1 515 ? 25.485  12.772  39.345  1.00 156.69 ?  514  ARG A O   1 
ATOM   3703 C  CB  . ARG A 1 515 ? 24.350  16.244  39.363  1.00 135.09 ?  514  ARG A CB  1 
ATOM   3704 C  CG  . ARG A 1 515 ? 24.008  16.727  40.770  1.00 134.53 ?  514  ARG A CG  1 
ATOM   3705 C  CD  . ARG A 1 515 ? 22.882  17.752  40.827  1.00 130.12 ?  514  ARG A CD  1 
ATOM   3706 N  NE  . ARG A 1 515 ? 23.304  19.109  40.499  1.00 121.47 ?  514  ARG A NE  1 
ATOM   3707 C  CZ  . ARG A 1 515 ? 23.548  20.035  41.421  1.00 120.68 ?  514  ARG A CZ  1 
ATOM   3708 N  NH1 . ARG A 1 515 ? 23.427  19.733  42.705  1.00 136.74 ?  514  ARG A NH1 1 
ATOM   3709 N  NH2 . ARG A 1 515 ? 23.914  21.256  41.071  1.00 109.69 ?  514  ARG A NH2 1 
ATOM   3710 N  N   . GLN A 1 516 ? 24.208  13.782  40.892  1.00 161.08 ?  515  GLN A N   1 
ATOM   3711 C  CA  . GLN A 1 516 ? 23.753  12.547  41.530  1.00 151.11 ?  515  GLN A CA  1 
ATOM   3712 C  C   . GLN A 1 516 ? 22.468  12.774  42.312  1.00 148.21 ?  515  GLN A C   1 
ATOM   3713 O  O   . GLN A 1 516 ? 21.504  12.027  42.152  1.00 149.59 ?  515  GLN A O   1 
ATOM   3714 C  CB  . GLN A 1 516 ? 24.826  11.990  42.474  1.00 148.17 ?  515  GLN A CB  1 
ATOM   3715 C  CG  . GLN A 1 516 ? 25.221  10.535  42.222  1.00 147.65 ?  515  GLN A CG  1 
ATOM   3716 C  CD  . GLN A 1 516 ? 25.858  10.325  40.867  1.00 139.60 ?  515  GLN A CD  1 
ATOM   3717 O  OE1 . GLN A 1 516 ? 25.193  9.918   39.912  1.00 139.43 ?  515  GLN A OE1 1 
ATOM   3718 N  NE2 . GLN A 1 516 ? 27.149  10.623  40.767  1.00 134.04 ?  515  GLN A NE2 1 
ATOM   3719 N  N   . ASN B 1 29  ? -11.233 71.081  61.719  1.00 185.11 ?  28   ASN B N   1 
ATOM   3720 C  CA  . ASN B 1 29  ? -10.209 70.913  60.696  1.00 170.62 ?  28   ASN B CA  1 
ATOM   3721 C  C   . ASN B 1 29  ? -10.833 70.455  59.384  1.00 181.64 ?  28   ASN B C   1 
ATOM   3722 O  O   . ASN B 1 29  ? -11.589 69.486  59.363  1.00 188.39 ?  28   ASN B O   1 
ATOM   3723 C  CB  . ASN B 1 29  ? -9.149  69.911  61.168  1.00 183.58 ?  28   ASN B CB  1 
ATOM   3724 C  CG  . ASN B 1 29  ? -8.003  69.756  60.185  1.00 151.03 ?  28   ASN B CG  1 
ATOM   3725 O  OD1 . ASN B 1 29  ? -7.613  70.707  59.512  1.00 151.77 ?  28   ASN B OD1 1 
ATOM   3726 N  ND2 . ASN B 1 29  ? -7.451  68.551  60.106  1.00 148.09 ?  28   ASN B ND2 1 
ATOM   3727 N  N   . PRO B 1 30  ? -10.534 71.168  58.286  1.00 191.28 ?  29   PRO B N   1 
ATOM   3728 C  CA  . PRO B 1 30  ? -11.074 70.841  56.959  1.00 190.55 ?  29   PRO B CA  1 
ATOM   3729 C  C   . PRO B 1 30  ? -10.672 69.458  56.432  1.00 184.67 ?  29   PRO B C   1 
ATOM   3730 O  O   . PRO B 1 30  ? -11.507 68.790  55.827  1.00 172.19 ?  29   PRO B O   1 
ATOM   3731 C  CB  . PRO B 1 30  ? -10.500 71.948  56.061  1.00 190.72 ?  29   PRO B CB  1 
ATOM   3732 C  CG  . PRO B 1 30  ? -9.410  72.600  56.864  1.00 195.89 ?  29   PRO B CG  1 
ATOM   3733 C  CD  . PRO B 1 30  ? -9.834  72.462  58.286  1.00 196.42 ?  29   PRO B CD  1 
ATOM   3734 N  N   . GLU B 1 31  ? -9.422  69.048  56.635  1.00 186.97 ?  30   GLU B N   1 
ATOM   3735 C  CA  . GLU B 1 31  ? -8.946  67.762  56.122  1.00 190.59 ?  30   GLU B CA  1 
ATOM   3736 C  C   . GLU B 1 31  ? -9.564  66.523  56.785  1.00 205.83 ?  30   GLU B C   1 
ATOM   3737 O  O   . GLU B 1 31  ? -9.899  65.556  56.103  1.00 207.76 ?  30   GLU B O   1 
ATOM   3738 C  CB  . GLU B 1 31  ? -7.423  67.677  56.255  1.00 195.88 ?  30   GLU B CB  1 
ATOM   3739 C  CG  . GLU B 1 31  ? -6.673  68.821  55.612  1.00 204.26 ?  30   GLU B CG  1 
ATOM   3740 C  CD  . GLU B 1 31  ? -5.176  68.715  55.806  1.00 211.62 ?  30   GLU B CD  1 
ATOM   3741 O  OE1 . GLU B 1 31  ? -4.743  67.950  56.693  1.00 218.12 ?  30   GLU B OE1 1 
ATOM   3742 O  OE2 . GLU B 1 31  ? -4.431  69.401  55.075  1.00 211.25 ?  30   GLU B OE2 1 
ATOM   3743 N  N   . THR B 1 32  ? -9.690  66.541  58.110  1.00 216.08 ?  31   THR B N   1 
ATOM   3744 C  CA  . THR B 1 32  ? -10.218 65.387  58.841  1.00 198.34 ?  31   THR B CA  1 
ATOM   3745 C  C   . THR B 1 32  ? -11.729 65.176  58.744  1.00 206.78 ?  31   THR B C   1 
ATOM   3746 O  O   . THR B 1 32  ? -12.195 64.041  58.829  1.00 211.82 ?  31   THR B O   1 
ATOM   3747 C  CB  . THR B 1 32  ? -9.856  65.460  60.337  1.00 196.23 ?  31   THR B CB  1 
ATOM   3748 O  OG1 . THR B 1 32  ? -10.435 66.636  60.913  1.00 200.00 ?  31   THR B OG1 1 
ATOM   3749 C  CG2 . THR B 1 32  ? -8.347  65.491  60.524  1.00 193.95 ?  31   THR B CG2 1 
ATOM   3750 N  N   . ASN B 1 33  ? -12.502 66.249  58.598  1.00 229.20 ?  32   ASN B N   1 
ATOM   3751 C  CA  . ASN B 1 33  ? -13.943 66.083  58.419  1.00 245.41 ?  32   ASN B CA  1 
ATOM   3752 C  C   . ASN B 1 33  ? -14.291 65.508  57.045  1.00 259.63 ?  32   ASN B C   1 
ATOM   3753 O  O   . ASN B 1 33  ? -15.202 64.690  56.927  1.00 281.50 ?  32   ASN B O   1 
ATOM   3754 C  CB  . ASN B 1 33  ? -14.693 67.403  58.653  1.00 245.95 ?  32   ASN B CB  1 
ATOM   3755 C  CG  . ASN B 1 33  ? -14.186 68.537  57.787  1.00 246.01 ?  32   ASN B CG  1 
ATOM   3756 O  OD1 . ASN B 1 33  ? -14.255 68.479  56.560  1.00 244.71 ?  32   ASN B OD1 1 
ATOM   3757 N  ND2 . ASN B 1 33  ? -13.707 69.596  58.427  1.00 247.33 ?  32   ASN B ND2 1 
ATOM   3758 N  N   . LEU B 1 34  ? -13.571 65.932  56.010  1.00 222.29 ?  33   LEU B N   1 
ATOM   3759 C  CA  . LEU B 1 34  ? -13.793 65.390  54.670  1.00 184.73 ?  33   LEU B CA  1 
ATOM   3760 C  C   . LEU B 1 34  ? -13.327 63.936  54.610  1.00 164.62 ?  33   LEU B C   1 
ATOM   3761 O  O   . LEU B 1 34  ? -13.883 63.133  53.866  1.00 169.52 ?  33   LEU B O   1 
ATOM   3762 C  CB  . LEU B 1 34  ? -13.105 66.244  53.598  1.00 168.78 ?  33   LEU B CB  1 
ATOM   3763 C  CG  . LEU B 1 34  ? -11.611 66.157  53.301  1.00 151.36 ?  33   LEU B CG  1 
ATOM   3764 C  CD1 . LEU B 1 34  ? -11.325 65.085  52.265  1.00 121.35 ?  33   LEU B CD1 1 
ATOM   3765 C  CD2 . LEU B 1 34  ? -11.112 67.507  52.816  1.00 163.23 ?  33   LEU B CD2 1 
ATOM   3766 N  N   . LEU B 1 35  ? -12.292 63.608  55.378  1.00 146.32 ?  34   LEU B N   1 
ATOM   3767 C  CA  . LEU B 1 35  ? -11.811 62.231  55.468  1.00 141.28 ?  34   LEU B CA  1 
ATOM   3768 C  C   . LEU B 1 35  ? -12.862 61.354  56.135  1.00 127.57 ?  34   LEU B C   1 
ATOM   3769 O  O   . LEU B 1 35  ? -13.017 60.182  55.803  1.00 124.59 ?  34   LEU B O   1 
ATOM   3770 C  CB  . LEU B 1 35  ? -10.507 62.161  56.257  1.00 159.00 ?  34   LEU B CB  1 
ATOM   3771 C  CG  . LEU B 1 35  ? -9.202  62.218  55.471  1.00 163.10 ?  34   LEU B CG  1 
ATOM   3772 C  CD1 . LEU B 1 35  ? -8.022  62.174  56.433  1.00 168.21 ?  34   LEU B CD1 1 
ATOM   3773 C  CD2 . LEU B 1 35  ? -9.140  61.068  54.480  1.00 151.94 ?  34   LEU B CD2 1 
ATOM   3774 N  N   . PHE B 1 36  ? -13.562 61.937  57.100  1.00 126.45 ?  35   PHE B N   1 
ATOM   3775 C  CA  . PHE B 1 36  ? -14.716 61.311  57.729  1.00 135.50 ?  35   PHE B CA  1 
ATOM   3776 C  C   . PHE B 1 36  ? -15.821 61.167  56.692  1.00 149.29 ?  35   PHE B C   1 
ATOM   3777 O  O   . PHE B 1 36  ? -16.467 60.126  56.593  1.00 154.44 ?  35   PHE B O   1 
ATOM   3778 C  CB  . PHE B 1 36  ? -15.178 62.138  58.931  1.00 139.25 ?  35   PHE B CB  1 
ATOM   3779 C  CG  . PHE B 1 36  ? -16.599 61.884  59.345  1.00 130.11 ?  35   PHE B CG  1 
ATOM   3780 C  CD1 . PHE B 1 36  ? -16.918 60.812  60.155  1.00 131.03 ?  35   PHE B CD1 1 
ATOM   3781 C  CD2 . PHE B 1 36  ? -17.612 62.747  58.952  1.00 131.26 ?  35   PHE B CD2 1 
ATOM   3782 C  CE1 . PHE B 1 36  ? -18.222 60.591  60.544  1.00 138.22 ?  35   PHE B CE1 1 
ATOM   3783 C  CE2 . PHE B 1 36  ? -18.916 62.532  59.338  1.00 133.27 ?  35   PHE B CE2 1 
ATOM   3784 C  CZ  . PHE B 1 36  ? -19.223 61.454  60.136  1.00 137.25 ?  35   PHE B CZ  1 
ATOM   3785 N  N   . ASN B 1 37  ? -16.020 62.230  55.918  1.00 156.07 ?  36   ASN B N   1 
ATOM   3786 C  CA  . ASN B 1 37  ? -17.012 62.251  54.848  1.00 155.23 ?  36   ASN B CA  1 
ATOM   3787 C  C   . ASN B 1 37  ? -16.659 61.278  53.721  1.00 138.92 ?  36   ASN B C   1 
ATOM   3788 O  O   . ASN B 1 37  ? -17.542 60.649  53.137  1.00 133.78 ?  36   ASN B O   1 
ATOM   3789 C  CB  . ASN B 1 37  ? -17.162 63.668  54.291  1.00 164.56 ?  36   ASN B CB  1 
ATOM   3790 C  CG  . ASN B 1 37  ? -18.012 64.560  55.176  1.00 170.76 ?  36   ASN B CG  1 
ATOM   3791 O  OD1 . ASN B 1 37  ? -17.589 65.647  55.571  1.00 178.47 ?  36   ASN B OD1 1 
ATOM   3792 N  ND2 . ASN B 1 37  ? -19.223 64.108  55.485  1.00 168.48 ?  36   ASN B ND2 1 
ATOM   3793 N  N   . LEU B 1 38  ? -15.370 61.176  53.402  1.00 126.09 ?  37   LEU B N   1 
ATOM   3794 C  CA  . LEU B 1 38  ? -14.910 60.219  52.400  1.00 123.67 ?  37   LEU B CA  1 
ATOM   3795 C  C   . LEU B 1 38  ? -15.180 58.791  52.863  1.00 123.95 ?  37   LEU B C   1 
ATOM   3796 O  O   . LEU B 1 38  ? -15.643 57.956  52.087  1.00 112.39 ?  37   LEU B O   1 
ATOM   3797 C  CB  . LEU B 1 38  ? -13.420 60.397  52.100  1.00 106.68 ?  37   LEU B CB  1 
ATOM   3798 C  CG  . LEU B 1 38  ? -13.027 61.483  51.096  1.00 116.14 ?  37   LEU B CG  1 
ATOM   3799 C  CD1 . LEU B 1 38  ? -11.647 61.199  50.509  1.00 107.83 ?  37   LEU B CD1 1 
ATOM   3800 C  CD2 . LEU B 1 38  ? -14.074 61.636  50.001  1.00 105.16 ?  37   LEU B CD2 1 
ATOM   3801 N  N   . ASN B 1 39  ? -14.884 58.516  54.130  1.00 130.02 ?  38   ASN B N   1 
ATOM   3802 C  CA  . ASN B 1 39  ? -15.163 57.210  54.717  1.00 131.00 ?  38   ASN B CA  1 
ATOM   3803 C  C   . ASN B 1 39  ? -16.662 57.005  54.882  1.00 129.59 ?  38   ASN B C   1 
ATOM   3804 O  O   . ASN B 1 39  ? -17.153 55.880  54.826  1.00 135.44 ?  38   ASN B O   1 
ATOM   3805 C  CB  . ASN B 1 39  ? -14.454 57.050  56.063  1.00 144.19 ?  38   ASN B CB  1 
ATOM   3806 C  CG  . ASN B 1 39  ? -12.953 56.894  55.916  1.00 158.44 ?  38   ASN B CG  1 
ATOM   3807 O  OD1 . ASN B 1 39  ? -12.460 55.808  55.615  1.00 145.52 ?  38   ASN B OD1 1 
ATOM   3808 N  ND2 . ASN B 1 39  ? -12.218 57.979  56.133  1.00 182.46 ?  38   ASN B ND2 1 
ATOM   3809 N  N   . SER B 1 40  ? -17.385 58.101  55.095  1.00 127.29 ?  39   SER B N   1 
ATOM   3810 C  CA  . SER B 1 40  ? -18.842 58.059  55.177  1.00 137.08 ?  39   SER B CA  1 
ATOM   3811 C  C   . SER B 1 40  ? -19.434 57.605  53.846  1.00 141.45 ?  39   SER B C   1 
ATOM   3812 O  O   . SER B 1 40  ? -20.441 56.896  53.811  1.00 141.68 ?  39   SER B O   1 
ATOM   3813 C  CB  . SER B 1 40  ? -19.404 59.425  55.575  1.00 149.14 ?  39   SER B CB  1 
ATOM   3814 O  OG  . SER B 1 40  ? -20.779 59.528  55.249  1.00 153.03 ?  39   SER B OG  1 
ATOM   3815 N  N   . CYS B 1 41  ? -18.811 58.032  52.752  1.00 142.73 ?  40   CYS B N   1 
ATOM   3816 C  CA  . CYS B 1 41  ? -19.225 57.597  51.424  1.00 134.94 ?  40   CYS B CA  1 
ATOM   3817 C  C   . CYS B 1 41  ? -18.914 56.126  51.209  1.00 132.05 ?  40   CYS B C   1 
ATOM   3818 O  O   . CYS B 1 41  ? -19.763 55.365  50.754  1.00 135.93 ?  40   CYS B O   1 
ATOM   3819 C  CB  . CYS B 1 41  ? -18.523 58.414  50.336  1.00 134.99 ?  40   CYS B CB  1 
ATOM   3820 S  SG  . CYS B 1 41  ? -19.342 59.939  49.837  1.00 108.09 ?  40   CYS B SG  1 
ATOM   3821 N  N   . SER B 1 42  ? -17.697 55.731  51.573  1.00 132.81 ?  41   SER B N   1 
ATOM   3822 C  CA  . SER B 1 42  ? -17.219 54.373  51.338  1.00 119.22 ?  41   SER B CA  1 
ATOM   3823 C  C   . SER B 1 42  ? -18.045 53.337  52.098  1.00 112.29 ?  41   SER B C   1 
ATOM   3824 O  O   . SER B 1 42  ? -18.303 52.244  51.587  1.00 95.94  ?  41   SER B O   1 
ATOM   3825 C  CB  . SER B 1 42  ? -15.741 54.269  51.723  1.00 116.47 ?  41   SER B CB  1 
ATOM   3826 O  OG  . SER B 1 42  ? -15.220 52.983  51.448  1.00 117.99 ?  41   SER B OG  1 
ATOM   3827 N  N   . LYS B 1 43  ? -18.483 53.697  53.301  1.00 117.48 ?  42   LYS B N   1 
ATOM   3828 C  CA  . LYS B 1 43  ? -19.380 52.843  54.071  1.00 123.29 ?  42   LYS B CA  1 
ATOM   3829 C  C   . LYS B 1 43  ? -20.645 52.586  53.273  1.00 122.14 ?  42   LYS B C   1 
ATOM   3830 O  O   . LYS B 1 43  ? -21.089 51.450  53.133  1.00 115.80 ?  42   LYS B O   1 
ATOM   3831 C  CB  . LYS B 1 43  ? -19.738 53.467  55.423  1.00 135.71 ?  42   LYS B CB  1 
ATOM   3832 C  CG  . LYS B 1 43  ? -18.615 53.522  56.447  1.00 136.80 ?  42   LYS B CG  1 
ATOM   3833 C  CD  . LYS B 1 43  ? -19.163 53.228  57.838  1.00 134.85 ?  42   LYS B CD  1 
ATOM   3834 C  CE  . LYS B 1 43  ? -20.367 54.108  58.159  1.00 127.89 ?  42   LYS B CE  1 
ATOM   3835 N  NZ  . LYS B 1 43  ? -21.131 53.603  59.334  1.00 122.37 ?  42   LYS B NZ  1 
ATOM   3836 N  N   . SER B 1 44  ? -21.227 53.663  52.762  1.00 125.82 ?  43   SER B N   1 
ATOM   3837 C  CA  . SER B 1 44  ? -22.463 53.571  52.004  1.00 131.57 ?  43   SER B CA  1 
ATOM   3838 C  C   . SER B 1 44  ? -22.209 53.470  50.511  1.00 145.86 ?  43   SER B C   1 
ATOM   3839 O  O   . SER B 1 44  ? -23.151 53.480  49.725  1.00 149.76 ?  43   SER B O   1 
ATOM   3840 C  CB  . SER B 1 44  ? -23.361 54.772  52.299  1.00 132.27 ?  43   SER B CB  1 
ATOM   3841 O  OG  . SER B 1 44  ? -24.618 54.624  51.664  1.00 131.15 ?  43   SER B OG  1 
ATOM   3842 N  N   . LYS B 1 45  ? -20.935 53.387  50.134  1.00 158.07 ?  44   LYS B N   1 
ATOM   3843 C  CA  . LYS B 1 45  ? -20.532 53.160  48.745  1.00 174.32 ?  44   LYS B CA  1 
ATOM   3844 C  C   . LYS B 1 45  ? -21.116 54.168  47.762  1.00 182.55 ?  44   LYS B C   1 
ATOM   3845 O  O   . LYS B 1 45  ? -21.484 53.806  46.646  1.00 196.99 ?  44   LYS B O   1 
ATOM   3846 C  CB  . LYS B 1 45  ? -20.919 51.749  48.298  1.00 181.27 ?  44   LYS B CB  1 
ATOM   3847 C  CG  . LYS B 1 45  ? -19.813 50.708  48.445  1.00 189.62 ?  44   LYS B CG  1 
ATOM   3848 C  CD  . LYS B 1 45  ? -20.102 49.468  47.599  1.00 192.99 ?  44   LYS B CD  1 
ATOM   3849 C  CE  . LYS B 1 45  ? -19.143 48.332  47.921  1.00 191.20 ?  44   LYS B CE  1 
ATOM   3850 N  NZ  . LYS B 1 45  ? -19.366 47.767  49.279  1.00 185.73 ?  44   LYS B NZ  1 
ATOM   3851 N  N   . ASP B 1 46  ? -21.204 55.426  48.174  1.00 158.39 ?  45   ASP B N   1 
ATOM   3852 C  CA  . ASP B 1 46  ? -21.671 56.487  47.291  1.00 131.83 ?  45   ASP B CA  1 
ATOM   3853 C  C   . ASP B 1 46  ? -20.483 57.096  46.548  1.00 118.25 ?  45   ASP B C   1 
ATOM   3854 O  O   . ASP B 1 46  ? -19.949 58.119  46.965  1.00 118.97 ?  45   ASP B O   1 
ATOM   3855 C  CB  . ASP B 1 46  ? -22.418 57.558  48.094  1.00 131.10 ?  45   ASP B CB  1 
ATOM   3856 C  CG  . ASP B 1 46  ? -23.154 58.561  47.215  1.00 128.08 ?  45   ASP B CG  1 
ATOM   3857 O  OD1 . ASP B 1 46  ? -22.622 58.954  46.156  1.00 132.57 ?  45   ASP B OD1 1 
ATOM   3858 O  OD2 . ASP B 1 46  ? -24.262 58.987  47.607  1.00 120.80 ?  45   ASP B OD2 1 
ATOM   3859 N  N   . LEU B 1 47  ? -20.087 56.485  45.436  1.00 123.10 ?  46   LEU B N   1 
ATOM   3860 C  CA  . LEU B 1 47  ? -18.933 56.960  44.678  1.00 125.58 ?  46   LEU B CA  1 
ATOM   3861 C  C   . LEU B 1 47  ? -19.199 58.339  44.088  1.00 134.51 ?  46   LEU B C   1 
ATOM   3862 O  O   . LEU B 1 47  ? -18.285 59.154  43.938  1.00 138.42 ?  46   LEU B O   1 
ATOM   3863 C  CB  . LEU B 1 47  ? -18.581 55.981  43.555  1.00 125.97 ?  46   LEU B CB  1 
ATOM   3864 C  CG  . LEU B 1 47  ? -17.384 56.375  42.682  1.00 130.17 ?  46   LEU B CG  1 
ATOM   3865 C  CD1 . LEU B 1 47  ? -16.093 56.401  43.497  1.00 121.65 ?  46   LEU B CD1 1 
ATOM   3866 C  CD2 . LEU B 1 47  ? -17.257 55.478  41.460  1.00 134.20 ?  46   LEU B CD2 1 
ATOM   3867 N  N   . SER B 1 48  ? -20.463 58.595  43.769  1.00 136.39 ?  47   SER B N   1 
ATOM   3868 C  CA  . SER B 1 48  ? -20.873 59.870  43.195  1.00 136.29 ?  47   SER B CA  1 
ATOM   3869 C  C   . SER B 1 48  ? -20.622 61.047  44.146  1.00 135.09 ?  47   SER B C   1 
ATOM   3870 O  O   . SER B 1 48  ? -20.072 62.073  43.742  1.00 128.44 ?  47   SER B O   1 
ATOM   3871 C  CB  . SER B 1 48  ? -22.352 59.809  42.808  1.00 134.84 ?  47   SER B CB  1 
ATOM   3872 O  OG  . SER B 1 48  ? -22.825 61.072  42.379  1.00 144.13 ?  47   SER B OG  1 
ATOM   3873 N  N   . ALA B 1 49  ? -21.017 60.890  45.407  1.00 134.76 ?  48   ALA B N   1 
ATOM   3874 C  CA  . ALA B 1 49  ? -20.802 61.925  46.415  1.00 129.65 ?  48   ALA B CA  1 
ATOM   3875 C  C   . ALA B 1 49  ? -19.328 62.079  46.786  1.00 128.23 ?  48   ALA B C   1 
ATOM   3876 O  O   . ALA B 1 49  ? -18.846 63.196  46.960  1.00 134.15 ?  48   ALA B O   1 
ATOM   3877 C  CB  . ALA B 1 49  ? -21.627 61.637  47.657  1.00 130.76 ?  48   ALA B CB  1 
ATOM   3878 N  N   . ALA B 1 50  ? -18.622 60.958  46.921  1.00 121.50 ?  49   ALA B N   1 
ATOM   3879 C  CA  . ALA B 1 50  ? -17.191 60.977  47.220  1.00 114.80 ?  49   ALA B CA  1 
ATOM   3880 C  C   . ALA B 1 50  ? -16.421 61.706  46.127  1.00 128.31 ?  49   ALA B C   1 
ATOM   3881 O  O   . ALA B 1 50  ? -15.409 62.353  46.390  1.00 137.86 ?  49   ALA B O   1 
ATOM   3882 C  CB  . ALA B 1 50  ? -16.660 59.568  47.386  1.00 98.16  ?  49   ALA B CB  1 
ATOM   3883 N  N   . LEU B 1 51  ? -16.902 61.578  44.896  1.00 126.84 ?  50   LEU B N   1 
ATOM   3884 C  CA  . LEU B 1 51  ? -16.322 62.297  43.775  1.00 122.32 ?  50   LEU B CA  1 
ATOM   3885 C  C   . LEU B 1 51  ? -16.511 63.794  43.975  1.00 125.62 ?  50   LEU B C   1 
ATOM   3886 O  O   . LEU B 1 51  ? -15.579 64.571  43.794  1.00 127.41 ?  50   LEU B O   1 
ATOM   3887 C  CB  . LEU B 1 51  ? -16.957 61.845  42.461  1.00 119.75 ?  50   LEU B CB  1 
ATOM   3888 C  CG  . LEU B 1 51  ? -16.186 60.784  41.676  1.00 116.63 ?  50   LEU B CG  1 
ATOM   3889 C  CD1 . LEU B 1 51  ? -16.609 60.787  40.213  1.00 119.86 ?  50   LEU B CD1 1 
ATOM   3890 C  CD2 . LEU B 1 51  ? -14.680 60.985  41.817  1.00 94.58  ?  50   LEU B CD2 1 
ATOM   3891 N  N   . ALA B 1 52  ? -17.722 64.182  44.370  1.00 130.30 ?  51   ALA B N   1 
ATOM   3892 C  CA  . ALA B 1 52  ? -18.069 65.580  44.618  1.00 123.47 ?  51   ALA B CA  1 
ATOM   3893 C  C   . ALA B 1 52  ? -17.225 66.191  45.742  1.00 135.18 ?  51   ALA B C   1 
ATOM   3894 O  O   . ALA B 1 52  ? -16.834 67.358  45.670  1.00 133.57 ?  51   ALA B O   1 
ATOM   3895 C  CB  . ALA B 1 52  ? -19.554 65.703  44.943  1.00 116.61 ?  51   ALA B CB  1 
ATOM   3896 N  N   . LEU B 1 53  ? -16.975 65.407  46.790  1.00 138.48 ?  52   LEU B N   1 
ATOM   3897 C  CA  . LEU B 1 53  ? -16.100 65.826  47.884  1.00 133.00 ?  52   LEU B CA  1 
ATOM   3898 C  C   . LEU B 1 53  ? -14.683 66.033  47.367  1.00 127.85 ?  52   LEU B C   1 
ATOM   3899 O  O   . LEU B 1 53  ? -14.006 66.996  47.731  1.00 136.66 ?  52   LEU B O   1 
ATOM   3900 C  CB  . LEU B 1 53  ? -16.101 64.788  49.007  1.00 132.85 ?  52   LEU B CB  1 
ATOM   3901 C  CG  . LEU B 1 53  ? -17.458 64.407  49.600  1.00 137.08 ?  52   LEU B CG  1 
ATOM   3902 C  CD1 . LEU B 1 53  ? -17.280 63.521  50.817  1.00 128.51 ?  52   LEU B CD1 1 
ATOM   3903 C  CD2 . LEU B 1 53  ? -18.252 65.654  49.952  1.00 145.04 ?  52   LEU B CD2 1 
ATOM   3904 N  N   . TYR B 1 54  ? -14.246 65.101  46.526  1.00 116.86 ?  53   TYR B N   1 
ATOM   3905 C  CA  . TYR B 1 54  ? -12.955 65.170  45.857  1.00 114.40 ?  53   TYR B CA  1 
ATOM   3906 C  C   . TYR B 1 54  ? -12.933 66.384  44.940  1.00 123.94 ?  53   TYR B C   1 
ATOM   3907 O  O   . TYR B 1 54  ? -11.949 67.120  44.883  1.00 127.78 ?  53   TYR B O   1 
ATOM   3908 C  CB  . TYR B 1 54  ? -12.706 63.891  45.064  1.00 114.74 ?  53   TYR B CB  1 
ATOM   3909 C  CG  . TYR B 1 54  ? -11.464 63.886  44.203  1.00 113.05 ?  53   TYR B CG  1 
ATOM   3910 C  CD1 . TYR B 1 54  ? -10.199 63.846  44.778  1.00 105.72 ?  53   TYR B CD1 1 
ATOM   3911 C  CD2 . TYR B 1 54  ? -11.555 63.896  42.817  1.00 114.36 ?  53   TYR B CD2 1 
ATOM   3912 C  CE1 . TYR B 1 54  ? -9.060  63.823  43.998  1.00 114.85 ?  53   TYR B CE1 1 
ATOM   3913 C  CE2 . TYR B 1 54  ? -10.420 63.876  42.027  1.00 124.84 ?  53   TYR B CE2 1 
ATOM   3914 C  CZ  . TYR B 1 54  ? -9.176  63.840  42.622  1.00 131.28 ?  53   TYR B CZ  1 
ATOM   3915 O  OH  . TYR B 1 54  ? -8.044  63.821  41.838  1.00 145.65 ?  53   TYR B OH  1 
ATOM   3916 N  N   . ASP B 1 55  ? -14.036 66.579  44.221  1.00 125.03 ?  54   ASP B N   1 
ATOM   3917 C  CA  . ASP B 1 55  ? -14.191 67.731  43.339  1.00 127.30 ?  54   ASP B CA  1 
ATOM   3918 C  C   . ASP B 1 55  ? -14.134 69.028  44.140  1.00 121.38 ?  54   ASP B C   1 
ATOM   3919 O  O   . ASP B 1 55  ? -13.533 70.003  43.700  1.00 119.52 ?  54   ASP B O   1 
ATOM   3920 C  CB  . ASP B 1 55  ? -15.506 67.653  42.552  1.00 140.17 ?  54   ASP B CB  1 
ATOM   3921 C  CG  . ASP B 1 55  ? -15.551 66.469  41.598  1.00 135.98 ?  54   ASP B CG  1 
ATOM   3922 O  OD1 . ASP B 1 55  ? -14.535 66.211  40.919  1.00 138.18 ?  54   ASP B OD1 1 
ATOM   3923 O  OD2 . ASP B 1 55  ? -16.608 65.805  41.513  1.00 121.71 ?  54   ASP B OD2 1 
ATOM   3924 N  N   . ALA B 1 56  ? -14.768 69.042  45.310  1.00 129.60 ?  55   ALA B N   1 
ATOM   3925 C  CA  . ALA B 1 56  ? -14.722 70.214  46.178  1.00 137.10 ?  55   ALA B CA  1 
ATOM   3926 C  C   . ALA B 1 56  ? -13.308 70.449  46.706  1.00 150.59 ?  55   ALA B C   1 
ATOM   3927 O  O   . ALA B 1 56  ? -12.853 71.588  46.812  1.00 157.19 ?  55   ALA B O   1 
ATOM   3928 C  CB  . ALA B 1 56  ? -15.699 70.058  47.335  1.00 134.68 ?  55   ALA B CB  1 
ATOM   3929 N  N   . ALA B 1 57  ? -12.621 69.364  47.051  1.00 156.92 ?  56   ALA B N   1 
ATOM   3930 C  CA  . ALA B 1 57  ? -11.271 69.457  47.598  1.00 163.22 ?  56   ALA B CA  1 
ATOM   3931 C  C   . ALA B 1 57  ? -10.246 69.870  46.540  1.00 162.79 ?  56   ALA B C   1 
ATOM   3932 O  O   . ALA B 1 57  ? -9.378  70.707  46.786  1.00 159.79 ?  56   ALA B O   1 
ATOM   3933 C  CB  . ALA B 1 57  ? -10.869 68.131  48.226  1.00 162.77 ?  56   ALA B CB  1 
ATOM   3934 N  N   . ILE B 1 58  ? -10.364 69.276  45.358  1.00 166.23 ?  57   ILE B N   1 
ATOM   3935 C  CA  . ILE B 1 58  ? -9.425  69.522  44.266  1.00 164.92 ?  57   ILE B CA  1 
ATOM   3936 C  C   . ILE B 1 58  ? -9.494  70.960  43.745  1.00 160.20 ?  57   ILE B C   1 
ATOM   3937 O  O   . ILE B 1 58  ? -8.489  71.500  43.277  1.00 159.04 ?  57   ILE B O   1 
ATOM   3938 C  CB  . ILE B 1 58  ? -9.652  68.525  43.091  1.00 151.97 ?  57   ILE B CB  1 
ATOM   3939 C  CG1 . ILE B 1 58  ? -8.439  68.488  42.164  1.00 149.68 ?  57   ILE B CG1 1 
ATOM   3940 C  CG2 . ILE B 1 58  ? -10.918 68.842  42.309  1.00 149.18 ?  57   ILE B CG2 1 
ATOM   3941 C  CD1 . ILE B 1 58  ? -7.171  68.095  42.867  1.00 144.85 ?  57   ILE B CD1 1 
ATOM   3942 N  N   . THR B 1 59  ? -10.668 71.580  43.833  1.00 158.02 ?  58   THR B N   1 
ATOM   3943 C  CA  . THR B 1 59  ? -10.825 72.963  43.395  1.00 153.07 ?  58   THR B CA  1 
ATOM   3944 C  C   . THR B 1 59  ? -10.388 73.970  44.459  1.00 167.08 ?  58   THR B C   1 
ATOM   3945 O  O   . THR B 1 59  ? -9.918  75.055  44.119  1.00 167.77 ?  58   THR B O   1 
ATOM   3946 C  CB  . THR B 1 59  ? -12.284 73.265  42.971  1.00 150.06 ?  58   THR B CB  1 
ATOM   3947 O  OG1 . THR B 1 59  ? -12.358 74.586  42.422  1.00 159.77 ?  58   THR B OG1 1 
ATOM   3948 C  CG2 . THR B 1 59  ? -13.234 73.162  44.149  1.00 126.11 ?  58   THR B CG2 1 
ATOM   3949 N  N   . SER B 1 60  ? -10.540 73.617  45.735  1.00 180.32 ?  59   SER B N   1 
ATOM   3950 C  CA  . SER B 1 60  ? -10.399 74.585  46.822  1.00 176.31 ?  59   SER B CA  1 
ATOM   3951 C  C   . SER B 1 60  ? -8.961  75.082  46.892  1.00 215.41 ?  59   SER B C   1 
ATOM   3952 O  O   . SER B 1 60  ? -8.721  76.281  47.042  1.00 219.35 ?  59   SER B O   1 
ATOM   3953 C  CB  . SER B 1 60  ? -10.813 73.983  48.165  1.00 172.16 ?  59   SER B CB  1 
ATOM   3954 O  OG  . SER B 1 60  ? -9.719  73.340  48.792  1.00 133.27 ?  59   SER B OG  1 
ATOM   3955 N  N   . SER B 1 61  ? -8.027  74.133  46.829  1.00 258.10 ?  60   SER B N   1 
ATOM   3956 C  CA  . SER B 1 61  ? -6.585  74.370  46.959  1.00 278.72 ?  60   SER B CA  1 
ATOM   3957 C  C   . SER B 1 61  ? -6.155  74.715  48.382  1.00 282.57 ?  60   SER B C   1 
ATOM   3958 O  O   . SER B 1 61  ? -4.979  74.605  48.714  1.00 301.33 ?  60   SER B O   1 
ATOM   3959 C  CB  . SER B 1 61  ? -6.115  75.465  45.997  1.00 296.27 ?  60   SER B CB  1 
ATOM   3960 O  OG  . SER B 1 61  ? -4.711  75.641  46.069  1.00 310.88 ?  60   SER B OG  1 
ATOM   3961 N  N   . GLU B 1 62  ? -7.089  75.157  49.214  1.00 252.05 ?  61   GLU B N   1 
ATOM   3962 C  CA  . GLU B 1 62  ? -6.748  75.490  50.589  1.00 224.95 ?  61   GLU B CA  1 
ATOM   3963 C  C   . GLU B 1 62  ? -6.349  74.239  51.359  1.00 213.13 ?  61   GLU B C   1 
ATOM   3964 O  O   . GLU B 1 62  ? -5.468  74.288  52.216  1.00 211.56 ?  61   GLU B O   1 
ATOM   3965 C  CB  . GLU B 1 62  ? -7.911  76.179  51.287  1.00 212.57 ?  61   GLU B CB  1 
ATOM   3966 C  CG  . GLU B 1 62  ? -8.238  77.549  50.729  1.00 207.47 ?  61   GLU B CG  1 
ATOM   3967 C  CD  . GLU B 1 62  ? -9.271  78.267  51.564  1.00 203.61 ?  61   GLU B CD  1 
ATOM   3968 O  OE1 . GLU B 1 62  ? -9.824  77.634  52.486  1.00 198.61 ?  61   GLU B OE1 1 
ATOM   3969 O  OE2 . GLU B 1 62  ? -9.525  79.461  51.304  1.00 207.85 ?  61   GLU B OE2 1 
ATOM   3970 N  N   . VAL B 1 63  ? -7.009  73.123  51.056  1.00 201.14 ?  62   VAL B N   1 
ATOM   3971 C  CA  . VAL B 1 63  ? -6.714  71.846  51.702  1.00 192.49 ?  62   VAL B CA  1 
ATOM   3972 C  C   . VAL B 1 63  ? -5.636  71.048  50.954  1.00 188.37 ?  62   VAL B C   1 
ATOM   3973 O  O   . VAL B 1 63  ? -5.622  71.014  49.723  1.00 184.18 ?  62   VAL B O   1 
ATOM   3974 C  CB  . VAL B 1 63  ? -8.003  71.001  51.830  1.00 172.27 ?  62   VAL B CB  1 
ATOM   3975 C  CG1 . VAL B 1 63  ? -8.710  70.883  50.485  1.00 166.49 ?  62   VAL B CG1 1 
ATOM   3976 C  CG2 . VAL B 1 63  ? -7.701  69.628  52.387  1.00 163.73 ?  62   VAL B CG2 1 
ATOM   3977 N  N   . ARG B 1 64  ? -4.750  70.393  51.706  1.00 183.96 ?  63   ARG B N   1 
ATOM   3978 C  CA  . ARG B 1 64  ? -3.856  69.382  51.142  1.00 176.89 ?  63   ARG B CA  1 
ATOM   3979 C  C   . ARG B 1 64  ? -4.415  67.995  51.374  1.00 176.75 ?  63   ARG B C   1 
ATOM   3980 O  O   . ARG B 1 64  ? -4.856  67.673  52.481  1.00 184.12 ?  63   ARG B O   1 
ATOM   3981 C  CB  . ARG B 1 64  ? -2.448  69.455  51.739  1.00 177.40 ?  63   ARG B CB  1 
ATOM   3982 C  CG  . ARG B 1 64  ? -1.474  70.345  50.986  1.00 183.78 ?  63   ARG B CG  1 
ATOM   3983 C  CD  . ARG B 1 64  ? -0.072  70.295  51.591  1.00 196.89 ?  63   ARG B CD  1 
ATOM   3984 N  NE  . ARG B 1 64  ? 0.059   71.134  52.780  1.00 209.79 ?  63   ARG B NE  1 
ATOM   3985 C  CZ  . ARG B 1 64  ? 1.110   71.908  53.040  1.00 214.03 ?  63   ARG B CZ  1 
ATOM   3986 N  NH1 . ARG B 1 64  ? 2.131   71.959  52.195  1.00 213.88 ?  63   ARG B NH1 1 
ATOM   3987 N  NH2 . ARG B 1 64  ? 1.140   72.638  54.146  1.00 217.19 ?  63   ARG B NH2 1 
ATOM   3988 N  N   . LEU B 1 65  ? -4.380  67.170  50.331  1.00 166.67 ?  64   LEU B N   1 
ATOM   3989 C  CA  . LEU B 1 65  ? -5.006  65.862  50.397  1.00 147.59 ?  64   LEU B CA  1 
ATOM   3990 C  C   . LEU B 1 65  ? -3.951  64.818  50.760  1.00 139.76 ?  64   LEU B C   1 
ATOM   3991 O  O   . LEU B 1 65  ? -2.969  64.625  50.043  1.00 131.30 ?  64   LEU B O   1 
ATOM   3992 C  CB  . LEU B 1 65  ? -5.663  65.520  49.056  1.00 134.71 ?  64   LEU B CB  1 
ATOM   3993 C  CG  . LEU B 1 65  ? -6.895  66.317  48.609  1.00 127.84 ?  64   LEU B CG  1 
ATOM   3994 C  CD1 . LEU B 1 65  ? -7.421  65.813  47.272  1.00 112.55 ?  64   LEU B CD1 1 
ATOM   3995 C  CD2 . LEU B 1 65  ? -7.987  66.276  49.663  1.00 138.36 ?  64   LEU B CD2 1 
ATOM   3996 N  N   . SER B 1 66  ? -4.174  64.146  51.885  1.00 139.10 ?  65   SER B N   1 
ATOM   3997 C  CA  . SER B 1 66  ? -3.244  63.153  52.410  1.00 137.34 ?  65   SER B CA  1 
ATOM   3998 C  C   . SER B 1 66  ? -3.423  61.826  51.694  1.00 128.64 ?  65   SER B C   1 
ATOM   3999 O  O   . SER B 1 66  ? -4.426  61.610  51.013  1.00 111.80 ?  65   SER B O   1 
ATOM   4000 C  CB  . SER B 1 66  ? -3.432  62.970  53.917  1.00 138.53 ?  65   SER B CB  1 
ATOM   4001 O  OG  . SER B 1 66  ? -2.415  62.151  54.470  1.00 133.93 ?  65   SER B OG  1 
ATOM   4002 N  N   . GLN B 1 67  ? -2.434  60.948  51.824  1.00 126.16 ?  66   GLN B N   1 
ATOM   4003 C  CA  . GLN B 1 67  ? -2.495  59.633  51.201  1.00 124.65 ?  66   GLN B CA  1 
ATOM   4004 C  C   . GLN B 1 67  ? -3.750  58.904  51.677  1.00 132.37 ?  66   GLN B C   1 
ATOM   4005 O  O   . GLN B 1 67  ? -4.317  58.099  50.946  1.00 132.39 ?  66   GLN B O   1 
ATOM   4006 C  CB  . GLN B 1 67  ? -1.239  58.814  51.523  1.00 128.04 ?  66   GLN B CB  1 
ATOM   4007 C  CG  . GLN B 1 67  ? -0.943  58.632  53.010  1.00 147.34 ?  66   GLN B CG  1 
ATOM   4008 C  CD  . GLN B 1 67  ? -0.141  59.785  53.609  1.00 177.06 ?  66   GLN B CD  1 
ATOM   4009 O  OE1 . GLN B 1 67  ? -0.275  60.938  53.194  1.00 191.79 ?  66   GLN B OE1 1 
ATOM   4010 N  NE2 . GLN B 1 67  ? 0.701   59.472  54.589  1.00 183.35 ?  66   GLN B NE2 1 
ATOM   4011 N  N   . GLN B 1 68  ? -4.188  59.216  52.896  1.00 139.35 ?  67   GLN B N   1 
ATOM   4012 C  CA  . GLN B 1 68  ? -5.414  58.656  53.457  1.00 145.99 ?  67   GLN B CA  1 
ATOM   4013 C  C   . GLN B 1 68  ? -6.611  58.953  52.555  1.00 142.95 ?  67   GLN B C   1 
ATOM   4014 O  O   . GLN B 1 68  ? -7.472  58.098  52.338  1.00 137.03 ?  67   GLN B O   1 
ATOM   4015 C  CB  . GLN B 1 68  ? -5.666  59.233  54.853  1.00 159.55 ?  67   GLN B CB  1 
ATOM   4016 C  CG  . GLN B 1 68  ? -4.803  58.640  55.957  1.00 165.47 ?  67   GLN B CG  1 
ATOM   4017 C  CD  . GLN B 1 68  ? -4.900  57.135  56.032  1.00 165.74 ?  67   GLN B CD  1 
ATOM   4018 O  OE1 . GLN B 1 68  ? -5.967  56.558  55.826  1.00 164.96 ?  67   GLN B OE1 1 
ATOM   4019 N  NE2 . GLN B 1 68  ? -3.780  56.487  56.326  1.00 172.04 ?  67   GLN B NE2 1 
ATOM   4020 N  N   . HIS B 1 69  ? -6.643  60.176  52.032  1.00 142.17 ?  68   HIS B N   1 
ATOM   4021 C  CA  . HIS B 1 69  ? -7.714  60.646  51.156  1.00 133.08 ?  68   HIS B CA  1 
ATOM   4022 C  C   . HIS B 1 69  ? -7.833  59.827  49.883  1.00 127.80 ?  68   HIS B C   1 
ATOM   4023 O  O   . HIS B 1 69  ? -8.911  59.348  49.537  1.00 128.74 ?  68   HIS B O   1 
ATOM   4024 C  CB  . HIS B 1 69  ? -7.506  62.114  50.782  1.00 136.27 ?  68   HIS B CB  1 
ATOM   4025 C  CG  . HIS B 1 69  ? -7.422  63.038  51.956  1.00 140.00 ?  68   HIS B CG  1 
ATOM   4026 N  ND1 . HIS B 1 69  ? -6.498  62.885  52.967  1.00 144.82 ?  68   HIS B ND1 1 
ATOM   4027 C  CD2 . HIS B 1 69  ? -8.145  64.137  52.272  1.00 142.57 ?  68   HIS B CD2 1 
ATOM   4028 C  CE1 . HIS B 1 69  ? -6.655  63.852  53.853  1.00 153.13 ?  68   HIS B CE1 1 
ATOM   4029 N  NE2 . HIS B 1 69  ? -7.651  64.623  53.457  1.00 154.10 ?  68   HIS B NE2 1 
ATOM   4030 N  N   . PHE B 1 70  ? -6.714  59.697  49.177  1.00 129.51 ?  69   PHE B N   1 
ATOM   4031 C  CA  . PHE B 1 70  ? -6.696  59.035  47.880  1.00 123.67 ?  69   PHE B CA  1 
ATOM   4032 C  C   . PHE B 1 70  ? -6.902  57.528  47.972  1.00 124.84 ?  69   PHE B C   1 
ATOM   4033 O  O   . PHE B 1 70  ? -7.443  56.916  47.051  1.00 125.67 ?  69   PHE B O   1 
ATOM   4034 C  CB  . PHE B 1 70  ? -5.368  59.309  47.179  1.00 121.30 ?  69   PHE B CB  1 
ATOM   4035 C  CG  . PHE B 1 70  ? -5.121  60.760  46.880  1.00 128.48 ?  69   PHE B CG  1 
ATOM   4036 C  CD1 . PHE B 1 70  ? -5.675  61.358  45.762  1.00 134.94 ?  69   PHE B CD1 1 
ATOM   4037 C  CD2 . PHE B 1 70  ? -4.309  61.518  47.705  1.00 136.48 ?  69   PHE B CD2 1 
ATOM   4038 C  CE1 . PHE B 1 70  ? -5.438  62.693  45.479  1.00 145.28 ?  69   PHE B CE1 1 
ATOM   4039 C  CE2 . PHE B 1 70  ? -4.066  62.850  47.427  1.00 138.54 ?  69   PHE B CE2 1 
ATOM   4040 C  CZ  . PHE B 1 70  ? -4.632  63.439  46.313  1.00 144.69 ?  69   PHE B CZ  1 
ATOM   4041 N  N   . GLN B 1 71  ? -6.478  56.934  49.084  1.00 125.12 ?  70   GLN B N   1 
ATOM   4042 C  CA  . GLN B 1 71  ? -6.711  55.513  49.323  1.00 113.08 ?  70   GLN B CA  1 
ATOM   4043 C  C   . GLN B 1 71  ? -8.194  55.204  49.458  1.00 93.47  ?  70   GLN B C   1 
ATOM   4044 O  O   . GLN B 1 71  ? -8.706  54.305  48.801  1.00 90.69  ?  70   GLN B O   1 
ATOM   4045 C  CB  . GLN B 1 71  ? -5.962  55.043  50.568  1.00 123.50 ?  70   GLN B CB  1 
ATOM   4046 C  CG  . GLN B 1 71  ? -4.452  55.091  50.434  1.00 118.73 ?  70   GLN B CG  1 
ATOM   4047 C  CD  . GLN B 1 71  ? -3.755  55.095  51.779  1.00 124.50 ?  70   GLN B CD  1 
ATOM   4048 O  OE1 . GLN B 1 71  ? -4.383  54.888  52.818  1.00 125.71 ?  70   GLN B OE1 1 
ATOM   4049 N  NE2 . GLN B 1 71  ? -2.452  55.341  51.767  1.00 133.28 ?  70   GLN B NE2 1 
ATOM   4050 N  N   . THR B 1 72  ? -8.875  55.958  50.315  1.00 95.89  ?  71   THR B N   1 
ATOM   4051 C  CA  . THR B 1 72  ? -10.302 55.767  50.555  1.00 99.05  ?  71   THR B CA  1 
ATOM   4052 C  C   . THR B 1 72  ? -11.083 55.863  49.251  1.00 93.23  ?  71   THR B C   1 
ATOM   4053 O  O   . THR B 1 72  ? -12.019 55.100  49.018  1.00 104.83 ?  71   THR B O   1 
ATOM   4054 C  CB  . THR B 1 72  ? -10.848 56.807  51.556  1.00 108.15 ?  71   THR B CB  1 
ATOM   4055 O  OG1 . THR B 1 72  ? -10.204 56.636  52.823  1.00 108.16 ?  71   THR B OG1 1 
ATOM   4056 C  CG2 . THR B 1 72  ? -12.350 56.653  51.733  1.00 115.22 ?  71   THR B CG2 1 
ATOM   4057 N  N   . LEU B 1 73  ? -10.679 56.801  48.402  1.00 105.42 ?  72   LEU B N   1 
ATOM   4058 C  CA  . LEU B 1 73  ? -11.316 57.010  47.109  1.00 113.04 ?  72   LEU B CA  1 
ATOM   4059 C  C   . LEU B 1 73  ? -11.019 55.885  46.126  1.00 123.91 ?  72   LEU B C   1 
ATOM   4060 O  O   . LEU B 1 73  ? -11.932 55.349  45.499  1.00 133.43 ?  72   LEU B O   1 
ATOM   4061 C  CB  . LEU B 1 73  ? -10.880 58.350  46.522  1.00 110.58 ?  72   LEU B CB  1 
ATOM   4062 C  CG  . LEU B 1 73  ? -12.033 59.267  46.126  1.00 111.00 ?  72   LEU B CG  1 
ATOM   4063 C  CD1 . LEU B 1 73  ? -13.027 59.392  47.259  1.00 101.95 ?  72   LEU B CD1 1 
ATOM   4064 C  CD2 . LEU B 1 73  ? -11.476 60.624  45.771  1.00 127.80 ?  72   LEU B CD2 1 
ATOM   4065 N  N   . LEU B 1 74  ? -9.743  55.530  45.999  1.00 120.79 ?  73   LEU B N   1 
ATOM   4066 C  CA  . LEU B 1 74  ? -9.334  54.462  45.092  1.00 111.58 ?  73   LEU B CA  1 
ATOM   4067 C  C   . LEU B 1 74  ? -9.960  53.125  45.486  1.00 110.19 ?  73   LEU B C   1 
ATOM   4068 O  O   . LEU B 1 74  ? -10.357 52.337  44.627  1.00 99.25  ?  73   LEU B O   1 
ATOM   4069 C  CB  . LEU B 1 74  ? -7.810  54.327  45.066  1.00 96.41  ?  73   LEU B CB  1 
ATOM   4070 C  CG  . LEU B 1 74  ? -7.048  55.232  44.101  1.00 97.94  ?  73   LEU B CG  1 
ATOM   4071 C  CD1 . LEU B 1 74  ? -5.594  54.801  44.005  1.00 101.00 ?  73   LEU B CD1 1 
ATOM   4072 C  CD2 . LEU B 1 74  ? -7.703  55.218  42.732  1.00 108.03 ?  73   LEU B CD2 1 
ATOM   4073 N  N   . TYR B 1 75  ? -10.058 52.881  46.788  1.00 120.34 ?  74   TYR B N   1 
ATOM   4074 C  CA  . TYR B 1 75  ? -10.671 51.661  47.284  1.00 115.64 ?  74   TYR B CA  1 
ATOM   4075 C  C   . TYR B 1 75  ? -12.139 51.659  46.875  1.00 123.01 ?  74   TYR B C   1 
ATOM   4076 O  O   . TYR B 1 75  ? -12.685 50.625  46.482  1.00 138.90 ?  74   TYR B O   1 
ATOM   4077 C  CB  . TYR B 1 75  ? -10.529 51.542  48.808  1.00 109.51 ?  74   TYR B CB  1 
ATOM   4078 C  CG  . TYR B 1 75  ? -9.100  51.466  49.318  1.00 114.83 ?  74   TYR B CG  1 
ATOM   4079 C  CD1 . TYR B 1 75  ? -8.031  51.283  48.447  1.00 112.50 ?  74   TYR B CD1 1 
ATOM   4080 C  CD2 . TYR B 1 75  ? -8.821  51.597  50.674  1.00 125.03 ?  74   TYR B CD2 1 
ATOM   4081 C  CE1 . TYR B 1 75  ? -6.726  51.226  48.913  1.00 116.79 ?  74   TYR B CE1 1 
ATOM   4082 C  CE2 . TYR B 1 75  ? -7.518  51.538  51.150  1.00 123.32 ?  74   TYR B CE2 1 
ATOM   4083 C  CZ  . TYR B 1 75  ? -6.477  51.353  50.264  1.00 119.99 ?  74   TYR B CZ  1 
ATOM   4084 O  OH  . TYR B 1 75  ? -5.184  51.295  50.732  1.00 115.30 ?  74   TYR B OH  1 
ATOM   4085 N  N   . LEU B 1 76  ? -12.762 52.832  46.940  1.00 105.09 ?  75   LEU B N   1 
ATOM   4086 C  CA  . LEU B 1 76  ? -14.154 52.984  46.541  1.00 96.99  ?  75   LEU B CA  1 
ATOM   4087 C  C   . LEU B 1 76  ? -14.318 52.757  45.044  1.00 114.37 ?  75   LEU B C   1 
ATOM   4088 O  O   . LEU B 1 76  ? -15.355 52.279  44.587  1.00 123.47 ?  75   LEU B O   1 
ATOM   4089 C  CB  . LEU B 1 76  ? -14.674 54.369  46.927  1.00 89.50  ?  75   LEU B CB  1 
ATOM   4090 C  CG  . LEU B 1 76  ? -16.195 54.519  46.953  1.00 96.72  ?  75   LEU B CG  1 
ATOM   4091 C  CD1 . LEU B 1 76  ? -16.817 53.390  47.758  1.00 105.08 ?  75   LEU B CD1 1 
ATOM   4092 C  CD2 . LEU B 1 76  ? -16.597 55.868  47.525  1.00 92.11  ?  75   LEU B CD2 1 
ATOM   4093 N  N   . CYS B 1 77  ? -13.286 53.111  44.286  1.00 114.59 ?  76   CYS B N   1 
ATOM   4094 C  CA  . CYS B 1 77  ? -13.292 52.939  42.838  1.00 106.62 ?  76   CYS B CA  1 
ATOM   4095 C  C   . CYS B 1 77  ? -13.333 51.462  42.428  1.00 98.70  ?  76   CYS B C   1 
ATOM   4096 O  O   . CYS B 1 77  ? -14.059 51.084  41.506  1.00 85.86  ?  76   CYS B O   1 
ATOM   4097 C  CB  . CYS B 1 77  ? -12.071 53.630  42.232  1.00 107.00 ?  76   CYS B CB  1 
ATOM   4098 S  SG  . CYS B 1 77  ? -12.201 55.439  42.198  1.00 90.97  ?  76   CYS B SG  1 
ATOM   4099 N  N   . SER B 1 78  ? -12.545 50.637  43.111  1.00 100.82 ?  77   SER B N   1 
ATOM   4100 C  CA  . SER B 1 78  ? -12.542 49.196  42.871  1.00 83.45  ?  77   SER B CA  1 
ATOM   4101 C  C   . SER B 1 78  ? -13.824 48.576  43.379  1.00 84.55  ?  77   SER B C   1 
ATOM   4102 O  O   . SER B 1 78  ? -14.336 47.631  42.790  1.00 107.10 ?  77   SER B O   1 
ATOM   4103 C  CB  . SER B 1 78  ? -11.342 48.529  43.531  1.00 84.78  ?  77   SER B CB  1 
ATOM   4104 O  OG  . SER B 1 78  ? -10.144 49.129  43.086  1.00 92.19  ?  77   SER B OG  1 
ATOM   4105 N  N   . ALA B 1 79  ? -14.321 49.100  44.493  1.00 78.02  ?  78   ALA B N   1 
ATOM   4106 C  CA  . ALA B 1 79  ? -15.609 48.687  45.031  1.00 112.76 ?  78   ALA B CA  1 
ATOM   4107 C  C   . ALA B 1 79  ? -16.724 48.917  44.010  1.00 111.94 ?  78   ALA B C   1 
ATOM   4108 O  O   . ALA B 1 79  ? -17.726 48.194  43.982  1.00 99.82  ?  78   ALA B O   1 
ATOM   4109 C  CB  . ALA B 1 79  ? -15.905 49.442  46.319  1.00 110.76 ?  78   ALA B CB  1 
ATOM   4110 N  N   . SER B 1 80  ? -16.534 49.939  43.182  1.00 117.36 ?  79   SER B N   1 
ATOM   4111 C  CA  . SER B 1 80  ? -17.486 50.311  42.142  1.00 115.23 ?  79   SER B CA  1 
ATOM   4112 C  C   . SER B 1 80  ? -17.521 49.359  40.945  1.00 109.54 ?  79   SER B C   1 
ATOM   4113 O  O   . SER B 1 80  ? -18.551 49.240  40.288  1.00 118.34 ?  79   SER B O   1 
ATOM   4114 C  CB  . SER B 1 80  ? -17.182 51.723  41.651  1.00 124.72 ?  79   SER B CB  1 
ATOM   4115 O  OG  . SER B 1 80  ? -16.809 52.558  42.731  1.00 127.55 ?  79   SER B OG  1 
ATOM   4116 N  N   . ILE B 1 81  ? -16.395 48.710  40.650  1.00 94.62  ?  80   ILE B N   1 
ATOM   4117 C  CA  . ILE B 1 81  ? -16.278 47.866  39.458  1.00 87.17  ?  80   ILE B CA  1 
ATOM   4118 C  C   . ILE B 1 81  ? -17.331 46.761  39.380  1.00 105.04 ?  80   ILE B C   1 
ATOM   4119 O  O   . ILE B 1 81  ? -17.979 46.592  38.345  1.00 117.93 ?  80   ILE B O   1 
ATOM   4120 C  CB  . ILE B 1 81  ? -14.885 47.207  39.372  1.00 82.87  ?  80   ILE B CB  1 
ATOM   4121 C  CG1 . ILE B 1 81  ? -13.798 48.271  39.264  1.00 82.00  ?  80   ILE B CG1 1 
ATOM   4122 C  CG2 . ILE B 1 81  ? -14.798 46.278  38.173  1.00 92.30  ?  80   ILE B CG2 1 
ATOM   4123 C  CD1 . ILE B 1 81  ? -12.425 47.697  38.974  1.00 79.93  ?  80   ILE B CD1 1 
ATOM   4124 N  N   . THR B 1 82  ? -17.509 46.023  40.474  1.00 110.12 ?  81   THR B N   1 
ATOM   4125 C  CA  . THR B 1 82  ? -18.462 44.915  40.502  1.00 112.85 ?  81   THR B CA  1 
ATOM   4126 C  C   . THR B 1 82  ? -19.883 45.412  40.277  1.00 114.24 ?  81   THR B C   1 
ATOM   4127 O  O   . THR B 1 82  ? -20.692 44.742  39.636  1.00 115.25 ?  81   THR B O   1 
ATOM   4128 C  CB  . THR B 1 82  ? -18.403 44.141  41.830  1.00 125.26 ?  81   THR B CB  1 
ATOM   4129 O  OG1 . THR B 1 82  ? -19.176 44.820  42.830  1.00 130.75 ?  81   THR B OG1 1 
ATOM   4130 C  CG2 . THR B 1 82  ? -16.957 43.997  42.292  1.00 124.52 ?  81   THR B CG2 1 
ATOM   4131 N  N   . ASP B 1 83  ? -20.189 46.580  40.830  1.00 123.16 ?  82   ASP B N   1 
ATOM   4132 C  CA  . ASP B 1 83  ? -21.481 47.209  40.606  1.00 125.89 ?  82   ASP B CA  1 
ATOM   4133 C  C   . ASP B 1 83  ? -21.485 47.904  39.241  1.00 115.92 ?  82   ASP B C   1 
ATOM   4134 O  O   . ASP B 1 83  ? -20.440 48.297  38.724  1.00 96.31  ?  82   ASP B O   1 
ATOM   4135 C  CB  . ASP B 1 83  ? -21.787 48.208  41.730  1.00 124.09 ?  82   ASP B CB  1 
ATOM   4136 C  CG  . ASP B 1 83  ? -23.227 48.696  41.716  1.00 131.93 ?  82   ASP B CG  1 
ATOM   4137 O  OD1 . ASP B 1 83  ? -23.960 48.390  40.755  1.00 143.74 ?  82   ASP B OD1 1 
ATOM   4138 O  OD2 . ASP B 1 83  ? -23.627 49.388  42.678  1.00 126.15 ?  82   ASP B OD2 1 
ATOM   4139 N  N   . ILE B 1 84  ? -22.665 48.045  38.654  1.00 124.19 ?  83   ILE B N   1 
ATOM   4140 C  CA  . ILE B 1 84  ? -22.805 48.784  37.407  1.00 118.41 ?  83   ILE B CA  1 
ATOM   4141 C  C   . ILE B 1 84  ? -23.435 50.133  37.743  1.00 125.95 ?  83   ILE B C   1 
ATOM   4142 O  O   . ILE B 1 84  ? -23.901 50.327  38.867  1.00 134.61 ?  83   ILE B O   1 
ATOM   4143 C  CB  . ILE B 1 84  ? -23.614 47.993  36.361  1.00 99.18  ?  83   ILE B CB  1 
ATOM   4144 C  CG1 . ILE B 1 84  ? -24.738 47.216  37.040  1.00 95.41  ?  83   ILE B CG1 1 
ATOM   4145 C  CG2 . ILE B 1 84  ? -22.725 46.954  35.706  1.00 81.50  ?  83   ILE B CG2 1 
ATOM   4146 C  CD1 . ILE B 1 84  ? -26.114 47.683  36.698  1.00 95.15  ?  83   ILE B CD1 1 
ATOM   4147 N  N   . SER B 1 85  ? -23.407 51.061  36.787  1.00 129.07 ?  84   SER B N   1 
ATOM   4148 C  CA  . SER B 1 85  ? -23.813 52.462  36.990  1.00 129.44 ?  84   SER B CA  1 
ATOM   4149 C  C   . SER B 1 85  ? -22.781 53.239  37.813  1.00 115.58 ?  84   SER B C   1 
ATOM   4150 O  O   . SER B 1 85  ? -22.917 54.446  38.007  1.00 111.80 ?  84   SER B O   1 
ATOM   4151 C  CB  . SER B 1 85  ? -25.196 52.573  37.649  1.00 125.10 ?  84   SER B CB  1 
ATOM   4152 O  OG  . SER B 1 85  ? -25.145 52.217  39.019  1.00 91.33  ?  84   SER B OG  1 
ATOM   4153 N  N   . LEU B 1 86  ? -21.760 52.549  38.310  1.00 113.86 ?  85   LEU B N   1 
ATOM   4154 C  CA  . LEU B 1 86  ? -20.690 53.217  39.035  1.00 123.41 ?  85   LEU B CA  1 
ATOM   4155 C  C   . LEU B 1 86  ? -19.346 52.936  38.379  1.00 131.40 ?  85   LEU B C   1 
ATOM   4156 O  O   . LEU B 1 86  ? -18.351 53.608  38.653  1.00 148.04 ?  85   LEU B O   1 
ATOM   4157 C  CB  . LEU B 1 86  ? -20.661 52.763  40.494  1.00 129.85 ?  85   LEU B CB  1 
ATOM   4158 C  CG  . LEU B 1 86  ? -21.941 52.988  41.297  1.00 137.88 ?  85   LEU B CG  1 
ATOM   4159 C  CD1 . LEU B 1 86  ? -21.780 52.442  42.704  1.00 143.31 ?  85   LEU B CD1 1 
ATOM   4160 C  CD2 . LEU B 1 86  ? -22.305 54.463  41.331  1.00 141.07 ?  85   LEU B CD2 1 
ATOM   4161 N  N   . GLN B 1 87  ? -19.329 51.945  37.497  1.00 126.47 ?  86   GLN B N   1 
ATOM   4162 C  CA  . GLN B 1 87  ? -18.091 51.503  36.878  1.00 120.04 ?  86   GLN B CA  1 
ATOM   4163 C  C   . GLN B 1 87  ? -17.451 52.592  36.020  1.00 118.16 ?  86   GLN B C   1 
ATOM   4164 O  O   . GLN B 1 87  ? -16.258 52.860  36.144  1.00 117.89 ?  86   GLN B O   1 
ATOM   4165 C  CB  . GLN B 1 87  ? -18.353 50.246  36.054  1.00 129.27 ?  86   GLN B CB  1 
ATOM   4166 C  CG  . GLN B 1 87  ? -17.106 49.516  35.622  1.00 132.84 ?  86   GLN B CG  1 
ATOM   4167 C  CD  . GLN B 1 87  ? -17.438 48.305  34.788  1.00 139.20 ?  86   GLN B CD  1 
ATOM   4168 O  OE1 . GLN B 1 87  ? -17.640 48.406  33.580  1.00 141.06 ?  86   GLN B OE1 1 
ATOM   4169 N  NE2 . GLN B 1 87  ? -17.486 47.144  35.428  1.00 137.73 ?  86   GLN B NE2 1 
ATOM   4170 N  N   . TYR B 1 88  ? -18.250 53.224  35.164  1.00 115.52 ?  87   TYR B N   1 
ATOM   4171 C  CA  . TYR B 1 88  ? -17.726 54.203  34.211  1.00 110.19 ?  87   TYR B CA  1 
ATOM   4172 C  C   . TYR B 1 88  ? -17.159 55.426  34.925  1.00 113.34 ?  87   TYR B C   1 
ATOM   4173 O  O   . TYR B 1 88  ? -16.127 55.968  34.525  1.00 107.36 ?  87   TYR B O   1 
ATOM   4174 C  CB  . TYR B 1 88  ? -18.792 54.614  33.190  1.00 109.41 ?  87   TYR B CB  1 
ATOM   4175 C  CG  . TYR B 1 88  ? -20.025 55.296  33.729  1.00 106.27 ?  87   TYR B CG  1 
ATOM   4176 C  CD1 . TYR B 1 88  ? -20.995 54.585  34.422  1.00 107.32 ?  87   TYR B CD1 1 
ATOM   4177 C  CD2 . TYR B 1 88  ? -20.246 56.645  33.491  1.00 115.46 ?  87   TYR B CD2 1 
ATOM   4178 C  CE1 . TYR B 1 88  ? -22.135 55.211  34.893  1.00 120.62 ?  87   TYR B CE1 1 
ATOM   4179 C  CE2 . TYR B 1 88  ? -21.386 57.276  33.949  1.00 121.63 ?  87   TYR B CE2 1 
ATOM   4180 C  CZ  . TYR B 1 88  ? -22.324 56.560  34.655  1.00 121.63 ?  87   TYR B CZ  1 
ATOM   4181 O  OH  . TYR B 1 88  ? -23.455 57.195  35.117  1.00 119.56 ?  87   TYR B OH  1 
ATOM   4182 N  N   . LEU B 1 89  ? -17.838 55.852  35.985  1.00 110.46 ?  88   LEU B N   1 
ATOM   4183 C  CA  . LEU B 1 89  ? -17.342 56.939  36.816  1.00 96.53  ?  88   LEU B CA  1 
ATOM   4184 C  C   . LEU B 1 89  ? -16.009 56.541  37.443  1.00 97.90  ?  88   LEU B C   1 
ATOM   4185 O  O   . LEU B 1 89  ? -15.090 57.347  37.555  1.00 114.83 ?  88   LEU B O   1 
ATOM   4186 C  CB  . LEU B 1 89  ? -18.353 57.275  37.917  1.00 99.93  ?  88   LEU B CB  1 
ATOM   4187 C  CG  . LEU B 1 89  ? -19.158 58.571  37.834  1.00 107.61 ?  88   LEU B CG  1 
ATOM   4188 C  CD1 . LEU B 1 89  ? -19.874 58.665  36.514  1.00 105.79 ?  88   LEU B CD1 1 
ATOM   4189 C  CD2 . LEU B 1 89  ? -20.153 58.653  38.980  1.00 110.05 ?  88   LEU B CD2 1 
ATOM   4190 N  N   . ALA B 1 90  ? -15.918 55.284  37.853  1.00 89.08  ?  89   ALA B N   1 
ATOM   4191 C  CA  . ALA B 1 90  ? -14.717 54.764  38.492  1.00 88.81  ?  89   ALA B CA  1 
ATOM   4192 C  C   . ALA B 1 90  ? -13.511 54.711  37.552  1.00 98.25  ?  89   ALA B C   1 
ATOM   4193 O  O   . ALA B 1 90  ? -12.382 54.949  37.968  1.00 107.27 ?  89   ALA B O   1 
ATOM   4194 C  CB  . ALA B 1 90  ? -14.996 53.388  39.088  1.00 86.30  ?  89   ALA B CB  1 
ATOM   4195 N  N   . ILE B 1 91  ? -13.737 54.384  36.288  1.00 105.63 ?  90   ILE B N   1 
ATOM   4196 C  CA  . ILE B 1 91  ? -12.618 54.299  35.361  1.00 123.88 ?  90   ILE B CA  1 
ATOM   4197 C  C   . ILE B 1 91  ? -11.923 55.615  35.027  1.00 146.64 ?  90   ILE B C   1 
ATOM   4198 O  O   . ILE B 1 91  ? -10.718 55.735  35.228  1.00 166.55 ?  90   ILE B O   1 
ATOM   4199 C  CB  . ILE B 1 91  ? -13.057 53.629  34.067  1.00 124.03 ?  90   ILE B CB  1 
ATOM   4200 C  CG1 . ILE B 1 91  ? -13.482 52.196  34.393  1.00 113.44 ?  90   ILE B CG1 1 
ATOM   4201 C  CG2 . ILE B 1 91  ? -11.943 53.677  33.000  1.00 133.07 ?  90   ILE B CG2 1 
ATOM   4202 C  CD1 . ILE B 1 91  ? -14.679 51.720  33.622  1.00 113.01 ?  90   ILE B CD1 1 
ATOM   4203 N  N   . ASP B 1 92  ? -12.665 56.606  34.549  1.00 141.18 ?  91   ASP B N   1 
ATOM   4204 C  CA  . ASP B 1 92  ? -12.032 57.847  34.118  1.00 136.58 ?  91   ASP B CA  1 
ATOM   4205 C  C   . ASP B 1 92  ? -11.333 58.566  35.284  1.00 131.64 ?  91   ASP B C   1 
ATOM   4206 O  O   . ASP B 1 92  ? -10.200 59.030  35.140  1.00 129.63 ?  91   ASP B O   1 
ATOM   4207 C  CB  . ASP B 1 92  ? -13.050 58.769  33.425  1.00 134.83 ?  91   ASP B CB  1 
ATOM   4208 C  CG  . ASP B 1 92  ? -14.200 59.182  34.335  1.00 132.90 ?  91   ASP B CG  1 
ATOM   4209 O  OD1 . ASP B 1 92  ? -14.166 58.879  35.549  1.00 142.57 ?  91   ASP B OD1 1 
ATOM   4210 O  OD2 . ASP B 1 92  ? -15.139 59.834  33.835  1.00 124.68 ?  91   ASP B OD2 1 
ATOM   4211 N  N   . ARG B 1 93  ? -11.996 58.631  36.435  1.00 118.09 ?  92   ARG B N   1 
ATOM   4212 C  CA  . ARG B 1 93  ? -11.447 59.327  37.586  1.00 114.49 ?  92   ARG B CA  1 
ATOM   4213 C  C   . ARG B 1 93  ? -10.305 58.566  38.236  1.00 118.97 ?  92   ARG B C   1 
ATOM   4214 O  O   . ARG B 1 93  ? -9.300  59.153  38.627  1.00 132.62 ?  92   ARG B O   1 
ATOM   4215 C  CB  . ARG B 1 93  ? -12.538 59.557  38.631  1.00 112.66 ?  92   ARG B CB  1 
ATOM   4216 C  CG  . ARG B 1 93  ? -13.512 60.689  38.375  1.00 119.05 ?  92   ARG B CG  1 
ATOM   4217 C  CD  . ARG B 1 93  ? -12.930 62.035  38.753  1.00 115.89 ?  92   ARG B CD  1 
ATOM   4218 N  NE  . ARG B 1 93  ? -13.178 63.057  37.739  1.00 107.10 ?  92   ARG B NE  1 
ATOM   4219 C  CZ  . ARG B 1 93  ? -14.193 63.914  37.758  1.00 121.68 ?  92   ARG B CZ  1 
ATOM   4220 N  NH1 . ARG B 1 93  ? -15.028 63.948  38.791  1.00 126.47 ?  92   ARG B NH1 1 
ATOM   4221 N  NH2 . ARG B 1 93  ? -14.345 64.774  36.761  1.00 132.78 ?  92   ARG B NH2 1 
ATOM   4222 N  N   . GLY B 1 94  ? -10.470 57.253  38.335  1.00 86.60  ?  93   GLY B N   1 
ATOM   4223 C  CA  . GLY B 1 94  ? -9.554  56.403  39.073  1.00 85.45  ?  93   GLY B CA  1 
ATOM   4224 C  C   . GLY B 1 94  ? -8.100  56.509  38.672  1.00 102.83 ?  93   GLY B C   1 
ATOM   4225 O  O   . GLY B 1 94  ? -7.221  56.538  39.524  1.00 119.06 ?  93   GLY B O   1 
ATOM   4226 N  N   . PHE B 1 95  ? -7.844  56.569  37.371  1.00 115.90 ?  94   PHE B N   1 
ATOM   4227 C  CA  . PHE B 1 95  ? -6.487  56.726  36.860  1.00 128.21 ?  94   PHE B CA  1 
ATOM   4228 C  C   . PHE B 1 95  ? -5.986  58.108  37.246  1.00 139.76 ?  94   PHE B C   1 
ATOM   4229 O  O   . PHE B 1 95  ? -4.858  58.271  37.708  1.00 137.90 ?  94   PHE B O   1 
ATOM   4230 C  CB  . PHE B 1 95  ? -6.440  56.542  35.345  1.00 136.23 ?  94   PHE B CB  1 
ATOM   4231 C  CG  . PHE B 1 95  ? -6.821  55.166  34.889  1.00 129.36 ?  94   PHE B CG  1 
ATOM   4232 C  CD1 . PHE B 1 95  ? -5.929  54.117  34.997  1.00 118.78 ?  94   PHE B CD1 1 
ATOM   4233 C  CD2 . PHE B 1 95  ? -8.068  54.924  34.340  1.00 133.33 ?  94   PHE B CD2 1 
ATOM   4234 C  CE1 . PHE B 1 95  ? -6.277  52.855  34.571  1.00 121.75 ?  94   PHE B CE1 1 
ATOM   4235 C  CE2 . PHE B 1 95  ? -8.424  53.661  33.914  1.00 124.24 ?  94   PHE B CE2 1 
ATOM   4236 C  CZ  . PHE B 1 95  ? -7.526  52.627  34.028  1.00 116.74 ?  94   PHE B CZ  1 
ATOM   4237 N  N   . GLU B 1 96  ? -6.841  59.104  37.035  1.00 158.02 ?  95   GLU B N   1 
ATOM   4238 C  CA  . GLU B 1 96  ? -6.524  60.489  37.355  1.00 163.27 ?  95   GLU B CA  1 
ATOM   4239 C  C   . GLU B 1 96  ? -6.293  60.709  38.848  1.00 160.96 ?  95   GLU B C   1 
ATOM   4240 O  O   . GLU B 1 96  ? -5.335  61.378  39.239  1.00 165.36 ?  95   GLU B O   1 
ATOM   4241 C  CB  . GLU B 1 96  ? -7.646  61.406  36.869  1.00 172.17 ?  95   GLU B CB  1 
ATOM   4242 C  CG  . GLU B 1 96  ? -7.630  62.788  37.495  1.00 180.54 ?  95   GLU B CG  1 
ATOM   4243 C  CD  . GLU B 1 96  ? -8.855  63.598  37.136  1.00 182.26 ?  95   GLU B CD  1 
ATOM   4244 O  OE1 . GLU B 1 96  ? -9.494  63.289  36.107  1.00 179.98 ?  95   GLU B OE1 1 
ATOM   4245 O  OE2 . GLU B 1 96  ? -9.176  64.545  37.883  1.00 185.46 ?  95   GLU B OE2 1 
ATOM   4246 N  N   . ILE B 1 97  ? -7.170  60.145  39.676  1.00 143.04 ?  96   ILE B N   1 
ATOM   4247 C  CA  . ILE B 1 97  ? -7.045  60.262  41.127  1.00 128.73 ?  96   ILE B CA  1 
ATOM   4248 C  C   . ILE B 1 97  ? -5.749  59.655  41.652  1.00 122.64 ?  96   ILE B C   1 
ATOM   4249 O  O   . ILE B 1 97  ? -5.047  60.266  42.458  1.00 142.34 ?  96   ILE B O   1 
ATOM   4250 C  CB  . ILE B 1 97  ? -8.229  59.587  41.843  1.00 115.81 ?  96   ILE B CB  1 
ATOM   4251 C  CG1 . ILE B 1 97  ? -9.511  60.388  41.619  1.00 126.60 ?  96   ILE B CG1 1 
ATOM   4252 C  CG2 . ILE B 1 97  ? -7.962  59.460  43.328  1.00 107.44 ?  96   ILE B CG2 1 
ATOM   4253 C  CD1 . ILE B 1 97  ? -10.716 59.821  42.342  1.00 119.92 ?  96   ILE B CD1 1 
ATOM   4254 N  N   . PHE B 1 98  ? -5.432  58.457  41.175  1.00 96.34  ?  97   PHE B N   1 
ATOM   4255 C  CA  . PHE B 1 98  ? -4.225  57.747  41.584  1.00 93.22  ?  97   PHE B CA  1 
ATOM   4256 C  C   . PHE B 1 98  ? -2.949  58.512  41.237  1.00 111.97 ?  97   PHE B C   1 
ATOM   4257 O  O   . PHE B 1 98  ? -2.042  58.618  42.059  1.00 120.93 ?  97   PHE B O   1 
ATOM   4258 C  CB  . PHE B 1 98  ? -4.182  56.357  40.953  1.00 104.33 ?  97   PHE B CB  1 
ATOM   4259 C  CG  . PHE B 1 98  ? -2.845  55.675  41.071  1.00 108.03 ?  97   PHE B CG  1 
ATOM   4260 C  CD1 . PHE B 1 98  ? -2.494  55.000  42.232  1.00 113.96 ?  97   PHE B CD1 1 
ATOM   4261 C  CD2 . PHE B 1 98  ? -1.938  55.708  40.023  1.00 106.59 ?  97   PHE B CD2 1 
ATOM   4262 C  CE1 . PHE B 1 98  ? -1.267  54.366  42.344  1.00 111.85 ?  97   PHE B CE1 1 
ATOM   4263 C  CE2 . PHE B 1 98  ? -0.708  55.082  40.128  1.00 110.91 ?  97   PHE B CE2 1 
ATOM   4264 C  CZ  . PHE B 1 98  ? -0.371  54.408  41.290  1.00 113.44 ?  97   PHE B CZ  1 
ATOM   4265 N  N   . ASP B 1 99  ? -2.869  59.010  40.007  1.00 134.61 ?  98   ASP B N   1 
ATOM   4266 C  CA  . ASP B 1 99  ? -1.662  59.684  39.538  1.00 158.72 ?  98   ASP B CA  1 
ATOM   4267 C  C   . ASP B 1 99  ? -1.390  60.996  40.281  1.00 187.98 ?  98   ASP B C   1 
ATOM   4268 O  O   . ASP B 1 99  ? -0.240  61.423  40.389  1.00 210.91 ?  98   ASP B O   1 
ATOM   4269 C  CB  . ASP B 1 99  ? -1.754  59.942  38.030  1.00 151.90 ?  98   ASP B CB  1 
ATOM   4270 C  CG  . ASP B 1 99  ? -1.272  58.762  37.205  1.00 152.41 ?  98   ASP B CG  1 
ATOM   4271 O  OD1 . ASP B 1 99  ? -0.467  57.962  37.727  1.00 153.94 ?  98   ASP B OD1 1 
ATOM   4272 O  OD2 . ASP B 1 99  ? -1.703  58.630  36.038  1.00 150.67 ?  98   ASP B OD2 1 
ATOM   4273 N  N   . ARG B 1 100 ? -2.439  61.633  40.791  1.00 174.45 ?  99   ARG B N   1 
ATOM   4274 C  CA  . ARG B 1 100 ? -2.277  62.833  41.606  1.00 155.54 ?  99   ARG B CA  1 
ATOM   4275 C  C   . ARG B 1 100 ? -1.610  62.509  42.943  1.00 132.22 ?  99   ARG B C   1 
ATOM   4276 O  O   . ARG B 1 100 ? -0.713  63.218  43.400  1.00 133.97 ?  99   ARG B O   1 
ATOM   4277 C  CB  . ARG B 1 100 ? -3.624  63.522  41.835  1.00 161.31 ?  99   ARG B CB  1 
ATOM   4278 C  CG  . ARG B 1 100 ? -3.508  64.800  42.655  1.00 178.55 ?  99   ARG B CG  1 
ATOM   4279 C  CD  . ARG B 1 100 ? -4.633  65.773  42.357  1.00 183.49 ?  99   ARG B CD  1 
ATOM   4280 N  NE  . ARG B 1 100 ? -4.459  66.461  41.079  1.00 192.83 ?  99   ARG B NE  1 
ATOM   4281 C  CZ  . ARG B 1 100 ? -5.188  66.222  39.992  1.00 199.30 ?  99   ARG B CZ  1 
ATOM   4282 N  NH1 . ARG B 1 100 ? -6.152  65.312  40.021  1.00 194.97 ?  99   ARG B NH1 1 
ATOM   4283 N  NH2 . ARG B 1 100 ? -4.956  66.899  38.875  1.00 205.22 ?  99   ARG B NH2 1 
ATOM   4284 N  N   . MET B 1 101 ? -2.053  61.420  43.555  1.00 115.57 ?  100  MET B N   1 
ATOM   4285 C  CA  . MET B 1 101 ? -1.535  60.994  44.845  1.00 116.60 ?  100  MET B CA  1 
ATOM   4286 C  C   . MET B 1 101 ? -0.070  60.580  44.774  1.00 123.26 ?  100  MET B C   1 
ATOM   4287 O  O   . MET B 1 101 ? 0.721   60.921  45.652  1.00 131.72 ?  100  MET B O   1 
ATOM   4288 C  CB  . MET B 1 101 ? -2.377  59.826  45.356  1.00 117.61 ?  100  MET B CB  1 
ATOM   4289 C  CG  . MET B 1 101 ? -1.822  59.079  46.548  1.00 128.26 ?  100  MET B CG  1 
ATOM   4290 S  SD  . MET B 1 101 ? -2.435  57.377  46.564  1.00 136.11 ?  100  MET B SD  1 
ATOM   4291 C  CE  . MET B 1 101 ? -0.987  56.499  45.982  1.00 108.42 ?  100  MET B CE  1 
ATOM   4292 N  N   . VAL B 1 102 ? 0.288   59.842  43.729  1.00 121.88 ?  101  VAL B N   1 
ATOM   4293 C  CA  . VAL B 1 102 ? 1.669   59.417  43.531  1.00 130.67 ?  101  VAL B CA  1 
ATOM   4294 C  C   . VAL B 1 102 ? 2.556   60.603  43.145  1.00 143.04 ?  101  VAL B C   1 
ATOM   4295 O  O   . VAL B 1 102 ? 3.761   60.587  43.396  1.00 164.09 ?  101  VAL B O   1 
ATOM   4296 C  CB  . VAL B 1 102 ? 1.779   58.296  42.473  1.00 130.75 ?  101  VAL B CB  1 
ATOM   4297 C  CG1 . VAL B 1 102 ? 1.473   58.821  41.086  1.00 132.06 ?  101  VAL B CG1 1 
ATOM   4298 C  CG2 . VAL B 1 102 ? 3.160   57.650  42.517  1.00 136.88 ?  101  VAL B CG2 1 
ATOM   4299 N  N   . SER B 1 103 ? 1.952   61.625  42.536  1.00 149.22 ?  102  SER B N   1 
ATOM   4300 C  CA  . SER B 1 103 ? 2.685   62.802  42.059  1.00 158.60 ?  102  SER B CA  1 
ATOM   4301 C  C   . SER B 1 103 ? 3.446   63.520  43.168  1.00 156.57 ?  102  SER B C   1 
ATOM   4302 O  O   . SER B 1 103 ? 4.504   64.104  42.928  1.00 151.46 ?  102  SER B O   1 
ATOM   4303 C  CB  . SER B 1 103 ? 1.729   63.782  41.379  1.00 165.79 ?  102  SER B CB  1 
ATOM   4304 O  OG  . SER B 1 103 ? 2.415   64.935  40.919  1.00 168.55 ?  102  SER B OG  1 
ATOM   4305 N  N   . SER B 1 104 ? 2.905   63.469  44.380  1.00 163.06 ?  103  SER B N   1 
ATOM   4306 C  CA  . SER B 1 104 ? 3.558   64.051  45.551  1.00 175.13 ?  103  SER B CA  1 
ATOM   4307 C  C   . SER B 1 104 ? 4.894   63.360  45.863  1.00 192.24 ?  103  SER B C   1 
ATOM   4308 O  O   . SER B 1 104 ? 5.714   63.879  46.625  1.00 204.74 ?  103  SER B O   1 
ATOM   4309 C  CB  . SER B 1 104 ? 2.623   63.977  46.758  1.00 161.81 ?  103  SER B CB  1 
ATOM   4310 O  OG  . SER B 1 104 ? 1.385   64.605  46.472  1.00 140.85 ?  103  SER B OG  1 
ATOM   4311 N  N   . GLY B 1 105 ? 5.096   62.188  45.262  1.00 194.07 ?  104  GLY B N   1 
ATOM   4312 C  CA  . GLY B 1 105 ? 6.316   61.413  45.414  1.00 196.85 ?  104  GLY B CA  1 
ATOM   4313 C  C   . GLY B 1 105 ? 6.235   60.366  46.507  1.00 190.29 ?  104  GLY B C   1 
ATOM   4314 O  O   . GLY B 1 105 ? 7.206   59.658  46.778  1.00 173.88 ?  104  GLY B O   1 
ATOM   4315 N  N   . ILE B 1 106 ? 5.064   60.258  47.127  1.00 191.74 ?  105  ILE B N   1 
ATOM   4316 C  CA  . ILE B 1 106 ? 4.820   59.213  48.114  1.00 190.83 ?  105  ILE B CA  1 
ATOM   4317 C  C   . ILE B 1 106 ? 4.569   57.865  47.428  1.00 184.08 ?  105  ILE B C   1 
ATOM   4318 O  O   . ILE B 1 106 ? 3.729   57.752  46.531  1.00 183.11 ?  105  ILE B O   1 
ATOM   4319 C  CB  . ILE B 1 106 ? 3.631   59.577  49.035  1.00 180.61 ?  105  ILE B CB  1 
ATOM   4320 C  CG1 . ILE B 1 106 ? 2.378   59.910  48.218  1.00 169.08 ?  105  ILE B CG1 1 
ATOM   4321 C  CG2 . ILE B 1 106 ? 3.991   60.757  49.917  1.00 177.76 ?  105  ILE B CG2 1 
ATOM   4322 C  CD1 . ILE B 1 106 ? 1.277   58.881  48.346  1.00 149.55 ?  105  ILE B CD1 1 
ATOM   4323 N  N   . SER B 1 107 ? 5.318   56.846  47.842  1.00 177.07 ?  106  SER B N   1 
ATOM   4324 C  CA  . SER B 1 107 ? 5.165   55.509  47.278  1.00 166.93 ?  106  SER B CA  1 
ATOM   4325 C  C   . SER B 1 107 ? 3.794   54.923  47.604  1.00 160.07 ?  106  SER B C   1 
ATOM   4326 O  O   . SER B 1 107 ? 3.378   54.926  48.760  1.00 171.32 ?  106  SER B O   1 
ATOM   4327 C  CB  . SER B 1 107 ? 6.266   54.576  47.792  1.00 168.34 ?  106  SER B CB  1 
ATOM   4328 O  OG  . SER B 1 107 ? 7.559   55.109  47.550  1.00 157.94 ?  106  SER B OG  1 
ATOM   4329 N  N   . PRO B 1 108 ? 3.070   54.457  46.576  1.00 146.46 ?  107  PRO B N   1 
ATOM   4330 C  CA  . PRO B 1 108 ? 1.690   53.974  46.702  1.00 134.54 ?  107  PRO B CA  1 
ATOM   4331 C  C   . PRO B 1 108 ? 1.580   52.724  47.586  1.00 132.59 ?  107  PRO B C   1 
ATOM   4332 O  O   . PRO B 1 108 ? 2.570   52.016  47.759  1.00 131.51 ?  107  PRO B O   1 
ATOM   4333 C  CB  . PRO B 1 108 ? 1.300   53.669  45.251  1.00 125.45 ?  107  PRO B CB  1 
ATOM   4334 C  CG  . PRO B 1 108 ? 2.598   53.351  44.588  1.00 128.04 ?  107  PRO B CG  1 
ATOM   4335 C  CD  . PRO B 1 108 ? 3.562   54.324  45.194  1.00 139.00 ?  107  PRO B CD  1 
ATOM   4336 N  N   . ASN B 1 109 ? 0.411   52.504  48.183  1.00 131.34 ?  108  ASN B N   1 
ATOM   4337 C  CA  . ASN B 1 109 ? 0.145   51.319  49.007  1.00 135.51 ?  108  ASN B CA  1 
ATOM   4338 C  C   . ASN B 1 109 ? -0.153  50.085  48.159  1.00 133.49 ?  108  ASN B C   1 
ATOM   4339 O  O   . ASN B 1 109 ? -0.639  50.217  47.035  1.00 133.78 ?  108  ASN B O   1 
ATOM   4340 C  CB  . ASN B 1 109 ? -1.015  51.589  49.963  1.00 142.84 ?  108  ASN B CB  1 
ATOM   4341 C  CG  . ASN B 1 109 ? -0.861  52.898  50.693  1.00 162.82 ?  108  ASN B CG  1 
ATOM   4342 O  OD1 . ASN B 1 109 ? -1.427  53.912  50.289  1.00 159.41 ?  108  ASN B OD1 1 
ATOM   4343 N  ND2 . ASN B 1 109 ? -0.080  52.891  51.769  1.00 181.72 ?  108  ASN B ND2 1 
ATOM   4344 N  N   . GLU B 1 110 ? 0.148   48.897  48.682  1.00 129.56 ?  109  GLU B N   1 
ATOM   4345 C  CA  . GLU B 1 110 ? -0.140  47.647  47.972  1.00 121.89 ?  109  GLU B CA  1 
ATOM   4346 C  C   . GLU B 1 110 ? -1.617  47.529  47.600  1.00 115.39 ?  109  GLU B C   1 
ATOM   4347 O  O   . GLU B 1 110 ? -1.962  47.063  46.515  1.00 103.88 ?  109  GLU B O   1 
ATOM   4348 C  CB  . GLU B 1 110 ? 0.288   46.434  48.799  1.00 129.80 ?  109  GLU B CB  1 
ATOM   4349 C  CG  . GLU B 1 110 ? 0.114   45.095  48.073  1.00 127.60 ?  109  GLU B CG  1 
ATOM   4350 C  CD  . GLU B 1 110 ? -1.304  44.563  48.153  1.00 124.37 ?  109  GLU B CD  1 
ATOM   4351 O  OE1 . GLU B 1 110 ? -1.958  44.763  49.198  1.00 138.95 ?  109  GLU B OE1 1 
ATOM   4352 O  OE2 . GLU B 1 110 ? -1.771  43.961  47.164  1.00 108.28 ?  109  GLU B OE2 1 
ATOM   4353 N  N   . ALA B 1 111 ? -2.490  47.915  48.520  1.00 119.79 ?  110  ALA B N   1 
ATOM   4354 C  CA  . ALA B 1 111 ? -3.917  47.880  48.249  1.00 111.03 ?  110  ALA B CA  1 
ATOM   4355 C  C   . ALA B 1 111 ? -4.265  48.827  47.098  1.00 102.35 ?  110  ALA B C   1 
ATOM   4356 O  O   . ALA B 1 111 ? -5.109  48.509  46.262  1.00 81.43  ?  110  ALA B O   1 
ATOM   4357 C  CB  . ALA B 1 111 ? -4.709  48.234  49.502  1.00 107.33 ?  110  ALA B CB  1 
ATOM   4358 N  N   . SER B 1 112 ? -3.620  49.992  47.066  1.00 118.48 ?  111  SER B N   1 
ATOM   4359 C  CA  . SER B 1 112 ? -3.898  51.004  46.042  1.00 116.52 ?  111  SER B CA  1 
ATOM   4360 C  C   . SER B 1 112 ? -3.438  50.614  44.623  1.00 105.31 ?  111  SER B C   1 
ATOM   4361 O  O   . SER B 1 112 ? -4.148  50.878  43.646  1.00 86.50  ?  111  SER B O   1 
ATOM   4362 C  CB  . SER B 1 112 ? -3.272  52.346  46.440  1.00 107.30 ?  111  SER B CB  1 
ATOM   4363 O  OG  . SER B 1 112 ? -1.890  52.220  46.712  1.00 118.12 ?  111  SER B OG  1 
ATOM   4364 N  N   . VAL B 1 113 ? -2.253  50.014  44.500  1.00 96.37  ?  112  VAL B N   1 
ATOM   4365 C  CA  . VAL B 1 113 ? -1.738  49.625  43.184  1.00 90.09  ?  112  VAL B CA  1 
ATOM   4366 C  C   . VAL B 1 113 ? -2.600  48.534  42.559  1.00 103.50 ?  112  VAL B C   1 
ATOM   4367 O  O   . VAL B 1 113 ? -2.822  48.520  41.349  1.00 121.39 ?  112  VAL B O   1 
ATOM   4368 C  CB  . VAL B 1 113 ? -0.262  49.150  43.258  1.00 93.70  ?  112  VAL B CB  1 
ATOM   4369 C  CG1 . VAL B 1 113 ? -0.054  48.206  44.411  1.00 119.86 ?  112  VAL B CG1 1 
ATOM   4370 C  CG2 . VAL B 1 113 ? 0.170   48.489  41.956  1.00 84.55  ?  112  VAL B CG2 1 
ATOM   4371 N  N   . THR B 1 114 ? -3.106  47.634  43.394  1.00 102.55 ?  113  THR B N   1 
ATOM   4372 C  CA  . THR B 1 114 ? -4.047  46.623  42.931  1.00 90.60  ?  113  THR B CA  1 
ATOM   4373 C  C   . THR B 1 114 ? -5.358  47.266  42.514  1.00 80.82  ?  113  THR B C   1 
ATOM   4374 O  O   . THR B 1 114 ? -5.971  46.865  41.532  1.00 90.85  ?  113  THR B O   1 
ATOM   4375 C  CB  . THR B 1 114 ? -4.342  45.573  44.005  1.00 99.17  ?  113  THR B CB  1 
ATOM   4376 O  OG1 . THR B 1 114 ? -3.110  45.060  44.524  1.00 111.23 ?  113  THR B OG1 1 
ATOM   4377 C  CG2 . THR B 1 114 ? -5.138  44.443  43.399  1.00 73.99  ?  113  THR B CG2 1 
ATOM   4378 N  N   . SER B 1 115 ? -5.771  48.277  43.269  1.00 82.72  ?  114  SER B N   1 
ATOM   4379 C  CA  . SER B 1 115 ? -7.032  48.959  43.025  1.00 93.18  ?  114  SER B CA  1 
ATOM   4380 C  C   . SER B 1 115 ? -7.044  49.556  41.620  1.00 97.77  ?  114  SER B C   1 
ATOM   4381 O  O   . SER B 1 115 ? -8.009  49.388  40.870  1.00 90.74  ?  114  SER B O   1 
ATOM   4382 C  CB  . SER B 1 115 ? -7.266  50.045  44.079  1.00 105.17 ?  114  SER B CB  1 
ATOM   4383 O  OG  . SER B 1 115 ? -8.564  50.604  43.965  1.00 101.67 ?  114  SER B OG  1 
ATOM   4384 N  N   . VAL B 1 116 ? -5.964  50.247  41.269  1.00 106.78 ?  115  VAL B N   1 
ATOM   4385 C  CA  . VAL B 1 116 ? -5.812  50.798  39.930  1.00 120.20 ?  115  VAL B CA  1 
ATOM   4386 C  C   . VAL B 1 116 ? -5.640  49.681  38.911  1.00 116.63 ?  115  VAL B C   1 
ATOM   4387 O  O   . VAL B 1 116 ? -6.099  49.794  37.775  1.00 119.15 ?  115  VAL B O   1 
ATOM   4388 C  CB  . VAL B 1 116 ? -4.617  51.756  39.848  1.00 137.18 ?  115  VAL B CB  1 
ATOM   4389 C  CG1 . VAL B 1 116 ? -4.535  52.401  38.469  1.00 132.83 ?  115  VAL B CG1 1 
ATOM   4390 C  CG2 . VAL B 1 116 ? -4.742  52.815  40.918  1.00 152.02 ?  115  VAL B CG2 1 
ATOM   4391 N  N   . ALA B 1 117 ? -4.971  48.605  39.320  1.00 112.77 ?  116  ALA B N   1 
ATOM   4392 C  CA  . ALA B 1 117 ? -4.801  47.440  38.457  1.00 109.19 ?  116  ALA B CA  1 
ATOM   4393 C  C   . ALA B 1 117 ? -6.164  46.856  38.115  1.00 107.70 ?  116  ALA B C   1 
ATOM   4394 O  O   . ALA B 1 117 ? -6.426  46.517  36.964  1.00 101.19 ?  116  ALA B O   1 
ATOM   4395 C  CB  . ALA B 1 117 ? -3.915  46.392  39.118  1.00 100.61 ?  116  ALA B CB  1 
ATOM   4396 N  N   . ARG B 1 118 ? -7.029  46.752  39.123  1.00 107.64 ?  117  ARG B N   1 
ATOM   4397 C  CA  . ARG B 1 118 ? -8.399  46.285  38.923  1.00 110.09 ?  117  ARG B CA  1 
ATOM   4398 C  C   . ARG B 1 118 ? -9.149  47.228  37.999  1.00 108.34 ?  117  ARG B C   1 
ATOM   4399 O  O   . ARG B 1 118 ? -9.827  46.792  37.075  1.00 126.40 ?  117  ARG B O   1 
ATOM   4400 C  CB  . ARG B 1 118 ? -9.146  46.167  40.256  1.00 122.96 ?  117  ARG B CB  1 
ATOM   4401 C  CG  . ARG B 1 118 ? -8.611  45.100  41.190  1.00 122.46 ?  117  ARG B CG  1 
ATOM   4402 C  CD  . ARG B 1 118 ? -9.098  43.729  40.780  1.00 130.76 ?  117  ARG B CD  1 
ATOM   4403 N  NE  . ARG B 1 118 ? -8.110  42.694  41.061  1.00 131.62 ?  117  ARG B NE  1 
ATOM   4404 C  CZ  . ARG B 1 118 ? -7.989  42.071  42.227  1.00 128.30 ?  117  ARG B CZ  1 
ATOM   4405 N  NH1 . ARG B 1 118 ? -8.796  42.378  43.235  1.00 114.14 ?  117  ARG B NH1 1 
ATOM   4406 N  NH2 . ARG B 1 118 ? -7.059  41.140  42.382  1.00 137.22 ?  117  ARG B NH2 1 
ATOM   4407 N  N   . LEU B 1 119 ? -9.037  48.522  38.274  1.00 101.97 ?  118  LEU B N   1 
ATOM   4408 C  CA  . LEU B 1 119 ? -9.677  49.555  37.467  1.00 100.69 ?  118  LEU B CA  1 
ATOM   4409 C  C   . LEU B 1 119 ? -9.174  49.512  36.026  1.00 90.42  ?  118  LEU B C   1 
ATOM   4410 O  O   . LEU B 1 119 ? -9.953  49.613  35.073  1.00 75.41  ?  118  LEU B O   1 
ATOM   4411 C  CB  . LEU B 1 119 ? -9.413  50.929  38.082  1.00 112.21 ?  118  LEU B CB  1 
ATOM   4412 C  CG  . LEU B 1 119 ? -10.565 51.915  38.270  1.00 77.79  ?  118  LEU B CG  1 
ATOM   4413 C  CD1 . LEU B 1 119 ? -11.795 51.246  38.848  1.00 76.76  ?  118  LEU B CD1 1 
ATOM   4414 C  CD2 . LEU B 1 119 ? -10.092 52.999  39.198  1.00 88.22  ?  118  LEU B CD2 1 
ATOM   4415 N  N   . ALA B 1 120 ? -7.863  49.342  35.883  1.00 97.60  ?  119  ALA B N   1 
ATOM   4416 C  CA  . ALA B 1 120 ? -7.234  49.243  34.574  1.00 104.89 ?  119  ALA B CA  1 
ATOM   4417 C  C   . ALA B 1 120 ? -7.698  48.009  33.844  1.00 99.87  ?  119  ALA B C   1 
ATOM   4418 O  O   . ALA B 1 120 ? -8.261  48.108  32.770  1.00 81.93  ?  119  ALA B O   1 
ATOM   4419 C  CB  . ALA B 1 120 ? -5.726  49.228  34.706  1.00 117.02 ?  119  ALA B CB  1 
ATOM   4420 N  N   . ALA B 1 121 ? -7.480  46.852  34.458  1.00 113.87 ?  120  ALA B N   1 
ATOM   4421 C  CA  . ALA B 1 121 ? -7.805  45.563  33.855  1.00 111.17 ?  120  ALA B CA  1 
ATOM   4422 C  C   . ALA B 1 121 ? -9.286  45.423  33.539  1.00 75.02  ?  120  ALA B C   1 
ATOM   4423 O  O   . ALA B 1 121 ? -9.652  44.719  32.598  1.00 83.10  ?  120  ALA B O   1 
ATOM   4424 C  CB  . ALA B 1 121 ? -7.364  44.428  34.767  1.00 134.57 ?  120  ALA B CB  1 
ATOM   4425 N  N   . ALA B 1 122 ? -10.131 46.083  34.328  1.00 71.55  ?  121  ALA B N   1 
ATOM   4426 C  CA  . ALA B 1 122 ? -11.575 45.957  34.166  1.00 91.90  ?  121  ALA B CA  1 
ATOM   4427 C  C   . ALA B 1 122 ? -11.965 46.361  32.759  1.00 104.47 ?  121  ALA B C   1 
ATOM   4428 O  O   . ALA B 1 122 ? -12.817 45.733  32.130  1.00 121.93 ?  121  ALA B O   1 
ATOM   4429 C  CB  . ALA B 1 122 ? -12.313 46.808  35.186  1.00 93.74  ?  121  ALA B CB  1 
ATOM   4430 N  N   . LYS B 1 123 ? -11.330 47.417  32.270  1.00 97.40  ?  122  LYS B N   1 
ATOM   4431 C  CA  . LYS B 1 123 ? -11.542 47.843  30.903  1.00 112.33 ?  122  LYS B CA  1 
ATOM   4432 C  C   . LYS B 1 123 ? -10.169 48.064  30.274  1.00 107.70 ?  122  LYS B C   1 
ATOM   4433 O  O   . LYS B 1 123 ? -9.956  49.014  29.524  1.00 90.81  ?  122  LYS B O   1 
ATOM   4434 C  CB  . LYS B 1 123 ? -12.398 49.110  30.880  1.00 128.22 ?  122  LYS B CB  1 
ATOM   4435 C  CG  . LYS B 1 123 ? -13.761 48.904  31.538  1.00 138.89 ?  122  LYS B CG  1 
ATOM   4436 C  CD  . LYS B 1 123 ? -14.657 48.044  30.674  1.00 142.27 ?  122  LYS B CD  1 
ATOM   4437 C  CE  . LYS B 1 123 ? -15.783 47.382  31.445  1.00 127.68 ?  122  LYS B CE  1 
ATOM   4438 N  NZ  . LYS B 1 123 ? -17.046 48.176  31.393  1.00 115.21 ?  122  LYS B NZ  1 
ATOM   4439 N  N   . GLY B 1 124 ? -9.263  47.127  30.544  1.00 119.88 ?  123  GLY B N   1 
ATOM   4440 C  CA  . GLY B 1 124 ? -7.907  47.171  30.029  1.00 120.14 ?  123  GLY B CA  1 
ATOM   4441 C  C   . GLY B 1 124 ? -7.765  46.767  28.585  1.00 113.84 ?  123  GLY B C   1 
ATOM   4442 O  O   . GLY B 1 124 ? -8.720  46.223  28.038  1.00 93.27  ?  123  GLY B O   1 
ATOM   4443 N  N   . ASN B 1 125 ? -6.607  46.991  27.951  1.00 139.13 ?  124  ASN B N   1 
ATOM   4444 C  CA  . ASN B 1 125 ? -5.334  47.492  28.524  1.00 131.31 ?  124  ASN B CA  1 
ATOM   4445 C  C   . ASN B 1 125 ? -4.823  46.718  29.747  1.00 111.92 ?  124  ASN B C   1 
ATOM   4446 O  O   . ASN B 1 125 ? -4.805  47.230  30.866  1.00 103.99 ?  124  ASN B O   1 
ATOM   4447 C  CB  . ASN B 1 125 ? -5.437  48.990  28.870  1.00 128.66 ?  124  ASN B CB  1 
ATOM   4448 C  CG  . ASN B 1 125 ? -4.078  49.640  29.089  1.00 121.35 ?  124  ASN B CG  1 
ATOM   4449 O  OD1 . ASN B 1 125 ? -3.078  48.959  29.315  1.00 117.88 ?  124  ASN B OD1 1 
ATOM   4450 N  ND2 . ASN B 1 125 ? -4.037  50.966  29.017  1.00 121.70 ?  124  ASN B ND2 1 
ATOM   4451 N  N   . GLY B 1 126 ? -4.418  45.477  29.508  1.00 102.20 ?  125  GLY B N   1 
ATOM   4452 C  CA  . GLY B 1 126 ? -3.728  44.685  30.502  1.00 87.06  ?  125  GLY B CA  1 
ATOM   4453 C  C   . GLY B 1 126 ? -2.311  45.165  30.759  1.00 90.89  ?  125  GLY B C   1 
ATOM   4454 O  O   . GLY B 1 126 ? -1.811  45.076  31.885  1.00 88.46  ?  125  GLY B O   1 
ATOM   4455 N  N   . ASP B 1 127 ? -1.666  45.667  29.706  1.00 96.77  ?  126  ASP B N   1 
ATOM   4456 C  CA  . ASP B 1 127 ? -0.247  46.034  29.741  1.00 107.16 ?  126  ASP B CA  1 
ATOM   4457 C  C   . ASP B 1 127 ? 0.083   47.083  30.796  1.00 116.94 ?  126  ASP B C   1 
ATOM   4458 O  O   . ASP B 1 127 ? 1.154   47.046  31.410  1.00 103.60 ?  126  ASP B O   1 
ATOM   4459 C  CB  . ASP B 1 127 ? 0.191   46.538  28.367  1.00 111.16 ?  126  ASP B CB  1 
ATOM   4460 C  CG  . ASP B 1 127 ? -0.363  45.698  27.236  1.00 110.07 ?  126  ASP B CG  1 
ATOM   4461 O  OD1 . ASP B 1 127 ? -1.569  45.836  26.933  1.00 88.08  -1 126  ASP B OD1 1 
ATOM   4462 O  OD2 . ASP B 1 127 ? 0.407   44.903  26.651  1.00 116.08 ?  126  ASP B OD2 1 
ATOM   4463 N  N   . TYR B 1 128 ? -0.837  48.020  30.997  1.00 124.83 ?  127  TYR B N   1 
ATOM   4464 C  CA  . TYR B 1 128 ? -0.666  49.037  32.024  1.00 127.47 ?  127  TYR B CA  1 
ATOM   4465 C  C   . TYR B 1 128 ? -0.787  48.394  33.394  1.00 120.86 ?  127  TYR B C   1 
ATOM   4466 O  O   . TYR B 1 128 ? 0.043   48.622  34.273  1.00 128.22 ?  127  TYR B O   1 
ATOM   4467 C  CB  . TYR B 1 128 ? -1.698  50.149  31.854  1.00 129.80 ?  127  TYR B CB  1 
ATOM   4468 C  CG  . TYR B 1 128 ? -1.821  51.073  33.040  1.00 131.68 ?  127  TYR B CG  1 
ATOM   4469 C  CD1 . TYR B 1 128 ? -0.810  51.970  33.357  1.00 149.07 ?  127  TYR B CD1 1 
ATOM   4470 C  CD2 . TYR B 1 128 ? -2.955  51.056  33.835  1.00 121.30 ?  127  TYR B CD2 1 
ATOM   4471 C  CE1 . TYR B 1 128 ? -0.925  52.822  34.441  1.00 155.45 ?  127  TYR B CE1 1 
ATOM   4472 C  CE2 . TYR B 1 128 ? -3.080  51.901  34.920  1.00 133.51 ?  127  TYR B CE2 1 
ATOM   4473 C  CZ  . TYR B 1 128 ? -2.063  52.784  35.219  1.00 147.83 ?  127  TYR B CZ  1 
ATOM   4474 O  OH  . TYR B 1 128 ? -2.180  53.630  36.299  1.00 150.13 ?  127  TYR B OH  1 
ATOM   4475 N  N   . ALA B 1 129 ? -1.807  47.552  33.544  1.00 113.12 ?  128  ALA B N   1 
ATOM   4476 C  CA  . ALA B 1 129 ? -2.078  46.851  34.794  1.00 107.49 ?  128  ALA B CA  1 
ATOM   4477 C  C   . ALA B 1 129 ? -0.868  46.027  35.225  1.00 111.64 ?  128  ALA B C   1 
ATOM   4478 O  O   . ALA B 1 129 ? -0.538  45.962  36.410  1.00 121.43 ?  128  ALA B O   1 
ATOM   4479 C  CB  . ALA B 1 129 ? -3.306  45.965  34.645  1.00 90.01  ?  128  ALA B CB  1 
ATOM   4480 N  N   . PHE B 1 130 ? -0.230  45.384  34.253  1.00 80.11  ?  129  PHE B N   1 
ATOM   4481 C  CA  . PHE B 1 130 ? 0.998   44.634  34.483  1.00 102.12 ?  129  PHE B CA  1 
ATOM   4482 C  C   . PHE B 1 130 ? 2.121   45.581  34.922  1.00 125.23 ?  129  PHE B C   1 
ATOM   4483 O  O   . PHE B 1 130 ? 2.890   45.265  35.833  1.00 142.90 ?  129  PHE B O   1 
ATOM   4484 C  CB  . PHE B 1 130 ? 1.392   43.858  33.225  1.00 92.44  ?  129  PHE B CB  1 
ATOM   4485 C  CG  . PHE B 1 130 ? 2.463   42.814  33.449  1.00 104.38 ?  129  PHE B CG  1 
ATOM   4486 C  CD1 . PHE B 1 130 ? 2.910   42.502  34.725  1.00 126.71 ?  129  PHE B CD1 1 
ATOM   4487 C  CD2 . PHE B 1 130 ? 3.024   42.145  32.373  1.00 112.58 ?  129  PHE B CD2 1 
ATOM   4488 C  CE1 . PHE B 1 130 ? 3.898   41.548  34.921  1.00 129.59 ?  129  PHE B CE1 1 
ATOM   4489 C  CE2 . PHE B 1 130 ? 4.010   41.189  32.561  1.00 118.96 ?  129  PHE B CE2 1 
ATOM   4490 C  CZ  . PHE B 1 130 ? 4.446   40.890  33.840  1.00 122.43 ?  129  PHE B CZ  1 
ATOM   4491 N  N   . LYS B 1 131 ? 2.231   46.725  34.249  1.00 120.76 ?  130  LYS B N   1 
ATOM   4492 C  CA  . LYS B 1 131 ? 3.340   47.649  34.472  1.00 122.47 ?  130  LYS B CA  1 
ATOM   4493 C  C   . LYS B 1 131 ? 3.345   48.246  35.882  1.00 124.91 ?  130  LYS B C   1 
ATOM   4494 O  O   . LYS B 1 131 ? 4.405   48.413  36.488  1.00 129.83 ?  130  LYS B O   1 
ATOM   4495 C  CB  . LYS B 1 131 ? 3.300   48.780  33.444  1.00 125.62 ?  130  LYS B CB  1 
ATOM   4496 C  CG  . LYS B 1 131 ? 4.621   49.522  33.298  1.00 139.17 ?  130  LYS B CG  1 
ATOM   4497 C  CD  . LYS B 1 131 ? 5.667   48.598  32.698  1.00 141.10 ?  130  LYS B CD  1 
ATOM   4498 C  CE  . LYS B 1 131 ? 6.985   49.303  32.430  1.00 146.17 ?  130  LYS B CE  1 
ATOM   4499 N  NZ  . LYS B 1 131 ? 7.961   48.354  31.824  1.00 145.20 1  130  LYS B NZ  1 
ATOM   4500 N  N   . VAL B 1 132 ? 2.164   48.573  36.398  1.00 116.23 ?  131  VAL B N   1 
ATOM   4501 C  CA  . VAL B 1 132 ? 2.053   49.145  37.739  1.00 125.98 ?  131  VAL B CA  1 
ATOM   4502 C  C   . VAL B 1 132 ? 2.464   48.131  38.807  1.00 130.98 ?  131  VAL B C   1 
ATOM   4503 O  O   . VAL B 1 132 ? 3.009   48.495  39.850  1.00 136.93 ?  131  VAL B O   1 
ATOM   4504 C  CB  . VAL B 1 132 ? 0.629   49.651  38.036  1.00 118.89 ?  131  VAL B CB  1 
ATOM   4505 C  CG1 . VAL B 1 132 ? 0.660   50.635  39.192  1.00 133.37 ?  131  VAL B CG1 1 
ATOM   4506 C  CG2 . VAL B 1 132 ? 0.050   50.336  36.825  1.00 109.45 ?  131  VAL B CG2 1 
ATOM   4507 N  N   . VAL B 1 133 ? 2.191   46.859  38.543  1.00 122.02 ?  132  VAL B N   1 
ATOM   4508 C  CA  . VAL B 1 133 ? 2.552   45.795  39.467  1.00 110.73 ?  132  VAL B CA  1 
ATOM   4509 C  C   . VAL B 1 133 ? 4.070   45.666  39.566  1.00 111.09 ?  132  VAL B C   1 
ATOM   4510 O  O   . VAL B 1 133 ? 4.615   45.515  40.661  1.00 122.38 ?  132  VAL B O   1 
ATOM   4511 C  CB  . VAL B 1 133 ? 1.947   44.441  39.032  1.00 111.70 ?  132  VAL B CB  1 
ATOM   4512 C  CG1 . VAL B 1 133 ? 2.432   43.316  39.937  1.00 106.84 ?  132  VAL B CG1 1 
ATOM   4513 C  CG2 . VAL B 1 133 ? 0.432   44.512  39.033  1.00 114.01 ?  132  VAL B CG2 1 
ATOM   4514 N  N   . LYS B 1 134 ? 4.753   45.723  38.425  1.00 110.48 ?  133  LYS B N   1 
ATOM   4515 C  CA  . LYS B 1 134 ? 6.212   45.650  38.412  1.00 123.24 ?  133  LYS B CA  1 
ATOM   4516 C  C   . LYS B 1 134 ? 6.851   46.849  39.109  1.00 144.74 ?  133  LYS B C   1 
ATOM   4517 O  O   . LYS B 1 134 ? 7.812   46.693  39.864  1.00 153.42 ?  133  LYS B O   1 
ATOM   4518 C  CB  . LYS B 1 134 ? 6.744   45.537  36.983  1.00 123.85 ?  133  LYS B CB  1 
ATOM   4519 C  CG  . LYS B 1 134 ? 6.078   44.464  36.140  1.00 111.54 ?  133  LYS B CG  1 
ATOM   4520 C  CD  . LYS B 1 134 ? 6.903   44.185  34.893  1.00 117.93 ?  133  LYS B CD  1 
ATOM   4521 C  CE  . LYS B 1 134 ? 8.372   43.979  35.272  1.00 130.10 ?  133  LYS B CE  1 
ATOM   4522 N  NZ  . LYS B 1 134 ? 9.292   44.062  34.104  1.00 136.56 1  133  LYS B NZ  1 
ATOM   4523 N  N   . GLU B 1 135 ? 6.325   48.042  38.843  1.00 154.53 ?  134  GLU B N   1 
ATOM   4524 C  CA  . GLU B 1 135 ? 6.823   49.248  39.493  1.00 160.53 ?  134  GLU B CA  1 
ATOM   4525 C  C   . GLU B 1 135 ? 6.640   49.192  40.992  1.00 144.93 ?  134  GLU B C   1 
ATOM   4526 O  O   . GLU B 1 135 ? 7.456   49.720  41.739  1.00 141.87 ?  134  GLU B O   1 
ATOM   4527 C  CB  . GLU B 1 135 ? 6.123   50.507  38.978  1.00 171.53 ?  134  GLU B CB  1 
ATOM   4528 C  CG  . GLU B 1 135 ? 6.629   51.059  37.666  1.00 183.36 ?  134  GLU B CG  1 
ATOM   4529 C  CD  . GLU B 1 135 ? 6.128   52.466  37.418  1.00 192.23 ?  134  GLU B CD  1 
ATOM   4530 O  OE1 . GLU B 1 135 ? 5.046   52.807  37.937  1.00 193.52 ?  134  GLU B OE1 1 
ATOM   4531 O  OE2 . GLU B 1 135 ? 6.816   53.231  36.708  1.00 196.90 -1 134  GLU B OE2 1 
ATOM   4532 N  N   . PHE B 1 136 ? 5.561   48.563  41.432  1.00 136.35 ?  135  PHE B N   1 
ATOM   4533 C  CA  . PHE B 1 136 ? 5.323   48.456  42.855  1.00 135.86 ?  135  PHE B CA  1 
ATOM   4534 C  C   . PHE B 1 136 ? 6.288   47.486  43.537  1.00 137.92 ?  135  PHE B C   1 
ATOM   4535 O  O   . PHE B 1 136 ? 6.861   47.812  44.575  1.00 141.09 ?  135  PHE B O   1 
ATOM   4536 C  CB  . PHE B 1 136 ? 3.884   48.046  43.136  1.00 146.10 ?  135  PHE B CB  1 
ATOM   4537 C  CG  . PHE B 1 136 ? 3.526   48.159  44.574  1.00 163.42 ?  135  PHE B CG  1 
ATOM   4538 C  CD1 . PHE B 1 136 ? 3.345   49.401  45.144  1.00 178.41 ?  135  PHE B CD1 1 
ATOM   4539 C  CD2 . PHE B 1 136 ? 3.409   47.037  45.369  1.00 163.09 ?  135  PHE B CD2 1 
ATOM   4540 C  CE1 . PHE B 1 136 ? 3.039   49.521  46.470  1.00 181.42 ?  135  PHE B CE1 1 
ATOM   4541 C  CE2 . PHE B 1 136 ? 3.098   47.161  46.693  1.00 171.04 ?  135  PHE B CE2 1 
ATOM   4542 C  CZ  . PHE B 1 136 ? 2.926   48.407  47.249  1.00 178.14 ?  135  PHE B CZ  1 
ATOM   4543 N  N   . VAL B 1 137 ? 6.475   46.302  42.959  1.00 135.03 ?  136  VAL B N   1 
ATOM   4544 C  CA  . VAL B 1 137 ? 7.349   45.293  43.564  1.00 139.53 ?  136  VAL B CA  1 
ATOM   4545 C  C   . VAL B 1 137 ? 8.794   45.810  43.578  1.00 142.79 ?  136  VAL B C   1 
ATOM   4546 O  O   . VAL B 1 137 ? 9.631   45.336  44.350  1.00 140.70 ?  136  VAL B O   1 
ATOM   4547 C  CB  . VAL B 1 137 ? 7.265   43.931  42.824  1.00 121.49 ?  136  VAL B CB  1 
ATOM   4548 C  CG1 . VAL B 1 137 ? 7.927   44.016  41.458  1.00 124.12 ?  136  VAL B CG1 1 
ATOM   4549 C  CG2 . VAL B 1 137 ? 7.898   42.823  43.653  1.00 119.59 ?  136  VAL B CG2 1 
ATOM   4550 N  N   . SER B 1 138 ? 9.066   46.790  42.720  1.00 142.64 ?  137  SER B N   1 
ATOM   4551 C  CA  . SER B 1 138 ? 10.360  47.464  42.655  1.00 151.91 ?  137  SER B CA  1 
ATOM   4552 C  C   . SER B 1 138 ? 10.678  48.225  43.949  1.00 154.66 ?  137  SER B C   1 
ATOM   4553 O  O   . SER B 1 138 ? 11.837  48.314  44.355  1.00 156.17 ?  137  SER B O   1 
ATOM   4554 C  CB  . SER B 1 138 ? 10.398  48.412  41.458  1.00 152.64 ?  137  SER B CB  1 
ATOM   4555 O  OG  . SER B 1 138 ? 9.802   47.811  40.321  1.00 152.69 ?  137  SER B OG  1 
ATOM   4556 N  N   . VAL B 1 139 ? 9.651   48.810  44.561  1.00 158.32 ?  138  VAL B N   1 
ATOM   4557 C  CA  . VAL B 1 139 ? 9.812   49.578  45.795  1.00 168.41 ?  138  VAL B CA  1 
ATOM   4558 C  C   . VAL B 1 139 ? 10.377  48.711  46.924  1.00 181.37 ?  138  VAL B C   1 
ATOM   4559 O  O   . VAL B 1 139 ? 11.453  48.992  47.458  1.00 195.80 ?  138  VAL B O   1 
ATOM   4560 C  CB  . VAL B 1 139 ? 8.467   50.194  46.250  1.00 157.08 ?  138  VAL B CB  1 
ATOM   4561 C  CG1 . VAL B 1 139 ? 8.617   50.882  47.603  1.00 167.48 ?  138  VAL B CG1 1 
ATOM   4562 C  CG2 . VAL B 1 139 ? 7.943   51.160  45.200  1.00 140.95 ?  138  VAL B CG2 1 
ATOM   4563 N  N   . GLY B 1 140 ? 9.644   47.660  47.281  1.00 189.36 ?  139  GLY B N   1 
ATOM   4564 C  CA  . GLY B 1 140 ? 10.131  46.656  48.212  1.00 174.21 ?  139  GLY B CA  1 
ATOM   4565 C  C   . GLY B 1 140 ? 10.155  47.051  49.676  1.00 171.66 ?  139  GLY B C   1 
ATOM   4566 O  O   . GLY B 1 140 ? 10.338  46.194  50.544  1.00 157.31 ?  139  GLY B O   1 
ATOM   4567 N  N   . GLY B 1 141 ? 9.955   48.335  49.958  1.00 190.43 ?  140  GLY B N   1 
ATOM   4568 C  CA  . GLY B 1 141 ? 9.976   48.818  51.327  1.00 194.52 ?  140  GLY B CA  1 
ATOM   4569 C  C   . GLY B 1 141 ? 8.791   48.272  52.092  1.00 184.01 ?  140  GLY B C   1 
ATOM   4570 O  O   . GLY B 1 141 ? 8.941   47.659  53.148  1.00 189.16 ?  140  GLY B O   1 
ATOM   4571 N  N   . VAL B 1 142 ? 7.603   48.496  51.545  1.00 173.48 ?  141  VAL B N   1 
ATOM   4572 C  CA  . VAL B 1 142 ? 6.386   47.890  52.065  1.00 169.15 ?  141  VAL B CA  1 
ATOM   4573 C  C   . VAL B 1 142 ? 5.632   47.357  50.857  1.00 166.71 ?  141  VAL B C   1 
ATOM   4574 O  O   . VAL B 1 142 ? 4.435   47.595  50.694  1.00 162.60 ?  141  VAL B O   1 
ATOM   4575 C  CB  . VAL B 1 142 ? 5.501   48.887  52.858  1.00 171.29 ?  141  VAL B CB  1 
ATOM   4576 C  CG1 . VAL B 1 142 ? 4.453   48.136  53.678  1.00 167.07 ?  141  VAL B CG1 1 
ATOM   4577 C  CG2 . VAL B 1 142 ? 6.347   49.756  53.777  1.00 177.57 ?  141  VAL B CG2 1 
ATOM   4578 N  N   . SER B 1 143 ? 6.352   46.652  49.990  1.00 165.82 ?  142  SER B N   1 
ATOM   4579 C  CA  . SER B 1 143 ? 5.746   46.134  48.776  1.00 159.51 ?  142  SER B CA  1 
ATOM   4580 C  C   . SER B 1 143 ? 4.681   45.107  49.135  1.00 188.36 ?  142  SER B C   1 
ATOM   4581 O  O   . SER B 1 143 ? 3.518   45.266  48.765  1.00 193.55 ?  142  SER B O   1 
ATOM   4582 C  CB  . SER B 1 143 ? 6.802   45.513  47.855  1.00 149.54 ?  142  SER B CB  1 
ATOM   4583 O  OG  . SER B 1 143 ? 7.468   44.433  48.486  1.00 146.74 ?  142  SER B OG  1 
ATOM   4584 N  N   . ILE B 1 144 ? 5.072   44.085  49.893  1.00 215.31 ?  143  ILE B N   1 
ATOM   4585 C  CA  . ILE B 1 144 ? 4.149   43.022  50.269  1.00 208.63 ?  143  ILE B CA  1 
ATOM   4586 C  C   . ILE B 1 144 ? 3.443   42.525  49.009  1.00 199.82 ?  143  ILE B C   1 
ATOM   4587 O  O   . ILE B 1 144 ? 2.213   42.557  48.938  1.00 199.61 ?  143  ILE B O   1 
ATOM   4588 C  CB  . ILE B 1 144 ? 3.105   43.498  51.315  1.00 205.18 ?  143  ILE B CB  1 
ATOM   4589 C  CG1 . ILE B 1 144 ? 3.755   44.396  52.372  1.00 211.86 ?  143  ILE B CG1 1 
ATOM   4590 C  CG2 . ILE B 1 144 ? 2.398   42.313  51.966  1.00 200.00 ?  143  ILE B CG2 1 
ATOM   4591 C  CD1 . ILE B 1 144 ? 4.669   43.658  53.335  1.00 211.70 ?  143  ILE B CD1 1 
ATOM   4592 N  N   . PRO B 1 145 ? 4.219   42.121  47.986  1.00 190.91 ?  144  PRO B N   1 
ATOM   4593 C  CA  . PRO B 1 145 ? 3.609   41.852  46.681  1.00 172.74 ?  144  PRO B CA  1 
ATOM   4594 C  C   . PRO B 1 145 ? 2.579   40.735  46.782  1.00 166.90 ?  144  PRO B C   1 
ATOM   4595 O  O   . PRO B 1 145 ? 2.927   39.589  47.053  1.00 172.30 ?  144  PRO B O   1 
ATOM   4596 C  CB  . PRO B 1 145 ? 4.805   41.440  45.824  1.00 171.82 ?  144  PRO B CB  1 
ATOM   4597 C  CG  . PRO B 1 145 ? 5.749   40.823  46.803  1.00 188.95 ?  144  PRO B CG  1 
ATOM   4598 C  CD  . PRO B 1 145 ? 5.636   41.711  48.012  1.00 194.15 ?  144  PRO B CD  1 
ATOM   4599 N  N   . ARG B 1 146 ? 1.316   41.085  46.569  1.00 145.05 ?  145  ARG B N   1 
ATOM   4600 C  CA  . ARG B 1 146 ? 0.210   40.156  46.768  1.00 136.53 ?  145  ARG B CA  1 
ATOM   4601 C  C   . ARG B 1 146 ? -0.197  39.454  45.476  1.00 139.85 ?  145  ARG B C   1 
ATOM   4602 O  O   . ARG B 1 146 ? -0.065  40.014  44.389  1.00 144.08 ?  145  ARG B O   1 
ATOM   4603 C  CB  . ARG B 1 146 ? -0.992  40.909  47.352  1.00 144.97 ?  145  ARG B CB  1 
ATOM   4604 C  CG  . ARG B 1 146 ? -2.116  40.037  47.878  1.00 144.62 ?  145  ARG B CG  1 
ATOM   4605 C  CD  . ARG B 1 146 ? -1.949  39.736  49.363  1.00 144.72 ?  145  ARG B CD  1 
ATOM   4606 N  NE  . ARG B 1 146 ? -2.103  40.929  50.195  1.00 152.10 ?  145  ARG B NE  1 
ATOM   4607 C  CZ  . ARG B 1 146 ? -3.228  41.270  50.818  1.00 157.79 ?  145  ARG B CZ  1 
ATOM   4608 N  NH1 . ARG B 1 146 ? -4.308  40.507  50.710  1.00 158.88 ?  145  ARG B NH1 1 
ATOM   4609 N  NH2 . ARG B 1 146 ? -3.273  42.374  51.552  1.00 159.17 ?  145  ARG B NH2 1 
ATOM   4610 N  N   . LEU B 1 147 ? -0.664  38.213  45.599  1.00 147.80 ?  146  LEU B N   1 
ATOM   4611 C  CA  . LEU B 1 147 ? -1.207  37.473  44.462  1.00 161.45 ?  146  LEU B CA  1 
ATOM   4612 C  C   . LEU B 1 147 ? -2.334  38.289  43.845  1.00 157.60 ?  146  LEU B C   1 
ATOM   4613 O  O   . LEU B 1 147 ? -2.524  38.313  42.630  1.00 155.14 ?  146  LEU B O   1 
ATOM   4614 C  CB  . LEU B 1 147 ? -1.705  36.086  44.889  1.00 177.51 ?  146  LEU B CB  1 
ATOM   4615 C  CG  . LEU B 1 147 ? -2.792  35.949  45.958  1.00 190.04 ?  146  LEU B CG  1 
ATOM   4616 C  CD1 . LEU B 1 147 ? -4.176  35.806  45.332  1.00 187.03 ?  146  LEU B CD1 1 
ATOM   4617 C  CD2 . LEU B 1 147 ? -2.483  34.771  46.869  1.00 200.26 ?  146  LEU B CD2 1 
ATOM   4618 N  N   . ARG B 1 148 ? -3.083  38.949  44.721  1.00 147.54 ?  147  ARG B N   1 
ATOM   4619 C  CA  . ARG B 1 148 ? -4.218  39.779  44.353  1.00 131.50 ?  147  ARG B CA  1 
ATOM   4620 C  C   . ARG B 1 148 ? -3.805  40.953  43.459  1.00 121.14 ?  147  ARG B C   1 
ATOM   4621 O  O   . ARG B 1 148 ? -4.577  41.401  42.615  1.00 111.12 ?  147  ARG B O   1 
ATOM   4622 C  CB  . ARG B 1 148 ? -4.906  40.273  45.630  1.00 135.30 ?  147  ARG B CB  1 
ATOM   4623 C  CG  . ARG B 1 148 ? -6.051  41.230  45.429  1.00 130.60 ?  147  ARG B CG  1 
ATOM   4624 C  CD  . ARG B 1 148 ? -5.765  42.551  46.112  1.00 115.47 ?  147  ARG B CD  1 
ATOM   4625 N  NE  . ARG B 1 148 ? -5.916  42.495  47.559  1.00 103.27 ?  147  ARG B NE  1 
ATOM   4626 C  CZ  . ARG B 1 148 ? -5.279  43.303  48.399  1.00 107.93 ?  147  ARG B CZ  1 
ATOM   4627 N  NH1 . ARG B 1 148 ? -4.437  44.215  47.932  1.00 111.55 ?  147  ARG B NH1 1 
ATOM   4628 N  NH2 . ARG B 1 148 ? -5.474  43.194  49.704  1.00 116.08 ?  147  ARG B NH2 1 
ATOM   4629 N  N   . THR B 1 149 ? -2.583  41.444  43.645  1.00 129.08 ?  148  THR B N   1 
ATOM   4630 C  CA  . THR B 1 149 ? -2.033  42.499  42.789  1.00 125.75 ?  148  THR B CA  1 
ATOM   4631 C  C   . THR B 1 149 ? -1.740  42.025  41.357  1.00 115.82 ?  148  THR B C   1 
ATOM   4632 O  O   . THR B 1 149 ? -2.184  42.634  40.383  1.00 110.25 ?  148  THR B O   1 
ATOM   4633 C  CB  . THR B 1 149 ? -0.737  43.089  43.403  1.00 91.58  ?  148  THR B CB  1 
ATOM   4634 O  OG1 . THR B 1 149 ? -1.038  43.718  44.656  1.00 100.95 ?  148  THR B OG1 1 
ATOM   4635 C  CG2 . THR B 1 149 ? -0.118  44.112  42.476  1.00 88.29  ?  148  THR B CG2 1 
ATOM   4636 N  N   . TYR B 1 150 ? -0.981  40.938  41.246  1.00 115.62 ?  149  TYR B N   1 
ATOM   4637 C  CA  . TYR B 1 150 ? -0.680  40.304  39.966  1.00 103.28 ?  149  TYR B CA  1 
ATOM   4638 C  C   . TYR B 1 150 ? -1.920  39.784  39.231  1.00 101.43 ?  149  TYR B C   1 
ATOM   4639 O  O   . TYR B 1 150 ? -1.889  39.598  38.017  1.00 71.11  ?  149  TYR B O   1 
ATOM   4640 C  CB  . TYR B 1 150 ? 0.312   39.155  40.170  1.00 110.20 ?  149  TYR B CB  1 
ATOM   4641 C  CG  . TYR B 1 150 ? 1.772   39.551  40.130  1.00 128.10 ?  149  TYR B CG  1 
ATOM   4642 C  CD1 . TYR B 1 150 ? 2.458   39.616  38.924  1.00 139.16 ?  149  TYR B CD1 1 
ATOM   4643 C  CD2 . TYR B 1 150 ? 2.472   39.840  41.295  1.00 135.14 ?  149  TYR B CD2 1 
ATOM   4644 C  CE1 . TYR B 1 150 ? 3.799   39.968  38.879  1.00 141.82 ?  149  TYR B CE1 1 
ATOM   4645 C  CE2 . TYR B 1 150 ? 3.816   40.193  41.260  1.00 132.04 ?  149  TYR B CE2 1 
ATOM   4646 C  CZ  . TYR B 1 150 ? 4.472   40.256  40.050  1.00 129.99 ?  149  TYR B CZ  1 
ATOM   4647 O  OH  . TYR B 1 150 ? 5.804   40.606  40.013  1.00 114.51 ?  149  TYR B OH  1 
ATOM   4648 N  N   . ALA B 1 151 ? -2.994  39.519  39.972  1.00 117.75 ?  150  ALA B N   1 
ATOM   4649 C  CA  . ALA B 1 151 ? -4.161  38.816  39.426  1.00 118.31 ?  150  ALA B CA  1 
ATOM   4650 C  C   . ALA B 1 151 ? -4.882  39.526  38.262  1.00 121.26 ?  150  ALA B C   1 
ATOM   4651 O  O   . ALA B 1 151 ? -5.040  38.924  37.201  1.00 134.42 ?  150  ALA B O   1 
ATOM   4652 C  CB  . ALA B 1 151 ? -5.166  38.511  40.553  1.00 117.70 ?  150  ALA B CB  1 
ATOM   4653 N  N   . PRO B 1 152 ? -5.321  40.792  38.441  1.00 106.70 ?  151  PRO B N   1 
ATOM   4654 C  CA  . PRO B 1 152 ? -6.096  41.417  37.358  1.00 101.95 ?  151  PRO B CA  1 
ATOM   4655 C  C   . PRO B 1 152 ? -5.302  41.624  36.063  1.00 96.59  ?  151  PRO B C   1 
ATOM   4656 O  O   . PRO B 1 152 ? -5.891  41.608  34.980  1.00 81.26  ?  151  PRO B O   1 
ATOM   4657 C  CB  . PRO B 1 152 ? -6.512  42.762  37.958  1.00 111.49 ?  151  PRO B CB  1 
ATOM   4658 C  CG  . PRO B 1 152 ? -5.453  43.067  38.943  1.00 115.97 ?  151  PRO B CG  1 
ATOM   4659 C  CD  . PRO B 1 152 ? -5.072  41.745  39.539  1.00 112.67 ?  151  PRO B CD  1 
ATOM   4660 N  N   . ALA B 1 153 ? -3.995  41.844  36.181  1.00 95.63  ?  152  ALA B N   1 
ATOM   4661 C  CA  . ALA B 1 153 ? -3.132  41.998  35.012  1.00 93.10  ?  152  ALA B CA  1 
ATOM   4662 C  C   . ALA B 1 153 ? -3.153  40.735  34.157  1.00 97.14  ?  152  ALA B C   1 
ATOM   4663 O  O   . ALA B 1 153 ? -3.333  40.798  32.942  1.00 72.04  ?  152  ALA B O   1 
ATOM   4664 C  CB  . ALA B 1 153 ? -1.713  42.326  35.436  1.00 99.58  ?  152  ALA B CB  1 
ATOM   4665 N  N   . LEU B 1 154 ? -2.959  39.591  34.805  1.00 112.10 ?  153  LEU B N   1 
ATOM   4666 C  CA  . LEU B 1 154 ? -2.998  38.297  34.135  1.00 107.85 ?  153  LEU B CA  1 
ATOM   4667 C  C   . LEU B 1 154 ? -4.396  37.962  33.633  1.00 105.26 ?  153  LEU B C   1 
ATOM   4668 O  O   . LEU B 1 154 ? -4.566  37.503  32.504  1.00 101.37 ?  153  LEU B O   1 
ATOM   4669 C  CB  . LEU B 1 154 ? -2.508  37.199  35.085  1.00 96.50  ?  153  LEU B CB  1 
ATOM   4670 C  CG  . LEU B 1 154 ? -2.539  35.751  34.597  1.00 79.22  ?  153  LEU B CG  1 
ATOM   4671 C  CD1 . LEU B 1 154 ? -1.294  35.008  35.038  1.00 77.54  ?  153  LEU B CD1 1 
ATOM   4672 C  CD2 . LEU B 1 154 ? -3.781  35.077  35.147  1.00 67.09  ?  153  LEU B CD2 1 
ATOM   4673 N  N   . LEU B 1 155 ? -5.392  38.206  34.480  1.00 101.90 ?  154  LEU B N   1 
ATOM   4674 C  CA  . LEU B 1 155 ? -6.776  37.859  34.176  1.00 90.58  ?  154  LEU B CA  1 
ATOM   4675 C  C   . LEU B 1 155 ? -7.280  38.585  32.943  1.00 91.50  ?  154  LEU B C   1 
ATOM   4676 O  O   . LEU B 1 155 ? -7.953  37.996  32.100  1.00 100.17 ?  154  LEU B O   1 
ATOM   4677 C  CB  . LEU B 1 155 ? -7.685  38.177  35.361  1.00 83.48  ?  154  LEU B CB  1 
ATOM   4678 C  CG  . LEU B 1 155 ? -7.833  37.071  36.402  1.00 82.43  ?  154  LEU B CG  1 
ATOM   4679 C  CD1 . LEU B 1 155 ? -8.964  37.392  37.363  1.00 89.22  ?  154  LEU B CD1 1 
ATOM   4680 C  CD2 . LEU B 1 155 ? -8.079  35.750  35.720  1.00 78.28  ?  154  LEU B CD2 1 
ATOM   4681 N  N   . CYS B 1 156 ? -6.946  39.865  32.842  1.00 100.86 ?  155  CYS B N   1 
ATOM   4682 C  CA  . CYS B 1 156 ? -7.343  40.665  31.694  1.00 107.67 ?  155  CYS B CA  1 
ATOM   4683 C  C   . CYS B 1 156 ? -6.665  40.151  30.436  1.00 70.89  ?  155  CYS B C   1 
ATOM   4684 O  O   . CYS B 1 156 ? -7.308  39.957  29.416  1.00 71.56  ?  155  CYS B O   1 
ATOM   4685 C  CB  . CYS B 1 156 ? -6.987  42.131  31.921  1.00 132.96 ?  155  CYS B CB  1 
ATOM   4686 S  SG  . CYS B 1 156 ? -7.601  43.251  30.659  1.00 94.02  ?  155  CYS B SG  1 
ATOM   4687 N  N   . PHE B 1 157 ? -5.364  39.899  30.537  1.00 71.55  ?  156  PHE B N   1 
ATOM   4688 C  CA  . PHE B 1 157 ? -4.574  39.334  29.442  1.00 96.16  ?  156  PHE B CA  1 
ATOM   4689 C  C   . PHE B 1 157 ? -5.072  37.973  28.979  1.00 95.18  ?  156  PHE B C   1 
ATOM   4690 O  O   . PHE B 1 157 ? -4.899  37.602  27.819  1.00 88.61  ?  156  PHE B O   1 
ATOM   4691 C  CB  . PHE B 1 157 ? -3.104  39.231  29.855  1.00 103.20 ?  156  PHE B CB  1 
ATOM   4692 C  CG  . PHE B 1 157 ? -2.294  40.459  29.542  1.00 115.99 ?  156  PHE B CG  1 
ATOM   4693 C  CD1 . PHE B 1 157 ? -2.727  41.365  28.581  1.00 132.42 ?  156  PHE B CD1 1 
ATOM   4694 C  CD2 . PHE B 1 157 ? -1.111  40.719  30.219  1.00 109.45 ?  156  PHE B CD2 1 
ATOM   4695 C  CE1 . PHE B 1 157 ? -1.980  42.490  28.279  1.00 135.24 ?  156  PHE B CE1 1 
ATOM   4696 C  CE2 . PHE B 1 157 ? -0.359  41.843  29.924  1.00 117.22 ?  156  PHE B CE2 1 
ATOM   4697 C  CZ  . PHE B 1 157 ? -0.795  42.729  28.952  1.00 129.34 ?  156  PHE B CZ  1 
ATOM   4698 N  N   . CYS B 1 158 ? -5.642  37.208  29.901  1.00 110.93 ?  157  CYS B N   1 
ATOM   4699 C  CA  . CYS B 1 158 ? -6.222  35.913  29.569  1.00 112.66 ?  157  CYS B CA  1 
ATOM   4700 C  C   . CYS B 1 158 ? -7.547  36.044  28.811  1.00 108.89 ?  157  CYS B C   1 
ATOM   4701 O  O   . CYS B 1 158 ? -7.784  35.351  27.819  1.00 98.62  ?  157  CYS B O   1 
ATOM   4702 C  CB  . CYS B 1 158 ? -6.395  35.078  30.834  1.00 67.99  ?  157  CYS B CB  1 
ATOM   4703 S  SG  . CYS B 1 158 ? -4.884  34.164  31.226  1.00 106.94 ?  157  CYS B SG  1 
ATOM   4704 N  N   . GLU B 1 159 ? -8.413  36.927  29.294  1.00 116.86 ?  158  GLU B N   1 
ATOM   4705 C  CA  . GLU B 1 159 ? -9.701  37.165  28.657  1.00 99.05  ?  158  GLU B CA  1 
ATOM   4706 C  C   . GLU B 1 159 ? -9.509  37.743  27.254  1.00 102.70 ?  158  GLU B C   1 
ATOM   4707 O  O   . GLU B 1 159 ? -10.270 37.441  26.332  1.00 86.16  ?  158  GLU B O   1 
ATOM   4708 C  CB  . GLU B 1 159 ? -10.545 38.108  29.515  1.00 90.30  ?  158  GLU B CB  1 
ATOM   4709 C  CG  . GLU B 1 159 ? -11.936 38.400  28.980  1.00 122.17 ?  158  GLU B CG  1 
ATOM   4710 C  CD  . GLU B 1 159 ? -12.926 37.287  29.254  1.00 154.60 ?  158  GLU B CD  1 
ATOM   4711 O  OE1 . GLU B 1 159 ? -12.506 36.117  29.377  1.00 170.53 ?  158  GLU B OE1 1 
ATOM   4712 O  OE2 . GLU B 1 159 ? -14.135 37.586  29.341  1.00 172.38 ?  158  GLU B OE2 1 
ATOM   4713 N  N   . LYS B 1 160 ? -8.457  38.544  27.099  1.00 108.58 ?  159  LYS B N   1 
ATOM   4714 C  CA  . LYS B 1 160 ? -8.124  39.191  25.832  1.00 97.17  ?  159  LYS B CA  1 
ATOM   4715 C  C   . LYS B 1 160 ? -7.397  38.209  24.911  1.00 89.37  ?  159  LYS B C   1 
ATOM   4716 O  O   . LYS B 1 160 ? -7.057  38.533  23.773  1.00 108.02 ?  159  LYS B O   1 
ATOM   4717 C  CB  . LYS B 1 160 ? -7.257  40.432  26.097  1.00 108.59 ?  159  LYS B CB  1 
ATOM   4718 C  CG  . LYS B 1 160 ? -7.122  41.409  24.934  1.00 124.72 ?  159  LYS B CG  1 
ATOM   4719 C  CD  . LYS B 1 160 ? -6.029  42.444  25.194  1.00 127.60 ?  159  LYS B CD  1 
ATOM   4720 C  CE  . LYS B 1 160 ? -6.301  43.249  26.455  1.00 117.96 ?  159  LYS B CE  1 
ATOM   4721 N  NZ  . LYS B 1 160 ? -5.222  44.236  26.736  1.00 109.85 ?  159  LYS B NZ  1 
ATOM   4722 N  N   . LEU B 1 161 ? -7.152  37.014  25.437  1.00 89.32  ?  160  LEU B N   1 
ATOM   4723 C  CA  . LEU B 1 161 ? -6.558  35.898  24.702  1.00 90.60  ?  160  LEU B CA  1 
ATOM   4724 C  C   . LEU B 1 161 ? -5.106  36.141  24.307  1.00 95.32  ?  160  LEU B C   1 
ATOM   4725 O  O   . LEU B 1 161 ? -4.576  35.461  23.429  1.00 90.12  ?  160  LEU B O   1 
ATOM   4726 C  CB  . LEU B 1 161 ? -7.381  35.565  23.453  1.00 80.43  ?  160  LEU B CB  1 
ATOM   4727 C  CG  . LEU B 1 161 ? -8.654  34.742  23.663  1.00 82.34  ?  160  LEU B CG  1 
ATOM   4728 C  CD1 . LEU B 1 161 ? -9.145  34.172  22.348  1.00 80.39  ?  160  LEU B CD1 1 
ATOM   4729 C  CD2 . LEU B 1 161 ? -8.429  33.627  24.675  1.00 109.51 ?  160  LEU B CD2 1 
ATOM   4730 N  N   . GLU B 1 162 ? -4.456  37.092  24.968  1.00 115.13 ?  161  GLU B N   1 
ATOM   4731 C  CA  . GLU B 1 162 ? -3.026  37.289  24.777  1.00 116.91 ?  161  GLU B CA  1 
ATOM   4732 C  C   . GLU B 1 162 ? -2.282  36.303  25.662  1.00 113.12 ?  161  GLU B C   1 
ATOM   4733 O  O   . GLU B 1 162 ? -2.049  36.561  26.842  1.00 114.26 ?  161  GLU B O   1 
ATOM   4734 C  CB  . GLU B 1 162 ? -2.620  38.731  25.080  1.00 117.75 ?  161  GLU B CB  1 
ATOM   4735 C  CG  . GLU B 1 162 ? -3.139  39.734  24.060  1.00 132.32 ?  161  GLU B CG  1 
ATOM   4736 C  CD  . GLU B 1 162 ? -2.539  41.115  24.233  1.00 154.61 ?  161  GLU B CD  1 
ATOM   4737 O  OE1 . GLU B 1 162 ? -1.781  41.320  25.203  1.00 158.46 ?  161  GLU B OE1 1 
ATOM   4738 O  OE2 . GLU B 1 162 ? -2.825  41.996  23.394  1.00 164.63 ?  161  GLU B OE2 1 
ATOM   4739 N  N   . ALA B 1 163 ? -1.913  35.171  25.075  1.00 116.79 ?  162  ALA B N   1 
ATOM   4740 C  CA  . ALA B 1 163 ? -1.376  34.045  25.830  1.00 118.03 ?  162  ALA B CA  1 
ATOM   4741 C  C   . ALA B 1 163 ? 0.003   34.336  26.401  1.00 107.31 ?  162  ALA B C   1 
ATOM   4742 O  O   . ALA B 1 163 ? 0.245   34.111  27.581  1.00 95.47  ?  162  ALA B O   1 
ATOM   4743 C  CB  . ALA B 1 163 ? -1.326  32.800  24.957  1.00 129.31 ?  162  ALA B CB  1 
ATOM   4744 N  N   . GLU B 1 164 ? 0.913   34.812  25.558  1.00 111.39 ?  163  GLU B N   1 
ATOM   4745 C  CA  . GLU B 1 164 ? 2.284   35.056  25.992  1.00 108.44 ?  163  GLU B CA  1 
ATOM   4746 C  C   . GLU B 1 164 ? 2.353   36.106  27.094  1.00 107.19 ?  163  GLU B C   1 
ATOM   4747 O  O   . GLU B 1 164 ? 3.236   36.055  27.947  1.00 100.37 ?  163  GLU B O   1 
ATOM   4748 C  CB  . GLU B 1 164 ? 3.159   35.471  24.811  1.00 123.20 ?  163  GLU B CB  1 
ATOM   4749 C  CG  . GLU B 1 164 ? 4.550   34.857  24.852  1.00 138.62 ?  163  GLU B CG  1 
ATOM   4750 C  CD  . GLU B 1 164 ? 4.519   33.348  24.685  1.00 147.27 ?  163  GLU B CD  1 
ATOM   4751 O  OE1 . GLU B 1 164 ? 3.535   32.833  24.114  1.00 156.86 ?  163  GLU B OE1 1 
ATOM   4752 O  OE2 . GLU B 1 164 ? 5.476   32.674  25.122  1.00 148.06 ?  163  GLU B OE2 1 
ATOM   4753 N  N   . LYS B 1 165 ? 1.444   37.076  27.056  1.00 117.80 ?  164  LYS B N   1 
ATOM   4754 C  CA  . LYS B 1 165 ? 1.353   38.070  28.123  1.00 124.24 ?  164  LYS B CA  1 
ATOM   4755 C  C   . LYS B 1 165 ? 0.912   37.457  29.454  1.00 115.46 ?  164  LYS B C   1 
ATOM   4756 O  O   . LYS B 1 165 ? 1.475   37.770  30.498  1.00 130.93 ?  164  LYS B O   1 
ATOM   4757 C  CB  . LYS B 1 165 ? 0.417   39.218  27.727  1.00 133.82 ?  164  LYS B CB  1 
ATOM   4758 C  CG  . LYS B 1 165 ? 1.027   40.268  26.796  1.00 138.08 ?  164  LYS B CG  1 
ATOM   4759 C  CD  . LYS B 1 165 ? 1.314   39.753  25.395  1.00 154.29 ?  164  LYS B CD  1 
ATOM   4760 C  CE  . LYS B 1 165 ? 1.953   40.842  24.548  1.00 163.07 ?  164  LYS B CE  1 
ATOM   4761 N  NZ  . LYS B 1 165 ? 2.331   40.330  23.205  1.00 174.44 ?  164  LYS B NZ  1 
ATOM   4762 N  N   . GLY B 1 166 ? -0.095  36.592  29.414  1.00 100.81 ?  165  GLY B N   1 
ATOM   4763 C  CA  . GLY B 1 166 ? -0.563  35.920  30.614  1.00 91.06  ?  165  GLY B CA  1 
ATOM   4764 C  C   . GLY B 1 166 ? 0.525   35.043  31.217  1.00 91.28  ?  165  GLY B C   1 
ATOM   4765 O  O   . GLY B 1 166 ? 0.676   34.964  32.439  1.00 96.72  ?  165  GLY B O   1 
ATOM   4766 N  N   . TYR B 1 167 ? 1.286   34.389  30.348  1.00 79.69  ?  166  TYR B N   1 
ATOM   4767 C  CA  . TYR B 1 167 ? 2.377   33.516  30.756  1.00 81.73  ?  166  TYR B CA  1 
ATOM   4768 C  C   . TYR B 1 167 ? 3.471   34.350  31.408  1.00 87.55  ?  166  TYR B C   1 
ATOM   4769 O  O   . TYR B 1 167 ? 4.111   33.915  32.363  1.00 101.89 ?  166  TYR B O   1 
ATOM   4770 C  CB  . TYR B 1 167 ? 2.933   32.744  29.555  1.00 98.72  ?  166  TYR B CB  1 
ATOM   4771 C  CG  . TYR B 1 167 ? 1.951   31.779  28.921  1.00 101.56 ?  166  TYR B CG  1 
ATOM   4772 C  CD1 . TYR B 1 167 ? 0.637   31.691  29.369  1.00 99.58  ?  166  TYR B CD1 1 
ATOM   4773 C  CD2 . TYR B 1 167 ? 2.319   31.006  27.830  1.00 104.32 ?  166  TYR B CD2 1 
ATOM   4774 C  CE1 . TYR B 1 167 ? -0.265  30.836  28.778  1.00 96.12  ?  166  TYR B CE1 1 
ATOM   4775 C  CE2 . TYR B 1 167 ? 1.419   30.152  27.226  1.00 95.82  ?  166  TYR B CE2 1 
ATOM   4776 C  CZ  . TYR B 1 167 ? 0.127   30.070  27.707  1.00 88.79  ?  166  TYR B CZ  1 
ATOM   4777 O  OH  . TYR B 1 167 ? -0.782  29.219  27.121  1.00 87.13  ?  166  TYR B OH  1 
ATOM   4778 N  N   . GLU B 1 168 ? 3.682   35.552  30.875  1.00 96.74  ?  167  GLU B N   1 
ATOM   4779 C  CA  . GLU B 1 168 ? 4.683   36.483  31.398  1.00 103.19 ?  167  GLU B CA  1 
ATOM   4780 C  C   . GLU B 1 168 ? 4.350   36.911  32.823  1.00 95.76  ?  167  GLU B C   1 
ATOM   4781 O  O   . GLU B 1 168 ? 5.232   36.978  33.675  1.00 108.53 ?  167  GLU B O   1 
ATOM   4782 C  CB  . GLU B 1 168 ? 4.802   37.724  30.504  1.00 110.83 ?  167  GLU B CB  1 
ATOM   4783 C  CG  . GLU B 1 168 ? 6.053   37.759  29.635  1.00 128.85 ?  167  GLU B CG  1 
ATOM   4784 C  CD  . GLU B 1 168 ? 6.505   39.176  29.318  1.00 140.31 ?  167  GLU B CD  1 
ATOM   4785 O  OE1 . GLU B 1 168 ? 5.864   40.129  29.809  1.00 139.08 ?  167  GLU B OE1 1 
ATOM   4786 O  OE2 . GLU B 1 168 ? 7.504   39.339  28.584  1.00 144.62 ?  167  GLU B OE2 1 
ATOM   4787 N  N   . VAL B 1 169 ? 3.078   37.201  33.078  1.00 79.48  ?  168  VAL B N   1 
ATOM   4788 C  CA  . VAL B 1 169 ? 2.651   37.578  34.417  1.00 78.02  ?  168  VAL B CA  1 
ATOM   4789 C  C   . VAL B 1 169 ? 2.898   36.417  35.364  1.00 102.39 ?  168  VAL B C   1 
ATOM   4790 O  O   . VAL B 1 169 ? 3.355   36.609  36.489  1.00 107.01 ?  168  VAL B O   1 
ATOM   4791 C  CB  . VAL B 1 169 ? 1.155   37.954  34.475  1.00 78.69  ?  168  VAL B CB  1 
ATOM   4792 C  CG1 . VAL B 1 169 ? 0.805   38.501  35.849  1.00 77.93  ?  168  VAL B CG1 1 
ATOM   4793 C  CG2 . VAL B 1 169 ? 0.804   38.965  33.404  1.00 82.93  ?  168  VAL B CG2 1 
ATOM   4794 N  N   . GLU B 1 170 ? 2.616   35.206  34.889  1.00 111.45 ?  169  GLU B N   1 
ATOM   4795 C  CA  . GLU B 1 170 ? 2.841   34.007  35.685  1.00 115.00 ?  169  GLU B CA  1 
ATOM   4796 C  C   . GLU B 1 170 ? 4.310   33.901  36.049  1.00 112.06 ?  169  GLU B C   1 
ATOM   4797 O  O   . GLU B 1 170 ? 4.657   33.674  37.209  1.00 122.48 ?  169  GLU B O   1 
ATOM   4798 C  CB  . GLU B 1 170 ? 2.395   32.745  34.933  1.00 121.32 ?  169  GLU B CB  1 
ATOM   4799 C  CG  . GLU B 1 170 ? 3.045   31.461  35.450  1.00 135.03 ?  169  GLU B CG  1 
ATOM   4800 C  CD  . GLU B 1 170 ? 2.738   30.240  34.597  1.00 140.90 ?  169  GLU B CD  1 
ATOM   4801 O  OE1 . GLU B 1 170 ? 1.545   29.950  34.380  1.00 138.08 ?  169  GLU B OE1 1 
ATOM   4802 O  OE2 . GLU B 1 170 ? 3.687   29.560  34.152  1.00 148.22 ?  169  GLU B OE2 1 
ATOM   4803 N  N   . GLU B 1 171 ? 5.166   34.095  35.052  1.00 107.56 ?  170  GLU B N   1 
ATOM   4804 C  CA  . GLU B 1 171 ? 6.604   34.034  35.248  1.00 117.70 ?  170  GLU B CA  1 
ATOM   4805 C  C   . GLU B 1 171 ? 7.051   35.053  36.293  1.00 129.37 ?  170  GLU B C   1 
ATOM   4806 O  O   . GLU B 1 171 ? 7.874   34.747  37.155  1.00 139.97 ?  170  GLU B O   1 
ATOM   4807 C  CB  . GLU B 1 171 ? 7.338   34.258  33.919  1.00 127.85 ?  170  GLU B CB  1 
ATOM   4808 C  CG  . GLU B 1 171 ? 8.831   33.929  33.951  1.00 155.26 ?  170  GLU B CG  1 
ATOM   4809 C  CD  . GLU B 1 171 ? 9.131   32.543  34.503  1.00 175.51 ?  170  GLU B CD  1 
ATOM   4810 O  OE1 . GLU B 1 171 ? 8.382   31.592  34.192  1.00 175.72 ?  170  GLU B OE1 1 
ATOM   4811 O  OE2 . GLU B 1 171 ? 10.124  32.404  35.249  1.00 185.34 ?  170  GLU B OE2 1 
ATOM   4812 N  N   . HIS B 1 172 ? 6.486   36.255  36.232  1.00 122.59 ?  171  HIS B N   1 
ATOM   4813 C  CA  . HIS B 1 172 ? 6.829   37.295  37.195  1.00 122.22 ?  171  HIS B CA  1 
ATOM   4814 C  C   . HIS B 1 172 ? 6.306   36.970  38.584  1.00 114.51 ?  171  HIS B C   1 
ATOM   4815 O  O   . HIS B 1 172 ? 6.955   37.297  39.581  1.00 124.68 ?  171  HIS B O   1 
ATOM   4816 C  CB  . HIS B 1 172 ? 6.307   38.652  36.732  1.00 129.61 ?  171  HIS B CB  1 
ATOM   4817 C  CG  . HIS B 1 172 ? 7.058   39.202  35.566  1.00 132.27 ?  171  HIS B CG  1 
ATOM   4818 N  ND1 . HIS B 1 172 ? 7.254   40.558  35.375  1.00 130.16 ?  171  HIS B ND1 1 
ATOM   4819 C  CD2 . HIS B 1 172 ? 7.674   38.589  34.533  1.00 134.74 ?  171  HIS B CD2 1 
ATOM   4820 C  CE1 . HIS B 1 172 ? 7.950   40.745  34.275  1.00 140.43 ?  171  HIS B CE1 1 
ATOM   4821 N  NE2 . HIS B 1 172 ? 8.221   39.565  33.737  1.00 138.29 ?  171  HIS B NE2 1 
ATOM   4822 N  N   . MET B 1 173 ? 5.134   36.345  38.654  1.00 92.21  ?  172  MET B N   1 
ATOM   4823 C  CA  . MET B 1 173 ? 4.610   35.888  39.933  1.00 91.43  ?  172  MET B CA  1 
ATOM   4824 C  C   . MET B 1 173 ? 5.600   34.923  40.578  1.00 110.85 ?  172  MET B C   1 
ATOM   4825 O  O   . MET B 1 173 ? 5.858   34.993  41.778  1.00 100.37 ?  172  MET B O   1 
ATOM   4826 C  CB  . MET B 1 173 ? 3.252   35.212  39.773  1.00 83.20  ?  172  MET B CB  1 
ATOM   4827 C  CG  . MET B 1 173 ? 2.131   36.122  39.312  1.00 75.46  ?  172  MET B CG  1 
ATOM   4828 S  SD  . MET B 1 173 ? 0.572   35.218  39.302  1.00 92.76  ?  172  MET B SD  1 
ATOM   4829 C  CE  . MET B 1 173 ? -0.489  36.332  38.398  1.00 80.30  ?  172  MET B CE  1 
ATOM   4830 N  N   . GLU B 1 174 ? 6.147   34.022  39.765  1.00 129.48 ?  173  GLU B N   1 
ATOM   4831 C  CA  . GLU B 1 174 ? 7.124   33.043  40.235  1.00 132.38 ?  173  GLU B CA  1 
ATOM   4832 C  C   . GLU B 1 174 ? 8.387   33.723  40.750  1.00 128.87 ?  173  GLU B C   1 
ATOM   4833 O  O   . GLU B 1 174 ? 8.972   33.276  41.734  1.00 129.18 ?  173  GLU B O   1 
ATOM   4834 C  CB  . GLU B 1 174 ? 7.488   32.056  39.123  1.00 137.31 ?  173  GLU B CB  1 
ATOM   4835 C  CG  . GLU B 1 174 ? 6.365   31.111  38.718  1.00 142.20 ?  173  GLU B CG  1 
ATOM   4836 C  CD  . GLU B 1 174 ? 6.797   30.119  37.655  1.00 149.38 ?  173  GLU B CD  1 
ATOM   4837 O  OE1 . GLU B 1 174 ? 7.907   30.283  37.104  1.00 155.30 ?  173  GLU B OE1 1 
ATOM   4838 O  OE2 . GLU B 1 174 ? 6.028   29.174  37.375  1.00 142.35 ?  173  GLU B OE2 1 
ATOM   4839 N  N   . ALA B 1 175 ? 8.809   34.793  40.080  1.00 126.03 ?  174  ALA B N   1 
ATOM   4840 C  CA  . ALA B 1 175 ? 9.990   35.533  40.509  1.00 125.70 ?  174  ALA B CA  1 
ATOM   4841 C  C   . ALA B 1 175 ? 9.683   36.139  41.868  1.00 124.50 ?  174  ALA B C   1 
ATOM   4842 O  O   . ALA B 1 175 ? 10.503  36.099  42.789  1.00 123.33 ?  174  ALA B O   1 
ATOM   4843 C  CB  . ALA B 1 175 ? 10.354  36.608  39.501  1.00 130.89 ?  174  ALA B CB  1 
ATOM   4844 N  N   . ALA B 1 176 ? 8.484   36.702  41.979  1.00 128.59 ?  175  ALA B N   1 
ATOM   4845 C  CA  . ALA B 1 176 ? 7.994   37.225  43.243  1.00 132.96 ?  175  ALA B CA  1 
ATOM   4846 C  C   . ALA B 1 176 ? 7.710   36.026  44.138  1.00 142.80 ?  175  ALA B C   1 
ATOM   4847 O  O   . ALA B 1 176 ? 7.810   34.880  43.699  1.00 141.40 ?  175  ALA B O   1 
ATOM   4848 C  CB  . ALA B 1 176 ? 6.748   38.076  43.047  1.00 122.73 ?  175  ALA B CB  1 
ATOM   4849 N  N   . GLY B 1 177 ? 7.334   36.269  45.385  1.00 143.89 ?  176  GLY B N   1 
ATOM   4850 C  CA  . GLY B 1 177 ? 7.041   35.165  46.278  1.00 145.03 ?  176  GLY B CA  1 
ATOM   4851 C  C   . GLY B 1 177 ? 5.642   34.607  46.104  1.00 136.68 ?  176  GLY B C   1 
ATOM   4852 O  O   . GLY B 1 177 ? 5.164   33.845  46.945  1.00 143.64 ?  176  GLY B O   1 
ATOM   4853 N  N   . ILE B 1 178 ? 4.991   34.959  45.000  1.00 131.19 ?  177  ILE B N   1 
ATOM   4854 C  CA  . ILE B 1 178 ? 3.616   34.527  44.776  1.00 127.83 ?  177  ILE B CA  1 
ATOM   4855 C  C   . ILE B 1 178 ? 3.426   33.212  44.032  1.00 128.89 ?  177  ILE B C   1 
ATOM   4856 O  O   . ILE B 1 178 ? 3.972   33.014  42.949  1.00 142.09 ?  177  ILE B O   1 
ATOM   4857 C  CB  . ILE B 1 178 ? 2.846   35.607  43.987  1.00 119.71 ?  177  ILE B CB  1 
ATOM   4858 C  CG1 . ILE B 1 178 ? 2.758   36.895  44.801  1.00 121.68 ?  177  ILE B CG1 1 
ATOM   4859 C  CG2 . ILE B 1 178 ? 1.451   35.125  43.642  1.00 110.07 ?  177  ILE B CG2 1 
ATOM   4860 C  CD1 . ILE B 1 178 ? 2.194   36.670  46.181  1.00 135.20 ?  177  ILE B CD1 1 
ATOM   4861 N  N   . ALA B 1 179 ? 2.663   32.307  44.643  1.00 124.22 ?  178  ALA B N   1 
ATOM   4862 C  CA  . ALA B 1 179 ? 2.167   31.116  43.962  1.00 120.48 ?  178  ALA B CA  1 
ATOM   4863 C  C   . ALA B 1 179 ? 0.716   31.343  43.530  1.00 119.47 ?  178  ALA B C   1 
ATOM   4864 O  O   . ALA B 1 179 ? 0.023   32.185  44.104  1.00 104.50 ?  178  ALA B O   1 
ATOM   4865 C  CB  . ALA B 1 179 ? 2.281   29.897  44.851  1.00 113.11 ?  178  ALA B CB  1 
ATOM   4866 N  N   . LEU B 1 180 ? 0.256   30.588  42.535  1.00 125.41 ?  179  LEU B N   1 
ATOM   4867 C  CA  . LEU B 1 180 ? -1.068  30.813  41.945  1.00 107.83 ?  179  LEU B CA  1 
ATOM   4868 C  C   . LEU B 1 180 ? -2.187  30.016  42.619  1.00 96.73  ?  179  LEU B C   1 
ATOM   4869 O  O   . LEU B 1 180 ? -2.055  28.812  42.832  1.00 91.69  ?  179  LEU B O   1 
ATOM   4870 C  CB  . LEU B 1 180 ? -1.049  30.492  40.450  1.00 92.94  ?  179  LEU B CB  1 
ATOM   4871 C  CG  . LEU B 1 180 ? -0.088  31.291  39.571  1.00 95.72  ?  179  LEU B CG  1 
ATOM   4872 C  CD1 . LEU B 1 180 ? 1.144   30.469  39.214  1.00 90.33  ?  179  LEU B CD1 1 
ATOM   4873 C  CD2 . LEU B 1 180 ? -0.811  31.762  38.321  1.00 109.36 ?  179  LEU B CD2 1 
ATOM   4874 N  N   . GLU B 1 181 ? -3.299  30.684  42.916  1.00 108.81 ?  180  GLU B N   1 
ATOM   4875 C  CA  . GLU B 1 181 ? -4.496  30.004  43.409  1.00 116.56 ?  180  GLU B CA  1 
ATOM   4876 C  C   . GLU B 1 181 ? -5.273  29.435  42.229  1.00 108.05 ?  180  GLU B C   1 
ATOM   4877 O  O   . GLU B 1 181 ? -4.923  29.679  41.078  1.00 92.62  ?  180  GLU B O   1 
ATOM   4878 C  CB  . GLU B 1 181 ? -5.380  30.947  44.223  1.00 121.87 ?  180  GLU B CB  1 
ATOM   4879 C  CG  . GLU B 1 181 ? -5.038  30.993  45.704  1.00 134.94 ?  180  GLU B CG  1 
ATOM   4880 C  CD  . GLU B 1 181 ? -5.878  31.998  46.463  1.00 140.25 ?  180  GLU B CD  1 
ATOM   4881 O  OE1 . GLU B 1 181 ? -7.048  32.216  46.074  1.00 149.92 ?  180  GLU B OE1 1 
ATOM   4882 O  OE2 . GLU B 1 181 ? -5.363  32.576  47.444  1.00 134.54 ?  180  GLU B OE2 1 
ATOM   4883 N  N   . GLU B 1 182 ? -6.321  28.673  42.516  1.00 116.98 ?  181  GLU B N   1 
ATOM   4884 C  CA  . GLU B 1 182 ? -7.038  27.933  41.481  1.00 118.69 ?  181  GLU B CA  1 
ATOM   4885 C  C   . GLU B 1 182 ? -7.583  28.834  40.367  1.00 108.79 ?  181  GLU B C   1 
ATOM   4886 O  O   . GLU B 1 182 ? -7.319  28.592  39.189  1.00 119.35 ?  181  GLU B O   1 
ATOM   4887 C  CB  . GLU B 1 182 ? -8.184  27.134  42.114  1.00 123.52 ?  181  GLU B CB  1 
ATOM   4888 C  CG  . GLU B 1 182 ? -9.073  26.407  41.117  1.00 117.91 ?  181  GLU B CG  1 
ATOM   4889 C  CD  . GLU B 1 182 ? -10.532 26.399  41.530  1.00 119.96 ?  181  GLU B CD  1 
ATOM   4890 O  OE1 . GLU B 1 182 ? -10.843 26.864  42.649  1.00 128.75 ?  181  GLU B OE1 1 
ATOM   4891 O  OE2 . GLU B 1 182 ? -11.369 25.932  40.730  1.00 112.67 ?  181  GLU B OE2 1 
ATOM   4892 N  N   . ALA B 1 183 ? -8.309  29.881  40.752  1.00 97.76  ?  182  ALA B N   1 
ATOM   4893 C  CA  . ALA B 1 183 ? -8.943  30.809  39.810  1.00 101.71 ?  182  ALA B CA  1 
ATOM   4894 C  C   . ALA B 1 183 ? -7.988  31.328  38.729  1.00 87.20  ?  182  ALA B C   1 
ATOM   4895 O  O   . ALA B 1 183 ? -8.366  31.484  37.565  1.00 66.45  ?  182  ALA B O   1 
ATOM   4896 C  CB  . ALA B 1 183 ? -9.559  31.979  40.575  1.00 109.37 ?  182  ALA B CB  1 
ATOM   4897 N  N   . GLU B 1 184 ? -6.761  31.635  39.133  1.00 96.67  ?  183  GLU B N   1 
ATOM   4898 C  CA  . GLU B 1 184 ? -5.760  32.162  38.214  1.00 96.49  ?  183  GLU B CA  1 
ATOM   4899 C  C   . GLU B 1 184 ? -5.278  31.110  37.235  1.00 97.52  ?  183  GLU B C   1 
ATOM   4900 O  O   . GLU B 1 184 ? -5.130  31.388  36.044  1.00 124.31 ?  183  GLU B O   1 
ATOM   4901 C  CB  . GLU B 1 184 ? -4.567  32.733  38.985  1.00 100.07 ?  183  GLU B CB  1 
ATOM   4902 C  CG  . GLU B 1 184 ? -4.889  34.019  39.705  1.00 112.04 ?  183  GLU B CG  1 
ATOM   4903 C  CD  . GLU B 1 184 ? -5.606  33.792  41.019  1.00 122.74 ?  183  GLU B CD  1 
ATOM   4904 O  OE1 . GLU B 1 184 ? -5.288  32.805  41.710  1.00 131.89 ?  183  GLU B OE1 1 
ATOM   4905 O  OE2 . GLU B 1 184 ? -6.510  34.587  41.350  1.00 123.54 ?  183  GLU B OE2 1 
ATOM   4906 N  N   . ILE B 1 185 ? -5.039  29.903  37.738  1.00 82.24  ?  184  ILE B N   1 
ATOM   4907 C  CA  . ILE B 1 185 ? -4.552  28.820  36.900  1.00 82.40  ?  184  ILE B CA  1 
ATOM   4908 C  C   . ILE B 1 185 ? -5.606  28.439  35.875  1.00 99.39  ?  184  ILE B C   1 
ATOM   4909 O  O   . ILE B 1 185 ? -5.289  28.185  34.714  1.00 107.04 ?  184  ILE B O   1 
ATOM   4910 C  CB  . ILE B 1 185 ? -4.173  27.583  37.725  1.00 82.22  ?  184  ILE B CB  1 
ATOM   4911 C  CG1 . ILE B 1 185 ? -3.425  27.988  38.996  1.00 95.41  ?  184  ILE B CG1 1 
ATOM   4912 C  CG2 . ILE B 1 185 ? -3.322  26.640  36.895  1.00 74.23  ?  184  ILE B CG2 1 
ATOM   4913 C  CD1 . ILE B 1 185 ? -2.753  26.830  39.711  1.00 96.54  ?  184  ILE B CD1 1 
ATOM   4914 N  N   . SER B 1 186 ? -6.863  28.436  36.304  1.00 105.33 ?  185  SER B N   1 
ATOM   4915 C  CA  . SER B 1 186 ? -7.967  28.071  35.427  1.00 119.82 ?  185  SER B CA  1 
ATOM   4916 C  C   . SER B 1 186 ? -8.051  29.036  34.249  1.00 100.71 ?  185  SER B C   1 
ATOM   4917 O  O   . SER B 1 186 ? -8.277  28.622  33.114  1.00 92.76  ?  185  SER B O   1 
ATOM   4918 C  CB  . SER B 1 186 ? -9.290  28.059  36.195  1.00 137.49 ?  185  SER B CB  1 
ATOM   4919 O  OG  . SER B 1 186 ? -9.792  29.373  36.372  1.00 155.95 ?  185  SER B OG  1 
ATOM   4920 N  N   . ALA B 1 187 ? -7.860  30.321  34.526  1.00 92.62  ?  186  ALA B N   1 
ATOM   4921 C  CA  . ALA B 1 187 ? -7.852  31.325  33.476  1.00 86.54  ?  186  ALA B CA  1 
ATOM   4922 C  C   . ALA B 1 187 ? -6.691  31.091  32.519  1.00 95.10  ?  186  ALA B C   1 
ATOM   4923 O  O   . ALA B 1 187 ? -6.849  31.205  31.304  1.00 110.08 ?  186  ALA B O   1 
ATOM   4924 C  CB  . ALA B 1 187 ? -7.774  32.707  34.069  1.00 73.38  ?  186  ALA B CB  1 
ATOM   4925 N  N   . LEU B 1 188 ? -5.533  30.747  33.070  1.00 77.36  ?  187  LEU B N   1 
ATOM   4926 C  CA  . LEU B 1 188 ? -4.373  30.418  32.255  1.00 84.17  ?  187  LEU B CA  1 
ATOM   4927 C  C   . LEU B 1 188 ? -4.615  29.161  31.427  1.00 101.52 ?  187  LEU B C   1 
ATOM   4928 O  O   . LEU B 1 188 ? -4.184  29.070  30.274  1.00 117.60 ?  187  LEU B O   1 
ATOM   4929 C  CB  . LEU B 1 188 ? -3.138  30.252  33.133  1.00 78.45  ?  187  LEU B CB  1 
ATOM   4930 C  CG  . LEU B 1 188 ? -2.452  31.559  33.516  1.00 76.13  ?  187  LEU B CG  1 
ATOM   4931 C  CD1 . LEU B 1 188 ? -1.287  31.297  34.446  1.00 89.55  ?  187  LEU B CD1 1 
ATOM   4932 C  CD2 . LEU B 1 188 ? -1.981  32.286  32.261  1.00 73.67  ?  187  LEU B CD2 1 
ATOM   4933 N  N   . LEU B 1 189 ? -5.313  28.197  32.020  1.00 85.95  ?  188  LEU B N   1 
ATOM   4934 C  CA  . LEU B 1 189 ? -5.689  26.975  31.319  1.00 95.95  ?  188  LEU B CA  1 
ATOM   4935 C  C   . LEU B 1 189 ? -6.646  27.278  30.172  1.00 97.18  ?  188  LEU B C   1 
ATOM   4936 O  O   . LEU B 1 189 ? -6.498  26.756  29.067  1.00 90.50  ?  188  LEU B O   1 
ATOM   4937 C  CB  . LEU B 1 189 ? -6.351  25.992  32.287  1.00 106.41 ?  188  LEU B CB  1 
ATOM   4938 C  CG  . LEU B 1 189 ? -6.845  24.643  31.761  1.00 67.67  ?  188  LEU B CG  1 
ATOM   4939 C  CD1 . LEU B 1 189 ? -5.760  23.581  31.839  1.00 68.53  ?  188  LEU B CD1 1 
ATOM   4940 C  CD2 . LEU B 1 189 ? -8.117  24.213  32.472  1.00 67.14  ?  188  LEU B CD2 1 
ATOM   4941 N  N   . LYS B 1 190 ? -7.611  28.152  30.451  1.00 102.76 ?  189  LYS B N   1 
ATOM   4942 C  CA  . LYS B 1 190 ? -8.652  28.529  29.497  1.00 89.66  ?  189  LYS B CA  1 
ATOM   4943 C  C   . LYS B 1 190 ? -8.042  29.036  28.204  1.00 92.33  ?  189  LYS B C   1 
ATOM   4944 O  O   . LYS B 1 190 ? -8.443  28.637  27.112  1.00 109.19 ?  189  LYS B O   1 
ATOM   4945 C  CB  . LYS B 1 190 ? -9.550  29.606  30.109  1.00 67.26  ?  189  LYS B CB  1 
ATOM   4946 C  CG  . LYS B 1 190 ? -10.558 30.224  29.173  1.00 68.29  ?  189  LYS B CG  1 
ATOM   4947 C  CD  . LYS B 1 190 ? -11.728 29.287  28.945  1.00 81.76  ?  189  LYS B CD  1 
ATOM   4948 C  CE  . LYS B 1 190 ? -13.050 30.038  28.912  1.00 89.63  ?  189  LYS B CE  1 
ATOM   4949 N  NZ  . LYS B 1 190 ? -13.346 30.709  30.212  1.00 82.62  ?  189  LYS B NZ  1 
ATOM   4950 N  N   . VAL B 1 191 ? -7.045  29.898  28.352  1.00 78.49  ?  190  VAL B N   1 
ATOM   4951 C  CA  . VAL B 1 191 ? -6.367  30.527  27.231  1.00 88.36  ?  190  VAL B CA  1 
ATOM   4952 C  C   . VAL B 1 191 ? -5.534  29.551  26.425  1.00 96.96  ?  190  VAL B C   1 
ATOM   4953 O  O   . VAL B 1 191 ? -5.564  29.567  25.193  1.00 122.96 ?  190  VAL B O   1 
ATOM   4954 C  CB  . VAL B 1 191 ? -5.471  31.657  27.719  1.00 99.22  ?  190  VAL B CB  1 
ATOM   4955 C  CG1 . VAL B 1 191 ? -4.668  32.247  26.571  1.00 106.05 ?  190  VAL B CG1 1 
ATOM   4956 C  CG2 . VAL B 1 191 ? -6.324  32.692  28.358  1.00 98.28  ?  190  VAL B CG2 1 
ATOM   4957 N  N   . SER B 1 192 ? -4.785  28.710  27.125  1.00 80.82  ?  191  SER B N   1 
ATOM   4958 C  CA  . SER B 1 192 ? -3.936  27.732  26.465  1.00 92.18  ?  191  SER B CA  1 
ATOM   4959 C  C   . SER B 1 192 ? -4.785  26.825  25.576  1.00 92.93  ?  191  SER B C   1 
ATOM   4960 O  O   . SER B 1 192 ? -4.357  26.421  24.494  1.00 78.26  ?  191  SER B O   1 
ATOM   4961 C  CB  . SER B 1 192 ? -3.157  26.923  27.498  1.00 87.70  ?  191  SER B CB  1 
ATOM   4962 O  OG  . SER B 1 192 ? -2.105  27.693  28.051  1.00 76.76  ?  191  SER B OG  1 
ATOM   4963 N  N   . ALA B 1 193 ? -5.999  26.533  26.035  1.00 105.94 ?  192  ALA B N   1 
ATOM   4964 C  CA  . ALA B 1 193 ? -6.968  25.765  25.261  1.00 100.52 ?  192  ALA B CA  1 
ATOM   4965 C  C   . ALA B 1 193 ? -7.429  26.545  24.036  1.00 96.81  ?  192  ALA B C   1 
ATOM   4966 O  O   . ALA B 1 193 ? -7.515  25.998  22.939  1.00 109.16 ?  192  ALA B O   1 
ATOM   4967 C  CB  . ALA B 1 193 ? -8.160  25.388  26.129  1.00 100.43 ?  192  ALA B CB  1 
ATOM   4968 N  N   . ALA B 1 194 ? -7.734  27.823  24.238  1.00 87.94  ?  193  ALA B N   1 
ATOM   4969 C  CA  . ALA B 1 194 ? -8.215  28.701  23.171  1.00 91.02  ?  193  ALA B CA  1 
ATOM   4970 C  C   . ALA B 1 194 ? -7.142  28.931  22.100  1.00 93.39  ?  193  ALA B C   1 
ATOM   4971 O  O   . ALA B 1 194 ? -7.460  29.064  20.917  1.00 83.63  ?  193  ALA B O   1 
ATOM   4972 C  CB  . ALA B 1 194 ? -8.693  30.030  23.746  1.00 85.59  ?  193  ALA B CB  1 
ATOM   4973 N  N   . THR B 1 195 ? -5.883  29.038  22.525  1.00 92.02  ?  194  THR B N   1 
ATOM   4974 C  CA  . THR B 1 195 ? -4.764  29.154  21.591  1.00 93.92  ?  194  THR B CA  1 
ATOM   4975 C  C   . THR B 1 195 ? -4.410  27.770  21.046  1.00 96.92  ?  194  THR B C   1 
ATOM   4976 O  O   . THR B 1 195 ? -3.581  27.633  20.144  1.00 103.65 ?  194  THR B O   1 
ATOM   4977 C  CB  . THR B 1 195 ? -3.521  29.775  22.270  1.00 93.97  ?  194  THR B CB  1 
ATOM   4978 O  OG1 . THR B 1 195 ? -3.932  30.852  23.118  1.00 80.95  ?  194  THR B OG1 1 
ATOM   4979 C  CG2 . THR B 1 195 ? -2.528  30.303  21.238  1.00 100.05 ?  194  THR B CG2 1 
ATOM   4980 N  N   . GLY B 1 196 ? -5.073  26.753  21.590  1.00 83.55  ?  195  GLY B N   1 
ATOM   4981 C  CA  . GLY B 1 196 ? -4.885  25.372  21.185  1.00 84.96  ?  195  GLY B CA  1 
ATOM   4982 C  C   . GLY B 1 196 ? -3.463  24.852  21.289  1.00 95.95  ?  195  GLY B C   1 
ATOM   4983 O  O   . GLY B 1 196 ? -3.055  23.982  20.519  1.00 96.68  ?  195  GLY B O   1 
ATOM   4984 N  N   . ARG B 1 197 ? -2.714  25.355  22.264  1.00 107.52 ?  196  ARG B N   1 
ATOM   4985 C  CA  . ARG B 1 197 ? -1.384  24.825  22.539  1.00 109.17 ?  196  ARG B CA  1 
ATOM   4986 C  C   . ARG B 1 197 ? -1.510  23.772  23.623  1.00 123.12 ?  196  ARG B C   1 
ATOM   4987 O  O   . ARG B 1 197 ? -1.852  24.070  24.766  1.00 136.96 ?  196  ARG B O   1 
ATOM   4988 C  CB  . ARG B 1 197 ? -0.404  25.924  22.940  1.00 99.77  ?  196  ARG B CB  1 
ATOM   4989 C  CG  . ARG B 1 197 ? -0.976  26.952  23.880  1.00 100.43 ?  196  ARG B CG  1 
ATOM   4990 C  CD  . ARG B 1 197 ? 0.094   27.939  24.275  1.00 106.00 ?  196  ARG B CD  1 
ATOM   4991 N  NE  . ARG B 1 197 ? 0.214   29.041  23.329  1.00 98.09  ?  196  ARG B NE  1 
ATOM   4992 C  CZ  . ARG B 1 197 ? 1.325   29.745  23.151  1.00 96.01  ?  196  ARG B CZ  1 
ATOM   4993 N  NH1 . ARG B 1 197 ? 2.419   29.446  23.840  1.00 94.06  ?  196  ARG B NH1 1 
ATOM   4994 N  NH2 . ARG B 1 197 ? 1.344   30.740  22.276  1.00 102.95 ?  196  ARG B NH2 1 
ATOM   4995 N  N   . GLU B 1 198 ? -1.245  22.533  23.237  1.00 129.15 ?  197  GLU B N   1 
ATOM   4996 C  CA  . GLU B 1 198 ? -1.473  21.370  24.082  1.00 123.82 ?  197  GLU B CA  1 
ATOM   4997 C  C   . GLU B 1 198 ? -0.615  21.312  25.343  1.00 124.05 ?  197  GLU B C   1 
ATOM   4998 O  O   . GLU B 1 198 ? -1.139  21.100  26.435  1.00 112.28 ?  197  GLU B O   1 
ATOM   4999 C  CB  . GLU B 1 198 ? -1.244  20.100  23.262  1.00 124.34 ?  197  GLU B CB  1 
ATOM   5000 C  CG  . GLU B 1 198 ? 0.144   19.991  22.600  1.00 136.61 ?  197  GLU B CG  1 
ATOM   5001 C  CD  . GLU B 1 198 ? 0.289   20.826  21.328  1.00 131.08 ?  197  GLU B CD  1 
ATOM   5002 O  OE1 . GLU B 1 198 ? -0.281  21.936  21.252  1.00 130.34 ?  197  GLU B OE1 1 
ATOM   5003 O  OE2 . GLU B 1 198 ? 0.987   20.369  20.399  1.00 126.43 ?  197  GLU B OE2 1 
ATOM   5004 N  N   . ASN B 1 199 ? 0.691   21.515  25.195  1.00 142.15 ?  198  ASN B N   1 
ATOM   5005 C  CA  . ASN B 1 199 ? 1.624   21.335  26.301  1.00 145.69 ?  198  ASN B CA  1 
ATOM   5006 C  C   . ASN B 1 199 ? 1.338   22.304  27.435  1.00 126.98 ?  198  ASN B C   1 
ATOM   5007 O  O   . ASN B 1 199 ? 1.510   21.971  28.604  1.00 133.92 ?  198  ASN B O   1 
ATOM   5008 C  CB  . ASN B 1 199 ? 3.064   21.505  25.819  1.00 167.25 ?  198  ASN B CB  1 
ATOM   5009 C  CG  . ASN B 1 199 ? 3.449   22.959  25.640  1.00 192.48 ?  198  ASN B CG  1 
ATOM   5010 O  OD1 . ASN B 1 199 ? 4.047   23.566  26.528  1.00 206.65 ?  198  ASN B OD1 1 
ATOM   5011 N  ND2 . ASN B 1 199 ? 3.093   23.532  24.494  1.00 200.29 ?  198  ASN B ND2 1 
ATOM   5012 N  N   . LYS B 1 200 ? 0.902   23.507  27.080  1.00 115.80 ?  199  LYS B N   1 
ATOM   5013 C  CA  . LYS B 1 200 ? 0.536   24.502  28.068  1.00 93.61  ?  199  LYS B CA  1 
ATOM   5014 C  C   . LYS B 1 200 ? -0.711  24.068  28.818  1.00 105.05 ?  199  LYS B C   1 
ATOM   5015 O  O   . LYS B 1 200 ? -0.828  24.287  30.021  1.00 117.31 ?  199  LYS B O   1 
ATOM   5016 C  CB  . LYS B 1 200 ? 0.309   25.851  27.412  1.00 78.33  ?  199  LYS B CB  1 
ATOM   5017 C  CG  . LYS B 1 200 ? 1.209   26.929  27.952  1.00 86.55  ?  199  LYS B CG  1 
ATOM   5018 C  CD  . LYS B 1 200 ? 2.684   26.585  27.809  1.00 86.23  ?  199  LYS B CD  1 
ATOM   5019 C  CE  . LYS B 1 200 ? 3.555   27.645  28.477  1.00 89.25  ?  199  LYS B CE  1 
ATOM   5020 N  NZ  . LYS B 1 200 ? 5.002   27.414  28.209  1.00 100.10 ?  199  LYS B NZ  1 
ATOM   5021 N  N   . VAL B 1 201 ? -1.653  23.473  28.094  1.00 94.84  ?  200  VAL B N   1 
ATOM   5022 C  CA  . VAL B 1 201 ? -2.846  22.907  28.712  1.00 89.24  ?  200  VAL B CA  1 
ATOM   5023 C  C   . VAL B 1 201 ? -2.460  21.740  29.623  1.00 93.09  ?  200  VAL B C   1 
ATOM   5024 O  O   . VAL B 1 201 ? -3.023  21.556  30.704  1.00 80.62  ?  200  VAL B O   1 
ATOM   5025 C  CB  . VAL B 1 201 ? -3.856  22.431  27.646  1.00 74.70  ?  200  VAL B CB  1 
ATOM   5026 C  CG1 . VAL B 1 201 ? -5.060  21.773  28.289  1.00 73.46  ?  200  VAL B CG1 1 
ATOM   5027 C  CG2 . VAL B 1 201 ? -4.301  23.596  26.802  1.00 78.55  ?  200  VAL B CG2 1 
ATOM   5028 N  N   . TYR B 1 202 ? -1.482  20.961  29.176  1.00 97.78  ?  201  TYR B N   1 
ATOM   5029 C  CA  . TYR B 1 202 ? -0.989  19.821  29.936  1.00 76.18  ?  201  TYR B CA  1 
ATOM   5030 C  C   . TYR B 1 202 ? -0.335  20.252  31.248  1.00 108.54 ?  201  TYR B C   1 
ATOM   5031 O  O   . TYR B 1 202 ? -0.682  19.748  32.315  1.00 107.04 ?  201  TYR B O   1 
ATOM   5032 C  CB  . TYR B 1 202 ? 0.001   19.023  29.094  1.00 78.84  ?  201  TYR B CB  1 
ATOM   5033 C  CG  . TYR B 1 202 ? 0.492   17.773  29.766  1.00 82.77  ?  201  TYR B CG  1 
ATOM   5034 C  CD1 . TYR B 1 202 ? -0.353  16.687  29.955  1.00 92.73  ?  201  TYR B CD1 1 
ATOM   5035 C  CD2 . TYR B 1 202 ? 1.798   17.677  30.220  1.00 86.45  ?  201  TYR B CD2 1 
ATOM   5036 C  CE1 . TYR B 1 202 ? 0.093   15.533  30.574  1.00 103.85 ?  201  TYR B CE1 1 
ATOM   5037 C  CE2 . TYR B 1 202 ? 2.253   16.532  30.841  1.00 107.28 ?  201  TYR B CE2 1 
ATOM   5038 C  CZ  . TYR B 1 202 ? 1.396   15.463  31.018  1.00 118.54 ?  201  TYR B CZ  1 
ATOM   5039 O  OH  . TYR B 1 202 ? 1.850   14.321  31.636  1.00 140.22 ?  201  TYR B OH  1 
ATOM   5040 N  N   . ARG B 1 203 ? 0.589   21.209  31.160  1.00 98.06  ?  202  ARG B N   1 
ATOM   5041 C  CA  . ARG B 1 203 ? 1.316   21.720  32.325  1.00 83.31  ?  202  ARG B CA  1 
ATOM   5042 C  C   . ARG B 1 203 ? 0.346   22.304  33.345  1.00 86.74  ?  202  ARG B C   1 
ATOM   5043 O  O   . ARG B 1 203 ? 0.487   22.073  34.544  1.00 114.43 ?  202  ARG B O   1 
ATOM   5044 C  CB  . ARG B 1 203 ? 2.359   22.767  31.909  1.00 88.38  ?  202  ARG B CB  1 
ATOM   5045 C  CG  . ARG B 1 203 ? 3.068   23.453  33.073  1.00 109.98 ?  202  ARG B CG  1 
ATOM   5046 C  CD  . ARG B 1 203 ? 4.130   24.454  32.604  1.00 130.57 ?  202  ARG B CD  1 
ATOM   5047 N  NE  . ARG B 1 203 ? 4.885   25.015  33.727  1.00 140.35 ?  202  ARG B NE  1 
ATOM   5048 C  CZ  . ARG B 1 203 ? 5.966   25.783  33.605  1.00 138.34 ?  202  ARG B CZ  1 
ATOM   5049 N  NH1 . ARG B 1 203 ? 6.437   26.089  32.404  1.00 136.66 ?  202  ARG B NH1 1 
ATOM   5050 N  NH2 . ARG B 1 203 ? 6.581   26.244  34.687  1.00 132.68 ?  202  ARG B NH2 1 
ATOM   5051 N  N   . TYR B 1 204 ? -0.633  23.063  32.864  1.00 78.03  ?  203  TYR B N   1 
ATOM   5052 C  CA  . TYR B 1 204 ? -1.603  23.711  33.740  1.00 83.21  ?  203  TYR B CA  1 
ATOM   5053 C  C   . TYR B 1 204 ? -2.552  22.698  34.373  1.00 78.28  ?  203  TYR B C   1 
ATOM   5054 O  O   . TYR B 1 204 ? -3.107  22.940  35.444  1.00 85.86  ?  203  TYR B O   1 
ATOM   5055 C  CB  . TYR B 1 204 ? -2.401  24.767  32.977  1.00 96.78  ?  203  TYR B CB  1 
ATOM   5056 C  CG  . TYR B 1 204 ? -1.603  25.995  32.617  1.00 109.99 ?  203  TYR B CG  1 
ATOM   5057 C  CD1 . TYR B 1 204 ? -0.356  26.232  33.183  1.00 109.06 ?  203  TYR B CD1 1 
ATOM   5058 C  CD2 . TYR B 1 204 ? -2.092  26.913  31.704  1.00 119.93 ?  203  TYR B CD2 1 
ATOM   5059 C  CE1 . TYR B 1 204 ? 0.377   27.352  32.851  1.00 104.57 ?  203  TYR B CE1 1 
ATOM   5060 C  CE2 . TYR B 1 204 ? -1.365  28.031  31.363  1.00 125.59 ?  203  TYR B CE2 1 
ATOM   5061 C  CZ  . TYR B 1 204 ? -0.135  28.247  31.943  1.00 123.17 ?  203  TYR B CZ  1 
ATOM   5062 O  OH  . TYR B 1 204 ? 0.588   29.365  31.605  1.00 143.24 ?  203  TYR B OH  1 
ATOM   5063 N  N   . LEU B 1 205 ? -2.775  21.583  33.691  1.00 80.55  ?  204  LEU B N   1 
ATOM   5064 C  CA  . LEU B 1 205 ? -3.543  20.498  34.288  1.00 84.52  ?  204  LEU B CA  1 
ATOM   5065 C  C   . LEU B 1 205 ? -2.791  19.847  35.451  1.00 87.38  ?  204  LEU B C   1 
ATOM   5066 O  O   . LEU B 1 205 ? -3.397  19.483  36.454  1.00 96.85  ?  204  LEU B O   1 
ATOM   5067 C  CB  . LEU B 1 205 ? -3.907  19.450  33.243  1.00 84.63  ?  204  LEU B CB  1 
ATOM   5068 C  CG  . LEU B 1 205 ? -5.057  19.837  32.310  1.00 83.06  ?  204  LEU B CG  1 
ATOM   5069 C  CD1 . LEU B 1 205 ? -5.253  18.761  31.254  1.00 101.85 ?  204  LEU B CD1 1 
ATOM   5070 C  CD2 . LEU B 1 205 ? -6.356  20.111  33.066  1.00 69.85  ?  204  LEU B CD2 1 
ATOM   5071 N  N   . HIS B 1 206 ? -1.476  19.685  35.311  1.00 86.02  ?  205  HIS B N   1 
ATOM   5072 C  CA  . HIS B 1 206 ? -0.657  19.173  36.410  1.00 78.00  ?  205  HIS B CA  1 
ATOM   5073 C  C   . HIS B 1 206 ? -0.544  20.183  37.547  1.00 98.96  ?  205  HIS B C   1 
ATOM   5074 O  O   . HIS B 1 206 ? -0.546  19.810  38.719  1.00 103.08 ?  205  HIS B O   1 
ATOM   5075 C  CB  . HIS B 1 206 ? 0.745   18.802  35.929  1.00 75.58  ?  205  HIS B CB  1 
ATOM   5076 C  CG  . HIS B 1 206 ? 0.833   17.443  35.312  1.00 90.88  ?  205  HIS B CG  1 
ATOM   5077 N  ND1 . HIS B 1 206 ? -0.230  16.563  35.300  1.00 98.06  ?  205  HIS B ND1 1 
ATOM   5078 C  CD2 . HIS B 1 206 ? 1.860   16.801  34.710  1.00 97.51  ?  205  HIS B CD2 1 
ATOM   5079 C  CE1 . HIS B 1 206 ? 0.137   15.446  34.700  1.00 96.54  ?  205  HIS B CE1 1 
ATOM   5080 N  NE2 . HIS B 1 206 ? 1.402   15.562  34.334  1.00 92.86  ?  205  HIS B NE2 1 
ATOM   5081 N  N   . LYS B 1 207 ? -0.449  21.463  37.195  1.00 105.18 ?  206  LYS B N   1 
ATOM   5082 C  CA  . LYS B 1 207 ? -0.408  22.525  38.194  1.00 100.78 ?  206  LYS B CA  1 
ATOM   5083 C  C   . LYS B 1 207 ? -1.710  22.555  38.992  1.00 93.28  ?  206  LYS B C   1 
ATOM   5084 O  O   . LYS B 1 207 ? -1.691  22.742  40.207  1.00 102.81 ?  206  LYS B O   1 
ATOM   5085 C  CB  . LYS B 1 207 ? -0.138  23.888  37.542  1.00 100.07 ?  206  LYS B CB  1 
ATOM   5086 C  CG  . LYS B 1 207 ? 1.334   24.145  37.219  1.00 101.38 ?  206  LYS B CG  1 
ATOM   5087 C  CD  . LYS B 1 207 ? 1.563   25.570  36.726  1.00 110.80 ?  206  LYS B CD  1 
ATOM   5088 C  CE  . LYS B 1 207 ? 3.035   25.837  36.423  1.00 124.00 ?  206  LYS B CE  1 
ATOM   5089 N  NZ  . LYS B 1 207 ? 3.253   27.159  35.762  1.00 126.40 ?  206  LYS B NZ  1 
ATOM   5090 N  N   . LEU B 1 208 ? -2.836  22.356  38.314  1.00 83.42  ?  207  LEU B N   1 
ATOM   5091 C  CA  . LEU B 1 208 ? -4.121  22.299  39.001  1.00 84.21  ?  207  LEU B CA  1 
ATOM   5092 C  C   . LEU B 1 208 ? -4.140  21.121  39.956  1.00 94.19  ?  207  LEU B C   1 
ATOM   5093 O  O   . LEU B 1 208 ? -4.621  21.224  41.081  1.00 116.41 ?  207  LEU B O   1 
ATOM   5094 C  CB  . LEU B 1 208 ? -5.277  22.182  38.011  1.00 94.06  ?  207  LEU B CB  1 
ATOM   5095 C  CG  . LEU B 1 208 ? -5.773  23.489  37.399  1.00 108.61 ?  207  LEU B CG  1 
ATOM   5096 C  CD1 . LEU B 1 208 ? -7.008  23.236  36.547  1.00 109.24 ?  207  LEU B CD1 1 
ATOM   5097 C  CD2 . LEU B 1 208 ? -6.059  24.508  38.487  1.00 113.38 ?  207  LEU B CD2 1 
ATOM   5098 N  N   . ARG B 1 209 ? -3.609  19.998  39.493  1.00 86.77  ?  208  ARG B N   1 
ATOM   5099 C  CA  . ARG B 1 209 ? -3.515  18.789  40.300  1.00 93.90  ?  208  ARG B CA  1 
ATOM   5100 C  C   . ARG B 1 209 ? -2.619  18.963  41.525  1.00 113.87 ?  208  ARG B C   1 
ATOM   5101 O  O   . ARG B 1 209 ? -2.948  18.509  42.621  1.00 74.92  ?  208  ARG B O   1 
ATOM   5102 C  CB  . ARG B 1 209 ? -3.010  17.645  39.429  1.00 78.48  ?  208  ARG B CB  1 
ATOM   5103 C  CG  . ARG B 1 209 ? -2.734  16.376  40.173  1.00 87.59  ?  208  ARG B CG  1 
ATOM   5104 C  CD  . ARG B 1 209 ? -1.897  15.453  39.314  1.00 89.34  ?  208  ARG B CD  1 
ATOM   5105 N  NE  . ARG B 1 209 ? -0.567  15.992  39.029  1.00 78.98  ?  208  ARG B NE  1 
ATOM   5106 C  CZ  . ARG B 1 209 ? 0.402   16.147  39.925  1.00 87.66  ?  208  ARG B CZ  1 
ATOM   5107 N  NH1 . ARG B 1 209 ? 0.200   15.822  41.194  1.00 105.34 ?  208  ARG B NH1 1 
ATOM   5108 N  NH2 . ARG B 1 209 ? 1.577   16.637  39.552  1.00 79.19  ?  208  ARG B NH2 1 
ATOM   5109 N  N   . GLU B 1 210 ? -1.481  19.618  41.316  1.00 111.53 ?  209  GLU B N   1 
ATOM   5110 C  CA  . GLU B 1 210 ? -0.474  19.829  42.354  1.00 96.65  ?  209  GLU B CA  1 
ATOM   5111 C  C   . GLU B 1 210 ? -0.921  20.804  43.436  1.00 79.65  ?  209  GLU B C   1 
ATOM   5112 O  O   . GLU B 1 210 ? -0.520  20.685  44.593  1.00 93.17  ?  209  GLU B O   1 
ATOM   5113 C  CB  . GLU B 1 210 ? 0.824   20.328  41.724  1.00 98.24  ?  209  GLU B CB  1 
ATOM   5114 C  CG  . GLU B 1 210 ? 2.062   20.033  42.533  1.00 103.98 ?  209  GLU B CG  1 
ATOM   5115 C  CD  . GLU B 1 210 ? 3.311   20.075  41.685  1.00 117.47 ?  209  GLU B CD  1 
ATOM   5116 O  OE1 . GLU B 1 210 ? 3.192   20.347  40.473  1.00 103.78 ?  209  GLU B OE1 1 
ATOM   5117 O  OE2 . GLU B 1 210 ? 4.411   19.839  42.226  1.00 137.46 ?  209  GLU B OE2 1 
ATOM   5118 N  N   . TYR B 1 211 ? -1.728  21.785  43.045  1.00 73.65  ?  210  TYR B N   1 
ATOM   5119 C  CA  . TYR B 1 211 ? -2.101  22.876  43.940  1.00 82.21  ?  210  TYR B CA  1 
ATOM   5120 C  C   . TYR B 1 211 ? -3.600  22.947  44.240  1.00 82.92  ?  210  TYR B C   1 
ATOM   5121 O  O   . TYR B 1 211 ? -4.042  23.812  44.992  1.00 87.94  ?  210  TYR B O   1 
ATOM   5122 C  CB  . TYR B 1 211 ? -1.603  24.209  43.368  1.00 77.14  ?  210  TYR B CB  1 
ATOM   5123 C  CG  . TYR B 1 211 ? -0.093  24.266  43.259  1.00 101.31 ?  210  TYR B CG  1 
ATOM   5124 C  CD1 . TYR B 1 211 ? 0.682   24.722  44.319  1.00 128.04 ?  210  TYR B CD1 1 
ATOM   5125 C  CD2 . TYR B 1 211 ? 0.561   23.843  42.108  1.00 104.02 ?  210  TYR B CD2 1 
ATOM   5126 C  CE1 . TYR B 1 211 ? 2.063   24.768  44.232  1.00 138.47 ?  210  TYR B CE1 1 
ATOM   5127 C  CE2 . TYR B 1 211 ? 1.942   23.885  42.010  1.00 116.83 ?  210  TYR B CE2 1 
ATOM   5128 C  CZ  . TYR B 1 211 ? 2.687   24.349  43.075  1.00 136.14 ?  210  TYR B CZ  1 
ATOM   5129 O  OH  . TYR B 1 211 ? 4.061   24.393  42.982  1.00 146.23 ?  210  TYR B OH  1 
ATOM   5130 N  N   . VAL B 1 212 ? -4.386  22.069  43.623  1.00 89.56  ?  211  VAL B N   1 
ATOM   5131 C  CA  . VAL B 1 212 ? -5.803  21.922  43.973  1.00 100.16 ?  211  VAL B CA  1 
ATOM   5132 C  C   . VAL B 1 212 ? -6.183  20.442  43.955  1.00 109.48 ?  211  VAL B C   1 
ATOM   5133 O  O   . VAL B 1 212 ? -5.631  19.660  43.177  1.00 112.25 ?  211  VAL B O   1 
ATOM   5134 C  CB  . VAL B 1 212 ? -6.753  22.694  43.012  1.00 121.17 ?  211  VAL B CB  1 
ATOM   5135 C  CG1 . VAL B 1 212 ? -8.154  22.794  43.612  1.00 105.44 ?  211  VAL B CG1 1 
ATOM   5136 C  CG2 . VAL B 1 212 ? -6.220  24.087  42.688  1.00 124.48 ?  211  VAL B CG2 1 
ATOM   5137 N  N   . GLY B 1 213 ? -7.129  20.056  44.802  1.00 111.22 ?  212  GLY B N   1 
ATOM   5138 C  CA  . GLY B 1 213 ? -7.594  18.685  44.798  1.00 121.42 ?  212  GLY B CA  1 
ATOM   5139 C  C   . GLY B 1 213 ? -8.923  18.636  44.079  1.00 120.69 ?  212  GLY B C   1 
ATOM   5140 O  O   . GLY B 1 213 ? -8.977  18.341  42.886  1.00 103.93 ?  212  GLY B O   1 
ATOM   5141 N  N   . CYS B 1 214 ? -9.995  18.950  44.797  1.00 133.88 ?  213  CYS B N   1 
ATOM   5142 C  CA  . CYS B 1 214 ? -11.302 19.090  44.172  1.00 137.84 ?  213  CYS B CA  1 
ATOM   5143 C  C   . CYS B 1 214 ? -11.415 20.462  43.521  1.00 144.26 ?  213  CYS B C   1 
ATOM   5144 O  O   . CYS B 1 214 ? -11.134 21.482  44.149  1.00 156.27 ?  213  CYS B O   1 
ATOM   5145 C  CB  . CYS B 1 214 ? -12.417 18.884  45.197  1.00 133.14 ?  213  CYS B CB  1 
ATOM   5146 S  SG  . CYS B 1 214 ? -12.334 17.295  46.053  1.00 204.96 ?  213  CYS B SG  1 
ATOM   5147 N  N   . VAL B 1 215 ? -11.826 20.481  42.258  1.00 135.32 ?  214  VAL B N   1 
ATOM   5148 C  CA  . VAL B 1 215 ? -11.862 21.717  41.485  1.00 120.46 ?  214  VAL B CA  1 
ATOM   5149 C  C   . VAL B 1 215 ? -13.274 22.271  41.405  1.00 107.78 ?  214  VAL B C   1 
ATOM   5150 O  O   . VAL B 1 215 ? -14.251 21.543  41.589  1.00 114.09 ?  214  VAL B O   1 
ATOM   5151 C  CB  . VAL B 1 215 ? -11.331 21.512  40.061  1.00 126.46 ?  214  VAL B CB  1 
ATOM   5152 C  CG1 . VAL B 1 215 ? -9.893  21.031  40.102  1.00 134.00 ?  214  VAL B CG1 1 
ATOM   5153 C  CG2 . VAL B 1 215 ? -12.213 20.528  39.304  1.00 131.21 ?  214  VAL B CG2 1 
ATOM   5154 N  N   . SER B 1 216 ? -13.378 23.564  41.124  1.00 97.14  ?  215  SER B N   1 
ATOM   5155 C  CA  . SER B 1 216 ? -14.682 24.196  41.015  1.00 109.17 ?  215  SER B CA  1 
ATOM   5156 C  C   . SER B 1 216 ? -15.381 23.764  39.737  1.00 121.00 ?  215  SER B C   1 
ATOM   5157 O  O   . SER B 1 216 ? -14.762 23.191  38.841  1.00 123.67 ?  215  SER B O   1 
ATOM   5158 C  CB  . SER B 1 216 ? -14.552 25.717  41.049  1.00 105.59 ?  215  SER B CB  1 
ATOM   5159 O  OG  . SER B 1 216 ? -15.824 26.329  40.942  1.00 102.56 ?  215  SER B OG  1 
ATOM   5160 N  N   . GLU B 1 217 ? -16.680 24.029  39.668  1.00 134.33 ?  216  GLU B N   1 
ATOM   5161 C  CA  . GLU B 1 217 ? -17.472 23.665  38.504  1.00 147.20 ?  216  GLU B CA  1 
ATOM   5162 C  C   . GLU B 1 217 ? -17.018 24.724  37.501  1.00 153.48 ?  216  GLU B C   1 
ATOM   5163 O  O   . GLU B 1 217 ? -16.949 24.452  36.305  1.00 161.22 ?  216  GLU B O   1 
ATOM   5164 C  CB  . GLU B 1 217 ? -18.961 23.811  38.804  1.00 155.99 ?  216  GLU B CB  1 
ATOM   5165 C  CG  . GLU B 1 217 ? -19.461 22.842  39.859  1.00 166.37 ?  216  GLU B CG  1 
ATOM   5166 C  CD  . GLU B 1 217 ? -20.940 22.552  39.721  1.00 184.30 ?  216  GLU B CD  1 
ATOM   5167 O  OE1 . GLU B 1 217 ? -21.727 23.514  39.607  1.00 193.88 ?  216  GLU B OE1 1 
ATOM   5168 O  OE2 . GLU B 1 217 ? -21.315 21.360  39.714  1.00 190.20 ?  216  GLU B OE2 1 
ATOM   5169 N  N   . GLU B 1 218 ? -16.725 25.931  37.982  1.00 149.53 ?  217  GLU B N   1 
ATOM   5170 C  CA  . GLU B 1 218 ? -16.128 26.940  37.084  1.00 144.46 ?  217  GLU B CA  1 
ATOM   5171 C  C   . GLU B 1 218 ? -15.014 26.390  36.034  1.00 108.81 ?  217  GLU B C   1 
ATOM   5172 O  O   . GLU B 1 218 ? -15.203 26.137  34.841  1.00 125.54 ?  217  GLU B O   1 
ATOM   5173 C  CB  . GLU B 1 218 ? -15.713 28.191  37.863  1.00 149.37 ?  217  GLU B CB  1 
ATOM   5174 C  CG  . GLU B 1 218 ? -16.843 28.902  38.578  1.00 165.84 ?  217  GLU B CG  1 
ATOM   5175 C  CD  . GLU B 1 218 ? -16.353 30.083  39.383  1.00 185.86 ?  217  GLU B CD  1 
ATOM   5176 O  OE1 . GLU B 1 218 ? -15.121 30.226  39.532  1.00 178.28 ?  217  GLU B OE1 1 
ATOM   5177 O  OE2 . GLU B 1 218 ? -17.200 30.864  39.869  1.00 202.56 ?  217  GLU B OE2 1 
ATOM   5178 N  N   . THR B 1 219 ? -13.944 25.978  36.706  1.00 102.08 ?  218  THR B N   1 
ATOM   5179 C  CA  . THR B 1 219 ? -12.967 25.079  36.105  1.00 101.31 ?  218  THR B CA  1 
ATOM   5180 C  C   . THR B 1 219 ? -13.284 23.761  35.407  1.00 102.11 ?  218  THR B C   1 
ATOM   5181 O  O   . THR B 1 219 ? -12.680 23.424  34.396  1.00 101.23 ?  218  THR B O   1 
ATOM   5182 C  CB  . THR B 1 219 ? -11.986 24.825  37.263  1.00 106.35 ?  218  THR B CB  1 
ATOM   5183 O  OG1 . THR B 1 219 ? -11.841 26.024  38.035  1.00 114.67 ?  218  THR B OG1 1 
ATOM   5184 C  CG2 . THR B 1 219 ? -10.620 24.417  36.729  1.00 96.31  ?  218  THR B CG2 1 
ATOM   5185 N  N   . LEU B 1 220 ? -14.240 23.020  35.955  1.00 110.11 ?  219  LEU B N   1 
ATOM   5186 C  CA  . LEU B 1 220 ? -14.624 21.723  35.406  1.00 115.81 ?  219  LEU B CA  1 
ATOM   5187 C  C   . LEU B 1 220 ? -15.153 21.828  33.974  1.00 118.55 ?  219  LEU B C   1 
ATOM   5188 O  O   . LEU B 1 220 ? -14.807 21.014  33.119  1.00 120.15 ?  219  LEU B O   1 
ATOM   5189 C  CB  . LEU B 1 220 ? -15.675 21.066  36.300  1.00 117.21 ?  219  LEU B CB  1 
ATOM   5190 C  CG  . LEU B 1 220 ? -16.034 19.616  35.987  1.00 119.33 ?  219  LEU B CG  1 
ATOM   5191 C  CD1 . LEU B 1 220 ? -14.870 18.703  36.329  1.00 118.52 ?  219  LEU B CD1 1 
ATOM   5192 C  CD2 . LEU B 1 220 ? -17.288 19.207  36.739  1.00 127.15 ?  219  LEU B CD2 1 
ATOM   5193 N  N   . LYS B 1 221 ? -15.972 22.843  33.713  1.00 116.91 ?  220  LYS B N   1 
ATOM   5194 C  CA  . LYS B 1 221 ? -16.508 23.064  32.373  1.00 115.91 ?  220  LYS B CA  1 
ATOM   5195 C  C   . LYS B 1 221 ? -15.387 23.440  31.411  1.00 99.20  ?  220  LYS B C   1 
ATOM   5196 O  O   . LYS B 1 221 ? -15.357 22.982  30.272  1.00 109.46 ?  220  LYS B O   1 
ATOM   5197 C  CB  . LYS B 1 221 ? -17.581 24.157  32.386  1.00 129.77 ?  220  LYS B CB  1 
ATOM   5198 C  CG  . LYS B 1 221 ? -18.238 24.405  31.029  1.00 145.74 ?  220  LYS B CG  1 
ATOM   5199 C  CD  . LYS B 1 221 ? -19.249 25.545  31.090  1.00 153.54 ?  220  LYS B CD  1 
ATOM   5200 C  CE  . LYS B 1 221 ? -19.890 25.792  29.730  1.00 152.57 ?  220  LYS B CE  1 
ATOM   5201 N  NZ  . LYS B 1 221 ? -20.852 26.929  29.768  1.00 148.04 ?  220  LYS B NZ  1 
ATOM   5202 N  N   . ILE B 1 222 ? -14.460 24.265  31.891  1.00 85.07  ?  221  ILE B N   1 
ATOM   5203 C  CA  . ILE B 1 222 ? -13.285 24.661  31.120  1.00 87.40  ?  221  ILE B CA  1 
ATOM   5204 C  C   . ILE B 1 222 ? -12.461 23.435  30.735  1.00 94.08  ?  221  ILE B C   1 
ATOM   5205 O  O   . ILE B 1 222 ? -11.991 23.322  29.604  1.00 93.30  ?  221  ILE B O   1 
ATOM   5206 C  CB  . ILE B 1 222 ? -12.411 25.663  31.908  1.00 83.52  ?  221  ILE B CB  1 
ATOM   5207 C  CG1 . ILE B 1 222 ? -13.111 27.022  31.984  1.00 83.75  ?  221  ILE B CG1 1 
ATOM   5208 C  CG2 . ILE B 1 222 ? -11.069 25.850  31.241  1.00 67.56  ?  221  ILE B CG2 1 
ATOM   5209 C  CD1 . ILE B 1 222 ? -12.519 27.971  33.012  1.00 66.13  ?  221  ILE B CD1 1 
ATOM   5210 N  N   . ILE B 1 223 ? -12.270 22.531  31.692  1.00 103.19 ?  222  ILE B N   1 
ATOM   5211 C  CA  . ILE B 1 223 ? -11.602 21.256  31.438  1.00 102.04 ?  222  ILE B CA  1 
ATOM   5212 C  C   . ILE B 1 223 ? -12.384 20.427  30.423  1.00 95.43  ?  222  ILE B C   1 
ATOM   5213 O  O   . ILE B 1 223 ? -11.810 19.806  29.528  1.00 102.99 ?  222  ILE B O   1 
ATOM   5214 C  CB  . ILE B 1 223 ? -11.417 20.448  32.736  1.00 103.22 ?  222  ILE B CB  1 
ATOM   5215 C  CG1 . ILE B 1 223 ? -10.599 21.255  33.747  1.00 105.46 ?  222  ILE B CG1 1 
ATOM   5216 C  CG2 . ILE B 1 223 ? -10.699 19.138  32.451  1.00 98.92  ?  222  ILE B CG2 1 
ATOM   5217 C  CD1 . ILE B 1 223 ? -10.887 20.901  35.182  1.00 108.57 ?  222  ILE B CD1 1 
ATOM   5218 N  N   . GLU B 1 224 ? -13.702 20.419  30.575  1.00 73.27  ?  223  GLU B N   1 
ATOM   5219 C  CA  . GLU B 1 224 ? -14.568 19.659  29.685  1.00 87.54  ?  223  GLU B CA  1 
ATOM   5220 C  C   . GLU B 1 224 ? -14.488 20.170  28.246  1.00 103.01 ?  223  GLU B C   1 
ATOM   5221 O  O   . GLU B 1 224 ? -14.446 19.382  27.304  1.00 105.39 ?  223  GLU B O   1 
ATOM   5222 C  CB  . GLU B 1 224 ? -16.008 19.704  30.195  1.00 100.72 ?  223  GLU B CB  1 
ATOM   5223 C  CG  . GLU B 1 224 ? -16.939 18.710  29.532  1.00 115.00 ?  223  GLU B CG  1 
ATOM   5224 C  CD  . GLU B 1 224 ? -18.357 18.802  30.062  1.00 123.62 ?  223  GLU B CD  1 
ATOM   5225 O  OE1 . GLU B 1 224 ? -18.613 19.666  30.929  1.00 121.48 ?  223  GLU B OE1 1 
ATOM   5226 O  OE2 . GLU B 1 224 ? -19.213 18.009  29.613  1.00 126.84 ?  223  GLU B OE2 1 
ATOM   5227 N  N   . GLU B 1 225 ? -14.439 21.491  28.092  1.00 111.14 ?  224  GLU B N   1 
ATOM   5228 C  CA  . GLU B 1 225 ? -14.437 22.129  26.777  1.00 107.22 ?  224  GLU B CA  1 
ATOM   5229 C  C   . GLU B 1 225 ? -13.180 21.831  25.960  1.00 107.45 ?  224  GLU B C   1 
ATOM   5230 O  O   . GLU B 1 225 ? -13.254 21.728  24.736  1.00 139.92 ?  224  GLU B O   1 
ATOM   5231 C  CB  . GLU B 1 225 ? -14.607 23.644  26.920  1.00 113.74 ?  224  GLU B CB  1 
ATOM   5232 C  CG  . GLU B 1 225 ? -16.013 24.077  27.301  1.00 136.38 ?  224  GLU B CG  1 
ATOM   5233 C  CD  . GLU B 1 225 ? -17.073 23.552  26.347  1.00 164.72 ?  224  GLU B CD  1 
ATOM   5234 O  OE1 . GLU B 1 225 ? -16.819 23.513  25.122  1.00 176.35 ?  224  GLU B OE1 1 
ATOM   5235 O  OE2 . GLU B 1 225 ? -18.167 23.182  26.823  1.00 174.82 ?  224  GLU B OE2 1 
ATOM   5236 N  N   . TRP B 1 226 ? -12.032 21.718  26.622  1.00 75.66  ?  225  TRP B N   1 
ATOM   5237 C  CA  . TRP B 1 226 ? -10.793 21.378  25.926  1.00 76.46  ?  225  TRP B CA  1 
ATOM   5238 C  C   . TRP B 1 226 ? -10.853 19.979  25.326  1.00 118.20 ?  225  TRP B C   1 
ATOM   5239 O  O   . TRP B 1 226 ? -10.463 19.766  24.179  1.00 120.01 ?  225  TRP B O   1 
ATOM   5240 C  CB  . TRP B 1 226 ? -9.587  21.468  26.855  1.00 74.71  ?  225  TRP B CB  1 
ATOM   5241 C  CG  . TRP B 1 226 ? -8.409  20.676  26.353  1.00 89.62  ?  225  TRP B CG  1 
ATOM   5242 C  CD1 . TRP B 1 226 ? -7.995  19.456  26.801  1.00 89.18  ?  225  TRP B CD1 1 
ATOM   5243 C  CD2 . TRP B 1 226 ? -7.498  21.051  25.311  1.00 98.14  ?  225  TRP B CD2 1 
ATOM   5244 N  NE1 . TRP B 1 226 ? -6.886  19.046  26.103  1.00 92.36  ?  225  TRP B NE1 1 
ATOM   5245 C  CE2 . TRP B 1 226 ? -6.559  20.006  25.184  1.00 93.11  ?  225  TRP B CE2 1 
ATOM   5246 C  CE3 . TRP B 1 226 ? -7.384  22.166  24.476  1.00 121.28 ?  225  TRP B CE3 1 
ATOM   5247 C  CZ2 . TRP B 1 226 ? -5.520  20.044  24.253  1.00 108.47 ?  225  TRP B CZ2 1 
ATOM   5248 C  CZ3 . TRP B 1 226 ? -6.349  22.203  23.551  1.00 127.34 ?  225  TRP B CZ3 1 
ATOM   5249 C  CH2 . TRP B 1 226 ? -5.432  21.148  23.449  1.00 121.94 ?  225  TRP B CH2 1 
ATOM   5250 N  N   . PHE B 1 227 ? -11.322 19.024  26.122  1.00 106.04 ?  226  PHE B N   1 
ATOM   5251 C  CA  . PHE B 1 227 ? -11.377 17.625  25.708  1.00 116.67 ?  226  PHE B CA  1 
ATOM   5252 C  C   . PHE B 1 227 ? -12.342 17.408  24.547  1.00 124.93 ?  226  PHE B C   1 
ATOM   5253 O  O   . PHE B 1 227 ? -12.134 16.525  23.715  1.00 124.17 ?  226  PHE B O   1 
ATOM   5254 C  CB  . PHE B 1 227 ? -11.750 16.740  26.894  1.00 120.59 ?  226  PHE B CB  1 
ATOM   5255 C  CG  . PHE B 1 227 ? -10.618 16.533  27.858  1.00 115.63 ?  226  PHE B CG  1 
ATOM   5256 C  CD1 . PHE B 1 227 ? -9.467  15.872  27.460  1.00 110.85 ?  226  PHE B CD1 1 
ATOM   5257 C  CD2 . PHE B 1 227 ? -10.698 17.001  29.155  1.00 104.37 ?  226  PHE B CD2 1 
ATOM   5258 C  CE1 . PHE B 1 227 ? -8.416  15.684  28.335  1.00 83.60  ?  226  PHE B CE1 1 
ATOM   5259 C  CE2 . PHE B 1 227 ? -9.650  16.814  30.035  1.00 94.62  ?  226  PHE B CE2 1 
ATOM   5260 C  CZ  . PHE B 1 227 ? -8.507  16.153  29.621  1.00 87.49  ?  226  PHE B CZ  1 
ATOM   5261 N  N   . CYS B 1 228 ? -13.410 18.198  24.516  1.00 137.44 ?  227  CYS B N   1 
ATOM   5262 C  CA  . CYS B 1 228 ? -14.343 18.197  23.392  1.00 152.87 ?  227  CYS B CA  1 
ATOM   5263 C  C   . CYS B 1 228 ? -13.732 18.875  22.160  1.00 151.22 ?  227  CYS B C   1 
ATOM   5264 O  O   . CYS B 1 228 ? -14.241 18.738  21.048  1.00 166.30 ?  227  CYS B O   1 
ATOM   5265 C  CB  . CYS B 1 228 ? -15.645 18.897  23.786  1.00 163.25 ?  227  CYS B CB  1 
ATOM   5266 S  SG  . CYS B 1 228 ? -16.528 18.106  25.145  1.00 149.55 ?  227  CYS B SG  1 
ATOM   5267 N  N   . GLY B 1 229 ? -12.637 19.600  22.374  1.00 152.11 ?  228  GLY B N   1 
ATOM   5268 C  CA  . GLY B 1 229 ? -11.933 20.294  21.311  1.00 136.84 ?  228  GLY B CA  1 
ATOM   5269 C  C   . GLY B 1 229 ? -11.307 19.357  20.295  1.00 138.11 ?  228  GLY B C   1 
ATOM   5270 O  O   . GLY B 1 229 ? -10.735 18.332  20.661  1.00 130.28 ?  228  GLY B O   1 
ATOM   5271 N  N   . GLU B 1 230 ? -11.435 19.702  19.015  1.00 153.02 ?  229  GLU B N   1 
ATOM   5272 C  CA  . GLU B 1 230 ? -10.896 18.886  17.929  1.00 165.82 ?  229  GLU B CA  1 
ATOM   5273 C  C   . GLU B 1 230 ? -9.393  18.704  18.112  1.00 160.41 ?  229  GLU B C   1 
ATOM   5274 O  O   . GLU B 1 230 ? -8.839  17.643  17.819  1.00 164.33 ?  229  GLU B O   1 
ATOM   5275 C  CB  . GLU B 1 230 ? -11.179 19.532  16.566  1.00 181.76 ?  229  GLU B CB  1 
ATOM   5276 C  CG  . GLU B 1 230 ? -12.638 19.514  16.129  1.00 188.12 ?  229  GLU B CG  1 
ATOM   5277 C  CD  . GLU B 1 230 ? -13.232 18.121  16.094  1.00 192.81 ?  229  GLU B CD  1 
ATOM   5278 O  OE1 . GLU B 1 230 ? -12.574 17.196  15.573  1.00 196.67 ?  229  GLU B OE1 1 
ATOM   5279 O  OE2 . GLU B 1 230 ? -14.366 17.954  16.589  1.00 196.26 ?  229  GLU B OE2 1 
ATOM   5280 N  N   . LYS B 1 231 ? -8.753  19.759  18.605  1.00 154.20 ?  230  LYS B N   1 
ATOM   5281 C  CA  . LYS B 1 231 ? -7.321  19.780  18.888  1.00 144.72 ?  230  LYS B CA  1 
ATOM   5282 C  C   . LYS B 1 231 ? -6.895  18.688  19.861  1.00 142.67 ?  230  LYS B C   1 
ATOM   5283 O  O   . LYS B 1 231 ? -5.849  18.069  19.687  1.00 154.32 ?  230  LYS B O   1 
ATOM   5284 C  CB  . LYS B 1 231 ? -6.927  21.153  19.428  1.00 153.50 ?  230  LYS B CB  1 
ATOM   5285 C  CG  . LYS B 1 231 ? -7.295  22.277  18.469  1.00 178.27 ?  230  LYS B CG  1 
ATOM   5286 C  CD  . LYS B 1 231 ? -7.150  23.646  19.104  1.00 177.97 ?  230  LYS B CD  1 
ATOM   5287 C  CE  . LYS B 1 231 ? -7.462  24.750  18.102  1.00 177.64 ?  230  LYS B CE  1 
ATOM   5288 N  NZ  . LYS B 1 231 ? -7.321  26.110  18.695  1.00 170.79 ?  230  LYS B NZ  1 
ATOM   5289 N  N   . ALA B 1 232 ? -7.705  18.472  20.892  1.00 136.19 ?  231  ALA B N   1 
ATOM   5290 C  CA  . ALA B 1 232 ? -7.415  17.475  21.917  1.00 133.06 ?  231  ALA B CA  1 
ATOM   5291 C  C   . ALA B 1 232 ? -7.356  16.059  21.345  1.00 139.17 ?  231  ALA B C   1 
ATOM   5292 O  O   . ALA B 1 232 ? -6.515  15.257  21.753  1.00 129.92 ?  231  ALA B O   1 
ATOM   5293 C  CB  . ALA B 1 232 ? -8.447  17.550  23.026  1.00 128.26 ?  231  ALA B CB  1 
ATOM   5294 N  N   . GLY B 1 233 ? -8.273  15.752  20.428  1.00 153.11 ?  232  GLY B N   1 
ATOM   5295 C  CA  . GLY B 1 233 ? -8.339  14.448  19.785  1.00 158.66 ?  232  GLY B CA  1 
ATOM   5296 C  C   . GLY B 1 233 ? -7.121  14.153  18.927  1.00 160.19 ?  232  GLY B C   1 
ATOM   5297 O  O   . GLY B 1 233 ? -6.563  13.060  18.958  1.00 162.20 ?  232  GLY B O   1 
ATOM   5298 N  N   . GLU B 1 234 ? -6.721  15.146  18.146  1.00 160.93 ?  233  GLU B N   1 
ATOM   5299 C  CA  . GLU B 1 234 ? -5.595  15.040  17.225  1.00 155.44 ?  233  GLU B CA  1 
ATOM   5300 C  C   . GLU B 1 234 ? -4.261  14.868  17.951  1.00 146.80 ?  233  GLU B C   1 
ATOM   5301 O  O   . GLU B 1 234 ? -3.368  14.163  17.476  1.00 138.75 ?  233  GLU B O   1 
ATOM   5302 C  CB  . GLU B 1 234 ? -5.529  16.280  16.332  1.00 158.14 ?  233  GLU B CB  1 
ATOM   5303 C  CG  . GLU B 1 234 ? -6.810  16.574  15.557  1.00 165.46 ?  233  GLU B CG  1 
ATOM   5304 C  CD  . GLU B 1 234 ? -6.823  17.970  14.963  1.00 162.12 ?  233  GLU B CD  1 
ATOM   5305 O  OE1 . GLU B 1 234 ? -5.790  18.666  15.055  1.00 157.58 ?  233  GLU B OE1 1 
ATOM   5306 O  OE2 . GLU B 1 234 ? -7.867  18.375  14.412  1.00 156.75 ?  233  GLU B OE2 1 
ATOM   5307 N  N   . VAL B 1 235 ? -4.139  15.522  19.103  1.00 163.93 ?  234  VAL B N   1 
ATOM   5308 C  CA  . VAL B 1 235 ? -2.847  15.780  19.742  1.00 181.21 ?  234  VAL B CA  1 
ATOM   5309 C  C   . VAL B 1 235 ? -2.195  14.623  20.519  1.00 174.15 ?  234  VAL B C   1 
ATOM   5310 O  O   . VAL B 1 235 ? -1.000  14.689  20.810  1.00 168.10 ?  234  VAL B O   1 
ATOM   5311 C  CB  . VAL B 1 235 ? -2.968  16.971  20.710  1.00 187.30 ?  234  VAL B CB  1 
ATOM   5312 C  CG1 . VAL B 1 235 ? -3.541  16.514  22.045  1.00 176.22 ?  234  VAL B CG1 1 
ATOM   5313 C  CG2 . VAL B 1 235 ? -1.621  17.596  20.909  1.00 198.28 ?  234  VAL B CG2 1 
ATOM   5314 N  N   . GLY B 1 236 ? -2.957  13.585  20.861  1.00 170.83 ?  235  GLY B N   1 
ATOM   5315 C  CA  . GLY B 1 236 ? -2.480  12.544  21.765  1.00 199.56 ?  235  GLY B CA  1 
ATOM   5316 C  C   . GLY B 1 236 ? -1.060  12.066  21.499  1.00 228.19 ?  235  GLY B C   1 
ATOM   5317 O  O   . GLY B 1 236 ? -0.295  11.858  22.433  1.00 216.23 ?  235  GLY B O   1 
ATOM   5318 N  N   . ASP B 1 237 ? -0.718  11.926  20.218  1.00 248.50 ?  236  ASP B N   1 
ATOM   5319 C  CA  . ASP B 1 237 ? 0.648   11.658  19.745  1.00 252.58 ?  236  ASP B CA  1 
ATOM   5320 C  C   . ASP B 1 237 ? 1.412   10.636  20.591  1.00 240.31 ?  236  ASP B C   1 
ATOM   5321 O  O   . ASP B 1 237 ? 0.998   9.483   20.725  1.00 233.39 ?  236  ASP B O   1 
ATOM   5322 C  CB  . ASP B 1 237 ? 1.443   12.973  19.678  1.00 258.86 ?  236  ASP B CB  1 
ATOM   5323 C  CG  . ASP B 1 237 ? 2.724   12.851  18.863  1.00 265.77 ?  236  ASP B CG  1 
ATOM   5324 O  OD1 . ASP B 1 237 ? 2.837   11.891  18.073  1.00 268.30 ?  236  ASP B OD1 1 
ATOM   5325 O  OD2 . ASP B 1 237 ? 3.617   13.710  19.026  1.00 266.11 ?  236  ASP B OD2 1 
ATOM   5326 N  N   . ASN B 1 238 ? 2.531   11.077  21.157  1.00 249.54 ?  237  ASN B N   1 
ATOM   5327 C  CA  . ASN B 1 238 ? 3.335   10.258  22.052  1.00 240.99 ?  237  ASN B CA  1 
ATOM   5328 C  C   . ASN B 1 238 ? 3.975   11.095  23.159  1.00 236.51 ?  237  ASN B C   1 
ATOM   5329 O  O   . ASN B 1 238 ? 4.248   12.279  22.963  1.00 235.95 ?  237  ASN B O   1 
ATOM   5330 C  CB  . ASN B 1 238 ? 4.413   9.521   21.250  1.00 232.44 ?  237  ASN B CB  1 
ATOM   5331 C  CG  . ASN B 1 238 ? 5.410   10.468  20.598  1.00 233.79 ?  237  ASN B CG  1 
ATOM   5332 O  OD1 . ASN B 1 238 ? 5.131   11.653  20.412  1.00 236.86 ?  237  ASN B OD1 1 
ATOM   5333 N  ND2 . ASN B 1 238 ? 6.578   9.944   20.239  1.00 236.12 ?  237  ASN B ND2 1 
ATOM   5334 N  N   . GLY B 1 239 ? 4.202   10.496  24.326  1.00 233.96 ?  238  GLY B N   1 
ATOM   5335 C  CA  . GLY B 1 239 ? 3.727   9.161   24.645  1.00 239.88 ?  238  GLY B CA  1 
ATOM   5336 C  C   . GLY B 1 239 ? 4.669   8.029   24.290  1.00 246.69 ?  238  GLY B C   1 
ATOM   5337 O  O   . GLY B 1 239 ? 4.312   6.866   24.449  1.00 247.00 ?  238  GLY B O   1 
ATOM   5338 N  N   . ILE B 1 240 ? 5.867   8.375   23.825  1.00 248.80 ?  239  ILE B N   1 
ATOM   5339 C  CA  . ILE B 1 240 ? 6.848   7.405   23.339  1.00 265.46 ?  239  ILE B CA  1 
ATOM   5340 C  C   . ILE B 1 240 ? 7.250   6.497   24.512  1.00 271.13 ?  239  ILE B C   1 
ATOM   5341 O  O   . ILE B 1 240 ? 7.324   6.965   25.650  1.00 261.96 ?  239  ILE B O   1 
ATOM   5342 C  CB  . ILE B 1 240 ? 8.079   8.152   22.710  1.00 207.12 ?  239  ILE B CB  1 
ATOM   5343 C  CG1 . ILE B 1 240 ? 8.741   7.347   21.584  1.00 209.72 ?  239  ILE B CG1 1 
ATOM   5344 C  CG2 . ILE B 1 240 ? 9.085   8.587   23.772  1.00 206.20 ?  239  ILE B CG2 1 
ATOM   5345 C  CD1 . ILE B 1 240 ? 10.074  7.892   21.129  1.00 212.99 ?  239  ILE B CD1 1 
ATOM   5346 N  N   . GLY B 1 241 ? 7.473   5.203   24.271  1.00 279.08 ?  240  GLY B N   1 
ATOM   5347 C  CA  . GLY B 1 241 ? 7.480   4.580   22.952  1.00 283.35 ?  240  GLY B CA  1 
ATOM   5348 C  C   . GLY B 1 241 ? 6.266   4.171   22.107  1.00 279.79 ?  240  GLY B C   1 
ATOM   5349 O  O   . GLY B 1 241 ? 6.409   4.143   20.884  1.00 282.88 ?  240  GLY B O   1 
ATOM   5350 N  N   . SER B 1 242 ? 5.092   3.855   22.666  1.00 255.55 ?  241  SER B N   1 
ATOM   5351 C  CA  . SER B 1 242 ? 4.763   3.932   24.086  1.00 221.74 ?  241  SER B CA  1 
ATOM   5352 C  C   . SER B 1 242 ? 5.451   2.865   24.917  1.00 207.56 ?  241  SER B C   1 
ATOM   5353 O  O   . SER B 1 242 ? 5.739   1.767   24.439  1.00 210.24 ?  241  SER B O   1 
ATOM   5354 C  CB  . SER B 1 242 ? 3.245   3.826   24.281  1.00 197.05 ?  241  SER B CB  1 
ATOM   5355 O  OG  . SER B 1 242 ? 2.561   4.877   23.617  1.00 182.59 ?  241  SER B OG  1 
ATOM   5356 N  N   . ASP B 1 243 ? 5.700   3.202   26.175  1.00 186.97 ?  242  ASP B N   1 
ATOM   5357 C  CA  . ASP B 1 243 ? 6.277   2.267   27.119  1.00 181.39 ?  242  ASP B CA  1 
ATOM   5358 C  C   . ASP B 1 243 ? 5.483   2.342   28.410  1.00 174.26 ?  242  ASP B C   1 
ATOM   5359 O  O   . ASP B 1 243 ? 5.765   3.179   29.268  1.00 173.50 ?  242  ASP B O   1 
ATOM   5360 C  CB  . ASP B 1 243 ? 7.756   2.580   27.362  1.00 196.97 ?  242  ASP B CB  1 
ATOM   5361 C  CG  . ASP B 1 243 ? 8.490   1.447   28.055  1.00 214.74 ?  242  ASP B CG  1 
ATOM   5362 O  OD1 . ASP B 1 243 ? 7.900   0.801   28.946  1.00 222.43 ?  242  ASP B OD1 1 
ATOM   5363 O  OD2 . ASP B 1 243 ? 9.663   1.200   27.707  1.00 218.98 ?  242  ASP B OD2 1 
ATOM   5364 N  N   . VAL B 1 244 ? 4.475   1.483   28.532  1.00 170.31 ?  243  VAL B N   1 
ATOM   5365 C  CA  . VAL B 1 244 ? 3.661   1.442   29.738  1.00 158.70 ?  243  VAL B CA  1 
ATOM   5366 C  C   . VAL B 1 244 ? 4.556   1.151   30.943  1.00 171.70 ?  243  VAL B C   1 
ATOM   5367 O  O   . VAL B 1 244 ? 4.311   1.647   32.037  1.00 174.94 ?  243  VAL B O   1 
ATOM   5368 C  CB  . VAL B 1 244 ? 2.528   0.399   29.634  1.00 146.57 ?  243  VAL B CB  1 
ATOM   5369 C  CG1 . VAL B 1 244 ? 1.515   0.826   28.581  1.00 140.26 ?  243  VAL B CG1 1 
ATOM   5370 C  CG2 . VAL B 1 244 ? 3.084   -0.983  29.313  1.00 152.13 ?  243  VAL B CG2 1 
ATOM   5371 N  N   . GLY B 1 245 ? 5.599   0.353   30.724  1.00 189.21 ?  244  GLY B N   1 
ATOM   5372 C  CA  . GLY B 1 245 ? 6.582   0.058   31.749  1.00 198.05 ?  244  GLY B CA  1 
ATOM   5373 C  C   . GLY B 1 245 ? 7.317   1.296   32.232  1.00 202.13 ?  244  GLY B C   1 
ATOM   5374 O  O   . GLY B 1 245 ? 7.407   1.533   33.433  1.00 198.56 ?  244  GLY B O   1 
ATOM   5375 N  N   . MET B 1 246 ? 7.834   2.089   31.295  1.00 202.63 ?  245  MET B N   1 
ATOM   5376 C  CA  . MET B 1 246 ? 8.532   3.329   31.637  1.00 188.81 ?  245  MET B CA  1 
ATOM   5377 C  C   . MET B 1 246 ? 7.589   4.313   32.306  1.00 172.78 ?  245  MET B C   1 
ATOM   5378 O  O   . MET B 1 246 ? 7.951   4.967   33.283  1.00 180.25 ?  245  MET B O   1 
ATOM   5379 C  CB  . MET B 1 246 ? 9.145   3.982   30.394  1.00 193.30 ?  245  MET B CB  1 
ATOM   5380 C  CG  . MET B 1 246 ? 9.667   5.399   30.632  1.00 192.17 ?  245  MET B CG  1 
ATOM   5381 S  SD  . MET B 1 246 ? 10.223  6.258   29.142  1.00 153.98 ?  245  MET B SD  1 
ATOM   5382 C  CE  . MET B 1 246 ? 11.663  5.288   28.698  1.00 183.00 ?  245  MET B CE  1 
ATOM   5383 N  N   . LEU B 1 247 ? 6.380   4.418   31.767  1.00 168.46 ?  246  LEU B N   1 
ATOM   5384 C  CA  . LEU B 1 247 ? 5.376   5.315   32.319  1.00 160.85 ?  246  LEU B CA  1 
ATOM   5385 C  C   . LEU B 1 247 ? 4.987   4.882   33.731  1.00 160.81 ?  246  LEU B C   1 
ATOM   5386 O  O   . LEU B 1 247 ? 4.989   5.693   34.653  1.00 160.80 ?  246  LEU B O   1 
ATOM   5387 C  CB  . LEU B 1 247 ? 4.143   5.362   31.415  1.00 148.88 ?  246  LEU B CB  1 
ATOM   5388 C  CG  . LEU B 1 247 ? 4.149   6.422   30.310  1.00 145.55 ?  246  LEU B CG  1 
ATOM   5389 C  CD1 . LEU B 1 247 ? 2.821   6.422   29.570  1.00 148.01 ?  246  LEU B CD1 1 
ATOM   5390 C  CD2 . LEU B 1 247 ? 4.463   7.805   30.865  1.00 145.25 ?  246  LEU B CD2 1 
ATOM   5391 N  N   . ARG B 1 248 ? 4.666   3.598   33.892  1.00 150.95 ?  247  ARG B N   1 
ATOM   5392 C  CA  . ARG B 1 248 ? 4.273   3.044   35.189  1.00 143.12 ?  247  ARG B CA  1 
ATOM   5393 C  C   . ARG B 1 248 ? 5.432   3.091   36.184  1.00 140.90 ?  247  ARG B C   1 
ATOM   5394 O  O   . ARG B 1 248 ? 5.221   3.273   37.383  1.00 144.67 ?  247  ARG B O   1 
ATOM   5395 C  CB  . ARG B 1 248 ? 3.762   1.610   35.031  1.00 146.46 ?  247  ARG B CB  1 
ATOM   5396 C  CG  . ARG B 1 248 ? 3.067   1.033   36.258  1.00 137.14 ?  247  ARG B CG  1 
ATOM   5397 C  CD  . ARG B 1 248 ? 2.305   -0.236  35.897  1.00 127.79 ?  247  ARG B CD  1 
ATOM   5398 N  NE  . ARG B 1 248 ? 3.123   -1.154  35.109  1.00 124.10 ?  247  ARG B NE  1 
ATOM   5399 C  CZ  . ARG B 1 248 ? 2.645   -2.199  34.441  1.00 118.68 ?  247  ARG B CZ  1 
ATOM   5400 N  NH1 . ARG B 1 248 ? 1.346   -2.463  34.460  1.00 123.32 ?  247  ARG B NH1 1 
ATOM   5401 N  NH2 . ARG B 1 248 ? 3.465   -2.978  33.749  1.00 115.44 ?  247  ARG B NH2 1 
ATOM   5402 N  N   . GLU B 1 249 ? 6.653   2.919   35.681  1.00 139.65 ?  248  GLU B N   1 
ATOM   5403 C  CA  . GLU B 1 249 ? 7.850   3.062   36.506  1.00 136.38 ?  248  GLU B CA  1 
ATOM   5404 C  C   . GLU B 1 249 ? 7.963   4.509   36.960  1.00 125.77 ?  248  GLU B C   1 
ATOM   5405 O  O   . GLU B 1 249 ? 8.355   4.792   38.092  1.00 125.81 ?  248  GLU B O   1 
ATOM   5406 C  CB  . GLU B 1 249 ? 9.101   2.640   35.734  1.00 144.35 ?  248  GLU B CB  1 
ATOM   5407 C  CG  . GLU B 1 249 ? 10.415  2.937   36.433  1.00 159.52 ?  248  GLU B CG  1 
ATOM   5408 C  CD  . GLU B 1 249 ? 11.611  2.456   35.635  1.00 175.59 ?  248  GLU B CD  1 
ATOM   5409 O  OE1 . GLU B 1 249 ? 11.428  2.072   34.459  1.00 174.94 ?  248  GLU B OE1 1 
ATOM   5410 O  OE2 . GLU B 1 249 ? 12.733  2.457   36.182  1.00 186.77 ?  248  GLU B OE2 1 
ATOM   5411 N  N   . ALA B 1 250 ? 7.615   5.418   36.054  1.00 123.91 ?  249  ALA B N   1 
ATOM   5412 C  CA  . ALA B 1 250 ? 7.586   6.844   36.347  1.00 109.88 ?  249  ALA B CA  1 
ATOM   5413 C  C   . ALA B 1 250 ? 6.358   7.183   37.192  1.00 106.62 ?  249  ALA B C   1 
ATOM   5414 O  O   . ALA B 1 250 ? 6.404   8.098   38.011  1.00 101.08 ?  249  ALA B O   1 
ATOM   5415 C  CB  . ALA B 1 250 ? 7.601   7.660   35.065  1.00 108.40 ?  249  ALA B CB  1 
ATOM   5416 N  N   . VAL B 1 251 ? 5.253   6.470   36.972  1.00 117.31 ?  250  VAL B N   1 
ATOM   5417 C  CA  . VAL B 1 251 ? 4.055   6.670   37.788  1.00 116.04 ?  250  VAL B CA  1 
ATOM   5418 C  C   . VAL B 1 251 ? 4.364   6.275   39.227  1.00 121.63 ?  250  VAL B C   1 
ATOM   5419 O  O   . VAL B 1 251 ? 3.966   6.960   40.161  1.00 125.81 ?  250  VAL B O   1 
ATOM   5420 C  CB  . VAL B 1 251 ? 2.836   5.838   37.295  1.00 164.05 ?  250  VAL B CB  1 
ATOM   5421 C  CG1 . VAL B 1 251 ? 1.727   5.832   38.341  1.00 160.60 ?  250  VAL B CG1 1 
ATOM   5422 C  CG2 . VAL B 1 251 ? 2.297   6.370   35.988  1.00 158.93 ?  250  VAL B CG2 1 
ATOM   5423 N  N   . LEU B 1 252 ? 5.086   5.170   39.392  1.00 116.33 ?  251  LEU B N   1 
ATOM   5424 C  CA  . LEU B 1 252 ? 5.455   4.673   40.713  1.00 112.83 ?  251  LEU B CA  1 
ATOM   5425 C  C   . LEU B 1 252 ? 6.382   5.639   41.437  1.00 121.39 ?  251  LEU B C   1 
ATOM   5426 O  O   . LEU B 1 252 ? 6.210   5.913   42.624  1.00 139.46 ?  251  LEU B O   1 
ATOM   5427 C  CB  . LEU B 1 252 ? 6.124   3.298   40.590  1.00 119.93 ?  251  LEU B CB  1 
ATOM   5428 C  CG  . LEU B 1 252 ? 6.505   2.512   41.849  1.00 125.66 ?  251  LEU B CG  1 
ATOM   5429 C  CD1 . LEU B 1 252 ? 6.274   1.026   41.613  1.00 123.57 ?  251  LEU B CD1 1 
ATOM   5430 C  CD2 . LEU B 1 252 ? 7.954   2.760   42.264  1.00 111.81 ?  251  LEU B CD2 1 
ATOM   5431 N  N   . ASN B 1 253 ? 7.362   6.152   40.703  1.00 128.09 ?  252  ASN B N   1 
ATOM   5432 C  CA  . ASN B 1 253 ? 8.429   6.963   41.281  1.00 133.97 ?  252  ASN B CA  1 
ATOM   5433 C  C   . ASN B 1 253 ? 7.917   8.328   41.773  1.00 140.81 ?  252  ASN B C   1 
ATOM   5434 O  O   . ASN B 1 253 ? 8.459   8.903   42.714  1.00 143.08 ?  252  ASN B O   1 
ATOM   5435 C  CB  . ASN B 1 253 ? 9.542   7.131   40.240  1.00 131.05 ?  252  ASN B CB  1 
ATOM   5436 C  CG  . ASN B 1 253 ? 10.844  7.634   40.827  1.00 137.93 ?  252  ASN B CG  1 
ATOM   5437 O  OD1 . ASN B 1 253 ? 10.888  8.178   41.926  1.00 142.14 ?  252  ASN B OD1 1 
ATOM   5438 N  ND2 . ASN B 1 253 ? 11.928  7.436   40.085  1.00 144.41 ?  252  ASN B ND2 1 
ATOM   5439 N  N   . ASN B 1 254 ? 6.840   8.818   41.166  1.00 161.15 ?  253  ASN B N   1 
ATOM   5440 C  CA  . ASN B 1 254 ? 6.322   10.158  41.462  1.00 162.48 ?  253  ASN B CA  1 
ATOM   5441 C  C   . ASN B 1 254 ? 5.192   10.175  42.495  1.00 138.80 ?  253  ASN B C   1 
ATOM   5442 O  O   . ASN B 1 254 ? 4.407   11.125  42.559  1.00 136.34 ?  253  ASN B O   1 
ATOM   5443 C  CB  . ASN B 1 254 ? 5.845   10.836  40.173  1.00 171.90 ?  253  ASN B CB  1 
ATOM   5444 C  CG  . ASN B 1 254 ? 6.985   11.160  39.221  1.00 175.59 ?  253  ASN B CG  1 
ATOM   5445 O  OD1 . ASN B 1 254 ? 7.614   12.213  39.326  1.00 174.59 ?  253  ASN B OD1 1 
ATOM   5446 N  ND2 . ASN B 1 254 ? 7.249   10.261  38.281  1.00 180.24 ?  253  ASN B ND2 1 
ATOM   5447 N  N   . GLY B 1 255 ? 5.102   9.122   43.297  1.00 133.84 ?  254  GLY B N   1 
ATOM   5448 C  CA  . GLY B 1 255 ? 3.996   8.978   44.224  1.00 129.51 ?  254  GLY B CA  1 
ATOM   5449 C  C   . GLY B 1 255 ? 2.917   8.172   43.542  1.00 129.28 ?  254  GLY B C   1 
ATOM   5450 O  O   . GLY B 1 255 ? 3.142   7.635   42.471  1.00 135.50 ?  254  GLY B O   1 
ATOM   5451 N  N   . GLY B 1 256 ? 1.746   8.073   44.152  1.00 133.11 ?  255  GLY B N   1 
ATOM   5452 C  CA  . GLY B 1 256 ? 0.661   7.340   43.530  1.00 166.27 ?  255  GLY B CA  1 
ATOM   5453 C  C   . GLY B 1 256 ? 0.054   8.023   42.316  1.00 167.35 ?  255  GLY B C   1 
ATOM   5454 O  O   . GLY B 1 256 ? -0.353  7.372   41.351  1.00 148.10 ?  255  GLY B O   1 
ATOM   5455 N  N   . GLY B 1 257 ? 0.025   9.349   42.357  1.00 176.73 ?  256  GLY B N   1 
ATOM   5456 C  CA  . GLY B 1 257 ? -0.844  10.139  41.501  1.00 164.87 ?  256  GLY B CA  1 
ATOM   5457 C  C   . GLY B 1 257 ? -0.651  10.240  39.999  1.00 150.63 ?  256  GLY B C   1 
ATOM   5458 O  O   . GLY B 1 257 ? -1.629  10.190  39.255  1.00 155.56 ?  256  GLY B O   1 
ATOM   5459 N  N   . TRP B 1 258 ? 0.587   10.381  39.537  1.00 135.42 ?  257  TRP B N   1 
ATOM   5460 C  CA  . TRP B 1 258 ? 0.798   10.886  38.185  1.00 125.73 ?  257  TRP B CA  1 
ATOM   5461 C  C   . TRP B 1 258 ? 2.114   10.494  37.511  1.00 133.13 ?  257  TRP B C   1 
ATOM   5462 O  O   . TRP B 1 258 ? 3.063   10.069  38.167  1.00 123.98 ?  257  TRP B O   1 
ATOM   5463 C  CB  . TRP B 1 258 ? 0.702   12.410  38.221  1.00 124.65 ?  257  TRP B CB  1 
ATOM   5464 C  CG  . TRP B 1 258 ? 1.711   13.021  39.149  1.00 132.15 ?  257  TRP B CG  1 
ATOM   5465 C  CD1 . TRP B 1 258 ? 1.624   13.117  40.509  1.00 133.46 ?  257  TRP B CD1 1 
ATOM   5466 C  CD2 . TRP B 1 258 ? 2.961   13.617  38.788  1.00 136.23 ?  257  TRP B CD2 1 
ATOM   5467 N  NE1 . TRP B 1 258 ? 2.742   13.733  41.014  1.00 133.79 ?  257  TRP B NE1 1 
ATOM   5468 C  CE2 . TRP B 1 258 ? 3.581   14.053  39.975  1.00 133.35 ?  257  TRP B CE2 1 
ATOM   5469 C  CE3 . TRP B 1 258 ? 3.620   13.827  37.571  1.00 141.61 ?  257  TRP B CE3 1 
ATOM   5470 C  CZ2 . TRP B 1 258 ? 4.820   14.683  39.986  1.00 138.01 ?  257  TRP B CZ2 1 
ATOM   5471 C  CZ3 . TRP B 1 258 ? 4.851   14.453  37.583  1.00 144.72 ?  257  TRP B CZ3 1 
ATOM   5472 C  CH2 . TRP B 1 258 ? 5.439   14.874  38.782  1.00 141.99 ?  257  TRP B CH2 1 
ATOM   5473 N  N   . HIS B 1 259 ? 2.137   10.627  36.184  1.00 145.57 ?  258  HIS B N   1 
ATOM   5474 C  CA  . HIS B 1 259 ? 3.362   10.527  35.386  1.00 154.97 ?  258  HIS B CA  1 
ATOM   5475 C  C   . HIS B 1 259 ? 3.582   11.794  34.551  1.00 161.45 ?  258  HIS B C   1 
ATOM   5476 O  O   . HIS B 1 259 ? 2.642   12.347  33.984  1.00 169.59 ?  258  HIS B O   1 
ATOM   5477 C  CB  . HIS B 1 259 ? 3.317   9.289   34.489  1.00 156.27 ?  258  HIS B CB  1 
ATOM   5478 C  CG  . HIS B 1 259 ? 2.270   9.347   33.421  1.00 152.30 ?  258  HIS B CG  1 
ATOM   5479 N  ND1 . HIS B 1 259 ? 2.429   10.069  32.258  1.00 144.41 ?  258  HIS B ND1 1 
ATOM   5480 C  CD2 . HIS B 1 259 ? 1.043   8.779   33.347  1.00 153.08 ?  258  HIS B CD2 1 
ATOM   5481 C  CE1 . HIS B 1 259 ? 1.350   9.932   31.507  1.00 137.76 ?  258  HIS B CE1 1 
ATOM   5482 N  NE2 . HIS B 1 259 ? 0.493   9.159   32.147  1.00 147.83 ?  258  HIS B NE2 1 
ATOM   5483 N  N   . GLY B 1 260 ? 4.831   12.242  34.479  1.00 158.59 ?  259  GLY B N   1 
ATOM   5484 C  CA  . GLY B 1 260 ? 5.167   13.520  33.871  1.00 149.98 ?  259  GLY B CA  1 
ATOM   5485 C  C   . GLY B 1 260 ? 5.254   13.673  32.358  1.00 132.94 ?  259  GLY B C   1 
ATOM   5486 O  O   . GLY B 1 260 ? 5.115   14.785  31.849  1.00 128.15 ?  259  GLY B O   1 
ATOM   5487 N  N   . HIS B 1 261 ? 5.504   12.579  31.643  1.00 125.39 ?  260  HIS B N   1 
ATOM   5488 C  CA  . HIS B 1 261 ? 5.981   12.638  30.256  1.00 128.73 ?  260  HIS B CA  1 
ATOM   5489 C  C   . HIS B 1 261 ? 5.091   13.364  29.231  1.00 123.06 ?  260  HIS B C   1 
ATOM   5490 O  O   . HIS B 1 261 ? 5.612   14.020  28.333  1.00 121.90 ?  260  HIS B O   1 
ATOM   5491 C  CB  . HIS B 1 261 ? 6.259   11.220  29.760  1.00 135.55 ?  260  HIS B CB  1 
ATOM   5492 C  CG  . HIS B 1 261 ? 7.479   10.598  30.368  1.00 139.49 ?  260  HIS B CG  1 
ATOM   5493 N  ND1 . HIS B 1 261 ? 7.528   10.188  31.683  1.00 140.46 ?  260  HIS B ND1 1 
ATOM   5494 C  CD2 . HIS B 1 261 ? 8.697   10.324  29.843  1.00 146.80 ?  260  HIS B CD2 1 
ATOM   5495 C  CE1 . HIS B 1 261 ? 8.722   9.683   31.940  1.00 145.74 ?  260  HIS B CE1 1 
ATOM   5496 N  NE2 . HIS B 1 261 ? 9.450   9.754   30.841  1.00 149.81 ?  260  HIS B NE2 1 
ATOM   5497 N  N   . GLY B 1 262 ? 3.771   13.241  29.332  1.00 111.07 ?  261  GLY B N   1 
ATOM   5498 C  CA  . GLY B 1 262 ? 2.900   13.976  28.426  1.00 88.22  ?  261  GLY B CA  1 
ATOM   5499 C  C   . GLY B 1 262 ? 1.578   13.320  28.075  1.00 123.57 ?  261  GLY B C   1 
ATOM   5500 O  O   . GLY B 1 262 ? 0.993   12.607  28.890  1.00 121.58 ?  261  GLY B O   1 
ATOM   5501 N  N   . TRP B 1 263 ? 1.101   13.572  26.857  1.00 110.92 ?  262  TRP B N   1 
ATOM   5502 C  CA  . TRP B 1 263 ? -0.159  12.997  26.394  1.00 107.16 ?  262  TRP B CA  1 
ATOM   5503 C  C   . TRP B 1 263 ? 0.077   11.592  25.851  1.00 115.07 ?  262  TRP B C   1 
ATOM   5504 O  O   . TRP B 1 263 ? 1.171   11.278  25.373  1.00 106.93 ?  262  TRP B O   1 
ATOM   5505 C  CB  . TRP B 1 263 ? -0.803  13.864  25.316  1.00 95.65  ?  262  TRP B CB  1 
ATOM   5506 C  CG  . TRP B 1 263 ? -1.073  15.269  25.739  1.00 93.45  ?  262  TRP B CG  1 
ATOM   5507 C  CD1 . TRP B 1 263 ? -0.280  16.357  25.521  1.00 98.07  ?  262  TRP B CD1 1 
ATOM   5508 C  CD2 . TRP B 1 263 ? -2.206  15.738  26.483  1.00 91.33  ?  262  TRP B CD2 1 
ATOM   5509 N  NE1 . TRP B 1 263 ? -0.860  17.479  26.063  1.00 101.63 ?  262  TRP B NE1 1 
ATOM   5510 C  CE2 . TRP B 1 263 ? -2.039  17.126  26.662  1.00 94.51  ?  262  TRP B CE2 1 
ATOM   5511 C  CE3 . TRP B 1 263 ? -3.345  15.120  27.006  1.00 81.80  ?  262  TRP B CE3 1 
ATOM   5512 C  CZ2 . TRP B 1 263 ? -2.973  17.906  27.346  1.00 78.93  ?  262  TRP B CZ2 1 
ATOM   5513 C  CZ3 . TRP B 1 263 ? -4.270  15.897  27.682  1.00 79.50  ?  262  TRP B CZ3 1 
ATOM   5514 C  CH2 . TRP B 1 263 ? -4.078  17.275  27.846  1.00 78.04  ?  262  TRP B CH2 1 
ATOM   5515 N  N   . VAL B 1 264 ? -0.950  10.749  25.923  1.00 125.08 ?  263  VAL B N   1 
ATOM   5516 C  CA  . VAL B 1 264 ? -0.830  9.362   25.481  1.00 139.16 ?  263  VAL B CA  1 
ATOM   5517 C  C   . VAL B 1 264 ? -1.928  8.967   24.494  1.00 139.20 ?  263  VAL B C   1 
ATOM   5518 O  O   . VAL B 1 264 ? -3.078  9.375   24.647  1.00 130.02 ?  263  VAL B O   1 
ATOM   5519 C  CB  . VAL B 1 264 ? -0.868  8.393   26.688  1.00 146.91 ?  263  VAL B CB  1 
ATOM   5520 C  CG1 . VAL B 1 264 ? -0.731  6.947   26.233  1.00 148.92 ?  263  VAL B CG1 1 
ATOM   5521 C  CG2 . VAL B 1 264 ? 0.229   8.736   27.683  1.00 154.16 ?  263  VAL B CG2 1 
ATOM   5522 N  N   . GLY B 1 265 ? -1.558  8.158   23.500  1.00 152.63 ?  264  GLY B N   1 
ATOM   5523 C  CA  . GLY B 1 265 ? -2.503  7.503   22.608  1.00 163.63 ?  264  GLY B CA  1 
ATOM   5524 C  C   . GLY B 1 265 ? -3.036  8.269   21.412  1.00 169.12 ?  264  GLY B C   1 
ATOM   5525 O  O   . GLY B 1 265 ? -2.557  9.352   21.079  1.00 164.60 ?  264  GLY B O   1 
ATOM   5526 N  N   . GLU B 1 266 ? -4.034  7.681   20.755  1.00 181.94 ?  265  GLU B N   1 
ATOM   5527 C  CA  . GLU B 1 266 ? -4.639  8.261   19.558  1.00 185.86 ?  265  GLU B CA  1 
ATOM   5528 C  C   . GLU B 1 266 ? -6.156  8.331   19.655  1.00 177.29 ?  265  GLU B C   1 
ATOM   5529 O  O   . GLU B 1 266 ? -6.778  7.626   20.450  1.00 165.92 ?  265  GLU B O   1 
ATOM   5530 C  CB  . GLU B 1 266 ? -4.288  7.454   18.306  1.00 190.45 ?  265  GLU B CB  1 
ATOM   5531 C  CG  . GLU B 1 266 ? -2.817  7.314   17.978  1.00 187.44 ?  265  GLU B CG  1 
ATOM   5532 C  CD  . GLU B 1 266 ? -2.571  6.225   16.950  1.00 180.63 ?  265  GLU B CD  1 
ATOM   5533 O  OE1 . GLU B 1 266 ? -3.555  5.602   16.499  1.00 171.23 ?  265  GLU B OE1 1 
ATOM   5534 O  OE2 . GLU B 1 266 ? -1.399  6.000   16.586  1.00 184.01 ?  265  GLU B OE2 1 
ATOM   5535 N  N   . GLY B 1 267 ? -6.746  9.194   18.836  1.00 175.40 ?  266  GLY B N   1 
ATOM   5536 C  CA  . GLY B 1 267 ? -8.187  9.244   18.706  1.00 173.72 ?  266  GLY B CA  1 
ATOM   5537 C  C   . GLY B 1 267 ? -8.774  10.360  19.535  1.00 156.49 ?  266  GLY B C   1 
ATOM   5538 O  O   . GLY B 1 267 ? -8.051  11.177  20.096  1.00 149.79 ?  266  GLY B O   1 
ATOM   5539 N  N   . LYS B 1 268 ? -10.094 10.381  19.631  1.00 149.83 ?  267  LYS B N   1 
ATOM   5540 C  CA  . LYS B 1 268 ? -10.772 11.417  20.388  1.00 136.81 ?  267  LYS B CA  1 
ATOM   5541 C  C   . LYS B 1 268 ? -10.916 10.972  21.839  1.00 134.47 ?  267  LYS B C   1 
ATOM   5542 O  O   . LYS B 1 268 ? -10.791 9.785   22.154  1.00 116.12 ?  267  LYS B O   1 
ATOM   5543 C  CB  . LYS B 1 268 ? -12.144 11.730  19.785  1.00 129.05 ?  267  LYS B CB  1 
ATOM   5544 C  CG  . LYS B 1 268 ? -13.024 10.505  19.599  1.00 138.84 ?  267  LYS B CG  1 
ATOM   5545 C  CD  . LYS B 1 268 ? -14.455 10.762  20.044  1.00 135.76 ?  267  LYS B CD  1 
ATOM   5546 C  CE  . LYS B 1 268 ? -15.258 9.468   20.046  1.00 122.90 ?  267  LYS B CE  1 
ATOM   5547 N  NZ  . LYS B 1 268 ? -16.626 9.645   20.609  1.00 107.00 ?  267  LYS B NZ  1 
ATOM   5548 N  N   . TRP B 1 269 ? -11.147 11.939  22.719  1.00 139.57 ?  268  TRP B N   1 
ATOM   5549 C  CA  . TRP B 1 269 ? -11.315 11.676  24.141  1.00 143.44 ?  268  TRP B CA  1 
ATOM   5550 C  C   . TRP B 1 269 ? -12.755 11.264  24.430  1.00 142.74 ?  268  TRP B C   1 
ATOM   5551 O  O   . TRP B 1 269 ? -13.684 11.712  23.755  1.00 142.02 ?  268  TRP B O   1 
ATOM   5552 C  CB  . TRP B 1 269 ? -10.944 12.909  24.965  1.00 135.91 ?  268  TRP B CB  1 
ATOM   5553 C  CG  . TRP B 1 269 ? -9.490  13.274  24.933  1.00 134.20 ?  268  TRP B CG  1 
ATOM   5554 C  CD1 . TRP B 1 269 ? -8.925  14.324  24.272  1.00 134.97 ?  268  TRP B CD1 1 
ATOM   5555 C  CD2 . TRP B 1 269 ? -8.423  12.621  25.637  1.00 132.10 ?  268  TRP B CD2 1 
ATOM   5556 N  NE1 . TRP B 1 269 ? -7.569  14.349  24.497  1.00 141.06 ?  268  TRP B NE1 1 
ATOM   5557 C  CE2 . TRP B 1 269 ? -7.236  13.317  25.334  1.00 138.99 ?  268  TRP B CE2 1 
ATOM   5558 C  CE3 . TRP B 1 269 ? -8.355  11.510  26.480  1.00 128.29 ?  268  TRP B CE3 1 
ATOM   5559 C  CZ2 . TRP B 1 269 ? -5.995  12.937  25.848  1.00 138.51 ?  268  TRP B CZ2 1 
ATOM   5560 C  CZ3 . TRP B 1 269 ? -7.124  11.140  26.993  1.00 138.27 ?  268  TRP B CZ3 1 
ATOM   5561 C  CH2 . TRP B 1 269 ? -5.961  11.848  26.672  1.00 137.35 ?  268  TRP B CH2 1 
ATOM   5562 N  N   . THR B 1 270 ? -12.939 10.410  25.431  1.00 136.90 ?  269  THR B N   1 
ATOM   5563 C  CA  . THR B 1 270 ? -14.279 10.060  25.881  1.00 130.35 ?  269  THR B CA  1 
ATOM   5564 C  C   . THR B 1 270 ? -14.509 10.555  27.303  1.00 122.58 ?  269  THR B C   1 
ATOM   5565 O  O   . THR B 1 270 ? -13.793 10.176  28.230  1.00 117.10 ?  269  THR B O   1 
ATOM   5566 C  CB  . THR B 1 270 ? -14.506 8.538   25.827  1.00 136.55 ?  269  THR B CB  1 
ATOM   5567 O  OG1 . THR B 1 270 ? -14.253 8.059   24.500  1.00 139.34 ?  269  THR B OG1 1 
ATOM   5568 C  CG2 . THR B 1 270 ? -15.932 8.193   26.229  1.00 141.24 ?  269  THR B CG2 1 
ATOM   5569 N  N   . VAL B 1 271 ? -15.538 11.379  27.470  1.00 120.61 ?  270  VAL B N   1 
ATOM   5570 C  CA  . VAL B 1 271 ? -15.811 12.024  28.748  1.00 107.32 ?  270  VAL B CA  1 
ATOM   5571 C  C   . VAL B 1 271 ? -17.078 11.478  29.392  1.00 120.15 ?  270  VAL B C   1 
ATOM   5572 O  O   . VAL B 1 271 ? -18.146 11.484  28.787  1.00 127.24 ?  270  VAL B O   1 
ATOM   5573 C  CB  . VAL B 1 271 ? -15.949 13.556  28.581  1.00 96.93  ?  270  VAL B CB  1 
ATOM   5574 C  CG1 . VAL B 1 271 ? -16.450 14.200  29.866  1.00 93.19  ?  270  VAL B CG1 1 
ATOM   5575 C  CG2 . VAL B 1 271 ? -14.625 14.169  28.143  1.00 83.64  ?  270  VAL B CG2 1 
ATOM   5576 N  N   . LYS B 1 272 ? -16.953 11.011  30.628  1.00 135.85 ?  271  LYS B N   1 
ATOM   5577 C  CA  . LYS B 1 272 ? -18.099 10.528  31.382  1.00 149.58 ?  271  LYS B CA  1 
ATOM   5578 C  C   . LYS B 1 272 ? -18.091 11.120  32.786  1.00 150.23 ?  271  LYS B C   1 
ATOM   5579 O  O   . LYS B 1 272 ? -17.047 11.204  33.431  1.00 155.69 ?  271  LYS B O   1 
ATOM   5580 C  CB  . LYS B 1 272 ? -18.116 8.997   31.434  1.00 159.32 ?  271  LYS B CB  1 
ATOM   5581 C  CG  . LYS B 1 272 ? -18.544 8.340   30.126  1.00 165.86 ?  271  LYS B CG  1 
ATOM   5582 C  CD  . LYS B 1 272 ? -18.285 6.837   30.116  1.00 170.72 ?  271  LYS B CD  1 
ATOM   5583 C  CE  . LYS B 1 272 ? -16.802 6.518   30.012  1.00 173.70 ?  271  LYS B CE  1 
ATOM   5584 N  NZ  . LYS B 1 272 ? -16.562 5.051   29.895  1.00 174.39 ?  271  LYS B NZ  1 
ATOM   5585 N  N   . LYS B 1 273 ? -19.262 11.540  33.250  1.00 144.72 ?  272  LYS B N   1 
ATOM   5586 C  CA  . LYS B 1 273 ? -19.391 12.066  34.601  1.00 136.97 ?  272  LYS B CA  1 
ATOM   5587 C  C   . LYS B 1 273 ? -20.095 11.036  35.480  1.00 133.26 ?  272  LYS B C   1 
ATOM   5588 O  O   . LYS B 1 273 ? -21.284 10.761  35.302  1.00 130.48 ?  272  LYS B O   1 
ATOM   5589 C  CB  . LYS B 1 273 ? -20.166 13.385  34.590  1.00 138.56 ?  272  LYS B CB  1 
ATOM   5590 C  CG  . LYS B 1 273 ? -19.665 14.413  35.586  1.00 135.56 ?  272  LYS B CG  1 
ATOM   5591 C  CD  . LYS B 1 273 ? -20.685 15.519  35.784  1.00 145.42 ?  272  LYS B CD  1 
ATOM   5592 C  CE  . LYS B 1 273 ? -21.985 14.963  36.342  1.00 157.59 ?  272  LYS B CE  1 
ATOM   5593 N  NZ  . LYS B 1 273 ? -22.979 16.035  36.623  1.00 155.18 ?  272  LYS B NZ  1 
ATOM   5594 N  N   . GLY B 1 274 ? -19.354 10.479  36.434  1.00 133.36 ?  273  GLY B N   1 
ATOM   5595 C  CA  . GLY B 1 274 ? -19.840 9.361   37.221  1.00 147.07 ?  273  GLY B CA  1 
ATOM   5596 C  C   . GLY B 1 274 ? -19.314 9.306   38.641  1.00 152.51 ?  273  GLY B C   1 
ATOM   5597 O  O   . GLY B 1 274 ? -18.284 9.895   38.963  1.00 135.40 ?  273  GLY B O   1 
ATOM   5598 N  N   . ASN B 1 275 ? -20.027 8.577   39.492  1.00 167.16 ?  274  ASN B N   1 
ATOM   5599 C  CA  . ASN B 1 275 ? -19.560 8.290   40.839  1.00 178.17 ?  274  ASN B CA  1 
ATOM   5600 C  C   . ASN B 1 275 ? -18.424 7.272   40.838  1.00 171.87 ?  274  ASN B C   1 
ATOM   5601 O  O   . ASN B 1 275 ? -18.038 6.757   39.788  1.00 162.37 ?  274  ASN B O   1 
ATOM   5602 C  CB  . ASN B 1 275 ? -20.713 7.771   41.701  1.00 192.36 ?  274  ASN B CB  1 
ATOM   5603 C  CG  . ASN B 1 275 ? -21.622 8.880   42.194  1.00 195.58 ?  274  ASN B CG  1 
ATOM   5604 O  OD1 . ASN B 1 275 ? -22.764 9.004   41.750  1.00 199.46 ?  274  ASN B OD1 1 
ATOM   5605 N  ND2 . ASN B 1 275 ? -21.118 9.697   43.114  1.00 193.86 ?  274  ASN B ND2 1 
ATOM   5606 N  N   . VAL B 1 276 ? -17.886 6.997   42.021  1.00 169.09 ?  275  VAL B N   1 
ATOM   5607 C  CA  . VAL B 1 276 ? -16.838 5.996   42.177  1.00 162.96 ?  275  VAL B CA  1 
ATOM   5608 C  C   . VAL B 1 276 ? -17.170 5.051   43.328  1.00 174.86 ?  275  VAL B C   1 
ATOM   5609 O  O   . VAL B 1 276 ? -17.934 5.402   44.229  1.00 181.27 ?  275  VAL B O   1 
ATOM   5610 C  CB  . VAL B 1 276 ? -15.465 6.642   42.434  1.00 147.67 ?  275  VAL B CB  1 
ATOM   5611 C  CG1 . VAL B 1 276 ? -14.947 7.322   41.175  1.00 142.43 ?  275  VAL B CG1 1 
ATOM   5612 C  CG2 . VAL B 1 276 ? -15.551 7.625   43.593  1.00 140.73 ?  275  VAL B CG2 1 
ATOM   5613 N  N   . SER B 1 277 ? -16.589 3.856   43.298  1.00 178.78 ?  276  SER B N   1 
ATOM   5614 C  CA  . SER B 1 277 ? -16.860 2.848   44.318  1.00 188.26 ?  276  SER B CA  1 
ATOM   5615 C  C   . SER B 1 277 ? -16.233 3.223   45.653  1.00 192.88 ?  276  SER B C   1 
ATOM   5616 O  O   . SER B 1 277 ? -15.440 4.160   45.736  1.00 188.06 ?  276  SER B O   1 
ATOM   5617 C  CB  . SER B 1 277 ? -16.345 1.481   43.874  1.00 187.24 ?  276  SER B CB  1 
ATOM   5618 O  OG  . SER B 1 277 ? -16.491 0.511   44.897  1.00 192.53 ?  276  SER B OG  1 
ATOM   5619 N  N   . SER B 1 278 ? -16.608 2.496   46.700  1.00 196.20 ?  277  SER B N   1 
ATOM   5620 C  CA  . SER B 1 278 ? -15.948 2.620   47.994  1.00 181.99 ?  277  SER B CA  1 
ATOM   5621 C  C   . SER B 1 278 ? -14.486 2.216   47.868  1.00 160.20 ?  277  SER B C   1 
ATOM   5622 O  O   . SER B 1 278 ? -13.609 2.822   48.482  1.00 149.55 ?  277  SER B O   1 
ATOM   5623 C  CB  . SER B 1 278 ? -16.644 1.760   49.043  1.00 182.82 ?  277  SER B CB  1 
ATOM   5624 O  OG  . SER B 1 278 ? -15.991 1.831   50.296  1.00 190.74 ?  277  SER B OG  1 
ATOM   5625 N  N   . THR B 1 279 ? -14.239 1.174   47.077  1.00 155.86 ?  278  THR B N   1 
ATOM   5626 C  CA  . THR B 1 279 ? -12.883 0.753   46.737  1.00 146.63 ?  278  THR B CA  1 
ATOM   5627 C  C   . THR B 1 279 ? -12.277 1.746   45.745  1.00 146.96 ?  278  THR B C   1 
ATOM   5628 O  O   . THR B 1 279 ? -11.085 1.700   45.444  1.00 147.05 ?  278  THR B O   1 
ATOM   5629 C  CB  . THR B 1 279 ? -12.853 -0.675  46.148  1.00 131.77 ?  278  THR B CB  1 
ATOM   5630 O  OG1 . THR B 1 279 ? -11.506 -1.166  46.135  1.00 120.61 ?  278  THR B OG1 1 
ATOM   5631 C  CG2 . THR B 1 279 ? -13.414 -0.689  44.737  1.00 130.85 ?  278  THR B CG2 1 
ATOM   5632 N  N   . GLY B 1 280 ? -13.119 2.633   45.227  1.00 140.31 ?  279  GLY B N   1 
ATOM   5633 C  CA  . GLY B 1 280 ? -12.670 3.686   44.341  1.00 130.62 ?  279  GLY B CA  1 
ATOM   5634 C  C   . GLY B 1 280 ? -12.559 3.356   42.869  1.00 123.23 ?  279  GLY B C   1 
ATOM   5635 O  O   . GLY B 1 280 ? -11.802 4.009   42.158  1.00 122.59 ?  279  GLY B O   1 
ATOM   5636 N  N   . ARG B 1 281 ? -13.299 2.360   42.393  1.00 144.12 ?  280  ARG B N   1 
ATOM   5637 C  CA  . ARG B 1 281 ? -13.292 2.091   40.961  1.00 147.00 ?  280  ARG B CA  1 
ATOM   5638 C  C   . ARG B 1 281 ? -14.274 3.038   40.279  1.00 141.71 ?  280  ARG B C   1 
ATOM   5639 O  O   . ARG B 1 281 ? -15.431 3.146   40.685  1.00 149.18 ?  280  ARG B O   1 
ATOM   5640 C  CB  . ARG B 1 281 ? -13.613 0.617   40.656  1.00 156.12 ?  280  ARG B CB  1 
ATOM   5641 C  CG  . ARG B 1 281 ? -14.993 0.137   41.065  1.00 167.77 ?  280  ARG B CG  1 
ATOM   5642 C  CD  . ARG B 1 281 ? -15.215 -1.321  40.691  1.00 180.27 ?  280  ARG B CD  1 
ATOM   5643 N  NE  . ARG B 1 281 ? -15.261 -1.513  39.245  1.00 183.31 ?  280  ARG B NE  1 
ATOM   5644 C  CZ  . ARG B 1 281 ? -16.372 -1.438  38.518  1.00 189.62 ?  280  ARG B CZ  1 
ATOM   5645 N  NH1 . ARG B 1 281 ? -17.532 -1.177  39.104  1.00 189.46 ?  280  ARG B NH1 1 
ATOM   5646 N  NH2 . ARG B 1 281 ? -16.323 -1.625  37.207  1.00 193.93 ?  280  ARG B NH2 1 
ATOM   5647 N  N   . CYS B 1 282 ? -13.798 3.763   39.272  1.00 128.15 ?  281  CYS B N   1 
ATOM   5648 C  CA  . CYS B 1 282 ? -14.662 4.692   38.553  1.00 131.25 ?  281  CYS B CA  1 
ATOM   5649 C  C   . CYS B 1 282 ? -15.639 3.927   37.680  1.00 127.89 ?  281  CYS B C   1 
ATOM   5650 O  O   . CYS B 1 282 ? -15.237 3.151   36.812  1.00 120.53 ?  281  CYS B O   1 
ATOM   5651 C  CB  . CYS B 1 282 ? -13.860 5.676   37.700  1.00 140.06 ?  281  CYS B CB  1 
ATOM   5652 S  SG  . CYS B 1 282 ? -14.894 6.837   36.741  1.00 95.97  ?  281  CYS B SG  1 
ATOM   5653 N  N   . LEU B 1 283 ? -16.923 4.165   37.920  1.00 134.95 ?  282  LEU B N   1 
ATOM   5654 C  CA  . LEU B 1 283 ? -18.006 3.451   37.258  1.00 151.42 ?  282  LEU B CA  1 
ATOM   5655 C  C   . LEU B 1 283 ? -17.909 3.576   35.742  1.00 167.83 ?  282  LEU B C   1 
ATOM   5656 O  O   . LEU B 1 283 ? -18.276 2.656   35.004  1.00 186.34 ?  282  LEU B O   1 
ATOM   5657 C  CB  . LEU B 1 283 ? -19.348 3.990   37.739  1.00 142.87 ?  282  LEU B CB  1 
ATOM   5658 C  CG  . LEU B 1 283 ? -19.520 3.959   39.255  1.00 129.66 ?  282  LEU B CG  1 
ATOM   5659 C  CD1 . LEU B 1 283 ? -20.896 4.466   39.640  1.00 127.77 ?  282  LEU B CD1 1 
ATOM   5660 C  CD2 . LEU B 1 283 ? -19.271 2.560   39.802  1.00 133.00 ?  282  LEU B CD2 1 
ATOM   5661 N  N   . SER B 1 284 ? -17.414 4.726   35.295  1.00 152.94 ?  283  SER B N   1 
ATOM   5662 C  CA  . SER B 1 284 ? -17.321 5.033   33.877  1.00 141.41 ?  283  SER B CA  1 
ATOM   5663 C  C   . SER B 1 284 ? -16.320 4.154   33.124  1.00 151.26 ?  283  SER B C   1 
ATOM   5664 O  O   . SER B 1 284 ? -16.654 3.601   32.077  1.00 169.18 ?  283  SER B O   1 
ATOM   5665 C  CB  . SER B 1 284 ? -16.959 6.504   33.702  1.00 130.28 ?  283  SER B CB  1 
ATOM   5666 O  OG  . SER B 1 284 ? -17.849 7.329   34.435  1.00 130.97 ?  283  SER B OG  1 
ATOM   5667 N  N   . CYS B 1 285 ? -15.102 4.020   33.644  1.00 144.37 ?  284  CYS B N   1 
ATOM   5668 C  CA  . CYS B 1 285 ? -14.067 3.278   32.923  1.00 145.38 ?  284  CYS B CA  1 
ATOM   5669 C  C   . CYS B 1 285 ? -13.665 1.998   33.650  1.00 144.04 ?  284  CYS B C   1 
ATOM   5670 O  O   . CYS B 1 285 ? -12.755 1.293   33.209  1.00 132.97 ?  284  CYS B O   1 
ATOM   5671 C  CB  . CYS B 1 285 ? -12.824 4.142   32.682  1.00 154.40 ?  284  CYS B CB  1 
ATOM   5672 S  SG  . CYS B 1 285 ? -11.872 4.601   34.155  1.00 127.69 ?  284  CYS B SG  1 
ATOM   5673 N  N   . SER B 1 286 ? -14.315 1.729   34.781  1.00 164.66 ?  285  SER B N   1 
ATOM   5674 C  CA  . SER B 1 286 ? -14.111 0.493   35.540  1.00 179.14 ?  285  SER B CA  1 
ATOM   5675 C  C   . SER B 1 286 ? -12.681 0.370   36.056  1.00 179.53 ?  285  SER B C   1 
ATOM   5676 O  O   . SER B 1 286 ? -12.190 -0.734  36.298  1.00 191.80 ?  285  SER B O   1 
ATOM   5677 C  CB  . SER B 1 286 ? -14.468 -0.730  34.694  1.00 184.09 ?  285  SER B CB  1 
ATOM   5678 O  OG  . SER B 1 286 ? -14.333 -1.920  35.450  1.00 188.22 ?  285  SER B OG  1 
ATOM   5679 N  N   . GLU B 1 287 ? -12.021 1.509   36.224  1.00 152.46 ?  286  GLU B N   1 
ATOM   5680 C  CA  . GLU B 1 287 ? -10.668 1.541   36.756  1.00 135.13 ?  286  GLU B CA  1 
ATOM   5681 C  C   . GLU B 1 287 ? -10.677 2.199   38.122  1.00 138.31 ?  286  GLU B C   1 
ATOM   5682 O  O   . GLU B 1 287 ? -11.382 3.187   38.330  1.00 141.88 ?  286  GLU B O   1 
ATOM   5683 C  CB  . GLU B 1 287 ? -9.731  2.295   35.812  1.00 130.96 ?  286  GLU B CB  1 
ATOM   5684 C  CG  . GLU B 1 287 ? -8.325  1.725   35.729  1.00 130.54 ?  286  GLU B CG  1 
ATOM   5685 C  CD  . GLU B 1 287 ? -8.213  0.612   34.706  1.00 146.00 ?  286  GLU B CD  1 
ATOM   5686 O  OE1 . GLU B 1 287 ? -9.255  0.207   34.149  1.00 154.82 ?  286  GLU B OE1 1 
ATOM   5687 O  OE2 . GLU B 1 287 ? -7.081  0.147   34.453  1.00 147.94 ?  286  GLU B OE2 1 
ATOM   5688 N  N   . GLN B 1 288 ? -9.934  1.634   39.069  1.00 144.07 ?  287  GLN B N   1 
ATOM   5689 C  CA  . GLN B 1 288 ? -9.879  2.225   40.400  1.00 134.16 ?  287  GLN B CA  1 
ATOM   5690 C  C   . GLN B 1 288 ? -8.705  3.179   40.560  1.00 118.21 ?  287  GLN B C   1 
ATOM   5691 O  O   . GLN B 1 288 ? -7.610  2.950   40.044  1.00 98.30  ?  287  GLN B O   1 
ATOM   5692 C  CB  . GLN B 1 288 ? -9.845  1.155   41.488  1.00 136.58 ?  287  GLN B CB  1 
ATOM   5693 C  CG  . GLN B 1 288 ? -8.622  0.289   41.523  1.00 151.72 ?  287  GLN B CG  1 
ATOM   5694 C  CD  . GLN B 1 288 ? -8.625  -0.599  42.744  1.00 177.03 ?  287  GLN B CD  1 
ATOM   5695 O  OE1 . GLN B 1 288 ? -9.684  -0.912  43.292  1.00 184.61 ?  287  GLN B OE1 1 
ATOM   5696 N  NE2 . GLN B 1 288 ? -7.443  -1.007  43.183  1.00 189.26 ?  287  GLN B NE2 1 
ATOM   5697 N  N   . LEU B 1 289 ? -8.971  4.261   41.281  1.00 120.51 ?  288  LEU B N   1 
ATOM   5698 C  CA  . LEU B 1 289 ? -8.029  5.353   41.470  1.00 126.09 ?  288  LEU B CA  1 
ATOM   5699 C  C   . LEU B 1 289 ? -6.845  4.952   42.352  1.00 141.47 ?  288  LEU B C   1 
ATOM   5700 O  O   . LEU B 1 289 ? -6.981  4.124   43.254  1.00 164.71 ?  288  LEU B O   1 
ATOM   5701 C  CB  . LEU B 1 289 ? -8.760  6.553   42.076  1.00 127.49 ?  288  LEU B CB  1 
ATOM   5702 C  CG  . LEU B 1 289 ? -10.114 6.868   41.432  1.00 129.93 ?  288  LEU B CG  1 
ATOM   5703 C  CD1 . LEU B 1 289 ? -10.794 8.040   42.116  1.00 137.09 ?  288  LEU B CD1 1 
ATOM   5704 C  CD2 . LEU B 1 289 ? -9.956  7.135   39.943  1.00 121.88 ?  288  LEU B CD2 1 
ATOM   5705 N  N   . ALA B 1 290 ? -5.683  5.533   42.070  1.00 124.53 ?  289  ALA B N   1 
ATOM   5706 C  CA  . ALA B 1 290 ? -4.452  5.229   42.799  1.00 115.05 ?  289  ALA B CA  1 
ATOM   5707 C  C   . ALA B 1 290 ? -4.453  5.798   44.225  1.00 115.77 ?  289  ALA B C   1 
ATOM   5708 O  O   . ALA B 1 290 ? -5.250  6.676   44.558  1.00 107.58 ?  289  ALA B O   1 
ATOM   5709 C  CB  . ALA B 1 290 ? -3.253  5.744   42.029  1.00 111.96 ?  289  ALA B CB  1 
ATOM   5710 N  N   . CYS B 1 291 ? -3.566  5.273   45.068  1.00 180.32 ?  290  CYS B N   1 
ATOM   5711 C  CA  . CYS B 1 291 ? -3.432  5.732   46.451  1.00 175.70 ?  290  CYS B CA  1 
ATOM   5712 C  C   . CYS B 1 291 ? -2.781  7.109   46.589  1.00 164.30 ?  290  CYS B C   1 
ATOM   5713 O  O   . CYS B 1 291 ? -1.802  7.422   45.909  1.00 149.23 ?  290  CYS B O   1 
ATOM   5714 C  CB  . CYS B 1 291 ? -2.622  4.714   47.263  1.00 176.66 ?  290  CYS B CB  1 
ATOM   5715 S  SG  . CYS B 1 291 ? -0.914  4.488   46.697  1.00 247.31 ?  290  CYS B SG  1 
ATOM   5716 N  N   . VAL B 1 292 ? -3.340  7.926   47.477  1.00 172.18 ?  291  VAL B N   1 
ATOM   5717 C  CA  . VAL B 1 292 ? -2.752  9.213   47.837  1.00 183.60 ?  291  VAL B CA  1 
ATOM   5718 C  C   . VAL B 1 292 ? -1.401  9.058   48.537  1.00 195.50 ?  291  VAL B C   1 
ATOM   5719 O  O   . VAL B 1 292 ? -1.261  8.257   49.460  1.00 221.28 ?  291  VAL B O   1 
ATOM   5720 C  CB  . VAL B 1 292 ? -3.714  10.024  48.749  1.00 194.69 ?  291  VAL B CB  1 
ATOM   5721 C  CG1 . VAL B 1 292 ? -4.268  9.155   49.879  1.00 189.61 ?  291  VAL B CG1 1 
ATOM   5722 C  CG2 . VAL B 1 292 ? -3.044  11.288  49.279  1.00 192.13 ?  291  VAL B CG2 1 
ATOM   5723 N  N   . ASP B 1 293 ? -0.401  9.804   48.077  1.00 182.35 ?  292  ASP B N   1 
ATOM   5724 C  CA  . ASP B 1 293 ? 0.875   9.895   48.783  1.00 170.93 ?  292  ASP B CA  1 
ATOM   5725 C  C   . ASP B 1 293 ? 1.199   11.352  49.103  1.00 173.58 ?  292  ASP B C   1 
ATOM   5726 O  O   . ASP B 1 293 ? 1.328   12.181  48.202  1.00 185.00 ?  292  ASP B O   1 
ATOM   5727 C  CB  . ASP B 1 293 ? 2.009   9.260   47.975  1.00 166.70 ?  292  ASP B CB  1 
ATOM   5728 C  CG  . ASP B 1 293 ? 1.962   7.740   47.988  1.00 163.05 ?  292  ASP B CG  1 
ATOM   5729 O  OD1 . ASP B 1 293 ? 1.298   7.168   48.875  1.00 141.84 ?  292  ASP B OD1 1 
ATOM   5730 O  OD2 . ASP B 1 293 ? 2.603   7.113   47.119  1.00 173.47 ?  292  ASP B OD2 1 
ATOM   5731 N  N   . THR B 1 294 ? 1.325   11.659  50.389  1.00 165.94 ?  293  THR B N   1 
ATOM   5732 C  CA  . THR B 1 294 ? 1.521   13.034  50.841  1.00 164.72 ?  293  THR B CA  1 
ATOM   5733 C  C   . THR B 1 294 ? 2.910   13.547  50.465  1.00 168.81 ?  293  THR B C   1 
ATOM   5734 O  O   . THR B 1 294 ? 3.862   12.770  50.379  1.00 165.91 ?  293  THR B O   1 
ATOM   5735 C  CB  . THR B 1 294 ? 1.317   13.158  52.364  1.00 161.22 ?  293  THR B CB  1 
ATOM   5736 O  OG1 . THR B 1 294 ? 2.165   12.224  53.043  1.00 174.62 ?  293  THR B OG1 1 
ATOM   5737 C  CG2 . THR B 1 294 ? -0.135  12.873  52.732  1.00 151.07 ?  293  THR B CG2 1 
ATOM   5738 N  N   . ASN B 1 295 ? 3.019   14.854  50.235  1.00 178.67 ?  294  ASN B N   1 
ATOM   5739 C  CA  . ASN B 1 295 ? 4.258   15.452  49.738  1.00 181.60 ?  294  ASN B CA  1 
ATOM   5740 C  C   . ASN B 1 295 ? 5.394   15.363  50.748  1.00 188.78 ?  294  ASN B C   1 
ATOM   5741 O  O   . ASN B 1 295 ? 5.237   15.744  51.907  1.00 197.71 ?  294  ASN B O   1 
ATOM   5742 C  CB  . ASN B 1 295 ? 4.034   16.919  49.364  1.00 176.12 ?  294  ASN B CB  1 
ATOM   5743 C  CG  . ASN B 1 295 ? 2.856   17.114  48.438  1.00 169.11 ?  294  ASN B CG  1 
ATOM   5744 O  OD1 . ASN B 1 295 ? 1.863   17.742  48.805  1.00 156.64 ?  294  ASN B OD1 1 
ATOM   5745 N  ND2 . ASN B 1 295 ? 2.958   16.579  47.227  1.00 179.05 ?  294  ASN B ND2 1 
ATOM   5746 N  N   . GLU B 1 296 ? 6.538   14.864  50.295  1.00 187.35 ?  295  GLU B N   1 
ATOM   5747 C  CA  . GLU B 1 296 ? 7.692   14.652  51.162  1.00 187.77 ?  295  GLU B CA  1 
ATOM   5748 C  C   . GLU B 1 296 ? 8.162   15.922  51.878  1.00 192.95 ?  295  GLU B C   1 
ATOM   5749 O  O   . GLU B 1 296 ? 8.317   15.923  53.097  1.00 185.79 ?  295  GLU B O   1 
ATOM   5750 C  CB  . GLU B 1 296 ? 8.846   14.051  50.357  1.00 182.70 ?  295  GLU B CB  1 
ATOM   5751 C  CG  . GLU B 1 296 ? 10.079  13.715  51.182  1.00 189.40 ?  295  GLU B CG  1 
ATOM   5752 C  CD  . GLU B 1 296 ? 11.061  14.866  51.258  1.00 203.00 ?  295  GLU B CD  1 
ATOM   5753 O  OE1 . GLU B 1 296 ? 10.909  15.827  50.476  1.00 210.94 ?  295  GLU B OE1 1 
ATOM   5754 O  OE2 . GLU B 1 296 ? 11.980  14.815  52.101  1.00 206.38 ?  295  GLU B OE2 1 
ATOM   5755 N  N   . VAL B 1 297 ? 8.403   16.990  51.122  1.00 203.14 ?  296  VAL B N   1 
ATOM   5756 C  CA  . VAL B 1 297 ? 8.898   18.242  51.700  1.00 217.63 ?  296  VAL B CA  1 
ATOM   5757 C  C   . VAL B 1 297 ? 7.928   18.855  52.713  1.00 217.06 ?  296  VAL B C   1 
ATOM   5758 O  O   . VAL B 1 297 ? 8.353   19.449  53.705  1.00 226.68 ?  296  VAL B O   1 
ATOM   5759 C  CB  . VAL B 1 297 ? 9.221   19.288  50.596  1.00 186.27 ?  296  VAL B CB  1 
ATOM   5760 C  CG1 . VAL B 1 297 ? 7.975   19.655  49.799  1.00 189.40 ?  296  VAL B CG1 1 
ATOM   5761 C  CG2 . VAL B 1 297 ? 9.867   20.533  51.197  1.00 186.74 ?  296  VAL B CG2 1 
ATOM   5762 N  N   . GLU B 1 298 ? 6.629   18.697  52.476  1.00 212.19 ?  297  GLU B N   1 
ATOM   5763 C  CA  . GLU B 1 298 ? 5.632   19.203  53.412  1.00 188.87 ?  297  GLU B CA  1 
ATOM   5764 C  C   . GLU B 1 298 ? 5.609   18.393  54.706  1.00 178.74 ?  297  GLU B C   1 
ATOM   5765 O  O   . GLU B 1 298 ? 5.467   18.959  55.790  1.00 169.55 ?  297  GLU B O   1 
ATOM   5766 C  CB  . GLU B 1 298 ? 4.249   19.219  52.761  1.00 170.84 ?  297  GLU B CB  1 
ATOM   5767 C  CG  . GLU B 1 298 ? 4.136   20.222  51.625  1.00 165.58 ?  297  GLU B CG  1 
ATOM   5768 C  CD  . GLU B 1 298 ? 4.495   21.630  52.068  1.00 159.03 ?  297  GLU B CD  1 
ATOM   5769 O  OE1 . GLU B 1 298 ? 4.028   22.051  53.147  1.00 158.43 ?  297  GLU B OE1 1 
ATOM   5770 O  OE2 . GLU B 1 298 ? 5.255   22.311  51.347  1.00 171.16 ?  297  GLU B OE2 1 
ATOM   5771 N  N   . THR B 1 299 ? 5.744   17.074  54.587  1.00 180.49 ?  298  THR B N   1 
ATOM   5772 C  CA  . THR B 1 299 ? 5.824   16.197  55.754  1.00 173.90 ?  298  THR B CA  1 
ATOM   5773 C  C   . THR B 1 299 ? 7.031   16.577  56.614  1.00 181.68 ?  298  THR B C   1 
ATOM   5774 O  O   . THR B 1 299 ? 6.925   16.652  57.838  1.00 193.00 ?  298  THR B O   1 
ATOM   5775 C  CB  . THR B 1 299 ? 5.898   14.698  55.368  1.00 156.13 ?  298  THR B CB  1 
ATOM   5776 O  OG1 . THR B 1 299 ? 7.026   14.463  54.517  1.00 160.95 ?  298  THR B OG1 1 
ATOM   5777 C  CG2 . THR B 1 299 ? 4.628   14.266  54.656  1.00 136.14 ?  298  THR B CG2 1 
ATOM   5778 N  N   . GLN B 1 300 ? 8.178   16.791  55.972  1.00 177.41 ?  299  GLN B N   1 
ATOM   5779 C  CA  . GLN B 1 300 ? 9.401   17.150  56.687  1.00 172.85 ?  299  GLN B CA  1 
ATOM   5780 C  C   . GLN B 1 300 ? 9.229   18.454  57.459  1.00 182.26 ?  299  GLN B C   1 
ATOM   5781 O  O   . GLN B 1 300 ? 9.698   18.576  58.591  1.00 185.42 ?  299  GLN B O   1 
ATOM   5782 C  CB  . GLN B 1 300 ? 10.578  17.268  55.718  1.00 174.61 ?  299  GLN B CB  1 
ATOM   5783 C  CG  . GLN B 1 300 ? 10.965  15.961  55.050  1.00 181.73 ?  299  GLN B CG  1 
ATOM   5784 C  CD  . GLN B 1 300 ? 11.417  14.906  56.044  1.00 185.46 ?  299  GLN B CD  1 
ATOM   5785 O  OE1 . GLN B 1 300 ? 11.937  15.220  57.116  1.00 183.32 ?  299  GLN B OE1 1 
ATOM   5786 N  NE2 . GLN B 1 300 ? 11.220  13.642  55.688  1.00 187.11 ?  299  GLN B NE2 1 
ATOM   5787 N  N   . LYS B 1 301 ? 8.565   19.428  56.843  1.00 191.47 ?  300  LYS B N   1 
ATOM   5788 C  CA  . LYS B 1 301 ? 8.303   20.702  57.504  1.00 207.83 ?  300  LYS B CA  1 
ATOM   5789 C  C   . LYS B 1 301 ? 7.297   20.488  58.624  1.00 222.58 ?  300  LYS B C   1 
ATOM   5790 O  O   . LYS B 1 301 ? 7.321   21.188  59.634  1.00 225.11 ?  300  LYS B O   1 
ATOM   5791 C  CB  . LYS B 1 301 ? 7.796   21.751  56.514  1.00 211.00 ?  300  LYS B CB  1 
ATOM   5792 C  CG  . LYS B 1 301 ? 8.829   22.169  55.479  1.00 215.00 ?  300  LYS B CG  1 
ATOM   5793 C  CD  . LYS B 1 301 ? 10.158  22.539  56.129  1.00 212.00 ?  300  LYS B CD  1 
ATOM   5794 C  CE  . LYS B 1 301 ? 10.062  23.823  56.940  1.00 210.37 ?  300  LYS B CE  1 
ATOM   5795 N  NZ  . LYS B 1 301 ? 11.371  24.181  57.555  1.00 211.63 ?  300  LYS B NZ  1 
ATOM   5796 N  N   . PHE B 1 302 ? 6.412   19.514  58.432  1.00 229.05 ?  301  PHE B N   1 
ATOM   5797 C  CA  . PHE B 1 302 ? 5.470   19.121  59.473  1.00 219.33 ?  301  PHE B CA  1 
ATOM   5798 C  C   . PHE B 1 302 ? 6.170   18.454  60.648  1.00 200.16 ?  301  PHE B C   1 
ATOM   5799 O  O   . PHE B 1 302 ? 5.850   18.730  61.803  1.00 199.04 ?  301  PHE B O   1 
ATOM   5800 C  CB  . PHE B 1 302 ? 4.402   18.183  58.918  1.00 219.77 ?  301  PHE B CB  1 
ATOM   5801 C  CG  . PHE B 1 302 ? 3.318   17.867  59.900  1.00 220.60 ?  301  PHE B CG  1 
ATOM   5802 C  CD1 . PHE B 1 302 ? 2.346   18.802  60.206  1.00 222.45 ?  301  PHE B CD1 1 
ATOM   5803 C  CD2 . PHE B 1 302 ? 3.282   16.635  60.531  1.00 222.96 ?  301  PHE B CD2 1 
ATOM   5804 C  CE1 . PHE B 1 302 ? 1.351   18.509  61.118  1.00 223.58 ?  301  PHE B CE1 1 
ATOM   5805 C  CE2 . PHE B 1 302 ? 2.293   16.336  61.443  1.00 221.29 ?  301  PHE B CE2 1 
ATOM   5806 C  CZ  . PHE B 1 302 ? 1.325   17.274  61.736  1.00 221.36 ?  301  PHE B CZ  1 
ATOM   5807 N  N   . VAL B 1 303 ? 7.108   17.563  60.344  1.00 176.64 ?  302  VAL B N   1 
ATOM   5808 C  CA  . VAL B 1 303 ? 7.924   16.928  61.369  1.00 158.57 ?  302  VAL B CA  1 
ATOM   5809 C  C   . VAL B 1 303 ? 8.695   17.978  62.159  1.00 158.73 ?  302  VAL B C   1 
ATOM   5810 O  O   . VAL B 1 303 ? 8.676   17.984  63.388  1.00 154.36 ?  302  VAL B O   1 
ATOM   5811 C  CB  . VAL B 1 303 ? 8.915   15.916  60.755  1.00 147.12 ?  302  VAL B CB  1 
ATOM   5812 C  CG1 . VAL B 1 303 ? 9.884   15.406  61.813  1.00 130.18 ?  302  VAL B CG1 1 
ATOM   5813 C  CG2 . VAL B 1 303 ? 8.166   14.765  60.097  1.00 133.45 ?  302  VAL B CG2 1 
ATOM   5814 N  N   . ASP B 1 304 ? 9.368   18.866  61.433  1.00 159.84 ?  303  ASP B N   1 
ATOM   5815 C  CA  . ASP B 1 304 ? 10.152  19.942  62.031  1.00 166.48 ?  303  ASP B CA  1 
ATOM   5816 C  C   . ASP B 1 304 ? 9.303   20.905  62.860  1.00 177.13 ?  303  ASP B C   1 
ATOM   5817 O  O   . ASP B 1 304 ? 9.734   21.370  63.914  1.00 173.87 ?  303  ASP B O   1 
ATOM   5818 C  CB  . ASP B 1 304 ? 10.891  20.717  60.940  1.00 174.94 ?  303  ASP B CB  1 
ATOM   5819 C  CG  . ASP B 1 304 ? 11.972  19.891  60.270  1.00 172.25 ?  303  ASP B CG  1 
ATOM   5820 O  OD1 . ASP B 1 304 ? 11.918  18.646  60.364  1.00 153.69 ?  303  ASP B OD1 1 
ATOM   5821 O  OD2 . ASP B 1 304 ? 12.875  20.487  59.646  1.00 176.86 ?  303  ASP B OD2 1 
ATOM   5822 N  N   . SER B 1 305 ? 8.109   21.218  62.364  1.00 193.23 ?  304  SER B N   1 
ATOM   5823 C  CA  . SER B 1 305 ? 7.199   22.141  63.041  1.00 202.14 ?  304  SER B CA  1 
ATOM   5824 C  C   . SER B 1 305 ? 6.700   21.616  64.388  1.00 200.29 ?  304  SER B C   1 
ATOM   5825 O  O   . SER B 1 305 ? 6.700   22.344  65.379  1.00 213.01 ?  304  SER B O   1 
ATOM   5826 C  CB  . SER B 1 305 ? 6.005   22.462  62.146  1.00 209.66 ?  304  SER B CB  1 
ATOM   5827 O  OG  . SER B 1 305 ? 5.332   21.276  61.775  1.00 213.80 ?  304  SER B OG  1 
ATOM   5828 N  N   . LEU B 1 306 ? 6.253   20.362  64.419  1.00 181.84 ?  305  LEU B N   1 
ATOM   5829 C  CA  . LEU B 1 306 ? 5.745   19.777  65.658  1.00 163.17 ?  305  LEU B CA  1 
ATOM   5830 C  C   . LEU B 1 306 ? 6.861   19.637  66.686  1.00 149.08 ?  305  LEU B C   1 
ATOM   5831 O  O   . LEU B 1 306 ? 6.638   19.836  67.880  1.00 145.59 ?  305  LEU B O   1 
ATOM   5832 C  CB  . LEU B 1 306 ? 5.068   18.425  65.393  1.00 169.80 ?  305  LEU B CB  1 
ATOM   5833 C  CG  . LEU B 1 306 ? 5.812   17.237  64.771  1.00 181.02 ?  305  LEU B CG  1 
ATOM   5834 C  CD1 . LEU B 1 306 ? 6.636   16.456  65.788  1.00 182.81 ?  305  LEU B CD1 1 
ATOM   5835 C  CD2 . LEU B 1 306 ? 4.817   16.309  64.088  1.00 185.67 ?  305  LEU B CD2 1 
ATOM   5836 N  N   . VAL B 1 307 ? 8.057   19.292  66.218  1.00 141.41 ?  306  VAL B N   1 
ATOM   5837 C  CA  . VAL B 1 307 ? 9.220   19.194  67.088  1.00 127.63 ?  306  VAL B CA  1 
ATOM   5838 C  C   . VAL B 1 307 ? 9.457   20.558  67.726  1.00 173.05 ?  306  VAL B C   1 
ATOM   5839 O  O   . VAL B 1 307 ? 9.770   20.662  68.912  1.00 171.88 ?  306  VAL B O   1 
ATOM   5840 C  CB  . VAL B 1 307 ? 10.475  18.733  66.317  1.00 130.08 ?  306  VAL B CB  1 
ATOM   5841 C  CG1 . VAL B 1 307 ? 11.733  18.953  67.143  1.00 155.62 ?  306  VAL B CG1 1 
ATOM   5842 C  CG2 . VAL B 1 307 ? 10.346  17.273  65.916  1.00 127.38 ?  306  VAL B CG2 1 
ATOM   5843 N  N   . ALA B 1 308 ? 9.282   21.603  66.922  1.00 176.98 ?  307  ALA B N   1 
ATOM   5844 C  CA  . ALA B 1 308 ? 9.440   22.981  67.375  1.00 187.03 ?  307  ALA B CA  1 
ATOM   5845 C  C   . ALA B 1 308 ? 8.428   23.316  68.469  1.00 195.40 ?  307  ALA B C   1 
ATOM   5846 O  O   . ALA B 1 308 ? 8.745   24.043  69.412  1.00 201.43 ?  307  ALA B O   1 
ATOM   5847 C  CB  . ALA B 1 308 ? 9.303   23.946  66.207  1.00 187.06 ?  307  ALA B CB  1 
ATOM   5848 N  N   . LEU B 1 309 ? 7.209   22.799  68.332  1.00 194.94 ?  308  LEU B N   1 
ATOM   5849 C  CA  . LEU B 1 309 ? 6.157   23.046  69.318  1.00 203.72 ?  308  LEU B CA  1 
ATOM   5850 C  C   . LEU B 1 309 ? 6.462   22.347  70.639  1.00 210.27 ?  308  LEU B C   1 
ATOM   5851 O  O   . LEU B 1 309 ? 5.938   22.721  71.687  1.00 221.63 ?  308  LEU B O   1 
ATOM   5852 C  CB  . LEU B 1 309 ? 4.797   22.579  68.796  1.00 201.71 ?  308  LEU B CB  1 
ATOM   5853 C  CG  . LEU B 1 309 ? 4.325   23.068  67.426  1.00 203.95 ?  308  LEU B CG  1 
ATOM   5854 C  CD1 . LEU B 1 309 ? 2.917   22.564  67.143  1.00 194.70 ?  308  LEU B CD1 1 
ATOM   5855 C  CD2 . LEU B 1 309 ? 4.391   24.586  67.327  1.00 212.23 ?  308  LEU B CD2 1 
ATOM   5856 N  N   . ALA B 1 310 ? 7.294   21.313  70.575  1.00 200.87 ?  309  ALA B N   1 
ATOM   5857 C  CA  . ALA B 1 310 ? 7.681   20.565  71.764  1.00 178.06 ?  309  ALA B CA  1 
ATOM   5858 C  C   . ALA B 1 310 ? 8.747   21.332  72.541  1.00 179.77 ?  309  ALA B C   1 
ATOM   5859 O  O   . ALA B 1 310 ? 8.677   21.456  73.762  1.00 174.69 ?  309  ALA B O   1 
ATOM   5860 C  CB  . ALA B 1 310 ? 8.181   19.184  71.387  1.00 158.49 ?  309  ALA B CB  1 
ATOM   5861 N  N   . MET B 1 311 ? 9.742   21.833  71.816  1.00 188.63 ?  310  MET B N   1 
ATOM   5862 C  CA  . MET B 1 311 ? 10.813  22.638  72.396  1.00 210.54 ?  310  MET B CA  1 
ATOM   5863 C  C   . MET B 1 311 ? 10.292  23.924  73.047  1.00 218.52 ?  310  MET B C   1 
ATOM   5864 O  O   . MET B 1 311 ? 10.952  24.509  73.908  1.00 227.30 ?  310  MET B O   1 
ATOM   5865 C  CB  . MET B 1 311 ? 11.847  22.981  71.321  1.00 223.75 ?  310  MET B CB  1 
ATOM   5866 C  CG  . MET B 1 311 ? 12.519  21.761  70.718  1.00 226.79 ?  310  MET B CG  1 
ATOM   5867 S  SD  . MET B 1 311 ? 13.397  20.759  71.932  1.00 264.23 ?  310  MET B SD  1 
ATOM   5868 C  CE  . MET B 1 311 ? 14.058  19.469  70.881  1.00 203.46 ?  310  MET B CE  1 
ATOM   5869 N  N   . ASP B 1 312 ? 9.102   24.350  72.635  1.00 193.66 ?  311  ASP B N   1 
ATOM   5870 C  CA  . ASP B 1 312 ? 8.473   25.551  73.172  1.00 168.77 ?  311  ASP B CA  1 
ATOM   5871 C  C   . ASP B 1 312 ? 7.453   25.205  74.251  1.00 150.68 ?  311  ASP B C   1 
ATOM   5872 O  O   . ASP B 1 312 ? 6.259   25.447  74.088  1.00 136.49 ?  311  ASP B O   1 
ATOM   5873 C  CB  . ASP B 1 312 ? 7.794   26.338  72.047  1.00 161.55 ?  311  ASP B CB  1 
ATOM   5874 C  CG  . ASP B 1 312 ? 7.830   27.837  72.272  1.00 159.55 ?  311  ASP B CG  1 
ATOM   5875 O  OD1 . ASP B 1 312 ? 8.878   28.349  72.718  1.00 164.69 ?  311  ASP B OD1 1 
ATOM   5876 O  OD2 . ASP B 1 312 ? 6.805   28.500  72.007  1.00 152.26 ?  311  ASP B OD2 1 
ATOM   5877 N  N   . ASN B 1 323 ? 13.471  20.442  74.621  1.00 228.46 ?  322  ASN B N   1 
ATOM   5878 C  CA  . ASN B 1 323 ? 12.914  19.195  75.131  1.00 226.07 ?  322  ASN B CA  1 
ATOM   5879 C  C   . ASN B 1 323 ? 13.943  18.070  75.079  1.00 233.53 ?  322  ASN B C   1 
ATOM   5880 O  O   . ASN B 1 323 ? 14.011  17.322  74.102  1.00 233.75 ?  322  ASN B O   1 
ATOM   5881 C  CB  . ASN B 1 323 ? 11.661  18.810  74.338  1.00 209.52 ?  322  ASN B CB  1 
ATOM   5882 C  CG  . ASN B 1 323 ? 10.779  17.820  75.078  1.00 194.97 ?  322  ASN B CG  1 
ATOM   5883 O  OD1 . ASN B 1 323 ? 11.267  16.941  75.787  1.00 194.81 ?  322  ASN B OD1 1 
ATOM   5884 N  ND2 . ASN B 1 323 ? 9.468   17.958  74.911  1.00 186.75 ?  322  ASN B ND2 1 
ATOM   5885 N  N   . VAL B 1 324 ? 14.745  17.963  76.135  1.00 234.22 ?  323  VAL B N   1 
ATOM   5886 C  CA  . VAL B 1 324 ? 15.755  16.914  76.240  1.00 233.53 ?  323  VAL B CA  1 
ATOM   5887 C  C   . VAL B 1 324 ? 15.117  15.533  76.328  1.00 224.62 ?  323  VAL B C   1 
ATOM   5888 O  O   . VAL B 1 324 ? 15.718  14.532  75.938  1.00 220.82 ?  323  VAL B O   1 
ATOM   5889 C  CB  . VAL B 1 324 ? 16.666  17.130  77.466  1.00 234.79 ?  323  VAL B CB  1 
ATOM   5890 C  CG1 . VAL B 1 324 ? 17.497  18.392  77.294  1.00 239.68 ?  323  VAL B CG1 1 
ATOM   5891 C  CG2 . VAL B 1 324 ? 15.839  17.201  78.745  1.00 227.86 ?  323  VAL B CG2 1 
ATOM   5892 N  N   . VAL B 1 325 ? 13.899  15.487  76.853  1.00 220.14 ?  324  VAL B N   1 
ATOM   5893 C  CA  . VAL B 1 325 ? 13.134  14.253  76.924  1.00 220.98 ?  324  VAL B CA  1 
ATOM   5894 C  C   . VAL B 1 325 ? 12.721  13.761  75.535  1.00 228.15 ?  324  VAL B C   1 
ATOM   5895 O  O   . VAL B 1 325 ? 12.709  12.559  75.263  1.00 232.75 ?  324  VAL B O   1 
ATOM   5896 C  CB  . VAL B 1 325 ? 11.887  14.434  77.796  1.00 210.42 ?  324  VAL B CB  1 
ATOM   5897 C  CG1 . VAL B 1 325 ? 11.068  13.177  77.784  1.00 207.08 ?  324  VAL B CG1 1 
ATOM   5898 C  CG2 . VAL B 1 325 ? 12.287  14.796  79.218  1.00 209.02 ?  324  VAL B CG2 1 
ATOM   5899 N  N   . PHE B 1 326 ? 12.395  14.701  74.656  1.00 222.03 ?  325  PHE B N   1 
ATOM   5900 C  CA  . PHE B 1 326 ? 12.002  14.369  73.293  1.00 206.96 ?  325  PHE B CA  1 
ATOM   5901 C  C   . PHE B 1 326 ? 13.200  13.919  72.463  1.00 197.88 ?  325  PHE B C   1 
ATOM   5902 O  O   . PHE B 1 326 ? 13.069  13.069  71.585  1.00 209.26 ?  325  PHE B O   1 
ATOM   5903 C  CB  . PHE B 1 326 ? 11.324  15.564  72.627  1.00 204.44 ?  325  PHE B CB  1 
ATOM   5904 C  CG  . PHE B 1 326 ? 10.948  15.326  71.195  1.00 197.09 ?  325  PHE B CG  1 
ATOM   5905 C  CD1 . PHE B 1 326 ? 9.904   14.476  70.870  1.00 180.91 ?  325  PHE B CD1 1 
ATOM   5906 C  CD2 . PHE B 1 326 ? 11.646  15.947  70.172  1.00 199.96 ?  325  PHE B CD2 1 
ATOM   5907 C  CE1 . PHE B 1 326 ? 9.559   14.256  69.556  1.00 178.82 ?  325  PHE B CE1 1 
ATOM   5908 C  CE2 . PHE B 1 326 ? 11.305  15.728  68.859  1.00 198.92 ?  325  PHE B CE2 1 
ATOM   5909 C  CZ  . PHE B 1 326 ? 10.263  14.881  68.549  1.00 193.14 ?  325  PHE B CZ  1 
ATOM   5910 N  N   . SER B 1 327 ? 14.364  14.495  72.744  1.00 183.68 ?  326  SER B N   1 
ATOM   5911 C  CA  . SER B 1 327 ? 15.605  14.068  72.107  1.00 173.24 ?  326  SER B CA  1 
ATOM   5912 C  C   . SER B 1 327 ? 15.864  12.587  72.386  1.00 176.89 ?  326  SER B C   1 
ATOM   5913 O  O   . SER B 1 327 ? 16.379  11.867  71.531  1.00 165.10 ?  326  SER B O   1 
ATOM   5914 C  CB  . SER B 1 327 ? 16.780  14.923  72.591  1.00 172.54 ?  326  SER B CB  1 
ATOM   5915 O  OG  . SER B 1 327 ? 18.024  14.356  72.217  1.00 169.01 ?  326  SER B OG  1 
ATOM   5916 N  N   . GLU B 1 328 ? 15.498  12.145  73.587  1.00 211.45 ?  327  GLU B N   1 
ATOM   5917 C  CA  . GLU B 1 328 ? 15.575  10.733  73.962  1.00 230.34 ?  327  GLU B CA  1 
ATOM   5918 C  C   . GLU B 1 328 ? 14.662  9.889   73.080  1.00 219.59 ?  327  GLU B C   1 
ATOM   5919 O  O   . GLU B 1 328 ? 15.030  8.798   72.643  1.00 219.55 ?  327  GLU B O   1 
ATOM   5920 C  CB  . GLU B 1 328 ? 15.193  10.544  75.434  1.00 237.06 ?  327  GLU B CB  1 
ATOM   5921 C  CG  . GLU B 1 328 ? 16.236  11.026  76.429  1.00 234.16 ?  327  GLU B CG  1 
ATOM   5922 C  CD  . GLU B 1 328 ? 17.300  9.986   76.715  1.00 231.45 ?  327  GLU B CD  1 
ATOM   5923 O  OE1 . GLU B 1 328 ? 17.046  9.092   77.549  1.00 226.86 ?  327  GLU B OE1 1 
ATOM   5924 O  OE2 . GLU B 1 328 ? 18.390  10.066  76.111  1.00 233.61 ?  327  GLU B OE2 1 
ATOM   5925 N  N   . PHE B 1 329 ? 13.462  10.404  72.834  1.00 196.92 ?  328  PHE B N   1 
ATOM   5926 C  CA  . PHE B 1 329 ? 12.473  9.714   72.017  1.00 167.04 ?  328  PHE B CA  1 
ATOM   5927 C  C   . PHE B 1 329 ? 12.948  9.579   70.573  1.00 166.55 ?  328  PHE B C   1 
ATOM   5928 O  O   . PHE B 1 329 ? 12.749  8.539   69.942  1.00 153.26 ?  328  PHE B O   1 
ATOM   5929 C  CB  . PHE B 1 329 ? 11.130  10.440  72.061  1.00 150.98 ?  328  PHE B CB  1 
ATOM   5930 C  CG  . PHE B 1 329 ? 9.990   9.633   71.508  1.00 137.64 ?  328  PHE B CG  1 
ATOM   5931 C  CD1 . PHE B 1 329 ? 10.010  8.250   71.575  1.00 131.41 ?  328  PHE B CD1 1 
ATOM   5932 C  CD2 . PHE B 1 329 ? 8.902   10.252  70.926  1.00 133.10 ?  328  PHE B CD2 1 
ATOM   5933 C  CE1 . PHE B 1 329 ? 8.963   7.501   71.074  1.00 121.93 ?  328  PHE B CE1 1 
ATOM   5934 C  CE2 . PHE B 1 329 ? 7.848   9.507   70.424  1.00 123.37 ?  328  PHE B CE2 1 
ATOM   5935 C  CZ  . PHE B 1 329 ? 7.880   8.130   70.498  1.00 116.17 ?  328  PHE B CZ  1 
ATOM   5936 N  N   . GLN B 1 330 ? 13.562  10.643  70.057  1.00 179.97 ?  329  GLN B N   1 
ATOM   5937 C  CA  . GLN B 1 330 ? 14.056  10.669  68.681  1.00 179.51 ?  329  GLN B CA  1 
ATOM   5938 C  C   . GLN B 1 330 ? 15.004  9.503   68.425  1.00 189.92 ?  329  GLN B C   1 
ATOM   5939 O  O   . GLN B 1 330 ? 14.857  8.766   67.449  1.00 184.36 ?  329  GLN B O   1 
ATOM   5940 C  CB  . GLN B 1 330 ? 14.780  11.991  68.386  1.00 169.08 ?  329  GLN B CB  1 
ATOM   5941 C  CG  . GLN B 1 330 ? 13.906  13.244  68.425  1.00 154.15 ?  329  GLN B CG  1 
ATOM   5942 C  CD  . GLN B 1 330 ? 14.722  14.525  68.313  1.00 143.99 ?  329  GLN B CD  1 
ATOM   5943 O  OE1 . GLN B 1 330 ? 15.873  14.584  68.749  1.00 138.37 ?  329  GLN B OE1 1 
ATOM   5944 N  NE2 . GLN B 1 330 ? 14.131  15.554  67.719  1.00 142.29 ?  329  GLN B NE2 1 
ATOM   5945 N  N   . ASP B 1 331 ? 15.979  9.347   69.315  1.00 221.09 ?  330  ASP B N   1 
ATOM   5946 C  CA  . ASP B 1 331 ? 16.948  8.264   69.221  1.00 245.27 ?  330  ASP B CA  1 
ATOM   5947 C  C   . ASP B 1 331 ? 16.294  6.895   69.388  1.00 238.62 ?  330  ASP B C   1 
ATOM   5948 O  O   . ASP B 1 331 ? 16.609  5.956   68.660  1.00 244.97 ?  330  ASP B O   1 
ATOM   5949 C  CB  . ASP B 1 331 ? 18.045  8.450   70.271  1.00 263.62 ?  330  ASP B CB  1 
ATOM   5950 C  CG  . ASP B 1 331 ? 19.087  7.353   70.224  1.00 276.68 ?  330  ASP B CG  1 
ATOM   5951 O  OD1 . ASP B 1 331 ? 19.366  6.842   69.118  1.00 285.83 ?  330  ASP B OD1 1 
ATOM   5952 O  OD2 . ASP B 1 331 ? 19.628  7.000   71.293  1.00 277.87 ?  330  ASP B OD2 1 
ATOM   5953 N  N   . TRP B 1 332 ? 15.383  6.791   70.351  1.00 211.19 ?  331  TRP B N   1 
ATOM   5954 C  CA  . TRP B 1 332 ? 14.734  5.522   70.661  1.00 187.38 ?  331  TRP B CA  1 
ATOM   5955 C  C   . TRP B 1 332 ? 13.899  5.030   69.482  1.00 165.15 ?  331  TRP B C   1 
ATOM   5956 O  O   . TRP B 1 332 ? 13.915  3.842   69.147  1.00 152.50 ?  331  TRP B O   1 
ATOM   5957 C  CB  . TRP B 1 332 ? 13.879  5.654   71.924  1.00 182.10 ?  331  TRP B CB  1 
ATOM   5958 C  CG  . TRP B 1 332 ? 13.301  4.354   72.387  1.00 179.86 ?  331  TRP B CG  1 
ATOM   5959 C  CD1 . TRP B 1 332 ? 13.914  3.416   73.166  1.00 183.41 ?  331  TRP B CD1 1 
ATOM   5960 C  CD2 . TRP B 1 332 ? 11.987  3.858   72.122  1.00 173.40 ?  331  TRP B CD2 1 
ATOM   5961 N  NE1 . TRP B 1 332 ? 13.067  2.358   73.390  1.00 178.94 ?  331  TRP B NE1 1 
ATOM   5962 C  CE2 . TRP B 1 332 ? 11.876  2.607   72.761  1.00 173.94 ?  331  TRP B CE2 1 
ATOM   5963 C  CE3 . TRP B 1 332 ? 10.895  4.348   71.403  1.00 175.45 ?  331  TRP B CE3 1 
ATOM   5964 C  CZ2 . TRP B 1 332 ? 10.716  1.841   72.703  1.00 173.71 ?  331  TRP B CZ2 1 
ATOM   5965 C  CZ3 . TRP B 1 332 ? 9.747   3.587   71.346  1.00 179.23 ?  331  TRP B CZ3 1 
ATOM   5966 C  CH2 . TRP B 1 332 ? 9.665   2.346   71.990  1.00 174.51 ?  331  TRP B CH2 1 
ATOM   5967 N  N   . LEU B 1 333 ? 13.163  5.949   68.865  1.00 158.43 ?  332  LEU B N   1 
ATOM   5968 C  CA  . LEU B 1 333 ? 12.310  5.604   67.738  1.00 154.73 ?  332  LEU B CA  1 
ATOM   5969 C  C   . LEU B 1 333 ? 13.179  5.178   66.563  1.00 170.99 ?  332  LEU B C   1 
ATOM   5970 O  O   . LEU B 1 333 ? 12.840  4.244   65.838  1.00 172.68 ?  332  LEU B O   1 
ATOM   5971 C  CB  . LEU B 1 333 ? 11.421  6.777   67.340  1.00 143.78 ?  332  LEU B CB  1 
ATOM   5972 C  CG  . LEU B 1 333 ? 10.350  6.436   66.304  1.00 142.63 ?  332  LEU B CG  1 
ATOM   5973 C  CD1 . LEU B 1 333 ? 9.489   5.278   66.777  1.00 137.62 ?  332  LEU B CD1 1 
ATOM   5974 C  CD2 . LEU B 1 333 ? 9.495   7.651   65.996  1.00 142.94 ?  332  LEU B CD2 1 
ATOM   5975 N  N   . GLU B 1 334 ? 14.296  5.879   66.384  1.00 183.09 ?  333  GLU B N   1 
ATOM   5976 C  CA  . GLU B 1 334 ? 15.262  5.570   65.334  1.00 197.70 ?  333  GLU B CA  1 
ATOM   5977 C  C   . GLU B 1 334 ? 15.784  4.141   65.490  1.00 210.27 ?  333  GLU B C   1 
ATOM   5978 O  O   . GLU B 1 334 ? 15.882  3.390   64.518  1.00 223.77 ?  333  GLU B O   1 
ATOM   5979 C  CB  . GLU B 1 334 ? 16.432  6.562   65.382  1.00 203.61 ?  333  GLU B CB  1 
ATOM   5980 C  CG  . GLU B 1 334 ? 16.239  7.877   64.622  1.00 203.75 ?  333  GLU B CG  1 
ATOM   5981 C  CD  . GLU B 1 334 ? 16.253  7.706   63.106  1.00 199.33 ?  333  GLU B CD  1 
ATOM   5982 O  OE1 . GLU B 1 334 ? 17.230  7.135   62.580  1.00 196.69 ?  333  GLU B OE1 1 
ATOM   5983 O  OE2 . GLU B 1 334 ? 15.298  8.152   62.435  1.00 196.18 ?  333  GLU B OE2 1 
ATOM   5984 N  N   . LYS B 1 335 ? 16.101  3.777   66.729  1.00 208.06 ?  334  LYS B N   1 
ATOM   5985 C  CA  . LYS B 1 335 ? 16.621  2.453   67.070  1.00 199.85 ?  334  LYS B CA  1 
ATOM   5986 C  C   . LYS B 1 335 ? 15.681  1.267   66.817  1.00 190.16 ?  334  LYS B C   1 
ATOM   5987 O  O   . LYS B 1 335 ? 16.067  0.288   66.180  1.00 188.38 ?  334  LYS B O   1 
ATOM   5988 C  CB  . LYS B 1 335 ? 17.039  2.445   68.546  1.00 197.24 ?  334  LYS B CB  1 
ATOM   5989 C  CG  . LYS B 1 335 ? 17.602  1.121   69.037  1.00 199.44 ?  334  LYS B CG  1 
ATOM   5990 C  CD  . LYS B 1 335 ? 18.860  0.736   68.276  1.00 207.64 ?  334  LYS B CD  1 
ATOM   5991 C  CE  . LYS B 1 335 ? 19.527  -0.484  68.890  1.00 205.59 ?  334  LYS B CE  1 
ATOM   5992 N  NZ  . LYS B 1 335 ? 19.969  -0.225  70.289  1.00 201.38 ?  334  LYS B NZ  1 
ATOM   5993 N  N   . HIS B 1 336 ? 14.449  1.364   67.310  1.00 180.54 ?  335  HIS B N   1 
ATOM   5994 C  CA  . HIS B 1 336 ? 13.522  0.226   67.330  1.00 179.79 ?  335  HIS B CA  1 
ATOM   5995 C  C   . HIS B 1 336 ? 12.655  0.038   66.084  1.00 176.95 ?  335  HIS B C   1 
ATOM   5996 O  O   . HIS B 1 336 ? 11.704  -0.743  66.110  1.00 176.39 ?  335  HIS B O   1 
ATOM   5997 C  CB  . HIS B 1 336 ? 12.620  0.308   68.566  1.00 176.93 ?  335  HIS B CB  1 
ATOM   5998 C  CG  . HIS B 1 336 ? 13.310  -0.003  69.845  1.00 174.46 ?  335  HIS B CG  1 
ATOM   5999 N  ND1 . HIS B 1 336 ? 14.679  -0.254  69.924  1.00 175.86 ?  335  HIS B ND1 1 
ATOM   6000 C  CD2 . HIS B 1 336 ? 12.861  -0.129  71.116  1.00 164.19 ?  335  HIS B CD2 1 
ATOM   6001 C  CE1 . HIS B 1 336 ? 15.015  -0.502  71.161  1.00 170.45 ?  335  HIS B CE1 1 
ATOM   6002 N  NE2 . HIS B 1 336 ? 13.918  -0.433  71.920  1.00 162.09 ?  335  HIS B NE2 1 
ATOM   6003 N  N   . GLY B 1 337 ? 12.953  0.770   65.015  1.00 180.65 ?  336  GLY B N   1 
ATOM   6004 C  CA  . GLY B 1 337 ? 12.150  0.699   63.804  1.00 186.61 ?  336  GLY B CA  1 
ATOM   6005 C  C   . GLY B 1 337 ? 12.147  -0.707  63.223  1.00 191.10 ?  336  GLY B C   1 
ATOM   6006 O  O   . GLY B 1 337 ? 13.087  -1.470  63.446  1.00 209.37 ?  336  GLY B O   1 
ATOM   6007 N  N   . ASP B 1 338 ? 11.099  -1.060  62.482  1.00 176.28 ?  337  ASP B N   1 
ATOM   6008 C  CA  . ASP B 1 338 ? 10.033  -0.135  62.131  1.00 162.61 ?  337  ASP B CA  1 
ATOM   6009 C  C   . ASP B 1 338 ? 8.675   -0.738  62.474  1.00 154.76 ?  337  ASP B C   1 
ATOM   6010 O  O   . ASP B 1 338 ? 8.498   -1.953  62.451  1.00 160.99 ?  337  ASP B O   1 
ATOM   6011 C  CB  . ASP B 1 338 ? 10.083  0.198   60.635  1.00 178.35 ?  337  ASP B CB  1 
ATOM   6012 C  CG  . ASP B 1 338 ? 11.474  0.583   60.158  1.00 181.64 ?  337  ASP B CG  1 
ATOM   6013 O  OD1 . ASP B 1 338 ? 12.072  1.518   60.730  1.00 182.09 ?  337  ASP B OD1 1 
ATOM   6014 O  OD2 . ASP B 1 338 ? 11.969  -0.047  59.200  1.00 178.26 ?  337  ASP B OD2 1 
ATOM   6015 N  N   . TYR B 1 339 ? 7.723   0.125   62.804  1.00 151.16 ?  338  TYR B N   1 
ATOM   6016 C  CA  . TYR B 1 339 ? 6.374   -0.291  63.161  1.00 150.31 ?  338  TYR B CA  1 
ATOM   6017 C  C   . TYR B 1 339 ? 5.381   0.144   62.078  1.00 145.94 ?  338  TYR B C   1 
ATOM   6018 O  O   . TYR B 1 339 ? 5.403   1.290   61.640  1.00 149.05 ?  338  TYR B O   1 
ATOM   6019 C  CB  . TYR B 1 339 ? 6.002   0.282   64.533  1.00 156.28 ?  338  TYR B CB  1 
ATOM   6020 C  CG  . TYR B 1 339 ? 6.937   -0.175  65.641  1.00 166.57 ?  338  TYR B CG  1 
ATOM   6021 C  CD1 . TYR B 1 339 ? 7.546   -1.423  65.591  1.00 173.62 ?  338  TYR B CD1 1 
ATOM   6022 C  CD2 . TYR B 1 339 ? 7.232   0.651   66.721  1.00 165.23 ?  338  TYR B CD2 1 
ATOM   6023 C  CE1 . TYR B 1 339 ? 8.409   -1.843  66.589  1.00 177.11 ?  338  TYR B CE1 1 
ATOM   6024 C  CE2 . TYR B 1 339 ? 8.095   0.237   67.724  1.00 170.26 ?  338  TYR B CE2 1 
ATOM   6025 C  CZ  . TYR B 1 339 ? 8.679   -1.010  67.654  1.00 174.60 ?  338  TYR B CZ  1 
ATOM   6026 O  OH  . TYR B 1 339 ? 9.537   -1.426  68.649  1.00 171.89 ?  338  TYR B OH  1 
ATOM   6027 N  N   . GLU B 1 340 ? 4.530   -0.773  61.633  1.00 134.28 ?  339  GLU B N   1 
ATOM   6028 C  CA  . GLU B 1 340 ? 3.531   -0.464  60.613  1.00 122.38 ?  339  GLU B CA  1 
ATOM   6029 C  C   . GLU B 1 340 ? 2.473   0.504   61.133  1.00 111.29 ?  339  GLU B C   1 
ATOM   6030 O  O   . GLU B 1 340 ? 1.934   1.311   60.384  1.00 111.77 ?  339  GLU B O   1 
ATOM   6031 C  CB  . GLU B 1 340 ? 2.868   -1.753  60.114  1.00 139.33 ?  339  GLU B CB  1 
ATOM   6032 C  CG  . GLU B 1 340 ? 3.805   -2.644  59.331  1.00 162.62 ?  339  GLU B CG  1 
ATOM   6033 C  CD  . GLU B 1 340 ? 3.748   -2.415  57.834  1.00 185.53 ?  339  GLU B CD  1 
ATOM   6034 O  OE1 . GLU B 1 340 ? 2.634   -2.374  57.272  1.00 188.31 ?  339  GLU B OE1 1 
ATOM   6035 O  OE2 . GLU B 1 340 ? 4.823   -2.251  57.221  1.00 197.92 ?  339  GLU B OE2 1 
ATOM   6036 N  N   . ALA B 1 341 ? 2.175   0.421   62.421  1.00 113.77 ?  340  ALA B N   1 
ATOM   6037 C  CA  . ALA B 1 341 ? 1.215   1.334   63.025  1.00 116.91 ?  340  ALA B CA  1 
ATOM   6038 C  C   . ALA B 1 341 ? 1.641   1.746   64.419  1.00 129.40 ?  340  ALA B C   1 
ATOM   6039 O  O   . ALA B 1 341 ? 2.483   1.100   65.041  1.00 166.69 ?  340  ALA B O   1 
ATOM   6040 C  CB  . ALA B 1 341 ? -0.165  0.701   63.066  1.00 115.36 ?  340  ALA B CB  1 
ATOM   6041 N  N   . ILE B 1 342 ? 1.066   2.844   64.895  1.00 121.79 ?  341  ILE B N   1 
ATOM   6042 C  CA  . ILE B 1 342 ? 1.317   3.317   66.247  1.00 100.70 ?  341  ILE B CA  1 
ATOM   6043 C  C   . ILE B 1 342 ? -0.012  3.802   66.830  1.00 110.39 ?  341  ILE B C   1 
ATOM   6044 O  O   . ILE B 1 342 ? -0.844  4.359   66.116  1.00 98.99  ?  341  ILE B O   1 
ATOM   6045 C  CB  . ILE B 1 342 ? 2.394   4.426   66.285  1.00 101.72 ?  341  ILE B CB  1 
ATOM   6046 C  CG1 . ILE B 1 342 ? 2.030   5.568   65.348  1.00 127.83 ?  341  ILE B CG1 1 
ATOM   6047 C  CG2 . ILE B 1 342 ? 3.760   3.875   65.904  1.00 103.86 ?  341  ILE B CG2 1 
ATOM   6048 C  CD1 . ILE B 1 342 ? 1.484   6.747   66.069  1.00 141.63 ?  341  ILE B CD1 1 
ATOM   6049 N  N   . VAL B 1 343 ? -0.216  3.562   68.123  1.00 112.72 ?  342  VAL B N   1 
ATOM   6050 C  CA  . VAL B 1 343 ? -1.508  3.806   68.760  1.00 104.85 ?  342  VAL B CA  1 
ATOM   6051 C  C   . VAL B 1 343 ? -1.481  4.915   69.802  1.00 102.59 ?  342  VAL B C   1 
ATOM   6052 O  O   . VAL B 1 343 ? -0.522  5.056   70.565  1.00 94.90  ?  342  VAL B O   1 
ATOM   6053 C  CB  . VAL B 1 343 ? -2.046  2.535   69.458  1.00 94.45  ?  342  VAL B CB  1 
ATOM   6054 C  CG1 . VAL B 1 343 ? -3.558  2.619   69.638  1.00 93.51  ?  342  VAL B CG1 1 
ATOM   6055 C  CG2 . VAL B 1 343 ? -1.657  1.287   68.686  1.00 97.38  ?  342  VAL B CG2 1 
ATOM   6056 N  N   . ASP B 1 344 ? -2.561  5.687   69.830  1.00 104.43 ?  343  ASP B N   1 
ATOM   6057 C  CA  . ASP B 1 344 ? -2.764  6.707   70.843  1.00 111.19 ?  343  ASP B CA  1 
ATOM   6058 C  C   . ASP B 1 344 ? -3.347  6.043   72.083  1.00 120.51 ?  343  ASP B C   1 
ATOM   6059 O  O   . ASP B 1 344 ? -4.548  5.774   72.144  1.00 107.91 ?  343  ASP B O   1 
ATOM   6060 C  CB  . ASP B 1 344 ? -3.681  7.816   70.313  1.00 113.17 ?  343  ASP B CB  1 
ATOM   6061 C  CG  . ASP B 1 344 ? -4.041  8.844   71.371  1.00 118.89 ?  343  ASP B CG  1 
ATOM   6062 O  OD1 . ASP B 1 344 ? -3.375  8.890   72.427  1.00 140.29 ?  343  ASP B OD1 1 
ATOM   6063 O  OD2 . ASP B 1 344 ? -4.985  9.627   71.138  1.00 96.58  ?  343  ASP B OD2 1 
ATOM   6064 N  N   . GLY B 1 345 ? -2.475  5.752   73.046  1.00 136.93 ?  344  GLY B N   1 
ATOM   6065 C  CA  . GLY B 1 345 ? -2.842  5.018   74.244  1.00 137.91 ?  344  GLY B CA  1 
ATOM   6066 C  C   . GLY B 1 345 ? -4.017  5.584   75.020  1.00 125.10 ?  344  GLY B C   1 
ATOM   6067 O  O   . GLY B 1 345 ? -4.927  4.849   75.400  1.00 115.04 ?  344  GLY B O   1 
ATOM   6068 N  N   . ALA B 1 346 ? -3.997  6.893   75.250  1.00 121.77 ?  345  ALA B N   1 
ATOM   6069 C  CA  . ALA B 1 346 ? -5.049  7.565   76.011  1.00 112.77 ?  345  ALA B CA  1 
ATOM   6070 C  C   . ALA B 1 346 ? -6.423  7.395   75.366  1.00 112.86 ?  345  ALA B C   1 
ATOM   6071 O  O   . ALA B 1 346 ? -7.383  7.023   76.032  1.00 107.48 ?  345  ALA B O   1 
ATOM   6072 C  CB  . ALA B 1 346 ? -4.725  9.036   76.170  1.00 112.12 ?  345  ALA B CB  1 
ATOM   6073 N  N   . ASN B 1 347 ? -6.505  7.680   74.070  1.00 129.47 ?  346  ASN B N   1 
ATOM   6074 C  CA  . ASN B 1 347 ? -7.770  7.648   73.341  1.00 129.62 ?  346  ASN B CA  1 
ATOM   6075 C  C   . ASN B 1 347 ? -8.532  6.336   73.457  1.00 127.47 ?  346  ASN B C   1 
ATOM   6076 O  O   . ASN B 1 347 ? -9.738  6.339   73.715  1.00 132.26 ?  346  ASN B O   1 
ATOM   6077 C  CB  . ASN B 1 347 ? -7.531  7.943   71.860  1.00 135.75 ?  346  ASN B CB  1 
ATOM   6078 C  CG  . ASN B 1 347 ? -8.811  8.209   71.109  1.00 143.73 ?  346  ASN B CG  1 
ATOM   6079 O  OD1 . ASN B 1 347 ? -9.773  8.729   71.673  1.00 136.69 ?  346  ASN B OD1 1 
ATOM   6080 N  ND2 . ASN B 1 347 ? -8.835  7.849   69.830  1.00 165.19 ?  346  ASN B ND2 1 
ATOM   6081 N  N   . ILE B 1 348 ? -7.830  5.222   73.254  1.00 121.65 ?  347  ILE B N   1 
ATOM   6082 C  CA  . ILE B 1 348 ? -8.464  3.909   73.299  1.00 111.92 ?  347  ILE B CA  1 
ATOM   6083 C  C   . ILE B 1 348 ? -9.062  3.630   74.672  1.00 97.63  ?  347  ILE B C   1 
ATOM   6084 O  O   . ILE B 1 348 ? -10.257 3.359   74.791  1.00 90.08  ?  347  ILE B O   1 
ATOM   6085 C  CB  . ILE B 1 348 ? -7.468  2.785   72.963  1.00 114.17 ?  347  ILE B CB  1 
ATOM   6086 C  CG1 . ILE B 1 348 ? -6.579  3.188   71.786  1.00 116.73 ?  347  ILE B CG1 1 
ATOM   6087 C  CG2 . ILE B 1 348 ? -8.198  1.484   72.681  1.00 116.82 ?  347  ILE B CG2 1 
ATOM   6088 C  CD1 . ILE B 1 348 ? -7.318  3.348   70.471  1.00 113.68 ?  347  ILE B CD1 1 
ATOM   6089 N  N   . GLY B 1 349 ? -8.221  3.714   75.702  1.00 94.94  ?  348  GLY B N   1 
ATOM   6090 C  CA  . GLY B 1 349 ? -8.602  3.393   77.068  1.00 100.33 ?  348  GLY B CA  1 
ATOM   6091 C  C   . GLY B 1 349 ? -9.712  4.266   77.612  1.00 114.11 ?  348  GLY B C   1 
ATOM   6092 O  O   . GLY B 1 349 ? -10.531 3.816   78.409  1.00 131.25 ?  348  GLY B O   1 
ATOM   6093 N  N   . LEU B 1 350 ? -9.717  5.524   77.191  1.00 110.51 ?  349  LEU B N   1 
ATOM   6094 C  CA  . LEU B 1 350 ? -10.693 6.510   77.639  1.00 114.45 ?  349  LEU B CA  1 
ATOM   6095 C  C   . LEU B 1 350 ? -11.982 6.491   76.814  1.00 105.10 ?  349  LEU B C   1 
ATOM   6096 O  O   . LEU B 1 350 ? -12.991 7.068   77.224  1.00 100.87 ?  349  LEU B O   1 
ATOM   6097 C  CB  . LEU B 1 350 ? -10.073 7.909   77.606  1.00 132.85 ?  349  LEU B CB  1 
ATOM   6098 C  CG  . LEU B 1 350 ? -8.923  8.158   78.587  1.00 140.03 ?  349  LEU B CG  1 
ATOM   6099 C  CD1 . LEU B 1 350 ? -8.078  9.336   78.131  1.00 141.57 ?  349  LEU B CD1 1 
ATOM   6100 C  CD2 . LEU B 1 350 ? -9.446  8.383   79.999  1.00 148.15 ?  349  LEU B CD2 1 
ATOM   6101 N  N   . TYR B 1 351 ? -11.955 5.808   75.671  1.00 100.16 ?  350  TYR B N   1 
ATOM   6102 C  CA  . TYR B 1 351 ? -13.115 5.767   74.781  1.00 96.77  ?  350  TYR B CA  1 
ATOM   6103 C  C   . TYR B 1 351 ? -14.363 5.171   75.415  1.00 116.92 ?  350  TYR B C   1 
ATOM   6104 O  O   . TYR B 1 351 ? -14.341 4.081   75.989  1.00 129.49 ?  350  TYR B O   1 
ATOM   6105 C  CB  . TYR B 1 351 ? -12.776 4.980   73.511  1.00 91.99  ?  350  TYR B CB  1 
ATOM   6106 C  CG  . TYR B 1 351 ? -13.831 5.073   72.424  1.00 116.15 ?  350  TYR B CG  1 
ATOM   6107 C  CD1 . TYR B 1 351 ? -14.243 6.306   71.931  1.00 134.65 ?  350  TYR B CD1 1 
ATOM   6108 C  CD2 . TYR B 1 351 ? -14.401 3.928   71.878  1.00 118.42 ?  350  TYR B CD2 1 
ATOM   6109 C  CE1 . TYR B 1 351 ? -15.202 6.396   70.933  1.00 138.24 ?  350  TYR B CE1 1 
ATOM   6110 C  CE2 . TYR B 1 351 ? -15.355 4.009   70.879  1.00 126.36 ?  350  TYR B CE2 1 
ATOM   6111 C  CZ  . TYR B 1 351 ? -15.754 5.246   70.412  1.00 135.94 ?  350  TYR B CZ  1 
ATOM   6112 O  OH  . TYR B 1 351 ? -16.705 5.341   69.421  1.00 141.40 ?  350  TYR B OH  1 
ATOM   6113 N  N   . GLN B 1 352 ? -15.449 5.929   75.289  1.00 123.70 ?  351  GLN B N   1 
ATOM   6114 C  CA  . GLN B 1 352 ? -16.769 5.616   75.838  1.00 133.26 ?  351  GLN B CA  1 
ATOM   6115 C  C   . GLN B 1 352 ? -16.775 5.305   77.337  1.00 144.82 ?  351  GLN B C   1 
ATOM   6116 O  O   . GLN B 1 352 ? -17.777 4.827   77.877  1.00 145.91 ?  351  GLN B O   1 
ATOM   6117 C  CB  . GLN B 1 352 ? -17.386 4.460   75.050  1.00 129.61 ?  351  GLN B CB  1 
ATOM   6118 C  CG  . GLN B 1 352 ? -17.333 4.707   73.552  1.00 134.04 ?  351  GLN B CG  1 
ATOM   6119 C  CD  . GLN B 1 352 ? -18.563 4.226   72.819  1.00 138.36 ?  351  GLN B CD  1 
ATOM   6120 O  OE1 . GLN B 1 352 ? -18.616 3.090   72.357  1.00 153.37 ?  351  GLN B OE1 1 
ATOM   6121 N  NE2 . GLN B 1 352 ? -19.558 5.098   72.696  1.00 127.52 ?  351  GLN B NE2 1 
ATOM   6122 N  N   . GLN B 1 353 ? -15.649 5.563   77.998  1.00 146.68 ?  352  GLN B N   1 
ATOM   6123 C  CA  . GLN B 1 353 ? -15.555 5.456   79.447  1.00 134.96 ?  352  GLN B CA  1 
ATOM   6124 C  C   . GLN B 1 353 ? -16.214 6.702   80.014  1.00 132.49 ?  352  GLN B C   1 
ATOM   6125 O  O   . GLN B 1 353 ? -16.080 7.778   79.427  1.00 119.69 ?  352  GLN B O   1 
ATOM   6126 C  CB  . GLN B 1 353 ? -14.104 5.338   79.902  1.00 119.69 ?  352  GLN B CB  1 
ATOM   6127 C  CG  . GLN B 1 353 ? -13.363 4.181   79.271  1.00 125.63 ?  352  GLN B CG  1 
ATOM   6128 C  CD  . GLN B 1 353 ? -13.654 2.851   79.937  1.00 146.12 ?  352  GLN B CD  1 
ATOM   6129 O  OE1 . GLN B 1 353 ? -12.855 2.358   80.734  1.00 158.49 ?  352  GLN B OE1 1 
ATOM   6130 N  NE2 . GLN B 1 353 ? -14.794 2.256   79.606  1.00 150.27 ?  352  GLN B NE2 1 
ATOM   6131 N  N   . ASN B 1 354 ? -16.915 6.593   81.138  1.00 130.95 ?  353  ASN B N   1 
ATOM   6132 C  CA  . ASN B 1 354 ? -17.527 7.792   81.682  1.00 120.86 ?  353  ASN B CA  1 
ATOM   6133 C  C   . ASN B 1 354 ? -16.428 8.707   82.217  1.00 125.57 ?  353  ASN B C   1 
ATOM   6134 O  O   . ASN B 1 354 ? -15.383 8.237   82.677  1.00 121.77 ?  353  ASN B O   1 
ATOM   6135 C  CB  . ASN B 1 354 ? -18.533 7.451   82.778  1.00 119.37 ?  353  ASN B CB  1 
ATOM   6136 C  CG  . ASN B 1 354 ? -19.575 8.540   82.968  1.00 135.70 ?  353  ASN B CG  1 
ATOM   6137 O  OD1 . ASN B 1 354 ? -19.275 9.731   82.869  1.00 139.27 ?  353  ASN B OD1 1 
ATOM   6138 N  ND2 . ASN B 1 354 ? -20.806 8.134   83.257  1.00 139.60 ?  353  ASN B ND2 1 
ATOM   6139 N  N   . PHE B 1 355 ? -16.667 10.012  82.145  1.00 135.93 ?  354  PHE B N   1 
ATOM   6140 C  CA  . PHE B 1 355 ? -15.685 10.998  82.578  1.00 138.84 ?  354  PHE B CA  1 
ATOM   6141 C  C   . PHE B 1 355 ? -15.640 11.176  84.094  1.00 125.90 ?  354  PHE B C   1 
ATOM   6142 O  O   . PHE B 1 355 ? -14.586 11.471  84.653  1.00 116.87 ?  354  PHE B O   1 
ATOM   6143 C  CB  . PHE B 1 355 ? -15.952 12.347  81.896  1.00 156.44 ?  354  PHE B CB  1 
ATOM   6144 C  CG  . PHE B 1 355 ? -17.411 12.688  81.763  1.00 171.90 ?  354  PHE B CG  1 
ATOM   6145 C  CD1 . PHE B 1 355 ? -18.150 13.056  82.881  1.00 187.84 ?  354  PHE B CD1 1 
ATOM   6146 C  CD2 . PHE B 1 355 ? -18.041 12.663  80.524  1.00 166.59 ?  354  PHE B CD2 1 
ATOM   6147 C  CE1 . PHE B 1 355 ? -19.486 13.370  82.776  1.00 186.02 ?  354  PHE B CE1 1 
ATOM   6148 C  CE2 . PHE B 1 355 ? -19.386 12.989  80.413  1.00 168.19 ?  354  PHE B CE2 1 
ATOM   6149 C  CZ  . PHE B 1 355 ? -20.110 13.350  81.534  1.00 176.84 ?  354  PHE B CZ  1 
ATOM   6150 N  N   . VAL B 1 356 ? -16.778 10.991  84.757  1.00 127.93 ?  355  VAL B N   1 
ATOM   6151 C  CA  . VAL B 1 356 ? -16.868 11.230  86.195  1.00 132.52 ?  355  VAL B CA  1 
ATOM   6152 C  C   . VAL B 1 356 ? -16.140 10.163  87.024  1.00 139.31 ?  355  VAL B C   1 
ATOM   6153 O  O   . VAL B 1 356 ? -15.291 10.493  87.851  1.00 148.83 ?  355  VAL B O   1 
ATOM   6154 C  CB  . VAL B 1 356 ? -18.353 11.333  86.643  1.00 157.08 ?  355  VAL B CB  1 
ATOM   6155 C  CG1 . VAL B 1 356 ? -19.208 10.262  85.987  1.00 154.92 ?  355  VAL B CG1 1 
ATOM   6156 C  CG2 . VAL B 1 356 ? -18.479 11.279  88.157  1.00 163.07 ?  355  VAL B CG2 1 
ATOM   6157 N  N   . ASP B 1 357 ? -16.446 8.890   86.803  1.00 136.75 ?  356  ASP B N   1 
ATOM   6158 C  CA  . ASP B 1 357 ? -15.616 7.826   87.364  1.00 136.10 ?  356  ASP B CA  1 
ATOM   6159 C  C   . ASP B 1 357 ? -14.443 7.600   86.420  1.00 138.37 ?  356  ASP B C   1 
ATOM   6160 O  O   . ASP B 1 357 ? -14.625 7.271   85.251  1.00 145.06 ?  356  ASP B O   1 
ATOM   6161 C  CB  . ASP B 1 357 ? -16.451 6.563   87.614  1.00 135.27 ?  356  ASP B CB  1 
ATOM   6162 C  CG  . ASP B 1 357 ? -17.220 6.124   86.393  1.00 135.73 ?  356  ASP B CG  1 
ATOM   6163 O  OD1 . ASP B 1 357 ? -17.956 6.966   85.830  1.00 135.06 ?  356  ASP B OD1 1 
ATOM   6164 O  OD2 . ASP B 1 357 ? -17.150 4.930   86.041  1.00 144.23 ?  356  ASP B OD2 1 
ATOM   6165 N  N   . GLY B 1 358 ? -13.237 7.803   86.936  1.00 134.92 ?  357  GLY B N   1 
ATOM   6166 C  CA  . GLY B 1 358 ? -12.037 7.719   86.124  1.00 131.05 ?  357  GLY B CA  1 
ATOM   6167 C  C   . GLY B 1 358 ? -11.663 6.317   85.705  1.00 127.61 ?  357  GLY B C   1 
ATOM   6168 O  O   . GLY B 1 358 ? -10.645 5.787   86.145  1.00 134.65 ?  357  GLY B O   1 
ATOM   6169 N  N   . SER B 1 359 ? -12.483 5.717   84.848  1.00 131.62 ?  358  SER B N   1 
ATOM   6170 C  CA  . SER B 1 359 ? -12.202 4.387   84.328  1.00 92.98  ?  358  SER B CA  1 
ATOM   6171 C  C   . SER B 1 359 ? -11.063 4.429   83.323  1.00 91.59  ?  358  SER B C   1 
ATOM   6172 O  O   . SER B 1 359 ? -10.770 5.476   82.749  1.00 104.73 ?  358  SER B O   1 
ATOM   6173 C  CB  . SER B 1 359 ? -13.452 3.791   83.675  1.00 93.50  ?  358  SER B CB  1 
ATOM   6174 O  OG  . SER B 1 359 ? -14.577 3.886   84.530  1.00 108.78 ?  358  SER B OG  1 
ATOM   6175 N  N   . PHE B 1 360 ? -10.392 3.298   83.142  1.00 109.08 ?  359  PHE B N   1 
ATOM   6176 C  CA  . PHE B 1 360 ? -9.493  3.145   82.010  1.00 100.77 ?  359  PHE B CA  1 
ATOM   6177 C  C   . PHE B 1 360 ? -9.562  1.723   81.457  1.00 107.65 ?  359  PHE B C   1 
ATOM   6178 O  O   . PHE B 1 360 ? -9.323  0.755   82.179  1.00 125.77 ?  359  PHE B O   1 
ATOM   6179 C  CB  . PHE B 1 360 ? -8.067  3.499   82.406  1.00 89.95  ?  359  PHE B CB  1 
ATOM   6180 C  CG  . PHE B 1 360 ? -7.087  3.360   81.290  1.00 89.35  ?  359  PHE B CG  1 
ATOM   6181 C  CD1 . PHE B 1 360 ? -6.877  4.409   80.412  1.00 89.01  ?  359  PHE B CD1 1 
ATOM   6182 C  CD2 . PHE B 1 360 ? -6.373  2.191   81.111  1.00 97.20  ?  359  PHE B CD2 1 
ATOM   6183 C  CE1 . PHE B 1 360 ? -5.975  4.301   79.378  1.00 88.80  ?  359  PHE B CE1 1 
ATOM   6184 C  CE2 . PHE B 1 360 ? -5.468  2.075   80.070  1.00 106.31 ?  359  PHE B CE2 1 
ATOM   6185 C  CZ  . PHE B 1 360 ? -5.268  3.134   79.205  1.00 95.32  ?  359  PHE B CZ  1 
ATOM   6186 N  N   . SER B 1 361 ? -9.885  1.611   80.172  1.00 106.15 ?  360  SER B N   1 
ATOM   6187 C  CA  . SER B 1 361 ? -10.138 0.319   79.542  1.00 117.95 ?  360  SER B CA  1 
ATOM   6188 C  C   . SER B 1 361 ? -8.909  -0.311  78.890  1.00 108.12 ?  360  SER B C   1 
ATOM   6189 O  O   . SER B 1 361 ? -8.627  -0.060  77.723  1.00 95.74  ?  360  SER B O   1 
ATOM   6190 C  CB  . SER B 1 361 ? -11.245 0.455   78.499  1.00 122.00 ?  360  SER B CB  1 
ATOM   6191 O  OG  . SER B 1 361 ? -11.547 -0.805  77.936  1.00 134.36 ?  360  SER B OG  1 
ATOM   6192 N  N   . LEU B 1 362 ? -8.191  -1.145  79.631  1.00 112.26 ?  361  LEU B N   1 
ATOM   6193 C  CA  . LEU B 1 362 ? -7.119  -1.934  79.034  1.00 114.27 ?  361  LEU B CA  1 
ATOM   6194 C  C   . LEU B 1 362 ? -7.675  -2.995  78.077  1.00 121.94 ?  361  LEU B C   1 
ATOM   6195 O  O   . LEU B 1 362 ? -6.987  -3.432  77.155  1.00 108.98 ?  361  LEU B O   1 
ATOM   6196 C  CB  . LEU B 1 362 ? -6.263  -2.586  80.129  1.00 113.58 ?  361  LEU B CB  1 
ATOM   6197 C  CG  . LEU B 1 362 ? -5.028  -3.372  79.678  1.00 114.93 ?  361  LEU B CG  1 
ATOM   6198 C  CD1 . LEU B 1 362 ? -3.869  -3.139  80.621  1.00 112.74 ?  361  LEU B CD1 1 
ATOM   6199 C  CD2 . LEU B 1 362 ? -5.341  -4.860  79.605  1.00 122.84 ?  361  LEU B CD2 1 
ATOM   6200 N  N   . SER B 1 363 ? -8.924  -3.398  78.295  1.00 129.26 ?  362  SER B N   1 
ATOM   6201 C  CA  . SER B 1 363 ? -9.587  -4.371  77.426  1.00 137.25 ?  362  SER B CA  1 
ATOM   6202 C  C   . SER B 1 363 ? -9.682  -3.883  75.980  1.00 142.37 ?  362  SER B C   1 
ATOM   6203 O  O   . SER B 1 363 ? -9.468  -4.650  75.039  1.00 143.94 ?  362  SER B O   1 
ATOM   6204 C  CB  . SER B 1 363 ? -10.983 -4.708  77.962  1.00 130.21 ?  362  SER B CB  1 
ATOM   6205 O  OG  . SER B 1 363 ? -11.714 -3.539  78.294  1.00 125.43 ?  362  SER B OG  1 
ATOM   6206 N  N   . GLN B 1 364 ? -10.002 -2.604  75.814  1.00 133.11 ?  363  GLN B N   1 
ATOM   6207 C  CA  . GLN B 1 364 ? -10.099 -1.986  74.495  1.00 115.74 ?  363  GLN B CA  1 
ATOM   6208 C  C   . GLN B 1 364 ? -8.724  -1.787  73.869  1.00 102.50 ?  363  GLN B C   1 
ATOM   6209 O  O   . GLN B 1 364 ? -8.581  -1.862  72.654  1.00 107.58 ?  363  GLN B O   1 
ATOM   6210 C  CB  . GLN B 1 364 ? -10.857 -0.662  74.597  1.00 108.04 ?  363  GLN B CB  1 
ATOM   6211 C  CG  . GLN B 1 364 ? -12.331 -0.866  74.934  1.00 110.78 ?  363  GLN B CG  1 
ATOM   6212 C  CD  . GLN B 1 364 ? -13.079 0.430   75.174  1.00 109.18 ?  363  GLN B CD  1 
ATOM   6213 O  OE1 . GLN B 1 364 ? -12.482 1.502   75.239  1.00 112.86 ?  363  GLN B OE1 1 
ATOM   6214 N  NE2 . GLN B 1 364 ? -14.398 0.333   75.322  1.00 101.67 ?  363  GLN B NE2 1 
ATOM   6215 N  N   . LEU B 1 365 ? -7.719  -1.521  74.697  1.00 100.10 ?  364  LEU B N   1 
ATOM   6216 C  CA  . LEU B 1 365 ? -6.335  -1.477  74.228  1.00 102.16 ?  364  LEU B CA  1 
ATOM   6217 C  C   . LEU B 1 365 ? -5.900  -2.823  73.668  1.00 108.81 ?  364  LEU B C   1 
ATOM   6218 O  O   . LEU B 1 365 ? -5.279  -2.897  72.610  1.00 108.88 ?  364  LEU B O   1 
ATOM   6219 C  CB  . LEU B 1 365 ? -5.382  -1.088  75.361  1.00 106.82 ?  364  LEU B CB  1 
ATOM   6220 C  CG  . LEU B 1 365 ? -4.909  0.357   75.459  1.00 90.36  ?  364  LEU B CG  1 
ATOM   6221 C  CD1 . LEU B 1 365 ? -4.347  0.797   74.120  1.00 90.76  ?  364  LEU B CD1 1 
ATOM   6222 C  CD2 . LEU B 1 365 ? -6.035  1.255   75.913  1.00 89.63  ?  364  LEU B CD2 1 
ATOM   6223 N  N   . GLU B 1 366 ? -6.238  -3.886  74.392  1.00 111.51 ?  365  GLU B N   1 
ATOM   6224 C  CA  . GLU B 1 366 ? -5.838  -5.233  74.016  1.00 115.19 ?  365  GLU B CA  1 
ATOM   6225 C  C   . GLU B 1 366 ? -6.521  -5.634  72.719  1.00 117.24 ?  365  GLU B C   1 
ATOM   6226 O  O   . GLU B 1 366 ? -5.925  -6.296  71.871  1.00 118.35 ?  365  GLU B O   1 
ATOM   6227 C  CB  . GLU B 1 366 ? -6.183  -6.227  75.131  1.00 127.42 ?  365  GLU B CB  1 
ATOM   6228 C  CG  . GLU B 1 366 ? -5.330  -7.490  75.141  1.00 146.12 ?  365  GLU B CG  1 
ATOM   6229 C  CD  . GLU B 1 366 ? -5.787  -8.499  76.184  1.00 154.69 ?  365  GLU B CD  1 
ATOM   6230 O  OE1 . GLU B 1 366 ? -6.759  -8.207  76.914  1.00 157.45 ?  365  GLU B OE1 1 
ATOM   6231 O  OE2 . GLU B 1 366 ? -5.180  -9.589  76.265  1.00 145.73 ?  365  GLU B OE2 1 
ATOM   6232 N  N   . SER B 1 367 ? -7.767  -5.199  72.564  1.00 114.18 ?  366  SER B N   1 
ATOM   6233 C  CA  . SER B 1 367 ? -8.551  -5.498  71.374  1.00 101.35 ?  366  SER B CA  1 
ATOM   6234 C  C   . SER B 1 367 ? -7.893  -4.917  70.129  1.00 120.60 ?  366  SER B C   1 
ATOM   6235 O  O   . SER B 1 367 ? -7.709  -5.615  69.131  1.00 122.21 ?  366  SER B O   1 
ATOM   6236 C  CB  . SER B 1 367 ? -9.971  -4.951  71.524  1.00 97.67  ?  366  SER B CB  1 
ATOM   6237 O  OG  . SER B 1 367 ? -10.622 -5.538  72.637  1.00 107.50 ?  366  SER B OG  1 
ATOM   6238 N  N   . VAL B 1 368 ? -7.536  -3.637  70.206  1.00 133.58 ?  367  VAL B N   1 
ATOM   6239 C  CA  . VAL B 1 368 ? -6.911  -2.920  69.097  1.00 96.80  ?  367  VAL B CA  1 
ATOM   6240 C  C   . VAL B 1 368 ? -5.573  -3.550  68.723  1.00 98.03  ?  367  VAL B C   1 
ATOM   6241 O  O   . VAL B 1 368 ? -5.229  -3.668  67.548  1.00 125.14 ?  367  VAL B O   1 
ATOM   6242 C  CB  . VAL B 1 368 ? -6.716  -1.433  69.460  1.00 95.07  ?  367  VAL B CB  1 
ATOM   6243 C  CG1 . VAL B 1 368 ? -5.698  -0.767  68.554  1.00 95.58  ?  367  VAL B CG1 1 
ATOM   6244 C  CG2 . VAL B 1 368 ? -8.051  -0.703  69.419  1.00 94.57  ?  367  VAL B CG2 1 
ATOM   6245 N  N   . MET B 1 369 ? -4.835  -3.985  69.733  1.00 107.21 ?  368  MET B N   1 
ATOM   6246 C  CA  . MET B 1 369 ? -3.575  -4.684  69.523  1.00 110.48 ?  368  MET B CA  1 
ATOM   6247 C  C   . MET B 1 369 ? -3.767  -6.056  68.875  1.00 111.64 ?  368  MET B C   1 
ATOM   6248 O  O   . MET B 1 369 ? -2.995  -6.450  68.004  1.00 107.15 ?  368  MET B O   1 
ATOM   6249 C  CB  . MET B 1 369 ? -2.835  -4.808  70.851  1.00 116.04 ?  368  MET B CB  1 
ATOM   6250 C  CG  . MET B 1 369 ? -2.430  -3.462  71.409  1.00 96.71  ?  368  MET B CG  1 
ATOM   6251 S  SD  . MET B 1 369 ? -0.744  -3.069  70.943  1.00 180.65 ?  368  MET B SD  1 
ATOM   6252 C  CE  . MET B 1 369 ? 0.076   -4.522  71.582  1.00 184.60 ?  368  MET B CE  1 
ATOM   6253 N  N   . LYS B 1 370 ? -4.802  -6.774  69.299  1.00 122.79 ?  369  LYS B N   1 
ATOM   6254 C  CA  . LYS B 1 370 ? -5.083  -8.106  68.765  1.00 155.49 ?  369  LYS B CA  1 
ATOM   6255 C  C   . LYS B 1 370 ? -5.475  -8.064  67.288  1.00 172.01 ?  369  LYS B C   1 
ATOM   6256 O  O   . LYS B 1 370 ? -4.959  -8.837  66.478  1.00 189.03 ?  369  LYS B O   1 
ATOM   6257 C  CB  . LYS B 1 370 ? -6.189  -8.797  69.573  1.00 168.07 ?  369  LYS B CB  1 
ATOM   6258 C  CG  . LYS B 1 370 ? -5.745  -9.333  70.930  1.00 162.64 ?  369  LYS B CG  1 
ATOM   6259 C  CD  . LYS B 1 370 ? -6.855  -10.149 71.597  1.00 152.16 ?  369  LYS B CD  1 
ATOM   6260 C  CE  . LYS B 1 370 ? -7.181  -9.636  72.995  1.00 140.20 ?  369  LYS B CE  1 
ATOM   6261 N  NZ  . LYS B 1 370 ? -8.642  -9.422  73.203  1.00 139.08 ?  369  LYS B NZ  1 
ATOM   6262 N  N   . GLU B 1 371 ? -6.395  -7.167  66.945  1.00 160.04 ?  370  GLU B N   1 
ATOM   6263 C  CA  . GLU B 1 371 ? -6.892  -7.063  65.576  1.00 137.45 ?  370  GLU B CA  1 
ATOM   6264 C  C   . GLU B 1 371 ? -5.831  -6.557  64.595  1.00 121.06 ?  370  GLU B C   1 
ATOM   6265 O  O   . GLU B 1 371 ? -5.686  -7.099  63.500  1.00 122.37 ?  370  GLU B O   1 
ATOM   6266 C  CB  . GLU B 1 371 ? -8.118  -6.148  65.528  1.00 123.96 ?  370  GLU B CB  1 
ATOM   6267 C  CG  . GLU B 1 371 ? -8.681  -5.957  64.136  1.00 123.56 ?  370  GLU B CG  1 
ATOM   6268 C  CD  . GLU B 1 371 ? -9.088  -7.269  63.489  1.00 129.54 ?  370  GLU B CD  1 
ATOM   6269 O  OE1 . GLU B 1 371 ? -9.865  -8.028  64.108  1.00 127.21 ?  370  GLU B OE1 1 
ATOM   6270 O  OE2 . GLU B 1 371 ? -8.628  -7.541  62.359  1.00 130.32 ?  370  GLU B OE2 1 
ATOM   6271 N  N   . LEU B 1 372 ? -5.081  -5.535  65.000  1.00 105.28 ?  371  LEU B N   1 
ATOM   6272 C  CA  . LEU B 1 372 ? -4.096  -4.902  64.126  1.00 106.04 ?  371  LEU B CA  1 
ATOM   6273 C  C   . LEU B 1 372 ? -2.985  -5.889  63.770  1.00 125.45 ?  371  LEU B C   1 
ATOM   6274 O  O   . LEU B 1 372 ? -2.532  -5.940  62.627  1.00 136.11 ?  371  LEU B O   1 
ATOM   6275 C  CB  . LEU B 1 372 ? -3.514  -3.656  64.790  1.00 103.73 ?  371  LEU B CB  1 
ATOM   6276 C  CG  . LEU B 1 372 ? -2.646  -2.709  63.957  1.00 122.21 ?  371  LEU B CG  1 
ATOM   6277 C  CD1 . LEU B 1 372 ? -2.795  -1.296  64.507  1.00 129.36 ?  371  LEU B CD1 1 
ATOM   6278 C  CD2 . LEU B 1 372 ? -1.173  -3.116  63.888  1.00 130.19 ?  371  LEU B CD2 1 
ATOM   6279 N  N   . TYR B 1 373 ? -2.525  -6.641  64.765  1.00 124.28 ?  372  TYR B N   1 
ATOM   6280 C  CA  . TYR B 1 373 ? -1.513  -7.668  64.546  1.00 143.06 ?  372  TYR B CA  1 
ATOM   6281 C  C   . TYR B 1 373 ? -1.948  -8.714  63.529  1.00 168.25 ?  372  TYR B C   1 
ATOM   6282 O  O   . TYR B 1 373 ? -1.222  -9.020  62.583  1.00 173.74 ?  372  TYR B O   1 
ATOM   6283 C  CB  . TYR B 1 373 ? -1.171  -8.364  65.869  1.00 154.97 ?  372  TYR B CB  1 
ATOM   6284 C  CG  . TYR B 1 373 ? -0.242  -9.551  65.711  1.00 168.06 ?  372  TYR B CG  1 
ATOM   6285 C  CD1 . TYR B 1 373 ? 1.130   -9.387  65.595  1.00 172.29 ?  372  TYR B CD1 1 
ATOM   6286 C  CD2 . TYR B 1 373 ? -0.752  -10.845 65.672  1.00 171.83 ?  372  TYR B CD2 1 
ATOM   6287 C  CE1 . TYR B 1 373 ? 1.969   -10.478 65.445  1.00 180.44 ?  372  TYR B CE1 1 
ATOM   6288 C  CE2 . TYR B 1 373 ? 0.075   -11.937 65.522  1.00 178.50 ?  372  TYR B CE2 1 
ATOM   6289 C  CZ  . TYR B 1 373 ? 1.435   -11.751 65.410  1.00 184.46 ?  372  TYR B CZ  1 
ATOM   6290 O  OH  . TYR B 1 373 ? 2.261   -12.842 65.261  1.00 191.34 ?  372  TYR B OH  1 
ATOM   6291 N  N   . ARG B 1 374 ? -3.146  -9.249  63.732  1.00 182.86 ?  373  ARG B N   1 
ATOM   6292 C  CA  . ARG B 1 374 ? -3.680  -10.292 62.870  1.00 202.26 ?  373  ARG B CA  1 
ATOM   6293 C  C   . ARG B 1 374 ? -4.074  -9.754  61.503  1.00 216.29 ?  373  ARG B C   1 
ATOM   6294 O  O   . ARG B 1 374 ? -3.939  -10.451 60.498  1.00 217.02 ?  373  ARG B O   1 
ATOM   6295 C  CB  . ARG B 1 374 ? -4.882  -10.966 63.532  1.00 198.08 ?  373  ARG B CB  1 
ATOM   6296 C  CG  . ARG B 1 374 ? -5.352  -12.232 62.838  1.00 205.37 ?  373  ARG B CG  1 
ATOM   6297 C  CD  . ARG B 1 374 ? -6.639  -12.716 63.468  1.00 205.02 ?  373  ARG B CD  1 
ATOM   6298 N  NE  . ARG B 1 374 ? -7.620  -11.639 63.553  1.00 202.76 ?  373  ARG B NE  1 
ATOM   6299 C  CZ  . ARG B 1 374 ? -8.600  -11.590 64.449  1.00 205.09 ?  373  ARG B CZ  1 
ATOM   6300 N  NH1 . ARG B 1 374 ? -8.729  -12.557 65.347  1.00 206.80 ?  373  ARG B NH1 1 
ATOM   6301 N  NH2 . ARG B 1 374 ? -9.446  -10.568 64.453  1.00 203.97 ?  373  ARG B NH2 1 
ATOM   6302 N  N   . GLU B 1 375 ? -4.558  -8.516  61.468  1.00 204.92 ?  374  GLU B N   1 
ATOM   6303 C  CA  . GLU B 1 375 ? -4.942  -7.895  60.206  1.00 187.38 ?  374  GLU B CA  1 
ATOM   6304 C  C   . GLU B 1 375 ? -3.701  -7.700  59.344  1.00 191.11 ?  374  GLU B C   1 
ATOM   6305 O  O   . GLU B 1 375 ? -3.705  -8.033  58.157  1.00 212.39 ?  374  GLU B O   1 
ATOM   6306 C  CB  . GLU B 1 375 ? -5.665  -6.563  60.446  1.00 175.48 ?  374  GLU B CB  1 
ATOM   6307 C  CG  . GLU B 1 375 ? -6.039  -5.798  59.186  1.00 175.76 ?  374  GLU B CG  1 
ATOM   6308 C  CD  . GLU B 1 375 ? -4.907  -4.927  58.678  1.00 179.45 ?  374  GLU B CD  1 
ATOM   6309 O  OE1 . GLU B 1 375 ? -3.998  -4.618  59.478  1.00 176.36 ?  374  GLU B OE1 1 
ATOM   6310 O  OE2 . GLU B 1 375 ? -4.924  -4.558  57.483  1.00 184.58 ?  374  GLU B OE2 1 
ATOM   6311 N  N   . SER B 1 376 ? -2.642  -7.154  59.936  1.00 174.75 ?  375  SER B N   1 
ATOM   6312 C  CA  . SER B 1 376 ? -1.371  -7.070  59.234  1.00 157.70 ?  375  SER B CA  1 
ATOM   6313 C  C   . SER B 1 376 ? -0.808  -8.472  59.024  1.00 164.73 ?  375  SER B C   1 
ATOM   6314 O  O   . SER B 1 376 ? -0.205  -8.761  57.989  1.00 162.26 ?  375  SER B O   1 
ATOM   6315 C  CB  . SER B 1 376 ? -0.379  -6.209  60.016  1.00 135.68 ?  375  SER B CB  1 
ATOM   6316 O  OG  . SER B 1 376 ? -0.001  -6.843  61.226  1.00 127.64 ?  375  SER B OG  1 
ATOM   6317 N  N   . GLY B 1 377 ? -0.994  -9.332  60.021  1.00 172.19 ?  376  GLY B N   1 
ATOM   6318 C  CA  . GLY B 1 377 ? -0.484  -10.685 59.952  1.00 179.28 ?  376  GLY B CA  1 
ATOM   6319 C  C   . GLY B 1 377 ? 0.995   -10.692 60.259  1.00 187.46 ?  376  GLY B C   1 
ATOM   6320 O  O   . GLY B 1 377 ? 1.570   -9.656  60.597  1.00 177.85 ?  376  GLY B O   1 
ATOM   6321 N  N   . ASN B 1 378 ? 1.605   -11.864 60.122  1.00 210.87 ?  377  ASN B N   1 
ATOM   6322 C  CA  . ASN B 1 378 ? 3.036   -12.042 60.330  1.00 229.86 ?  377  ASN B CA  1 
ATOM   6323 C  C   . ASN B 1 378 ? 3.597   -11.428 61.610  1.00 233.30 ?  377  ASN B C   1 
ATOM   6324 O  O   . ASN B 1 378 ? 3.100   -11.663 62.712  1.00 225.03 ?  377  ASN B O   1 
ATOM   6325 C  CB  . ASN B 1 378 ? 3.791   -11.457 59.131  1.00 241.31 ?  377  ASN B CB  1 
ATOM   6326 C  CG  . ASN B 1 378 ? 3.500   -12.200 57.841  1.00 253.30 ?  377  ASN B CG  1 
ATOM   6327 O  OD1 . ASN B 1 378 ? 3.272   -13.409 57.845  1.00 259.35 ?  377  ASN B OD1 1 
ATOM   6328 N  ND2 . ASN B 1 378 ? 3.494   -11.474 56.727  1.00 255.94 ?  377  ASN B ND2 1 
ATOM   6329 N  N   . ASN B 1 379 ? 4.647   -10.632 61.427  1.00 235.48 ?  378  ASN B N   1 
ATOM   6330 C  CA  . ASN B 1 379 ? 5.450   -10.079 62.514  1.00 226.78 ?  378  ASN B CA  1 
ATOM   6331 C  C   . ASN B 1 379 ? 5.230   -8.586  62.783  1.00 216.16 ?  378  ASN B C   1 
ATOM   6332 O  O   . ASN B 1 379 ? 6.199   -7.827  62.856  1.00 218.29 ?  378  ASN B O   1 
ATOM   6333 C  CB  . ASN B 1 379 ? 6.934   -10.314 62.205  1.00 217.62 ?  378  ASN B CB  1 
ATOM   6334 C  CG  . ASN B 1 379 ? 7.811   -10.275 63.444  1.00 204.27 ?  378  ASN B CG  1 
ATOM   6335 O  OD1 . ASN B 1 379 ? 7.380   -9.851  64.517  1.00 196.10 ?  378  ASN B OD1 1 
ATOM   6336 N  ND2 . ASN B 1 379 ? 9.056   -10.718 63.297  1.00 203.96 ?  378  ASN B ND2 1 
ATOM   6337 N  N   . LYS B 1 380 ? 3.980   -8.146  62.912  1.00 200.28 ?  379  LYS B N   1 
ATOM   6338 C  CA  . LYS B 1 380 ? 3.739   -6.709  63.041  1.00 179.66 ?  379  LYS B CA  1 
ATOM   6339 C  C   . LYS B 1 380 ? 2.882   -6.318  64.249  1.00 162.46 ?  379  LYS B C   1 
ATOM   6340 O  O   . LYS B 1 380 ? 1.711   -6.681  64.334  1.00 153.34 ?  379  LYS B O   1 
ATOM   6341 C  CB  . LYS B 1 380 ? 3.075   -6.195  61.763  1.00 184.96 ?  379  LYS B CB  1 
ATOM   6342 C  CG  . LYS B 1 380 ? 3.949   -6.287  60.519  1.00 189.48 ?  379  LYS B CG  1 
ATOM   6343 C  CD  . LYS B 1 380 ? 3.119   -6.120  59.257  1.00 184.19 ?  379  LYS B CD  1 
ATOM   6344 C  CE  . LYS B 1 380 ? 3.989   -6.017  58.020  1.00 180.72 ?  379  LYS B CE  1 
ATOM   6345 N  NZ  . LYS B 1 380 ? 3.208   -5.506  56.863  1.00 178.06 ?  379  LYS B NZ  1 
ATOM   6346 N  N   . TRP B 1 381 ? 3.465   -5.534  65.153  1.00 163.31 ?  380  TRP B N   1 
ATOM   6347 C  CA  . TRP B 1 381 ? 2.766   -5.041  66.341  1.00 159.39 ?  380  TRP B CA  1 
ATOM   6348 C  C   . TRP B 1 381 ? 2.783   -3.508  66.360  1.00 145.52 ?  380  TRP B C   1 
ATOM   6349 O  O   . TRP B 1 381 ? 3.756   -2.891  65.922  1.00 139.25 ?  380  TRP B O   1 
ATOM   6350 C  CB  . TRP B 1 381 ? 3.394   -5.602  67.625  1.00 156.56 ?  380  TRP B CB  1 
ATOM   6351 C  CG  . TRP B 1 381 ? 2.960   -7.011  68.002  1.00 150.85 ?  380  TRP B CG  1 
ATOM   6352 C  CD1 . TRP B 1 381 ? 3.680   -8.163  67.846  1.00 155.25 ?  380  TRP B CD1 1 
ATOM   6353 C  CD2 . TRP B 1 381 ? 1.724   -7.397  68.618  1.00 140.95 ?  380  TRP B CD2 1 
ATOM   6354 N  NE1 . TRP B 1 381 ? 2.965   -9.240  68.317  1.00 147.78 ?  380  TRP B NE1 1 
ATOM   6355 C  CE2 . TRP B 1 381 ? 1.758   -8.795  68.798  1.00 137.03 ?  380  TRP B CE2 1 
ATOM   6356 C  CE3 . TRP B 1 381 ? 0.585   -6.696  69.029  1.00 125.20 ?  380  TRP B CE3 1 
ATOM   6357 C  CZ2 . TRP B 1 381 ? 0.703   -9.505  69.371  1.00 124.49 ?  380  TRP B CZ2 1 
ATOM   6358 C  CZ3 . TRP B 1 381 ? -0.463  -7.401  69.601  1.00 110.66 ?  380  TRP B CZ3 1 
ATOM   6359 C  CH2 . TRP B 1 381 ? -0.397  -8.790  69.765  1.00 110.99 ?  380  TRP B CH2 1 
ATOM   6360 N  N   . PRO B 1 382 ? 1.704   -2.887  66.860  1.00 142.02 ?  381  PRO B N   1 
ATOM   6361 C  CA  . PRO B 1 382 ? 1.582   -1.425  66.897  1.00 145.37 ?  381  PRO B CA  1 
ATOM   6362 C  C   . PRO B 1 382 ? 2.127   -0.809  68.191  1.00 150.20 ?  381  PRO B C   1 
ATOM   6363 O  O   . PRO B 1 382 ? 1.775   -1.272  69.278  1.00 173.39 ?  381  PRO B O   1 
ATOM   6364 C  CB  . PRO B 1 382 ? 0.075   -1.208  66.773  1.00 145.76 ?  381  PRO B CB  1 
ATOM   6365 C  CG  . PRO B 1 382 ? -0.529  -2.420  67.411  1.00 146.84 ?  381  PRO B CG  1 
ATOM   6366 C  CD  . PRO B 1 382 ? 0.466   -3.554  67.299  1.00 146.36 ?  381  PRO B CD  1 
ATOM   6367 N  N   . LEU B 1 383 ? 2.967   0.219   68.081  1.00 133.45 ?  382  LEU B N   1 
ATOM   6368 C  CA  . LEU B 1 383 ? 3.523   0.872   69.268  1.00 126.22 ?  382  LEU B CA  1 
ATOM   6369 C  C   . LEU B 1 383 ? 2.449   1.668   70.008  1.00 127.57 ?  382  LEU B C   1 
ATOM   6370 O  O   . LEU B 1 383 ? 1.571   2.266   69.390  1.00 132.25 ?  382  LEU B O   1 
ATOM   6371 C  CB  . LEU B 1 383 ? 4.703   1.777   68.891  1.00 114.07 ?  382  LEU B CB  1 
ATOM   6372 C  CG  . LEU B 1 383 ? 5.383   2.590   69.999  1.00 113.54 ?  382  LEU B CG  1 
ATOM   6373 C  CD1 . LEU B 1 383 ? 6.864   2.700   69.721  1.00 114.91 ?  382  LEU B CD1 1 
ATOM   6374 C  CD2 . LEU B 1 383 ? 4.790   3.983   70.136  1.00 111.69 ?  382  LEU B CD2 1 
ATOM   6375 N  N   . ILE B 1 384 ? 2.525   1.677   71.335  1.00 132.11 ?  383  ILE B N   1 
ATOM   6376 C  CA  . ILE B 1 384 ? 1.554   2.406   72.136  1.00 130.39 ?  383  ILE B CA  1 
ATOM   6377 C  C   . ILE B 1 384 ? 2.219   3.477   72.978  1.00 135.14 ?  383  ILE B C   1 
ATOM   6378 O  O   . ILE B 1 384 ? 3.195   3.214   73.685  1.00 144.21 ?  383  ILE B O   1 
ATOM   6379 C  CB  . ILE B 1 384 ? 0.784   1.487   73.085  1.00 131.05 ?  383  ILE B CB  1 
ATOM   6380 C  CG1 . ILE B 1 384 ? 0.422   0.166   72.411  1.00 131.46 ?  383  ILE B CG1 1 
ATOM   6381 C  CG2 . ILE B 1 384 ? -0.442  2.206   73.640  1.00 128.05 ?  383  ILE B CG2 1 
ATOM   6382 C  CD1 . ILE B 1 384 ? 0.110   -0.918  73.408  1.00 125.95 ?  383  ILE B CD1 1 
ATOM   6383 N  N   . LEU B 1 385 ? 1.675   4.684   72.909  1.00 123.84 ?  384  LEU B N   1 
ATOM   6384 C  CA  . LEU B 1 385 ? 2.178   5.780   73.716  1.00 120.94 ?  384  LEU B CA  1 
ATOM   6385 C  C   . LEU B 1 385 ? 1.201   6.127   74.830  1.00 118.56 ?  384  LEU B C   1 
ATOM   6386 O  O   . LEU B 1 385 ? 0.058   6.525   74.579  1.00 92.39  ?  384  LEU B O   1 
ATOM   6387 C  CB  . LEU B 1 385 ? 2.465   6.997   72.839  1.00 115.66 ?  384  LEU B CB  1 
ATOM   6388 C  CG  . LEU B 1 385 ? 3.767   6.812   72.060  1.00 119.65 ?  384  LEU B CG  1 
ATOM   6389 C  CD1 . LEU B 1 385 ? 3.718   7.543   70.738  1.00 122.70 ?  384  LEU B CD1 1 
ATOM   6390 C  CD2 . LEU B 1 385 ? 4.964   7.262   72.888  1.00 127.54 ?  384  LEU B CD2 1 
ATOM   6391 N  N   . LEU B 1 386 ? 1.670   5.949   76.061  1.00 114.02 ?  385  LEU B N   1 
ATOM   6392 C  CA  . LEU B 1 386 ? 0.877   6.202   77.253  1.00 109.53 ?  385  LEU B CA  1 
ATOM   6393 C  C   . LEU B 1 386 ? 1.696   6.937   78.297  1.00 120.89 ?  385  LEU B C   1 
ATOM   6394 O  O   . LEU B 1 386 ? 2.921   6.819   78.329  1.00 120.84 ?  385  LEU B O   1 
ATOM   6395 C  CB  . LEU B 1 386 ? 0.336   4.895   77.826  1.00 122.35 ?  385  LEU B CB  1 
ATOM   6396 C  CG  . LEU B 1 386 ? -1.159  4.684   77.602  1.00 113.32 ?  385  LEU B CG  1 
ATOM   6397 C  CD1 . LEU B 1 386 ? -1.575  3.290   78.029  1.00 99.11  ?  385  LEU B CD1 1 
ATOM   6398 C  CD2 . LEU B 1 386 ? -1.942  5.738   78.373  1.00 90.01  ?  385  LEU B CD2 1 
ATOM   6399 N  N   . HIS B 1 387 ? 1.015   7.701   79.143  1.00 154.84 ?  386  HIS B N   1 
ATOM   6400 C  CA  . HIS B 1 387 ? 1.681   8.485   80.173  1.00 168.78 ?  386  HIS B CA  1 
ATOM   6401 C  C   . HIS B 1 387 ? 2.372   7.628   81.222  1.00 165.49 ?  386  HIS B C   1 
ATOM   6402 O  O   . HIS B 1 387 ? 1.981   6.489   81.466  1.00 180.39 ?  386  HIS B O   1 
ATOM   6403 C  CB  . HIS B 1 387 ? 0.674   9.395   80.868  1.00 183.13 ?  386  HIS B CB  1 
ATOM   6404 C  CG  . HIS B 1 387 ? 0.650   10.789  80.329  1.00 199.44 ?  386  HIS B CG  1 
ATOM   6405 N  ND1 . HIS B 1 387 ? 1.185   11.855  81.016  1.00 207.14 ?  386  HIS B ND1 1 
ATOM   6406 C  CD2 . HIS B 1 387 ? 0.153   11.287  79.174  1.00 210.89 ?  386  HIS B CD2 1 
ATOM   6407 C  CE1 . HIS B 1 387 ? 1.019   12.959  80.302  1.00 218.25 ?  386  HIS B CE1 1 
ATOM   6408 N  NE2 . HIS B 1 387 ? 0.398   12.641  79.185  1.00 219.33 ?  386  HIS B NE2 1 
ATOM   6409 N  N   . LYS B 1 388 ? 3.398   8.193   81.847  1.00 132.93 ?  387  LYS B N   1 
ATOM   6410 C  CA  . LYS B 1 388 ? 4.040   7.553   82.981  1.00 119.76 ?  387  LYS B CA  1 
ATOM   6411 C  C   . LYS B 1 388 ? 2.980   7.403   84.059  1.00 128.31 ?  387  LYS B C   1 
ATOM   6412 O  O   . LYS B 1 388 ? 2.933   6.404   84.777  1.00 154.61 ?  387  LYS B O   1 
ATOM   6413 C  CB  . LYS B 1 388 ? 5.223   8.382   83.487  1.00 119.61 ?  387  LYS B CB  1 
ATOM   6414 C  CG  . LYS B 1 388 ? 6.364   7.576   84.086  1.00 117.48 ?  387  LYS B CG  1 
ATOM   6415 C  CD  . LYS B 1 388 ? 7.459   7.359   83.054  1.00 111.84 ?  387  LYS B CD  1 
ATOM   6416 C  CE  . LYS B 1 388 ? 8.682   6.699   83.665  1.00 111.87 ?  387  LYS B CE  1 
ATOM   6417 N  NZ  . LYS B 1 388 ? 9.777   6.577   82.664  1.00 104.37 ?  387  LYS B NZ  1 
ATOM   6418 N  N   . ARG B 1 389 ? 2.131   8.423   84.146  1.00 123.01 ?  388  ARG B N   1 
ATOM   6419 C  CA  . ARG B 1 389 ? 0.987   8.454   85.049  1.00 134.41 ?  388  ARG B CA  1 
ATOM   6420 C  C   . ARG B 1 389 ? 0.044   7.261   84.918  1.00 126.18 ?  388  ARG B C   1 
ATOM   6421 O  O   . ARG B 1 389 ? -0.234  6.562   85.893  1.00 134.72 ?  388  ARG B O   1 
ATOM   6422 C  CB  . ARG B 1 389 ? 0.192   9.741   84.810  1.00 153.68 ?  388  ARG B CB  1 
ATOM   6423 C  CG  . ARG B 1 389 ? 1.032   11.008  84.812  1.00 174.59 ?  388  ARG B CG  1 
ATOM   6424 C  CD  . ARG B 1 389 ? 1.143   11.578  86.215  1.00 180.62 ?  388  ARG B CD  1 
ATOM   6425 N  NE  . ARG B 1 389 ? -0.169  11.933  86.745  1.00 181.22 ?  388  ARG B NE  1 
ATOM   6426 C  CZ  . ARG B 1 389 ? -0.411  12.206  88.022  1.00 181.37 ?  388  ARG B CZ  1 
ATOM   6427 N  NH1 . ARG B 1 389 ? 0.572   12.159  88.909  1.00 176.03 ?  388  ARG B NH1 1 
ATOM   6428 N  NH2 . ARG B 1 389 ? -1.637  12.522  88.412  1.00 185.17 ?  388  ARG B NH2 1 
ATOM   6429 N  N   . ARG B 1 390 ? -0.462  7.047   83.710  1.00 114.18 ?  389  ARG B N   1 
ATOM   6430 C  CA  . ARG B 1 390 ? -1.392  5.950   83.457  1.00 112.77 ?  389  ARG B CA  1 
ATOM   6431 C  C   . ARG B 1 390 ? -0.784  4.551   83.486  1.00 111.13 ?  389  ARG B C   1 
ATOM   6432 O  O   . ARG B 1 390 ? -1.431  3.621   83.960  1.00 116.07 ?  389  ARG B O   1 
ATOM   6433 C  CB  . ARG B 1 390 ? -2.117  6.179   82.132  1.00 109.01 ?  389  ARG B CB  1 
ATOM   6434 C  CG  . ARG B 1 390 ? -3.153  7.272   82.263  1.00 108.87 ?  389  ARG B CG  1 
ATOM   6435 C  CD  . ARG B 1 390 ? -4.274  6.798   83.166  1.00 113.39 ?  389  ARG B CD  1 
ATOM   6436 N  NE  . ARG B 1 390 ? -5.319  7.802   83.337  1.00 119.99 ?  389  ARG B NE  1 
ATOM   6437 C  CZ  . ARG B 1 390 ? -6.333  7.977   82.500  1.00 117.67 ?  389  ARG B CZ  1 
ATOM   6438 N  NH1 . ARG B 1 390 ? -6.434  7.220   81.421  1.00 128.71 ?  389  ARG B NH1 1 
ATOM   6439 N  NH2 . ARG B 1 390 ? -7.244  8.910   82.737  1.00 106.72 ?  389  ARG B NH2 1 
ATOM   6440 N  N   . VAL B 1 391 ? 0.428   4.386   82.963  1.00 108.30 ?  390  VAL B N   1 
ATOM   6441 C  CA  . VAL B 1 391 ? 1.047   3.062   82.963  1.00 117.91 ?  390  VAL B CA  1 
ATOM   6442 C  C   . VAL B 1 391 ? 1.351   2.597   84.387  1.00 132.65 ?  390  VAL B C   1 
ATOM   6443 O  O   . VAL B 1 391 ? 1.169   1.421   84.707  1.00 148.87 ?  390  VAL B O   1 
ATOM   6444 C  CB  . VAL B 1 391 ? 2.345   3.002   82.116  1.00 104.63 ?  390  VAL B CB  1 
ATOM   6445 C  CG1 . VAL B 1 391 ? 2.047   3.329   80.664  1.00 102.85 ?  390  VAL B CG1 1 
ATOM   6446 C  CG2 . VAL B 1 391 ? 3.428   3.922   82.672  1.00 120.72 ?  390  VAL B CG2 1 
ATOM   6447 N  N   . LYS B 1 392 ? 1.797   3.513   85.243  1.00 118.14 ?  391  LYS B N   1 
ATOM   6448 C  CA  . LYS B 1 392 ? 2.128   3.148   86.607  1.00 101.95 ?  391  LYS B CA  1 
ATOM   6449 C  C   . LYS B 1 392 ? 0.876   2.677   87.324  1.00 108.65 ?  391  LYS B C   1 
ATOM   6450 O  O   . LYS B 1 392 ? 0.905   1.657   88.009  1.00 132.14 ?  391  LYS B O   1 
ATOM   6451 C  CB  . LYS B 1 392 ? 2.764   4.314   87.359  1.00 97.44  ?  391  LYS B CB  1 
ATOM   6452 C  CG  . LYS B 1 392 ? 4.251   4.482   87.097  1.00 98.75  ?  391  LYS B CG  1 
ATOM   6453 C  CD  . LYS B 1 392 ? 4.906   5.422   88.113  1.00 116.42 ?  391  LYS B CD  1 
ATOM   6454 C  CE  . LYS B 1 392 ? 4.489   6.883   87.934  1.00 113.19 ?  391  LYS B CE  1 
ATOM   6455 N  NZ  . LYS B 1 392 ? 3.137   7.200   88.491  1.00 99.46  ?  391  LYS B NZ  1 
ATOM   6456 N  N   . THR B 1 393 ? -0.228  3.395   87.141  1.00 94.94  ?  392  THR B N   1 
ATOM   6457 C  CA  . THR B 1 393 ? -1.492  2.994   87.755  1.00 94.91  ?  392  THR B CA  1 
ATOM   6458 C  C   . THR B 1 393 ? -1.921  1.618   87.249  1.00 102.77 ?  392  THR B C   1 
ATOM   6459 O  O   . THR B 1 393 ? -2.447  0.806   88.009  1.00 114.74 ?  392  THR B O   1 
ATOM   6460 C  CB  . THR B 1 393 ? -2.608  4.015   87.485  1.00 100.11 ?  392  THR B CB  1 
ATOM   6461 O  OG1 . THR B 1 393 ? -2.258  5.272   88.079  1.00 105.26 ?  392  THR B OG1 1 
ATOM   6462 C  CG2 . THR B 1 393 ? -3.924  3.539   88.074  1.00 94.32  ?  392  THR B CG2 1 
ATOM   6463 N  N   . LEU B 1 394 ? -1.694  1.359   85.965  1.00 109.00 ?  393  LEU B N   1 
ATOM   6464 C  CA  . LEU B 1 394 ? -1.930  0.031   85.402  1.00 110.39 ?  393  LEU B CA  1 
ATOM   6465 C  C   . LEU B 1 394 ? -0.928  -0.986  85.936  1.00 112.63 ?  393  LEU B C   1 
ATOM   6466 O  O   . LEU B 1 394 ? -1.273  -2.145  86.164  1.00 124.60 ?  393  LEU B O   1 
ATOM   6467 C  CB  . LEU B 1 394 ? -1.879  0.072   83.883  1.00 110.40 ?  393  LEU B CB  1 
ATOM   6468 C  CG  . LEU B 1 394 ? -3.254  0.002   83.222  1.00 114.42 ?  393  LEU B CG  1 
ATOM   6469 C  CD1 . LEU B 1 394 ? -4.215  1.024   83.826  1.00 112.23 ?  393  LEU B CD1 1 
ATOM   6470 C  CD2 . LEU B 1 394 ? -3.107  0.211   81.733  1.00 114.21 ?  393  LEU B CD2 1 
ATOM   6471 N  N   . LEU B 1 395 ? 0.319   -0.553  86.095  1.00 98.19  ?  394  LEU B N   1 
ATOM   6472 C  CA  . LEU B 1 395 ? 1.350   -1.374  86.714  1.00 98.21  ?  394  LEU B CA  1 
ATOM   6473 C  C   . LEU B 1 395 ? 0.994   -1.703  88.162  1.00 113.31 ?  394  LEU B C   1 
ATOM   6474 O  O   . LEU B 1 395 ? 1.306   -2.776  88.667  1.00 106.18 ?  394  LEU B O   1 
ATOM   6475 C  CB  . LEU B 1 395 ? 2.702   -0.668  86.652  1.00 98.78  ?  394  LEU B CB  1 
ATOM   6476 C  CG  . LEU B 1 395 ? 3.462   -0.775  85.331  1.00 98.60  ?  394  LEU B CG  1 
ATOM   6477 C  CD1 . LEU B 1 395 ? 4.891   -0.277  85.487  1.00 99.98  ?  394  LEU B CD1 1 
ATOM   6478 C  CD2 . LEU B 1 395 ? 3.441   -2.214  84.828  1.00 99.54  ?  394  LEU B CD2 1 
ATOM   6479 N  N   . GLU B 1 396 ? 0.365   -0.749  88.835  1.00 118.68 ?  395  GLU B N   1 
ATOM   6480 C  CA  . GLU B 1 396 ? -0.028  -0.910  90.229  1.00 112.46 ?  395  GLU B CA  1 
ATOM   6481 C  C   . GLU B 1 396 ? -1.130  -1.959  90.374  1.00 112.95 ?  395  GLU B C   1 
ATOM   6482 O  O   . GLU B 1 396 ? -1.208  -2.643  91.392  1.00 114.24 ?  395  GLU B O   1 
ATOM   6483 C  CB  . GLU B 1 396 ? -0.464  0.434   90.797  1.00 107.98 ?  395  GLU B CB  1 
ATOM   6484 C  CG  . GLU B 1 396 ? 0.716   1.247   91.302  1.00 109.46 ?  395  GLU B CG  1 
ATOM   6485 C  CD  . GLU B 1 396 ? 0.331   2.644   91.715  1.00 126.77 ?  395  GLU B CD  1 
ATOM   6486 O  OE1 . GLU B 1 396 ? -0.833  2.853   92.119  1.00 167.38 ?  395  GLU B OE1 1 
ATOM   6487 O  OE2 . GLU B 1 396 ? 1.195   3.538   91.612  1.00 101.16 ?  395  GLU B OE2 1 
ATOM   6488 N  N   . ASN B 1 397 ? -1.998  -2.056  89.369  1.00 112.48 ?  396  ASN B N   1 
ATOM   6489 C  CA  . ASN B 1 397 ? -3.034  -3.089  89.339  1.00 113.64 ?  396  ASN B CA  1 
ATOM   6490 C  C   . ASN B 1 397 ? -2.426  -4.467  89.081  1.00 126.62 ?  396  ASN B C   1 
ATOM   6491 O  O   . ASN B 1 397 ? -1.720  -4.660  88.092  1.00 126.59 ?  396  ASN B O   1 
ATOM   6492 C  CB  . ASN B 1 397 ? -4.085  -2.768  88.278  1.00 103.46 ?  396  ASN B CB  1 
ATOM   6493 C  CG  . ASN B 1 397 ? -5.345  -3.609  88.424  1.00 106.52 ?  396  ASN B CG  1 
ATOM   6494 O  OD1 . ASN B 1 397 ? -5.295  -4.840  88.419  1.00 104.05 ?  396  ASN B OD1 1 
ATOM   6495 N  ND2 . ASN B 1 397 ? -6.485  -2.942  88.545  1.00 119.53 ?  396  ASN B ND2 1 
ATOM   6496 N  N   . PRO B 1 398 ? -2.723  -5.435  89.961  1.00 127.58 ?  397  PRO B N   1 
ATOM   6497 C  CA  . PRO B 1 398 ? -2.142  -6.785  89.930  1.00 125.55 ?  397  PRO B CA  1 
ATOM   6498 C  C   . PRO B 1 398 ? -2.543  -7.603  88.705  1.00 124.22 ?  397  PRO B C   1 
ATOM   6499 O  O   . PRO B 1 398 ? -1.725  -8.363  88.181  1.00 131.55 ?  397  PRO B O   1 
ATOM   6500 C  CB  . PRO B 1 398 ? -2.698  -7.436  91.203  1.00 136.84 ?  397  PRO B CB  1 
ATOM   6501 C  CG  . PRO B 1 398 ? -3.138  -6.297  92.070  1.00 141.97 ?  397  PRO B CG  1 
ATOM   6502 C  CD  . PRO B 1 398 ? -3.599  -5.239  91.128  1.00 131.35 ?  397  PRO B CD  1 
ATOM   6503 N  N   . THR B 1 399 ? -3.790  -7.454  88.270  1.00 123.77 ?  398  THR B N   1 
ATOM   6504 C  CA  . THR B 1 399 ? -4.314  -8.181  87.118  1.00 128.68 ?  398  THR B CA  1 
ATOM   6505 C  C   . THR B 1 399 ? -3.509  -7.926  85.843  1.00 137.11 ?  398  THR B C   1 
ATOM   6506 O  O   . THR B 1 399 ? -3.024  -8.855  85.191  1.00 105.17 ?  398  THR B O   1 
ATOM   6507 C  CB  . THR B 1 399 ? -5.784  -7.792  86.847  1.00 128.68 ?  398  THR B CB  1 
ATOM   6508 O  OG1 . THR B 1 399 ? -6.548  -7.870  88.058  1.00 105.45 ?  398  THR B OG1 1 
ATOM   6509 C  CG2 . THR B 1 399 ? -6.392  -8.686  85.769  1.00 129.27 ?  398  THR B CG2 1 
ATOM   6510 N  N   . HIS B 1 400 ? -3.379  -6.646  85.508  1.00 131.25 ?  399  HIS B N   1 
ATOM   6511 C  CA  . HIS B 1 400 ? -2.792  -6.198  84.249  1.00 115.40 ?  399  HIS B CA  1 
ATOM   6512 C  C   . HIS B 1 400 ? -1.264  -6.180  84.249  1.00 109.88 ?  399  HIS B C   1 
ATOM   6513 O  O   . HIS B 1 400 ? -0.648  -6.196  83.185  1.00 118.02 ?  399  HIS B O   1 
ATOM   6514 C  CB  . HIS B 1 400 ? -3.321  -4.802  83.912  1.00 97.28  ?  399  HIS B CB  1 
ATOM   6515 C  CG  . HIS B 1 400 ? -4.801  -4.661  84.086  1.00 96.83  ?  399  HIS B CG  1 
ATOM   6516 N  ND1 . HIS B 1 400 ? -5.389  -3.507  84.558  1.00 95.61  ?  399  HIS B ND1 1 
ATOM   6517 C  CD2 . HIS B 1 400 ? -5.813  -5.533  83.858  1.00 99.84  ?  399  HIS B CD2 1 
ATOM   6518 C  CE1 . HIS B 1 400 ? -6.699  -3.673  84.613  1.00 103.27 ?  399  HIS B CE1 1 
ATOM   6519 N  NE2 . HIS B 1 400 ? -6.983  -4.892  84.192  1.00 110.29 ?  399  HIS B NE2 1 
ATOM   6520 N  N   . ARG B 1 401 ? -0.666  -6.140  85.439  1.00 107.30 ?  400  ARG B N   1 
ATOM   6521 C  CA  . ARG B 1 401 ? 0.763   -5.849  85.600  1.00 112.05 ?  400  ARG B CA  1 
ATOM   6522 C  C   . ARG B 1 401 ? 1.664   -6.731  84.733  1.00 115.76 ?  400  ARG B C   1 
ATOM   6523 O  O   . ARG B 1 401 ? 2.645   -6.253  84.157  1.00 119.07 ?  400  ARG B O   1 
ATOM   6524 C  CB  . ARG B 1 401 ? 1.181   -5.988  87.069  1.00 108.65 ?  400  ARG B CB  1 
ATOM   6525 C  CG  . ARG B 1 401 ? 2.633   -5.590  87.332  1.00 106.28 ?  400  ARG B CG  1 
ATOM   6526 C  CD  . ARG B 1 401 ? 2.896   -5.344  88.811  1.00 106.48 ?  400  ARG B CD  1 
ATOM   6527 N  NE  . ARG B 1 401 ? 4.208   -4.756  89.087  1.00 107.33 ?  400  ARG B NE  1 
ATOM   6528 C  CZ  . ARG B 1 401 ? 5.370   -5.379  88.920  1.00 109.46 ?  400  ARG B CZ  1 
ATOM   6529 N  NH1 . ARG B 1 401 ? 5.403   -6.632  88.486  1.00 111.06 ?  400  ARG B NH1 1 
ATOM   6530 N  NH2 . ARG B 1 401 ? 6.503   -4.749  89.199  1.00 110.36 ?  400  ARG B NH2 1 
ATOM   6531 N  N   . ASN B 1 402 ? 1.338   -8.017  84.661  1.00 120.99 ?  401  ASN B N   1 
ATOM   6532 C  CA  . ASN B 1 402 ? 2.116   -8.956  83.866  1.00 125.33 ?  401  ASN B CA  1 
ATOM   6533 C  C   . ASN B 1 402 ? 2.059   -8.610  82.380  1.00 113.09 ?  401  ASN B C   1 
ATOM   6534 O  O   . ASN B 1 402 ? 3.066   -8.669  81.675  1.00 107.26 ?  401  ASN B O   1 
ATOM   6535 C  CB  . ASN B 1 402 ? 1.616   -10.385 84.097  1.00 130.72 ?  401  ASN B CB  1 
ATOM   6536 C  CG  . ASN B 1 402 ? 2.522   -11.430 83.468  1.00 135.88 ?  401  ASN B CG  1 
ATOM   6537 O  OD1 . ASN B 1 402 ? 3.659   -11.140 83.099  1.00 140.29 ?  401  ASN B OD1 1 
ATOM   6538 N  ND2 . ASN B 1 402 ? 2.022   -12.654 83.350  1.00 138.32 ?  401  ASN B ND2 1 
ATOM   6539 N  N   . LEU B 1 403 ? 0.870   -8.236  81.921  1.00 109.97 ?  402  LEU B N   1 
ATOM   6540 C  CA  . LEU B 1 403 ? 0.634   -7.921  80.515  1.00 109.63 ?  402  LEU B CA  1 
ATOM   6541 C  C   . LEU B 1 403 ? 1.311   -6.624  80.075  1.00 103.57 ?  402  LEU B C   1 
ATOM   6542 O  O   . LEU B 1 403 ? 1.943   -6.570  79.019  1.00 101.73 ?  402  LEU B O   1 
ATOM   6543 C  CB  . LEU B 1 403 ? -0.869  -7.835  80.248  1.00 105.41 ?  402  LEU B CB  1 
ATOM   6544 C  CG  . LEU B 1 403 ? -1.302  -7.378  78.857  1.00 111.03 ?  402  LEU B CG  1 
ATOM   6545 C  CD1 . LEU B 1 403 ? -0.676  -8.275  77.797  1.00 118.93 ?  402  LEU B CD1 1 
ATOM   6546 C  CD2 . LEU B 1 403 ? -2.817  -7.388  78.749  1.00 119.64 ?  402  LEU B CD2 1 
ATOM   6547 N  N   . VAL B 1 404 ? 1.161   -5.581  80.886  1.00 101.23 ?  403  VAL B N   1 
ATOM   6548 C  CA  . VAL B 1 404 ? 1.706   -4.268  80.565  1.00 98.30  ?  403  VAL B CA  1 
ATOM   6549 C  C   . VAL B 1 404 ? 3.226   -4.318  80.543  1.00 111.98 ?  403  VAL B C   1 
ATOM   6550 O  O   . VAL B 1 404 ? 3.866   -3.708  79.687  1.00 114.37 ?  403  VAL B O   1 
ATOM   6551 C  CB  . VAL B 1 404 ? 1.242   -3.200  81.570  1.00 100.67 ?  403  VAL B CB  1 
ATOM   6552 C  CG1 . VAL B 1 404 ? 1.824   -1.835  81.208  1.00 95.82  ?  403  VAL B CG1 1 
ATOM   6553 C  CG2 . VAL B 1 404 ? -0.274  -3.139  81.610  1.00 100.75 ?  403  VAL B CG2 1 
ATOM   6554 N  N   . GLU B 1 405 ? 3.800   -5.056  81.486  1.00 123.46 ?  404  GLU B N   1 
ATOM   6555 C  CA  . GLU B 1 405 ? 5.244   -5.218  81.539  1.00 142.01 ?  404  GLU B CA  1 
ATOM   6556 C  C   . GLU B 1 405 ? 5.721   -5.952  80.293  1.00 137.51 ?  404  GLU B C   1 
ATOM   6557 O  O   . GLU B 1 405 ? 6.790   -5.656  79.759  1.00 139.18 ?  404  GLU B O   1 
ATOM   6558 C  CB  . GLU B 1 405 ? 5.667   -5.969  82.805  1.00 171.18 ?  404  GLU B CB  1 
ATOM   6559 C  CG  . GLU B 1 405 ? 7.153   -6.311  82.857  1.00 199.51 ?  404  GLU B CG  1 
ATOM   6560 C  CD  . GLU B 1 405 ? 8.041   -5.128  82.501  1.00 214.12 ?  404  GLU B CD  1 
ATOM   6561 O  OE1 . GLU B 1 405 ? 7.805   -4.019  83.028  1.00 218.03 ?  404  GLU B OE1 1 
ATOM   6562 O  OE2 . GLU B 1 405 ? 8.977   -5.306  81.692  1.00 221.84 ?  404  GLU B OE2 1 
ATOM   6563 N  N   . GLU B 1 406 ? 4.915   -6.899  79.825  1.00 140.88 ?  405  GLU B N   1 
ATOM   6564 C  CA  . GLU B 1 406 ? 5.238   -7.639  78.611  1.00 148.54 ?  405  GLU B CA  1 
ATOM   6565 C  C   . GLU B 1 406 ? 5.356   -6.701  77.409  1.00 138.63 ?  405  GLU B C   1 
ATOM   6566 O  O   . GLU B 1 406 ? 6.245   -6.862  76.575  1.00 145.04 ?  405  GLU B O   1 
ATOM   6567 C  CB  . GLU B 1 406 ? 4.190   -8.723  78.342  1.00 154.40 ?  405  GLU B CB  1 
ATOM   6568 C  CG  . GLU B 1 406 ? 4.535   -9.642  77.175  1.00 157.70 ?  405  GLU B CG  1 
ATOM   6569 C  CD  . GLU B 1 406 ? 3.524   -10.757 76.990  1.00 157.30 ?  405  GLU B CD  1 
ATOM   6570 O  OE1 . GLU B 1 406 ? 2.363   -10.582 77.416  1.00 161.22 ?  405  GLU B OE1 1 
ATOM   6571 O  OE2 . GLU B 1 406 ? 3.890   -11.808 76.420  1.00 154.57 ?  405  GLU B OE2 1 
ATOM   6572 N  N   . TRP B 1 407 ? 4.460   -5.723  77.325  1.00 125.40 ?  406  TRP B N   1 
ATOM   6573 C  CA  . TRP B 1 407 ? 4.506   -4.740  76.247  1.00 115.18 ?  406  TRP B CA  1 
ATOM   6574 C  C   . TRP B 1 407 ? 5.757   -3.870  76.332  1.00 120.21 ?  406  TRP B C   1 
ATOM   6575 O  O   . TRP B 1 407 ? 6.447   -3.664  75.334  1.00 127.28 ?  406  TRP B O   1 
ATOM   6576 C  CB  . TRP B 1 407 ? 3.251   -3.865  76.271  1.00 104.44 ?  406  TRP B CB  1 
ATOM   6577 C  CG  . TRP B 1 407 ? 2.015   -4.626  75.914  1.00 104.80 ?  406  TRP B CG  1 
ATOM   6578 C  CD1 . TRP B 1 407 ? 1.948   -5.919  75.482  1.00 109.86 ?  406  TRP B CD1 1 
ATOM   6579 C  CD2 . TRP B 1 407 ? 0.664   -4.150  75.968  1.00 98.62  ?  406  TRP B CD2 1 
ATOM   6580 N  NE1 . TRP B 1 407 ? 0.640   -6.277  75.260  1.00 112.21 ?  406  TRP B NE1 1 
ATOM   6581 C  CE2 . TRP B 1 407 ? -0.170  -5.208  75.551  1.00 102.92 ?  406  TRP B CE2 1 
ATOM   6582 C  CE3 . TRP B 1 407 ? 0.077   -2.933  76.327  1.00 95.33  ?  406  TRP B CE3 1 
ATOM   6583 C  CZ2 . TRP B 1 407 ? -1.557  -5.087  75.482  1.00 97.14  ?  406  TRP B CZ2 1 
ATOM   6584 C  CZ3 . TRP B 1 407 ? -1.303  -2.814  76.257  1.00 94.26  ?  406  TRP B CZ3 1 
ATOM   6585 C  CH2 . TRP B 1 407 ? -2.103  -3.885  75.838  1.00 95.13  ?  406  TRP B CH2 1 
ATOM   6586 N  N   . ILE B 1 408 ? 6.045   -3.371  77.529  1.00 112.90 ?  407  ILE B N   1 
ATOM   6587 C  CA  . ILE B 1 408 ? 7.203   -2.510  77.750  1.00 106.43 ?  407  ILE B CA  1 
ATOM   6588 C  C   . ILE B 1 408 ? 8.523   -3.223  77.468  1.00 116.61 ?  407  ILE B C   1 
ATOM   6589 O  O   . ILE B 1 408 ? 9.427   -2.654  76.853  1.00 111.47 ?  407  ILE B O   1 
ATOM   6590 C  CB  . ILE B 1 408 ? 7.226   -1.976  79.197  1.00 102.36 ?  407  ILE B CB  1 
ATOM   6591 C  CG1 . ILE B 1 408 ? 5.943   -1.200  79.491  1.00 115.48 ?  407  ILE B CG1 1 
ATOM   6592 C  CG2 . ILE B 1 408 ? 8.457   -1.115  79.440  1.00 103.57 ?  407  ILE B CG2 1 
ATOM   6593 C  CD1 . ILE B 1 408 ? 6.015   -0.323  80.725  1.00 114.68 ?  407  ILE B CD1 1 
ATOM   6594 N  N   . SER B 1 409 ? 8.623   -4.474  77.908  1.00 133.65 ?  408  SER B N   1 
ATOM   6595 C  CA  . SER B 1 409 ? 9.839   -5.260  77.723  1.00 149.14 ?  408  SER B CA  1 
ATOM   6596 C  C   . SER B 1 409 ? 10.059  -5.611  76.258  1.00 157.66 ?  408  SER B C   1 
ATOM   6597 O  O   . SER B 1 409 ? 11.186  -5.576  75.764  1.00 164.72 ?  408  SER B O   1 
ATOM   6598 C  CB  . SER B 1 409 ? 9.784   -6.539  78.559  1.00 159.54 ?  408  SER B CB  1 
ATOM   6599 O  OG  . SER B 1 409 ? 8.692   -7.352  78.169  1.00 166.25 ?  408  SER B OG  1 
ATOM   6600 N  N   . ASN B 1 410 ? 8.974   -5.960  75.575  1.00 158.85 ?  409  ASN B N   1 
ATOM   6601 C  CA  . ASN B 1 410 ? 9.021   -6.277  74.153  1.00 156.63 ?  409  ASN B CA  1 
ATOM   6602 C  C   . ASN B 1 410 ? 9.409   -5.062  73.312  1.00 148.73 ?  409  ASN B C   1 
ATOM   6603 O  O   . ASN B 1 410 ? 10.164  -5.179  72.346  1.00 146.55 ?  409  ASN B O   1 
ATOM   6604 C  CB  . ASN B 1 410 ? 7.669   -6.830  73.693  1.00 163.74 ?  409  ASN B CB  1 
ATOM   6605 C  CG  . ASN B 1 410 ? 7.744   -7.514  72.343  1.00 176.67 ?  409  ASN B CG  1 
ATOM   6606 O  OD1 . ASN B 1 410 ? 8.828   -7.712  71.793  1.00 186.71 ?  409  ASN B OD1 1 
ATOM   6607 N  ND2 . ASN B 1 410 ? 6.589   -7.888  71.805  1.00 174.83 ?  409  ASN B ND2 1 
ATOM   6608 N  N   . GLY B 1 411 ? 8.896   -3.897  73.695  1.00 146.36 ?  410  GLY B N   1 
ATOM   6609 C  CA  . GLY B 1 411 ? 9.123   -2.671  72.951  1.00 147.95 ?  410  GLY B CA  1 
ATOM   6610 C  C   . GLY B 1 411 ? 7.859   -2.176  72.274  1.00 149.13 ?  410  GLY B C   1 
ATOM   6611 O  O   . GLY B 1 411 ? 7.908   -1.337  71.372  1.00 150.50 ?  410  GLY B O   1 
ATOM   6612 N  N   . VAL B 1 412 ? 6.723   -2.709  72.715  1.00 146.87 ?  411  VAL B N   1 
ATOM   6613 C  CA  . VAL B 1 412 ? 5.422   -2.370  72.146  1.00 130.01 ?  411  VAL B CA  1 
ATOM   6614 C  C   . VAL B 1 412 ? 4.738   -1.235  72.921  1.00 119.55 ?  411  VAL B C   1 
ATOM   6615 O  O   . VAL B 1 412 ? 3.713   -0.700  72.493  1.00 111.03 ?  411  VAL B O   1 
ATOM   6616 C  CB  . VAL B 1 412 ? 4.501   -3.605  72.116  1.00 128.97 ?  411  VAL B CB  1 
ATOM   6617 C  CG1 . VAL B 1 412 ? 3.357   -3.390  71.150  1.00 117.82 ?  411  VAL B CG1 1 
ATOM   6618 C  CG2 . VAL B 1 412 ? 5.293   -4.827  71.693  1.00 138.13 ?  411  VAL B CG2 1 
ATOM   6619 N  N   . LEU B 1 413 ? 5.306   -0.875  74.068  1.00 123.92 ?  412  LEU B N   1 
ATOM   6620 C  CA  . LEU B 1 413 ? 4.791   0.240   74.857  1.00 115.38 ?  412  LEU B CA  1 
ATOM   6621 C  C   . LEU B 1 413 ? 5.885   1.246   75.203  1.00 112.78 ?  412  LEU B C   1 
ATOM   6622 O  O   . LEU B 1 413 ? 7.037   0.878   75.439  1.00 117.21 ?  412  LEU B O   1 
ATOM   6623 C  CB  . LEU B 1 413 ? 4.128   -0.254  76.146  1.00 104.15 ?  412  LEU B CB  1 
ATOM   6624 C  CG  . LEU B 1 413 ? 3.221   0.793   76.803  1.00 95.15  ?  412  LEU B CG  1 
ATOM   6625 C  CD1 . LEU B 1 413 ? 1.796   0.661   76.330  1.00 93.86  ?  412  LEU B CD1 1 
ATOM   6626 C  CD2 . LEU B 1 413 ? 3.284   0.737   78.316  1.00 95.04  ?  412  LEU B CD2 1 
ATOM   6627 N  N   . TYR B 1 414 ? 5.512   2.520   75.220  1.00 97.80  ?  413  TYR B N   1 
ATOM   6628 C  CA  . TYR B 1 414 ? 6.415   3.581   75.637  1.00 98.71  ?  413  TYR B CA  1 
ATOM   6629 C  C   . TYR B 1 414 ? 5.710   4.470   76.647  1.00 115.90 ?  413  TYR B C   1 
ATOM   6630 O  O   . TYR B 1 414 ? 4.508   4.726   76.541  1.00 95.78  ?  413  TYR B O   1 
ATOM   6631 C  CB  . TYR B 1 414 ? 6.895   4.400   74.441  1.00 99.92  ?  413  TYR B CB  1 
ATOM   6632 C  CG  . TYR B 1 414 ? 8.033   5.356   74.744  1.00 101.66 ?  413  TYR B CG  1 
ATOM   6633 C  CD1 . TYR B 1 414 ? 9.356   4.934   74.686  1.00 106.57 ?  413  TYR B CD1 1 
ATOM   6634 C  CD2 . TYR B 1 414 ? 7.785   6.685   75.070  1.00 101.42 ?  413  TYR B CD2 1 
ATOM   6635 C  CE1 . TYR B 1 414 ? 10.402  5.808   74.952  1.00 114.29 ?  413  TYR B CE1 1 
ATOM   6636 C  CE2 . TYR B 1 414 ? 8.822   7.565   75.338  1.00 111.05 ?  413  TYR B CE2 1 
ATOM   6637 C  CZ  . TYR B 1 414 ? 10.129  7.123   75.278  1.00 116.36 ?  413  TYR B CZ  1 
ATOM   6638 O  OH  . TYR B 1 414 ? 11.163  7.996   75.545  1.00 107.91 ?  413  TYR B OH  1 
ATOM   6639 N  N   . ALA B 1 415 ? 6.470   4.935   77.631  1.00 125.53 ?  414  ALA B N   1 
ATOM   6640 C  CA  . ALA B 1 415 ? 5.907   5.724   78.711  1.00 119.17 ?  414  ALA B CA  1 
ATOM   6641 C  C   . ALA B 1 415 ? 6.137   7.209   78.465  1.00 119.85 ?  414  ALA B C   1 
ATOM   6642 O  O   . ALA B 1 415 ? 7.268   7.699   78.513  1.00 108.26 ?  414  ALA B O   1 
ATOM   6643 C  CB  . ALA B 1 415 ? 6.505   5.302   80.042  1.00 119.18 ?  414  ALA B CB  1 
ATOM   6644 N  N   . THR B 1 416 ? 5.048   7.906   78.163  1.00 122.85 ?  415  THR B N   1 
ATOM   6645 C  CA  . THR B 1 416 ? 5.056   9.351   78.000  1.00 121.58 ?  415  THR B CA  1 
ATOM   6646 C  C   . THR B 1 416 ? 5.244   10.052  79.348  1.00 133.97 ?  415  THR B C   1 
ATOM   6647 O  O   . THR B 1 416 ? 4.586   9.710   80.328  1.00 155.84 ?  415  THR B O   1 
ATOM   6648 C  CB  . THR B 1 416 ? 3.754   9.833   77.324  1.00 111.47 ?  415  THR B CB  1 
ATOM   6649 O  OG1 . THR B 1 416 ? 3.765   9.440   75.948  1.00 107.15 ?  415  THR B OG1 1 
ATOM   6650 C  CG2 . THR B 1 416 ? 3.615   11.343  77.399  1.00 115.33 ?  415  THR B CG2 1 
ATOM   6651 N  N   . PRO B 1 417 ? 6.144   11.043  79.391  1.00 126.81 ?  416  PRO B N   1 
ATOM   6652 C  CA  . PRO B 1 417 ? 6.525   11.856  80.553  1.00 127.99 ?  416  PRO B CA  1 
ATOM   6653 C  C   . PRO B 1 417 ? 5.388   12.798  80.971  1.00 133.77 ?  416  PRO B C   1 
ATOM   6654 O  O   . PRO B 1 417 ? 4.376   12.840  80.275  1.00 135.09 ?  416  PRO B O   1 
ATOM   6655 C  CB  . PRO B 1 417 ? 7.751   12.621  80.043  1.00 127.12 ?  416  PRO B CB  1 
ATOM   6656 C  CG  . PRO B 1 417 ? 8.250   11.799  78.916  1.00 126.74 ?  416  PRO B CG  1 
ATOM   6657 C  CD  . PRO B 1 417 ? 7.036   11.295  78.250  1.00 126.82 ?  416  PRO B CD  1 
ATOM   6658 N  N   . PRO B 1 418 ? 5.528   13.516  82.101  1.00 148.57 ?  417  PRO B N   1 
ATOM   6659 C  CA  . PRO B 1 418 ? 4.395   14.319  82.577  1.00 159.07 ?  417  PRO B CA  1 
ATOM   6660 C  C   . PRO B 1 418 ? 3.972   15.449  81.632  1.00 168.52 ?  417  PRO B C   1 
ATOM   6661 O  O   . PRO B 1 418 ? 2.774   15.623  81.412  1.00 177.95 ?  417  PRO B O   1 
ATOM   6662 C  CB  . PRO B 1 418 ? 4.918   14.888  83.900  1.00 159.25 ?  417  PRO B CB  1 
ATOM   6663 C  CG  . PRO B 1 418 ? 6.403   14.910  83.729  1.00 158.78 ?  417  PRO B CG  1 
ATOM   6664 C  CD  . PRO B 1 418 ? 6.675   13.624  83.020  1.00 152.40 ?  417  PRO B CD  1 
ATOM   6665 N  N   . GLY B 1 419 ? 4.922   16.199  81.084  1.00 189.57 ?  418  GLY B N   1 
ATOM   6666 C  CA  . GLY B 1 419 ? 4.587   17.226  80.114  1.00 178.30 ?  418  GLY B CA  1 
ATOM   6667 C  C   . GLY B 1 419 ? 4.463   16.593  78.742  1.00 182.45 ?  418  GLY B C   1 
ATOM   6668 O  O   . GLY B 1 419 ? 5.446   16.074  78.212  1.00 162.45 ?  418  GLY B O   1 
ATOM   6669 N  N   . SER B 1 420 ? 3.268   16.617  78.159  1.00 211.33 ?  419  SER B N   1 
ATOM   6670 C  CA  . SER B 1 420 ? 3.083   15.940  76.879  1.00 222.22 ?  419  SER B CA  1 
ATOM   6671 C  C   . SER B 1 420 ? 3.374   16.864  75.667  1.00 268.76 ?  419  SER B C   1 
ATOM   6672 O  O   . SER B 1 420 ? 4.332   16.572  74.952  1.00 267.71 ?  419  SER B O   1 
ATOM   6673 C  CB  . SER B 1 420 ? 1.691   15.293  76.809  1.00 227.46 ?  419  SER B CB  1 
ATOM   6674 O  OG  . SER B 1 420 ? 1.622   14.144  77.629  1.00 233.43 ?  419  SER B OG  1 
ATOM   6675 N  N   . ASN B 1 421 ? 2.623   17.937  75.370  1.00 267.03 ?  420  ASN B N   1 
ATOM   6676 C  CA  . ASN B 1 421 ? 1.332   18.346  75.926  1.00 265.32 ?  420  ASN B CA  1 
ATOM   6677 C  C   . ASN B 1 421 ? 0.287   17.864  74.923  1.00 257.24 ?  420  ASN B C   1 
ATOM   6678 O  O   . ASN B 1 421 ? 0.251   18.356  73.794  1.00 269.86 ?  420  ASN B O   1 
ATOM   6679 C  CB  . ASN B 1 421 ? 1.271   19.864  76.122  1.00 275.98 ?  420  ASN B CB  1 
ATOM   6680 C  CG  . ASN B 1 421 ? 0.038   20.312  76.883  1.00 275.90 ?  420  ASN B CG  1 
ATOM   6681 O  OD1 . ASN B 1 421 ? -1.039  19.735  76.744  1.00 273.09 ?  420  ASN B OD1 1 
ATOM   6682 N  ND2 . ASN B 1 421 ? 0.187   21.363  77.682  1.00 277.99 ?  420  ASN B ND2 1 
ATOM   6683 N  N   . ASP B 1 422 ? -0.563  16.927  75.348  1.00 231.24 ?  421  ASP B N   1 
ATOM   6684 C  CA  . ASP B 1 422 ? -1.531  16.273  74.468  1.00 198.55 ?  421  ASP B CA  1 
ATOM   6685 C  C   . ASP B 1 422 ? -0.646  15.716  73.371  1.00 180.59 ?  421  ASP B C   1 
ATOM   6686 O  O   . ASP B 1 422 ? -0.791  16.040  72.193  1.00 169.11 ?  421  ASP B O   1 
ATOM   6687 C  CB  . ASP B 1 422 ? -2.601  17.234  73.940  1.00 190.08 ?  421  ASP B CB  1 
ATOM   6688 C  CG  . ASP B 1 422 ? -3.743  16.517  73.238  1.00 169.68 ?  421  ASP B CG  1 
ATOM   6689 O  OD1 . ASP B 1 422 ? -3.488  15.527  72.518  1.00 161.37 ?  421  ASP B OD1 1 
ATOM   6690 O  OD2 . ASP B 1 422 ? -4.902  16.946  73.413  1.00 155.32 ?  421  ASP B OD2 1 
ATOM   6691 N  N   . ASP B 1 423 ? 0.263   14.848  73.798  1.00 177.08 ?  422  ASP B N   1 
ATOM   6692 C  CA  . ASP B 1 423 ? 1.549   14.663  73.139  1.00 160.07 ?  422  ASP B CA  1 
ATOM   6693 C  C   . ASP B 1 423 ? 1.528   14.409  71.637  1.00 148.99 ?  422  ASP B C   1 
ATOM   6694 O  O   . ASP B 1 423 ? 0.693   13.678  71.100  1.00 120.37 ?  422  ASP B O   1 
ATOM   6695 C  CB  . ASP B 1 423 ? 2.324   13.540  73.830  1.00 171.06 ?  422  ASP B CB  1 
ATOM   6696 C  CG  . ASP B 1 423 ? 1.467   12.340  74.150  1.00 192.94 ?  422  ASP B CG  1 
ATOM   6697 O  OD1 . ASP B 1 423 ? 0.238   12.502  74.299  1.00 192.82 ?  422  ASP B OD1 1 
ATOM   6698 O  OD2 . ASP B 1 423 ? 2.033   11.234  74.272  1.00 205.38 ?  422  ASP B OD2 1 
ATOM   6699 N  N   . TRP B 1 424 ? 2.483   15.054  70.979  1.00 156.37 ?  423  TRP B N   1 
ATOM   6700 C  CA  . TRP B 1 424 ? 2.758   14.867  69.568  1.00 162.81 ?  423  TRP B CA  1 
ATOM   6701 C  C   . TRP B 1 424 ? 3.591   13.607  69.362  1.00 142.75 ?  423  TRP B C   1 
ATOM   6702 O  O   . TRP B 1 424 ? 3.928   13.256  68.233  1.00 148.61 ?  423  TRP B O   1 
ATOM   6703 C  CB  . TRP B 1 424 ? 3.485   16.094  69.002  1.00 184.20 ?  423  TRP B CB  1 
ATOM   6704 C  CG  . TRP B 1 424 ? 2.708   17.378  69.139  1.00 196.40 ?  423  TRP B CG  1 
ATOM   6705 C  CD1 . TRP B 1 424 ? 1.886   17.938  68.204  1.00 201.08 ?  423  TRP B CD1 1 
ATOM   6706 C  CD2 . TRP B 1 424 ? 2.680   18.258  70.275  1.00 197.64 ?  423  TRP B CD2 1 
ATOM   6707 N  NE1 . TRP B 1 424 ? 1.350   19.108  68.684  1.00 201.04 ?  423  TRP B NE1 1 
ATOM   6708 C  CE2 . TRP B 1 424 ? 1.819   19.327  69.948  1.00 200.79 ?  423  TRP B CE2 1 
ATOM   6709 C  CE3 . TRP B 1 424 ? 3.297   18.246  71.529  1.00 197.96 ?  423  TRP B CE3 1 
ATOM   6710 C  CZ2 . TRP B 1 424 ? 1.561   20.372  70.833  1.00 207.13 ?  423  TRP B CZ2 1 
ATOM   6711 C  CZ3 . TRP B 1 424 ? 3.037   19.287  72.404  1.00 204.95 ?  423  TRP B CZ3 1 
ATOM   6712 C  CH2 . TRP B 1 424 ? 2.176   20.334  72.051  1.00 211.18 ?  423  TRP B CH2 1 
ATOM   6713 N  N   . TYR B 1 425 ? 3.941   12.958  70.470  1.00 133.35 ?  424  TYR B N   1 
ATOM   6714 C  CA  . TYR B 1 425 ? 4.699   11.707  70.468  1.00 127.85 ?  424  TYR B CA  1 
ATOM   6715 C  C   . TYR B 1 425 ? 4.211   10.686  69.439  1.00 126.65 ?  424  TYR B C   1 
ATOM   6716 O  O   . TYR B 1 425 ? 5.027   10.016  68.810  1.00 125.34 ?  424  TYR B O   1 
ATOM   6717 C  CB  . TYR B 1 425 ? 4.695   11.071  71.870  1.00 120.77 ?  424  TYR B CB  1 
ATOM   6718 C  CG  . TYR B 1 425 ? 5.684   11.683  72.851  1.00 108.10 ?  424  TYR B CG  1 
ATOM   6719 C  CD1 . TYR B 1 425 ? 5.483   12.945  73.388  1.00 105.31 ?  424  TYR B CD1 1 
ATOM   6720 C  CD2 . TYR B 1 425 ? 6.805   10.975  73.262  1.00 105.13 ?  424  TYR B CD2 1 
ATOM   6721 C  CE1 . TYR B 1 425 ? 6.381   13.495  74.292  1.00 116.79 ?  424  TYR B CE1 1 
ATOM   6722 C  CE2 . TYR B 1 425 ? 7.713   11.514  74.159  1.00 115.24 ?  424  TYR B CE2 1 
ATOM   6723 C  CZ  . TYR B 1 425 ? 7.495   12.774  74.675  1.00 122.77 ?  424  TYR B CZ  1 
ATOM   6724 O  OH  . TYR B 1 425 ? 8.389   13.321  75.571  1.00 107.84 ?  424  TYR B OH  1 
ATOM   6725 N  N   . TRP B 1 426 ? 2.899   10.532  69.281  1.00 131.32 ?  425  TRP B N   1 
ATOM   6726 C  CA  . TRP B 1 426 ? 2.404   9.639   68.229  1.00 136.12 ?  425  TRP B CA  1 
ATOM   6727 C  C   . TRP B 1 426 ? 2.399   10.295  66.838  1.00 142.44 ?  425  TRP B C   1 
ATOM   6728 O  O   . TRP B 1 426 ? 2.679   9.636   65.836  1.00 125.18 ?  425  TRP B O   1 
ATOM   6729 C  CB  . TRP B 1 426 ? 0.992   9.128   68.546  1.00 126.39 ?  425  TRP B CB  1 
ATOM   6730 C  CG  . TRP B 1 426 ? -0.058  10.181  68.669  1.00 128.32 ?  425  TRP B CG  1 
ATOM   6731 C  CD1 . TRP B 1 426 ? -0.666  10.851  67.649  1.00 135.30 ?  425  TRP B CD1 1 
ATOM   6732 C  CD2 . TRP B 1 426 ? -0.685  10.632  69.870  1.00 122.15 ?  425  TRP B CD2 1 
ATOM   6733 N  NE1 . TRP B 1 426 ? -1.602  11.720  68.140  1.00 131.63 ?  425  TRP B NE1 1 
ATOM   6734 C  CE2 . TRP B 1 426 ? -1.639  11.603  69.503  1.00 122.20 ?  425  TRP B CE2 1 
ATOM   6735 C  CE3 . TRP B 1 426 ? -0.522  10.322  71.219  1.00 126.97 ?  425  TRP B CE3 1 
ATOM   6736 C  CZ2 . TRP B 1 426 ? -2.424  12.266  70.437  1.00 121.77 ?  425  TRP B CZ2 1 
ATOM   6737 C  CZ3 . TRP B 1 426 ? -1.299  10.983  72.145  1.00 136.49 ?  425  TRP B CZ3 1 
ATOM   6738 C  CH2 . TRP B 1 426 ? -2.242  11.942  71.751  1.00 135.60 ?  425  TRP B CH2 1 
ATOM   6739 N  N   . LEU B 1 427 ? 2.092   11.589  66.775  1.00 148.67 ?  426  LEU B N   1 
ATOM   6740 C  CA  . LEU B 1 427 ? 2.112   12.307  65.503  1.00 155.98 ?  426  LEU B CA  1 
ATOM   6741 C  C   . LEU B 1 427 ? 3.512   12.275  64.930  1.00 110.04 ?  426  LEU B C   1 
ATOM   6742 O  O   . LEU B 1 427 ? 3.701   12.015  63.745  1.00 127.36 ?  426  LEU B O   1 
ATOM   6743 C  CB  . LEU B 1 427 ? 1.645   13.754  65.660  1.00 108.89 ?  426  LEU B CB  1 
ATOM   6744 C  CG  . LEU B 1 427 ? 0.137   13.997  65.695  1.00 107.84 ?  426  LEU B CG  1 
ATOM   6745 C  CD1 . LEU B 1 427 ? -0.162  15.481  65.858  1.00 109.77 ?  426  LEU B CD1 1 
ATOM   6746 C  CD2 . LEU B 1 427 ? -0.535  13.444  64.450  1.00 125.75 ?  426  LEU B CD2 1 
ATOM   6747 N  N   . TYR B 1 428 ? 4.492   12.531  65.789  1.00 110.30 ?  427  TYR B N   1 
ATOM   6748 C  CA  . TYR B 1 428 ? 5.890   12.467  65.398  1.00 128.03 ?  427  TYR B CA  1 
ATOM   6749 C  C   . TYR B 1 428 ? 6.214   11.066  64.901  1.00 146.26 ?  427  TYR B C   1 
ATOM   6750 O  O   . TYR B 1 428 ? 6.829   10.906  63.851  1.00 166.27 ?  427  TYR B O   1 
ATOM   6751 C  CB  . TYR B 1 428 ? 6.798   12.854  66.568  1.00 132.55 ?  427  TYR B CB  1 
ATOM   6752 C  CG  . TYR B 1 428 ? 8.263   12.518  66.378  1.00 143.38 ?  427  TYR B CG  1 
ATOM   6753 C  CD1 . TYR B 1 428 ? 9.109   13.381  65.688  1.00 152.42 ?  427  TYR B CD1 1 
ATOM   6754 C  CD2 . TYR B 1 428 ? 8.806   11.354  66.905  1.00 140.35 ?  427  TYR B CD2 1 
ATOM   6755 C  CE1 . TYR B 1 428 ? 10.453  13.087  65.520  1.00 146.89 ?  427  TYR B CE1 1 
ATOM   6756 C  CE2 . TYR B 1 428 ? 10.147  11.052  66.740  1.00 144.46 ?  427  TYR B CE2 1 
ATOM   6757 C  CZ  . TYR B 1 428 ? 10.966  11.922  66.050  1.00 145.03 ?  427  TYR B CZ  1 
ATOM   6758 O  OH  . TYR B 1 428 ? 12.300  11.625  65.885  1.00 146.04 ?  427  TYR B OH  1 
ATOM   6759 N  N   . ALA B 1 429 ? 5.788   10.057  65.653  1.00 133.31 ?  428  ALA B N   1 
ATOM   6760 C  CA  . ALA B 1 429 ? 6.083   8.672   65.303  1.00 131.14 ?  428  ALA B CA  1 
ATOM   6761 C  C   . ALA B 1 429 ? 5.376   8.229   64.020  1.00 137.16 ?  428  ALA B C   1 
ATOM   6762 O  O   . ALA B 1 429 ? 5.960   7.524   63.192  1.00 142.63 ?  428  ALA B O   1 
ATOM   6763 C  CB  . ALA B 1 429 ? 5.707   7.752   66.450  1.00 118.54 ?  428  ALA B CB  1 
ATOM   6764 N  N   . ALA B 1 430 ? 4.127   8.653   63.849  1.00 124.61 ?  429  ALA B N   1 
ATOM   6765 C  CA  . ALA B 1 430 ? 3.365   8.303   62.652  1.00 123.23 ?  429  ALA B CA  1 
ATOM   6766 C  C   . ALA B 1 430 ? 3.966   8.927   61.399  1.00 131.69 ?  429  ALA B C   1 
ATOM   6767 O  O   . ALA B 1 430 ? 4.157   8.251   60.390  1.00 122.91 ?  429  ALA B O   1 
ATOM   6768 C  CB  . ALA B 1 430 ? 1.907   8.730   62.802  1.00 115.35 ?  429  ALA B CB  1 
ATOM   6769 N  N   . ALA B 1 431 ? 4.274   10.217  61.477  1.00 140.57 ?  430  ALA B N   1 
ATOM   6770 C  CA  . ALA B 1 431 ? 4.820   10.952  60.343  1.00 135.98 ?  430  ALA B CA  1 
ATOM   6771 C  C   . ALA B 1 431 ? 6.231   10.495  59.999  1.00 142.46 ?  430  ALA B C   1 
ATOM   6772 O  O   . ALA B 1 431 ? 6.578   10.383  58.824  1.00 160.72 ?  430  ALA B O   1 
ATOM   6773 C  CB  . ALA B 1 431 ? 4.802   12.447  60.624  1.00 127.95 ?  430  ALA B CB  1 
ATOM   6774 N  N   . LYS B 1 432 ? 7.046   10.245  61.021  1.00 131.55 ?  431  LYS B N   1 
ATOM   6775 C  CA  . LYS B 1 432 ? 8.436   9.848   60.809  1.00 142.73 ?  431  LYS B CA  1 
ATOM   6776 C  C   . LYS B 1 432 ? 8.551   8.507   60.086  1.00 138.67 ?  431  LYS B C   1 
ATOM   6777 O  O   . LYS B 1 432 ? 9.466   8.300   59.288  1.00 129.55 ?  431  LYS B O   1 
ATOM   6778 C  CB  . LYS B 1 432 ? 9.185   9.792   62.139  1.00 161.59 ?  431  LYS B CB  1 
ATOM   6779 C  CG  . LYS B 1 432 ? 10.689  9.659   61.994  1.00 180.12 ?  431  LYS B CG  1 
ATOM   6780 C  CD  . LYS B 1 432 ? 11.399  10.399  63.107  1.00 189.62 ?  431  LYS B CD  1 
ATOM   6781 C  CE  . LYS B 1 432 ? 12.893  10.140  63.090  1.00 201.52 ?  431  LYS B CE  1 
ATOM   6782 N  NZ  . LYS B 1 432 ? 13.203  8.726   63.438  1.00 204.47 ?  431  LYS B NZ  1 
ATOM   6783 N  N   . LEU B 1 433 ? 7.640   7.590   60.388  1.00 139.60 ?  432  LEU B N   1 
ATOM   6784 C  CA  . LEU B 1 433 ? 7.614   6.300   59.709  1.00 138.45 ?  432  LEU B CA  1 
ATOM   6785 C  C   . LEU B 1 433 ? 6.652   6.318   58.518  1.00 139.32 ?  432  LEU B C   1 
ATOM   6786 O  O   . LEU B 1 433 ? 6.583   5.349   57.757  1.00 127.10 ?  432  LEU B O   1 
ATOM   6787 C  CB  . LEU B 1 433 ? 7.238   5.180   60.686  1.00 130.99 ?  432  LEU B CB  1 
ATOM   6788 C  CG  . LEU B 1 433 ? 8.378   4.599   61.535  1.00 130.97 ?  432  LEU B CG  1 
ATOM   6789 C  CD1 . LEU B 1 433 ? 8.816   5.548   62.641  1.00 117.17 ?  432  LEU B CD1 1 
ATOM   6790 C  CD2 . LEU B 1 433 ? 7.982   3.253   62.109  1.00 116.57 ?  432  LEU B CD2 1 
ATOM   6791 N  N   . LYS B 1 434 ? 5.908   7.417   58.378  1.00 150.64 ?  433  LYS B N   1 
ATOM   6792 C  CA  . LYS B 1 434 ? 4.886   7.577   57.334  1.00 156.08 ?  433  LYS B CA  1 
ATOM   6793 C  C   . LYS B 1 434 ? 3.869   6.442   57.392  1.00 164.69 ?  433  LYS B C   1 
ATOM   6794 O  O   . LYS B 1 434 ? 3.270   6.062   56.385  1.00 172.35 ?  433  LYS B O   1 
ATOM   6795 C  CB  . LYS B 1 434 ? 5.517   7.662   55.940  1.00 149.85 ?  433  LYS B CB  1 
ATOM   6796 C  CG  . LYS B 1 434 ? 6.202   8.991   55.653  1.00 144.62 ?  433  LYS B CG  1 
ATOM   6797 C  CD  . LYS B 1 434 ? 6.926   8.983   54.315  1.00 134.50 ?  433  LYS B CD  1 
ATOM   6798 C  CE  . LYS B 1 434 ? 8.075   7.989   54.294  1.00 148.46 ?  433  LYS B CE  1 
ATOM   6799 N  NZ  . LYS B 1 434 ? 9.109   8.311   55.314  1.00 146.76 ?  433  LYS B NZ  1 
ATOM   6800 N  N   . CYS B 1 435 ? 3.678   5.918   58.596  1.00 161.19 ?  434  CYS B N   1 
ATOM   6801 C  CA  . CYS B 1 435 ? 2.849   4.746   58.826  1.00 161.23 ?  434  CYS B CA  1 
ATOM   6802 C  C   . CYS B 1 435 ? 1.438   5.130   59.263  1.00 153.75 ?  434  CYS B C   1 
ATOM   6803 O  O   . CYS B 1 435 ? 1.003   6.263   59.067  1.00 168.25 ?  434  CYS B O   1 
ATOM   6804 C  CB  . CYS B 1 435 ? 3.508   3.833   59.865  1.00 165.77 ?  434  CYS B CB  1 
ATOM   6805 S  SG  . CYS B 1 435 ? 3.526   4.475   61.552  1.00 123.04 ?  434  CYS B SG  1 
ATOM   6806 N  N   . LEU B 1 436 ? 0.718   4.168   59.829  1.00 141.43 ?  435  LEU B N   1 
ATOM   6807 C  CA  . LEU B 1 436 ? -0.661  4.383   60.253  1.00 120.73 ?  435  LEU B CA  1 
ATOM   6808 C  C   . LEU B 1 436 ? -0.749  5.074   61.613  1.00 117.73 ?  435  LEU B C   1 
ATOM   6809 O  O   . LEU B 1 436 ? 0.183   5.018   62.413  1.00 113.98 ?  435  LEU B O   1 
ATOM   6810 C  CB  . LEU B 1 436 ? -1.426  3.056   60.303  1.00 108.40 ?  435  LEU B CB  1 
ATOM   6811 C  CG  . LEU B 1 436 ? -1.842  2.388   58.988  1.00 115.28 ?  435  LEU B CG  1 
ATOM   6812 C  CD1 . LEU B 1 436 ? -0.651  1.808   58.230  1.00 128.81 ?  435  LEU B CD1 1 
ATOM   6813 C  CD2 . LEU B 1 436 ? -2.885  1.315   59.249  1.00 111.47 ?  435  LEU B CD2 1 
ATOM   6814 N  N   . LEU B 1 437 ? -1.866  5.756   61.843  1.00 123.79 ?  436  LEU B N   1 
ATOM   6815 C  CA  . LEU B 1 437 ? -2.184  6.345   63.142  1.00 121.91 ?  436  LEU B CA  1 
ATOM   6816 C  C   . LEU B 1 437 ? -3.537  5.842   63.629  1.00 136.07 ?  436  LEU B C   1 
ATOM   6817 O  O   . LEU B 1 437 ? -4.488  5.803   62.854  1.00 162.87 ?  436  LEU B O   1 
ATOM   6818 C  CB  . LEU B 1 437 ? -2.209  7.867   63.047  1.00 118.47 ?  436  LEU B CB  1 
ATOM   6819 C  CG  . LEU B 1 437 ? -2.449  8.593   64.365  1.00 111.37 ?  436  LEU B CG  1 
ATOM   6820 C  CD1 . LEU B 1 437 ? -1.138  8.813   65.056  1.00 102.02 ?  436  LEU B CD1 1 
ATOM   6821 C  CD2 . LEU B 1 437 ? -3.170  9.912   64.148  1.00 121.39 ?  436  LEU B CD2 1 
ATOM   6822 N  N   . VAL B 1 438 ? -3.646  5.478   64.904  1.00 121.70 ?  437  VAL B N   1 
ATOM   6823 C  CA  . VAL B 1 438 ? -4.937  5.026   65.424  1.00 108.82 ?  437  VAL B CA  1 
ATOM   6824 C  C   . VAL B 1 438 ? -5.459  5.946   66.516  1.00 111.95 ?  437  VAL B C   1 
ATOM   6825 O  O   . VAL B 1 438 ? -4.940  5.955   67.630  1.00 95.32  ?  437  VAL B O   1 
ATOM   6826 C  CB  . VAL B 1 438 ? -4.865  3.600   65.992  1.00 97.12  ?  437  VAL B CB  1 
ATOM   6827 C  CG1 . VAL B 1 438 ? -6.262  3.031   66.146  1.00 96.69  ?  437  VAL B CG1 1 
ATOM   6828 C  CG2 . VAL B 1 438 ? -4.022  2.704   65.100  1.00 98.76  ?  437  VAL B CG2 1 
ATOM   6829 N  N   . THR B 1 439 ? -6.499  6.709   66.199  1.00 116.81 ?  438  THR B N   1 
ATOM   6830 C  CA  . THR B 1 439 ? -7.028  7.694   67.134  1.00 115.33 ?  438  THR B CA  1 
ATOM   6831 C  C   . THR B 1 439 ? -8.445  8.104   66.739  1.00 97.22  ?  438  THR B C   1 
ATOM   6832 O  O   . THR B 1 439 ? -8.807  8.063   65.567  1.00 98.78  ?  438  THR B O   1 
ATOM   6833 C  CB  . THR B 1 439 ? -6.136  8.956   67.190  1.00 140.16 ?  438  THR B CB  1 
ATOM   6834 O  OG1 . THR B 1 439 ? -4.756  8.586   67.280  1.00 152.72 ?  438  THR B OG1 1 
ATOM   6835 C  CG2 . THR B 1 439 ? -6.489  9.810   68.377  1.00 142.20 ?  438  THR B CG2 1 
ATOM   6836 N  N   . ASN B 1 440 ? -9.246  8.492   67.722  1.00 109.36 ?  439  ASN B N   1 
ATOM   6837 C  CA  . ASN B 1 440 ? -10.590 8.985   67.464  1.00 122.10 ?  439  ASN B CA  1 
ATOM   6838 C  C   . ASN B 1 440 ? -10.631 10.505  67.571  1.00 125.64 ?  439  ASN B C   1 
ATOM   6839 O  O   . ASN B 1 440 ? -11.704 11.107  67.580  1.00 123.97 ?  439  ASN B O   1 
ATOM   6840 C  CB  . ASN B 1 440 ? -11.596 8.353   68.423  1.00 139.25 ?  439  ASN B CB  1 
ATOM   6841 C  CG  . ASN B 1 440 ? -12.914 8.037   67.750  1.00 143.96 ?  439  ASN B CG  1 
ATOM   6842 O  OD1 . ASN B 1 440 ? -13.408 8.815   66.934  1.00 156.17 ?  439  ASN B OD1 1 
ATOM   6843 N  ND2 . ASN B 1 440 ? -13.491 6.889   68.084  1.00 136.71 ?  439  ASN B ND2 1 
ATOM   6844 N  N   . ASP B 1 441 ? -9.451  11.116  67.637  1.00 126.89 ?  440  ASP B N   1 
ATOM   6845 C  CA  . ASP B 1 441 ? -9.335  12.559  67.799  1.00 135.74 ?  440  ASP B CA  1 
ATOM   6846 C  C   . ASP B 1 441 ? -9.742  13.252  66.507  1.00 169.07 ?  440  ASP B C   1 
ATOM   6847 O  O   . ASP B 1 441 ? -9.164  13.015  65.445  1.00 177.36 ?  440  ASP B O   1 
ATOM   6848 C  CB  . ASP B 1 441 ? -7.906  12.952  68.186  1.00 150.40 ?  440  ASP B CB  1 
ATOM   6849 C  CG  . ASP B 1 441 ? -7.857  14.093  69.187  1.00 147.69 ?  440  ASP B CG  1 
ATOM   6850 O  OD1 . ASP B 1 441 ? -8.840  14.859  69.277  1.00 141.50 ?  440  ASP B OD1 1 
ATOM   6851 O  OD2 . ASP B 1 441 ? -6.826  14.226  69.884  1.00 138.83 ?  440  ASP B OD2 1 
ATOM   6852 N  N   . GLU B 1 442 ? -10.752 14.107  66.619  1.00 190.51 ?  441  GLU B N   1 
ATOM   6853 C  CA  . GLU B 1 442 ? -11.190 14.965  65.528  1.00 204.85 ?  441  GLU B CA  1 
ATOM   6854 C  C   . GLU B 1 442 ? -10.061 15.878  65.075  1.00 204.54 ?  441  GLU B C   1 
ATOM   6855 O  O   . GLU B 1 442 ? -10.010 16.283  63.915  1.00 219.63 ?  441  GLU B O   1 
ATOM   6856 C  CB  . GLU B 1 442 ? -12.404 15.800  65.954  1.00 218.12 ?  441  GLU B CB  1 
ATOM   6857 C  CG  . GLU B 1 442 ? -13.672 14.999  66.245  1.00 231.26 ?  441  GLU B CG  1 
ATOM   6858 C  CD  . GLU B 1 442 ? -13.637 14.265  67.583  1.00 239.39 ?  441  GLU B CD  1 
ATOM   6859 O  OE1 . GLU B 1 442 ? -12.614 14.350  68.298  1.00 244.20 ?  441  GLU B OE1 1 
ATOM   6860 O  OE2 . GLU B 1 442 ? -14.640 13.602  67.922  1.00 241.94 ?  441  GLU B OE2 1 
ATOM   6861 N  N   . MET B 1 443 ? -9.154  16.179  66.003  1.00 187.68 ?  442  MET B N   1 
ATOM   6862 C  CA  . MET B 1 443 ? -8.018  17.072  65.775  1.00 172.68 ?  442  MET B CA  1 
ATOM   6863 C  C   . MET B 1 443 ? -8.509  18.434  65.310  1.00 180.83 ?  442  MET B C   1 
ATOM   6864 O  O   . MET B 1 443 ? -7.801  19.147  64.598  1.00 184.99 ?  442  MET B O   1 
ATOM   6865 C  CB  . MET B 1 443 ? -7.043  16.504  64.734  1.00 167.75 ?  442  MET B CB  1 
ATOM   6866 C  CG  . MET B 1 443 ? -6.894  14.980  64.717  1.00 159.57 ?  442  MET B CG  1 
ATOM   6867 S  SD  . MET B 1 443 ? -5.505  14.326  65.670  1.00 168.90 ?  442  MET B SD  1 
ATOM   6868 C  CE  . MET B 1 443 ? -4.292  14.013  64.390  1.00 113.58 ?  442  MET B CE  1 
ATOM   6869 N  N   . ARG B 1 444 ? -9.737  18.778  65.686  1.00 190.35 ?  443  ARG B N   1 
ATOM   6870 C  CA  . ARG B 1 444 ? -10.306 20.076  65.344  1.00 202.83 ?  443  ARG B CA  1 
ATOM   6871 C  C   . ARG B 1 444 ? -10.099 21.105  66.456  1.00 216.14 ?  443  ARG B C   1 
ATOM   6872 O  O   . ARG B 1 444 ? -11.057 21.529  67.103  1.00 216.41 ?  443  ARG B O   1 
ATOM   6873 C  CB  . ARG B 1 444 ? -11.796 19.934  65.025  1.00 200.40 ?  443  ARG B CB  1 
ATOM   6874 C  CG  . ARG B 1 444 ? -12.115 18.830  64.020  1.00 192.59 ?  443  ARG B CG  1 
ATOM   6875 C  CD  . ARG B 1 444 ? -11.259 18.925  62.762  1.00 186.45 ?  443  ARG B CD  1 
ATOM   6876 N  NE  . ARG B 1 444 ? -11.537 20.139  62.005  1.00 187.89 ?  443  ARG B NE  1 
ATOM   6877 C  CZ  . ARG B 1 444 ? -12.543 20.267  61.148  1.00 184.96 ?  443  ARG B CZ  1 
ATOM   6878 N  NH1 . ARG B 1 444 ? -13.372 19.253  60.941  1.00 175.61 ?  443  ARG B NH1 1 
ATOM   6879 N  NH2 . ARG B 1 444 ? -12.722 21.410  60.501  1.00 190.61 ?  443  ARG B NH2 1 
ATOM   6880 N  N   . ASP B 1 445 ? -8.853  21.503  66.680  1.00 229.89 ?  444  ASP B N   1 
ATOM   6881 C  CA  . ASP B 1 445 ? -8.554  22.512  67.689  1.00 231.68 ?  444  ASP B CA  1 
ATOM   6882 C  C   . ASP B 1 445 ? -7.579  23.535  67.104  1.00 241.05 ?  444  ASP B C   1 
ATOM   6883 O  O   . ASP B 1 445 ? -6.898  23.249  66.118  1.00 243.71 ?  444  ASP B O   1 
ATOM   6884 C  CB  . ASP B 1 445 ? -7.988  21.855  68.953  1.00 231.69 ?  444  ASP B CB  1 
ATOM   6885 C  CG  . ASP B 1 445 ? -7.626  22.863  70.027  1.00 233.38 ?  444  ASP B CG  1 
ATOM   6886 O  OD1 . ASP B 1 445 ? -6.543  23.476  69.925  1.00 232.50 ?  444  ASP B OD1 1 
ATOM   6887 O  OD2 . ASP B 1 445 ? -8.431  23.049  70.964  1.00 234.60 ?  444  ASP B OD2 1 
ATOM   6888 N  N   . HIS B 1 446 ? -7.537  24.732  67.686  1.00 258.66 ?  445  HIS B N   1 
ATOM   6889 C  CA  . HIS B 1 446 ? -6.738  25.828  67.142  1.00 273.01 ?  445  HIS B CA  1 
ATOM   6890 C  C   . HIS B 1 446 ? -5.261  25.451  67.050  1.00 278.57 ?  445  HIS B C   1 
ATOM   6891 O  O   . HIS B 1 446 ? -4.618  25.714  66.037  1.00 295.05 ?  445  HIS B O   1 
ATOM   6892 C  CB  . HIS B 1 446 ? -6.912  27.097  67.983  1.00 276.73 ?  445  HIS B CB  1 
ATOM   6893 C  CG  . HIS B 1 446 ? -8.341  27.444  68.269  1.00 277.15 ?  445  HIS B CG  1 
ATOM   6894 N  ND1 . HIS B 1 446 ? -9.253  27.730  67.274  1.00 280.06 ?  445  HIS B ND1 1 
ATOM   6895 C  CD2 . HIS B 1 446 ? -9.016  27.554  69.437  1.00 274.88 ?  445  HIS B CD2 1 
ATOM   6896 C  CE1 . HIS B 1 446 ? -10.425 28.001  67.817  1.00 280.11 ?  445  HIS B CE1 1 
ATOM   6897 N  NE2 . HIS B 1 446 ? -10.309 27.901  69.130  1.00 277.07 ?  445  HIS B NE2 1 
ATOM   6898 N  N   . ILE B 1 447 ? -4.740  24.827  68.105  1.00 263.79 ?  446  ILE B N   1 
ATOM   6899 C  CA  . ILE B 1 447 ? -3.344  24.390  68.146  1.00 255.32 ?  446  ILE B CA  1 
ATOM   6900 C  C   . ILE B 1 447 ? -3.088  23.425  66.994  1.00 255.03 ?  446  ILE B C   1 
ATOM   6901 O  O   . ILE B 1 447 ? -2.077  23.523  66.297  1.00 253.75 ?  446  ILE B O   1 
ATOM   6902 C  CB  . ILE B 1 447 ? -2.968  23.698  69.487  1.00 171.77 ?  446  ILE B CB  1 
ATOM   6903 C  CG1 . ILE B 1 447 ? -2.833  24.705  70.638  1.00 176.08 ?  446  ILE B CG1 1 
ATOM   6904 C  CG2 . ILE B 1 447 ? -1.622  23.005  69.366  1.00 167.77 ?  446  ILE B CG2 1 
ATOM   6905 C  CD1 . ILE B 1 447 ? -4.115  25.394  71.069  1.00 177.19 ?  446  ILE B CD1 1 
ATOM   6906 N  N   . PHE B 1 448 ? -4.019  22.493  66.807  1.00 255.27 ?  447  PHE B N   1 
ATOM   6907 C  CA  . PHE B 1 448 ? -3.957  21.534  65.708  1.00 256.44 ?  447  PHE B CA  1 
ATOM   6908 C  C   . PHE B 1 448 ? -4.135  22.254  64.368  1.00 269.52 ?  447  PHE B C   1 
ATOM   6909 O  O   . PHE B 1 448 ? -3.407  21.990  63.410  1.00 266.26 ?  447  PHE B O   1 
ATOM   6910 C  CB  . PHE B 1 448 ? -5.024  20.446  65.880  1.00 251.96 ?  447  PHE B CB  1 
ATOM   6911 C  CG  . PHE B 1 448 ? -4.853  19.606  67.125  1.00 245.58 ?  447  PHE B CG  1 
ATOM   6912 C  CD1 . PHE B 1 448 ? -3.603  19.411  67.695  1.00 237.93 ?  447  PHE B CD1 1 
ATOM   6913 C  CD2 . PHE B 1 448 ? -5.954  19.015  67.727  1.00 239.36 ?  447  PHE B CD2 1 
ATOM   6914 C  CE1 . PHE B 1 448 ? -3.462  18.640  68.839  1.00 237.09 ?  447  PHE B CE1 1 
ATOM   6915 C  CE2 . PHE B 1 448 ? -5.818  18.248  68.864  1.00 226.07 ?  447  PHE B CE2 1 
ATOM   6916 C  CZ  . PHE B 1 448 ? -4.574  18.060  69.421  1.00 225.57 ?  447  PHE B CZ  1 
ATOM   6917 N  N   . GLU B 1 449 ? -5.122  23.146  64.302  1.00 289.76 ?  448  GLU B N   1 
ATOM   6918 C  CA  . GLU B 1 449 ? -5.426  23.873  63.070  1.00 313.28 ?  448  GLU B CA  1 
ATOM   6919 C  C   . GLU B 1 449 ? -4.367  24.908  62.694  1.00 327.58 ?  448  GLU B C   1 
ATOM   6920 O  O   . GLU B 1 449 ? -4.105  25.126  61.511  1.00 338.10 ?  448  GLU B O   1 
ATOM   6921 C  CB  . GLU B 1 449 ? -6.792  24.570  63.195  1.00 321.44 ?  448  GLU B CB  1 
ATOM   6922 C  CG  . GLU B 1 449 ? -7.379  25.089  61.881  1.00 332.65 ?  448  GLU B CG  1 
ATOM   6923 C  CD  . GLU B 1 449 ? -6.895  26.488  61.515  1.00 344.52 ?  448  GLU B CD  1 
ATOM   6924 O  OE1 . GLU B 1 449 ? -6.496  27.249  62.422  1.00 349.08 ?  448  GLU B OE1 1 
ATOM   6925 O  OE2 . GLU B 1 449 ? -6.915  26.826  60.313  1.00 350.24 ?  448  GLU B OE2 1 
ATOM   6926 N  N   . LEU B 1 450 ? -3.759  25.540  63.694  1.00 306.72 ?  449  LEU B N   1 
ATOM   6927 C  CA  . LEU B 1 450 ? -2.695  26.516  63.446  1.00 292.28 ?  449  LEU B CA  1 
ATOM   6928 C  C   . LEU B 1 450 ? -1.470  26.104  62.630  1.00 286.49 ?  449  LEU B C   1 
ATOM   6929 O  O   . LEU B 1 450 ? -1.046  26.816  61.720  1.00 290.42 ?  449  LEU B O   1 
ATOM   6930 C  CB  . LEU B 1 450 ? -2.255  27.180  64.757  1.00 273.76 ?  449  LEU B CB  1 
ATOM   6931 C  CG  . LEU B 1 450 ? -3.304  28.044  65.462  1.00 249.48 ?  449  LEU B CG  1 
ATOM   6932 C  CD1 . LEU B 1 450 ? -2.788  28.516  66.810  1.00 241.69 ?  449  LEU B CD1 1 
ATOM   6933 C  CD2 . LEU B 1 450 ? -3.711  29.223  64.585  1.00 241.17 ?  449  LEU B CD2 1 
ATOM   6934 N  N   . LEU B 1 451 ? -0.903  24.956  62.973  1.00 272.33 ?  450  LEU B N   1 
ATOM   6935 C  CA  . LEU B 1 451 ? 0.172   24.364  62.180  1.00 264.17 ?  450  LEU B CA  1 
ATOM   6936 C  C   . LEU B 1 451 ? -0.248  23.577  60.900  1.00 214.77 ?  450  LEU B C   1 
ATOM   6937 O  O   . LEU B 1 451 ? 0.497   23.395  59.936  1.00 225.52 ?  450  LEU B O   1 
ATOM   6938 C  CB  . LEU B 1 451 ? 0.900   23.318  63.029  1.00 242.11 ?  450  LEU B CB  1 
ATOM   6939 C  CG  . LEU B 1 451 ? 2.022   22.508  62.375  1.00 233.15 ?  450  LEU B CG  1 
ATOM   6940 C  CD1 . LEU B 1 451 ? 3.153   23.417  61.954  1.00 238.34 ?  450  LEU B CD1 1 
ATOM   6941 C  CD2 . LEU B 1 451 ? 2.529   21.412  63.304  1.00 226.12 ?  450  LEU B CD2 1 
ATOM   6942 N  N   . GLY B 1 452 ? -1.519  23.185  60.912  1.00 216.35 ?  451  GLY B N   1 
ATOM   6943 C  CA  . GLY B 1 452 ? -2.097  22.445  59.804  1.00 219.42 ?  451  GLY B CA  1 
ATOM   6944 C  C   . GLY B 1 452 ? -3.592  22.625  59.605  1.00 216.18 ?  451  GLY B C   1 
ATOM   6945 O  O   . GLY B 1 452 ? -4.378  22.390  60.527  1.00 209.00 ?  451  GLY B O   1 
ATOM   6946 N  N   . SER B 1 453 ? -3.990  22.994  58.391  1.00 212.75 ?  452  SER B N   1 
ATOM   6947 C  CA  . SER B 1 453 ? -5.372  23.373  58.132  1.00 205.77 ?  452  SER B CA  1 
ATOM   6948 C  C   . SER B 1 453 ? -5.903  22.694  56.879  1.00 193.95 ?  452  SER B C   1 
ATOM   6949 O  O   . SER B 1 453 ? -6.820  21.877  56.959  1.00 202.45 ?  452  SER B O   1 
ATOM   6950 C  CB  . SER B 1 453 ? -5.492  24.895  57.998  1.00 219.61 ?  452  SER B CB  1 
ATOM   6951 O  OG  . SER B 1 453 ? -6.810  25.281  57.647  1.00 222.09 ?  452  SER B OG  1 
ATOM   6952 N  N   . THR B 1 454 ? -5.346  23.035  55.724  1.00 186.88 ?  453  THR B N   1 
ATOM   6953 C  CA  . THR B 1 454 ? -5.731  22.357  54.499  1.00 180.66 ?  453  THR B CA  1 
ATOM   6954 C  C   . THR B 1 454 ? -4.838  21.155  54.215  1.00 167.20 ?  453  THR B C   1 
ATOM   6955 O  O   . THR B 1 454 ? -5.301  20.154  53.664  1.00 164.18 ?  453  THR B O   1 
ATOM   6956 C  CB  . THR B 1 454 ? -5.696  23.312  53.302  1.00 192.46 ?  453  THR B CB  1 
ATOM   6957 O  OG1 . THR B 1 454 ? -4.359  23.789  53.103  1.00 199.24 ?  453  THR B OG1 1 
ATOM   6958 C  CG2 . THR B 1 454 ? -6.629  24.499  53.551  1.00 196.26 ?  453  THR B CG2 1 
ATOM   6959 N  N   . PHE B 1 455 ? -3.559  21.250  54.568  1.00 165.69 ?  454  PHE B N   1 
ATOM   6960 C  CA  . PHE B 1 455 ? -2.674  20.103  54.414  1.00 173.17 ?  454  PHE B CA  1 
ATOM   6961 C  C   . PHE B 1 455 ? -3.042  18.963  55.356  1.00 178.14 ?  454  PHE B C   1 
ATOM   6962 O  O   . PHE B 1 455 ? -3.013  17.787  54.980  1.00 185.31 ?  454  PHE B O   1 
ATOM   6963 C  CB  . PHE B 1 455 ? -1.218  20.487  54.657  1.00 172.44 ?  454  PHE B CB  1 
ATOM   6964 C  CG  . PHE B 1 455 ? -0.280  19.311  54.618  1.00 172.22 ?  454  PHE B CG  1 
ATOM   6965 C  CD1 . PHE B 1 455 ? 0.249   18.874  53.416  1.00 179.83 ?  454  PHE B CD1 1 
ATOM   6966 C  CD2 . PHE B 1 455 ? 0.052   18.625  55.778  1.00 164.10 ?  454  PHE B CD2 1 
ATOM   6967 C  CE1 . PHE B 1 455 ? 1.099   17.790  53.373  1.00 176.72 ?  454  PHE B CE1 1 
ATOM   6968 C  CE2 . PHE B 1 455 ? 0.903   17.537  55.740  1.00 161.20 ?  454  PHE B CE2 1 
ATOM   6969 C  CZ  . PHE B 1 455 ? 1.428   17.121  54.537  1.00 166.95 ?  454  PHE B CZ  1 
ATOM   6970 N  N   . PHE B 1 456 ? -3.347  19.315  56.599  1.00 166.97 ?  455  PHE B N   1 
ATOM   6971 C  CA  . PHE B 1 456 ? -3.613  18.309  57.618  1.00 148.86 ?  455  PHE B CA  1 
ATOM   6972 C  C   . PHE B 1 456 ? -4.836  17.476  57.247  1.00 135.39 ?  455  PHE B C   1 
ATOM   6973 O  O   . PHE B 1 456 ? -4.880  16.281  57.528  1.00 124.24 ?  455  PHE B O   1 
ATOM   6974 C  CB  . PHE B 1 456 ? -3.796  18.928  59.006  1.00 166.81 ?  455  PHE B CB  1 
ATOM   6975 C  CG  . PHE B 1 456 ? -3.467  17.973  60.128  1.00 167.58 ?  455  PHE B CG  1 
ATOM   6976 C  CD1 . PHE B 1 456 ? -2.248  17.312  60.148  1.00 161.53 ?  455  PHE B CD1 1 
ATOM   6977 C  CD2 . PHE B 1 456 ? -4.388  17.693  61.125  1.00 160.67 ?  455  PHE B CD2 1 
ATOM   6978 C  CE1 . PHE B 1 456 ? -1.939  16.430  61.151  1.00 153.92 ?  455  PHE B CE1 1 
ATOM   6979 C  CE2 . PHE B 1 456 ? -4.083  16.798  62.137  1.00 155.14 ?  455  PHE B CE2 1 
ATOM   6980 C  CZ  . PHE B 1 456 ? -2.858  16.168  62.148  1.00 154.94 ?  455  PHE B CZ  1 
ATOM   6981 N  N   . GLN B 1 457 ? -5.842  18.110  56.651  1.00 139.42 ?  456  GLN B N   1 
ATOM   6982 C  CA  . GLN B 1 457 ? -7.018  17.372  56.203  1.00 152.91 ?  456  GLN B CA  1 
ATOM   6983 C  C   . GLN B 1 457 ? -6.601  16.285  55.214  1.00 153.44 ?  456  GLN B C   1 
ATOM   6984 O  O   . GLN B 1 457 ? -7.173  15.205  55.212  1.00 127.46 ?  456  GLN B O   1 
ATOM   6985 C  CB  . GLN B 1 457 ? -8.043  18.295  55.529  1.00 168.34 ?  456  GLN B CB  1 
ATOM   6986 C  CG  . GLN B 1 457 ? -9.078  18.946  56.443  1.00 168.14 ?  456  GLN B CG  1 
ATOM   6987 C  CD  . GLN B 1 457 ? -10.200 19.624  55.655  1.00 163.81 ?  456  GLN B CD  1 
ATOM   6988 O  OE1 . GLN B 1 457 ? -10.194 19.630  54.421  1.00 139.04 ?  456  GLN B OE1 1 
ATOM   6989 N  NE2 . GLN B 1 457 ? -11.167 20.196  56.368  1.00 153.95 ?  456  GLN B NE2 1 
ATOM   6990 N  N   . LYS B 1 458 ? -5.590  16.564  54.394  1.00 162.78 ?  457  LYS B N   1 
ATOM   6991 C  CA  . LYS B 1 458 ? -5.074  15.576  53.445  1.00 157.46 ?  457  LYS B CA  1 
ATOM   6992 C  C   . LYS B 1 458 ? -4.355  14.417  54.141  1.00 142.01 ?  457  LYS B C   1 
ATOM   6993 O  O   . LYS B 1 458 ? -4.564  13.251  53.802  1.00 130.42 ?  457  LYS B O   1 
ATOM   6994 C  CB  . LYS B 1 458 ? -4.132  16.237  52.431  1.00 160.87 ?  457  LYS B CB  1 
ATOM   6995 C  CG  . LYS B 1 458 ? -3.469  15.244  51.487  1.00 163.80 ?  457  LYS B CG  1 
ATOM   6996 C  CD  . LYS B 1 458 ? -2.510  15.927  50.528  1.00 170.35 ?  457  LYS B CD  1 
ATOM   6997 C  CE  . LYS B 1 458 ? -1.810  14.913  49.631  1.00 170.57 ?  457  LYS B CE  1 
ATOM   6998 N  NZ  . LYS B 1 458 ? -0.902  15.564  48.640  1.00 173.27 ?  457  LYS B NZ  1 
ATOM   6999 N  N   . TRP B 1 459 ? -3.500  14.749  55.104  1.00 141.55 ?  458  TRP B N   1 
ATOM   7000 C  CA  . TRP B 1 459 ? -2.738  13.748  55.844  1.00 144.23 ?  458  TRP B CA  1 
ATOM   7001 C  C   . TRP B 1 459 ? -3.638  12.861  56.706  1.00 140.02 ?  458  TRP B C   1 
ATOM   7002 O  O   . TRP B 1 459 ? -3.347  11.682  56.918  1.00 119.19 ?  458  TRP B O   1 
ATOM   7003 C  CB  . TRP B 1 459 ? -1.680  14.419  56.711  1.00 137.13 ?  458  TRP B CB  1 
ATOM   7004 C  CG  . TRP B 1 459 ? -0.610  13.470  57.152  1.00 137.85 ?  458  TRP B CG  1 
ATOM   7005 C  CD1 . TRP B 1 459 ? 0.434   13.008  56.403  1.00 124.86 ?  458  TRP B CD1 1 
ATOM   7006 C  CD2 . TRP B 1 459 ? -0.474  12.868  58.446  1.00 134.31 ?  458  TRP B CD2 1 
ATOM   7007 N  NE1 . TRP B 1 459 ? 1.207   12.150  57.150  1.00 122.67 ?  458  TRP B NE1 1 
ATOM   7008 C  CE2 . TRP B 1 459 ? 0.671   12.049  58.409  1.00 135.10 ?  458  TRP B CE2 1 
ATOM   7009 C  CE3 . TRP B 1 459 ? -1.212  12.940  59.635  1.00 116.03 ?  458  TRP B CE3 1 
ATOM   7010 C  CZ2 . TRP B 1 459 ? 1.098   11.308  59.508  1.00 129.76 ?  458  TRP B CZ2 1 
ATOM   7011 C  CZ3 . TRP B 1 459 ? -0.788  12.203  60.726  1.00 113.15 ?  458  TRP B CZ3 1 
ATOM   7012 C  CH2 . TRP B 1 459 ? 0.356   11.397  60.654  1.00 131.16 ?  458  TRP B CH2 1 
ATOM   7013 N  N   . LYS B 1 460 ? -4.705  13.450  57.237  1.00 148.98 ?  459  LYS B N   1 
ATOM   7014 C  CA  . LYS B 1 460 ? -5.688  12.708  58.019  1.00 155.98 ?  459  LYS B CA  1 
ATOM   7015 C  C   . LYS B 1 460 ? -6.377  11.665  57.139  1.00 170.56 ?  459  LYS B C   1 
ATOM   7016 O  O   . LYS B 1 460 ? -6.615  10.540  57.572  1.00 162.28 ?  459  LYS B O   1 
ATOM   7017 C  CB  . LYS B 1 460 ? -6.719  13.650  58.647  1.00 143.69 ?  459  LYS B CB  1 
ATOM   7018 C  CG  . LYS B 1 460 ? -6.229  14.385  59.893  1.00 129.92 ?  459  LYS B CG  1 
ATOM   7019 C  CD  . LYS B 1 460 ? -7.316  15.290  60.465  1.00 132.26 ?  459  LYS B CD  1 
ATOM   7020 C  CE  . LYS B 1 460 ? -8.642  14.548  60.600  1.00 135.09 ?  459  LYS B CE  1 
ATOM   7021 N  NZ  . LYS B 1 460 ? -9.796  15.466  60.828  1.00 139.63 ?  459  LYS B NZ  1 
ATOM   7022 N  N   . GLU B 1 461 ? -6.720  12.046  55.910  1.00 185.22 ?  460  GLU B N   1 
ATOM   7023 C  CA  . GLU B 1 461 ? -7.337  11.099  54.986  1.00 184.44 ?  460  GLU B CA  1 
ATOM   7024 C  C   . GLU B 1 461 ? -6.370  9.975   54.661  1.00 167.31 ?  460  GLU B C   1 
ATOM   7025 O  O   . GLU B 1 461 ? -6.771  8.827   54.483  1.00 173.69 ?  460  GLU B O   1 
ATOM   7026 C  CB  . GLU B 1 461 ? -7.767  11.759  53.667  1.00 207.67 ?  460  GLU B CB  1 
ATOM   7027 C  CG  . GLU B 1 461 ? -8.540  13.079  53.710  1.00 213.86 ?  460  GLU B CG  1 
ATOM   7028 C  CD  . GLU B 1 461 ? -9.898  13.010  54.390  1.00 217.24 ?  460  GLU B CD  1 
ATOM   7029 O  OE1 . GLU B 1 461 ? -10.183 12.040  55.122  1.00 220.46 ?  460  GLU B OE1 1 
ATOM   7030 O  OE2 . GLU B 1 461 ? -10.715 13.921  54.145  1.00 218.74 ?  460  GLU B OE2 1 
ATOM   7031 N  N   . ARG B 1 462 ? -5.095  10.326  54.556  1.00 158.14 ?  461  ARG B N   1 
ATOM   7032 C  CA  . ARG B 1 462 ? -4.057  9.357   54.242  1.00 145.50 ?  461  ARG B CA  1 
ATOM   7033 C  C   . ARG B 1 462 ? -3.788  8.346   55.360  1.00 124.66 ?  461  ARG B C   1 
ATOM   7034 O  O   . ARG B 1 462 ? -3.616  7.158   55.093  1.00 119.70 ?  461  ARG B O   1 
ATOM   7035 C  CB  . ARG B 1 462 ? -2.755  10.079  53.888  1.00 157.03 ?  461  ARG B CB  1 
ATOM   7036 C  CG  . ARG B 1 462 ? -1.620  9.117   53.629  1.00 161.14 ?  461  ARG B CG  1 
ATOM   7037 C  CD  . ARG B 1 462 ? -1.955  8.182   52.474  1.00 150.08 ?  461  ARG B CD  1 
ATOM   7038 N  NE  . ARG B 1 462 ? -0.988  7.095   52.328  1.00 142.21 ?  461  ARG B NE  1 
ATOM   7039 C  CZ  . ARG B 1 462 ? 0.287   7.246   51.977  1.00 145.54 ?  461  ARG B CZ  1 
ATOM   7040 N  NH1 . ARG B 1 462 ? 0.783   8.454   51.736  1.00 157.40 ?  461  ARG B NH1 1 
ATOM   7041 N  NH2 . ARG B 1 462 ? 1.072   6.181   51.875  1.00 135.73 ?  461  ARG B NH2 1 
ATOM   7042 N  N   . HIS B 1 463 ? -3.768  8.803   56.608  1.00 130.46 ?  462  HIS B N   1 
ATOM   7043 C  CA  . HIS B 1 463 ? -3.206  7.980   57.680  1.00 124.61 ?  462  HIS B CA  1 
ATOM   7044 C  C   . HIS B 1 463 ? -4.081  7.703   58.905  1.00 121.00 ?  462  HIS B C   1 
ATOM   7045 O  O   . HIS B 1 463 ? -3.799  6.769   59.656  1.00 108.90 ?  462  HIS B O   1 
ATOM   7046 C  CB  . HIS B 1 463 ? -1.893  8.606   58.159  1.00 114.24 ?  462  HIS B CB  1 
ATOM   7047 C  CG  . HIS B 1 463 ? -0.716  8.272   57.299  1.00 116.85 ?  462  HIS B CG  1 
ATOM   7048 N  ND1 . HIS B 1 463 ? 0.452   9.003   57.314  1.00 128.38 ?  462  HIS B ND1 1 
ATOM   7049 C  CD2 . HIS B 1 463 ? -0.511  7.255   56.429  1.00 118.50 ?  462  HIS B CD2 1 
ATOM   7050 C  CE1 . HIS B 1 463 ? 1.318   8.464   56.474  1.00 134.56 ?  462  HIS B CE1 1 
ATOM   7051 N  NE2 . HIS B 1 463 ? 0.758   7.401   55.926  1.00 127.15 ?  462  HIS B NE2 1 
ATOM   7052 N  N   . GLN B 1 464 ? -5.137  8.481   59.118  1.00 123.00 ?  463  GLN B N   1 
ATOM   7053 C  CA  . GLN B 1 464 ? -5.895  8.332   60.357  1.00 128.12 ?  463  GLN B CA  1 
ATOM   7054 C  C   . GLN B 1 464 ? -6.832  7.136   60.303  1.00 133.81 ?  463  GLN B C   1 
ATOM   7055 O  O   . GLN B 1 464 ? -7.571  6.943   59.335  1.00 134.39 ?  463  GLN B O   1 
ATOM   7056 C  CB  . GLN B 1 464 ? -6.690  9.598   60.674  1.00 131.97 ?  463  GLN B CB  1 
ATOM   7057 C  CG  . GLN B 1 464 ? -6.715  9.945   62.158  1.00 124.00 ?  463  GLN B CG  1 
ATOM   7058 C  CD  . GLN B 1 464 ? -7.667  11.082  62.479  1.00 129.98 ?  463  GLN B CD  1 
ATOM   7059 O  OE1 . GLN B 1 464 ? -8.429  11.531  61.623  1.00 147.95 ?  463  GLN B OE1 1 
ATOM   7060 N  NE2 . GLN B 1 464 ? -7.631  11.549  63.720  1.00 118.09 ?  463  GLN B NE2 1 
ATOM   7061 N  N   . VAL B 1 465 ? -6.794  6.348   61.371  1.00 136.60 ?  464  VAL B N   1 
ATOM   7062 C  CA  . VAL B 1 465 ? -7.649  5.183   61.529  1.00 118.76 ?  464  VAL B CA  1 
ATOM   7063 C  C   . VAL B 1 465 ? -8.647  5.474   62.633  1.00 107.53 ?  464  VAL B C   1 
ATOM   7064 O  O   . VAL B 1 465 ? -8.298  6.082   63.640  1.00 117.02 ?  464  VAL B O   1 
ATOM   7065 C  CB  . VAL B 1 465 ? -6.823  3.922   61.885  1.00 103.16 ?  464  VAL B CB  1 
ATOM   7066 C  CG1 . VAL B 1 465 ? -7.716  2.711   62.086  1.00 110.20 ?  464  VAL B CG1 1 
ATOM   7067 C  CG2 . VAL B 1 465 ? -5.763  3.650   60.825  1.00 105.29 ?  464  VAL B CG2 1 
ATOM   7068 N  N   . ARG B 1 466 ? -9.885  5.030   62.458  1.00 108.75 ?  465  ARG B N   1 
ATOM   7069 C  CA  . ARG B 1 466 ? -10.929 5.322   63.431  1.00 116.16 ?  465  ARG B CA  1 
ATOM   7070 C  C   . ARG B 1 466 ? -11.613 4.048   63.905  1.00 121.16 ?  465  ARG B C   1 
ATOM   7071 O  O   . ARG B 1 466 ? -11.656 3.048   63.189  1.00 130.65 ?  465  ARG B O   1 
ATOM   7072 C  CB  . ARG B 1 466 ? -11.949 6.307   62.860  1.00 110.84 ?  465  ARG B CB  1 
ATOM   7073 C  CG  . ARG B 1 466 ? -11.337 7.644   62.487  1.00 104.00 ?  465  ARG B CG  1 
ATOM   7074 C  CD  . ARG B 1 466 ? -12.397 8.723   62.316  1.00 133.09 ?  465  ARG B CD  1 
ATOM   7075 N  NE  . ARG B 1 466 ? -11.809 10.006  61.929  1.00 152.67 ?  465  ARG B NE  1 
ATOM   7076 C  CZ  . ARG B 1 466 ? -11.350 10.294  60.714  1.00 139.44 ?  465  ARG B CZ  1 
ATOM   7077 N  NH1 . ARG B 1 466 ? -11.399 9.387   59.746  1.00 132.59 ?  465  ARG B NH1 1 
ATOM   7078 N  NH2 . ARG B 1 466 ? -10.832 11.491  60.468  1.00 125.17 ?  465  ARG B NH2 1 
ATOM   7079 N  N   . TYR B 1 467 ? -12.136 4.087   65.125  1.00 116.92 ?  466  TYR B N   1 
ATOM   7080 C  CA  . TYR B 1 467 ? -12.744 2.907   65.720  1.00 114.62 ?  466  TYR B CA  1 
ATOM   7081 C  C   . TYR B 1 467 ? -14.107 3.149   66.348  1.00 118.90 ?  466  TYR B C   1 
ATOM   7082 O  O   . TYR B 1 467 ? -14.430 4.256   66.782  1.00 123.54 ?  466  TYR B O   1 
ATOM   7083 C  CB  . TYR B 1 467 ? -11.801 2.317   66.769  1.00 113.26 ?  466  TYR B CB  1 
ATOM   7084 C  CG  . TYR B 1 467 ? -11.373 3.301   67.832  1.00 124.83 ?  466  TYR B CG  1 
ATOM   7085 C  CD1 . TYR B 1 467 ? -12.156 3.534   68.956  1.00 129.07 ?  466  TYR B CD1 1 
ATOM   7086 C  CD2 . TYR B 1 467 ? -10.179 3.996   67.714  1.00 142.29 ?  466  TYR B CD2 1 
ATOM   7087 C  CE1 . TYR B 1 467 ? -11.763 4.434   69.925  1.00 142.27 ?  466  TYR B CE1 1 
ATOM   7088 C  CE2 . TYR B 1 467 ? -9.780  4.900   68.681  1.00 155.01 ?  466  TYR B CE2 1 
ATOM   7089 C  CZ  . TYR B 1 467 ? -10.574 5.113   69.785  1.00 158.48 ?  466  TYR B CZ  1 
ATOM   7090 O  OH  . TYR B 1 467 ? -10.180 6.011   70.753  1.00 189.45 ?  466  TYR B OH  1 
ATOM   7091 N  N   . THR B 1 468 ? -14.894 2.080   66.389  1.00 120.38 ?  467  THR B N   1 
ATOM   7092 C  CA  . THR B 1 468 ? -16.164 2.065   67.095  1.00 124.53 ?  467  THR B CA  1 
ATOM   7093 C  C   . THR B 1 468 ? -16.226 0.821   67.985  1.00 135.06 ?  467  THR B C   1 
ATOM   7094 O  O   . THR B 1 468 ? -15.748 -0.247  67.607  1.00 137.60 ?  467  THR B O   1 
ATOM   7095 C  CB  . THR B 1 468 ? -17.352 2.087   66.107  1.00 126.12 ?  467  THR B CB  1 
ATOM   7096 O  OG1 . THR B 1 468 ? -17.208 3.196   65.209  1.00 142.69 ?  467  THR B OG1 1 
ATOM   7097 C  CG2 . THR B 1 468 ? -18.679 2.200   66.849  1.00 118.80 ?  467  THR B CG2 1 
ATOM   7098 N  N   . PHE B 1 469 ? -16.786 0.976   69.179  1.00 129.31 ?  468  PHE B N   1 
ATOM   7099 C  CA  . PHE B 1 469 ? -16.851 -0.095  70.166  1.00 119.33 ?  468  PHE B CA  1 
ATOM   7100 C  C   . PHE B 1 469 ? -18.291 -0.296  70.623  1.00 130.01 ?  468  PHE B C   1 
ATOM   7101 O  O   . PHE B 1 469 ? -18.906 0.643   71.111  1.00 153.12 ?  468  PHE B O   1 
ATOM   7102 C  CB  . PHE B 1 469 ? -15.964 0.235   71.366  1.00 110.54 ?  468  PHE B CB  1 
ATOM   7103 C  CG  . PHE B 1 469 ? -14.569 -0.313  71.272  1.00 101.09 ?  468  PHE B CG  1 
ATOM   7104 C  CD1 . PHE B 1 469 ? -14.328 -1.666  71.445  1.00 100.16 ?  468  PHE B CD1 1 
ATOM   7105 C  CD2 . PHE B 1 469 ? -13.497 0.527   71.024  1.00 94.74  ?  468  PHE B CD2 1 
ATOM   7106 C  CE1 . PHE B 1 469 ? -13.039 -2.173  71.365  1.00 98.43  ?  468  PHE B CE1 1 
ATOM   7107 C  CE2 . PHE B 1 469 ? -12.212 0.029   70.943  1.00 94.23  ?  468  PHE B CE2 1 
ATOM   7108 C  CZ  . PHE B 1 469 ? -11.981 -1.322  71.116  1.00 98.22  ?  468  PHE B CZ  1 
ATOM   7109 N  N   . VAL B 1 470 ? -18.858 -1.484  70.437  1.00 130.48 ?  469  VAL B N   1 
ATOM   7110 C  CA  . VAL B 1 470 ? -20.180 -1.733  71.012  1.00 142.65 ?  469  VAL B CA  1 
ATOM   7111 C  C   . VAL B 1 470 ? -20.348 -3.104  71.670  1.00 154.89 ?  469  VAL B C   1 
ATOM   7112 O  O   . VAL B 1 470 ? -20.418 -4.135  71.006  1.00 160.30 ?  469  VAL B O   1 
ATOM   7113 C  CB  . VAL B 1 470 ? -21.287 -1.552  69.946  1.00 145.57 ?  469  VAL B CB  1 
ATOM   7114 C  CG1 . VAL B 1 470 ? -20.931 -2.287  68.653  1.00 139.60 ?  469  VAL B CG1 1 
ATOM   7115 C  CG2 . VAL B 1 470 ? -22.654 -1.982  70.493  1.00 151.61 ?  469  VAL B CG2 1 
ATOM   7116 N  N   . LYS B 1 471 ? -20.413 -3.081  72.998  1.00 165.09 ?  470  LYS B N   1 
ATOM   7117 C  CA  . LYS B 1 471 ? -20.837 -4.220  73.817  1.00 190.69 ?  470  LYS B CA  1 
ATOM   7118 C  C   . LYS B 1 471 ? -20.241 -5.616  73.463  1.00 191.00 ?  470  LYS B C   1 
ATOM   7119 O  O   . LYS B 1 471 ? -20.952 -6.614  73.546  1.00 204.46 ?  470  LYS B O   1 
ATOM   7120 C  CB  . LYS B 1 471 ? -22.378 -4.277  73.759  1.00 205.22 ?  470  LYS B CB  1 
ATOM   7121 C  CG  . LYS B 1 471 ? -23.080 -5.180  74.780  1.00 211.30 ?  470  LYS B CG  1 
ATOM   7122 C  CD  . LYS B 1 471 ? -24.587 -5.086  74.681  1.00 209.52 ?  470  LYS B CD  1 
ATOM   7123 C  CE  . LYS B 1 471 ? -25.257 -5.972  75.710  1.00 199.73 ?  470  LYS B CE  1 
ATOM   7124 N  NZ  . LYS B 1 471 ? -26.433 -5.312  76.324  1.00 190.30 ?  470  LYS B NZ  1 
ATOM   7125 N  N   . GLY B 1 472 ? -18.976 -5.732  73.057  1.00 178.34 ?  471  GLY B N   1 
ATOM   7126 C  CA  . GLY B 1 472 ? -17.955 -4.707  73.109  1.00 138.89 ?  471  GLY B CA  1 
ATOM   7127 C  C   . GLY B 1 472 ? -16.939 -5.193  72.103  1.00 128.12 ?  471  GLY B C   1 
ATOM   7128 O  O   . GLY B 1 472 ? -15.984 -5.880  72.450  1.00 102.39 ?  471  GLY B O   1 
ATOM   7129 N  N   . ASN B 1 473 ? -17.161 -4.859  70.837  1.00 144.92 ?  472  ASN B N   1 
ATOM   7130 C  CA  . ASN B 1 473 ? -16.259 -5.310  69.799  1.00 145.55 ?  472  ASN B CA  1 
ATOM   7131 C  C   . ASN B 1 473 ? -15.639 -4.146  69.063  1.00 140.62 ?  472  ASN B C   1 
ATOM   7132 O  O   . ASN B 1 473 ? -16.194 -3.050  69.043  1.00 139.06 ?  472  ASN B O   1 
ATOM   7133 C  CB  . ASN B 1 473 ? -17.021 -6.183  68.797  1.00 147.74 ?  472  ASN B CB  1 
ATOM   7134 C  CG  . ASN B 1 473 ? -17.388 -7.548  69.362  1.00 158.58 ?  472  ASN B CG  1 
ATOM   7135 O  OD1 . ASN B 1 473 ? -16.654 -8.529  69.209  1.00 175.05 ?  472  ASN B OD1 1 
ATOM   7136 N  ND2 . ASN B 1 473 ? -18.539 -7.612  70.022  1.00 151.71 ?  472  ASN B ND2 1 
ATOM   7137 N  N   . LEU B 1 474 ? -14.472 -4.389  68.483  1.00 127.23 ?  473  LEU B N   1 
ATOM   7138 C  CA  . LEU B 1 474 ? -13.743 -3.347  67.802  1.00 116.61 ?  473  LEU B CA  1 
ATOM   7139 C  C   . LEU B 1 474 ? -14.292 -3.183  66.395  1.00 129.16 ?  473  LEU B C   1 
ATOM   7140 O  O   . LEU B 1 474 ? -14.411 -4.166  65.667  1.00 135.29 ?  473  LEU B O   1 
ATOM   7141 C  CB  . LEU B 1 474 ? -12.263 -3.685  67.766  1.00 105.45 ?  473  LEU B CB  1 
ATOM   7142 C  CG  . LEU B 1 474 ? -11.337 -2.694  67.061  1.00 109.75 ?  473  LEU B CG  1 
ATOM   7143 C  CD1 . LEU B 1 474 ? -11.441 -1.327  67.697  1.00 108.14 ?  473  LEU B CD1 1 
ATOM   7144 C  CD2 . LEU B 1 474 ? -9.903  -3.196  67.110  1.00 108.76 ?  473  LEU B CD2 1 
ATOM   7145 N  N   . LYS B 1 475 ? -14.629 -1.964  65.994  1.00 127.66 ?  474  LYS B N   1 
ATOM   7146 C  CA  . LYS B 1 475 ? -14.909 -1.725  64.585  1.00 116.04 ?  474  LYS B CA  1 
ATOM   7147 C  C   . LYS B 1 475 ? -13.833 -0.853  63.992  1.00 110.60 ?  474  LYS B C   1 
ATOM   7148 O  O   . LYS B 1 475 ? -13.636 0.275   64.429  1.00 116.02 ?  474  LYS B O   1 
ATOM   7149 C  CB  . LYS B 1 475 ? -16.287 -1.095  64.392  1.00 121.08 ?  474  LYS B CB  1 
ATOM   7150 C  CG  . LYS B 1 475 ? -16.824 -1.250  62.977  1.00 133.90 ?  474  LYS B CG  1 
ATOM   7151 C  CD  . LYS B 1 475 ? -17.642 -2.526  62.871  1.00 141.91 ?  474  LYS B CD  1 
ATOM   7152 C  CE  . LYS B 1 475 ? -18.124 -2.786  61.442  1.00 145.29 ?  474  LYS B CE  1 
ATOM   7153 N  NZ  . LYS B 1 475 ? -17.004 -3.006  60.462  1.00 142.96 ?  474  LYS B NZ  1 
ATOM   7154 N  N   . LEU B 1 476 ? -13.136 -1.365  62.993  1.00 122.51 ?  475  LEU B N   1 
ATOM   7155 C  CA  . LEU B 1 476 ? -12.032 -0.613  62.431  1.00 137.53 ?  475  LEU B CA  1 
ATOM   7156 C  C   . LEU B 1 476 ? -12.420 0.119   61.147  1.00 145.56 ?  475  LEU B C   1 
ATOM   7157 O  O   . LEU B 1 476 ? -12.728 -0.498  60.127  1.00 155.56 ?  475  LEU B O   1 
ATOM   7158 C  CB  . LEU B 1 476 ? -10.855 -1.550  62.172  1.00 135.56 ?  475  LEU B CB  1 
ATOM   7159 C  CG  . LEU B 1 476 ? -9.918  -1.742  63.361  1.00 118.10 ?  475  LEU B CG  1 
ATOM   7160 C  CD1 . LEU B 1 476 ? -8.628  -2.424  62.941  1.00 104.36 ?  475  LEU B CD1 1 
ATOM   7161 C  CD2 . LEU B 1 476 ? -9.622  -0.396  63.986  1.00 101.26 ?  475  LEU B CD2 1 
ATOM   7162 N  N   . GLU B 1 477 ? -12.405 1.445   61.208  1.00 141.13 ?  476  GLU B N   1 
ATOM   7163 C  CA  . GLU B 1 477 ? -12.559 2.261   60.015  1.00 147.60 ?  476  GLU B CA  1 
ATOM   7164 C  C   . GLU B 1 477 ? -11.183 2.542   59.436  1.00 134.51 ?  476  GLU B C   1 
ATOM   7165 O  O   . GLU B 1 477 ? -10.212 2.690   60.170  1.00 139.18 ?  476  GLU B O   1 
ATOM   7166 C  CB  . GLU B 1 477 ? -13.292 3.560   60.333  1.00 162.56 ?  476  GLU B CB  1 
ATOM   7167 C  CG  . GLU B 1 477 ? -14.599 3.354   61.090  1.00 174.45 ?  476  GLU B CG  1 
ATOM   7168 C  CD  . GLU B 1 477 ? -15.358 4.646   61.309  1.00 180.85 ?  476  GLU B CD  1 
ATOM   7169 O  OE1 . GLU B 1 477 ? -15.236 5.556   60.462  1.00 186.84 ?  476  GLU B OE1 1 
ATOM   7170 O  OE2 . GLU B 1 477 ? -16.084 4.748   62.320  1.00 176.90 ?  476  GLU B OE2 1 
ATOM   7171 N  N   . MET B 1 478 ? -11.091 2.632   58.121  1.00 135.73 ?  477  MET B N   1 
ATOM   7172 C  CA  . MET B 1 478 ? -9.782  2.763   57.503  1.00 145.18 ?  477  MET B CA  1 
ATOM   7173 C  C   . MET B 1 478 ? -9.677  3.993   56.619  1.00 148.74 ?  477  MET B C   1 
ATOM   7174 O  O   . MET B 1 478 ? -10.683 4.489   56.110  1.00 151.56 ?  477  MET B O   1 
ATOM   7175 C  CB  . MET B 1 478 ? -9.462  1.508   56.688  1.00 147.57 ?  477  MET B CB  1 
ATOM   7176 C  CG  . MET B 1 478 ? -9.199  0.281   57.534  1.00 135.91 ?  477  MET B CG  1 
ATOM   7177 S  SD  . MET B 1 478 ? -7.840  0.591   58.670  1.00 132.21 ?  477  MET B SD  1 
ATOM   7178 C  CE  . MET B 1 478 ? -6.438  0.231   57.614  1.00 112.78 ?  477  MET B CE  1 
ATOM   7179 N  N   . PRO B 1 479 ? -8.448  4.497   56.442  1.00 140.42 ?  478  PRO B N   1 
ATOM   7180 C  CA  . PRO B 1 479 ? -8.207  5.530   55.440  1.00 146.74 ?  478  PRO B CA  1 
ATOM   7181 C  C   . PRO B 1 479 ? -8.582  4.998   54.067  1.00 169.23 ?  478  PRO B C   1 
ATOM   7182 O  O   . PRO B 1 479 ? -8.334  3.821   53.801  1.00 181.74 ?  478  PRO B O   1 
ATOM   7183 C  CB  . PRO B 1 479 ? -6.701  5.786   55.563  1.00 135.72 ?  478  PRO B CB  1 
ATOM   7184 C  CG  . PRO B 1 479 ? -6.154  4.523   56.156  1.00 127.56 ?  478  PRO B CG  1 
ATOM   7185 C  CD  . PRO B 1 479 ? -7.206  4.117   57.136  1.00 128.20 ?  478  PRO B CD  1 
ATOM   7186 N  N   . SER B 1 480 ? -9.179  5.834   53.223  1.00 157.86 ?  479  SER B N   1 
ATOM   7187 C  CA  . SER B 1 480 ? -9.647  5.376   51.922  1.00 158.85 ?  479  SER B CA  1 
ATOM   7188 C  C   . SER B 1 480 ? -8.487  4.822   51.105  1.00 154.22 ?  479  SER B C   1 
ATOM   7189 O  O   . SER B 1 480 ? -7.413  5.422   51.060  1.00 150.90 ?  479  SER B O   1 
ATOM   7190 C  CB  . SER B 1 480 ? -10.343 6.510   51.165  1.00 161.89 ?  479  SER B CB  1 
ATOM   7191 O  OG  . SER B 1 480 ? -11.551 6.886   51.803  1.00 161.59 ?  479  SER B OG  1 
ATOM   7192 N  N   . PRO B 1 481 ? -8.704  3.667   50.460  1.00 141.87 ?  480  PRO B N   1 
ATOM   7193 C  CA  . PRO B 1 481 ? -7.685  3.000   49.643  1.00 134.84 ?  480  PRO B CA  1 
ATOM   7194 C  C   . PRO B 1 481 ? -7.274  3.848   48.443  1.00 136.33 ?  480  PRO B C   1 
ATOM   7195 O  O   . PRO B 1 481 ? -6.196  3.646   47.883  1.00 134.95 ?  480  PRO B O   1 
ATOM   7196 C  CB  . PRO B 1 481 ? -8.385  1.715   49.197  1.00 125.14 ?  480  PRO B CB  1 
ATOM   7197 C  CG  . PRO B 1 481 ? -9.839  2.049   49.244  1.00 124.51 ?  480  PRO B CG  1 
ATOM   7198 C  CD  . PRO B 1 481 ? -9.979  2.931   50.447  1.00 132.61 ?  480  PRO B CD  1 
ATOM   7199 N  N   . PHE B 1 482 ? -8.128  4.794   48.064  1.00 141.74 ?  481  PHE B N   1 
ATOM   7200 C  CA  . PHE B 1 482 ? -7.886  5.633   46.896  1.00 135.93 ?  481  PHE B CA  1 
ATOM   7201 C  C   . PHE B 1 482 ? -7.850  7.109   47.287  1.00 133.52 ?  481  PHE B C   1 
ATOM   7202 O  O   . PHE B 1 482 ? -8.547  7.542   48.208  1.00 115.62 ?  481  PHE B O   1 
ATOM   7203 C  CB  . PHE B 1 482 ? -8.964  5.400   45.834  1.00 111.82 ?  481  PHE B CB  1 
ATOM   7204 C  CG  . PHE B 1 482 ? -10.304 5.980   46.194  1.00 99.39  ?  481  PHE B CG  1 
ATOM   7205 C  CD1 . PHE B 1 482 ? -11.143 5.328   47.076  1.00 103.71 ?  481  PHE B CD1 1 
ATOM   7206 C  CD2 . PHE B 1 482 ? -10.723 7.181   45.648  1.00 95.41  ?  481  PHE B CD2 1 
ATOM   7207 C  CE1 . PHE B 1 482 ? -12.374 5.866   47.406  1.00 106.43 ?  481  PHE B CE1 1 
ATOM   7208 C  CE2 . PHE B 1 482 ? -11.955 7.721   45.974  1.00 95.89  ?  481  PHE B CE2 1 
ATOM   7209 C  CZ  . PHE B 1 482 ? -12.780 7.066   46.851  1.00 102.29 ?  481  PHE B CZ  1 
ATOM   7210 N  N   . SER B 1 483 ? -7.043  7.874   46.562  1.00 137.80 ?  482  SER B N   1 
ATOM   7211 C  CA  . SER B 1 483 ? -6.932  9.311   46.764  1.00 151.77 ?  482  SER B CA  1 
ATOM   7212 C  C   . SER B 1 483 ? -8.185  10.065  46.335  1.00 134.18 ?  482  SER B C   1 
ATOM   7213 O  O   . SER B 1 483 ? -8.860  9.676   45.384  1.00 137.32 ?  482  SER B O   1 
ATOM   7214 C  CB  . SER B 1 483 ? -5.737  9.848   45.979  1.00 190.03 ?  482  SER B CB  1 
ATOM   7215 O  OG  . SER B 1 483 ? -5.946  9.703   44.586  1.00 216.36 ?  482  SER B OG  1 
ATOM   7216 N  N   . VAL B 1 484 ? -8.486  11.156  47.033  1.00 113.08 ?  483  VAL B N   1 
ATOM   7217 C  CA  . VAL B 1 484 ? -9.474  12.113  46.546  1.00 106.56 ?  483  VAL B CA  1 
ATOM   7218 C  C   . VAL B 1 484 ? -8.738  13.354  46.028  1.00 105.15 ?  483  VAL B C   1 
ATOM   7219 O  O   . VAL B 1 484 ? -8.557  14.351  46.729  1.00 112.74 ?  483  VAL B O   1 
ATOM   7220 C  CB  . VAL B 1 484 ? -10.515 12.470  47.637  1.00 113.90 ?  483  VAL B CB  1 
ATOM   7221 C  CG1 . VAL B 1 484 ? -9.838  12.798  48.978  1.00 127.32 ?  483  VAL B CG1 1 
ATOM   7222 C  CG2 . VAL B 1 484 ? -11.448 13.587  47.166  1.00 87.30  ?  483  VAL B CG2 1 
ATOM   7223 N  N   . VAL B 1 485 ? -8.287  13.268  44.785  1.00 104.74 ?  484  VAL B N   1 
ATOM   7224 C  CA  . VAL B 1 485 ? -7.483  14.326  44.198  1.00 117.33 ?  484  VAL B CA  1 
ATOM   7225 C  C   . VAL B 1 485 ? -7.490  14.143  42.677  1.00 113.41 ?  484  VAL B C   1 
ATOM   7226 O  O   . VAL B 1 485 ? -7.911  13.096  42.181  1.00 112.99 ?  484  VAL B O   1 
ATOM   7227 C  CB  . VAL B 1 485 ? -6.035  14.302  44.766  1.00 105.32 ?  484  VAL B CB  1 
ATOM   7228 C  CG1 . VAL B 1 485 ? -5.276  13.090  44.250  1.00 88.90  ?  484  VAL B CG1 1 
ATOM   7229 C  CG2 . VAL B 1 485 ? -5.287  15.592  44.450  1.00 120.10 ?  484  VAL B CG2 1 
ATOM   7230 N  N   . ILE B 1 486 ? -7.069  15.167  41.938  1.00 102.40 ?  485  ILE B N   1 
ATOM   7231 C  CA  . ILE B 1 486 ? -6.887  15.038  40.497  1.00 104.75 ?  485  ILE B CA  1 
ATOM   7232 C  C   . ILE B 1 486 ? -5.858  13.957  40.200  1.00 108.47 ?  485  ILE B C   1 
ATOM   7233 O  O   . ILE B 1 486 ? -4.750  13.969  40.735  1.00 99.78  ?  485  ILE B O   1 
ATOM   7234 C  CB  . ILE B 1 486 ? -6.434  16.356  39.846  1.00 102.89 ?  485  ILE B CB  1 
ATOM   7235 C  CG1 . ILE B 1 486 ? -7.524  17.415  39.983  1.00 112.08 ?  485  ILE B CG1 1 
ATOM   7236 C  CG2 . ILE B 1 486 ? -6.111  16.144  38.376  1.00 89.49  ?  485  ILE B CG2 1 
ATOM   7237 C  CD1 . ILE B 1 486 ? -7.085  18.787  39.534  1.00 110.54 ?  485  ILE B CD1 1 
ATOM   7238 N  N   . GLN B 1 487 ? -6.238  13.007  39.357  1.00 120.98 ?  486  GLN B N   1 
ATOM   7239 C  CA  . GLN B 1 487 ? -5.351  11.905  39.032  1.00 125.82 ?  486  GLN B CA  1 
ATOM   7240 C  C   . GLN B 1 487 ? -5.105  11.746  37.534  1.00 122.23 ?  486  GLN B C   1 
ATOM   7241 O  O   . GLN B 1 487 ? -6.009  11.928  36.715  1.00 133.06 ?  486  GLN B O   1 
ATOM   7242 C  CB  . GLN B 1 487 ? -5.914  10.610  39.604  1.00 131.24 ?  486  GLN B CB  1 
ATOM   7243 C  CG  . GLN B 1 487 ? -4.960  9.445   39.533  1.00 137.58 ?  486  GLN B CG  1 
ATOM   7244 C  CD  . GLN B 1 487 ? -5.663  8.143   39.803  1.00 143.79 ?  486  GLN B CD  1 
ATOM   7245 O  OE1 . GLN B 1 487 ? -6.660  8.113   40.521  1.00 150.25 ?  486  GLN B OE1 1 
ATOM   7246 N  NE2 . GLN B 1 487 ? -5.163  7.060   39.220  1.00 143.01 ?  486  GLN B NE2 1 
ATOM   7247 N  N   . GLU B 1 488 ? -3.867  11.403  37.190  1.00 111.66 ?  487  GLU B N   1 
ATOM   7248 C  CA  . GLU B 1 488 ? -3.494  11.136  35.810  1.00 105.43 ?  487  GLU B CA  1 
ATOM   7249 C  C   . GLU B 1 488 ? -3.005  9.697   35.711  1.00 98.92  ?  487  GLU B C   1 
ATOM   7250 O  O   . GLU B 1 488 ? -2.271  9.228   36.579  1.00 120.62 ?  487  GLU B O   1 
ATOM   7251 C  CB  . GLU B 1 488 ? -2.418  12.108  35.339  1.00 113.33 ?  487  GLU B CB  1 
ATOM   7252 C  CG  . GLU B 1 488 ? -2.329  12.245  33.840  1.00 117.59 ?  487  GLU B CG  1 
ATOM   7253 C  CD  . GLU B 1 488 ? -0.909  12.268  33.347  1.00 116.57 ?  487  GLU B CD  1 
ATOM   7254 O  OE1 . GLU B 1 488 ? -0.022  12.630  34.141  1.00 102.16 ?  487  GLU B OE1 1 
ATOM   7255 O  OE2 . GLU B 1 488 ? -0.684  11.958  32.159  1.00 127.15 ?  487  GLU B OE2 1 
ATOM   7256 N  N   . SER B 1 489 ? -3.388  9.004   34.646  1.00 89.96  ?  488  SER B N   1 
ATOM   7257 C  CA  . SER B 1 489 ? -3.128  7.573   34.547  1.00 101.58 ?  488  SER B CA  1 
ATOM   7258 C  C   . SER B 1 489 ? -2.202  7.203   33.398  1.00 100.75 ?  488  SER B C   1 
ATOM   7259 O  O   . SER B 1 489 ? -2.023  7.966   32.450  1.00 113.15 ?  488  SER B O   1 
ATOM   7260 C  CB  . SER B 1 489 ? -4.449  6.806   34.406  1.00 118.96 ?  488  SER B CB  1 
ATOM   7261 O  OG  . SER B 1 489 ? -5.286  7.015   35.535  1.00 136.25 ?  488  SER B OG  1 
ATOM   7262 N  N   . GLU B 1 490 ? -1.610  6.020   33.512  1.00 90.69  ?  489  GLU B N   1 
ATOM   7263 C  CA  . GLU B 1 490 ? -0.693  5.476   32.519  1.00 106.73 ?  489  GLU B CA  1 
ATOM   7264 C  C   . GLU B 1 490 ? -1.430  5.121   31.224  1.00 121.21 ?  489  GLU B C   1 
ATOM   7265 O  O   . GLU B 1 490 ? -0.809  4.956   30.174  1.00 119.71 ?  489  GLU B O   1 
ATOM   7266 C  CB  . GLU B 1 490 ? 0.036   4.251   33.076  1.00 119.81 ?  489  GLU B CB  1 
ATOM   7267 C  CG  . GLU B 1 490 ? -0.880  3.128   33.533  1.00 131.71 ?  489  GLU B CG  1 
ATOM   7268 C  CD  . GLU B 1 490 ? -0.115  1.869   33.900  1.00 142.10 ?  489  GLU B CD  1 
ATOM   7269 O  OE1 . GLU B 1 490 ? 1.010   1.687   33.389  1.00 141.96 ?  489  GLU B OE1 1 
ATOM   7270 O  OE2 . GLU B 1 490 ? -0.638  1.058   34.696  1.00 150.27 ?  489  GLU B OE2 1 
ATOM   7271 N  N   . LYS B 1 491 ? -2.752  4.994   31.310  1.00 132.94 ?  490  LYS B N   1 
ATOM   7272 C  CA  . LYS B 1 491 ? -3.588  4.778   30.132  1.00 142.85 ?  490  LYS B CA  1 
ATOM   7273 C  C   . LYS B 1 491 ? -3.942  6.137   29.510  1.00 148.80 ?  490  LYS B C   1 
ATOM   7274 O  O   . LYS B 1 491 ? -4.817  6.251   28.649  1.00 159.45 ?  490  LYS B O   1 
ATOM   7275 C  CB  . LYS B 1 491 ? -4.846  3.983   30.524  1.00 142.94 ?  490  LYS B CB  1 
ATOM   7276 C  CG  . LYS B 1 491 ? -5.801  3.580   29.387  1.00 152.94 ?  490  LYS B CG  1 
ATOM   7277 C  CD  . LYS B 1 491 ? -5.116  2.821   28.251  1.00 139.36 ?  490  LYS B CD  1 
ATOM   7278 C  CE  . LYS B 1 491 ? -6.117  2.468   27.149  1.00 120.96 ?  490  LYS B CE  1 
ATOM   7279 N  NZ  . LYS B 1 491 ? -5.478  1.811   25.973  1.00 123.15 ?  490  LYS B NZ  1 
ATOM   7280 N  N   . GLY B 1 492 ? -3.223  7.167   29.944  1.00 140.24 ?  491  GLY B N   1 
ATOM   7281 C  CA  . GLY B 1 492 ? -3.488  8.523   29.511  1.00 132.53 ?  491  GLY B CA  1 
ATOM   7282 C  C   . GLY B 1 492 ? -4.879  8.966   29.904  1.00 124.35 ?  491  GLY B C   1 
ATOM   7283 O  O   . GLY B 1 492 ? -5.619  9.508   29.084  1.00 144.68 ?  491  GLY B O   1 
ATOM   7284 N  N   . SER B 1 493 ? -5.236  8.754   31.165  1.00 104.49 ?  492  SER B N   1 
ATOM   7285 C  CA  . SER B 1 493 ? -6.599  9.015   31.601  1.00 101.29 ?  492  SER B CA  1 
ATOM   7286 C  C   . SER B 1 493 ? -6.597  9.994   32.759  1.00 95.29  ?  492  SER B C   1 
ATOM   7287 O  O   . SER B 1 493 ? -5.732  9.945   33.628  1.00 91.98  ?  492  SER B O   1 
ATOM   7288 C  CB  . SER B 1 493 ? -7.297  7.713   31.997  1.00 109.83 ?  492  SER B CB  1 
ATOM   7289 O  OG  . SER B 1 493 ? -7.317  6.799   30.915  1.00 109.16 ?  492  SER B OG  1 
ATOM   7290 N  N   . TRP B 1 494 ? -7.591  10.871  32.775  1.00 100.37 ?  493  TRP B N   1 
ATOM   7291 C  CA  . TRP B 1 494 ? -7.657  11.928  33.771  1.00 99.73  ?  493  TRP B CA  1 
ATOM   7292 C  C   . TRP B 1 494 ? -8.928  11.833  34.601  1.00 102.25 ?  493  TRP B C   1 
ATOM   7293 O  O   . TRP B 1 494 ? -10.028 11.735  34.059  1.00 119.23 ?  493  TRP B O   1 
ATOM   7294 C  CB  . TRP B 1 494 ? -7.578  13.296  33.088  1.00 96.17  ?  493  TRP B CB  1 
ATOM   7295 C  CG  . TRP B 1 494 ? -6.218  13.621  32.522  1.00 102.13 ?  493  TRP B CG  1 
ATOM   7296 C  CD1 . TRP B 1 494 ? -5.666  13.127  31.372  1.00 108.92 ?  493  TRP B CD1 1 
ATOM   7297 C  CD2 . TRP B 1 494 ? -5.241  14.502  33.087  1.00 98.72  ?  493  TRP B CD2 1 
ATOM   7298 N  NE1 . TRP B 1 494 ? -4.408  13.651  31.187  1.00 107.19 ?  493  TRP B NE1 1 
ATOM   7299 C  CE2 . TRP B 1 494 ? -4.125  14.499  32.225  1.00 103.91 ?  493  TRP B CE2 1 
ATOM   7300 C  CE3 . TRP B 1 494 ? -5.201  15.294  34.237  1.00 93.43  ?  493  TRP B CE3 1 
ATOM   7301 C  CZ2 . TRP B 1 494 ? -2.984  15.255  32.480  1.00 109.46 ?  493  TRP B CZ2 1 
ATOM   7302 C  CZ3 . TRP B 1 494 ? -4.070  16.041  34.489  1.00 96.37  ?  493  TRP B CZ3 1 
ATOM   7303 C  CH2 . TRP B 1 494 ? -2.976  16.016  33.616  1.00 105.17 ?  493  TRP B CH2 1 
ATOM   7304 N  N   . HIS B 1 495 ? -8.773  11.854  35.919  1.00 90.48  ?  494  HIS B N   1 
ATOM   7305 C  CA  . HIS B 1 495 ? -9.916  11.782  36.816  1.00 79.25  ?  494  HIS B CA  1 
ATOM   7306 C  C   . HIS B 1 495 ? -9.949  13.017  37.703  1.00 86.88  ?  494  HIS B C   1 
ATOM   7307 O  O   . HIS B 1 495 ? -8.949  13.374  38.326  1.00 88.06  ?  494  HIS B O   1 
ATOM   7308 C  CB  . HIS B 1 495 ? -9.861  10.515  37.661  1.00 87.55  ?  494  HIS B CB  1 
ATOM   7309 C  CG  . HIS B 1 495 ? -10.115 9.263   36.885  1.00 83.46  ?  494  HIS B CG  1 
ATOM   7310 N  ND1 . HIS B 1 495 ? -9.101  8.513   36.329  1.00 84.20  ?  494  HIS B ND1 1 
ATOM   7311 C  CD2 . HIS B 1 495 ? -11.269 8.631   36.567  1.00 117.54 ?  494  HIS B CD2 1 
ATOM   7312 C  CE1 . HIS B 1 495 ? -9.620  7.469   35.708  1.00 127.14 ?  494  HIS B CE1 1 
ATOM   7313 N  NE2 . HIS B 1 495 ? -10.934 7.518   35.837  1.00 127.21 ?  494  HIS B NE2 1 
ATOM   7314 N  N   . PHE B 1 496 ? -11.101 13.673  37.751  1.00 92.15  ?  495  PHE B N   1 
ATOM   7315 C  CA  . PHE B 1 496 ? -11.222 14.927  38.480  1.00 95.00  ?  495  PHE B CA  1 
ATOM   7316 C  C   . PHE B 1 496 ? -12.307 14.872  39.538  1.00 101.21 ?  495  PHE B C   1 
ATOM   7317 O  O   . PHE B 1 496 ? -13.474 14.632  39.231  1.00 106.64 ?  495  PHE B O   1 
ATOM   7318 C  CB  . PHE B 1 496 ? -11.503 16.088  37.517  1.00 99.82  ?  495  PHE B CB  1 
ATOM   7319 C  CG  . PHE B 1 496 ? -10.511 16.201  36.395  1.00 114.67 ?  495  PHE B CG  1 
ATOM   7320 C  CD1 . PHE B 1 496 ? -10.698 15.508  35.209  1.00 125.58 ?  495  PHE B CD1 1 
ATOM   7321 C  CD2 . PHE B 1 496 ? -9.385  17.001  36.529  1.00 111.58 ?  495  PHE B CD2 1 
ATOM   7322 C  CE1 . PHE B 1 496 ? -9.783  15.613  34.179  1.00 120.84 ?  495  PHE B CE1 1 
ATOM   7323 C  CE2 . PHE B 1 496 ? -8.465  17.108  35.504  1.00 108.38 ?  495  PHE B CE2 1 
ATOM   7324 C  CZ  . PHE B 1 496 ? -8.664  16.413  34.327  1.00 114.73 ?  495  PHE B CZ  1 
ATOM   7325 N  N   . PRO B 1 497 ? -11.916 15.086  40.801  1.00 99.88  ?  496  PRO B N   1 
ATOM   7326 C  CA  . PRO B 1 497 ? -12.906 15.215  41.870  1.00 88.91  ?  496  PRO B CA  1 
ATOM   7327 C  C   . PRO B 1 497 ? -13.590 16.582  41.821  1.00 88.62  ?  496  PRO B C   1 
ATOM   7328 O  O   . PRO B 1 497 ? -13.080 17.510  41.198  1.00 92.68  ?  496  PRO B O   1 
ATOM   7329 C  CB  . PRO B 1 497 ? -12.067 15.045  43.138  1.00 85.48  ?  496  PRO B CB  1 
ATOM   7330 C  CG  . PRO B 1 497 ? -10.710 15.511  42.756  1.00 92.16  ?  496  PRO B CG  1 
ATOM   7331 C  CD  . PRO B 1 497 ? -10.534 15.121  41.313  1.00 96.91  ?  496  PRO B CD  1 
ATOM   7332 N  N   . VAL B 1 498 ? -14.741 16.692  42.473  1.00 98.52  ?  497  VAL B N   1 
ATOM   7333 C  CA  . VAL B 1 498 ? -15.526 17.921  42.470  1.00 118.56 ?  497  VAL B CA  1 
ATOM   7334 C  C   . VAL B 1 498 ? -15.756 18.387  43.908  1.00 151.44 ?  497  VAL B C   1 
ATOM   7335 O  O   . VAL B 1 498 ? -15.843 17.568  44.822  1.00 171.74 ?  497  VAL B O   1 
ATOM   7336 C  CB  . VAL B 1 498 ? -16.876 17.716  41.739  1.00 116.02 ?  497  VAL B CB  1 
ATOM   7337 C  CG1 . VAL B 1 498 ? -17.700 18.994  41.722  1.00 116.95 ?  497  VAL B CG1 1 
ATOM   7338 C  CG2 . VAL B 1 498 ? -16.634 17.230  40.316  1.00 100.93 ?  497  VAL B CG2 1 
ATOM   7339 N  N   . SER B 1 499 ? -15.838 19.699  44.107  1.00 156.79 ?  498  SER B N   1 
ATOM   7340 C  CA  . SER B 1 499 ? -16.064 20.265  45.432  1.00 165.77 ?  498  SER B CA  1 
ATOM   7341 C  C   . SER B 1 499 ? -17.461 19.922  45.954  1.00 181.43 ?  498  SER B C   1 
ATOM   7342 O  O   . SER B 1 499 ? -18.385 19.695  45.170  1.00 180.49 ?  498  SER B O   1 
ATOM   7343 C  CB  . SER B 1 499 ? -15.868 21.782  45.391  1.00 166.55 ?  498  SER B CB  1 
ATOM   7344 O  OG  . SER B 1 499 ? -16.173 22.377  46.639  1.00 175.81 ?  498  SER B OG  1 
ATOM   7345 N  N   . CYS B 1 500 ? -17.602 19.873  47.278  1.00 186.67 ?  499  CYS B N   1 
ATOM   7346 C  CA  . CYS B 1 500 ? -18.857 19.484  47.923  1.00 185.80 ?  499  CYS B CA  1 
ATOM   7347 C  C   . CYS B 1 500 ? -19.978 20.473  47.610  1.00 187.40 ?  499  CYS B C   1 
ATOM   7348 O  O   . CYS B 1 500 ? -21.064 20.409  48.190  1.00 186.71 ?  499  CYS B O   1 
ATOM   7349 C  CB  . CYS B 1 500 ? -18.664 19.367  49.439  1.00 185.61 ?  499  CYS B CB  1 
ATOM   7350 S  SG  . CYS B 1 500 ? -19.993 18.502  50.328  1.00 228.65 ?  499  CYS B SG  1 
ATOM   7351 N  N   . SER B 1 506 ? -20.052 12.301  51.012  1.00 205.48 ?  505  SER B N   1 
ATOM   7352 C  CA  . SER B 1 506 ? -20.817 11.095  50.717  1.00 200.40 ?  505  SER B CA  1 
ATOM   7353 C  C   . SER B 1 506 ? -20.487 10.545  49.329  1.00 193.60 ?  505  SER B C   1 
ATOM   7354 O  O   . SER B 1 506 ? -19.349 10.167  49.051  1.00 185.53 ?  505  SER B O   1 
ATOM   7355 C  CB  . SER B 1 506 ? -22.320 11.378  50.828  1.00 202.19 ?  505  SER B CB  1 
ATOM   7356 O  OG  . SER B 1 506 ? -22.765 12.228  49.783  1.00 196.51 ?  505  SER B OG  1 
ATOM   7357 N  N   . SER B 1 507 ? -21.498 10.504  48.468  1.00 202.83 ?  506  SER B N   1 
ATOM   7358 C  CA  . SER B 1 507 ? -21.375 9.980   47.110  1.00 198.82 ?  506  SER B CA  1 
ATOM   7359 C  C   . SER B 1 507 ? -20.870 11.047  46.142  1.00 191.35 ?  506  SER B C   1 
ATOM   7360 O  O   . SER B 1 507 ? -21.655 11.685  45.439  1.00 193.30 ?  506  SER B O   1 
ATOM   7361 C  CB  . SER B 1 507 ? -22.710 9.412   46.627  1.00 207.47 ?  506  SER B CB  1 
ATOM   7362 O  OG  . SER B 1 507 ? -23.108 8.310   47.425  1.00 216.22 ?  506  SER B OG  1 
ATOM   7363 N  N   . ARG B 1 508 ? -19.555 11.245  46.127  1.00 187.07 ?  507  ARG B N   1 
ATOM   7364 C  CA  . ARG B 1 508 ? -18.927 12.292  45.325  1.00 179.02 ?  507  ARG B CA  1 
ATOM   7365 C  C   . ARG B 1 508 ? -19.125 12.100  43.824  1.00 161.09 ?  507  ARG B C   1 
ATOM   7366 O  O   . ARG B 1 508 ? -19.207 10.976  43.329  1.00 151.06 ?  507  ARG B O   1 
ATOM   7367 C  CB  . ARG B 1 508 ? -17.425 12.347  45.626  1.00 180.24 ?  507  ARG B CB  1 
ATOM   7368 C  CG  . ARG B 1 508 ? -16.677 13.484  44.938  1.00 170.33 ?  507  ARG B CG  1 
ATOM   7369 C  CD  . ARG B 1 508 ? -15.193 13.446  45.254  1.00 168.82 ?  507  ARG B CD  1 
ATOM   7370 N  NE  . ARG B 1 508 ? -14.918 13.677  46.667  1.00 167.89 ?  507  ARG B NE  1 
ATOM   7371 C  CZ  . ARG B 1 508 ? -14.783 14.880  47.214  1.00 158.45 ?  507  ARG B CZ  1 
ATOM   7372 N  NH1 . ARG B 1 508 ? -14.894 15.968  46.465  1.00 153.27 ?  507  ARG B NH1 1 
ATOM   7373 N  NH2 . ARG B 1 508 ? -14.534 14.995  48.511  1.00 156.44 ?  507  ARG B NH2 1 
ATOM   7374 N  N   . THR B 1 509 ? -19.207 13.219  43.111  1.00 155.71 ?  508  THR B N   1 
ATOM   7375 C  CA  . THR B 1 509 ? -19.333 13.208  41.661  1.00 150.56 ?  508  THR B CA  1 
ATOM   7376 C  C   . THR B 1 509 ? -17.964 13.460  41.039  1.00 123.55 ?  508  THR B C   1 
ATOM   7377 O  O   . THR B 1 509 ? -17.221 14.329  41.490  1.00 103.06 ?  508  THR B O   1 
ATOM   7378 C  CB  . THR B 1 509 ? -20.333 14.273  41.170  1.00 159.66 ?  508  THR B CB  1 
ATOM   7379 O  OG1 . THR B 1 509 ? -21.542 14.188  41.935  1.00 165.45 ?  508  THR B OG1 1 
ATOM   7380 C  CG2 . THR B 1 509 ? -20.654 14.073  39.698  1.00 159.89 ?  508  THR B CG2 1 
ATOM   7381 N  N   . TRP B 1 510 ? -17.639 12.694  40.004  1.00 112.88 ?  509  TRP B N   1 
ATOM   7382 C  CA  . TRP B 1 510 ? -16.326 12.759  39.375  1.00 104.13 ?  509  TRP B CA  1 
ATOM   7383 C  C   . TRP B 1 510 ? -16.423 13.017  37.887  1.00 114.47 ?  509  TRP B C   1 
ATOM   7384 O  O   . TRP B 1 510 ? -17.498 12.923  37.298  1.00 131.35 ?  509  TRP B O   1 
ATOM   7385 C  CB  . TRP B 1 510 ? -15.564 11.454  39.605  1.00 111.89 ?  509  TRP B CB  1 
ATOM   7386 C  CG  . TRP B 1 510 ? -15.011 11.298  40.983  1.00 126.35 ?  509  TRP B CG  1 
ATOM   7387 C  CD1 . TRP B 1 510 ? -15.708 11.008  42.119  1.00 135.54 ?  509  TRP B CD1 1 
ATOM   7388 C  CD2 . TRP B 1 510 ? -13.634 11.380  41.367  1.00 108.41 ?  509  TRP B CD2 1 
ATOM   7389 N  NE1 . TRP B 1 510 ? -14.853 10.929  43.191  1.00 122.90 ?  509  TRP B NE1 1 
ATOM   7390 C  CE2 . TRP B 1 510 ? -13.574 11.151  42.755  1.00 107.61 ?  509  TRP B CE2 1 
ATOM   7391 C  CE3 . TRP B 1 510 ? -12.448 11.635  40.674  1.00 100.03 ?  509  TRP B CE3 1 
ATOM   7392 C  CZ2 . TRP B 1 510 ? -12.374 11.169  43.462  1.00 103.14 ?  509  TRP B CZ2 1 
ATOM   7393 C  CZ3 . TRP B 1 510 ? -11.261 11.652  41.376  1.00 95.25  ?  509  TRP B CZ3 1 
ATOM   7394 C  CH2 . TRP B 1 510 ? -11.232 11.423  42.756  1.00 96.88  ?  509  TRP B CH2 1 
ATOM   7395 N  N   . MET B 1 511 ? -15.285 13.337  37.282  1.00 120.56 ?  510  MET B N   1 
ATOM   7396 C  CA  . MET B 1 511 ? -15.193 13.409  35.834  1.00 136.58 ?  510  MET B CA  1 
ATOM   7397 C  C   . MET B 1 511 ? -14.144 12.407  35.364  1.00 119.29 ?  510  MET B C   1 
ATOM   7398 O  O   . MET B 1 511 ? -13.061 12.305  35.946  1.00 100.91 ?  510  MET B O   1 
ATOM   7399 C  CB  . MET B 1 511 ? -14.843 14.827  35.370  1.00 164.22 ?  510  MET B CB  1 
ATOM   7400 C  CG  . MET B 1 511 ? -14.681 14.957  33.856  1.00 177.43 ?  510  MET B CG  1 
ATOM   7401 S  SD  . MET B 1 511 ? -14.236 16.611  33.267  1.00 135.30 ?  510  MET B SD  1 
ATOM   7402 C  CE  . MET B 1 511 ? -15.852 17.350  33.040  1.00 87.27  ?  510  MET B CE  1 
ATOM   7403 N  N   . CYS B 1 512 ? -14.479 11.664  34.315  1.00 118.34 ?  511  CYS B N   1 
ATOM   7404 C  CA  . CYS B 1 512 ? -13.582 10.653  33.774  1.00 112.00 ?  511  CYS B CA  1 
ATOM   7405 C  C   . CYS B 1 512 ? -13.215 10.960  32.328  1.00 109.29 ?  511  CYS B C   1 
ATOM   7406 O  O   . CYS B 1 512 ? -14.077 11.283  31.515  1.00 120.89 ?  511  CYS B O   1 
ATOM   7407 C  CB  . CYS B 1 512 ? -14.220 9.268   33.864  1.00 113.54 ?  511  CYS B CB  1 
ATOM   7408 S  SG  . CYS B 1 512 ? -13.185 7.935   33.216  1.00 149.27 ?  511  CYS B SG  1 
ATOM   7409 N  N   . ILE B 1 513 ? -11.929 10.866  32.014  1.00 92.64  ?  512  ILE B N   1 
ATOM   7410 C  CA  . ILE B 1 513 ? -11.452 11.116  30.662  1.00 82.97  ?  512  ILE B CA  1 
ATOM   7411 C  C   . ILE B 1 513 ? -10.671 9.901   30.157  1.00 84.83  ?  512  ILE B C   1 
ATOM   7412 O  O   . ILE B 1 513 ? -9.684  9.493   30.768  1.00 100.89 ?  512  ILE B O   1 
ATOM   7413 C  CB  . ILE B 1 513 ? -10.591 12.403  30.605  1.00 80.59  ?  512  ILE B CB  1 
ATOM   7414 C  CG1 . ILE B 1 513 ? -11.472 13.618  30.301  1.00 79.62  ?  512  ILE B CG1 1 
ATOM   7415 C  CG2 . ILE B 1 513 ? -9.495  12.295  29.561  1.00 81.20  ?  512  ILE B CG2 1 
ATOM   7416 C  CD1 . ILE B 1 513 ? -12.254 14.119  31.474  1.00 78.58  ?  512  ILE B CD1 1 
ATOM   7417 N  N   . SER B 1 514 ? -11.127 9.314   29.053  1.00 93.55  ?  513  SER B N   1 
ATOM   7418 C  CA  . SER B 1 514 ? -10.515 8.093   28.533  1.00 104.39 ?  513  SER B CA  1 
ATOM   7419 C  C   . SER B 1 514 ? -10.200 8.174   27.038  1.00 109.53 ?  513  SER B C   1 
ATOM   7420 O  O   . SER B 1 514 ? -11.019 8.644   26.252  1.00 110.24 ?  513  SER B O   1 
ATOM   7421 C  CB  . SER B 1 514 ? -11.436 6.901   28.798  1.00 118.99 ?  513  SER B CB  1 
ATOM   7422 O  OG  . SER B 1 514 ? -11.931 6.929   30.125  1.00 125.35 ?  513  SER B OG  1 
ATOM   7423 N  N   . ARG B 1 515 ? -9.015  7.711   26.648  1.00 108.81 ?  514  ARG B N   1 
ATOM   7424 C  CA  . ARG B 1 515 ? -8.661  7.626   25.234  1.00 118.56 ?  514  ARG B CA  1 
ATOM   7425 C  C   . ARG B 1 515 ? -8.467  6.191   24.737  1.00 137.10 ?  514  ARG B C   1 
ATOM   7426 O  O   . ARG B 1 515 ? -7.623  5.463   25.255  1.00 142.65 ?  514  ARG B O   1 
ATOM   7427 C  CB  . ARG B 1 515 ? -7.387  8.415   24.951  1.00 121.22 ?  514  ARG B CB  1 
ATOM   7428 C  CG  . ARG B 1 515 ? -7.078  8.536   23.467  1.00 140.89 ?  514  ARG B CG  1 
ATOM   7429 C  CD  . ARG B 1 515 ? -5.747  9.225   23.211  1.00 147.64 ?  514  ARG B CD  1 
ATOM   7430 N  NE  . ARG B 1 515 ? -5.770  10.676  23.377  1.00 148.30 ?  514  ARG B NE  1 
ATOM   7431 C  CZ  . ARG B 1 515 ? -5.820  11.538  22.366  1.00 154.76 ?  514  ARG B CZ  1 
ATOM   7432 N  NH1 . ARG B 1 515 ? -5.852  11.090  21.119  1.00 163.78 ?  514  ARG B NH1 1 
ATOM   7433 N  NH2 . ARG B 1 515 ? -5.827  12.845  22.593  1.00 154.90 ?  514  ARG B NH2 1 
ATOM   7434 N  N   . GLN B 1 516 ? -9.246  5.793   23.735  1.00 151.07 ?  515  GLN B N   1 
ATOM   7435 C  CA  . GLN B 1 516 ? -9.105  4.473   23.125  1.00 156.98 ?  515  GLN B CA  1 
ATOM   7436 C  C   . GLN B 1 516 ? -9.792  4.428   21.764  1.00 154.68 ?  515  GLN B C   1 
ATOM   7437 O  O   . GLN B 1 516 ? -10.943 4.009   21.653  1.00 150.28 ?  515  GLN B O   1 
ATOM   7438 C  CB  . GLN B 1 516 ? -9.668  3.380   24.036  1.00 166.14 ?  515  GLN B CB  1 
ATOM   7439 C  CG  . GLN B 1 516 ? -8.657  2.289   24.397  1.00 170.32 ?  515  GLN B CG  1 
ATOM   7440 C  CD  . GLN B 1 516 ? -8.160  1.508   23.191  1.00 177.54 ?  515  GLN B CD  1 
ATOM   7441 O  OE1 . GLN B 1 516 ? -8.788  1.503   22.131  1.00 181.57 ?  515  GLN B OE1 1 
ATOM   7442 N  NE2 . GLN B 1 516 ? -7.024  0.837   23.351  1.00 174.92 ?  515  GLN B NE2 1 
HETATM 7443 ZN ZN  . ZN  C 2 .   ? 29.152  12.567  29.293  1.00 113.23 ?  1001 ZN  A ZN  1 
HETATM 7444 ZN ZN  . ZN  D 2 .   ? -12.766 6.466   34.953  1.00 106.12 ?  1001 ZN  B ZN  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   . ASN A 29  ? 3.6251 2.5242 2.4129 -0.8381 -0.5314 0.8582  28   ASN A N   
2    C  CA  . ASN A 29  ? 3.6421 2.4725 2.4799 -0.7820 -0.5578 0.8388  28   ASN A CA  
3    C  C   . ASN A 29  ? 3.5799 2.4328 2.4450 -0.7671 -0.5261 0.8007  28   ASN A C   
4    O  O   . ASN A 29  ? 3.6391 2.5632 2.4930 -0.7657 -0.4871 0.7787  28   ASN A O   
5    C  CB  . ASN A 29  ? 3.6572 2.4759 2.5021 -0.7316 -0.5767 0.8322  28   ASN A CB  
6    C  CG  . ASN A 29  ? 3.6239 2.3701 2.5230 -0.6727 -0.6041 0.8119  28   ASN A CG  
7    O  OD1 . ASN A 29  ? 3.6482 2.3835 2.5743 -0.6534 -0.5897 0.7810  28   ASN A OD1 
8    N  ND2 . ASN A 29  ? 3.6068 2.3041 2.5234 -0.6448 -0.6437 0.8285  28   ASN A ND2 
9    N  N   . PRO A 30  ? 3.3482 2.1396 2.2493 -0.7577 -0.5437 0.7924  29   PRO A N   
10   C  CA  . PRO A 30  ? 3.1350 1.9379 2.0639 -0.7469 -0.5208 0.7583  29   PRO A CA  
11   C  C   . PRO A 30  ? 2.9694 1.7823 1.9142 -0.6912 -0.5102 0.7223  29   PRO A C   
12   O  O   . PRO A 30  ? 2.9072 1.7727 1.8561 -0.6911 -0.4769 0.6982  29   PRO A O   
13   C  CB  . PRO A 30  ? 3.2749 1.9910 2.2346 -0.7441 -0.5534 0.7589  29   PRO A CB  
14   C  CG  . PRO A 30  ? 3.3398 2.0203 2.2815 -0.7747 -0.5825 0.8005  29   PRO A CG  
15   C  CD  . PRO A 30  ? 3.3335 2.0397 2.2491 -0.7621 -0.5873 0.8165  29   PRO A CD  
16   N  N   . GLU A 31  ? 3.1122 1.8764 2.0692 -0.6451 -0.5389 0.7197  30   GLU A N   
17   C  CA  . GLU A 31  ? 3.1490 1.9168 2.1231 -0.5898 -0.5328 0.6864  30   GLU A CA  
18   C  C   . GLU A 31  ? 3.1718 2.0257 2.1164 -0.5906 -0.4999 0.6799  30   GLU A C   
19   O  O   . GLU A 31  ? 3.2505 2.1343 2.2024 -0.5639 -0.4777 0.6490  30   GLU A O   
20   C  CB  . GLU A 31  ? 3.2164 1.9171 2.2168 -0.5433 -0.5712 0.6880  30   GLU A CB  
21   C  CG  . GLU A 31  ? 3.3462 1.9581 2.3784 -0.5389 -0.6027 0.6908  30   GLU A CG  
22   C  CD  . GLU A 31  ? 3.4831 2.0337 2.5494 -0.4924 -0.6379 0.6925  30   GLU A CD  
23   O  OE1 . GLU A 31  ? 3.5256 2.1049 2.5865 -0.4744 -0.6439 0.7035  30   GLU A OE1 
24   O  OE2 . GLU A 31  ? 3.5910 2.0665 2.6923 -0.4747 -0.6591 0.6820  30   GLU A OE2 
25   N  N   . THR A 32  ? 3.4360 2.3276 2.3454 -0.6219 -0.4971 0.7076  31   THR A N   
26   C  CA  . THR A 32  ? 3.4023 2.3741 2.2796 -0.6264 -0.4651 0.6996  31   THR A CA  
27   C  C   . THR A 32  ? 3.5904 2.6315 2.4579 -0.6582 -0.4177 0.6840  31   THR A C   
28   O  O   . THR A 32  ? 3.4958 2.5991 2.3518 -0.6486 -0.3846 0.6615  31   THR A O   
29   C  CB  . THR A 32  ? 3.3567 2.3486 2.1943 -0.6576 -0.4746 0.7321  31   THR A CB  
30   O  OG1 . THR A 32  ? 3.4764 2.4742 2.2936 -0.7150 -0.4699 0.7585  31   THR A OG1 
31   C  CG2 . THR A 32  ? 3.4042 2.3316 2.2585 -0.6267 -0.5236 0.7507  31   THR A CG2 
32   N  N   . ASN A 33  ? 4.0239 3.0554 2.9002 -0.6964 -0.4148 0.6959  32   ASN A N   
33   C  CA  . ASN A 33  ? 4.1164 3.2111 2.9988 -0.7266 -0.3727 0.6824  32   ASN A CA  
34   C  C   . ASN A 33  ? 3.9488 3.0364 2.8651 -0.6884 -0.3654 0.6487  32   ASN A C   
35   O  O   . ASN A 33  ? 3.9413 3.0978 2.8661 -0.6915 -0.3268 0.6268  32   ASN A O   
36   C  CB  . ASN A 33  ? 4.3064 3.3894 3.1968 -0.7769 -0.3765 0.7047  32   ASN A CB  
37   C  CG  . ASN A 33  ? 4.4966 3.6066 3.3479 -0.8252 -0.3726 0.7365  32   ASN A CG  
38   O  OD1 . ASN A 33  ? 4.5740 3.6892 3.3922 -0.8189 -0.3802 0.7466  32   ASN A OD1 
39   N  ND2 . ASN A 33  ? 4.5600 3.6884 3.4147 -0.8758 -0.3617 0.7524  32   ASN A ND2 
40   N  N   . LEU A 34  ? 3.4659 2.4724 2.4066 -0.6510 -0.4018 0.6411  33   LEU A N   
41   C  CA  . LEU A 34  ? 2.9328 1.9286 1.9098 -0.6091 -0.3986 0.6023  33   LEU A CA  
42   C  C   . LEU A 34  ? 2.7167 1.7643 1.7009 -0.5602 -0.3789 0.5677  33   LEU A C   
43   O  O   . LEU A 34  ? 2.8429 1.9430 1.8652 -0.5339 -0.3530 0.5253  33   LEU A O   
44   C  CB  . LEU A 34  ? 2.8387 1.7283 1.8338 -0.5835 -0.4414 0.6017  33   LEU A CB  
45   C  CG  . LEU A 34  ? 2.6094 1.4850 1.6495 -0.5290 -0.4414 0.5500  33   LEU A CG  
46   C  CD1 . LEU A 34  ? 2.6065 1.3924 1.6631 -0.5349 -0.4710 0.5496  33   LEU A CD1 
47   C  CD2 . LEU A 34  ? 2.3189 1.1786 1.3610 -0.4740 -0.4516 0.5346  33   LEU A CD2 
48   N  N   . LEU A 35  ? 2.6106 1.6424 1.5588 -0.5500 -0.3940 0.5880  34   LEU A N   
49   C  CA  . LEU A 35  ? 2.5851 1.6651 1.5355 -0.5087 -0.3773 0.5587  34   LEU A CA  
50   C  C   . LEU A 35  ? 2.5893 1.7708 1.5304 -0.5297 -0.3281 0.5423  34   LEU A C   
51   O  O   . LEU A 35  ? 2.5830 1.8172 1.5472 -0.4953 -0.3031 0.5028  34   LEU A O   
52   C  CB  . LEU A 35  ? 2.7538 1.7967 1.6728 -0.4966 -0.4085 0.5860  34   LEU A CB  
53   C  CG  . LEU A 35  ? 2.7143 1.7887 1.6353 -0.4516 -0.4018 0.5600  34   LEU A CG  
54   C  CD1 . LEU A 35  ? 2.7798 1.7934 1.7194 -0.4134 -0.4437 0.5689  34   LEU A CD1 
55   C  CD2 . LEU A 35  ? 2.6926 1.8422 1.5700 -0.4775 -0.3733 0.5643  34   LEU A CD2 
56   N  N   . PHE A 36  ? 2.6127 1.8201 1.5208 -0.5871 -0.3136 0.5722  35   PHE A N   
57   C  CA  . PHE A 36  ? 2.6816 1.9860 1.5876 -0.6116 -0.2622 0.5543  35   PHE A CA  
58   C  C   . PHE A 36  ? 2.9263 2.2783 1.9007 -0.5955 -0.2350 0.5142  35   PHE A C   
59   O  O   . PHE A 36  ? 2.9577 2.3807 1.9581 -0.5756 -0.1991 0.4778  35   PHE A O   
60   C  CB  . PHE A 36  ? 2.6829 2.0008 1.5399 -0.6810 -0.2524 0.5962  35   PHE A CB  
61   C  CG  . PHE A 36  ? 2.6052 2.0203 1.4793 -0.7119 -0.1965 0.5757  35   PHE A CG  
62   C  CD1 . PHE A 36  ? 2.5241 2.0110 1.3747 -0.7148 -0.1563 0.5550  35   PHE A CD1 
63   C  CD2 . PHE A 36  ? 2.7162 2.1512 1.6322 -0.7401 -0.1839 0.5770  35   PHE A CD2 
64   C  CE1 . PHE A 36  ? 2.5773 2.1540 1.4514 -0.7411 -0.1019 0.5328  35   PHE A CE1 
65   C  CE2 . PHE A 36  ? 2.7355 2.2647 1.6784 -0.7670 -0.1318 0.5580  35   PHE A CE2 
66   C  CZ  . PHE A 36  ? 2.6815 2.2815 1.6056 -0.7661 -0.0893 0.5348  35   PHE A CZ  
67   N  N   . ASN A 37  ? 3.1000 2.4100 2.1037 -0.6051 -0.2548 0.5219  36   ASN A N   
68   C  CA  . ASN A 37  ? 2.8232 2.1712 1.8910 -0.5933 -0.2381 0.4892  36   ASN A CA  
69   C  C   . ASN A 37  ? 2.5736 1.9176 1.6768 -0.5320 -0.2426 0.4473  36   ASN A C   
70   O  O   . ASN A 37  ? 2.5738 1.9799 1.7227 -0.5160 -0.2166 0.4150  36   ASN A O   
71   C  CB  . ASN A 37  ? 2.7971 2.0926 1.8793 -0.6229 -0.2636 0.5097  36   ASN A CB  
72   C  CG  . ASN A 37  ? 2.8164 2.1480 1.8869 -0.6879 -0.2457 0.5409  36   ASN A CG  
73   O  OD1 . ASN A 37  ? 2.7727 2.1893 1.8461 -0.7072 -0.2040 0.5343  36   ASN A OD1 
74   N  ND2 . ASN A 37  ? 2.8575 2.1246 1.9164 -0.7230 -0.2754 0.5735  36   ASN A ND2 
75   N  N   . LEU A 38  ? 2.3921 1.6637 1.4776 -0.4989 -0.2759 0.4490  37   LEU A N   
76   C  CA  . LEU A 38  ? 2.2917 1.5585 1.4043 -0.4431 -0.2791 0.4106  37   LEU A CA  
77   C  C   . LEU A 38  ? 2.2785 1.6157 1.3911 -0.4213 -0.2480 0.3877  37   LEU A C   
78   O  O   . LEU A 38  ? 1.9795 1.3550 1.1294 -0.3914 -0.2317 0.3524  37   LEU A O   
79   C  CB  . LEU A 38  ? 2.0011 1.1807 1.0978 -0.4137 -0.3177 0.4176  37   LEU A CB  
80   C  CG  . LEU A 38  ? 2.1103 1.2127 1.2237 -0.4119 -0.3471 0.4167  37   LEU A CG  
81   C  CD1 . LEU A 38  ? 2.1245 1.1620 1.2410 -0.3654 -0.3727 0.4032  37   LEU A CD1 
82   C  CD2 . LEU A 38  ? 1.9885 1.1242 1.1412 -0.4132 -0.3323 0.3872  37   LEU A CD2 
83   N  N   . ASN A 39  ? 2.4415 1.7919 1.5092 -0.4385 -0.2420 0.4087  38   ASN A N   
84   C  CA  . ASN A 39  ? 2.3273 1.7418 1.3871 -0.4246 -0.2115 0.3874  38   ASN A CA  
85   C  C   . ASN A 39  ? 2.2818 1.7802 1.3714 -0.4449 -0.1667 0.3686  38   ASN A C   
86   O  O   . ASN A 39  ? 2.2436 1.7950 1.3564 -0.4207 -0.1396 0.3358  38   ASN A O   
87   C  CB  . ASN A 39  ? 2.2108 1.6146 1.2069 -0.4449 -0.2194 0.4169  38   ASN A CB  
88   C  CG  . ASN A 39  ? 2.1075 1.4420 1.0872 -0.4141 -0.2619 0.4299  38   ASN A CG  
89   O  OD1 . ASN A 39  ? 2.0698 1.3569 1.0831 -0.3813 -0.2845 0.4183  38   ASN A OD1 
90   N  ND2 . ASN A 39  ? 2.2419 1.5716 1.1709 -0.4258 -0.2728 0.4535  38   ASN A ND2 
91   N  N   . SER A 40  ? 2.3134 1.8234 1.4072 -0.4893 -0.1591 0.3893  39   SER A N   
92   C  CA  . SER A 40  ? 2.2507 1.8429 1.3871 -0.5091 -0.1171 0.3722  39   SER A CA  
93   C  C   . SER A 40  ? 2.1695 1.7840 1.3775 -0.4749 -0.1144 0.3393  39   SER A C   
94   O  O   . SER A 40  ? 2.1875 1.8729 1.4400 -0.4662 -0.0805 0.3125  39   SER A O   
95   C  CB  . SER A 40  ? 2.3794 1.9770 1.5093 -0.5659 -0.1131 0.4040  39   SER A CB  
96   O  OG  . SER A 40  ? 2.4381 2.1088 1.6322 -0.5779 -0.0807 0.3856  39   SER A OG  
97   N  N   . CYS A 41  ? 2.1715 1.7237 1.3904 -0.4577 -0.1509 0.3418  40   CYS A N   
98   C  CA  . CYS A 41  ? 1.9834 1.5472 1.2585 -0.4275 -0.1550 0.3133  40   CYS A CA  
99   C  C   . CYS A 41  ? 1.8712 1.4485 1.1530 -0.3792 -0.1478 0.2821  40   CYS A C   
100  O  O   . CYS A 41  ? 1.8337 1.4618 1.1642 -0.3611 -0.1301 0.2567  40   CYS A O   
101  C  CB  . CYS A 41  ? 2.0276 1.5158 1.3013 -0.4257 -0.1948 0.3216  40   CYS A CB  
102  S  SG  . CYS A 41  ? 1.9649 1.4587 1.2695 -0.4751 -0.2016 0.3417  40   CYS A SG  
103  N  N   . SER A 42  ? 1.9113 1.4432 1.1472 -0.3596 -0.1635 0.2861  41   SER A N   
104  C  CA  . SER A 42  ? 1.7577 1.2961 0.9959 -0.3158 -0.1601 0.2590  41   SER A CA  
105  C  C   . SER A 42  ? 1.5953 1.2091 0.8477 -0.3138 -0.1207 0.2396  41   SER A C   
106  O  O   . SER A 42  ? 1.8084 1.4451 1.0855 -0.2810 -0.1113 0.2118  41   SER A O   
107  C  CB  . SER A 42  ? 1.7100 1.1912 0.9004 -0.3006 -0.1847 0.2715  41   SER A CB  
108  O  OG  . SER A 42  ? 1.6160 1.1046 0.8120 -0.2599 -0.1825 0.2454  41   SER A OG  
109  N  N   . LYS A 43  ? 1.6325 1.2819 0.8667 -0.3505 -0.0970 0.2538  42   LYS A N   
110  C  CA  . LYS A 43  ? 1.6430 1.3658 0.8944 -0.3538 -0.0538 0.2318  42   LYS A CA  
111  C  C   . LYS A 43  ? 1.5999 1.3731 0.9305 -0.3393 -0.0364 0.2071  42   LYS A C   
112  O  O   . LYS A 43  ? 1.5909 1.3981 0.9511 -0.3114 -0.0181 0.1783  42   LYS A O   
113  C  CB  . LYS A 43  ? 1.8760 1.6293 1.0949 -0.4031 -0.0289 0.2514  42   LYS A CB  
114  C  CG  . LYS A 43  ? 2.0989 1.8135 1.2353 -0.4220 -0.0430 0.2771  42   LYS A CG  
115  C  CD  . LYS A 43  ? 2.1749 1.9068 1.2824 -0.4011 -0.0289 0.2551  42   LYS A CD  
116  C  CE  . LYS A 43  ? 2.1102 1.7792 1.1866 -0.3707 -0.0702 0.2641  42   LYS A CE  
117  N  NZ  . LYS A 43  ? 2.2283 1.8388 1.2513 -0.3962 -0.1052 0.3079  42   LYS A NZ  
118  N  N   . SER A 44  ? 1.7371 1.5136 1.1032 -0.3601 -0.0447 0.2204  43   SER A N   
119  C  CA  . SER A 44  ? 1.8952 1.7203 1.3415 -0.3514 -0.0347 0.2038  43   SER A CA  
120  C  C   . SER A 44  ? 2.0950 1.8786 1.5618 -0.3239 -0.0709 0.1985  43   SER A C   
121  O  O   . SER A 44  ? 2.1422 1.9568 1.6710 -0.3203 -0.0730 0.1911  43   SER A O   
122  C  CB  . SER A 44  ? 1.8701 1.7337 1.3500 -0.3941 -0.0218 0.2210  43   SER A CB  
123  O  OG  . SER A 44  ? 1.9279 1.7331 1.3752 -0.4189 -0.0549 0.2504  43   SER A OG  
124  N  N   . LYS A 45  ? 2.1892 1.9037 1.6040 -0.3077 -0.0995 0.2034  44   LYS A N   
125  C  CA  . LYS A 45  ? 2.2372 1.9063 1.6570 -0.2809 -0.1303 0.1939  44   LYS A CA  
126  C  C   . LYS A 45  ? 2.2937 1.9536 1.7462 -0.2995 -0.1509 0.2024  44   LYS A C   
127  O  O   . LYS A 45  ? 2.4820 2.1389 1.9612 -0.2823 -0.1655 0.1889  44   LYS A O   
128  C  CB  . LYS A 45  ? 2.3100 2.0063 1.7565 -0.2429 -0.1206 0.1657  44   LYS A CB  
129  C  CG  . LYS A 45  ? 2.4646 2.2275 1.9833 -0.2400 -0.1028 0.1528  44   LYS A CG  
130  C  CD  . LYS A 45  ? 2.5636 2.3406 2.1013 -0.2029 -0.0977 0.1284  44   LYS A CD  
131  C  CE  . LYS A 45  ? 2.5287 2.3678 2.1460 -0.1988 -0.0841 0.1187  44   LYS A CE  
132  N  NZ  . LYS A 45  ? 2.4611 2.3092 2.0981 -0.1645 -0.0815 0.0978  44   LYS A NZ  
133  N  N   . ASP A 46  ? 2.1189 1.7718 1.5647 -0.3379 -0.1541 0.2262  45   ASP A N   
134  C  CA  . ASP A 46  ? 1.9585 1.5960 1.4287 -0.3611 -0.1769 0.2364  45   ASP A CA  
135  C  C   . ASP A 46  ? 1.8429 1.3884 1.2624 -0.3596 -0.2115 0.2430  45   ASP A C   
136  O  O   . ASP A 46  ? 1.8021 1.3070 1.1911 -0.3872 -0.2222 0.2659  45   ASP A O   
137  C  CB  . ASP A 46  ? 1.9685 1.6470 1.4620 -0.4063 -0.1621 0.2584  45   ASP A CB  
138  C  CG  . ASP A 46  ? 2.0625 1.7423 1.5953 -0.4323 -0.1836 0.2673  45   ASP A CG  
139  O  OD1 . ASP A 46  ? 2.1107 1.7253 1.6200 -0.4299 -0.2172 0.2668  45   ASP A OD1 
140  O  OD2 . ASP A 46  ? 2.0678 1.8160 1.6569 -0.4567 -0.1660 0.2738  45   ASP A OD2 
141  N  N   . LEU A 47  ? 1.8176 1.3298 1.2301 -0.3284 -0.2280 0.2223  46   LEU A N   
142  C  CA  . LEU A 47  ? 1.9601 1.3862 1.3298 -0.3208 -0.2561 0.2203  46   LEU A CA  
143  C  C   . LEU A 47  ? 2.2278 1.6147 1.5989 -0.3545 -0.2803 0.2315  46   LEU A C   
144  O  O   . LEU A 47  ? 2.3350 1.6477 1.6709 -0.3619 -0.3004 0.2390  46   LEU A O   
145  C  CB  . LEU A 47  ? 1.7833 1.1937 1.1479 -0.2819 -0.2619 0.1915  46   LEU A CB  
146  C  CG  . LEU A 47  ? 1.8133 1.1407 1.1400 -0.2672 -0.2847 0.1800  46   LEU A CG  
147  C  CD1 . LEU A 47  ? 1.8370 1.1223 1.1312 -0.2571 -0.2864 0.1920  46   LEU A CD1 
148  C  CD2 . LEU A 47  ? 1.8061 1.1345 1.1326 -0.2350 -0.2846 0.1505  46   LEU A CD2 
149  N  N   . SER A 48  ? 2.3018 1.7378 1.7171 -0.3752 -0.2800 0.2328  47   SER A N   
150  C  CA  . SER A 48  ? 2.3596 1.7666 1.7801 -0.4117 -0.3039 0.2435  47   SER A CA  
151  C  C   . SER A 48  ? 2.3972 1.7800 1.8004 -0.4482 -0.3050 0.2728  47   SER A C   
152  O  O   . SER A 48  ? 2.4332 1.7450 1.8092 -0.4684 -0.3297 0.2806  47   SER A O   
153  C  CB  . SER A 48  ? 2.3137 1.7915 1.7946 -0.4279 -0.3035 0.2434  47   SER A CB  
154  O  OG  . SER A 48  ? 2.3648 1.9239 1.8910 -0.4369 -0.2740 0.2552  47   SER A OG  
155  N  N   . ALA A 49  ? 2.2687 1.7094 1.6862 -0.4589 -0.2776 0.2884  48   ALA A N   
156  C  CA  . ALA A 49  ? 2.1215 1.5451 1.5168 -0.4967 -0.2757 0.3194  48   ALA A CA  
157  C  C   . ALA A 49  ? 2.0675 1.4081 1.4026 -0.4827 -0.2904 0.3274  48   ALA A C   
158  O  O   . ALA A 49  ? 2.1513 1.4300 1.4590 -0.5102 -0.3105 0.3502  48   ALA A O   
159  C  CB  . ALA A 49  ? 2.0683 1.5784 1.4887 -0.5117 -0.2382 0.3297  48   ALA A CB  
160  N  N   . ALA A 50  ? 1.9816 1.3214 1.3005 -0.4402 -0.2820 0.3100  49   ALA A N   
161  C  CA  . ALA A 50  ? 2.1358 1.4030 1.4085 -0.4205 -0.2979 0.3156  49   ALA A CA  
162  C  C   . ALA A 50  ? 2.2823 1.4607 1.5419 -0.4146 -0.3303 0.3067  49   ALA A C   
163  O  O   . ALA A 50  ? 2.4742 1.5788 1.7044 -0.4171 -0.3507 0.3223  49   ALA A O   
164  C  CB  . ALA A 50  ? 1.7896 1.0805 1.0567 -0.3756 -0.2834 0.2946  49   ALA A CB  
165  N  N   . LEU A 51  ? 2.2814 1.4661 1.5632 -0.4076 -0.3354 0.2811  50   LEU A N   
166  C  CA  . LEU A 51  ? 2.3475 1.4524 1.6150 -0.4072 -0.3624 0.2664  50   LEU A CA  
167  C  C   . LEU A 51  ? 2.5568 1.6139 1.8165 -0.4534 -0.3823 0.2918  50   LEU A C   
168  O  O   . LEU A 51  ? 2.7389 1.7072 1.9738 -0.4537 -0.4046 0.2927  50   LEU A O   
169  C  CB  . LEU A 51  ? 2.2519 1.3831 1.5393 -0.3987 -0.3634 0.2366  50   LEU A CB  
170  C  CG  . LEU A 51  ? 2.2178 1.3335 1.4932 -0.3535 -0.3606 0.2025  50   LEU A CG  
171  C  CD1 . LEU A 51  ? 2.2536 1.3644 1.5320 -0.3593 -0.3723 0.1775  50   LEU A CD1 
172  C  CD2 . LEU A 51  ? 2.2698 1.3035 1.5145 -0.3306 -0.3713 0.1969  50   LEU A CD2 
173  N  N   . ALA A 52  ? 2.5360 1.6525 1.8215 -0.4923 -0.3735 0.3114  51   ALA A N   
174  C  CA  . ALA A 52  ? 2.4293 1.5115 1.7114 -0.5426 -0.3905 0.3382  51   ALA A CA  
175  C  C   . ALA A 52  ? 2.5799 1.6068 1.8273 -0.5547 -0.3981 0.3703  51   ALA A C   
176  O  O   . ALA A 52  ? 2.6640 1.6111 1.8926 -0.5790 -0.4237 0.3848  51   ALA A O   
177  C  CB  . ALA A 52  ? 2.1841 1.3569 1.5091 -0.5799 -0.3742 0.3532  51   ALA A CB  
178  N  N   . LEU A 53  ? 2.5851 1.6527 1.8230 -0.5401 -0.3776 0.3824  52   LEU A N   
179  C  CA  . LEU A 53  ? 2.5861 1.6032 1.7866 -0.5494 -0.3881 0.4153  52   LEU A CA  
180  C  C   . LEU A 53  ? 2.5180 1.4359 1.6974 -0.5145 -0.4157 0.4046  52   LEU A C   
181  O  O   . LEU A 53  ? 2.7261 1.5651 1.8840 -0.5311 -0.4411 0.4305  52   LEU A O   
182  C  CB  . LEU A 53  ? 2.5924 1.6775 1.7825 -0.5408 -0.3604 0.4262  52   LEU A CB  
183  C  CG  . LEU A 53  ? 2.6129 1.8019 1.8281 -0.5710 -0.3257 0.4321  52   LEU A CG  
184  C  CD1 . LEU A 53  ? 2.4656 1.7038 1.6566 -0.5684 -0.3003 0.4438  52   LEU A CD1 
185  C  CD2 . LEU A 53  ? 2.7606 1.9462 1.9817 -0.6300 -0.3319 0.4616  52   LEU A CD2 
186  N  N   . TYR A 54  ? 2.3118 1.2349 1.5010 -0.4663 -0.4101 0.3666  53   TYR A N   
187  C  CA  . TYR A 54  ? 2.3127 1.1513 1.4920 -0.4289 -0.4307 0.3478  53   TYR A CA  
188  C  C   . TYR A 54  ? 2.4101 1.1630 1.5877 -0.4451 -0.4558 0.3375  53   TYR A C   
189  O  O   . TYR A 54  ? 2.4692 1.1327 1.6359 -0.4376 -0.4792 0.3447  53   TYR A O   
190  C  CB  . TYR A 54  ? 2.1877 1.0625 1.3794 -0.3798 -0.4141 0.3069  53   TYR A CB  
191  C  CG  . TYR A 54  ? 2.2499 1.0488 1.4395 -0.3416 -0.4289 0.2774  53   TYR A CG  
192  C  CD1 . TYR A 54  ? 2.1833 0.9253 1.3668 -0.3179 -0.4442 0.2897  53   TYR A CD1 
193  C  CD2 . TYR A 54  ? 2.2920 1.0799 1.4875 -0.3296 -0.4267 0.2363  53   TYR A CD2 
194  C  CE1 . TYR A 54  ? 2.2270 0.9042 1.4186 -0.2807 -0.4541 0.2593  53   TYR A CE1 
195  C  CE2 . TYR A 54  ? 2.2889 1.0113 1.4824 -0.2961 -0.4344 0.2045  53   TYR A CE2 
196  C  CZ  . TYR A 54  ? 2.3184 0.9870 1.5142 -0.2700 -0.4464 0.2145  53   TYR A CZ  
197  O  OH  . TYR A 54  ? 2.3372 0.9449 1.5406 -0.2347 -0.4508 0.1796  53   TYR A OH  
198  N  N   . ASP A 55  ? 2.4500 1.2285 1.6402 -0.4672 -0.4524 0.3201  54   ASP A N   
199  C  CA  . ASP A 55  ? 2.7001 1.4014 1.8842 -0.4900 -0.4759 0.3085  54   ASP A CA  
200  C  C   . ASP A 55  ? 2.8768 1.5239 2.0498 -0.5355 -0.4965 0.3503  54   ASP A C   
201  O  O   . ASP A 55  ? 3.0505 1.5979 2.2115 -0.5409 -0.5214 0.3481  54   ASP A O   
202  C  CB  . ASP A 55  ? 2.7087 1.4606 1.9081 -0.5109 -0.4706 0.2874  54   ASP A CB  
203  C  CG  . ASP A 55  ? 2.5971 1.3887 1.8024 -0.4700 -0.4554 0.2468  54   ASP A CG  
204  O  OD1 . ASP A 55  ? 2.5616 1.2999 1.7527 -0.4322 -0.4576 0.2191  54   ASP A OD1 
205  O  OD2 . ASP A 55  ? 2.4784 1.3545 1.7057 -0.4765 -0.4416 0.2432  54   ASP A OD2 
206  N  N   . ALA A 56  ? 2.8544 1.5675 2.0318 -0.5695 -0.4845 0.3870  55   ALA A N   
207  C  CA  . ALA A 56  ? 2.8582 1.5331 2.0218 -0.6182 -0.5005 0.4327  55   ALA A CA  
208  C  C   . ALA A 56  ? 2.8900 1.4897 2.0297 -0.6013 -0.5189 0.4578  55   ALA A C   
209  O  O   . ALA A 56  ? 3.0036 1.5251 2.1313 -0.6279 -0.5451 0.4838  55   ALA A O   
210  C  CB  . ALA A 56  ? 2.7224 1.4978 1.8967 -0.6568 -0.4763 0.4621  55   ALA A CB  
211  N  N   . ALA A 57  ? 2.8166 1.4451 1.9541 -0.5563 -0.5065 0.4498  56   ALA A N   
212  C  CA  . ALA A 57  ? 3.0033 1.5755 2.1232 -0.5382 -0.5251 0.4770  56   ALA A CA  
213  C  C   . ALA A 57  ? 3.2030 1.6595 2.3294 -0.5128 -0.5557 0.4620  56   ALA A C   
214  O  O   . ALA A 57  ? 3.4132 1.8302 2.5447 -0.5123 -0.5757 0.4848  56   ALA A O   
215  C  CB  . ALA A 57  ? 2.9772 1.6126 2.0978 -0.4948 -0.5049 0.4659  56   ALA A CB  
216  N  N   . ILE A 58  ? 3.1598 1.5970 2.3016 -0.4824 -0.5509 0.4113  57   ILE A N   
217  C  CA  . ILE A 58  ? 3.2524 1.5871 2.4054 -0.4547 -0.5724 0.3858  57   ILE A CA  
218  C  C   . ILE A 58  ? 3.5932 1.8798 2.7515 -0.4913 -0.5908 0.3962  57   ILE A C   
219  O  O   . ILE A 58  ? 3.9173 2.1338 3.0929 -0.4719 -0.6085 0.3893  57   ILE A O   
220  C  CB  . ILE A 58  ? 3.0388 1.3734 2.2011 -0.4212 -0.5575 0.3244  57   ILE A CB  
221  C  CG1 . ILE A 58  ? 2.8135 1.2536 1.9818 -0.3905 -0.5268 0.3068  57   ILE A CG1 
222  C  CG2 . ILE A 58  ? 3.1119 1.3510 2.2894 -0.3794 -0.5717 0.2948  57   ILE A CG2 
223  C  CD1 . ILE A 58  ? 2.7875 1.2517 1.9601 -0.3708 -0.5091 0.2521  57   ILE A CD1 
224  N  N   . THR A 59  ? 3.5658 1.8917 2.7135 -0.5433 -0.5858 0.4107  58   THR A N   
225  C  CA  . THR A 59  ? 3.4707 1.7627 2.6211 -0.5854 -0.6021 0.4244  58   THR A CA  
226  C  C   . THR A 59  ? 3.6866 1.9900 2.8327 -0.6174 -0.6124 0.4786  58   THR A C   
227  O  O   . THR A 59  ? 3.6798 1.9289 2.8309 -0.6363 -0.6323 0.4902  58   THR A O   
228  C  CB  . THR A 59  ? 3.0189 1.3542 2.1660 -0.6296 -0.5934 0.4142  58   THR A CB  
229  O  OG1 . THR A 59  ? 2.8458 1.2727 1.9898 -0.6612 -0.5754 0.4480  58   THR A OG1 
230  C  CG2 . THR A 59  ? 2.8329 1.1637 1.9785 -0.6043 -0.5845 0.3626  58   THR A CG2 
231  N  N   . SER A 60  ? 3.9601 2.3338 3.0943 -0.6246 -0.5979 0.5099  59   SER A N   
232  C  CA  . SER A 60  ? 4.0356 2.4475 3.1575 -0.6702 -0.5986 0.5592  59   SER A CA  
233  C  C   . SER A 60  ? 3.9688 2.3304 3.0877 -0.6753 -0.6243 0.5943  59   SER A C   
234  O  O   . SER A 60  ? 4.1244 2.4783 3.2387 -0.7206 -0.6337 0.6195  59   SER A O   
235  C  CB  . SER A 60  ? 3.9507 2.4548 3.0570 -0.6736 -0.5712 0.5766  59   SER A CB  
236  O  OG  . SER A 60  ? 3.9283 2.4237 3.0262 -0.6387 -0.5778 0.5893  59   SER A OG  
237  N  N   . SER A 61  ? 3.9747 2.3035 3.0987 -0.6325 -0.6374 0.5983  60   SER A N   
238  C  CA  . SER A 61  ? 3.9609 2.2583 3.0806 -0.6460 -0.6620 0.6406  60   SER A CA  
239  C  C   . SER A 61  ? 3.5306 1.7285 2.6772 -0.6176 -0.6956 0.6392  60   SER A C   
240  O  O   . SER A 61  ? 3.3810 1.5492 2.5228 -0.6464 -0.7170 0.6755  60   SER A O   
241  C  CB  . SER A 61  ? 3.7308 2.0854 2.8322 -0.6364 -0.6548 0.6669  60   SER A CB  
242  O  OG  . SER A 61  ? 3.5347 1.9818 2.6095 -0.6719 -0.6237 0.6774  60   SER A OG  
243  N  N   . GLU A 62  ? 3.4772 1.6236 2.6535 -0.5638 -0.6999 0.5995  61   GLU A N   
244  C  CA  . GLU A 62  ? 3.3715 1.5485 2.5536 -0.5217 -0.6786 0.5607  61   GLU A CA  
245  C  C   . GLU A 62  ? 3.2394 1.4690 2.4149 -0.4987 -0.6745 0.5817  61   GLU A C   
246  O  O   . GLU A 62  ? 3.1557 1.3666 2.3394 -0.4909 -0.6963 0.6128  61   GLU A O   
247  C  CB  . GLU A 62  ? 3.4285 1.5307 2.6463 -0.4722 -0.6849 0.5130  61   GLU A CB  
248  C  CG  . GLU A 62  ? 3.5006 1.5533 2.7206 -0.4922 -0.6848 0.4813  61   GLU A CG  
249  C  CD  . GLU A 62  ? 3.3343 1.4400 2.5307 -0.5156 -0.6608 0.4567  61   GLU A CD  
250  O  OE1 . GLU A 62  ? 3.1418 1.3247 2.3200 -0.5232 -0.6433 0.4701  61   GLU A OE1 
251  O  OE2 . GLU A 62  ? 3.2958 1.3670 2.4928 -0.5276 -0.6597 0.4237  61   GLU A OE2 
252  N  N   . VAL A 63  ? 3.2177 1.5131 2.3780 -0.4896 -0.6479 0.5651  62   VAL A N   
253  C  CA  . VAL A 63  ? 3.2615 1.6124 2.4118 -0.4694 -0.6409 0.5808  62   VAL A CA  
254  C  C   . VAL A 63  ? 3.2762 1.5995 2.4586 -0.4048 -0.6461 0.5508  62   VAL A C   
255  O  O   . VAL A 63  ? 3.1938 1.4853 2.3948 -0.3763 -0.6382 0.5059  62   VAL A O   
256  C  CB  . VAL A 63  ? 3.0661 1.5062 2.1852 -0.4909 -0.6071 0.5782  62   VAL A CB  
257  C  CG1 . VAL A 63  ? 2.8956 1.3934 2.0009 -0.4710 -0.5984 0.5912  62   VAL A CG1 
258  C  CG2 . VAL A 63  ? 3.1315 1.6102 2.2263 -0.5544 -0.5976 0.6068  62   VAL A CG2 
259  N  N   . ARG A 64  ? 3.3104 1.6484 2.5000 -0.3840 -0.6593 0.5747  63   ARG A N   
260  C  CA  . ARG A 64  ? 3.2999 1.6401 2.5180 -0.3262 -0.6581 0.5492  63   ARG A CA  
261  C  C   . ARG A 64  ? 3.2681 1.6944 2.4524 -0.3302 -0.6334 0.5521  63   ARG A C   
262  O  O   . ARG A 64  ? 3.4092 1.8877 2.5602 -0.3650 -0.6303 0.5880  63   ARG A O   
263  C  CB  . ARG A 64  ? 3.4102 1.7187 2.6645 -0.2983 -0.6887 0.5720  63   ARG A CB  
264  C  CG  . ARG A 64  ? 3.4781 1.7004 2.7868 -0.2649 -0.7070 0.5491  63   ARG A CG  
265  C  CD  . ARG A 64  ? 3.5905 1.7915 2.9422 -0.2351 -0.7369 0.5741  63   ARG A CD  
266  N  NE  . ARG A 64  ? 3.5398 1.7079 2.9530 -0.1734 -0.7360 0.5330  63   ARG A NE  
267  C  CZ  . ARG A 64  ? 3.5111 1.6656 2.9769 -0.1363 -0.7581 0.5447  63   ARG A CZ  
268  N  NH1 . ARG A 64  ? 3.4759 1.6433 2.9355 -0.1557 -0.7865 0.5979  63   ARG A NH1 
269  N  NH2 . ARG A 64  ? 3.4948 1.6253 3.0207 -0.0810 -0.7511 0.5022  63   ARG A NH2 
270  N  N   . LEU A 65  ? 3.0917 1.5323 2.2834 -0.2951 -0.6145 0.5121  64   LEU A N   
271  C  CA  . LEU A 65  ? 2.7423 1.2613 1.9024 -0.2978 -0.5880 0.5087  64   LEU A CA  
272  C  C   . LEU A 65  ? 2.8735 1.4204 2.0476 -0.2567 -0.5934 0.5094  64   LEU A C   
273  O  O   . LEU A 65  ? 2.9982 1.5094 2.2130 -0.2085 -0.6025 0.4834  64   LEU A O   
274  C  CB  . LEU A 65  ? 2.5952 1.1225 1.7513 -0.2902 -0.5625 0.4653  64   LEU A CB  
275  C  CG  . LEU A 65  ? 2.5979 1.1298 1.7394 -0.3367 -0.5505 0.4628  64   LEU A CG  
276  C  CD1 . LEU A 65  ? 2.7949 1.2340 1.9530 -0.3466 -0.5747 0.4600  64   LEU A CD1 
277  C  CD2 . LEU A 65  ? 2.3490 0.9523 1.5007 -0.3256 -0.5144 0.4140  64   LEU A CD2 
278  N  N   . SER A 66  ? 2.9091 1.5233 2.0511 -0.2775 -0.5860 0.5371  65   SER A N   
279  C  CA  . SER A 66  ? 2.8597 1.5064 2.0120 -0.2458 -0.5934 0.5416  65   SER A CA  
280  C  C   . SER A 66  ? 2.3341 1.0102 1.4878 -0.2106 -0.5700 0.5017  65   SER A C   
281  O  O   . SER A 66  ? 2.2833 0.9897 1.4293 -0.2199 -0.5397 0.4718  65   SER A O   
282  C  CB  . SER A 66  ? 2.8457 1.5558 1.9562 -0.2839 -0.5899 0.5785  65   SER A CB  
283  O  OG  . SER A 66  ? 2.8822 1.6177 2.0047 -0.2575 -0.6035 0.5865  65   SER A OG  
284  N  N   . GLN A 67  ? 2.3089 0.9985 1.4882 -0.1687 -0.5782 0.4926  66   GLN A N   
285  C  CA  . GLN A 67  ? 2.2187 0.9590 1.4190 -0.1303 -0.5488 0.4425  66   GLN A CA  
286  C  C   . GLN A 67  ? 2.1435 0.9746 1.3087 -0.1529 -0.5094 0.4282  66   GLN A C   
287  O  O   . GLN A 67  ? 2.2837 1.1526 1.4649 -0.1343 -0.4792 0.3832  66   GLN A O   
288  C  CB  . GLN A 67  ? 2.4899 1.2370 1.7229 -0.0879 -0.5666 0.4429  66   GLN A CB  
289  C  CG  . GLN A 67  ? 2.7753 1.4383 2.0637 -0.0531 -0.5996 0.4438  66   GLN A CG  
290  C  CD  . GLN A 67  ? 3.1766 1.8144 2.4759 -0.0755 -0.6309 0.4889  66   GLN A CD  
291  O  OE1 . GLN A 67  ? 3.3758 2.0500 2.6313 -0.1180 -0.6328 0.5247  66   GLN A OE1 
292  N  NE2 . GLN A 67  ? 3.3026 1.8803 2.6619 -0.0474 -0.6532 0.4846  66   GLN A NE2 
293  N  N   . GLN A 68  ? 2.1652 1.0287 1.2832 -0.1944 -0.5093 0.4660  67   GLN A N   
294  C  CA  . GLN A 68  ? 2.1629 1.1101 1.2514 -0.2185 -0.4697 0.4524  67   GLN A CA  
295  C  C   . GLN A 68  ? 2.2988 1.2579 1.3976 -0.2327 -0.4430 0.4252  67   GLN A C   
296  O  O   . GLN A 68  ? 2.2553 1.2805 1.3585 -0.2291 -0.4089 0.3944  67   GLN A O   
297  C  CB  . GLN A 68  ? 2.1526 1.1242 1.1852 -0.2675 -0.4728 0.4978  67   GLN A CB  
298  C  CG  . GLN A 68  ? 2.3170 1.3168 1.3268 -0.2600 -0.4847 0.5148  67   GLN A CG  
299  C  CD  . GLN A 68  ? 2.5250 1.4823 1.5593 -0.2520 -0.5251 0.5444  67   GLN A CD  
300  O  OE1 . GLN A 68  ? 2.6557 1.5499 1.7347 -0.2217 -0.5500 0.5409  67   GLN A OE1 
301  N  NE2 . GLN A 68  ? 2.5655 1.5579 1.5724 -0.2798 -0.5309 0.5717  67   GLN A NE2 
302  N  N   . HIS A 69  ? 2.4306 1.3255 1.5344 -0.2508 -0.4609 0.4388  68   HIS A N   
303  C  CA  . HIS A 69  ? 2.4439 1.3455 1.5572 -0.2697 -0.4420 0.4179  68   HIS A CA  
304  C  C   . HIS A 69  ? 2.3939 1.3302 1.5372 -0.2392 -0.4167 0.3652  68   HIS A C   
305  O  O   . HIS A 69  ? 2.5546 1.5558 1.6980 -0.2533 -0.3881 0.3501  68   HIS A O   
306  C  CB  . HIS A 69  ? 2.6344 1.4501 1.7498 -0.2912 -0.4702 0.4386  68   HIS A CB  
307  C  CG  . HIS A 69  ? 2.8125 1.5991 1.8931 -0.3336 -0.4931 0.4953  68   HIS A CG  
308  N  ND1 . HIS A 69  ? 2.9093 1.6254 1.9848 -0.3655 -0.5166 0.5217  68   HIS A ND1 
309  C  CD2 . HIS A 69  ? 2.9359 1.7524 1.9804 -0.3532 -0.4969 0.5317  68   HIS A CD2 
310  C  CE1 . HIS A 69  ? 3.0830 1.8068 2.1353 -0.3984 -0.5283 0.5640  68   HIS A CE1 
311  N  NE2 . HIS A 69  ? 3.0749 1.8593 2.1067 -0.3925 -0.5165 0.5704  68   HIS A NE2 
312  N  N   . PHE A 70  ? 2.3351 1.2272 1.5054 -0.1989 -0.4276 0.3378  69   PHE A N   
313  C  CA  . PHE A 70  ? 2.5207 1.4445 1.7129 -0.1712 -0.4048 0.2891  69   PHE A CA  
314  C  C   . PHE A 70  ? 2.5394 1.5219 1.7409 -0.1349 -0.3875 0.2671  69   PHE A C   
315  O  O   . PHE A 70  ? 2.5467 1.5610 1.7633 -0.1123 -0.3683 0.2301  69   PHE A O   
316  C  CB  . PHE A 70  ? 2.5870 1.4401 1.8028 -0.1427 -0.4188 0.2618  69   PHE A CB  
317  C  CG  . PHE A 70  ? 2.4318 1.2438 1.6657 -0.1090 -0.4398 0.2692  69   PHE A CG  
318  C  CD1 . PHE A 70  ? 2.3813 1.2270 1.6354 -0.0688 -0.4291 0.2443  69   PHE A CD1 
319  C  CD2 . PHE A 70  ? 2.4634 1.2032 1.6982 -0.1187 -0.4723 0.3038  69   PHE A CD2 
320  C  CE1 . PHE A 70  ? 2.5269 1.3400 1.8071 -0.0373 -0.4501 0.2524  69   PHE A CE1 
321  C  CE2 . PHE A 70  ? 2.6858 1.3884 1.9466 -0.0861 -0.4956 0.3137  69   PHE A CE2 
322  C  CZ  . PHE A 70  ? 2.7360 1.4779 2.0222 -0.0447 -0.4843 0.2876  69   PHE A CZ  
323  N  N   . GLN A 71  ? 2.3580 1.3545 1.5443 -0.1372 -0.3967 0.2968  70   GLN A N   
324  C  CA  . GLN A 71  ? 2.2070 1.2641 1.3936 -0.1156 -0.3815 0.2847  70   GLN A CA  
325  C  C   . GLN A 71  ? 1.9761 1.0962 1.1514 -0.1413 -0.3506 0.2750  70   GLN A C   
326  O  O   . GLN A 71  ? 2.0417 1.2029 1.2330 -0.1244 -0.3286 0.2418  70   GLN A O   
327  C  CB  . GLN A 71  ? 2.4139 1.4840 1.5793 -0.1196 -0.3960 0.3176  70   GLN A CB  
328  C  CG  . GLN A 71  ? 2.5529 1.5693 1.7395 -0.0911 -0.4301 0.3312  70   GLN A CG  
329  C  CD  . GLN A 71  ? 2.7223 1.7577 1.9455 -0.0443 -0.4232 0.2955  70   GLN A CD  
330  O  OE1 . GLN A 71  ? 2.8012 1.8855 2.0194 -0.0348 -0.4177 0.2948  70   GLN A OE1 
331  N  NE2 . GLN A 71  ? 2.8246 1.8211 2.0831 -0.0174 -0.4225 0.2646  70   GLN A NE2 
332  N  N   . THR A 72  ? 1.8332 0.9590 0.9848 -0.1833 -0.3499 0.3048  71   THR A N   
333  C  CA  . THR A 72  ? 1.7963 0.9844 0.9455 -0.2103 -0.3201 0.2986  71   THR A CA  
334  C  C   . THR A 72  ? 2.1134 1.3049 1.2926 -0.2027 -0.3105 0.2677  71   THR A C   
335  O  O   . THR A 72  ? 1.9141 1.1647 1.1092 -0.2009 -0.2857 0.2469  71   THR A O   
336  C  CB  . THR A 72  ? 1.8542 1.0392 0.9779 -0.2601 -0.3223 0.3361  71   THR A CB  
337  O  OG1 . THR A 72  ? 1.9200 1.1064 1.0065 -0.2740 -0.3310 0.3675  71   THR A OG1 
338  C  CG2 . THR A 72  ? 1.8153 1.0697 0.9498 -0.2857 -0.2890 0.3260  71   THR A CG2 
339  N  N   . LEU A 73  ? 2.1588 1.2837 1.3458 -0.1991 -0.3320 0.2649  72   LEU A N   
340  C  CA  . LEU A 73  ? 2.1368 1.2564 1.3435 -0.1982 -0.3278 0.2378  72   LEU A CA  
341  C  C   . LEU A 73  ? 2.0755 1.2181 1.2984 -0.1604 -0.3156 0.1994  72   LEU A C   
342  O  O   . LEU A 73  ? 2.2449 1.4340 1.4815 -0.1627 -0.2991 0.1813  72   LEU A O   
343  C  CB  . LEU A 73  ? 2.1973 1.2326 1.4020 -0.2062 -0.3538 0.2422  72   LEU A CB  
344  C  CG  . LEU A 73  ? 2.1789 1.2094 1.3856 -0.2459 -0.3559 0.2491  72   LEU A CG  
345  C  CD1 . LEU A 73  ? 2.0995 1.1801 1.2987 -0.2841 -0.3446 0.2818  72   LEU A CD1 
346  C  CD2 . LEU A 73  ? 2.3464 1.2853 1.5469 -0.2554 -0.3833 0.2549  72   LEU A CD2 
347  N  N   . LEU A 74  ? 1.9423 1.0550 1.1669 -0.1269 -0.3244 0.1889  73   LEU A N   
348  C  CA  . LEU A 74  ? 1.8650 0.9997 1.1033 -0.0929 -0.3118 0.1535  73   LEU A CA  
349  C  C   . LEU A 74  ? 1.7773 0.9886 1.0182 -0.0883 -0.2890 0.1489  73   LEU A C   
350  O  O   . LEU A 74  ? 1.6746 0.9182 0.9268 -0.0762 -0.2747 0.1233  73   LEU A O   
351  C  CB  . LEU A 74  ? 1.8466 0.9410 1.0935 -0.0586 -0.3240 0.1449  73   LEU A CB  
352  C  CG  . LEU A 74  ? 1.8729 0.8975 1.1296 -0.0456 -0.3362 0.1237  73   LEU A CG  
353  C  CD1 . LEU A 74  ? 2.0359 1.0002 1.2835 -0.0739 -0.3561 0.1451  73   LEU A CD1 
354  C  CD2 . LEU A 74  ? 1.8538 0.8549 1.1313 -0.0080 -0.3440 0.1153  73   LEU A CD2 
355  N  N   . TYR A 75  ? 1.8732 1.1104 1.1011 -0.0999 -0.2863 0.1739  74   TYR A N   
356  C  CA  . TYR A 75  ? 1.9874 1.2932 1.2159 -0.0984 -0.2632 0.1681  74   TYR A CA  
357  C  C   . TYR A 75  ? 1.9644 1.3124 1.2084 -0.1182 -0.2451 0.1607  74   TYR A C   
358  O  O   . TYR A 75  ? 2.0456 1.4389 1.3063 -0.1062 -0.2275 0.1406  74   TYR A O   
359  C  CB  . TYR A 75  ? 2.0140 1.3347 1.2170 -0.1141 -0.2639 0.1962  74   TYR A CB  
360  C  CG  . TYR A 75  ? 2.1292 1.4147 1.3224 -0.0944 -0.2862 0.2079  74   TYR A CG  
361  C  CD1 . TYR A 75  ? 2.1666 1.4231 1.3814 -0.0592 -0.2965 0.1871  74   TYR A CD1 
362  C  CD2 . TYR A 75  ? 2.2760 1.5570 1.4400 -0.1133 -0.2982 0.2411  74   TYR A CD2 
363  C  CE1 . TYR A 75  ? 2.3090 1.5376 1.5270 -0.0394 -0.3179 0.1981  74   TYR A CE1 
364  C  CE2 . TYR A 75  ? 2.4385 1.6883 1.5996 -0.0956 -0.3240 0.2558  74   TYR A CE2 
365  C  CZ  . TYR A 75  ? 2.4311 1.6561 1.6245 -0.0569 -0.3339 0.2340  74   TYR A CZ  
366  O  OH  . TYR A 75  ? 2.5130 1.7117 1.7152 -0.0372 -0.3600 0.2486  74   TYR A OH  
367  N  N   . LEU A 76  ? 1.5622 0.8939 0.8051 -0.1487 -0.2515 0.1782  75   LEU A N   
368  C  CA  . LEU A 76  ? 1.5382 0.9106 0.8047 -0.1693 -0.2382 0.1742  75   LEU A CA  
369  C  C   . LEU A 76  ? 1.5570 0.9222 0.8429 -0.1554 -0.2432 0.1489  75   LEU A C   
370  O  O   . LEU A 76  ? 1.6675 1.0796 0.9801 -0.1590 -0.2314 0.1395  75   LEU A O   
371  C  CB  . LEU A 76  ? 1.6515 1.0070 0.9130 -0.2084 -0.2462 0.2010  75   LEU A CB  
372  C  CG  . LEU A 76  ? 1.7520 1.1659 1.0436 -0.2353 -0.2284 0.2040  75   LEU A CG  
373  C  CD1 . LEU A 76  ? 1.7338 1.2184 1.0384 -0.2290 -0.1981 0.1962  75   LEU A CD1 
374  C  CD2 . LEU A 76  ? 1.6255 1.0249 0.9082 -0.2771 -0.2347 0.2337  75   LEU A CD2 
375  N  N   . CYS A 77  ? 1.5913 0.8974 0.8644 -0.1408 -0.2611 0.1380  76   CYS A N   
376  C  CA  . CYS A 77  ? 1.6576 0.9514 0.9376 -0.1319 -0.2659 0.1126  76   CYS A CA  
377  C  C   . CYS A 77  ? 1.8019 1.1391 1.0929 -0.1067 -0.2510 0.0913  76   CYS A C   
378  O  O   . CYS A 77  ? 1.6726 1.0337 0.9773 -0.1106 -0.2492 0.0799  76   CYS A O   
379  C  CB  . CYS A 77  ? 1.5762 0.7963 0.8383 -0.1208 -0.2830 0.1007  76   CYS A CB  
380  S  SG  . CYS A 77  ? 1.7805 0.9368 1.0321 -0.1543 -0.3050 0.1186  76   CYS A SG  
381  N  N   . SER A 78  ? 1.9886 1.3344 1.2735 -0.0829 -0.2431 0.0879  77   SER A N   
382  C  CA  . SER A 78  ? 1.8517 1.2374 1.1462 -0.0607 -0.2289 0.0695  77   SER A CA  
383  C  C   . SER A 78  ? 1.8268 1.2742 1.1431 -0.0703 -0.2121 0.0753  77   SER A C   
384  O  O   . SER A 78  ? 1.9615 1.4398 1.2955 -0.0623 -0.2047 0.0619  77   SER A O   
385  C  CB  . SER A 78  ? 1.8012 1.1807 1.0859 -0.0358 -0.2269 0.0659  77   SER A CB  
386  O  OG  . SER A 78  ? 1.8473 1.1717 1.1228 -0.0237 -0.2413 0.0597  77   SER A OG  
387  N  N   . ALA A 79  ? 1.4991 0.9632 0.8149 -0.0883 -0.2055 0.0951  78   ALA A N   
388  C  CA  . ALA A 79  ? 1.4633 0.9861 0.8045 -0.1000 -0.1854 0.0984  78   ALA A CA  
389  C  C   . ALA A 79  ? 1.6154 1.1566 0.9902 -0.1132 -0.1889 0.0966  78   ALA A C   
390  O  O   . ALA A 79  ? 1.6374 1.2275 1.0477 -0.1116 -0.1751 0.0908  78   ALA A O   
391  C  CB  . ALA A 79  ? 1.5955 1.1283 0.9239 -0.1235 -0.1772 0.1199  78   ALA A CB  
392  N  N   . SER A 80  ? 1.7752 1.2750 1.1407 -0.1268 -0.2092 0.1017  79   SER A N   
393  C  CA  . SER A 80  ? 1.8454 1.3565 1.2375 -0.1436 -0.2195 0.1023  79   SER A CA  
394  C  C   . SER A 80  ? 1.6666 1.1821 1.0655 -0.1267 -0.2257 0.0839  79   SER A C   
395  O  O   . SER A 80  ? 1.5060 1.0521 0.9378 -0.1363 -0.2310 0.0858  79   SER A O   
396  C  CB  . SER A 80  ? 1.8451 1.3040 1.2175 -0.1664 -0.2406 0.1119  79   SER A CB  
397  O  OG  . SER A 80  ? 1.6918 1.1315 1.0465 -0.1792 -0.2386 0.1301  79   SER A OG  
398  N  N   . ILE A 81  ? 1.5576 1.0442 0.9273 -0.1034 -0.2262 0.0679  80   ILE A N   
399  C  CA  . ILE A 81  ? 1.4768 0.9603 0.8417 -0.0911 -0.2321 0.0505  80   ILE A CA  
400  C  C   . ILE A 81  ? 1.4680 1.0059 0.8711 -0.0864 -0.2243 0.0510  80   ILE A C   
401  O  O   . ILE A 81  ? 1.5322 1.0773 0.9467 -0.0943 -0.2375 0.0503  80   ILE A O   
402  C  CB  . ILE A 81  ? 1.5012 0.9583 0.8369 -0.0653 -0.2266 0.0331  80   ILE A CB  
403  C  CG1 . ILE A 81  ? 1.7841 1.1831 1.0911 -0.0665 -0.2363 0.0307  80   ILE A CG1 
404  C  CG2 . ILE A 81  ? 1.4345 0.8931 0.7623 -0.0569 -0.2294 0.0157  80   ILE A CG2 
405  C  CD1 . ILE A 81  ? 1.9846 1.3576 1.2723 -0.0409 -0.2324 0.0112  80   ILE A CD1 
406  N  N   . THR A 82  ? 1.4410 1.0146 0.8634 -0.0748 -0.2043 0.0526  81   THR A N   
407  C  CA  . THR A 82  ? 1.5801 1.2021 1.0448 -0.0671 -0.1944 0.0506  81   THR A CA  
408  C  C   . THR A 82  ? 1.6590 1.3127 1.1719 -0.0870 -0.2017 0.0644  81   THR A C   
409  O  O   . THR A 82  ? 1.6142 1.2945 1.1645 -0.0838 -0.2079 0.0651  81   THR A O   
410  C  CB  . THR A 82  ? 1.7136 1.3651 1.1873 -0.0542 -0.1687 0.0462  81   THR A CB  
411  O  OG1 . THR A 82  ? 1.9552 1.6509 1.4782 -0.0475 -0.1581 0.0425  81   THR A OG1 
412  C  CG2 . THR A 82  ? 1.7301 1.3879 1.1997 -0.0707 -0.1579 0.0582  81   THR A CG2 
413  N  N   . ASP A 83  ? 1.8007 1.4524 1.3164 -0.1085 -0.2028 0.0772  82   ASP A N   
414  C  CA  . ASP A 83  ? 1.8487 1.5327 1.4136 -0.1302 -0.2113 0.0912  82   ASP A CA  
415  C  C   . ASP A 83  ? 1.9047 1.5585 1.4553 -0.1447 -0.2430 0.0946  82   ASP A C   
416  O  O   . ASP A 83  ? 1.8988 1.5005 1.3950 -0.1430 -0.2541 0.0855  82   ASP A O   
417  C  CB  . ASP A 83  ? 1.9435 1.6366 1.5139 -0.1529 -0.2010 0.1047  82   ASP A CB  
418  C  CG  . ASP A 83  ? 2.0386 1.7808 1.6743 -0.1740 -0.2034 0.1182  82   ASP A CG  
419  O  OD1 . ASP A 83  ? 2.0159 1.7435 1.6553 -0.1946 -0.2298 0.1282  82   ASP A OD1 
420  O  OD2 . ASP A 83  ? 2.1041 1.9010 1.7897 -0.1707 -0.1783 0.1173  82   ASP A OD2 
421  N  N   . ILE A 84  ? 2.0383 1.7259 1.6392 -0.1598 -0.2577 0.1067  83   ILE A N   
422  C  CA  . ILE A 84  ? 2.1307 1.7926 1.7152 -0.1795 -0.2909 0.1116  83   ILE A CA  
423  C  C   . ILE A 84  ? 2.0520 1.7054 1.6405 -0.2129 -0.3049 0.1254  83   ILE A C   
424  O  O   . ILE A 84  ? 2.1410 1.7445 1.6820 -0.2305 -0.3257 0.1224  83   ILE A O   
425  C  CB  . ILE A 84  ? 1.8885 1.5886 1.5230 -0.1778 -0.3083 0.1199  83   ILE A CB  
426  C  CG1 . ILE A 84  ? 1.8811 1.6492 1.6044 -0.1748 -0.2947 0.1314  83   ILE A CG1 
427  C  CG2 . ILE A 84  ? 1.8539 1.5412 1.4630 -0.1530 -0.3051 0.1067  83   ILE A CG2 
428  C  CD1 . ILE A 84  ? 1.9133 1.7137 1.6931 -0.2011 -0.3218 0.1522  83   ILE A CD1 
429  N  N   . SER A 85  ? 1.8166 1.5174 1.4602 -0.2232 -0.2915 0.1387  84   SER A N   
430  C  CA  . SER A 85  ? 1.7836 1.4856 1.4414 -0.2586 -0.3060 0.1548  84   SER A CA  
431  C  C   . SER A 85  ? 1.7101 1.3503 1.3041 -0.2718 -0.3053 0.1529  84   SER A C   
432  O  O   . SER A 85  ? 1.5069 1.1308 1.0982 -0.3037 -0.3213 0.1647  84   SER A O   
433  C  CB  . SER A 85  ? 1.7564 1.5310 1.4935 -0.2664 -0.2862 0.1679  84   SER A CB  
434  O  OG  . SER A 85  ? 1.8831 1.6674 1.6432 -0.3034 -0.3017 0.1854  84   SER A OG  
435  N  N   . LEU A 86  ? 1.6918 1.2961 1.2377 -0.2478 -0.2895 0.1392  85   LEU A N   
436  C  CA  . LEU A 86  ? 1.7207 1.2628 1.2116 -0.2550 -0.2908 0.1384  85   LEU A CA  
437  C  C   . LEU A 86  ? 1.8497 1.3289 1.2818 -0.2346 -0.2981 0.1176  85   LEU A C   
438  O  O   . LEU A 86  ? 2.0689 1.4896 1.4605 -0.2385 -0.3034 0.1148  85   LEU A O   
439  C  CB  . LEU A 86  ? 1.7784 1.3382 1.2715 -0.2501 -0.2638 0.1468  85   LEU A CB  
440  C  CG  . LEU A 86  ? 1.7697 1.3916 1.3161 -0.2729 -0.2486 0.1647  85   LEU A CG  
441  C  CD1 . LEU A 86  ? 1.7227 1.3548 1.2533 -0.2691 -0.2210 0.1695  85   LEU A CD1 
442  C  CD2 . LEU A 86  ? 1.9272 1.5367 1.4825 -0.3126 -0.2685 0.1820  85   LEU A CD2 
443  N  N   . GLN A 87  ? 1.9045 1.3963 1.3358 -0.2131 -0.2973 0.1031  86   GLN A N   
444  C  CA  . GLN A 87  ? 1.9754 1.4198 1.3573 -0.1913 -0.2970 0.0810  86   GLN A CA  
445  C  C   . GLN A 87  ? 1.8434 1.2211 1.1791 -0.2068 -0.3163 0.0686  86   GLN A C   
446  O  O   . GLN A 87  ? 1.7739 1.1014 1.0746 -0.1931 -0.3116 0.0547  86   GLN A O   
447  C  CB  . GLN A 87  ? 2.1410 1.6143 1.5313 -0.1733 -0.2951 0.0705  86   GLN A CB  
448  C  CG  . GLN A 87  ? 2.1089 1.5493 1.4574 -0.1476 -0.2862 0.0479  86   GLN A CG  
449  C  CD  . GLN A 87  ? 1.9819 1.4472 1.3339 -0.1363 -0.2867 0.0399  86   GLN A CD  
450  O  OE1 . GLN A 87  ? 1.9629 1.4118 1.2917 -0.1504 -0.3035 0.0335  86   GLN A OE1 
451  N  NE2 . GLN A 87  ? 1.9183 1.4211 1.2957 -0.1138 -0.2693 0.0406  86   GLN A NE2 
452  N  N   . TYR A 88  ? 1.7624 1.1392 1.1005 -0.2356 -0.3384 0.0728  87   TYR A N   
453  C  CA  . TYR A 88  ? 1.8037 1.1178 1.0922 -0.2527 -0.3560 0.0552  87   TYR A CA  
454  C  C   . TYR A 88  ? 2.1118 1.3633 1.3755 -0.2609 -0.3577 0.0522  87   TYR A C   
455  O  O   . TYR A 88  ? 2.2811 1.4728 1.5028 -0.2532 -0.3576 0.0279  87   TYR A O   
456  C  CB  . TYR A 88  ? 1.7948 1.1232 1.0910 -0.2884 -0.3832 0.0645  87   TYR A CB  
457  C  CG  . TYR A 88  ? 1.8046 1.1612 1.1450 -0.3166 -0.3937 0.0913  87   TYR A CG  
458  C  CD1 . TYR A 88  ? 1.7612 1.1904 1.1664 -0.3111 -0.3836 0.1129  87   TYR A CD1 
459  C  CD2 . TYR A 88  ? 1.8755 1.1858 1.1948 -0.3496 -0.4115 0.0931  87   TYR A CD2 
460  C  CE1 . TYR A 88  ? 1.8054 1.2666 1.2556 -0.3381 -0.3895 0.1359  87   TYR A CE1 
461  C  CE2 . TYR A 88  ? 1.8826 1.2216 1.2439 -0.3785 -0.4205 0.1186  87   TYR A CE2 
462  C  CZ  . TYR A 88  ? 1.7781 1.1956 1.2060 -0.3726 -0.4084 0.1401  87   TYR A CZ  
463  O  OH  . TYR A 88  ? 1.6635 1.1166 1.1384 -0.4023 -0.4136 0.1642  87   TYR A OH  
464  N  N   . LEU A 89  ? 2.2176 1.4820 1.5092 -0.2774 -0.3588 0.0765  88   LEU A N   
465  C  CA  . LEU A 89  ? 2.2288 1.4328 1.5001 -0.2863 -0.3623 0.0799  88   LEU A CA  
466  C  C   . LEU A 89  ? 2.0695 1.2473 1.3265 -0.2508 -0.3453 0.0721  88   LEU A C   
467  O  O   . LEU A 89  ? 2.1599 1.2694 1.3903 -0.2465 -0.3506 0.0614  88   LEU A O   
468  C  CB  . LEU A 89  ? 2.3642 1.5954 1.6686 -0.3160 -0.3662 0.1113  88   LEU A CB  
469  C  CG  . LEU A 89  ? 2.3462 1.6489 1.6930 -0.3075 -0.3450 0.1325  88   LEU A CG  
470  C  CD1 . LEU A 89  ? 2.5716 1.8462 1.9031 -0.2999 -0.3342 0.1444  88   LEU A CD1 
471  C  CD2 . LEU A 89  ? 2.1698 1.5278 1.5635 -0.3412 -0.3506 0.1547  88   LEU A CD2 
472  N  N   . ALA A 90  ? 1.9036 1.1349 1.1815 -0.2257 -0.3263 0.0769  89   ALA A N   
473  C  CA  . ALA A 90  ? 1.8915 1.1086 1.1602 -0.1939 -0.3124 0.0730  89   ALA A CA  
474  C  C   . ALA A 90  ? 1.9646 1.1322 1.2041 -0.1708 -0.3127 0.0418  89   ALA A C   
475  O  O   . ALA A 90  ? 2.0979 1.2235 1.3278 -0.1521 -0.3112 0.0372  89   ALA A O   
476  C  CB  . ALA A 90  ? 1.7444 1.0299 1.0379 -0.1744 -0.2925 0.0792  89   ALA A CB  
477  N  N   . ILE A 91  ? 1.8083 0.9836 1.0360 -0.1731 -0.3146 0.0212  90   ILE A N   
478  C  CA  . ILE A 91  ? 1.8030 0.9373 1.0005 -0.1562 -0.3106 -0.0126 90   ILE A CA  
479  C  C   . ILE A 91  ? 2.0070 1.0638 1.1812 -0.1703 -0.3231 -0.0247 90   ILE A C   
480  O  O   . ILE A 91  ? 2.2931 1.3035 1.4590 -0.1480 -0.3171 -0.0434 90   ILE A O   
481  C  CB  . ILE A 91  ? 1.8711 1.0304 1.0529 -0.1644 -0.3116 -0.0289 90   ILE A CB  
482  C  CG1 . ILE A 91  ? 1.7746 1.0034 0.9826 -0.1480 -0.3000 -0.0181 90   ILE A CG1 
483  C  CG2 . ILE A 91  ? 1.8436 0.9595 0.9895 -0.1515 -0.3033 -0.0661 90   ILE A CG2 
484  C  CD1 . ILE A 91  ? 1.6623 0.9331 0.8822 -0.1719 -0.3132 -0.0058 90   ILE A CD1 
485  N  N   . ASP A 92  ? 2.0558 1.0987 1.2236 -0.2073 -0.3411 -0.0151 91   ASP A N   
486  C  CA  . ASP A 92  ? 2.2009 1.1657 1.3445 -0.2262 -0.3550 -0.0278 91   ASP A CA  
487  C  C   . ASP A 92  ? 2.2394 1.1618 1.3966 -0.2152 -0.3568 -0.0123 91   ASP A C   
488  O  O   . ASP A 92  ? 2.2466 1.0998 1.3913 -0.2030 -0.3581 -0.0328 91   ASP A O   
489  C  CB  . ASP A 92  ? 2.2424 1.2090 1.3818 -0.2721 -0.3764 -0.0140 91   ASP A CB  
490  C  CG  . ASP A 92  ? 2.5076 1.4432 1.6054 -0.2933 -0.3859 -0.0449 91   ASP A CG  
491  O  OD1 . ASP A 92  ? 2.6500 1.5391 1.7173 -0.2758 -0.3748 -0.0812 91   ASP A OD1 
492  O  OD2 . ASP A 92  ? 2.6183 1.5778 1.7144 -0.3288 -0.4043 -0.0334 91   ASP A OD2 
493  N  N   . ARG A 93  ? 2.1551 1.1195 1.3391 -0.2202 -0.3569 0.0242  92   ARG A N   
494  C  CA  . ARG A 93  ? 2.1053 1.0353 1.2984 -0.2162 -0.3619 0.0474  92   ARG A CA  
495  C  C   . ARG A 93  ? 2.0508 0.9770 1.2517 -0.1739 -0.3503 0.0422  92   ARG A C   
496  O  O   . ARG A 93  ? 2.1670 1.0344 1.3689 -0.1627 -0.3590 0.0456  92   ARG A O   
497  C  CB  . ARG A 93  ? 2.1722 1.1518 1.3853 -0.2424 -0.3636 0.0873  92   ARG A CB  
498  C  CG  . ARG A 93  ? 2.2885 1.2475 1.4983 -0.2872 -0.3816 0.0978  92   ARG A CG  
499  C  CD  . ARG A 93  ? 2.4065 1.2798 1.6028 -0.2986 -0.3982 0.1070  92   ARG A CD  
500  N  NE  . ARG A 93  ? 2.5735 1.3866 1.7499 -0.3254 -0.4157 0.0883  92   ARG A NE  
501  C  CZ  . ARG A 93  ? 2.6196 1.4341 1.7985 -0.3703 -0.4308 0.1058  92   ARG A CZ  
502  N  NH1 . ARG A 93  ? 2.5183 1.3980 1.7234 -0.3916 -0.4272 0.1407  92   ARG A NH1 
503  N  NH2 . ARG A 93  ? 2.6646 1.4184 1.8207 -0.3955 -0.4481 0.0863  92   ARG A NH2 
504  N  N   . GLY A 94  ? 1.9790 0.9663 1.1887 -0.1510 -0.3331 0.0352  93   GLY A N   
505  C  CA  . GLY A 94  ? 1.8976 0.8931 1.1183 -0.1144 -0.3234 0.0347  93   GLY A CA  
506  C  C   . GLY A 94  ? 1.8627 0.7951 1.0833 -0.0866 -0.3255 0.0101  93   GLY A C   
507  O  O   . GLY A 94  ? 1.8182 0.7318 1.0537 -0.0669 -0.3309 0.0241  93   GLY A O   
508  N  N   . PHE A 95  ? 2.1394 1.0402 1.3449 -0.0858 -0.3215 -0.0269 94   PHE A N   
509  C  CA  . PHE A 95  ? 2.3644 1.2070 1.5754 -0.0585 -0.3184 -0.0576 94   PHE A CA  
510  C  C   . PHE A 95  ? 2.4808 1.2425 1.6980 -0.0651 -0.3381 -0.0480 94   PHE A C   
511  O  O   . PHE A 95  ? 2.5015 1.2285 1.7442 -0.0367 -0.3425 -0.0467 94   PHE A O   
512  C  CB  . PHE A 95  ? 2.5300 1.3622 1.7162 -0.0611 -0.3049 -0.1031 94   PHE A CB  
513  C  CG  . PHE A 95  ? 2.4798 1.3831 1.6606 -0.0523 -0.2868 -0.1131 94   PHE A CG  
514  C  CD1 . PHE A 95  ? 2.4845 1.4139 1.6852 -0.0163 -0.2701 -0.1262 94   PHE A CD1 
515  C  CD2 . PHE A 95  ? 2.4701 1.4145 1.6301 -0.0809 -0.2889 -0.1068 94   PHE A CD2 
516  C  CE1 . PHE A 95  ? 2.5289 1.5203 1.7237 -0.0111 -0.2547 -0.1335 94   PHE A CE1 
517  C  CE2 . PHE A 95  ? 2.5270 1.5314 1.6838 -0.0737 -0.2753 -0.1126 94   PHE A CE2 
518  C  CZ  . PHE A 95  ? 2.5222 1.5485 1.6940 -0.0397 -0.2577 -0.1263 94   PHE A CZ  
519  N  N   . GLU A 96  ? 2.6154 1.3453 1.8123 -0.1030 -0.3519 -0.0409 95   GLU A N   
520  C  CA  . GLU A 96  ? 2.7472 1.3949 1.9472 -0.1152 -0.3727 -0.0300 95   GLU A CA  
521  C  C   . GLU A 96  ? 2.5865 1.2377 1.8064 -0.1142 -0.3878 0.0194  95   GLU A C   
522  O  O   . GLU A 96  ? 2.5608 1.1495 1.7983 -0.0998 -0.4024 0.0280  95   GLU A O   
523  C  CB  . GLU A 96  ? 3.0236 1.6440 2.1959 -0.1617 -0.3851 -0.0311 95   GLU A CB  
524  C  CG  . GLU A 96  ? 3.1583 1.8539 2.3236 -0.1939 -0.3857 -0.0038 95   GLU A CG  
525  C  CD  . GLU A 96  ? 3.3906 2.0596 2.5346 -0.2405 -0.4012 -0.0045 95   GLU A CD  
526  O  OE1 . GLU A 96  ? 3.5305 2.1274 2.6544 -0.2477 -0.4073 -0.0360 95   GLU A OE1 
527  O  OE2 . GLU A 96  ? 3.4283 2.1494 2.5778 -0.2707 -0.4068 0.0248  95   GLU A OE2 
528  N  N   . ILE A 97  ? 2.5184 1.2418 1.7354 -0.1310 -0.3843 0.0515  96   ILE A N   
529  C  CA  . ILE A 97  ? 2.4020 1.1397 1.6280 -0.1358 -0.3948 0.0981  96   ILE A CA  
530  C  C   . ILE A 97  ? 2.3259 1.0610 1.5733 -0.0938 -0.3946 0.0991  96   ILE A C   
531  O  O   . ILE A 97  ? 2.3646 1.0607 1.6219 -0.0905 -0.4142 0.1288  96   ILE A O   
532  C  CB  . ILE A 97  ? 2.3026 1.1283 1.5233 -0.1572 -0.3826 0.1221  96   ILE A CB  
533  C  CG1 . ILE A 97  ? 2.6521 1.4821 1.8624 -0.2025 -0.3879 0.1317  96   ILE A CG1 
534  C  CG2 . ILE A 97  ? 2.0350 0.8817 1.2581 -0.1586 -0.3876 0.1633  96   ILE A CG2 
535  C  CD1 . ILE A 97  ? 2.6990 1.6161 1.9150 -0.2230 -0.3741 0.1536  96   ILE A CD1 
536  N  N   . PHE A 98  ? 2.3183 1.0963 1.5740 -0.0637 -0.3746 0.0686  97   PHE A N   
537  C  CA  . PHE A 98  ? 2.2585 1.0439 1.5400 -0.0230 -0.3727 0.0652  97   PHE A CA  
538  C  C   . PHE A 98  ? 2.2688 0.9696 1.5750 -0.0016 -0.3887 0.0545  97   PHE A C   
539  O  O   . PHE A 98  ? 2.2311 0.9092 1.5601 0.0138  -0.4074 0.0814  97   PHE A O   
540  C  CB  . PHE A 98  ? 2.2592 1.0992 1.5445 0.0009  -0.3468 0.0283  97   PHE A CB  
541  C  CG  . PHE A 98  ? 2.1427 0.9836 1.4609 0.0438  -0.3430 0.0138  97   PHE A CG  
542  C  CD1 . PHE A 98  ? 1.9029 0.7904 1.2344 0.0580  -0.3460 0.0392  97   PHE A CD1 
543  C  CD2 . PHE A 98  ? 2.2506 1.0482 1.5879 0.0685  -0.3353 -0.0272 97   PHE A CD2 
544  C  CE1 . PHE A 98  ? 1.8789 0.7722 1.2462 0.0960  -0.3449 0.0275  97   PHE A CE1 
545  C  CE2 . PHE A 98  ? 2.2301 1.0349 1.6073 0.1085  -0.3304 -0.0412 97   PHE A CE2 
546  C  CZ  . PHE A 98  ? 2.0264 0.8806 1.4207 0.1224  -0.3369 -0.0122 97   PHE A CZ  
547  N  N   . ASP A 99  ? 2.4727 1.1245 1.7742 -0.0030 -0.3827 0.0157  98   ASP A N   
548  C  CA  . ASP A 99  ? 2.6695 1.2383 1.9992 0.0203  -0.3922 -0.0057 98   ASP A CA  
549  C  C   . ASP A 99  ? 2.7639 1.2603 2.0995 0.0028  -0.4246 0.0330  98   ASP A C   
550  O  O   . ASP A 99  ? 2.6762 1.1070 2.0483 0.0279  -0.4399 0.0310  98   ASP A O   
551  C  CB  . ASP A 99  ? 2.6806 1.2153 1.9936 0.0159  -0.3746 -0.0604 98   ASP A CB  
552  C  CG  . ASP A 99  ? 2.5863 1.1637 1.9096 0.0475  -0.3449 -0.1049 98   ASP A CG  
553  O  OD1 . ASP A 99  ? 2.5790 1.1894 1.9388 0.0818  -0.3415 -0.0982 98   ASP A OD1 
554  O  OD2 . ASP A 99  ? 2.5363 1.1163 1.8297 0.0350  -0.3259 -0.1448 98   ASP A OD2 
555  N  N   . ARG A 100 ? 2.8858 1.3942 2.1894 -0.0408 -0.4352 0.0684  99   ARG A N   
556  C  CA  . ARG A 100 ? 3.0892 1.5358 2.3923 -0.0647 -0.4660 0.1117  99   ARG A CA  
557  C  C   . ARG A 100 ? 3.2998 1.7277 2.6282 -0.0483 -0.4915 0.1561  99   ARG A C   
558  O  O   . ARG A 100 ? 3.6203 1.9638 2.9712 -0.0419 -0.5168 0.1674  99   ARG A O   
559  C  CB  . ARG A 100 ? 3.0391 1.5126 2.3045 -0.1181 -0.4683 0.1396  99   ARG A CB  
560  C  CG  . ARG A 100 ? 3.0793 1.4913 2.3378 -0.1517 -0.4986 0.1859  99   ARG A CG  
561  C  CD  . ARG A 100 ? 3.1057 1.4092 2.3740 -0.1527 -0.5153 0.1647  99   ARG A CD  
562  N  NE  . ARG A 100 ? 3.1539 1.4517 2.4035 -0.1665 -0.4987 0.1174  99   ARG A NE  
563  C  CZ  . ARG A 100 ? 3.0928 1.3894 2.3141 -0.2148 -0.5029 0.1250  99   ARG A CZ  
564  N  NH1 . ARG A 100 ? 3.0128 1.3156 2.2236 -0.2536 -0.5194 0.1764  99   ARG A NH1 
565  N  NH2 . ARG A 100 ? 3.0670 1.3585 2.2699 -0.2268 -0.4911 0.0818  99   ARG A NH2 
566  N  N   . MET A 101 ? 3.1828 1.6862 2.5065 -0.0437 -0.4868 0.1822  100  MET A N   
567  C  CA  . MET A 101 ? 3.2636 1.7559 2.6117 -0.0239 -0.5119 0.2207  100  MET A CA  
568  C  C   . MET A 101 ? 2.8855 1.3915 2.2845 0.0327  -0.5101 0.1997  100  MET A C   
569  O  O   . MET A 101 ? 2.9978 1.4871 2.4287 0.0541  -0.5353 0.2276  100  MET A O   
570  C  CB  . MET A 101 ? 3.2360 1.8091 2.5540 -0.0446 -0.5085 0.2593  100  MET A CB  
571  C  CG  . MET A 101 ? 3.2304 1.8139 2.5047 -0.0992 -0.5127 0.2975  100  MET A CG  
572  S  SD  . MET A 101 ? 5.8981 4.3801 5.1702 -0.1262 -0.5567 0.3484  100  MET A SD  
573  C  CE  . MET A 101 ? 2.9376 1.4248 2.2240 -0.1042 -0.5855 0.3925  100  MET A CE  
574  N  N   . VAL A 102 ? 2.6538 1.1850 2.0606 0.0532  -0.4788 0.1444  101  VAL A N   
575  C  CA  . VAL A 102 ? 2.5312 1.0720 1.9877 0.1031  -0.4686 0.1106  101  VAL A CA  
576  C  C   . VAL A 102 ? 2.8041 1.2424 2.3004 0.1184  -0.4920 0.1070  101  VAL A C   
577  O  O   . VAL A 102 ? 2.9386 1.3544 2.4922 0.1564  -0.5072 0.1099  101  VAL A O   
578  C  CB  . VAL A 102 ? 2.3833 0.9675 1.8441 0.1245  -0.4299 0.0507  101  VAL A CB  
579  C  CG1 . VAL A 102 ? 2.2745 0.8518 1.7987 0.1750  -0.4256 0.0230  101  VAL A CG1 
580  C  CG2 . VAL A 102 ? 2.4414 1.1213 1.8691 0.1115  -0.4097 0.0562  101  VAL A CG2 
581  N  N   . SER A 103 ? 2.9786 1.3543 2.4486 0.0882  -0.4967 0.1021  102  SER A N   
582  C  CA  . SER A 103 ? 3.1796 1.4486 2.6836 0.0981  -0.5188 0.0967  102  SER A CA  
583  C  C   . SER A 103 ? 3.1934 1.4447 2.7333 0.1024  -0.5561 0.1545  102  SER A C   
584  O  O   . SER A 103 ? 3.0629 1.2764 2.6657 0.1280  -0.5652 0.1484  102  SER A O   
585  C  CB  . SER A 103 ? 3.2687 1.4824 2.7294 0.0547  -0.5196 0.0887  102  SER A CB  
586  O  OG  . SER A 103 ? 3.2636 1.4849 2.6844 0.0086  -0.5409 0.1459  102  SER A OG  
587  N  N   . SER A 104 ? 3.2515 1.5444 2.7530 0.0744  -0.5726 0.2091  103  SER A N   
588  C  CA  . SER A 104 ? 3.3226 1.6232 2.8475 0.0695  -0.6045 0.2665  103  SER A CA  
589  C  C   . SER A 104 ? 3.3356 1.6588 2.9297 0.1195  -0.6133 0.2651  103  SER A C   
590  O  O   . SER A 104 ? 3.3491 1.6666 2.9789 0.1226  -0.6417 0.3049  103  SER A O   
591  C  CB  . SER A 104 ? 3.2345 1.5894 2.6961 0.0272  -0.6115 0.3166  103  SER A CB  
592  O  OG  . SER A 104 ? 3.1286 1.4713 2.5341 -0.0200 -0.6025 0.3202  103  SER A OG  
593  N  N   . GLY A 105 ? 3.2886 1.6396 2.9026 0.1566  -0.5892 0.2196  104  GLY A N   
594  C  CA  . GLY A 105 ? 3.1766 1.5559 2.8633 0.2050  -0.5936 0.2124  104  GLY A CA  
595  C  C   . GLY A 105 ? 2.9481 1.4013 2.6194 0.2070  -0.6034 0.2449  104  GLY A C   
596  O  O   . GLY A 105 ? 2.8996 1.3842 2.6321 0.2433  -0.6110 0.2450  104  GLY A O   
597  N  N   . ILE A 106 ? 2.8442 1.3290 2.4367 0.1670  -0.6019 0.2718  105  ILE A N   
598  C  CA  . ILE A 106 ? 2.9272 1.4997 2.5017 0.1649  -0.5997 0.2921  105  ILE A CA  
599  C  C   . ILE A 106 ? 2.8932 1.5355 2.4805 0.1907  -0.5563 0.2355  105  ILE A C   
600  O  O   . ILE A 106 ? 2.9413 1.5940 2.4998 0.1798  -0.5218 0.1955  105  ILE A O   
601  C  CB  . ILE A 106 ? 2.9113 1.5213 2.4041 0.1103  -0.5996 0.3321  105  ILE A CB  
602  C  CG1 . ILE A 106 ? 2.8411 1.5470 2.3127 0.1099  -0.5852 0.3354  105  ILE A CG1 
603  C  CG2 . ILE A 106 ? 2.6631 1.2669 2.1104 0.0786  -0.5701 0.3072  105  ILE A CG2 
604  C  CD1 . ILE A 106 ? 2.6083 1.3633 2.0041 0.0608  -0.5718 0.3585  105  ILE A CD1 
605  N  N   . SER A 107 ? 2.8221 1.5112 2.4535 0.2231  -0.5605 0.2339  106  SER A N   
606  C  CA  . SER A 107 ? 2.8351 1.5942 2.4769 0.2441  -0.5208 0.1850  106  SER A CA  
607  C  C   . SER A 107 ? 2.8346 1.6534 2.3998 0.2047  -0.4989 0.1910  106  SER A C   
608  O  O   . SER A 107 ? 2.8408 1.6845 2.3688 0.1783  -0.5170 0.2354  106  SER A O   
609  C  CB  . SER A 107 ? 2.8069 1.6115 2.5085 0.2799  -0.5326 0.1894  106  SER A CB  
610  O  OG  . SER A 107 ? 2.6617 1.5297 2.3757 0.2989  -0.4928 0.1403  106  SER A OG  
611  N  N   . PRO A 108 ? 2.7450 1.5859 2.2870 0.1996  -0.4600 0.1460  107  PRO A N   
612  C  CA  . PRO A 108 ? 2.6337 1.5193 2.1102 0.1616  -0.4402 0.1504  107  PRO A CA  
613  C  C   . PRO A 108 ? 2.6292 1.5899 2.0877 0.1558  -0.4386 0.1703  107  PRO A C   
614  O  O   . PRO A 108 ? 2.6812 1.6709 2.1778 0.1841  -0.4437 0.1665  107  PRO A O   
615  C  CB  . PRO A 108 ? 2.5307 1.4287 2.0034 0.1683  -0.4031 0.0954  107  PRO A CB  
616  C  CG  . PRO A 108 ? 2.5259 1.4227 2.0586 0.2125  -0.3959 0.0617  107  PRO A CG  
617  C  CD  . PRO A 108 ? 2.6645 1.4989 2.2425 0.2297  -0.4315 0.0880  107  PRO A CD  
618  N  N   . ASN A 109 ? 2.5562 1.5476 1.9598 0.1184  -0.4318 0.1909  108  ASN A N   
619  C  CA  . ASN A 109 ? 2.3107 1.3688 1.6906 0.1084  -0.4281 0.2071  108  ASN A CA  
620  C  C   . ASN A 109 ? 2.1985 1.3167 1.5844 0.1240  -0.3945 0.1658  108  ASN A C   
621  O  O   . ASN A 109 ? 2.2263 1.3422 1.6118 0.1263  -0.3706 0.1315  108  ASN A O   
622  C  CB  . ASN A 109 ? 2.2705 1.3414 1.5927 0.0628  -0.4269 0.2378  108  ASN A CB  
623  C  CG  . ASN A 109 ? 2.3176 1.4520 1.6098 0.0488  -0.4219 0.2529  108  ASN A CG  
624  O  OD1 . ASN A 109 ? 2.4156 1.5717 1.7270 0.0684  -0.4343 0.2571  108  ASN A OD1 
625  N  ND2 . ASN A 109 ? 2.2785 1.4442 1.5257 0.0139  -0.4031 0.2596  108  ASN A ND2 
626  N  N   . GLU A 110 ? 2.2178 1.3879 1.6070 0.1319  -0.3952 0.1709  109  GLU A N   
627  C  CA  . GLU A 110 ? 2.0798 1.3078 1.4727 0.1433  -0.3658 0.1366  109  GLU A CA  
628  C  C   . GLU A 110 ? 1.9049 1.1572 1.2580 0.1179  -0.3378 0.1229  109  GLU A C   
629  O  O   . GLU A 110 ? 1.7889 1.0575 1.1485 0.1264  -0.3137 0.0887  109  GLU A O   
630  C  CB  . GLU A 110 ? 2.2447 1.5220 1.6381 0.1464  -0.3751 0.1515  109  GLU A CB  
631  C  CG  . GLU A 110 ? 2.3960 1.7326 1.7934 0.1559  -0.3475 0.1197  109  GLU A CG  
632  C  CD  . GLU A 110 ? 2.4160 1.7892 1.7647 0.1268  -0.3251 0.1176  109  GLU A CD  
633  O  OE1 . GLU A 110 ? 2.5812 1.9548 1.8925 0.0993  -0.3341 0.1463  109  GLU A OE1 
634  O  OE2 . GLU A 110 ? 2.1982 1.5997 1.5473 0.1306  -0.2983 0.0875  109  GLU A OE2 
635  N  N   . ALA A 111 ? 1.8352 1.0909 1.1491 0.0853  -0.3418 0.1510  110  ALA A N   
636  C  CA  . ALA A 111 ? 1.7791 1.0599 1.0646 0.0606  -0.3172 0.1418  110  ALA A CA  
637  C  C   . ALA A 111 ? 1.8591 1.1020 1.1507 0.0574  -0.3112 0.1252  110  ALA A C   
638  O  O   . ALA A 111 ? 1.7782 1.0442 1.0666 0.0531  -0.2897 0.1018  110  ALA A O   
639  C  CB  . ALA A 111 ? 1.8171 1.1098 1.0637 0.0255  -0.3214 0.1751  110  ALA A CB  
640  N  N   . SER A 112 ? 2.0317 1.2139 1.3321 0.0581  -0.3326 0.1383  111  SER A N   
641  C  CA  . SER A 112 ? 2.0841 1.2227 1.3856 0.0505  -0.3302 0.1236  111  SER A CA  
642  C  C   . SER A 112 ? 1.9930 1.1291 1.3161 0.0760  -0.3144 0.0801  111  SER A C   
643  O  O   . SER A 112 ? 2.1012 1.2337 1.4135 0.0646  -0.3014 0.0597  111  SER A O   
644  C  CB  . SER A 112 ? 2.2530 1.3206 1.5603 0.0457  -0.3581 0.1473  111  SER A CB  
645  O  OG  . SER A 112 ? 2.4786 1.5208 1.8202 0.0773  -0.3759 0.1486  111  SER A OG  
646  N  N   . VAL A 113 ? 1.7996 0.9390 1.1531 0.1082  -0.3162 0.0667  112  VAL A N   
647  C  CA  . VAL A 113 ? 1.7968 0.9380 1.1699 0.1309  -0.2978 0.0241  112  VAL A CA  
648  C  C   . VAL A 113 ? 1.9333 1.1320 1.2868 0.1220  -0.2730 0.0062  112  VAL A C   
649  O  O   . VAL A 113 ? 2.0908 1.2873 1.4391 0.1223  -0.2570 -0.0243 112  VAL A O   
650  C  CB  . VAL A 113 ? 1.6697 0.8135 1.0875 0.1669  -0.3029 0.0149  112  VAL A CB  
651  C  CG1 . VAL A 113 ? 1.5818 0.7395 1.0169 0.1867  -0.2774 -0.0312 112  VAL A CG1 
652  C  CG2 . VAL A 113 ? 1.6923 0.7723 1.1385 0.1788  -0.3290 0.0303  112  VAL A CG2 
653  N  N   . THR A 114 ? 1.8747 1.1222 1.2158 0.1122  -0.2706 0.0253  113  THR A N   
654  C  CA  . THR A 114 ? 1.8017 1.0990 1.1281 0.1024  -0.2497 0.0122  113  THR A CA  
655  C  C   . THR A 114 ? 1.8289 1.1156 1.1349 0.0759  -0.2457 0.0128  113  THR A C   
656  O  O   . THR A 114 ? 1.8050 1.1088 1.1053 0.0714  -0.2324 -0.0070 113  THR A O   
657  C  CB  . THR A 114 ? 1.6884 1.0346 1.0062 0.0957  -0.2472 0.0310  113  THR A CB  
658  O  OG1 . THR A 114 ? 1.8907 1.2448 1.2267 0.1161  -0.2572 0.0362  113  THR A OG1 
659  C  CG2 . THR A 114 ? 1.4662 0.8597 0.7786 0.0917  -0.2259 0.0139  113  THR A CG2 
660  N  N   . SER A 115 ? 1.8051 1.0641 1.1010 0.0565  -0.2596 0.0379  114  SER A N   
661  C  CA  . SER A 115 ? 1.7869 1.0393 1.0689 0.0283  -0.2586 0.0430  114  SER A CA  
662  C  C   . SER A 115 ? 1.9347 1.1498 1.2138 0.0266  -0.2586 0.0177  114  SER A C   
663  O  O   . SER A 115 ? 2.0321 1.2663 1.3034 0.0115  -0.2513 0.0082  114  SER A O   
664  C  CB  . SER A 115 ? 1.7415 0.9684 1.0136 0.0061  -0.2741 0.0763  114  SER A CB  
665  O  OG  . SER A 115 ? 1.7499 1.0158 1.0147 -0.0004 -0.2711 0.0986  114  SER A OG  
666  N  N   . VAL A 116 ? 1.9505 1.1121 1.2368 0.0414  -0.2678 0.0065  115  VAL A N   
667  C  CA  . VAL A 116 ? 2.0449 1.1667 1.3236 0.0393  -0.2653 -0.0234 115  VAL A CA  
668  C  C   . VAL A 116 ? 2.1740 1.3289 1.4502 0.0520  -0.2458 -0.0551 115  VAL A C   
669  O  O   . VAL A 116 ? 2.2793 1.4270 1.5359 0.0375  -0.2404 -0.0751 115  VAL A O   
670  C  CB  . VAL A 116 ? 2.0780 1.1317 1.3711 0.0553  -0.2768 -0.0322 115  VAL A CB  
671  C  CG1 . VAL A 116 ? 2.0328 1.0967 1.3573 0.0909  -0.2750 -0.0365 115  VAL A CG1 
672  C  CG2 . VAL A 116 ? 2.2822 1.2929 1.5622 0.0508  -0.2704 -0.0691 115  VAL A CG2 
673  N  N   . ALA A 117 ? 2.1181 1.3097 1.4117 0.0757  -0.2368 -0.0578 116  ALA A N   
674  C  CA  . ALA A 117 ? 1.9024 1.1298 1.1939 0.0854  -0.2180 -0.0838 116  ALA A CA  
675  C  C   . ALA A 117 ? 1.6724 0.9388 0.9450 0.0628  -0.2131 -0.0778 116  ALA A C   
676  O  O   . ALA A 117 ? 1.6342 0.9053 0.8900 0.0547  -0.2048 -0.0982 116  ALA A O   
677  C  CB  . ALA A 117 ? 1.8922 1.1549 1.2089 0.1114  -0.2121 -0.0826 116  ALA A CB  
678  N  N   . ARG A 118 ? 1.6210 0.9152 0.8976 0.0516  -0.2183 -0.0496 117  ARG A N   
679  C  CA  . ARG A 118 ? 1.7473 1.0788 1.0186 0.0324  -0.2149 -0.0421 117  ARG A CA  
680  C  C   . ARG A 118 ? 1.8327 1.1379 1.0883 0.0075  -0.2239 -0.0453 117  ARG A C   
681  O  O   . ARG A 118 ? 1.9010 1.2240 1.1480 -0.0038 -0.2222 -0.0533 117  ARG A O   
682  C  CB  . ARG A 118 ? 1.8851 1.2492 1.1676 0.0244  -0.2153 -0.0149 117  ARG A CB  
683  C  CG  . ARG A 118 ? 1.8354 1.2325 1.1276 0.0425  -0.2069 -0.0114 117  ARG A CG  
684  C  CD  . ARG A 118 ? 1.9123 1.3451 1.2095 0.0292  -0.2023 0.0093  117  ARG A CD  
685  N  NE  . ARG A 118 ? 2.1947 1.6562 1.4942 0.0423  -0.1951 0.0113  117  ARG A NE  
686  C  CZ  . ARG A 118 ? 2.4123 1.9107 1.7195 0.0501  -0.1826 -0.0002 117  ARG A CZ  
687  N  NH1 . ARG A 118 ? 2.5819 2.0924 1.8964 0.0469  -0.1772 -0.0116 117  ARG A NH1 
688  N  NH2 . ARG A 118 ? 2.3841 1.9049 1.6904 0.0590  -0.1779 0.0013  117  ARG A NH2 
689  N  N   . LEU A 119 ? 1.8854 1.1473 1.1367 -0.0033 -0.2363 -0.0368 118  LEU A N   
690  C  CA  . LEU A 119 ? 1.9286 1.1612 1.1639 -0.0302 -0.2476 -0.0393 118  LEU A CA  
691  C  C   . LEU A 119 ? 1.8686 1.0766 1.0795 -0.0310 -0.2439 -0.0718 118  LEU A C   
692  O  O   . LEU A 119 ? 1.5387 0.7521 0.7326 -0.0541 -0.2498 -0.0756 118  LEU A O   
693  C  CB  . LEU A 119 ? 1.8546 1.0361 1.0887 -0.0402 -0.2615 -0.0267 118  LEU A CB  
694  C  CG  . LEU A 119 ? 1.7397 0.9402 0.9877 -0.0532 -0.2672 0.0082  118  LEU A CG  
695  C  CD1 . LEU A 119 ? 1.7597 0.9014 1.0042 -0.0579 -0.2817 0.0204  118  LEU A CD1 
696  C  CD2 . LEU A 119 ? 1.5248 0.7587 0.7786 -0.0829 -0.2705 0.0221  118  LEU A CD2 
697  N  N   . ALA A 120 ? 1.9262 1.1101 1.1367 -0.0068 -0.2339 -0.0950 119  ALA A N   
698  C  CA  . ALA A 120 ? 1.8997 1.0629 1.0858 -0.0065 -0.2237 -0.1308 119  ALA A CA  
699  C  C   . ALA A 120 ? 1.9554 1.1681 1.1299 -0.0115 -0.2145 -0.1353 119  ALA A C   
700  O  O   . ALA A 120 ? 1.8828 1.0920 1.0268 -0.0355 -0.2182 -0.1451 119  ALA A O   
701  C  CB  . ALA A 120 ? 1.5956 0.7327 0.7972 0.0244  -0.2115 -0.1543 119  ALA A CB  
702  N  N   . ALA A 121 ? 1.9695 1.2262 1.1670 0.0090  -0.2049 -0.1265 120  ALA A N   
703  C  CA  . ALA A 121 ? 1.8443 1.1452 1.0353 0.0068  -0.1963 -0.1292 120  ALA A CA  
704  C  C   . ALA A 121 ? 1.8172 1.1412 1.0030 -0.0194 -0.2103 -0.1083 120  ALA A C   
705  O  O   . ALA A 121 ? 1.7990 1.1398 0.9665 -0.0324 -0.2105 -0.1130 120  ALA A O   
706  C  CB  . ALA A 121 ? 1.7301 1.0704 0.9501 0.0317  -0.1862 -0.1209 120  ALA A CB  
707  N  N   . ALA A 122 ? 1.8305 1.1562 1.0350 -0.0283 -0.2226 -0.0842 121  ALA A N   
708  C  CA  . ALA A 122 ? 1.9048 1.2600 1.1206 -0.0497 -0.2353 -0.0624 121  ALA A CA  
709  C  C   . ALA A 122 ? 2.0405 1.3784 1.2257 -0.0779 -0.2494 -0.0695 121  ALA A C   
710  O  O   . ALA A 122 ? 2.1179 1.4852 1.3072 -0.0915 -0.2588 -0.0581 121  ALA A O   
711  C  CB  . ALA A 122 ? 1.8706 1.2283 1.1113 -0.0573 -0.2430 -0.0389 121  ALA A CB  
712  N  N   . LYS A 123 ? 2.1156 1.4032 1.2700 -0.0878 -0.2525 -0.0883 122  LYS A N   
713  C  CA  . LYS A 123 ? 2.2265 1.4921 1.3416 -0.1190 -0.2661 -0.0986 122  LYS A CA  
714  C  C   . LYS A 123 ? 2.1104 1.3341 1.1804 -0.1184 -0.2527 -0.1368 122  LYS A C   
715  O  O   . LYS A 123 ? 2.0460 1.2192 1.0989 -0.1238 -0.2533 -0.1546 122  LYS A O   
716  C  CB  . LYS A 123 ? 2.4430 1.6874 1.5614 -0.1455 -0.2874 -0.0836 122  LYS A CB  
717  C  CG  . LYS A 123 ? 2.4314 1.7243 1.5955 -0.1528 -0.2999 -0.0483 122  LYS A CG  
718  C  CD  . LYS A 123 ? 2.3200 1.6478 1.4842 -0.1717 -0.3155 -0.0365 122  LYS A CD  
719  C  CE  . LYS A 123 ? 2.1451 1.5308 1.3692 -0.1649 -0.3187 -0.0069 122  LYS A CE  
720  N  NZ  . LYS A 123 ? 1.8996 1.2977 1.1528 -0.1912 -0.3399 0.0156  122  LYS A NZ  
721  N  N   . GLY A 124 ? 2.1021 1.3475 1.1560 -0.1116 -0.2386 -0.1502 123  GLY A N   
722  C  CA  . GLY A 124 ? 2.2822 1.4984 1.2909 -0.1161 -0.2220 -0.1884 123  GLY A CA  
723  C  C   . GLY A 124 ? 2.2426 1.4385 1.2650 -0.0838 -0.1962 -0.2172 123  GLY A C   
724  O  O   . GLY A 124 ? 1.8489 1.0648 0.8687 -0.0695 -0.1748 -0.2350 123  GLY A O   
725  N  N   . ASN A 125 ? 2.5386 1.6946 1.5792 -0.0733 -0.1995 -0.2207 124  ASN A N   
726  C  CA  . ASN A 125 ? 2.7441 1.8712 1.8015 -0.0438 -0.1792 -0.2498 124  ASN A CA  
727  C  C   . ASN A 125 ? 2.7234 1.8897 1.8291 -0.0075 -0.1687 -0.2372 124  ASN A C   
728  O  O   . ASN A 125 ? 2.7368 1.8927 1.8793 0.0125  -0.1756 -0.2216 124  ASN A O   
729  C  CB  . ASN A 125 ? 2.7848 1.8524 1.8507 -0.0439 -0.1905 -0.2527 124  ASN A CB  
730  C  CG  . ASN A 125 ? 2.7673 1.7927 1.8463 -0.0182 -0.1706 -0.2908 124  ASN A CG  
731  O  OD1 . ASN A 125 ? 2.6694 1.7197 1.7664 0.0067  -0.1482 -0.3093 124  ASN A OD1 
732  N  ND2 . ASN A 125 ? 2.8775 1.8389 1.9528 -0.0241 -0.1789 -0.3030 124  ASN A ND2 
733  N  N   . GLY A 126 ? 2.6291 1.8393 1.7317 -0.0021 -0.1537 -0.2429 125  GLY A N   
734  C  CA  . GLY A 126 ? 2.5426 1.7888 1.6877 0.0301  -0.1424 -0.2368 125  GLY A CA  
735  C  C   . GLY A 126 ? 2.4711 1.6939 1.6458 0.0600  -0.1268 -0.2634 125  GLY A C   
736  O  O   . GLY A 126 ? 2.7520 1.9874 1.9710 0.0871  -0.1296 -0.2494 125  GLY A O   
737  N  N   . ASP A 127 ? 2.3218 1.5103 1.4728 0.0540  -0.1109 -0.3025 126  ASP A N   
738  C  CA  . ASP A 127 ? 2.2817 1.4488 1.4675 0.0838  -0.0918 -0.3348 126  ASP A CA  
739  C  C   . ASP A 127 ? 2.5374 1.6608 1.7659 0.1064  -0.1079 -0.3239 126  ASP A C   
740  O  O   . ASP A 127 ? 2.6449 1.7641 1.9239 0.1395  -0.0998 -0.3356 126  ASP A O   
741  C  CB  . ASP A 127 ? 2.3660 1.4979 1.5122 0.0680  -0.0696 -0.3832 126  ASP A CB  
742  C  CG  . ASP A 127 ? 2.7017 1.8156 1.8920 0.1008  -0.0447 -0.4225 126  ASP A CG  
743  O  OD1 . ASP A 127 ? 2.8357 1.9663 2.0895 0.1358  -0.0490 -0.4077 126  ASP A OD1 
744  O  OD2 . ASP A 127 ? 2.7925 1.8769 1.9558 0.0911  -0.0209 -0.4686 126  ASP A OD2 
745  N  N   . TYR A 128 ? 2.5138 1.6071 1.7246 0.0867  -0.1330 -0.2982 127  TYR A N   
746  C  CA  . TYR A 128 ? 2.4836 1.5344 1.7275 0.1006  -0.1527 -0.2794 127  TYR A CA  
747  C  C   . TYR A 128 ? 2.4464 1.5431 1.7290 0.1209  -0.1628 -0.2426 127  TYR A C   
748  O  O   . TYR A 128 ? 2.5114 1.5958 1.8391 0.1485  -0.1693 -0.2352 127  TYR A O   
749  C  CB  . TYR A 128 ? 2.5212 1.5335 1.7357 0.0697  -0.1764 -0.2585 127  TYR A CB  
750  C  CG  . TYR A 128 ? 2.5930 1.5626 1.8377 0.0789  -0.1988 -0.2326 127  TYR A CG  
751  C  CD1 . TYR A 128 ? 2.6959 1.5986 1.9595 0.0928  -0.2000 -0.2544 127  TYR A CD1 
752  C  CD2 . TYR A 128 ? 2.6082 1.6035 1.8619 0.0720  -0.2183 -0.1861 127  TYR A CD2 
753  C  CE1 . TYR A 128 ? 2.8069 1.6670 2.0970 0.0988  -0.2239 -0.2262 127  TYR A CE1 
754  C  CE2 . TYR A 128 ? 2.6914 1.6484 1.9659 0.0751  -0.2393 -0.1591 127  TYR A CE2 
755  C  CZ  . TYR A 128 ? 2.7945 1.6828 2.0869 0.0882  -0.2441 -0.1769 127  TYR A CZ  
756  O  OH  . TYR A 128 ? 2.9163 1.7622 2.2286 0.0892  -0.2685 -0.1458 127  TYR A OH  
757  N  N   . ALA A 129 ? 2.2985 1.4476 1.5637 0.1063  -0.1647 -0.2205 128  ALA A N   
758  C  CA  . ALA A 129 ? 2.0711 1.2653 1.3632 0.1194  -0.1724 -0.1882 128  ALA A CA  
759  C  C   . ALA A 129 ? 2.0165 1.2336 1.3493 0.1522  -0.1596 -0.2027 128  ALA A C   
760  O  O   . ALA A 129 ? 2.1277 1.3534 1.4950 0.1708  -0.1720 -0.1806 128  ALA A O   
761  C  CB  . ALA A 129 ? 1.9022 1.1472 1.1721 0.1002  -0.1713 -0.1716 128  ALA A CB  
762  N  N   . PHE A 130 ? 1.8622 1.0922 1.1904 0.1565  -0.1355 -0.2385 129  PHE A N   
763  C  CA  . PHE A 130 ? 1.8777 1.1336 1.2511 0.1867  -0.1203 -0.2563 129  PHE A CA  
764  C  C   . PHE A 130 ? 1.9880 1.1988 1.4079 0.2139  -0.1257 -0.2670 129  PHE A C   
765  O  O   . PHE A 130 ? 2.0911 1.3169 1.5615 0.2399  -0.1357 -0.2520 129  PHE A O   
766  C  CB  . PHE A 130 ? 1.9536 1.2327 1.3083 0.1804  -0.0895 -0.2947 129  PHE A CB  
767  C  CG  . PHE A 130 ? 2.0879 1.4134 1.4893 0.2060  -0.0717 -0.3087 129  PHE A CG  
768  C  CD1 . PHE A 130 ? 2.0589 1.4088 1.5112 0.2302  -0.0870 -0.2835 129  PHE A CD1 
769  C  CD2 . PHE A 130 ? 2.2671 1.6131 1.6602 0.2027  -0.0397 -0.3472 129  PHE A CD2 
770  C  CE1 . PHE A 130 ? 2.0603 1.4565 1.5595 0.2517  -0.0728 -0.2954 129  PHE A CE1 
771  C  CE2 . PHE A 130 ? 2.2540 1.6472 1.6946 0.2241  -0.0220 -0.3604 129  PHE A CE2 
772  C  CZ  . PHE A 130 ? 2.1475 1.5666 1.6444 0.2495  -0.0395 -0.3343 129  PHE A CZ  
773  N  N   . LYS A 131 ? 2.0659 1.2190 1.4694 0.2066  -0.1217 -0.2917 130  LYS A N   
774  C  CA  . LYS A 131 ? 2.2324 1.3372 1.6847 0.2344  -0.1222 -0.3109 130  LYS A CA  
775  C  C   . LYS A 131 ? 2.2721 1.3506 1.7598 0.2481  -0.1565 -0.2691 130  LYS A C   
776  O  O   . LYS A 131 ? 2.2285 1.2990 1.7784 0.2805  -0.1629 -0.2691 130  LYS A O   
777  C  CB  . LYS A 131 ? 2.1570 1.1988 1.5767 0.2190  -0.1110 -0.3479 130  LYS A CB  
778  C  CG  . LYS A 131 ? 2.1098 1.1070 1.5842 0.2507  -0.0988 -0.3847 130  LYS A CG  
779  C  CD  . LYS A 131 ? 2.2144 1.1392 1.6524 0.2326  -0.0911 -0.4200 130  LYS A CD  
780  C  CE  . LYS A 131 ? 2.3041 1.1771 1.8054 0.2673  -0.0807 -0.4560 130  LYS A CE  
781  N  NZ  . LYS A 131 ? 2.3679 1.1665 1.8307 0.2482  -0.0698 -0.4973 130  LYS A NZ  
782  N  N   . VAL A 132 ? 2.2045 1.2731 1.6548 0.2221  -0.1792 -0.2319 131  VAL A N   
783  C  CA  . VAL A 132 ? 2.1674 1.2113 1.6396 0.2272  -0.2115 -0.1892 131  VAL A CA  
784  C  C   . VAL A 132 ? 2.1162 1.2129 1.6248 0.2468  -0.2218 -0.1614 131  VAL A C   
785  O  O   . VAL A 132 ? 2.2907 1.3670 1.8400 0.2651  -0.2452 -0.1378 131  VAL A O   
786  C  CB  . VAL A 132 ? 2.6919 1.7223 2.1137 0.1903  -0.2286 -0.1572 131  VAL A CB  
787  C  CG1 . VAL A 132 ? 2.5061 1.6017 1.8937 0.1703  -0.2195 -0.1454 131  VAL A CG1 
788  C  CG2 . VAL A 132 ? 2.8007 1.8028 2.2385 0.1902  -0.2605 -0.1126 131  VAL A CG2 
789  N  N   . VAL A 133 ? 1.8983 1.0603 1.3917 0.2412  -0.2066 -0.1632 132  VAL A N   
790  C  CA  . VAL A 133 ? 1.8663 1.0812 1.3885 0.2557  -0.2148 -0.1409 132  VAL A CA  
791  C  C   . VAL A 133 ? 1.7851 1.0104 1.3745 0.2923  -0.2090 -0.1613 132  VAL A C   
792  O  O   . VAL A 133 ? 1.6474 0.8856 1.2787 0.3100  -0.2308 -0.1358 132  VAL A O   
793  C  CB  . VAL A 133 ? 1.8433 1.1205 1.3328 0.2390  -0.1990 -0.1408 132  VAL A CB  
794  C  CG1 . VAL A 133 ? 1.6774 1.0052 1.1953 0.2522  -0.2074 -0.1214 132  VAL A CG1 
795  C  CG2 . VAL A 133 ? 2.0302 1.3035 1.4680 0.2067  -0.2065 -0.1176 132  VAL A CG2 
796  N  N   . LYS A 134 ? 1.8224 1.0450 1.4231 0.3020  -0.1796 -0.2075 133  LYS A N   
797  C  CA  . LYS A 134 ? 1.9284 1.1634 1.6011 0.3376  -0.1683 -0.2334 133  LYS A CA  
798  C  C   . LYS A 134 ? 2.1647 1.3436 1.8936 0.3632  -0.1934 -0.2224 133  LYS A C   
799  O  O   . LYS A 134 ? 2.1819 1.3791 1.9796 0.3923  -0.2073 -0.2115 133  LYS A O   
800  C  CB  . LYS A 134 ? 1.9651 1.2014 1.6312 0.3380  -0.1274 -0.2892 133  LYS A CB  
801  C  CG  . LYS A 134 ? 1.9077 1.1887 1.5136 0.3093  -0.1039 -0.3007 133  LYS A CG  
802  C  CD  . LYS A 134 ? 1.9699 1.2589 1.5746 0.3104  -0.0629 -0.3554 133  LYS A CD  
803  C  CE  . LYS A 134 ? 2.0226 1.3353 1.7128 0.3484  -0.0475 -0.3805 133  LYS A CE  
804  N  NZ  . LYS A 134 ? 1.9708 1.2747 1.6618 0.3500  -0.0051 -0.4398 133  LYS A NZ  
805  N  N   . GLU A 135 ? 2.4076 1.5171 2.1093 0.3511  -0.2011 -0.2244 134  GLU A N   
806  C  CA  . GLU A 135 ? 2.4118 1.4555 2.1583 0.3697  -0.2287 -0.2095 134  GLU A CA  
807  C  C   . GLU A 135 ? 2.2263 1.2784 1.9814 0.3675  -0.2711 -0.1482 134  GLU A C   
808  O  O   . GLU A 135 ? 2.0679 1.0937 1.8829 0.3919  -0.2993 -0.1269 134  GLU A O   
809  C  CB  . GLU A 135 ? 2.4387 1.4087 2.1387 0.3473  -0.2277 -0.2225 134  GLU A CB  
810  C  CG  . GLU A 135 ? 2.4353 1.3763 2.1433 0.3565  -0.1918 -0.2856 134  GLU A CG  
811  C  CD  . GLU A 135 ? 2.4777 1.3374 2.1452 0.3350  -0.1959 -0.2982 134  GLU A CD  
812  O  OE1 . GLU A 135 ? 2.4404 1.2863 2.0513 0.3015  -0.2158 -0.2643 134  GLU A OE1 
813  O  OE2 . GLU A 135 ? 2.6257 1.4355 2.3208 0.3510  -0.1786 -0.3432 134  GLU A OE2 
814  N  N   . PHE A 136 ? 2.2778 1.3678 1.9724 0.3368  -0.2753 -0.1204 135  PHE A N   
815  C  CA  . PHE A 136 ? 2.3038 1.4085 1.9901 0.3267  -0.3097 -0.0658 135  PHE A CA  
816  C  C   . PHE A 136 ? 2.3498 1.5095 2.0876 0.3497  -0.3211 -0.0519 135  PHE A C   
817  O  O   . PHE A 136 ? 2.4524 1.5985 2.2227 0.3593  -0.3570 -0.0143 135  PHE A O   
818  C  CB  . PHE A 136 ? 2.3200 1.4540 1.9306 0.2880  -0.3041 -0.0481 135  PHE A CB  
819  C  CG  . PHE A 136 ? 2.4449 1.5882 2.0345 0.2706  -0.3347 0.0043  135  PHE A CG  
820  C  CD1 . PHE A 136 ? 2.6166 1.7033 2.1953 0.2574  -0.3632 0.0379  135  PHE A CD1 
821  C  CD2 . PHE A 136 ? 2.4205 1.6281 1.9979 0.2644  -0.3345 0.0193  135  PHE A CD2 
822  C  CE1 . PHE A 136 ? 2.6171 1.7143 2.1694 0.2367  -0.3895 0.0861  135  PHE A CE1 
823  C  CE2 . PHE A 136 ? 2.4147 1.6312 1.9655 0.2447  -0.3601 0.0642  135  PHE A CE2 
824  C  CZ  . PHE A 136 ? 2.5103 1.6731 2.0469 0.2300  -0.3870 0.0979  135  PHE A CZ  
825  N  N   . VAL A 137 ? 2.3421 1.5636 2.0857 0.3555  -0.2928 -0.0799 136  VAL A N   
826  C  CA  . VAL A 137 ? 2.3906 1.6713 2.1818 0.3736  -0.3018 -0.0691 136  VAL A CA  
827  C  C   . VAL A 137 ? 2.4173 1.6807 2.3030 0.4143  -0.3139 -0.0776 136  VAL A C   
828  O  O   . VAL A 137 ? 2.3623 1.6603 2.3012 0.4314  -0.3370 -0.0555 136  VAL A O   
829  C  CB  . VAL A 137 ? 2.2620 1.6096 2.0397 0.3687  -0.2665 -0.0998 136  VAL A CB  
830  C  CG1 . VAL A 137 ? 2.2735 1.6182 2.0844 0.3876  -0.2299 -0.1535 136  VAL A CG1 
831  C  CG2 . VAL A 137 ? 2.1927 1.6034 2.0040 0.3767  -0.2806 -0.0803 136  VAL A CG2 
832  N  N   . SER A 138 ? 2.4076 1.6164 2.3162 0.4291  -0.2991 -0.1103 137  SER A N   
833  C  CA  . SER A 138 ? 2.4682 1.6510 2.4730 0.4702  -0.3074 -0.1240 137  SER A CA  
834  C  C   . SER A 138 ? 2.5503 1.6963 2.5902 0.4789  -0.3616 -0.0693 137  SER A C   
835  O  O   . SER A 138 ? 2.6339 1.7923 2.7627 0.5121  -0.3821 -0.0601 137  SER A O   
836  C  CB  . SER A 138 ? 2.6336 1.7547 2.6421 0.4783  -0.2795 -0.1720 137  SER A CB  
837  O  OG  . SER A 138 ? 2.5789 1.7242 2.5271 0.4569  -0.2356 -0.2131 137  SER A OG  
838  N  N   . VAL A 139 ? 2.6927 1.7950 2.6648 0.4476  -0.3856 -0.0316 138  VAL A N   
839  C  CA  . VAL A 139 ? 2.8831 1.9444 2.8736 0.4476  -0.4384 0.0249  138  VAL A CA  
840  C  C   . VAL A 139 ? 3.0370 2.1594 3.0520 0.4506  -0.4688 0.0648  138  VAL A C   
841  O  O   . VAL A 139 ? 3.3289 2.4472 3.4262 0.4801  -0.5008 0.0844  138  VAL A O   
842  C  CB  . VAL A 139 ? 2.8378 1.8533 2.7393 0.4050  -0.4532 0.0582  138  VAL A CB  
843  C  CG1 . VAL A 139 ? 2.9409 1.9189 2.8532 0.3990  -0.5086 0.1213  138  VAL A CG1 
844  C  CG2 . VAL A 139 ? 2.7700 1.7198 2.6506 0.3998  -0.4304 0.0230  138  VAL A CG2 
845  N  N   . GLY A 140 ? 2.9522 2.1301 2.8978 0.4195  -0.4601 0.0766  139  GLY A N   
846  C  CA  . GLY A 140 ? 2.7923 2.0347 2.7526 0.4185  -0.4819 0.1048  139  GLY A CA  
847  C  C   . GLY A 140 ? 2.7574 1.9814 2.7083 0.4039  -0.5379 0.1696  139  GLY A C   
848  O  O   . GLY A 140 ? 2.5882 1.8646 2.5311 0.3930  -0.5578 0.1963  139  GLY A O   
849  N  N   . GLY A 141 ? 2.8461 1.9946 2.7938 0.4001  -0.5645 0.1961  140  GLY A N   
850  C  CA  . GLY A 141 ? 2.8651 1.9900 2.8002 0.3827  -0.6202 0.2615  140  GLY A CA  
851  C  C   . GLY A 141 ? 2.8005 1.9540 2.6290 0.3321  -0.6203 0.2893  140  GLY A C   
852  O  O   . GLY A 141 ? 2.8325 2.0261 2.6446 0.3167  -0.6480 0.3243  140  GLY A O   
853  N  N   . VAL A 142 ? 2.7367 1.8711 2.4940 0.3053  -0.5886 0.2721  141  VAL A N   
854  C  CA  . VAL A 142 ? 2.6730 1.8421 2.3360 0.2604  -0.5764 0.2860  141  VAL A CA  
855  C  C   . VAL A 142 ? 2.5199 1.7111 2.1524 0.2564  -0.5220 0.2340  141  VAL A C   
856  O  O   . VAL A 142 ? 2.4473 1.6279 2.0142 0.2247  -0.5049 0.2348  141  VAL A O   
857  C  CB  . VAL A 142 ? 2.6986 1.8184 2.2985 0.2209  -0.6026 0.3340  141  VAL A CB  
858  C  CG1 . VAL A 142 ? 2.6266 1.7936 2.1398 0.1762  -0.5948 0.3524  141  VAL A CG1 
859  C  CG2 . VAL A 142 ? 2.6902 1.7651 2.3313 0.2292  -0.6602 0.3852  141  VAL A CG2 
860  N  N   . SER A 143 ? 2.4835 1.7069 2.1672 0.2880  -0.4959 0.1901  142  SER A N   
861  C  CA  . SER A 143 ? 2.6130 1.8567 2.2721 0.2853  -0.4476 0.1419  142  SER A CA  
862  C  C   . SER A 143 ? 2.6655 1.9629 2.2575 0.2536  -0.4303 0.1447  142  SER A C   
863  O  O   . SER A 143 ? 2.5661 1.8573 2.1040 0.2289  -0.4085 0.1363  142  SER A O   
864  C  CB  . SER A 143 ? 2.5736 1.8441 2.3007 0.3228  -0.4246 0.0974  142  SER A CB  
865  O  OG  . SER A 143 ? 2.4561 1.7865 2.2159 0.3334  -0.4351 0.1054  142  SER A OG  
866  N  N   . ILE A 144 ? 2.7974 2.1469 2.3978 0.2546  -0.4414 0.1563  143  ILE A N   
867  C  CA  . ILE A 144 ? 2.7200 2.1210 2.2640 0.2272  -0.4255 0.1556  143  ILE A CA  
868  C  C   . ILE A 144 ? 2.5840 2.0036 2.1090 0.2253  -0.3803 0.1122  143  ILE A C   
869  O  O   . ILE A 144 ? 2.6048 2.0275 2.0740 0.1981  -0.3637 0.1121  143  ILE A O   
870  C  CB  . ILE A 144 ? 2.6660 2.0522 2.1399 0.1875  -0.4409 0.1940  143  ILE A CB  
871  C  CG1 . ILE A 144 ? 2.7934 2.1401 2.2811 0.1862  -0.4885 0.2410  143  ILE A CG1 
872  C  CG2 . ILE A 144 ? 2.5980 2.0390 2.0229 0.1619  -0.4308 0.1958  143  ILE A CG2 
873  C  CD1 . ILE A 144 ? 2.8206 2.2008 2.3372 0.1942  -0.5217 0.2643  143  ILE A CD1 
874  N  N   . PRO A 145 ? 2.4351 1.8670 2.0087 0.2531  -0.3606 0.0759  144  PRO A N   
875  C  CA  . PRO A 145 ? 2.2093 1.6486 1.7628 0.2493  -0.3219 0.0380  144  PRO A CA  
876  C  C   . PRO A 145 ? 2.0082 1.4959 1.5189 0.2277  -0.3030 0.0320  144  PRO A C   
877  O  O   . PRO A 145 ? 2.0193 1.5525 1.5470 0.2336  -0.3003 0.0254  144  PRO A O   
878  C  CB  . PRO A 145 ? 2.1597 1.6101 1.7749 0.2814  -0.3075 0.0041  144  PRO A CB  
879  C  CG  . PRO A 145 ? 2.2503 1.7322 1.9143 0.2978  -0.3325 0.0222  144  PRO A CG  
880  C  CD  . PRO A 145 ? 2.3636 1.8111 2.0127 0.2868  -0.3714 0.0679  144  PRO A CD  
881  N  N   . ARG A 146 ? 1.9351 1.4125 1.3953 0.2029  -0.2904 0.0340  145  ARG A N   
882  C  CA  . ARG A 146 ? 1.8892 1.4071 1.3138 0.1835  -0.2725 0.0280  145  ARG A CA  
883  C  C   . ARG A 146 ? 1.9220 1.4502 1.3480 0.1871  -0.2429 -0.0061 145  ARG A C   
884  O  O   . ARG A 146 ? 1.8664 1.3638 1.3003 0.1939  -0.2354 -0.0211 145  ARG A O   
885  C  CB  . ARG A 146 ? 1.8195 1.3282 1.1951 0.1539  -0.2746 0.0499  145  ARG A CB  
886  C  CG  . ARG A 146 ? 1.7191 1.2702 1.0650 0.1359  -0.2584 0.0448  145  ARG A CG  
887  C  CD  . ARG A 146 ? 1.7771 1.3240 1.0803 0.1070  -0.2540 0.0610  145  ARG A CD  
888  N  NE  . ARG A 146 ? 2.0781 1.6146 1.3594 0.0924  -0.2781 0.0938  145  ARG A NE  
889  C  CZ  . ARG A 146 ? 2.1795 1.7140 1.4203 0.0635  -0.2755 0.1115  145  ARG A CZ  
890  N  NH1 . ARG A 146 ? 2.0743 1.6190 1.3016 0.0498  -0.2494 0.0980  145  ARG A NH1 
891  N  NH2 . ARG A 146 ? 2.2499 1.7739 1.4655 0.0471  -0.2995 0.1436  145  ARG A NH2 
892  N  N   . LEU A 147 ? 1.9982 1.5675 1.4151 0.1808  -0.2277 -0.0179 146  LEU A N   
893  C  CA  . LEU A 147 ? 1.9154 1.4957 1.3283 0.1793  -0.2029 -0.0446 146  LEU A CA  
894  C  C   . LEU A 147 ? 1.8585 1.4117 1.2443 0.1642  -0.1947 -0.0458 146  LEU A C   
895  O  O   . LEU A 147 ? 1.8923 1.4338 1.2785 0.1659  -0.1824 -0.0653 146  LEU A O   
896  C  CB  . LEU A 147 ? 1.9836 1.6065 1.3869 0.1703  -0.1921 -0.0503 146  LEU A CB  
897  C  CG  . LEU A 147 ? 1.8660 1.5011 1.2640 0.1659  -0.1701 -0.0726 146  LEU A CG  
898  C  CD1 . LEU A 147 ? 1.8653 1.5377 1.2826 0.1720  -0.1630 -0.0856 146  LEU A CD1 
899  C  CD2 . LEU A 147 ? 1.6372 1.2739 1.0067 0.1463  -0.1625 -0.0676 146  LEU A CD2 
900  N  N   . ARG A 148 ? 1.8652 1.4105 1.2268 0.1469  -0.2017 -0.0249 147  ARG A N   
901  C  CA  . ARG A 148 ? 1.8247 1.3511 1.1669 0.1305  -0.1955 -0.0233 147  ARG A CA  
902  C  C   . ARG A 148 ? 1.8376 1.3191 1.1856 0.1354  -0.2016 -0.0280 147  ARG A C   
903  O  O   . ARG A 148 ? 1.7383 1.2056 1.0744 0.1238  -0.1953 -0.0348 147  ARG A O   
904  C  CB  . ARG A 148 ? 1.8806 1.4105 1.2008 0.1103  -0.2001 0.0000  147  ARG A CB  
905  C  CG  . ARG A 148 ? 2.0700 1.5695 1.3854 0.1076  -0.2210 0.0244  147  ARG A CG  
906  C  CD  . ARG A 148 ? 2.1697 1.6768 1.4569 0.0818  -0.2210 0.0461  147  ARG A CD  
907  N  NE  . ARG A 148 ? 2.1900 1.6706 1.4673 0.0759  -0.2441 0.0743  147  ARG A NE  
908  C  CZ  . ARG A 148 ? 2.1157 1.5559 1.3887 0.0669  -0.2558 0.0900  147  ARG A CZ  
909  N  NH1 . ARG A 148 ? 2.3408 1.7653 1.6177 0.0618  -0.2459 0.0784  147  ARG A NH1 
910  N  NH2 . ARG A 148 ? 1.8912 1.3054 1.1551 0.0606  -0.2799 0.1192  147  ARG A NH2 
911  N  N   . THR A 149 ? 1.8779 1.3355 1.2458 0.1516  -0.2158 -0.0238 148  THR A N   
912  C  CA  . THR A 149 ? 1.9552 1.3659 1.3336 0.1598  -0.2197 -0.0344 148  THR A CA  
913  C  C   . THR A 149 ? 1.9890 1.4049 1.3755 0.1695  -0.2003 -0.0691 148  THR A C   
914  O  O   . THR A 149 ? 2.1170 1.5058 1.4885 0.1606  -0.1938 -0.0836 148  THR A O   
915  C  CB  . THR A 149 ? 2.0059 1.3888 1.4143 0.1788  -0.2402 -0.0226 148  THR A CB  
916  O  OG1 . THR A 149 ? 2.0216 1.4206 1.4679 0.2048  -0.2330 -0.0451 148  THR A OG1 
917  C  CG2 . THR A 149 ? 2.0796 1.4760 1.4802 0.1707  -0.2598 0.0120  148  THR A CG2 
918  N  N   . TYR A 150 ? 1.7914 1.2425 1.1996 0.1849  -0.1917 -0.0819 149  TYR A N   
919  C  CA  . TYR A 150 ? 1.6389 1.1044 1.0521 0.1907  -0.1703 -0.1137 149  TYR A CA  
920  C  C   . TYR A 150 ? 1.7276 1.2067 1.1057 0.1684  -0.1576 -0.1197 149  TYR A C   
921  O  O   . TYR A 150 ? 1.6383 1.1149 1.0055 0.1642  -0.1427 -0.1432 149  TYR A O   
922  C  CB  . TYR A 150 ? 1.6460 1.1550 1.0906 0.2071  -0.1648 -0.1204 149  TYR A CB  
923  C  CG  . TYR A 150 ? 1.7166 1.2180 1.2105 0.2342  -0.1699 -0.1289 149  TYR A CG  
924  C  CD1 . TYR A 150 ? 1.7180 1.1816 1.2269 0.2457  -0.1624 -0.1517 149  TYR A CD1 
925  C  CD2 . TYR A 150 ? 1.6839 1.2163 1.2128 0.2482  -0.1831 -0.1148 149  TYR A CD2 
926  C  CE1 . TYR A 150 ? 1.6197 1.0771 1.1852 0.2741  -0.1661 -0.1613 149  TYR A CE1 
927  C  CE2 . TYR A 150 ? 1.5710 1.1004 1.1562 0.2750  -0.1906 -0.1203 149  TYR A CE2 
928  C  CZ  . TYR A 150 ? 1.5495 1.0414 1.1566 0.2896  -0.1812 -0.1439 149  TYR A CZ  
929  O  OH  . TYR A 150 ? 1.6427 1.1317 1.3163 0.3195  -0.1878 -0.1511 149  TYR A OH  
930  N  N   . ALA A 151 ? 1.8905 1.3848 1.2521 0.1533  -0.1637 -0.0983 150  ALA A N   
931  C  CA  . ALA A 151 ? 1.8351 1.3494 1.1760 0.1356  -0.1546 -0.1000 150  ALA A CA  
932  C  C   . ALA A 151 ? 1.8226 1.3104 1.1413 0.1197  -0.1531 -0.1084 150  ALA A C   
933  O  O   . ALA A 151 ? 1.8455 1.3429 1.1518 0.1124  -0.1432 -0.1230 150  ALA A O   
934  C  CB  . ALA A 151 ? 1.9253 1.4591 1.2613 0.1248  -0.1599 -0.0777 150  ALA A CB  
935  N  N   . PRO A 152 ? 1.8568 1.3110 1.1677 0.1109  -0.1644 -0.0979 151  PRO A N   
936  C  CA  . PRO A 152 ? 1.7364 1.1690 1.0246 0.0914  -0.1659 -0.1043 151  PRO A CA  
937  C  C   . PRO A 152 ? 1.7022 1.1141 0.9779 0.0940  -0.1559 -0.1337 151  PRO A C   
938  O  O   . PRO A 152 ? 1.9238 1.3325 1.1739 0.0756  -0.1535 -0.1428 151  PRO A O   
939  C  CB  . PRO A 152 ? 1.7870 1.1858 1.0734 0.0826  -0.1803 -0.0881 151  PRO A CB  
940  C  CG  . PRO A 152 ? 1.8849 1.2969 1.1880 0.0924  -0.1857 -0.0675 151  PRO A CG  
941  C  CD  . PRO A 152 ? 1.8998 1.3318 1.2192 0.1147  -0.1782 -0.0792 151  PRO A CD  
942  N  N   . ALA A 153 ? 1.5520 0.9517 0.8469 0.1156  -0.1503 -0.1485 152  ALA A N   
943  C  CA  . ALA A 153 ? 1.7743 1.1580 1.0628 0.1202  -0.1347 -0.1820 152  ALA A CA  
944  C  C   . ALA A 153 ? 1.8738 1.2949 1.1478 0.1123  -0.1185 -0.1950 152  ALA A C   
945  O  O   . ALA A 153 ? 1.8757 1.2861 1.1169 0.0946  -0.1097 -0.2136 152  ALA A O   
946  C  CB  . ALA A 153 ? 1.7623 1.1352 1.0898 0.1494  -0.1309 -0.1942 152  ALA A CB  
947  N  N   . LEU A 154 ? 1.8829 1.3459 1.1774 0.1221  -0.1159 -0.1842 153  LEU A N   
948  C  CA  . LEU A 154 ? 1.8155 1.3134 1.0987 0.1134  -0.1023 -0.1926 153  LEU A CA  
949  C  C   . LEU A 154 ? 1.8010 1.3023 1.0516 0.0864  -0.1101 -0.1787 153  LEU A C   
950  O  O   . LEU A 154 ? 1.9054 1.4103 1.1277 0.0691  -0.1018 -0.1905 153  LEU A O   
951  C  CB  . LEU A 154 ? 1.7223 1.2608 1.0373 0.1290  -0.1003 -0.1833 153  LEU A CB  
952  C  CG  . LEU A 154 ? 1.5304 1.1058 0.8385 0.1196  -0.0880 -0.1885 153  LEU A CG  
953  C  CD1 . LEU A 154 ? 1.2334 0.8412 0.5775 0.1386  -0.0774 -0.1984 153  LEU A CD1 
954  C  CD2 . LEU A 154 ? 1.5752 1.1653 0.8761 0.1073  -0.0995 -0.1640 153  LEU A CD2 
955  N  N   . LEU A 155 ? 1.6608 1.1622 0.9171 0.0815  -0.1262 -0.1532 154  LEU A N   
956  C  CA  . LEU A 155 ? 1.6607 1.1699 0.9009 0.0595  -0.1358 -0.1376 154  LEU A CA  
957  C  C   . LEU A 155 ? 1.8024 1.2836 1.0071 0.0364  -0.1415 -0.1451 154  LEU A C   
958  O  O   . LEU A 155 ? 1.8931 1.3823 1.0755 0.0164  -0.1452 -0.1417 154  LEU A O   
959  C  CB  . LEU A 155 ? 1.5839 1.0999 0.8444 0.0597  -0.1485 -0.1126 154  LEU A CB  
960  C  CG  . LEU A 155 ? 1.6068 1.1576 0.8908 0.0685  -0.1451 -0.1012 154  LEU A CG  
961  C  CD1 . LEU A 155 ? 1.6886 1.2513 0.9872 0.0889  -0.1363 -0.1095 154  LEU A CD1 
962  C  CD2 . LEU A 155 ? 1.4596 1.0171 0.7603 0.0641  -0.1534 -0.0811 154  LEU A CD2 
963  N  N   . CYS A 156 ? 1.7535 1.1993 0.9512 0.0370  -0.1446 -0.1541 155  CYS A N   
964  C  CA  . CYS A 156 ? 1.7855 1.2002 0.9454 0.0127  -0.1508 -0.1642 155  CYS A CA  
965  C  C   . CYS A 156 ? 1.7638 1.1771 0.8907 0.0041  -0.1331 -0.1926 155  CYS A C   
966  O  O   . CYS A 156 ? 1.7687 1.1777 0.8560 -0.0240 -0.1387 -0.1935 155  CYS A O   
967  C  CB  . CYS A 156 ? 1.9482 1.3205 1.1097 0.0159  -0.1568 -0.1701 155  CYS A CB  
968  S  SG  . CYS A 156 ? 1.7696 1.1003 0.8841 -0.0190 -0.1695 -0.1794 155  CYS A SG  
969  N  N   . PHE A 157 ? 1.7614 1.1806 0.9052 0.0264  -0.1121 -0.2150 156  PHE A N   
970  C  CA  . PHE A 157 ? 1.9772 1.4035 1.0955 0.0191  -0.0890 -0.2445 156  PHE A CA  
971  C  C   . PHE A 157 ? 1.8654 1.3275 0.9666 0.0018  -0.0884 -0.2316 156  PHE A C   
972  O  O   . PHE A 157 ? 1.8266 1.2899 0.8857 -0.0214 -0.0773 -0.2470 156  PHE A O   
973  C  CB  . PHE A 157 ? 2.0721 1.5076 1.2290 0.0502  -0.0671 -0.2679 156  PHE A CB  
974  C  CG  . PHE A 157 ? 2.2564 1.6493 1.4244 0.0642  -0.0629 -0.2902 156  PHE A CG  
975  C  CD1 . PHE A 157 ? 2.4964 1.8444 1.6262 0.0429  -0.0717 -0.2980 156  PHE A CD1 
976  C  CD2 . PHE A 157 ? 2.3439 1.7398 1.5631 0.0978  -0.0527 -0.3026 156  PHE A CD2 
977  C  CE1 . PHE A 157 ? 2.7519 2.0542 1.8926 0.0550  -0.0684 -0.3196 156  PHE A CE1 
978  C  CE2 . PHE A 157 ? 2.5526 1.9041 1.7879 0.1122  -0.0509 -0.3222 156  PHE A CE2 
979  C  CZ  . PHE A 157 ? 2.6830 1.9855 1.8781 0.0909  -0.0577 -0.3317 156  PHE A CZ  
980  N  N   . CYS A 158 ? 1.7919 1.2811 0.9244 0.0117  -0.0999 -0.2039 157  CYS A N   
981  C  CA  . CYS A 158 ? 1.8157 1.3339 0.9400 -0.0025 -0.1029 -0.1880 157  CYS A CA  
982  C  C   . CYS A 158 ? 1.7981 1.3043 0.8881 -0.0341 -0.1247 -0.1688 157  CYS A C   
983  O  O   . CYS A 158 ? 1.6020 1.1158 0.6589 -0.0582 -0.1254 -0.1658 157  CYS A O   
984  C  CB  . CYS A 158 ? 1.7774 1.3231 0.9471 0.0178  -0.1083 -0.1676 157  CYS A CB  
985  S  SG  . CYS A 158 ? 2.1614 1.7387 1.3622 0.0418  -0.0853 -0.1847 157  CYS A SG  
986  N  N   . GLU A 159 ? 1.9260 1.4154 1.0267 -0.0353 -0.1446 -0.1529 158  GLU A N   
987  C  CA  . GLU A 159 ? 2.0154 1.4965 1.0949 -0.0637 -0.1696 -0.1318 158  GLU A CA  
988  C  C   . GLU A 159 ? 2.2724 1.7275 1.2897 -0.0949 -0.1696 -0.1495 158  GLU A C   
989  O  O   . GLU A 159 ? 2.4609 1.9191 1.4515 -0.1245 -0.1865 -0.1332 158  GLU A O   
990  C  CB  . GLU A 159 ? 1.9482 1.4210 1.0588 -0.0579 -0.1874 -0.1139 158  GLU A CB  
991  C  CG  . GLU A 159 ? 2.1891 1.6602 1.2938 -0.0845 -0.2162 -0.0890 158  GLU A CG  
992  C  CD  . GLU A 159 ? 2.3724 1.8743 1.5120 -0.0830 -0.2286 -0.0614 158  GLU A CD  
993  O  OE1 . GLU A 159 ? 2.3403 1.8595 1.4858 -0.0726 -0.2159 -0.0641 158  GLU A OE1 
994  O  OE2 . GLU A 159 ? 2.5592 2.0680 1.7248 -0.0921 -0.2514 -0.0376 158  GLU A OE2 
995  N  N   . LYS A 160 ? 2.1962 1.6276 1.1966 -0.0884 -0.1503 -0.1820 159  LYS A N   
996  C  CA  . LYS A 160 ? 1.9371 1.3520 0.8941 -0.1153 -0.1411 -0.2044 159  LYS A CA  
997  C  C   . LYS A 160 ? 1.7963 1.2406 0.7416 -0.1231 -0.1139 -0.2215 159  LYS A C   
998  O  O   . LYS A 160 ? 2.0469 1.4880 0.9622 -0.1447 -0.1004 -0.2419 159  LYS A O   
999  C  CB  . LYS A 160 ? 1.9108 1.2839 0.8611 -0.1040 -0.1309 -0.2349 159  LYS A CB  
1000 C  CG  . LYS A 160 ? 1.8482 1.1870 0.7909 -0.1159 -0.1593 -0.2204 159  LYS A CG  
1001 C  CD  . LYS A 160 ? 1.8145 1.1156 0.7743 -0.0954 -0.1504 -0.2426 159  LYS A CD  
1002 C  CE  . LYS A 160 ? 1.8419 1.1169 0.7710 -0.0982 -0.1223 -0.2888 159  LYS A CE  
1003 N  NZ  . LYS A 160 ? 1.8466 1.0780 0.7983 -0.0753 -0.1159 -0.3101 159  LYS A NZ  
1004 N  N   . LEU A 161 ? 1.6327 1.1055 0.6009 -0.1062 -0.1053 -0.2147 160  LEU A N   
1005 C  CA  . LEU A 161 ? 1.5974 1.1026 0.5574 -0.1152 -0.0819 -0.2257 160  LEU A CA  
1006 C  C   . LEU A 161 ? 1.6081 1.1133 0.5658 -0.1037 -0.0453 -0.2704 160  LEU A C   
1007 O  O   . LEU A 161 ? 1.6345 1.1642 0.5764 -0.1191 -0.0232 -0.2856 160  LEU A O   
1008 C  CB  . LEU A 161 ? 1.5562 1.0719 0.4826 -0.1552 -0.0936 -0.2073 160  LEU A CB  
1009 C  CG  . LEU A 161 ? 1.5708 1.0987 0.5048 -0.1677 -0.1233 -0.1640 160  LEU A CG  
1010 C  CD1 . LEU A 161 ? 1.5029 1.0113 0.4560 -0.1607 -0.1556 -0.1391 160  LEU A CD1 
1011 C  CD2 . LEU A 161 ? 1.7597 1.2950 0.6571 -0.2075 -0.1313 -0.1490 160  LEU A CD2 
1012 N  N   . GLU A 162 ? 1.6982 1.1745 0.6735 -0.0762 -0.0392 -0.2913 161  GLU A N   
1013 C  CA  . GLU A 162 ? 1.9302 1.4041 0.9163 -0.0577 -0.0047 -0.3349 161  GLU A CA  
1014 C  C   . GLU A 162 ? 2.0599 1.5644 1.0831 -0.0300 0.0097  -0.3367 161  GLU A C   
1015 O  O   . GLU A 162 ? 2.0810 1.5899 1.1615 0.0034  0.0009  -0.3252 161  GLU A O   
1016 C  CB  . GLU A 162 ? 2.1099 1.5334 1.1048 -0.0372 -0.0067 -0.3550 161  GLU A CB  
1017 C  CG  . GLU A 162 ? 2.2835 1.6734 1.2525 -0.0596 -0.0350 -0.3376 161  GLU A CG  
1018 C  CD  . GLU A 162 ? 2.5242 1.8836 1.4721 -0.0730 -0.0209 -0.3723 161  GLU A CD  
1019 O  OE1 . GLU A 162 ? 2.5121 1.8768 1.4705 -0.0617 0.0123  -0.4119 161  GLU A OE1 
1020 O  OE2 . GLU A 162 ? 2.6810 2.0124 1.6045 -0.0949 -0.0427 -0.3613 161  GLU A OE2 
1021 N  N   . ALA A 163 ? 2.1624 1.7054 1.1757 -0.0454 0.0303  -0.3439 162  ALA A N   
1022 C  CA  . ALA A 163 ? 2.1023 1.6864 1.1574 -0.0264 0.0401  -0.3377 162  ALA A CA  
1023 C  C   . ALA A 163 ? 1.9894 1.5882 1.1073 0.0115  0.0636  -0.3663 162  ALA A C   
1024 O  O   . ALA A 163 ? 1.6861 1.3016 0.8618 0.0414  0.0524  -0.3500 162  ALA A O   
1025 C  CB  . ALA A 163 ? 2.1124 1.7300 1.1342 -0.0583 0.0554  -0.3374 162  ALA A CB  
1026 N  N   . GLU A 164 ? 2.0130 1.6057 1.1202 0.0090  0.0956  -0.4091 163  GLU A N   
1027 C  CA  . GLU A 164 ? 2.1202 1.7283 1.2947 0.0456  0.1203  -0.4402 163  GLU A CA  
1028 C  C   . GLU A 164 ? 2.0352 1.6102 1.2581 0.0810  0.0980  -0.4312 163  GLU A C   
1029 O  O   . GLU A 164 ? 1.8911 1.4839 1.1854 0.1167  0.1015  -0.4359 163  GLU A O   
1030 C  CB  . GLU A 164 ? 2.3421 1.9447 1.4926 0.0337  0.1618  -0.4927 163  GLU A CB  
1031 C  CG  . GLU A 164 ? 2.3770 2.0339 1.5221 0.0157  0.1974  -0.5113 163  GLU A CG  
1032 C  CD  . GLU A 164 ? 2.3980 2.0731 1.4845 -0.0261 0.1813  -0.4759 163  GLU A CD  
1033 O  OE1 . GLU A 164 ? 2.3567 2.0035 1.3990 -0.0487 0.1522  -0.4504 163  GLU A OE1 
1034 O  OE2 . GLU A 164 ? 2.4315 2.1534 1.5277 -0.0356 0.1952  -0.4704 163  GLU A OE2 
1035 N  N   . LYS A 165 ? 2.2388 1.7658 1.4228 0.0687  0.0743  -0.4178 164  LYS A N   
1036 C  CA  . LYS A 165 ? 2.2746 1.7669 1.4947 0.0949  0.0497  -0.4030 164  LYS A CA  
1037 C  C   . LYS A 165 ? 2.2120 1.7317 1.4734 0.1126  0.0244  -0.3617 164  LYS A C   
1038 O  O   . LYS A 165 ? 2.2993 1.8179 1.6164 0.1439  0.0151  -0.3548 164  LYS A O   
1039 C  CB  . LYS A 165 ? 2.2926 1.7333 1.4579 0.0706  0.0294  -0.3948 164  LYS A CB  
1040 C  CG  . LYS A 165 ? 2.2755 1.6759 1.4046 0.0573  0.0508  -0.4385 164  LYS A CG  
1041 C  CD  . LYS A 165 ? 2.2693 1.6545 1.4598 0.0948  0.0694  -0.4710 164  LYS A CD  
1042 C  CE  . LYS A 165 ? 2.3719 1.7188 1.5283 0.0819  0.0980  -0.5229 164  LYS A CE  
1043 N  NZ  . LYS A 165 ? 2.4262 1.8065 1.5352 0.0529  0.1316  -0.5505 164  LYS A NZ  
1044 N  N   . GLY A 166 ? 2.0116 1.5534 1.2433 0.0906  0.0124  -0.3346 165  GLY A N   
1045 C  CA  . GLY A 166 ? 1.8464 1.4144 1.1081 0.1017  -0.0078 -0.2998 165  GLY A CA  
1046 C  C   . GLY A 166 ? 1.6920 1.3046 1.0076 0.1243  0.0045  -0.3052 165  GLY A C   
1047 O  O   . GLY A 166 ? 1.7235 1.3483 1.0786 0.1444  -0.0118 -0.2849 165  GLY A O   
1048 N  N   . TYR A 167 ? 1.5820 1.2221 0.8970 0.1176  0.0331  -0.3321 166  TYR A N   
1049 C  CA  . TYR A 167 ? 1.6674 1.3556 1.0378 0.1363  0.0467  -0.3396 166  TYR A CA  
1050 C  C   . TYR A 167 ? 1.7849 1.4650 1.2188 0.1735  0.0461  -0.3522 166  TYR A C   
1051 O  O   . TYR A 167 ? 1.7955 1.5049 1.2853 0.1959  0.0364  -0.3400 166  TYR A O   
1052 C  CB  . TYR A 167 ? 1.7523 1.4730 1.1067 0.1169  0.0813  -0.3677 166  TYR A CB  
1053 C  CG  . TYR A 167 ? 1.9513 1.6823 1.2479 0.0792  0.0783  -0.3498 166  TYR A CG  
1054 C  CD1 . TYR A 167 ? 1.9495 1.6595 1.2174 0.0676  0.0473  -0.3144 166  TYR A CD1 
1055 C  CD2 . TYR A 167 ? 2.1018 1.8624 1.3741 0.0541  0.1067  -0.3683 166  TYR A CD2 
1056 C  CE1 . TYR A 167 ? 1.9490 1.6648 1.1719 0.0353  0.0414  -0.2963 166  TYR A CE1 
1057 C  CE2 . TYR A 167 ? 2.1947 1.9599 1.4137 0.0178  0.1000  -0.3479 166  TYR A CE2 
1058 C  CZ  . TYR A 167 ? 2.0835 1.8243 1.2805 0.0101  0.0657  -0.3112 166  TYR A CZ  
1059 O  OH  . TYR A 167 ? 2.0898 1.8318 1.2420 -0.0235 0.0557  -0.2887 166  TYR A OH  
1060 N  N   . GLU A 168 ? 1.9289 1.5666 1.3539 0.1784  0.0544  -0.3760 167  GLU A N   
1061 C  CA  . GLU A 168 ? 1.8998 1.5185 1.3857 0.2136  0.0527  -0.3893 167  GLU A CA  
1062 C  C   . GLU A 168 ? 1.9774 1.5756 1.4868 0.2309  0.0145  -0.3513 167  GLU A C   
1063 O  O   . GLU A 168 ? 2.1502 1.7599 1.7246 0.2605  0.0048  -0.3458 167  GLU A O   
1064 C  CB  . GLU A 168 ? 1.9123 1.4809 1.3739 0.2100  0.0697  -0.4246 167  GLU A CB  
1065 C  CG  . GLU A 168 ? 1.9629 1.5033 1.4909 0.2472  0.0682  -0.4406 167  GLU A CG  
1066 C  CD  . GLU A 168 ? 2.0449 1.5356 1.5503 0.2428  0.0909  -0.4837 167  GLU A CD  
1067 O  OE1 . GLU A 168 ? 2.0677 1.5683 1.5268 0.2175  0.1228  -0.5159 167  GLU A OE1 
1068 O  OE2 . GLU A 168 ? 2.0212 1.4607 1.5524 0.2624  0.0766  -0.4857 167  GLU A OE2 
1069 N  N   . VAL A 169 ? 1.8421 1.4110 1.3010 0.2114  -0.0074 -0.3248 168  VAL A N   
1070 C  CA  . VAL A 169 ? 1.8827 1.4362 1.3573 0.2224  -0.0402 -0.2888 168  VAL A CA  
1071 C  C   . VAL A 169 ? 1.8729 1.4763 1.3755 0.2287  -0.0507 -0.2654 168  VAL A C   
1072 O  O   . VAL A 169 ? 1.9183 1.5243 1.4606 0.2482  -0.0706 -0.2466 168  VAL A O   
1073 C  CB  . VAL A 169 ? 1.6565 1.1742 1.0754 0.1983  -0.0582 -0.2669 168  VAL A CB  
1074 C  CG1 . VAL A 169 ? 1.6891 1.2314 1.0638 0.1706  -0.0543 -0.2581 168  VAL A CG1 
1075 C  CG2 . VAL A 169 ? 1.3238 0.8285 0.7580 0.2072  -0.0877 -0.2319 168  VAL A CG2 
1076 N  N   . GLU A 170 ? 1.8470 1.4878 1.3281 0.2105  -0.0384 -0.2666 169  GLU A N   
1077 C  CA  . GLU A 170 ? 1.8902 1.5771 1.3941 0.2126  -0.0463 -0.2486 169  GLU A CA  
1078 C  C   . GLU A 170 ? 1.8710 1.5890 1.4443 0.2399  -0.0434 -0.2582 169  GLU A C   
1079 O  O   . GLU A 170 ? 1.8554 1.5924 1.4598 0.2511  -0.0644 -0.2362 169  GLU A O   
1080 C  CB  . GLU A 170 ? 1.9273 1.6445 1.3996 0.1876  -0.0308 -0.2526 169  GLU A CB  
1081 C  CG  . GLU A 170 ? 1.9349 1.7043 1.4407 0.1906  -0.0304 -0.2463 169  GLU A CG  
1082 C  CD  . GLU A 170 ? 1.8808 1.6772 1.3590 0.1648  -0.0133 -0.2523 169  GLU A CD  
1083 O  OE1 . GLU A 170 ? 1.7649 1.5435 1.1961 0.1430  -0.0195 -0.2390 169  GLU A OE1 
1084 O  OE2 . GLU A 170 ? 1.8625 1.6989 1.3698 0.1658  0.0055  -0.2688 169  GLU A OE2 
1085 N  N   . GLU A 171 ? 1.8964 1.6212 1.4944 0.2489  -0.0169 -0.2921 170  GLU A N   
1086 C  CA  . GLU A 171 ? 2.1482 1.9057 1.8243 0.2772  -0.0103 -0.3063 170  GLU A CA  
1087 C  C   . GLU A 171 ? 2.2819 2.0117 2.0022 0.3047  -0.0403 -0.2872 170  GLU A C   
1088 O  O   . GLU A 171 ? 2.5613 2.3229 2.3421 0.3241  -0.0559 -0.2745 170  GLU A O   
1089 C  CB  . GLU A 171 ? 2.3532 2.1145 2.0441 0.2811  0.0283  -0.3516 170  GLU A CB  
1090 C  CG  . GLU A 171 ? 2.4660 2.2772 2.2451 0.3074  0.0441  -0.3720 170  GLU A CG  
1091 C  CD  . GLU A 171 ? 2.5476 2.3941 2.3232 0.2937  0.0899  -0.4124 170  GLU A CD  
1092 O  OE1 . GLU A 171 ? 2.5154 2.3636 2.2191 0.2589  0.1025  -0.4128 170  GLU A OE1 
1093 O  OE2 . GLU A 171 ? 2.6053 2.4791 2.4518 0.3167  0.1134  -0.4431 170  GLU A OE2 
1094 N  N   . HIS A 172 ? 2.1095 1.7799 1.8002 0.3043  -0.0503 -0.2836 171  HIS A N   
1095 C  CA  . HIS A 172 ? 1.9480 1.5840 1.6708 0.3249  -0.0817 -0.2604 171  HIS A CA  
1096 C  C   . HIS A 172 ? 1.7862 1.4314 1.4881 0.3142  -0.1143 -0.2168 171  HIS A C   
1097 O  O   . HIS A 172 ? 1.9498 1.5974 1.6916 0.3301  -0.1419 -0.1926 171  HIS A O   
1098 C  CB  . HIS A 172 ? 1.9763 1.5440 1.6679 0.3221  -0.0831 -0.2682 171  HIS A CB  
1099 C  CG  . HIS A 172 ? 2.0927 1.6328 1.8411 0.3504  -0.0730 -0.2970 171  HIS A CG  
1100 N  ND1 . HIS A 172 ? 2.1904 1.7333 1.9445 0.3523  -0.0346 -0.3443 171  HIS A ND1 
1101 C  CD2 . HIS A 172 ? 2.1592 1.6665 1.9628 0.3776  -0.0959 -0.2860 171  HIS A CD2 
1102 C  CE1 . HIS A 172 ? 2.2947 1.8078 2.1088 0.3817  -0.0316 -0.3651 171  HIS A CE1 
1103 N  NE2 . HIS A 172 ? 2.2918 1.7814 2.1395 0.3985  -0.0704 -0.3287 171  HIS A NE2 
1104 N  N   . MET A 173 ? 1.7354 1.3853 1.3747 0.2860  -0.1108 -0.2074 172  MET A N   
1105 C  CA  . MET A 173 ? 1.6615 1.3225 1.2753 0.2723  -0.1341 -0.1731 172  MET A CA  
1106 C  C   . MET A 173 ? 2.0056 1.7187 1.6585 0.2795  -0.1439 -0.1628 172  MET A C   
1107 O  O   . MET A 173 ? 2.0074 1.7232 1.6641 0.2798  -0.1712 -0.1341 172  MET A O   
1108 C  CB  . MET A 173 ? 1.6203 1.2815 1.1723 0.2438  -0.1233 -0.1719 172  MET A CB  
1109 C  CG  . MET A 173 ? 1.5401 1.1525 1.0510 0.2320  -0.1212 -0.1742 172  MET A CG  
1110 S  SD  . MET A 173 ? 2.0207 1.6372 1.4725 0.2007  -0.1146 -0.1675 172  MET A SD  
1111 C  CE  . MET A 173 ? 1.2048 0.8258 0.6477 0.1948  -0.1381 -0.1326 172  MET A CE  
1112 N  N   . GLU A 174 ? 2.3121 2.0676 1.9886 0.2807  -0.1217 -0.1853 173  GLU A N   
1113 C  CA  . GLU A 174 ? 2.3060 2.1153 2.0247 0.2856  -0.1300 -0.1780 173  GLU A CA  
1114 C  C   . GLU A 174 ? 2.1125 1.9278 1.9044 0.3151  -0.1505 -0.1702 173  GLU A C   
1115 O  O   . GLU A 174 ? 2.1445 1.9850 1.9608 0.3176  -0.1777 -0.1458 173  GLU A O   
1116 C  CB  . GLU A 174 ? 2.4441 2.2970 2.1721 0.2772  -0.0988 -0.2049 173  GLU A CB  
1117 C  CG  . GLU A 174 ? 2.5931 2.4771 2.3943 0.3003  -0.0809 -0.2311 173  GLU A CG  
1118 C  CD  . GLU A 174 ? 2.6769 2.5765 2.4623 0.2875  -0.0402 -0.2654 173  GLU A CD  
1119 O  OE1 . GLU A 174 ? 2.6986 2.5885 2.4183 0.2597  -0.0311 -0.2638 173  GLU A OE1 
1120 O  OE2 . GLU A 174 ? 2.6715 2.5936 2.5113 0.3044  -0.0175 -0.2937 173  GLU A OE2 
1121 N  N   . ALA A 175 ? 1.8716 1.6603 1.6975 0.3363  -0.1391 -0.1908 174  ALA A N   
1122 C  CA  . ALA A 175 ? 1.9462 1.7356 1.8538 0.3690  -0.1560 -0.1879 174  ALA A CA  
1123 C  C   . ALA A 175 ? 2.1328 1.8883 2.0437 0.3753  -0.2003 -0.1473 174  ALA A C   
1124 O  O   . ALA A 175 ? 2.1393 1.9170 2.1134 0.3935  -0.2275 -0.1287 174  ALA A O   
1125 C  CB  . ALA A 175 ? 1.9623 1.7222 1.8984 0.3881  -0.1287 -0.2250 174  ALA A CB  
1126 N  N   . ALA A 176 ? 2.2602 1.9642 2.1046 0.3585  -0.2090 -0.1319 175  ALA A N   
1127 C  CA  . ALA A 176 ? 2.3018 1.9677 2.1416 0.3600  -0.2487 -0.0933 175  ALA A CA  
1128 C  C   . ALA A 176 ? 2.2679 1.9639 2.0980 0.3468  -0.2828 -0.0543 175  ALA A C   
1129 O  O   . ALA A 176 ? 2.3780 2.0700 2.2532 0.3614  -0.3174 -0.0278 175  ALA A O   
1130 C  CB  . ALA A 176 ? 2.2885 1.8968 2.0578 0.3407  -0.2456 -0.0880 175  ALA A CB  
1131 N  N   . GLY A 177 ? 1.9492 1.6725 1.7229 0.3192  -0.2758 -0.0500 176  GLY A N   
1132 C  CA  . GLY A 177 ? 1.8696 1.5983 1.5946 0.3015  -0.2405 -0.0759 176  GLY A CA  
1133 C  C   . GLY A 177 ? 1.9031 1.6491 1.5671 0.2716  -0.2414 -0.0630 176  GLY A C   
1134 O  O   . GLY A 177 ? 1.8686 1.6544 1.5406 0.2647  -0.2531 -0.0532 176  GLY A O   
1135 N  N   . ILE A 178 ? 1.9436 1.6594 1.5495 0.2535  -0.2295 -0.0640 177  ILE A N   
1136 C  CA  . ILE A 178 ? 2.1244 1.8530 1.6771 0.2270  -0.2255 -0.0566 177  ILE A CA  
1137 C  C   . ILE A 178 ? 2.0183 1.7704 1.5633 0.2200  -0.1963 -0.0832 177  ILE A C   
1138 O  O   . ILE A 178 ? 1.8806 1.6190 1.4287 0.2254  -0.1764 -0.1038 177  ILE A O   
1139 C  CB  . ILE A 178 ? 2.3785 2.0682 1.8803 0.2104  -0.2283 -0.0420 177  ILE A CB  
1140 C  CG1 . ILE A 178 ? 2.5611 2.2268 2.0648 0.2121  -0.2591 -0.0114 177  ILE A CG1 
1141 C  CG2 . ILE A 178 ? 2.3996 2.1062 1.8561 0.1857  -0.2191 -0.0404 177  ILE A CG2 
1142 C  CD1 . ILE A 178 ? 2.6274 2.2686 2.0768 0.1882  -0.2633 0.0081  177  ILE A CD1 
1143 N  N   . ALA A 179 ? 2.0855 1.8702 1.6172 0.2054  -0.1949 -0.0823 178  ALA A N   
1144 C  CA  . ALA A 179 ? 2.0238 1.8267 1.5448 0.1950  -0.1707 -0.1025 178  ALA A CA  
1145 C  C   . ALA A 179 ? 1.8186 1.5941 1.2922 0.1787  -0.1597 -0.1027 178  ALA A C   
1146 O  O   . ALA A 179 ? 1.7636 1.5174 1.2114 0.1717  -0.1695 -0.0872 178  ALA A O   
1147 C  CB  . ALA A 179 ? 2.2212 2.0647 1.7483 0.1843  -0.1748 -0.1016 178  ALA A CB  
1148 N  N   . LEU A 180 ? 1.7053 1.4850 1.1699 0.1710  -0.1399 -0.1188 179  LEU A N   
1149 C  CA  . LEU A 180 ? 1.5183 1.2719 0.9496 0.1589  -0.1308 -0.1195 179  LEU A CA  
1150 C  C   . LEU A 180 ? 1.5180 1.2752 0.9256 0.1426  -0.1311 -0.1122 179  LEU A C   
1151 O  O   . LEU A 180 ? 1.7923 1.5732 1.2031 0.1357  -0.1291 -0.1157 179  LEU A O   
1152 C  CB  . LEU A 180 ? 1.5155 1.2708 0.9450 0.1546  -0.1129 -0.1371 179  LEU A CB  
1153 C  CG  . LEU A 180 ? 1.6454 1.3967 1.0955 0.1683  -0.1044 -0.1528 179  LEU A CG  
1154 C  CD1 . LEU A 180 ? 1.7180 1.4832 1.1613 0.1576  -0.0841 -0.1708 179  LEU A CD1 
1155 C  CD2 . LEU A 180 ? 1.7236 1.4339 1.1613 0.1731  -0.1090 -0.1508 179  LEU A CD2 
1156 N  N   . GLU A 181 ? 1.5200 1.2536 0.9070 0.1363  -0.1327 -0.1033 180  GLU A N   
1157 C  CA  . GLU A 181 ? 1.7127 1.4480 1.0839 0.1226  -0.1278 -0.1009 180  GLU A CA  
1158 C  C   . GLU A 181 ? 1.5871 1.3178 0.9572 0.1158  -0.1173 -0.1088 180  GLU A C   
1159 O  O   . GLU A 181 ? 1.4995 1.2250 0.8722 0.1187  -0.1139 -0.1152 180  GLU A O   
1160 C  CB  . GLU A 181 ? 1.9589 1.6772 1.3150 0.1176  -0.1318 -0.0884 180  GLU A CB  
1161 C  CG  . GLU A 181 ? 2.0874 1.8154 1.4326 0.1136  -0.1410 -0.0788 180  GLU A CG  
1162 C  CD  . GLU A 181 ? 2.2295 1.9423 1.5561 0.1047  -0.1430 -0.0654 180  GLU A CD  
1163 O  OE1 . GLU A 181 ? 2.4296 2.1336 1.7550 0.0988  -0.1327 -0.0670 180  GLU A OE1 
1164 O  OE2 . GLU A 181 ? 2.2428 1.9543 1.5571 0.1018  -0.1559 -0.0517 180  GLU A OE2 
1165 N  N   . GLU A 182 ? 1.6706 1.4024 1.0372 0.1060  -0.1125 -0.1086 181  GLU A N   
1166 C  CA  . GLU A 182 ? 1.6822 1.4098 1.0513 0.0982  -0.1074 -0.1118 181  GLU A CA  
1167 C  C   . GLU A 182 ? 1.6493 1.3575 1.0122 0.0960  -0.1096 -0.1075 181  GLU A C   
1168 O  O   . GLU A 182 ? 1.7834 1.4895 1.1406 0.0905  -0.1078 -0.1112 181  GLU A O   
1169 C  CB  . GLU A 182 ? 1.8132 1.5407 1.1884 0.0911  -0.1037 -0.1116 181  GLU A CB  
1170 C  CG  . GLU A 182 ? 1.7498 1.4681 1.1331 0.0834  -0.1036 -0.1094 181  GLU A CG  
1171 C  CD  . GLU A 182 ? 1.7552 1.4653 1.1551 0.0816  -0.1023 -0.1053 181  GLU A CD  
1172 O  OE1 . GLU A 182 ? 1.6546 1.3692 1.0568 0.0845  -0.0966 -0.1078 181  GLU A OE1 
1173 O  OE2 . GLU A 182 ? 1.9056 1.6061 1.3181 0.0764  -0.1071 -0.0990 181  GLU A OE2 
1174 N  N   . ALA A 183 ? 1.5970 1.2917 0.9579 0.0968  -0.1135 -0.0996 182  ALA A N   
1175 C  CA  . ALA A 183 ? 1.5712 1.2465 0.9254 0.0916  -0.1184 -0.0946 182  ALA A CA  
1176 C  C   . ALA A 183 ? 1.3570 1.0229 0.6979 0.0932  -0.1178 -0.1033 182  ALA A C   
1177 O  O   . ALA A 183 ? 1.2648 0.9198 0.5930 0.0827  -0.1194 -0.1040 182  ALA A O   
1178 C  CB  . ALA A 183 ? 1.5826 1.2475 0.9378 0.0920  -0.1225 -0.0853 182  ALA A CB  
1179 N  N   . GLU A 184 ? 1.3463 1.0167 0.6913 0.1054  -0.1157 -0.1101 183  GLU A N   
1180 C  CA  . GLU A 184 ? 1.4847 1.1477 0.8253 0.1102  -0.1110 -0.1233 183  GLU A CA  
1181 C  C   . GLU A 184 ? 1.5983 1.2791 0.9358 0.1034  -0.1004 -0.1347 183  GLU A C   
1182 O  O   . GLU A 184 ? 1.7496 1.4214 1.0707 0.0956  -0.0938 -0.1451 183  GLU A O   
1183 C  CB  . GLU A 184 ? 1.5195 1.1839 0.8772 0.1279  -0.1137 -0.1260 183  GLU A CB  
1184 C  CG  . GLU A 184 ? 1.7746 1.4134 1.1299 0.1316  -0.1250 -0.1140 183  GLU A CG  
1185 C  CD  . GLU A 184 ? 1.9783 1.6258 1.3325 0.1269  -0.1315 -0.0973 183  GLU A CD  
1186 O  OE1 . GLU A 184 ? 2.2698 1.9420 1.6308 0.1282  -0.1301 -0.0971 183  GLU A OE1 
1187 O  OE2 . GLU A 184 ? 1.8207 1.4513 1.1664 0.1198  -0.1368 -0.0859 183  GLU A OE2 
1188 N  N   . ILE A 185 ? 1.5176 1.2231 0.8673 0.1031  -0.0981 -0.1334 184  ILE A N   
1189 C  CA  . ILE A 185 ? 1.5887 1.3123 0.9359 0.0932  -0.0883 -0.1419 184  ILE A CA  
1190 C  C   . ILE A 185 ? 1.6784 1.3889 1.0028 0.0730  -0.0904 -0.1348 184  ILE A C   
1191 O  O   . ILE A 185 ? 1.8452 1.5572 1.1517 0.0600  -0.0825 -0.1420 184  ILE A O   
1192 C  CB  . ILE A 185 ? 1.7551 1.5055 1.1203 0.0942  -0.0879 -0.1408 184  ILE A CB  
1193 C  CG1 . ILE A 185 ? 1.7945 1.5558 1.1796 0.1110  -0.0938 -0.1401 184  ILE A CG1 
1194 C  CG2 . ILE A 185 ? 1.8507 1.6242 1.2184 0.0848  -0.0761 -0.1511 184  ILE A CG2 
1195 C  CD1 . ILE A 185 ? 1.7091 1.5007 1.1113 0.1102  -0.0944 -0.1420 184  ILE A CD1 
1196 N  N   . SER A 186 ? 1.6034 1.3019 0.9300 0.0693  -0.1012 -0.1203 185  SER A N   
1197 C  CA  . SER A 186 ? 1.5727 1.2585 0.8870 0.0516  -0.1091 -0.1086 185  SER A CA  
1198 C  C   . SER A 186 ? 1.6515 1.3183 0.9385 0.0406  -0.1125 -0.1093 185  SER A C   
1199 O  O   . SER A 186 ? 1.6874 1.3488 0.9510 0.0209  -0.1152 -0.1053 185  SER A O   
1200 C  CB  . SER A 186 ? 1.5209 1.2008 0.8560 0.0543  -0.1189 -0.0951 185  SER A CB  
1201 O  OG  . SER A 186 ? 1.6656 1.3333 1.0030 0.0591  -0.1247 -0.0901 185  SER A OG  
1202 N  N   . ALA A 187 ? 1.5631 1.2176 0.8496 0.0506  -0.1135 -0.1137 186  ALA A N   
1203 C  CA  . ALA A 187 ? 1.4073 1.0400 0.6661 0.0398  -0.1161 -0.1183 186  ALA A CA  
1204 C  C   . ALA A 187 ? 1.5487 1.1858 0.7846 0.0335  -0.0999 -0.1388 186  ALA A C   
1205 O  O   . ALA A 187 ? 1.8342 1.4586 1.0349 0.0127  -0.1000 -0.1425 186  ALA A O   
1206 C  CB  . ALA A 187 ? 1.2604 0.8765 0.5268 0.0524  -0.1199 -0.1199 186  ALA A CB  
1207 N  N   . LEU A 188 ? 1.4150 1.0723 0.6721 0.0501  -0.0858 -0.1526 187  LEU A N   
1208 C  CA  . LEU A 188 ? 1.4579 1.1295 0.7067 0.0471  -0.0657 -0.1746 187  LEU A CA  
1209 C  C   . LEU A 188 ? 1.5034 1.1898 0.7311 0.0229  -0.0611 -0.1702 187  LEU A C   
1210 O  O   . LEU A 188 ? 1.6804 1.3702 0.8800 0.0061  -0.0462 -0.1850 187  LEU A O   
1211 C  CB  . LEU A 188 ? 1.6258 1.3216 0.9149 0.0717  -0.0562 -0.1856 187  LEU A CB  
1212 C  CG  . LEU A 188 ? 1.7281 1.4073 1.0350 0.0935  -0.0564 -0.1958 187  LEU A CG  
1213 C  CD1 . LEU A 188 ? 1.7099 1.4155 1.0620 0.1169  -0.0537 -0.2000 187  LEU A CD1 
1214 C  CD2 . LEU A 188 ? 1.8470 1.5090 1.1318 0.0869  -0.0410 -0.2202 187  LEU A CD2 
1215 N  N   . LEU A 189 ? 1.4920 1.1866 0.7332 0.0200  -0.0727 -0.1508 188  LEU A N   
1216 C  CA  . LEU A 189 ? 1.6591 1.3612 0.8825 -0.0043 -0.0736 -0.1408 188  LEU A CA  
1217 C  C   . LEU A 189 ? 1.8452 1.5228 1.0268 -0.0309 -0.0860 -0.1285 188  LEU A C   
1218 O  O   . LEU A 189 ? 1.9663 1.6468 1.1128 -0.0570 -0.0796 -0.1297 188  LEU A O   
1219 C  CB  . LEU A 189 ? 1.5276 1.2358 0.7790 0.0003  -0.0852 -0.1237 188  LEU A CB  
1220 C  CG  . LEU A 189 ? 1.3512 1.0610 0.5903 -0.0240 -0.0902 -0.1096 188  LEU A CG  
1221 C  CD1 . LEU A 189 ? 1.3361 1.0762 0.5832 -0.0276 -0.0723 -0.1223 188  LEU A CD1 
1222 C  CD2 . LEU A 189 ? 1.1420 0.8386 0.4055 -0.0206 -0.1087 -0.0898 188  LEU A CD2 
1223 N  N   . LYS A 190 ? 1.8246 1.4801 1.0092 -0.0266 -0.1043 -0.1159 189  LYS A N   
1224 C  CA  . LYS A 190 ? 1.7159 1.3489 0.8668 -0.0517 -0.1227 -0.1001 189  LYS A CA  
1225 C  C   . LYS A 190 ? 1.7358 1.3605 0.8345 -0.0734 -0.1106 -0.1182 189  LYS A C   
1226 O  O   . LYS A 190 ? 1.8714 1.4892 0.9280 -0.1052 -0.1182 -0.1079 189  LYS A O   
1227 C  CB  . LYS A 190 ? 1.4927 1.1094 0.6635 -0.0407 -0.1408 -0.0886 189  LYS A CB  
1228 C  CG  . LYS A 190 ? 1.3787 0.9741 0.5182 -0.0660 -0.1621 -0.0738 189  LYS A CG  
1229 C  CD  . LYS A 190 ? 1.5827 1.1672 0.7475 -0.0550 -0.1769 -0.0650 189  LYS A CD  
1230 C  CE  . LYS A 190 ? 1.6311 1.2213 0.8385 -0.0519 -0.1979 -0.0376 189  LYS A CE  
1231 N  NZ  . LYS A 190 ? 1.5924 1.1754 0.8202 -0.0504 -0.2141 -0.0266 189  LYS A NZ  
1232 N  N   . VAL A 191 ? 1.7026 1.3270 0.8038 -0.0570 -0.0915 -0.1455 190  VAL A N   
1233 C  CA  . VAL A 191 ? 1.7229 1.3364 0.7784 -0.0743 -0.0755 -0.1702 190  VAL A CA  
1234 C  C   . VAL A 191 ? 1.8328 1.4688 0.8623 -0.0941 -0.0527 -0.1834 190  VAL A C   
1235 O  O   . VAL A 191 ? 2.0327 1.6709 1.0284 -0.1240 -0.0480 -0.1849 190  VAL A O   
1236 C  CB  . VAL A 191 ? 1.6015 1.2075 0.6783 -0.0472 -0.0596 -0.1978 190  VAL A CB  
1237 C  CG1 . VAL A 191 ? 1.5299 1.1235 0.5628 -0.0637 -0.0376 -0.2303 190  VAL A CG1 
1238 C  CG2 . VAL A 191 ? 1.6175 1.1993 0.7115 -0.0346 -0.0819 -0.1833 190  VAL A CG2 
1239 N  N   . SER A 192 ? 1.7195 1.3863 0.7885 -0.0764 -0.0378 -0.1889 191  SER A N   
1240 C  CA  . SER A 192 ? 1.7591 1.4539 0.8120 -0.0953 -0.0144 -0.2006 191  SER A CA  
1241 C  C   . SER A 192 ? 1.7223 1.4101 0.7319 -0.1339 -0.0314 -0.1725 191  SER A C   
1242 O  O   . SER A 192 ? 1.4393 1.1434 0.4224 -0.1620 -0.0159 -0.1773 191  SER A O   
1243 C  CB  . SER A 192 ? 1.6156 1.3458 0.7255 -0.0705 -0.0026 -0.2053 191  SER A CB  
1244 O  OG  . SER A 192 ? 1.5897 1.3316 0.7360 -0.0405 0.0163  -0.2334 191  SER A OG  
1245 N  N   . ALA A 193 ? 1.6188 1.2906 0.6450 -0.1310 -0.0632 -0.1398 192  ALA A N   
1246 C  CA  . ALA A 193 ? 1.5852 1.2446 0.5816 -0.1638 -0.0871 -0.1072 192  ALA A CA  
1247 C  C   . ALA A 193 ? 1.6226 1.2702 0.5877 -0.1904 -0.0963 -0.0995 192  ALA A C   
1248 O  O   . ALA A 193 ? 1.7588 1.4112 0.6938 -0.2241 -0.0971 -0.0869 192  ALA A O   
1249 C  CB  . ALA A 193 ? 1.5754 1.2230 0.6167 -0.1469 -0.1169 -0.0778 192  ALA A CB  
1250 N  N   . ALA A 194 ? 1.6284 1.2589 0.5986 -0.1776 -0.1043 -0.1060 193  ALA A N   
1251 C  CA  . ALA A 194 ? 1.7191 1.3356 0.6596 -0.2029 -0.1156 -0.0999 193  ALA A CA  
1252 C  C   . ALA A 194 ? 1.6246 1.2543 0.5322 -0.2208 -0.0839 -0.1294 193  ALA A C   
1253 O  O   . ALA A 194 ? 1.8291 1.4548 0.6997 -0.2554 -0.0895 -0.1192 193  ALA A O   
1254 C  CB  . ALA A 194 ? 1.4722 1.0671 0.4272 -0.1852 -0.1304 -0.1019 193  ALA A CB  
1255 N  N   . THR A 195 ? 1.5259 1.1704 0.4479 -0.1976 -0.0510 -0.1663 194  THR A N   
1256 C  CA  . THR A 195 ? 1.6741 1.3337 0.5721 -0.2101 -0.0162 -0.1997 194  THR A CA  
1257 C  C   . THR A 195 ? 1.6979 1.3865 0.5832 -0.2318 0.0013  -0.1963 194  THR A C   
1258 O  O   . THR A 195 ? 1.9495 1.6558 0.8155 -0.2457 0.0328  -0.2225 194  THR A O   
1259 C  CB  . THR A 195 ? 1.7652 1.4286 0.6897 -0.1758 0.0125  -0.2421 194  THR A CB  
1260 O  OG1 . THR A 195 ? 1.8960 1.5757 0.8585 -0.1483 0.0185  -0.2438 194  THR A OG1 
1261 C  CG2 . THR A 195 ? 1.5568 1.1867 0.4865 -0.1606 -0.0031 -0.2468 194  THR A CG2 
1262 N  N   . GLY A 196 ? 1.5640 1.2558 0.4603 -0.2359 -0.0187 -0.1646 195  GLY A N   
1263 C  CA  . GLY A 196 ? 1.7277 1.4427 0.6111 -0.2603 -0.0068 -0.1560 195  GLY A CA  
1264 C  C   . GLY A 196 ? 1.9543 1.7053 0.8575 -0.2463 0.0336  -0.1906 195  GLY A C   
1265 O  O   . GLY A 196 ? 2.1422 1.9177 1.0255 -0.2727 0.0575  -0.1986 195  GLY A O   
1266 N  N   . ARG A 197 ? 1.9812 1.7368 0.9250 -0.2068 0.0409  -0.2104 196  ARG A N   
1267 C  CA  . ARG A 197 ? 1.9438 1.7363 0.9159 -0.1915 0.0757  -0.2412 196  ARG A CA  
1268 C  C   . ARG A 197 ? 1.9162 1.7249 0.9053 -0.1936 0.0669  -0.2215 196  ARG A C   
1269 O  O   . ARG A 197 ? 1.9030 1.7013 0.9323 -0.1660 0.0439  -0.2056 196  ARG A O   
1270 C  CB  . ARG A 197 ? 1.8370 1.6241 0.8445 -0.1498 0.0867  -0.2722 196  ARG A CB  
1271 C  CG  . ARG A 197 ? 1.7591 1.5273 0.7538 -0.1451 0.0980  -0.2976 196  ARG A CG  
1272 C  CD  . ARG A 197 ? 2.0038 1.7988 0.9848 -0.1635 0.1368  -0.3279 196  ARG A CD  
1273 N  NE  . ARG A 197 ? 2.0703 1.9068 1.0945 -0.1451 0.1723  -0.3592 196  ARG A NE  
1274 C  CZ  . ARG A 197 ? 2.1301 1.9704 1.1973 -0.1097 0.1931  -0.3960 196  ARG A CZ  
1275 N  NH1 . ARG A 197 ? 2.0996 1.8983 1.1651 -0.0902 0.1817  -0.4056 196  ARG A NH1 
1276 N  NH2 . ARG A 197 ? 2.1785 2.0665 1.3002 -0.0929 0.2231  -0.4210 196  ARG A NH2 
1277 N  N   . GLU A 198 ? 1.9895 1.8275 0.9653 -0.2235 0.0840  -0.2190 197  GLU A N   
1278 C  CA  . GLU A 198 ? 2.0868 1.9384 1.0800 -0.2314 0.0726  -0.1958 197  GLU A CA  
1279 C  C   . GLU A 198 ? 2.1420 2.0272 1.2161 -0.1898 0.0822  -0.2110 197  GLU A C   
1280 O  O   . GLU A 198 ? 2.1940 2.0703 1.3054 -0.1705 0.0573  -0.1905 197  GLU A O   
1281 C  CB  . GLU A 198 ? 2.2353 2.1102 1.1921 -0.2783 0.0889  -0.1883 197  GLU A CB  
1282 C  CG  . GLU A 198 ? 2.3441 2.2677 1.3087 -0.2858 0.1375  -0.2268 197  GLU A CG  
1283 C  CD  . GLU A 198 ? 2.4014 2.3151 1.3388 -0.2936 0.1534  -0.2452 197  GLU A CD  
1284 O  OE1 . GLU A 198 ? 2.3763 2.2539 1.3080 -0.2749 0.1346  -0.2443 197  GLU A OE1 
1285 O  OE2 . GLU A 198 ? 2.4705 2.4136 1.3920 -0.3204 0.1859  -0.2619 197  GLU A OE2 
1286 N  N   . ASN A 199 ? 2.0612 1.9853 1.1633 -0.1769 0.1179  -0.2473 198  ASN A N   
1287 C  CA  . ASN A 199 ? 1.8744 1.8368 1.0551 -0.1416 0.1259  -0.2601 198  ASN A CA  
1288 C  C   . ASN A 199 ? 1.9302 1.8690 1.1512 -0.0978 0.1020  -0.2561 198  ASN A C   
1289 O  O   . ASN A 199 ? 2.0973 2.0514 1.3694 -0.0755 0.0892  -0.2477 198  ASN A O   
1290 C  CB  . ASN A 199 ? 1.9584 1.9681 1.1670 -0.1363 0.1693  -0.3006 198  ASN A CB  
1291 C  CG  . ASN A 199 ? 2.2875 2.3376 1.4749 -0.1779 0.1969  -0.3049 198  ASN A CG  
1292 O  OD1 . ASN A 199 ? 2.3553 2.3921 1.4998 -0.2135 0.1812  -0.2752 198  ASN A OD1 
1293 N  ND2 . ASN A 199 ? 2.4976 2.5975 1.7183 -0.1742 0.2385  -0.3417 198  ASN A ND2 
1294 N  N   . LYS A 200 ? 1.8251 1.7266 1.0195 -0.0889 0.0961  -0.2622 199  LYS A N   
1295 C  CA  . LYS A 200 ? 1.7338 1.6100 0.9594 -0.0523 0.0739  -0.2565 199  LYS A CA  
1296 C  C   . LYS A 200 ? 1.6331 1.4842 0.8571 -0.0520 0.0390  -0.2215 199  LYS A C   
1297 O  O   . LYS A 200 ? 1.6989 1.5501 0.9640 -0.0242 0.0245  -0.2150 199  LYS A O   
1298 C  CB  . LYS A 200 ? 1.7719 1.6126 0.9667 -0.0479 0.0763  -0.2714 199  LYS A CB  
1299 C  CG  . LYS A 200 ? 1.7187 1.5631 0.9639 -0.0089 0.0856  -0.2956 199  LYS A CG  
1300 C  CD  . LYS A 200 ? 1.7120 1.6057 1.0033 0.0011  0.1185  -0.3250 199  LYS A CD  
1301 C  CE  . LYS A 200 ? 1.6592 1.5537 1.0120 0.0437  0.1204  -0.3429 199  LYS A CE  
1302 N  NZ  . LYS A 200 ? 1.6413 1.5845 1.0496 0.0569  0.1534  -0.3748 199  LYS A NZ  
1303 N  N   . VAL A 201 ? 1.5258 1.3554 0.7038 -0.0834 0.0255  -0.1993 200  VAL A N   
1304 C  CA  . VAL A 201 ? 1.5165 1.3236 0.7014 -0.0827 -0.0050 -0.1685 200  VAL A CA  
1305 C  C   . VAL A 201 ? 1.5094 1.3441 0.7358 -0.0762 -0.0049 -0.1643 200  VAL A C   
1306 O  O   . VAL A 201 ? 1.3847 1.2099 0.6396 -0.0580 -0.0227 -0.1531 200  VAL A O   
1307 C  CB  . VAL A 201 ? 1.4641 1.2438 0.5988 -0.1190 -0.0219 -0.1429 200  VAL A CB  
1308 C  CG1 . VAL A 201 ? 1.3895 1.1483 0.5449 -0.1151 -0.0508 -0.1139 200  VAL A CG1 
1309 C  CG2 . VAL A 201 ? 1.3241 1.0750 0.4159 -0.1281 -0.0278 -0.1443 200  VAL A CG2 
1310 N  N   . TYR A 202 ? 1.6041 1.4747 0.8333 -0.0930 0.0167  -0.1753 201  TYR A N   
1311 C  CA  . TYR A 202 ? 1.6319 1.5328 0.9003 -0.0912 0.0174  -0.1730 201  TYR A CA  
1312 C  C   . TYR A 202 ? 1.7129 1.6320 1.0342 -0.0534 0.0158  -0.1856 201  TYR A C   
1313 O  O   . TYR A 202 ? 1.8902 1.8060 1.2352 -0.0430 -0.0013 -0.1749 201  TYR A O   
1314 C  CB  . TYR A 202 ? 1.6041 1.5466 0.8686 -0.1179 0.0442  -0.1847 201  TYR A CB  
1315 C  CG  . TYR A 202 ? 1.6507 1.6269 0.9542 -0.1227 0.0444  -0.1811 201  TYR A CG  
1316 C  CD1 . TYR A 202 ? 1.5231 1.4780 0.8167 -0.1423 0.0239  -0.1563 201  TYR A CD1 
1317 C  CD2 . TYR A 202 ? 1.7820 1.8111 1.1357 -0.1086 0.0639  -0.2027 201  TYR A CD2 
1318 C  CE1 . TYR A 202 ? 1.5372 1.5200 0.8638 -0.1498 0.0233  -0.1545 201  TYR A CE1 
1319 C  CE2 . TYR A 202 ? 1.7016 1.7642 1.0915 -0.1161 0.0618  -0.1987 201  TYR A CE2 
1320 C  CZ  . TYR A 202 ? 1.6173 1.6554 0.9901 -0.1381 0.0418  -0.1753 201  TYR A CZ  
1321 O  OH  . TYR A 202 ? 1.5869 1.6554 0.9932 -0.1483 0.0390  -0.1728 201  TYR A OH  
1322 N  N   . ARG A 203 ? 1.5730 1.5078 0.9108 -0.0339 0.0324  -0.2083 202  ARG A N   
1323 C  CA  . ARG A 203 ? 1.4443 1.3950 0.8333 0.0012  0.0279  -0.2172 202  ARG A CA  
1324 C  C   . ARG A 203 ? 1.3383 1.2522 0.7249 0.0192  0.0012  -0.2008 202  ARG A C   
1325 O  O   . ARG A 203 ? 1.5296 1.4534 0.9462 0.0335  -0.0121 -0.1948 202  ARG A O   
1326 C  CB  . ARG A 203 ? 1.4420 1.4043 0.8483 0.0195  0.0484  -0.2432 202  ARG A CB  
1327 C  CG  . ARG A 203 ? 1.4515 1.4218 0.9100 0.0565  0.0384  -0.2478 202  ARG A CG  
1328 C  CD  . ARG A 203 ? 1.6323 1.6084 1.1136 0.0756  0.0587  -0.2747 202  ARG A CD  
1329 N  NE  . ARG A 203 ? 1.9589 1.9799 1.4589 0.0642  0.0914  -0.2987 202  ARG A NE  
1330 C  CZ  . ARG A 203 ? 2.0372 2.1075 1.6057 0.0823  0.1031  -0.3133 202  ARG A CZ  
1331 N  NH1 . ARG A 203 ? 2.0561 2.1336 1.6766 0.1118  0.0805  -0.3035 202  ARG A NH1 
1332 N  NH2 . ARG A 203 ? 1.9317 2.0460 1.5175 0.0693  0.1369  -0.3368 202  ARG A NH2 
1333 N  N   . TYR A 204 ? 1.1969 1.0707 0.5467 0.0156  -0.0061 -0.1940 203  TYR A N   
1334 C  CA  . TYR A 204 ? 1.2915 1.1333 0.6405 0.0310  -0.0276 -0.1803 203  TYR A CA  
1335 C  C   . TYR A 204 ? 1.2978 1.1278 0.6442 0.0214  -0.0442 -0.1609 203  TYR A C   
1336 O  O   . TYR A 204 ? 1.5666 1.3837 0.9245 0.0357  -0.0577 -0.1535 203  TYR A O   
1337 C  CB  . TYR A 204 ? 1.5060 1.3122 0.8218 0.0287  -0.0306 -0.1794 203  TYR A CB  
1338 C  CG  . TYR A 204 ? 1.6118 1.4197 0.9359 0.0448  -0.0168 -0.2010 203  TYR A CG  
1339 C  CD1 . TYR A 204 ? 1.7334 1.5723 1.1018 0.0655  -0.0069 -0.2157 203  TYR A CD1 
1340 C  CD2 . TYR A 204 ? 1.5104 1.2877 0.8024 0.0396  -0.0157 -0.2065 203  TYR A CD2 
1341 C  CE1 . TYR A 204 ? 1.7281 1.5655 1.1129 0.0831  0.0053  -0.2362 203  TYR A CE1 
1342 C  CE2 . TYR A 204 ? 1.6641 1.4374 0.9656 0.0548  -0.0024 -0.2291 203  TYR A CE2 
1343 C  CZ  . TYR A 204 ? 1.8140 1.6163 1.1645 0.0780  0.0087  -0.2443 203  TYR A CZ  
1344 O  OH  . TYR A 204 ? 2.1150 1.9105 1.4838 0.0960  0.0215  -0.2676 203  TYR A OH  
1345 N  N   . LEU A 205 ? 1.1554 0.9869 0.4857 -0.0041 -0.0427 -0.1531 204  LEU A N   
1346 C  CA  . LEU A 205 ? 1.3322 1.1517 0.6685 -0.0116 -0.0571 -0.1381 204  LEU A CA  
1347 C  C   . LEU A 205 ? 1.4014 1.2483 0.7706 -0.0017 -0.0567 -0.1454 204  LEU A C   
1348 O  O   . LEU A 205 ? 1.3669 1.2018 0.7461 0.0046  -0.0684 -0.1403 204  LEU A O   
1349 C  CB  . LEU A 205 ? 1.3940 1.2052 0.7074 -0.0428 -0.0584 -0.1254 204  LEU A CB  
1350 C  CG  . LEU A 205 ? 1.5069 1.2828 0.7879 -0.0570 -0.0705 -0.1085 204  LEU A CG  
1351 C  CD1 . LEU A 205 ? 1.5563 1.3260 0.8132 -0.0913 -0.0736 -0.0929 204  LEU A CD1 
1352 C  CD2 . LEU A 205 ? 1.3999 1.1460 0.6963 -0.0417 -0.0897 -0.0964 204  LEU A CD2 
1353 N  N   . HIS A 206 ? 1.4462 1.3319 0.8331 -0.0019 -0.0428 -0.1584 205  HIS A N   
1354 C  CA  . HIS A 206 ? 1.3795 1.2969 0.8012 0.0069  -0.0455 -0.1643 205  HIS A CA  
1355 C  C   . HIS A 206 ? 1.5378 1.4523 0.9753 0.0344  -0.0551 -0.1665 205  HIS A C   
1356 O  O   . HIS A 206 ? 1.7666 1.6883 1.2179 0.0395  -0.0668 -0.1641 205  HIS A O   
1357 C  CB  . HIS A 206 ? 1.3612 1.3265 0.8076 0.0007  -0.0283 -0.1769 205  HIS A CB  
1358 C  CG  . HIS A 206 ? 1.4570 1.4356 0.8965 -0.0302 -0.0223 -0.1725 205  HIS A CG  
1359 N  ND1 . HIS A 206 ? 1.3704 1.3162 0.7871 -0.0485 -0.0350 -0.1575 205  HIS A ND1 
1360 C  CD2 . HIS A 206 ? 1.6280 1.6490 1.0834 -0.0469 -0.0049 -0.1807 205  HIS A CD2 
1361 C  CE1 . HIS A 206 ? 1.5592 1.5224 0.9743 -0.0766 -0.0280 -0.1545 205  HIS A CE1 
1362 N  NE2 . HIS A 206 ? 1.7061 1.7171 1.1429 -0.0775 -0.0087 -0.1684 205  HIS A NE2 
1363 N  N   . LYS A 207 ? 1.5253 1.4273 0.9569 0.0489  -0.0508 -0.1706 206  LYS A N   
1364 C  CA  . LYS A 207 ? 1.4459 1.3387 0.8885 0.0725  -0.0614 -0.1692 206  LYS A CA  
1365 C  C   . LYS A 207 ? 1.3661 1.2299 0.7910 0.0710  -0.0756 -0.1569 206  LYS A C   
1366 O  O   . LYS A 207 ? 1.5589 1.4257 0.9923 0.0802  -0.0864 -0.1535 206  LYS A O   
1367 C  CB  . LYS A 207 ? 1.5153 1.3907 0.9501 0.0842  -0.0543 -0.1758 206  LYS A CB  
1368 C  CG  . LYS A 207 ? 1.6045 1.4921 1.0720 0.1089  -0.0567 -0.1823 206  LYS A CG  
1369 C  CD  . LYS A 207 ? 1.6617 1.5945 1.1694 0.1127  -0.0439 -0.1965 206  LYS A CD  
1370 C  CE  . LYS A 207 ? 1.7895 1.7311 1.3386 0.1402  -0.0474 -0.2029 206  LYS A CE  
1371 N  NZ  . LYS A 207 ? 1.8298 1.8211 1.4309 0.1467  -0.0342 -0.2178 206  LYS A NZ  
1372 N  N   . LEU A 208 ? 1.1718 1.0091 0.5732 0.0577  -0.0754 -0.1503 207  LEU A N   
1373 C  CA  . LEU A 208 ? 1.2385 1.0505 0.6316 0.0565  -0.0850 -0.1416 207  LEU A CA  
1374 C  C   . LEU A 208 ? 1.4161 1.2383 0.8184 0.0496  -0.0890 -0.1436 207  LEU A C   
1375 O  O   . LEU A 208 ? 1.6017 1.4148 1.0028 0.0546  -0.0945 -0.1434 207  LEU A O   
1376 C  CB  . LEU A 208 ? 1.3848 1.1697 0.7615 0.0435  -0.0864 -0.1324 207  LEU A CB  
1377 C  CG  . LEU A 208 ? 1.3787 1.1418 0.7414 0.0484  -0.0890 -0.1270 207  LEU A CG  
1378 C  CD1 . LEU A 208 ? 1.4949 1.2343 0.8470 0.0332  -0.0965 -0.1137 207  LEU A CD1 
1379 C  CD2 . LEU A 208 ? 1.3622 1.1169 0.7316 0.0648  -0.0941 -0.1257 207  LEU A CD2 
1380 N  N   . ARG A 209 ? 1.5302 1.3708 0.9391 0.0352  -0.0852 -0.1468 208  ARG A N   
1381 C  CA  . ARG A 209 ? 1.6056 1.4538 1.0216 0.0246  -0.0897 -0.1501 208  ARG A CA  
1382 C  C   . ARG A 209 ? 1.8182 1.6889 1.2444 0.0347  -0.0967 -0.1550 208  ARG A C   
1383 O  O   . ARG A 209 ? 2.2304 2.0933 1.6499 0.0311  -0.1028 -0.1578 208  ARG A O   
1384 C  CB  . ARG A 209 ? 1.4605 1.3292 0.8839 0.0050  -0.0847 -0.1515 208  ARG A CB  
1385 C  CG  . ARG A 209 ? 1.4185 1.2924 0.8486 -0.0091 -0.0908 -0.1556 208  ARG A CG  
1386 C  CD  . ARG A 209 ? 1.4720 1.3806 0.9172 -0.0272 -0.0866 -0.1578 208  ARG A CD  
1387 N  NE  . ARG A 209 ? 1.4642 1.4187 0.9343 -0.0158 -0.0854 -0.1635 208  ARG A NE  
1388 C  CZ  . ARG A 209 ? 1.5388 1.5183 1.0225 -0.0080 -0.0736 -0.1661 208  ARG A CZ  
1389 N  NH1 . ARG A 209 ? 1.6872 1.6503 1.1521 -0.0141 -0.0617 -0.1637 208  ARG A NH1 
1390 N  NH2 . ARG A 209 ? 1.5223 1.5429 1.0395 0.0052  -0.0744 -0.1717 208  ARG A NH2 
1391 N  N   . GLU A 210 ? 1.6167 1.5142 1.0592 0.0466  -0.0960 -0.1561 209  GLU A N   
1392 C  CA  . GLU A 210 ? 1.4399 1.3629 0.8986 0.0556  -0.1073 -0.1560 209  GLU A CA  
1393 C  C   . GLU A 210 ? 1.5688 1.4705 1.0099 0.0659  -0.1170 -0.1502 209  GLU A C   
1394 O  O   . GLU A 210 ? 1.7226 1.6357 1.1615 0.0634  -0.1297 -0.1479 209  GLU A O   
1395 C  CB  . GLU A 210 ? 1.2578 1.2119 0.7482 0.0694  -0.1039 -0.1585 209  GLU A CB  
1396 C  CG  . GLU A 210 ? 1.5704 1.5640 1.0931 0.0733  -0.1177 -0.1570 209  GLU A CG  
1397 C  CD  . GLU A 210 ? 1.7422 1.7747 1.3103 0.0839  -0.1093 -0.1637 209  GLU A CD  
1398 O  OE1 . GLU A 210 ? 1.6352 1.6610 1.2013 0.0863  -0.0900 -0.1719 209  GLU A OE1 
1399 O  OE2 . GLU A 210 ? 1.8591 1.9302 1.4659 0.0886  -0.1217 -0.1614 209  GLU A OE2 
1400 N  N   . TYR A 211 ? 1.5907 1.4632 1.0173 0.0741  -0.1117 -0.1467 210  TYR A N   
1401 C  CA  . TYR A 211 ? 1.5860 1.4413 0.9978 0.0827  -0.1187 -0.1399 210  TYR A CA  
1402 C  C   . TYR A 211 ? 1.5566 1.3828 0.9474 0.0760  -0.1128 -0.1405 210  TYR A C   
1403 O  O   . TYR A 211 ? 1.4987 1.3131 0.8759 0.0791  -0.1152 -0.1359 210  TYR A O   
1404 C  CB  . TYR A 211 ? 1.6036 1.4516 1.0232 0.0996  -0.1193 -0.1348 210  TYR A CB  
1405 C  CG  . TYR A 211 ? 1.7282 1.6044 1.1786 0.1111  -0.1246 -0.1359 210  TYR A CG  
1406 C  CD1 . TYR A 211 ? 1.7708 1.6652 1.2419 0.1117  -0.1125 -0.1460 210  TYR A CD1 
1407 C  CD2 . TYR A 211 ? 1.8127 1.6986 1.2743 0.1203  -0.1417 -0.1263 210  TYR A CD2 
1408 C  CE1 . TYR A 211 ? 1.7484 1.6732 1.2579 0.1242  -0.1140 -0.1500 210  TYR A CE1 
1409 C  CE2 . TYR A 211 ? 1.8761 1.7893 1.3778 0.1337  -0.1485 -0.1265 210  TYR A CE2 
1410 C  CZ  . TYR A 211 ? 1.8443 1.7784 1.3737 0.1371  -0.1329 -0.1402 210  TYR A CZ  
1411 O  OH  . TYR A 211 ? 1.9217 1.8874 1.5007 0.1523  -0.1363 -0.1435 210  TYR A OH  
1412 N  N   . VAL A 212 ? 1.6666 1.4820 1.0585 0.0665  -0.1050 -0.1451 211  VAL A N   
1413 C  CA  . VAL A 212 ? 1.6955 1.4863 1.0805 0.0616  -0.0996 -0.1475 211  VAL A CA  
1414 C  C   . VAL A 212 ? 1.7535 1.5394 1.1439 0.0476  -0.0968 -0.1552 211  VAL A C   
1415 O  O   . VAL A 212 ? 1.7252 1.5206 1.1227 0.0402  -0.0977 -0.1541 211  VAL A O   
1416 C  CB  . VAL A 212 ? 1.9935 1.7629 1.3810 0.0673  -0.0967 -0.1396 211  VAL A CB  
1417 C  CG1 . VAL A 212 ? 1.8479 1.5985 1.2392 0.0665  -0.0916 -0.1417 211  VAL A CG1 
1418 C  CG2 . VAL A 212 ? 2.0309 1.8014 1.4138 0.0789  -0.1000 -0.1324 211  VAL A CG2 
1419 N  N   . GLY A 213 ? 1.8171 1.5870 1.2051 0.0429  -0.0921 -0.1641 212  GLY A N   
1420 C  CA  . GLY A 213 ? 1.8457 1.6021 1.2417 0.0306  -0.0898 -0.1726 212  GLY A CA  
1421 C  C   . GLY A 213 ? 1.8030 1.5306 1.2167 0.0337  -0.0867 -0.1682 212  GLY A C   
1422 O  O   . GLY A 213 ? 1.6548 1.3750 1.0764 0.0299  -0.0920 -0.1563 212  GLY A O   
1423 N  N   . CYS A 214 ? 1.9435 1.6567 1.3649 0.0392  -0.0785 -0.1770 213  CYS A N   
1424 C  CA  . CYS A 214 ? 1.9666 1.6569 1.4156 0.0459  -0.0775 -0.1710 213  CYS A CA  
1425 C  C   . CYS A 214 ? 2.0574 1.7546 1.5054 0.0558  -0.0815 -0.1550 213  CYS A C   
1426 O  O   . CYS A 214 ? 2.1433 1.8544 1.5765 0.0612  -0.0774 -0.1564 213  CYS A O   
1427 C  CB  . CYS A 214 ? 1.9132 1.5900 1.3798 0.0492  -0.0636 -0.1899 213  CYS A CB  
1428 S  SG  . CYS A 214 ? 4.2076 3.9046 3.6474 0.0505  -0.0490 -0.2047 213  CYS A SG  
1429 N  N   . VAL A 215 ? 2.0224 1.7076 1.4830 0.0552  -0.0914 -0.1385 214  VAL A N   
1430 C  CA  . VAL A 215 ? 1.7919 1.4813 1.2460 0.0601  -0.0975 -0.1238 214  VAL A CA  
1431 C  C   . VAL A 215 ? 1.7588 1.4380 1.2418 0.0676  -0.0986 -0.1173 214  VAL A C   
1432 O  O   . VAL A 215 ? 1.7304 1.3966 1.2461 0.0697  -0.0969 -0.1209 214  VAL A O   
1433 C  CB  . VAL A 215 ? 1.6336 1.3195 1.0749 0.0500  -0.1084 -0.1095 214  VAL A CB  
1434 C  CG1 . VAL A 215 ? 1.6190 1.3152 1.0384 0.0532  -0.1097 -0.1044 214  VAL A CG1 
1435 C  CG2 . VAL A 215 ? 1.7323 1.4255 1.1626 0.0387  -0.1067 -0.1156 214  VAL A CG2 
1436 N  N   . SER A 216 ? 1.8297 1.5151 1.3052 0.0717  -0.1015 -0.1085 215  SER A N   
1437 C  CA  . SER A 216 ? 1.8054 1.4872 1.3109 0.0769  -0.1041 -0.1002 215  SER A CA  
1438 C  C   . SER A 216 ? 1.7532 1.4196 1.2787 0.0713  -0.1224 -0.0813 215  SER A C   
1439 O  O   . SER A 216 ? 1.8122 1.4702 1.3172 0.0608  -0.1322 -0.0733 215  SER A O   
1440 C  CB  . SER A 216 ? 1.7222 1.4131 1.2105 0.0792  -0.1040 -0.0951 215  SER A CB  
1441 O  OG  . SER A 216 ? 1.6396 1.3254 1.1003 0.0732  -0.1156 -0.0849 215  SER A OG  
1442 N  N   . GLU A 217 ? 1.8401 1.5050 1.4068 0.0765  -0.1274 -0.0730 216  GLU A N   
1443 C  CA  . GLU A 217 ? 2.1011 1.7521 1.6939 0.0708  -0.1502 -0.0505 216  GLU A CA  
1444 C  C   . GLU A 217 ? 2.1719 1.8199 1.7271 0.0572  -0.1675 -0.0324 216  GLU A C   
1445 O  O   . GLU A 217 ? 2.0236 1.6574 1.5684 0.0436  -0.1863 -0.0150 216  GLU A O   
1446 C  CB  . GLU A 217 ? 2.2221 1.8791 1.8776 0.0814  -0.1514 -0.0465 216  GLU A CB  
1447 C  CG  . GLU A 217 ? 2.3598 2.0162 2.0606 0.0943  -0.1332 -0.0667 216  GLU A CG  
1448 C  CD  . GLU A 217 ? 2.4975 2.1308 2.2424 0.0954  -0.1497 -0.0555 216  GLU A CD  
1449 O  OE1 . GLU A 217 ? 2.6371 2.2531 2.3561 0.0818  -0.1716 -0.0355 216  GLU A OE1 
1450 O  OE2 . GLU A 217 ? 2.4683 2.1001 2.2748 0.1090  -0.1404 -0.0668 216  GLU A OE2 
1451 N  N   . GLU A 218 ? 2.2529 1.9117 1.7856 0.0587  -0.1613 -0.0368 217  GLU A N   
1452 C  CA  . GLU A 218 ? 2.1760 1.8291 1.6711 0.0458  -0.1746 -0.0255 217  GLU A CA  
1453 C  C   . GLU A 218 ? 2.0331 1.6800 1.4808 0.0347  -0.1732 -0.0294 217  GLU A C   
1454 O  O   . GLU A 218 ? 2.0962 1.7325 1.5195 0.0175  -0.1881 -0.0161 217  GLU A O   
1455 C  CB  . GLU A 218 ? 2.2582 1.9197 1.7398 0.0507  -0.1659 -0.0328 217  GLU A CB  
1456 C  CG  . GLU A 218 ? 2.2359 1.9085 1.7617 0.0571  -0.1655 -0.0281 217  GLU A CG  
1457 C  CD  . GLU A 218 ? 2.1580 1.8449 1.7090 0.0707  -0.1430 -0.0447 217  GLU A CD  
1458 O  OE1 . GLU A 218 ? 2.2007 1.8873 1.7299 0.0745  -0.1305 -0.0591 217  GLU A OE1 
1459 O  OE2 . GLU A 218 ? 2.0727 1.7731 1.6648 0.0754  -0.1373 -0.0442 217  GLU A OE2 
1460 N  N   . THR A 219 ? 1.8694 1.5254 1.3046 0.0424  -0.1552 -0.0475 218  THR A N   
1461 C  CA  . THR A 219 ? 1.7943 1.4519 1.1956 0.0333  -0.1503 -0.0537 218  THR A CA  
1462 C  C   . THR A 219 ? 1.7167 1.3637 1.1224 0.0194  -0.1604 -0.0418 218  THR A C   
1463 O  O   . THR A 219 ? 1.7821 1.4263 1.1558 0.0020  -0.1639 -0.0366 218  THR A O   
1464 C  CB  . THR A 219 ? 1.8688 1.5424 1.2667 0.0447  -0.1326 -0.0731 218  THR A CB  
1465 O  OG1 . THR A 219 ? 1.9959 1.6755 1.3925 0.0567  -0.1266 -0.0796 218  THR A OG1 
1466 C  CG2 . THR A 219 ? 1.8256 1.5081 1.1949 0.0364  -0.1261 -0.0804 218  THR A CG2 
1467 N  N   . LEU A 220 ? 1.6473 1.2876 1.0933 0.0261  -0.1641 -0.0382 219  LEU A N   
1468 C  CA  . LEU A 220 ? 1.7068 1.3312 1.1646 0.0145  -0.1757 -0.0258 219  LEU A CA  
1469 C  C   . LEU A 220 ? 1.8476 1.4572 1.2907 -0.0053 -0.1999 0.0010  219  LEU A C   
1470 O  O   . LEU A 220 ? 1.8468 1.4462 1.2672 -0.0254 -0.2084 0.0130  219  LEU A O   
1471 C  CB  . LEU A 220 ? 1.7406 1.3560 1.2529 0.0285  -0.1755 -0.0288 219  LEU A CB  
1472 C  CG  . LEU A 220 ? 1.8437 1.4373 1.3753 0.0200  -0.1854 -0.0203 219  LEU A CG  
1473 C  CD1 . LEU A 220 ? 1.7394 1.3393 1.2448 0.0140  -0.1698 -0.0379 219  LEU A CD1 
1474 C  CD2 . LEU A 220 ? 1.9286 1.5094 1.5241 0.0362  -0.1871 -0.0229 219  LEU A CD2 
1475 N  N   . LYS A 221 ? 1.8933 1.5025 1.3470 -0.0027 -0.2119 0.0116  220  LYS A N   
1476 C  CA  . LYS A 221 ? 1.6394 1.2359 1.0748 -0.0243 -0.2384 0.0381  220  LYS A CA  
1477 C  C   . LYS A 221 ? 1.3763 0.9752 0.7430 -0.0455 -0.2326 0.0335  220  LYS A C   
1478 O  O   . LYS A 221 ? 1.3981 0.9851 0.7320 -0.0720 -0.2486 0.0519  220  LYS A O   
1479 C  CB  . LYS A 221 ? 1.6008 1.2008 1.0659 -0.0174 -0.2521 0.0483  220  LYS A CB  
1480 C  CG  . LYS A 221 ? 1.8360 1.4370 1.3777 0.0018  -0.2580 0.0540  220  LYS A CG  
1481 C  CD  . LYS A 221 ? 1.9898 1.5991 1.5651 0.0037  -0.2751 0.0686  220  LYS A CD  
1482 C  CE  . LYS A 221 ? 2.0495 1.6659 1.7111 0.0248  -0.2763 0.0706  220  LYS A CE  
1483 N  NZ  . LYS A 221 ? 1.9796 1.6108 1.6604 0.0470  -0.2410 0.0388  220  LYS A NZ  
1484 N  N   . ILE A 222 ? 1.2417 0.8554 0.5878 -0.0347 -0.2096 0.0086  221  ILE A N   
1485 C  CA  . ILE A 222 ? 1.3194 0.9377 0.6094 -0.0498 -0.1976 -0.0033 221  ILE A CA  
1486 C  C   . ILE A 222 ? 1.4671 1.0899 0.7358 -0.0651 -0.1888 -0.0052 221  ILE A C   
1487 O  O   . ILE A 222 ? 1.4253 1.0451 0.6481 -0.0917 -0.1903 -0.0002 221  ILE A O   
1488 C  CB  . ILE A 222 ? 1.1979 0.8303 0.4847 -0.0298 -0.1752 -0.0298 221  ILE A CB  
1489 C  CG1 . ILE A 222 ? 1.1662 0.7913 0.4595 -0.0236 -0.1843 -0.0265 221  ILE A CG1 
1490 C  CG2 . ILE A 222 ? 1.1799 0.8202 0.4228 -0.0404 -0.1576 -0.0475 221  ILE A CG2 
1491 C  CD1 . ILE A 222 ? 1.1309 0.7648 0.4329 -0.0017 -0.1673 -0.0462 221  ILE A CD1 
1492 N  N   . ILE A 223 ? 1.5920 1.2227 0.8918 -0.0512 -0.1789 -0.0132 222  ILE A N   
1493 C  CA  . ILE A 223 ? 1.4427 1.0781 0.7307 -0.0663 -0.1721 -0.0134 222  ILE A CA  
1494 C  C   . ILE A 223 ? 1.2948 0.9075 0.5731 -0.0931 -0.1961 0.0165  222  ILE A C   
1495 O  O   . ILE A 223 ? 1.3192 0.9335 0.5597 -0.1203 -0.1938 0.0224  222  ILE A O   
1496 C  CB  . ILE A 223 ? 1.5606 1.2043 0.8865 -0.0478 -0.1614 -0.0267 222  ILE A CB  
1497 C  CG1 . ILE A 223 ? 1.6351 1.3008 0.9676 -0.0243 -0.1423 -0.0514 222  ILE A CG1 
1498 C  CG2 . ILE A 223 ? 1.5571 1.2068 0.8715 -0.0663 -0.1552 -0.0268 222  ILE A CG2 
1499 C  CD1 . ILE A 223 ? 1.7442 1.4124 1.1135 -0.0046 -0.1377 -0.0615 222  ILE A CD1 
1500 N  N   . GLU A 224 ? 1.3201 0.9128 0.6354 -0.0862 -0.2193 0.0362  223  GLU A N   
1501 C  CA  . GLU A 224 ? 1.4670 1.0343 0.7839 -0.1088 -0.2486 0.0697  223  GLU A CA  
1502 C  C   . GLU A 224 ? 1.8018 1.3635 1.0599 -0.1420 -0.2634 0.0882  223  GLU A C   
1503 O  O   . GLU A 224 ? 1.7754 1.3250 1.0006 -0.1736 -0.2758 0.1091  223  GLU A O   
1504 C  CB  . GLU A 224 ? 1.3568 0.9083 0.7380 -0.0892 -0.2699 0.0846  223  GLU A CB  
1505 C  CG  . GLU A 224 ? 1.7407 1.2626 1.1449 -0.1050 -0.3020 0.1192  223  GLU A CG  
1506 C  CD  . GLU A 224 ? 1.9722 1.4828 1.4525 -0.0816 -0.3209 0.1309  223  GLU A CD  
1507 O  OE1 . GLU A 224 ? 1.9615 1.4903 1.4705 -0.0565 -0.3070 0.1118  223  GLU A OE1 
1508 O  OE2 . GLU A 224 ? 2.0612 1.5454 1.5758 -0.0886 -0.3494 0.1594  223  GLU A OE2 
1509 N  N   . GLU A 225 ? 2.0510 1.6204 1.2913 -0.1378 -0.2616 0.0798  224  GLU A N   
1510 C  CA  . GLU A 225 ? 2.0348 1.5971 1.2151 -0.1705 -0.2755 0.0933  224  GLU A CA  
1511 C  C   . GLU A 225 ? 1.8763 1.4503 0.9911 -0.1963 -0.2513 0.0773  224  GLU A C   
1512 O  O   . GLU A 225 ? 2.0393 1.6038 1.0977 -0.2344 -0.2636 0.0942  224  GLU A O   
1513 C  CB  . GLU A 225 ? 2.2310 1.7969 1.4095 -0.1595 -0.2769 0.0834  224  GLU A CB  
1514 C  CG  . GLU A 225 ? 2.4621 2.0187 1.6960 -0.1469 -0.3071 0.1069  224  GLU A CG  
1515 C  CD  . GLU A 225 ? 2.6910 2.2517 1.9178 -0.1428 -0.3099 0.0991  224  GLU A CD  
1516 O  OE1 . GLU A 225 ? 2.7711 2.3378 1.9537 -0.1449 -0.2865 0.0725  224  GLU A OE1 
1517 O  OE2 . GLU A 225 ? 2.7911 2.3489 2.0608 -0.1374 -0.3356 0.1192  224  GLU A OE2 
1518 N  N   . TRP A 226 ? 1.5358 1.1329 0.6584 -0.1770 -0.2169 0.0445  225  TRP A N   
1519 C  CA  . TRP A 226 ? 1.5661 1.1815 0.6406 -0.1980 -0.1898 0.0261  225  TRP A CA  
1520 C  C   . TRP A 226 ? 1.7388 1.3507 0.7963 -0.2285 -0.1955 0.0464  225  TRP A C   
1521 O  O   . TRP A 226 ? 1.9632 1.5772 0.9611 -0.2662 -0.1908 0.0511  225  TRP A O   
1522 C  CB  . TRP A 226 ? 1.5141 1.1579 0.6148 -0.1680 -0.1560 -0.0101 225  TRP A CB  
1523 C  CG  . TRP A 226 ? 1.6962 1.3650 0.7726 -0.1863 -0.1296 -0.0250 225  TRP A CG  
1524 C  CD1 . TRP A 226 ? 1.7236 1.4073 0.8257 -0.1855 -0.1213 -0.0254 225  TRP A CD1 
1525 C  CD2 . TRP A 226 ? 1.8930 1.5772 0.9169 -0.2101 -0.1061 -0.0435 225  TRP A CD2 
1526 N  NE1 . TRP A 226 ? 1.6988 1.4099 0.7717 -0.2072 -0.0950 -0.0408 225  TRP A NE1 
1527 C  CE2 . TRP A 226 ? 1.8180 1.5308 0.8435 -0.2218 -0.0831 -0.0537 225  TRP A CE2 
1528 C  CE3 . TRP A 226 ? 2.0571 1.7337 1.0330 -0.2240 -0.1007 -0.0551 225  TRP A CE3 
1529 C  CZ2 . TRP A 226 ? 1.7898 1.5280 0.7752 -0.2453 -0.0524 -0.0754 225  TRP A CZ2 
1530 C  CZ3 . TRP A 226 ? 2.1126 1.8137 1.0566 -0.2443 -0.0690 -0.0781 225  TRP A CZ3 
1531 C  CH2 . TRP A 226 ? 1.9486 1.6793 0.8911 -0.2562 -0.0445 -0.0889 225  TRP A CH2 
1532 N  N   . PHE A 227 ? 1.6055 1.2107 0.7120 -0.2148 -0.2041 0.0571  226  PHE A N   
1533 C  CA  . PHE A 227 ? 1.8226 1.4209 0.9171 -0.2437 -0.2100 0.0765  226  PHE A CA  
1534 C  C   . PHE A 227 ? 1.9684 1.5357 1.0281 -0.2809 -0.2457 0.1184  226  PHE A C   
1535 O  O   . PHE A 227 ? 2.0824 1.6473 1.0957 -0.3209 -0.2468 0.1341  226  PHE A O   
1536 C  CB  . PHE A 227 ? 1.7830 1.3741 0.9392 -0.2207 -0.2134 0.0770  226  PHE A CB  
1537 C  CG  . PHE A 227 ? 1.7935 1.4175 0.9696 -0.2004 -0.1803 0.0422  226  PHE A CG  
1538 C  CD1 . PHE A 227 ? 1.7878 1.4390 0.9353 -0.2229 -0.1570 0.0306  226  PHE A CD1 
1539 C  CD2 . PHE A 227 ? 1.7627 1.3932 0.9869 -0.1612 -0.1734 0.0224  226  PHE A CD2 
1540 C  CE1 . PHE A 227 ? 1.6221 1.3073 0.7949 -0.2045 -0.1306 0.0012  226  PHE A CE1 
1541 C  CE2 . PHE A 227 ? 1.6960 1.3568 0.9368 -0.1453 -0.1483 -0.0057 226  PHE A CE2 
1542 C  CZ  . PHE A 227 ? 1.6399 1.3285 0.8581 -0.1659 -0.1285 -0.0156 226  PHE A CZ  
1543 N  N   . CYS A 228 ? 1.9280 1.4732 1.0109 -0.2698 -0.2763 0.1382  227  CYS A N   
1544 C  CA  . CYS A 228 ? 2.1614 1.6788 1.2133 -0.3046 -0.3160 0.1807  227  CYS A CA  
1545 C  C   . CYS A 228 ? 2.2718 1.7976 1.2406 -0.3394 -0.3103 0.1766  227  CYS A C   
1546 O  O   . CYS A 228 ? 2.4014 1.9127 1.3377 -0.3765 -0.3355 0.2078  227  CYS A O   
1547 C  CB  . CYS A 228 ? 2.2773 1.7743 1.3915 -0.2800 -0.3508 0.2024  227  CYS A CB  
1548 S  SG  . CYS A 228 ? 1.8437 1.3249 1.0536 -0.2439 -0.3577 0.2065  227  CYS A SG  
1549 N  N   . GLY A 229 ? 2.1945 1.7471 1.1466 -0.3241 -0.2729 0.1344  228  GLY A N   
1550 C  CA  . GLY A 229 ? 2.1533 1.7225 1.0617 -0.3461 -0.2532 0.1178  228  GLY A CA  
1551 C  C   . GLY A 229 ? 2.2622 1.8441 1.1290 -0.3874 -0.2362 0.1214  228  GLY A C   
1552 O  O   . GLY A 229 ? 2.2965 1.8927 1.1599 -0.3899 -0.2149 0.1109  228  GLY A O   
1553 N  N   . GLU A 230 ? 2.3744 1.9517 1.2080 -0.4226 -0.2460 0.1362  229  GLU A N   
1554 C  CA  . GLU A 230 ? 2.5304 2.1175 1.3190 -0.4679 -0.2324 0.1424  229  GLU A CA  
1555 C  C   . GLU A 230 ? 2.4322 2.0579 1.2043 -0.4643 -0.1779 0.0963  229  GLU A C   
1556 O  O   . GLU A 230 ? 2.4575 2.0988 1.2119 -0.4882 -0.1598 0.0962  229  GLU A O   
1557 C  CB  . GLU A 230 ? 2.6998 2.2752 1.4523 -0.5055 -0.2514 0.1611  229  GLU A CB  
1558 C  CG  . GLU A 230 ? 2.7583 2.2988 1.5298 -0.5187 -0.3087 0.2135  229  GLU A CG  
1559 C  CD  . GLU A 230 ? 2.7772 2.3078 1.5120 -0.5593 -0.3295 0.2323  229  GLU A CD  
1560 O  OE1 . GLU A 230 ? 2.7726 2.3207 1.4610 -0.5791 -0.2980 0.2039  229  GLU A OE1 
1561 O  OE2 . GLU A 230 ? 2.7529 2.2582 1.5072 -0.5717 -0.3780 0.2751  229  GLU A OE2 
1562 N  N   . LYS A 231 ? 2.3070 1.9480 1.0904 -0.4337 -0.1531 0.0581  230  LYS A N   
1563 C  CA  . LYS A 231 ? 2.3607 2.0385 1.1406 -0.4237 -0.1028 0.0124  230  LYS A CA  
1564 C  C   . LYS A 231 ? 2.3227 2.0190 1.1291 -0.4090 -0.0881 0.0055  230  LYS A C   
1565 O  O   . LYS A 231 ? 2.2192 1.9462 1.0136 -0.4255 -0.0556 -0.0119 230  LYS A O   
1566 C  CB  . LYS A 231 ? 2.3674 2.0503 1.1662 -0.3867 -0.0866 -0.0233 230  LYS A CB  
1567 C  CG  . LYS A 231 ? 2.4890 2.2076 1.2916 -0.3731 -0.0367 -0.0715 230  LYS A CG  
1568 C  CD  . LYS A 231 ? 2.7174 2.4517 1.4736 -0.4136 -0.0110 -0.0836 230  LYS A CD  
1569 C  CE  . LYS A 231 ? 2.6835 2.4511 1.4498 -0.3962 0.0385  -0.1352 230  LYS A CE  
1570 N  NZ  . LYS A 231 ? 2.5183 2.3170 1.3257 -0.3722 0.0601  -0.1511 230  LYS A NZ  
1571 N  N   . ALA A 232 ? 2.3171 1.9953 1.1594 -0.3797 -0.1121 0.0186  231  ALA A N   
1572 C  CA  . ALA A 232 ? 2.2922 1.9832 1.1581 -0.3661 -0.1024 0.0125  231  ALA A CA  
1573 C  C   . ALA A 232 ? 2.3585 2.0468 1.2016 -0.4068 -0.1102 0.0408  231  ALA A C   
1574 O  O   . ALA A 232 ? 2.3522 2.0700 1.1960 -0.4151 -0.0834 0.0256  231  ALA A O   
1575 C  CB  . ALA A 232 ? 2.2698 1.9371 1.1816 -0.3279 -0.1289 0.0219  231  ALA A CB  
1576 N  N   . GLY A 233 ? 2.3902 2.0431 1.2161 -0.4331 -0.1488 0.0837  232  GLY A N   
1577 C  CA  . GLY A 233 ? 2.2995 1.9405 1.1043 -0.4737 -0.1635 0.1175  232  GLY A CA  
1578 C  C   . GLY A 233 ? 2.2417 1.9142 1.0064 -0.5165 -0.1315 0.1077  232  GLY A C   
1579 O  O   . GLY A 233 ? 2.0125 1.7006 0.7702 -0.5386 -0.1177 0.1107  232  GLY A O   
1580 N  N   . GLU A 234 ? 2.4926 2.1738 1.2298 -0.5308 -0.1198 0.0959  233  GLU A N   
1581 C  CA  . GLU A 234 ? 2.7076 2.4164 1.4026 -0.5744 -0.0896 0.0855  233  GLU A CA  
1582 C  C   . GLU A 234 ? 2.7470 2.5081 1.4546 -0.5619 -0.0352 0.0385  233  GLU A C   
1583 O  O   . GLU A 234 ? 2.7446 2.5317 1.4379 -0.5936 -0.0138 0.0378  233  GLU A O   
1584 C  CB  . GLU A 234 ? 2.7898 2.4912 1.4501 -0.5918 -0.0915 0.0814  233  GLU A CB  
1585 C  CG  . GLU A 234 ? 2.8814 2.5368 1.5332 -0.6066 -0.1461 0.1275  233  GLU A CG  
1586 C  CD  . GLU A 234 ? 2.9169 2.5654 1.5422 -0.6146 -0.1492 0.1185  233  GLU A CD  
1587 O  OE1 . GLU A 234 ? 3.0401 2.7156 1.6476 -0.6122 -0.1080 0.0766  233  GLU A OE1 
1588 O  OE2 . GLU A 234 ? 2.8433 2.4588 1.4678 -0.6237 -0.1936 0.1532  233  GLU A OE2 
1589 N  N   . VAL A 235 ? 2.8242 2.6013 1.5620 -0.5167 -0.0141 0.0001  234  VAL A N   
1590 C  CA  . VAL A 235 ? 2.9021 2.7300 1.6573 -0.5029 0.0374  -0.0474 234  VAL A CA  
1591 C  C   . VAL A 235 ? 2.8349 2.6826 1.6318 -0.4800 0.0436  -0.0536 234  VAL A C   
1592 O  O   . VAL A 235 ? 2.9649 2.8605 1.7807 -0.4776 0.0830  -0.0846 234  VAL A O   
1593 C  CB  . VAL A 235 ? 2.9632 2.7978 1.7333 -0.4664 0.0575  -0.0870 234  VAL A CB  
1594 C  CG1 . VAL A 235 ? 2.9840 2.8078 1.8017 -0.4137 0.0440  -0.0953 234  VAL A CG1 
1595 C  CG2 . VAL A 235 ? 2.9269 2.8113 1.7030 -0.4679 0.1116  -0.1329 234  VAL A CG2 
1596 N  N   . GLY A 236 ? 2.7489 2.5604 1.5621 -0.4633 0.0044  -0.0253 235  GLY A N   
1597 C  CA  . GLY A 236 ? 2.5920 2.4129 1.4429 -0.4374 0.0037  -0.0319 235  GLY A CA  
1598 C  C   . GLY A 236 ? 2.7220 2.5870 1.5906 -0.4575 0.0310  -0.0398 235  GLY A C   
1599 O  O   . GLY A 236 ? 2.3509 2.2518 1.2833 -0.4251 0.0496  -0.0647 235  GLY A O   
1600 N  N   . ASP A 237 ? 3.1426 3.0055 1.9593 -0.5124 0.0305  -0.0156 236  ASP A N   
1601 C  CA  . ASP A 237 ? 3.3710 3.2801 2.1894 -0.5435 0.0610  -0.0231 236  ASP A CA  
1602 C  C   . ASP A 237 ? 3.3692 3.3432 2.2134 -0.5270 0.1144  -0.0755 236  ASP A C   
1603 O  O   . ASP A 237 ? 3.4810 3.4639 2.3155 -0.5224 0.1348  -0.0981 236  ASP A O   
1604 C  CB  . ASP A 237 ? 3.4697 3.3676 2.2366 -0.6038 0.0546  0.0092  236  ASP A CB  
1605 C  CG  . ASP A 237 ? 3.4523 3.3632 2.1896 -0.6197 0.0770  -0.0084 236  ASP A CG  
1606 O  OD1 . ASP A 237 ? 3.4599 3.3346 2.1833 -0.6064 0.0544  -0.0012 236  ASP A OD1 
1607 O  OD2 . ASP A 237 ? 3.4059 3.3644 2.1344 -0.6469 0.1176  -0.0305 236  ASP A OD2 
1608 N  N   . ASN A 238 ? 3.2255 3.2443 2.1390 -0.5067 0.1321  -0.0930 237  ASN A N   
1609 C  CA  . ASN A 238 ? 3.0857 3.1719 2.0372 -0.4913 0.1815  -0.1402 237  ASN A CA  
1610 C  C   . ASN A 238 ? 2.9873 3.1281 1.9857 -0.5077 0.2006  -0.1427 237  ASN A C   
1611 O  O   . ASN A 238 ? 2.8056 2.9292 1.8305 -0.5094 0.1714  -0.1151 237  ASN A O   
1612 C  CB  . ASN A 238 ? 3.0446 3.1330 2.0588 -0.4261 0.1802  -0.1683 237  ASN A CB  
1613 C  CG  . ASN A 238 ? 3.0311 3.1748 2.0728 -0.4093 0.2291  -0.2178 237  ASN A CG  
1614 O  OD1 . ASN A 238 ? 3.0523 3.2574 2.1244 -0.4241 0.2643  -0.2369 237  ASN A OD1 
1615 N  ND2 . ASN A 238 ? 2.9572 3.0796 1.9926 -0.3786 0.2317  -0.2395 237  ASN A ND2 
1616 N  N   . GLY A 239 ? 3.0549 3.2622 2.0660 -0.5206 0.2506  -0.1775 238  GLY A N   
1617 C  CA  . GLY A 239 ? 3.0477 3.3156 2.1035 -0.5421 0.2724  -0.1808 238  GLY A CA  
1618 C  C   . GLY A 239 ? 3.1532 3.4952 2.3002 -0.5031 0.3083  -0.2250 238  GLY A C   
1619 O  O   . GLY A 239 ? 3.0956 3.4721 2.2405 -0.4985 0.3499  -0.2629 238  GLY A O   
1620 N  N   . ILE A 240 ? 3.3214 3.6885 2.5501 -0.4750 0.2930  -0.2226 239  ILE A N   
1621 C  CA  . ILE A 240 ? 3.5716 3.8988 2.8132 -0.4741 0.2460  -0.1859 239  ILE A CA  
1622 C  C   . ILE A 240 ? 3.8517 4.1413 3.0278 -0.5330 0.2276  -0.1449 239  ILE A C   
1623 O  O   . ILE A 240 ? 3.9387 4.2698 3.0986 -0.5815 0.2546  -0.1432 239  ILE A O   
1624 C  CB  . ILE A 240 ? 2.5759 2.8381 1.8199 -0.4259 0.2058  -0.1768 239  ILE A CB  
1625 C  CG1 . ILE A 240 ? 2.5325 2.8124 1.8074 -0.3781 0.2246  -0.2130 239  ILE A CG1 
1626 C  CG2 . ILE A 240 ? 2.4601 2.7129 1.7592 -0.4040 0.1723  -0.1623 239  ILE A CG2 
1627 C  CD1 . ILE A 240 ? 2.4746 2.7001 1.7584 -0.3315 0.1888  -0.2060 239  ILE A CD1 
1628 N  N   . GLY A 241 ? 4.0024 4.2144 3.1444 -0.5293 0.1820  -0.1115 240  GLY A N   
1629 C  CA  . GLY A 241 ? 4.0267 4.1939 3.1186 -0.5789 0.1562  -0.0686 240  GLY A CA  
1630 C  C   . GLY A 241 ? 3.9730 4.1582 3.1153 -0.5910 0.1457  -0.0575 240  GLY A C   
1631 O  O   . GLY A 241 ? 4.0313 4.1635 3.1556 -0.6135 0.1116  -0.0225 240  GLY A O   
1632 N  N   . SER A 242 ? 3.4550 3.7151 2.6644 -0.5757 0.1743  -0.0883 241  SER A N   
1633 C  CA  . SER A 242 ? 3.0407 3.3337 2.3061 -0.5872 0.1691  -0.0845 241  SER A CA  
1634 C  C   . SER A 242 ? 2.5347 2.8792 1.8850 -0.5334 0.1767  -0.1180 241  SER A C   
1635 O  O   . SER A 242 ? 2.3743 2.7467 1.7403 -0.5001 0.1994  -0.1464 241  SER A O   
1636 C  CB  . SER A 242 ? 2.9592 3.3088 2.2119 -0.6476 0.2024  -0.0814 241  SER A CB  
1637 O  OG  . SER A 242 ? 2.7398 3.1598 2.0018 -0.6460 0.2524  -0.1163 241  SER A OG  
1638 N  N   . ASP A 243 ? 2.1318 2.4854 1.5355 -0.5254 0.1555  -0.1142 242  ASP A N   
1639 C  CA  . ASP A 243 ? 1.8977 2.2135 1.2862 -0.5638 0.1285  -0.0839 242  ASP A CA  
1640 C  C   . ASP A 243 ? 2.0256 2.2942 1.4419 -0.5299 0.0885  -0.0797 242  ASP A C   
1641 O  O   . ASP A 243 ? 2.1500 2.4460 1.6165 -0.4861 0.0864  -0.1018 242  ASP A O   
1642 C  CB  . ASP A 243 ? 1.8223 2.2116 1.2473 -0.6060 0.1514  -0.0868 242  ASP A CB  
1643 C  CG  . ASP A 243 ? 1.6367 2.1172 1.1451 -0.5754 0.1763  -0.1212 242  ASP A CG  
1644 O  OD1 . ASP A 243 ? 1.5248 2.0207 1.0491 -0.5315 0.1901  -0.1451 242  ASP A OD1 
1645 O  OD2 . ASP A 243 ? 1.6463 2.1842 1.2073 -0.5969 0.1814  -0.1236 242  ASP A OD2 
1646 N  N   . VAL A 244 ? 2.0309 2.2270 1.4139 -0.5516 0.0571  -0.0514 243  VAL A N   
1647 C  CA  . VAL A 244 ? 1.9696 2.1138 1.3723 -0.5244 0.0219  -0.0496 243  VAL A CA  
1648 C  C   . VAL A 244 ? 2.0886 2.2842 1.5542 -0.5172 0.0196  -0.0676 243  VAL A C   
1649 O  O   . VAL A 244 ? 2.2758 2.4534 1.7647 -0.4815 0.0002  -0.0791 243  VAL A O   
1650 C  CB  . VAL A 244 ? 1.8956 1.9566 1.2607 -0.5550 -0.0083 -0.0177 243  VAL A CB  
1651 C  CG1 . VAL A 244 ? 2.0195 2.0195 1.3299 -0.5511 -0.0180 0.0023  243  VAL A CG1 
1652 C  CG2 . VAL A 244 ? 1.8924 1.9738 1.2510 -0.6157 -0.0015 0.0001  243  VAL A CG2 
1653 N  N   . GLY A 245 ? 1.9759 2.2370 1.4680 -0.5538 0.0387  -0.0693 244  GLY A N   
1654 C  CA  . GLY A 245 ? 1.9081 2.2278 1.4647 -0.5510 0.0356  -0.0846 244  GLY A CA  
1655 C  C   . GLY A 245 ? 1.8459 2.2173 1.4525 -0.4990 0.0426  -0.1113 244  GLY A C   
1656 O  O   . GLY A 245 ? 1.7611 2.1312 1.3990 -0.4755 0.0196  -0.1197 244  GLY A O   
1657 N  N   . MET A 246 ? 1.8063 2.2213 1.4187 -0.4833 0.0740  -0.1247 245  MET A N   
1658 C  CA  . MET A 246 ? 1.6432 2.1007 1.3031 -0.4321 0.0813  -0.1485 245  MET A CA  
1659 C  C   . MET A 246 ? 1.4270 1.8139 1.0589 -0.3897 0.0551  -0.1476 245  MET A C   
1660 O  O   . MET A 246 ? 1.4204 1.8212 1.0900 -0.3533 0.0406  -0.1588 245  MET A O   
1661 C  CB  . MET A 246 ? 1.7314 2.2387 1.3970 -0.4266 0.1231  -0.1653 245  MET A CB  
1662 C  CG  . MET A 246 ? 1.7109 2.2434 1.4186 -0.3704 0.1288  -0.1885 245  MET A CG  
1663 S  SD  . MET A 246 ? 3.3536 3.9283 3.0601 -0.3621 0.1793  -0.2135 245  MET A SD  
1664 C  CE  . MET A 246 ? 1.5803 2.0636 1.1746 -0.3851 0.1764  -0.1942 245  MET A CE  
1665 N  N   . LEU A 247 ? 1.3094 1.6228 0.8760 -0.3967 0.0485  -0.1324 246  LEU A N   
1666 C  CA  . LEU A 247 ? 1.3797 1.6255 0.9184 -0.3605 0.0264  -0.1302 246  LEU A CA  
1667 C  C   . LEU A 247 ? 1.3398 1.5513 0.8906 -0.3505 -0.0058 -0.1283 246  LEU A C   
1668 O  O   . LEU A 247 ? 1.2400 1.4399 0.8012 -0.3123 -0.0180 -0.1381 246  LEU A O   
1669 C  CB  . LEU A 247 ? 1.4924 1.6704 0.9654 -0.3761 0.0231  -0.1107 246  LEU A CB  
1670 C  CG  . LEU A 247 ? 1.4696 1.6495 0.9135 -0.3626 0.0441  -0.1165 246  LEU A CG  
1671 C  CD1 . LEU A 247 ? 1.3563 1.6152 0.8242 -0.3734 0.0824  -0.1350 246  LEU A CD1 
1672 C  CD2 . LEU A 247 ? 1.6496 1.7651 1.0282 -0.3887 0.0346  -0.0911 246  LEU A CD2 
1673 N  N   . ARG A 248 ? 1.5618 1.7529 1.1066 -0.3868 -0.0193 -0.1163 247  ARG A N   
1674 C  CA  . ARG A 248 ? 1.6299 1.7854 1.1816 -0.3814 -0.0474 -0.1190 247  ARG A CA  
1675 C  C   . ARG A 248 ? 1.5094 1.7278 1.1127 -0.3640 -0.0520 -0.1361 247  ARG A C   
1676 O  O   . ARG A 248 ? 1.4019 1.5985 1.0068 -0.3405 -0.0715 -0.1443 247  ARG A O   
1677 C  CB  . ARG A 248 ? 1.6379 1.7587 1.1759 -0.4272 -0.0600 -0.1046 247  ARG A CB  
1678 C  CG  . ARG A 248 ? 1.6540 1.6930 1.1438 -0.4401 -0.0685 -0.0840 247  ARG A CG  
1679 C  CD  . ARG A 248 ? 1.7268 1.7294 1.2085 -0.4861 -0.0827 -0.0688 247  ARG A CD  
1680 N  NE  . ARG A 248 ? 1.9342 1.9111 1.4322 -0.4830 -0.1037 -0.0823 247  ARG A NE  
1681 C  CZ  . ARG A 248 ? 2.1335 2.0822 1.6327 -0.5209 -0.1177 -0.0764 247  ARG A CZ  
1682 N  NH1 . ARG A 248 ? 2.1661 2.1094 1.6528 -0.5652 -0.1141 -0.0536 247  ARG A NH1 
1683 N  NH2 . ARG A 248 ? 2.2082 2.1324 1.7176 -0.5174 -0.1354 -0.0935 247  ARG A NH2 
1684 N  N   . GLU A 249 ? 1.4691 1.7678 1.1159 -0.3765 -0.0341 -0.1410 248  GLU A N   
1685 C  CA  . GLU A 249 ? 1.3457 1.7126 1.0520 -0.3586 -0.0399 -0.1541 248  GLU A CA  
1686 C  C   . GLU A 249 ? 1.4289 1.8022 1.1464 -0.3078 -0.0384 -0.1644 248  GLU A C   
1687 O  O   . GLU A 249 ? 1.6041 1.9890 1.3449 -0.2854 -0.0590 -0.1698 248  GLU A O   
1688 C  CB  . GLU A 249 ? 1.3629 1.8188 1.1229 -0.3830 -0.0178 -0.1571 248  GLU A CB  
1689 C  CG  . GLU A 249 ? 1.4990 2.0355 1.3347 -0.3603 -0.0227 -0.1690 248  GLU A CG  
1690 C  CD  . GLU A 249 ? 1.6276 2.2191 1.5030 -0.3303 0.0073  -0.1817 248  GLU A CD  
1691 O  OE1 . GLU A 249 ? 1.7826 2.3993 1.6549 -0.3501 0.0409  -0.1845 248  GLU A OE1 
1692 O  OE2 . GLU A 249 ? 1.6043 2.2125 1.5132 -0.2887 -0.0024 -0.1896 248  GLU A OE2 
1693 N  N   . ALA A 250 ? 1.4008 1.7636 1.0977 -0.2928 -0.0157 -0.1659 249  ALA A N   
1694 C  CA  . ALA A 250 ? 1.1582 1.5204 0.8627 -0.2468 -0.0130 -0.1754 249  ALA A CA  
1695 C  C   . ALA A 250 ? 1.2260 1.5125 0.8853 -0.2249 -0.0351 -0.1708 249  ALA A C   
1696 O  O   . ALA A 250 ? 1.3698 1.6575 1.0427 -0.1910 -0.0462 -0.1764 249  ALA A O   
1697 C  CB  . ALA A 250 ? 1.1634 1.5382 0.8578 -0.2421 0.0198  -0.1816 249  ALA A CB  
1698 N  N   . VAL A 251 ? 1.3605 1.5823 0.9697 -0.2445 -0.0417 -0.1599 250  VAL A N   
1699 C  CA  . VAL A 251 ? 1.2845 1.4379 0.8582 -0.2249 -0.0599 -0.1576 250  VAL A CA  
1700 C  C   . VAL A 251 ? 1.3879 1.5422 0.9755 -0.2214 -0.0832 -0.1638 250  VAL A C   
1701 O  O   . VAL A 251 ? 1.4784 1.6092 1.0554 -0.1948 -0.0944 -0.1683 250  VAL A O   
1702 C  CB  . VAL A 251 ? 1.6582 1.7414 1.1857 -0.2454 -0.0639 -0.1441 250  VAL A CB  
1703 C  CG1 . VAL A 251 ? 1.8667 1.9350 1.3939 -0.2821 -0.0756 -0.1387 250  VAL A CG1 
1704 C  CG2 . VAL A 251 ? 1.3901 1.4124 0.8915 -0.2181 -0.0764 -0.1444 250  VAL A CG2 
1705 N  N   . LEU A 252 ? 1.4377 1.6199 1.0458 -0.2516 -0.0904 -0.1640 251  LEU A N   
1706 C  CA  . LEU A 252 ? 1.4839 1.6679 1.0996 -0.2562 -0.1140 -0.1705 251  LEU A CA  
1707 C  C   . LEU A 252 ? 1.4173 1.6506 1.0665 -0.2277 -0.1231 -0.1757 251  LEU A C   
1708 O  O   . LEU A 252 ? 1.3777 1.5894 1.0106 -0.2153 -0.1416 -0.1798 251  LEU A O   
1709 C  CB  . LEU A 252 ? 1.6306 1.8416 1.2655 -0.2982 -0.1198 -0.1688 251  LEU A CB  
1710 C  CG  . LEU A 252 ? 1.2374 1.4452 0.8725 -0.3128 -0.1460 -0.1764 251  LEU A CG  
1711 C  CD1 . LEU A 252 ? 1.2644 1.3861 0.8482 -0.3148 -0.1554 -0.1828 251  LEU A CD1 
1712 C  CD2 . LEU A 252 ? 1.2623 1.5128 0.9274 -0.3546 -0.1506 -0.1737 251  LEU A CD2 
1713 N  N   . ASN A 253 ? 1.2818 1.5796 0.9779 -0.2177 -0.1092 -0.1755 252  ASN A N   
1714 C  CA  . ASN A 253 ? 1.2641 1.6164 1.0078 -0.1928 -0.1208 -0.1777 252  ASN A CA  
1715 C  C   . ASN A 253 ? 1.3549 1.6709 1.0752 -0.1549 -0.1273 -0.1778 252  ASN A C   
1716 O  O   . ASN A 253 ? 1.3788 1.7141 1.1178 -0.1383 -0.1481 -0.1757 252  ASN A O   
1717 C  CB  . ASN A 253 ? 1.2300 1.6559 1.0356 -0.1880 -0.0988 -0.1807 252  ASN A CB  
1718 C  CG  . ASN A 253 ? 1.2660 1.7591 1.1406 -0.1678 -0.1146 -0.1808 252  ASN A CG  
1719 O  OD1 . ASN A 253 ? 1.2933 1.7734 1.1623 -0.1516 -0.1422 -0.1761 252  ASN A OD1 
1720 N  ND2 . ASN A 253 ? 1.3072 1.8743 1.2496 -0.1696 -0.0971 -0.1855 252  ASN A ND2 
1721 N  N   . ASN A 254 ? 1.6391 1.9016 1.3172 -0.1444 -0.1119 -0.1780 253  ASN A N   
1722 C  CA  . ASN A 254 ? 1.8059 2.0347 1.4627 -0.1109 -0.1150 -0.1777 253  ASN A CA  
1723 C  C   . ASN A 254 ? 1.7655 1.9318 1.3709 -0.1134 -0.1295 -0.1776 253  ASN A C   
1724 O  O   . ASN A 254 ? 1.7778 1.9053 1.3561 -0.0918 -0.1277 -0.1769 253  ASN A O   
1725 C  CB  . ASN A 254 ? 1.8662 2.0780 1.5108 -0.0973 -0.0901 -0.1788 253  ASN A CB  
1726 C  CG  . ASN A 254 ? 1.8941 2.1667 1.5893 -0.0891 -0.0711 -0.1848 253  ASN A CG  
1727 O  OD1 . ASN A 254 ? 1.8800 2.2040 1.6278 -0.0764 -0.0798 -0.1868 253  ASN A OD1 
1728 N  ND2 . ASN A 254 ? 1.9100 2.1777 1.5908 -0.0971 -0.0451 -0.1882 253  ASN A ND2 
1729 N  N   . GLY A 255 ? 1.8280 1.9858 1.4220 -0.1405 -0.1426 -0.1803 254  GLY A N   
1730 C  CA  . GLY A 255 ? 1.6079 1.7047 1.1550 -0.1463 -0.1502 -0.1857 254  GLY A CA  
1731 C  C   . GLY A 255 ? 1.6246 1.6764 1.1513 -0.1636 -0.1375 -0.1853 254  GLY A C   
1732 O  O   . GLY A 255 ? 1.5872 1.6595 1.1308 -0.1792 -0.1270 -0.1795 254  GLY A O   
1733 N  N   . GLY A 256 ? 1.7825 1.7740 1.2750 -0.1632 -0.1389 -0.1910 255  GLY A N   
1734 C  CA  . GLY A 256 ? 1.8317 1.7744 1.3101 -0.1764 -0.1311 -0.1874 255  GLY A CA  
1735 C  C   . GLY A 256 ? 1.8424 1.7755 1.3184 -0.1610 -0.1176 -0.1752 255  GLY A C   
1736 O  O   . GLY A 256 ? 1.8865 1.8024 1.3589 -0.1780 -0.1121 -0.1649 255  GLY A O   
1737 N  N   . GLY A 257 ? 1.8747 1.8179 1.3499 -0.1316 -0.1140 -0.1751 256  GLY A N   
1738 C  CA  . GLY A 257 ? 1.8429 1.7630 1.3067 -0.1147 -0.1044 -0.1667 256  GLY A CA  
1739 C  C   . GLY A 257 ? 1.6728 1.6111 1.1396 -0.1204 -0.0914 -0.1566 256  GLY A C   
1740 O  O   . GLY A 257 ? 1.6875 1.5898 1.1354 -0.1234 -0.0886 -0.1466 256  GLY A O   
1741 N  N   . TRP A 258 ? 1.5663 1.5604 1.0569 -0.1225 -0.0832 -0.1596 257  TRP A N   
1742 C  CA  . TRP A 258 ? 1.4924 1.5050 0.9820 -0.1222 -0.0657 -0.1560 257  TRP A CA  
1743 C  C   . TRP A 258 ? 1.5642 1.6399 1.0850 -0.1362 -0.0516 -0.1611 257  TRP A C   
1744 O  O   . TRP A 258 ? 1.5176 1.6341 1.0723 -0.1373 -0.0579 -0.1672 257  TRP A O   
1745 C  CB  . TRP A 258 ? 1.5902 1.5988 1.0772 -0.0892 -0.0625 -0.1600 257  TRP A CB  
1746 C  CG  . TRP A 258 ? 1.7661 1.8106 1.2842 -0.0676 -0.0691 -0.1685 257  TRP A CG  
1747 C  CD1 . TRP A 258 ? 1.7949 1.8282 1.3121 -0.0581 -0.0866 -0.1697 257  TRP A CD1 
1748 C  CD2 . TRP A 258 ? 1.8468 1.9439 1.4027 -0.0543 -0.0597 -0.1760 257  TRP A CD2 
1749 N  NE1 . TRP A 258 ? 1.8108 1.8851 1.3598 -0.0412 -0.0927 -0.1731 257  TRP A NE1 
1750 C  CE2 . TRP A 258 ? 1.8755 1.9893 1.4543 -0.0362 -0.0769 -0.1772 257  TRP A CE2 
1751 C  CE3 . TRP A 258 ? 1.9286 2.0603 1.5023 -0.0564 -0.0374 -0.1829 257  TRP A CE3 
1752 C  CZ2 . TRP A 258 ? 1.9905 2.1525 1.6165 -0.0176 -0.0764 -0.1819 257  TRP A CZ2 
1753 C  CZ3 . TRP A 258 ? 1.9340 2.1152 1.5568 -0.0365 -0.0319 -0.1927 257  TRP A CZ3 
1754 C  CH2 . TRP A 258 ? 1.9444 2.1396 1.5965 -0.0159 -0.0532 -0.1907 257  TRP A CH2 
1755 N  N   . HIS A 259 ? 1.6622 1.7479 1.1718 -0.1481 -0.0322 -0.1590 258  HIS A N   
1756 C  CA  . HIS A 259 ? 1.6730 1.8229 1.2143 -0.1578 -0.0107 -0.1682 258  HIS A CA  
1757 C  C   . HIS A 259 ? 1.5688 1.7292 1.1075 -0.1369 0.0092  -0.1787 258  HIS A C   
1758 O  O   . HIS A 259 ? 1.4934 1.6100 0.9894 -0.1356 0.0108  -0.1730 258  HIS A O   
1759 C  CB  . HIS A 259 ? 1.7775 1.9344 1.3038 -0.2014 -0.0004 -0.1590 258  HIS A CB  
1760 C  CG  . HIS A 259 ? 1.8445 1.9595 1.3182 -0.2182 0.0071  -0.1471 258  HIS A CG  
1761 N  ND1 . HIS A 259 ? 1.8453 1.9796 1.3045 -0.2190 0.0317  -0.1549 258  HIS A ND1 
1762 C  CD2 . HIS A 259 ? 1.7769 1.8309 1.2098 -0.2357 -0.0087 -0.1276 258  HIS A CD2 
1763 C  CE1 . HIS A 259 ? 1.7974 1.8856 1.2033 -0.2394 0.0288  -0.1387 258  HIS A CE1 
1764 N  NE2 . HIS A 259 ? 1.7489 1.7884 1.1419 -0.2485 0.0031  -0.1203 258  HIS A NE2 
1765 N  N   . GLY A 260 ? 1.5863 1.8044 1.1741 -0.1208 0.0233  -0.1945 259  GLY A N   
1766 C  CA  . GLY A 260 ? 1.7578 1.9839 1.3516 -0.0961 0.0417  -0.2092 259  GLY A CA  
1767 C  C   . GLY A 260 ? 1.9075 2.1456 1.4765 -0.1179 0.0738  -0.2183 259  GLY A C   
1768 O  O   . GLY A 260 ? 1.9307 2.1517 1.4798 -0.1039 0.0867  -0.2289 259  GLY A O   
1769 N  N   . HIS A 261 ? 2.0026 2.2689 1.5687 -0.1554 0.0866  -0.2145 260  HIS A N   
1770 C  CA  . HIS A 261 ? 2.0071 2.3070 1.5617 -0.1798 0.1234  -0.2278 260  HIS A CA  
1771 C  C   . HIS A 261 ? 1.7927 2.0458 1.2761 -0.1916 0.1336  -0.2262 260  HIS A C   
1772 O  O   . HIS A 261 ? 1.7757 2.0533 1.2540 -0.1941 0.1657  -0.2478 260  HIS A O   
1773 C  CB  . HIS A 261 ? 2.1066 2.4381 1.6626 -0.2245 0.1308  -0.2177 260  HIS A CB  
1774 C  CG  . HIS A 261 ? 2.1502 2.5507 1.7841 -0.2194 0.1328  -0.2266 260  HIS A CG  
1775 N  ND1 . HIS A 261 ? 2.1848 2.5976 1.8307 -0.2480 0.1177  -0.2114 260  HIS A ND1 
1776 C  CD2 . HIS A 261 ? 2.1456 2.6064 1.8534 -0.1897 0.1456  -0.2481 260  HIS A CD2 
1777 C  CE1 . HIS A 261 ? 2.1625 2.6433 1.8841 -0.2378 0.1205  -0.2226 260  HIS A CE1 
1778 N  NE2 . HIS A 261 ? 2.1432 2.6554 1.9066 -0.2014 0.1367  -0.2439 260  HIS A NE2 
1779 N  N   . GLY A 262 ? 1.6899 1.8774 1.1205 -0.1998 0.1070  -0.2023 261  GLY A N   
1780 C  CA  . GLY A 262 ? 1.6775 1.8214 1.0433 -0.2113 0.1107  -0.1978 261  GLY A CA  
1781 C  C   . GLY A 262 ? 1.7764 1.8634 1.0856 -0.2410 0.0858  -0.1656 261  GLY A C   
1782 O  O   . GLY A 262 ? 1.7543 1.8116 1.0742 -0.2356 0.0575  -0.1476 261  GLY A O   
1783 N  N   . TRP A 263 ? 1.8733 1.9432 1.1223 -0.2724 0.0959  -0.1590 262  TRP A N   
1784 C  CA  . TRP A 263 ? 1.9351 1.9510 1.1297 -0.3041 0.0704  -0.1248 262  TRP A CA  
1785 C  C   . TRP A 263 ? 2.0783 2.1074 1.2639 -0.3489 0.0720  -0.1066 262  TRP A C   
1786 O  O   . TRP A 263 ? 2.1189 2.2046 1.3210 -0.3670 0.1020  -0.1224 262  TRP A O   
1787 C  CB  . TRP A 263 ? 1.9670 1.9579 1.0949 -0.3236 0.0761  -0.1220 262  TRP A CB  
1788 C  CG  . TRP A 263 ? 1.9116 1.8826 1.0403 -0.2865 0.0726  -0.1372 262  TRP A CG  
1789 C  CD1 . TRP A 263 ? 1.9627 1.9621 1.1016 -0.2668 0.1015  -0.1716 262  TRP A CD1 
1790 C  CD2 . TRP A 263 ? 1.8156 1.7329 0.9376 -0.2655 0.0386  -0.1188 262  TRP A CD2 
1791 N  NE1 . TRP A 263 ? 1.9355 1.8986 1.0700 -0.2368 0.0856  -0.1740 262  TRP A NE1 
1792 C  CE2 . TRP A 263 ? 1.9105 1.8263 1.0350 -0.2362 0.0478  -0.1418 262  TRP A CE2 
1793 C  CE3 . TRP A 263 ? 1.7023 1.5733 0.8216 -0.2684 0.0022  -0.0863 262  TRP A CE3 
1794 C  CZ2 . TRP A 263 ? 1.7944 1.6674 0.9159 -0.2128 0.0219  -0.1315 262  TRP A CZ2 
1795 C  CZ3 . TRP A 263 ? 1.6686 1.5004 0.7903 -0.2425 -0.0214 -0.0783 262  TRP A CZ3 
1796 C  CH2 . TRP A 263 ? 1.6821 1.5169 0.8035 -0.2165 -0.0115 -0.0999 262  TRP A CH2 
1797 N  N   . VAL A 264 ? 2.1901 2.1670 1.3537 -0.3670 0.0395  -0.0730 263  VAL A N   
1798 C  CA  . VAL A 264 ? 2.3448 2.3231 1.4984 -0.4112 0.0356  -0.0512 263  VAL A CA  
1799 C  C   . VAL A 264 ? 2.3897 2.3153 1.4781 -0.4522 0.0140  -0.0139 263  VAL A C   
1800 O  O   . VAL A 264 ? 2.2679 2.1410 1.3381 -0.4383 -0.0138 0.0031  263  VAL A O   
1801 C  CB  . VAL A 264 ? 2.4423 2.4074 1.6465 -0.3962 0.0133  -0.0452 263  VAL A CB  
1802 C  CG1 . VAL A 264 ? 2.4877 2.3852 1.6919 -0.3718 -0.0228 -0.0279 263  VAL A CG1 
1803 C  CG2 . VAL A 264 ? 2.5328 2.5034 1.7317 -0.4435 0.0118  -0.0261 263  VAL A CG2 
1804 N  N   . GLY A 265 ? 2.5535 2.4961 1.6081 -0.5045 0.0263  0.0002  264  GLY A N   
1805 C  CA  . GLY A 265 ? 2.5702 2.4616 1.5667 -0.5500 0.0000  0.0429  264  GLY A CA  
1806 C  C   . GLY A 265 ? 2.4561 2.3330 1.3809 -0.5715 0.0024  0.0510  264  GLY A C   
1807 O  O   . GLY A 265 ? 2.2403 2.1502 1.1560 -0.5550 0.0309  0.0189  264  GLY A O   
1808 N  N   . GLU A 266 ? 2.5342 2.3591 1.4079 -0.6102 -0.0301 0.0951  265  GLU A N   
1809 C  CA  . GLU A 266 ? 2.6265 2.4323 1.4224 -0.6401 -0.0354 0.1102  265  GLU A CA  
1810 C  C   . GLU A 266 ? 2.4987 2.2312 1.2846 -0.6350 -0.0902 0.1525  265  GLU A C   
1811 O  O   . GLU A 266 ? 2.4056 2.0990 1.2349 -0.6234 -0.1225 0.1767  265  GLU A O   
1812 C  CB  . GLU A 266 ? 2.7497 2.5763 1.4762 -0.7107 -0.0167 0.1262  265  GLU A CB  
1813 C  CG  . GLU A 266 ? 2.6138 2.5198 1.3549 -0.7193 0.0410  0.0837  265  GLU A CG  
1814 C  CD  . GLU A 266 ? 2.5899 2.5176 1.2972 -0.7837 0.0557  0.1017  265  GLU A CD  
1815 O  OE1 . GLU A 266 ? 2.6694 2.5468 1.3428 -0.8206 0.0183  0.1477  265  GLU A OE1 
1816 O  OE2 . GLU A 266 ? 2.5888 2.5853 1.3126 -0.7957 0.1033  0.0696  265  GLU A OE2 
1817 N  N   . GLY A 267 ? 2.3936 2.1085 1.1257 -0.6445 -0.1005 0.1601  266  GLY A N   
1818 C  CA  . GLY A 267 ? 2.3488 2.0016 1.0772 -0.6452 -0.1534 0.2032  266  GLY A CA  
1819 C  C   . GLY A 267 ? 2.1983 1.8303 0.9640 -0.5905 -0.1716 0.1925  266  GLY A C   
1820 O  O   . GLY A 267 ? 2.2940 1.9600 1.0925 -0.5492 -0.1418 0.1488  266  GLY A O   
1821 N  N   . LYS A 268 ? 2.1006 1.6787 0.8740 -0.5885 -0.2214 0.2330  267  LYS A N   
1822 C  CA  . LYS A 268 ? 1.9805 1.5397 0.7982 -0.5394 -0.2413 0.2269  267  LYS A CA  
1823 C  C   . LYS A 268 ? 1.8595 1.4051 0.7690 -0.4890 -0.2498 0.2188  267  LYS A C   
1824 O  O   . LYS A 268 ? 1.7707 1.3050 0.7074 -0.4967 -0.2540 0.2294  267  LYS A O   
1825 C  CB  . LYS A 268 ? 2.0989 1.6167 0.8993 -0.5589 -0.2882 0.2706  267  LYS A CB  
1826 C  CG  . LYS A 268 ? 2.4565 1.9983 1.2136 -0.5946 -0.2725 0.2644  267  LYS A CG  
1827 C  CD  . LYS A 268 ? 2.6272 2.1327 1.3811 -0.6183 -0.3208 0.3085  267  LYS A CD  
1828 C  CE  . LYS A 268 ? 2.5337 2.0201 1.3274 -0.5787 -0.3489 0.3127  267  LYS A CE  
1829 N  NZ  . LYS A 268 ? 2.5548 2.0021 1.4055 -0.5477 -0.3865 0.3397  267  LYS A NZ  
1830 N  N   . TRP A 269 ? 1.9936 1.5402 0.9469 -0.4403 -0.2507 0.1981  268  TRP A N   
1831 C  CA  . TRP A 269 ? 1.9562 1.4931 0.9913 -0.3916 -0.2544 0.1846  268  TRP A CA  
1832 C  C   . TRP A 269 ? 1.9421 1.4266 1.0213 -0.3821 -0.2998 0.2212  268  TRP A C   
1833 O  O   . TRP A 269 ? 2.0864 1.5469 1.1469 -0.3955 -0.3317 0.2522  268  TRP A O   
1834 C  CB  . TRP A 269 ? 1.8982 1.4613 0.9602 -0.3456 -0.2333 0.1464  268  TRP A CB  
1835 C  CG  . TRP A 269 ? 2.0206 1.6340 1.0651 -0.3412 -0.1891 0.1058  268  TRP A CG  
1836 C  CD1 . TRP A 269 ? 2.1192 1.7580 1.1227 -0.3446 -0.1676 0.0848  268  TRP A CD1 
1837 C  CD2 . TRP A 269 ? 2.0949 1.7394 1.1671 -0.3329 -0.1620 0.0812  268  TRP A CD2 
1838 N  NE1 . TRP A 269 ? 2.1188 1.8030 1.1299 -0.3354 -0.1282 0.0483  268  TRP A NE1 
1839 C  CE2 . TRP A 269 ? 2.1581 1.8489 1.2111 -0.3290 -0.1255 0.0472  268  TRP A CE2 
1840 C  CE3 . TRP A 269 ? 1.9828 1.6194 1.0958 -0.3294 -0.1663 0.0842  268  TRP A CE3 
1841 C  CZ2 . TRP A 269 ? 2.0936 1.8274 1.1734 -0.3200 -0.0956 0.0191  268  TRP A CZ2 
1842 C  CZ3 . TRP A 269 ? 1.9079 1.5864 1.0392 -0.3242 -0.1368 0.0559  268  TRP A CZ3 
1843 C  CH2 . TRP A 269 ? 1.9397 1.6682 1.0571 -0.3191 -0.1029 0.0252  268  TRP A CH2 
1844 N  N   . THR A 270 ? 1.9726 1.4404 1.1133 -0.3590 -0.3027 0.2159  269  THR A N   
1845 C  CA  . THR A 270 ? 2.2092 1.6302 1.4110 -0.3383 -0.3388 0.2395  269  THR A CA  
1846 C  C   . THR A 270 ? 2.1750 1.6067 1.4420 -0.2844 -0.3218 0.2026  269  THR A C   
1847 O  O   . THR A 270 ? 2.1657 1.6179 1.4479 -0.2707 -0.2937 0.1704  269  THR A O   
1848 C  CB  . THR A 270 ? 2.2599 1.6399 1.4786 -0.3619 -0.3600 0.2675  269  THR A CB  
1849 O  OG1 . THR A 270 ? 2.3160 1.7126 1.5543 -0.3530 -0.3304 0.2352  269  THR A OG1 
1850 C  CG2 . THR A 270 ? 2.2193 1.5899 1.3663 -0.4210 -0.3759 0.3064  269  THR A CG2 
1851 N  N   . VAL A 271 ? 2.1552 1.5752 1.4600 -0.2569 -0.3396 0.2083  270  VAL A N   
1852 C  CA  . VAL A 271 ? 2.2046 1.6386 1.5637 -0.2095 -0.3214 0.1736  270  VAL A CA  
1853 C  C   . VAL A 271 ? 2.4054 1.8018 1.8429 -0.1843 -0.3405 0.1804  270  VAL A C   
1854 O  O   . VAL A 271 ? 2.6155 1.9808 2.0814 -0.1875 -0.3758 0.2146  270  VAL A O   
1855 C  CB  . VAL A 271 ? 1.6928 1.1501 1.0415 -0.1936 -0.3187 0.1663  270  VAL A CB  
1856 C  CG1 . VAL A 271 ? 1.9984 1.4332 1.3351 -0.2143 -0.3580 0.2085  270  VAL A CG1 
1857 C  CG2 . VAL A 271 ? 1.5403 1.0062 0.9497 -0.1484 -0.3060 0.1389  270  VAL A CG2 
1858 N  N   . LYS A 272 ? 2.4122 1.8119 1.8859 -0.1600 -0.3173 0.1468  271  LYS A N   
1859 C  CA  . LYS A 272 ? 2.3532 1.7189 1.9024 -0.1339 -0.3271 0.1427  271  LYS A CA  
1860 C  C   . LYS A 272 ? 2.3544 1.7442 1.9374 -0.0955 -0.2970 0.0993  271  LYS A C   
1861 O  O   . LYS A 272 ? 2.3912 1.8121 1.9439 -0.0931 -0.2680 0.0691  271  LYS A O   
1862 C  CB  . LYS A 272 ? 2.2399 1.5704 1.7985 -0.1514 -0.3323 0.1470  271  LYS A CB  
1863 C  CG  . LYS A 272 ? 2.3005 1.5929 1.8432 -0.1878 -0.3694 0.1965  271  LYS A CG  
1864 C  CD  . LYS A 272 ? 2.2859 1.5503 1.8220 -0.2123 -0.3690 0.1981  271  LYS A CD  
1865 C  CE  . LYS A 272 ? 2.2298 1.4559 1.7417 -0.2542 -0.4064 0.2509  271  LYS A CE  
1866 N  NZ  . LYS A 272 ? 2.0707 1.2698 1.5732 -0.2825 -0.4059 0.2542  271  LYS A NZ  
1867 N  N   . LYS A 273 ? 2.3134 1.6909 1.9603 -0.0670 -0.3048 0.0977  272  LYS A N   
1868 C  CA  . LYS A 273 ? 2.1878 1.5848 1.8688 -0.0336 -0.2761 0.0578  272  LYS A CA  
1869 C  C   . LYS A 273 ? 2.2578 1.6195 2.0023 -0.0173 -0.2726 0.0404  272  LYS A C   
1870 O  O   . LYS A 273 ? 2.2353 1.5660 2.0423 -0.0068 -0.2947 0.0584  272  LYS A O   
1871 C  CB  . LYS A 273 ? 2.0157 1.4340 1.7223 -0.0136 -0.2798 0.0622  272  LYS A CB  
1872 C  CG  . LYS A 273 ? 1.9085 1.3548 1.5542 -0.0302 -0.2850 0.0780  272  LYS A CG  
1873 C  CD  . LYS A 273 ? 1.9055 1.3674 1.5805 -0.0143 -0.2942 0.0864  272  LYS A CD  
1874 C  CE  . LYS A 273 ? 2.0013 1.4355 1.7447 -0.0090 -0.3286 0.1177  272  LYS A CE  
1875 N  NZ  . LYS A 273 ? 1.9958 1.4040 1.7114 -0.0410 -0.3667 0.1621  272  LYS A NZ  
1876 N  N   . GLY A 274 ? 2.3329 1.6988 2.0638 -0.0156 -0.2459 0.0049  273  GLY A N   
1877 C  CA  . GLY A 274 ? 2.4065 1.7339 2.1861 -0.0064 -0.2408 -0.0155 273  GLY A CA  
1878 C  C   . GLY A 274 ? 2.4030 1.7468 2.1759 0.0057  -0.2052 -0.0646 273  GLY A C   
1879 O  O   . GLY A 274 ? 2.3906 1.7746 2.1121 0.0011  -0.1871 -0.0794 273  GLY A O   
1880 N  N   . ASN A 275 ? 2.4809 1.7919 2.3065 0.0205  -0.1959 -0.0900 274  ASN A N   
1881 C  CA  . ASN A 275 ? 2.4504 1.7679 2.2628 0.0244  -0.1642 -0.1374 274  ASN A CA  
1882 C  C   . ASN A 275 ? 2.5254 1.8313 2.2911 -0.0046 -0.1657 -0.1422 274  ASN A C   
1883 O  O   . ASN A 275 ? 2.5161 1.8078 2.2646 -0.0270 -0.1890 -0.1094 274  ASN A O   
1884 C  CB  . ASN A 275 ? 2.3291 1.6125 2.2128 0.0474  -0.1510 -0.1673 274  ASN A CB  
1885 C  CG  . ASN A 275 ? 2.2816 1.5939 2.2053 0.0759  -0.1345 -0.1794 274  ASN A CG  
1886 O  OD1 . ASN A 275 ? 2.2464 1.5800 2.1624 0.0853  -0.1020 -0.2190 274  ASN A OD1 
1887 N  ND2 . ASN A 275 ? 2.3104 1.6255 2.2747 0.0865  -0.1578 -0.1439 274  ASN A ND2 
1888 N  N   . VAL A 276 ? 2.5115 1.8246 2.2558 -0.0072 -0.1414 -0.1824 275  VAL A N   
1889 C  CA  . VAL A 276 ? 2.5171 1.8218 2.2225 -0.0358 -0.1430 -0.1898 275  VAL A CA  
1890 C  C   . VAL A 276 ? 2.7307 1.9959 2.4566 -0.0363 -0.1284 -0.2306 275  VAL A C   
1891 O  O   . VAL A 276 ? 2.8580 2.1183 2.6119 -0.0147 -0.1072 -0.2629 275  VAL A O   
1892 C  CB  . VAL A 276 ? 2.3844 1.7464 2.0271 -0.0480 -0.1319 -0.1962 275  VAL A CB  
1893 C  CG1 . VAL A 276 ? 2.2954 1.6898 1.9130 -0.0547 -0.1462 -0.1583 275  VAL A CG1 
1894 C  CG2 . VAL A 276 ? 2.3881 1.7803 2.0223 -0.0288 -0.1070 -0.2281 275  VAL A CG2 
1895 N  N   . SER A 277 ? 2.9854 2.2230 2.6952 -0.0634 -0.1382 -0.2307 276  SER A N   
1896 C  CA  . SER A 277 ? 3.1011 2.2926 2.8268 -0.0693 -0.1274 -0.2692 276  SER A CA  
1897 C  C   . SER A 277 ? 3.0173 2.2395 2.7012 -0.0732 -0.1003 -0.3139 276  SER A C   
1898 O  O   . SER A 277 ? 3.0346 2.3142 2.6757 -0.0741 -0.0938 -0.3105 276  SER A O   
1899 C  CB  . SER A 277 ? 3.1973 2.3510 2.9139 -0.1022 -0.1482 -0.2534 276  SER A CB  
1900 O  OG  . SER A 277 ? 3.2099 2.4071 2.8670 -0.1303 -0.1474 -0.2526 276  SER A OG  
1901 N  N   . SER A 278 ? 2.9184 2.0989 2.6148 -0.0764 -0.0857 -0.3557 277  SER A N   
1902 C  CA  . SER A 278 ? 2.7573 1.9578 2.4053 -0.0898 -0.0639 -0.3987 277  SER A CA  
1903 C  C   . SER A 278 ? 2.6610 1.8921 2.2526 -0.1242 -0.0786 -0.3858 277  SER A C   
1904 O  O   . SER A 278 ? 2.5550 1.8343 2.0985 -0.1329 -0.0702 -0.3980 277  SER A O   
1905 C  CB  . SER A 278 ? 2.8144 1.9553 2.4865 -0.0910 -0.0465 -0.4473 277  SER A CB  
1906 O  OG  . SER A 278 ? 2.8398 1.9563 2.5756 -0.0571 -0.0309 -0.4611 277  SER A OG  
1907 N  N   . THR A 279 ? 2.6661 1.8707 2.2672 -0.1446 -0.1016 -0.3591 278  THR A N   
1908 C  CA  . THR A 279 ? 2.5250 1.7641 2.0839 -0.1776 -0.1159 -0.3420 278  THR A CA  
1909 C  C   . THR A 279 ? 2.4570 1.7617 1.9976 -0.1704 -0.1217 -0.3064 278  THR A C   
1910 O  O   . THR A 279 ? 2.2489 1.5989 1.7580 -0.1913 -0.1285 -0.2948 278  THR A O   
1911 C  CB  . THR A 279 ? 2.4559 1.6478 2.0315 -0.2045 -0.1374 -0.3211 278  THR A CB  
1912 O  OG1 . THR A 279 ? 2.5879 1.7046 2.1981 -0.2018 -0.1337 -0.3491 278  THR A OG1 
1913 C  CG2 . THR A 279 ? 2.4318 1.6547 1.9673 -0.2437 -0.1462 -0.3194 278  THR A CG2 
1914 N  N   . GLY A 280 ? 2.7358 2.0454 2.3004 -0.1406 -0.1187 -0.2908 279  GLY A N   
1915 C  CA  . GLY A 280 ? 2.8753 2.2397 2.4241 -0.1311 -0.1223 -0.2611 279  GLY A CA  
1916 C  C   . GLY A 280 ? 2.8639 2.2241 2.4190 -0.1447 -0.1425 -0.2184 279  GLY A C   
1917 O  O   . GLY A 280 ? 2.7683 2.1756 2.3013 -0.1481 -0.1455 -0.1959 279  GLY A O   
1918 N  N   . ARG A 281 ? 2.7716 2.0731 2.3568 -0.1532 -0.1561 -0.2076 280  ARG A N   
1919 C  CA  . ARG A 281 ? 2.6138 1.9024 2.2029 -0.1699 -0.1776 -0.1639 280  ARG A CA  
1920 C  C   . ARG A 281 ? 2.4284 1.7119 2.0421 -0.1447 -0.1853 -0.1387 280  ARG A C   
1921 O  O   . ARG A 281 ? 2.4018 1.6508 2.0586 -0.1195 -0.1836 -0.1498 280  ARG A O   
1922 C  CB  . ARG A 281 ? 2.7051 1.9276 2.3163 -0.1926 -0.1934 -0.1589 280  ARG A CB  
1923 C  CG  . ARG A 281 ? 2.6521 1.8638 2.2535 -0.2230 -0.2164 -0.1128 280  ARG A CG  
1924 C  CD  . ARG A 281 ? 2.6201 1.7519 2.2552 -0.2381 -0.2361 -0.1031 280  ARG A CD  
1925 N  NE  . ARG A 281 ? 2.6265 1.7092 2.3155 -0.2065 -0.2454 -0.0980 280  ARG A NE  
1926 C  CZ  . ARG A 281 ? 2.6161 1.6566 2.3311 -0.2111 -0.2735 -0.0553 280  ARG A CZ  
1927 N  NH1 . ARG A 281 ? 2.6584 1.6971 2.3424 -0.2493 -0.2933 -0.0147 280  ARG A NH1 
1928 N  NH2 . ARG A 281 ? 2.5685 1.5701 2.3424 -0.1793 -0.2824 -0.0524 280  ARG A NH2 
1929 N  N   . CYS A 282 ? 2.2958 1.6157 1.8842 -0.1520 -0.1927 -0.1069 281  CYS A N   
1930 C  CA  . CYS A 282 ? 2.1718 1.4879 1.7779 -0.1331 -0.2034 -0.0808 281  CYS A CA  
1931 C  C   . CYS A 282 ? 2.1004 1.3548 1.7409 -0.1426 -0.2306 -0.0503 281  CYS A C   
1932 O  O   . CYS A 282 ? 2.0574 1.2962 1.6783 -0.1755 -0.2463 -0.0242 281  CYS A O   
1933 C  CB  . CYS A 282 ? 2.2713 1.6393 1.8353 -0.1420 -0.2032 -0.0582 281  CYS A CB  
1934 S  SG  . CYS A 282 ? 2.1120 1.4760 1.6889 -0.1255 -0.2198 -0.0249 281  CYS A SG  
1935 N  N   . LEU A 283 ? 2.2219 1.4421 1.9167 -0.1145 -0.2365 -0.0526 282  LEU A N   
1936 C  CA  . LEU A 283 ? 2.5377 1.6937 2.2801 -0.1176 -0.2649 -0.0252 282  LEU A CA  
1937 C  C   . LEU A 283 ? 2.7824 1.9358 2.5005 -0.1431 -0.2952 0.0297  282  LEU A C   
1938 O  O   . LEU A 283 ? 3.1318 2.2360 2.8606 -0.1661 -0.3214 0.0595  282  LEU A O   
1939 C  CB  . LEU A 283 ? 2.4926 1.6268 2.3059 -0.0780 -0.2641 -0.0372 282  LEU A CB  
1940 C  CG  . LEU A 283 ? 2.3902 1.5253 2.2272 -0.0540 -0.2310 -0.0938 282  LEU A CG  
1941 C  CD1 . LEU A 283 ? 2.3726 1.4888 2.2875 -0.0164 -0.2288 -0.1036 282  LEU A CD1 
1942 C  CD2 . LEU A 283 ? 2.4674 1.5591 2.3029 -0.0727 -0.2265 -0.1183 282  LEU A CD2 
1943 N  N   . SER A 284 ? 2.5218 1.7258 2.2038 -0.1413 -0.2916 0.0426  283  SER A N   
1944 C  CA  . SER A 284 ? 2.3735 1.5793 2.0240 -0.1667 -0.3175 0.0913  283  SER A CA  
1945 C  C   . SER A 284 ? 2.5092 1.7207 2.1029 -0.2127 -0.3204 0.1095  283  SER A C   
1946 O  O   . SER A 284 ? 2.6506 1.8264 2.2367 -0.2417 -0.3493 0.1509  283  SER A O   
1947 C  CB  . SER A 284 ? 2.0435 1.3018 1.6666 -0.1537 -0.3085 0.0927  283  SER A CB  
1948 O  OG  . SER A 284 ? 1.9887 1.3012 1.5650 -0.1569 -0.2779 0.0643  283  SER A OG  
1949 N  N   . CYS A 285 ? 2.3073 1.5649 1.8634 -0.2211 -0.2918 0.0805  284  CYS A N   
1950 C  CA  . CYS A 285 ? 2.1488 1.4255 1.6543 -0.2647 -0.2899 0.0957  284  CYS A CA  
1951 C  C   . CYS A 285 ? 2.3210 1.5842 1.8331 -0.2814 -0.2813 0.0744  284  CYS A C   
1952 O  O   . CYS A 285 ? 2.3887 1.6722 1.8655 -0.3183 -0.2772 0.0835  284  CYS A O   
1953 C  CB  . CYS A 285 ? 1.8669 1.2156 1.3240 -0.2677 -0.2659 0.0852  284  CYS A CB  
1954 S  SG  . CYS A 285 ? 2.1049 1.5072 1.5676 -0.2373 -0.2308 0.0317  284  CYS A SG  
1955 N  N   . SER A 286 ? 2.4247 1.6558 1.9813 -0.2559 -0.2770 0.0442  285  SER A N   
1956 C  CA  . SER A 286 ? 2.5646 1.7713 2.1301 -0.2721 -0.2724 0.0220  285  SER A CA  
1957 C  C   . SER A 286 ? 2.4215 1.6898 1.9511 -0.2866 -0.2480 -0.0042 285  SER A C   
1958 O  O   . SER A 286 ? 2.5500 1.8093 2.0732 -0.3154 -0.2483 -0.0105 285  SER A O   
1959 C  CB  . SER A 286 ? 2.8729 2.0245 2.4395 -0.3104 -0.2996 0.0590  285  SER A CB  
1960 O  OG  . SER A 286 ? 3.0389 2.1283 2.6487 -0.2960 -0.3269 0.0846  285  SER A OG  
1961 N  N   . GLU A 287 ? 2.1277 1.4579 1.6378 -0.2672 -0.2290 -0.0180 286  GLU A N   
1962 C  CA  . GLU A 287 ? 2.1003 1.4915 1.5870 -0.2747 -0.2081 -0.0430 286  GLU A CA  
1963 C  C   . GLU A 287 ? 2.1013 1.5072 1.6011 -0.2400 -0.1923 -0.0819 286  GLU A C   
1964 O  O   . GLU A 287 ? 2.0837 1.4847 1.5967 -0.2082 -0.1897 -0.0853 286  GLU A O   
1965 C  CB  . GLU A 287 ? 2.1248 1.5788 1.5777 -0.2842 -0.1983 -0.0276 286  GLU A CB  
1966 C  CG  . GLU A 287 ? 2.1348 1.6041 1.5642 -0.3300 -0.2010 -0.0049 286  GLU A CG  
1967 C  CD  . GLU A 287 ? 2.2409 1.6756 1.6546 -0.3512 -0.2197 0.0373  286  GLU A CD  
1968 O  OE1 . GLU A 287 ? 2.4233 1.8509 1.8343 -0.3301 -0.2255 0.0494  286  GLU A OE1 
1969 O  OE2 . GLU A 287 ? 2.1590 1.5743 1.5610 -0.3918 -0.2303 0.0602  286  GLU A OE2 
1970 N  N   . GLN A 288 ? 2.1431 1.5660 1.6380 -0.2489 -0.1830 -0.1103 287  GLN A N   
1971 C  CA  . GLN A 288 ? 2.1401 1.5778 1.6382 -0.2219 -0.1687 -0.1460 287  GLN A CA  
1972 C  C   . GLN A 288 ? 2.2132 1.7233 1.6897 -0.2114 -0.1558 -0.1527 287  GLN A C   
1973 O  O   . GLN A 288 ? 1.4021 0.9583 0.8645 -0.2310 -0.1544 -0.1429 287  GLN A O   
1974 C  CB  . GLN A 288 ? 2.0824 1.4939 1.5840 -0.2362 -0.1675 -0.1765 287  GLN A CB  
1975 C  CG  . GLN A 288 ? 2.1855 1.6332 1.6686 -0.2706 -0.1694 -0.1783 287  GLN A CG  
1976 C  CD  . GLN A 288 ? 2.4453 1.8691 1.9264 -0.2838 -0.1685 -0.2126 287  GLN A CD  
1977 O  OE1 . GLN A 288 ? 2.5273 1.8905 2.0237 -0.2747 -0.1679 -0.2317 287  GLN A OE1 
1978 N  NE2 . GLN A 288 ? 2.5856 2.0574 2.0500 -0.3061 -0.1686 -0.2218 287  GLN A NE2 
1979 N  N   . LEU A 289 ? 2.0707 1.5900 1.5491 -0.1800 -0.1462 -0.1687 288  LEU A N   
1980 C  CA  . LEU A 289 ? 2.0937 1.6730 1.5554 -0.1662 -0.1364 -0.1735 288  LEU A CA  
1981 C  C   . LEU A 289 ? 2.2030 1.8192 1.6524 -0.1796 -0.1338 -0.1936 288  LEU A C   
1982 O  O   . LEU A 289 ? 2.4912 2.0823 1.9396 -0.1890 -0.1346 -0.2159 288  LEU A O   
1983 C  CB  . LEU A 289 ? 2.0981 1.6716 1.5646 -0.1329 -0.1283 -0.1839 288  LEU A CB  
1984 C  CG  . LEU A 289 ? 2.0211 1.5687 1.5028 -0.1191 -0.1338 -0.1607 288  LEU A CG  
1985 C  CD1 . LEU A 289 ? 2.0829 1.6241 1.5770 -0.0882 -0.1256 -0.1718 288  LEU A CD1 
1986 C  CD2 . LEU A 289 ? 2.1041 1.6866 1.5692 -0.1263 -0.1365 -0.1355 288  LEU A CD2 
1987 N  N   . ALA A 290 ? 1.9421 1.6175 1.3844 -0.1810 -0.1313 -0.1866 289  ALA A N   
1988 C  CA  . ALA A 290 ? 1.7289 1.4468 1.1668 -0.1946 -0.1335 -0.2002 289  ALA A CA  
1989 C  C   . ALA A 290 ? 1.7618 1.4813 1.1871 -0.1761 -0.1309 -0.2218 289  ALA A C   
1990 O  O   . ALA A 290 ? 1.7603 1.4636 1.1827 -0.1507 -0.1241 -0.2234 289  ALA A O   
1991 C  CB  . ALA A 290 ? 1.5733 1.3565 1.0183 -0.1981 -0.1313 -0.1873 289  ALA A CB  
1992 N  N   . CYS A 291 ? 3.8833 2.5913 1.5898 0.1614  -0.2728 -0.2695 290  CYS A N   
1993 C  CA  . CYS A 291 ? 3.0748 1.8245 0.8900 0.1382  -0.2922 -0.2836 290  CYS A CA  
1994 C  C   . CYS A 291 ? 3.3987 2.1777 1.2585 0.1390  -0.3063 -0.3219 290  CYS A C   
1995 O  O   . CYS A 291 ? 3.0968 1.8736 0.9154 0.1486  -0.2747 -0.3334 290  CYS A O   
1996 C  CB  . CYS A 291 ? 3.0071 1.7667 0.8519 0.1083  -0.2419 -0.2638 290  CYS A CB  
1997 S  SG  . CYS A 291 ? 3.3611 2.1629 1.3298 0.0805  -0.2675 -0.2710 290  CYS A SG  
1998 N  N   . VAL A 292 ? 3.3054 2.1097 1.2468 0.1289  -0.3519 -0.3415 291  VAL A N   
1999 C  CA  . VAL A 292 ? 3.5921 2.4121 1.5780 0.1254  -0.3634 -0.3756 291  VAL A CA  
2000 C  C   . VAL A 292 ? 3.8089 2.6440 1.8188 0.1141  -0.3131 -0.3759 291  VAL A C   
2001 O  O   . VAL A 292 ? 4.0977 2.9492 2.1453 0.0943  -0.2905 -0.3570 291  VAL A O   
2002 C  CB  . VAL A 292 ? 3.5446 2.3882 1.6204 0.1072  -0.4156 -0.3926 291  VAL A CB  
2003 C  CG1 . VAL A 292 ? 3.4149 2.2822 1.5571 0.0838  -0.4144 -0.3710 291  VAL A CG1 
2004 C  CG2 . VAL A 292 ? 3.5004 2.3455 1.6181 0.0996  -0.4206 -0.4240 291  VAL A CG2 
2005 N  N   . ASP A 293 ? 3.7176 2.5494 1.7022 0.1292  -0.2953 -0.3987 292  ASP A N   
2006 C  CA  . ASP A 293 ? 3.5859 2.4410 1.5998 0.1251  -0.2535 -0.4055 292  ASP A CA  
2007 C  C   . ASP A 293 ? 3.4666 2.3159 1.5251 0.1296  -0.2800 -0.4376 292  ASP A C   
2008 O  O   . ASP A 293 ? 3.5870 2.4121 1.6079 0.1488  -0.2972 -0.4611 292  ASP A O   
2009 C  CB  . ASP A 293 ? 3.6801 2.5414 1.6219 0.1423  -0.1990 -0.4032 292  ASP A CB  
2010 C  CG  . ASP A 293 ? 3.6450 2.5102 1.5500 0.1280  -0.1593 -0.3682 292  ASP A CG  
2011 O  OD1 . ASP A 293 ? 3.5406 2.4077 1.4860 0.1050  -0.1670 -0.3474 292  ASP A OD1 
2012 O  OD2 . ASP A 293 ? 3.7218 2.5854 1.5557 0.1382  -0.1185 -0.3613 292  ASP A OD2 
2013 N  N   . THR A 294 ? 3.2539 2.1196 1.3886 0.1110  -0.2827 -0.4376 293  THR A N   
2014 C  CA  . THR A 294 ? 3.0727 1.9216 1.2533 0.1094  -0.3103 -0.4624 293  THR A CA  
2015 C  C   . THR A 294 ? 3.0362 1.8738 1.1823 0.1393  -0.2837 -0.4861 293  THR A C   
2016 O  O   . THR A 294 ? 2.9689 1.8352 1.0920 0.1535  -0.2368 -0.4813 293  THR A O   
2017 C  CB  . THR A 294 ? 2.8593 1.7274 1.1246 0.0820  -0.3156 -0.4514 293  THR A CB  
2018 O  OG1 . THR A 294 ? 2.6568 1.5380 0.9544 0.0577  -0.3428 -0.4325 293  THR A OG1 
2019 C  CG2 . THR A 294 ? 2.8536 1.6950 1.1596 0.0785  -0.3386 -0.4729 293  THR A CG2 
2020 N  N   . ASN A 295 ? 3.0839 1.8816 1.2266 0.1483  -0.3128 -0.5128 294  ASN A N   
2021 C  CA  . ASN A 295 ? 3.1695 1.9466 1.2684 0.1830  -0.2933 -0.5382 294  ASN A CA  
2022 C  C   . ASN A 295 ? 3.1731 1.9676 1.3048 0.1961  -0.2620 -0.5407 294  ASN A C   
2023 O  O   . ASN A 295 ? 3.1658 1.9522 1.3566 0.1788  -0.2766 -0.5366 294  ASN A O   
2024 C  CB  . ASN A 295 ? 3.3649 2.0842 1.4500 0.1859  -0.3349 -0.5663 294  ASN A CB  
2025 C  CG  . ASN A 295 ? 3.5778 2.2685 1.6008 0.2263  -0.3178 -0.5936 294  ASN A CG  
2026 O  OD1 . ASN A 295 ? 3.6574 2.3767 1.6318 0.2518  -0.2804 -0.5922 294  ASN A OD1 
2027 N  ND2 . ASN A 295 ? 3.6400 2.2727 1.6627 0.2312  -0.3433 -0.6188 294  ASN A ND2 
2028 N  N   . GLU A 296 ? 3.2623 2.0859 1.3549 0.2278  -0.2181 -0.5480 295  GLU A N   
2029 C  CA  . GLU A 296 ? 3.2315 2.0889 1.3518 0.2481  -0.1843 -0.5528 295  GLU A CA  
2030 C  C   . GLU A 296 ? 3.1353 1.9400 1.2780 0.2638  -0.2089 -0.5719 295  GLU A C   
2031 O  O   . GLU A 296 ? 3.0873 1.9007 1.2807 0.2582  -0.2078 -0.5647 295  GLU A O   
2032 C  CB  . GLU A 296 ? 3.3718 2.2750 1.4434 0.2831  -0.1350 -0.5641 295  GLU A CB  
2033 C  CG  . GLU A 296 ? 3.4632 2.4169 1.5084 0.2646  -0.1007 -0.5420 295  GLU A CG  
2034 C  CD  . GLU A 296 ? 3.3950 2.3908 1.4931 0.2304  -0.0866 -0.5150 295  GLU A CD  
2035 O  OE1 . GLU A 296 ? 3.4689 2.4938 1.6189 0.2346  -0.0768 -0.5185 295  GLU A OE1 
2036 O  OE2 . GLU A 296 ? 3.3202 2.3163 1.4042 0.2014  -0.0862 -0.4903 295  GLU A OE2 
2037 N  N   . VAL A 297 ? 3.1322 1.8769 1.2311 0.2837  -0.2302 -0.5959 296  VAL A N   
2038 C  CA  . VAL A 297 ? 3.1443 1.8211 1.2506 0.2982  -0.2531 -0.6137 296  VAL A CA  
2039 C  C   . VAL A 297 ? 3.2706 1.9159 1.4347 0.2528  -0.2894 -0.5991 296  VAL A C   
2040 O  O   . VAL A 297 ? 3.3827 1.9901 1.5724 0.2557  -0.2973 -0.6006 296  VAL A O   
2041 C  CB  . VAL A 297 ? 3.2732 1.8825 1.3166 0.3205  -0.2727 -0.6425 296  VAL A CB  
2042 C  CG1 . VAL A 297 ? 3.2801 1.8653 1.3120 0.2841  -0.3102 -0.6423 296  VAL A CG1 
2043 C  CG2 . VAL A 297 ? 3.2806 1.8107 1.3221 0.3386  -0.2904 -0.6596 296  VAL A CG2 
2044 N  N   . GLU A 298 ? 2.9993 1.6615 1.1817 0.2127  -0.3105 -0.5846 297  GLU A N   
2045 C  CA  . GLU A 298 ? 3.0953 1.7473 1.3402 0.1671  -0.3414 -0.5699 297  GLU A CA  
2046 C  C   . GLU A 298 ? 3.1934 1.8938 1.4933 0.1560  -0.3200 -0.5459 297  GLU A C   
2047 O  O   . GLU A 298 ? 3.1814 1.8603 1.5284 0.1346  -0.3349 -0.5387 297  GLU A O   
2048 C  CB  . GLU A 298 ? 2.9674 1.6358 1.2167 0.1350  -0.3698 -0.5632 297  GLU A CB  
2049 C  CG  . GLU A 298 ? 3.0333 1.6538 1.2368 0.1382  -0.3999 -0.5895 297  GLU A CG  
2050 C  CD  . GLU A 298 ? 3.1057 1.6563 1.3220 0.1258  -0.4257 -0.6089 297  GLU A CD  
2051 O  OE1 . GLU A 298 ? 3.1554 1.6565 1.3336 0.1586  -0.4127 -0.6259 297  GLU A OE1 
2052 O  OE2 . GLU A 298 ? 3.0677 1.6124 1.3301 0.0832  -0.4580 -0.6075 297  GLU A OE2 
2053 N  N   . THR A 299 ? 3.1850 1.9494 1.4760 0.1685  -0.2835 -0.5341 298  THR A N   
2054 C  CA  . THR A 299 ? 3.0908 1.9062 1.4298 0.1578  -0.2609 -0.5144 298  THR A CA  
2055 C  C   . THR A 299 ? 3.1735 1.9716 1.5298 0.1822  -0.2527 -0.5232 298  THR A C   
2056 O  O   . THR A 299 ? 3.2120 2.0059 1.6171 0.1611  -0.2633 -0.5105 298  THR A O   
2057 C  CB  . THR A 299 ? 3.1698 2.0560 1.4876 0.1694  -0.2153 -0.5054 298  THR A CB  
2058 O  OG1 . THR A 299 ? 3.2873 2.1831 1.5584 0.2145  -0.1863 -0.5268 298  THR A OG1 
2059 C  CG2 . THR A 299 ? 3.0483 1.9463 1.3420 0.1472  -0.2193 -0.4904 298  THR A CG2 
2060 N  N   . GLN A 300 ? 3.1499 1.9373 1.4629 0.2301  -0.2340 -0.5448 299  GLN A N   
2061 C  CA  . GLN A 300 ? 3.1657 1.9365 1.4849 0.2666  -0.2253 -0.5546 299  GLN A CA  
2062 C  C   . GLN A 300 ? 3.3104 1.9884 1.6403 0.2514  -0.2632 -0.5553 299  GLN A C   
2063 O  O   . GLN A 300 ? 3.3807 2.0445 1.7366 0.2566  -0.2639 -0.5481 299  GLN A O   
2064 C  CB  . GLN A 300 ? 3.1168 1.8943 1.3851 0.3256  -0.2003 -0.5795 299  GLN A CB  
2065 C  CG  . GLN A 300 ? 3.1911 1.9634 1.4638 0.3757  -0.1890 -0.5900 299  GLN A CG  
2066 C  CD  . GLN A 300 ? 3.1609 2.0328 1.4806 0.3834  -0.1577 -0.5794 299  GLN A CD  
2067 O  OE1 . GLN A 300 ? 3.1465 2.0266 1.5103 0.3482  -0.1679 -0.5599 299  GLN A OE1 
2068 N  NE2 . GLN A 300 ? 3.1982 2.1534 1.5114 0.4288  -0.1187 -0.5937 299  GLN A NE2 
2069 N  N   . LYS A 301 ? 3.2727 1.8885 1.5805 0.2309  -0.2936 -0.5641 300  LYS A N   
2070 C  CA  . LYS A 301 ? 3.3945 1.9212 1.7098 0.2088  -0.3264 -0.5660 300  LYS A CA  
2071 C  C   . LYS A 301 ? 3.4360 1.9775 1.8179 0.1555  -0.3418 -0.5414 300  LYS A C   
2072 O  O   . LYS A 301 ? 3.5859 2.0695 1.9833 0.1417  -0.3549 -0.5359 300  LYS A O   
2073 C  CB  . LYS A 301 ? 3.4983 1.9689 1.7784 0.1943  -0.3543 -0.5844 300  LYS A CB  
2074 C  CG  . LYS A 301 ? 3.6463 2.0176 1.9223 0.1744  -0.3825 -0.5917 300  LYS A CG  
2075 C  CD  . LYS A 301 ? 3.7883 2.0988 2.0327 0.2215  -0.3683 -0.5965 300  LYS A CD  
2076 C  CE  . LYS A 301 ? 3.9161 2.2155 2.0942 0.2850  -0.3509 -0.6210 300  LYS A CE  
2077 N  NZ  . LYS A 301 ? 3.9243 2.1851 2.0757 0.3424  -0.3344 -0.6245 300  LYS A NZ  
2078 N  N   . PHE A 302 ? 3.4535 2.0690 1.8708 0.1261  -0.3389 -0.5256 301  PHE A N   
2079 C  CA  . PHE A 302 ? 3.1619 1.8054 1.6451 0.0800  -0.3496 -0.5020 301  PHE A CA  
2080 C  C   . PHE A 302 ? 2.8681 1.5368 1.3723 0.0970  -0.3258 -0.4901 301  PHE A C   
2081 O  O   . PHE A 302 ? 2.6893 1.3345 1.2290 0.0741  -0.3359 -0.4774 301  PHE A O   
2082 C  CB  . PHE A 302 ? 3.0582 1.7703 1.5653 0.0524  -0.3524 -0.4888 301  PHE A CB  
2083 C  CG  . PHE A 302 ? 2.9518 1.6909 1.5276 0.0038  -0.3698 -0.4678 301  PHE A CG  
2084 C  CD1 . PHE A 302 ? 2.7295 1.5120 1.3451 -0.0047 -0.3524 -0.4480 301  PHE A CD1 
2085 C  CD2 . PHE A 302 ? 2.9605 1.6887 1.5627 -0.0330 -0.4034 -0.4701 301  PHE A CD2 
2086 C  CE1 . PHE A 302 ? 2.6199 1.4295 1.2987 -0.0477 -0.3676 -0.4294 301  PHE A CE1 
2087 C  CE2 . PHE A 302 ? 2.8686 1.6324 1.5382 -0.0753 -0.4177 -0.4525 301  PHE A CE2 
2088 C  CZ  . PHE A 302 ? 2.7024 1.5048 1.4097 -0.0819 -0.3994 -0.4312 301  PHE A CZ  
2089 N  N   . VAL A 303 ? 2.8920 1.6137 1.3734 0.1368  -0.2930 -0.4953 302  VAL A N   
2090 C  CA  . VAL A 303 ? 2.9366 1.7153 1.4565 0.1598  -0.2644 -0.4824 302  VAL A CA  
2091 C  C   . VAL A 303 ? 3.0808 1.7868 1.5816 0.1919  -0.2719 -0.4903 302  VAL A C   
2092 O  O   . VAL A 303 ? 3.0530 1.7736 1.6064 0.1826  -0.2699 -0.4681 302  VAL A O   
2093 C  CB  . VAL A 303 ? 2.8982 1.7637 1.4070 0.1974  -0.2236 -0.4889 302  VAL A CB  
2094 C  CG1 . VAL A 303 ? 2.7913 1.7314 1.3533 0.2256  -0.1956 -0.4782 302  VAL A CG1 
2095 C  CG2 . VAL A 303 ? 2.8964 1.8294 1.4234 0.1629  -0.2103 -0.4739 302  VAL A CG2 
2096 N  N   . ASP A 304 ? 3.1451 1.7714 1.5701 0.2307  -0.2796 -0.5193 303  ASP A N   
2097 C  CA  . ASP A 304 ? 3.2761 1.8160 1.6688 0.2675  -0.2868 -0.5270 303  ASP A CA  
2098 C  C   . ASP A 304 ? 3.4835 1.9408 1.8956 0.2194  -0.3151 -0.5109 303  ASP A C   
2099 O  O   . ASP A 304 ? 3.4547 1.8632 1.8616 0.2362  -0.3154 -0.5022 303  ASP A O   
2100 C  CB  . ASP A 304 ? 3.4840 1.9663 1.8142 0.3076  -0.2890 -0.5517 303  ASP A CB  
2101 C  CG  . ASP A 304 ? 3.3577 1.9202 1.6666 0.3649  -0.2556 -0.5686 303  ASP A CG  
2102 O  OD1 . ASP A 304 ? 3.2441 1.9130 1.5876 0.3596  -0.2311 -0.5612 303  ASP A OD1 
2103 O  OD2 . ASP A 304 ? 3.0193 1.5407 1.2772 0.4133  -0.2524 -0.5893 303  ASP A OD2 
2104 N  N   . SER A 305 ? 3.6125 2.0622 2.0499 0.1604  -0.3370 -0.5055 304  SER A N   
2105 C  CA  . SER A 305 ? 3.6853 2.0724 2.1497 0.1070  -0.3610 -0.4916 304  SER A CA  
2106 C  C   . SER A 305 ? 3.4391 1.8594 1.9543 0.0825  -0.3556 -0.4666 304  SER A C   
2107 O  O   . SER A 305 ? 3.4828 1.8379 1.9973 0.0750  -0.3593 -0.4537 304  SER A O   
2108 C  CB  . SER A 305 ? 3.8595 2.2636 2.3518 0.0526  -0.3839 -0.4944 304  SER A CB  
2109 O  OG  . SER A 305 ? 4.0285 2.3820 2.5504 -0.0006 -0.4043 -0.4848 304  SER A OG  
2110 N  N   . LEU A 306 ? 3.3083 1.8504 1.8869 0.0691  -0.3399 -0.4492 305  LEU A N   
2111 C  CA  . LEU A 306 ? 2.8560 1.4725 1.5166 0.0452  -0.3265 -0.4142 305  LEU A CA  
2112 C  C   . LEU A 306 ? 2.7622 1.3994 1.4273 0.0946  -0.3024 -0.4026 305  LEU A C   
2113 O  O   . LEU A 306 ? 2.4675 1.0965 1.1639 0.0831  -0.3009 -0.3794 305  LEU A O   
2114 C  CB  . LEU A 306 ? 2.7306 1.4637 1.4503 0.0208  -0.3156 -0.4008 305  LEU A CB  
2115 C  CG  . LEU A 306 ? 2.5324 1.3453 1.2431 0.0539  -0.2892 -0.4077 305  LEU A CG  
2116 C  CD1 . LEU A 306 ? 2.3995 1.2962 1.1518 0.0832  -0.2565 -0.3929 305  LEU A CD1 
2117 C  CD2 . LEU A 306 ? 2.4102 1.2798 1.1459 0.0184  -0.2924 -0.4006 305  LEU A CD2 
2118 N  N   . VAL A 307 ? 2.9275 1.5931 1.5581 0.1518  -0.2842 -0.4203 306  VAL A N   
2119 C  CA  . VAL A 307 ? 2.9922 1.6910 1.6254 0.2081  -0.2637 -0.4156 306  VAL A CA  
2120 C  C   . VAL A 307 ? 3.2954 1.8708 1.8770 0.2330  -0.2779 -0.4143 306  VAL A C   
2121 O  O   . VAL A 307 ? 3.3827 1.9756 1.9859 0.2540  -0.2696 -0.3944 306  VAL A O   
2122 C  CB  . VAL A 307 ? 2.6689 1.4210 1.2694 0.2665  -0.2421 -0.4416 306  VAL A CB  
2123 C  CG1 . VAL A 307 ? 2.6635 1.4296 1.2509 0.3362  -0.2286 -0.4455 306  VAL A CG1 
2124 C  CG2 . VAL A 307 ? 2.4258 1.3110 1.0821 0.2443  -0.2183 -0.4355 306  VAL A CG2 
2125 N  N   . ALA A 308 ? 3.5545 1.9996 2.0624 0.2300  -0.2997 -0.4357 307  ALA A N   
2126 C  CA  . ALA A 308 ? 3.8660 2.1685 2.3087 0.2510  -0.3128 -0.4362 307  ALA A CA  
2127 C  C   . ALA A 308 ? 3.9542 2.2262 2.4351 0.2004  -0.3188 -0.4019 307  ALA A C   
2128 O  O   . ALA A 308 ? 4.0368 2.2478 2.4898 0.2301  -0.3156 -0.3862 307  ALA A O   
2129 C  CB  . ALA A 308 ? 4.0703 2.2373 2.4287 0.2439  -0.3360 -0.4685 307  ALA A CB  
2130 N  N   . LEU A 309 ? 3.9631 2.2775 2.5036 0.1271  -0.3271 -0.3905 308  LEU A N   
2131 C  CA  . LEU A 309 ? 3.9307 2.2338 2.5157 0.0734  -0.3296 -0.3590 308  LEU A CA  
2132 C  C   . LEU A 309 ? 3.7382 2.1529 2.3864 0.0921  -0.3073 -0.3292 308  LEU A C   
2133 O  O   . LEU A 309 ? 3.7557 2.1536 2.4242 0.0696  -0.3042 -0.3010 308  LEU A O   
2134 C  CB  . LEU A 309 ? 3.9232 2.2586 2.5598 -0.0043 -0.3450 -0.3592 308  LEU A CB  
2135 C  CG  . LEU A 309 ? 3.9310 2.2301 2.6003 -0.0675 -0.3505 -0.3346 308  LEU A CG  
2136 C  CD1 . LEU A 309 ? 4.0473 2.1776 2.6343 -0.0709 -0.3607 -0.3403 308  LEU A CD1 
2137 C  CD2 . LEU A 309 ? 3.8862 2.2417 2.6150 -0.1366 -0.3664 -0.3392 308  LEU A CD2 
2138 N  N   . ALA A 310 ? 3.3957 1.9253 2.0726 0.1311  -0.2909 -0.3367 309  ALA A N   
2139 C  CA  . ALA A 310 ? 3.0314 1.6804 1.7719 0.1463  -0.2707 -0.3149 309  ALA A CA  
2140 C  C   . ALA A 310 ? 2.9309 1.5505 1.6356 0.2098  -0.2639 -0.3068 309  ALA A C   
2141 O  O   . ALA A 310 ? 3.0181 1.6643 1.7533 0.2048  -0.2584 -0.2799 309  ALA A O   
2142 C  CB  . ALA A 310 ? 2.9582 1.7358 1.7386 0.1602  -0.2540 -0.3283 309  ALA A CB  
2143 N  N   . MET A 311 ? 2.8480 1.4117 1.4837 0.2734  -0.2653 -0.3306 310  MET A N   
2144 C  CA  . MET A 311 ? 3.2114 1.7397 1.8021 0.3460  -0.2623 -0.3261 310  MET A CA  
2145 C  C   . MET A 311 ? 3.3857 1.7775 1.9292 0.3323  -0.2736 -0.2997 310  MET A C   
2146 O  O   . MET A 311 ? 3.3815 1.7580 1.8998 0.3833  -0.2706 -0.2840 310  MET A O   
2147 C  CB  . MET A 311 ? 3.3993 1.8783 1.9163 0.4173  -0.2635 -0.3604 310  MET A CB  
2148 C  CG  . MET A 311 ? 3.3192 1.9410 1.8771 0.4404  -0.2457 -0.3852 310  MET A CG  
2149 S  SD  . MET A 311 ? 3.2966 2.1122 1.9430 0.4697  -0.2227 -0.3735 310  MET A SD  
2150 C  CE  . MET A 311 ? 2.5146 1.4633 1.1902 0.4842  -0.1993 -0.4067 310  MET A CE  
2151 N  N   . ASP A 312 ? 3.4077 1.7022 1.9369 0.2638  -0.2863 -0.2952 311  ASP A N   
2152 C  CA  . ASP A 312 ? 3.4616 1.6271 1.9489 0.2358  -0.2926 -0.2687 311  ASP A CA  
2153 C  C   . ASP A 312 ? 3.3021 1.5388 1.8692 0.1651  -0.2860 -0.2372 311  ASP A C   
2154 O  O   . ASP A 312 ? 3.2047 1.5548 1.8506 0.1207  -0.2836 -0.2409 311  ASP A O   
2155 C  CB  . ASP A 312 ? 3.6662 1.6663 2.0797 0.2025  -0.3098 -0.2862 311  ASP A CB  
2156 C  CG  . ASP A 312 ? 3.8994 1.7238 2.2204 0.2168  -0.3132 -0.2686 311  ASP A CG  
2157 O  OD1 . ASP A 312 ? 3.8806 1.7110 2.2138 0.2128  -0.3032 -0.2328 311  ASP A OD1 
2158 O  OD2 . ASP A 312 ? 4.0498 1.7237 2.2792 0.2329  -0.3253 -0.2905 311  ASP A OD2 
2159 N  N   . ASN A 323 ? 3.1084 1.9749 1.8851 0.3410  -0.2280 -0.2855 322  ASN A N   
2160 C  CA  . ASN A 323 ? 3.1819 2.0760 1.9445 0.4085  -0.2260 -0.2788 322  ASN A CA  
2161 C  C   . ASN A 323 ? 3.4152 2.4668 2.2232 0.4553  -0.2101 -0.3021 322  ASN A C   
2162 O  O   . ASN A 323 ? 3.3819 2.4977 2.2151 0.4408  -0.1985 -0.3242 322  ASN A O   
2163 C  CB  . ASN A 323 ? 2.8922 1.8018 1.6878 0.3787  -0.2267 -0.2441 322  ASN A CB  
2164 C  CG  . ASN A 323 ? 2.8283 1.5782 1.5690 0.3428  -0.2389 -0.2198 322  ASN A CG  
2165 O  OD1 . ASN A 323 ? 3.0021 1.6492 1.6723 0.3851  -0.2460 -0.2066 322  ASN A OD1 
2166 N  ND2 . ASN A 323 ? 2.5684 1.2968 1.3393 0.2645  -0.2409 -0.2141 322  ASN A ND2 
2167 N  N   . VAL A 324 ? 3.6354 2.7504 2.4515 0.5109  -0.2093 -0.2976 323  VAL A N   
2168 C  CA  . VAL A 324 ? 3.5230 2.8054 2.3922 0.5528  -0.1944 -0.3213 323  VAL A CA  
2169 C  C   . VAL A 324 ? 3.3018 2.7188 2.2654 0.4833  -0.1776 -0.3193 323  VAL A C   
2170 O  O   . VAL A 324 ? 3.3557 2.9019 2.3668 0.4880  -0.1592 -0.3429 323  VAL A O   
2171 C  CB  . VAL A 324 ? 3.5259 2.8519 2.3848 0.6278  -0.2023 -0.3169 323  VAL A CB  
2172 C  CG1 . VAL A 324 ? 3.4470 2.7876 2.3376 0.5912  -0.2077 -0.2840 323  VAL A CG1 
2173 C  CG2 . VAL A 324 ? 3.4756 2.9798 2.3879 0.6768  -0.1883 -0.3491 323  VAL A CG2 
2174 N  N   . VAL A 325 ? 3.0710 2.4537 2.0582 0.4184  -0.1822 -0.2917 324  VAL A N   
2175 C  CA  . VAL A 325 ? 2.6970 2.1800 1.7622 0.3511  -0.1683 -0.2880 324  VAL A CA  
2176 C  C   . VAL A 325 ? 2.6215 2.0983 1.6885 0.3141  -0.1583 -0.3039 324  VAL A C   
2177 O  O   . VAL A 325 ? 2.4685 2.0497 1.5880 0.2841  -0.1397 -0.3140 324  VAL A O   
2178 C  CB  . VAL A 325 ? 2.5107 1.9482 1.5935 0.2958  -0.1764 -0.2556 324  VAL A CB  
2179 C  CG1 . VAL A 325 ? 2.4406 1.9188 1.5325 0.3272  -0.1811 -0.2406 324  VAL A CG1 
2180 C  CG2 . VAL A 325 ? 2.5107 1.7874 1.5334 0.2744  -0.1918 -0.2410 324  VAL A CG2 
2181 N  N   . PHE A 326 ? 2.7296 2.0770 1.7331 0.3147  -0.1711 -0.3058 325  PHE A N   
2182 C  CA  . PHE A 326 ? 2.6816 2.0099 1.6711 0.2885  -0.1659 -0.3223 325  PHE A CA  
2183 C  C   . PHE A 326 ? 2.6839 2.0713 1.6555 0.3419  -0.1502 -0.3536 325  PHE A C   
2184 O  O   . PHE A 326 ? 2.5767 2.0161 1.5614 0.3201  -0.1336 -0.3678 325  PHE A O   
2185 C  CB  . PHE A 326 ? 2.7670 1.9411 1.6947 0.2697  -0.1876 -0.3178 325  PHE A CB  
2186 C  CG  . PHE A 326 ? 2.7714 1.9205 1.6751 0.2489  -0.1868 -0.3367 325  PHE A CG  
2187 C  CD1 . PHE A 326 ? 2.5866 1.7856 1.5332 0.1912  -0.1807 -0.3309 325  PHE A CD1 
2188 C  CD2 . PHE A 326 ? 2.9888 2.0594 1.8200 0.2906  -0.1931 -0.3607 325  PHE A CD2 
2189 C  CE1 . PHE A 326 ? 2.6615 1.8355 1.5780 0.1761  -0.1814 -0.3468 325  PHE A CE1 
2190 C  CE2 . PHE A 326 ? 3.0785 2.1270 1.8817 0.2733  -0.1932 -0.3788 325  PHE A CE2 
2191 C  CZ  . PHE A 326 ? 2.9596 2.0607 1.8047 0.2160  -0.1878 -0.3709 325  PHE A CZ  
2192 N  N   . SER A 327 ? 2.7886 2.1656 1.7256 0.4142  -0.1547 -0.3641 326  SER A N   
2193 C  CA  . SER A 327 ? 2.9780 2.4337 1.9067 0.4742  -0.1382 -0.3957 326  SER A CA  
2194 C  C   . SER A 327 ? 2.9789 2.6141 1.9920 0.4549  -0.1115 -0.4039 326  SER A C   
2195 O  O   . SER A 327 ? 2.9589 2.6740 1.9822 0.4625  -0.0883 -0.4280 326  SER A O   
2196 C  CB  . SER A 327 ? 3.0773 2.4976 1.9585 0.5615  -0.1507 -0.4031 326  SER A CB  
2197 O  OG  . SER A 327 ? 2.9989 2.5357 1.8929 0.6227  -0.1330 -0.4344 326  SER A OG  
2198 N  N   . GLU A 328 ? 3.0338 2.7292 2.1040 0.4273  -0.1137 -0.3846 327  GLU A N   
2199 C  CA  . GLU A 328 ? 2.8762 2.7296 2.0272 0.3949  -0.0901 -0.3915 327  GLU A CA  
2200 C  C   . GLU A 328 ? 2.6967 2.5526 1.8631 0.3244  -0.0726 -0.3895 327  GLU A C   
2201 O  O   . GLU A 328 ? 2.6139 2.5743 1.8133 0.3098  -0.0446 -0.4071 327  GLU A O   
2202 C  CB  . GLU A 328 ? 2.8931 2.7900 2.0923 0.3761  -0.0996 -0.3709 327  GLU A CB  
2203 C  CG  . GLU A 328 ? 2.8986 2.8382 2.0940 0.4490  -0.1125 -0.3760 327  GLU A CG  
2204 C  CD  . GLU A 328 ? 2.7866 2.7936 2.0334 0.4287  -0.1187 -0.3601 327  GLU A CD  
2205 O  OE1 . GLU A 328 ? 2.6724 2.6588 1.9458 0.3602  -0.1169 -0.3404 327  GLU A OE1 
2206 O  OE2 . GLU A 328 ? 2.8093 2.8917 2.0672 0.4850  -0.1266 -0.3689 327  GLU A OE2 
2207 N  N   . PHE A 329 ? 2.6063 2.3454 1.7450 0.2819  -0.0887 -0.3684 328  PHE A N   
2208 C  CA  . PHE A 329 ? 2.4399 2.1669 1.5842 0.2204  -0.0780 -0.3635 328  PHE A CA  
2209 C  C   . PHE A 329 ? 2.4458 2.1670 1.5470 0.2350  -0.0620 -0.3861 328  PHE A C   
2210 O  O   . PHE A 329 ? 2.3706 2.1513 1.4893 0.2003  -0.0371 -0.3909 328  PHE A O   
2211 C  CB  . PHE A 329 ? 2.3305 1.9380 1.4526 0.1820  -0.1032 -0.3400 328  PHE A CB  
2212 C  CG  . PHE A 329 ? 2.2780 1.8823 1.4129 0.1218  -0.0966 -0.3315 328  PHE A CG  
2213 C  CD1 . PHE A 329 ? 2.2207 1.9236 1.3996 0.0918  -0.0699 -0.3337 328  PHE A CD1 
2214 C  CD2 . PHE A 329 ? 2.3250 1.8262 1.4245 0.0960  -0.1176 -0.3227 328  PHE A CD2 
2215 C  CE1 . PHE A 329 ? 2.1176 1.8042 1.2970 0.0419  -0.0641 -0.3241 328  PHE A CE1 
2216 C  CE2 . PHE A 329 ? 2.2912 1.7903 1.3978 0.0490  -0.1144 -0.3151 328  PHE A CE2 
2217 C  CZ  . PHE A 329 ? 2.1292 1.7154 1.2716 0.0245  -0.0875 -0.3143 328  PHE A CZ  
2218 N  N   . GLN A 330 ? 2.5417 2.1837 1.5798 0.2859  -0.0753 -0.3995 329  GLN A N   
2219 C  CA  . GLN A 330 ? 2.7188 2.3520 1.7074 0.3084  -0.0608 -0.4238 329  GLN A CA  
2220 C  C   . GLN A 330 ? 2.8323 2.6152 1.8604 0.3261  -0.0241 -0.4449 329  GLN A C   
2221 O  O   . GLN A 330 ? 2.8377 2.6621 1.8614 0.2999  0.0026  -0.4534 329  GLN A O   
2222 C  CB  . GLN A 330 ? 2.8414 2.3683 1.7553 0.3697  -0.0815 -0.4387 329  GLN A CB  
2223 C  CG  . GLN A 330 ? 2.7550 2.1252 1.6187 0.3468  -0.1150 -0.4249 329  GLN A CG  
2224 C  CD  . GLN A 330 ? 2.8184 2.0775 1.6076 0.4079  -0.1346 -0.4394 329  GLN A CD  
2225 O  OE1 . GLN A 330 ? 2.7097 1.9995 1.4954 0.4696  -0.1315 -0.4482 329  GLN A OE1 
2226 N  NE2 . GLN A 330 ? 3.0431 2.1726 1.7684 0.3935  -0.1554 -0.4447 329  GLN A NE2 
2227 N  N   . ASP A 331 ? 2.9819 2.8468 2.0466 0.3706  -0.0228 -0.4533 330  ASP A N   
2228 C  CA  . ASP A 331 ? 2.8924 2.9198 2.0078 0.3884  0.0099  -0.4767 330  ASP A CA  
2229 C  C   . ASP A 331 ? 2.7465 2.8646 1.9272 0.3130  0.0345  -0.4666 330  ASP A C   
2230 O  O   . ASP A 331 ? 2.6985 2.9152 1.9011 0.2947  0.0705  -0.4831 330  ASP A O   
2231 C  CB  . ASP A 331 ? 2.9243 3.0209 2.0682 0.4526  -0.0016 -0.4865 330  ASP A CB  
2232 C  CG  . ASP A 331 ? 3.0225 3.0153 2.0919 0.5324  -0.0257 -0.4956 330  ASP A CG  
2233 O  OD1 . ASP A 331 ? 3.0625 2.9696 2.0658 0.5467  -0.0245 -0.5067 330  ASP A OD1 
2234 O  OD2 . ASP A 331 ? 3.0332 3.0242 2.1040 0.5824  -0.0463 -0.4919 330  ASP A OD2 
2235 N  N   . TRP A 332 ? 2.6517 2.7315 1.8593 0.2689  0.0165  -0.4398 331  TRP A N   
2236 C  CA  . TRP A 332 ? 2.4661 2.6163 1.7312 0.2000  0.0357  -0.4296 331  TRP A CA  
2237 C  C   . TRP A 332 ? 2.2854 2.4062 1.5240 0.1480  0.0591  -0.4255 331  TRP A C   
2238 O  O   . TRP A 332 ? 2.1343 2.3460 1.4063 0.1099  0.0933  -0.4331 331  TRP A O   
2239 C  CB  . TRP A 332 ? 2.4059 2.4987 1.6914 0.1694  0.0087  -0.4013 331  TRP A CB  
2240 C  CG  . TRP A 332 ? 2.3981 2.5570 1.7395 0.1055  0.0256  -0.3928 331  TRP A CG  
2241 C  CD1 . TRP A 332 ? 2.4394 2.7157 1.8460 0.0966  0.0349  -0.4013 331  TRP A CD1 
2242 C  CD2 . TRP A 332 ? 2.3383 2.4477 1.6698 0.0436  0.0352  -0.3769 331  TRP A CD2 
2243 N  NE1 . TRP A 332 ? 2.4545 2.7484 1.8908 0.0295  0.0503  -0.3919 331  TRP A NE1 
2244 C  CE2 . TRP A 332 ? 2.3570 2.5458 1.7455 -0.0018 0.0512  -0.3755 331  TRP A CE2 
2245 C  CE3 . TRP A 332 ? 2.3005 2.3027 1.5761 0.0244  0.0297  -0.3647 331  TRP A CE3 
2246 C  CZ2 . TRP A 332 ? 2.2831 2.4398 1.6705 -0.0622 0.0634  -0.3611 331  TRP A CZ2 
2247 C  CZ3 . TRP A 332 ? 2.2629 2.2413 1.5395 -0.0322 0.0400  -0.3496 331  TRP A CZ3 
2248 C  CH2 . TRP A 332 ? 2.2223 2.2724 1.5520 -0.0738 0.0574  -0.3471 331  TRP A CH2 
2249 N  N   . LEU A 333 ? 2.2582 2.2499 1.4327 0.1463  0.0405  -0.4142 332  LEU A N   
2250 C  CA  . LEU A 333 ? 2.1981 2.1449 1.3366 0.1011  0.0556  -0.4063 332  LEU A CA  
2251 C  C   . LEU A 333 ? 2.2716 2.2825 1.3859 0.1142  0.0941  -0.4296 332  LEU A C   
2252 O  O   . LEU A 333 ? 2.2414 2.2862 1.3559 0.0685  0.1260  -0.4262 332  LEU A O   
2253 C  CB  . LEU A 333 ? 2.1808 1.9829 1.2576 0.1027  0.0210  -0.3932 332  LEU A CB  
2254 C  CG  . LEU A 333 ? 2.1144 1.8411 1.1440 0.0625  0.0200  -0.3805 332  LEU A CG  
2255 C  CD1 . LEU A 333 ? 1.9578 1.5790 0.9742 0.0495  -0.0220 -0.3624 332  LEU A CD1 
2256 C  CD2 . LEU A 333 ? 2.2559 1.9549 1.2134 0.0830  0.0349  -0.3975 332  LEU A CD2 
2257 N  N   . GLU A 334 ? 2.3543 2.3798 1.4443 0.1775  0.0928  -0.4531 333  GLU A N   
2258 C  CA  . GLU A 334 ? 2.4086 2.5030 1.4756 0.1978  0.1305  -0.4784 333  GLU A CA  
2259 C  C   . GLU A 334 ? 2.4825 2.7345 1.6212 0.1662  0.1729  -0.4887 333  GLU A C   
2260 O  O   . GLU A 334 ? 2.5834 2.8804 1.7080 0.1363  0.2136  -0.4953 333  GLU A O   
2261 C  CB  . GLU A 334 ? 2.4293 2.5187 1.4638 0.2802  0.1192  -0.5043 333  GLU A CB  
2262 C  CG  . GLU A 334 ? 2.5553 2.4968 1.4960 0.3067  0.0945  -0.5059 333  GLU A CG  
2263 C  CD  . GLU A 334 ? 2.6592 2.5867 1.5416 0.2870  0.1232  -0.5127 333  GLU A CD  
2264 O  OE1 . GLU A 334 ? 2.6158 2.5077 1.4894 0.2264  0.1283  -0.4907 333  GLU A OE1 
2265 O  OE2 . GLU A 334 ? 2.7348 2.6831 1.5744 0.3358  0.1405  -0.5398 333  GLU A OE2 
2266 N  N   . LYS A 335 ? 2.4877 2.8225 1.6994 0.1719  0.1639  -0.4912 334  LYS A N   
2267 C  CA  . LYS A 335 ? 2.4905 2.9791 1.7787 0.1362  0.1986  -0.5038 334  LYS A CA  
2268 C  C   . LYS A 335 ? 2.4992 2.9618 1.7915 0.0501  0.2192  -0.4821 334  LYS A C   
2269 O  O   . LYS A 335 ? 2.5519 3.0951 1.8605 0.0078  0.2636  -0.4917 334  LYS A O   
2270 C  CB  . LYS A 335 ? 2.4537 3.0210 1.8120 0.1611  0.1757  -0.5094 334  LYS A CB  
2271 C  CG  . LYS A 335 ? 2.4537 3.0375 1.8008 0.2528  0.1532  -0.5285 334  LYS A CG  
2272 C  CD  . LYS A 335 ? 2.3299 2.9833 1.7372 0.2780  0.1284  -0.5301 334  LYS A CD  
2273 C  CE  . LYS A 335 ? 2.2313 3.0813 1.7251 0.2607  0.1581  -0.5572 334  LYS A CE  
2274 N  NZ  . LYS A 335 ? 2.2965 3.2614 1.7967 0.3127  0.1844  -0.5935 334  LYS A NZ  
2275 N  N   . HIS A 336 ? 2.5034 2.8528 1.7794 0.0247  0.1879  -0.4532 335  HIS A N   
2276 C  CA  . HIS A 336 ? 2.5166 2.8382 1.7991 -0.0496 0.2020  -0.4323 335  HIS A CA  
2277 C  C   . HIS A 336 ? 2.6903 2.9080 1.8935 -0.0770 0.2148  -0.4163 335  HIS A C   
2278 O  O   . HIS A 336 ? 2.6799 2.8516 1.8731 -0.1317 0.2231  -0.3961 335  HIS A O   
2279 C  CB  . HIS A 336 ? 2.4323 2.6965 1.7411 -0.0624 0.1639  -0.4104 335  HIS A CB  
2280 C  CG  . HIS A 336 ? 2.3799 2.7509 1.7664 -0.0544 0.1575  -0.4221 335  HIS A CG  
2281 N  ND1 . HIS A 336 ? 2.4554 2.8875 1.8636 0.0089  0.1426  -0.4405 335  HIS A ND1 
2282 C  CD2 . HIS A 336 ? 2.2788 2.7029 1.7205 -0.0992 0.1625  -0.4191 335  HIS A CD2 
2283 C  CE1 . HIS A 336 ? 2.3940 2.9177 1.8684 0.0040  0.1372  -0.4476 335  HIS A CE1 
2284 N  NE2 . HIS A 336 ? 2.3004 2.8223 1.7975 -0.0632 0.1493  -0.4360 335  HIS A NE2 
2285 N  N   . GLY A 337 ? 2.8660 3.0452 2.0077 -0.0363 0.2160  -0.4262 336  GLY A N   
2286 C  CA  . GLY A 337 ? 3.0065 3.0822 2.0637 -0.0532 0.2218  -0.4120 336  GLY A CA  
2287 C  C   . GLY A 337 ? 3.1138 3.2209 2.1549 -0.1106 0.2722  -0.4064 336  GLY A C   
2288 O  O   . GLY A 337 ? 3.2550 3.4831 2.3421 -0.1282 0.3129  -0.4241 336  GLY A O   
2289 N  N   . ASP A 338 ? 2.8932 2.8914 1.8650 -0.1393 0.2705  -0.3825 337  ASP A N   
2290 C  CA  . ASP A 338 ? 2.6799 2.5505 1.6000 -0.1167 0.2218  -0.3668 337  ASP A CA  
2291 C  C   . ASP A 338 ? 2.4876 2.2800 1.3960 -0.1618 0.2088  -0.3369 337  ASP A C   
2292 O  O   . ASP A 338 ? 2.3888 2.1905 1.2890 -0.2094 0.2442  -0.3258 337  ASP A O   
2293 C  CB  . ASP A 338 ? 2.9346 2.7449 1.7617 -0.0864 0.2254  -0.3737 337  ASP A CB  
2294 C  CG  . ASP A 338 ? 2.9584 2.8491 1.7902 -0.0401 0.2452  -0.4054 337  ASP A CG  
2295 O  OD1 . ASP A 338 ? 2.9348 2.9150 1.7735 -0.0561 0.2964  -0.4171 337  ASP A OD1 
2296 O  OD2 . ASP A 338 ? 2.8998 2.7636 1.7273 0.0123  0.2107  -0.4195 337  ASP A OD2 
2297 N  N   . TYR A 339 ? 2.4751 2.1885 1.3798 -0.1466 0.1593  -0.3248 338  TYR A N   
2298 C  CA  . TYR A 339 ? 2.4783 2.1236 1.3761 -0.1801 0.1426  -0.2988 338  TYR A CA  
2299 C  C   . TYR A 339 ? 2.5212 2.0583 1.3307 -0.1713 0.1215  -0.2856 338  TYR A C   
2300 O  O   . TYR A 339 ? 2.6314 2.1248 1.4104 -0.1354 0.0887  -0.2943 338  TYR A O   
2301 C  CB  . TYR A 339 ? 2.4675 2.1141 1.4330 -0.1753 0.1033  -0.2934 338  TYR A CB  
2302 C  CG  . TYR A 339 ? 2.4817 2.2293 1.5321 -0.1849 0.1179  -0.3033 338  TYR A CG  
2303 C  CD1 . TYR A 339 ? 2.5066 2.3275 1.5909 -0.1497 0.1205  -0.3255 338  TYR A CD1 
2304 C  CD2 . TYR A 339 ? 2.4022 2.1698 1.4949 -0.2254 0.1267  -0.2921 338  TYR A CD2 
2305 C  CE1 . TYR A 339 ? 2.4650 2.3838 1.6247 -0.1541 0.1300  -0.3357 338  TYR A CE1 
2306 C  CE2 . TYR A 339 ? 2.3837 2.2461 1.5513 -0.2341 0.1370  -0.3038 338  TYR A CE2 
2307 C  CZ  . TYR A 339 ? 2.4485 2.3901 1.6505 -0.1981 0.1377  -0.3254 338  TYR A CZ  
2308 O  OH  . TYR A 339 ? 2.4662 2.5085 1.7411 -0.2023 0.1445  -0.3383 338  TYR A OH  
2309 N  N   . GLU A 340 ? 2.3524 1.8440 1.1173 -0.2042 0.1400  -0.2656 339  GLU A N   
2310 C  CA  . GLU A 340 ? 2.3786 1.7689 1.0540 -0.1957 0.1205  -0.2504 339  GLU A CA  
2311 C  C   . GLU A 340 ? 2.2989 1.6347 0.9905 -0.1819 0.0635  -0.2414 339  GLU A C   
2312 O  O   . GLU A 340 ? 2.3302 1.6007 0.9625 -0.1593 0.0321  -0.2402 339  GLU A O   
2313 C  CB  . GLU A 340 ? 2.4229 1.7725 1.0408 -0.2329 0.1577  -0.2288 339  GLU A CB  
2314 C  CG  . GLU A 340 ? 2.5947 1.9817 1.1723 -0.2505 0.2168  -0.2354 339  GLU A CG  
2315 C  CD  . GLU A 340 ? 2.8683 2.1887 1.3345 -0.2261 0.2195  -0.2328 339  GLU A CD  
2316 O  OE1 . GLU A 340 ? 3.0012 2.2256 1.3982 -0.2176 0.1924  -0.2135 339  GLU A OE1 
2317 O  OE2 . GLU A 340 ? 2.9654 2.3321 1.4107 -0.2130 0.2487  -0.2510 339  GLU A OE2 
2318 N  N   . ALA A 341 ? 2.1937 1.5612 0.9650 -0.1967 0.0509  -0.2364 340  ALA A N   
2319 C  CA  . ALA A 341 ? 2.1972 1.5295 0.9952 -0.1860 0.0007  -0.2299 340  ALA A CA  
2320 C  C   . ALA A 341 ? 2.0716 1.4640 0.9636 -0.1865 -0.0116 -0.2370 340  ALA A C   
2321 O  O   . ALA A 341 ? 2.1714 1.6315 1.1103 -0.1995 0.0178  -0.2431 340  ALA A O   
2322 C  CB  . ALA A 341 ? 2.2749 1.5555 1.0492 -0.2035 -0.0053 -0.2073 340  ALA A CB  
2323 N  N   . ILE A 342 ? 1.9469 1.3168 0.8646 -0.1736 -0.0549 -0.2367 341  ILE A N   
2324 C  CA  . ILE A 342 ? 1.9933 1.4079 0.9899 -0.1736 -0.0676 -0.2399 341  ILE A CA  
2325 C  C   . ILE A 342 ? 2.0260 1.4175 1.0548 -0.1815 -0.1024 -0.2275 341  ILE A C   
2326 O  O   . ILE A 342 ? 1.9529 1.2950 0.9480 -0.1742 -0.1320 -0.2256 341  ILE A O   
2327 C  CB  . ILE A 342 ? 1.7613 1.1808 0.7585 -0.1446 -0.0796 -0.2584 341  ILE A CB  
2328 C  CG1 . ILE A 342 ? 1.7615 1.2435 0.7658 -0.1354 -0.0418 -0.2719 341  ILE A CG1 
2329 C  CG2 . ILE A 342 ? 1.7116 1.1361 0.7652 -0.1415 -0.1079 -0.2568 341  ILE A CG2 
2330 C  CD1 . ILE A 342 ? 1.8189 1.2852 0.7784 -0.1007 -0.0432 -0.2919 341  ILE A CD1 
2331 N  N   . VAL A 343 ? 2.0357 1.4701 1.1306 -0.1955 -0.0988 -0.2211 342  VAL A N   
2332 C  CA  . VAL A 343 ? 1.8438 1.2690 0.9739 -0.2045 -0.1246 -0.2094 342  VAL A CA  
2333 C  C   . VAL A 343 ? 1.7945 1.2424 0.9804 -0.2009 -0.1444 -0.2116 342  VAL A C   
2334 O  O   . VAL A 343 ? 1.5383 1.0254 0.7539 -0.1967 -0.1303 -0.2166 342  VAL A O   
2335 C  CB  . VAL A 343 ? 1.7620 1.2075 0.9149 -0.2260 -0.1039 -0.1978 342  VAL A CB  
2336 C  CG1 . VAL A 343 ? 1.5776 0.9988 0.7412 -0.2275 -0.1302 -0.1864 342  VAL A CG1 
2337 C  CG2 . VAL A 343 ? 1.7011 1.1306 0.8014 -0.2371 -0.0698 -0.1962 342  VAL A CG2 
2338 N  N   . ASP A 344 ? 1.9570 1.3822 1.1554 -0.2027 -0.1768 -0.2077 343  ASP A N   
2339 C  CA  . ASP A 344 ? 1.8710 1.3111 1.1197 -0.2068 -0.1935 -0.2061 343  ASP A CA  
2340 C  C   . ASP A 344 ? 1.7024 1.1857 1.0046 -0.2214 -0.1839 -0.1938 343  ASP A C   
2341 O  O   . ASP A 344 ? 1.7101 1.1934 1.0263 -0.2290 -0.1965 -0.1867 343  ASP A O   
2342 C  CB  . ASP A 344 ? 1.8635 1.2686 1.1062 -0.2089 -0.2302 -0.2104 343  ASP A CB  
2343 C  CG  . ASP A 344 ? 1.8889 1.3065 1.1827 -0.2217 -0.2437 -0.2065 343  ASP A CG  
2344 O  OD1 . ASP A 344 ? 2.0669 1.5084 1.3880 -0.2213 -0.2266 -0.2008 343  ASP A OD1 
2345 O  OD2 . ASP A 344 ? 1.8155 1.2202 1.1201 -0.2327 -0.2713 -0.2097 343  ASP A OD2 
2346 N  N   . GLY A 345 ? 1.5676 1.0907 0.8970 -0.2216 -0.1623 -0.1935 344  GLY A N   
2347 C  CA  . GLY A 345 ? 1.6490 1.2146 1.0224 -0.2343 -0.1504 -0.1852 344  GLY A CA  
2348 C  C   . GLY A 345 ? 1.5879 1.1592 1.0002 -0.2428 -0.1698 -0.1758 344  GLY A C   
2349 O  O   . GLY A 345 ? 1.3390 0.9229 0.7680 -0.2508 -0.1687 -0.1700 344  GLY A O   
2350 N  N   . ALA A 346 ? 1.5977 1.1564 1.0206 -0.2414 -0.1865 -0.1751 345  ALA A N   
2351 C  CA  . ALA A 346 ? 1.7514 1.3224 1.2145 -0.2546 -0.2010 -0.1665 345  ALA A CA  
2352 C  C   . ALA A 346 ? 1.8473 1.4148 1.3141 -0.2603 -0.2192 -0.1669 345  ALA A C   
2353 O  O   . ALA A 346 ? 1.6876 1.2874 1.1884 -0.2661 -0.2186 -0.1607 345  ALA A O   
2354 C  CB  . ALA A 346 ? 1.9425 1.4842 1.4036 -0.2574 -0.2146 -0.1666 345  ALA A CB  
2355 N  N   . ASN A 347 ? 2.0389 1.5686 1.4669 -0.2542 -0.2361 -0.1757 346  ASN A N   
2356 C  CA  . ASN A 347 ? 1.9976 1.5234 1.4220 -0.2531 -0.2598 -0.1785 346  ASN A CA  
2357 C  C   . ASN A 347 ? 1.7292 1.2704 1.1539 -0.2454 -0.2507 -0.1718 346  ASN A C   
2358 O  O   . ASN A 347 ? 1.6481 1.2141 1.1011 -0.2442 -0.2658 -0.1701 346  ASN A O   
2359 C  CB  . ASN A 347 ? 2.1966 1.6752 1.5638 -0.2426 -0.2761 -0.1902 346  ASN A CB  
2360 C  CG  . ASN A 347 ? 2.3471 1.8240 1.7048 -0.2363 -0.3054 -0.1949 346  ASN A CG  
2361 O  OD1 . ASN A 347 ? 2.7404 2.1915 2.0486 -0.2194 -0.3059 -0.1946 346  ASN A OD1 
2362 N  ND2 . ASN A 347 ? 2.1099 1.6170 1.5139 -0.2497 -0.3294 -0.1995 346  ASN A ND2 
2363 N  N   . ILE A 348 ? 1.6601 1.1860 1.0521 -0.2402 -0.2254 -0.1694 347  ILE A N   
2364 C  CA  . ILE A 348 ? 1.7383 1.2589 1.1163 -0.2353 -0.2131 -0.1634 347  ILE A CA  
2365 C  C   . ILE A 348 ? 1.5467 1.1100 0.9777 -0.2410 -0.2067 -0.1582 347  ILE A C   
2366 O  O   . ILE A 348 ? 1.3725 0.9405 0.8114 -0.2311 -0.2180 -0.1558 347  ILE A O   
2367 C  CB  . ILE A 348 ? 1.6905 1.1900 1.0282 -0.2394 -0.1813 -0.1635 347  ILE A CB  
2368 C  CG1 . ILE A 348 ? 1.7981 1.2663 1.0871 -0.2337 -0.1812 -0.1702 347  ILE A CG1 
2369 C  CG2 . ILE A 348 ? 1.4648 0.9328 0.7682 -0.2365 -0.1701 -0.1572 347  ILE A CG2 
2370 C  CD1 . ILE A 348 ? 1.8483 1.2689 1.0820 -0.2191 -0.2013 -0.1700 347  ILE A CD1 
2371 N  N   . GLY A 349 ? 1.5020 1.0976 0.9658 -0.2526 -0.1894 -0.1576 348  GLY A N   
2372 C  CA  . GLY A 349 ? 1.3924 1.0287 0.8992 -0.2580 -0.1790 -0.1538 348  GLY A CA  
2373 C  C   . GLY A 349 ? 1.5069 1.1772 1.0590 -0.2574 -0.1966 -0.1506 348  GLY A C   
2374 O  O   . GLY A 349 ? 1.5487 1.2423 1.1215 -0.2533 -0.1911 -0.1492 348  GLY A O   
2375 N  N   . LEU A 350 ? 1.6041 1.2791 1.1718 -0.2630 -0.2165 -0.1514 349  LEU A N   
2376 C  CA  . LEU A 350 ? 1.5503 1.2691 1.1679 -0.2692 -0.2301 -0.1499 349  LEU A CA  
2377 C  C   . LEU A 350 ? 1.4668 1.1893 1.0816 -0.2542 -0.2542 -0.1559 349  LEU A C   
2378 O  O   . LEU A 350 ? 1.2628 1.0337 0.9199 -0.2514 -0.2622 -0.1569 349  LEU A O   
2379 C  CB  . LEU A 350 ? 1.4477 1.1693 1.0847 -0.2889 -0.2382 -0.1488 349  LEU A CB  
2380 C  CG  . LEU A 350 ? 1.5889 1.3106 1.2287 -0.2965 -0.2160 -0.1404 349  LEU A CG  
2381 C  CD1 . LEU A 350 ? 1.5565 1.2298 1.1573 -0.2950 -0.2173 -0.1433 349  LEU A CD1 
2382 C  CD2 . LEU A 350 ? 1.8532 1.6115 1.5372 -0.3147 -0.2124 -0.1317 349  LEU A CD2 
2383 N  N   . TYR A 351 ? 1.4938 1.1683 1.0561 -0.2415 -0.2652 -0.1602 350  TYR A N   
2384 C  CA  . TYR A 351 ? 1.6284 1.2956 1.1703 -0.2184 -0.2880 -0.1645 350  TYR A CA  
2385 C  C   . TYR A 351 ? 1.8728 1.5327 1.4026 -0.2010 -0.2708 -0.1589 350  TYR A C   
2386 O  O   . TYR A 351 ? 2.1364 1.7631 1.6369 -0.2066 -0.2445 -0.1544 350  TYR A O   
2387 C  CB  . TYR A 351 ? 1.7393 1.3474 1.2144 -0.2082 -0.3000 -0.1684 350  TYR A CB  
2388 C  CG  . TYR A 351 ? 1.9488 1.5479 1.3958 -0.1810 -0.3306 -0.1734 350  TYR A CG  
2389 C  CD1 . TYR A 351 ? 1.9232 1.4927 1.3307 -0.1531 -0.3267 -0.1668 350  TYR A CD1 
2390 C  CD2 . TYR A 351 ? 2.0749 1.6897 1.5284 -0.1818 -0.3648 -0.1859 350  TYR A CD2 
2391 C  CE1 . TYR A 351 ? 1.9017 1.4592 1.2752 -0.1206 -0.3571 -0.1703 350  TYR A CE1 
2392 C  CE2 . TYR A 351 ? 2.0096 1.6233 1.4357 -0.1525 -0.3968 -0.1924 350  TYR A CE2 
2393 C  CZ  . TYR A 351 ? 1.9237 1.5090 1.3086 -0.1188 -0.3932 -0.1834 350  TYR A CZ  
2394 O  OH  . TYR A 351 ? 1.7770 1.3581 1.1274 -0.0825 -0.4273 -0.1888 350  TYR A OH  
2395 N  N   . GLN A 352 ? 1.8896 1.5813 1.4417 -0.1803 -0.2845 -0.1612 351  GLN A N   
2396 C  CA  . GLN A 352 ? 1.7609 1.5108 1.3579 -0.1741 -0.3154 -0.1699 351  GLN A CA  
2397 C  C   . GLN A 352 ? 1.8014 1.6282 1.4699 -0.1790 -0.3077 -0.1709 351  GLN A C   
2398 O  O   . GLN A 352 ? 1.8337 1.7262 1.5496 -0.1722 -0.3288 -0.1796 351  GLN A O   
2399 C  CB  . GLN A 352 ? 1.7951 1.5283 1.3550 -0.1337 -0.3410 -0.1739 351  GLN A CB  
2400 C  CG  . GLN A 352 ? 1.9150 1.7030 1.5066 -0.1260 -0.3808 -0.1874 351  GLN A CG  
2401 C  CD  . GLN A 352 ? 1.9388 1.7005 1.4776 -0.0785 -0.4088 -0.1907 351  GLN A CD  
2402 O  OE1 . GLN A 352 ? 1.9081 1.5961 1.3780 -0.0532 -0.3959 -0.1801 351  GLN A OE1 
2403 N  NE2 . GLN A 352 ? 1.8839 1.7039 1.4514 -0.0669 -0.4477 -0.2058 351  GLN A NE2 
2404 N  N   . GLN A 353 ? 1.8726 1.6966 1.5483 -0.1906 -0.2767 -0.1637 352  GLN A N   
2405 C  CA  . GLN A 353 ? 1.8171 1.7117 1.5533 -0.1941 -0.2650 -0.1640 352  GLN A CA  
2406 C  C   . GLN A 353 ? 1.7722 1.7221 1.5651 -0.2280 -0.2641 -0.1627 352  GLN A C   
2407 O  O   . GLN A 353 ? 1.6025 1.5219 1.3822 -0.2520 -0.2650 -0.1595 352  GLN A O   
2408 C  CB  . GLN A 353 ? 1.7418 1.6114 1.4589 -0.1943 -0.2338 -0.1587 352  GLN A CB  
2409 C  CG  . GLN A 353 ? 1.5346 1.3810 1.2408 -0.2225 -0.2149 -0.1520 352  GLN A CG  
2410 C  CD  . GLN A 353 ? 1.4150 1.1925 1.0632 -0.2229 -0.2171 -0.1516 352  GLN A CD  
2411 O  OE1 . GLN A 353 ? 1.6578 1.3985 1.2685 -0.2039 -0.2320 -0.1542 352  GLN A OE1 
2412 N  NE2 . GLN A 353 ? 1.2947 1.0559 0.9317 -0.2415 -0.2016 -0.1484 352  GLN A NE2 
2413 N  N   . ASN A 354 ? 1.9321 1.9596 1.7836 -0.2292 -0.2619 -0.1657 353  ASN A N   
2414 C  CA  . ASN A 354 ? 1.9643 2.0488 1.8715 -0.2653 -0.2588 -0.1639 353  ASN A CA  
2415 C  C   . ASN A 354 ? 1.9852 2.0538 1.8915 -0.2947 -0.2310 -0.1498 353  ASN A C   
2416 O  O   . ASN A 354 ? 1.8368 1.8724 1.7120 -0.2846 -0.2112 -0.1433 353  ASN A O   
2417 C  CB  . ASN A 354 ? 2.0264 2.2014 1.9897 -0.2495 -0.2587 -0.1717 353  ASN A CB  
2418 C  CG  . ASN A 354 ? 2.0719 2.3284 2.1031 -0.2824 -0.2662 -0.1773 353  ASN A CG  
2419 O  OD1 . ASN A 354 ? 2.1342 2.3805 2.1749 -0.3247 -0.2551 -0.1688 353  ASN A OD1 
2420 N  ND2 . ASN A 354 ? 2.0547 2.3918 2.1317 -0.2631 -0.2852 -0.1928 353  ASN A ND2 
2421 N  N   . PHE A 355 ? 2.1801 2.2693 2.1165 -0.3312 -0.2303 -0.1458 354  PHE A N   
2422 C  CA  . PHE A 355 ? 2.0926 2.1562 2.0181 -0.3560 -0.2062 -0.1300 354  PHE A CA  
2423 C  C   . PHE A 355 ? 2.0824 2.1993 2.0349 -0.3550 -0.1788 -0.1218 354  PHE A C   
2424 O  O   . PHE A 355 ? 1.8554 2.0026 1.8344 -0.3839 -0.1635 -0.1119 354  PHE A O   
2425 C  CB  . PHE A 355 ? 2.2867 2.3397 2.2254 -0.3968 -0.2129 -0.1273 354  PHE A CB  
2426 C  CG  . PHE A 355 ? 2.5792 2.5500 2.4679 -0.3995 -0.2285 -0.1298 354  PHE A CG  
2427 C  CD1 . PHE A 355 ? 2.6731 2.5910 2.5109 -0.3701 -0.2283 -0.1302 354  PHE A CD1 
2428 C  CD2 . PHE A 355 ? 2.6390 2.5854 2.5302 -0.4332 -0.2416 -0.1335 354  PHE A CD2 
2429 C  CE1 . PHE A 355 ? 2.6756 2.5247 2.4673 -0.3697 -0.2401 -0.1339 354  PHE A CE1 
2430 C  CE2 . PHE A 355 ? 2.6969 2.5646 2.5371 -0.4315 -0.2556 -0.1382 354  PHE A CE2 
2431 C  CZ  . PHE A 355 ? 2.7124 2.5348 2.5034 -0.3974 -0.2544 -0.1382 354  PHE A CZ  
2432 N  N   . VAL A 356 ? 2.3019 2.4231 2.2405 -0.3223 -0.1717 -0.1262 355  VAL A N   
2433 C  CA  . VAL A 356 ? 2.3766 2.5433 2.3312 -0.3129 -0.1475 -0.1231 355  VAL A CA  
2434 C  C   . VAL A 356 ? 1.9113 2.0544 1.8392 -0.3233 -0.1229 -0.1084 355  VAL A C   
2435 O  O   . VAL A 356 ? 1.9643 2.1525 1.9145 -0.3352 -0.1032 -0.0999 355  VAL A O   
2436 C  CB  . VAL A 356 ? 1.9909 2.1549 1.9293 -0.2732 -0.1498 -0.1358 355  VAL A CB  
2437 C  CG1 . VAL A 356 ? 2.0008 2.2191 1.9593 -0.2608 -0.1274 -0.1375 355  VAL A CG1 
2438 C  CG2 . VAL A 356 ? 1.9921 2.1703 1.9439 -0.2531 -0.1768 -0.1489 355  VAL A CG2 
2439 N  N   . ASP A 357 ? 1.6567 1.7370 1.5374 -0.3177 -0.1231 -0.1058 356  ASP A N   
2440 C  CA  . ASP A 357 ? 1.7704 1.7912 1.6215 -0.3184 -0.1419 -0.1092 356  ASP A CA  
2441 C  C   . ASP A 357 ? 1.9315 1.9286 1.7640 -0.2956 -0.1571 -0.1230 356  ASP A C   
2442 O  O   . ASP A 357 ? 2.0148 1.9750 1.8296 -0.2974 -0.1751 -0.1266 356  ASP A O   
2443 C  CB  . ASP A 357 ? 1.7364 1.7101 1.5461 -0.3191 -0.1330 -0.1018 356  ASP A CB  
2444 C  CG  . ASP A 357 ? 1.8720 1.8551 1.6652 -0.3022 -0.1172 -0.1059 356  ASP A CG  
2445 O  OD1 . ASP A 357 ? 1.8316 1.8560 1.6410 -0.3012 -0.1022 -0.1023 356  ASP A OD1 
2446 O  OD2 . ASP A 357 ? 2.0177 1.9696 1.7816 -0.2918 -0.1190 -0.1146 356  ASP A OD2 
2447 N  N   . GLY A 358 ? 1.8548 1.8634 1.6825 -0.2740 -0.1492 -0.1306 357  GLY A N   
2448 C  CA  . GLY A 358 ? 1.7922 1.7635 1.5902 -0.2520 -0.1605 -0.1409 357  GLY A CA  
2449 C  C   . GLY A 358 ? 1.7062 1.6126 1.4546 -0.2543 -0.1600 -0.1416 357  GLY A C   
2450 O  O   . GLY A 358 ? 1.7274 1.5933 1.4404 -0.2399 -0.1613 -0.1480 357  GLY A O   
2451 N  N   . SER A 359 ? 1.6442 1.5389 1.3868 -0.2714 -0.1565 -0.1348 358  SER A N   
2452 C  CA  . SER A 359 ? 1.6855 1.5340 1.3874 -0.2728 -0.1527 -0.1370 358  SER A CA  
2453 C  C   . SER A 359 ? 2.0313 1.8855 1.7212 -0.2702 -0.1322 -0.1424 358  SER A C   
2454 O  O   . SER A 359 ? 2.2456 2.1374 1.9574 -0.2694 -0.1219 -0.1417 358  SER A O   
2455 C  CB  . SER A 359 ? 1.7517 1.5898 1.4514 -0.2853 -0.1554 -0.1299 358  SER A CB  
2456 O  OG  . SER A 359 ? 1.9625 1.8325 1.6839 -0.2929 -0.1440 -0.1207 358  SER A OG  
2457 N  N   . PHE A 360 ? 1.9512 1.7720 1.6065 -0.2712 -0.1249 -0.1495 359  PHE A N   
2458 C  CA  . PHE A 360 ? 1.7010 1.4826 1.3266 -0.2729 -0.1319 -0.1500 359  PHE A CA  
2459 C  C   . PHE A 360 ? 1.8130 1.5530 1.3988 -0.2715 -0.1238 -0.1574 359  PHE A C   
2460 O  O   . PHE A 360 ? 2.0499 1.7930 1.6274 -0.2791 -0.1056 -0.1652 359  PHE A O   
2461 C  CB  . PHE A 360 ? 1.4966 1.2895 1.1202 -0.2782 -0.1246 -0.1495 359  PHE A CB  
2462 C  CG  . PHE A 360 ? 1.3174 1.0756 0.9094 -0.2770 -0.1284 -0.1525 359  PHE A CG  
2463 C  CD1 . PHE A 360 ? 1.4170 1.1535 1.0047 -0.2745 -0.1457 -0.1477 359  PHE A CD1 
2464 C  CD2 . PHE A 360 ? 1.3285 1.0778 0.8944 -0.2805 -0.1129 -0.1619 359  PHE A CD2 
2465 C  CE1 . PHE A 360 ? 1.4903 1.1938 1.0441 -0.2702 -0.1487 -0.1527 359  PHE A CE1 
2466 C  CE2 . PHE A 360 ? 1.3937 1.1170 0.9293 -0.2779 -0.1131 -0.1655 359  PHE A CE2 
2467 C  CZ  . PHE A 360 ? 1.4459 1.1448 0.9734 -0.2700 -0.1316 -0.1610 359  PHE A CZ  
2468 N  N   . SER A 361 ? 1.6410 1.3392 1.1979 -0.2633 -0.1369 -0.1555 360  SER A N   
2469 C  CA  . SER A 361 ? 1.5748 1.2207 1.0839 -0.2605 -0.1284 -0.1587 360  SER A CA  
2470 C  C   . SER A 361 ? 1.4425 1.0602 0.9134 -0.2741 -0.1124 -0.1622 360  SER A C   
2471 O  O   . SER A 361 ? 1.4709 1.0559 0.9094 -0.2691 -0.1206 -0.1593 360  SER A O   
2472 C  CB  . SER A 361 ? 1.3158 0.9275 0.8024 -0.2394 -0.1506 -0.1542 360  SER A CB  
2473 O  OG  . SER A 361 ? 1.5886 1.2186 1.0976 -0.2236 -0.1571 -0.1549 360  SER A OG  
2474 N  N   . LEU A 362 ? 1.4877 1.1242 0.9632 -0.2916 -0.0891 -0.1705 361  LEU A N   
2475 C  CA  . LEU A 362 ? 1.5745 1.1944 1.0176 -0.3090 -0.0679 -0.1771 361  LEU A CA  
2476 C  C   . LEU A 362 ? 1.7273 1.2722 1.1114 -0.3121 -0.0594 -0.1739 361  LEU A C   
2477 O  O   . LEU A 362 ? 1.8441 1.3560 1.1856 -0.3246 -0.0436 -0.1745 361  LEU A O   
2478 C  CB  . LEU A 362 ? 1.5801 1.2517 1.0500 -0.3289 -0.0472 -0.1906 361  LEU A CB  
2479 C  CG  . LEU A 362 ? 1.7226 1.4022 1.1733 -0.3508 -0.0231 -0.2015 361  LEU A CG  
2480 C  CD1 . LEU A 362 ? 1.6264 1.3879 1.1209 -0.3541 -0.0177 -0.2138 361  LEU A CD1 
2481 C  CD2 . LEU A 362 ? 1.9943 1.6315 1.4106 -0.3779 0.0004  -0.2088 361  LEU A CD2 
2482 N  N   . SER A 363 ? 1.7046 1.2212 1.0826 -0.2987 -0.0684 -0.1703 362  SER A N   
2483 C  CA  . SER A 363 ? 1.8406 1.2728 1.1535 -0.2924 -0.0645 -0.1646 362  SER A CA  
2484 C  C   . SER A 363 ? 2.0593 1.4520 1.3300 -0.2758 -0.0796 -0.1540 362  SER A C   
2485 O  O   . SER A 363 ? 2.2591 1.5847 1.4632 -0.2821 -0.0658 -0.1488 362  SER A O   
2486 C  CB  . SER A 363 ? 1.7005 1.1170 1.0181 -0.2683 -0.0779 -0.1633 362  SER A CB  
2487 O  OG  . SER A 363 ? 1.4459 0.9186 0.8148 -0.2452 -0.1051 -0.1601 362  SER A OG  
2488 N  N   . GLN A 364 ? 1.9496 1.3826 1.2560 -0.2570 -0.1073 -0.1514 363  GLN A N   
2489 C  CA  . GLN A 364 ? 1.8721 1.2769 1.1433 -0.2409 -0.1267 -0.1455 363  GLN A CA  
2490 C  C   . GLN A 364 ? 1.5187 0.9267 0.7727 -0.2575 -0.1121 -0.1487 363  GLN A C   
2491 O  O   . GLN A 364 ? 1.6635 1.0246 0.8601 -0.2506 -0.1140 -0.1445 363  GLN A O   
2492 C  CB  . GLN A 364 ? 1.4775 0.9276 0.7964 -0.2217 -0.1609 -0.1458 363  GLN A CB  
2493 C  CG  . GLN A 364 ? 1.4893 0.9400 0.8190 -0.1974 -0.1781 -0.1438 363  GLN A CG  
2494 C  CD  . GLN A 364 ? 1.5658 1.0778 0.9532 -0.1859 -0.2085 -0.1468 363  GLN A CD  
2495 O  OE1 . GLN A 364 ? 1.5286 1.0713 0.9477 -0.1689 -0.2204 -0.1483 363  GLN A OE1 
2496 N  NE2 . GLN A 364 ? 1.5579 1.0881 0.9581 -0.1960 -0.2202 -0.1492 363  GLN A NE2 
2497 N  N   . LEU A 365 ? 1.4609 0.9270 0.7623 -0.2749 -0.0987 -0.1568 364  LEU A N   
2498 C  CA  . LEU A 365 ? 1.5715 1.0513 0.8610 -0.2873 -0.0809 -0.1631 364  LEU A CA  
2499 C  C   . LEU A 365 ? 1.8154 1.2583 1.0539 -0.3089 -0.0474 -0.1643 364  LEU A C   
2500 O  O   . LEU A 365 ? 1.6350 1.0577 0.8313 -0.3118 -0.0355 -0.1647 364  LEU A O   
2501 C  CB  . LEU A 365 ? 1.5628 1.1157 0.9126 -0.2953 -0.0747 -0.1720 364  LEU A CB  
2502 C  CG  . LEU A 365 ? 1.7120 1.2897 1.0877 -0.2796 -0.0968 -0.1723 364  LEU A CG  
2503 C  CD1 . LEU A 365 ? 1.8714 1.4656 1.2887 -0.2718 -0.1203 -0.1661 364  LEU A CD1 
2504 C  CD2 . LEU A 365 ? 1.6721 1.3015 1.0729 -0.2827 -0.0824 -0.1819 364  LEU A CD2 
2505 N  N   . GLU A 366 ? 2.0718 1.5061 1.3135 -0.3266 -0.0301 -0.1662 365  GLU A N   
2506 C  CA  . GLU A 366 ? 2.1633 1.5600 1.3591 -0.3568 0.0053  -0.1688 365  GLU A CA  
2507 C  C   . GLU A 366 ? 2.3376 1.6379 1.4472 -0.3468 0.0056  -0.1538 365  GLU A C   
2508 O  O   . GLU A 366 ? 2.5527 1.8181 1.6094 -0.3676 0.0339  -0.1520 365  GLU A O   
2509 C  CB  . GLU A 366 ? 2.2081 1.6061 1.4221 -0.3787 0.0201  -0.1764 365  GLU A CB  
2510 C  CG  . GLU A 366 ? 2.2569 1.6572 1.4551 -0.4238 0.0603  -0.1883 365  GLU A CG  
2511 C  CD  . GLU A 366 ? 2.1860 1.5739 1.3928 -0.4476 0.0728  -0.1986 365  GLU A CD  
2512 O  OE1 . GLU A 366 ? 2.1533 1.5317 1.3769 -0.4242 0.0509  -0.1959 365  GLU A OE1 
2513 O  OE2 . GLU A 366 ? 2.1904 1.5813 1.3877 -0.4910 0.1052  -0.2116 365  GLU A OE2 
2514 N  N   . SER A 367 ? 2.0336 1.2954 1.1281 -0.3137 -0.0256 -0.1433 366  SER A N   
2515 C  CA  . SER A 367 ? 2.0099 1.1801 1.0184 -0.2937 -0.0328 -0.1283 366  SER A CA  
2516 C  C   . SER A 367 ? 2.1823 1.3444 1.1511 -0.2872 -0.0343 -0.1255 366  SER A C   
2517 O  O   . SER A 367 ? 2.4443 1.5388 1.3332 -0.2958 -0.0124 -0.1165 366  SER A O   
2518 C  CB  . SER A 367 ? 1.7933 0.9490 0.8077 -0.2531 -0.0719 -0.1220 366  SER A CB  
2519 O  OG  . SER A 367 ? 1.7826 0.9366 0.8219 -0.2540 -0.0687 -0.1249 366  SER A OG  
2520 N  N   . VAL A 368 ? 2.0366 1.2616 1.0551 -0.2733 -0.0580 -0.1335 367  VAL A N   
2521 C  CA  . VAL A 368 ? 2.0246 1.2401 1.0038 -0.2628 -0.0631 -0.1344 367  VAL A CA  
2522 C  C   . VAL A 368 ? 2.0286 1.2493 0.9816 -0.2922 -0.0196 -0.1390 367  VAL A C   
2523 O  O   . VAL A 368 ? 2.3089 1.4880 1.1928 -0.2885 -0.0091 -0.1345 367  VAL A O   
2524 C  CB  . VAL A 368 ? 1.7917 1.0683 0.8294 -0.2468 -0.0945 -0.1453 367  VAL A CB  
2525 C  CG1 . VAL A 368 ? 1.6854 0.9741 0.7618 -0.2259 -0.1335 -0.1432 367  VAL A CG1 
2526 C  CG2 . VAL A 368 ? 1.7984 1.1488 0.9023 -0.2650 -0.0774 -0.1575 367  VAL A CG2 
2527 N  N   . MET A 369 ? 1.8021 1.0796 0.8099 -0.3209 0.0058  -0.1492 368  MET A N   
2528 C  CA  . MET A 369 ? 1.9599 1.2601 0.9548 -0.3529 0.0489  -0.1572 368  MET A CA  
2529 C  C   . MET A 369 ? 2.1645 1.3785 1.0750 -0.3762 0.0803  -0.1443 368  MET A C   
2530 O  O   . MET A 369 ? 2.1639 1.3630 1.0240 -0.3922 0.1108  -0.1435 368  MET A O   
2531 C  CB  . MET A 369 ? 2.1046 1.4905 1.1798 -0.3775 0.0643  -0.1733 368  MET A CB  
2532 C  CG  . MET A 369 ? 2.0267 1.4919 1.1740 -0.3551 0.0395  -0.1842 368  MET A CG  
2533 S  SD  . MET A 369 ? 2.1338 1.6735 1.2960 -0.3560 0.0620  -0.2020 368  MET A SD  
2534 C  CE  . MET A 369 ? 2.1845 1.7682 1.3612 -0.4067 0.1103  -0.2142 368  MET A CE  
2535 N  N   . LYS A 370 ? 2.3984 1.5512 1.2887 -0.3768 0.0740  -0.1339 369  LYS A N   
2536 C  CA  . LYS A 370 ? 2.7398 1.7907 1.5405 -0.3978 0.1030  -0.1195 369  LYS A CA  
2537 C  C   . LYS A 370 ? 3.0005 1.9656 1.7005 -0.3711 0.0959  -0.1008 369  LYS A C   
2538 O  O   . LYS A 370 ? 3.3489 2.2616 1.9743 -0.3955 0.1330  -0.0924 369  LYS A O   
2539 C  CB  . LYS A 370 ? 2.8421 1.8398 1.6401 -0.3944 0.0927  -0.1141 369  LYS A CB  
2540 C  CG  . LYS A 370 ? 2.7908 1.8454 1.6578 -0.4324 0.1123  -0.1321 369  LYS A CG  
2541 C  CD  . LYS A 370 ? 2.8317 1.8137 1.6759 -0.4276 0.1059  -0.1272 369  LYS A CD  
2542 C  CE  . LYS A 370 ? 2.7755 1.8387 1.7135 -0.4158 0.0820  -0.1420 369  LYS A CE  
2543 N  NZ  . LYS A 370 ? 2.7228 1.7419 1.6491 -0.3688 0.0466  -0.1320 369  LYS A NZ  
2544 N  N   . GLU A 371 ? 2.8774 1.8312 1.5738 -0.3228 0.0491  -0.0952 370  GLU A N   
2545 C  CA  . GLU A 371 ? 2.8240 1.7002 1.4236 -0.2913 0.0348  -0.0795 370  GLU A CA  
2546 C  C   . GLU A 371 ? 2.6894 1.5960 1.2680 -0.2959 0.0494  -0.0859 370  GLU A C   
2547 O  O   . GLU A 371 ? 2.9940 1.8298 1.4737 -0.2933 0.0664  -0.0727 370  GLU A O   
2548 C  CB  . GLU A 371 ? 2.7424 1.6198 1.3569 -0.2401 -0.0226 -0.0779 370  GLU A CB  
2549 C  CG  . GLU A 371 ? 2.8486 1.6562 1.3661 -0.2015 -0.0461 -0.0652 370  GLU A CG  
2550 C  CD  . GLU A 371 ? 2.9250 1.6074 1.3206 -0.1999 -0.0226 -0.0413 370  GLU A CD  
2551 O  OE1 . GLU A 371 ? 2.8941 1.5269 1.2795 -0.1969 -0.0215 -0.0327 370  GLU A OE1 
2552 O  OE2 . GLU A 371 ? 2.9842 1.6112 1.2875 -0.1994 -0.0051 -0.0307 370  GLU A OE2 
2553 N  N   . LEU A 372 ? 2.2379 1.2455 0.9032 -0.2995 0.0431  -0.1060 371  LEU A N   
2554 C  CA  . LEU A 372 ? 2.4007 1.4417 1.0506 -0.2958 0.0529  -0.1159 371  LEU A CA  
2555 C  C   . LEU A 372 ? 2.6105 1.6464 1.2180 -0.3352 0.1112  -0.1150 371  LEU A C   
2556 O  O   . LEU A 372 ? 2.8142 1.8210 1.3490 -0.3292 0.1268  -0.1115 371  LEU A O   
2557 C  CB  . LEU A 372 ? 2.2938 1.4357 1.0424 -0.2884 0.0345  -0.1375 371  LEU A CB  
2558 C  CG  . LEU A 372 ? 2.2829 1.4554 1.0175 -0.2724 0.0345  -0.1512 371  LEU A CG  
2559 C  CD1 . LEU A 372 ? 2.1824 1.4054 0.9874 -0.2480 -0.0072 -0.1653 371  LEU A CD1 
2560 C  CD2 . LEU A 372 ? 2.3114 1.5415 1.0587 -0.3005 0.0844  -0.1631 371  LEU A CD2 
2561 N  N   . TYR A 373 ? 2.5871 1.6554 1.2398 -0.3771 0.1439  -0.1201 372  TYR A N   
2562 C  CA  . TYR A 373 ? 2.8396 1.9212 1.4675 -0.4237 0.2021  -0.1234 372  TYR A CA  
2563 C  C   . TYR A 373 ? 3.1788 2.1414 1.6772 -0.4322 0.2282  -0.0992 372  TYR A C   
2564 O  O   . TYR A 373 ? 3.3058 2.2716 1.7547 -0.4471 0.2644  -0.0993 372  TYR A O   
2565 C  CB  . TYR A 373 ? 2.8561 1.9824 1.5497 -0.4705 0.2278  -0.1340 372  TYR A CB  
2566 C  CG  . TYR A 373 ? 2.9590 2.1232 1.6456 -0.5258 0.2881  -0.1435 372  TYR A CG  
2567 C  CD1 . TYR A 373 ? 2.9432 2.2334 1.6998 -0.5323 0.3038  -0.1683 372  TYR A CD1 
2568 C  CD2 . TYR A 373 ? 3.1171 2.1926 1.7262 -0.5712 0.3300  -0.1288 372  TYR A CD2 
2569 C  CE1 . TYR A 373 ? 3.0597 2.4039 1.8198 -0.5830 0.3592  -0.1806 372  TYR A CE1 
2570 C  CE2 . TYR A 373 ? 3.1835 2.3025 1.7913 -0.6293 0.3883  -0.1394 372  TYR A CE2 
2571 C  CZ  . TYR A 373 ? 3.1041 2.3661 1.7927 -0.6352 0.4025  -0.1666 372  TYR A CZ  
2572 O  OH  . TYR A 373 ? 3.0605 2.3835 1.7569 -0.6930 0.4607  -0.1804 372  TYR A OH  
2573 N  N   . ARG A 374 ? 3.2960 2.1526 1.7348 -0.4196 0.2109  -0.0781 373  ARG A N   
2574 C  CA  . ARG A 374 ? 3.4984 2.2266 1.8013 -0.4220 0.2336  -0.0515 373  ARG A CA  
2575 C  C   . ARG A 374 ? 3.4800 2.1804 1.7123 -0.3744 0.2087  -0.0442 373  ARG A C   
2576 O  O   . ARG A 374 ? 3.7049 2.3402 1.8332 -0.3824 0.2406  -0.0293 373  ARG A O   
2577 C  CB  . ARG A 374 ? 3.6264 2.2423 1.8776 -0.4113 0.2178  -0.0313 373  ARG A CB  
2578 C  CG  . ARG A 374 ? 3.6224 2.2198 1.8785 -0.3459 0.1523  -0.0266 373  ARG A CG  
2579 C  CD  . ARG A 374 ? 3.8502 2.3027 1.9899 -0.3186 0.1423  0.0012  373  ARG A CD  
2580 N  NE  . ARG A 374 ? 4.0308 2.3864 2.0354 -0.3190 0.1698  0.0233  373  ARG A NE  
2581 C  CZ  . ARG A 374 ? 4.1890 2.4075 2.0665 -0.2872 0.1614  0.0510  373  ARG A CZ  
2582 N  NH1 . ARG A 374 ? 4.1860 2.3536 2.0594 -0.2496 0.1249  0.0579  373  ARG A NH1 
2583 N  NH2 . ARG A 374 ? 4.3464 2.4787 2.0969 -0.2894 0.1899  0.0721  373  ARG A NH2 
2584 N  N   . GLU A 375 ? 3.2285 1.9764 1.5138 -0.3274 0.1528  -0.0555 374  GLU A N   
2585 C  CA  . GLU A 375 ? 3.2028 1.9353 1.4314 -0.2837 0.1239  -0.0555 374  GLU A CA  
2586 C  C   . GLU A 375 ? 3.3114 2.1124 1.5485 -0.2979 0.1554  -0.0724 374  GLU A C   
2587 O  O   . GLU A 375 ? 3.5548 2.3101 1.6960 -0.2878 0.1713  -0.0648 374  GLU A O   
2588 C  CB  . GLU A 375 ? 2.9778 1.7505 1.2710 -0.2388 0.0575  -0.0674 374  GLU A CB  
2589 C  CG  . GLU A 375 ? 2.9419 1.6295 1.1660 -0.1956 0.0143  -0.0499 374  GLU A CG  
2590 C  CD  . GLU A 375 ? 3.0658 1.6832 1.1671 -0.1650 0.0070  -0.0394 374  GLU A CD  
2591 O  OE1 . GLU A 375 ? 3.0270 1.6809 1.1183 -0.1674 0.0191  -0.0526 374  GLU A OE1 
2592 O  OE2 . GLU A 375 ? 3.1922 1.7169 1.2024 -0.1345 -0.0118 -0.0187 374  GLU A OE2 
2593 N  N   . SER A 376 ? 3.1497 2.0609 1.4986 -0.3174 0.1643  -0.0958 375  SER A N   
2594 C  CA  . SER A 376 ? 3.1583 2.1501 1.5300 -0.3292 0.1968  -0.1156 375  SER A CA  
2595 C  C   . SER A 376 ? 3.3353 2.3126 1.6519 -0.3773 0.2652  -0.1075 375  SER A C   
2596 O  O   . SER A 376 ? 3.2328 2.2431 1.5182 -0.3801 0.2969  -0.1164 375  SER A O   
2597 C  CB  . SER A 376 ? 2.9911 2.1016 1.4941 -0.3350 0.1884  -0.1410 375  SER A CB  
2598 O  OG  . SER A 376 ? 2.8759 2.0170 1.4345 -0.3791 0.2159  -0.1410 375  SER A OG  
2599 N  N   . GLY A 377 ? 3.4943 2.4204 1.7971 -0.4162 0.2891  -0.0918 376  GLY A N   
2600 C  CA  . GLY A 377 ? 3.3703 2.2839 1.6330 -0.4751 0.3567  -0.0855 376  GLY A CA  
2601 C  C   . GLY A 377 ? 3.1826 2.2195 1.5600 -0.5217 0.3873  -0.1111 376  GLY A C   
2602 O  O   . GLY A 377 ? 2.9824 2.1084 1.4665 -0.5047 0.3551  -0.1314 376  GLY A O   
2603 N  N   . ASN A 378 ? 3.4920 2.5358 1.8441 -0.5816 0.4507  -0.1106 377  ASN A N   
2604 C  CA  . ASN A 378 ? 3.6646 2.8195 2.1172 -0.6362 0.4840  -0.1351 377  ASN A CA  
2605 C  C   . ASN A 378 ? 3.6310 2.9540 2.1874 -0.6276 0.4896  -0.1699 377  ASN A C   
2606 O  O   . ASN A 378 ? 3.6482 3.0736 2.2812 -0.6743 0.5221  -0.1921 377  ASN A O   
2607 C  CB  . ASN A 378 ? 3.9127 3.0191 2.2993 -0.7099 0.5535  -0.1246 377  ASN A CB  
2608 C  CG  . ASN A 378 ? 4.0937 3.0339 2.3881 -0.7272 0.5525  -0.0936 377  ASN A CG  
2609 O  OD1 . ASN A 378 ? 4.1155 3.0443 2.4549 -0.7540 0.5457  -0.0985 377  ASN A OD1 
2610 N  ND2 . ASN A 378 ? 4.2061 3.0132 2.3649 -0.7076 0.5583  -0.0620 377  ASN A ND2 
2611 N  N   . ASN A 379 ? 3.5960 2.9494 2.1549 -0.5676 0.4575  -0.1770 378  ASN A N   
2612 C  CA  . ASN A 379 ? 3.5612 3.0612 2.1982 -0.5547 0.4691  -0.2090 378  ASN A CA  
2613 C  C   . ASN A 379 ? 3.2476 2.8311 1.9904 -0.5117 0.4180  -0.2296 378  ASN A C   
2614 O  O   . ASN A 379 ? 3.1441 2.8555 1.9785 -0.5219 0.4306  -0.2562 378  ASN A O   
2615 C  CB  . ASN A 379 ? 3.8094 3.2961 2.3696 -0.5209 0.4814  -0.2085 378  ASN A CB  
2616 C  CG  . ASN A 379 ? 3.9239 3.3095 2.4203 -0.4606 0.4253  -0.1929 378  ASN A CG  
2617 O  OD1 . ASN A 379 ? 3.9798 3.2886 2.4713 -0.4501 0.3844  -0.1762 378  ASN A OD1 
2618 N  ND2 . ASN A 379 ? 3.9331 3.3229 2.3809 -0.4204 0.4229  -0.2008 378  ASN A ND2 
2619 N  N   . LYS A 380 ? 3.0714 2.5846 1.8002 -0.4648 0.3613  -0.2176 379  LYS A N   
2620 C  CA  . LYS A 380 ? 2.7721 2.3477 1.5836 -0.4212 0.3139  -0.2339 379  LYS A CA  
2621 C  C   . LYS A 380 ? 2.6908 2.2221 1.5380 -0.4143 0.2689  -0.2222 379  LYS A C   
2622 O  O   . LYS A 380 ? 2.6743 2.1022 1.4642 -0.4186 0.2559  -0.1992 379  LYS A O   
2623 C  CB  . LYS A 380 ? 2.6702 2.2285 1.4431 -0.3647 0.2870  -0.2394 379  LYS A CB  
2624 C  CG  . LYS A 380 ? 2.6050 2.2375 1.3655 -0.3586 0.3268  -0.2596 379  LYS A CG  
2625 C  CD  . LYS A 380 ? 2.3619 2.1370 1.2275 -0.3623 0.3411  -0.2879 379  LYS A CD  
2626 C  CE  . LYS A 380 ? 2.2968 2.1608 1.1566 -0.3528 0.3827  -0.3110 379  LYS A CE  
2627 N  NZ  . LYS A 380 ? 2.2894 2.1544 1.1001 -0.4082 0.4448  -0.3042 379  LYS A NZ  
2628 N  N   . TRP A 381 ? 2.6266 2.2400 1.5665 -0.4003 0.2462  -0.2386 380  TRP A N   
2629 C  CA  . TRP A 381 ? 2.5553 2.1482 1.5405 -0.3932 0.2069  -0.2310 380  TRP A CA  
2630 C  C   . TRP A 381 ? 2.2808 1.8751 1.2877 -0.3410 0.1589  -0.2348 380  TRP A C   
2631 O  O   . TRP A 381 ? 2.2692 1.9163 1.2900 -0.3142 0.1590  -0.2514 380  TRP A O   
2632 C  CB  . TRP A 381 ? 2.7333 2.4167 1.8035 -0.4232 0.2209  -0.2463 380  TRP A CB  
2633 C  CG  . TRP A 381 ? 2.9862 2.6457 2.0405 -0.4804 0.2568  -0.2413 380  TRP A CG  
2634 C  CD1 . TRP A 381 ? 3.1033 2.8205 2.1646 -0.5273 0.3067  -0.2551 380  TRP A CD1 
2635 C  CD2 . TRP A 381 ? 3.0333 2.6036 2.0618 -0.4979 0.2462  -0.2233 380  TRP A CD2 
2636 N  NE1 . TRP A 381 ? 3.1293 2.7880 2.1658 -0.5776 0.3284  -0.2460 380  TRP A NE1 
2637 C  CE2 . TRP A 381 ? 3.0950 2.6595 2.1082 -0.5569 0.2913  -0.2264 380  TRP A CE2 
2638 C  CE3 . TRP A 381 ? 2.9988 2.4959 2.0155 -0.4692 0.2038  -0.2065 380  TRP A CE3 
2639 C  CZ2 . TRP A 381 ? 3.1466 2.6209 2.1253 -0.5843 0.2940  -0.2125 380  TRP A CZ2 
2640 C  CZ3 . TRP A 381 ? 3.0034 2.4239 1.9914 -0.4920 0.2064  -0.1934 380  TRP A CZ3 
2641 C  CH2 . TRP A 381 ? 3.1027 2.5055 2.0680 -0.5473 0.2506  -0.1961 380  TRP A CH2 
2642 N  N   . PRO A 382 ? 2.0394 1.5752 1.0483 -0.3270 0.1188  -0.2206 381  PRO A N   
2643 C  CA  . PRO A 382 ? 1.9406 1.4664 0.9635 -0.2857 0.0746  -0.2232 381  PRO A CA  
2644 C  C   . PRO A 382 ? 2.0190 1.6150 1.1262 -0.2757 0.0580  -0.2336 381  PRO A C   
2645 O  O   . PRO A 382 ? 2.2445 1.8629 1.3978 -0.2949 0.0574  -0.2297 381  PRO A O   
2646 C  CB  . PRO A 382 ? 1.8083 1.2488 0.7965 -0.2804 0.0431  -0.2040 381  PRO A CB  
2647 C  CG  . PRO A 382 ? 1.7670 1.1947 0.7617 -0.3144 0.0631  -0.1932 381  PRO A CG  
2648 C  CD  . PRO A 382 ? 1.8847 1.3587 0.8792 -0.3484 0.1137  -0.2027 381  PRO A CD  
2649 N  N   . LEU A 383 ? 1.8478 1.4716 0.9671 -0.2434 0.0449  -0.2468 382  LEU A N   
2650 C  CA  . LEU A 383 ? 1.7986 1.4769 0.9838 -0.2274 0.0282  -0.2544 382  LEU A CA  
2651 C  C   . LEU A 383 ? 1.8469 1.4802 1.0509 -0.2220 -0.0106 -0.2406 382  LEU A C   
2652 O  O   . LEU A 383 ? 1.9818 1.5478 1.1478 -0.2139 -0.0346 -0.2328 382  LEU A O   
2653 C  CB  . LEU A 383 ? 1.6833 1.3880 0.8623 -0.1895 0.0257  -0.2718 382  LEU A CB  
2654 C  CG  . LEU A 383 ? 1.5856 1.3301 0.8141 -0.1624 0.0068  -0.2785 382  LEU A CG  
2655 C  CD1 . LEU A 383 ? 1.5718 1.3811 0.8033 -0.1324 0.0252  -0.3004 382  LEU A CD1 
2656 C  CD2 . LEU A 383 ? 1.6562 1.3252 0.8670 -0.1418 -0.0327 -0.2707 382  LEU A CD2 
2657 N  N   . ILE A 384 ? 1.6647 1.3418 0.9278 -0.2268 -0.0165 -0.2391 383  ILE A N   
2658 C  CA  . ILE A 384 ? 1.6067 1.2540 0.8937 -0.2241 -0.0482 -0.2265 383  ILE A CA  
2659 C  C   . ILE A 384 ? 1.7558 1.4313 1.0775 -0.2012 -0.0632 -0.2305 383  ILE A C   
2660 O  O   . ILE A 384 ? 1.8492 1.5901 1.2038 -0.1960 -0.0491 -0.2390 383  ILE A O   
2661 C  CB  . ILE A 384 ? 1.4987 1.1571 0.8154 -0.2509 -0.0430 -0.2169 383  ILE A CB  
2662 C  CG1 . ILE A 384 ? 1.4876 1.1140 0.7634 -0.2741 -0.0215 -0.2130 383  ILE A CG1 
2663 C  CG2 . ILE A 384 ? 1.6311 1.2562 0.9645 -0.2476 -0.0739 -0.2040 383  ILE A CG2 
2664 C  CD1 . ILE A 384 ? 1.4444 1.0878 0.7454 -0.3018 -0.0065 -0.2101 383  ILE A CD1 
2665 N  N   . LEU A 385 ? 1.8223 1.4467 1.1339 -0.1881 -0.0924 -0.2247 384  LEU A N   
2666 C  CA  . LEU A 385 ? 1.7878 1.4171 1.1202 -0.1684 -0.1067 -0.2244 384  LEU A CA  
2667 C  C   . LEU A 385 ? 1.6636 1.2857 1.0314 -0.1829 -0.1235 -0.2089 384  LEU A C   
2668 O  O   . LEU A 385 ? 1.4088 0.9882 0.7713 -0.1951 -0.1427 -0.2013 384  LEU A O   
2669 C  CB  . LEU A 385 ? 2.0168 1.5886 1.3061 -0.1441 -0.1234 -0.2321 384  LEU A CB  
2670 C  CG  . LEU A 385 ? 2.0557 1.6532 1.3186 -0.1174 -0.1042 -0.2500 384  LEU A CG  
2671 C  CD1 . LEU A 385 ? 2.0027 1.5357 1.2068 -0.1013 -0.1154 -0.2604 384  LEU A CD1 
2672 C  CD2 . LEU A 385 ? 1.9883 1.6229 1.2715 -0.0873 -0.1023 -0.2552 384  LEU A CD2 
2673 N  N   . LEU A 386 ? 1.7695 1.4414 1.1737 -0.1802 -0.1159 -0.2060 385  LEU A N   
2674 C  CA  . LEU A 386 ? 1.8471 1.5232 1.2846 -0.1923 -0.1260 -0.1916 385  LEU A CA  
2675 C  C   . LEU A 386 ? 1.8886 1.5800 1.3344 -0.1700 -0.1285 -0.1885 385  LEU A C   
2676 O  O   . LEU A 386 ? 1.5750 1.3020 1.0155 -0.1461 -0.1185 -0.1996 385  LEU A O   
2677 C  CB  . LEU A 386 ? 1.6402 1.3614 1.1078 -0.2143 -0.1117 -0.1899 385  LEU A CB  
2678 C  CG  . LEU A 386 ? 1.3910 1.0844 0.8618 -0.2352 -0.1197 -0.1813 385  LEU A CG  
2679 C  CD1 . LEU A 386 ? 1.3147 1.0423 0.8029 -0.2523 -0.1021 -0.1834 385  LEU A CD1 
2680 C  CD2 . LEU A 386 ? 1.2781 0.9549 0.7694 -0.2384 -0.1391 -0.1687 385  LEU A CD2 
2681 N  N   . HIS A 387 ? 2.0228 1.6887 1.4792 -0.1762 -0.1414 -0.1733 386  HIS A N   
2682 C  CA  . HIS A 387 ? 2.1787 1.8432 1.6308 -0.1543 -0.1440 -0.1656 386  HIS A CA  
2683 C  C   . HIS A 387 ? 2.0240 1.7668 1.5041 -0.1465 -0.1303 -0.1685 386  HIS A C   
2684 O  O   . HIS A 387 ? 2.0834 1.8706 1.5918 -0.1683 -0.1202 -0.1724 386  HIS A O   
2685 C  CB  . HIS A 387 ? 2.3886 2.0065 1.8431 -0.1707 -0.1562 -0.1469 386  HIS A CB  
2686 C  CG  . HIS A 387 ? 2.7092 2.2857 2.1343 -0.1471 -0.1611 -0.1367 386  HIS A CG  
2687 N  ND1 . HIS A 387 ? 2.8893 2.4971 2.3205 -0.1326 -0.1547 -0.1256 386  HIS A ND1 
2688 C  CD2 . HIS A 387 ? 2.8509 2.3485 2.2319 -0.1335 -0.1720 -0.1359 386  HIS A CD2 
2689 C  CE1 . HIS A 387 ? 3.0117 2.5585 2.4009 -0.1091 -0.1610 -0.1158 386  HIS A CE1 
2690 N  NE2 . HIS A 387 ? 3.0230 2.4988 2.3811 -0.1102 -0.1710 -0.1222 386  HIS A NE2 
2691 N  N   . LYS A 388 ? 1.8391 1.5957 1.3072 -0.1136 -0.1312 -0.1680 387  LYS A N   
2692 C  CA  . LYS A 388 ? 1.5796 1.4149 1.0731 -0.1037 -0.1229 -0.1721 387  LYS A CA  
2693 C  C   . LYS A 388 ? 1.6622 1.5071 1.1795 -0.1289 -0.1224 -0.1572 387  LYS A C   
2694 O  O   . LYS A 388 ? 1.8400 1.7500 1.3861 -0.1397 -0.1133 -0.1657 387  LYS A O   
2695 C  CB  . LYS A 388 ? 1.4741 1.3155 0.9428 -0.0565 -0.1291 -0.1716 387  LYS A CB  
2696 C  CG  . LYS A 388 ? 1.5314 1.3852 0.9815 -0.0231 -0.1274 -0.1912 387  LYS A CG  
2697 C  CD  . LYS A 388 ? 1.7337 1.6025 1.1600 0.0317  -0.1352 -0.1919 387  LYS A CD  
2698 C  CE  . LYS A 388 ? 1.6097 1.5874 1.0731 0.0395  -0.1304 -0.2021 387  LYS A CE  
2699 N  NZ  . LYS A 388 ? 1.5205 1.5910 1.0244 0.0233  -0.1148 -0.2304 387  LYS A NZ  
2700 N  N   . ARG A 389 ? 1.5721 1.3543 1.0770 -0.1397 -0.1309 -0.1371 388  ARG A N   
2701 C  CA  . ARG A 389 ? 1.6493 1.4435 1.1780 -0.1643 -0.1280 -0.1234 388  ARG A CA  
2702 C  C   . ARG A 389 ? 1.5109 1.3409 1.0724 -0.1922 -0.1208 -0.1342 388  ARG A C   
2703 O  O   . ARG A 389 ? 1.5481 1.4265 1.1319 -0.2000 -0.1128 -0.1368 388  ARG A O   
2704 C  CB  . ARG A 389 ? 1.8611 1.5877 1.3773 -0.1805 -0.1356 -0.1034 388  ARG A CB  
2705 C  CG  . ARG A 389 ? 2.1108 1.8610 1.6478 -0.1976 -0.1288 -0.0880 388  ARG A CG  
2706 C  CD  . ARG A 389 ? 2.3508 2.0433 1.8785 -0.2186 -0.1321 -0.0682 388  ARG A CD  
2707 N  NE  . ARG A 389 ? 2.5130 2.1354 1.9916 -0.1995 -0.1378 -0.0581 388  ARG A NE  
2708 C  CZ  . ARG A 389 ? 2.5841 2.1786 2.0310 -0.1878 -0.1327 -0.0377 388  ARG A CZ  
2709 N  NH1 . ARG A 389 ? 2.5213 2.1600 1.9835 -0.1948 -0.1213 -0.0258 388  ARG A NH1 
2710 N  NH2 . ARG A 389 ? 2.6922 2.2081 2.0850 -0.1671 -0.1386 -0.0288 388  ARG A NH2 
2711 N  N   . ARG A 390 ? 1.5233 1.3227 1.0808 -0.2050 -0.1242 -0.1407 389  ARG A N   
2712 C  CA  . ARG A 390 ? 1.5941 1.4116 1.1696 -0.2264 -0.1179 -0.1493 389  ARG A CA  
2713 C  C   . ARG A 390 ? 1.5286 1.3996 1.1112 -0.2254 -0.1028 -0.1670 389  ARG A C   
2714 O  O   . ARG A 390 ? 1.5836 1.4812 1.1831 -0.2419 -0.0939 -0.1726 389  ARG A O   
2715 C  CB  . ARG A 390 ? 1.7447 1.5138 1.3026 -0.2342 -0.1263 -0.1521 389  ARG A CB  
2716 C  CG  . ARG A 390 ? 1.8353 1.5651 1.3976 -0.2466 -0.1420 -0.1405 389  ARG A CG  
2717 C  CD  . ARG A 390 ? 1.6676 1.4228 1.2598 -0.2625 -0.1401 -0.1365 389  ARG A CD  
2718 N  NE  . ARG A 390 ? 1.6745 1.4091 1.2790 -0.2750 -0.1553 -0.1293 389  ARG A NE  
2719 C  CZ  . ARG A 390 ? 1.6964 1.4362 1.3199 -0.2847 -0.1576 -0.1172 389  ARG A CZ  
2720 N  NH1 . ARG A 390 ? 1.7941 1.5499 1.4178 -0.2787 -0.1462 -0.1085 389  ARG A NH1 
2721 N  NH2 . ARG A 390 ? 1.5895 1.3213 1.2302 -0.3009 -0.1708 -0.1144 389  ARG A NH2 
2722 N  N   . VAL A 391 ? 1.4256 1.3131 0.9948 -0.2066 -0.0996 -0.1778 390  VAL A N   
2723 C  CA  . VAL A 391 ? 1.4663 1.4164 1.0474 -0.2094 -0.0840 -0.1980 390  VAL A CA  
2724 C  C   . VAL A 391 ? 1.6390 1.6527 1.2446 -0.2070 -0.0808 -0.2029 390  VAL A C   
2725 O  O   . VAL A 391 ? 1.6841 1.7399 1.3077 -0.2281 -0.0687 -0.2176 390  VAL A O   
2726 C  CB  . VAL A 391 ? 1.3933 1.3589 0.9584 -0.1846 -0.0814 -0.2102 390  VAL A CB  
2727 C  CG1 . VAL A 391 ? 1.3927 1.4483 0.9811 -0.1834 -0.0667 -0.2327 390  VAL A CG1 
2728 C  CG2 . VAL A 391 ? 1.3153 1.2306 0.8541 -0.1930 -0.0786 -0.2123 390  VAL A CG2 
2729 N  N   . LYS A 392 ? 1.6703 1.6842 1.2706 -0.1825 -0.0918 -0.1905 391  LYS A N   
2730 C  CA  . LYS A 392 ? 1.5053 1.5785 1.1203 -0.1742 -0.0915 -0.1943 391  LYS A CA  
2731 C  C   . LYS A 392 ? 1.4066 1.4814 1.0381 -0.2013 -0.0867 -0.1909 391  LYS A C   
2732 O  O   . LYS A 392 ? 1.7131 1.8432 1.3616 -0.2109 -0.0802 -0.2073 391  LYS A O   
2733 C  CB  . LYS A 392 ? 1.4783 1.5349 1.0701 -0.1390 -0.1038 -0.1770 391  LYS A CB  
2734 C  CG  . LYS A 392 ? 1.5081 1.5919 1.0849 -0.0995 -0.1090 -0.1875 391  LYS A CG  
2735 C  CD  . LYS A 392 ? 1.5689 1.6384 1.1151 -0.0600 -0.1209 -0.1706 391  LYS A CD  
2736 C  CE  . LYS A 392 ? 1.6853 1.7695 1.2096 -0.0118 -0.1284 -0.1805 391  LYS A CE  
2737 N  NZ  . LYS A 392 ? 1.6654 1.8571 1.2254 -0.0074 -0.1223 -0.2134 391  LYS A NZ  
2738 N  N   . THR A 393 ? 1.1155 1.1331 0.7424 -0.2129 -0.0905 -0.1723 392  THR A N   
2739 C  CA  . THR A 393 ? 1.0967 1.1150 0.7387 -0.2331 -0.0859 -0.1697 392  THR A CA  
2740 C  C   . THR A 393 ? 1.4406 1.4667 1.0905 -0.2561 -0.0753 -0.1889 392  THR A C   
2741 O  O   . THR A 393 ? 1.2565 1.3029 0.9160 -0.2683 -0.0686 -0.1981 392  THR A O   
2742 C  CB  . THR A 393 ? 1.3734 1.3397 1.0148 -0.2405 -0.0924 -0.1494 392  THR A CB  
2743 O  OG1 . THR A 393 ? 1.4430 1.3944 1.0726 -0.2265 -0.0983 -0.1304 392  THR A OG1 
2744 C  CG2 . THR A 393 ? 1.2567 1.2326 0.9157 -0.2553 -0.0870 -0.1498 392  THR A CG2 
2745 N  N   . LEU A 394 ? 1.5431 1.5450 1.1820 -0.2620 -0.0728 -0.1948 393  LEU A N   
2746 C  CA  . LEU A 394 ? 1.5185 1.5174 1.1541 -0.2857 -0.0592 -0.2110 393  LEU A CA  
2747 C  C   . LEU A 394 ? 1.3393 1.4057 0.9889 -0.2950 -0.0474 -0.2347 393  LEU A C   
2748 O  O   . LEU A 394 ? 1.3220 1.3933 0.9737 -0.3196 -0.0359 -0.2490 393  LEU A O   
2749 C  CB  . LEU A 394 ? 1.6226 1.5800 1.2359 -0.2882 -0.0575 -0.2097 393  LEU A CB  
2750 C  CG  . LEU A 394 ? 1.7038 1.5952 1.2991 -0.2967 -0.0621 -0.1989 393  LEU A CG  
2751 C  CD1 . LEU A 394 ? 1.8074 1.6872 1.3968 -0.3179 -0.0490 -0.2081 393  LEU A CD1 
2752 C  CD2 . LEU A 394 ? 1.7193 1.5929 1.3260 -0.2848 -0.0794 -0.1812 393  LEU A CD2 
2753 N  N   . LEU A 395 ? 1.0911 1.2090 0.7486 -0.2743 -0.0514 -0.2404 394  LEU A N   
2754 C  CA  . LEU A 395 ? 1.1786 1.3798 0.8564 -0.2782 -0.0449 -0.2656 394  LEU A CA  
2755 C  C   . LEU A 395 ? 1.5022 1.7340 1.1912 -0.2818 -0.0485 -0.2711 394  LEU A C   
2756 O  O   . LEU A 395 ? 1.3920 1.6743 1.0956 -0.3031 -0.0404 -0.2963 394  LEU A O   
2757 C  CB  . LEU A 395 ? 1.2909 1.5418 0.9721 -0.2425 -0.0536 -0.2685 394  LEU A CB  
2758 C  CG  . LEU A 395 ? 1.2481 1.5068 0.9248 -0.2381 -0.0454 -0.2774 394  LEU A CG  
2759 C  CD1 . LEU A 395 ? 1.3276 1.6554 1.0119 -0.1972 -0.0541 -0.2875 394  LEU A CD1 
2760 C  CD2 . LEU A 395 ? 1.1283 1.4091 0.8153 -0.2806 -0.0227 -0.2991 394  LEU A CD2 
2761 N  N   . GLU A 396 ? 1.7528 1.9546 1.4332 -0.2630 -0.0596 -0.2487 395  GLU A N   
2762 C  CA  . GLU A 396 ? 1.7051 1.9325 1.3894 -0.2611 -0.0624 -0.2507 395  GLU A CA  
2763 C  C   . GLU A 396 ? 1.7683 1.9722 1.4540 -0.2920 -0.0516 -0.2629 395  GLU A C   
2764 O  O   . GLU A 396 ? 1.9330 2.1733 1.6234 -0.3000 -0.0494 -0.2807 395  GLU A O   
2765 C  CB  . GLU A 396 ? 1.6304 1.8243 1.3019 -0.2382 -0.0717 -0.2210 395  GLU A CB  
2766 C  CG  . GLU A 396 ? 1.5388 1.7604 1.1976 -0.2032 -0.0826 -0.2112 395  GLU A CG  
2767 C  CD  . GLU A 396 ? 1.6308 1.8022 1.2702 -0.1892 -0.0871 -0.1788 395  GLU A CD  
2768 O  OE1 . GLU A 396 ? 1.6657 1.8127 1.3103 -0.2055 -0.0815 -0.1692 395  GLU A OE1 
2769 O  OE2 . GLU A 396 ? 1.6690 1.8243 1.2864 -0.1623 -0.0952 -0.1637 395  GLU A OE2 
2770 N  N   . ASN A 397 ? 1.6561 1.7951 1.3323 -0.3063 -0.0461 -0.2542 396  ASN A N   
2771 C  CA  . ASN A 397 ? 1.5659 1.6680 1.2332 -0.3303 -0.0360 -0.2647 396  ASN A CA  
2772 C  C   . ASN A 397 ? 1.5432 1.6686 1.2109 -0.3613 -0.0221 -0.2939 396  ASN A C   
2773 O  O   . ASN A 397 ? 1.4832 1.6157 1.1511 -0.3714 -0.0152 -0.2986 396  ASN A O   
2774 C  CB  . ASN A 397 ? 1.5548 1.5810 1.2058 -0.3312 -0.0365 -0.2472 396  ASN A CB  
2775 C  CG  . ASN A 397 ? 1.4948 1.4749 1.1305 -0.3417 -0.0303 -0.2530 396  ASN A CG  
2776 O  OD1 . ASN A 397 ? 1.4833 1.4528 1.1060 -0.3653 -0.0179 -0.2737 396  ASN A OD1 
2777 N  ND2 . ASN A 397 ? 1.4205 1.3727 1.0568 -0.3242 -0.0386 -0.2361 396  ASN A ND2 
2778 N  N   . PRO A 398 ? 1.6546 1.7935 1.3214 -0.3786 -0.0165 -0.3153 397  PRO A N   
2779 C  CA  . PRO A 398 ? 1.7386 1.9041 1.4078 -0.4161 -0.0025 -0.3475 397  PRO A CA  
2780 C  C   . PRO A 398 ? 1.6728 1.7631 1.3152 -0.4473 0.0153  -0.3480 397  PRO A C   
2781 O  O   . PRO A 398 ? 1.7690 1.8828 1.4153 -0.4786 0.0302  -0.3657 397  PRO A O   
2782 C  CB  . PRO A 398 ? 1.9403 2.1153 1.6054 -0.4228 -0.0038 -0.3667 397  PRO A CB  
2783 C  CG  . PRO A 398 ? 1.8923 2.0141 1.5431 -0.3945 -0.0112 -0.3419 397  PRO A CG  
2784 C  CD  . PRO A 398 ? 1.6919 1.8232 1.3546 -0.3643 -0.0223 -0.3118 397  PRO A CD  
2785 N  N   . THR A 399 ? 1.6876 1.6912 1.3013 -0.4374 0.0142  -0.3286 398  THR A N   
2786 C  CA  . THR A 399 ? 1.8546 1.7705 1.4293 -0.4583 0.0286  -0.3238 398  THR A CA  
2787 C  C   . THR A 399 ? 1.7623 1.6827 1.3350 -0.4634 0.0350  -0.3145 398  THR A C   
2788 O  O   . THR A 399 ? 1.6834 1.5894 1.2392 -0.4986 0.0558  -0.3266 398  THR A O   
2789 C  CB  . THR A 399 ? 1.3124 1.1477 0.8601 -0.4313 0.0189  -0.3013 398  THR A CB  
2790 O  OG1 . THR A 399 ? 1.2862 1.1265 0.8386 -0.4183 0.0127  -0.3087 398  THR A OG1 
2791 C  CG2 . THR A 399 ? 1.5055 1.2405 1.0003 -0.4483 0.0325  -0.2971 398  THR A CG2 
2792 N  N   . HIS A 400 ? 1.6490 1.5881 1.2367 -0.4293 0.0186  -0.2939 399  HIS A N   
2793 C  CA  . HIS A 400 ? 1.5618 1.4926 1.1404 -0.4247 0.0211  -0.2829 399  HIS A CA  
2794 C  C   . HIS A 400 ? 1.6242 1.6406 1.2305 -0.4311 0.0285  -0.2991 399  HIS A C   
2795 O  O   . HIS A 400 ? 1.8058 1.8169 1.3994 -0.4375 0.0395  -0.2980 399  HIS A O   
2796 C  CB  . HIS A 400 ? 1.4799 1.3896 1.0603 -0.3871 -0.0010 -0.2572 399  HIS A CB  
2797 C  CG  . HIS A 400 ? 1.5549 1.4061 1.1209 -0.3747 -0.0114 -0.2436 399  HIS A CG  
2798 N  ND1 . HIS A 400 ? 1.7470 1.5289 1.2768 -0.3883 -0.0020 -0.2456 399  HIS A ND1 
2799 C  CD2 . HIS A 400 ? 1.3771 1.2319 0.9598 -0.3489 -0.0295 -0.2286 399  HIS A CD2 
2800 C  CE1 . HIS A 400 ? 1.7019 1.4534 1.2294 -0.3656 -0.0160 -0.2338 399  HIS A CE1 
2801 N  NE2 . HIS A 400 ? 1.4186 1.2190 0.9817 -0.3446 -0.0317 -0.2240 399  HIS A NE2 
2802 N  N   . ARG A 401 ? 1.5181 1.6162 1.1597 -0.4260 0.0221  -0.3151 400  ARG A N   
2803 C  CA  . ARG A 401 ? 1.5573 1.7483 1.2292 -0.4150 0.0211  -0.3285 400  ARG A CA  
2804 C  C   . ARG A 401 ? 1.7872 2.0112 1.4618 -0.4474 0.0454  -0.3482 400  ARG A C   
2805 O  O   . ARG A 401 ? 1.8463 2.1096 1.5292 -0.4295 0.0465  -0.3482 400  ARG A O   
2806 C  CB  . ARG A 401 ? 1.5301 1.8046 1.2335 -0.4073 0.0106  -0.3468 400  ARG A CB  
2807 C  CG  . ARG A 401 ? 1.4882 1.8640 1.2214 -0.3852 0.0048  -0.3609 400  ARG A CG  
2808 C  CD  . ARG A 401 ? 1.3847 1.8307 1.1376 -0.3594 -0.0141 -0.3694 400  ARG A CD  
2809 N  NE  . ARG A 401 ? 1.4164 1.9516 1.1903 -0.3251 -0.0241 -0.3790 400  ARG A NE  
2810 C  CZ  . ARG A 401 ? 1.5237 2.1526 1.3283 -0.3397 -0.0144 -0.4100 400  ARG A CZ  
2811 N  NH1 . ARG A 401 ? 1.4187 2.0601 1.2352 -0.3958 0.0078  -0.4341 400  ARG A NH1 
2812 N  NH2 . ARG A 401 ? 1.6776 2.3883 1.4995 -0.2980 -0.0263 -0.4179 400  ARG A NH2 
2813 N  N   . ASN A 402 ? 2.0162 2.2221 1.6810 -0.4956 0.0666  -0.3655 401  ASN A N   
2814 C  CA  . ASN A 402 ? 2.1728 2.4110 1.8396 -0.5357 0.0951  -0.3845 401  ASN A CA  
2815 C  C   . ASN A 402 ? 2.1847 2.3565 1.8128 -0.5306 0.1067  -0.3632 401  ASN A C   
2816 O  O   . ASN A 402 ? 2.2060 2.4310 1.8440 -0.5357 0.1223  -0.3725 401  ASN A O   
2817 C  CB  . ASN A 402 ? 2.3105 2.5210 1.9642 -0.5948 0.1175  -0.4054 401  ASN A CB  
2818 C  CG  . ASN A 402 ? 2.3919 2.4644 1.9885 -0.6010 0.1192  -0.3842 401  ASN A CG  
2819 O  OD1 . ASN A 402 ? 2.4618 2.4886 2.0480 -0.5611 0.0962  -0.3624 401  ASN A OD1 
2820 N  ND2 . ASN A 402 ? 2.3773 2.3831 1.9349 -0.6509 0.1475  -0.3910 401  ASN A ND2 
2821 N  N   . LEU A 403 ? 2.0930 2.1542 1.6765 -0.5178 0.0984  -0.3363 402  LEU A N   
2822 C  CA  . LEU A 403 ? 1.8557 1.8447 1.3935 -0.5113 0.1059  -0.3160 402  LEU A CA  
2823 C  C   . LEU A 403 ? 1.6482 1.6713 1.1982 -0.4667 0.0893  -0.3062 402  LEU A C   
2824 O  O   . LEU A 403 ? 1.6593 1.6915 1.1941 -0.4681 0.1044  -0.3077 402  LEU A O   
2825 C  CB  . LEU A 403 ? 1.8417 1.7131 1.3315 -0.5029 0.0954  -0.2925 402  LEU A CB  
2826 C  CG  . LEU A 403 ? 1.8696 1.6589 1.3062 -0.4872 0.0942  -0.2694 402  LEU A CG  
2827 C  CD1 . LEU A 403 ? 2.0144 1.7882 1.4149 -0.5232 0.1290  -0.2752 402  LEU A CD1 
2828 C  CD2 . LEU A 403 ? 1.7942 1.4830 1.1900 -0.4748 0.0803  -0.2505 402  LEU A CD2 
2829 N  N   . VAL A 404 ? 1.4904 1.5283 1.0631 -0.4282 0.0603  -0.2967 403  VAL A N   
2830 C  CA  . VAL A 404 ? 1.4751 1.5258 1.0510 -0.3859 0.0427  -0.2864 403  VAL A CA  
2831 C  C   . VAL A 404 ? 1.6355 1.7848 1.2410 -0.3765 0.0517  -0.3072 403  VAL A C   
2832 O  O   . VAL A 404 ? 1.6765 1.8274 1.2682 -0.3545 0.0529  -0.3054 403  VAL A O   
2833 C  CB  . VAL A 404 ? 1.3406 1.3824 0.9316 -0.3529 0.0133  -0.2714 403  VAL A CB  
2834 C  CG1 . VAL A 404 ? 1.1830 1.2243 0.7696 -0.3133 -0.0033 -0.2617 403  VAL A CG1 
2835 C  CG2 . VAL A 404 ? 1.1999 1.1592 0.7685 -0.3580 0.0039  -0.2532 403  VAL A CG2 
2836 N  N   . GLU A 405 ? 1.7576 1.9930 1.4032 -0.3907 0.0571  -0.3296 404  GLU A N   
2837 C  CA  . GLU A 405 ? 2.0535 2.4007 1.7342 -0.3799 0.0644  -0.3538 404  GLU A CA  
2838 C  C   . GLU A 405 ? 2.0854 2.4470 1.7546 -0.4109 0.0971  -0.3662 404  GLU A C   
2839 O  O   . GLU A 405 ? 2.0749 2.4977 1.7545 -0.3884 0.1034  -0.3770 404  GLU A O   
2840 C  CB  . GLU A 405 ? 2.1845 2.6265 1.9108 -0.3933 0.0619  -0.3787 404  GLU A CB  
2841 C  CG  . GLU A 405 ? 2.3474 2.9244 2.1172 -0.3851 0.0696  -0.4096 404  GLU A CG  
2842 C  CD  . GLU A 405 ? 2.4058 3.0047 2.1715 -0.3239 0.0552  -0.4025 404  GLU A CD  
2843 O  OE1 . GLU A 405 ? 2.4900 3.0408 2.2383 -0.2803 0.0283  -0.3808 404  GLU A OE1 
2844 O  OE2 . GLU A 405 ? 2.3327 2.9939 2.1095 -0.3200 0.0724  -0.4193 404  GLU A OE2 
2845 N  N   . GLU A 406 ? 2.0066 2.3064 1.6485 -0.4605 0.1191  -0.3636 405  GLU A N   
2846 C  CA  . GLU A 406 ? 2.0697 2.3660 1.6886 -0.4965 0.1548  -0.3708 405  GLU A CA  
2847 C  C   . GLU A 406 ? 2.0645 2.3117 1.6433 -0.4612 0.1521  -0.3530 405  GLU A C   
2848 O  O   . GLU A 406 ? 2.2975 2.5945 1.8756 -0.4628 0.1744  -0.3650 405  GLU A O   
2849 C  CB  . GLU A 406 ? 2.2808 2.4860 1.8589 -0.5505 0.1759  -0.3640 405  GLU A CB  
2850 C  CG  . GLU A 406 ? 2.5936 2.7920 2.1424 -0.5978 0.2190  -0.3712 405  GLU A CG  
2851 C  CD  . GLU A 406 ? 2.6685 2.9918 2.2718 -0.6432 0.2458  -0.4079 405  GLU A CD  
2852 O  OE1 . GLU A 406 ? 2.6384 2.9851 2.2694 -0.6735 0.2431  -0.4245 405  GLU A OE1 
2853 O  OE2 . GLU A 406 ? 2.6918 3.0946 2.3111 -0.6487 0.2697  -0.4224 405  GLU A OE2 
2854 N  N   . TRP A 407 ? 1.9241 2.0788 1.4708 -0.4299 0.1248  -0.3267 406  TRP A N   
2855 C  CA  . TRP A 407 ? 1.7027 1.8055 1.2097 -0.3951 0.1159  -0.3119 406  TRP A CA  
2856 C  C   . TRP A 407 ? 1.5756 1.7549 1.1102 -0.3494 0.1048  -0.3241 406  TRP A C   
2857 O  O   . TRP A 407 ? 1.5870 1.7777 1.1009 -0.3347 0.1175  -0.3299 406  TRP A O   
2858 C  CB  . TRP A 407 ? 1.5432 1.5434 1.0195 -0.3750 0.0859  -0.2854 406  TRP A CB  
2859 C  CG  . TRP A 407 ? 1.5228 1.4358 0.9568 -0.4074 0.0958  -0.2721 406  TRP A CG  
2860 C  CD1 . TRP A 407 ? 1.6720 1.5714 1.0813 -0.4519 0.1299  -0.2782 406  TRP A CD1 
2861 C  CD2 . TRP A 407 ? 1.4673 1.2926 0.8751 -0.3964 0.0721  -0.2508 406  TRP A CD2 
2862 N  NE1 . TRP A 407 ? 1.7530 1.5494 1.1140 -0.4646 0.1276  -0.2602 406  TRP A NE1 
2863 C  CE2 . TRP A 407 ? 1.5710 1.3278 0.9339 -0.4286 0.0913  -0.2444 406  TRP A CE2 
2864 C  CE3 . TRP A 407 ? 1.4194 1.2192 0.8370 -0.3634 0.0377  -0.2372 406  TRP A CE3 
2865 C  CZ2 . TRP A 407 ? 1.4797 1.1484 0.8080 -0.4204 0.0739  -0.2259 406  TRP A CZ2 
2866 C  CZ3 . TRP A 407 ? 1.4340 1.1583 0.8258 -0.3615 0.0223  -0.2206 406  TRP A CZ3 
2867 C  CH2 . TRP A 407 ? 1.4273 1.0892 0.7752 -0.3858 0.0390  -0.2156 406  TRP A CH2 
2868 N  N   . ILE A 408 ? 1.4934 1.7215 1.0688 -0.3242 0.0819  -0.3281 407  ILE A N   
2869 C  CA  . ILE A 408 ? 1.4843 1.7735 1.0783 -0.2732 0.0677  -0.3376 407  ILE A CA  
2870 C  C   . ILE A 408 ? 1.5365 1.9414 1.1597 -0.2758 0.0939  -0.3673 407  ILE A C   
2871 O  O   . ILE A 408 ? 1.5600 1.9917 1.1745 -0.2360 0.0941  -0.3752 407  ILE A O   
2872 C  CB  . ILE A 408 ? 1.3916 1.7111 1.0175 -0.2481 0.0406  -0.3350 407  ILE A CB  
2873 C  CG1 . ILE A 408 ? 1.2120 1.4291 0.8145 -0.2480 0.0182  -0.3069 407  ILE A CG1 
2874 C  CG2 . ILE A 408 ? 1.2231 1.5941 0.8569 -0.1896 0.0256  -0.3431 407  ILE A CG2 
2875 C  CD1 . ILE A 408 ? 1.1885 1.4156 0.8064 -0.2152 -0.0080 -0.2982 407  ILE A CD1 
2876 N  N   . SER A 409 ? 1.6474 2.1231 1.3059 -0.3229 0.1163  -0.3861 408  SER A N   
2877 C  CA  . SER A 409 ? 1.8096 2.4118 1.5057 -0.3348 0.1441  -0.4180 408  SER A CA  
2878 C  C   . SER A 409 ? 1.8395 2.4129 1.4966 -0.3543 0.1772  -0.4172 408  SER A C   
2879 O  O   . SER A 409 ? 1.7412 2.3957 1.4109 -0.3323 0.1927  -0.4362 408  SER A O   
2880 C  CB  . SER A 409 ? 2.0102 2.6913 1.7536 -0.3901 0.1598  -0.4405 408  SER A CB  
2881 O  OG  . SER A 409 ? 2.1157 2.7059 1.8258 -0.4498 0.1793  -0.4281 408  SER A OG  
2882 N  N   . ASN A 410 ? 2.0243 2.4831 1.6303 -0.3920 0.1882  -0.3954 409  ASN A N   
2883 C  CA  . ASN A 410 ? 2.1527 2.5633 1.7056 -0.4095 0.2184  -0.3892 409  ASN A CA  
2884 C  C   . ASN A 410 ? 2.2174 2.5866 1.7314 -0.3506 0.2020  -0.3801 409  ASN A C   
2885 O  O   . ASN A 410 ? 2.3315 2.7294 1.8249 -0.3443 0.2271  -0.3902 409  ASN A O   
2886 C  CB  . ASN A 410 ? 2.0550 2.3380 1.5516 -0.4534 0.2272  -0.3648 409  ASN A CB  
2887 C  CG  . ASN A 410 ? 1.8921 2.2011 1.4058 -0.5230 0.2589  -0.3770 409  ASN A CG  
2888 O  OD1 . ASN A 410 ? 1.7936 2.2156 1.3501 -0.5520 0.2881  -0.4047 409  ASN A OD1 
2889 N  ND2 . ASN A 410 ? 1.8032 2.0075 1.2826 -0.5504 0.2536  -0.3584 409  ASN A ND2 
2890 N  N   . GLY A 411 ? 2.0489 2.3494 1.5509 -0.3099 0.1613  -0.3623 410  GLY A N   
2891 C  CA  . GLY A 411 ? 1.8857 2.1283 1.3453 -0.2589 0.1420  -0.3540 410  GLY A CA  
2892 C  C   . GLY A 411 ? 1.7871 1.8940 1.1869 -0.2671 0.1265  -0.3266 410  GLY A C   
2893 O  O   . GLY A 411 ? 1.9204 1.9654 1.2718 -0.2384 0.1158  -0.3206 410  GLY A O   
2894 N  N   . VAL A 412 ? 1.6060 1.6691 1.0080 -0.3045 0.1244  -0.3126 411  VAL A N   
2895 C  CA  . VAL A 412 ? 1.6264 1.5716 0.9765 -0.3110 0.1085  -0.2882 411  VAL A CA  
2896 C  C   . VAL A 412 ? 1.5564 1.4634 0.9235 -0.2837 0.0668  -0.2751 411  VAL A C   
2897 O  O   . VAL A 412 ? 1.4870 1.3094 0.8211 -0.2804 0.0460  -0.2575 411  VAL A O   
2898 C  CB  . VAL A 412 ? 1.8078 1.7161 1.1418 -0.3620 0.1298  -0.2798 411  VAL A CB  
2899 C  CG1 . VAL A 412 ? 1.8689 1.6600 1.1337 -0.3614 0.1192  -0.2571 411  VAL A CG1 
2900 C  CG2 . VAL A 412 ? 1.9026 1.8706 1.2369 -0.3998 0.1760  -0.2963 411  VAL A CG2 
2901 N  N   . LEU A 413 ? 1.5873 1.5611 1.0057 -0.2651 0.0553  -0.2840 412  LEU A N   
2902 C  CA  . LEU A 413 ? 1.5280 1.4687 0.9592 -0.2396 0.0203  -0.2712 412  LEU A CA  
2903 C  C   . LEU A 413 ? 1.4709 1.4504 0.9146 -0.1942 0.0076  -0.2808 412  LEU A C   
2904 O  O   . LEU A 413 ? 1.4387 1.5050 0.9079 -0.1830 0.0231  -0.3000 412  LEU A O   
2905 C  CB  . LEU A 413 ? 1.5392 1.5000 1.0096 -0.2611 0.0153  -0.2660 412  LEU A CB  
2906 C  CG  . LEU A 413 ? 1.5714 1.4810 1.0458 -0.2458 -0.0162 -0.2475 412  LEU A CG  
2907 C  CD1 . LEU A 413 ? 1.6084 1.4407 1.0561 -0.2649 -0.0236 -0.2318 412  LEU A CD1 
2908 C  CD2 . LEU A 413 ? 1.6758 1.6389 1.1948 -0.2461 -0.0218 -0.2488 412  LEU A CD2 
2909 N  N   . TYR A 414 ? 1.5027 1.4161 0.9258 -0.1679 -0.0205 -0.2685 413  TYR A N   
2910 C  CA  . TYR A 414 ? 1.5976 1.5221 1.0209 -0.1227 -0.0354 -0.2735 413  TYR A CA  
2911 C  C   . TYR A 414 ? 1.6684 1.5433 1.0977 -0.1163 -0.0626 -0.2545 413  TYR A C   
2912 O  O   . TYR A 414 ? 1.5618 1.3707 0.9791 -0.1363 -0.0758 -0.2395 413  TYR A O   
2913 C  CB  . TYR A 414 ? 1.8440 1.7237 1.2185 -0.0941 -0.0374 -0.2817 413  TYR A CB  
2914 C  CG  . TYR A 414 ? 1.8875 1.7782 1.2525 -0.0411 -0.0475 -0.2918 413  TYR A CG  
2915 C  CD1 . TYR A 414 ? 1.8743 1.6924 1.2198 -0.0185 -0.0750 -0.2790 413  TYR A CD1 
2916 C  CD2 . TYR A 414 ? 1.8997 1.8704 1.2714 -0.0129 -0.0285 -0.3147 413  TYR A CD2 
2917 C  CE1 . TYR A 414 ? 1.8902 1.7010 1.2146 0.0337  -0.0844 -0.2868 413  TYR A CE1 
2918 C  CE2 . TYR A 414 ? 1.9722 1.9494 1.3294 0.0442  -0.0393 -0.3248 413  TYR A CE2 
2919 C  CZ  . TYR A 414 ? 1.8694 1.7588 1.1984 0.0689  -0.0678 -0.3099 413  TYR A CZ  
2920 O  OH  . TYR A 414 ? 1.7356 1.6151 1.0389 0.1291  -0.0786 -0.3184 413  TYR A OH  
2921 N  N   . ALA A 415 ? 1.9036 1.8132 1.3493 -0.0869 -0.0705 -0.2555 414  ALA A N   
2922 C  CA  . ALA A 415 ? 1.9260 1.7928 1.3739 -0.0824 -0.0911 -0.2361 414  ALA A CA  
2923 C  C   . ALA A 415 ? 1.9802 1.7719 1.3853 -0.0469 -0.1092 -0.2308 414  ALA A C   
2924 O  O   . ALA A 415 ? 2.0384 1.8495 1.4293 -0.0036 -0.1102 -0.2404 414  ALA A O   
2925 C  CB  . ALA A 415 ? 1.9321 1.8744 1.4160 -0.0742 -0.0889 -0.2372 414  ALA A CB  
2926 N  N   . THR A 416 ? 1.8656 1.5710 1.2484 -0.0646 -0.1240 -0.2176 415  THR A N   
2927 C  CA  . THR A 416 ? 1.8497 1.4697 1.1888 -0.0402 -0.1416 -0.2125 415  THR A CA  
2928 C  C   . THR A 416 ? 1.9439 1.5559 1.2849 -0.0235 -0.1489 -0.1965 415  THR A C   
2929 O  O   . THR A 416 ? 1.8939 1.5264 1.2658 -0.0493 -0.1483 -0.1816 415  THR A O   
2930 C  CB  . THR A 416 ? 1.6430 1.1817 0.9639 -0.0711 -0.1567 -0.2053 415  THR A CB  
2931 O  OG1 . THR A 416 ? 1.5875 1.1322 0.9435 -0.1065 -0.1608 -0.1876 415  THR A OG1 
2932 C  CG2 . THR A 416 ? 1.6618 1.2067 0.9729 -0.0846 -0.1505 -0.2188 415  THR A CG2 
2933 N  N   . PRO A 417 ? 2.1062 1.6833 1.4074 0.0230  -0.1554 -0.1992 416  PRO A N   
2934 C  CA  . PRO A 417 ? 2.2406 1.8014 1.5287 0.0475  -0.1619 -0.1823 416  PRO A CA  
2935 C  C   . PRO A 417 ? 2.3352 1.8010 1.6036 0.0178  -0.1726 -0.1576 416  PRO A C   
2936 O  O   . PRO A 417 ? 2.3777 1.7891 1.6409 -0.0159 -0.1787 -0.1581 416  PRO A O   
2937 C  CB  . PRO A 417 ? 2.3339 1.8680 1.5730 0.1104  -0.1667 -0.1946 416  PRO A CB  
2938 C  CG  . PRO A 417 ? 2.2249 1.8151 1.4752 0.1182  -0.1557 -0.2221 416  PRO A CG  
2939 C  CD  . PRO A 417 ? 2.1439 1.7054 1.4075 0.0625  -0.1544 -0.2200 416  PRO A CD  
2940 N  N   . PRO A 418 ? 2.2797 1.7307 1.5367 0.0289  -0.1743 -0.1370 417  PRO A N   
2941 C  CA  . PRO A 418 ? 2.3451 1.7141 1.5856 -0.0047 -0.1789 -0.1121 417  PRO A CA  
2942 C  C   . PRO A 418 ? 2.6664 1.9060 1.8435 0.0004  -0.1902 -0.1096 417  PRO A C   
2943 O  O   . PRO A 418 ? 2.7323 1.9369 1.8664 0.0447  -0.1954 -0.1245 417  PRO A O   
2944 C  CB  . PRO A 418 ? 2.2300 1.6204 1.4622 0.0172  -0.1749 -0.0923 417  PRO A CB  
2945 C  CG  . PRO A 418 ? 2.2676 1.7072 1.4842 0.0795  -0.1766 -0.1081 417  PRO A CG  
2946 C  CD  . PRO A 418 ? 2.1900 1.7121 1.4531 0.0691  -0.1706 -0.1361 417  PRO A CD  
2947 N  N   . GLY A 419 ? 2.7676 1.9393 1.9398 -0.0460 -0.1931 -0.0932 418  GLY A N   
2948 C  CA  . GLY A 419 ? 2.8132 1.8545 1.9249 -0.0525 -0.2032 -0.0909 418  GLY A CA  
2949 C  C   . GLY A 419 ? 2.9212 1.9379 2.0350 -0.0741 -0.2143 -0.1150 418  GLY A C   
2950 O  O   . GLY A 419 ? 3.0216 1.9322 2.0900 -0.0889 -0.2249 -0.1184 418  GLY A O   
2951 N  N   . SER A 420 ? 2.9986 2.1086 2.1599 -0.0770 -0.2119 -0.1323 419  SER A N   
2952 C  CA  . SER A 420 ? 3.0997 2.1944 2.2571 -0.0906 -0.2222 -0.1552 419  SER A CA  
2953 C  C   . SER A 420 ? 3.1320 2.3325 2.3458 -0.1044 -0.2153 -0.1647 419  SER A C   
2954 O  O   . SER A 420 ? 3.1896 2.4707 2.4287 -0.0825 -0.2014 -0.1646 419  SER A O   
2955 C  CB  . SER A 420 ? 3.1264 2.1665 2.2219 -0.0398 -0.2267 -0.1750 419  SER A CB  
2956 O  OG  . SER A 420 ? 3.0759 2.2018 2.1845 0.0052  -0.2139 -0.1843 419  SER A OG  
2957 N  N   . ASN A 421 ? 3.0570 2.2575 2.2876 -0.1396 -0.2252 -0.1736 420  ASN A N   
2958 C  CA  . ASN A 421 ? 2.8609 1.9871 2.0762 -0.1754 -0.2440 -0.1766 420  ASN A CA  
2959 C  C   . ASN A 421 ? 2.8470 2.0279 2.1029 -0.2060 -0.2515 -0.1845 420  ASN A C   
2960 O  O   . ASN A 421 ? 2.8184 2.0796 2.1133 -0.2047 -0.2396 -0.1802 420  ASN A O   
2961 C  CB  . ASN A 421 ? 2.6532 1.6848 1.7995 -0.1527 -0.2564 -0.1957 420  ASN A CB  
2962 C  CG  . ASN A 421 ? 2.6362 1.5803 1.7618 -0.1931 -0.2758 -0.1997 420  ASN A CG  
2963 O  OD1 . ASN A 421 ? 2.5605 1.5341 1.7289 -0.2388 -0.2851 -0.1986 420  ASN A OD1 
2964 N  ND2 . ASN A 421 ? 2.8094 1.6456 1.8683 -0.1757 -0.2824 -0.2066 420  ASN A ND2 
2965 N  N   . ASP A 422 ? 2.8678 2.0035 2.1113 -0.2322 -0.2725 -0.1973 421  ASP A N   
2966 C  CA  . ASP A 422 ? 2.6816 1.8619 1.9488 -0.2491 -0.2841 -0.2081 421  ASP A CA  
2967 C  C   . ASP A 422 ? 2.5841 1.7560 1.8053 -0.2124 -0.2807 -0.2252 421  ASP A C   
2968 O  O   . ASP A 422 ? 2.3538 1.4829 1.5365 -0.2113 -0.2980 -0.2445 421  ASP A O   
2969 C  CB  . ASP A 422 ? 2.5508 1.6961 1.8218 -0.2878 -0.3106 -0.2189 421  ASP A CB  
2970 C  CG  . ASP A 422 ? 2.3411 1.5453 1.6427 -0.3011 -0.3249 -0.2268 421  ASP A CG  
2971 O  OD1 . ASP A 422 ? 2.1775 1.4058 1.4612 -0.2752 -0.3201 -0.2323 421  ASP A OD1 
2972 O  OD2 . ASP A 422 ? 2.3680 1.5952 1.7100 -0.3367 -0.3402 -0.2273 421  ASP A OD2 
2973 N  N   . ASP A 423 ? 2.6702 1.8900 1.8975 -0.1840 -0.2573 -0.2194 422  ASP A N   
2974 C  CA  . ASP A 423 ? 2.6533 1.8615 1.8357 -0.1426 -0.2460 -0.2331 422  ASP A CA  
2975 C  C   . ASP A 423 ? 2.6221 1.8048 1.7590 -0.1325 -0.2540 -0.2543 422  ASP A C   
2976 O  O   . ASP A 423 ? 2.4195 1.6294 1.5644 -0.1483 -0.2580 -0.2562 422  ASP A O   
2977 C  CB  . ASP A 423 ? 2.6233 1.9155 1.8357 -0.1250 -0.2195 -0.2264 422  ASP A CB  
2978 C  CG  . ASP A 423 ? 2.5331 1.8490 1.7760 -0.1216 -0.2109 -0.2091 422  ASP A CG  
2979 O  OD1 . ASP A 423 ? 2.4845 1.7460 1.6975 -0.1016 -0.2156 -0.2070 422  ASP A OD1 
2980 O  OD2 . ASP A 423 ? 2.4862 1.8687 1.7762 -0.1371 -0.1998 -0.1976 422  ASP A OD2 
2981 N  N   . TRP A 424 ? 2.8223 1.9476 1.9045 -0.1015 -0.2561 -0.2702 423  TRP A N   
2982 C  CA  . TRP A 424 ? 3.0353 2.1382 2.0645 -0.0817 -0.2584 -0.2923 423  TRP A CA  
2983 C  C   . TRP A 424 ? 2.8370 2.0143 1.8715 -0.0541 -0.2275 -0.2939 423  TRP A C   
2984 O  O   . TRP A 424 ? 2.8873 2.0672 1.8822 -0.0372 -0.2194 -0.3095 423  TRP A O   
2985 C  CB  . TRP A 424 ? 3.4176 2.4259 2.3833 -0.0573 -0.2720 -0.3111 423  TRP A CB  
2986 C  CG  . TRP A 424 ? 3.7239 2.7214 2.6819 -0.0207 -0.2585 -0.3062 423  TRP A CG  
2987 C  CD1 . TRP A 424 ? 3.8591 2.8841 2.7933 0.0298  -0.2391 -0.3176 423  TRP A CD1 
2988 C  CD2 . TRP A 424 ? 3.8715 2.8329 2.8443 -0.0289 -0.2629 -0.2881 423  TRP A CD2 
2989 N  NE1 . TRP A 424 ? 3.9191 2.9273 2.8515 0.0586  -0.2350 -0.3088 423  TRP A NE1 
2990 C  CE2 . TRP A 424 ? 3.9693 2.9326 2.9200 0.0234  -0.2486 -0.2892 423  TRP A CE2 
2991 C  CE3 . TRP A 424 ? 3.9083 2.8394 2.9087 -0.0744 -0.2762 -0.2716 423  TRP A CE3 
2992 C  CZ2 . TRP A 424 ? 4.0684 2.9926 3.0154 0.0337  -0.2491 -0.2715 423  TRP A CZ2 
2993 C  CZ3 . TRP A 424 ? 4.0268 2.9196 3.0245 -0.0693 -0.2725 -0.2536 423  TRP A CZ3 
2994 C  CH2 . TRP A 424 ? 4.1136 2.9979 3.0805 -0.0142 -0.2599 -0.2526 423  TRP A CH2 
2995 N  N   . TYR A 425 ? 2.6095 1.8497 1.6925 -0.0520 -0.2097 -0.2789 424  TYR A N   
2996 C  CA  . TYR A 425 ? 2.4236 1.7484 1.5246 -0.0339 -0.1797 -0.2816 424  TYR A CA  
2997 C  C   . TYR A 425 ? 2.2830 1.6375 1.3751 -0.0511 -0.1675 -0.2854 424  TYR A C   
2998 O  O   . TYR A 425 ? 2.2863 1.6718 1.3545 -0.0314 -0.1459 -0.2986 424  TYR A O   
2999 C  CB  . TYR A 425 ? 2.3257 1.7173 1.4879 -0.0436 -0.1682 -0.2642 424  TYR A CB  
3000 C  CG  . TYR A 425 ? 2.1789 1.5593 1.3395 -0.0113 -0.1708 -0.2616 424  TYR A CG  
3001 C  CD1 . TYR A 425 ? 2.1316 1.4297 1.2740 -0.0153 -0.1921 -0.2520 424  TYR A CD1 
3002 C  CD2 . TYR A 425 ? 1.9912 1.4438 1.1662 0.0230  -0.1519 -0.2688 424  TYR A CD2 
3003 C  CE1 . TYR A 425 ? 2.0902 1.3640 1.2183 0.0172  -0.1937 -0.2464 424  TYR A CE1 
3004 C  CE2 . TYR A 425 ? 1.9640 1.4044 1.1302 0.0603  -0.1570 -0.2657 424  TYR A CE2 
3005 C  CZ  . TYR A 425 ? 2.0170 1.3610 1.1548 0.0587  -0.1776 -0.2527 424  TYR A CZ  
3006 O  OH  . TYR A 425 ? 1.9762 1.2937 1.0928 0.0983  -0.1821 -0.2464 424  TYR A OH  
3007 N  N   . TRP A 426 ? 2.2708 1.6147 1.3784 -0.0860 -0.1806 -0.2736 425  TRP A N   
3008 C  CA  . TRP A 426 ? 2.3343 1.6852 1.4181 -0.0988 -0.1732 -0.2746 425  TRP A CA  
3009 C  C   . TRP A 426 ? 2.4017 1.6855 1.4196 -0.0884 -0.1927 -0.2902 425  TRP A C   
3010 O  O   . TRP A 426 ? 2.4287 1.7137 1.4023 -0.0803 -0.1785 -0.2975 425  TRP A O   
3011 C  CB  . TRP A 426 ? 2.2351 1.6040 1.3578 -0.1321 -0.1798 -0.2564 425  TRP A CB  
3012 C  CG  . TRP A 426 ? 2.2652 1.5995 1.4091 -0.1491 -0.2125 -0.2505 425  TRP A CG  
3013 C  CD1 . TRP A 426 ? 2.3251 1.6102 1.4413 -0.1561 -0.2422 -0.2579 425  TRP A CD1 
3014 C  CD2 . TRP A 426 ? 2.3233 1.6776 1.5227 -0.1637 -0.2172 -0.2372 425  TRP A CD2 
3015 N  NE1 . TRP A 426 ? 2.2163 1.4952 1.3733 -0.1777 -0.2640 -0.2512 425  TRP A NE1 
3016 C  CE2 . TRP A 426 ? 2.2870 1.6051 1.4929 -0.1826 -0.2474 -0.2370 425  TRP A CE2 
3017 C  CE3 . TRP A 426 ? 2.5636 1.9665 1.8061 -0.1631 -0.1988 -0.2267 425  TRP A CE3 
3018 C  CZ2 . TRP A 426 ? 2.5423 1.8707 1.7963 -0.2029 -0.2554 -0.2248 425  TRP A CZ2 
3019 C  CZ3 . TRP A 426 ? 2.7528 2.1595 2.0363 -0.1792 -0.2088 -0.2137 425  TRP A CZ3 
3020 C  CH2 . TRP A 426 ? 2.8393 2.2085 2.1282 -0.1999 -0.2348 -0.2120 425  TRP A CH2 
3021 N  N   . LEU A 427 ? 2.2822 1.5062 1.2902 -0.0906 -0.2239 -0.2962 426  LEU A N   
3022 C  CA  . LEU A 427 ? 2.0651 1.2225 1.0090 -0.0813 -0.2463 -0.3158 426  LEU A CA  
3023 C  C   . LEU A 427 ? 2.1751 1.3191 1.0644 -0.0419 -0.2281 -0.3354 426  LEU A C   
3024 O  O   . LEU A 427 ? 2.3901 1.5161 1.2222 -0.0300 -0.2258 -0.3486 426  LEU A O   
3025 C  CB  . LEU A 427 ? 2.0553 1.1512 1.0028 -0.0968 -0.2810 -0.3215 426  LEU A CB  
3026 C  CG  . LEU A 427 ? 2.0938 1.1965 1.0789 -0.1347 -0.3076 -0.3124 426  LEU A CG  
3027 C  CD1 . LEU A 427 ? 1.9864 1.0320 0.9762 -0.1557 -0.3372 -0.3212 426  LEU A CD1 
3028 C  CD2 . LEU A 427 ? 2.2271 1.3311 1.1767 -0.1360 -0.3206 -0.3190 426  LEU A CD2 
3029 N  N   . TYR A 428 ? 1.9911 1.1461 0.8953 -0.0181 -0.2150 -0.3376 427  TYR A N   
3030 C  CA  . TYR A 428 ? 2.1455 1.3040 1.0067 0.0262  -0.1951 -0.3572 427  TYR A CA  
3031 C  C   . TYR A 428 ? 2.4166 1.6513 1.2777 0.0290  -0.1595 -0.3570 427  TYR A C   
3032 O  O   . TYR A 428 ? 2.8801 2.1057 1.6848 0.0503  -0.1478 -0.3742 427  TYR A O   
3033 C  CB  . TYR A 428 ? 2.0781 1.2482 0.9630 0.0552  -0.1880 -0.3565 427  TYR A CB  
3034 C  CG  . TYR A 428 ? 2.1627 1.3743 1.0238 0.1052  -0.1614 -0.3752 427  TYR A CG  
3035 C  CD1 . TYR A 428 ? 2.2828 1.4284 1.0754 0.1472  -0.1689 -0.4001 427  TYR A CD1 
3036 C  CD2 . TYR A 428 ? 2.1470 1.4680 1.0555 0.1106  -0.1289 -0.3708 427  TYR A CD2 
3037 C  CE1 . TYR A 428 ? 2.3349 1.5277 1.1083 0.1983  -0.1439 -0.4193 427  TYR A CE1 
3038 C  CE2 . TYR A 428 ? 2.1584 1.5344 1.0534 0.1562  -0.1040 -0.3908 427  TYR A CE2 
3039 C  CZ  . TYR A 428 ? 2.2406 1.5548 1.0688 0.2025  -0.1112 -0.4147 427  TYR A CZ  
3040 O  OH  . TYR A 428 ? 2.2323 1.6098 1.0492 0.2529  -0.0857 -0.4366 427  TYR A OH  
3041 N  N   . ALA A 429 ? 2.1805 1.4874 1.1015 0.0047  -0.1408 -0.3381 428  ALA A N   
3042 C  CA  . ALA A 429 ? 2.1043 1.4836 1.0300 -0.0014 -0.1031 -0.3370 428  ALA A CA  
3043 C  C   . ALA A 429 ? 2.2464 1.5915 1.1194 -0.0192 -0.1027 -0.3344 428  ALA A C   
3044 O  O   . ALA A 429 ? 2.2500 1.6176 1.0837 -0.0112 -0.0737 -0.3424 428  ALA A O   
3045 C  CB  . ALA A 429 ? 1.9335 1.3851 0.9317 -0.0280 -0.0872 -0.3193 428  ALA A CB  
3046 N  N   . ALA A 430 ? 1.9453 1.2387 0.8148 -0.0414 -0.1345 -0.3235 429  ALA A N   
3047 C  CA  . ALA A 430 ? 1.9912 1.2469 0.8038 -0.0513 -0.1407 -0.3208 429  ALA A CA  
3048 C  C   . ALA A 430 ? 2.3631 1.5682 1.0955 -0.0214 -0.1479 -0.3442 429  ALA A C   
3049 O  O   . ALA A 430 ? 2.2966 1.4994 0.9705 -0.0154 -0.1273 -0.3471 429  ALA A O   
3050 C  CB  . ALA A 430 ? 1.9719 1.1935 0.8031 -0.0747 -0.1783 -0.3083 429  ALA A CB  
3051 N  N   . ALA A 431 ? 2.3397 1.4989 1.0643 -0.0035 -0.1756 -0.3611 430  ALA A N   
3052 C  CA  . ALA A 431 ? 2.3534 1.4541 0.9996 0.0263  -0.1872 -0.3877 430  ALA A CA  
3053 C  C   . ALA A 431 ? 2.4161 1.5535 1.0333 0.0618  -0.1481 -0.4030 430  ALA A C   
3054 O  O   . ALA A 431 ? 2.4325 1.5487 0.9764 0.0813  -0.1388 -0.4186 430  ALA A O   
3055 C  CB  . ALA A 431 ? 2.2494 1.2833 0.8956 0.0316  -0.2254 -0.4021 430  ALA A CB  
3056 N  N   . LYS A 432 ? 2.1958 1.3934 0.8697 0.0723  -0.1258 -0.4002 431  LYS A N   
3057 C  CA  . LYS A 432 ? 2.3859 1.6381 1.0464 0.1092  -0.0891 -0.4174 431  LYS A CA  
3058 C  C   . LYS A 432 ? 2.5110 1.8225 1.1536 0.0944  -0.0475 -0.4118 431  LYS A C   
3059 O  O   . LYS A 432 ? 2.6702 2.0028 1.2654 0.1218  -0.0202 -0.4302 431  LYS A O   
3060 C  CB  . LYS A 432 ? 2.2252 1.5421 0.9575 0.1222  -0.0774 -0.4143 431  LYS A CB  
3061 C  CG  . LYS A 432 ? 2.3568 1.7310 1.0788 0.1718  -0.0483 -0.4378 431  LYS A CG  
3062 C  CD  . LYS A 432 ? 2.6338 1.9220 1.2893 0.2208  -0.0711 -0.4633 431  LYS A CD  
3063 C  CE  . LYS A 432 ? 2.7662 2.1154 1.4146 0.2795  -0.0441 -0.4880 431  LYS A CE  
3064 N  NZ  . LYS A 432 ? 2.9052 2.1574 1.4820 0.3320  -0.0673 -0.5139 431  LYS A NZ  
3065 N  N   . LEU A 433 ? 2.4349 1.7687 1.1113 0.0508  -0.0411 -0.3862 432  LEU A N   
3066 C  CA  . LEU A 433 ? 2.4822 1.8555 1.1361 0.0283  -0.0008 -0.3762 432  LEU A CA  
3067 C  C   . LEU A 433 ? 2.4910 1.7865 1.0617 0.0211  -0.0161 -0.3704 432  LEU A C   
3068 O  O   . LEU A 433 ? 2.3233 1.6270 0.8500 0.0060  0.0158  -0.3609 432  LEU A O   
3069 C  CB  . LEU A 433 ? 2.4719 1.9008 1.1969 -0.0137 0.0163  -0.3526 432  LEU A CB  
3070 C  CG  . LEU A 433 ? 2.2531 1.7874 1.0514 -0.0142 0.0486  -0.3587 432  LEU A CG  
3071 C  CD1 . LEU A 433 ? 2.3160 1.9159 1.0887 0.0004  0.0952  -0.3769 432  LEU A CD1 
3072 C  CD2 . LEU A 433 ? 2.0728 1.6115 0.9155 0.0166  0.0204  -0.3688 432  LEU A CD2 
3073 N  N   . LYS A 434 ? 2.6480 1.8681 1.1961 0.0301  -0.0653 -0.3762 433  LYS A N   
3074 C  CA  . LYS A 434 ? 2.6651 1.8141 1.1382 0.0270  -0.0908 -0.3738 433  LYS A CA  
3075 C  C   . LYS A 434 ? 2.6636 1.8176 1.1418 -0.0072 -0.0816 -0.3437 433  LYS A C   
3076 O  O   . LYS A 434 ? 2.7764 1.8887 1.1789 -0.0077 -0.0817 -0.3363 433  LYS A O   
3077 C  CB  . LYS A 434 ? 2.6839 1.8107 1.0620 0.0570  -0.0725 -0.3938 433  LYS A CB  
3078 C  CG  . LYS A 434 ? 2.7582 1.8485 1.1104 0.0953  -0.0952 -0.4266 433  LYS A CG  
3079 C  CD  . LYS A 434 ? 2.8603 1.9434 1.1261 0.1289  -0.0699 -0.4479 433  LYS A CD  
3080 C  CE  . LYS A 434 ? 2.8557 2.0286 1.1409 0.1339  -0.0087 -0.4472 433  LYS A CE  
3081 N  NZ  . LYS A 434 ? 2.9153 2.0935 1.1274 0.1732  0.0179  -0.4731 433  LYS A NZ  
3082 N  N   . CYS A 435 ? 2.4425 1.6430 1.0044 -0.0328 -0.0736 -0.3268 434  CYS A N   
3083 C  CA  . CYS A 435 ? 2.3921 1.5980 0.9640 -0.0645 -0.0597 -0.2995 434  CYS A CA  
3084 C  C   . CYS A 435 ? 2.2885 1.4592 0.8871 -0.0757 -0.1058 -0.2870 434  CYS A C   
3085 O  O   . CYS A 435 ? 2.1718 1.3104 0.7707 -0.0629 -0.1488 -0.3000 434  CYS A O   
3086 C  CB  . CYS A 435 ? 2.4290 1.7126 1.0731 -0.0872 -0.0192 -0.2917 434  CYS A CB  
3087 S  SG  . CYS A 435 ? 2.2290 1.5570 0.9834 -0.0913 -0.0424 -0.2929 434  CYS A SG  
3088 N  N   . LEU A 436 ? 2.2994 1.4787 0.9222 -0.1007 -0.0954 -0.2637 435  LEU A N   
3089 C  CA  . LEU A 436 ? 2.3164 1.4723 0.9653 -0.1083 -0.1349 -0.2514 435  LEU A CA  
3090 C  C   . LEU A 436 ? 2.1849 1.3829 0.9319 -0.1188 -0.1513 -0.2534 435  LEU A C   
3091 O  O   . LEU A 436 ? 2.1031 1.3508 0.9003 -0.1251 -0.1253 -0.2563 435  LEU A O   
3092 C  CB  . LEU A 436 ? 2.3423 1.4802 0.9680 -0.1252 -0.1168 -0.2261 435  LEU A CB  
3093 C  CG  . LEU A 436 ? 2.4692 1.5429 0.9861 -0.1143 -0.1115 -0.2156 435  LEU A CG  
3094 C  CD1 . LEU A 436 ? 2.5766 1.6517 1.0328 -0.1150 -0.0632 -0.2198 435  LEU A CD1 
3095 C  CD2 . LEU A 436 ? 2.4110 1.4540 0.9147 -0.1273 -0.1063 -0.1893 435  LEU A CD2 
3096 N  N   . LEU A 437 ? 2.1506 1.3325 0.9232 -0.1199 -0.1945 -0.2526 436  LEU A N   
3097 C  CA  . LEU A 437 ? 2.1590 1.3766 1.0198 -0.1337 -0.2089 -0.2500 436  LEU A CA  
3098 C  C   . LEU A 437 ? 2.3111 1.5331 1.2003 -0.1457 -0.2257 -0.2333 436  LEU A C   
3099 O  O   . LEU A 437 ? 2.6830 1.8725 1.5299 -0.1363 -0.2516 -0.2318 436  LEU A O   
3100 C  CB  . LEU A 437 ? 2.1452 1.3452 1.0192 -0.1270 -0.2437 -0.2687 436  LEU A CB  
3101 C  CG  . LEU A 437 ? 2.0100 1.2404 0.9670 -0.1429 -0.2543 -0.2647 436  LEU A CG  
3102 C  CD1 . LEU A 437 ? 1.9396 1.1952 0.9214 -0.1365 -0.2265 -0.2681 436  LEU A CD1 
3103 C  CD2 . LEU A 437 ? 2.0770 1.2789 1.0427 -0.1485 -0.2974 -0.2779 436  LEU A CD2 
3104 N  N   . VAL A 438 ? 1.9435 1.2073 0.9012 -0.1624 -0.2123 -0.2222 437  VAL A N   
3105 C  CA  . VAL A 438 ? 1.7809 1.0525 0.7690 -0.1700 -0.2268 -0.2084 437  VAL A CA  
3106 C  C   . VAL A 438 ? 1.9352 1.2435 1.0023 -0.1805 -0.2491 -0.2108 437  VAL A C   
3107 O  O   . VAL A 438 ? 2.0025 1.3463 1.1210 -0.1915 -0.2312 -0.2083 437  VAL A O   
3108 C  CB  . VAL A 438 ? 1.7605 1.0440 0.7544 -0.1826 -0.1907 -0.1928 437  VAL A CB  
3109 C  CG1 . VAL A 438 ? 1.7672 1.0355 0.7609 -0.1794 -0.2075 -0.1798 437  VAL A CG1 
3110 C  CG2 . VAL A 438 ? 1.8299 1.0864 0.7540 -0.1824 -0.1556 -0.1912 437  VAL A CG2 
3111 N  N   . THR A 439 ? 1.9383 1.2410 1.0132 -0.1775 -0.2881 -0.2162 438  THR A N   
3112 C  CA  . THR A 439 ? 1.9662 1.3028 1.1124 -0.1925 -0.3089 -0.2196 438  THR A CA  
3113 C  C   . THR A 439 ? 2.0257 1.3713 1.1805 -0.1892 -0.3475 -0.2236 438  THR A C   
3114 O  O   . THR A 439 ? 2.0427 1.3586 1.1394 -0.1716 -0.3661 -0.2293 438  THR A O   
3115 C  CB  . THR A 439 ? 2.0356 1.3560 1.1849 -0.1982 -0.3166 -0.2344 438  THR A CB  
3116 O  OG1 . THR A 439 ? 2.3550 1.6665 1.4812 -0.1899 -0.2841 -0.2348 438  THR A OG1 
3117 C  CG2 . THR A 439 ? 1.8378 1.1886 1.0585 -0.2197 -0.3256 -0.2321 438  THR A CG2 
3118 N  N   . ASN A 440 ? 2.0396 1.4317 1.2659 -0.2040 -0.3590 -0.2211 439  ASN A N   
3119 C  CA  . ASN A 440 ? 2.0809 1.5009 1.3289 -0.2011 -0.3964 -0.2285 439  ASN A CA  
3120 C  C   . ASN A 440 ? 1.8819 1.3133 1.1633 -0.2244 -0.4235 -0.2468 439  ASN A C   
3121 O  O   . ASN A 440 ? 1.7007 1.1705 1.0154 -0.2306 -0.4562 -0.2580 439  ASN A O   
3122 C  CB  . ASN A 440 ? 2.1207 1.5924 1.4266 -0.2016 -0.3898 -0.2156 439  ASN A CB  
3123 C  CG  . ASN A 440 ? 2.0672 1.5499 1.3556 -0.1749 -0.4151 -0.2159 439  ASN A CG  
3124 O  OD1 . ASN A 440 ? 1.9476 1.3822 1.1611 -0.1504 -0.4188 -0.2137 439  ASN A OD1 
3125 N  ND2 . ASN A 440 ? 2.1686 1.7151 1.5224 -0.1766 -0.4316 -0.2181 439  ASN A ND2 
3126 N  N   . ASP A 441 ? 1.8487 1.2458 1.1188 -0.2370 -0.4099 -0.2513 440  ASP A N   
3127 C  CA  . ASP A 441 ? 2.1752 1.5649 1.4688 -0.2634 -0.4309 -0.2675 440  ASP A CA  
3128 C  C   . ASP A 441 ? 2.5046 1.8607 1.7479 -0.2584 -0.4664 -0.2922 440  ASP A C   
3129 O  O   . ASP A 441 ? 2.5666 1.8684 1.7393 -0.2392 -0.4616 -0.2994 440  ASP A O   
3130 C  CB  . ASP A 441 ? 2.3418 1.6936 1.6298 -0.2721 -0.4050 -0.2635 440  ASP A CB  
3131 C  CG  . ASP A 441 ? 2.2361 1.6218 1.5920 -0.2977 -0.3912 -0.2500 440  ASP A CG  
3132 O  OD1 . ASP A 441 ? 2.0784 1.5064 1.4868 -0.3218 -0.4092 -0.2530 440  ASP A OD1 
3133 O  OD2 . ASP A 441 ? 2.1964 1.5709 1.5523 -0.2928 -0.3621 -0.2373 440  ASP A OD2 
3134 N  N   . GLU A 442 ? 2.6799 2.0745 1.9608 -0.2762 -0.5021 -0.3075 441  GLU A N   
3135 C  CA  . GLU A 442 ? 2.9276 2.2956 2.1700 -0.2800 -0.5405 -0.3364 441  GLU A CA  
3136 C  C   . GLU A 442 ? 2.9006 2.2048 2.1245 -0.3033 -0.5343 -0.3485 441  GLU A C   
3137 O  O   . GLU A 442 ? 3.0679 2.3255 2.2391 -0.2935 -0.5456 -0.3670 441  GLU A O   
3138 C  CB  . GLU A 442 ? 3.1678 2.6077 2.4681 -0.2986 -0.5803 -0.3530 441  GLU A CB  
3139 C  CG  . GLU A 442 ? 3.3431 2.8240 2.7280 -0.3480 -0.5786 -0.3556 441  GLU A CG  
3140 C  CD  . GLU A 442 ? 3.3411 2.8603 2.7821 -0.3518 -0.5409 -0.3260 441  GLU A CD  
3141 O  OE1 . GLU A 442 ? 3.3613 2.8911 2.7884 -0.3174 -0.5227 -0.3068 441  GLU A OE1 
3142 O  OE2 . GLU A 442 ? 3.3224 2.8560 2.8163 -0.3906 -0.5289 -0.3223 441  GLU A OE2 
3143 N  N   . MET A 443 ? 2.7164 2.0263 1.9904 -0.3280 -0.5095 -0.3337 442  MET A N   
3144 C  CA  . MET A 443 ? 2.4603 1.7031 1.7178 -0.3476 -0.4982 -0.3383 442  MET A CA  
3145 C  C   . MET A 443 ? 2.2103 1.4270 1.4643 -0.3720 -0.5247 -0.3653 442  MET A C   
3146 O  O   . MET A 443 ? 2.2932 1.4369 1.5035 -0.3687 -0.5173 -0.3740 442  MET A O   
3147 C  CB  . MET A 443 ? 2.4410 1.6248 1.6334 -0.3114 -0.4694 -0.3310 442  MET A CB  
3148 C  CG  . MET A 443 ? 2.4483 1.5902 1.5594 -0.2789 -0.4800 -0.3487 442  MET A CG  
3149 S  SD  . MET A 443 ? 3.2240 2.3364 2.2822 -0.2369 -0.4362 -0.3353 442  MET A SD  
3150 C  CE  . MET A 443 ? 1.8802 1.0696 0.9832 -0.2284 -0.4104 -0.3054 442  MET A CE  
3151 N  N   . ARG A 444 ? 2.3171 1.6016 1.6234 -0.3940 -0.5521 -0.3785 443  ARG A N   
3152 C  CA  . ARG A 444 ? 2.5290 1.8079 1.8465 -0.4212 -0.5737 -0.4058 443  ARG A CA  
3153 C  C   . ARG A 444 ? 2.8037 2.0713 2.1716 -0.4727 -0.5604 -0.4017 443  ARG A C   
3154 O  O   . ARG A 444 ? 2.7852 2.1208 2.2244 -0.5127 -0.5721 -0.4097 443  ARG A O   
3155 C  CB  . ARG A 444 ? 2.4181 1.7836 1.7704 -0.4223 -0.6104 -0.4261 443  ARG A CB  
3156 C  CG  . ARG A 444 ? 2.3066 1.7710 1.7373 -0.4375 -0.6183 -0.4165 443  ARG A CG  
3157 C  CD  . ARG A 444 ? 2.3229 1.8783 1.7995 -0.4476 -0.6579 -0.4444 443  ARG A CD  
3158 N  NE  . ARG A 444 ? 2.4135 1.9610 1.9088 -0.4887 -0.6687 -0.4736 443  ARG A NE  
3159 C  CZ  . ARG A 444 ? 2.3766 2.0125 1.9482 -0.5283 -0.6900 -0.4976 443  ARG A CZ  
3160 N  NH1 . ARG A 444 ? 2.3210 2.0664 1.9598 -0.5286 -0.7044 -0.4954 443  ARG A NH1 
3161 N  NH2 . ARG A 444 ? 2.4357 2.0528 2.0175 -0.5677 -0.6970 -0.5260 443  ARG A NH2 
3162 N  N   . ASP A 445 ? 2.9676 2.1464 2.2930 -0.4698 -0.5348 -0.3893 444  ASP A N   
3163 C  CA  . ASP A 445 ? 2.9788 2.1214 2.3301 -0.5130 -0.5176 -0.3799 444  ASP A CA  
3164 C  C   . ASP A 445 ? 3.2615 2.2914 2.5475 -0.5109 -0.5130 -0.3916 444  ASP A C   
3165 O  O   . ASP A 445 ? 3.3339 2.3122 2.5519 -0.4684 -0.5146 -0.4001 444  ASP A O   
3166 C  CB  . ASP A 445 ? 2.8151 1.9567 2.1759 -0.5090 -0.4894 -0.3472 444  ASP A CB  
3167 C  CG  . ASP A 445 ? 2.8140 1.9052 2.1864 -0.5497 -0.4687 -0.3327 444  ASP A CG  
3168 O  OD1 . ASP A 445 ? 2.8661 1.8525 2.1752 -0.5388 -0.4574 -0.3308 444  ASP A OD1 
3169 O  OD2 . ASP A 445 ? 2.7699 1.9242 2.2102 -0.5903 -0.4629 -0.3225 444  ASP A OD2 
3170 N  N   . HIS A 446 ? 3.5012 2.4916 2.8056 -0.5569 -0.5051 -0.3911 445  HIS A N   
3171 C  CA  . HIS A 446 ? 3.7193 2.6000 2.9664 -0.5638 -0.5041 -0.4053 445  HIS A CA  
3172 C  C   . HIS A 446 ? 3.6943 2.4740 2.8539 -0.5129 -0.4877 -0.3945 445  HIS A C   
3173 O  O   . HIS A 446 ? 3.7989 2.5096 2.8954 -0.4876 -0.4954 -0.4142 445  HIS A O   
3174 C  CB  . HIS A 446 ? 3.8540 2.7057 3.1347 -0.6238 -0.4909 -0.3976 445  HIS A CB  
3175 C  CG  . HIS A 446 ? 3.8932 2.8597 3.2709 -0.6748 -0.5011 -0.4056 445  HIS A CG  
3176 N  ND1 . HIS A 446 ? 3.9126 2.9468 3.3271 -0.6902 -0.5313 -0.4407 445  HIS A ND1 
3177 C  CD2 . HIS A 446 ? 3.8824 2.9155 3.3285 -0.7110 -0.4854 -0.3849 445  HIS A CD2 
3178 C  CE1 . HIS A 446 ? 3.8716 3.0115 3.3763 -0.7327 -0.5349 -0.4428 445  HIS A CE1 
3179 N  NE2 . HIS A 446 ? 3.8761 3.0178 3.4019 -0.7466 -0.5059 -0.4085 445  HIS A NE2 
3180 N  N   . ILE A 447 ? 3.4979 2.2726 2.6543 -0.4974 -0.4655 -0.3656 446  ILE A N   
3181 C  CA  . ILE A 447 ? 3.4731 2.1666 2.5529 -0.4459 -0.4500 -0.3571 446  ILE A CA  
3182 C  C   . ILE A 447 ? 3.4520 2.1694 2.4955 -0.3945 -0.4589 -0.3733 446  ILE A C   
3183 O  O   . ILE A 447 ? 3.3777 2.0229 2.3509 -0.3566 -0.4574 -0.3865 446  ILE A O   
3184 C  CB  . ILE A 447 ? 2.4304 1.1343 1.5206 -0.4385 -0.4274 -0.3266 446  ILE A CB  
3185 C  CG1 . ILE A 447 ? 2.4918 1.1370 1.5873 -0.4792 -0.4121 -0.3066 446  ILE A CG1 
3186 C  CG2 . ILE A 447 ? 2.3452 0.9965 1.3651 -0.3763 -0.4146 -0.3248 446  ILE A CG2 
3187 C  CD1 . ILE A 447 ? 2.4613 1.1714 1.6365 -0.5454 -0.4156 -0.3043 446  ILE A CD1 
3188 N  N   . PHE A 448 ? 3.4954 2.3131 2.5841 -0.3926 -0.4667 -0.3715 447  PHE A N   
3189 C  CA  . PHE A 448 ? 3.5319 2.3781 2.5873 -0.3496 -0.4731 -0.3833 447  PHE A CA  
3190 C  C   . PHE A 448 ? 4.0372 2.8671 3.0661 -0.3483 -0.4963 -0.4126 447  PHE A C   
3191 O  O   . PHE A 448 ? 4.1120 2.9022 3.0763 -0.3084 -0.4950 -0.4256 447  PHE A O   
3192 C  CB  . PHE A 448 ? 3.4364 2.3837 2.5418 -0.3501 -0.4759 -0.3713 447  PHE A CB  
3193 C  CG  . PHE A 448 ? 3.2605 2.2293 2.3859 -0.3463 -0.4529 -0.3455 447  PHE A CG  
3194 C  CD1 . PHE A 448 ? 3.1790 2.1494 2.2740 -0.2994 -0.4254 -0.3338 447  PHE A CD1 
3195 C  CD2 . PHE A 448 ? 3.1405 2.1615 2.3393 -0.3823 -0.4462 -0.3265 447  PHE A CD2 
3196 C  CE1 . PHE A 448 ? 3.0804 2.1011 2.2168 -0.2895 -0.3951 -0.3055 447  PHE A CE1 
3197 C  CE2 . PHE A 448 ? 3.0286 2.0948 2.2634 -0.3693 -0.4149 -0.2968 447  PHE A CE2 
3198 C  CZ  . PHE A 448 ? 3.0161 2.0813 2.2196 -0.3233 -0.3909 -0.2871 447  PHE A CZ  
3199 N  N   . GLU A 449 ? 4.5081 3.3737 3.5878 -0.3925 -0.5170 -0.4249 448  GLU A N   
3200 C  CA  . GLU A 449 ? 4.9233 3.7896 3.9867 -0.3965 -0.5434 -0.4562 448  GLU A CA  
3201 C  C   . GLU A 449 ? 5.3102 4.0700 4.3108 -0.3927 -0.5430 -0.4753 448  GLU A C   
3202 O  O   . GLU A 449 ? 5.6367 4.3809 4.5977 -0.3778 -0.5602 -0.5013 448  GLU A O   
3203 C  CB  . GLU A 449 ? 4.9499 3.8942 4.0915 -0.4471 -0.5661 -0.4685 448  GLU A CB  
3204 C  CG  . GLU A 449 ? 4.9827 3.9583 4.1140 -0.4450 -0.5982 -0.5021 448  GLU A CG  
3205 C  CD  . GLU A 449 ? 4.9364 3.9364 4.0204 -0.3910 -0.6039 -0.5003 448  GLU A CD  
3206 O  OE1 . GLU A 449 ? 4.8174 3.8712 3.9220 -0.3735 -0.5961 -0.4776 448  GLU A OE1 
3207 O  OE2 . GLU A 449 ? 5.0071 3.9683 4.0295 -0.3668 -0.6148 -0.5213 448  GLU A OE2 
3208 N  N   . LEU A 450 ? 4.7887 3.4720 3.7769 -0.4065 -0.5250 -0.4632 449  LEU A N   
3209 C  CA  . LEU A 450 ? 4.3633 2.9327 3.2804 -0.3944 -0.5233 -0.4793 449  LEU A CA  
3210 C  C   . LEU A 450 ? 4.0711 2.6118 2.9144 -0.3281 -0.5162 -0.4849 449  LEU A C   
3211 O  O   . LEU A 450 ? 4.0859 2.5813 2.8757 -0.3091 -0.5270 -0.5105 449  LEU A O   
3212 C  CB  . LEU A 450 ? 4.2550 2.7385 3.1593 -0.4115 -0.5030 -0.4599 449  LEU A CB  
3213 C  CG  . LEU A 450 ? 4.1149 2.5498 3.0362 -0.4705 -0.5101 -0.4719 449  LEU A CG  
3214 C  CD1 . LEU A 450 ? 4.1249 2.4849 2.9853 -0.4612 -0.5259 -0.5062 449  LEU A CD1 
3215 C  CD2 . LEU A 450 ? 3.9674 2.5127 2.9846 -0.5277 -0.5237 -0.4765 449  LEU A CD2 
3216 N  N   . LEU A 451 ? 3.7931 2.3646 2.6347 -0.2947 -0.4968 -0.4627 450  LEU A N   
3217 C  CA  . LEU A 451 ? 3.5360 2.1071 2.3199 -0.2358 -0.4866 -0.4680 450  LEU A CA  
3218 C  C   . LEU A 451 ? 3.4623 2.1084 2.2547 -0.2306 -0.5029 -0.4795 450  LEU A C   
3219 O  O   . LEU A 451 ? 3.4453 2.0750 2.1800 -0.1941 -0.5036 -0.4958 450  LEU A O   
3220 C  CB  . LEU A 451 ? 3.2477 1.8402 2.0327 -0.2071 -0.4605 -0.4442 450  LEU A CB  
3221 C  CG  . LEU A 451 ? 3.1977 1.7059 1.9216 -0.1658 -0.4412 -0.4440 450  LEU A CG  
3222 C  CD1 . LEU A 451 ? 3.3015 1.7320 2.0296 -0.1958 -0.4418 -0.4347 450  LEU A CD1 
3223 C  CD2 . LEU A 451 ? 2.8949 1.4468 1.6153 -0.1287 -0.4168 -0.4299 450  LEU A CD2 
3224 N  N   . GLY A 452 ? 3.4906 2.2179 2.3514 -0.2643 -0.5153 -0.4703 451  GLY A N   
3225 C  CA  . GLY A 452 ? 3.5308 2.3294 2.3987 -0.2565 -0.5324 -0.4772 451  GLY A CA  
3226 C  C   . GLY A 452 ? 3.6926 2.4678 2.5257 -0.2576 -0.5574 -0.5091 451  GLY A C   
3227 O  O   . GLY A 452 ? 3.9199 2.6644 2.7691 -0.2930 -0.5724 -0.5268 451  GLY A O   
3228 N  N   . SER A 453 ? 3.6161 2.4042 2.3983 -0.2205 -0.5609 -0.5172 452  SER A N   
3229 C  CA  . SER A 453 ? 3.5581 2.3164 2.2932 -0.2142 -0.5824 -0.5485 452  SER A CA  
3230 C  C   . SER A 453 ? 3.2363 2.0556 1.9569 -0.1984 -0.6024 -0.5545 452  SER A C   
3231 O  O   . SER A 453 ? 3.0922 1.9842 1.8629 -0.2127 -0.6152 -0.5433 452  SER A O   
3232 C  CB  . SER A 453 ? 3.8173 2.4948 2.4722 -0.1732 -0.5627 -0.5577 452  SER A CB  
3233 O  OG  . SER A 453 ? 3.7635 2.4520 2.3951 -0.1349 -0.5312 -0.5355 452  SER A OG  
3234 N  N   . THR A 454 ? 3.1696 1.9545 1.8159 -0.1662 -0.6055 -0.5726 453  THR A N   
3235 C  CA  . THR A 454 ? 3.0772 1.9028 1.6861 -0.1409 -0.6196 -0.5755 453  THR A CA  
3236 C  C   . THR A 454 ? 2.9562 1.7824 1.5223 -0.0997 -0.5847 -0.5490 453  THR A C   
3237 O  O   . THR A 454 ? 2.9572 1.8266 1.5117 -0.0840 -0.5853 -0.5332 453  THR A O   
3238 C  CB  . THR A 454 ? 3.1698 1.9577 1.7166 -0.1293 -0.6397 -0.6094 453  THR A CB  
3239 O  OG1 . THR A 454 ? 3.1968 1.9113 1.6799 -0.0988 -0.6134 -0.6150 453  THR A OG1 
3240 C  CG2 . THR A 454 ? 3.2303 2.0168 1.8214 -0.1770 -0.6716 -0.6390 453  THR A CG2 
3241 N  N   . PHE A 455 ? 3.0862 1.8630 1.6278 -0.0830 -0.5535 -0.5452 454  PHE A N   
3242 C  CA  . PHE A 455 ? 3.0746 1.8563 1.5839 -0.0497 -0.5148 -0.5240 454  PHE A CA  
3243 C  C   . PHE A 455 ? 2.9381 1.7722 1.5066 -0.0666 -0.5043 -0.4941 454  PHE A C   
3244 O  O   . PHE A 455 ? 3.0170 1.8792 1.5640 -0.0484 -0.4841 -0.4752 454  PHE A O   
3245 C  CB  . PHE A 455 ? 3.1749 1.9000 1.6551 -0.0288 -0.4881 -0.5316 454  PHE A CB  
3246 C  CG  . PHE A 455 ? 3.1783 1.9207 1.6354 0.0021  -0.4462 -0.5142 454  PHE A CG  
3247 C  CD1 . PHE A 455 ? 3.1678 1.9507 1.5939 0.0186  -0.4298 -0.5005 454  PHE A CD1 
3248 C  CD2 . PHE A 455 ? 3.1893 1.9070 1.6527 0.0143  -0.4224 -0.5123 454  PHE A CD2 
3249 C  CE1 . PHE A 455 ? 3.1451 1.9493 1.5531 0.0399  -0.3883 -0.4869 454  PHE A CE1 
3250 C  CE2 . PHE A 455 ? 3.0658 1.8120 1.5129 0.0413  -0.3838 -0.5009 454  PHE A CE2 
3251 C  CZ  . PHE A 455 ? 3.0095 1.8020 1.4316 0.0509  -0.3654 -0.4890 454  PHE A CZ  
3252 N  N   . PHE A 456 ? 2.8202 1.6647 1.4600 -0.1030 -0.5164 -0.4900 455  PHE A N   
3253 C  CA  . PHE A 456 ? 2.7906 1.6822 1.4885 -0.1195 -0.5057 -0.4632 455  PHE A CA  
3254 C  C   . PHE A 456 ? 2.4262 1.3755 1.1342 -0.1189 -0.5195 -0.4505 455  PHE A C   
3255 O  O   . PHE A 456 ? 2.4515 1.4243 1.1580 -0.1089 -0.4980 -0.4277 455  PHE A O   
3256 C  CB  . PHE A 456 ? 2.7867 1.6793 1.5567 -0.1611 -0.5177 -0.4629 455  PHE A CB  
3257 C  CG  . PHE A 456 ? 2.7676 1.6877 1.5861 -0.1729 -0.4971 -0.4368 455  PHE A CG  
3258 C  CD1 . PHE A 456 ? 2.6458 1.5478 1.4358 -0.1476 -0.4633 -0.4252 455  PHE A CD1 
3259 C  CD2 . PHE A 456 ? 2.6713 1.6399 1.5654 -0.2097 -0.5113 -0.4267 455  PHE A CD2 
3260 C  CE1 . PHE A 456 ? 2.4266 1.3557 1.2589 -0.1589 -0.4455 -0.4037 455  PHE A CE1 
3261 C  CE2 . PHE A 456 ? 2.2811 1.2739 1.2168 -0.2201 -0.4920 -0.4034 455  PHE A CE2 
3262 C  CZ  . PHE A 456 ? 2.1873 1.1579 1.0902 -0.1949 -0.4599 -0.3921 455  PHE A CZ  
3263 N  N   . GLN A 457 ? 2.4660 1.4349 1.1784 -0.1273 -0.5554 -0.4667 456  GLN A N   
3264 C  CA  . GLN A 457 ? 2.5344 1.5518 1.2443 -0.1179 -0.5743 -0.4578 456  GLN A CA  
3265 C  C   . GLN A 457 ? 2.6420 1.6381 1.2654 -0.0770 -0.5548 -0.4471 456  GLN A C   
3266 O  O   . GLN A 457 ? 2.5913 1.6102 1.2007 -0.0639 -0.5525 -0.4270 456  GLN A O   
3267 C  CB  . GLN A 457 ? 2.8550 1.9023 1.5862 -0.1334 -0.6193 -0.4830 456  GLN A CB  
3268 C  CG  . GLN A 457 ? 3.0552 2.1603 1.8822 -0.1744 -0.6405 -0.4852 456  GLN A CG  
3269 C  CD  . GLN A 457 ? 3.0235 2.1080 1.9021 -0.2054 -0.6175 -0.4775 456  GLN A CD  
3270 O  OE1 . GLN A 457 ? 3.1393 2.1623 1.9919 -0.2074 -0.6027 -0.4869 456  GLN A OE1 
3271 N  NE2 . GLN A 457 ? 2.7491 1.8823 1.6965 -0.2267 -0.6149 -0.4602 456  GLN A NE2 
3272 N  N   . LYS A 458 ? 2.8568 1.8060 1.4180 -0.0567 -0.5399 -0.4608 457  LYS A N   
3273 C  CA  . LYS A 458 ? 2.9586 1.8879 1.4355 -0.0210 -0.5144 -0.4510 457  LYS A CA  
3274 C  C   . LYS A 458 ? 2.8556 1.7902 1.3333 -0.0175 -0.4711 -0.4249 457  LYS A C   
3275 O  O   . LYS A 458 ? 2.9263 1.8676 1.3657 -0.0044 -0.4550 -0.4040 457  LYS A O   
3276 C  CB  . LYS A 458 ? 3.0001 1.8839 1.4161 -0.0004 -0.5053 -0.4741 457  LYS A CB  
3277 C  CG  . LYS A 458 ? 3.0344 1.9077 1.4304 -0.0006 -0.5454 -0.5024 457  LYS A CG  
3278 C  CD  . LYS A 458 ? 3.1526 1.9739 1.5028 0.0137  -0.5360 -0.5281 457  LYS A CD  
3279 C  CE  . LYS A 458 ? 3.1666 1.9692 1.4453 0.0499  -0.4924 -0.5189 457  LYS A CE  
3280 N  NZ  . LYS A 458 ? 3.2985 2.0538 1.5389 0.0679  -0.4805 -0.5442 457  LYS A NZ  
3281 N  N   . TRP A 459 ? 2.6698 1.5984 1.1884 -0.0304 -0.4526 -0.4265 458  TRP A N   
3282 C  CA  . TRP A 459 ? 2.5582 1.4987 1.0841 -0.0297 -0.4124 -0.4068 458  TRP A CA  
3283 C  C   . TRP A 459 ? 2.4958 1.4727 1.0675 -0.0494 -0.4160 -0.3830 458  TRP A C   
3284 O  O   . TRP A 459 ? 2.5315 1.5168 1.0813 -0.0452 -0.3853 -0.3638 458  TRP A O   
3285 C  CB  . TRP A 459 ? 2.5851 1.5110 1.1446 -0.0354 -0.3985 -0.4161 458  TRP A CB  
3286 C  CG  . TRP A 459 ? 2.5889 1.5288 1.1400 -0.0256 -0.3545 -0.4045 458  TRP A CG  
3287 C  CD1 . TRP A 459 ? 2.4155 1.3513 0.9086 0.0023  -0.3189 -0.4102 458  TRP A CD1 
3288 C  CD2 . TRP A 459 ? 2.4286 1.3981 1.0328 -0.0452 -0.3404 -0.3873 458  TRP A CD2 
3289 N  NE1 . TRP A 459 ? 2.3615 1.3271 0.8712 0.0000  -0.2835 -0.3994 458  TRP A NE1 
3290 C  CE2 . TRP A 459 ? 2.4116 1.4041 0.9997 -0.0286 -0.2945 -0.3818 458  TRP A CE2 
3291 C  CE3 . TRP A 459 ? 2.4284 1.4207 1.1043 -0.0754 -0.3589 -0.3746 458  TRP A CE3 
3292 C  CZ2 . TRP A 459 ? 2.3739 1.4240 1.0341 -0.0413 -0.2650 -0.3598 458  TRP A CZ2 
3293 C  CZ3 . TRP A 459 ? 2.1380 1.1813 0.8797 -0.0852 -0.3279 -0.3512 458  TRP A CZ3 
3294 C  CH2 . TRP A 459 ? 2.1917 1.2621 0.9246 -0.0685 -0.2830 -0.3447 458  TRP A CH2 
3295 N  N   . LYS A 460 ? 2.3323 1.3319 0.9668 -0.0722 -0.4518 -0.3857 459  LYS A N   
3296 C  CA  . LYS A 460 ? 2.2664 1.3039 0.9472 -0.0878 -0.4584 -0.3657 459  LYS A CA  
3297 C  C   . LYS A 460 ? 2.5553 1.5935 1.1813 -0.0670 -0.4621 -0.3513 459  LYS A C   
3298 O  O   . LYS A 460 ? 2.5834 1.6256 1.2011 -0.0671 -0.4408 -0.3296 459  LYS A O   
3299 C  CB  . LYS A 460 ? 2.2334 1.3043 0.9946 -0.1162 -0.4954 -0.3749 459  LYS A CB  
3300 C  CG  . LYS A 460 ? 2.1852 1.2547 1.0073 -0.1433 -0.4846 -0.3764 459  LYS A CG  
3301 C  CD  . LYS A 460 ? 2.1600 1.2644 1.0604 -0.1775 -0.5157 -0.3841 459  LYS A CD  
3302 C  CE  . LYS A 460 ? 2.1202 1.2827 1.0567 -0.1815 -0.5363 -0.3738 459  LYS A CE  
3303 N  NZ  . LYS A 460 ? 2.1126 1.3215 1.1211 -0.2129 -0.5697 -0.3886 459  LYS A NZ  
3304 N  N   . GLU A 461 ? 2.7447 1.7728 1.3263 -0.0483 -0.4881 -0.3631 460  GLU A N   
3305 C  CA  . GLU A 461 ? 2.9941 2.0110 1.5087 -0.0222 -0.4919 -0.3479 460  GLU A CA  
3306 C  C   . GLU A 461 ? 3.0479 2.0263 1.4866 -0.0082 -0.4420 -0.3315 460  GLU A C   
3307 O  O   . GLU A 461 ? 3.2394 2.2013 1.6319 0.0014  -0.4251 -0.3079 460  GLU A O   
3308 C  CB  . GLU A 461 ? 3.2205 2.2357 1.6998 -0.0033 -0.5301 -0.3663 460  GLU A CB  
3309 C  CG  . GLU A 461 ? 3.2987 2.3588 1.8556 -0.0242 -0.5759 -0.3898 460  GLU A CG  
3310 C  CD  . GLU A 461 ? 3.3191 2.4319 1.9374 -0.0324 -0.6021 -0.3805 460  GLU A CD  
3311 O  OE1 . GLU A 461 ? 3.3156 2.4240 1.9207 -0.0226 -0.5853 -0.3549 460  GLU A OE1 
3312 O  OE2 . GLU A 461 ? 3.3073 2.4684 1.9911 -0.0515 -0.6383 -0.4009 460  GLU A OE2 
3313 N  N   . ARG A 462 ? 2.7713 1.7355 1.1971 -0.0077 -0.4170 -0.3449 461  ARG A N   
3314 C  CA  . ARG A 462 ? 2.6974 1.6400 1.0600 0.0028  -0.3661 -0.3348 461  ARG A CA  
3315 C  C   . ARG A 462 ? 2.6003 1.5571 0.9883 -0.0169 -0.3286 -0.3149 461  ARG A C   
3316 O  O   . ARG A 462 ? 2.5141 1.4555 0.8450 -0.0144 -0.2901 -0.2971 461  ARG A O   
3317 C  CB  . ARG A 462 ? 2.7661 1.6996 1.1168 0.0124  -0.3522 -0.3588 461  ARG A CB  
3318 C  CG  . ARG A 462 ? 2.8270 1.7553 1.1230 0.0237  -0.2973 -0.3543 461  ARG A CG  
3319 C  CD  . ARG A 462 ? 2.9513 1.8563 1.1580 0.0397  -0.2790 -0.3383 461  ARG A CD  
3320 N  NE  . ARG A 462 ? 3.1360 2.0469 1.2982 0.0425  -0.2202 -0.3327 461  ARG A NE  
3321 C  CZ  . ARG A 462 ? 3.2396 2.1606 1.3963 0.0233  -0.1790 -0.3104 461  ARG A CZ  
3322 N  NH1 . ARG A 462 ? 3.2269 2.1445 1.4140 0.0037  -0.1915 -0.2906 461  ARG A NH1 
3323 N  NH2 . ARG A 462 ? 3.2977 2.2354 1.4194 0.0223  -0.1238 -0.3095 461  ARG A NH2 
3324 N  N   . HIS A 463 ? 2.5979 1.5827 1.0682 -0.0391 -0.3372 -0.3181 462  HIS A N   
3325 C  CA  . HIS A 463 ? 2.4449 1.4686 0.9731 -0.0563 -0.2922 -0.2989 462  HIS A CA  
3326 C  C   . HIS A 463 ? 2.4541 1.5166 1.0694 -0.0778 -0.2988 -0.2799 462  HIS A C   
3327 O  O   . HIS A 463 ? 2.3991 1.4896 1.0487 -0.0911 -0.2617 -0.2617 462  HIS A O   
3328 C  CB  . HIS A 463 ? 2.2416 1.2811 0.8025 -0.0559 -0.2747 -0.3160 462  HIS A CB  
3329 C  CG  . HIS A 463 ? 2.3177 1.3403 0.8046 -0.0345 -0.2433 -0.3281 462  HIS A CG  
3330 N  ND1 . HIS A 463 ? 2.3864 1.4059 0.8720 -0.0193 -0.2374 -0.3514 462  HIS A ND1 
3331 C  CD2 . HIS A 463 ? 2.3788 1.3861 0.7871 -0.0246 -0.2137 -0.3198 462  HIS A CD2 
3332 C  CE1 . HIS A 463 ? 2.3950 1.4072 0.8094 0.0011  -0.2062 -0.3593 462  HIS A CE1 
3333 N  NE2 . HIS A 463 ? 2.4591 1.4648 0.8259 -0.0046 -0.1897 -0.3397 462  HIS A NE2 
3334 N  N   . GLN A 464 ? 2.4300 1.4991 1.0818 -0.0823 -0.3449 -0.2863 463  GLN A N   
3335 C  CA  . GLN A 464 ? 2.3023 1.4154 1.0421 -0.1013 -0.3509 -0.2719 463  GLN A CA  
3336 C  C   . GLN A 464 ? 2.3977 1.5094 1.1207 -0.0948 -0.3466 -0.2488 463  GLN A C   
3337 O  O   . GLN A 464 ? 2.4544 1.5342 1.1106 -0.0739 -0.3688 -0.2480 463  GLN A O   
3338 C  CB  . GLN A 464 ? 2.2382 1.3693 1.0312 -0.1124 -0.3980 -0.2889 463  GLN A CB  
3339 C  CG  . GLN A 464 ? 2.0535 1.2305 0.9458 -0.1380 -0.3910 -0.2818 463  GLN A CG  
3340 C  CD  . GLN A 464 ? 2.2116 1.4118 1.1577 -0.1553 -0.4339 -0.2960 463  GLN A CD  
3341 O  OE1 . GLN A 464 ? 2.3508 1.5425 1.2676 -0.1482 -0.4724 -0.3122 463  GLN A OE1 
3342 N  NE2 . GLN A 464 ? 2.2175 1.4511 1.2421 -0.1796 -0.4270 -0.2907 463  GLN A NE2 
3343 N  N   . VAL A 465 ? 2.2883 1.4305 1.0679 -0.1105 -0.3192 -0.2310 464  VAL A N   
3344 C  CA  . VAL A 465 ? 2.2362 1.3708 1.0051 -0.1059 -0.3115 -0.2092 464  VAL A CA  
3345 C  C   . VAL A 465 ? 1.9578 1.1398 0.8119 -0.1130 -0.3373 -0.2075 464  VAL A C   
3346 O  O   . VAL A 465 ? 2.2432 1.4680 1.1736 -0.1322 -0.3387 -0.2150 464  VAL A O   
3347 C  CB  . VAL A 465 ? 2.0082 1.1386 0.7706 -0.1211 -0.2572 -0.1927 464  VAL A CB  
3348 C  CG1 . VAL A 465 ? 2.0321 1.1355 0.7702 -0.1170 -0.2486 -0.1710 464  VAL A CG1 
3349 C  CG2 . VAL A 465 ? 2.0713 1.1697 0.7581 -0.1175 -0.2267 -0.1962 464  VAL A CG2 
3350 N  N   . ARG A 466 ? 2.0720 1.2455 0.9088 -0.0946 -0.3576 -0.1979 465  ARG A N   
3351 C  CA  . ARG A 466 ? 2.1961 1.4233 1.1123 -0.0963 -0.3833 -0.1990 465  ARG A CA  
3352 C  C   . ARG A 466 ? 2.3117 1.5269 1.2229 -0.0869 -0.3643 -0.1781 465  ARG A C   
3353 O  O   . ARG A 466 ? 2.4672 1.6200 1.2953 -0.0716 -0.3471 -0.1638 465  ARG A O   
3354 C  CB  . ARG A 466 ? 2.3843 1.6275 1.2941 -0.0764 -0.4374 -0.2149 465  ARG A CB  
3355 C  CG  . ARG A 466 ? 2.3710 1.6116 1.2705 -0.0857 -0.4595 -0.2389 465  ARG A CG  
3356 C  CD  . ARG A 466 ? 2.5211 1.8028 1.4477 -0.0787 -0.5148 -0.2599 465  ARG A CD  
3357 N  NE  . ARG A 466 ? 2.8228 2.0879 1.7244 -0.0877 -0.5377 -0.2857 465  ARG A NE  
3358 C  CZ  . ARG A 466 ? 2.8686 2.1454 1.8197 -0.1201 -0.5350 -0.3003 465  ARG A CZ  
3359 N  NH1 . ARG A 466 ? 2.8638 2.1737 1.8932 -0.1460 -0.5103 -0.2899 465  ARG A NH1 
3360 N  NH2 . ARG A 466 ? 2.8528 2.1009 1.7675 -0.1247 -0.5574 -0.3257 465  ARG A NH2 
3361 N  N   . TYR A 467 ? 2.2198 1.4878 1.2131 -0.0964 -0.3654 -0.1761 466  TYR A N   
3362 C  CA  . TYR A 467 ? 2.1222 1.3740 1.1092 -0.0858 -0.3481 -0.1594 466  TYR A CA  
3363 C  C   . TYR A 467 ? 2.0636 1.3713 1.1123 -0.0691 -0.3793 -0.1636 466  TYR A C   
3364 O  O   . TYR A 467 ? 2.0166 1.3922 1.1389 -0.0810 -0.4028 -0.1782 466  TYR A O   
3365 C  CB  . TYR A 467 ? 2.1071 1.3640 1.1254 -0.1160 -0.3015 -0.1517 466  TYR A CB  
3366 C  CG  . TYR A 467 ? 2.2028 1.5308 1.3170 -0.1417 -0.2996 -0.1609 466  TYR A CG  
3367 C  CD1 . TYR A 467 ? 2.3071 1.6870 1.4921 -0.1434 -0.3062 -0.1603 466  TYR A CD1 
3368 C  CD2 . TYR A 467 ? 2.1815 1.5208 1.3090 -0.1610 -0.2904 -0.1698 466  TYR A CD2 
3369 C  CE1 . TYR A 467 ? 2.2221 1.6603 1.4851 -0.1670 -0.3021 -0.1658 466  TYR A CE1 
3370 C  CE2 . TYR A 467 ? 2.2215 1.6131 1.4246 -0.1812 -0.2885 -0.1753 466  TYR A CE2 
3371 C  CZ  . TYR A 467 ? 2.2351 1.6746 1.5041 -0.1859 -0.2936 -0.1721 466  TYR A CZ  
3372 O  OH  . TYR A 467 ? 2.2571 1.7424 1.5925 -0.2064 -0.2894 -0.1747 466  TYR A OH  
3373 N  N   . THR A 468 ? 2.1342 1.4106 1.1488 -0.0412 -0.3782 -0.1514 467  THR A N   
3374 C  CA  . THR A 468 ? 2.2548 1.5879 1.3299 -0.0216 -0.3995 -0.1550 467  THR A CA  
3375 C  C   . THR A 468 ? 2.3656 1.6654 1.4326 -0.0190 -0.3664 -0.1408 467  THR A C   
3376 O  O   . THR A 468 ? 2.5767 1.7889 1.5605 -0.0144 -0.3413 -0.1263 467  THR A O   
3377 C  CB  . THR A 468 ? 2.3498 1.6846 1.3882 0.0266  -0.4461 -0.1602 467  THR A CB  
3378 O  OG1 . THR A 468 ? 2.5126 1.8731 1.5511 0.0212  -0.4778 -0.1767 467  THR A OG1 
3379 C  CG2 . THR A 468 ? 2.2452 1.6604 1.3601 0.0480  -0.4689 -0.1684 467  THR A CG2 
3380 N  N   . PHE A 469 ? 2.2496 1.6168 1.3997 -0.0245 -0.3648 -0.1460 468  PHE A N   
3381 C  CA  . PHE A 469 ? 2.1360 1.4784 1.2860 -0.0247 -0.3346 -0.1373 468  PHE A CA  
3382 C  C   . PHE A 469 ? 2.3417 1.7254 1.5245 0.0147  -0.3577 -0.1420 468  PHE A C   
3383 O  O   . PHE A 469 ? 2.3788 1.8599 1.6489 0.0113  -0.3760 -0.1545 468  PHE A O   
3384 C  CB  . PHE A 469 ? 1.9951 1.3825 1.2132 -0.0697 -0.3038 -0.1403 468  PHE A CB  
3385 C  CG  . PHE A 469 ? 1.9345 1.2671 1.1089 -0.1009 -0.2668 -0.1335 468  PHE A CG  
3386 C  CD1 . PHE A 469 ? 2.0325 1.2947 1.1510 -0.1041 -0.2362 -0.1244 468  PHE A CD1 
3387 C  CD2 . PHE A 469 ? 1.8235 1.1766 1.0130 -0.1276 -0.2619 -0.1384 468  PHE A CD2 
3388 C  CE1 . PHE A 469 ? 1.9644 1.1913 1.0512 -0.1375 -0.2008 -0.1212 468  PHE A CE1 
3389 C  CE2 . PHE A 469 ? 1.6844 1.0024 0.8402 -0.1530 -0.2277 -0.1349 468  PHE A CE2 
3390 C  CZ  . PHE A 469 ? 1.7103 0.9723 0.8191 -0.1600 -0.1967 -0.1269 468  PHE A CZ  
3391 N  N   . VAL A 470 ? 2.4899 1.7991 1.6010 0.0527  -0.3558 -0.1326 469  VAL A N   
3392 C  CA  . VAL A 470 ? 2.5353 1.8798 1.6733 0.0967  -0.3740 -0.1382 469  VAL A CA  
3393 C  C   . VAL A 470 ? 2.7336 1.9908 1.8155 0.1097  -0.3443 -0.1284 469  VAL A C   
3394 O  O   . VAL A 470 ? 2.7798 1.9224 1.7561 0.1301  -0.3376 -0.1146 469  VAL A O   
3395 C  CB  . VAL A 470 ? 2.4321 1.7828 1.5351 0.1539  -0.4212 -0.1419 469  VAL A CB  
3396 C  CG1 . VAL A 470 ? 2.2764 1.7542 1.4731 0.1452  -0.4563 -0.1611 469  VAL A CG1 
3397 C  CG2 . VAL A 470 ? 2.3960 1.6362 1.3814 0.1653  -0.4231 -0.1274 469  VAL A CG2 
3398 N  N   . LYS A 471 ? 2.9609 2.2673 2.1088 0.0952  -0.3253 -0.1359 470  LYS A N   
3399 C  CA  . LYS A 471 ? 2.9885 2.2286 2.0979 0.1113  -0.3022 -0.1336 470  LYS A CA  
3400 C  C   . LYS A 471 ? 2.9674 2.0660 1.9673 0.0946  -0.2723 -0.1184 470  LYS A C   
3401 O  O   . LYS A 471 ? 3.2026 2.2033 2.1274 0.1216  -0.2624 -0.1126 470  LYS A O   
3402 C  CB  . LYS A 471 ? 2.9844 2.2332 2.0825 0.1822  -0.3325 -0.1388 470  LYS A CB  
3403 C  CG  . LYS A 471 ? 3.0121 2.2084 2.0837 0.2081  -0.3137 -0.1420 470  LYS A CG  
3404 C  CD  . LYS A 471 ? 2.8130 2.0740 1.9637 0.1657  -0.2844 -0.1531 470  LYS A CD  
3405 C  CE  . LYS A 471 ? 2.7854 1.9810 1.8964 0.1934  -0.2670 -0.1589 470  LYS A CE  
3406 N  NZ  . LYS A 471 ? 2.7027 1.9483 1.8754 0.1512  -0.2372 -0.1702 470  LYS A NZ  
3407 N  N   . GLY A 472 ? 2.7263 1.8142 1.7160 0.0490  -0.2567 -0.1127 471  GLY A N   
3408 C  CA  . GLY A 472 ? 2.7745 1.7455 1.6691 0.0234  -0.2246 -0.0993 471  GLY A CA  
3409 C  C   . GLY A 472 ? 2.7466 1.7486 1.6650 -0.0312 -0.2042 -0.0997 471  GLY A C   
3410 O  O   . GLY A 472 ? 1.9102 0.9967 0.9135 -0.0655 -0.1936 -0.1106 471  GLY A O   
3411 N  N   . ASN A 473 ? 2.7069 1.6381 1.5437 -0.0342 -0.1993 -0.0875 472  ASN A N   
3412 C  CA  . ASN A 473 ? 2.6558 1.6079 1.4999 -0.0777 -0.1799 -0.0881 472  ASN A CA  
3413 C  C   . ASN A 473 ? 2.4117 1.3733 1.2301 -0.0564 -0.2096 -0.0856 472  ASN A C   
3414 O  O   . ASN A 473 ? 2.4927 1.4343 1.2752 -0.0089 -0.2443 -0.0818 472  ASN A O   
3415 C  CB  . ASN A 473 ? 3.0692 1.9314 1.8395 -0.1158 -0.1331 -0.0790 472  ASN A CB  
3416 C  CG  . ASN A 473 ? 3.2839 2.1724 2.1066 -0.1562 -0.1013 -0.0899 472  ASN A CG  
3417 O  OD1 . ASN A 473 ? 3.3115 2.2697 2.1938 -0.1960 -0.0833 -0.1002 472  ASN A OD1 
3418 N  ND2 . ASN A 473 ? 3.4031 2.2354 2.2002 -0.1427 -0.0962 -0.0894 472  ASN A ND2 
3419 N  N   . LEU A 474 ? 2.2313 1.2262 1.0675 -0.0895 -0.1970 -0.0902 473  LEU A N   
3420 C  CA  . LEU A 474 ? 2.1550 1.1754 0.9840 -0.0763 -0.2251 -0.0943 473  LEU A CA  
3421 C  C   . LEU A 474 ? 2.2695 1.1997 0.9819 -0.0506 -0.2316 -0.0811 473  LEU A C   
3422 O  O   . LEU A 474 ? 2.2270 1.0714 0.8563 -0.0649 -0.1965 -0.0671 473  LEU A O   
3423 C  CB  . LEU A 474 ? 1.9763 1.0509 0.8526 -0.1165 -0.2057 -0.1043 473  LEU A CB  
3424 C  CG  . LEU A 474 ? 1.9749 1.0096 0.8129 -0.1545 -0.1552 -0.0990 473  LEU A CG  
3425 C  CD1 . LEU A 474 ? 2.0604 1.0351 0.8067 -0.1536 -0.1436 -0.0916 473  LEU A CD1 
3426 C  CD2 . LEU A 474 ? 1.8718 0.9891 0.7961 -0.1884 -0.1381 -0.1125 473  LEU A CD2 
3427 N  N   . LYS A 475 ? 2.4464 1.3994 1.1532 -0.0134 -0.2776 -0.0867 474  LYS A N   
3428 C  CA  . LYS A 475 ? 2.6567 1.5461 1.2617 0.0126  -0.2925 -0.0791 474  LYS A CA  
3429 C  C   . LYS A 475 ? 2.4137 1.3624 1.0558 -0.0088 -0.3009 -0.0955 474  LYS A C   
3430 O  O   . LYS A 475 ? 2.1231 1.1595 0.8560 -0.0125 -0.3290 -0.1135 474  LYS A O   
3431 C  CB  . LYS A 475 ? 2.8071 1.6881 1.3798 0.0725  -0.3431 -0.0785 474  LYS A CB  
3432 C  CG  . LYS A 475 ? 2.8945 1.6795 1.3312 0.1096  -0.3551 -0.0638 474  LYS A CG  
3433 C  CD  . LYS A 475 ? 3.0395 1.7013 1.3692 0.1334  -0.3332 -0.0378 474  LYS A CD  
3434 C  CE  . LYS A 475 ? 3.3128 1.8699 1.4950 0.1691  -0.3413 -0.0196 474  LYS A CE  
3435 N  NZ  . LYS A 475 ? 3.3666 1.8912 1.4959 0.1298  -0.3058 -0.0149 474  LYS A NZ  
3436 N  N   . LEU A 476 ? 2.6570 1.5565 1.2292 -0.0255 -0.2729 -0.0899 475  LEU A N   
3437 C  CA  . LEU A 476 ? 2.6402 1.5861 1.2396 -0.0447 -0.2743 -0.1065 475  LEU A CA  
3438 C  C   . LEU A 476 ? 2.7425 1.6704 1.2782 -0.0133 -0.3125 -0.1142 475  LEU A C   
3439 O  O   . LEU A 476 ? 2.8295 1.6780 1.2533 0.0080  -0.3076 -0.1003 475  LEU A O   
3440 C  CB  . LEU A 476 ? 2.4560 1.3786 1.0282 -0.0819 -0.2191 -0.1015 475  LEU A CB  
3441 C  CG  . LEU A 476 ? 2.1162 1.1024 0.7838 -0.1214 -0.1888 -0.1089 475  LEU A CG  
3442 C  CD1 . LEU A 476 ? 2.1236 1.1092 0.7693 -0.1517 -0.1432 -0.1113 475  LEU A CD1 
3443 C  CD2 . LEU A 476 ? 2.0157 1.0873 0.7845 -0.1211 -0.2220 -0.1274 475  LEU A CD2 
3444 N  N   . GLU A 477 ? 2.5522 1.5505 1.1556 -0.0121 -0.3507 -0.1369 476  GLU A N   
3445 C  CA  . GLU A 477 ? 2.3873 1.3773 0.9392 0.0097  -0.3869 -0.1513 476  GLU A CA  
3446 C  C   . GLU A 477 ? 2.3590 1.3387 0.8885 -0.0146 -0.3573 -0.1598 476  GLU A C   
3447 O  O   . GLU A 477 ? 2.2750 1.2928 0.8721 -0.0469 -0.3290 -0.1647 476  GLU A O   
3448 C  CB  . GLU A 477 ? 2.3158 1.3844 0.9499 0.0162  -0.4406 -0.1752 476  GLU A CB  
3449 C  CG  . GLU A 477 ? 2.6025 1.6703 1.1923 0.0333  -0.4828 -0.1968 476  GLU A CG  
3450 C  CD  . GLU A 477 ? 2.8596 1.8820 1.3520 0.0828  -0.5155 -0.1899 476  GLU A CD  
3451 O  OE1 . GLU A 477 ? 3.0018 2.0408 1.5112 0.1094  -0.5365 -0.1821 476  GLU A OE1 
3452 O  OE2 . GLU A 477 ? 2.8136 1.7836 1.2083 0.0991  -0.5205 -0.1926 476  GLU A OE2 
3453 N  N   . MET A 478 ? 2.4935 1.4240 0.9252 0.0053  -0.3652 -0.1626 477  MET A N   
3454 C  CA  . MET A 478 ? 2.4797 1.3924 0.8714 -0.0105 -0.3318 -0.1693 477  MET A CA  
3455 C  C   . MET A 478 ? 2.5183 1.4394 0.8875 0.0039  -0.3703 -0.1965 477  MET A C   
3456 O  O   . MET A 478 ? 2.6137 1.5383 0.9675 0.0295  -0.4216 -0.2067 477  MET A O   
3457 C  CB  . MET A 478 ? 2.5956 1.4286 0.8715 -0.0048 -0.2900 -0.1454 477  MET A CB  
3458 C  CG  . MET A 478 ? 2.4809 1.2982 0.7735 -0.0308 -0.2414 -0.1223 477  MET A CG  
3459 S  SD  . MET A 478 ? 2.7471 1.6443 1.1563 -0.0768 -0.2027 -0.1352 477  MET A SD  
3460 C  CE  . MET A 478 ? 2.4155 1.2895 0.7486 -0.0904 -0.1508 -0.1368 477  MET A CE  
3461 N  N   . PRO A 479 ? 2.5350 1.4622 0.9032 -0.0112 -0.3470 -0.2113 478  PRO A N   
3462 C  CA  . PRO A 479 ? 2.7047 1.6199 1.0264 0.0049  -0.3784 -0.2380 478  PRO A CA  
3463 C  C   . PRO A 479 ? 3.0019 1.8645 1.2145 0.0388  -0.3861 -0.2274 478  PRO A C   
3464 O  O   . PRO A 479 ? 3.2210 2.0323 1.3558 0.0423  -0.3476 -0.2025 478  PRO A O   
3465 C  CB  . PRO A 479 ? 2.6401 1.5618 0.9674 -0.0117 -0.3367 -0.2486 478  PRO A CB  
3466 C  CG  . PRO A 479 ? 2.5831 1.5057 0.9172 -0.0304 -0.2785 -0.2224 478  PRO A CG  
3467 C  CD  . PRO A 479 ? 2.4292 1.3750 0.8326 -0.0395 -0.2919 -0.2066 478  PRO A CD  
3468 N  N   . SER A 480 ? 1.9667 1.5174 1.2330 -0.1899 -0.0610 -0.4390 479  SER A N   
3469 C  CA  . SER A 480 ? 2.0271 1.5495 1.3466 -0.1735 -0.0627 -0.4211 479  SER A CA  
3470 C  C   . SER A 480 ? 2.0810 1.6268 1.4119 -0.1878 -0.0868 -0.3909 479  SER A C   
3471 O  O   . SER A 480 ? 2.2135 1.8122 1.5318 -0.1899 -0.0997 -0.3697 479  SER A O   
3472 C  CB  . SER A 480 ? 1.9013 1.4322 1.2489 -0.1386 -0.0532 -0.4016 479  SER A CB  
3473 O  OG  . SER A 480 ? 1.7649 1.2642 1.1610 -0.1250 -0.0565 -0.3847 479  SER A OG  
3474 N  N   . PRO A 481 ? 1.8683 1.3747 1.2261 -0.1985 -0.0923 -0.3889 480  PRO A N   
3475 C  CA  . PRO A 481 ? 1.8343 1.3632 1.2028 -0.2167 -0.1119 -0.3612 480  PRO A CA  
3476 C  C   . PRO A 481 ? 1.8131 1.3791 1.2011 -0.1965 -0.1164 -0.3235 480  PRO A C   
3477 O  O   . PRO A 481 ? 1.5054 1.1110 0.8962 -0.2097 -0.1284 -0.3024 480  PRO A O   
3478 C  CB  . PRO A 481 ? 1.8136 1.2801 1.2068 -0.2302 -0.1143 -0.3671 480  PRO A CB  
3479 C  CG  . PRO A 481 ? 1.6965 1.1138 1.1116 -0.2037 -0.0970 -0.3842 480  PRO A CG  
3480 C  CD  . PRO A 481 ? 1.6373 1.0759 1.0202 -0.1950 -0.0805 -0.4120 480  PRO A CD  
3481 N  N   . PHE A 482 ? 1.9781 1.5331 1.3801 -0.1664 -0.1056 -0.3174 481  PHE A N   
3482 C  CA  . PHE A 482 ? 1.7906 1.3729 1.2075 -0.1483 -0.1090 -0.2847 481  PHE A CA  
3483 C  C   . PHE A 482 ? 1.7737 1.3875 1.1789 -0.1236 -0.1009 -0.2834 481  PHE A C   
3484 O  O   . PHE A 482 ? 1.8795 1.4798 1.2749 -0.1136 -0.0886 -0.3049 481  PHE A O   
3485 C  CB  . PHE A 482 ? 1.5999 1.1369 1.0489 -0.1384 -0.1099 -0.2696 481  PHE A CB  
3486 C  CG  . PHE A 482 ? 1.5103 1.0132 0.9776 -0.1134 -0.0969 -0.2846 481  PHE A CG  
3487 C  CD1 . PHE A 482 ? 1.6884 1.1473 1.1639 -0.1165 -0.0871 -0.3168 481  PHE A CD1 
3488 C  CD2 . PHE A 482 ? 1.3490 0.8647 0.8286 -0.0878 -0.0934 -0.2682 481  PHE A CD2 
3489 C  CE1 . PHE A 482 ? 1.6620 1.0947 1.1631 -0.0926 -0.0716 -0.3331 481  PHE A CE1 
3490 C  CE2 . PHE A 482 ? 1.3864 0.8770 0.8905 -0.0657 -0.0810 -0.2815 481  PHE A CE2 
3491 C  CZ  . PHE A 482 ? 1.4619 0.9131 0.9796 -0.0671 -0.0689 -0.3142 481  PHE A CZ  
3492 N  N   . SER A 483 ? 1.8243 1.4793 1.2306 -0.1154 -0.1065 -0.2590 482  SER A N   
3493 C  CA  . SER A 483 ? 2.1209 1.8026 1.5193 -0.0923 -0.1014 -0.2528 482  SER A CA  
3494 C  C   . SER A 483 ? 2.1528 1.8068 1.5686 -0.0695 -0.0928 -0.2469 482  SER A C   
3495 O  O   . SER A 483 ? 2.2986 1.9246 1.7368 -0.0690 -0.0960 -0.2348 482  SER A O   
3496 C  CB  . SER A 483 ? 2.5052 2.2344 1.9057 -0.0900 -0.1092 -0.2310 482  SER A CB  
3497 O  OG  . SER A 483 ? 2.7433 2.4649 2.1607 -0.0902 -0.1104 -0.2114 482  SER A OG  
3498 N  N   . VAL A 484 ? 2.1150 1.7784 1.5213 -0.0528 -0.0841 -0.2530 483  VAL A N   
3499 C  CA  . VAL A 484 ? 1.9326 1.5842 1.3578 -0.0310 -0.0784 -0.2420 483  VAL A CA  
3500 C  C   . VAL A 484 ? 1.8097 1.4972 1.2250 -0.0206 -0.0837 -0.2219 483  VAL A C   
3501 O  O   . VAL A 484 ? 1.7907 1.4958 1.1908 -0.0113 -0.0795 -0.2246 483  VAL A O   
3502 C  CB  . VAL A 484 ? 1.7915 1.4274 1.2190 -0.0203 -0.0619 -0.2634 483  VAL A CB  
3503 C  CG1 . VAL A 484 ? 1.6797 1.3088 1.1341 0.0009  -0.0583 -0.2494 483  VAL A CG1 
3504 C  CG2 . VAL A 484 ? 1.8803 1.4784 1.3201 -0.0298 -0.0536 -0.2895 483  VAL A CG2 
3505 N  N   . VAL A 485 ? 1.8039 1.5005 1.2261 -0.0243 -0.0924 -0.2024 484  VAL A N   
3506 C  CA  . VAL A 485 ? 1.8760 1.6046 1.2912 -0.0157 -0.0955 -0.1873 484  VAL A CA  
3507 C  C   . VAL A 485 ? 1.8974 1.6228 1.3207 -0.0223 -0.1001 -0.1690 484  VAL A C   
3508 O  O   . VAL A 485 ? 1.9269 1.6300 1.3585 -0.0370 -0.1039 -0.1658 484  VAL A O   
3509 C  CB  . VAL A 485 ? 1.7376 1.5052 1.1405 -0.0219 -0.0999 -0.1920 484  VAL A CB  
3510 C  CG1 . VAL A 485 ? 1.7131 1.4930 1.1223 -0.0427 -0.1051 -0.1916 484  VAL A CG1 
3511 C  CG2 . VAL A 485 ? 1.8141 1.6102 1.2157 -0.0069 -0.1016 -0.1806 484  VAL A CG2 
3512 N  N   . ILE A 486 ? 1.7565 1.5010 1.1750 -0.0138 -0.0998 -0.1572 485  ILE A N   
3513 C  CA  . ILE A 486 ? 1.6389 1.3863 1.0553 -0.0248 -0.1016 -0.1425 485  ILE A CA  
3514 C  C   . ILE A 486 ? 1.7449 1.5153 1.1625 -0.0453 -0.1012 -0.1451 485  ILE A C   
3515 O  O   . ILE A 486 ? 1.6839 1.4891 1.1047 -0.0440 -0.0994 -0.1541 485  ILE A O   
3516 C  CB  . ILE A 486 ? 1.6092 1.3759 1.0169 -0.0131 -0.0979 -0.1363 485  ILE A CB  
3517 C  CG1 . ILE A 486 ? 1.6018 1.3450 1.0089 0.0026  -0.1001 -0.1307 485  ILE A CG1 
3518 C  CG2 . ILE A 486 ? 1.6613 1.4359 1.0596 -0.0293 -0.0957 -0.1258 485  ILE A CG2 
3519 C  CD1 . ILE A 486 ? 1.4675 1.2242 0.8644 0.0143  -0.0973 -0.1276 485  ILE A CD1 
3520 N  N   . GLN A 487 ? 1.9308 1.6822 1.3486 -0.0658 -0.1050 -0.1351 486  GLN A N   
3521 C  CA  . GLN A 487 ? 1.9399 1.7115 1.3600 -0.0899 -0.1044 -0.1359 486  GLN A CA  
3522 C  C   . GLN A 487 ? 1.7442 1.5233 1.1534 -0.1088 -0.1013 -0.1193 486  GLN A C   
3523 O  O   . GLN A 487 ? 1.4406 1.1898 0.8388 -0.1107 -0.1064 -0.1040 486  GLN A O   
3524 C  CB  . GLN A 487 ? 2.1489 1.8872 1.5764 -0.1043 -0.1118 -0.1412 486  GLN A CB  
3525 C  CG  . GLN A 487 ? 2.2795 2.0404 1.7109 -0.1302 -0.1128 -0.1454 486  GLN A CG  
3526 C  CD  . GLN A 487 ? 2.3327 2.0720 1.7618 -0.1589 -0.1175 -0.1285 486  GLN A CD  
3527 O  OE1 . GLN A 487 ? 2.4795 2.1704 1.9085 -0.1606 -0.1256 -0.1167 486  GLN A OE1 
3528 N  NE2 . GLN A 487 ? 2.2760 2.0525 1.7063 -0.1827 -0.1133 -0.1255 486  GLN A NE2 
3529 N  N   . GLU A 488 ? 1.8932 1.7153 1.3056 -0.1237 -0.0927 -0.1225 487  GLU A N   
3530 C  CA  . GLU A 488 ? 1.9746 1.8107 1.3731 -0.1475 -0.0848 -0.1102 487  GLU A CA  
3531 C  C   . GLU A 488 ? 1.9435 1.7890 1.3473 -0.1808 -0.0855 -0.1059 487  GLU A C   
3532 O  O   . GLU A 488 ? 2.2396 2.1107 1.6640 -0.1831 -0.0859 -0.1183 487  GLU A O   
3533 C  CB  . GLU A 488 ? 2.0401 1.9255 1.4413 -0.1369 -0.0675 -0.1201 487  GLU A CB  
3534 C  CG  . GLU A 488 ? 2.0387 1.9319 1.4145 -0.1575 -0.0551 -0.1110 487  GLU A CG  
3535 C  CD  . GLU A 488 ? 1.9375 1.8921 1.3285 -0.1653 -0.0327 -0.1247 487  GLU A CD  
3536 O  OE1 . GLU A 488 ? 1.8426 1.8338 1.2675 -0.1438 -0.0285 -0.1407 487  GLU A OE1 
3537 O  OE2 . GLU A 488 ? 1.9076 1.8751 1.2782 -0.1938 -0.0193 -0.1190 487  GLU A OE2 
3538 N  N   . SER A 489 ? 1.5774 1.4022 0.9611 -0.2095 -0.0878 -0.0866 488  SER A N   
3539 C  CA  . SER A 489 ? 1.8418 1.6662 1.2279 -0.2453 -0.0909 -0.0784 488  SER A CA  
3540 C  C   . SER A 489 ? 1.8810 1.7472 1.2522 -0.2751 -0.0736 -0.0712 488  SER A C   
3541 O  O   . SER A 489 ? 1.7129 1.5913 1.0631 -0.2713 -0.0620 -0.0692 488  SER A O   
3542 C  CB  . SER A 489 ? 1.3185 1.0750 0.6958 -0.2589 -0.1116 -0.0587 488  SER A CB  
3543 O  OG  . SER A 489 ? 1.5441 1.2923 0.9278 -0.2913 -0.1175 -0.0532 488  SER A OG  
3544 N  N   . GLU A 490 ? 2.0267 1.9168 1.4081 -0.3066 -0.0699 -0.0696 489  GLU A N   
3545 C  CA  . GLU A 490 ? 2.0603 1.9964 1.4300 -0.3385 -0.0491 -0.0648 489  GLU A CA  
3546 C  C   . GLU A 490 ? 1.9992 1.8947 1.3226 -0.3703 -0.0548 -0.0365 489  GLU A C   
3547 O  O   . GLU A 490 ? 2.0531 1.9773 1.3497 -0.3896 -0.0355 -0.0334 489  GLU A O   
3548 C  CB  . GLU A 490 ? 2.1193 2.0956 1.5165 -0.3667 -0.0443 -0.0693 489  GLU A CB  
3549 C  CG  . GLU A 490 ? 2.2245 2.1491 1.6185 -0.3935 -0.0671 -0.0535 489  GLU A CG  
3550 C  CD  . GLU A 490 ? 2.2669 2.1618 1.6841 -0.3670 -0.0855 -0.0680 489  GLU A CD  
3551 O  OE1 . GLU A 490 ? 2.1988 2.1119 1.6304 -0.3290 -0.0825 -0.0864 489  GLU A OE1 
3552 O  OE2 . GLU A 490 ? 2.4333 2.2847 1.8522 -0.3864 -0.1025 -0.0615 489  GLU A OE2 
3553 N  N   . LYS A 491 ? 1.8950 1.7231 1.2096 -0.3767 -0.0816 -0.0161 490  LYS A N   
3554 C  CA  . LYS A 491 ? 1.9284 1.7079 1.2029 -0.4006 -0.0964 0.0158  490  LYS A CA  
3555 C  C   . LYS A 491 ? 2.1255 1.8738 1.3959 -0.3628 -0.1073 0.0151  490  LYS A C   
3556 O  O   . LYS A 491 ? 2.2221 1.9380 1.5205 -0.3332 -0.1219 0.0081  490  LYS A O   
3557 C  CB  . LYS A 491 ? 2.0620 1.7842 1.3394 -0.4279 -0.1222 0.0403  490  LYS A CB  
3558 C  CG  . LYS A 491 ? 2.1342 1.8243 1.4530 -0.4015 -0.1367 0.0248  490  LYS A CG  
3559 C  CD  . LYS A 491 ? 2.2433 1.8624 1.5665 -0.4241 -0.1641 0.0489  490  LYS A CD  
3560 C  CE  . LYS A 491 ? 2.2734 1.9045 1.5909 -0.4729 -0.1619 0.0596  490  LYS A CE  
3561 N  NZ  . LYS A 491 ? 2.2390 1.7942 1.5660 -0.4927 -0.1902 0.0808  490  LYS A NZ  
3562 N  N   . GLY A 492 ? 2.2390 1.9970 1.4740 -0.3657 -0.0993 0.0209  491  GLY A N   
3563 C  CA  . GLY A 492 ? 2.1083 1.8462 1.3428 -0.3296 -0.1072 0.0168  491  GLY A CA  
3564 C  C   . GLY A 492 ? 1.8290 1.6050 1.1003 -0.2901 -0.0909 -0.0176 491  GLY A C   
3565 O  O   . GLY A 492 ? 1.6241 1.4528 0.8953 -0.2870 -0.0660 -0.0372 491  GLY A O   
3566 N  N   . SER A 493 ? 1.8075 1.5577 1.1108 -0.2601 -0.1045 -0.0253 492  SER A N   
3567 C  CA  . SER A 493 ? 1.7354 1.4284 1.0446 -0.2452 -0.1284 -0.0104 492  SER A CA  
3568 C  C   . SER A 493 ? 1.5298 1.2321 0.8607 -0.2024 -0.1234 -0.0328 492  SER A C   
3569 O  O   . SER A 493 ? 1.5674 1.3045 0.9162 -0.1880 -0.1101 -0.0561 492  SER A O   
3570 C  CB  . SER A 493 ? 2.0048 1.6534 1.3366 -0.2553 -0.1471 -0.0005 492  SER A CB  
3571 O  OG  . SER A 493 ? 2.1337 1.7717 1.4456 -0.2980 -0.1534 0.0226  492  SER A OG  
3572 N  N   . TRP A 494 ? 1.4631 1.1364 0.7937 -0.1840 -0.1353 -0.0242 493  TRP A N   
3573 C  CA  . TRP A 494 ? 1.5401 1.2226 0.8890 -0.1469 -0.1297 -0.0438 493  TRP A CA  
3574 C  C   . TRP A 494 ? 1.5784 1.2201 0.9572 -0.1274 -0.1443 -0.0423 493  TRP A C   
3575 O  O   . TRP A 494 ? 1.7873 1.3917 1.1711 -0.1318 -0.1625 -0.0208 493  TRP A O   
3576 C  CB  . TRP A 494 ? 1.5468 1.2431 0.8723 -0.1387 -0.1241 -0.0427 493  TRP A CB  
3577 C  CG  . TRP A 494 ? 1.5772 1.3208 0.8866 -0.1454 -0.1018 -0.0578 493  TRP A CG  
3578 C  CD1 . TRP A 494 ? 1.7067 1.4704 0.9918 -0.1768 -0.0914 -0.0526 493  TRP A CD1 
3579 C  CD2 . TRP A 494 ? 1.4395 1.2175 0.7613 -0.1198 -0.0863 -0.0812 493  TRP A CD2 
3580 N  NE1 . TRP A 494 ? 1.5572 1.3687 0.8445 -0.1699 -0.0677 -0.0747 493  TRP A NE1 
3581 C  CE2 . TRP A 494 ? 1.5030 1.3218 0.8145 -0.1340 -0.0663 -0.0912 493  TRP A CE2 
3582 C  CE3 . TRP A 494 ? 1.1948 0.9729 0.5365 -0.0876 -0.0875 -0.0937 493  TRP A CE3 
3583 C  CZ2 . TRP A 494 ? 1.4896 1.3470 0.8176 -0.1132 -0.0497 -0.1131 493  TRP A CZ2 
3584 C  CZ3 . TRP A 494 ? 1.2437 1.0570 0.5943 -0.0703 -0.0736 -0.1118 493  TRP A CZ3 
3585 C  CH2 . TRP A 494 ? 1.3625 1.2140 0.7098 -0.0812 -0.0559 -0.1214 493  TRP A CH2 
3586 N  N   . HIS A 495 ? 1.2874 0.9382 0.6877 -0.1070 -0.1363 -0.0656 494  HIS A N   
3587 C  CA  . HIS A 495 ? 1.2124 0.8300 0.6422 -0.0885 -0.1430 -0.0719 494  HIS A CA  
3588 C  C   . HIS A 495 ? 1.3558 0.9905 0.7916 -0.0596 -0.1332 -0.0889 494  HIS A C   
3589 O  O   . HIS A 495 ? 1.4775 1.1461 0.9038 -0.0532 -0.1215 -0.1050 494  HIS A O   
3590 C  CB  . HIS A 495 ? 1.2313 0.8350 0.6762 -0.0977 -0.1424 -0.0854 494  HIS A CB  
3591 C  CG  . HIS A 495 ? 1.3716 0.9450 0.8172 -0.1259 -0.1558 -0.0658 494  HIS A CG  
3592 N  ND1 . HIS A 495 ? 1.3623 0.9572 0.7871 -0.1548 -0.1531 -0.0592 494  HIS A ND1 
3593 C  CD2 . HIS A 495 ? 1.4946 1.0172 0.9624 -0.1303 -0.1729 -0.0502 494  HIS A CD2 
3594 C  CE1 . HIS A 495 ? 1.5242 1.0810 0.9519 -0.1787 -0.1682 -0.0388 494  HIS A CE1 
3595 N  NE2 . HIS A 495 ? 1.5901 1.1005 1.0449 -0.1634 -0.1820 -0.0322 494  HIS A NE2 
3596 N  N   . PHE A 496 ? 1.2519 0.8644 0.7061 -0.0434 -0.1397 -0.0829 495  PHE A N   
3597 C  CA  . PHE A 496 ? 1.3393 0.9669 0.7979 -0.0196 -0.1307 -0.0955 495  PHE A CA  
3598 C  C   . PHE A 496 ? 1.5716 1.1766 1.0645 -0.0039 -0.1284 -0.1073 495  PHE A C   
3599 O  O   . PHE A 496 ? 1.6143 1.1909 1.1361 -0.0012 -0.1396 -0.0946 495  PHE A O   
3600 C  CB  . PHE A 496 ? 1.4194 1.0518 0.8662 -0.0155 -0.1368 -0.0790 495  PHE A CB  
3601 C  CG  . PHE A 496 ? 1.5982 1.2496 1.0105 -0.0325 -0.1357 -0.0705 495  PHE A CG  
3602 C  CD1 . PHE A 496 ? 1.7609 1.3970 1.1594 -0.0565 -0.1476 -0.0494 495  PHE A CD1 
3603 C  CD2 . PHE A 496 ? 1.5417 1.2260 0.9363 -0.0257 -0.1224 -0.0840 495  PHE A CD2 
3604 C  CE1 . PHE A 496 ? 1.7814 1.4378 1.1447 -0.0752 -0.1417 -0.0452 495  PHE A CE1 
3605 C  CE2 . PHE A 496 ? 1.6889 1.3926 1.0574 -0.0400 -0.1168 -0.0812 495  PHE A CE2 
3606 C  CZ  . PHE A 496 ? 1.8338 1.5251 1.1844 -0.0658 -0.1243 -0.0635 495  PHE A CZ  
3607 N  N   . PRO A 497 ? 1.6270 1.2457 1.1182 0.0055  -0.1140 -0.1317 496  PRO A N   
3608 C  CA  . PRO A 497 ? 1.6162 1.2194 1.1358 0.0200  -0.1051 -0.1483 496  PRO A CA  
3609 C  C   . PRO A 497 ? 1.6504 1.2640 1.1799 0.0369  -0.1024 -0.1426 496  PRO A C   
3610 O  O   . PRO A 497 ? 1.6690 1.3023 1.1753 0.0373  -0.1060 -0.1308 496  PRO A O   
3611 C  CB  . PRO A 497 ? 1.5195 1.1384 1.0185 0.0168  -0.0914 -0.1745 496  PRO A CB  
3612 C  CG  . PRO A 497 ? 1.4587 1.1116 0.9247 0.0112  -0.0939 -0.1675 496  PRO A CG  
3613 C  CD  . PRO A 497 ? 1.5286 1.1786 0.9922 0.0004  -0.1059 -0.1450 496  PRO A CD  
3614 N  N   . VAL A 498 ? 1.7492 1.3504 1.3153 0.0499  -0.0951 -0.1522 497  VAL A N   
3615 C  CA  . VAL A 498 ? 1.9094 1.5234 1.4900 0.0636  -0.0925 -0.1460 497  VAL A CA  
3616 C  C   . VAL A 498 ? 2.0128 1.6396 1.5979 0.0726  -0.0694 -0.1721 497  VAL A C   
3617 O  O   . VAL A 498 ? 2.0899 1.7054 1.6862 0.0720  -0.0557 -0.1960 497  VAL A O   
3618 C  CB  . VAL A 498 ? 1.9459 1.5401 1.5761 0.0700  -0.1075 -0.1265 497  VAL A CB  
3619 C  CG1 . VAL A 498 ? 2.0268 1.6002 1.7108 0.0802  -0.0980 -0.1442 497  VAL A CG1 
3620 C  CG2 . VAL A 498 ? 1.9041 1.5159 1.5422 0.0782  -0.1112 -0.1130 497  VAL A CG2 
3621 N  N   . SER A 499 ? 2.0143 1.6632 1.5866 0.0781  -0.0645 -0.1679 498  SER A N   
3622 C  CA  . SER A 499 ? 1.8149 1.4789 1.3850 0.0823  -0.0425 -0.1886 498  SER A CA  
3623 C  C   . SER A 499 ? 1.6303 1.2869 1.2585 0.0934  -0.0297 -0.1998 498  SER A C   
3624 O  O   . SER A 499 ? 1.5812 1.2252 1.2277 0.0940  -0.0144 -0.2248 498  SER A O   
3625 C  CB  . SER A 499 ? 1.7105 1.3966 1.2535 0.0831  -0.0437 -0.1765 498  SER A CB  
3626 O  OG  . SER A 499 ? 1.7393 1.4326 1.2385 0.0762  -0.0546 -0.1680 498  SER A OG  
3627 N  N   . SER A 506 ? 2.4733 1.8741 2.2140 0.0576  0.0653  -0.4476 505  SER A N   
3628 C  CA  . SER A 506 ? 2.5061 1.9499 2.2576 0.0732  0.0701  -0.4288 505  SER A CA  
3629 C  C   . SER A 506 ? 2.6659 2.1029 2.4807 0.0927  0.0435  -0.3869 505  SER A C   
3630 O  O   . SER A 506 ? 2.6526 2.1212 2.4850 0.1055  0.0422  -0.3670 505  SER A O   
3631 C  CB  . SER A 506 ? 2.4559 1.9428 2.1284 0.0568  0.0624  -0.4108 505  SER A CB  
3632 O  OG  . SER A 506 ? 2.3625 1.8496 2.0153 0.0489  0.0288  -0.3721 505  SER A OG  
3633 N  N   . SER A 507 ? 2.9779 2.3717 2.8245 0.091