data_9MHY
# 
_entry.id   9MHY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MHY         pdb_00009mhy 10.2210/pdb9mhy/pdb 
WWPDB D_1000291019 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-05 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MHY 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              david.critton@bms.com 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Critton 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8896-4896 
# 
_audit_author.name               'Critton, D.A.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-8896-4896 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                80 
_citation.page_last                 88 
_citation.title                     
'Structure-Based Design of Novel TLR7/8 Agonist Payloads Enabling an Immunomodulatory Conjugate Approach.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.4c00463 
_citation.pdbx_database_id_PubMed   39811121 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Poudel, Y.B.'     1  0000-0002-8694-1084 
primary 'Lo, J.C.'         2  ?                   
primary 'Norris, D.J.'     3  ?                   
primary 'Cox, M.'          4  ?                   
primary 'He, L.'           5  ?                   
primary 'Johnson, W.L.'    6  ?                   
primary 'A M Subbaiah, M.' 7  0000-0001-5707-966X 
primary 'Mondal, S.'       8  ?                   
primary 'Thangavel, S.'    9  ?                   
primary 'Subramani, L.'    10 ?                   
primary 'Reddy, M.'        11 ?                   
primary 'Jain, S.'         12 ?                   
primary 'Weiss, D.R.'      13 0000-0003-1073-940X 
primary 'Sivaprakasam, P.' 14 0000-0002-4115-5055 
primary 'Critton, D.'      15 ?                   
primary 'Mulligan, D.'     16 ?                   
primary 'Xie, C.'          17 ?                   
primary 'Dhar, P.'         18 ?                   
primary 'Li, Y.'           19 ?                   
primary 'Sega, E.'         20 ?                   
primary 'Yamazoe, S.'      21 0000-0002-2169-7674 
primary 'Gavai, A.V.'      22 0000-0002-6067-4176 
primary 'Mathur, A.'       23 ?                   
primary 'Zapf, C.W.'       24 0000-0001-5153-5206 
primary 'Chekler, E.P.'    25 ?                   
# 
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 'Toll-like receptor 8' 92307.766 2    ? ? 'residues 27-827' ? 
2 branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(2-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823   2    ? ? ?                 ? 
3 branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   4 ? 
? ?                 ? 
4 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   18   ? ? ?                 ? 
5 non-polymer syn 'SULFATE ION' 96.063    3    ? ? ?                 ? 
6 non-polymer syn 
;(3S,4R)-4-[({3-[(5-amino-7-{[(3S)-1-hydroxyhexan-3-yl]amino}-1H-pyrazolo[4,3-d]pyrimidin-1-yl)methyl]-4-methoxyphenyl}methyl)amino]oxolan-3-ol
;
485.579   2    ? ? ?                 ? 
7 water       nat water 18.015    1079 ? ? ?                 ? 
# 
_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       
;EENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGN
PGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKV
CEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFP
CVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSF
NYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLS
ENRISPLVKDTRQSYANSSSFQRHIRKRRSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPD
IACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNL
KVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASL
TELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSN
LLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDV
TEFLVPR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;EENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGN
PGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKV
CEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFP
CVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSF
NYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLS
ENRISPLVKDTRQSYANSSSFQRHIRKRRSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPD
IACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNL
KVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASL
TELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSN
LLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDV
TEFLVPR
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 2-acetamido-2-deoxy-beta-D-glucopyranose NAG   
5 'SULFATE ION' SO4   
6 
;(3S,4R)-4-[({3-[(5-amino-7-{[(3S)-1-hydroxyhexan-3-yl]amino}-1H-pyrazolo[4,3-d]pyrimidin-1-yl)methyl]-4-methoxyphenyl}methyl)amino]oxolan-3-ol
;
A1BLN 
7 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   GLU n 
1 3   ASN n 
1 4   PHE n 
1 5   SER n 
1 6   ARG n 
1 7   SER n 
1 8   TYR n 
1 9   PRO n 
1 10  CYS n 
1 11  ASP n 
1 12  GLU n 
1 13  LYS n 
1 14  LYS n 
1 15  GLN n 
1 16  ASN n 
1 17  ASP n 
1 18  SER n 
1 19  VAL n 
1 20  ILE n 
1 21  ALA n 
1 22  GLU n 
1 23  CYS n 
1 24  SER n 
1 25  ASN n 
1 26  ARG n 
1 27  ARG n 
1 28  LEU n 
1 29  GLN n 
1 30  GLU n 
1 31  VAL n 
1 32  PRO n 
1 33  GLN n 
1 34  THR n 
1 35  VAL n 
1 36  GLY n 
1 37  LYS n 
1 38  TYR n 
1 39  VAL n 
1 40  THR n 
1 41  GLU n 
1 42  LEU n 
1 43  ASP n 
1 44  LEU n 
1 45  SER n 
1 46  ASP n 
1 47  ASN n 
1 48  PHE n 
1 49  ILE n 
1 50  THR n 
1 51  HIS n 
1 52  ILE n 
1 53  THR n 
1 54  ASN n 
1 55  GLU n 
1 56  SER n 
1 57  PHE n 
1 58  GLN n 
1 59  GLY n 
1 60  LEU n 
1 61  GLN n 
1 62  ASN n 
1 63  LEU n 
1 64  THR n 
1 65  LYS n 
1 66  ILE n 
1 67  ASN n 
1 68  LEU n 
1 69  ASN n 
1 70  HIS n 
1 71  ASN n 
1 72  PRO n 
1 73  ASN n 
1 74  VAL n 
1 75  GLN n 
1 76  HIS n 
1 77  GLN n 
1 78  ASN n 
1 79  GLY n 
1 80  ASN n 
1 81  PRO n 
1 82  GLY n 
1 83  ILE n 
1 84  GLN n 
1 85  SER n 
1 86  ASN n 
1 87  GLY n 
1 88  LEU n 
1 89  ASN n 
1 90  ILE n 
1 91  THR n 
1 92  ASP n 
1 93  GLY n 
1 94  ALA n 
1 95  PHE n 
1 96  LEU n 
1 97  ASN n 
1 98  LEU n 
1 99  LYS n 
1 100 ASN n 
1 101 LEU n 
1 102 ARG n 
1 103 GLU n 
1 104 LEU n 
1 105 LEU n 
1 106 LEU n 
1 107 GLU n 
1 108 ASP n 
1 109 ASN n 
1 110 GLN n 
1 111 LEU n 
1 112 PRO n 
1 113 GLN n 
1 114 ILE n 
1 115 PRO n 
1 116 SER n 
1 117 GLY n 
1 118 LEU n 
1 119 PRO n 
1 120 GLU n 
1 121 SER n 
1 122 LEU n 
1 123 THR n 
1 124 GLU n 
1 125 LEU n 
1 126 SER n 
1 127 LEU n 
1 128 ILE n 
1 129 GLN n 
1 130 ASN n 
1 131 ASN n 
1 132 ILE n 
1 133 TYR n 
1 134 ASN n 
1 135 ILE n 
1 136 THR n 
1 137 LYS n 
1 138 GLU n 
1 139 GLY n 
1 140 ILE n 
1 141 SER n 
1 142 ARG n 
1 143 LEU n 
1 144 ILE n 
1 145 ASN n 
1 146 LEU n 
1 147 LYS n 
1 148 ASN n 
1 149 LEU n 
1 150 TYR n 
1 151 LEU n 
1 152 ALA n 
1 153 TRP n 
1 154 ASN n 
1 155 CYS n 
1 156 TYR n 
1 157 PHE n 
1 158 ASN n 
1 159 LYS n 
1 160 VAL n 
1 161 CYS n 
1 162 GLU n 
1 163 LYS n 
1 164 THR n 
1 165 ASN n 
1 166 ILE n 
1 167 GLU n 
1 168 ASP n 
1 169 GLY n 
1 170 VAL n 
1 171 PHE n 
1 172 GLU n 
1 173 THR n 
1 174 LEU n 
1 175 THR n 
1 176 ASN n 
1 177 LEU n 
1 178 GLU n 
1 179 LEU n 
1 180 LEU n 
1 181 SER n 
1 182 LEU n 
1 183 SER n 
1 184 PHE n 
1 185 ASN n 
1 186 SER n 
1 187 LEU n 
1 188 SER n 
1 189 HIS n 
1 190 VAL n 
1 191 PRO n 
1 192 PRO n 
1 193 LYS n 
1 194 LEU n 
1 195 PRO n 
1 196 SER n 
1 197 SER n 
1 198 LEU n 
1 199 ARG n 
1 200 LYS n 
1 201 LEU n 
1 202 PHE n 
1 203 LEU n 
1 204 SER n 
1 205 ASN n 
1 206 THR n 
1 207 GLN n 
1 208 ILE n 
1 209 LYS n 
1 210 TYR n 
1 211 ILE n 
1 212 SER n 
1 213 GLU n 
1 214 GLU n 
1 215 ASP n 
1 216 PHE n 
1 217 LYS n 
1 218 GLY n 
1 219 LEU n 
1 220 ILE n 
1 221 ASN n 
1 222 LEU n 
1 223 THR n 
1 224 LEU n 
1 225 LEU n 
1 226 ASP n 
1 227 LEU n 
1 228 SER n 
1 229 GLY n 
1 230 ASN n 
1 231 CYS n 
1 232 PRO n 
1 233 ARG n 
1 234 CYS n 
1 235 PHE n 
1 236 ASN n 
1 237 ALA n 
1 238 PRO n 
1 239 PHE n 
1 240 PRO n 
1 241 CYS n 
1 242 VAL n 
1 243 PRO n 
1 244 CYS n 
1 245 ASP n 
1 246 GLY n 
1 247 GLY n 
1 248 ALA n 
1 249 SER n 
1 250 ILE n 
1 251 ASN n 
1 252 ILE n 
1 253 ASP n 
1 254 ARG n 
1 255 PHE n 
1 256 ALA n 
1 257 PHE n 
1 258 GLN n 
1 259 ASN n 
1 260 LEU n 
1 261 THR n 
1 262 GLN n 
1 263 LEU n 
1 264 ARG n 
1 265 TYR n 
1 266 LEU n 
1 267 ASN n 
1 268 LEU n 
1 269 SER n 
1 270 SER n 
1 271 THR n 
1 272 SER n 
1 273 LEU n 
1 274 ARG n 
1 275 LYS n 
1 276 ILE n 
1 277 ASN n 
1 278 ALA n 
1 279 ALA n 
1 280 TRP n 
1 281 PHE n 
1 282 LYS n 
1 283 ASN n 
1 284 MET n 
1 285 PRO n 
1 286 HIS n 
1 287 LEU n 
1 288 LYS n 
1 289 VAL n 
1 290 LEU n 
1 291 ASP n 
1 292 LEU n 
1 293 GLU n 
1 294 PHE n 
1 295 ASN n 
1 296 TYR n 
1 297 LEU n 
1 298 VAL n 
1 299 GLY n 
1 300 GLU n 
1 301 ILE n 
1 302 ALA n 
1 303 SER n 
1 304 GLY n 
1 305 ALA n 
1 306 PHE n 
1 307 LEU n 
1 308 THR n 
1 309 MET n 
1 310 LEU n 
1 311 PRO n 
1 312 ARG n 
1 313 LEU n 
1 314 GLU n 
1 315 ILE n 
1 316 LEU n 
1 317 ASP n 
1 318 LEU n 
1 319 SER n 
1 320 PHE n 
1 321 ASN n 
1 322 TYR n 
1 323 ILE n 
1 324 LYS n 
1 325 GLY n 
1 326 SER n 
1 327 TYR n 
1 328 PRO n 
1 329 GLN n 
1 330 HIS n 
1 331 ILE n 
1 332 ASN n 
1 333 ILE n 
1 334 SER n 
1 335 ARG n 
1 336 ASN n 
1 337 PHE n 
1 338 SER n 
1 339 LYS n 
1 340 LEU n 
1 341 LEU n 
1 342 SER n 
1 343 LEU n 
1 344 ARG n 
1 345 ALA n 
1 346 LEU n 
1 347 HIS n 
1 348 LEU n 
1 349 ARG n 
1 350 GLY n 
1 351 TYR n 
1 352 VAL n 
1 353 PHE n 
1 354 GLN n 
1 355 GLU n 
1 356 LEU n 
1 357 ARG n 
1 358 GLU n 
1 359 ASP n 
1 360 ASP n 
1 361 PHE n 
1 362 GLN n 
1 363 PRO n 
1 364 LEU n 
1 365 MET n 
1 366 GLN n 
1 367 LEU n 
1 368 PRO n 
1 369 ASN n 
1 370 LEU n 
1 371 SER n 
1 372 THR n 
1 373 ILE n 
1 374 ASN n 
1 375 LEU n 
1 376 GLY n 
1 377 ILE n 
1 378 ASN n 
1 379 PHE n 
1 380 ILE n 
1 381 LYS n 
1 382 GLN n 
1 383 ILE n 
1 384 ASP n 
1 385 PHE n 
1 386 LYS n 
1 387 LEU n 
1 388 PHE n 
1 389 GLN n 
1 390 ASN n 
1 391 PHE n 
1 392 SER n 
1 393 ASN n 
1 394 LEU n 
1 395 GLU n 
1 396 ILE n 
1 397 ILE n 
1 398 TYR n 
1 399 LEU n 
1 400 SER n 
1 401 GLU n 
1 402 ASN n 
1 403 ARG n 
1 404 ILE n 
1 405 SER n 
1 406 PRO n 
1 407 LEU n 
1 408 VAL n 
1 409 LYS n 
1 410 ASP n 
1 411 THR n 
1 412 ARG n 
1 413 GLN n 
1 414 SER n 
1 415 TYR n 
1 416 ALA n 
1 417 ASN n 
1 418 SER n 
1 419 SER n 
1 420 SER n 
1 421 PHE n 
1 422 GLN n 
1 423 ARG n 
1 424 HIS n 
1 425 ILE n 
1 426 ARG n 
1 427 LYS n 
1 428 ARG n 
1 429 ARG n 
1 430 SER n 
1 431 THR n 
1 432 ASP n 
1 433 PHE n 
1 434 GLU n 
1 435 PHE n 
1 436 ASP n 
1 437 PRO n 
1 438 HIS n 
1 439 SER n 
1 440 ASN n 
1 441 PHE n 
1 442 TYR n 
1 443 HIS n 
1 444 PHE n 
1 445 THR n 
1 446 ARG n 
1 447 PRO n 
1 448 LEU n 
1 449 ILE n 
1 450 LYS n 
1 451 PRO n 
1 452 GLN n 
1 453 CYS n 
1 454 ALA n 
1 455 ALA n 
1 456 TYR n 
1 457 GLY n 
1 458 LYS n 
1 459 ALA n 
1 460 LEU n 
1 461 ASP n 
1 462 LEU n 
1 463 SER n 
1 464 LEU n 
1 465 ASN n 
1 466 SER n 
1 467 ILE n 
1 468 PHE n 
1 469 PHE n 
1 470 ILE n 
1 471 GLY n 
1 472 PRO n 
1 473 ASN n 
1 474 GLN n 
1 475 PHE n 
1 476 GLU n 
1 477 ASN n 
1 478 LEU n 
1 479 PRO n 
1 480 ASP n 
1 481 ILE n 
1 482 ALA n 
1 483 CYS n 
1 484 LEU n 
1 485 ASN n 
1 486 LEU n 
1 487 SER n 
1 488 ALA n 
1 489 ASN n 
1 490 SER n 
1 491 ASN n 
1 492 ALA n 
1 493 GLN n 
1 494 VAL n 
1 495 LEU n 
1 496 SER n 
1 497 GLY n 
1 498 THR n 
1 499 GLU n 
1 500 PHE n 
1 501 SER n 
1 502 ALA n 
1 503 ILE n 
1 504 PRO n 
1 505 HIS n 
1 506 VAL n 
1 507 LYS n 
1 508 TYR n 
1 509 LEU n 
1 510 ASP n 
1 511 LEU n 
1 512 THR n 
1 513 ASN n 
1 514 ASN n 
1 515 ARG n 
1 516 LEU n 
1 517 ASP n 
1 518 PHE n 
1 519 ASP n 
1 520 ASN n 
1 521 ALA n 
1 522 SER n 
1 523 ALA n 
1 524 LEU n 
1 525 THR n 
1 526 GLU n 
1 527 LEU n 
1 528 SER n 
1 529 ASP n 
1 530 LEU n 
1 531 GLU n 
1 532 VAL n 
1 533 LEU n 
1 534 ASP n 
1 535 LEU n 
1 536 SER n 
1 537 TYR n 
1 538 ASN n 
1 539 SER n 
1 540 HIS n 
1 541 TYR n 
1 542 PHE n 
1 543 ARG n 
1 544 ILE n 
1 545 ALA n 
1 546 GLY n 
1 547 VAL n 
1 548 THR n 
1 549 HIS n 
1 550 HIS n 
1 551 LEU n 
1 552 GLU n 
1 553 PHE n 
1 554 ILE n 
1 555 GLN n 
1 556 ASN n 
1 557 PHE n 
1 558 THR n 
1 559 ASN n 
1 560 LEU n 
1 561 LYS n 
1 562 VAL n 
1 563 LEU n 
1 564 ASN n 
1 565 LEU n 
1 566 SER n 
1 567 HIS n 
1 568 ASN n 
1 569 ASN n 
1 570 ILE n 
1 571 TYR n 
1 572 THR n 
1 573 LEU n 
1 574 THR n 
1 575 ASP n 
1 576 LYS n 
1 577 TYR n 
1 578 ASN n 
1 579 LEU n 
1 580 GLU n 
1 581 SER n 
1 582 LYS n 
1 583 SER n 
1 584 LEU n 
1 585 VAL n 
1 586 GLU n 
1 587 LEU n 
1 588 VAL n 
1 589 PHE n 
1 590 SER n 
1 591 GLY n 
1 592 ASN n 
1 593 ARG n 
1 594 LEU n 
1 595 ASP n 
1 596 ILE n 
1 597 LEU n 
1 598 TRP n 
1 599 ASN n 
1 600 ASP n 
1 601 ASP n 
1 602 ASP n 
1 603 ASN n 
1 604 ARG n 
1 605 TYR n 
1 606 ILE n 
1 607 SER n 
1 608 ILE n 
1 609 PHE n 
1 610 LYS n 
1 611 GLY n 
1 612 LEU n 
1 613 LYS n 
1 614 ASN n 
1 615 LEU n 
1 616 THR n 
1 617 ARG n 
1 618 LEU n 
1 619 ASP n 
1 620 LEU n 
1 621 SER n 
1 622 LEU n 
1 623 ASN n 
1 624 ARG n 
1 625 LEU n 
1 626 LYS n 
1 627 HIS n 
1 628 ILE n 
1 629 PRO n 
1 630 ASN n 
1 631 GLU n 
1 632 ALA n 
1 633 PHE n 
1 634 LEU n 
1 635 ASN n 
1 636 LEU n 
1 637 PRO n 
1 638 ALA n 
1 639 SER n 
1 640 LEU n 
1 641 THR n 
1 642 GLU n 
1 643 LEU n 
1 644 HIS n 
1 645 ILE n 
1 646 ASN n 
1 647 ASP n 
1 648 ASN n 
1 649 MET n 
1 650 LEU n 
1 651 LYS n 
1 652 PHE n 
1 653 PHE n 
1 654 ASN n 
1 655 TRP n 
1 656 THR n 
1 657 LEU n 
1 658 LEU n 
1 659 GLN n 
1 660 GLN n 
1 661 PHE n 
1 662 PRO n 
1 663 ARG n 
1 664 LEU n 
1 665 GLU n 
1 666 LEU n 
1 667 LEU n 
1 668 ASP n 
1 669 LEU n 
1 670 ARG n 
1 671 GLY n 
1 672 ASN n 
1 673 LYS n 
1 674 LEU n 
1 675 LEU n 
1 676 PHE n 
1 677 LEU n 
1 678 THR n 
1 679 ASP n 
1 680 SER n 
1 681 LEU n 
1 682 SER n 
1 683 ASP n 
1 684 PHE n 
1 685 THR n 
1 686 SER n 
1 687 SER n 
1 688 LEU n 
1 689 ARG n 
1 690 THR n 
1 691 LEU n 
1 692 LEU n 
1 693 LEU n 
1 694 SER n 
1 695 HIS n 
1 696 ASN n 
1 697 ARG n 
1 698 ILE n 
1 699 SER n 
1 700 HIS n 
1 701 LEU n 
1 702 PRO n 
1 703 SER n 
1 704 GLY n 
1 705 PHE n 
1 706 LEU n 
1 707 SER n 
1 708 GLU n 
1 709 VAL n 
1 710 SER n 
1 711 SER n 
1 712 LEU n 
1 713 LYS n 
1 714 HIS n 
1 715 LEU n 
1 716 ASP n 
1 717 LEU n 
1 718 SER n 
1 719 SER n 
1 720 ASN n 
1 721 LEU n 
1 722 LEU n 
1 723 LYS n 
1 724 THR n 
1 725 ILE n 
1 726 ASN n 
1 727 LYS n 
1 728 SER n 
1 729 ALA n 
1 730 LEU n 
1 731 GLU n 
1 732 THR n 
1 733 LYS n 
1 734 THR n 
1 735 THR n 
1 736 THR n 
1 737 LYS n 
1 738 LEU n 
1 739 SER n 
1 740 MET n 
1 741 LEU n 
1 742 GLU n 
1 743 LEU n 
1 744 HIS n 
1 745 GLY n 
1 746 ASN n 
1 747 PRO n 
1 748 PHE n 
1 749 GLU n 
1 750 CYS n 
1 751 THR n 
1 752 CYS n 
1 753 ASP n 
1 754 ILE n 
1 755 GLY n 
1 756 ASP n 
1 757 PHE n 
1 758 ARG n 
1 759 ARG n 
1 760 TRP n 
1 761 MET n 
1 762 ASP n 
1 763 GLU n 
1 764 HIS n 
1 765 LEU n 
1 766 ASN n 
1 767 VAL n 
1 768 LYS n 
1 769 ILE n 
1 770 PRO n 
1 771 ARG n 
1 772 LEU n 
1 773 VAL n 
1 774 ASP n 
1 775 VAL n 
1 776 ILE n 
1 777 CYS n 
1 778 ALA n 
1 779 SER n 
1 780 PRO n 
1 781 GLY n 
1 782 ASP n 
1 783 GLN n 
1 784 ARG n 
1 785 GLY n 
1 786 LYS n 
1 787 SER n 
1 788 ILE n 
1 789 VAL n 
1 790 SER n 
1 791 LEU n 
1 792 GLU n 
1 793 LEU n 
1 794 THR n 
1 795 THR n 
1 796 CYS n 
1 797 VAL n 
1 798 SER n 
1 799 ASP n 
1 800 VAL n 
1 801 THR n 
1 802 GLU n 
1 803 PHE n 
1 804 LEU n 
1 805 VAL n 
1 806 PRO n 
1 807 ARG n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   807 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TLR8, UNQ249/PRO286' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7227 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 'DManpa1-3[DManpa2-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-'                                                      
'Glycam Condensed Sequence' GMML     1.0 
2 2 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+2)][a-D-Manp]{}}}}}' LINUCS PDB-CARE ? 
3 3 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-                                                                            
'Glycam Condensed Sequence' GMML     1.0 
4 3 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}'                                       LINUCS PDB-CARE ? 
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 2 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 2 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
4 2 5 MAN C2 H2 3 BMA O6 HO6 sing ? 
5 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
6 3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BLN non-polymer                   . 
;(3S,4R)-4-[({3-[(5-amino-7-{[(3S)-1-hydroxyhexan-3-yl]amino}-1H-pyrazolo[4,3-d]pyrimidin-1-yl)methyl]-4-methoxyphenyl}methyl)amino]oxolan-3-ol
;
? 'C24 H35 N7 O4'  485.579 
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 
BMA   'D-saccharide, beta linking'  . beta-D-mannopyranose 'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
CYS   'L-peptide linking'           y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking'           y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking'           y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'             y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking'           y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer                   . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking'           y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking'           y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking'           y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MAN   'D-saccharide, alpha linking' . alpha-D-mannopyranose 'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
MET   'L-peptide linking'           y METHIONINE ? 'C5 H11 N O2 S'  149.211 
NAG   'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE   'L-peptide linking'           y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking'           y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking'           y SERINE ? 'C3 H7 N O3'     105.093 
SO4   non-polymer                   . 'SULFATE ION' ? 'O4 S -2'        96.063  
THR   'L-peptide linking'           y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking'           y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking'           y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking'           y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLU 1   27  ?   ?   ?   A . n 
A 1 2   GLU 2   28  ?   ?   ?   A . n 
A 1 3   ASN 3   29  ?   ?   ?   A . n 
A 1 4   PHE 4   30  ?   ?   ?   A . n 
A 1 5   SER 5   31  ?   ?   ?   A . n 
A 1 6   ARG 6   32  32  ARG ARG A . n 
A 1 7   SER 7   33  33  SER SER A . n 
A 1 8   TYR 8   34  34  TYR TYR A . n 
A 1 9   PRO 9   35  35  PRO PRO A . n 
A 1 10  CYS 10  36  36  CYS CYS A . n 
A 1 11  ASP 11  37  37  ASP ASP A . n 
A 1 12  GLU 12  38  38  GLU GLU A . n 
A 1 13  LYS 13  39  39  LYS LYS A . n 
A 1 14  LYS 14  40  40  LYS LYS A . n 
A 1 15  GLN 15  41  ?   ?   ?   A . n 
A 1 16  ASN 16  42  ?   ?   ?   A . n 
A 1 17  ASP 17  43  43  ASP ASP A . n 
A 1 18  SER 18  44  44  SER SER A . n 
A 1 19  VAL 19  45  45  VAL VAL A . n 
A 1 20  ILE 20  46  46  ILE ILE A . n 
A 1 21  ALA 21  47  47  ALA ALA A . n 
A 1 22  GLU 22  48  48  GLU GLU A . n 
A 1 23  CYS 23  49  49  CYS CYS A . n 
A 1 24  SER 24  50  50  SER SER A . n 
A 1 25  ASN 25  51  51  ASN ASN A . n 
A 1 26  ARG 26  52  52  ARG ARG A . n 
A 1 27  ARG 27  53  53  ARG ARG A . n 
A 1 28  LEU 28  54  54  LEU LEU A . n 
A 1 29  GLN 29  55  55  GLN GLN A . n 
A 1 30  GLU 30  56  56  GLU GLU A . n 
A 1 31  VAL 31  57  57  VAL VAL A . n 
A 1 32  PRO 32  58  58  PRO PRO A . n 
A 1 33  GLN 33  59  59  GLN GLN A . n 
A 1 34  THR 34  60  60  THR THR A . n 
A 1 35  VAL 35  61  61  VAL VAL A . n 
A 1 36  GLY 36  62  62  GLY GLY A . n 
A 1 37  LYS 37  63  63  LYS LYS A . n 
A 1 38  TYR 38  64  64  TYR TYR A . n 
A 1 39  VAL 39  65  65  VAL VAL A . n 
A 1 40  THR 40  66  66  THR THR A . n 
A 1 41  GLU 41  67  67  GLU GLU A . n 
A 1 42  LEU 42  68  68  LEU LEU A . n 
A 1 43  ASP 43  69  69  ASP ASP A . n 
A 1 44  LEU 44  70  70  LEU LEU A . n 
A 1 45  SER 45  71  71  SER SER A . n 
A 1 46  ASP 46  72  72  ASP ASP A . n 
A 1 47  ASN 47  73  73  ASN ASN A . n 
A 1 48  PHE 48  74  74  PHE PHE A . n 
A 1 49  ILE 49  75  75  ILE ILE A . n 
A 1 50  THR 50  76  76  THR THR A . n 
A 1 51  HIS 51  77  77  HIS HIS A . n 
A 1 52  ILE 52  78  78  ILE ILE A . n 
A 1 53  THR 53  79  79  THR THR A . n 
A 1 54  ASN 54  80  80  ASN ASN A . n 
A 1 55  GLU 55  81  81  GLU GLU A . n 
A 1 56  SER 56  82  82  SER SER A . n 
A 1 57  PHE 57  83  83  PHE PHE A . n 
A 1 58  GLN 58  84  84  GLN GLN A . n 
A 1 59  GLY 59  85  85  GLY GLY A . n 
A 1 60  LEU 60  86  86  LEU LEU A . n 
A 1 61  GLN 61  87  87  GLN GLN A . n 
A 1 62  ASN 62  88  88  ASN ASN A . n 
A 1 63  LEU 63  89  89  LEU LEU A . n 
A 1 64  THR 64  90  90  THR THR A . n 
A 1 65  LYS 65  91  91  LYS LYS A . n 
A 1 66  ILE 66  92  92  ILE ILE A . n 
A 1 67  ASN 67  93  93  ASN ASN A . n 
A 1 68  LEU 68  94  94  LEU LEU A . n 
A 1 69  ASN 69  95  95  ASN ASN A . n 
A 1 70  HIS 70  96  96  HIS HIS A . n 
A 1 71  ASN 71  97  97  ASN ASN A . n 
A 1 72  PRO 72  98  98  PRO PRO A . n 
A 1 73  ASN 73  99  99  ASN ASN A . n 
A 1 74  VAL 74  100 ?   ?   ?   A . n 
A 1 75  GLN 75  101 ?   ?   ?   A . n 
A 1 76  HIS 76  102 ?   ?   ?   A . n 
A 1 77  GLN 77  103 ?   ?   ?   A . n 
A 1 78  ASN 78  104 ?   ?   ?   A . n 
A 1 79  GLY 79  105 ?   ?   ?   A . n 
A 1 80  ASN 80  106 ?   ?   ?   A . n 
A 1 81  PRO 81  107 ?   ?   ?   A . n 
A 1 82  GLY 82  108 ?   ?   ?   A . n 
A 1 83  ILE 83  109 ?   ?   ?   A . n 
A 1 84  GLN 84  110 ?   ?   ?   A . n 
A 1 85  SER 85  111 ?   ?   ?   A . n 
A 1 86  ASN 86  112 ?   ?   ?   A . n 
A 1 87  GLY 87  113 113 GLY GLY A . n 
A 1 88  LEU 88  114 114 LEU LEU A . n 
A 1 89  ASN 89  115 115 ASN ASN A . n 
A 1 90  ILE 90  116 116 ILE ILE A . n 
A 1 91  THR 91  117 117 THR THR A . n 
A 1 92  ASP 92  118 118 ASP ASP A . n 
A 1 93  GLY 93  119 119 GLY GLY A . n 
A 1 94  ALA 94  120 120 ALA ALA A . n 
A 1 95  PHE 95  121 121 PHE PHE A . n 
A 1 96  LEU 96  122 122 LEU LEU A . n 
A 1 97  ASN 97  123 123 ASN ASN A . n 
A 1 98  LEU 98  124 124 LEU LEU A . n 
A 1 99  LYS 99  125 125 LYS LYS A . n 
A 1 100 ASN 100 126 126 ASN ASN A . n 
A 1 101 LEU 101 127 127 LEU LEU A . n 
A 1 102 ARG 102 128 128 ARG ARG A . n 
A 1 103 GLU 103 129 129 GLU GLU A . n 
A 1 104 LEU 104 130 130 LEU LEU A . n 
A 1 105 LEU 105 131 131 LEU LEU A . n 
A 1 106 LEU 106 132 132 LEU LEU A . n 
A 1 107 GLU 107 133 133 GLU GLU A . n 
A 1 108 ASP 108 134 134 ASP ASP A . n 
A 1 109 ASN 109 135 135 ASN ASN A . n 
A 1 110 GLN 110 136 136 GLN GLN A . n 
A 1 111 LEU 111 137 137 LEU LEU A . n 
A 1 112 PRO 112 138 138 PRO PRO A . n 
A 1 113 GLN 113 139 139 GLN GLN A . n 
A 1 114 ILE 114 140 140 ILE ILE A . n 
A 1 115 PRO 115 141 141 PRO PRO A . n 
A 1 116 SER 116 142 142 SER SER A . n 
A 1 117 GLY 117 143 143 GLY GLY A . n 
A 1 118 LEU 118 144 144 LEU LEU A . n 
A 1 119 PRO 119 145 145 PRO PRO A . n 
A 1 120 GLU 120 146 146 GLU GLU A . n 
A 1 121 SER 121 147 147 SER SER A . n 
A 1 122 LEU 122 148 148 LEU LEU A . n 
A 1 123 THR 123 149 149 THR THR A . n 
A 1 124 GLU 124 150 150 GLU GLU A . n 
A 1 125 LEU 125 151 151 LEU LEU A . n 
A 1 126 SER 126 152 152 SER SER A . n 
A 1 127 LEU 127 153 153 LEU LEU A . n 
A 1 128 ILE 128 154 154 ILE ILE A . n 
A 1 129 GLN 129 155 155 GLN GLN A . n 
A 1 130 ASN 130 156 156 ASN ASN A . n 
A 1 131 ASN 131 157 157 ASN ASN A . n 
A 1 132 ILE 132 158 158 ILE ILE A . n 
A 1 133 TYR 133 159 159 TYR TYR A . n 
A 1 134 ASN 134 160 160 ASN ASN A . n 
A 1 135 ILE 135 161 161 ILE ILE A . n 
A 1 136 THR 136 162 162 THR THR A . n 
A 1 137 LYS 137 163 163 LYS LYS A . n 
A 1 138 GLU 138 164 164 GLU GLU A . n 
A 1 139 GLY 139 165 165 GLY GLY A . n 
A 1 140 ILE 140 166 166 ILE ILE A . n 
A 1 141 SER 141 167 167 SER SER A . n 
A 1 142 ARG 142 168 168 ARG ARG A . n 
A 1 143 LEU 143 169 169 LEU LEU A . n 
A 1 144 ILE 144 170 170 ILE ILE A . n 
A 1 145 ASN 145 171 171 ASN ASN A . n 
A 1 146 LEU 146 172 172 LEU LEU A . n 
A 1 147 LYS 147 173 173 LYS LYS A . n 
A 1 148 ASN 148 174 174 ASN ASN A . n 
A 1 149 LEU 149 175 175 LEU LEU A . n 
A 1 150 TYR 150 176 176 TYR TYR A . n 
A 1 151 LEU 151 177 177 LEU LEU A . n 
A 1 152 ALA 152 178 178 ALA ALA A . n 
A 1 153 TRP 153 179 179 TRP TRP A . n 
A 1 154 ASN 154 180 180 ASN ASN A . n 
A 1 155 CYS 155 181 181 CYS CYS A . n 
A 1 156 TYR 156 182 182 TYR TYR A . n 
A 1 157 PHE 157 183 183 PHE PHE A . n 
A 1 158 ASN 158 184 184 ASN ASN A . n 
A 1 159 LYS 159 185 185 LYS LYS A . n 
A 1 160 VAL 160 186 186 VAL VAL A . n 
A 1 161 CYS 161 187 187 CYS CYS A . n 
A 1 162 GLU 162 188 188 GLU GLU A . n 
A 1 163 LYS 163 189 189 LYS LYS A . n 
A 1 164 THR 164 190 190 THR THR A . n 
A 1 165 ASN 165 191 191 ASN ASN A . n 
A 1 166 ILE 166 192 192 ILE ILE A . n 
A 1 167 GLU 167 193 193 GLU GLU A . n 
A 1 168 ASP 168 194 194 ASP ASP A . n 
A 1 169 GLY 169 195 195 GLY GLY A . n 
A 1 170 VAL 170 196 196 VAL VAL A . n 
A 1 171 PHE 171 197 197 PHE PHE A . n 
A 1 172 GLU 172 198 198 GLU GLU A . n 
A 1 173 THR 173 199 199 THR THR A . n 
A 1 174 LEU 174 200 200 LEU LEU A . n 
A 1 175 THR 175 201 201 THR THR A . n 
A 1 176 ASN 176 202 202 ASN ASN A . n 
A 1 177 LEU 177 203 203 LEU LEU A . n 
A 1 178 GLU 178 204 204 GLU GLU A . n 
A 1 179 LEU 179 205 205 LEU LEU A . n 
A 1 180 LEU 180 206 206 LEU LEU A . n 
A 1 181 SER 181 207 207 SER SER A . n 
A 1 182 LEU 182 208 208 LEU LEU A . n 
A 1 183 SER 183 209 209 SER SER A . n 
A 1 184 PHE 184 210 210 PHE PHE A . n 
A 1 185 ASN 185 211 211 ASN ASN A . n 
A 1 186 SER 186 212 212 SER SER A . n 
A 1 187 LEU 187 213 213 LEU LEU A . n 
A 1 188 SER 188 214 214 SER SER A . n 
A 1 189 HIS 189 215 215 HIS HIS A . n 
A 1 190 VAL 190 216 216 VAL VAL A . n 
A 1 191 PRO 191 217 217 PRO PRO A . n 
A 1 192 PRO 192 218 218 PRO PRO A . n 
A 1 193 LYS 193 219 219 LYS LYS A . n 
A 1 194 LEU 194 220 220 LEU LEU A . n 
A 1 195 PRO 195 221 221 PRO PRO A . n 
A 1 196 SER 196 222 222 SER SER A . n 
A 1 197 SER 197 223 223 SER SER A . n 
A 1 198 LEU 198 224 224 LEU LEU A . n 
A 1 199 ARG 199 225 225 ARG ARG A . n 
A 1 200 LYS 200 226 226 LYS LYS A . n 
A 1 201 LEU 201 227 227 LEU LEU A . n 
A 1 202 PHE 202 228 228 PHE PHE A . n 
A 1 203 LEU 203 229 229 LEU LEU A . n 
A 1 204 SER 204 230 230 SER SER A . n 
A 1 205 ASN 205 231 231 ASN ASN A . n 
A 1 206 THR 206 232 232 THR THR A . n 
A 1 207 GLN 207 233 233 GLN GLN A . n 
A 1 208 ILE 208 234 234 ILE ILE A . n 
A 1 209 LYS 209 235 235 LYS LYS A . n 
A 1 210 TYR 210 236 236 TYR TYR A . n 
A 1 211 ILE 211 237 237 ILE ILE A . n 
A 1 212 SER 212 238 238 SER SER A . n 
A 1 213 GLU 213 239 239 GLU GLU A . n 
A 1 214 GLU 214 240 240 GLU GLU A . n 
A 1 215 ASP 215 241 241 ASP ASP A . n 
A 1 216 PHE 216 242 242 PHE PHE A . n 
A 1 217 LYS 217 243 243 LYS LYS A . n 
A 1 218 GLY 218 244 244 GLY GLY A . n 
A 1 219 LEU 219 245 245 LEU LEU A . n 
A 1 220 ILE 220 246 246 ILE ILE A . n 
A 1 221 ASN 221 247 247 ASN ASN A . n 
A 1 222 LEU 222 248 248 LEU LEU A . n 
A 1 223 THR 223 249 249 THR THR A . n 
A 1 224 LEU 224 250 250 LEU LEU A . n 
A 1 225 LEU 225 251 251 LEU LEU A . n 
A 1 226 ASP 226 252 252 ASP ASP A . n 
A 1 227 LEU 227 253 253 LEU LEU A . n 
A 1 228 SER 228 254 254 SER SER A . n 
A 1 229 GLY 229 255 255 GLY GLY A . n 
A 1 230 ASN 230 256 256 ASN ASN A . n 
A 1 231 CYS 231 257 257 CYS CYS A . n 
A 1 232 PRO 232 258 258 PRO PRO A . n 
A 1 233 ARG 233 259 259 ARG ARG A . n 
A 1 234 CYS 234 260 260 CYS CYS A . n 
A 1 235 PHE 235 261 261 PHE PHE A . n 
A 1 236 ASN 236 262 262 ASN ASN A . n 
A 1 237 ALA 237 263 263 ALA ALA A . n 
A 1 238 PRO 238 264 264 PRO PRO A . n 
A 1 239 PHE 239 265 265 PHE PHE A . n 
A 1 240 PRO 240 266 266 PRO PRO A . n 
A 1 241 CYS 241 267 267 CYS CYS A . n 
A 1 242 VAL 242 268 268 VAL VAL A . n 
A 1 243 PRO 243 269 269 PRO PRO A . n 
A 1 244 CYS 244 270 270 CYS CYS A . n 
A 1 245 ASP 245 271 271 ASP ASP A . n 
A 1 246 GLY 246 272 272 GLY GLY A . n 
A 1 247 GLY 247 273 273 GLY GLY A . n 
A 1 248 ALA 248 274 274 ALA ALA A . n 
A 1 249 SER 249 275 275 SER SER A . n 
A 1 250 ILE 250 276 276 ILE ILE A . n 
A 1 251 ASN 251 277 277 ASN ASN A . n 
A 1 252 ILE 252 278 278 ILE ILE A . n 
A 1 253 ASP 253 279 279 ASP ASP A . n 
A 1 254 ARG 254 280 280 ARG ARG A . n 
A 1 255 PHE 255 281 281 PHE PHE A . n 
A 1 256 ALA 256 282 282 ALA ALA A . n 
A 1 257 PHE 257 283 283 PHE PHE A . n 
A 1 258 GLN 258 284 284 GLN GLN A . n 
A 1 259 ASN 259 285 285 ASN ASN A . n 
A 1 260 LEU 260 286 286 LEU LEU A . n 
A 1 261 THR 261 287 287 THR THR A . n 
A 1 262 GLN 262 288 288 GLN GLN A . n 
A 1 263 LEU 263 289 289 LEU LEU A . n 
A 1 264 ARG 264 290 290 ARG ARG A . n 
A 1 265 TYR 265 291 291 TYR TYR A . n 
A 1 266 LEU 266 292 292 LEU LEU A . n 
A 1 267 ASN 267 293 293 ASN ASN A . n 
A 1 268 LEU 268 294 294 LEU LEU A . n 
A 1 269 SER 269 295 295 SER SER A . n 
A 1 270 SER 270 296 296 SER SER A . n 
A 1 271 THR 271 297 297 THR THR A . n 
A 1 272 SER 272 298 298 SER SER A . n 
A 1 273 LEU 273 299 299 LEU LEU A . n 
A 1 274 ARG 274 300 300 ARG ARG A . n 
A 1 275 LYS 275 301 301 LYS LYS A . n 
A 1 276 ILE 276 302 302 ILE ILE A . n 
A 1 277 ASN 277 303 303 ASN ASN A . n 
A 1 278 ALA 278 304 304 ALA ALA A . n 
A 1 279 ALA 279 305 305 ALA ALA A . n 
A 1 280 TRP 280 306 306 TRP TRP A . n 
A 1 281 PHE 281 307 307 PHE PHE A . n 
A 1 282 LYS 282 308 308 LYS LYS A . n 
A 1 283 ASN 283 309 309 ASN ASN A . n 
A 1 284 MET 284 310 310 MET MET A . n 
A 1 285 PRO 285 311 311 PRO PRO A . n 
A 1 286 HIS 286 312 312 HIS HIS A . n 
A 1 287 LEU 287 313 313 LEU LEU A . n 
A 1 288 LYS 288 314 314 LYS LYS A . n 
A 1 289 VAL 289 315 315 VAL VAL A . n 
A 1 290 LEU 290 316 316 LEU LEU A . n 
A 1 291 ASP 291 317 317 ASP ASP A . n 
A 1 292 LEU 292 318 318 LEU LEU A . n 
A 1 293 GLU 293 319 319 GLU GLU A . n 
A 1 294 PHE 294 320 320 PHE PHE A . n 
A 1 295 ASN 295 321 321 ASN ASN A . n 
A 1 296 TYR 296 322 322 TYR TYR A . n 
A 1 297 LEU 297 323 323 LEU LEU A . n 
A 1 298 VAL 298 324 324 VAL VAL A . n 
A 1 299 GLY 299 325 325 GLY GLY A . n 
A 1 300 GLU 300 326 326 GLU GLU A . n 
A 1 301 ILE 301 327 327 ILE ILE A . n 
A 1 302 ALA 302 328 328 ALA ALA A . n 
A 1 303 SER 303 329 329 SER SER A . n 
A 1 304 GLY 304 330 330 GLY GLY A . n 
A 1 305 ALA 305 331 331 ALA ALA A . n 
A 1 306 PHE 306 332 332 PHE PHE A . n 
A 1 307 LEU 307 333 333 LEU LEU A . n 
A 1 308 THR 308 334 334 THR THR A . n 
A 1 309 MET 309 335 335 MET MET A . n 
A 1 310 LEU 310 336 336 LEU LEU A . n 
A 1 311 PRO 311 337 337 PRO PRO A . n 
A 1 312 ARG 312 338 338 ARG ARG A . n 
A 1 313 LEU 313 339 339 LEU LEU A . n 
A 1 314 GLU 314 340 340 GLU GLU A . n 
A 1 315 ILE 315 341 341 ILE ILE A . n 
A 1 316 LEU 316 342 342 LEU LEU A . n 
A 1 317 ASP 317 343 343 ASP ASP A . n 
A 1 318 LEU 318 344 344 LEU LEU A . n 
A 1 319 SER 319 345 345 SER SER A . n 
A 1 320 PHE 320 346 346 PHE PHE A . n 
A 1 321 ASN 321 347 347 ASN ASN A . n 
A 1 322 TYR 322 348 348 TYR TYR A . n 
A 1 323 ILE 323 349 349 ILE ILE A . n 
A 1 324 LYS 324 350 350 LYS LYS A . n 
A 1 325 GLY 325 351 351 GLY GLY A . n 
A 1 326 SER 326 352 352 SER SER A . n 
A 1 327 TYR 327 353 353 TYR TYR A . n 
A 1 328 PRO 328 354 354 PRO PRO A . n 
A 1 329 GLN 329 355 355 GLN GLN A . n 
A 1 330 HIS 330 356 356 HIS HIS A . n 
A 1 331 ILE 331 357 357 ILE ILE A . n 
A 1 332 ASN 332 358 358 ASN ASN A . n 
A 1 333 ILE 333 359 359 ILE ILE A . n 
A 1 334 SER 334 360 360 SER SER A . n 
A 1 335 ARG 335 361 361 ARG ARG A . n 
A 1 336 ASN 336 362 362 ASN ASN A . n 
A 1 337 PHE 337 363 363 PHE PHE A . n 
A 1 338 SER 338 364 364 SER SER A . n 
A 1 339 LYS 339 365 365 LYS LYS A . n 
A 1 340 LEU 340 366 366 LEU LEU A . n 
A 1 341 LEU 341 367 367 LEU LEU A . n 
A 1 342 SER 342 368 368 SER SER A . n 
A 1 343 LEU 343 369 369 LEU LEU A . n 
A 1 344 ARG 344 370 370 ARG ARG A . n 
A 1 345 ALA 345 371 371 ALA ALA A . n 
A 1 346 LEU 346 372 372 LEU LEU A . n 
A 1 347 HIS 347 373 373 HIS HIS A . n 
A 1 348 LEU 348 374 374 LEU LEU A . n 
A 1 349 ARG 349 375 375 ARG ARG A . n 
A 1 350 GLY 350 376 376 GLY GLY A . n 
A 1 351 TYR 351 377 377 TYR TYR A . n 
A 1 352 VAL 352 378 378 VAL VAL A . n 
A 1 353 PHE 353 379 379 PHE PHE A . n 
A 1 354 GLN 354 380 380 GLN GLN A . n 
A 1 355 GLU 355 381 381 GLU GLU A . n 
A 1 356 LEU 356 382 382 LEU LEU A . n 
A 1 357 ARG 357 383 383 ARG ARG A . n 
A 1 358 GLU 358 384 384 GLU GLU A . n 
A 1 359 ASP 359 385 385 ASP ASP A . n 
A 1 360 ASP 360 386 386 ASP ASP A . n 
A 1 361 PHE 361 387 387 PHE PHE A . n 
A 1 362 GLN 362 388 388 GLN GLN A . n 
A 1 363 PRO 363 389 389 PRO PRO A . n 
A 1 364 LEU 364 390 390 LEU LEU A . n 
A 1 365 MET 365 391 391 MET MET A . n 
A 1 366 GLN 366 392 392 GLN GLN A . n 
A 1 367 LEU 367 393 393 LEU LEU A . n 
A 1 368 PRO 368 394 394 PRO PRO A . n 
A 1 369 ASN 369 395 395 ASN ASN A . n 
A 1 370 LEU 370 396 396 LEU LEU A . n 
A 1 371 SER 371 397 397 SER SER A . n 
A 1 372 THR 372 398 398 THR THR A . n 
A 1 373 ILE 373 399 399 ILE ILE A . n 
A 1 374 ASN 374 400 400 ASN ASN A . n 
A 1 375 LEU 375 401 401 LEU LEU A . n 
A 1 376 GLY 376 402 402 GLY GLY A . n 
A 1 377 ILE 377 403 403 ILE ILE A . n 
A 1 378 ASN 378 404 404 ASN ASN A . n 
A 1 379 PHE 379 405 405 PHE PHE A . n 
A 1 380 ILE 380 406 406 ILE ILE A . n 
A 1 381 LYS 381 407 407 LYS LYS A . n 
A 1 382 GLN 382 408 408 GLN GLN A . n 
A 1 383 ILE 383 409 409 ILE ILE A . n 
A 1 384 ASP 384 410 410 ASP ASP A . n 
A 1 385 PHE 385 411 411 PHE PHE A . n 
A 1 386 LYS 386 412 412 LYS LYS A . n 
A 1 387 LEU 387 413 413 LEU LEU A . n 
A 1 388 PHE 388 414 414 PHE PHE A . n 
A 1 389 GLN 389 415 415 GLN GLN A . n 
A 1 390 ASN 390 416 416 ASN ASN A . n 
A 1 391 PHE 391 417 417 PHE PHE A . n 
A 1 392 SER 392 418 418 SER SER A . n 
A 1 393 ASN 393 419 419 ASN ASN A . n 
A 1 394 LEU 394 420 420 LEU LEU A . n 
A 1 395 GLU 395 421 421 GLU GLU A . n 
A 1 396 ILE 396 422 422 ILE ILE A . n 
A 1 397 ILE 397 423 423 ILE ILE A . n 
A 1 398 TYR 398 424 424 TYR TYR A . n 
A 1 399 LEU 399 425 425 LEU LEU A . n 
A 1 400 SER 400 426 426 SER SER A . n 
A 1 401 GLU 401 427 427 GLU GLU A . n 
A 1 402 ASN 402 428 428 ASN ASN A . n 
A 1 403 ARG 403 429 429 ARG ARG A . n 
A 1 404 ILE 404 430 430 ILE ILE A . n 
A 1 405 SER 405 431 431 SER SER A . n 
A 1 406 PRO 406 432 432 PRO PRO A . n 
A 1 407 LEU 407 433 433 LEU LEU A . n 
A 1 408 VAL 408 434 ?   ?   ?   A . n 
A 1 409 LYS 409 435 ?   ?   ?   A . n 
A 1 410 ASP 410 436 ?   ?   ?   A . n 
A 1 411 THR 411 437 ?   ?   ?   A . n 
A 1 412 ARG 412 438 ?   ?   ?   A . n 
A 1 413 GLN 413 439 ?   ?   ?   A . n 
A 1 414 SER 414 440 ?   ?   ?   A . n 
A 1 415 TYR 415 441 ?   ?   ?   A . n 
A 1 416 ALA 416 442 ?   ?   ?   A . n 
A 1 417 ASN 417 443 ?   ?   ?   A . n 
A 1 418 SER 418 444 ?   ?   ?   A . n 
A 1 419 SER 419 445 ?   ?   ?   A . n 
A 1 420 SER 420 446 ?   ?   ?   A . n 
A 1 421 PHE 421 447 ?   ?   ?   A . n 
A 1 422 GLN 422 448 ?   ?   ?   A . n 
A 1 423 ARG 423 449 ?   ?   ?   A . n 
A 1 424 HIS 424 450 ?   ?   ?   A . n 
A 1 425 ILE 425 451 ?   ?   ?   A . n 
A 1 426 ARG 426 452 ?   ?   ?   A . n 
A 1 427 LYS 427 453 ?   ?   ?   A . n 
A 1 428 ARG 428 454 ?   ?   ?   A . n 
A 1 429 ARG 429 455 ?   ?   ?   A . n 
A 1 430 SER 430 456 ?   ?   ?   A . n 
A 1 431 THR 431 457 ?   ?   ?   A . n 
A 1 432 ASP 432 458 ?   ?   ?   A . n 
A 1 433 PHE 433 459 459 PHE PHE A . n 
A 1 434 GLU 434 460 460 GLU GLU A . n 
A 1 435 PHE 435 461 461 PHE PHE A . n 
A 1 436 ASP 436 462 462 ASP ASP A . n 
A 1 437 PRO 437 463 463 PRO PRO A . n 
A 1 438 HIS 438 464 464 HIS HIS A . n 
A 1 439 SER 439 465 465 SER SER A . n 
A 1 440 ASN 440 466 466 ASN ASN A . n 
A 1 441 PHE 441 467 467 PHE PHE A . n 
A 1 442 TYR 442 468 468 TYR TYR A . n 
A 1 443 HIS 443 469 469 HIS HIS A . n 
A 1 444 PHE 444 470 470 PHE PHE A . n 
A 1 445 THR 445 471 471 THR THR A . n 
A 1 446 ARG 446 472 472 ARG ARG A . n 
A 1 447 PRO 447 473 473 PRO PRO A . n 
A 1 448 LEU 448 474 474 LEU LEU A . n 
A 1 449 ILE 449 475 475 ILE ILE A . n 
A 1 450 LYS 450 476 476 LYS LYS A . n 
A 1 451 PRO 451 477 477 PRO PRO A . n 
A 1 452 GLN 452 478 478 GLN GLN A . n 
A 1 453 CYS 453 479 479 CYS CYS A . n 
A 1 454 ALA 454 480 480 ALA ALA A . n 
A 1 455 ALA 455 481 481 ALA ALA A . n 
A 1 456 TYR 456 482 482 TYR TYR A . n 
A 1 457 GLY 457 483 483 GLY GLY A . n 
A 1 458 LYS 458 484 484 LYS LYS A . n 
A 1 459 ALA 459 485 485 ALA ALA A . n 
A 1 460 LEU 460 486 486 LEU LEU A . n 
A 1 461 ASP 461 487 487 ASP ASP A . n 
A 1 462 LEU 462 488 488 LEU LEU A . n 
A 1 463 SER 463 489 489 SER SER A . n 
A 1 464 LEU 464 490 490 LEU LEU A . n 
A 1 465 ASN 465 491 491 ASN ASN A . n 
A 1 466 SER 466 492 492 SER SER A . n 
A 1 467 ILE 467 493 493 ILE ILE A . n 
A 1 468 PHE 468 494 494 PHE PHE A . n 
A 1 469 PHE 469 495 495 PHE PHE A . n 
A 1 470 ILE 470 496 496 ILE ILE A . n 
A 1 471 GLY 471 497 497 GLY GLY A . n 
A 1 472 PRO 472 498 498 PRO PRO A . n 
A 1 473 ASN 473 499 499 ASN ASN A . n 
A 1 474 GLN 474 500 500 GLN GLN A . n 
A 1 475 PHE 475 501 501 PHE PHE A . n 
A 1 476 GLU 476 502 502 GLU GLU A . n 
A 1 477 ASN 477 503 503 ASN ASN A . n 
A 1 478 LEU 478 504 504 LEU LEU A . n 
A 1 479 PRO 479 505 505 PRO PRO A . n 
A 1 480 ASP 480 506 506 ASP ASP A . n 
A 1 481 ILE 481 507 507 ILE ILE A . n 
A 1 482 ALA 482 508 508 ALA ALA A . n 
A 1 483 CYS 483 509 509 CYS CYS A . n 
A 1 484 LEU 484 510 510 LEU LEU A . n 
A 1 485 ASN 485 511 511 ASN ASN A . n 
A 1 486 LEU 486 512 512 LEU LEU A . n 
A 1 487 SER 487 513 513 SER SER A . n 
A 1 488 ALA 488 514 514 ALA ALA A . n 
A 1 489 ASN 489 515 515 ASN ASN A . n 
A 1 490 SER 490 516 516 SER SER A . n 
A 1 491 ASN 491 517 517 ASN ASN A . n 
A 1 492 ALA 492 518 518 ALA ALA A . n 
A 1 493 GLN 493 519 519 GLN GLN A . n 
A 1 494 VAL 494 520 520 VAL VAL A . n 
A 1 495 LEU 495 521 521 LEU LEU A . n 
A 1 496 SER 496 522 522 SER SER A . n 
A 1 497 GLY 497 523 523 GLY GLY A . n 
A 1 498 THR 498 524 524 THR THR A . n 
A 1 499 GLU 499 525 525 GLU GLU A . n 
A 1 500 PHE 500 526 526 PHE PHE A . n 
A 1 501 SER 501 527 527 SER SER A . n 
A 1 502 ALA 502 528 528 ALA ALA A . n 
A 1 503 ILE 503 529 529 ILE ILE A . n 
A 1 504 PRO 504 530 530 PRO PRO A . n 
A 1 505 HIS 505 531 531 HIS HIS A . n 
A 1 506 VAL 506 532 532 VAL VAL A . n 
A 1 507 LYS 507 533 533 LYS LYS A . n 
A 1 508 TYR 508 534 534 TYR TYR A . n 
A 1 509 LEU 509 535 535 LEU LEU A . n 
A 1 510 ASP 510 536 536 ASP ASP A . n 
A 1 511 LEU 511 537 537 LEU LEU A . n 
A 1 512 THR 512 538 538 THR THR A . n 
A 1 513 ASN 513 539 539 ASN ASN A . n 
A 1 514 ASN 514 540 540 ASN ASN A . n 
A 1 515 ARG 515 541 541 ARG ARG A . n 
A 1 516 LEU 516 542 542 LEU LEU A . n 
A 1 517 ASP 517 543 543 ASP ASP A . n 
A 1 518 PHE 518 544 544 PHE PHE A . n 
A 1 519 ASP 519 545 545 ASP ASP A . n 
A 1 520 ASN 520 546 546 ASN ASN A . n 
A 1 521 ALA 521 547 547 ALA ALA A . n 
A 1 522 SER 522 548 548 SER SER A . n 
A 1 523 ALA 523 549 549 ALA ALA A . n 
A 1 524 LEU 524 550 550 LEU LEU A . n 
A 1 525 THR 525 551 551 THR THR A . n 
A 1 526 GLU 526 552 552 GLU GLU A . n 
A 1 527 LEU 527 553 553 LEU LEU A . n 
A 1 528 SER 528 554 554 SER SER A . n 
A 1 529 ASP 529 555 555 ASP ASP A . n 
A 1 530 LEU 530 556 556 LEU LEU A . n 
A 1 531 GLU 531 557 557 GLU GLU A . n 
A 1 532 VAL 532 558 558 VAL VAL A . n 
A 1 533 LEU 533 559 559 LEU LEU A . n 
A 1 534 ASP 534 560 560 ASP ASP A . n 
A 1 535 LEU 535 561 561 LEU LEU A . n 
A 1 536 SER 536 562 562 SER SER A . n 
A 1 537 TYR 537 563 563 TYR TYR A . n 
A 1 538 ASN 538 564 564 ASN ASN A . n 
A 1 539 SER 539 565 565 SER SER A . n 
A 1 540 HIS 540 566 566 HIS HIS A . n 
A 1 541 TYR 541 567 567 TYR TYR A . n 
A 1 542 PHE 542 568 568 PHE PHE A . n 
A 1 543 ARG 543 569 569 ARG ARG A . n 
A 1 544 ILE 544 570 570 ILE ILE A . n 
A 1 545 ALA 545 571 571 ALA ALA A . n 
A 1 546 GLY 546 572 572 GLY GLY A . n 
A 1 547 VAL 547 573 573 VAL VAL A . n 
A 1 548 THR 548 574 574 THR THR A . n 
A 1 549 HIS 549 575 575 HIS HIS A . n 
A 1 550 HIS 550 576 576 HIS HIS A . n 
A 1 551 LEU 551 577 577 LEU LEU A . n 
A 1 552 GLU 552 578 578 GLU GLU A . n 
A 1 553 PHE 553 579 579 PHE PHE A . n 
A 1 554 ILE 554 580 580 ILE ILE A . n 
A 1 555 GLN 555 581 581 GLN GLN A . n 
A 1 556 ASN 556 582 582 ASN ASN A . n 
A 1 557 PHE 557 583 583 PHE PHE A . n 
A 1 558 THR 558 584 584 THR THR A . n 
A 1 559 ASN 559 585 585 ASN ASN A . n 
A 1 560 LEU 560 586 586 LEU LEU A . n 
A 1 561 LYS 561 587 587 LYS LYS A . n 
A 1 562 VAL 562 588 588 VAL VAL A . n 
A 1 563 LEU 563 589 589 LEU LEU A . n 
A 1 564 ASN 564 590 590 ASN ASN A . n 
A 1 565 LEU 565 591 591 LEU LEU A . n 
A 1 566 SER 566 592 592 SER SER A . n 
A 1 567 HIS 567 593 593 HIS HIS A . n 
A 1 568 ASN 568 594 594 ASN ASN A . n 
A 1 569 ASN 569 595 595 ASN ASN A . n 
A 1 570 ILE 570 596 596 ILE ILE A . n 
A 1 571 TYR 571 597 597 TYR TYR A . n 
A 1 572 THR 572 598 598 THR THR A . n 
A 1 573 LEU 573 599 599 LEU LEU A . n 
A 1 574 THR 574 600 600 THR THR A . n 
A 1 575 ASP 575 601 601 ASP ASP A . n 
A 1 576 LYS 576 602 602 LYS LYS A . n 
A 1 577 TYR 577 603 603 TYR TYR A . n 
A 1 578 ASN 578 604 604 ASN ASN A . n 
A 1 579 LEU 579 605 605 LEU LEU A . n 
A 1 580 GLU 580 606 606 GLU GLU A . n 
A 1 581 SER 581 607 607 SER SER A . n 
A 1 582 LYS 582 608 608 LYS LYS A . n 
A 1 583 SER 583 609 609 SER SER A . n 
A 1 584 LEU 584 610 610 LEU LEU A . n 
A 1 585 VAL 585 611 611 VAL VAL A . n 
A 1 586 GLU 586 612 612 GLU GLU A . n 
A 1 587 LEU 587 613 613 LEU LEU A . n 
A 1 588 VAL 588 614 614 VAL VAL A . n 
A 1 589 PHE 589 615 615 PHE PHE A . n 
A 1 590 SER 590 616 616 SER SER A . n 
A 1 591 GLY 591 617 617 GLY GLY A . n 
A 1 592 ASN 592 618 618 ASN ASN A . n 
A 1 593 ARG 593 619 619 ARG ARG A . n 
A 1 594 LEU 594 620 620 LEU LEU A . n 
A 1 595 ASP 595 621 621 ASP ASP A . n 
A 1 596 ILE 596 622 622 ILE ILE A . n 
A 1 597 LEU 597 623 623 LEU LEU A . n 
A 1 598 TRP 598 624 624 TRP TRP A . n 
A 1 599 ASN 599 625 625 ASN ASN A . n 
A 1 600 ASP 600 626 626 ASP ASP A . n 
A 1 601 ASP 601 627 627 ASP ASP A . n 
A 1 602 ASP 602 628 628 ASP ASP A . n 
A 1 603 ASN 603 629 629 ASN ASN A . n 
A 1 604 ARG 604 630 630 ARG ARG A . n 
A 1 605 TYR 605 631 631 TYR TYR A . n 
A 1 606 ILE 606 632 632 ILE ILE A . n 
A 1 607 SER 607 633 633 SER SER A . n 
A 1 608 ILE 608 634 634 ILE ILE A . n 
A 1 609 PHE 609 635 635 PHE PHE A . n 
A 1 610 LYS 610 636 636 LYS LYS A . n 
A 1 611 GLY 611 637 637 GLY GLY A . n 
A 1 612 LEU 612 638 638 LEU LEU A . n 
A 1 613 LYS 613 639 639 LYS LYS A . n 
A 1 614 ASN 614 640 640 ASN ASN A . n 
A 1 615 LEU 615 641 641 LEU LEU A . n 
A 1 616 THR 616 642 642 THR THR A . n 
A 1 617 ARG 617 643 643 ARG ARG A . n 
A 1 618 LEU 618 644 644 LEU LEU A . n 
A 1 619 ASP 619 645 645 ASP ASP A . n 
A 1 620 LEU 620 646 646 LEU LEU A . n 
A 1 621 SER 621 647 647 SER SER A . n 
A 1 622 LEU 622 648 648 LEU LEU A . n 
A 1 623 ASN 623 649 649 ASN ASN A . n 
A 1 624 ARG 624 650 650 ARG ARG A . n 
A 1 625 LEU 625 651 651 LEU LEU A . n 
A 1 626 LYS 626 652 652 LYS LYS A . n 
A 1 627 HIS 627 653 653 HIS HIS A . n 
A 1 628 ILE 628 654 654 ILE ILE A . n 
A 1 629 PRO 629 655 655 PRO PRO A . n 
A 1 630 ASN 630 656 656 ASN ASN A . n 
A 1 631 GLU 631 657 657 GLU GLU A . n 
A 1 632 ALA 632 658 658 ALA ALA A . n 
A 1 633 PHE 633 659 659 PHE PHE A . n 
A 1 634 LEU 634 660 660 LEU LEU A . n 
A 1 635 ASN 635 661 661 ASN ASN A . n 
A 1 636 LEU 636 662 662 LEU LEU A . n 
A 1 637 PRO 637 663 663 PRO PRO A . n 
A 1 638 ALA 638 664 664 ALA ALA A . n 
A 1 639 SER 639 665 665 SER SER A . n 
A 1 640 LEU 640 666 666 LEU LEU A . n 
A 1 641 THR 641 667 667 THR THR A . n 
A 1 642 GLU 642 668 668 GLU GLU A . n 
A 1 643 LEU 643 669 669 LEU LEU A . n 
A 1 644 HIS 644 670 670 HIS HIS A . n 
A 1 645 ILE 645 671 671 ILE ILE A . n 
A 1 646 ASN 646 672 672 ASN ASN A . n 
A 1 647 ASP 647 673 673 ASP ASP A . n 
A 1 648 ASN 648 674 674 ASN ASN A . n 
A 1 649 MET 649 675 675 MET MET A . n 
A 1 650 LEU 650 676 676 LEU LEU A . n 
A 1 651 LYS 651 677 677 LYS LYS A . n 
A 1 652 PHE 652 678 678 PHE PHE A . n 
A 1 653 PHE 653 679 679 PHE PHE A . n 
A 1 654 ASN 654 680 680 ASN ASN A . n 
A 1 655 TRP 655 681 681 TRP TRP A . n 
A 1 656 THR 656 682 682 THR THR A . n 
A 1 657 LEU 657 683 683 LEU LEU A . n 
A 1 658 LEU 658 684 684 LEU LEU A . n 
A 1 659 GLN 659 685 685 GLN GLN A . n 
A 1 660 GLN 660 686 686 GLN GLN A . n 
A 1 661 PHE 661 687 687 PHE PHE A . n 
A 1 662 PRO 662 688 688 PRO PRO A . n 
A 1 663 ARG 663 689 689 ARG ARG A . n 
A 1 664 LEU 664 690 690 LEU LEU A . n 
A 1 665 GLU 665 691 691 GLU GLU A . n 
A 1 666 LEU 666 692 692 LEU LEU A . n 
A 1 667 LEU 667 693 693 LEU LEU A . n 
A 1 668 ASP 668 694 694 ASP ASP A . n 
A 1 669 LEU 669 695 695 LEU LEU A . n 
A 1 670 ARG 670 696 696 ARG ARG A . n 
A 1 671 GLY 671 697 697 GLY GLY A . n 
A 1 672 ASN 672 698 698 ASN ASN A . n 
A 1 673 LYS 673 699 699 LYS LYS A . n 
A 1 674 LEU 674 700 700 LEU LEU A . n 
A 1 675 LEU 675 701 701 LEU LEU A . n 
A 1 676 PHE 676 702 702 PHE PHE A . n 
A 1 677 LEU 677 703 703 LEU LEU A . n 
A 1 678 THR 678 704 704 THR THR A . n 
A 1 679 ASP 679 705 705 ASP ASP A . n 
A 1 680 SER 680 706 706 SER SER A . n 
A 1 681 LEU 681 707 707 LEU LEU A . n 
A 1 682 SER 682 708 708 SER SER A . n 
A 1 683 ASP 683 709 709 ASP ASP A . n 
A 1 684 PHE 684 710 710 PHE PHE A . n 
A 1 685 THR 685 711 711 THR THR A . n 
A 1 686 SER 686 712 712 SER SER A . n 
A 1 687 SER 687 713 713 SER SER A . n 
A 1 688 LEU 688 714 714 LEU LEU A . n 
A 1 689 ARG 689 715 715 ARG ARG A . n 
A 1 690 THR 690 716 716 THR THR A . n 
A 1 691 LEU 691 717 717 LEU LEU A . n 
A 1 692 LEU 692 718 718 LEU LEU A . n 
A 1 693 LEU 693 719 719 LEU LEU A . n 
A 1 694 SER 694 720 720 SER SER A . n 
A 1 695 HIS 695 721 721 HIS HIS A . n 
A 1 696 ASN 696 722 722 ASN ASN A . n 
A 1 697 ARG 697 723 723 ARG ARG A . n 
A 1 698 ILE 698 724 724 ILE ILE A . n 
A 1 699 SER 699 725 725 SER SER A . n 
A 1 700 HIS 700 726 726 HIS HIS A . n 
A 1 701 LEU 701 727 727 LEU LEU A . n 
A 1 702 PRO 702 728 728 PRO PRO A . n 
A 1 703 SER 703 729 729 SER SER A . n 
A 1 704 GLY 704 730 730 GLY GLY A . n 
A 1 705 PHE 705 731 731 PHE PHE A . n 
A 1 706 LEU 706 732 732 LEU LEU A . n 
A 1 707 SER 707 733 733 SER SER A . n 
A 1 708 GLU 708 734 734 GLU GLU A . n 
A 1 709 VAL 709 735 735 VAL VAL A . n 
A 1 710 SER 710 736 736 SER SER A . n 
A 1 711 SER 711 737 737 SER SER A . n 
A 1 712 LEU 712 738 738 LEU LEU A . n 
A 1 713 LYS 713 739 739 LYS LYS A . n 
A 1 714 HIS 714 740 740 HIS HIS A . n 
A 1 715 LEU 715 741 741 LEU LEU A . n 
A 1 716 ASP 716 742 742 ASP ASP A . n 
A 1 717 LEU 717 743 743 LEU LEU A . n 
A 1 718 SER 718 744 744 SER SER A . n 
A 1 719 SER 719 745 745 SER SER A . n 
A 1 720 ASN 720 746 746 ASN ASN A . n 
A 1 721 LEU 721 747 747 LEU LEU A . n 
A 1 722 LEU 722 748 748 LEU LEU A . n 
A 1 723 LYS 723 749 749 LYS LYS A . n 
A 1 724 THR 724 750 750 THR THR A . n 
A 1 725 ILE 725 751 751 ILE ILE A . n 
A 1 726 ASN 726 752 752 ASN ASN A . n 
A 1 727 LYS 727 753 753 LYS LYS A . n 
A 1 728 SER 728 754 754 SER SER A . n 
A 1 729 ALA 729 755 755 ALA ALA A . n 
A 1 730 LEU 730 756 756 LEU LEU A . n 
A 1 731 GLU 731 757 757 GLU GLU A . n 
A 1 732 THR 732 758 758 THR THR A . n 
A 1 733 LYS 733 759 759 LYS LYS A . n 
A 1 734 THR 734 760 760 THR THR A . n 
A 1 735 THR 735 761 761 THR THR A . n 
A 1 736 THR 736 762 762 THR THR A . n 
A 1 737 LYS 737 763 763 LYS LYS A . n 
A 1 738 LEU 738 764 764 LEU LEU A . n 
A 1 739 SER 739 765 765 SER SER A . n 
A 1 740 MET 740 766 766 MET MET A . n 
A 1 741 LEU 741 767 767 LEU LEU A . n 
A 1 742 GLU 742 768 768 GLU GLU A . n 
A 1 743 LEU 743 769 769 LEU LEU A . n 
A 1 744 HIS 744 770 770 HIS HIS A . n 
A 1 745 GLY 745 771 771 GLY GLY A . n 
A 1 746 ASN 746 772 772 ASN ASN A . n 
A 1 747 PRO 747 773 773 PRO PRO A . n 
A 1 748 PHE 748 774 774 PHE PHE A . n 
A 1 749 GLU 749 775 775 GLU GLU A . n 
A 1 750 CYS 750 776 776 CYS CYS A . n 
A 1 751 THR 751 777 777 THR THR A . n 
A 1 752 CYS 752 778 778 CYS CYS A . n 
A 1 753 ASP 753 779 779 ASP ASP A . n 
A 1 754 ILE 754 780 780 ILE ILE A . n 
A 1 755 GLY 755 781 781 GLY GLY A . n 
A 1 756 ASP 756 782 782 ASP ASP A . n 
A 1 757 PHE 757 783 783 PHE PHE A . n 
A 1 758 ARG 758 784 784 ARG ARG A . n 
A 1 759 ARG 759 785 785 ARG ARG A . n 
A 1 760 TRP 760 786 786 TRP TRP A . n 
A 1 761 MET 761 787 787 MET MET A . n 
A 1 762 ASP 762 788 788 ASP ASP A . n 
A 1 763 GLU 763 789 789 GLU GLU A . n 
A 1 764 HIS 764 790 790 HIS HIS A . n 
A 1 765 LEU 765 791 791 LEU LEU A . n 
A 1 766 ASN 766 792 792 ASN ASN A . n 
A 1 767 VAL 767 793 793 VAL VAL A . n 
A 1 768 LYS 768 794 794 LYS LYS A . n 
A 1 769 ILE 769 795 795 ILE ILE A . n 
A 1 770 PRO 770 796 796 PRO PRO A . n 
A 1 771 ARG 771 797 797 ARG ARG A . n 
A 1 772 LEU 772 798 798 LEU LEU A . n 
A 1 773 VAL 773 799 799 VAL VAL A . n 
A 1 774 ASP 774 800 800 ASP ASP A . n 
A 1 775 VAL 775 801 801 VAL VAL A . n 
A 1 776 ILE 776 802 802 ILE ILE A . n 
A 1 777 CYS 777 803 803 CYS CYS A . n 
A 1 778 ALA 778 804 804 ALA ALA A . n 
A 1 779 SER 779 805 805 SER SER A . n 
A 1 780 PRO 780 806 806 PRO PRO A . n 
A 1 781 GLY 781 807 807 GLY GLY A . n 
A 1 782 ASP 782 808 808 ASP ASP A . n 
A 1 783 GLN 783 809 809 GLN GLN A . n 
A 1 784 ARG 784 810 810 ARG ARG A . n 
A 1 785 GLY 785 811 811 GLY GLY A . n 
A 1 786 LYS 786 812 812 LYS LYS A . n 
A 1 787 SER 787 813 813 SER SER A . n 
A 1 788 ILE 788 814 814 ILE ILE A . n 
A 1 789 VAL 789 815 815 VAL VAL A . n 
A 1 790 SER 790 816 816 SER SER A . n 
A 1 791 LEU 791 817 817 LEU LEU A . n 
A 1 792 GLU 792 818 818 GLU GLU A . n 
A 1 793 LEU 793 819 ?   ?   ?   A . n 
A 1 794 THR 794 820 ?   ?   ?   A . n 
A 1 795 THR 795 821 ?   ?   ?   A . n 
A 1 796 CYS 796 822 ?   ?   ?   A . n 
A 1 797 VAL 797 823 ?   ?   ?   A . n 
A 1 798 SER 798 824 ?   ?   ?   A . n 
A 1 799 ASP 799 825 ?   ?   ?   A . n 
A 1 800 VAL 800 826 ?   ?   ?   A . n 
A 1 801 THR 801 827 ?   ?   ?   A . n 
A 1 802 GLU 802 828 ?   ?   ?   A . n 
A 1 803 PHE 803 829 ?   ?   ?   A . n 
A 1 804 LEU 804 830 ?   ?   ?   A . n 
A 1 805 VAL 805 831 ?   ?   ?   A . n 
A 1 806 PRO 806 832 ?   ?   ?   A . n 
A 1 807 ARG 807 833 ?   ?   ?   A . n 
B 1 1   GLU 1   27  ?   ?   ?   B . n 
B 1 2   GLU 2   28  ?   ?   ?   B . n 
B 1 3   ASN 3   29  ?   ?   ?   B . n 
B 1 4   PHE 4   30  ?   ?   ?   B . n 
B 1 5   SER 5   31  ?   ?   ?   B . n 
B 1 6   ARG 6   32  32  ARG ARG B . n 
B 1 7   SER 7   33  33  SER SER B . n 
B 1 8   TYR 8   34  34  TYR TYR B . n 
B 1 9   PRO 9   35  35  PRO PRO B . n 
B 1 10  CYS 10  36  36  CYS CYS B . n 
B 1 11  ASP 11  37  37  ASP ASP B . n 
B 1 12  GLU 12  38  38  GLU GLU B . n 
B 1 13  LYS 13  39  39  LYS LYS B . n 
B 1 14  LYS 14  40  40  LYS LYS B . n 
B 1 15  GLN 15  41  ?   ?   ?   B . n 
B 1 16  ASN 16  42  ?   ?   ?   B . n 
B 1 17  ASP 17  43  43  ASP ASP B . n 
B 1 18  SER 18  44  44  SER SER B . n 
B 1 19  VAL 19  45  45  VAL VAL B . n 
B 1 20  ILE 20  46  46  ILE ILE B . n 
B 1 21  ALA 21  47  47  ALA ALA B . n 
B 1 22  GLU 22  48  48  GLU GLU B . n 
B 1 23  CYS 23  49  49  CYS CYS B . n 
B 1 24  SER 24  50  50  SER SER B . n 
B 1 25  ASN 25  51  51  ASN ASN B . n 
B 1 26  ARG 26  52  52  ARG ARG B . n 
B 1 27  ARG 27  53  53  ARG ARG B . n 
B 1 28  LEU 28  54  54  LEU LEU B . n 
B 1 29  GLN 29  55  55  GLN GLN B . n 
B 1 30  GLU 30  56  56  GLU GLU B . n 
B 1 31  VAL 31  57  57  VAL VAL B . n 
B 1 32  PRO 32  58  58  PRO PRO B . n 
B 1 33  GLN 33  59  59  GLN GLN B . n 
B 1 34  THR 34  60  60  THR THR B . n 
B 1 35  VAL 35  61  61  VAL VAL B . n 
B 1 36  GLY 36  62  62  GLY GLY B . n 
B 1 37  LYS 37  63  63  LYS LYS B . n 
B 1 38  TYR 38  64  64  TYR TYR B . n 
B 1 39  VAL 39  65  65  VAL VAL B . n 
B 1 40  THR 40  66  66  THR THR B . n 
B 1 41  GLU 41  67  67  GLU GLU B . n 
B 1 42  LEU 42  68  68  LEU LEU B . n 
B 1 43  ASP 43  69  69  ASP ASP B . n 
B 1 44  LEU 44  70  70  LEU LEU B . n 
B 1 45  SER 45  71  71  SER SER B . n 
B 1 46  ASP 46  72  72  ASP ASP B . n 
B 1 47  ASN 47  73  73  ASN ASN B . n 
B 1 48  PHE 48  74  74  PHE PHE B . n 
B 1 49  ILE 49  75  75  ILE ILE B . n 
B 1 50  THR 50  76  76  THR THR B . n 
B 1 51  HIS 51  77  77  HIS HIS B . n 
B 1 52  ILE 52  78  78  ILE ILE B . n 
B 1 53  THR 53  79  79  THR THR B . n 
B 1 54  ASN 54  80  80  ASN ASN B . n 
B 1 55  GLU 55  81  81  GLU GLU B . n 
B 1 56  SER 56  82  82  SER SER B . n 
B 1 57  PHE 57  83  83  PHE PHE B . n 
B 1 58  GLN 58  84  84  GLN GLN B . n 
B 1 59  GLY 59  85  85  GLY GLY B . n 
B 1 60  LEU 60  86  86  LEU LEU B . n 
B 1 61  GLN 61  87  87  GLN GLN B . n 
B 1 62  ASN 62  88  88  ASN ASN B . n 
B 1 63  LEU 63  89  89  LEU LEU B . n 
B 1 64  THR 64  90  90  THR THR B . n 
B 1 65  LYS 65  91  91  LYS LYS B . n 
B 1 66  ILE 66  92  92  ILE ILE B . n 
B 1 67  ASN 67  93  93  ASN ASN B . n 
B 1 68  LEU 68  94  94  LEU LEU B . n 
B 1 69  ASN 69  95  95  ASN ASN B . n 
B 1 70  HIS 70  96  96  HIS HIS B . n 
B 1 71  ASN 71  97  97  ASN ASN B . n 
B 1 72  PRO 72  98  98  PRO PRO B . n 
B 1 73  ASN 73  99  99  ASN ASN B . n 
B 1 74  VAL 74  100 ?   ?   ?   B . n 
B 1 75  GLN 75  101 ?   ?   ?   B . n 
B 1 76  HIS 76  102 ?   ?   ?   B . n 
B 1 77  GLN 77  103 ?   ?   ?   B . n 
B 1 78  ASN 78  104 ?   ?   ?   B . n 
B 1 79  GLY 79  105 ?   ?   ?   B . n 
B 1 80  ASN 80  106 ?   ?   ?   B . n 
B 1 81  PRO 81  107 ?   ?   ?   B . n 
B 1 82  GLY 82  108 ?   ?   ?   B . n 
B 1 83  ILE 83  109 ?   ?   ?   B . n 
B 1 84  GLN 84  110 ?   ?   ?   B . n 
B 1 85  SER 85  111 ?   ?   ?   B . n 
B 1 86  ASN 86  112 ?   ?   ?   B . n 
B 1 87  GLY 87  113 113 GLY GLY B . n 
B 1 88  LEU 88  114 114 LEU LEU B . n 
B 1 89  ASN 89  115 115 ASN ASN B . n 
B 1 90  ILE 90  116 116 ILE ILE B . n 
B 1 91  THR 91  117 117 THR THR B . n 
B 1 92  ASP 92  118 118 ASP ASP B . n 
B 1 93  GLY 93  119 119 GLY GLY B . n 
B 1 94  ALA 94  120 120 ALA ALA B . n 
B 1 95  PHE 95  121 121 PHE PHE B . n 
B 1 96  LEU 96  122 122 LEU LEU B . n 
B 1 97  ASN 97  123 123 ASN ASN B . n 
B 1 98  LEU 98  124 124 LEU LEU B . n 
B 1 99  LYS 99  125 125 LYS LYS B . n 
B 1 100 ASN 100 126 126 ASN ASN B . n 
B 1 101 LEU 101 127 127 LEU LEU B . n 
B 1 102 ARG 102 128 128 ARG ARG B . n 
B 1 103 GLU 103 129 129 GLU GLU B . n 
B 1 104 LEU 104 130 130 LEU LEU B . n 
B 1 105 LEU 105 131 131 LEU LEU B . n 
B 1 106 LEU 106 132 132 LEU LEU B . n 
B 1 107 GLU 107 133 133 GLU GLU B . n 
B 1 108 ASP 108 134 134 ASP ASP B . n 
B 1 109 ASN 109 135 135 ASN ASN B . n 
B 1 110 GLN 110 136 136 GLN GLN B . n 
B 1 111 LEU 111 137 137 LEU LEU B . n 
B 1 112 PRO 112 138 138 PRO PRO B . n 
B 1 113 GLN 113 139 139 GLN GLN B . n 
B 1 114 ILE 114 140 140 ILE ILE B . n 
B 1 115 PRO 115 141 141 PRO PRO B . n 
B 1 116 SER 116 142 142 SER SER B . n 
B 1 117 GLY 117 143 143 GLY GLY B . n 
B 1 118 LEU 118 144 144 LEU LEU B . n 
B 1 119 PRO 119 145 145 PRO PRO B . n 
B 1 120 GLU 120 146 146 GLU GLU B . n 
B 1 121 SER 121 147 147 SER SER B . n 
B 1 122 LEU 122 148 148 LEU LEU B . n 
B 1 123 THR 123 149 149 THR THR B . n 
B 1 124 GLU 124 150 150 GLU GLU B . n 
B 1 125 LEU 125 151 151 LEU LEU B . n 
B 1 126 SER 126 152 152 SER SER B . n 
B 1 127 LEU 127 153 153 LEU LEU B . n 
B 1 128 ILE 128 154 154 ILE ILE B . n 
B 1 129 GLN 129 155 155 GLN GLN B . n 
B 1 130 ASN 130 156 156 ASN ASN B . n 
B 1 131 ASN 131 157 157 ASN ASN B . n 
B 1 132 ILE 132 158 158 ILE ILE B . n 
B 1 133 TYR 133 159 159 TYR TYR B . n 
B 1 134 ASN 134 160 160 ASN ASN B . n 
B 1 135 ILE 135 161 161 ILE ILE B . n 
B 1 136 THR 136 162 162 THR THR B . n 
B 1 137 LYS 137 163 163 LYS LYS B . n 
B 1 138 GLU 138 164 164 GLU GLU B . n 
B 1 139 GLY 139 165 165 GLY GLY B . n 
B 1 140 ILE 140 166 166 ILE ILE B . n 
B 1 141 SER 141 167 167 SER SER B . n 
B 1 142 ARG 142 168 168 ARG ARG B . n 
B 1 143 LEU 143 169 169 LEU LEU B . n 
B 1 144 ILE 144 170 170 ILE ILE B . n 
B 1 145 ASN 145 171 171 ASN ASN B . n 
B 1 146 LEU 146 172 172 LEU LEU B . n 
B 1 147 LYS 147 173 173 LYS LYS B . n 
B 1 148 ASN 148 174 174 ASN ASN B . n 
B 1 149 LEU 149 175 175 LEU LEU B . n 
B 1 150 TYR 150 176 176 TYR TYR B . n 
B 1 151 LEU 151 177 177 LEU LEU B . n 
B 1 152 ALA 152 178 178 ALA ALA B . n 
B 1 153 TRP 153 179 179 TRP TRP B . n 
B 1 154 ASN 154 180 180 ASN ASN B . n 
B 1 155 CYS 155 181 181 CYS CYS B . n 
B 1 156 TYR 156 182 182 TYR TYR B . n 
B 1 157 PHE 157 183 183 PHE PHE B . n 
B 1 158 ASN 158 184 184 ASN ASN B . n 
B 1 159 LYS 159 185 185 LYS LYS B . n 
B 1 160 VAL 160 186 186 VAL VAL B . n 
B 1 161 CYS 161 187 187 CYS CYS B . n 
B 1 162 GLU 162 188 188 GLU GLU B . n 
B 1 163 LYS 163 189 189 LYS LYS B . n 
B 1 164 THR 164 190 190 THR THR B . n 
B 1 165 ASN 165 191 191 ASN ASN B . n 
B 1 166 ILE 166 192 192 ILE ILE B . n 
B 1 167 GLU 167 193 193 GLU GLU B . n 
B 1 168 ASP 168 194 194 ASP ASP B . n 
B 1 169 GLY 169 195 195 GLY GLY B . n 
B 1 170 VAL 170 196 196 VAL VAL B . n 
B 1 171 PHE 171 197 197 PHE PHE B . n 
B 1 172 GLU 172 198 198 GLU GLU B . n 
B 1 173 THR 173 199 199 THR THR B . n 
B 1 174 LEU 174 200 200 LEU LEU B . n 
B 1 175 THR 175 201 201 THR THR B . n 
B 1 176 ASN 176 202 202 ASN ASN B . n 
B 1 177 LEU 177 203 203 LEU LEU B . n 
B 1 178 GLU 178 204 204 GLU GLU B . n 
B 1 179 LEU 179 205 205 LEU LEU B . n 
B 1 180 LEU 180 206 206 LEU LEU B . n 
B 1 181 SER 181 207 207 SER SER B . n 
B 1 182 LEU 182 208 208 LEU LEU B . n 
B 1 183 SER 183 209 209 SER SER B . n 
B 1 184 PHE 184 210 210 PHE PHE B . n 
B 1 185 ASN 185 211 211 ASN ASN B . n 
B 1 186 SER 186 212 212 SER SER B . n 
B 1 187 LEU 187 213 213 LEU LEU B . n 
B 1 188 SER 188 214 214 SER SER B . n 
B 1 189 HIS 189 215 215 HIS HIS B . n 
B 1 190 VAL 190 216 216 VAL VAL B . n 
B 1 191 PRO 191 217 217 PRO PRO B . n 
B 1 192 PRO 192 218 218 PRO PRO B . n 
B 1 193 LYS 193 219 219 LYS LYS B . n 
B 1 194 LEU 194 220 220 LEU LEU B . n 
B 1 195 PRO 195 221 221 PRO PRO B . n 
B 1 196 SER 196 222 222 SER SER B . n 
B 1 197 SER 197 223 223 SER SER B . n 
B 1 198 LEU 198 224 224 LEU LEU B . n 
B 1 199 ARG 199 225 225 ARG ARG B . n 
B 1 200 LYS 200 226 226 LYS LYS B . n 
B 1 201 LEU 201 227 227 LEU LEU B . n 
B 1 202 PHE 202 228 228 PHE PHE B . n 
B 1 203 LEU 203 229 229 LEU LEU B . n 
B 1 204 SER 204 230 230 SER SER B . n 
B 1 205 ASN 205 231 231 ASN ASN B . n 
B 1 206 THR 206 232 232 THR THR B . n 
B 1 207 GLN 207 233 233 GLN GLN B . n 
B 1 208 ILE 208 234 234 ILE ILE B . n 
B 1 209 LYS 209 235 235 LYS LYS B . n 
B 1 210 TYR 210 236 236 TYR TYR B . n 
B 1 211 ILE 211 237 237 ILE ILE B . n 
B 1 212 SER 212 238 238 SER SER B . n 
B 1 213 GLU 213 239 239 GLU GLU B . n 
B 1 214 GLU 214 240 240 GLU GLU B . n 
B 1 215 ASP 215 241 241 ASP ASP B . n 
B 1 216 PHE 216 242 242 PHE PHE B . n 
B 1 217 LYS 217 243 243 LYS LYS B . n 
B 1 218 GLY 218 244 244 GLY GLY B . n 
B 1 219 LEU 219 245 245 LEU LEU B . n 
B 1 220 ILE 220 246 246 ILE ILE B . n 
B 1 221 ASN 221 247 247 ASN ASN B . n 
B 1 222 LEU 222 248 248 LEU LEU B . n 
B 1 223 THR 223 249 249 THR THR B . n 
B 1 224 LEU 224 250 250 LEU LEU B . n 
B 1 225 LEU 225 251 251 LEU LEU B . n 
B 1 226 ASP 226 252 252 ASP ASP B . n 
B 1 227 LEU 227 253 253 LEU LEU B . n 
B 1 228 SER 228 254 254 SER SER B . n 
B 1 229 GLY 229 255 255 GLY GLY B . n 
B 1 230 ASN 230 256 256 ASN ASN B . n 
B 1 231 CYS 231 257 257 CYS CYS B . n 
B 1 232 PRO 232 258 258 PRO PRO B . n 
B 1 233 ARG 233 259 259 ARG ARG B . n 
B 1 234 CYS 234 260 260 CYS CYS B . n 
B 1 235 PHE 235 261 261 PHE PHE B . n 
B 1 236 ASN 236 262 262 ASN ASN B . n 
B 1 237 ALA 237 263 263 ALA ALA B . n 
B 1 238 PRO 238 264 264 PRO PRO B . n 
B 1 239 PHE 239 265 265 PHE PHE B . n 
B 1 240 PRO 240 266 266 PRO PRO B . n 
B 1 241 CYS 241 267 267 CYS CYS B . n 
B 1 242 VAL 242 268 268 VAL VAL B . n 
B 1 243 PRO 243 269 269 PRO PRO B . n 
B 1 244 CYS 244 270 270 CYS CYS B . n 
B 1 245 ASP 245 271 271 ASP ASP B . n 
B 1 246 GLY 246 272 272 GLY GLY B . n 
B 1 247 GLY 247 273 273 GLY GLY B . n 
B 1 248 ALA 248 274 274 ALA ALA B . n 
B 1 249 SER 249 275 275 SER SER B . n 
B 1 250 ILE 250 276 276 ILE ILE B . n 
B 1 251 ASN 251 277 277 ASN ASN B . n 
B 1 252 ILE 252 278 278 ILE ILE B . n 
B 1 253 ASP 253 279 279 ASP ASP B . n 
B 1 254 ARG 254 280 280 ARG ARG B . n 
B 1 255 PHE 255 281 281 PHE PHE B . n 
B 1 256 ALA 256 282 282 ALA ALA B . n 
B 1 257 PHE 257 283 283 PHE PHE B . n 
B 1 258 GLN 258 284 284 GLN GLN B . n 
B 1 259 ASN 259 285 285 ASN ASN B . n 
B 1 260 LEU 260 286 286 LEU LEU B . n 
B 1 261 THR 261 287 287 THR THR B . n 
B 1 262 GLN 262 288 288 GLN GLN B . n 
B 1 263 LEU 263 289 289 LEU LEU B . n 
B 1 264 ARG 264 290 290 ARG ARG B . n 
B 1 265 TYR 265 291 291 TYR TYR B . n 
B 1 266 LEU 266 292 292 LEU LEU B . n 
B 1 267 ASN 267 293 293 ASN ASN B . n 
B 1 268 LEU 268 294 294 LEU LEU B . n 
B 1 269 SER 269 295 295 SER SER B . n 
B 1 270 SER 270 296 296 SER SER B . n 
B 1 271 THR 271 297 297 THR THR B . n 
B 1 272 SER 272 298 298 SER SER B . n 
B 1 273 LEU 273 299 299 LEU LEU B . n 
B 1 274 ARG 274 300 300 ARG ARG B . n 
B 1 275 LYS 275 301 301 LYS LYS B . n 
B 1 276 ILE 276 302 302 ILE ILE B . n 
B 1 277 ASN 277 303 303 ASN ASN B . n 
B 1 278 ALA 278 304 304 ALA ALA B . n 
B 1 279 ALA 279 305 305 ALA ALA B . n 
B 1 280 TRP 280 306 306 TRP TRP B . n 
B 1 281 PHE 281 307 307 PHE PHE B . n 
B 1 282 LYS 282 308 308 LYS LYS B . n 
B 1 283 ASN 283 309 309 ASN ASN B . n 
B 1 284 MET 284 310 310 MET MET B . n 
B 1 285 PRO 285 311 311 PRO PRO B . n 
B 1 286 HIS 286 312 312 HIS HIS B . n 
B 1 287 LEU 287 313 313 LEU LEU B . n 
B 1 288 LYS 288 314 314 LYS LYS B . n 
B 1 289 VAL 289 315 315 VAL VAL B . n 
B 1 290 LEU 290 316 316 LEU LEU B . n 
B 1 291 ASP 291 317 317 ASP ASP B . n 
B 1 292 LEU 292 318 318 LEU LEU B . n 
B 1 293 GLU 293 319 319 GLU GLU B . n 
B 1 294 PHE 294 320 320 PHE PHE B . n 
B 1 295 ASN 295 321 321 ASN ASN B . n 
B 1 296 TYR 296 322 322 TYR TYR B . n 
B 1 297 LEU 297 323 323 LEU LEU B . n 
B 1 298 VAL 298 324 324 VAL VAL B . n 
B 1 299 GLY 299 325 325 GLY GLY B . n 
B 1 300 GLU 300 326 326 GLU GLU B . n 
B 1 301 ILE 301 327 327 ILE ILE B . n 
B 1 302 ALA 302 328 328 ALA ALA B . n 
B 1 303 SER 303 329 329 SER SER B . n 
B 1 304 GLY 304 330 330 GLY GLY B . n 
B 1 305 ALA 305 331 331 ALA ALA B . n 
B 1 306 PHE 306 332 332 PHE PHE B . n 
B 1 307 LEU 307 333 333 LEU LEU B . n 
B 1 308 THR 308 334 334 THR THR B . n 
B 1 309 MET 309 335 335 MET MET B . n 
B 1 310 LEU 310 336 336 LEU LEU B . n 
B 1 311 PRO 311 337 337 PRO PRO B . n 
B 1 312 ARG 312 338 338 ARG ARG B . n 
B 1 313 LEU 313 339 339 LEU LEU B . n 
B 1 314 GLU 314 340 340 GLU GLU B . n 
B 1 315 ILE 315 341 341 ILE ILE B . n 
B 1 316 LEU 316 342 342 LEU LEU B . n 
B 1 317 ASP 317 343 343 ASP ASP B . n 
B 1 318 LEU 318 344 344 LEU LEU B . n 
B 1 319 SER 319 345 345 SER SER B . n 
B 1 320 PHE 320 346 346 PHE PHE B . n 
B 1 321 ASN 321 347 347 ASN ASN B . n 
B 1 322 TYR 322 348 348 TYR TYR B . n 
B 1 323 ILE 323 349 349 ILE ILE B . n 
B 1 324 LYS 324 350 350 LYS LYS B . n 
B 1 325 GLY 325 351 351 GLY GLY B . n 
B 1 326 SER 326 352 352 SER SER B . n 
B 1 327 TYR 327 353 353 TYR TYR B . n 
B 1 328 PRO 328 354 354 PRO PRO B . n 
B 1 329 GLN 329 355 355 GLN GLN B . n 
B 1 330 HIS 330 356 356 HIS HIS B . n 
B 1 331 ILE 331 357 357 ILE ILE B . n 
B 1 332 ASN 332 358 358 ASN ASN B . n 
B 1 333 ILE 333 359 359 ILE ILE B . n 
B 1 334 SER 334 360 360 SER SER B . n 
B 1 335 ARG 335 361 361 ARG ARG B . n 
B 1 336 ASN 336 362 362 ASN ASN B . n 
B 1 337 PHE 337 363 363 PHE PHE B . n 
B 1 338 SER 338 364 364 SER SER B . n 
B 1 339 LYS 339 365 365 LYS LYS B . n 
B 1 340 LEU 340 366 366 LEU LEU B . n 
B 1 341 LEU 341 367 367 LEU LEU B . n 
B 1 342 SER 342 368 368 SER SER B . n 
B 1 343 LEU 343 369 369 LEU LEU B . n 
B 1 344 ARG 344 370 370 ARG ARG B . n 
B 1 345 ALA 345 371 371 ALA ALA B . n 
B 1 346 LEU 346 372 372 LEU LEU B . n 
B 1 347 HIS 347 373 373 HIS HIS B . n 
B 1 348 LEU 348 374 374 LEU LEU B . n 
B 1 349 ARG 349 375 375 ARG ARG B . n 
B 1 350 GLY 350 376 376 GLY GLY B . n 
B 1 351 TYR 351 377 377 TYR TYR B . n 
B 1 352 VAL 352 378 378 VAL VAL B . n 
B 1 353 PHE 353 379 379 PHE PHE B . n 
B 1 354 GLN 354 380 380 GLN GLN B . n 
B 1 355 GLU 355 381 381 GLU GLU B . n 
B 1 356 LEU 356 382 382 LEU LEU B . n 
B 1 357 ARG 357 383 383 ARG ARG B . n 
B 1 358 GLU 358 384 384 GLU GLU B . n 
B 1 359 ASP 359 385 385 ASP ASP B . n 
B 1 360 ASP 360 386 386 ASP ASP B . n 
B 1 361 PHE 361 387 387 PHE PHE B . n 
B 1 362 GLN 362 388 388 GLN GLN B . n 
B 1 363 PRO 363 389 389 PRO PRO B . n 
B 1 364 LEU 364 390 390 LEU LEU B . n 
B 1 365 MET 365 391 391 MET MET B . n 
B 1 366 GLN 366 392 392 GLN GLN B . n 
B 1 367 LEU 367 393 393 LEU LEU B . n 
B 1 368 PRO 368 394 394 PRO PRO B . n 
B 1 369 ASN 369 395 395 ASN ASN B . n 
B 1 370 LEU 370 396 396 LEU LEU B . n 
B 1 371 SER 371 397 397 SER SER B . n 
B 1 372 THR 372 398 398 THR THR B . n 
B 1 373 ILE 373 399 399 ILE ILE B . n 
B 1 374 ASN 374 400 400 ASN ASN B . n 
B 1 375 LEU 375 401 401 LEU LEU B . n 
B 1 376 GLY 376 402 402 GLY GLY B . n 
B 1 377 ILE 377 403 403 ILE ILE B . n 
B 1 378 ASN 378 404 404 ASN ASN B . n 
B 1 379 PHE 379 405 405 PHE PHE B . n 
B 1 380 ILE 380 406 406 ILE ILE B . n 
B 1 381 LYS 381 407 407 LYS LYS B . n 
B 1 382 GLN 382 408 408 GLN GLN B . n 
B 1 383 ILE 383 409 409 ILE ILE B . n 
B 1 384 ASP 384 410 410 ASP ASP B . n 
B 1 385 PHE 385 411 411 PHE PHE B . n 
B 1 386 LYS 386 412 412 LYS LYS B . n 
B 1 387 LEU 387 413 413 LEU LEU B . n 
B 1 388 PHE 388 414 414 PHE PHE B . n 
B 1 389 GLN 389 415 415 GLN GLN B . n 
B 1 390 ASN 390 416 416 ASN ASN B . n 
B 1 391 PHE 391 417 417 PHE PHE B . n 
B 1 392 SER 392 418 418 SER SER B . n 
B 1 393 ASN 393 419 419 ASN ASN B . n 
B 1 394 LEU 394 420 420 LEU LEU B . n 
B 1 395 GLU 395 421 421 GLU GLU B . n 
B 1 396 ILE 396 422 422 ILE ILE B . n 
B 1 397 ILE 397 423 423 ILE ILE B . n 
B 1 398 TYR 398 424 424 TYR TYR B . n 
B 1 399 LEU 399 425 425 LEU LEU B . n 
B 1 400 SER 400 426 426 SER SER B . n 
B 1 401 GLU 401 427 427 GLU GLU B . n 
B 1 402 ASN 402 428 428 ASN ASN B . n 
B 1 403 ARG 403 429 429 ARG ARG B . n 
B 1 404 ILE 404 430 430 ILE ILE B . n 
B 1 405 SER 405 431 431 SER SER B . n 
B 1 406 PRO 406 432 432 PRO PRO B . n 
B 1 407 LEU 407 433 433 LEU LEU B . n 
B 1 408 VAL 408 434 ?   ?   ?   B . n 
B 1 409 LYS 409 435 ?   ?   ?   B . n 
B 1 410 ASP 410 436 ?   ?   ?   B . n 
B 1 411 THR 411 437 ?   ?   ?   B . n 
B 1 412 ARG 412 438 ?   ?   ?   B . n 
B 1 413 GLN 413 439 ?   ?   ?   B . n 
B 1 414 SER 414 440 ?   ?   ?   B . n 
B 1 415 TYR 415 441 ?   ?   ?   B . n 
B 1 416 ALA 416 442 ?   ?   ?   B . n 
B 1 417 ASN 417 443 ?   ?   ?   B . n 
B 1 418 SER 418 444 ?   ?   ?   B . n 
B 1 419 SER 419 445 ?   ?   ?   B . n 
B 1 420 SER 420 446 ?   ?   ?   B . n 
B 1 421 PHE 421 447 ?   ?   ?   B . n 
B 1 422 GLN 422 448 ?   ?   ?   B . n 
B 1 423 ARG 423 449 ?   ?   ?   B . n 
B 1 424 HIS 424 450 ?   ?   ?   B . n 
B 1 425 ILE 425 451 ?   ?   ?   B . n 
B 1 426 ARG 426 452 ?   ?   ?   B . n 
B 1 427 LYS 427 453 ?   ?   ?   B . n 
B 1 428 ARG 428 454 ?   ?   ?   B . n 
B 1 429 ARG 429 455 ?   ?   ?   B . n 
B 1 430 SER 430 456 ?   ?   ?   B . n 
B 1 431 THR 431 457 ?   ?   ?   B . n 
B 1 432 ASP 432 458 ?   ?   ?   B . n 
B 1 433 PHE 433 459 459 PHE PHE B . n 
B 1 434 GLU 434 460 460 GLU GLU B . n 
B 1 435 PHE 435 461 461 PHE PHE B . n 
B 1 436 ASP 436 462 462 ASP ASP B . n 
B 1 437 PRO 437 463 463 PRO PRO B . n 
B 1 438 HIS 438 464 464 HIS HIS B . n 
B 1 439 SER 439 465 465 SER SER B . n 
B 1 440 ASN 440 466 466 ASN ASN B . n 
B 1 441 PHE 441 467 467 PHE PHE B . n 
B 1 442 TYR 442 468 468 TYR TYR B . n 
B 1 443 HIS 443 469 469 HIS HIS B . n 
B 1 444 PHE 444 470 470 PHE PHE B . n 
B 1 445 THR 445 471 471 THR THR B . n 
B 1 446 ARG 446 472 472 ARG ARG B . n 
B 1 447 PRO 447 473 473 PRO PRO B . n 
B 1 448 LEU 448 474 474 LEU LEU B . n 
B 1 449 ILE 449 475 475 ILE ILE B . n 
B 1 450 LYS 450 476 476 LYS LYS B . n 
B 1 451 PRO 451 477 477 PRO PRO B . n 
B 1 452 GLN 452 478 478 GLN GLN B . n 
B 1 453 CYS 453 479 479 CYS CYS B . n 
B 1 454 ALA 454 480 480 ALA ALA B . n 
B 1 455 ALA 455 481 481 ALA ALA B . n 
B 1 456 TYR 456 482 482 TYR TYR B . n 
B 1 457 GLY 457 483 483 GLY GLY B . n 
B 1 458 LYS 458 484 484 LYS LYS B . n 
B 1 459 ALA 459 485 485 ALA ALA B . n 
B 1 460 LEU 460 486 486 LEU LEU B . n 
B 1 461 ASP 461 487 487 ASP ASP B . n 
B 1 462 LEU 462 488 488 LEU LEU B . n 
B 1 463 SER 463 489 489 SER SER B . n 
B 1 464 LEU 464 490 490 LEU LEU B . n 
B 1 465 ASN 465 491 491 ASN ASN B . n 
B 1 466 SER 466 492 492 SER SER B . n 
B 1 467 ILE 467 493 493 ILE ILE B . n 
B 1 468 PHE 468 494 494 PHE PHE B . n 
B 1 469 PHE 469 495 495 PHE PHE B . n 
B 1 470 ILE 470 496 496 ILE ILE B . n 
B 1 471 GLY 471 497 497 GLY GLY B . n 
B 1 472 PRO 472 498 498 PRO PRO B . n 
B 1 473 ASN 473 499 499 ASN ASN B . n 
B 1 474 GLN 474 500 500 GLN GLN B . n 
B 1 475 PHE 475 501 501 PHE PHE B . n 
B 1 476 GLU 476 502 502 GLU GLU B . n 
B 1 477 ASN 477 503 503 ASN ASN B . n 
B 1 478 LEU 478 504 504 LEU LEU B . n 
B 1 479 PRO 479 505 505 PRO PRO B . n 
B 1 480 ASP 480 506 506 ASP ASP B . n 
B 1 481 ILE 481 507 507 ILE ILE B . n 
B 1 482 ALA 482 508 508 ALA ALA B . n 
B 1 483 CYS 483 509 509 CYS CYS B . n 
B 1 484 LEU 484 510 510 LEU LEU B . n 
B 1 485 ASN 485 511 511 ASN ASN B . n 
B 1 486 LEU 486 512 512 LEU LEU B . n 
B 1 487 SER 487 513 513 SER SER B . n 
B 1 488 ALA 488 514 514 ALA ALA B . n 
B 1 489 ASN 489 515 515 ASN ASN B . n 
B 1 490 SER 490 516 516 SER SER B . n 
B 1 491 ASN 491 517 517 ASN ASN B . n 
B 1 492 ALA 492 518 518 ALA ALA B . n 
B 1 493 GLN 493 519 519 GLN GLN B . n 
B 1 494 VAL 494 520 520 VAL VAL B . n 
B 1 495 LEU 495 521 521 LEU LEU B . n 
B 1 496 SER 496 522 522 SER SER B . n 
B 1 497 GLY 497 523 523 GLY GLY B . n 
B 1 498 THR 498 524 524 THR THR B . n 
B 1 499 GLU 499 525 525 GLU GLU B . n 
B 1 500 PHE 500 526 526 PHE PHE B . n 
B 1 501 SER 501 527 527 SER SER B . n 
B 1 502 ALA 502 528 528 ALA ALA B . n 
B 1 503 ILE 503 529 529 ILE ILE B . n 
B 1 504 PRO 504 530 530 PRO PRO B . n 
B 1 505 HIS 505 531 531 HIS HIS B . n 
B 1 506 VAL 506 532 532 VAL VAL B . n 
B 1 507 LYS 507 533 533 LYS LYS B . n 
B 1 508 TYR 508 534 534 TYR TYR B . n 
B 1 509 LEU 509 535 535 LEU LEU B . n 
B 1 510 ASP 510 536 536 ASP ASP B . n 
B 1 511 LEU 511 537 537 LEU LEU B . n 
B 1 512 THR 512 538 538 THR THR B . n 
B 1 513 ASN 513 539 539 ASN ASN B . n 
B 1 514 ASN 514 540 540 ASN ASN B . n 
B 1 515 ARG 515 541 541 ARG ARG B . n 
B 1 516 LEU 516 542 542 LEU LEU B . n 
B 1 517 ASP 517 543 543 ASP ASP B . n 
B 1 518 PHE 518 544 544 PHE PHE B . n 
B 1 519 ASP 519 545 545 ASP ASP B . n 
B 1 520 ASN 520 546 546 ASN ASN B . n 
B 1 521 ALA 521 547 547 ALA ALA B . n 
B 1 522 SER 522 548 548 SER SER B . n 
B 1 523 ALA 523 549 549 ALA ALA B . n 
B 1 524 LEU 524 550 550 LEU LEU B . n 
B 1 525 THR 525 551 551 THR THR B . n 
B 1 526 GLU 526 552 552 GLU GLU B . n 
B 1 527 LEU 527 553 553 LEU LEU B . n 
B 1 528 SER 528 554 554 SER SER B . n 
B 1 529 ASP 529 555 555 ASP ASP B . n 
B 1 530 LEU 530 556 556 LEU LEU B . n 
B 1 531 GLU 531 557 557 GLU GLU B . n 
B 1 532 VAL 532 558 558 VAL VAL B . n 
B 1 533 LEU 533 559 559 LEU LEU B . n 
B 1 534 ASP 534 560 560 ASP ASP B . n 
B 1 535 LEU 535 561 561 LEU LEU B . n 
B 1 536 SER 536 562 562 SER SER B . n 
B 1 537 TYR 537 563 563 TYR TYR B . n 
B 1 538 ASN 538 564 564 ASN ASN B . n 
B 1 539 SER 539 565 565 SER SER B . n 
B 1 540 HIS 540 566 566 HIS HIS B . n 
B 1 541 TYR 541 567 567 TYR TYR B . n 
B 1 542 PHE 542 568 568 PHE PHE B . n 
B 1 543 ARG 543 569 569 ARG ARG B . n 
B 1 544 ILE 544 570 570 ILE ILE B . n 
B 1 545 ALA 545 571 571 ALA ALA B . n 
B 1 546 GLY 546 572 572 GLY GLY B . n 
B 1 547 VAL 547 573 573 VAL VAL B . n 
B 1 548 THR 548 574 574 THR THR B . n 
B 1 549 HIS 549 575 575 HIS HIS B . n 
B 1 550 HIS 550 576 576 HIS HIS B . n 
B 1 551 LEU 551 577 577 LEU LEU B . n 
B 1 552 GLU 552 578 578 GLU GLU B . n 
B 1 553 PHE 553 579 579 PHE PHE B . n 
B 1 554 ILE 554 580 580 ILE ILE B . n 
B 1 555 GLN 555 581 581 GLN GLN B . n 
B 1 556 ASN 556 582 582 ASN ASN B . n 
B 1 557 PHE 557 583 583 PHE PHE B . n 
B 1 558 THR 558 584 584 THR THR B . n 
B 1 559 ASN 559 585 585 ASN ASN B . n 
B 1 560 LEU 560 586 586 LEU LEU B . n 
B 1 561 LYS 561 587 587 LYS LYS B . n 
B 1 562 VAL 562 588 588 VAL VAL B . n 
B 1 563 LEU 563 589 589 LEU LEU B . n 
B 1 564 ASN 564 590 590 ASN ASN B . n 
B 1 565 LEU 565 591 591 LEU LEU B . n 
B 1 566 SER 566 592 592 SER SER B . n 
B 1 567 HIS 567 593 593 HIS HIS B . n 
B 1 568 ASN 568 594 594 ASN ASN B . n 
B 1 569 ASN 569 595 595 ASN ASN B . n 
B 1 570 ILE 570 596 596 ILE ILE B . n 
B 1 571 TYR 571 597 597 TYR TYR B . n 
B 1 572 THR 572 598 598 THR THR B . n 
B 1 573 LEU 573 599 599 LEU LEU B . n 
B 1 574 THR 574 600 600 THR THR B . n 
B 1 575 ASP 575 601 601 ASP ASP B . n 
B 1 576 LYS 576 602 602 LYS LYS B . n 
B 1 577 TYR 577 603 603 TYR TYR B . n 
B 1 578 ASN 578 604 604 ASN ASN B . n 
B 1 579 LEU 579 605 605 LEU LEU B . n 
B 1 580 GLU 580 606 606 GLU GLU B . n 
B 1 581 SER 581 607 607 SER SER B . n 
B 1 582 LYS 582 608 608 LYS LYS B . n 
B 1 583 SER 583 609 609 SER SER B . n 
B 1 584 LEU 584 610 610 LEU LEU B . n 
B 1 585 VAL 585 611 611 VAL VAL B . n 
B 1 586 GLU 586 612 612 GLU GLU B . n 
B 1 587 LEU 587 613 613 LEU LEU B . n 
B 1 588 VAL 588 614 614 VAL VAL B . n 
B 1 589 PHE 589 615 615 PHE PHE B . n 
B 1 590 SER 590 616 616 SER SER B . n 
B 1 591 GLY 591 617 617 GLY GLY B . n 
B 1 592 ASN 592 618 618 ASN ASN B . n 
B 1 593 ARG 593 619 619 ARG ARG B . n 
B 1 594 LEU 594 620 620 LEU LEU B . n 
B 1 595 ASP 595 621 621 ASP ASP B . n 
B 1 596 ILE 596 622 622 ILE ILE B . n 
B 1 597 LEU 597 623 623 LEU LEU B . n 
B 1 598 TRP 598 624 624 TRP TRP B . n 
B 1 599 ASN 599 625 625 ASN ASN B . n 
B 1 600 ASP 600 626 626 ASP ASP B . n 
B 1 601 ASP 601 627 627 ASP ASP B . n 
B 1 602 ASP 602 628 628 ASP ASP B . n 
B 1 603 ASN 603 629 629 ASN ASN B . n 
B 1 604 ARG 604 630 630 ARG ARG B . n 
B 1 605 TYR 605 631 631 TYR TYR B . n 
B 1 606 ILE 606 632 632 ILE ILE B . n 
B 1 607 SER 607 633 633 SER SER B . n 
B 1 608 ILE 608 634 634 ILE ILE B . n 
B 1 609 PHE 609 635 635 PHE PHE B . n 
B 1 610 LYS 610 636 636 LYS LYS B . n 
B 1 611 GLY 611 637 637 GLY GLY B . n 
B 1 612 LEU 612 638 638 LEU LEU B . n 
B 1 613 LYS 613 639 639 LYS LYS B . n 
B 1 614 ASN 614 640 640 ASN ASN B . n 
B 1 615 LEU 615 641 641 LEU LEU B . n 
B 1 616 THR 616 642 642 THR THR B . n 
B 1 617 ARG 617 643 643 ARG ARG B . n 
B 1 618 LEU 618 644 644 LEU LEU B . n 
B 1 619 ASP 619 645 645 ASP ASP B . n 
B 1 620 LEU 620 646 646 LEU LEU B . n 
B 1 621 SER 621 647 647 SER SER B . n 
B 1 622 LEU 622 648 648 LEU LEU B . n 
B 1 623 ASN 623 649 649 ASN ASN B . n 
B 1 624 ARG 624 650 650 ARG ARG B . n 
B 1 625 LEU 625 651 651 LEU LEU B . n 
B 1 626 LYS 626 652 652 LYS LYS B . n 
B 1 627 HIS 627 653 653 HIS HIS B . n 
B 1 628 ILE 628 654 654 ILE ILE B . n 
B 1 629 PRO 629 655 655 PRO PRO B . n 
B 1 630 ASN 630 656 656 ASN ASN B . n 
B 1 631 GLU 631 657 657 GLU GLU B . n 
B 1 632 ALA 632 658 658 ALA ALA B . n 
B 1 633 PHE 633 659 659 PHE PHE B . n 
B 1 634 LEU 634 660 660 LEU LEU B . n 
B 1 635 ASN 635 661 661 ASN ASN B . n 
B 1 636 LEU 636 662 662 LEU LEU B . n 
B 1 637 PRO 637 663 663 PRO PRO B . n 
B 1 638 ALA 638 664 664 ALA ALA B . n 
B 1 639 SER 639 665 665 SER SER B . n 
B 1 640 LEU 640 666 666 LEU LEU B . n 
B 1 641 THR 641 667 667 THR THR B . n 
B 1 642 GLU 642 668 668 GLU GLU B . n 
B 1 643 LEU 643 669 669 LEU LEU B . n 
B 1 644 HIS 644 670 670 HIS HIS B . n 
B 1 645 ILE 645 671 671 ILE ILE B . n 
B 1 646 ASN 646 672 672 ASN ASN B . n 
B 1 647 ASP 647 673 673 ASP ASP B . n 
B 1 648 ASN 648 674 674 ASN ASN B . n 
B 1 649 MET 649 675 675 MET MET B . n 
B 1 650 LEU 650 676 676 LEU LEU B . n 
B 1 651 LYS 651 677 677 LYS LYS B . n 
B 1 652 PHE 652 678 678 PHE PHE B . n 
B 1 653 PHE 653 679 679 PHE PHE B . n 
B 1 654 ASN 654 680 680 ASN ASN B . n 
B 1 655 TRP 655 681 681 TRP TRP B . n 
B 1 656 THR 656 682 682 THR THR B . n 
B 1 657 LEU 657 683 683 LEU LEU B . n 
B 1 658 LEU 658 684 684 LEU LEU B . n 
B 1 659 GLN 659 685 685 GLN GLN B . n 
B 1 660 GLN 660 686 686 GLN GLN B . n 
B 1 661 PHE 661 687 687 PHE PHE B . n 
B 1 662 PRO 662 688 688 PRO PRO B . n 
B 1 663 ARG 663 689 689 ARG ARG B . n 
B 1 664 LEU 664 690 690 LEU LEU B . n 
B 1 665 GLU 665 691 691 GLU GLU B . n 
B 1 666 LEU 666 692 692 LEU LEU B . n 
B 1 667 LEU 667 693 693 LEU LEU B . n 
B 1 668 ASP 668 694 694 ASP ASP B . n 
B 1 669 LEU 669 695 695 LEU LEU B . n 
B 1 670 ARG 670 696 696 ARG ARG B . n 
B 1 671 GLY 671 697 697 GLY GLY B . n 
B 1 672 ASN 672 698 698 ASN ASN B . n 
B 1 673 LYS 673 699 699 LYS LYS B . n 
B 1 674 LEU 674 700 700 LEU LEU B . n 
B 1 675 LEU 675 701 701 LEU LEU B . n 
B 1 676 PHE 676 702 702 PHE PHE B . n 
B 1 677 LEU 677 703 703 LEU LEU B . n 
B 1 678 THR 678 704 704 THR THR B . n 
B 1 679 ASP 679 705 705 ASP ASP B . n 
B 1 680 SER 680 706 706 SER SER B . n 
B 1 681 LEU 681 707 707 LEU LEU B . n 
B 1 682 SER 682 708 708 SER SER B . n 
B 1 683 ASP 683 709 709 ASP ASP B . n 
B 1 684 PHE 684 710 710 PHE PHE B . n 
B 1 685 THR 685 711 711 THR THR B . n 
B 1 686 SER 686 712 712 SER SER B . n 
B 1 687 SER 687 713 713 SER SER B . n 
B 1 688 LEU 688 714 714 LEU LEU B . n 
B 1 689 ARG 689 715 715 ARG ARG B . n 
B 1 690 THR 690 716 716 THR THR B . n 
B 1 691 LEU 691 717 717 LEU LEU B . n 
B 1 692 LEU 692 718 718 LEU LEU B . n 
B 1 693 LEU 693 719 719 LEU LEU B . n 
B 1 694 SER 694 720 720 SER SER B . n 
B 1 695 HIS 695 721 721 HIS HIS B . n 
B 1 696 ASN 696 722 722 ASN ASN B . n 
B 1 697 ARG 697 723 723 ARG ARG B . n 
B 1 698 ILE 698 724 724 ILE ILE B . n 
B 1 699 SER 699 725 725 SER SER B . n 
B 1 700 HIS 700 726 726 HIS HIS B . n 
B 1 701 LEU 701 727 727 LEU LEU B . n 
B 1 702 PRO 702 728 728 PRO PRO B . n 
B 1 703 SER 703 729 729 SER SER B . n 
B 1 704 GLY 704 730 730 GLY GLY B . n 
B 1 705 PHE 705 731 731 PHE PHE B . n 
B 1 706 LEU 706 732 732 LEU LEU B . n 
B 1 707 SER 707 733 733 SER SER B . n 
B 1 708 GLU 708 734 734 GLU GLU B . n 
B 1 709 VAL 709 735 735 VAL VAL B . n 
B 1 710 SER 710 736 736 SER SER B . n 
B 1 711 SER 711 737 737 SER SER B . n 
B 1 712 LEU 712 738 738 LEU LEU B . n 
B 1 713 LYS 713 739 739 LYS LYS B . n 
B 1 714 HIS 714 740 740 HIS HIS B . n 
B 1 715 LEU 715 741 741 LEU LEU B . n 
B 1 716 ASP 716 742 742 ASP ASP B . n 
B 1 717 LEU 717 743 743 LEU LEU B . n 
B 1 718 SER 718 744 744 SER SER B . n 
B 1 719 SER 719 745 745 SER SER B . n 
B 1 720 ASN 720 746 746 ASN ASN B . n 
B 1 721 LEU 721 747 747 LEU LEU B . n 
B 1 722 LEU 722 748 748 LEU LEU B . n 
B 1 723 LYS 723 749 749 LYS LYS B . n 
B 1 724 THR 724 750 750 THR THR B . n 
B 1 725 ILE 725 751 751 ILE ILE B . n 
B 1 726 ASN 726 752 752 ASN ASN B . n 
B 1 727 LYS 727 753 753 LYS LYS B . n 
B 1 728 SER 728 754 754 SER SER B . n 
B 1 729 ALA 729 755 755 ALA ALA B . n 
B 1 730 LEU 730 756 756 LEU LEU B . n 
B 1 731 GLU 731 757 757 GLU GLU B . n 
B 1 732 THR 732 758 758 THR THR B . n 
B 1 733 LYS 733 759 759 LYS LYS B . n 
B 1 734 THR 734 760 760 THR THR B . n 
B 1 735 THR 735 761 761 THR THR B . n 
B 1 736 THR 736 762 762 THR THR B . n 
B 1 737 LYS 737 763 763 LYS LYS B . n 
B 1 738 LEU 738 764 764 LEU LEU B . n 
B 1 739 SER 739 765 765 SER SER B . n 
B 1 740 MET 740 766 766 MET MET B . n 
B 1 741 LEU 741 767 767 LEU LEU B . n 
B 1 742 GLU 742 768 768 GLU GLU B . n 
B 1 743 LEU 743 769 769 LEU LEU B . n 
B 1 744 HIS 744 770 770 HIS HIS B . n 
B 1 745 GLY 745 771 771 GLY GLY B . n 
B 1 746 ASN 746 772 772 ASN ASN B . n 
B 1 747 PRO 747 773 773 PRO PRO B . n 
B 1 748 PHE 748 774 774 PHE PHE B . n 
B 1 749 GLU 749 775 775 GLU GLU B . n 
B 1 750 CYS 750 776 776 CYS CYS B . n 
B 1 751 THR 751 777 777 THR THR B . n 
B 1 752 CYS 752 778 778 CYS CYS B . n 
B 1 753 ASP 753 779 779 ASP ASP B . n 
B 1 754 ILE 754 780 780 ILE ILE B . n 
B 1 755 GLY 755 781 781 GLY GLY B . n 
B 1 756 ASP 756 782 782 ASP ASP B . n 
B 1 757 PHE 757 783 783 PHE PHE B . n 
B 1 758 ARG 758 784 784 ARG ARG B . n 
B 1 759 ARG 759 785 785 ARG ARG B . n 
B 1 760 TRP 760 786 786 TRP TRP B . n 
B 1 761 MET 761 787 787 MET MET B . n 
B 1 762 ASP 762 788 788 ASP ASP B . n 
B 1 763 GLU 763 789 789 GLU GLU B . n 
B 1 764 HIS 764 790 790 HIS HIS B . n 
B 1 765 LEU 765 791 791 LEU LEU B . n 
B 1 766 ASN 766 792 792 ASN ASN B . n 
B 1 767 VAL 767 793 793 VAL VAL B . n 
B 1 768 LYS 768 794 794 LYS LYS B . n 
B 1 769 ILE 769 795 795 ILE ILE B . n 
B 1 770 PRO 770 796 796 PRO PRO B . n 
B 1 771 ARG 771 797 797 ARG ARG B . n 
B 1 772 LEU 772 798 798 LEU LEU B . n 
B 1 773 VAL 773 799 799 VAL VAL B . n 
B 1 774 ASP 774 800 800 ASP ASP B . n 
B 1 775 VAL 775 801 801 VAL VAL B . n 
B 1 776 ILE 776 802 802 ILE ILE B . n 
B 1 777 CYS 777 803 803 CYS CYS B . n 
B 1 778 ALA 778 804 804 ALA ALA B . n 
B 1 779 SER 779 805 805 SER SER B . n 
B 1 780 PRO 780 806 806 PRO PRO B . n 
B 1 781 GLY 781 807 807 GLY GLY B . n 
B 1 782 ASP 782 808 808 ASP ASP B . n 
B 1 783 GLN 783 809 809 GLN GLN B . n 
B 1 784 ARG 784 810 810 ARG ARG B . n 
B 1 785 GLY 785 811 811 GLY GLY B . n 
B 1 786 LYS 786 812 812 LYS LYS B . n 
B 1 787 SER 787 813 813 SER SER B . n 
B 1 788 ILE 788 814 814 ILE ILE B . n 
B 1 789 VAL 789 815 815 VAL VAL B . n 
B 1 790 SER 790 816 816 SER SER B . n 
B 1 791 LEU 791 817 817 LEU LEU B . n 
B 1 792 GLU 792 818 818 GLU GLU B . n 
B 1 793 LEU 793 819 ?   ?   ?   B . n 
B 1 794 THR 794 820 ?   ?   ?   B . n 
B 1 795 THR 795 821 ?   ?   ?   B . n 
B 1 796 CYS 796 822 ?   ?   ?   B . n 
B 1 797 VAL 797 823 ?   ?   ?   B . n 
B 1 798 SER 798 824 ?   ?   ?   B . n 
B 1 799 ASP 799 825 ?   ?   ?   B . n 
B 1 800 VAL 800 826 ?   ?   ?   B . n 
B 1 801 THR 801 827 ?   ?   ?   B . n 
B 1 802 GLU 802 828 ?   ?   ?   B . n 
B 1 803 PHE 803 829 ?   ?   ?   B . n 
B 1 804 LEU 804 830 ?   ?   ?   B . n 
B 1 805 VAL 805 831 ?   ?   ?   B . n 
B 1 806 PRO 806 832 ?   ?   ?   B . n 
B 1 807 ARG 807 833 ?   ?   ?   B . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 2 NAG 1 C NAG 1 C NAG 1 n 
C 2 NAG 2 C NAG 2 C NAG 2 n 
C 2 BMA 3 C BMA 3 C BMA 3 n 
C 2 MAN 4 C MAN 4 C MAN 4 n 
C 2 MAN 5 C MAN 5 C MAN 5 n 
D 3 NAG 1 D NAG 1 D NAG 1 n 
D 3 NAG 2 D NAG 2 D NAG 2 n 
D 3 BMA 3 D BMA 3 D BMA 3 n 
E 3 NAG 1 E NAG 1 E NAG 1 n 
E 3 NAG 2 E NAG 2 E NAG 2 n 
E 3 BMA 3 E BMA 3 E BMA 3 n 
F 2 NAG 1 F NAG 1 F NAG 1 n 
F 2 NAG 2 F NAG 2 F NAG 2 n 
F 2 BMA 3 F BMA 3 F BMA 3 n 
F 2 MAN 4 F MAN 4 F MAN 4 n 
F 2 MAN 5 F MAN 5 F MAN 5 n 
G 3 NAG 1 G NAG 1 G NAG 1 n 
G 3 NAG 2 G NAG 2 G NAG 2 n 
G 3 BMA 3 G BMA 3 G BMA 3 n 
H 3 NAG 1 H NAG 1 H NAG 1 n 
H 3 NAG 2 H NAG 2 H NAG 2 n 
H 3 BMA 3 H BMA 3 H BMA 3 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BLN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BLN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
I  4 NAG   1   901  901  NAG   NAG A . 
J  4 NAG   1   902  902  NAG   NAG A . 
K  4 NAG   1   903  903  NAG   NAG A . 
L  4 NAG   1   904  904  NAG   NAG A . 
M  4 NAG   1   905  905  NAG   NAG A . 
N  4 NAG   1   906  906  NAG   NAG A . 
O  4 NAG   1   907  907  NAG   NAG A . 
P  4 NAG   1   908  908  NAG   NAG A . 
Q  4 NAG   1   909  909  NAG   NAG A . 
R  5 SO4   1   910  910  SO4   SO4 A . 
S  5 SO4   1   911  911  SO4   SO4 A . 
T  6 A1BLN 1   912  912  A1BLN LIG A . 
U  4 NAG   1   901  901  NAG   NAG B . 
V  4 NAG   1   902  902  NAG   NAG B . 
W  4 NAG   1   903  903  NAG   NAG B . 
X  4 NAG   1   904  904  NAG   NAG B . 
Y  4 NAG   1   905  905  NAG   NAG B . 
Z  4 NAG   1   906  906  NAG   NAG B . 
AA 4 NAG   1   907  907  NAG   NAG B . 
BA 4 NAG   1   908  908  NAG   NAG B . 
CA 4 NAG   1   909  909  NAG   NAG B . 
DA 5 SO4   1   910  910  SO4   SO4 B . 
EA 6 A1BLN 1   911  911  A1BLN LIG B . 
FA 7 HOH   1   1001 1001 HOH   HOH A . 
FA 7 HOH   2   1002 1002 HOH   HOH A . 
FA 7 HOH   3   1003 1003 HOH   HOH A . 
FA 7 HOH   4   1004 1004 HOH   HOH A . 
FA 7 HOH   5   1005 1005 HOH   HOH A . 
FA 7 HOH   6   1006 1006 HOH   HOH A . 
FA 7 HOH   7   1007 1007 HOH   HOH A . 
FA 7 HOH   8   1008 1008 HOH   HOH A . 
FA 7 HOH   9   1009 1009 HOH   HOH A . 
FA 7 HOH   10  1010 1010 HOH   HOH A . 
FA 7 HOH   11  1011 1011 HOH   HOH A . 
FA 7 HOH   12  1012 1012 HOH   HOH A . 
FA 7 HOH   13  1013 1013 HOH   HOH A . 
FA 7 HOH   14  1014 1014 HOH   HOH A . 
FA 7 HOH   15  1015 1015 HOH   HOH A . 
FA 7 HOH   16  1016 1016 HOH   HOH A . 
FA 7 HOH   17  1017 1017 HOH   HOH A . 
FA 7 HOH   18  1018 1018 HOH   HOH A . 
FA 7 HOH   19  1019 1019 HOH   HOH A . 
FA 7 HOH   20  1020 1020 HOH   HOH A . 
FA 7 HOH   21  1021 1021 HOH   HOH A . 
FA 7 HOH   22  1022 1022 HOH   HOH A . 
FA 7 HOH   23  1023 1023 HOH   HOH A . 
FA 7 HOH   24  1024 1024 HOH   HOH A . 
FA 7 HOH   25  1025 1025 HOH   HOH A . 
FA 7 HOH   26  1026 1026 HOH   HOH A . 
FA 7 HOH   27  1027 1027 HOH   HOH A . 
FA 7 HOH   28  1028 1028 HOH   HOH A . 
FA 7 HOH   29  1029 1029 HOH   HOH A . 
FA 7 HOH   30  1030 1030 HOH   HOH A . 
FA 7 HOH   31  1031 1031 HOH   HOH A . 
FA 7 HOH   32  1032 1032 HOH   HOH A . 
FA 7 HOH   33  1033 1033 HOH   HOH A . 
FA 7 HOH   34  1034 1034 HOH   HOH A . 
FA 7 HOH   35  1035 1035 HOH   HOH A . 
FA 7 HOH   36  1036 1036 HOH   HOH A . 
FA 7 HOH   37  1037 1037 HOH   HOH A . 
FA 7 HOH   38  1038 1038 HOH   HOH A . 
FA 7 HOH   39  1039 1039 HOH   HOH A . 
FA 7 HOH   40  1040 1040 HOH   HOH A . 
FA 7 HOH   41  1041 1041 HOH   HOH A . 
FA 7 HOH   42  1042 1042 HOH   HOH A . 
FA 7 HOH   43  1043 1043 HOH   HOH A . 
FA 7 HOH   44  1044 1044 HOH   HOH A . 
FA 7 HOH   45  1045 1045 HOH   HOH A . 
FA 7 HOH   46  1046 1046 HOH   HOH A . 
FA 7 HOH   47  1047 1047 HOH   HOH A . 
FA 7 HOH   48  1048 1048 HOH   HOH A . 
FA 7 HOH   49  1049 1049 HOH   HOH A . 
FA 7 HOH   50  1050 1050 HOH   HOH A . 
FA 7 HOH   51  1051 1051 HOH   HOH A . 
FA 7 HOH   52  1052 1052 HOH   HOH A . 
FA 7 HOH   53  1053 1053 HOH   HOH A . 
FA 7 HOH   54  1054 1054 HOH   HOH A . 
FA 7 HOH   55  1055 1055 HOH   HOH A . 
FA 7 HOH   56  1056 1056 HOH   HOH A . 
FA 7 HOH   57  1057 1057 HOH   HOH A . 
FA 7 HOH   58  1058 1058 HOH   HOH A . 
FA 7 HOH   59  1059 1059 HOH   HOH A . 
FA 7 HOH   60  1060 1060 HOH   HOH A . 
FA 7 HOH   61  1061 1061 HOH   HOH A . 
FA 7 HOH   62  1062 1062 HOH   HOH A . 
FA 7 HOH   63  1063 1063 HOH   HOH A . 
FA 7 HOH   64  1064 1064 HOH   HOH A . 
FA 7 HOH   65  1065 1065 HOH   HOH A . 
FA 7 HOH   66  1066 1066 HOH   HOH A . 
FA 7 HOH   67  1067 1067 HOH   HOH A . 
FA 7 HOH   68  1068 1068 HOH   HOH A . 
FA 7 HOH   69  1069 1069 HOH   HOH A . 
FA 7 HOH   70  1070 1070 HOH   HOH A . 
FA 7 HOH   71  1071 1071 HOH   HOH A . 
FA 7 HOH   72  1072 1072 HOH   HOH A . 
FA 7 HOH   73  1073 1073 HOH   HOH A . 
FA 7 HOH   74  1074 1074 HOH   HOH A . 
FA 7 HOH   75  1075 1075 HOH   HOH A . 
FA 7 HOH   76  1076 1076 HOH   HOH A . 
FA 7 HOH   77  1077 1077 HOH   HOH A . 
FA 7 HOH   78  1078 1078 HOH   HOH A . 
FA 7 HOH   79  1079 1079 HOH   HOH A . 
FA 7 HOH   80  1080 1080 HOH   HOH A . 
FA 7 HOH   81  1081 1081 HOH   HOH A . 
FA 7 HOH   82  1082 1082 HOH   HOH A . 
FA 7 HOH   83  1083 1083 HOH   HOH A . 
FA 7 HOH   84  1084 1084 HOH   HOH A . 
FA 7 HOH   85  1085 1085 HOH   HOH A . 
FA 7 HOH   86  1086 1086 HOH   HOH A . 
FA 7 HOH   87  1087 1087 HOH   HOH A . 
FA 7 HOH   88  1088 1088 HOH   HOH A . 
FA 7 HOH   89  1089 1089 HOH   HOH A . 
FA 7 HOH   90  1090 1090 HOH   HOH A . 
FA 7 HOH   91  1091 1091 HOH   HOH A . 
FA 7 HOH   92  1092 1092 HOH   HOH A . 
FA 7 HOH   93  1093 1093 HOH   HOH A . 
FA 7 HOH   94  1094 1094 HOH   HOH A . 
FA 7 HOH   95  1095 1095 HOH   HOH A . 
FA 7 HOH   96  1096 1096 HOH   HOH A . 
FA 7 HOH   97  1097 1097 HOH   HOH A . 
FA 7 HOH   98  1098 1098 HOH   HOH A . 
FA 7 HOH   99  1099 1099 HOH   HOH A . 
FA 7 HOH   100 1100 1100 HOH   HOH A . 
FA 7 HOH   101 1101 1101 HOH   HOH A . 
FA 7 HOH   102 1102 1102 HOH   HOH A . 
FA 7 HOH   103 1103 1103 HOH   HOH A . 
FA 7 HOH   104 1104 1104 HOH   HOH A . 
FA 7 HOH   105 1105 1105 HOH   HOH A . 
FA 7 HOH   106 1106 1106 HOH   HOH A . 
FA 7 HOH   107 1107 1107 HOH   HOH A . 
FA 7 HOH   108 1108 1108 HOH   HOH A . 
FA 7 HOH   109 1109 1109 HOH   HOH A . 
FA 7 HOH   110 1110 1110 HOH   HOH A . 
FA 7 HOH   111 1111 1111 HOH   HOH A . 
FA 7 HOH   112 1112 1112 HOH   HOH A . 
FA 7 HOH   113 1113 1113 HOH   HOH A . 
FA 7 HOH   114 1114 1114 HOH   HOH A . 
FA 7 HOH   115 1115 1115 HOH   HOH A . 
FA 7 HOH   116 1116 1116 HOH   HOH A . 
FA 7 HOH   117 1117 1117 HOH   HOH A . 
FA 7 HOH   118 1118 1118 HOH   HOH A . 
FA 7 HOH   119 1119 1119 HOH   HOH A . 
FA 7 HOH   120 1120 1120 HOH   HOH A . 
FA 7 HOH   121 1121 1121 HOH   HOH A . 
FA 7 HOH   122 1122 1122 HOH   HOH A . 
FA 7 HOH   123 1123 1123 HOH   HOH A . 
FA 7 HOH   124 1124 1124 HOH   HOH A . 
FA 7 HOH   125 1125 1125 HOH   HOH A . 
FA 7 HOH   126 1126 1126 HOH   HOH A . 
FA 7 HOH   127 1127 1127 HOH   HOH A . 
FA 7 HOH   128 1128 1128 HOH   HOH A . 
FA 7 HOH   129 1129 1129 HOH   HOH A . 
FA 7 HOH   130 1130 1130 HOH   HOH A . 
FA 7 HOH   131 1131 1131 HOH   HOH A . 
FA 7 HOH   132 1132 1132 HOH   HOH A . 
FA 7 HOH   133 1133 1133 HOH   HOH A . 
FA 7 HOH   134 1134 1134 HOH   HOH A . 
FA 7 HOH   135 1135 1135 HOH   HOH A . 
FA 7 HOH   136 1136 1136 HOH   HOH A . 
FA 7 HOH   137 1137 1137 HOH   HOH A . 
FA 7 HOH   138 1138 1138 HOH   HOH A . 
FA 7 HOH   139 1139 1139 HOH   HOH A . 
FA 7 HOH   140 1140 1140 HOH   HOH A . 
FA 7 HOH   141 1141 1141 HOH   HOH A . 
FA 7 HOH   142 1142 1142 HOH   HOH A . 
FA 7 HOH   143 1143 1143 HOH   HOH A . 
FA 7 HOH   144 1144 1144 HOH   HOH A . 
FA 7 HOH   145 1145 1145 HOH   HOH A . 
FA 7 HOH   146 1146 1146 HOH   HOH A . 
FA 7 HOH   147 1147 1147 HOH   HOH A . 
FA 7 HOH   148 1148 1148 HOH   HOH A . 
FA 7 HOH   149 1149 1149 HOH   HOH A . 
FA 7 HOH   150 1150 1150 HOH   HOH A . 
FA 7 HOH   151 1151 1151 HOH   HOH A . 
FA 7 HOH   152 1152 1152 HOH   HOH A . 
FA 7 HOH   153 1153 1153 HOH   HOH A . 
FA 7 HOH   154 1154 1154 HOH   HOH A . 
FA 7 HOH   155 1155 1155 HOH   HOH A . 
FA 7 HOH   156 1156 1156 HOH   HOH A . 
FA 7 HOH   157 1157 1157 HOH   HOH A . 
FA 7 HOH   158 1158 1158 HOH   HOH A . 
FA 7 HOH   159 1159 1159 HOH   HOH A . 
FA 7 HOH   160 1160 1160 HOH   HOH A . 
FA 7 HOH   161 1161 1161 HOH   HOH A . 
FA 7 HOH   162 1162 1162 HOH   HOH A . 
FA 7 HOH   163 1163 1163 HOH   HOH A . 
FA 7 HOH   164 1164 1164 HOH   HOH A . 
FA 7 HOH   165 1165 1165 HOH   HOH A . 
FA 7 HOH   166 1166 1166 HOH   HOH A . 
FA 7 HOH   167 1167 1167 HOH   HOH A . 
FA 7 HOH   168 1168 1168 HOH   HOH A . 
FA 7 HOH   169 1169 1169 HOH   HOH A . 
FA 7 HOH   170 1170 1170 HOH   HOH A . 
FA 7 HOH   171 1171 1171 HOH   HOH A . 
FA 7 HOH   172 1172 1172 HOH   HOH A . 
FA 7 HOH   173 1173 1173 HOH   HOH A . 
FA 7 HOH   174 1174 1174 HOH   HOH A . 
FA 7 HOH   175 1175 1175 HOH   HOH A . 
FA 7 HOH   176 1176 1176 HOH   HOH A . 
FA 7 HOH   177 1177 1177 HOH   HOH A . 
FA 7 HOH   178 1178 1178 HOH   HOH A . 
FA 7 HOH   179 1179 1179 HOH   HOH A . 
FA 7 HOH   180 1180 1180 HOH   HOH A . 
FA 7 HOH   181 1181 1181 HOH   HOH A . 
FA 7 HOH   182 1182 1182 HOH   HOH A . 
FA 7 HOH   183 1183 1183 HOH   HOH A . 
FA 7 HOH   184 1184 1184 HOH   HOH A . 
FA 7 HOH   185 1185 1185 HOH   HOH A . 
FA 7 HOH   186 1186 1186 HOH   HOH A . 
FA 7 HOH   187 1187 1187 HOH   HOH A . 
FA 7 HOH   188 1188 1188 HOH   HOH A . 
FA 7 HOH   189 1189 1189 HOH   HOH A . 
FA 7 HOH   190 1190 1190 HOH   HOH A . 
FA 7 HOH   191 1191 1191 HOH   HOH A . 
FA 7 HOH   192 1192 1192 HOH   HOH A . 
FA 7 HOH   193 1193 1193 HOH   HOH A . 
FA 7 HOH   194 1194 1194 HOH   HOH A . 
FA 7 HOH   195 1195 1195 HOH   HOH A . 
FA 7 HOH   196 1196 1196 HOH   HOH A . 
FA 7 HOH   197 1197 1197 HOH   HOH A . 
FA 7 HOH   198 1198 1198 HOH   HOH A . 
FA 7 HOH   199 1199 1199 HOH   HOH A . 
FA 7 HOH   200 1200 1200 HOH   HOH A . 
FA 7 HOH   201 1201 1201 HOH   HOH A . 
FA 7 HOH   202 1202 1202 HOH   HOH A . 
FA 7 HOH   203 1203 1203 HOH   HOH A . 
FA 7 HOH   204 1204 1204 HOH   HOH A . 
FA 7 HOH   205 1205 1205 HOH   HOH A . 
FA 7 HOH   206 1206 1206 HOH   HOH A . 
FA 7 HOH   207 1207 1207 HOH   HOH A . 
FA 7 HOH   208 1208 1208 HOH   HOH A . 
FA 7 HOH   209 1209 1209 HOH   HOH A . 
FA 7 HOH   210 1210 1210 HOH   HOH A . 
FA 7 HOH   211 1211 1211 HOH   HOH A . 
FA 7 HOH   212 1212 1212 HOH   HOH A . 
FA 7 HOH   213 1213 1213 HOH   HOH A . 
FA 7 HOH   214 1214 1214 HOH   HOH A . 
FA 7 HOH   215 1215 1215 HOH   HOH A . 
FA 7 HOH   216 1216 1216 HOH   HOH A . 
FA 7 HOH   217 1217 1217 HOH   HOH A . 
FA 7 HOH   218 1218 1218 HOH   HOH A . 
FA 7 HOH   219 1219 1219 HOH   HOH A . 
FA 7 HOH   220 1220 1220 HOH   HOH A . 
FA 7 HOH   221 1221 1221 HOH   HOH A . 
FA 7 HOH   222 1222 1222 HOH   HOH A . 
FA 7 HOH   223 1223 1223 HOH   HOH A . 
FA 7 HOH   224 1224 1224 HOH   HOH A . 
FA 7 HOH   225 1225 1225 HOH   HOH A . 
FA 7 HOH   226 1226 1226 HOH   HOH A . 
FA 7 HOH   227 1227 1227 HOH   HOH A . 
FA 7 HOH   228 1228 1228 HOH   HOH A . 
FA 7 HOH   229 1229 1229 HOH   HOH A . 
FA 7 HOH   230 1230 1230 HOH   HOH A . 
FA 7 HOH   231 1231 1231 HOH   HOH A . 
FA 7 HOH   232 1232 1232 HOH   HOH A . 
FA 7 HOH   233 1233 1233 HOH   HOH A . 
FA 7 HOH   234 1234 1234 HOH   HOH A . 
FA 7 HOH   235 1235 1235 HOH   HOH A . 
FA 7 HOH   236 1236 1236 HOH   HOH A . 
FA 7 HOH   237 1237 1237 HOH   HOH A . 
FA 7 HOH   238 1238 1238 HOH   HOH A . 
FA 7 HOH   239 1239 1239 HOH   HOH A . 
FA 7 HOH   240 1240 1240 HOH   HOH A . 
FA 7 HOH   241 1241 1241 HOH   HOH A . 
FA 7 HOH   242 1242 1242 HOH   HOH A . 
FA 7 HOH   243 1243 1243 HOH   HOH A . 
FA 7 HOH   244 1244 1244 HOH   HOH A . 
FA 7 HOH   245 1245 1245 HOH   HOH A . 
FA 7 HOH   246 1246 1246 HOH   HOH A . 
FA 7 HOH   247 1247 1247 HOH   HOH A . 
FA 7 HOH   248 1248 1248 HOH   HOH A . 
FA 7 HOH   249 1249 1249 HOH   HOH A . 
FA 7 HOH   250 1250 1250 HOH   HOH A . 
FA 7 HOH   251 1251 1251 HOH   HOH A . 
FA 7 HOH   252 1252 1252 HOH   HOH A . 
FA 7 HOH   253 1253 1253 HOH   HOH A . 
FA 7 HOH   254 1254 1254 HOH   HOH A . 
FA 7 HOH   255 1255 1255 HOH   HOH A . 
FA 7 HOH   256 1256 1256 HOH   HOH A . 
FA 7 HOH   257 1257 1257 HOH   HOH A . 
FA 7 HOH   258 1258 1258 HOH   HOH A . 
FA 7 HOH   259 1259 1259 HOH   HOH A . 
FA 7 HOH   260 1260 1260 HOH   HOH A . 
FA 7 HOH   261 1261 1261 HOH   HOH A . 
FA 7 HOH   262 1262 1262 HOH   HOH A . 
FA 7 HOH   263 1263 1263 HOH   HOH A . 
FA 7 HOH   264 1264 1264 HOH   HOH A . 
FA 7 HOH   265 1265 1265 HOH   HOH A . 
FA 7 HOH   266 1266 1266 HOH   HOH A . 
FA 7 HOH   267 1267 1267 HOH   HOH A . 
FA 7 HOH   268 1268 1268 HOH   HOH A . 
FA 7 HOH   269 1269 1269 HOH   HOH A . 
FA 7 HOH   270 1270 1270 HOH   HOH A . 
FA 7 HOH   271 1271 1271 HOH   HOH A . 
FA 7 HOH   272 1272 1272 HOH   HOH A . 
FA 7 HOH   273 1273 1273 HOH   HOH A . 
FA 7 HOH   274 1274 1274 HOH   HOH A . 
FA 7 HOH   275 1275 1275 HOH   HOH A . 
FA 7 HOH   276 1276 1276 HOH   HOH A . 
FA 7 HOH   277 1277 1277 HOH   HOH A . 
FA 7 HOH   278 1278 1278 HOH   HOH A . 
FA 7 HOH   279 1279 1279 HOH   HOH A . 
FA 7 HOH   280 1280 1280 HOH   HOH A . 
FA 7 HOH   281 1281 1281 HOH   HOH A . 
FA 7 HOH   282 1282 1282 HOH   HOH A . 
FA 7 HOH   283 1283 1283 HOH   HOH A . 
FA 7 HOH   284 1284 1284 HOH   HOH A . 
FA 7 HOH   285 1285 1285 HOH   HOH A . 
FA 7 HOH   286 1286 1286 HOH   HOH A . 
FA 7 HOH   287 1287 1287 HOH   HOH A . 
FA 7 HOH   288 1288 1288 HOH   HOH A . 
FA 7 HOH   289 1289 1289 HOH   HOH A . 
FA 7 HOH   290 1290 1290 HOH   HOH A . 
FA 7 HOH   291 1291 1291 HOH   HOH A . 
FA 7 HOH   292 1292 1292 HOH   HOH A . 
FA 7 HOH   293 1293 1293 HOH   HOH A . 
FA 7 HOH   294 1294 1294 HOH   HOH A . 
FA 7 HOH   295 1295 1295 HOH   HOH A . 
FA 7 HOH   296 1296 1296 HOH   HOH A . 
FA 7 HOH   297 1297 1297 HOH   HOH A . 
FA 7 HOH   298 1298 1298 HOH   HOH A . 
FA 7 HOH   299 1299 1299 HOH   HOH A . 
FA 7 HOH   300 1300 1300 HOH   HOH A . 
FA 7 HOH   301 1301 1301 HOH   HOH A . 
FA 7 HOH   302 1302 1302 HOH   HOH A . 
FA 7 HOH   303 1303 1303 HOH   HOH A . 
FA 7 HOH   304 1304 1304 HOH   HOH A . 
FA 7 HOH   305 1305 1305 HOH   HOH A . 
FA 7 HOH   306 1306 1306 HOH   HOH A . 
FA 7 HOH   307 1307 1307 HOH   HOH A . 
FA 7 HOH   308 1308 1308 HOH   HOH A . 
FA 7 HOH   309 1309 1309 HOH   HOH A . 
FA 7 HOH   310 1310 1310 HOH   HOH A . 
FA 7 HOH   311 1311 1311 HOH   HOH A . 
FA 7 HOH   312 1312 1312 HOH   HOH A . 
FA 7 HOH   313 1313 1313 HOH   HOH A . 
FA 7 HOH   314 1314 1314 HOH   HOH A . 
FA 7 HOH   315 1315 1315 HOH   HOH A . 
FA 7 HOH   316 1316 1316 HOH   HOH A . 
FA 7 HOH   317 1317 1317 HOH   HOH A . 
FA 7 HOH   318 1318 1318 HOH   HOH A . 
FA 7 HOH   319 1319 1319 HOH   HOH A . 
FA 7 HOH   320 1320 1320 HOH   HOH A . 
FA 7 HOH   321 1321 1321 HOH   HOH A . 
FA 7 HOH   322 1322 1322 HOH   HOH A . 
FA 7 HOH   323 1323 1323 HOH   HOH A . 
FA 7 HOH   324 1324 1324 HOH   HOH A . 
FA 7 HOH   325 1325 1325 HOH   HOH A . 
FA 7 HOH   326 1326 1326 HOH   HOH A . 
FA 7 HOH   327 1327 1327 HOH   HOH A . 
FA 7 HOH   328 1328 1328 HOH   HOH A . 
FA 7 HOH   329 1329 1329 HOH   HOH A . 
FA 7 HOH   330 1330 1330 HOH   HOH A . 
FA 7 HOH   331 1331 1331 HOH   HOH A . 
FA 7 HOH   332 1332 1332 HOH   HOH A . 
FA 7 HOH   333 1333 1333 HOH   HOH A . 
FA 7 HOH   334 1334 1334 HOH   HOH A . 
FA 7 HOH   335 1335 1335 HOH   HOH A . 
FA 7 HOH   336 1336 1336 HOH   HOH A . 
FA 7 HOH   337 1337 1337 HOH   HOH A . 
FA 7 HOH   338 1338 1338 HOH   HOH A . 
FA 7 HOH   339 1339 1339 HOH   HOH A . 
FA 7 HOH   340 1340 1340 HOH   HOH A . 
FA 7 HOH   341 1341 1341 HOH   HOH A . 
FA 7 HOH   342 1342 1342 HOH   HOH A . 
FA 7 HOH   343 1343 1343 HOH   HOH A . 
FA 7 HOH   344 1344 1344 HOH   HOH A . 
FA 7 HOH   345 1345 1345 HOH   HOH A . 
FA 7 HOH   346 1346 1346 HOH   HOH A . 
FA 7 HOH   347 1347 1347 HOH   HOH A . 
FA 7 HOH   348 1348 1348 HOH   HOH A . 
FA 7 HOH   349 1349 1349 HOH   HOH A . 
FA 7 HOH   350 1350 1350 HOH   HOH A . 
FA 7 HOH   351 1351 1351 HOH   HOH A . 
FA 7 HOH   352 1352 1352 HOH   HOH A . 
FA 7 HOH   353 1353 1353 HOH   HOH A . 
FA 7 HOH   354 1354 1354 HOH   HOH A . 
FA 7 HOH   355 1355 1355 HOH   HOH A . 
FA 7 HOH   356 1356 1356 HOH   HOH A . 
FA 7 HOH   357 1357 1357 HOH   HOH A . 
FA 7 HOH   358 1358 1358 HOH   HOH A . 
FA 7 HOH   359 1359 1359 HOH   HOH A . 
FA 7 HOH   360 1360 1360 HOH   HOH A . 
FA 7 HOH   361 1361 1361 HOH   HOH A . 
FA 7 HOH   362 1362 1362 HOH   HOH A . 
FA 7 HOH   363 1363 1363 HOH   HOH A . 
FA 7 HOH   364 1364 1364 HOH   HOH A . 
FA 7 HOH   365 1365 1365 HOH   HOH A . 
FA 7 HOH   366 1366 1366 HOH   HOH A . 
FA 7 HOH   367 1367 1367 HOH   HOH A . 
FA 7 HOH   368 1368 1368 HOH   HOH A . 
FA 7 HOH   369 1369 1369 HOH   HOH A . 
FA 7 HOH   370 1370 1370 HOH   HOH A . 
FA 7 HOH   371 1371 1371 HOH   HOH A . 
FA 7 HOH   372 1372 1372 HOH   HOH A . 
FA 7 HOH   373 1373 1373 HOH   HOH A . 
FA 7 HOH   374 1374 1374 HOH   HOH A . 
FA 7 HOH   375 1375 1375 HOH   HOH A . 
FA 7 HOH   376 1376 1376 HOH   HOH A . 
FA 7 HOH   377 1377 1377 HOH   HOH A . 
FA 7 HOH   378 1378 1378 HOH   HOH A . 
FA 7 HOH   379 1379 1379 HOH   HOH A . 
FA 7 HOH   380 1380 1380 HOH   HOH A . 
FA 7 HOH   381 1381 1381 HOH   HOH A . 
FA 7 HOH   382 1382 1382 HOH   HOH A . 
FA 7 HOH   383 1383 1383 HOH   HOH A . 
FA 7 HOH   384 1384 1384 HOH   HOH A . 
FA 7 HOH   385 1385 1385 HOH   HOH A . 
FA 7 HOH   386 1386 1386 HOH   HOH A . 
FA 7 HOH   387 1387 1387 HOH   HOH A . 
FA 7 HOH   388 1388 1388 HOH   HOH A . 
FA 7 HOH   389 1389 1389 HOH   HOH A . 
FA 7 HOH   390 1390 1390 HOH   HOH A . 
FA 7 HOH   391 1391 1391 HOH   HOH A . 
FA 7 HOH   392 1392 1392 HOH   HOH A . 
FA 7 HOH   393 1393 1393 HOH   HOH A . 
FA 7 HOH   394 1394 1394 HOH   HOH A . 
FA 7 HOH   395 1395 1395 HOH   HOH A . 
FA 7 HOH   396 1396 1396 HOH   HOH A . 
FA 7 HOH   397 1397 1397 HOH   HOH A . 
FA 7 HOH   398 1398 1398 HOH   HOH A . 
FA 7 HOH   399 1399 1399 HOH   HOH A . 
FA 7 HOH   400 1400 1400 HOH   HOH A . 
FA 7 HOH   401 1401 1401 HOH   HOH A . 
FA 7 HOH   402 1402 1402 HOH   HOH A . 
FA 7 HOH   403 1403 1403 HOH   HOH A . 
FA 7 HOH   404 1404 1404 HOH   HOH A . 
FA 7 HOH   405 1405 1405 HOH   HOH A . 
FA 7 HOH   406 1406 1406 HOH   HOH A . 
FA 7 HOH   407 1407 1407 HOH   HOH A . 
FA 7 HOH   408 1408 1408 HOH   HOH A . 
FA 7 HOH   409 1409 1409 HOH   HOH A . 
FA 7 HOH   410 1410 1410 HOH   HOH A . 
FA 7 HOH   411 1411 1411 HOH   HOH A . 
FA 7 HOH   412 1412 1412 HOH   HOH A . 
FA 7 HOH   413 1413 1413 HOH   HOH A . 
FA 7 HOH   414 1414 1414 HOH   HOH A . 
FA 7 HOH   415 1415 1415 HOH   HOH A . 
FA 7 HOH   416 1416 1416 HOH   HOH A . 
FA 7 HOH   417 1417 1417 HOH   HOH A . 
FA 7 HOH   418 1418 1418 HOH   HOH A . 
FA 7 HOH   419 1419 1419 HOH   HOH A . 
FA 7 HOH   420 1420 1420 HOH   HOH A . 
FA 7 HOH   421 1421 1421 HOH   HOH A . 
FA 7 HOH   422 1422 1422 HOH   HOH A . 
FA 7 HOH   423 1423 1423 HOH   HOH A . 
FA 7 HOH   424 1424 1424 HOH   HOH A . 
FA 7 HOH   425 1425 1425 HOH   HOH A . 
FA 7 HOH   426 1426 1426 HOH   HOH A . 
FA 7 HOH   427 1427 1427 HOH   HOH A . 
FA 7 HOH   428 1428 1428 HOH   HOH A . 
FA 7 HOH   429 1429 1429 HOH   HOH A . 
FA 7 HOH   430 1430 1430 HOH   HOH A . 
FA 7 HOH   431 1431 1431 HOH   HOH A . 
FA 7 HOH   432 1432 1432 HOH   HOH A . 
FA 7 HOH   433 1433 1433 HOH   HOH A . 
FA 7 HOH   434 1434 1434 HOH   HOH A . 
FA 7 HOH   435 1435 1435 HOH   HOH A . 
FA 7 HOH   436 1436 1436 HOH   HOH A . 
FA 7 HOH   437 1437 1437 HOH   HOH A . 
FA 7 HOH   438 1438 1438 HOH   HOH A . 
FA 7 HOH   439 1439 1439 HOH   HOH A . 
FA 7 HOH   440 1440 1440 HOH   HOH A . 
FA 7 HOH   441 1441 1441 HOH   HOH A . 
FA 7 HOH   442 1442 1442 HOH   HOH A . 
FA 7 HOH   443 1443 1443 HOH   HOH A . 
FA 7 HOH   444 1444 1444 HOH   HOH A . 
FA 7 HOH   445 1445 1445 HOH   HOH A . 
FA 7 HOH   446 1446 1446 HOH   HOH A . 
FA 7 HOH   447 1447 1447 HOH   HOH A . 
FA 7 HOH   448 1448 1448 HOH   HOH A . 
FA 7 HOH   449 1449 1449 HOH   HOH A . 
FA 7 HOH   450 1450 1450 HOH   HOH A . 
FA 7 HOH   451 1451 1451 HOH   HOH A . 
FA 7 HOH   452 1452 1452 HOH   HOH A . 
FA 7 HOH   453 1453 1453 HOH   HOH A . 
FA 7 HOH   454 1454 1454 HOH   HOH A . 
FA 7 HOH   455 1455 1455 HOH   HOH A . 
FA 7 HOH   456 1456 1456 HOH   HOH A . 
FA 7 HOH   457 1457 1457 HOH   HOH A . 
FA 7 HOH   458 1458 1458 HOH   HOH A . 
FA 7 HOH   459 1459 1459 HOH   HOH A . 
FA 7 HOH   460 1460 1460 HOH   HOH A . 
FA 7 HOH   461 1461 1461 HOH   HOH A . 
FA 7 HOH   462 1462 1462 HOH   HOH A . 
FA 7 HOH   463 1463 1463 HOH   HOH A . 
FA 7 HOH   464 1464 1464 HOH   HOH A . 
FA 7 HOH   465 1465 1465 HOH   HOH A . 
FA 7 HOH   466 1466 1466 HOH   HOH A . 
FA 7 HOH   467 1467 1467 HOH   HOH A . 
FA 7 HOH   468 1468 1468 HOH   HOH A . 
FA 7 HOH   469 1469 1469 HOH   HOH A . 
FA 7 HOH   470 1470 1470 HOH   HOH A . 
FA 7 HOH   471 1471 1471 HOH   HOH A . 
FA 7 HOH   472 1472 1472 HOH   HOH A . 
FA 7 HOH   473 1473 1473 HOH   HOH A . 
FA 7 HOH   474 1474 1474 HOH   HOH A . 
FA 7 HOH   475 1475 1475 HOH   HOH A . 
FA 7 HOH   476 1476 1476 HOH   HOH A . 
FA 7 HOH   477 1477 1477 HOH   HOH A . 
FA 7 HOH   478 1478 1478 HOH   HOH A . 
FA 7 HOH   479 1479 1479 HOH   HOH A . 
FA 7 HOH   480 1480 1480 HOH   HOH A . 
FA 7 HOH   481 1481 1481 HOH   HOH A . 
FA 7 HOH   482 1482 1482 HOH   HOH A . 
FA 7 HOH   483 1483 1483 HOH   HOH A . 
FA 7 HOH   484 1484 1484 HOH   HOH A . 
FA 7 HOH   485 1485 1485 HOH   HOH A . 
FA 7 HOH   486 1486 1486 HOH   HOH A . 
FA 7 HOH   487 1487 1487 HOH   HOH A . 
FA 7 HOH   488 1488 1488 HOH   HOH A . 
FA 7 HOH   489 1489 1489 HOH   HOH A . 
FA 7 HOH   490 1490 1490 HOH   HOH A . 
FA 7 HOH   491 1491 1491 HOH   HOH A . 
FA 7 HOH   492 1492 1492 HOH   HOH A . 
FA 7 HOH   493 1493 1493 HOH   HOH A . 
FA 7 HOH   494 1494 1494 HOH   HOH A . 
FA 7 HOH   495 1495 1495 HOH   HOH A . 
FA 7 HOH   496 1496 1496 HOH   HOH A . 
FA 7 HOH   497 1497 1497 HOH   HOH A . 
FA 7 HOH   498 1498 1498 HOH   HOH A . 
FA 7 HOH   499 1499 1499 HOH   HOH A . 
FA 7 HOH   500 1500 1500 HOH   HOH A . 
FA 7 HOH   501 1501 1501 HOH   HOH A . 
FA 7 HOH   502 1502 1502 HOH   HOH A . 
FA 7 HOH   503 1503 1503 HOH   HOH A . 
FA 7 HOH   504 1504 1504 HOH   HOH A . 
FA 7 HOH   505 1505 1505 HOH   HOH A . 
FA 7 HOH   506 1506 1506 HOH   HOH A . 
FA 7 HOH   507 1507 1507 HOH   HOH A . 
FA 7 HOH   508 1508 1508 HOH   HOH A . 
FA 7 HOH   509 1509 1509 HOH   HOH A . 
FA 7 HOH   510 1510 1510 HOH   HOH A . 
FA 7 HOH   511 1511 1511 HOH   HOH A . 
FA 7 HOH   512 1512 1512 HOH   HOH A . 
FA 7 HOH   513 1513 1513 HOH   HOH A . 
FA 7 HOH   514 1514 1514 HOH   HOH A . 
FA 7 HOH   515 1515 1515 HOH   HOH A . 
FA 7 HOH   516 1516 1516 HOH   HOH A . 
FA 7 HOH   517 1517 1517 HOH   HOH A . 
FA 7 HOH   518 1518 1518 HOH   HOH A . 
FA 7 HOH   519 1519 1519 HOH   HOH A . 
FA 7 HOH   520 1520 1520 HOH   HOH A . 
FA 7 HOH   521 1521 1521 HOH   HOH A . 
FA 7 HOH   522 1522 1522 HOH   HOH A . 
FA 7 HOH   523 1523 1523 HOH   HOH A . 
FA 7 HOH   524 1524 1524 HOH   HOH A . 
FA 7 HOH   525 1525 1525 HOH   HOH A . 
FA 7 HOH   526 1526 1526 HOH   HOH A . 
FA 7 HOH   527 1527 1527 HOH   HOH A . 
FA 7 HOH   528 1528 1528 HOH   HOH A . 
FA 7 HOH   529 1529 1529 HOH   HOH A . 
FA 7 HOH   530 1530 1530 HOH   HOH A . 
FA 7 HOH   531 1531 1531 HOH   HOH A . 
FA 7 HOH   532 1532 1532 HOH   HOH A . 
FA 7 HOH   533 1533 1533 HOH   HOH A . 
FA 7 HOH   534 1534 1534 HOH   HOH A . 
FA 7 HOH   535 1535 1535 HOH   HOH A . 
FA 7 HOH   536 1536 1536 HOH   HOH A . 
FA 7 HOH   537 1537 1537 HOH   HOH A . 
FA 7 HOH   538 1538 1538 HOH   HOH A . 
FA 7 HOH   539 1539 1539 HOH   HOH A . 
GA 7 HOH   1   1001 1001 HOH   HOH B . 
GA 7 HOH   2   1002 1002 HOH   HOH B . 
GA 7 HOH   3   1003 1003 HOH   HOH B . 
GA 7 HOH   4   1004 1004 HOH   HOH B . 
GA 7 HOH   5   1005 1005 HOH   HOH B . 
GA 7 HOH   6   1006 1006 HOH   HOH B . 
GA 7 HOH   7   1007 1007 HOH   HOH B . 
GA 7 HOH   8   1008 1008 HOH   HOH B . 
GA 7 HOH   9   1009 1009 HOH   HOH B . 
GA 7 HOH   10  1010 1010 HOH   HOH B . 
GA 7 HOH   11  1011 1011 HOH   HOH B . 
GA 7 HOH   12  1012 1012 HOH   HOH B . 
GA 7 HOH   13  1013 1013 HOH   HOH B . 
GA 7 HOH   14  1014 1014 HOH   HOH B . 
GA 7 HOH   15  1015 1015 HOH   HOH B . 
GA 7 HOH   16  1016 1016 HOH   HOH B . 
GA 7 HOH   17  1017 1017 HOH   HOH B . 
GA 7 HOH   18  1018 1018 HOH   HOH B . 
GA 7 HOH   19  1019 1019 HOH   HOH B . 
GA 7 HOH   20  1020 1020 HOH   HOH B . 
GA 7 HOH   21  1021 1021 HOH   HOH B . 
GA 7 HOH   22  1022 1022 HOH   HOH B . 
GA 7 HOH   23  1023 1023 HOH   HOH B . 
GA 7 HOH   24  1024 1024 HOH   HOH B . 
GA 7 HOH   25  1025 1025 HOH   HOH B . 
GA 7 HOH   26  1026 1026 HOH   HOH B . 
GA 7 HOH   27  1027 1027 HOH   HOH B . 
GA 7 HOH   28  1028 1028 HOH   HOH B . 
GA 7 HOH   29  1029 1029 HOH   HOH B . 
GA 7 HOH   30  1030 1030 HOH   HOH B . 
GA 7 HOH   31  1031 1031 HOH   HOH B . 
GA 7 HOH   32  1032 1032 HOH   HOH B . 
GA 7 HOH   33  1033 1033 HOH   HOH B . 
GA 7 HOH   34  1034 1034 HOH   HOH B . 
GA 7 HOH   35  1035 1035 HOH   HOH B . 
GA 7 HOH   36  1036 1036 HOH   HOH B . 
GA 7 HOH   37  1037 1037 HOH   HOH B . 
GA 7 HOH   38  1038 1038 HOH   HOH B . 
GA 7 HOH   39  1039 1039 HOH   HOH B . 
GA 7 HOH   40  1040 1040 HOH   HOH B . 
GA 7 HOH   41  1041 1041 HOH   HOH B . 
GA 7 HOH   42  1042 1042 HOH   HOH B . 
GA 7 HOH   43  1043 1043 HOH   HOH B . 
GA 7 HOH   44  1044 1044 HOH   HOH B . 
GA 7 HOH   45  1045 1045 HOH   HOH B . 
GA 7 HOH   46  1046 1046 HOH   HOH B . 
GA 7 HOH   47  1047 1047 HOH   HOH B . 
GA 7 HOH   48  1048 1048 HOH   HOH B . 
GA 7 HOH   49  1049 1049 HOH   HOH B . 
GA 7 HOH   50  1050 1050 HOH   HOH B . 
GA 7 HOH   51  1051 1051 HOH   HOH B . 
GA 7 HOH   52  1052 1052 HOH   HOH B . 
GA 7 HOH   53  1053 1053 HOH   HOH B . 
GA 7 HOH   54  1054 1054 HOH   HOH B . 
GA 7 HOH   55  1055 1055 HOH   HOH B . 
GA 7 HOH   56  1056 1056 HOH   HOH B . 
GA 7 HOH   57  1057 1057 HOH   HOH B . 
GA 7 HOH   58  1058 1058 HOH   HOH B . 
GA 7 HOH   59  1059 1059 HOH   HOH B . 
GA 7 HOH   60  1060 1060 HOH   HOH B . 
GA 7 HOH   61  1061 1061 HOH   HOH B . 
GA 7 HOH   62  1062 1062 HOH   HOH B . 
GA 7 HOH   63  1063 1063 HOH   HOH B . 
GA 7 HOH   64  1064 1064 HOH   HOH B . 
GA 7 HOH   65  1065 1065 HOH   HOH B . 
GA 7 HOH   66  1066 1066 HOH   HOH B . 
GA 7 HOH   67  1067 1067 HOH   HOH B . 
GA 7 HOH   68  1068 1068 HOH   HOH B . 
GA 7 HOH   69  1069 1069 HOH   HOH B . 
GA 7 HOH   70  1070 1070 HOH   HOH B . 
GA 7 HOH   71  1071 1071 HOH   HOH B . 
GA 7 HOH   72  1072 1072 HOH   HOH B . 
GA 7 HOH   73  1073 1073 HOH   HOH B . 
GA 7 HOH   74  1074 1074 HOH   HOH B . 
GA 7 HOH   75  1075 1075 HOH   HOH B . 
GA 7 HOH   76  1076 1076 HOH   HOH B . 
GA 7 HOH   77  1077 1077 HOH   HOH B . 
GA 7 HOH   78  1078 1078 HOH   HOH B . 
GA 7 HOH   79  1079 1079 HOH   HOH B . 
GA 7 HOH   80  1080 1080 HOH   HOH B . 
GA 7 HOH   81  1081 1081 HOH   HOH B . 
GA 7 HOH   82  1082 1082 HOH   HOH B . 
GA 7 HOH   83  1083 1083 HOH   HOH B . 
GA 7 HOH   84  1084 1084 HOH   HOH B . 
GA 7 HOH   85  1085 1085 HOH   HOH B . 
GA 7 HOH   86  1086 1086 HOH   HOH B . 
GA 7 HOH   87  1087 1087 HOH   HOH B . 
GA 7 HOH   88  1088 1088 HOH   HOH B . 
GA 7 HOH   89  1089 1089 HOH   HOH B . 
GA 7 HOH   90  1090 1090 HOH   HOH B . 
GA 7 HOH   91  1091 1091 HOH   HOH B . 
GA 7 HOH   92  1092 1092 HOH   HOH B . 
GA 7 HOH   93  1093 1093 HOH   HOH B . 
GA 7 HOH   94  1094 1094 HOH   HOH B . 
GA 7 HOH   95  1095 1095 HOH   HOH B . 
GA 7 HOH   96  1096 1096 HOH   HOH B . 
GA 7 HOH   97  1097 1097 HOH   HOH B . 
GA 7 HOH   98  1098 1098 HOH   HOH B . 
GA 7 HOH   99  1099 1099 HOH   HOH B . 
GA 7 HOH   100 1100 1100 HOH   HOH B . 
GA 7 HOH   101 1101 1101 HOH   HOH B . 
GA 7 HOH   102 1102 1102 HOH   HOH B . 
GA 7 HOH   103 1103 1103 HOH   HOH B . 
GA 7 HOH   104 1104 1104 HOH   HOH B . 
GA 7 HOH   105 1105 1105 HOH   HOH B . 
GA 7 HOH   106 1106 1106 HOH   HOH B . 
GA 7 HOH   107 1107 1107 HOH   HOH B . 
GA 7 HOH   108 1108 1108 HOH   HOH B . 
GA 7 HOH   109 1109 1109 HOH   HOH B . 
GA 7 HOH   110 1110 1110 HOH   HOH B . 
GA 7 HOH   111 1111 1111 HOH   HOH B . 
GA 7 HOH   112 1112 1112 HOH   HOH B . 
GA 7 HOH   113 1113 1113 HOH   HOH B . 
GA 7 HOH   114 1114 1114 HOH   HOH B . 
GA 7 HOH   115 1115 1115 HOH   HOH B . 
GA 7 HOH   116 1116 1116 HOH   HOH B . 
GA 7 HOH   117 1117 1117 HOH   HOH B . 
GA 7 HOH   118 1118 1118 HOH   HOH B . 
GA 7 HOH   119 1119 1119 HOH   HOH B . 
GA 7 HOH   120 1120 1120 HOH   HOH B . 
GA 7 HOH   121 1121 1121 HOH   HOH B . 
GA 7 HOH   122 1122 1122 HOH   HOH B . 
GA 7 HOH   123 1123 1123 HOH   HOH B . 
GA 7 HOH   124 1124 1124 HOH   HOH B . 
GA 7 HOH   125 1125 1125 HOH   HOH B . 
GA 7 HOH   126 1126 1126 HOH   HOH B . 
GA 7 HOH   127 1127 1127 HOH   HOH B . 
GA 7 HOH   128 1128 1128 HOH   HOH B . 
GA 7 HOH   129 1129 1129 HOH   HOH B . 
GA 7 HOH   130 1130 1130 HOH   HOH B . 
GA 7 HOH   131 1131 1131 HOH   HOH B . 
GA 7 HOH   132 1132 1132 HOH   HOH B . 
GA 7 HOH   133 1133 1133 HOH   HOH B . 
GA 7 HOH   134 1134 1134 HOH   HOH B . 
GA 7 HOH   135 1135 1135 HOH   HOH B . 
GA 7 HOH   136 1136 1136 HOH   HOH B . 
GA 7 HOH   137 1137 1137 HOH   HOH B . 
GA 7 HOH   138 1138 1138 HOH   HOH B . 
GA 7 HOH   139 1139 1139 HOH   HOH B . 
GA 7 HOH   140 1140 1140 HOH   HOH B . 
GA 7 HOH   141 1141 1141 HOH   HOH B . 
GA 7 HOH   142 1142 1142 HOH   HOH B . 
GA 7 HOH   143 1143 1143 HOH   HOH B . 
GA 7 HOH   144 1144 1144 HOH   HOH B . 
GA 7 HOH   145 1145 1145 HOH   HOH B . 
GA 7 HOH   146 1146 1146 HOH   HOH B . 
GA 7 HOH   147 1147 1147 HOH   HOH B . 
GA 7 HOH   148 1148 1148 HOH   HOH B . 
GA 7 HOH   149 1149 1149 HOH   HOH B . 
GA 7 HOH   150 1150 1150 HOH   HOH B . 
GA 7 HOH   151 1151 1151 HOH   HOH B . 
GA 7 HOH   152 1152 1152 HOH   HOH B . 
GA 7 HOH   153 1153 1153 HOH   HOH B . 
GA 7 HOH   154 1154 1154 HOH   HOH B . 
GA 7 HOH   155 1155 1155 HOH   HOH B . 
GA 7 HOH   156 1156 1156 HOH   HOH B . 
GA 7 HOH   157 1157 1157 HOH   HOH B . 
GA 7 HOH   158 1158 1158 HOH   HOH B . 
GA 7 HOH   159 1159 1159 HOH   HOH B . 
GA 7 HOH   160 1160 1160 HOH   HOH B . 
GA 7 HOH   161 1161 1161 HOH   HOH B . 
GA 7 HOH   162 1162 1162 HOH   HOH B . 
GA 7 HOH   163 1163 1163 HOH   HOH B . 
GA 7 HOH   164 1164 1164 HOH   HOH B . 
GA 7 HOH   165 1165 1165 HOH   HOH B . 
GA 7 HOH   166 1166 1166 HOH   HOH B . 
GA 7 HOH   167 1167 1167 HOH   HOH B . 
GA 7 HOH   168 1168 1168 HOH   HOH B . 
GA 7 HOH   169 1169 1169 HOH   HOH B . 
GA 7 HOH   170 1170 1170 HOH   HOH B . 
GA 7 HOH   171 1171 1171 HOH   HOH B . 
GA 7 HOH   172 1172 1172 HOH   HOH B . 
GA 7 HOH   173 1173 1173 HOH   HOH B . 
GA 7 HOH   174 1174 1174 HOH   HOH B . 
GA 7 HOH   175 1175 1175 HOH   HOH B . 
GA 7 HOH   176 1176 1176 HOH   HOH B . 
GA 7 HOH   177 1177 1177 HOH   HOH B . 
GA 7 HOH   178 1178 1178 HOH   HOH B . 
GA 7 HOH   179 1179 1179 HOH   HOH B . 
GA 7 HOH   180 1180 1180 HOH   HOH B . 
GA 7 HOH   181 1181 1181 HOH   HOH B . 
GA 7 HOH   182 1182 1182 HOH   HOH B . 
GA 7 HOH   183 1183 1183 HOH   HOH B . 
GA 7 HOH   184 1184 1184 HOH   HOH B . 
GA 7 HOH   185 1185 1185 HOH   HOH B . 
GA 7 HOH   186 1186 1186 HOH   HOH B . 
GA 7 HOH   187 1187 1187 HOH   HOH B . 
GA 7 HOH   188 1188 1188 HOH   HOH B . 
GA 7 HOH   189 1189 1189 HOH   HOH B . 
GA 7 HOH   190 1190 1190 HOH   HOH B . 
GA 7 HOH   191 1191 1191 HOH   HOH B . 
GA 7 HOH   192 1192 1192 HOH   HOH B . 
GA 7 HOH   193 1193 1193 HOH   HOH B . 
GA 7 HOH   194 1194 1194 HOH   HOH B . 
GA 7 HOH   195 1195 1195 HOH   HOH B . 
GA 7 HOH   196 1196 1196 HOH   HOH B . 
GA 7 HOH   197 1197 1197 HOH   HOH B . 
GA 7 HOH   198 1198 1198 HOH   HOH B . 
GA 7 HOH   199 1199 1199 HOH   HOH B . 
GA 7 HOH   200 1200 1200 HOH   HOH B . 
GA 7 HOH   201 1201 1201 HOH   HOH B . 
GA 7 HOH   202 1202 1202 HOH   HOH B . 
GA 7 HOH   203 1203 1203 HOH   HOH B . 
GA 7 HOH   204 1204 1204 HOH   HOH B . 
GA 7 HOH   205 1205 1205 HOH   HOH B . 
GA 7 HOH   206 1206 1206 HOH   HOH B . 
GA 7 HOH   207 1207 1207 HOH   HOH B . 
GA 7 HOH   208 1208 1208 HOH   HOH B . 
GA 7 HOH   209 1209 1209 HOH   HOH B . 
GA 7 HOH   210 1210 1210 HOH   HOH B . 
GA 7 HOH   211 1211 1211 HOH   HOH B . 
GA 7 HOH   212 1212 1212 HOH   HOH B . 
GA 7 HOH   213 1213 1213 HOH   HOH B . 
GA 7 HOH   214 1214 1214 HOH   HOH B . 
GA 7 HOH   215 1215 1215 HOH   HOH B . 
GA 7 HOH   216 1216 1216 HOH   HOH B . 
GA 7 HOH   217 1217 1217 HOH   HOH B . 
GA 7 HOH   218 1218 1218 HOH   HOH B . 
GA 7 HOH   219 1219 1219 HOH   HOH B . 
GA 7 HOH   220 1220 1220 HOH   HOH B . 
GA 7 HOH   221 1221 1221 HOH   HOH B . 
GA 7 HOH   222 1222 1222 HOH   HOH B . 
GA 7 HOH   223 1223 1223 HOH   HOH B . 
GA 7 HOH   224 1224 1224 HOH   HOH B . 
GA 7 HOH   225 1225 1225 HOH   HOH B . 
GA 7 HOH   226 1226 1226 HOH   HOH B . 
GA 7 HOH   227 1227 1227 HOH   HOH B . 
GA 7 HOH   228 1228 1228 HOH   HOH B . 
GA 7 HOH   229 1229 1229 HOH   HOH B . 
GA 7 HOH   230 1230 1230 HOH   HOH B . 
GA 7 HOH   231 1231 1231 HOH   HOH B . 
GA 7 HOH   232 1232 1232 HOH   HOH B . 
GA 7 HOH   233 1233 1233 HOH   HOH B . 
GA 7 HOH   234 1234 1234 HOH   HOH B . 
GA 7 HOH   235 1235 1235 HOH   HOH B . 
GA 7 HOH   236 1236 1236 HOH   HOH B . 
GA 7 HOH   237 1237 1237 HOH   HOH B . 
GA 7 HOH   238 1238 1238 HOH   HOH B . 
GA 7 HOH   239 1239 1239 HOH   HOH B . 
GA 7 HOH   240 1240 1240 HOH   HOH B . 
GA 7 HOH   241 1241 1241 HOH   HOH B . 
GA 7 HOH   242 1242 1242 HOH   HOH B . 
GA 7 HOH   243 1243 1243 HOH   HOH B . 
GA 7 HOH   244 1244 1244 HOH   HOH B . 
GA 7 HOH   245 1245 1245 HOH   HOH B . 
GA 7 HOH   246 1246 1246 HOH   HOH B . 
GA 7 HOH   247 1247 1247 HOH   HOH B . 
GA 7 HOH   248 1248 1248 HOH   HOH B . 
GA 7 HOH   249 1249 1249 HOH   HOH B . 
GA 7 HOH   250 1250 1250 HOH   HOH B . 
GA 7 HOH   251 1251 1251 HOH   HOH B . 
GA 7 HOH   252 1252 1252 HOH   HOH B . 
GA 7 HOH   253 1253 1253 HOH   HOH B . 
GA 7 HOH   254 1254 1254 HOH   HOH B . 
GA 7 HOH   255 1255 1255 HOH   HOH B . 
GA 7 HOH   256 1256 1256 HOH   HOH B . 
GA 7 HOH   257 1257 1257 HOH   HOH B . 
GA 7 HOH   258 1258 1258 HOH   HOH B . 
GA 7 HOH   259 1259 1259 HOH   HOH B . 
GA 7 HOH   260 1260 1260 HOH   HOH B . 
GA 7 HOH   261 1261 1261 HOH   HOH B . 
GA 7 HOH   262 1262 1262 HOH   HOH B . 
GA 7 HOH   263 1263 1263 HOH   HOH B . 
GA 7 HOH   264 1264 1264 HOH   HOH B . 
GA 7 HOH   265 1265 1265 HOH   HOH B . 
GA 7 HOH   266 1266 1266 HOH   HOH B . 
GA 7 HOH   267 1267 1267 HOH   HOH B . 
GA 7 HOH   268 1268 1268 HOH   HOH B . 
GA 7 HOH   269 1269 1269 HOH   HOH B . 
GA 7 HOH   270 1270 1270 HOH   HOH B . 
GA 7 HOH   271 1271 1271 HOH   HOH B . 
GA 7 HOH   272 1272 1272 HOH   HOH B . 
GA 7 HOH   273 1273 1273 HOH   HOH B . 
GA 7 HOH   274 1274 1274 HOH   HOH B . 
GA 7 HOH   275 1275 1275 HOH   HOH B . 
GA 7 HOH   276 1276 1276 HOH   HOH B . 
GA 7 HOH   277 1277 1277 HOH   HOH B . 
GA 7 HOH   278 1278 1278 HOH   HOH B . 
GA 7 HOH   279 1279 1279 HOH   HOH B . 
GA 7 HOH   280 1280 1280 HOH   HOH B . 
GA 7 HOH   281 1281 1281 HOH   HOH B . 
GA 7 HOH   282 1282 1282 HOH   HOH B . 
GA 7 HOH   283 1283 1283 HOH   HOH B . 
GA 7 HOH   284 1284 1284 HOH   HOH B . 
GA 7 HOH   285 1285 1285 HOH   HOH B . 
GA 7 HOH   286 1286 1286 HOH   HOH B . 
GA 7 HOH   287 1287 1287 HOH   HOH B . 
GA 7 HOH   288 1288 1288 HOH   HOH B . 
GA 7 HOH   289 1289 1289 HOH   HOH B . 
GA 7 HOH   290 1290 1290 HOH   HOH B . 
GA 7 HOH   291 1291 1291 HOH   HOH B . 
GA 7 HOH   292 1292 1292 HOH   HOH B . 
GA 7 HOH   293 1293 1293 HOH   HOH B . 
GA 7 HOH   294 1294 1294 HOH   HOH B . 
GA 7 HOH   295 1295 1295 HOH   HOH B . 
GA 7 HOH   296 1296 1296 HOH   HOH B . 
GA 7 HOH   297 1297 1297 HOH   HOH B . 
GA 7 HOH   298 1298 1298 HOH   HOH B . 
GA 7 HOH   299 1299 1299 HOH   HOH B . 
GA 7 HOH   300 1300 1300 HOH   HOH B . 
GA 7 HOH   301 1301 1301 HOH   HOH B . 
GA 7 HOH   302 1302 1302 HOH   HOH B . 
GA 7 HOH   303 1303 1303 HOH   HOH B . 
GA 7 HOH   304 1304 1304 HOH   HOH B . 
GA 7 HOH   305 1305 1305 HOH   HOH B . 
GA 7 HOH   306 1306 1306 HOH   HOH B . 
GA 7 HOH   307 1307 1307 HOH   HOH B . 
GA 7 HOH   308 1308 1308 HOH   HOH B . 
GA 7 HOH   309 1309 1309 HOH   HOH B . 
GA 7 HOH   310 1310 1310 HOH   HOH B . 
GA 7 HOH   311 1311 1311 HOH   HOH B . 
GA 7 HOH   312 1312 1312 HOH   HOH B . 
GA 7 HOH   313 1313 1313 HOH   HOH B . 
GA 7 HOH   314 1314 1314 HOH   HOH B . 
GA 7 HOH   315 1315 1315 HOH   HOH B . 
GA 7 HOH   316 1316 1316 HOH   HOH B . 
GA 7 HOH   317 1317 1317 HOH   HOH B . 
GA 7 HOH   318 1318 1318 HOH   HOH B . 
GA 7 HOH   319 1319 1319 HOH   HOH B . 
GA 7 HOH   320 1320 1320 HOH   HOH B . 
GA 7 HOH   321 1321 1321 HOH   HOH B . 
GA 7 HOH   322 1322 1322 HOH   HOH B . 
GA 7 HOH   323 1323 1323 HOH   HOH B . 
GA 7 HOH   324 1324 1324 HOH   HOH B . 
GA 7 HOH   325 1325 1325 HOH   HOH B . 
GA 7 HOH   326 1326 1326 HOH   HOH B . 
GA 7 HOH   327 1327 1327 HOH   HOH B . 
GA 7 HOH   328 1328 1328 HOH   HOH B . 
GA 7 HOH   329 1329 1329 HOH   HOH B . 
GA 7 HOH   330 1330 1330 HOH   HOH B . 
GA 7 HOH   331 1331 1331 HOH   HOH B . 
GA 7 HOH   332 1332 1332 HOH   HOH B . 
GA 7 HOH   333 1333 1333 HOH   HOH B . 
GA 7 HOH   334 1334 1334 HOH   HOH B . 
GA 7 HOH   335 1335 1335 HOH   HOH B . 
GA 7 HOH   336 1336 1336 HOH   HOH B . 
GA 7 HOH   337 1337 1337 HOH   HOH B . 
GA 7 HOH   338 1338 1338 HOH   HOH B . 
GA 7 HOH   339 1339 1339 HOH   HOH B . 
GA 7 HOH   340 1340 1340 HOH   HOH B . 
GA 7 HOH   341 1341 1341 HOH   HOH B . 
GA 7 HOH   342 1342 1342 HOH   HOH B . 
GA 7 HOH   343 1343 1343 HOH   HOH B . 
GA 7 HOH   344 1344 1344 HOH   HOH B . 
GA 7 HOH   345 1345 1345 HOH   HOH B . 
GA 7 HOH   346 1346 1346 HOH   HOH B . 
GA 7 HOH   347 1347 1347 HOH   HOH B . 
GA 7 HOH   348 1348 1348 HOH   HOH B . 
GA 7 HOH   349 1349 1349 HOH   HOH B . 
GA 7 HOH   350 1350 1350 HOH   HOH B . 
GA 7 HOH   351 1351 1351 HOH   HOH B . 
GA 7 HOH   352 1352 1352 HOH   HOH B . 
GA 7 HOH   353 1353 1353 HOH   HOH B . 
GA 7 HOH   354 1354 1354 HOH   HOH B . 
GA 7 HOH   355 1355 1355 HOH   HOH B . 
GA 7 HOH   356 1356 1356 HOH   HOH B . 
GA 7 HOH   357 1357 1357 HOH   HOH B . 
GA 7 HOH   358 1358 1358 HOH   HOH B . 
GA 7 HOH   359 1359 1359 HOH   HOH B . 
GA 7 HOH   360 1360 1360 HOH   HOH B . 
GA 7 HOH   361 1361 1361 HOH   HOH B . 
GA 7 HOH   362 1362 1362 HOH   HOH B . 
GA 7 HOH   363 1363 1363 HOH   HOH B . 
GA 7 HOH   364 1364 1364 HOH   HOH B . 
GA 7 HOH   365 1365 1365 HOH   HOH B . 
GA 7 HOH   366 1366 1366 HOH   HOH B . 
GA 7 HOH   367 1367 1367 HOH   HOH B . 
GA 7 HOH   368 1368 1368 HOH   HOH B . 
GA 7 HOH   369 1369 1369 HOH   HOH B . 
GA 7 HOH   370 1370 1370 HOH   HOH B . 
GA 7 HOH   371 1371 1371 HOH   HOH B . 
GA 7 HOH   372 1372 1372 HOH   HOH B . 
GA 7 HOH   373 1373 1373 HOH   HOH B . 
GA 7 HOH   374 1374 1374 HOH   HOH B . 
GA 7 HOH   375 1375 1375 HOH   HOH B . 
GA 7 HOH   376 1376 1376 HOH   HOH B . 
GA 7 HOH   377 1377 1377 HOH   HOH B . 
GA 7 HOH   378 1378 1378 HOH   HOH B . 
GA 7 HOH   379 1379 1379 HOH   HOH B . 
GA 7 HOH   380 1380 1380 HOH   HOH B . 
GA 7 HOH   381 1381 1381 HOH   HOH B . 
GA 7 HOH   382 1382 1382 HOH   HOH B . 
GA 7 HOH   383 1383 1383 HOH   HOH B . 
GA 7 HOH   384 1384 1384 HOH   HOH B . 
GA 7 HOH   385 1385 1385 HOH   HOH B . 
GA 7 HOH   386 1386 1386 HOH   HOH B . 
GA 7 HOH   387 1387 1387 HOH   HOH B . 
GA 7 HOH   388 1388 1388 HOH   HOH B . 
GA 7 HOH   389 1389 1389 HOH   HOH B . 
GA 7 HOH   390 1390 1390 HOH   HOH B . 
GA 7 HOH   391 1391 1391 HOH   HOH B . 
GA 7 HOH   392 1392 1392 HOH   HOH B . 
GA 7 HOH   393 1393 1393 HOH   HOH B . 
GA 7 HOH   394 1394 1394 HOH   HOH B . 
GA 7 HOH   395 1395 1395 HOH   HOH B . 
GA 7 HOH   396 1396 1396 HOH   HOH B . 
GA 7 HOH   397 1397 1397 HOH   HOH B . 
GA 7 HOH   398 1398 1398 HOH   HOH B . 
GA 7 HOH   399 1399 1399 HOH   HOH B . 
GA 7 HOH   400 1400 1400 HOH   HOH B . 
GA 7 HOH   401 1401 1401 HOH   HOH B . 
GA 7 HOH   402 1402 1402 HOH   HOH B . 
GA 7 HOH   403 1403 1403 HOH   HOH B . 
GA 7 HOH   404 1404 1404 HOH   HOH B . 
GA 7 HOH   405 1405 1405 HOH   HOH B . 
GA 7 HOH   406 1406 1406 HOH   HOH B . 
GA 7 HOH   407 1407 1407 HOH   HOH B . 
GA 7 HOH   408 1408 1408 HOH   HOH B . 
GA 7 HOH   409 1409 1409 HOH   HOH B . 
GA 7 HOH   410 1410 1410 HOH   HOH B . 
GA 7 HOH   411 1411 1411 HOH   HOH B . 
GA 7 HOH   412 1412 1412 HOH   HOH B . 
GA 7 HOH   413 1413 1413 HOH   HOH B . 
GA 7 HOH   414 1414 1414 HOH   HOH B . 
GA 7 HOH   415 1415 1415 HOH   HOH B . 
GA 7 HOH   416 1416 1416 HOH   HOH B . 
GA 7 HOH   417 1417 1417 HOH   HOH B . 
GA 7 HOH   418 1418 1418 HOH   HOH B . 
GA 7 HOH   419 1419 1419 HOH   HOH B . 
GA 7 HOH   420 1420 1420 HOH   HOH B . 
GA 7 HOH   421 1421 1421 HOH   HOH B . 
GA 7 HOH   422 1422 1422 HOH   HOH B . 
GA 7 HOH   423 1423 1423 HOH   HOH B . 
GA 7 HOH   424 1424 1424 HOH   HOH B . 
GA 7 HOH   425 1425 1425 HOH   HOH B . 
GA 7 HOH   426 1426 1426 HOH   HOH B . 
GA 7 HOH   427 1427 1427 HOH   HOH B . 
GA 7 HOH   428 1428 1428 HOH   HOH B . 
GA 7 HOH   429 1429 1429 HOH   HOH B . 
GA 7 HOH   430 1430 1430 HOH   HOH B . 
GA 7 HOH   431 1431 1431 HOH   HOH B . 
GA 7 HOH   432 1432 1432 HOH   HOH B . 
GA 7 HOH   433 1433 1433 HOH   HOH B . 
GA 7 HOH   434 1434 1434 HOH   HOH B . 
GA 7 HOH   435 1435 1435 HOH   HOH B . 
GA 7 HOH   436 1436 1436 HOH   HOH B . 
GA 7 HOH   437 1437 1437 HOH   HOH B . 
GA 7 HOH   438 1438 1438 HOH   HOH B . 
GA 7 HOH   439 1439 1439 HOH   HOH B . 
GA 7 HOH   440 1440 1440 HOH   HOH B . 
GA 7 HOH   441 1441 1441 HOH   HOH B . 
GA 7 HOH   442 1442 1442 HOH   HOH B . 
GA 7 HOH   443 1443 1443 HOH   HOH B . 
GA 7 HOH   444 1444 1444 HOH   HOH B . 
GA 7 HOH   445 1445 1445 HOH   HOH B . 
GA 7 HOH   446 1446 1446 HOH   HOH B . 
GA 7 HOH   447 1447 1447 HOH   HOH B . 
GA 7 HOH   448 1448 1448 HOH   HOH B . 
GA 7 HOH   449 1449 1449 HOH   HOH B . 
GA 7 HOH   450 1450 1450 HOH   HOH B . 
GA 7 HOH   451 1451 1451 HOH   HOH B . 
GA 7 HOH   452 1452 1452 HOH   HOH B . 
GA 7 HOH   453 1453 1453 HOH   HOH B . 
GA 7 HOH   454 1454 1454 HOH   HOH B . 
GA 7 HOH   455 1455 1455 HOH   HOH B . 
GA 7 HOH   456 1456 1456 HOH   HOH B . 
GA 7 HOH   457 1457 1457 HOH   HOH B . 
GA 7 HOH   458 1458 1458 HOH   HOH B . 
GA 7 HOH   459 1459 1459 HOH   HOH B . 
GA 7 HOH   460 1460 1460 HOH   HOH B . 
GA 7 HOH   461 1461 1461 HOH   HOH B . 
GA 7 HOH   462 1462 1462 HOH   HOH B . 
GA 7 HOH   463 1463 1463 HOH   HOH B . 
GA 7 HOH   464 1464 1465 HOH   HOH B . 
GA 7 HOH   465 1465 1464 HOH   HOH B . 
GA 7 HOH   466 1466 1466 HOH   HOH B . 
GA 7 HOH   467 1467 1467 HOH   HOH B . 
GA 7 HOH   468 1468 1468 HOH   HOH B . 
GA 7 HOH   469 1469 1469 HOH   HOH B . 
GA 7 HOH   470 1470 1470 HOH   HOH B . 
GA 7 HOH   471 1471 1471 HOH   HOH B . 
GA 7 HOH   472 1472 1472 HOH   HOH B . 
GA 7 HOH   473 1473 1473 HOH   HOH B . 
GA 7 HOH   474 1474 1474 HOH   HOH B . 
GA 7 HOH   475 1475 1475 HOH   HOH B . 
GA 7 HOH   476 1476 1476 HOH   HOH B . 
GA 7 HOH   477 1477 1477 HOH   HOH B . 
GA 7 HOH   478 1478 1478 HOH   HOH B . 
GA 7 HOH   479 1479 1479 HOH   HOH B . 
GA 7 HOH   480 1480 1480 HOH   HOH B . 
GA 7 HOH   481 1481 1481 HOH   HOH B . 
GA 7 HOH   482 1482 1482 HOH   HOH B . 
GA 7 HOH   483 1483 1483 HOH   HOH B . 
GA 7 HOH   484 1484 1484 HOH   HOH B . 
GA 7 HOH   485 1485 1485 HOH   HOH B . 
GA 7 HOH   486 1486 1486 HOH   HOH B . 
GA 7 HOH   487 1487 1487 HOH   HOH B . 
GA 7 HOH   488 1488 1488 HOH   HOH B . 
GA 7 HOH   489 1489 1489 HOH   HOH B . 
GA 7 HOH   490 1490 1490 HOH   HOH B . 
GA 7 HOH   491 1491 1491 HOH   HOH B . 
GA 7 HOH   492 1492 1492 HOH   HOH B . 
GA 7 HOH   493 1493 1493 HOH   HOH B . 
GA 7 HOH   494 1494 1494 HOH   HOH B . 
GA 7 HOH   495 1495 1495 HOH   HOH B . 
GA 7 HOH   496 1496 1496 HOH   HOH B . 
GA 7 HOH   497 1497 1497 HOH   HOH B . 
GA 7 HOH   498 1498 1498 HOH   HOH B . 
GA 7 HOH   499 1499 1499 HOH   HOH B . 
GA 7 HOH   500 1500 1500 HOH   HOH B . 
GA 7 HOH   501 1501 1501 HOH   HOH B . 
GA 7 HOH   502 1502 1502 HOH   HOH B . 
GA 7 HOH   503 1503 1503 HOH   HOH B . 
GA 7 HOH   504 1504 1504 HOH   HOH B . 
GA 7 HOH   505 1505 1505 HOH   HOH B . 
GA 7 HOH   506 1506 1506 HOH   HOH B . 
GA 7 HOH   507 1507 1507 HOH   HOH B . 
GA 7 HOH   508 1508 1508 HOH   HOH B . 
GA 7 HOH   509 1509 1509 HOH   HOH B . 
GA 7 HOH   510 1510 1510 HOH   HOH B . 
GA 7 HOH   511 1511 1511 HOH   HOH B . 
GA 7 HOH   512 1512 1512 HOH   HOH B . 
GA 7 HOH   513 1513 1513 HOH   HOH B . 
GA 7 HOH   514 1514 1514 HOH   HOH B . 
GA 7 HOH   515 1515 1515 HOH   HOH B . 
GA 7 HOH   516 1516 1516 HOH   HOH B . 
GA 7 HOH   517 1517 1517 HOH   HOH B . 
GA 7 HOH   518 1518 1518 HOH   HOH B . 
GA 7 HOH   519 1519 1519 HOH   HOH B . 
GA 7 HOH   520 1520 1520 HOH   HOH B . 
GA 7 HOH   521 1521 1521 HOH   HOH B . 
GA 7 HOH   522 1522 1522 HOH   HOH B . 
GA 7 HOH   523 1523 1523 HOH   HOH B . 
GA 7 HOH   524 1524 1524 HOH   HOH B . 
GA 7 HOH   525 1525 1525 HOH   HOH B . 
GA 7 HOH   526 1526 1526 HOH   HOH B . 
GA 7 HOH   527 1527 1527 HOH   HOH B . 
GA 7 HOH   528 1528 1528 HOH   HOH B . 
GA 7 HOH   529 1529 1529 HOH   HOH B . 
GA 7 HOH   530 1530 1530 HOH   HOH B . 
GA 7 HOH   531 1531 1531 HOH   HOH B . 
GA 7 HOH   532 1532 1532 HOH   HOH B . 
GA 7 HOH   533 1533 1533 HOH   HOH B . 
GA 7 HOH   534 1534 1534 HOH   HOH B . 
GA 7 HOH   535 1535 1535 HOH   HOH B . 
GA 7 HOH   536 1536 1536 HOH   HOH B . 
GA 7 HOH   537 1537 1537 HOH   HOH B . 
GA 7 HOH   538 1538 1538 HOH   HOH B . 
GA 7 HOH   539 1539 1539 HOH   HOH B . 
GA 7 HOH   540 1540 1540 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 408 ? CD  ? A GLN 382 CD  
2  1 Y 1 A GLN 408 ? OE1 ? A GLN 382 OE1 
3  1 Y 1 A GLN 408 ? NE2 ? A GLN 382 NE2 
4  1 Y 1 A PHE 678 ? CG  ? A PHE 652 CG  
5  1 Y 1 A PHE 678 ? CD1 ? A PHE 652 CD1 
6  1 Y 1 A PHE 678 ? CD2 ? A PHE 652 CD2 
7  1 Y 1 A PHE 678 ? CE1 ? A PHE 652 CE1 
8  1 Y 1 A PHE 678 ? CE2 ? A PHE 652 CE2 
9  1 Y 1 A PHE 678 ? CZ  ? A PHE 652 CZ  
10 1 Y 1 B PHE 678 ? CG  ? B PHE 652 CG  
11 1 Y 1 B PHE 678 ? CD1 ? B PHE 652 CD1 
12 1 Y 1 B PHE 678 ? CD2 ? B PHE 652 CD2 
13 1 Y 1 B PHE 678 ? CE1 ? B PHE 652 CE1 
14 1 Y 1 B PHE 678 ? CE2 ? B PHE 652 CE2 
15 1 Y 1 B PHE 678 ? CZ  ? B PHE 652 CZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                      1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                      2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                      3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? '2.11.7 (20-MAY-2020)' 4 
# 
_cell.angle_alpha                  116.05 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.71 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  98.68 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MHY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.580 
_cell.length_a_esd                 ? 
_cell.length_b                     82.410 
_cell.length_b_esd                 ? 
_cell.length_c                     83.440 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9MHY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MHY 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.41 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M magnesium formate, 20% (w/v) PEG 3,350, 0.1 M TCEP' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-11-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MHY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.66 
_reflns.d_resolution_low                               73.03 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     202912 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           81.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.66 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10634 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.615 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.67440 
_refine.aniso_B[1][2]                            -0.60200 
_refine.aniso_B[1][3]                            0.19850 
_refine.aniso_B[2][2]                            1.93430 
_refine.aniso_B[2][3]                            0.12170 
_refine.aniso_B[3][3]                            -1.25990 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               37.15 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.944 
_refine.correlation_coeff_Fo_to_Fc_free          0.931 
_refine.details                                  
;HYDROGENS WERE FULLY REFINED
  WITH ZERO OCCUPANCY AT NUCLEAR POSITION.
;
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MHY 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.66 
_refine.ls_d_res_low                             73.03 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     121156 
_refine.ls_number_reflns_R_free                  6152 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    61.3 
_refine.ls_percent_reflns_R_free                 5.080 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.202 
_refine.ls_R_factor_R_free                       0.223 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.201 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.147 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.146 
_refine.pdbx_overall_SU_R_Blow_DPI               0.180 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.370 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        9MHY 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.260 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.66 
_refine_hist.d_res_low                        73.03 
_refine_hist.number_atoms_solvent             1079 
_refine_hist.number_atoms_total               13717 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        12023 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         615 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008 ? 25642 ? t_bond_d                  2.000  HARMONIC     
'X-RAY DIFFRACTION' ? 1.00  ? 46415 ? t_angle_deg               2.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 7868  ? t_dihedral_angle_d        2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_incorr_chiral_ct        ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_pseud_angle             ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_trig_c_planes           ?      ?            
'X-RAY DIFFRACTION' ? ?     ? 4086  ? t_gen_planes              5.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 13014 ? t_it                      10.000 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_nbd                     ?      ?            
'X-RAY DIFFRACTION' ? 3.47  ? ?     ? t_omega_torsion           ?      ?            
'X-RAY DIFFRACTION' ? 14.92 ? ?     ? t_other_torsion           ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_improper_torsion        ?      ?            
'X-RAY DIFFRACTION' ? ?     ? 1816  ? t_chiral_improper_torsion 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_sum_occupancies         ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_distance        ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_angle           ?      ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_torsion         ?      ?            
'X-RAY DIFFRACTION' ? ?     ? 19779 ? t_ideal_dist_contact      4.000  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.66 
_refine_ls_shell.d_res_low                        1.75 
_refine_ls_shell.number_reflns_all                2424 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             129 
_refine_ls_shell.number_reflns_R_work             2295 
_refine_ls_shell.percent_reflns_obs               8.16 
_refine_ls_shell.percent_reflns_R_free            5.32 
_refine_ls_shell.R_factor_all                     0.2305 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2290 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2565 
# 
_struct.entry_id                     9MHY 
_struct.title                        'Human TLR8 ectodomain with small molecule agonist 1' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9MHY 
_struct_keywords.text            'Toll-like receptor 8, agonist, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 2 ? 
D  N N 3 ? 
E  N N 3 ? 
F  N N 2 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 4 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 4 ? 
Q  N N 4 ? 
R  N N 5 ? 
S  N N 5 ? 
T  N N 6 ? 
U  N N 4 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 4 ? 
CA N N 4 ? 
DA N N 5 ? 
EA N N 6 ? 
FA N N 7 ? 
GA N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TLR8_HUMAN 
_struct_ref.pdbx_db_accession          Q9NR97 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGN
PGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKV
CEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFP
CVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSF
NYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLS
ENRISPLVKDTRQSYANSSSFQRHIRKRRSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPD
IACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNL
KVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASL
TELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSN
LLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDV
T
;
_struct_ref.pdbx_align_begin           27 
# 
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 9MHY A 1 ? 801 ? Q9NR97 27 ? 827 ? 27 827 
2 1 9MHY B 1 ? 801 ? Q9NR97 27 ? 827 ? 27 827 
# 
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 9MHY GLU A 802 ? UNP Q9NR97 ? ? 'expression tag' 828 1  
1 9MHY PHE A 803 ? UNP Q9NR97 ? ? 'expression tag' 829 2  
1 9MHY LEU A 804 ? UNP Q9NR97 ? ? 'expression tag' 830 3  
1 9MHY VAL A 805 ? UNP Q9NR97 ? ? 'expression tag' 831 4  
1 9MHY PRO A 806 ? UNP Q9NR97 ? ? 'expression tag' 832 5  
1 9MHY ARG A 807 ? UNP Q9NR97 ? ? 'expression tag' 833 6  
2 9MHY GLU B 802 ? UNP Q9NR97 ? ? 'expression tag' 828 7  
2 9MHY PHE B 803 ? UNP Q9NR97 ? ? 'expression tag' 829 8  
2 9MHY LEU B 804 ? UNP Q9NR97 ? ? 'expression tag' 830 9  
2 9MHY VAL B 805 ? UNP Q9NR97 ? ? 'expression tag' 831 10 
2 9MHY PRO B 806 ? UNP Q9NR97 ? ? 'expression tag' 832 11 
2 9MHY ARG B 807 ? UNP Q9NR97 ? ? 'expression tag' 833 12 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 136 ? SER A 141 ? THR A 162 SER A 167 1 ? 6  
HELX_P HELX_P2  AA2 CYS A 244 ? ALA A 248 ? CYS A 270 ALA A 274 5 ? 5  
HELX_P HELX_P3  AA3 ASN A 277 ? LYS A 282 ? ASN A 303 LYS A 308 5 ? 6  
HELX_P HELX_P4  AA4 LEU A 297 ? GLY A 304 ? LEU A 323 GLY A 330 1 ? 8  
HELX_P HELX_P5  AA5 ALA A 305 ? LEU A 310 ? ALA A 331 LEU A 336 5 ? 6  
HELX_P HELX_P6  AA6 SER A 334 ? LEU A 340 ? SER A 360 LEU A 366 5 ? 7  
HELX_P HELX_P7  AA7 ARG A 357 ? MET A 365 ? ARG A 383 MET A 391 5 ? 9  
HELX_P HELX_P8  AA8 PHE A 385 ? PHE A 391 ? PHE A 411 PHE A 417 5 ? 7  
HELX_P HELX_P9  AA9 LYS A 450 ? ALA A 455 ? LYS A 476 ALA A 481 1 ? 6  
HELX_P HELX_P10 AB1 ASN A 538 ? ARG A 543 ? ASN A 564 ARG A 569 1 ? 6  
HELX_P HELX_P11 AB2 LEU A 551 ? PHE A 557 ? LEU A 577 PHE A 583 5 ? 7  
HELX_P HELX_P12 AB3 ARG A 593 ? TRP A 598 ? ARG A 619 TRP A 624 1 ? 6  
HELX_P HELX_P13 AB4 PRO A 629 ? ASN A 635 ? PRO A 655 ASN A 661 1 ? 7  
HELX_P HELX_P14 AB5 ASN A 654 ? PHE A 661 ? ASN A 680 PHE A 687 5 ? 8  
HELX_P HELX_P15 AB6 SER A 680 ? THR A 685 ? SER A 706 THR A 711 1 ? 6  
HELX_P HELX_P16 AB7 ASN A 726 ? GLU A 731 ? ASN A 752 GLU A 757 1 ? 6  
HELX_P HELX_P17 AB8 THR A 751 ? ASP A 753 ? THR A 777 ASP A 779 5 ? 3  
HELX_P HELX_P18 AB9 ILE A 754 ? HIS A 764 ? ILE A 780 HIS A 790 1 ? 11 
HELX_P HELX_P19 AC1 ARG A 771 ? VAL A 775 ? ARG A 797 VAL A 801 5 ? 5  
HELX_P HELX_P20 AC2 PRO A 780 ? ARG A 784 ? PRO A 806 ARG A 810 5 ? 5  
HELX_P HELX_P21 AC3 SER A 787 ? LEU A 791 ? SER A 813 LEU A 817 5 ? 5  
HELX_P HELX_P22 AC4 THR B 136 ? SER B 141 ? THR B 162 SER B 167 1 ? 6  
HELX_P HELX_P23 AC5 CYS B 244 ? ALA B 248 ? CYS B 270 ALA B 274 5 ? 5  
HELX_P HELX_P24 AC6 ASN B 277 ? LYS B 282 ? ASN B 303 LYS B 308 5 ? 6  
HELX_P HELX_P25 AC7 LEU B 297 ? GLY B 304 ? LEU B 323 GLY B 330 1 ? 8  
HELX_P HELX_P26 AC8 ALA B 305 ? LEU B 310 ? ALA B 331 LEU B 336 5 ? 6  
HELX_P HELX_P27 AC9 SER B 334 ? LEU B 340 ? SER B 360 LEU B 366 5 ? 7  
HELX_P HELX_P28 AD1 ARG B 357 ? MET B 365 ? ARG B 383 MET B 391 5 ? 9  
HELX_P HELX_P29 AD2 PHE B 385 ? PHE B 391 ? PHE B 411 PHE B 417 5 ? 7  
HELX_P HELX_P30 AD3 LYS B 450 ? ALA B 455 ? LYS B 476 ALA B 481 1 ? 6  
HELX_P HELX_P31 AD4 ASN B 538 ? ARG B 543 ? ASN B 564 ARG B 569 1 ? 6  
HELX_P HELX_P32 AD5 LEU B 551 ? PHE B 557 ? LEU B 577 PHE B 583 5 ? 7  
HELX_P HELX_P33 AD6 ARG B 593 ? TRP B 598 ? ARG B 619 TRP B 624 1 ? 6  
HELX_P HELX_P34 AD7 PRO B 629 ? ASN B 635 ? PRO B 655 ASN B 661 1 ? 7  
HELX_P HELX_P35 AD8 ASN B 654 ? PHE B 661 ? ASN B 680 PHE B 687 5 ? 8  
HELX_P HELX_P36 AD9 SER B 680 ? THR B 685 ? SER B 706 THR B 711 1 ? 6  
HELX_P HELX_P37 AE1 ASN B 726 ? GLU B 731 ? ASN B 752 GLU B 757 1 ? 6  
HELX_P HELX_P38 AE2 THR B 751 ? ASP B 753 ? THR B 777 ASP B 779 5 ? 3  
HELX_P HELX_P39 AE3 ILE B 754 ? HIS B 764 ? ILE B 780 HIS B 790 1 ? 11 
HELX_P HELX_P40 AE4 ARG B 771 ? VAL B 775 ? ARG B 797 VAL B 801 5 ? 5  
HELX_P HELX_P41 AE5 PRO B 780 ? ARG B 784 ? PRO B 806 ARG B 810 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 10  SG  ? ? ? 1_555 A  CYS 23  SG ? ? A CYS 36  A CYS 49  1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf2  disulf ?    ? A CYS 155 SG  ? ? ? 1_555 A  CYS 161 SG ? ? A CYS 181 A CYS 187 1_555 ? ? ? ? ? ? ? 2.040 ? ?               
disulf3  disulf ?    ? A CYS 231 SG  ? ? ? 1_555 A  CYS 244 SG ? ? A CYS 257 A CYS 270 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf4  disulf ?    ? A CYS 234 SG  ? ? ? 1_555 A  CYS 241 SG ? ? A CYS 260 A CYS 267 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf5  disulf ?    ? A CYS 453 SG  ? ? ? 1_555 A  CYS 483 SG ? ? A CYS 479 A CYS 509 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf6  disulf ?    ? A CYS 750 SG  ? ? ? 1_555 A  CYS 777 SG ? ? A CYS 776 A CYS 803 1_555 ? ? ? ? ? ? ? 2.022 ? ?               
disulf7  disulf ?    ? B CYS 10  SG  ? ? ? 1_555 B  CYS 23  SG ? ? B CYS 36  B CYS 49  1_555 ? ? ? ? ? ? ? 2.039 ? ?               
disulf8  disulf ?    ? B CYS 155 SG  ? ? ? 1_555 B  CYS 161 SG ? ? B CYS 181 B CYS 187 1_555 ? ? ? ? ? ? ? 2.042 ? ?               
disulf9  disulf ?    ? B CYS 231 SG  ? ? ? 1_555 B  CYS 244 SG ? ? B CYS 257 B CYS 270 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf10 disulf ?    ? B CYS 234 SG  ? ? ? 1_555 B  CYS 241 SG ? ? B CYS 260 B CYS 267 1_555 ? ? ? ? ? ? ? 2.044 ? ?               
disulf11 disulf ?    ? B CYS 453 SG  ? ? ? 1_555 B  CYS 483 SG ? ? B CYS 479 B CYS 509 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf12 disulf ?    ? B CYS 750 SG  ? ? ? 1_555 B  CYS 777 SG ? ? B CYS 776 B CYS 803 1_555 ? ? ? ? ? ? ? 2.022 ? ?               
covale1  covale one  ? A ASN 62  ND2 ? ? ? 1_555 I  NAG .   C1 ? ? A ASN 88  A NAG 901 1_555 ? ? ? ? ? ? ? 1.431 ? N-Glycosylation 
covale2  covale one  ? A ASN 89  ND2 ? ? ? 1_555 J  NAG .   C1 ? ? A ASN 115 A NAG 902 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale3  covale one  ? A ASN 221 ND2 ? ? ? 1_555 K  NAG .   C1 ? ? A ASN 247 A NAG 903 1_555 ? ? ? ? ? ? ? 1.431 ? N-Glycosylation 
covale4  covale one  ? A ASN 267 ND2 ? ? ? 1_555 C  NAG .   C1 ? ? A ASN 293 C NAG 1   1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
covale5  covale one  ? A ASN 369 ND2 ? ? ? 1_555 L  NAG .   C1 ? ? A ASN 395 A NAG 904 1_555 ? ? ? ? ? ? ? 1.428 ? N-Glycosylation 
covale6  covale one  ? A ASN 390 ND2 ? ? ? 1_555 M  NAG .   C1 ? ? A ASN 416 A NAG 905 1_555 ? ? ? ? ? ? ? 1.431 ? N-Glycosylation 
covale7  covale one  ? A ASN 485 ND2 ? ? ? 1_555 D  NAG .   C1 ? ? A ASN 511 D NAG 1   1_555 ? ? ? ? ? ? ? 1.434 ? N-Glycosylation 
covale8  covale one  ? A ASN 520 ND2 ? ? ? 1_555 N  NAG .   C1 ? ? A ASN 546 A NAG 906 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale9  covale one  ? A ASN 556 ND2 ? ? ? 1_555 O  NAG .   C1 ? ? A ASN 582 A NAG 907 1_555 ? ? ? ? ? ? ? 1.432 ? N-Glycosylation 
covale10 covale one  ? A ASN 564 ND2 ? ? ? 1_555 E  NAG .   C1 ? ? A ASN 590 E NAG 1   1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale11 covale one  ? A ASN 614 ND2 ? ? ? 1_555 P  NAG .   C1 ? ? A ASN 640 A NAG 908 1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
covale12 covale one  ? A ASN 654 ND2 ? ? ? 1_555 Q  NAG .   C1 ? ? A ASN 680 A NAG 909 1_555 ? ? ? ? ? ? ? 1.433 ? N-Glycosylation 
covale13 covale one  ? B ASN 62  ND2 ? ? ? 1_555 U  NAG .   C1 ? ? B ASN 88  B NAG 901 1_555 ? ? ? ? ? ? ? 1.431 ? N-Glycosylation 
covale14 covale one  ? B ASN 89  ND2 ? ? ? 1_555 V  NAG .   C1 ? ? B ASN 115 B NAG 902 1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
covale15 covale one  ? B ASN 221 ND2 ? ? ? 1_555 W  NAG .   C1 ? ? B ASN 247 B NAG 903 1_555 ? ? ? ? ? ? ? 1.430 ? N-Glycosylation 
covale16 covale one  ? B ASN 267 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? B ASN 293 F NAG 1   1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale17 covale one  ? B ASN 369 ND2 ? ? ? 1_555 X  NAG .   C1 ? ? B ASN 395 B NAG 904 1_555 ? ? ? ? ? ? ? 1.428 ? N-Glycosylation 
covale18 covale one  ? B ASN 390 ND2 ? ? ? 1_555 Y  NAG .   C1 ? ? B ASN 416 B NAG 905 1_555 ? ? ? ? ? ? ? 1.431 ? N-Glycosylation 
covale19 covale one  ? B ASN 485 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? B ASN 511 G NAG 1   1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale20 covale one  ? B ASN 520 ND2 ? ? ? 1_555 Z  NAG .   C1 ? ? B ASN 546 B NAG 906 1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
covale21 covale one  ? B ASN 556 ND2 ? ? ? 1_555 AA NAG .   C1 ? ? B ASN 582 B NAG 907 1_555 ? ? ? ? ? ? ? 1.430 ? N-Glycosylation 
covale22 covale one  ? B ASN 564 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? B ASN 590 H NAG 1   1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale23 covale one  ? B ASN 614 ND2 ? ? ? 1_555 BA NAG .   C1 ? ? B ASN 640 B NAG 908 1_555 ? ? ? ? ? ? ? 1.437 ? N-Glycosylation 
covale24 covale one  ? B ASN 654 ND2 ? ? ? 1_555 CA NAG .   C1 ? ? B ASN 680 B NAG 909 1_555 ? ? ? ? ? ? ? 1.432 ? N-Glycosylation 
covale25 covale both ? C NAG .   O4  ? ? ? 1_555 C  NAG .   C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.413 ? ?               
covale26 covale both ? C NAG .   O4  ? ? ? 1_555 C  BMA .   C1 ? ? C NAG 2   C BMA 3   1_555 ? ? ? ? ? ? ? 1.403 ? ?               
covale27 covale both ? C BMA .   O3  ? ? ? 1_555 C  MAN .   C1 ? ? C BMA 3   C MAN 4   1_555 ? ? ? ? ? ? ? 1.419 ? ?               
covale28 covale one  ? C BMA .   O6  ? ? ? 1_555 C  MAN .   C2 ? ? C BMA 3   C MAN 5   1_555 ? ? ? ? ? ? ? 1.485 ? ?               
covale29 covale both ? D NAG .   O4  ? ? ? 1_555 D  NAG .   C1 ? ? D NAG 1   D NAG 2   1_555 ? ? ? ? ? ? ? 1.413 ? ?               
covale30 covale both ? D NAG .   O4  ? ? ? 1_555 D  BMA .   C1 ? ? D NAG 2   D BMA 3   1_555 ? ? ? ? ? ? ? 1.423 ? ?               
covale31 covale both ? E NAG .   O4  ? ? ? 1_555 E  NAG .   C1 ? ? E NAG 1   E NAG 2   1_555 ? ? ? ? ? ? ? 1.405 ? ?               
covale32 covale both ? E NAG .   O4  ? ? ? 1_555 E  BMA .   C1 ? ? E NAG 2   E BMA 3   1_555 ? ? ? ? ? ? ? 1.417 ? ?               
covale33 covale both ? F NAG .   O4  ? ? ? 1_555 F  NAG .   C1 ? ? F NAG 1   F NAG 2   1_555 ? ? ? ? ? ? ? 1.414 ? ?               
covale34 covale both ? F NAG .   O4  ? ? ? 1_555 F  BMA .   C1 ? ? F NAG 2   F BMA 3   1_555 ? ? ? ? ? ? ? 1.402 ? ?               
covale35 covale both ? F BMA .   O3  ? ? ? 1_555 F  MAN .   C1 ? ? F BMA 3   F MAN 4   1_555 ? ? ? ? ? ? ? 1.421 ? ?               
covale36 covale one  ? F BMA .   O6  ? ? ? 1_555 F  MAN .   C2 ? ? F BMA 3   F MAN 5   1_555 ? ? ? ? ? ? ? 1.478 ? ?               
covale37 covale both ? G NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.411 ? ?               
covale38 covale both ? G NAG .   O4  ? ? ? 1_555 G  BMA .   C1 ? ? G NAG 2   G BMA 3   1_555 ? ? ? ? ? ? ? 1.422 ? ?               
covale39 covale both ? H NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.396 ? ?               
covale40 covale both ? H NAG .   O4  ? ? ? 1_555 H  BMA .   C1 ? ? H NAG 2   H BMA 3   1_555 ? ? ? ? ? ? ? 1.416 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG AA .   ? ASN B 556 ? NAG B 907 ? 1_555 ASN B 582 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG BA .   ? ASN B 614 ? NAG B 908 ? 1_555 ASN B 640 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG C  .   ? ASN A 267 ? NAG C 1   ? 1_555 ASN A 293 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG CA .   ? ASN B 654 ? NAG B 909 ? 1_555 ASN B 680 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG D  .   ? ASN A 485 ? NAG D 1   ? 1_555 ASN A 511 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG E  .   ? ASN A 564 ? NAG E 1   ? 1_555 ASN A 590 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG F  .   ? ASN B 267 ? NAG F 1   ? 1_555 ASN B 293 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG G  .   ? ASN B 485 ? NAG G 1   ? 1_555 ASN B 511 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG H  .   ? ASN B 564 ? NAG H 1   ? 1_555 ASN B 590 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG I  .   ? ASN A 62  ? NAG A 901 ? 1_555 ASN A 88  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 NAG J  .   ? ASN A 89  ? NAG A 902 ? 1_555 ASN A 115 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
12 NAG K  .   ? ASN A 221 ? NAG A 903 ? 1_555 ASN A 247 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
13 NAG L  .   ? ASN A 369 ? NAG A 904 ? 1_555 ASN A 395 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
14 NAG M  .   ? ASN A 390 ? NAG A 905 ? 1_555 ASN A 416 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
15 NAG N  .   ? ASN A 520 ? NAG A 906 ? 1_555 ASN A 546 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
16 NAG O  .   ? ASN A 556 ? NAG A 907 ? 1_555 ASN A 582 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
17 NAG P  .   ? ASN A 614 ? NAG A 908 ? 1_555 ASN A 640 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
18 NAG Q  .   ? ASN A 654 ? NAG A 909 ? 1_555 ASN A 680 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
19 NAG U  .   ? ASN B 62  ? NAG B 901 ? 1_555 ASN B 88  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
20 NAG V  .   ? ASN B 89  ? NAG B 902 ? 1_555 ASN B 115 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
21 NAG W  .   ? ASN B 221 ? NAG B 903 ? 1_555 ASN B 247 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
22 NAG X  .   ? ASN B 369 ? NAG B 904 ? 1_555 ASN B 395 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
23 NAG Y  .   ? ASN B 390 ? NAG B 905 ? 1_555 ASN B 416 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
24 NAG Z  .   ? ASN B 520 ? NAG B 906 ? 1_555 ASN B 546 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
25 CYS A  10  ? CYS A 23  ? CYS A 36  ? 1_555 CYS A 49  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
26 CYS A  155 ? CYS A 161 ? CYS A 181 ? 1_555 CYS A 187 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
27 CYS A  231 ? CYS A 244 ? CYS A 257 ? 1_555 CYS A 270 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
28 CYS A  234 ? CYS A 241 ? CYS A 260 ? 1_555 CYS A 267 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
29 CYS A  453 ? CYS A 483 ? CYS A 479 ? 1_555 CYS A 509 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
30 CYS A  750 ? CYS A 777 ? CYS A 776 ? 1_555 CYS A 803 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
31 CYS B  10  ? CYS B 23  ? CYS B 36  ? 1_555 CYS B 49  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
32 CYS B  155 ? CYS B 161 ? CYS B 181 ? 1_555 CYS B 187 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
33 CYS B  231 ? CYS B 244 ? CYS B 257 ? 1_555 CYS B 270 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
34 CYS B  234 ? CYS B 241 ? CYS B 260 ? 1_555 CYS B 267 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
35 CYS B  453 ? CYS B 483 ? CYS B 479 ? 1_555 CYS B 509 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
36 CYS B  750 ? CYS B 777 ? CYS B 776 ? 1_555 CYS B 803 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 8   A . ? TYR 34  A PRO 9   A ? PRO 35  A 1 0.26  
2 ASN 71  A . ? ASN 97  A PRO 72  A ? PRO 98  A 1 -2.49 
3 SER 779 A . ? SER 805 A PRO 780 A ? PRO 806 A 1 -8.54 
4 TYR 8   B . ? TYR 34  B PRO 9   B ? PRO 35  B 1 2.50  
5 ASN 71  B . ? ASN 97  B PRO 72  B ? PRO 98  B 1 -2.47 
6 SER 779 B . ? SER 805 B PRO 780 B ? PRO 806 B 1 -8.47 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 28 ? 
AA2 ? 2  ? 
AA3 ? 2  ? 
AA4 ? 2  ? 
AA5 ? 2  ? 
AA6 ? 2  ? 
AA7 ? 2  ? 
AA8 ? 28 ? 
AA9 ? 2  ? 
AB1 ? 2  ? 
AB2 ? 2  ? 
AB3 ? 2  ? 
AB4 ? 2  ? 
AB5 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? parallel      
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? parallel      
AA1 6  7  ? parallel      
AA1 7  8  ? parallel      
AA1 8  9  ? parallel      
AA1 9  10 ? parallel      
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA1 12 13 ? parallel      
AA1 13 14 ? parallel      
AA1 14 15 ? parallel      
AA1 15 16 ? parallel      
AA1 16 17 ? parallel      
AA1 17 18 ? parallel      
AA1 18 19 ? parallel      
AA1 19 20 ? parallel      
AA1 20 21 ? parallel      
AA1 21 22 ? parallel      
AA1 22 23 ? parallel      
AA1 23 24 ? parallel      
AA1 24 25 ? parallel      
AA1 25 26 ? parallel      
AA1 26 27 ? parallel      
AA1 27 28 ? parallel      
AA2 1  2  ? parallel      
AA3 1  2  ? parallel      
AA4 1  2  ? parallel      
AA5 1  2  ? parallel      
AA6 1  2  ? parallel      
AA7 1  2  ? parallel      
AA8 1  2  ? anti-parallel 
AA8 2  3  ? parallel      
AA8 3  4  ? parallel      
AA8 4  5  ? parallel      
AA8 5  6  ? parallel      
AA8 6  7  ? parallel      
AA8 7  8  ? parallel      
AA8 8  9  ? parallel      
AA8 9  10 ? parallel      
AA8 10 11 ? parallel      
AA8 11 12 ? parallel      
AA8 12 13 ? parallel      
AA8 13 14 ? parallel      
AA8 14 15 ? parallel      
AA8 15 16 ? parallel      
AA8 16 17 ? parallel      
AA8 17 18 ? parallel      
AA8 18 19 ? parallel      
AA8 19 20 ? parallel      
AA8 20 21 ? parallel      
AA8 21 22 ? parallel      
AA8 22 23 ? parallel      
AA8 23 24 ? parallel      
AA8 24 25 ? parallel      
AA8 25 26 ? parallel      
AA8 26 27 ? parallel      
AA8 27 28 ? parallel      
AA9 1  2  ? parallel      
AB1 1  2  ? parallel      
AB2 1  2  ? parallel      
AB3 1  2  ? parallel      
AB4 1  2  ? parallel      
AB5 1  2  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 11  ? LYS A 13  ? ASP A 37  LYS A 39  
AA1 2  ILE A 20  ? GLU A 22  ? ILE A 46  GLU A 48  
AA1 3  GLU A 41  ? ASP A 43  ? GLU A 67  ASP A 69  
AA1 4  LYS A 65  ? ASN A 67  ? LYS A 91  ASN A 93  
AA1 5  GLU A 103 ? LEU A 105 ? GLU A 129 LEU A 131 
AA1 6  GLU A 124 ? SER A 126 ? GLU A 150 SER A 152 
AA1 7  ASN A 148 ? TYR A 150 ? ASN A 174 TYR A 176 
AA1 8  LEU A 179 ? SER A 181 ? LEU A 205 SER A 207 
AA1 9  LYS A 200 ? PHE A 202 ? LYS A 226 PHE A 228 
AA1 10 LEU A 224 ? ASP A 226 ? LEU A 250 ASP A 252 
AA1 11 TYR A 265 ? ASN A 267 ? TYR A 291 ASN A 293 
AA1 12 VAL A 289 ? ASP A 291 ? VAL A 315 ASP A 317 
AA1 13 ILE A 315 ? ASP A 317 ? ILE A 341 ASP A 343 
AA1 14 ALA A 345 ? HIS A 347 ? ALA A 371 HIS A 373 
AA1 15 THR A 372 ? ASN A 374 ? THR A 398 ASN A 400 
AA1 16 ILE A 396 ? TYR A 398 ? ILE A 422 TYR A 424 
AA1 17 ALA A 459 ? ASP A 461 ? ALA A 485 ASP A 487 
AA1 18 CYS A 483 ? ASN A 485 ? CYS A 509 ASN A 511 
AA1 19 TYR A 508 ? ASP A 510 ? TYR A 534 ASP A 536 
AA1 20 VAL A 532 ? ASP A 534 ? VAL A 558 ASP A 560 
AA1 21 VAL A 562 ? ASN A 564 ? VAL A 588 ASN A 590 
AA1 22 GLU A 586 ? VAL A 588 ? GLU A 612 VAL A 614 
AA1 23 ARG A 617 ? ASP A 619 ? ARG A 643 ASP A 645 
AA1 24 GLU A 642 ? HIS A 644 ? GLU A 668 HIS A 670 
AA1 25 LEU A 666 ? ASP A 668 ? LEU A 692 ASP A 694 
AA1 26 THR A 690 ? LEU A 692 ? THR A 716 LEU A 718 
AA1 27 HIS A 714 ? ASP A 716 ? HIS A 740 ASP A 742 
AA1 28 MET A 740 ? GLU A 742 ? MET A 766 GLU A 768 
AA2 1  HIS A 51  ? ILE A 52  ? HIS A 77  ILE A 78  
AA2 2  ASN A 89  ? ILE A 90  ? ASN A 115 ILE A 116 
AA3 1  ASN A 134 ? ILE A 135 ? ASN A 160 ILE A 161 
AA3 2  ASN A 165 ? ILE A 166 ? ASN A 191 ILE A 192 
AA4 1  TYR A 210 ? ILE A 211 ? TYR A 236 ILE A 237 
AA4 2  ASN A 251 ? ILE A 252 ? ASN A 277 ILE A 278 
AA5 1  GLU A 355 ? LEU A 356 ? GLU A 381 LEU A 382 
AA5 2  GLN A 382 ? ILE A 383 ? GLN A 408 ILE A 409 
AA6 1  GLU A 580 ? SER A 581 ? GLU A 606 SER A 607 
AA6 2  GLY A 611 ? LEU A 612 ? GLY A 637 LEU A 638 
AA7 1  PHE A 748 ? GLU A 749 ? PHE A 774 GLU A 775 
AA7 2  CYS A 777 ? SER A 779 ? CYS A 803 SER A 805 
AA8 1  ASP B 11  ? LYS B 13  ? ASP B 37  LYS B 39  
AA8 2  ILE B 20  ? GLU B 22  ? ILE B 46  GLU B 48  
AA8 3  GLU B 41  ? ASP B 43  ? GLU B 67  ASP B 69  
AA8 4  LYS B 65  ? ASN B 67  ? LYS B 91  ASN B 93  
AA8 5  GLU B 103 ? LEU B 105 ? GLU B 129 LEU B 131 
AA8 6  GLU B 124 ? SER B 126 ? GLU B 150 SER B 152 
AA8 7  ASN B 148 ? TYR B 150 ? ASN B 174 TYR B 176 
AA8 8  LEU B 179 ? SER B 181 ? LEU B 205 SER B 207 
AA8 9  LYS B 200 ? PHE B 202 ? LYS B 226 PHE B 228 
AA8 10 LEU B 224 ? ASP B 226 ? LEU B 250 ASP B 252 
AA8 11 TYR B 265 ? ASN B 267 ? TYR B 291 ASN B 293 
AA8 12 VAL B 289 ? ASP B 291 ? VAL B 315 ASP B 317 
AA8 13 ILE B 315 ? ASP B 317 ? ILE B 341 ASP B 343 
AA8 14 ALA B 345 ? HIS B 347 ? ALA B 371 HIS B 373 
AA8 15 THR B 372 ? ASN B 374 ? THR B 398 ASN B 400 
AA8 16 ILE B 396 ? TYR B 398 ? ILE B 422 TYR B 424 
AA8 17 ALA B 459 ? ASP B 461 ? ALA B 485 ASP B 487 
AA8 18 CYS B 483 ? ASN B 485 ? CYS B 509 ASN B 511 
AA8 19 TYR B 508 ? ASP B 510 ? TYR B 534 ASP B 536 
AA8 20 VAL B 532 ? ASP B 534 ? VAL B 558 ASP B 560 
AA8 21 VAL B 562 ? ASN B 564 ? VAL B 588 ASN B 590 
AA8 22 GLU B 586 ? VAL B 588 ? GLU B 612 VAL B 614 
AA8 23 ARG B 617 ? ASP B 619 ? ARG B 643 ASP B 645 
AA8 24 GLU B 642 ? HIS B 644 ? GLU B 668 HIS B 670 
AA8 25 LEU B 666 ? ASP B 668 ? LEU B 692 ASP B 694 
AA8 26 THR B 690 ? LEU B 692 ? THR B 716 LEU B 718 
AA8 27 HIS B 714 ? ASP B 716 ? HIS B 740 ASP B 742 
AA8 28 MET B 740 ? GLU B 742 ? MET B 766 GLU B 768 
AA9 1  HIS B 51  ? ILE B 52  ? HIS B 77  ILE B 78  
AA9 2  ASN B 89  ? ILE B 90  ? ASN B 115 ILE B 116 
AB1 1  ASN B 134 ? ILE B 135 ? ASN B 160 ILE B 161 
AB1 2  ASN B 165 ? ILE B 166 ? ASN B 191 ILE B 192 
AB2 1  TYR B 210 ? ILE B 211 ? TYR B 236 ILE B 237 
AB2 2  ASN B 251 ? ILE B 252 ? ASN B 277 ILE B 278 
AB3 1  GLU B 355 ? LEU B 356 ? GLU B 381 LEU B 382 
AB3 2  GLN B 382 ? ILE B 383 ? GLN B 408 ILE B 409 
AB4 1  GLU B 580 ? SER B 581 ? GLU B 606 SER B 607 
AB4 2  GLY B 611 ? LEU B 612 ? GLY B 637 LEU B 638 
AB5 1  PHE B 748 ? GLU B 749 ? PHE B 774 GLU B 775 
AB5 2  CYS B 777 ? SER B 779 ? CYS B 803 SER B 805 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N ASP A 11  ? N ASP A 37  O GLU A 22  ? O GLU A 48  
AA1 2  3  N ALA A 21  ? N ALA A 47  O GLU A 41  ? O GLU A 67  
AA1 3  4  N LEU A 42  ? N LEU A 68  O LYS A 65  ? O LYS A 91  
AA1 4  5  N ILE A 66  ? N ILE A 92  O LEU A 105 ? O LEU A 131 
AA1 5  6  N LEU A 104 ? N LEU A 130 O SER A 126 ? O SER A 152 
AA1 6  7  N LEU A 125 ? N LEU A 151 O TYR A 150 ? O TYR A 176 
AA1 7  8  N LEU A 149 ? N LEU A 175 O LEU A 179 ? O LEU A 205 
AA1 8  9  N LEU A 180 ? N LEU A 206 O PHE A 202 ? O PHE A 228 
AA1 9  10 N LEU A 201 ? N LEU A 227 O LEU A 224 ? O LEU A 250 
AA1 10 11 N LEU A 225 ? N LEU A 251 O ASN A 267 ? O ASN A 293 
AA1 11 12 N LEU A 266 ? N LEU A 292 O ASP A 291 ? O ASP A 317 
AA1 12 13 N LEU A 290 ? N LEU A 316 O ASP A 317 ? O ASP A 343 
AA1 13 14 N LEU A 316 ? N LEU A 342 O HIS A 347 ? O HIS A 373 
AA1 14 15 N LEU A 346 ? N LEU A 372 O ASN A 374 ? O ASN A 400 
AA1 15 16 N ILE A 373 ? N ILE A 399 O TYR A 398 ? O TYR A 424 
AA1 16 17 N ILE A 397 ? N ILE A 423 O ASP A 461 ? O ASP A 487 
AA1 17 18 N LEU A 460 ? N LEU A 486 O CYS A 483 ? O CYS A 509 
AA1 18 19 N LEU A 484 ? N LEU A 510 O ASP A 510 ? O ASP A 536 
AA1 19 20 N LEU A 509 ? N LEU A 535 O ASP A 534 ? O ASP A 560 
AA1 20 21 N LEU A 533 ? N LEU A 559 O VAL A 562 ? O VAL A 588 
AA1 21 22 N LEU A 563 ? N LEU A 589 O VAL A 588 ? O VAL A 614 
AA1 22 23 N LEU A 587 ? N LEU A 613 O ARG A 617 ? O ARG A 643 
AA1 23 24 N LEU A 618 ? N LEU A 644 O HIS A 644 ? O HIS A 670 
AA1 24 25 N LEU A 643 ? N LEU A 669 O ASP A 668 ? O ASP A 694 
AA1 25 26 N LEU A 667 ? N LEU A 693 O LEU A 692 ? O LEU A 718 
AA1 26 27 N LEU A 691 ? N LEU A 717 O HIS A 714 ? O HIS A 740 
AA1 27 28 N LEU A 715 ? N LEU A 741 O MET A 740 ? O MET A 766 
AA2 1  2  N ILE A 52  ? N ILE A 78  O ASN A 89  ? O ASN A 115 
AA3 1  2  N ILE A 135 ? N ILE A 161 O ASN A 165 ? O ASN A 191 
AA4 1  2  N ILE A 211 ? N ILE A 237 O ASN A 251 ? O ASN A 277 
AA5 1  2  N LEU A 356 ? N LEU A 382 O GLN A 382 ? O GLN A 408 
AA6 1  2  N SER A 581 ? N SER A 607 O GLY A 611 ? O GLY A 637 
AA7 1  2  N PHE A 748 ? N PHE A 774 O ALA A 778 ? O ALA A 804 
AA8 1  2  N ASP B 11  ? N ASP B 37  O GLU B 22  ? O GLU B 48  
AA8 2  3  N ALA B 21  ? N ALA B 47  O GLU B 41  ? O GLU B 67  
AA8 3  4  N LEU B 42  ? N LEU B 68  O LYS B 65  ? O LYS B 91  
AA8 4  5  N ILE B 66  ? N ILE B 92  O LEU B 105 ? O LEU B 131 
AA8 5  6  N LEU B 104 ? N LEU B 130 O SER B 126 ? O SER B 152 
AA8 6  7  N LEU B 125 ? N LEU B 151 O TYR B 150 ? O TYR B 176 
AA8 7  8  N LEU B 149 ? N LEU B 175 O LEU B 179 ? O LEU B 205 
AA8 8  9  N LEU B 180 ? N LEU B 206 O PHE B 202 ? O PHE B 228 
AA8 9  10 N LEU B 201 ? N LEU B 227 O LEU B 224 ? O LEU B 250 
AA8 10 11 N LEU B 225 ? N LEU B 251 O ASN B 267 ? O ASN B 293 
AA8 11 12 N LEU B 266 ? N LEU B 292 O ASP B 291 ? O ASP B 317 
AA8 12 13 N LEU B 290 ? N LEU B 316 O ASP B 317 ? O ASP B 343 
AA8 13 14 N LEU B 316 ? N LEU B 342 O HIS B 347 ? O HIS B 373 
AA8 14 15 N LEU B 346 ? N LEU B 372 O ASN B 374 ? O ASN B 400 
AA8 15 16 N ILE B 373 ? N ILE B 399 O TYR B 398 ? O TYR B 424 
AA8 16 17 N ILE B 397 ? N ILE B 423 O ASP B 461 ? O ASP B 487 
AA8 17 18 N LEU B 460 ? N LEU B 486 O CYS B 483 ? O CYS B 509 
AA8 18 19 N LEU B 484 ? N LEU B 510 O ASP B 510 ? O ASP B 536 
AA8 19 20 N LEU B 509 ? N LEU B 535 O ASP B 534 ? O ASP B 560 
AA8 20 21 N LEU B 533 ? N LEU B 559 O VAL B 562 ? O VAL B 588 
AA8 21 22 N LEU B 563 ? N LEU B 589 O VAL B 588 ? O VAL B 614 
AA8 22 23 N LEU B 587 ? N LEU B 613 O ARG B 617 ? O ARG B 643 
AA8 23 24 N LEU B 618 ? N LEU B 644 O HIS B 644 ? O HIS B 670 
AA8 24 25 N LEU B 643 ? N LEU B 669 O ASP B 668 ? O ASP B 694 
AA8 25 26 N LEU B 667 ? N LEU B 693 O LEU B 692 ? O LEU B 718 
AA8 26 27 N LEU B 691 ? N LEU B 717 O HIS B 714 ? O HIS B 740 
AA8 27 28 N LEU B 715 ? N LEU B 741 O MET B 740 ? O MET B 766 
AA9 1  2  N ILE B 52  ? N ILE B 78  O ASN B 89  ? O ASN B 115 
AB1 1  2  N ILE B 135 ? N ILE B 161 O ASN B 165 ? O ASN B 191 
AB2 1  2  N ILE B 211 ? N ILE B 237 O ASN B 251 ? O ASN B 277 
AB3 1  2  N LEU B 356 ? N LEU B 382 O GLN B 382 ? O GLN B 408 
AB4 1  2  N SER B 581 ? N SER B 607 O GLY B 611 ? O GLY B 637 
AB5 1  2  N PHE B 748 ? N PHE B 774 O ALA B 778 ? O ALA B 804 
# 
_pdbx_entry_details.entry_id                   9MHY 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 HD21 B ASN 680 ? ? C1  B NAG 909 ? ? 1.38 
2  1 HD21 A ASN 680 ? ? C1  A NAG 909 ? ? 1.38 
3  1 HD21 A ASN 582 ? ? C1  A NAG 907 ? ? 1.41 
4  1 HD21 B ASN 582 ? ? C1  B NAG 907 ? ? 1.41 
5  1 HD21 B ASN 247 ? ? C1  B NAG 903 ? ? 1.43 
6  1 HD21 B ASN 88  ? ? C1  B NAG 901 ? ? 1.43 
7  1 HD21 A ASN 88  ? ? C1  A NAG 901 ? ? 1.43 
8  1 HD21 A ASN 247 ? ? C1  A NAG 903 ? ? 1.44 
9  1 HD21 B ASN 416 ? ? C1  B NAG 905 ? ? 1.44 
10 1 HD21 A ASN 416 ? ? C1  A NAG 905 ? ? 1.44 
11 1 HD21 B ASN 395 ? ? C1  B NAG 904 ? ? 1.44 
12 1 HD21 A ASN 395 ? ? C1  A NAG 904 ? ? 1.45 
13 1 HD21 B ASN 546 ? ? C1  B NAG 906 ? ? 1.47 
14 1 HD21 A ASN 546 ? ? C1  A NAG 906 ? ? 1.47 
15 1 HD21 A ASN 640 ? ? C1  A NAG 908 ? ? 1.47 
16 1 HD21 B ASN 640 ? ? C1  B NAG 908 ? ? 1.47 
17 1 HD21 A ASN 115 ? ? C1  A NAG 902 ? ? 1.47 
18 1 HD21 B ASN 115 ? ? C1  B NAG 902 ? ? 1.47 
19 1 HD21 A ASN 511 ? ? C1  D NAG 1   ? ? 1.49 
20 1 HD21 B ASN 511 ? ? C1  G NAG 1   ? ? 1.49 
21 1 HH   A TYR 353 ? ? O   A PHE 405 ? ? 1.50 
22 1 O    A LEU 127 ? ? HG  A SER 147 ? ? 1.54 
23 1 OE2  A GLU 668 ? ? HE2 A HIS 670 ? ? 1.55 
24 1 O    A LEU 641 ? ? HG  A SER 665 ? ? 1.57 
25 1 HH   B TYR 353 ? ? O   B PHE 405 ? ? 1.57 
26 1 OD1  B ASP 545 ? ? HG1 B THR 574 ? ? 1.59 
27 1 OD1  A ASP 545 ? ? HG1 A THR 574 ? ? 1.59 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    TYR 
_pdbx_validate_symm_contact.auth_seq_id_1     482 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HO4 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    NAG 
_pdbx_validate_symm_contact.auth_seq_id_2     904 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_455 
_pdbx_validate_symm_contact.dist              1.34 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 73  ? ? -115.87 -168.72 
2  1 LEU A 86  ? ? -114.89 55.16   
3  1 ASN A 156 ? ? -124.76 -166.33 
4  1 PHE A 183 ? ? 53.39   -130.93 
5  1 SER A 214 ? ? 74.51   -35.37  
6  1 CYS A 257 ? ? 66.04   63.99   
7  1 MET A 310 ? ? -117.36 69.69   
8  1 ASN A 321 ? ? -120.43 -164.66 
9  1 SER A 329 ? ? -146.91 38.34   
10 1 VAL A 378 ? ? 81.83   101.69  
11 1 ASN A 419 ? ? -157.52 70.05   
12 1 GLU A 427 ? ? 66.39   64.09   
13 1 ASN A 428 ? ? -134.19 -158.24 
14 1 ASN A 491 ? ? -124.14 -159.51 
15 1 ASN A 540 ? ? -118.12 -161.71 
16 1 LEU A 550 ? ? 64.24   -0.86   
17 1 ASP A 601 ? ? 63.11   -58.87  
18 1 ASN A 618 ? ? -115.28 -166.56 
19 1 ASN A 674 ? ? -121.00 -158.84 
20 1 ASN A 674 ? ? -121.00 -159.13 
21 1 ASN A 698 ? ? -128.31 -161.16 
22 1 SER A 706 ? ? -149.15 51.15   
23 1 ASN A 746 ? ? -114.74 -157.85 
24 1 THR A 758 ? ? -149.36 -78.71  
25 1 LEU B 86  ? ? -114.89 55.20   
26 1 ASN B 156 ? ? -124.83 -166.52 
27 1 PHE B 183 ? ? 53.47   -130.35 
28 1 SER B 214 ? ? 74.85   -35.78  
29 1 CYS B 257 ? ? 65.50   64.04   
30 1 MET B 310 ? ? -117.07 69.93   
31 1 ASN B 321 ? ? -120.60 -164.50 
32 1 SER B 329 ? ? -147.14 38.12   
33 1 VAL B 378 ? ? 81.63   101.92  
34 1 ASN B 419 ? ? -158.06 70.58   
35 1 GLU B 427 ? ? 64.93   64.49   
36 1 ASN B 428 ? ? -134.38 -159.80 
37 1 ASN B 491 ? ? -123.67 -161.32 
38 1 ASN B 540 ? ? -118.88 -161.05 
39 1 LEU B 550 ? ? 64.67   -1.41   
40 1 ASP B 601 ? ? 66.52   -54.60  
41 1 ASN B 618 ? ? -115.53 -166.56 
42 1 ASN B 674 ? ? -120.36 -158.89 
43 1 ASN B 698 ? ? -128.13 -162.77 
44 1 SER B 706 ? ? -149.69 50.80   
45 1 ASN B 746 ? ? -115.18 -157.41 
46 1 THR B 758 ? ? -149.31 -78.75  
47 1 LEU B 817 ? ? 70.15   124.59  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 26.8916 6.3467 -30.5878 -0.0842 ? 0.0293  ? -0.0197 ? -0.0406 ? 0.0206  ? -0.0443 ? 0.4271 ? 
0.1200 ? -0.1875 ? 0.3426 ? -0.0779 ? 0.6681 ? -0.0451 ? 0.0001  ? 0.0478 ? 0.0162 ? 0.0601 ? 0.0915  ? -0.0771 ? -0.1034 ? 
-0.0150 ? 
2 'X-RAY DIFFRACTION' ? refined 64.9100 8.6508 -43.1961 -0.0911 ? -0.0235 ? -0.0235 ? 0.0111  ? -0.0267 ? -0.0780 ? 0.4765 ? 
0.0627 ? -0.2336 ? 0.3272 ? -0.1142 ? 0.5404 ? -0.0402 ? -0.0406 ? 0.0297 ? 0.0260 ? 0.0720 ? -0.0250 ? -0.0370 ? 0.1400  ? 
-0.0318 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1531 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.05 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A GLU 27  ? A GLU 1   
2   1 Y 1 A GLU 28  ? A GLU 2   
3   1 Y 1 A ASN 29  ? A ASN 3   
4   1 Y 1 A PHE 30  ? A PHE 4   
5   1 Y 1 A SER 31  ? A SER 5   
6   1 Y 1 A GLN 41  ? A GLN 15  
7   1 Y 1 A ASN 42  ? A ASN 16  
8   1 Y 1 A VAL 100 ? A VAL 74  
9   1 Y 1 A GLN 101 ? A GLN 75  
10  1 Y 1 A HIS 102 ? A HIS 76  
11  1 Y 1 A GLN 103 ? A GLN 77  
12  1 Y 1 A ASN 104 ? A ASN 78  
13  1 Y 1 A GLY 105 ? A GLY 79  
14  1 Y 1 A ASN 106 ? A ASN 80  
15  1 Y 1 A PRO 107 ? A PRO 81  
16  1 Y 1 A GLY 108 ? A GLY 82  
17  1 Y 1 A ILE 109 ? A ILE 83  
18  1 Y 1 A GLN 110 ? A GLN 84  
19  1 Y 1 A SER 111 ? A SER 85  
20  1 Y 1 A ASN 112 ? A ASN 86  
21  1 Y 1 A VAL 434 ? A VAL 408 
22  1 Y 1 A LYS 435 ? A LYS 409 
23  1 Y 1 A ASP 436 ? A ASP 410 
24  1 Y 1 A THR 437 ? A THR 411 
25  1 Y 1 A ARG 438 ? A ARG 412 
26  1 Y 1 A GLN 439 ? A GLN 413 
27  1 Y 1 A SER 440 ? A SER 414 
28  1 Y 1 A TYR 441 ? A TYR 415 
29  1 Y 1 A ALA 442 ? A ALA 416 
30  1 Y 1 A ASN 443 ? A ASN 417 
31  1 Y 1 A SER 444 ? A SER 418 
32  1 Y 1 A SER 445 ? A SER 419 
33  1 Y 1 A SER 446 ? A SER 420 
34  1 Y 1 A PHE 447 ? A PHE 421 
35  1 Y 1 A GLN 448 ? A GLN 422 
36  1 Y 1 A ARG 449 ? A ARG 423 
37  1 Y 1 A HIS 450 ? A HIS 424 
38  1 Y 1 A ILE 451 ? A ILE 425 
39  1 Y 1 A ARG 452 ? A ARG 426 
40  1 Y 1 A LYS 453 ? A LYS 427 
41  1 Y 1 A ARG 454 ? A ARG 428 
42  1 Y 1 A ARG 455 ? A ARG 429 
43  1 Y 1 A SER 456 ? A SER 430 
44  1 Y 1 A THR 457 ? A THR 431 
45  1 Y 1 A ASP 458 ? A ASP 432 
46  1 Y 1 A LEU 819 ? A LEU 793 
47  1 Y 1 A THR 820 ? A THR 794 
48  1 Y 1 A THR 821 ? A THR 795 
49  1 Y 1 A CYS 822 ? A CYS 796 
50  1 Y 1 A VAL 823 ? A VAL 797 
51  1 Y 1 A SER 824 ? A SER 798 
52  1 Y 1 A ASP 825 ? A ASP 799 
53  1 Y 1 A VAL 826 ? A VAL 800 
54  1 Y 1 A THR 827 ? A THR 801 
55  1 Y 1 A GLU 828 ? A GLU 802 
56  1 Y 1 A PHE 829 ? A PHE 803 
57  1 Y 1 A LEU 830 ? A LEU 804 
58  1 Y 1 A VAL 831 ? A VAL 805 
59  1 Y 1 A PRO 832 ? A PRO 806 
60  1 Y 1 A ARG 833 ? A ARG 807 
61  1 Y 1 B GLU 27  ? B GLU 1   
62  1 Y 1 B GLU 28  ? B GLU 2   
63  1 Y 1 B ASN 29  ? B ASN 3   
64  1 Y 1 B PHE 30  ? B PHE 4   
65  1 Y 1 B SER 31  ? B SER 5   
66  1 Y 1 B GLN 41  ? B GLN 15  
67  1 Y 1 B ASN 42  ? B ASN 16  
68  1 Y 1 B VAL 100 ? B VAL 74  
69  1 Y 1 B GLN 101 ? B GLN 75  
70  1 Y 1 B HIS 102 ? B HIS 76  
71  1 Y 1 B GLN 103 ? B GLN 77  
72  1 Y 1 B ASN 104 ? B ASN 78  
73  1 Y 1 B GLY 105 ? B GLY 79  
74  1 Y 1 B ASN 106 ? B ASN 80  
75  1 Y 1 B PRO 107 ? B PRO 81  
76  1 Y 1 B GLY 108 ? B GLY 82  
77  1 Y 1 B ILE 109 ? B ILE 83  
78  1 Y 1 B GLN 110 ? B GLN 84  
79  1 Y 1 B SER 111 ? B SER 85  
80  1 Y 1 B ASN 112 ? B ASN 86  
81  1 Y 1 B VAL 434 ? B VAL 408 
82  1 Y 1 B LYS 435 ? B LYS 409 
83  1 Y 1 B ASP 436 ? B ASP 410 
84  1 Y 1 B THR 437 ? B THR 411 
85  1 Y 1 B ARG 438 ? B ARG 412 
86  1 Y 1 B GLN 439 ? B GLN 413 
87  1 Y 1 B SER 440 ? B SER 414 
88  1 Y 1 B TYR 441 ? B TYR 415 
89  1 Y 1 B ALA 442 ? B ALA 416 
90  1 Y 1 B ASN 443 ? B ASN 417 
91  1 Y 1 B SER 444 ? B SER 418 
92  1 Y 1 B SER 445 ? B SER 419 
93  1 Y 1 B SER 446 ? B SER 420 
94  1 Y 1 B PHE 447 ? B PHE 421 
95  1 Y 1 B GLN 448 ? B GLN 422 
96  1 Y 1 B ARG 449 ? B ARG 423 
97  1 Y 1 B HIS 450 ? B HIS 424 
98  1 Y 1 B ILE 451 ? B ILE 425 
99  1 Y 1 B ARG 452 ? B ARG 426 
100 1 Y 1 B LYS 453 ? B LYS 427 
101 1 Y 1 B ARG 454 ? B ARG 428 
102 1 Y 1 B ARG 455 ? B ARG 429 
103 1 Y 1 B SER 456 ? B SER 430 
104 1 Y 1 B THR 457 ? B THR 431 
105 1 Y 1 B ASP 458 ? B ASP 432 
106 1 Y 1 B LEU 819 ? B LEU 793 
107 1 Y 1 B THR 820 ? B THR 794 
108 1 Y 1 B THR 821 ? B THR 795 
109 1 Y 1 B CYS 822 ? B CYS 796 
110 1 Y 1 B VAL 823 ? B VAL 797 
111 1 Y 1 B SER 824 ? B SER 798 
112 1 Y 1 B ASP 825 ? B ASP 799 
113 1 Y 1 B VAL 826 ? B VAL 800 
114 1 Y 1 B THR 827 ? B THR 801 
115 1 Y 1 B GLU 828 ? B GLU 802 
116 1 Y 1 B PHE 829 ? B PHE 803 
117 1 Y 1 B LEU 830 ? B LEU 804 
118 1 Y 1 B VAL 831 ? B VAL 805 
119 1 Y 1 B PRO 832 ? B PRO 806 
120 1 Y 1 B ARG 833 ? B ARG 807 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BLN N1   N Y N 1   
A1BLN N3   N Y N 2   
A1BLN C4   C Y N 3   
A1BLN C5   C Y N 4   
A1BLN C6   C Y N 5   
A1BLN C7   C Y N 6   
A1BLN C8   C Y N 7   
A1BLN C10  C Y N 8   
A1BLN C13  C N N 9   
A1BLN C15  C N S 10  
A1BLN C17  C N N 11  
A1BLN C20  C N N 12  
A1BLN C21  C N N 13  
A1BLN C22  C N N 14  
A1BLN C24  C N S 15  
A1BLN C1   C Y N 16  
A1BLN C2   C Y N 17  
A1BLN C3   C Y N 18  
A1BLN C9   C Y N 19  
A1BLN C11  C Y N 20  
A1BLN C12  C N N 21  
A1BLN C14  C N R 22  
A1BLN C16  C N N 23  
A1BLN C18  C N N 24  
A1BLN C19  C N N 25  
A1BLN C23  C N N 26  
A1BLN N2   N Y N 27  
A1BLN N4   N Y N 28  
A1BLN N5   N N N 29  
A1BLN N6   N N N 30  
A1BLN N7   N N N 31  
A1BLN O1   O N N 32  
A1BLN O2   O N N 33  
A1BLN O3   O N N 34  
A1BLN O4   O N N 35  
A1BLN H4   H N N 36  
A1BLN H8   H N N 37  
A1BLN H7   H N N 38  
A1BLN H10  H N N 39  
A1BLN H14  H N N 40  
A1BLN H15  H N N 41  
A1BLN H16  H N N 42  
A1BLN H22  H N N 43  
A1BLN H21  H N N 44  
A1BLN H23  H N N 45  
A1BLN H24  H N N 46  
A1BLN H26  H N N 47  
A1BLN H25  H N N 48  
A1BLN H29  H N N 49  
A1BLN H1   H N N 50  
A1BLN H2   H N N 51  
A1BLN H3   H N N 52  
A1BLN H5   H N N 53  
A1BLN H6   H N N 54  
A1BLN H9   H N N 55  
A1BLN H11  H N N 56  
A1BLN H13  H N N 57  
A1BLN H12  H N N 58  
A1BLN H17  H N N 59  
A1BLN H18  H N N 60  
A1BLN H19  H N N 61  
A1BLN H20  H N N 62  
A1BLN H27  H N N 63  
A1BLN H28  H N N 64  
A1BLN H31  H N N 65  
A1BLN H30  H N N 66  
A1BLN H32  H N N 67  
A1BLN H33  H N N 68  
A1BLN H34  H N N 69  
A1BLN H35  H N N 70  
ALA   N    N N N 71  
ALA   CA   C N S 72  
ALA   C    C N N 73  
ALA   O    O N N 74  
ALA   CB   C N N 75  
ALA   OXT  O N N 76  
ALA   H    H N N 77  
ALA   H2   H N N 78  
ALA   HA   H N N 79  
ALA   HB1  H N N 80  
ALA   HB2  H N N 81  
ALA   HB3  H N N 82  
ALA   HXT  H N N 83  
ARG   N    N N N 84  
ARG   CA   C N S 85  
ARG   C    C N N 86  
ARG   O    O N N 87  
ARG   CB   C N N 88  
ARG   CG   C N N 89  
ARG   CD   C N N 90  
ARG   NE   N N N 91  
ARG   CZ   C N N 92  
ARG   NH1  N N N 93  
ARG   NH2  N N N 94  
ARG   OXT  O N N 95  
ARG   H    H N N 96  
ARG   H2   H N N 97  
ARG   HA   H N N 98  
ARG   HB2  H N N 99  
ARG   HB3  H N N 100 
ARG   HG2  H N N 101 
ARG   HG3  H N N 102 
ARG   HD2  H N N 103 
ARG   HD3  H N N 104 
ARG   HE   H N N 105 
ARG   HH11 H N N 106 
ARG   HH12 H N N 107 
ARG   HH21 H N N 108 
ARG   HH22 H N N 109 
ARG   HXT  H N N 110 
ASN   N    N N N 111 
ASN   CA   C N S 112 
ASN   C    C N N 113 
ASN   O    O N N 114 
ASN   CB   C N N 115 
ASN   CG   C N N 116 
ASN   OD1  O N N 117 
ASN   ND2  N N N 118 
ASN   OXT  O N N 119 
ASN   H    H N N 120 
ASN   H2   H N N 121 
ASN   HA   H N N 122 
ASN   HB2  H N N 123 
ASN   HB3  H N N 124 
ASN   HD21 H N N 125 
ASN   HD22 H N N 126 
ASN   HXT  H N N 127 
ASP   N    N N N 128 
ASP   CA   C N S 129 
ASP   C    C N N 130 
ASP   O    O N N 131 
ASP   CB   C N N 132 
ASP   CG   C N N 133 
ASP   OD1  O N N 134 
ASP   OD2  O N N 135 
ASP   OXT  O N N 136 
ASP   H    H N N 137 
ASP   H2   H N N 138 
ASP   HA   H N N 139 
ASP   HB2  H N N 140 
ASP   HB3  H N N 141 
ASP   HD2  H N N 142 
ASP   HXT  H N N 143 
BMA   C1   C N R 144 
BMA   C2   C N S 145 
BMA   C3   C N S 146 
BMA   C4   C N S 147 
BMA   C5   C N R 148 
BMA   C6   C N N 149 
BMA   O1   O N N 150 
BMA   O2   O N N 151 
BMA   O3   O N N 152 
BMA   O4   O N N 153 
BMA   O5   O N N 154 
BMA   O6   O N N 155 
BMA   H1   H N N 156 
BMA   H2   H N N 157 
BMA   H3   H N N 158 
BMA   H4   H N N 159 
BMA   H5   H N N 160 
BMA   H61  H N N 161 
BMA   H62  H N N 162 
BMA   HO1  H N N 163 
BMA   HO2  H N N 164 
BMA   HO3  H N N 165 
BMA   HO4  H N N 166 
BMA   HO6  H N N 167 
CYS   N    N N N 168 
CYS   CA   C N R 169 
CYS   C    C N N 170 
CYS   O    O N N 171 
CYS   CB   C N N 172 
CYS   SG   S N N 173 
CYS   OXT  O N N 174 
CYS   H    H N N 175 
CYS   H2   H N N 176 
CYS   HA   H N N 177 
CYS   HB2  H N N 178 
CYS   HB3  H N N 179 
CYS   HG   H N N 180 
CYS   HXT  H N N 181 
GLN   N    N N N 182 
GLN   CA   C N S 183 
GLN   C    C N N 184 
GLN   O    O N N 185 
GLN   CB   C N N 186 
GLN   CG   C N N 187 
GLN   CD   C N N 188 
GLN   OE1  O N N 189 
GLN   NE2  N N N 190 
GLN   OXT  O N N 191 
GLN   H    H N N 192 
GLN   H2   H N N 193 
GLN   HA   H N N 194 
GLN   HB2  H N N 195 
GLN   HB3  H N N 196 
GLN   HG2  H N N 197 
GLN   HG3  H N N 198 
GLN   HE21 H N N 199 
GLN   HE22 H N N 200 
GLN   HXT  H N N 201 
GLU   N    N N N 202 
GLU   CA   C N S 203 
GLU   C    C N N 204 
GLU   O    O N N 205 
GLU   CB   C N N 206 
GLU   CG   C N N 207 
GLU   CD   C N N 208 
GLU   OE1  O N N 209 
GLU   OE2  O N N 210 
GLU   OXT  O N N 211 
GLU   H    H N N 212 
GLU   H2   H N N 213 
GLU   HA   H N N 214 
GLU   HB2  H N N 215 
GLU   HB3  H N N 216 
GLU   HG2  H N N 217 
GLU   HG3  H N N 218 
GLU   HE2  H N N 219 
GLU   HXT  H N N 220 
GLY   N    N N N 221 
GLY   CA   C N N 222 
GLY   C    C N N 223 
GLY   O    O N N 224 
GLY   OXT  O N N 225 
GLY   H    H N N 226 
GLY   H2   H N N 227 
GLY   HA2  H N N 228 
GLY   HA3  H N N 229 
GLY   HXT  H N N 230 
HIS   N    N N N 231 
HIS   CA   C N S 232 
HIS   C    C N N 233 
HIS   O    O N N 234 
HIS   CB   C N N 235 
HIS   CG   C Y N 236 
HIS   ND1  N Y N 237 
HIS   CD2  C Y N 238 
HIS   CE1  C Y N 239 
HIS   NE2  N Y N 240 
HIS   OXT  O N N 241 
HIS   H    H N N 242 
HIS   H2   H N N 243 
HIS   HA   H N N 244 
HIS   HB2  H N N 245 
HIS   HB3  H N N 246 
HIS   HD1  H N N 247 
HIS   HD2  H N N 248 
HIS   HE1  H N N 249 
HIS   HE2  H N N 250 
HIS   HXT  H N N 251 
HOH   O    O N N 252 
HOH   H1   H N N 253 
HOH   H2   H N N 254 
ILE   N    N N N 255 
ILE   CA   C N S 256 
ILE   C    C N N 257 
ILE   O    O N N 258 
ILE   CB   C N S 259 
ILE   CG1  C N N 260 
ILE   CG2  C N N 261 
ILE   CD1  C N N 262 
ILE   OXT  O N N 263 
ILE   H    H N N 264 
ILE   H2   H N N 265 
ILE   HA   H N N 266 
ILE   HB   H N N 267 
ILE   HG12 H N N 268 
ILE   HG13 H N N 269 
ILE   HG21 H N N 270 
ILE   HG22 H N N 271 
ILE   HG23 H N N 272 
ILE   HD11 H N N 273 
ILE   HD12 H N N 274 
ILE   HD13 H N N 275 
ILE   HXT  H N N 276 
LEU   N    N N N 277 
LEU   CA   C N S 278 
LEU   C    C N N 279 
LEU   O    O N N 280 
LEU   CB   C N N 281 
LEU   CG   C N N 282 
LEU   CD1  C N N 283 
LEU   CD2  C N N 284 
LEU   OXT  O N N 285 
LEU   H    H N N 286 
LEU   H2   H N N 287 
LEU   HA   H N N 288 
LEU   HB2  H N N 289 
LEU   HB3  H N N 290 
LEU   HG   H N N 291 
LEU   HD11 H N N 292 
LEU   HD12 H N N 293 
LEU   HD13 H N N 294 
LEU   HD21 H N N 295 
LEU   HD22 H N N 296 
LEU   HD23 H N N 297 
LEU   HXT  H N N 298 
LYS   N    N N N 299 
LYS   CA   C N S 300 
LYS   C    C N N 301 
LYS   O    O N N 302 
LYS   CB   C N N 303 
LYS   CG   C N N 304 
LYS   CD   C N N 305 
LYS   CE   C N N 306 
LYS   NZ   N N N 307 
LYS   OXT  O N N 308 
LYS   H    H N N 309 
LYS   H2   H N N 310 
LYS   HA   H N N 311 
LYS   HB2  H N N 312 
LYS   HB3  H N N 313 
LYS   HG2  H N N 314 
LYS   HG3  H N N 315 
LYS   HD2  H N N 316 
LYS   HD3  H N N 317 
LYS   HE2  H N N 318 
LYS   HE3  H N N 319 
LYS   HZ1  H N N 320 
LYS   HZ2  H N N 321 
LYS   HZ3  H N N 322 
LYS   HXT  H N N 323 
MAN   C1   C N S 324 
MAN   C2   C N S 325 
MAN   C3   C N S 326 
MAN   C4   C N S 327 
MAN   C5   C N R 328 
MAN   C6   C N N 329 
MAN   O1   O N N 330 
MAN   O2   O N N 331 
MAN   O3   O N N 332 
MAN   O4   O N N 333 
MAN   O5   O N N 334 
MAN   O6   O N N 335 
MAN   H1   H N N 336 
MAN   H2   H N N 337 
MAN   H3   H N N 338 
MAN   H4   H N N 339 
MAN   H5   H N N 340 
MAN   H61  H N N 341 
MAN   H62  H N N 342 
MAN   HO1  H N N 343 
MAN   HO2  H N N 344 
MAN   HO3  H N N 345 
MAN   HO4  H N N 346 
MAN   HO6  H N N 347 
MET   N    N N N 348 
MET   CA   C N S 349 
MET   C    C N N 350 
MET   O    O N N 351 
MET   CB   C N N 352 
MET   CG   C N N 353 
MET   SD   S N N 354 
MET   CE   C N N 355 
MET   OXT  O N N 356 
MET   H    H N N 357 
MET   H2   H N N 358 
MET   HA   H N N 359 
MET   HB2  H N N 360 
MET   HB3  H N N 361 
MET   HG2  H N N 362 
MET   HG3  H N N 363 
MET   HE1  H N N 364 
MET   HE2  H N N 365 
MET   HE3  H N N 366 
MET   HXT  H N N 367 
NAG   C1   C N R 368 
NAG   C2   C N R 369 
NAG   C3   C N R 370 
NAG   C4   C N S 371 
NAG   C5   C N R 372 
NAG   C6   C N N 373 
NAG   C7   C N N 374 
NAG   C8   C N N 375 
NAG   N2   N N N 376 
NAG   O1   O N N 377 
NAG   O3   O N N 378 
NAG   O4   O N N 379 
NAG   O5   O N N 380 
NAG   O6   O N N 381 
NAG   O7   O N N 382 
NAG   H1   H N N 383 
NAG   H2   H N N 384 
NAG   H3   H N N 385 
NAG   H4   H N N 386 
NAG   H5   H N N 387 
NAG   H61  H N N 388 
NAG   H62  H N N 389 
NAG   H81  H N N 390 
NAG   H82  H N N 391 
NAG   H83  H N N 392 
NAG   HN2  H N N 393 
NAG   HO1  H N N 394 
NAG   HO3  H N N 395 
NAG   HO4  H N N 396 
NAG   HO6  H N N 397 
PHE   N    N N N 398 
PHE   CA   C N S 399 
PHE   C    C N N 400 
PHE   O    O N N 401 
PHE   CB   C N N 402 
PHE   CG   C Y N 403 
PHE   CD1  C Y N 404 
PHE   CD2  C Y N 405 
PHE   CE1  C Y N 406 
PHE   CE2  C Y N 407 
PHE   CZ   C Y N 408 
PHE   OXT  O N N 409 
PHE   H    H N N 410 
PHE   H2   H N N 411 
PHE   HA   H N N 412 
PHE   HB2  H N N 413 
PHE   HB3  H N N 414 
PHE   HD1  H N N 415 
PHE   HD2  H N N 416 
PHE   HE1  H N N 417 
PHE   HE2  H N N 418 
PHE   HZ   H N N 419 
PHE   HXT  H N N 420 
PRO   N    N N N 421 
PRO   CA   C N S 422 
PRO   C    C N N 423 
PRO   O    O N N 424 
PRO   CB   C N N 425 
PRO   CG   C N N 426 
PRO   CD   C N N 427 
PRO   OXT  O N N 428 
PRO   H    H N N 429 
PRO   HA   H N N 430 
PRO   HB2  H N N 431 
PRO   HB3  H N N 432 
PRO   HG2  H N N 433 
PRO   HG3  H N N 434 
PRO   HD2  H N N 435 
PRO   HD3  H N N 436 
PRO   HXT  H N N 437 
SER   N    N N N 438 
SER   CA   C N S 439 
SER   C    C N N 440 
SER   O    O N N 441 
SER   CB   C N N 442 
SER   OG   O N N 443 
SER   OXT  O N N 444 
SER   H    H N N 445 
SER   H2   H N N 446 
SER   HA   H N N 447 
SER   HB2  H N N 448 
SER   HB3  H N N 449 
SER   HG   H N N 450 
SER   HXT  H N N 451 
SO4   S    S N N 452 
SO4   O1   O N N 453 
SO4   O2   O N N 454 
SO4   O3   O N N 455 
SO4   O4   O N N 456 
THR   N    N N N 457 
THR   CA   C N S 458 
THR   C    C N N 459 
THR   O    O N N 460 
THR   CB   C N R 461 
THR   OG1  O N N 462 
THR   CG2  C N N 463 
THR   OXT  O N N 464 
THR   H    H N N 465 
THR   H2   H N N 466 
THR   HA   H N N 467 
THR   HB   H N N 468 
THR   HG1  H N N 469 
THR   HG21 H N N 470 
THR   HG22 H N N 471 
THR   HG23 H N N 472 
THR   HXT  H N N 473 
TRP   N    N N N 474 
TRP   CA   C N S 475 
TRP   C    C N N 476 
TRP   O    O N N 477 
TRP   CB   C N N 478 
TRP   CG   C Y N 479 
TRP   CD1  C Y N 480 
TRP   CD2  C Y N 481 
TRP   NE1  N Y N 482 
TRP   CE2  C Y N 483 
TRP   CE3  C Y N 484 
TRP   CZ2  C Y N 485 
TRP   CZ3  C Y N 486 
TRP   CH2  C Y N 487 
TRP   OXT  O N N 488 
TRP   H    H N N 489 
TRP   H2   H N N 490 
TRP   HA   H N N 491 
TRP   HB2  H N N 492 
TRP   HB3  H N N 493 
TRP   HD1  H N N 494 
TRP   HE1  H N N 495 
TRP   HE3  H N N 496 
TRP   HZ2  H N N 497 
TRP   HZ3  H N N 498 
TRP   HH2  H N N 499 
TRP   HXT  H N N 500 
TYR   N    N N N 501 
TYR   CA   C N S 502 
TYR   C    C N N 503 
TYR   O    O N N 504 
TYR   CB   C N N 505 
TYR   CG   C Y N 506 
TYR   CD1  C Y N 507 
TYR   CD2  C Y N 508 
TYR   CE1  C Y N 509 
TYR   CE2  C Y N 510 
TYR   CZ   C Y N 511 
TYR   OH   O N N 512 
TYR   OXT  O N N 513 
TYR   H    H N N 514 
TYR   H2   H N N 515 
TYR   HA   H N N 516 
TYR   HB2  H N N 517 
TYR   HB3  H N N 518 
TYR   HD1  H N N 519 
TYR   HD2  H N N 520 
TYR   HE1  H N N 521 
TYR   HE2  H N N 522 
TYR   HH   H N N 523 
TYR   HXT  H N N 524 
VAL   N    N N N 525 
VAL   CA   C N S 526 
VAL   C    C N N 527 
VAL   O    O N N 528 
VAL   CB   C N N 529 
VAL   CG1  C N N 530 
VAL   CG2  C N N 531 
VAL   OXT  O N N 532 
VAL   H    H N N 533 
VAL   H2   H N N 534 
VAL   HA   H N N 535 
VAL   HB   H N N 536 
VAL   HG11 H N N 537 
VAL   HG12 H N N 538 
VAL   HG13 H N N 539 
VAL   HG21 H N N 540 
VAL   HG22 H N N 541 
VAL   HG23 H N N 542 
VAL   HXT  H N N 543 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BLN O3  C23  sing N N 1   
A1BLN C23 C22  sing N N 2   
A1BLN C1  C2   doub Y N 3   
A1BLN C1  C5   sing Y N 4   
A1BLN C2  C9   sing Y N 5   
A1BLN C17 O4   sing N N 6   
A1BLN N7  C19  sing N N 7   
A1BLN N7  C14  sing N N 8   
A1BLN C22 C24  sing N N 9   
A1BLN C15 C13  sing N N 10  
A1BLN C15 C14  sing N N 11  
A1BLN C15 O2   sing N N 12  
A1BLN C13 O1   sing N N 13  
A1BLN C19 C5   sing N N 14  
A1BLN C5  C3   doub Y N 15  
A1BLN C12 C14  sing N N 16  
A1BLN C12 O1   sing N N 17  
A1BLN C9  O4   sing N N 18  
A1BLN C9  C6   doub Y N 19  
A1BLN C24 N6   sing N N 20  
A1BLN C24 C21  sing N N 21  
A1BLN C3  C6   sing Y N 22  
A1BLN C6  C18  sing N N 23  
A1BLN N6  C10  sing N N 24  
A1BLN C21 C20  sing N N 25  
A1BLN C20 C16  sing N N 26  
A1BLN C18 N4   sing N N 27  
A1BLN C10 N3   doub Y N 28  
A1BLN C10 C8   sing Y N 29  
A1BLN N3  C11  sing Y N 30  
A1BLN N4  C8   sing Y N 31  
A1BLN N4  N1   sing Y N 32  
A1BLN C8  C7   doub Y N 33  
A1BLN C11 N5   sing N N 34  
A1BLN C11 N2   doub Y N 35  
A1BLN N1  C4   doub Y N 36  
A1BLN C7  N2   sing Y N 37  
A1BLN C7  C4   sing Y N 38  
A1BLN C4  H4   sing N N 39  
A1BLN C13 H8   sing N N 40  
A1BLN C13 H7   sing N N 41  
A1BLN C15 H10  sing N N 42  
A1BLN C17 H14  sing N N 43  
A1BLN C17 H15  sing N N 44  
A1BLN C17 H16  sing N N 45  
A1BLN C20 H22  sing N N 46  
A1BLN C20 H21  sing N N 47  
A1BLN C21 H23  sing N N 48  
A1BLN C21 H24  sing N N 49  
A1BLN C22 H26  sing N N 50  
A1BLN C22 H25  sing N N 51  
A1BLN C24 H29  sing N N 52  
A1BLN C1  H1   sing N N 53  
A1BLN C2  H2   sing N N 54  
A1BLN C3  H3   sing N N 55  
A1BLN C12 H5   sing N N 56  
A1BLN C12 H6   sing N N 57  
A1BLN C14 H9   sing N N 58  
A1BLN C16 H11  sing N N 59  
A1BLN C16 H13  sing N N 60  
A1BLN C16 H12  sing N N 61  
A1BLN C18 H17  sing N N 62  
A1BLN C18 H18  sing N N 63  
A1BLN C19 H19  sing N N 64  
A1BLN C19 H20  sing N N 65  
A1BLN C23 H27  sing N N 66  
A1BLN C23 H28  sing N N 67  
A1BLN N5  H31  sing N N 68  
A1BLN N5  H30  sing N N 69  
A1BLN N6  H32  sing N N 70  
A1BLN N7  H33  sing N N 71  
A1BLN O2  H34  sing N N 72  
A1BLN O3  H35  sing N N 73  
ALA   N   CA   sing N N 74  
ALA   N   H    sing N N 75  
ALA   N   H2   sing N N 76  
ALA   CA  C    sing N N 77  
ALA   CA  CB   sing N N 78  
ALA   CA  HA   sing N N 79  
ALA   C   O    doub N N 80  
ALA   C   OXT  sing N N 81  
ALA   CB  HB1  sing N N 82  
ALA   CB  HB2  sing N N 83  
ALA   CB  HB3  sing N N 84  
ALA   OXT HXT  sing N N 85  
ARG   N   CA   sing N N 86  
ARG   N   H    sing N N 87  
ARG   N   H2   sing N N 88  
ARG   CA  C    sing N N 89  
ARG   CA  CB   sing N N 90  
ARG   CA  HA   sing N N 91  
ARG   C   O    doub N N 92  
ARG   C   OXT  sing N N 93  
ARG   CB  CG   sing N N 94  
ARG   CB  HB2  sing N N 95  
ARG   CB  HB3  sing N N 96  
ARG   CG  CD   sing N N 97  
ARG   CG  HG2  sing N N 98  
ARG   CG  HG3  sing N N 99  
ARG   CD  NE   sing N N 100 
ARG   CD  HD2  sing N N 101 
ARG   CD  HD3  sing N N 102 
ARG   NE  CZ   sing N N 103 
ARG   NE  HE   sing N N 104 
ARG   CZ  NH1  sing N N 105 
ARG   CZ  NH2  doub N N 106 
ARG   NH1 HH11 sing N N 107 
ARG   NH1 HH12 sing N N 108 
ARG   NH2 HH21 sing N N 109 
ARG   NH2 HH22 sing N N 110 
ARG   OXT HXT  sing N N 111 
ASN   N   CA   sing N N 112 
ASN   N   H    sing N N 113 
ASN   N   H2   sing N N 114 
ASN   CA  C    sing N N 115 
ASN   CA  CB   sing N N 116 
ASN   CA  HA   sing N N 117 
ASN   C   O    doub N N 118 
ASN   C   OXT  sing N N 119 
ASN   CB  CG   sing N N 120 
ASN   CB  HB2  sing N N 121 
ASN   CB  HB3  sing N N 122 
ASN   CG  OD1  doub N N 123 
ASN   CG  ND2  sing N N 124 
ASN   ND2 HD21 sing N N 125 
ASN   ND2 HD22 sing N N 126 
ASN   OXT HXT  sing N N 127 
ASP   N   CA   sing N N 128 
ASP   N   H    sing N N 129 
ASP   N   H2   sing N N 130 
ASP   CA  C    sing N N 131 
ASP   CA  CB   sing N N 132 
ASP   CA  HA   sing N N 133 
ASP   C   O    doub N N 134 
ASP   C   OXT  sing N N 135 
ASP   CB  CG   sing N N 136 
ASP   CB  HB2  sing N N 137 
ASP   CB  HB3  sing N N 138 
ASP   CG  OD1  doub N N 139 
ASP   CG  OD2  sing N N 140 
ASP   OD2 HD2  sing N N 141 
ASP   OXT HXT  sing N N 142 
BMA   C1  C2   sing N N 143 
BMA   C1  O1   sing N N 144 
BMA   C1  O5   sing N N 145 
BMA   C1  H1   sing N N 146 
BMA   C2  C3   sing N N 147 
BMA   C2  O2   sing N N 148 
BMA   C2  H2   sing N N 149 
BMA   C3  C4   sing N N 150 
BMA   C3  O3   sing N N 151 
BMA   C3  H3   sing N N 152 
BMA   C4  C5   sing N N 153 
BMA   C4  O4   sing N N 154 
BMA   C4  H4   sing N N 155 
BMA   C5  C6   sing N N 156 
BMA   C5  O5   sing N N 157 
BMA   C5  H5   sing N N 158 
BMA   C6  O6   sing N N 159 
BMA   C6  H61  sing N N 160 
BMA   C6  H62  sing N N 161 
BMA   O1  HO1  sing N N 162 
BMA   O2  HO2  sing N N 163 
BMA   O3  HO3  sing N N 164 
BMA   O4  HO4  sing N N 165 
BMA   O6  HO6  sing N N 166 
CYS   N   CA   sing N N 167 
CYS   N   H    sing N N 168 
CYS   N   H2   sing N N 169 
CYS   CA  C    sing N N 170 
CYS   CA  CB   sing N N 171 
CYS   CA  HA   sing N N 172 
CYS   C   O    doub N N 173 
CYS   C   OXT  sing N N 174 
CYS   CB  SG   sing N N 175 
CYS   CB  HB2  sing N N 176 
CYS   CB  HB3  sing N N 177 
CYS   SG  HG   sing N N 178 
CYS   OXT HXT  sing N N 179 
GLN   N   CA   sing N N 180 
GLN   N   H    sing N N 181 
GLN   N   H2   sing N N 182 
GLN   CA  C    sing N N 183 
GLN   CA  CB   sing N N 184 
GLN   CA  HA   sing N N 185 
GLN   C   O    doub N N 186 
GLN   C   OXT  sing N N 187 
GLN   CB  CG   sing N N 188 
GLN   CB  HB2  sing N N 189 
GLN   CB  HB3  sing N N 190 
GLN   CG  CD   sing N N 191 
GLN   CG  HG2  sing N N 192 
GLN   CG  HG3  sing N N 193 
GLN   CD  OE1  doub N N 194 
GLN   CD  NE2  sing N N 195 
GLN   NE2 HE21 sing N N 196 
GLN   NE2 HE22 sing N N 197 
GLN   OXT HXT  sing N N 198 
GLU   N   CA   sing N N 199 
GLU   N   H    sing N N 200 
GLU   N   H2   sing N N 201 
GLU   CA  C    sing N N 202 
GLU   CA  CB   sing N N 203 
GLU   CA  HA   sing N N 204 
GLU   C   O    doub N N 205 
GLU   C   OXT  sing N N 206 
GLU   CB  CG   sing N N 207 
GLU   CB  HB2  sing N N 208 
GLU   CB  HB3  sing N N 209 
GLU   CG  CD   sing N N 210 
GLU   CG  HG2  sing N N 211 
GLU   CG  HG3  sing N N 212 
GLU   CD  OE1  doub N N 213 
GLU   CD  OE2  sing N N 214 
GLU   OE2 HE2  sing N N 215 
GLU   OXT HXT  sing N N 216 
GLY   N   CA   sing N N 217 
GLY   N   H    sing N N 218 
GLY   N   H2   sing N N 219 
GLY   CA  C    sing N N 220 
GLY   CA  HA2  sing N N 221 
GLY   CA  HA3  sing N N 222 
GLY   C   O    doub N N 223 
GLY   C   OXT  sing N N 224 
GLY   OXT HXT  sing N N 225 
HIS   N   CA   sing N N 226 
HIS   N   H    sing N N 227 
HIS   N   H2   sing N N 228 
HIS   CA  C    sing N N 229 
HIS   CA  CB   sing N N 230 
HIS   CA  HA   sing N N 231 
HIS   C   O    doub N N 232 
HIS   C   OXT  sing N N 233 
HIS   CB  CG   sing N N 234 
HIS   CB  HB2  sing N N 235 
HIS   CB  HB3  sing N N 236 
HIS   CG  ND1  sing Y N 237 
HIS   CG  CD2  doub Y N 238 
HIS   ND1 CE1  doub Y N 239 
HIS   ND1 HD1  sing N N 240 
HIS   CD2 NE2  sing Y N 241 
HIS   CD2 HD2  sing N N 242 
HIS   CE1 NE2  sing Y N 243 
HIS   CE1 HE1  sing N N 244 
HIS   NE2 HE2  sing N N 245 
HIS   OXT HXT  sing N N 246 
HOH   O   H1   sing N N 247 
HOH   O   H2   sing N N 248 
ILE   N   CA   sing N N 249 
ILE   N   H    sing N N 250 
ILE   N   H2   sing N N 251 
ILE   CA  C    sing N N 252 
ILE   CA  CB   sing N N 253 
ILE   CA  HA   sing N N 254 
ILE   C   O    doub N N 255 
ILE   C   OXT  sing N N 256 
ILE   CB  CG1  sing N N 257 
ILE   CB  CG2  sing N N 258 
ILE   CB  HB   sing N N 259 
ILE   CG1 CD1  sing N N 260 
ILE   CG1 HG12 sing N N 261 
ILE   CG1 HG13 sing N N 262 
ILE   CG2 HG21 sing N N 263 
ILE   CG2 HG22 sing N N 264 
ILE   CG2 HG23 sing N N 265 
ILE   CD1 HD11 sing N N 266 
ILE   CD1 HD12 sing N N 267 
ILE   CD1 HD13 sing N N 268 
ILE   OXT HXT  sing N N 269 
LEU   N   CA   sing N N 270 
LEU   N   H    sing N N 271 
LEU   N   H2   sing N N 272 
LEU   CA  C    sing N N 273 
LEU   CA  CB   sing N N 274 
LEU   CA  HA   sing N N 275 
LEU   C   O    doub N N 276 
LEU   C   OXT  sing N N 277 
LEU   CB  CG   sing N N 278 
LEU   CB  HB2  sing N N 279 
LEU   CB  HB3  sing N N 280 
LEU   CG  CD1  sing N N 281 
LEU   CG  CD2  sing N N 282 
LEU   CG  HG   sing N N 283 
LEU   CD1 HD11 sing N N 284 
LEU   CD1 HD12 sing N N 285 
LEU   CD1 HD13 sing N N 286 
LEU   CD2 HD21 sing N N 287 
LEU   CD2 HD22 sing N N 288 
LEU   CD2 HD23 sing N N 289 
LEU   OXT HXT  sing N N 290 
LYS   N   CA   sing N N 291 
LYS   N   H    sing N N 292 
LYS   N   H2   sing N N 293 
LYS   CA  C    sing N N 294 
LYS   CA  CB   sing N N 295 
LYS   CA  HA   sing N N 296 
LYS   C   O    doub N N 297 
LYS   C   OXT  sing N N 298 
LYS   CB  CG   sing N N 299 
LYS   CB  HB2  sing N N 300 
LYS   CB  HB3  sing N N 301 
LYS   CG  CD   sing N N 302 
LYS   CG  HG2  sing N N 303 
LYS   CG  HG3  sing N N 304 
LYS   CD  CE   sing N N 305 
LYS   CD  HD2  sing N N 306 
LYS   CD  HD3  sing N N 307 
LYS   CE  NZ   sing N N 308 
LYS   CE  HE2  sing N N 309 
LYS   CE  HE3  sing N N 310 
LYS   NZ  HZ1  sing N N 311 
LYS   NZ  HZ2  sing N N 312 
LYS   NZ  HZ3  sing N N 313 
LYS   OXT HXT  sing N N 314 
MAN   C1  C2   sing N N 315 
MAN   C1  O1   sing N N 316 
MAN   C1  O5   sing N N 317 
MAN   C1  H1   sing N N 318 
MAN   C2  C3   sing N N 319 
MAN   C2  O2   sing N N 320 
MAN   C2  H2   sing N N 321 
MAN   C3  C4   sing N N 322 
MAN   C3  O3   sing N N 323 
MAN   C3  H3   sing N N 324 
MAN   C4  C5   sing N N 325 
MAN   C4  O4   sing N N 326 
MAN   C4  H4   sing N N 327 
MAN   C5  C6   sing N N 328 
MAN   C5  O5   sing N N 329 
MAN   C5  H5   sing N N 330 
MAN   C6  O6   sing N N 331 
MAN   C6  H61  sing N N 332 
MAN   C6  H62  sing N N 333 
MAN   O1  HO1  sing N N 334 
MAN   O2  HO2  sing N N 335 
MAN   O3  HO3  sing N N 336 
MAN   O4  HO4  sing N N 337 
MAN   O6  HO6  sing N N 338 
MET   N   CA   sing N N 339 
MET   N   H    sing N N 340 
MET   N   H2   sing N N 341 
MET   CA  C    sing N N 342 
MET   CA  CB   sing N N 343 
MET   CA  HA   sing N N 344 
MET   C   O    doub N N 345 
MET   C   OXT  sing N N 346 
MET   CB  CG   sing N N 347 
MET   CB  HB2  sing N N 348 
MET   CB  HB3  sing N N 349 
MET   CG  SD   sing N N 350 
MET   CG  HG2  sing N N 351 
MET   CG  HG3  sing N N 352 
MET   SD  CE   sing N N 353 
MET   CE  HE1  sing N N 354 
MET   CE  HE2  sing N N 355 
MET   CE  HE3  sing N N 356 
MET   OXT HXT  sing N N 357 
NAG   C1  C2   sing N N 358 
NAG   C1  O1   sing N N 359 
NAG   C1  O5   sing N N 360 
NAG   C1  H1   sing N N 361 
NAG   C2  C3   sing N N 362 
NAG   C2  N2   sing N N 363 
NAG   C2  H2   sing N N 364 
NAG   C3  C4   sing N N 365 
NAG   C3  O3   sing N N 366 
NAG   C3  H3   sing N N 367 
NAG   C4  C5   sing N N 368 
NAG   C4  O4   sing N N 369 
NAG   C4  H4   sing N N 370 
NAG   C5  C6   sing N N 371 
NAG   C5  O5   sing N N 372 
NAG   C5  H5   sing N N 373 
NAG   C6  O6   sing N N 374 
NAG   C6  H61  sing N N 375 
NAG   C6  H62  sing N N 376 
NAG   C7  C8   sing N N 377 
NAG   C7  N2   sing N N 378 
NAG   C7  O7   doub N N 379 
NAG   C8  H81  sing N N 380 
NAG   C8  H82  sing N N 381 
NAG   C8  H83  sing N N 382 
NAG   N2  HN2  sing N N 383 
NAG   O1  HO1  sing N N 384 
NAG   O3  HO3  sing N N 385 
NAG   O4  HO4  sing N N 386 
NAG   O6  HO6  sing N N 387 
PHE   N   CA   sing N N 388 
PHE   N   H    sing N N 389 
PHE   N   H2   sing N N 390 
PHE   CA  C    sing N N 391 
PHE   CA  CB   sing N N 392 
PHE   CA  HA   sing N N 393 
PHE   C   O    doub N N 394 
PHE   C   OXT  sing N N 395 
PHE   CB  CG   sing N N 396 
PHE   CB  HB2  sing N N 397 
PHE   CB  HB3  sing N N 398 
PHE   CG  CD1  doub Y N 399 
PHE   CG  CD2  sing Y N 400 
PHE   CD1 CE1  sing Y N 401 
PHE   CD1 HD1  sing N N 402 
PHE   CD2 CE2  doub Y N 403 
PHE   CD2 HD2  sing N N 404 
PHE   CE1 CZ   doub Y N 405 
PHE   CE1 HE1  sing N N 406 
PHE   CE2 CZ   sing Y N 407 
PHE   CE2 HE2  sing N N 408 
PHE   CZ  HZ   sing N N 409 
PHE   OXT HXT  sing N N 410 
PRO   N   CA   sing N N 411 
PRO   N   CD   sing N N 412 
PRO   N   H    sing N N 413 
PRO   CA  C    sing N N 414 
PRO   CA  CB   sing N N 415 
PRO   CA  HA   sing N N 416 
PRO   C   O    doub N N 417 
PRO   C   OXT  sing N N 418 
PRO   CB  CG   sing N N 419 
PRO   CB  HB2  sing N N 420 
PRO   CB  HB3  sing N N 421 
PRO   CG  CD   sing N N 422 
PRO   CG  HG2  sing N N 423 
PRO   CG  HG3  sing N N 424 
PRO   CD  HD2  sing N N 425 
PRO   CD  HD3  sing N N 426 
PRO   OXT HXT  sing N N 427 
SER   N   CA   sing N N 428 
SER   N   H    sing N N 429 
SER   N   H2   sing N N 430 
SER   CA  C    sing N N 431 
SER   CA  CB   sing N N 432 
SER   CA  HA   sing N N 433 
SER   C   O    doub N N 434 
SER   C   OXT  sing N N 435 
SER   CB  OG   sing N N 436 
SER   CB  HB2  sing N N 437 
SER   CB  HB3  sing N N 438 
SER   OG  HG   sing N N 439 
SER   OXT HXT  sing N N 440 
SO4   S   O1   doub N N 441 
SO4   S   O2   doub N N 442 
SO4   S   O3   sing N N 443 
SO4   S   O4   sing N N 444 
THR   N   CA   sing N N 445 
THR   N   H    sing N N 446 
THR   N   H2   sing N N 447 
THR   CA  C    sing N N 448 
THR   CA  CB   sing N N 449 
THR   CA  HA   sing N N 450 
THR   C   O    doub N N 451 
THR   C   OXT  sing N N 452 
THR   CB  OG1  sing N N 453 
THR   CB  CG2  sing N N 454 
THR   CB  HB   sing N N 455 
THR   OG1 HG1  sing N N 456 
THR   CG2 HG21 sing N N 457 
THR   CG2 HG22 sing N N 458 
THR   CG2 HG23 sing N N 459 
THR   OXT HXT  sing N N 460 
TRP   N   CA   sing N N 461 
TRP   N   H    sing N N 462 
TRP   N   H2   sing N N 463 
TRP   CA  C    sing N N 464 
TRP   CA  CB   sing N N 465 
TRP   CA  HA   sing N N 466 
TRP   C   O    doub N N 467 
TRP   C   OXT  sing N N 468 
TRP   CB  CG   sing N N 469 
TRP   CB  HB2  sing N N 470 
TRP   CB  HB3  sing N N 471 
TRP   CG  CD1  doub Y N 472 
TRP   CG  CD2  sing Y N 473 
TRP   CD1 NE1  sing Y N 474 
TRP   CD1 HD1  sing N N 475 
TRP   CD2 CE2  doub Y N 476 
TRP   CD2 CE3  sing Y N 477 
TRP   NE1 CE2  sing Y N 478 
TRP   NE1 HE1  sing N N 479 
TRP   CE2 CZ2  sing Y N 480 
TRP   CE3 CZ3  doub Y N 481 
TRP   CE3 HE3  sing N N 482 
TRP   CZ2 CH2  doub Y N 483 
TRP   CZ2 HZ2  sing N N 484 
TRP   CZ3 CH2  sing Y N 485 
TRP   CZ3 HZ3  sing N N 486 
TRP   CH2 HH2  sing N N 487 
TRP   OXT HXT  sing N N 488 
TYR   N   CA   sing N N 489 
TYR   N   H    sing N N 490 
TYR   N   H2   sing N N 491 
TYR   CA  C    sing N N 492 
TYR   CA  CB   sing N N 493 
TYR   CA  HA   sing N N 494 
TYR   C   O    doub N N 495 
TYR   C   OXT  sing N N 496 
TYR   CB  CG   sing N N 497 
TYR   CB  HB2  sing N N 498 
TYR   CB  HB3  sing N N 499 
TYR   CG  CD1  doub Y N 500 
TYR   CG  CD2  sing Y N 501 
TYR   CD1 CE1  sing Y N 502 
TYR   CD1 HD1  sing N N 503 
TYR   CD2 CE2  doub Y N 504 
TYR   CD2 HD2  sing N N 505 
TYR   CE1 CZ   doub Y N 506 
TYR   CE1 HE1  sing N N 507 
TYR   CE2 CZ   sing Y N 508 
TYR   CE2 HE2  sing N N 509 
TYR   CZ  OH   sing N N 510 
TYR   OH  HH   sing N N 511 
TYR   OXT HXT  sing N N 512 
VAL   N   CA   sing N N 513 
VAL   N   H    sing N N 514 
VAL   N   H2   sing N N 515 
VAL   CA  C    sing N N 516 
VAL   CA  CB   sing N N 517 
VAL   CA  HA   sing N N 518 
VAL   C   O    doub N N 519 
VAL   C   OXT  sing N N 520 
VAL   CB  CG1  sing N N 521 
VAL   CB  CG2  sing N N 522 
VAL   CB  HB   sing N N 523 
VAL   CG1 HG11 sing N N 524 
VAL   CG1 HG12 sing N N 525 
VAL   CG1 HG13 sing N N 526 
VAL   CG2 HG21 sing N N 527 
VAL   CG2 HG22 sing N N 528 
VAL   CG2 HG23 sing N N 529 
VAL   OXT HXT  sing N N 530 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 BMA 3 n 
2 MAN 4 n 
2 MAN 5 n 
3 NAG 1 n 
3 NAG 2 n 
3 BMA 3 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3w3j 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MHY 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.013778 
_atom_sites.fract_transf_matrix[1][2]   0.002103 
_atom_sites.fract_transf_matrix[1][3]   0.003229 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012275 
_atom_sites.fract_transf_matrix[2][3]   0.006518 
_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]   0.013693 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N    . ARG   A  1 6   ? 19.556 39.509  -30.206 1.00 39.83  ? 32   ARG   A N    1 
ATOM   2     C CA   . ARG   A  1 6   ? 20.414 38.332  -30.380 1.00 40.18  ? 32   ARG   A CA   1 
ATOM   3     C C    . ARG   A  1 6   ? 20.848 37.778  -29.005 1.00 40.18  ? 32   ARG   A C    1 
ATOM   4     O O    . ARG   A  1 6   ? 21.611 38.424  -28.295 1.00 40.06  ? 32   ARG   A O    1 
ATOM   5     C CB   . ARG   A  1 6   ? 21.638 38.713  -31.242 1.00 40.98  ? 32   ARG   A CB   1 
ATOM   6     C CG   . ARG   A  1 6   ? 22.287 37.561  -31.996 1.00 41.67  ? 32   ARG   A CG   1 
ATOM   7     C CD   . ARG   A  1 6   ? 23.402 38.071  -32.902 1.00 42.10  ? 32   ARG   A CD   1 
ATOM   8     N NE   . ARG   A  1 6   ? 22.938 38.440  -34.241 1.00 42.24  ? 32   ARG   A NE   1 
ATOM   9     C CZ   . ARG   A  1 6   ? 22.724 37.586  -35.241 1.00 42.31  ? 32   ARG   A CZ   1 
ATOM   10    N NH1  . ARG   A  1 6   ? 22.891 36.281  -35.059 1.00 41.31  ? 32   ARG   A NH1  1 
ATOM   11    N NH2  . ARG   A  1 6   ? 22.319 38.030  -36.425 1.00 40.88  ? 32   ARG   A NH2  1 
ATOM   12    H HA   . ARG   A  1 6   ? 19.842 37.564  -30.900 0.00 57.99  ? 32   ARG   A HA   1 
ATOM   13    H HB2  . ARG   A  1 6   ? 21.316 39.443  -31.983 0.00 59.70  ? 32   ARG   A HB2  1 
ATOM   14    H HB3  . ARG   A  1 6   ? 22.399 39.162  -30.605 0.00 59.19  ? 32   ARG   A HB3  1 
ATOM   15    H HG2  . ARG   A  1 6   ? 22.716 36.858  -31.284 0.00 58.34  ? 32   ARG   A HG2  1 
ATOM   16    H HG3  . ARG   A  1 6   ? 21.538 37.067  -32.613 0.00 58.82  ? 32   ARG   A HG3  1 
ATOM   17    H HD2  . ARG   A  1 6   ? 23.821 38.971  -32.455 0.00 59.90  ? 32   ARG   A HD2  1 
ATOM   18    H HD3  . ARG   A  1 6   ? 24.189 37.325  -32.993 0.00 58.67  ? 32   ARG   A HD3  1 
ATOM   19    H HE   . ARG   A  1 6   ? 22.808 39.430  -34.426 0.00 60.67  ? 32   ARG   A HE   1 
ATOM   20    H HH11 . ARG   A  1 6   ? 23.187 35.885  -34.173 0.00 57.09  ? 32   ARG   A HH11 1 
ATOM   21    H HH12 . ARG   A  1 6   ? 22.708 35.646  -35.829 0.00 57.11  ? 32   ARG   A HH12 1 
ATOM   22    H HH21 . ARG   A  1 6   ? 22.183 39.023  -36.580 0.00 59.01  ? 32   ARG   A HH21 1 
ATOM   23    H HH22 . ARG   A  1 6   ? 22.142 37.379  -37.183 0.00 57.94  ? 32   ARG   A HH22 1 
ATOM   24    N N    . SER   A  1 7   ? 20.340 36.595  -28.628 1.00 40.16  ? 33   SER   A N    1 
ATOM   25    C CA   . SER   A  1 7   ? 20.631 35.970  -27.331 1.00 40.52  ? 33   SER   A CA   1 
ATOM   26    C C    . SER   A  1 7   ? 22.129 35.811  -27.055 1.00 39.96  ? 33   SER   A C    1 
ATOM   27    O O    . SER   A  1 7   ? 22.878 35.397  -27.943 1.00 39.94  ? 33   SER   A O    1 
ATOM   28    C CB   . SER   A  1 7   ? 19.968 34.597  -27.251 1.00 42.71  ? 33   SER   A CB   1 
ATOM   29    O OG   . SER   A  1 7   ? 20.255 33.957  -26.016 1.00 46.23  ? 33   SER   A OG   1 
ATOM   30    H H    . SER   A  1 7   ? 19.709 36.046  -29.203 0.00 57.01  ? 33   SER   A H    1 
ATOM   31    H HA   . SER   A  1 7   ? 20.200 36.591  -26.547 0.00 57.89  ? 33   SER   A HA   1 
ATOM   32    H HB2  . SER   A  1 7   ? 18.890 34.721  -27.340 0.00 59.72  ? 33   SER   A HB2  1 
ATOM   33    H HB3  . SER   A  1 7   ? 20.338 33.992  -28.079 0.00 58.70  ? 33   SER   A HB3  1 
ATOM   34    H HG   . SER   A  1 7   ? 20.387 32.980  -26.134 0.00 62.47  ? 33   SER   A HG   1 
ATOM   35    N N    . TYR   A  1 8   ? 22.553 36.110  -25.812 1.00 39.14  ? 34   TYR   A N    1 
ATOM   36    C CA   . TYR   A  1 8   ? 23.948 35.981  -25.385 1.00 39.13  ? 34   TYR   A CA   1 
ATOM   37    C C    . TYR   A  1 8   ? 23.996 35.789  -23.858 1.00 38.79  ? 34   TYR   A C    1 
ATOM   38    O O    . TYR   A  1 8   ? 23.307 36.536  -23.162 1.00 38.53  ? 34   TYR   A O    1 
ATOM   39    C CB   . TYR   A  1 8   ? 24.750 37.243  -25.759 1.00 39.24  ? 34   TYR   A CB   1 
ATOM   40    C CG   . TYR   A  1 8   ? 26.208 37.129  -25.379 1.00 40.37  ? 34   TYR   A CG   1 
ATOM   41    C CD1  . TYR   A  1 8   ? 27.113 36.490  -26.211 1.00 41.13  ? 34   TYR   A CD1  1 
ATOM   42    C CD2  . TYR   A  1 8   ? 26.655 37.538  -24.129 1.00 41.45  ? 34   TYR   A CD2  1 
ATOM   43    C CE1  . TYR   A  1 8   ? 28.442 36.326  -25.844 1.00 42.08  ? 34   TYR   A CE1  1 
ATOM   44    C CE2  . TYR   A  1 8   ? 27.972 37.335  -23.730 1.00 42.43  ? 34   TYR   A CE2  1 
ATOM   45    C CZ   . TYR   A  1 8   ? 28.863 36.726  -24.593 1.00 43.40  ? 34   TYR   A CZ   1 
ATOM   46    O OH   . TYR   A  1 8   ? 30.180 36.540  -24.238 1.00 45.54  ? 34   TYR   A OH   1 
ATOM   47    H H    . TYR   A  1 8   ? 21.940 36.455  -25.080 0.00 55.71  ? 34   TYR   A H    1 
ATOM   48    H HA   . TYR   A  1 8   ? 24.390 35.122  -25.886 0.00 54.06  ? 34   TYR   A HA   1 
ATOM   49    H HB2  . TYR   A  1 8   ? 24.693 37.395  -26.836 0.00 55.48  ? 34   TYR   A HB2  1 
ATOM   50    H HB3  . TYR   A  1 8   ? 24.329 38.100  -25.236 0.00 56.23  ? 34   TYR   A HB3  1 
ATOM   51    H HD1  . TYR   A  1 8   ? 26.786 36.155  -27.180 0.00 56.39  ? 34   TYR   A HD1  1 
ATOM   52    H HD2  . TYR   A  1 8   ? 25.959 37.985  -23.440 0.00 58.64  ? 34   TYR   A HD2  1 
ATOM   53    H HE1  . TYR   A  1 8   ? 29.130 35.841  -26.515 0.00 56.91  ? 34   TYR   A HE1  1 
ATOM   54    H HE2  . TYR   A  1 8   ? 28.294 37.680  -22.762 0.00 59.22  ? 34   TYR   A HE2  1 
ATOM   55    H HH   . TYR   A  1 8   ? 30.342 36.848  -23.308 0.00 61.94  ? 34   TYR   A HH   1 
ATOM   56    N N    . PRO   A  1 9   ? 24.816 34.862  -23.292 1.00 38.36  ? 35   PRO   A N    1 
ATOM   57    C CA   . PRO   A  1 9   ? 25.754 33.929  -23.945 1.00 38.15  ? 35   PRO   A CA   1 
ATOM   58    C C    . PRO   A  1 9   ? 25.162 32.619  -24.454 1.00 38.64  ? 35   PRO   A C    1 
ATOM   59    O O    . PRO   A  1 9   ? 25.901 31.840  -25.049 1.00 38.85  ? 35   PRO   A O    1 
ATOM   60    C CB   . PRO   A  1 9   ? 26.787 33.676  -22.841 1.00 38.61  ? 35   PRO   A CB   1 
ATOM   61    C CG   . PRO   A  1 9   ? 25.983 33.719  -21.582 1.00 39.13  ? 35   PRO   A CG   1 
ATOM   62    C CD   . PRO   A  1 9   ? 24.875 34.725  -21.822 1.00 37.59  ? 35   PRO   A CD   1 
ATOM   63    H HA   . PRO   A  1 9   ? 26.270 34.423  -24.766 0.00 52.10  ? 35   PRO   A HA   1 
ATOM   64    H HB2  . PRO   A  1 9   ? 27.252 32.700  -22.969 0.00 51.65  ? 35   PRO   A HB2  1 
ATOM   65    H HB3  . PRO   A  1 9   ? 27.535 34.466  -22.849 0.00 52.67  ? 35   PRO   A HB3  1 
ATOM   66    H HG2  . PRO   A  1 9   ? 25.567 32.733  -21.382 0.00 52.89  ? 35   PRO   A HG2  1 
ATOM   67    H HG3  . PRO   A  1 9   ? 26.618 34.040  -20.757 0.00 53.56  ? 35   PRO   A HG3  1 
ATOM   68    H HD2  . PRO   A  1 9   ? 23.929 34.341  -21.441 0.00 52.39  ? 35   PRO   A HD2  1 
ATOM   69    H HD3  . PRO   A  1 9   ? 25.128 35.679  -21.363 0.00 52.96  ? 35   PRO   A HD3  1 
ATOM   70    N N    . CYS   A  1 10  ? 23.862 32.364  -24.246 1.00 38.79  ? 36   CYS   A N    1 
ATOM   71    C CA   . CYS   A  1 10  ? 23.231 31.108  -24.661 1.00 39.99  ? 36   CYS   A CA   1 
ATOM   72    C C    . CYS   A  1 10  ? 22.651 31.199  -26.078 1.00 42.11  ? 36   CYS   A C    1 
ATOM   73    O O    . CYS   A  1 10  ? 22.378 32.293  -26.570 1.00 41.64  ? 36   CYS   A O    1 
ATOM   74    C CB   . CYS   A  1 10  ? 22.152 30.689  -23.660 1.00 39.77  ? 36   CYS   A CB   1 
ATOM   75    S SG   . CYS   A  1 10  ? 22.523 31.080  -21.926 1.00 40.12  ? 36   CYS   A SG   1 
ATOM   76    H H    . CYS   A  1 10  ? 23.208 32.997  -23.796 0.00 52.89  ? 36   CYS   A H    1 
ATOM   77    H HA   . CYS   A  1 10  ? 23.973 30.312  -24.664 0.00 52.49  ? 36   CYS   A HA   1 
ATOM   78    H HB2  . CYS   A  1 10  ? 21.224 31.196  -23.919 0.00 53.56  ? 36   CYS   A HB2  1 
ATOM   79    H HB3  . CYS   A  1 10  ? 22.012 29.612  -23.731 0.00 52.47  ? 36   CYS   A HB3  1 
ATOM   80    N N    . ASP   A  1 11  ? 22.435 30.031  -26.713 1.00 44.13  ? 37   ASP   A N    1 
ATOM   81    C CA   . ASP   A  1 11  ? 21.811 29.911  -28.037 1.00 46.50  ? 37   ASP   A CA   1 
ATOM   82    C C    . ASP   A  1 11  ? 20.383 29.392  -27.792 1.00 48.76  ? 37   ASP   A C    1 
ATOM   83    O O    . ASP   A  1 11  ? 20.231 28.336  -27.192 1.00 48.78  ? 37   ASP   A O    1 
ATOM   84    C CB   . ASP   A  1 11  ? 22.601 28.931  -28.927 1.00 47.97  ? 37   ASP   A CB   1 
ATOM   85    C CG   . ASP   A  1 11  ? 23.970 29.437  -29.348 1.00 52.54  ? 37   ASP   A CG   1 
ATOM   86    O OD1  . ASP   A  1 11  ? 24.030 30.461  -30.061 1.00 53.21  ? 37   ASP   A OD1  1 
ATOM   87    O OD2  . ASP   A  1 11  ? 24.980 28.800  -28.977 1.00 55.09  ? 37   ASP   A OD2  1 
ATOM   88    H H    . ASP   A  1 11  ? 22.688 29.132  -26.315 0.00 57.01  ? 37   ASP   A H    1 
ATOM   89    H HA   . ASP   A  1 11  ? 21.764 30.874  -28.543 0.00 60.92  ? 37   ASP   A HA   1 
ATOM   90    H HB2  . ASP   A  1 11  ? 22.745 27.997  -28.385 0.00 60.88  ? 37   ASP   A HB2  1 
ATOM   91    H HB3  . ASP   A  1 11  ? 22.027 28.743  -29.833 0.00 61.41  ? 37   ASP   A HB3  1 
ATOM   92    N N    . GLU   A  1 12  ? 19.348 30.119  -28.236 1.00 50.62  ? 38   GLU   A N    1 
ATOM   93    C CA   . GLU   A  1 12  ? 17.954 29.723  -27.985 1.00 52.95  ? 38   GLU   A CA   1 
ATOM   94    C C    . GLU   A  1 12  ? 17.270 28.949  -29.130 1.00 55.72  ? 38   GLU   A C    1 
ATOM   95    O O    . GLU   A  1 12  ? 17.050 29.518  -30.196 1.00 56.13  ? 38   GLU   A O    1 
ATOM   96    C CB   . GLU   A  1 12  ? 17.119 30.964  -27.658 1.00 54.69  ? 38   GLU   A CB   1 
ATOM   97    C CG   . GLU   A  1 12  ? 17.504 31.633  -26.347 1.00 58.58  ? 38   GLU   A CG   1 
ATOM   98    C CD   . GLU   A  1 12  ? 16.782 32.935  -26.059 1.00 64.01  ? 38   GLU   A CD   1 
ATOM   99    O OE1  . GLU   A  1 12  ? 16.183 33.508  -26.997 1.00 65.10  ? 38   GLU   A OE1  1 
ATOM   100   O OE2  . GLU   A  1 12  ? 16.833 33.393  -24.895 1.00 65.57  ? 38   GLU   A OE2  1 
ATOM   101   H H    . GLU   A  1 12  ? 19.442 30.963  -28.791 0.00 66.62  ? 38   GLU   A H    1 
ATOM   102   H HA   . GLU   A  1 12  ? 17.916 29.086  -27.102 0.00 69.02  ? 38   GLU   A HA   1 
ATOM   103   H HB2  . GLU   A  1 12  ? 17.247 31.686  -28.463 0.00 72.72  ? 38   GLU   A HB2  1 
ATOM   104   H HB3  . GLU   A  1 12  ? 16.072 30.673  -27.586 0.00 72.63  ? 38   GLU   A HB3  1 
ATOM   105   H HG2  . GLU   A  1 12  ? 17.283 30.947  -25.531 0.00 77.14  ? 38   GLU   A HG2  1 
ATOM   106   H HG3  . GLU   A  1 12  ? 18.571 31.850  -26.361 0.00 77.14  ? 38   GLU   A HG3  1 
ATOM   107   N N    . LYS   A  1 13  ? 16.874 27.676  -28.879 1.00 57.42  ? 39   LYS   A N    1 
ATOM   108   C CA   . LYS   A  1 13  ? 16.149 26.825  -29.837 1.00 59.52  ? 39   LYS   A CA   1 
ATOM   109   C C    . LYS   A  1 13  ? 14.690 26.678  -29.373 1.00 61.24  ? 39   LYS   A C    1 
ATOM   110   O O    . LYS   A  1 13  ? 14.450 26.496  -28.183 1.00 61.33  ? 39   LYS   A O    1 
ATOM   111   C CB   . LYS   A  1 13  ? 16.797 25.427  -29.941 1.00 62.04  ? 39   LYS   A CB   1 
ATOM   112   C CG   . LYS   A  1 13  ? 18.124 25.409  -30.706 1.00 66.95  ? 39   LYS   A CG   1 
ATOM   113   C CD   . LYS   A  1 13  ? 18.321 24.140  -31.544 1.00 71.91  ? 39   LYS   A CD   1 
ATOM   114   C CE   . LYS   A  1 13  ? 18.599 22.913  -30.707 1.00 76.05  ? 39   LYS   A CE   1 
ATOM   115   N NZ   . LYS   A  1 13  ? 18.747 21.695  -31.546 1.00 78.62  ? 39   LYS   A NZ   1 
ATOM   116   H H    . LYS   A  1 13  ? 17.046 27.203  -27.997 0.00 73.64  ? 39   LYS   A H    1 
ATOM   117   H HA   . LYS   A  1 13  ? 16.148 27.273  -30.829 0.00 76.46  ? 39   LYS   A HA   1 
ATOM   118   H HB2  . LYS   A  1 13  ? 16.989 25.051  -28.937 0.00 78.12  ? 39   LYS   A HB2  1 
ATOM   119   H HB3  . LYS   A  1 13  ? 16.101 24.761  -30.449 0.00 78.30  ? 39   LYS   A HB3  1 
ATOM   120   H HG2  . LYS   A  1 13  ? 18.168 26.264  -31.382 0.00 84.13  ? 39   LYS   A HG2  1 
ATOM   121   H HG3  . LYS   A  1 13  ? 18.942 25.462  -29.989 0.00 83.48  ? 39   LYS   A HG3  1 
ATOM   122   H HD2  . LYS   A  1 13  ? 17.427 23.951  -32.137 0.00 89.30  ? 39   LYS   A HD2  1 
ATOM   123   H HD3  . LYS   A  1 13  ? 19.173 24.289  -32.206 0.00 88.84  ? 39   LYS   A HD3  1 
ATOM   124   H HE2  . LYS   A  1 13  ? 19.529 23.059  -30.159 0.00 93.12  ? 39   LYS   A HE2  1 
ATOM   125   H HE3  . LYS   A  1 13  ? 17.774 22.750  -30.016 0.00 93.59  ? 39   LYS   A HE3  1 
ATOM   126   H HZ1  . LYS   A  1 13  ? 18.990 20.900  -30.964 0.00 95.51  ? 39   LYS   A HZ1  1 
ATOM   127   H HZ2  . LYS   A  1 13  ? 17.874 21.497  -32.024 0.00 96.16  ? 39   LYS   A HZ2  1 
ATOM   128   H HZ3  . LYS   A  1 13  ? 19.477 21.834  -32.237 0.00 95.77  ? 39   LYS   A HZ3  1 
ATOM   129   N N    . LYS   A  1 14  ? 13.722 26.743  -30.304 1.00 62.38  ? 40   LYS   A N    1 
ATOM   130   C CA   . LYS   A  1 14  ? 12.294 26.636  -29.971 1.00 63.67  ? 40   LYS   A CA   1 
ATOM   131   C C    . LYS   A  1 14  ? 11.761 25.265  -30.378 1.00 64.50  ? 40   LYS   A C    1 
ATOM   132   O O    . LYS   A  1 14  ? 11.391 24.462  -29.522 1.00 64.90  ? 40   LYS   A O    1 
ATOM   133   C CB   . LYS   A  1 14  ? 11.477 27.742  -30.669 1.00 66.04  ? 40   LYS   A CB   1 
ATOM   134   C CG   . LYS   A  1 14  ? 12.188 29.094  -30.849 1.00 70.95  ? 40   LYS   A CG   1 
ATOM   135   C CD   . LYS   A  1 14  ? 12.739 29.692  -29.545 1.00 76.04  ? 40   LYS   A CD   1 
ATOM   136   C CE   . LYS   A  1 14  ? 13.579 30.929  -29.783 1.00 80.03  ? 40   LYS   A CE   1 
ATOM   137   N NZ   . LYS   A  1 14  ? 12.758 32.111  -30.158 1.00 82.36  ? 40   LYS   A NZ   1 
ATOM   138   H H    . LYS   A  1 14  ? 13.897 26.852  -31.298 0.00 80.55  ? 40   LYS   A H    1 
ATOM   139   H HA   . LYS   A  1 14  ? 12.138 26.748  -28.899 0.00 82.87  ? 40   LYS   A HA   1 
ATOM   140   H HB2  . LYS   A  1 14  ? 11.198 27.387  -31.660 0.00 86.43  ? 40   LYS   A HB2  1 
ATOM   141   H HB3  . LYS   A  1 14  ? 10.576 27.923  -30.084 0.00 87.01  ? 40   LYS   A HB3  1 
ATOM   142   H HG2  . LYS   A  1 14  ? 13.017 28.970  -31.545 0.00 92.33  ? 40   LYS   A HG2  1 
ATOM   143   H HG3  . LYS   A  1 14  ? 11.474 29.806  -31.259 0.00 93.49  ? 40   LYS   A HG3  1 
ATOM   144   H HD2  . LYS   A  1 14  ? 11.906 29.966  -28.899 0.00 99.54  ? 40   LYS   A HD2  1 
ATOM   145   H HD3  . LYS   A  1 14  ? 13.374 28.963  -29.046 0.00 98.33  ? 40   LYS   A HD3  1 
ATOM   146   H HE2  . LYS   A  1 14  ? 14.123 31.169  -28.871 0.00 103.93 ? 40   LYS   A HE2  1 
ATOM   147   H HE3  . LYS   A  1 14  ? 14.280 30.734  -30.594 0.00 103.75 ? 40   LYS   A HE3  1 
ATOM   148   H HZ1  . LYS   A  1 14  ? 13.362 32.903  -30.351 0.00 108.19 ? 40   LYS   A HZ1  1 
ATOM   149   H HZ2  . LYS   A  1 14  ? 12.204 31.909  -30.985 0.00 108.19 ? 40   LYS   A HZ2  1 
ATOM   150   H HZ3  . LYS   A  1 14  ? 12.133 32.352  -29.395 0.00 108.34 ? 40   LYS   A HZ3  1 
ATOM   151   N N    . ASP   A  1 17  ? 6.522  22.659  -27.529 1.00 65.95  ? 43   ASP   A N    1 
ATOM   152   C CA   . ASP   A  1 17  ? 5.873  23.409  -26.456 1.00 66.26  ? 43   ASP   A CA   1 
ATOM   153   C C    . ASP   A  1 17  ? 6.911  23.862  -25.408 1.00 65.82  ? 43   ASP   A C    1 
ATOM   154   O O    . ASP   A  1 17  ? 6.697  23.684  -24.205 1.00 66.08  ? 43   ASP   A O    1 
ATOM   155   C CB   . ASP   A  1 17  ? 4.773  22.550  -25.799 1.00 68.48  ? 43   ASP   A CB   1 
ATOM   156   C CG   . ASP   A  1 17  ? 3.730  22.029  -26.771 1.00 73.76  ? 43   ASP   A CG   1 
ATOM   157   O OD1  . ASP   A  1 17  ? 3.763  20.815  -27.082 1.00 74.71  ? 43   ASP   A OD1  1 
ATOM   158   O OD2  . ASP   A  1 17  ? 2.875  22.830  -27.212 1.00 75.96  ? 43   ASP   A OD2  1 
ATOM   159   H HA   . ASP   A  1 17  ? 5.403  24.297  -26.876 0.00 88.09  ? 43   ASP   A HA   1 
ATOM   160   H HB2  . ASP   A  1 17  ? 5.238  21.692  -25.316 0.00 89.85  ? 43   ASP   A HB2  1 
ATOM   161   H HB3  . ASP   A  1 17  ? 4.251  23.154  -25.058 0.00 91.06  ? 43   ASP   A HB3  1 
ATOM   162   N N    . SER   A  1 18  ? 8.032  24.457  -25.867 1.00 64.75  ? 44   SER   A N    1 
ATOM   163   C CA   . SER   A  1 18  ? 9.097  24.927  -24.976 1.00 64.08  ? 44   SER   A CA   1 
ATOM   164   C C    . SER   A  1 18  ? 10.171 25.739  -25.740 1.00 62.83  ? 44   SER   A C    1 
ATOM   165   O O    . SER   A  1 18  ? 10.198 25.733  -26.972 1.00 63.33  ? 44   SER   A O    1 
ATOM   166   C CB   . SER   A  1 18  ? 9.750  23.742  -24.265 1.00 65.53  ? 44   SER   A CB   1 
ATOM   167   O OG   . SER   A  1 18  ? 10.167 22.758  -25.194 1.00 68.28  ? 44   SER   A OG   1 
ATOM   168   H H    . SER   A  1 18  ? 8.224  24.632  -26.848 0.00 84.99  ? 44   SER   A H    1 
ATOM   169   H HA   . SER   A  1 18  ? 8.663  25.576  -24.217 0.00 84.64  ? 44   SER   A HA   1 
ATOM   170   H HB2  . SER   A  1 18  ? 10.627 24.091  -23.721 0.00 84.80  ? 44   SER   A HB2  1 
ATOM   171   H HB3  . SER   A  1 18  ? 9.039  23.298  -23.569 0.00 85.16  ? 44   SER   A HB3  1 
ATOM   172   H HG   . SER   A  1 18  ? 10.610 22.008  -24.717 0.00 87.06  ? 44   SER   A HG   1 
ATOM   173   N N    . VAL   A  1 19  ? 11.042 26.448  -25.000 1.00 60.97  ? 45   VAL   A N    1 
ATOM   174   C CA   . VAL   A  1 19  ? 12.153 27.224  -25.564 1.00 59.50  ? 45   VAL   A CA   1 
ATOM   175   C C    . VAL   A  1 19  ? 13.386 26.926  -24.687 1.00 57.12  ? 45   VAL   A C    1 
ATOM   176   O O    . VAL   A  1 19  ? 13.370 27.165  -23.478 1.00 57.38  ? 45   VAL   A O    1 
ATOM   177   C CB   . VAL   A  1 19  ? 11.852 28.752  -25.744 1.00 60.54  ? 45   VAL   A CB   1 
ATOM   178   C CG1  . VAL   A  1 19  ? 10.894 29.280  -24.685 1.00 61.30  ? 45   VAL   A CG1  1 
ATOM   179   C CG2  . VAL   A  1 19  ? 13.135 29.587  -25.787 1.00 60.97  ? 45   VAL   A CG2  1 
ATOM   180   H H    . VAL   A  1 19  ? 11.001 26.494  -23.987 0.00 80.29  ? 45   VAL   A H    1 
ATOM   181   H HA   . VAL   A  1 19  ? 12.370 26.821  -26.553 0.00 77.91  ? 45   VAL   A HA   1 
ATOM   182   H HB   . VAL   A  1 19  ? 11.349 28.911  -26.698 0.00 80.71  ? 45   VAL   A HB   1 
ATOM   183   H HG11 . VAL   A  1 19  ? 10.830 30.363  -24.777 0.00 82.77  ? 45   VAL   A HG11 1 
ATOM   184   H HG12 . VAL   A  1 19  ? 9.908  28.844  -24.843 0.00 82.38  ? 45   VAL   A HG12 1 
ATOM   185   H HG13 . VAL   A  1 19  ? 11.269 29.009  -23.700 0.00 81.87  ? 45   VAL   A HG13 1 
ATOM   186   H HG21 . VAL   A  1 19  ? 12.885 30.578  -26.165 0.00 81.49  ? 45   VAL   A HG21 1 
ATOM   187   H HG22 . VAL   A  1 19  ? 13.547 29.682  -24.783 0.00 80.80  ? 45   VAL   A HG22 1 
ATOM   188   H HG23 . VAL   A  1 19  ? 13.855 29.113  -26.452 0.00 80.24  ? 45   VAL   A HG23 1 
ATOM   189   N N    . ILE   A  1 20  ? 14.432 26.373  -25.307 1.00 54.63  ? 46   ILE   A N    1 
ATOM   190   C CA   . ILE   A  1 20  ? 15.643 25.934  -24.634 1.00 52.65  ? 46   ILE   A CA   1 
ATOM   191   C C    . ILE   A  1 20  ? 16.782 26.941  -24.793 1.00 50.07  ? 46   ILE   A C    1 
ATOM   192   O O    . ILE   A  1 20  ? 17.076 27.357  -25.912 1.00 50.05  ? 46   ILE   A O    1 
ATOM   193   C CB   . ILE   A  1 20  ? 16.065 24.559  -25.233 1.00 53.33  ? 46   ILE   A CB   1 
ATOM   194   C CG1  . ILE   A  1 20  ? 14.918 23.508  -25.135 1.00 54.52  ? 46   ILE   A CG1  1 
ATOM   195   C CG2  . ILE   A  1 20  ? 17.345 24.054  -24.556 1.00 53.79  ? 46   ILE   A CG2  1 
ATOM   196   C CD1  . ILE   A  1 20  ? 15.082 22.273  -26.050 1.00 55.77  ? 46   ILE   A CD1  1 
ATOM   197   H H    . ILE   A  1 20  ? 14.476 26.221  -26.309 0.00 70.88  ? 46   ILE   A H    1 
ATOM   198   H HA   . ILE   A  1 20  ? 15.450 25.783  -23.574 0.00 68.14  ? 46   ILE   A HA   1 
ATOM   199   H HB   . ILE   A  1 20  ? 16.290 24.708  -26.288 0.00 67.90  ? 46   ILE   A HB   1 
ATOM   200   H HG12 . ILE   A  1 20  ? 14.874 23.134  -24.114 0.00 69.31  ? 46   ILE   A HG12 1 
ATOM   201   H HG13 . ILE   A  1 20  ? 13.964 23.964  -25.395 0.00 69.93  ? 46   ILE   A HG13 1 
ATOM   202   H HG21 . ILE   A  1 20  ? 17.437 22.978  -24.694 0.00 67.40  ? 46   ILE   A HG21 1 
ATOM   203   H HG22 . ILE   A  1 20  ? 18.207 24.541  -25.010 0.00 67.82  ? 46   ILE   A HG22 1 
ATOM   204   H HG23 . ILE   A  1 20  ? 17.302 24.289  -23.494 0.00 68.16  ? 46   ILE   A HG23 1 
ATOM   205   H HD11 . ILE   A  1 20  ? 14.126 21.756  -26.114 0.00 70.33  ? 46   ILE   A HD11 1 
ATOM   206   H HD12 . ILE   A  1 20  ? 15.397 22.602  -27.040 0.00 70.14  ? 46   ILE   A HD12 1 
ATOM   207   H HD13 . ILE   A  1 20  ? 15.828 21.604  -25.625 0.00 69.66  ? 46   ILE   A HD13 1 
ATOM   208   N N    . ALA   A  1 21  ? 17.459 27.280  -23.687 1.00 47.42  ? 47   ALA   A N    1 
ATOM   209   C CA   . ALA   A  1 21  ? 18.647 28.125  -23.704 1.00 45.43  ? 47   ALA   A CA   1 
ATOM   210   C C    . ALA   A  1 21  ? 19.848 27.184  -23.600 1.00 43.29  ? 47   ALA   A C    1 
ATOM   211   O O    . ALA   A  1 21  ? 20.128 26.657  -22.525 1.00 43.04  ? 47   ALA   A O    1 
ATOM   212   C CB   . ALA   A  1 21  ? 18.643 29.091  -22.534 1.00 45.36  ? 47   ALA   A CB   1 
ATOM   213   H H    . ALA   A  1 21  ? 17.204 26.971  -22.754 0.00 61.87  ? 47   ALA   A H    1 
ATOM   214   H HA   . ALA   A  1 21  ? 18.714 28.706  -24.622 0.00 59.70  ? 47   ALA   A HA   1 
ATOM   215   H HB1  . ALA   A  1 21  ? 19.614 29.580  -22.483 0.00 60.06  ? 47   ALA   A HB1  1 
ATOM   216   H HB2  . ALA   A  1 21  ? 17.869 29.836  -22.709 0.00 60.73  ? 47   ALA   A HB2  1 
ATOM   217   H HB3  . ALA   A  1 21  ? 18.452 28.550  -21.609 0.00 59.97  ? 47   ALA   A HB3  1 
ATOM   218   N N    . GLU   A  1 22  ? 20.488 26.896  -24.733 1.00 41.48  ? 48   GLU   A N    1 
ATOM   219   C CA   . GLU   A  1 22  ? 21.647 26.024  -24.768 1.00 40.37  ? 48   GLU   A CA   1 
ATOM   220   C C    . GLU   A  1 22  ? 22.807 26.885  -24.343 1.00 37.94  ? 48   GLU   A C    1 
ATOM   221   O O    . GLU   A  1 22  ? 23.203 27.776  -25.088 1.00 37.53  ? 48   GLU   A O    1 
ATOM   222   C CB   . GLU   A  1 22  ? 21.855 25.452  -26.178 1.00 43.95  ? 48   GLU   A CB   1 
ATOM   223   C CG   . GLU   A  1 22  ? 20.701 24.572  -26.625 1.00 51.41  ? 48   GLU   A CG   1 
ATOM   224   C CD   . GLU   A  1 22  ? 20.948 23.840  -27.930 1.00 60.59  ? 48   GLU   A CD   1 
ATOM   225   O OE1  . GLU   A  1 22  ? 21.026 22.589  -27.906 1.00 62.38  ? 48   GLU   A OE1  1 
ATOM   226   O OE2  . GLU   A  1 22  ? 21.076 24.520  -28.975 1.00 63.54  ? 48   GLU   A OE2  1 
ATOM   227   H H    . GLU   A  1 22  ? 20.220 27.255  -25.644 0.00 53.64  ? 48   GLU   A H    1 
ATOM   228   H HA   . GLU   A  1 22  ? 21.529 25.191  -24.078 0.00 51.07  ? 48   GLU   A HA   1 
ATOM   229   H HB2  . GLU   A  1 22  ? 21.951 26.268  -26.893 0.00 55.51  ? 48   GLU   A HB2  1 
ATOM   230   H HB3  . GLU   A  1 22  ? 22.760 24.846  -26.182 0.00 54.68  ? 48   GLU   A HB3  1 
ATOM   231   H HG2  . GLU   A  1 22  ? 20.515 23.824  -25.856 0.00 63.80  ? 48   GLU   A HG2  1 
ATOM   232   H HG3  . GLU   A  1 22  ? 19.816 25.193  -26.756 0.00 64.59  ? 48   GLU   A HG3  1 
ATOM   233   N N    . CYS   A  1 23  ? 23.294 26.688  -23.109 1.00 36.09  ? 49   CYS   A N    1 
ATOM   234   C CA   . CYS   A  1 23  ? 24.362 27.509  -22.534 1.00 35.04  ? 49   CYS   A CA   1 
ATOM   235   C C    . CYS   A  1 23  ? 25.517 26.653  -21.999 1.00 33.59  ? 49   CYS   A C    1 
ATOM   236   O O    . CYS   A  1 23  ? 26.289 27.144  -21.184 1.00 33.38  ? 49   CYS   A O    1 
ATOM   237   C CB   . CYS   A  1 23  ? 23.767 28.379  -21.424 1.00 35.87  ? 49   CYS   A CB   1 
ATOM   238   S SG   . CYS   A  1 23  ? 24.258 30.117  -21.484 1.00 40.01  ? 49   CYS   A SG   1 
ATOM   239   H H    . CYS   A  1 23  ? 22.966 25.965  -22.477 0.00 46.09  ? 49   CYS   A H    1 
ATOM   240   H HA   . CYS   A  1 23  ? 24.786 28.157  -23.300 0.00 45.37  ? 49   CYS   A HA   1 
ATOM   241   H HB2  . CYS   A  1 23  ? 22.681 28.353  -21.507 0.00 47.22  ? 49   CYS   A HB2  1 
ATOM   242   H HB3  . CYS   A  1 23  ? 24.050 27.980  -20.451 0.00 46.84  ? 49   CYS   A HB3  1 
ATOM   243   N N    . SER   A  1 24  ? 25.655 25.399  -22.448 1.00 32.41  ? 50   SER   A N    1 
ATOM   244   C CA   . SER   A  1 24  ? 26.685 24.510  -21.938 1.00 32.37  ? 50   SER   A CA   1 
ATOM   245   C C    . SER   A  1 24  ? 28.061 24.762  -22.535 1.00 32.80  ? 50   SER   A C    1 
ATOM   246   O O    . SER   A  1 24  ? 28.178 25.293  -23.643 1.00 32.85  ? 50   SER   A O    1 
ATOM   247   C CB   . SER   A  1 24  ? 26.288 23.058  -22.195 1.00 33.52  ? 50   SER   A CB   1 
ATOM   248   O OG   . SER   A  1 24  ? 26.396 22.731  -23.571 1.00 35.79  ? 50   SER   A OG   1 
ATOM   249   H H    . SER   A  1 24  ? 25.088 24.972  -23.173 0.00 40.62  ? 50   SER   A H    1 
ATOM   250   H HA   . SER   A  1 24  ? 26.758 24.635  -20.859 0.00 40.40  ? 50   SER   A HA   1 
ATOM   251   H HB2  . SER   A  1 24  ? 26.946 22.406  -21.623 0.00 40.67  ? 50   SER   A HB2  1 
ATOM   252   H HB3  . SER   A  1 24  ? 25.256 22.914  -21.878 0.00 41.18  ? 50   SER   A HB3  1 
ATOM   253   H HG   . SER   A  1 24  ? 26.119 21.788  -23.718 0.00 43.05  ? 50   SER   A HG   1 
ATOM   254   N N    . ASN   A  1 25  ? 29.097 24.319  -21.811 1.00 32.82  ? 51   ASN   A N    1 
ATOM   255   C CA   . ASN   A  1 25  ? 30.484 24.326  -22.244 1.00 33.76  ? 51   ASN   A CA   1 
ATOM   256   C C    . ASN   A  1 25  ? 30.940 25.644  -22.888 1.00 33.23  ? 51   ASN   A C    1 
ATOM   257   O O    . ASN   A  1 25  ? 31.502 25.623  -23.983 1.00 33.16  ? 51   ASN   A O    1 
ATOM   258   C CB   . ASN   A  1 25  ? 30.732 23.117  -23.179 1.00 36.29  ? 51   ASN   A CB   1 
ATOM   259   C CG   . ASN   A  1 25  ? 32.197 22.740  -23.333 1.00 42.03  ? 51   ASN   A CG   1 
ATOM   260   O OD1  . ASN   A  1 25  ? 32.863 22.311  -22.376 1.00 43.49  ? 51   ASN   A OD1  1 
ATOM   261   N ND2  . ASN   A  1 25  ? 32.739 22.884  -24.538 1.00 43.35  ? 51   ASN   A ND2  1 
ATOM   262   H H    . ASN   A  1 25  ? 28.991 23.934  -20.878 0.00 40.25  ? 51   ASN   A H    1 
ATOM   263   H HA   . ASN   A  1 25  ? 31.107 24.176  -21.364 0.00 41.13  ? 51   ASN   A HA   1 
ATOM   264   H HB2  . ASN   A  1 25  ? 30.228 22.253  -22.749 0.00 43.26  ? 51   ASN   A HB2  1 
ATOM   265   H HB3  . ASN   A  1 25  ? 30.305 23.324  -24.160 0.00 43.50  ? 51   ASN   A HB3  1 
ATOM   266   H HD21 . ASN   A  1 25  ? 33.715 22.643  -24.680 0.00 51.26  ? 51   ASN   A HD21 1 
ATOM   267   H HD22 . ASN   A  1 25  ? 32.192 23.234  -25.318 0.00 51.56  ? 51   ASN   A HD22 1 
ATOM   268   N N    . ARG   A  1 26  ? 30.736 26.779  -22.196 1.00 32.30  ? 52   ARG   A N    1 
ATOM   269   C CA   . ARG   A  1 26  ? 31.181 28.072  -22.711 1.00 32.69  ? 52   ARG   A CA   1 
ATOM   270   C C    . ARG   A  1 26  ? 31.934 28.921  -21.666 1.00 32.76  ? 52   ARG   A C    1 
ATOM   271   O O    . ARG   A  1 26  ? 31.947 30.151  -21.762 1.00 32.85  ? 52   ARG   A O    1 
ATOM   272   C CB   . ARG   A  1 26  ? 30.048 28.863  -23.388 1.00 33.58  ? 52   ARG   A CB   1 
ATOM   273   C CG   . ARG   A  1 26  ? 28.707 28.929  -22.694 1.00 35.01  ? 52   ARG   A CG   1 
ATOM   274   C CD   . ARG   A  1 26  ? 27.627 29.175  -23.732 1.00 37.03  ? 52   ARG   A CD   1 
ATOM   275   N NE   . ARG   A  1 26  ? 27.301 27.979  -24.503 1.00 39.06  ? 52   ARG   A NE   1 
ATOM   276   C CZ   . ARG   A  1 26  ? 26.602 27.973  -25.640 1.00 40.96  ? 52   ARG   A CZ   1 
ATOM   277   N NH1  . ARG   A  1 26  ? 26.155 29.113  -26.164 1.00 38.97  ? 52   ARG   A NH1  1 
ATOM   278   N NH2  . ARG   A  1 26  ? 26.342 26.828  -26.261 1.00 41.23  ? 52   ARG   A NH2  1 
ATOM   279   H H    . ARG   A  1 26  ? 30.276 26.827  -21.293 0.00 40.71  ? 52   ARG   A H    1 
ATOM   280   H HA   . ARG   A  1 26  ? 31.916 27.897  -23.494 0.00 41.14  ? 52   ARG   A HA   1 
ATOM   281   H HB2  . ARG   A  1 26  ? 30.366 29.893  -23.539 0.00 43.42  ? 52   ARG   A HB2  1 
ATOM   282   H HB3  . ARG   A  1 26  ? 29.882 28.410  -24.364 0.00 42.62  ? 52   ARG   A HB3  1 
ATOM   283   H HG2  . ARG   A  1 26  ? 28.484 28.011  -22.153 0.00 44.67  ? 52   ARG   A HG2  1 
ATOM   284   H HG3  . ARG   A  1 26  ? 28.696 29.790  -22.030 0.00 45.58  ? 52   ARG   A HG3  1 
ATOM   285   H HD2  . ARG   A  1 26  ? 26.722 29.519  -23.234 0.00 48.04  ? 52   ARG   A HD2  1 
ATOM   286   H HD3  . ARG   A  1 26  ? 27.996 29.938  -24.415 0.00 47.87  ? 52   ARG   A HD3  1 
ATOM   287   H HE   . ARG   A  1 26  ? 27.620 27.087  -24.138 0.00 48.95  ? 52   ARG   A HE   1 
ATOM   288   H HH11 . ARG   A  1 26  ? 26.314 30.012  -25.722 0.00 50.43  ? 52   ARG   A HH11 1 
ATOM   289   H HH12 . ARG   A  1 26  ? 25.624 29.088  -27.028 0.00 49.97  ? 52   ARG   A HH12 1 
ATOM   290   H HH21 . ARG   A  1 26  ? 26.681 25.951  -25.879 0.00 51.00  ? 52   ARG   A HH21 1 
ATOM   291   H HH22 . ARG   A  1 26  ? 25.817 26.823  -27.130 0.00 51.49  ? 52   ARG   A HH22 1 
ATOM   292   N N    . ARG   A  1 27  ? 32.638 28.252  -20.734 1.00 32.30  ? 53   ARG   A N    1 
ATOM   293   C CA   . ARG   A  1 27  ? 33.538 28.894  -19.773 1.00 32.92  ? 53   ARG   A CA   1 
ATOM   294   C C    . ARG   A  1 27  ? 32.861 29.928  -18.866 1.00 33.54  ? 53   ARG   A C    1 
ATOM   295   O O    . ARG   A  1 27  ? 33.511 30.877  -18.422 1.00 33.85  ? 53   ARG   A O    1 
ATOM   296   C CB   . ARG   A  1 27  ? 34.737 29.512  -20.533 1.00 33.44  ? 53   ARG   A CB   1 
ATOM   297   C CG   . ARG   A  1 27  ? 35.370 28.549  -21.559 1.00 35.31  ? 53   ARG   A CG   1 
ATOM   298   C CD   . ARG   A  1 27  ? 36.453 29.195  -22.415 1.00 36.70  ? 53   ARG   A CD   1 
ATOM   299   N NE   . ARG   A  1 27  ? 35.966 30.363  -23.157 1.00 37.58  ? 53   ARG   A NE   1 
ATOM   300   C CZ   . ARG   A  1 27  ? 35.225 30.319  -24.262 1.00 38.17  ? 53   ARG   A CZ   1 
ATOM   301   N NH1  . ARG   A  1 27  ? 34.846 29.150  -24.772 1.00 37.40  ? 53   ARG   A NH1  1 
ATOM   302   N NH2  . ARG   A  1 27  ? 34.843 31.441  -24.856 1.00 37.56  ? 53   ARG   A NH2  1 
ATOM   303   H H    . ARG   A  1 27  ? 32.600 27.246  -20.607 0.00 40.76  ? 53   ARG   A H    1 
ATOM   304   H HA   . ARG   A  1 27  ? 33.942 28.121  -19.120 0.00 42.11  ? 53   ARG   A HA   1 
ATOM   305   H HB2  . ARG   A  1 27  ? 34.395 30.403  -21.056 0.00 43.50  ? 53   ARG   A HB2  1 
ATOM   306   H HB3  . ARG   A  1 27  ? 35.512 29.778  -19.815 0.00 43.33  ? 53   ARG   A HB3  1 
ATOM   307   H HG2  . ARG   A  1 27  ? 35.819 27.712  -21.028 0.00 44.29  ? 53   ARG   A HG2  1 
ATOM   308   H HG3  . ARG   A  1 27  ? 34.607 28.184  -22.245 0.00 44.37  ? 53   ARG   A HG3  1 
ATOM   309   H HD2  . ARG   A  1 27  ? 37.251 29.537  -21.758 0.00 46.69  ? 53   ARG   A HD2  1 
ATOM   310   H HD3  . ARG   A  1 27  ? 36.849 28.465  -23.120 0.00 45.93  ? 53   ARG   A HD3  1 
ATOM   311   H HE   . ARG   A  1 27  ? 36.234 31.276  -22.802 0.00 48.52  ? 53   ARG   A HE   1 
ATOM   312   H HH11 . ARG   A  1 27  ? 35.108 28.266  -24.349 0.00 46.56  ? 53   ARG   A HH11 1 
ATOM   313   H HH12 . ARG   A  1 27  ? 34.272 29.133  -25.610 0.00 46.89  ? 53   ARG   A HH12 1 
ATOM   314   H HH21 . ARG   A  1 27  ? 35.122 32.341  -24.478 0.00 48.89  ? 53   ARG   A HH21 1 
ATOM   315   H HH22 . ARG   A  1 27  ? 34.273 31.408  -25.696 0.00 48.27  ? 53   ARG   A HH22 1 
ATOM   316   N N    . LEU   A  1 28  ? 31.574 29.732  -18.560 1.00 33.89  ? 54   LEU   A N    1 
ATOM   317   C CA   . LEU   A  1 28  ? 30.841 30.668  -17.714 1.00 34.80  ? 54   LEU   A CA   1 
ATOM   318   C C    . LEU   A  1 28  ? 31.286 30.489  -16.268 1.00 35.50  ? 54   LEU   A C    1 
ATOM   319   O O    . LEU   A  1 28  ? 31.289 29.366  -15.778 1.00 35.39  ? 54   LEU   A O    1 
ATOM   320   C CB   . LEU   A  1 28  ? 29.327 30.435  -17.827 1.00 35.05  ? 54   LEU   A CB   1 
ATOM   321   C CG   . LEU   A  1 28  ? 28.753 30.550  -19.229 1.00 36.20  ? 54   LEU   A CG   1 
ATOM   322   C CD1  . LEU   A  1 28  ? 27.309 30.100  -19.257 1.00 36.41  ? 54   LEU   A CD1  1 
ATOM   323   C CD2  . LEU   A  1 28  ? 28.903 31.973  -19.787 1.00 36.77  ? 54   LEU   A CD2  1 
ATOM   324   H H    . LEU   A  1 28  ? 31.024 28.931  -18.853 0.00 44.01  ? 54   LEU   A H    1 
ATOM   325   H HA   . LEU   A  1 28  ? 31.056 31.689  -18.024 0.00 46.77  ? 54   LEU   A HA   1 
ATOM   326   H HB2  . LEU   A  1 28  ? 29.101 29.434  -17.463 0.00 46.22  ? 54   LEU   A HB2  1 
ATOM   327   H HB3  . LEU   A  1 28  ? 28.818 31.170  -17.204 0.00 47.26  ? 54   LEU   A HB3  1 
ATOM   328   H HG   . LEU   A  1 28  ? 29.317 29.877  -19.872 0.00 47.31  ? 54   LEU   A HG   1 
ATOM   329   H HD11 . LEU   A  1 28  ? 26.911 30.227  -20.263 0.00 48.10  ? 54   LEU   A HD11 1 
ATOM   330   H HD12 . LEU   A  1 28  ? 27.264 29.051  -18.969 0.00 47.64  ? 54   LEU   A HD12 1 
ATOM   331   H HD13 . LEU   A  1 28  ? 26.740 30.700  -18.548 0.00 48.71  ? 54   LEU   A HD13 1 
ATOM   332   H HD21 . LEU   A  1 28  ? 28.316 32.061  -20.701 0.00 49.21  ? 54   LEU   A HD21 1 
ATOM   333   H HD22 . LEU   A  1 28  ? 28.546 32.685  -19.045 0.00 49.85  ? 54   LEU   A HD22 1 
ATOM   334   H HD23 . LEU   A  1 28  ? 29.951 32.160  -20.012 0.00 49.14  ? 54   LEU   A HD23 1 
ATOM   335   N N    . GLN   A  1 29  ? 31.711 31.577  -15.619 1.00 35.98  ? 55   GLN   A N    1 
ATOM   336   C CA   . GLN   A  1 29  ? 32.166 31.576  -14.223 1.00 37.47  ? 55   GLN   A CA   1 
ATOM   337   C C    . GLN   A  1 29  ? 30.998 31.775  -13.238 1.00 37.83  ? 55   GLN   A C    1 
ATOM   338   O O    . GLN   A  1 29  ? 31.139 31.457  -12.057 1.00 37.60  ? 55   GLN   A O    1 
ATOM   339   C CB   . GLN   A  1 29  ? 33.224 32.678  -14.009 1.00 40.50  ? 55   GLN   A CB   1 
ATOM   340   C CG   . GLN   A  1 29  ? 34.535 32.405  -14.755 1.00 46.63  ? 55   GLN   A CG   1 
ATOM   341   C CD   . GLN   A  1 29  ? 35.479 33.588  -14.779 1.00 54.21  ? 55   GLN   A CD   1 
ATOM   342   O OE1  . GLN   A  1 29  ? 35.226 34.652  -14.193 1.00 57.35  ? 55   GLN   A OE1  1 
ATOM   343   N NE2  . GLN   A  1 29  ? 36.600 33.430  -15.464 1.00 55.27  ? 55   GLN   A NE2  1 
ATOM   344   H H    . GLN   A  1 29  ? 31.750 32.499  -16.042 0.00 49.02  ? 55   GLN   A H    1 
ATOM   345   H HA   . GLN   A  1 29  ? 32.638 30.623  -13.991 0.00 50.18  ? 55   GLN   A HA   1 
ATOM   346   H HB2  . GLN   A  1 29  ? 32.821 33.629  -14.356 0.00 55.45  ? 55   GLN   A HB2  1 
ATOM   347   H HB3  . GLN   A  1 29  ? 33.453 32.742  -12.946 0.00 55.25  ? 55   GLN   A HB3  1 
ATOM   348   H HG2  . GLN   A  1 29  ? 35.050 31.580  -14.265 0.00 61.50  ? 55   GLN   A HG2  1 
ATOM   349   H HG3  . GLN   A  1 29  ? 34.314 32.141  -15.787 0.00 61.44  ? 55   GLN   A HG3  1 
ATOM   350   H HE21 . GLN   A  1 29  ? 36.786 32.552  -15.937 0.00 71.92  ? 55   GLN   A HE21 1 
ATOM   351   H HE22 . GLN   A  1 29  ? 37.272 34.188  -15.519 0.00 72.98  ? 55   GLN   A HE22 1 
ATOM   352   N N    . GLU   A  1 30  ? 29.872 32.341  -13.708 1.00 37.98  ? 56   GLU   A N    1 
ATOM   353   C CA   . GLU   A  1 30  ? 28.669 32.566  -12.912 1.00 38.52  ? 56   GLU   A CA   1 
ATOM   354   C C    . GLU   A  1 30  ? 27.437 32.287  -13.789 1.00 37.97  ? 56   GLU   A C    1 
ATOM   355   O O    . GLU   A  1 30  ? 27.545 32.239  -15.015 1.00 37.86  ? 56   GLU   A O    1 
ATOM   356   C CB   . GLU   A  1 30  ? 28.623 34.030  -12.411 1.00 41.76  ? 56   GLU   A CB   1 
ATOM   357   C CG   . GLU   A  1 30  ? 29.803 34.430  -11.542 1.00 49.43  ? 56   GLU   A CG   1 
ATOM   358   C CD   . GLU   A  1 30  ? 29.424 35.219  -10.304 1.00 59.02  ? 56   GLU   A CD   1 
ATOM   359   O OE1  . GLU   A  1 30  ? 29.286 34.596  -9.225  1.00 61.59  ? 56   GLU   A OE1  1 
ATOM   360   O OE2  . GLU   A  1 30  ? 29.252 36.456  -10.414 1.00 61.20  ? 56   GLU   A OE2  1 
ATOM   361   H H    . GLU   A  1 30  ? 29.759 32.681  -14.657 0.00 52.11  ? 56   GLU   A H    1 
ATOM   362   H HA   . GLU   A  1 30  ? 28.635 31.897  -12.054 0.00 53.14  ? 56   GLU   A HA   1 
ATOM   363   H HB2  . GLU   A  1 30  ? 28.609 34.694  -13.274 0.00 58.41  ? 56   GLU   A HB2  1 
ATOM   364   H HB3  . GLU   A  1 30  ? 27.717 34.170  -11.824 0.00 58.62  ? 56   GLU   A HB3  1 
ATOM   365   H HG2  . GLU   A  1 30  ? 30.315 33.528  -11.212 0.00 67.25  ? 56   GLU   A HG2  1 
ATOM   366   H HG3  . GLU   A  1 30  ? 30.483 35.043  -12.133 0.00 67.86  ? 56   GLU   A HG3  1 
ATOM   367   N N    . VAL   A  1 31  ? 26.252 32.149  -13.171 1.00 37.48  ? 57   VAL   A N    1 
ATOM   368   C CA   . VAL   A  1 31  ? 25.011 31.967  -13.919 1.00 37.72  ? 57   VAL   A CA   1 
ATOM   369   C C    . VAL   A  1 31  ? 24.747 33.298  -14.662 1.00 38.92  ? 57   VAL   A C    1 
ATOM   370   O O    . VAL   A  1 31  ? 24.805 34.355  -14.019 1.00 38.51  ? 57   VAL   A O    1 
ATOM   371   C CB   . VAL   A  1 31  ? 23.827 31.599  -12.988 1.00 37.71  ? 57   VAL   A CB   1 
ATOM   372   C CG1  . VAL   A  1 31  ? 22.512 31.577  -13.764 1.00 37.84  ? 57   VAL   A CG1  1 
ATOM   373   C CG2  . VAL   A  1 31  ? 24.072 30.257  -12.302 1.00 37.71  ? 57   VAL   A CG2  1 
ATOM   374   H H    . VAL   A  1 31  ? 26.130 32.174  -12.163 0.00 52.45  ? 57   VAL   A H    1 
ATOM   375   H HA   . VAL   A  1 31  ? 25.143 31.141  -14.614 0.00 51.71  ? 57   VAL   A HA   1 
ATOM   376   H HB   . VAL   A  1 31  ? 23.740 32.358  -12.212 0.00 53.31  ? 57   VAL   A HB   1 
ATOM   377   H HG11 . VAL   A  1 31  ? 21.759 31.058  -13.172 0.00 52.91  ? 57   VAL   A HG11 1 
ATOM   378   H HG12 . VAL   A  1 31  ? 22.175 32.597  -13.945 0.00 53.56  ? 57   VAL   A HG12 1 
ATOM   379   H HG13 . VAL   A  1 31  ? 22.663 31.058  -14.708 0.00 52.35  ? 57   VAL   A HG13 1 
ATOM   380   H HG21 . VAL   A  1 31  ? 23.201 29.984  -11.707 0.00 52.19  ? 57   VAL   A HG21 1 
ATOM   381   H HG22 . VAL   A  1 31  ? 24.244 29.500  -13.066 0.00 51.34  ? 57   VAL   A HG22 1 
ATOM   382   H HG23 . VAL   A  1 31  ? 24.945 30.338  -11.657 0.00 52.03  ? 57   VAL   A HG23 1 
ATOM   383   N N    . PRO   A  1 32  ? 24.579 33.299  -16.006 1.00 39.68  ? 58   PRO   A N    1 
ATOM   384   C CA   . PRO   A  1 32  ? 24.377 34.583  -16.699 1.00 40.47  ? 58   PRO   A CA   1 
ATOM   385   C C    . PRO   A  1 32  ? 23.108 35.297  -16.275 1.00 41.99  ? 58   PRO   A C    1 
ATOM   386   O O    . PRO   A  1 32  ? 22.051 34.668  -16.193 1.00 42.00  ? 58   PRO   A O    1 
ATOM   387   C CB   . PRO   A  1 32  ? 24.284 34.212  -18.184 1.00 40.93  ? 58   PRO   A CB   1 
ATOM   388   C CG   . PRO   A  1 32  ? 24.568 32.782  -18.279 1.00 41.23  ? 58   PRO   A CG   1 
ATOM   389   C CD   . PRO   A  1 32  ? 24.525 32.156  -16.935 1.00 39.22  ? 58   PRO   A CD   1 
ATOM   390   H HA   . PRO   A  1 32  ? 25.239 35.231  -16.546 0.00 57.04  ? 58   PRO   A HA   1 
ATOM   391   H HB2  . PRO   A  1 32  ? 23.283 34.425  -18.554 0.00 57.13  ? 58   PRO   A HB2  1 
ATOM   392   H HB3  . PRO   A  1 32  ? 25.024 34.781  -18.744 0.00 56.90  ? 58   PRO   A HB3  1 
ATOM   393   H HG2  . PRO   A  1 32  ? 23.823 32.319  -18.925 0.00 56.00  ? 58   PRO   A HG2  1 
ATOM   394   H HG3  . PRO   A  1 32  ? 25.558 32.666  -18.716 0.00 55.84  ? 58   PRO   A HG3  1 
ATOM   395   H HD2  . PRO   A  1 32  ? 23.600 31.597  -16.803 0.00 53.63  ? 58   PRO   A HD2  1 
ATOM   396   H HD3  . PRO   A  1 32  ? 25.400 31.519  -16.826 0.00 53.18  ? 58   PRO   A HD3  1 
ATOM   397   N N    . GLN   A  1 33  ? 23.207 36.614  -16.043 1.00 42.87  ? 59   GLN   A N    1 
ATOM   398   C CA   . GLN   A  1 33  ? 22.048 37.431  -15.709 1.00 44.60  ? 59   GLN   A CA   1 
ATOM   399   C C    . GLN   A  1 33  ? 21.391 38.010  -16.986 1.00 45.67  ? 59   GLN   A C    1 
ATOM   400   O O    . GLN   A  1 33  ? 20.670 38.999  -16.891 1.00 45.82  ? 59   GLN   A O    1 
ATOM   401   C CB   . GLN   A  1 33  ? 22.445 38.551  -14.728 1.00 46.42  ? 59   GLN   A CB   1 
ATOM   402   C CG   . GLN   A  1 33  ? 23.055 38.036  -13.420 1.00 50.39  ? 59   GLN   A CG   1 
ATOM   403   C CD   . GLN   A  1 33  ? 22.111 37.142  -12.643 1.00 55.06  ? 59   GLN   A CD   1 
ATOM   404   O OE1  . GLN   A  1 33  ? 22.351 35.935  -12.462 1.00 56.36  ? 59   GLN   A OE1  1 
ATOM   405   N NE2  . GLN   A  1 33  ? 21.010 37.712  -12.174 1.00 55.44  ? 59   GLN   A NE2  1 
ATOM   406   H H    . GLN   A  1 33  ? 24.075 37.139  -16.072 0.00 61.55  ? 59   GLN   A H    1 
ATOM   407   H HA   . GLN   A  1 33  ? 21.290 36.819  -15.223 0.00 64.33  ? 59   GLN   A HA   1 
ATOM   408   H HB2  . GLN   A  1 33  ? 23.177 39.198  -15.210 0.00 67.67  ? 59   GLN   A HB2  1 
ATOM   409   H HB3  . GLN   A  1 33  ? 21.559 39.127  -14.464 0.00 68.23  ? 59   GLN   A HB3  1 
ATOM   410   H HG2  . GLN   A  1 33  ? 23.958 37.468  -13.636 0.00 71.42  ? 59   GLN   A HG2  1 
ATOM   411   H HG3  . GLN   A  1 33  ? 23.299 38.888  -12.788 0.00 72.79  ? 59   GLN   A HG3  1 
ATOM   412   H HE21 . GLN   A  1 33  ? 20.839 38.699  -12.340 0.00 79.47  ? 59   GLN   A HE21 1 
ATOM   413   H HE22 . GLN   A  1 33  ? 20.342 37.165  -11.642 0.00 78.71  ? 59   GLN   A HE22 1 
ATOM   414   N N    . THR   A  1 34  ? 21.599 37.367  -18.168 1.00 46.02  ? 60   THR   A N    1 
ATOM   415   C CA   . THR   A  1 34  ? 21.022 37.802  -19.440 1.00 46.92  ? 60   THR   A CA   1 
ATOM   416   C C    . THR   A  1 34  ? 20.244 36.660  -20.129 1.00 47.85  ? 60   THR   A C    1 
ATOM   417   O O    . THR   A  1 34  ? 20.105 36.677  -21.353 1.00 48.15  ? 60   THR   A O    1 
ATOM   418   C CB   . THR   A  1 34  ? 22.123 38.384  -20.337 1.00 48.02  ? 60   THR   A CB   1 
ATOM   419   O OG1  . THR   A  1 34  ? 23.140 37.398  -20.520 1.00 48.90  ? 60   THR   A OG1  1 
ATOM   420   C CG2  . THR   A  1 34  ? 22.732 39.661  -19.759 1.00 48.35  ? 60   THR   A CG2  1 
ATOM   421   H H    . THR   A  1 34  ? 22.154 36.523  -18.272 0.00 64.95  ? 60   THR   A H    1 
ATOM   422   H HA   . THR   A  1 34  ? 20.301 38.600  -19.266 0.00 67.82  ? 60   THR   A HA   1 
ATOM   423   H HB   . THR   A  1 34  ? 21.703 38.647  -21.307 0.00 68.39  ? 60   THR   A HB   1 
ATOM   424   H HG1  . THR   A  1 34  ? 22.905 36.788  -21.267 0.00 67.84  ? 60   THR   A HG1  1 
ATOM   425   H HG21 . THR   A  1 34  ? 23.472 40.064  -20.448 0.00 69.45  ? 60   THR   A HG21 1 
ATOM   426   H HG22 . THR   A  1 34  ? 21.952 40.405  -19.601 0.00 70.28  ? 60   THR   A HG22 1 
ATOM   427   H HG23 . THR   A  1 34  ? 23.217 39.448  -18.807 0.00 69.39  ? 60   THR   A HG23 1 
ATOM   428   N N    . VAL   A  1 35  ? 19.710 35.690  -19.353 1.00 47.99  ? 61   VAL   A N    1 
ATOM   429   C CA   . VAL   A  1 35  ? 18.906 34.603  -19.919 1.00 48.65  ? 61   VAL   A CA   1 
ATOM   430   C C    . VAL   A  1 35  ? 17.529 35.197  -20.262 1.00 49.09  ? 61   VAL   A C    1 
ATOM   431   O O    . VAL   A  1 35  ? 17.045 36.079  -19.557 1.00 49.17  ? 61   VAL   A O    1 
ATOM   432   C CB   . VAL   A  1 35  ? 18.787 33.389  -18.954 1.00 49.36  ? 61   VAL   A CB   1 
ATOM   433   C CG1  . VAL   A  1 35  ? 17.907 32.289  -19.550 1.00 49.88  ? 61   VAL   A CG1  1 
ATOM   434   C CG2  . VAL   A  1 35  ? 20.166 32.833  -18.599 1.00 49.78  ? 61   VAL   A CG2  1 
ATOM   435   H H    . VAL   A  1 35  ? 19.797 35.637  -18.343 0.00 67.42  ? 61   VAL   A H    1 
ATOM   436   H HA   . VAL   A  1 35  ? 19.369 34.246  -20.838 0.00 67.03  ? 61   VAL   A HA   1 
ATOM   437   H HB   . VAL   A  1 35  ? 18.318 33.723  -18.029 0.00 68.37  ? 61   VAL   A HB   1 
ATOM   438   H HG11 . VAL   A  1 35  ? 18.046 31.372  -18.980 0.00 67.48  ? 61   VAL   A HG11 1 
ATOM   439   H HG12 . VAL   A  1 35  ? 16.862 32.589  -19.493 0.00 68.54  ? 61   VAL   A HG12 1 
ATOM   440   H HG13 . VAL   A  1 35  ? 18.195 32.130  -20.588 0.00 67.63  ? 61   VAL   A HG13 1 
ATOM   441   H HG21 . VAL   A  1 35  ? 20.046 31.965  -17.953 0.00 67.26  ? 61   VAL   A HG21 1 
ATOM   442   H HG22 . VAL   A  1 35  ? 20.681 32.547  -19.515 0.00 67.15  ? 61   VAL   A HG22 1 
ATOM   443   H HG23 . VAL   A  1 35  ? 20.738 33.597  -18.074 0.00 68.03  ? 61   VAL   A HG23 1 
ATOM   444   N N    . GLY   A  1 36  ? 16.929 34.736  -21.351 1.00 49.25  ? 62   GLY   A N    1 
ATOM   445   C CA   . GLY   A  1 36  ? 15.638 35.247  -21.787 1.00 49.85  ? 62   GLY   A CA   1 
ATOM   446   C C    . GLY   A  1 36  ? 14.510 34.976  -20.809 1.00 50.44  ? 62   GLY   A C    1 
ATOM   447   O O    . GLY   A  1 36  ? 14.418 33.879  -20.259 1.00 50.69  ? 62   GLY   A O    1 
ATOM   448   H H    . GLY   A  1 36  ? 17.307 34.010  -21.951 0.00 68.16  ? 62   GLY   A H    1 
ATOM   449   H HA2  . GLY   A  1 36  ? 15.724 36.322  -21.942 0.00 70.98  ? 62   GLY   A HA2  1 
ATOM   450   H HA3  . GLY   A  1 36  ? 15.378 34.786  -22.738 0.00 70.01  ? 62   GLY   A HA3  1 
ATOM   451   N N    . LYS   A  1 37  ? 13.651 35.979  -20.583 1.00 50.55  ? 63   LYS   A N    1 
ATOM   452   C CA   . LYS   A  1 37  ? 12.474 35.896  -19.704 1.00 51.09  ? 63   LYS   A CA   1 
ATOM   453   C C    . LYS   A  1 37  ? 11.536 34.737  -20.071 1.00 50.73  ? 63   LYS   A C    1 
ATOM   454   O O    . LYS   A  1 37  ? 10.862 34.188  -19.199 1.00 50.94  ? 63   LYS   A O    1 
ATOM   455   C CB   . LYS   A  1 37  ? 11.673 37.218  -19.772 1.00 53.56  ? 63   LYS   A CB   1 
ATOM   456   C CG   . LYS   A  1 37  ? 11.129 37.551  -21.175 1.00 59.06  ? 63   LYS   A CG   1 
ATOM   457   C CD   . LYS   A  1 37  ? 10.339 38.860  -21.223 1.00 64.48  ? 63   LYS   A CD   1 
ATOM   458   C CE   . LYS   A  1 37  ? 8.847  38.627  -21.231 1.00 68.86  ? 63   LYS   A CE   1 
ATOM   459   N NZ   . LYS   A  1 37  ? 8.087  39.898  -21.386 1.00 71.71  ? 63   LYS   A NZ   1 
ATOM   460   H H    . LYS   A  1 37  ? 13.772 36.901  -20.988 0.00 73.13  ? 63   LYS   A H    1 
ATOM   461   H HA   . LYS   A  1 37  ? 12.804 35.752  -18.677 0.00 73.77  ? 63   LYS   A HA   1 
ATOM   462   H HB2  . LYS   A  1 37  ? 10.821 37.146  -19.097 0.00 78.49  ? 63   LYS   A HB2  1 
ATOM   463   H HB3  . LYS   A  1 37  ? 12.319 38.038  -19.463 0.00 78.39  ? 63   LYS   A HB3  1 
ATOM   464   H HG2  . LYS   A  1 37  ? 11.960 37.649  -21.872 0.00 84.50  ? 63   LYS   A HG2  1 
ATOM   465   H HG3  . LYS   A  1 37  ? 10.462 36.759  -21.510 0.00 84.64  ? 63   LYS   A HG3  1 
ATOM   466   H HD2  . LYS   A  1 37  ? 10.587 39.461  -20.350 0.00 93.17  ? 63   LYS   A HD2  1 
ATOM   467   H HD3  . LYS   A  1 37  ? 10.600 39.395  -22.135 0.00 92.86  ? 63   LYS   A HD3  1 
ATOM   468   H HE2  . LYS   A  1 37  ? 8.583  37.980  -22.066 0.00 98.15  ? 63   LYS   A HE2  1 
ATOM   469   H HE3  . LYS   A  1 37  ? 8.551  38.166  -20.289 0.00 98.53  ? 63   LYS   A HE3  1 
ATOM   470   H HZ1  . LYS   A  1 37  ? 7.091  39.716  -21.317 0.00 103.72 ? 63   LYS   A HZ1  1 
ATOM   471   H HZ2  . LYS   A  1 37  ? 8.356  40.555  -20.660 0.00 103.74 ? 63   LYS   A HZ2  1 
ATOM   472   H HZ3  . LYS   A  1 37  ? 8.284  40.308  -22.293 0.00 103.39 ? 63   LYS   A HZ3  1 
ATOM   473   N N    . TYR   A  1 38  ? 11.452 34.419  -21.368 1.00 49.97  ? 64   TYR   A N    1 
ATOM   474   C CA   . TYR   A  1 38  ? 10.588 33.362  -21.892 1.00 50.01  ? 64   TYR   A CA   1 
ATOM   475   C C    . TYR   A  1 38  ? 11.231 31.957  -21.861 1.00 48.48  ? 64   TYR   A C    1 
ATOM   476   O O    . TYR   A  1 38  ? 10.520 30.980  -22.077 1.00 48.75  ? 64   TYR   A O    1 
ATOM   477   C CB   . TYR   A  1 38  ? 10.111 33.712  -23.321 1.00 51.13  ? 64   TYR   A CB   1 
ATOM   478   C CG   . TYR   A  1 38  ? 11.211 34.138  -24.269 1.00 53.13  ? 64   TYR   A CG   1 
ATOM   479   C CD1  . TYR   A  1 38  ? 12.091 33.211  -24.805 1.00 54.37  ? 64   TYR   A CD1  1 
ATOM   480   C CD2  . TYR   A  1 38  ? 11.401 35.476  -24.589 1.00 54.71  ? 64   TYR   A CD2  1 
ATOM   481   C CE1  . TYR   A  1 38  ? 13.124 33.599  -25.647 1.00 55.66  ? 64   TYR   A CE1  1 
ATOM   482   C CE2  . TYR   A  1 38  ? 12.424 35.876  -25.439 1.00 55.93  ? 64   TYR   A CE2  1 
ATOM   483   C CZ   . TYR   A  1 38  ? 13.288 34.934  -25.964 1.00 57.06  ? 64   TYR   A CZ   1 
ATOM   484   O OH   . TYR   A  1 38  ? 14.291 35.337  -26.816 1.00 59.22  ? 64   TYR   A OH   1 
ATOM   485   H H    . TYR   A  1 38  ? 11.987 34.901  -22.082 0.00 71.75  ? 64   TYR   A H    1 
ATOM   486   H HA   . TYR   A  1 38  ? 9.689  33.309  -21.281 0.00 71.90  ? 64   TYR   A HA   1 
ATOM   487   H HB2  . TYR   A  1 38  ? 9.611  32.847  -23.755 0.00 72.72  ? 64   TYR   A HB2  1 
ATOM   488   H HB3  . TYR   A  1 38  ? 9.413  34.545  -23.251 0.00 73.95  ? 64   TYR   A HB3  1 
ATOM   489   H HD1  . TYR   A  1 38  ? 11.981 32.171  -24.553 0.00 75.01  ? 64   TYR   A HD1  1 
ATOM   490   H HD2  . TYR   A  1 38  ? 10.737 36.221  -24.183 0.00 78.66  ? 64   TYR   A HD2  1 
ATOM   491   H HE1  . TYR   A  1 38  ? 13.786 32.854  -26.056 0.00 76.08  ? 64   TYR   A HE1  1 
ATOM   492   H HE2  . TYR   A  1 38  ? 12.543 36.917  -25.689 0.00 79.63  ? 64   TYR   A HE2  1 
ATOM   493   H HH   . TYR   A  1 38  ? 14.732 34.555  -27.239 0.00 80.95  ? 64   TYR   A HH   1 
ATOM   494   N N    . VAL   A  1 39  ? 12.549 31.844  -21.587 1.00 46.58  ? 65   VAL   A N    1 
ATOM   495   C CA   . VAL   A  1 39  ? 13.242 30.550  -21.528 1.00 45.26  ? 65   VAL   A CA   1 
ATOM   496   C C    . VAL   A  1 39  ? 12.579 29.619  -20.501 1.00 43.80  ? 65   VAL   A C    1 
ATOM   497   O O    . VAL   A  1 39  ? 12.284 30.052  -19.391 1.00 44.09  ? 65   VAL   A O    1 
ATOM   498   C CB   . VAL   A  1 39  ? 14.759 30.748  -21.224 1.00 45.98  ? 65   VAL   A CB   1 
ATOM   499   C CG1  . VAL   A  1 39  ? 15.432 29.439  -20.826 1.00 46.53  ? 65   VAL   A CG1  1 
ATOM   500   C CG2  . VAL   A  1 39  ? 15.485 31.379  -22.415 1.00 46.52  ? 65   VAL   A CG2  1 
ATOM   501   H H    . VAL   A  1 39  ? 13.165 32.631  -21.407 0.00 65.80  ? 65   VAL   A H    1 
ATOM   502   H HA   . VAL   A  1 39  ? 13.149 30.076  -22.505 0.00 62.57  ? 65   VAL   A HA   1 
ATOM   503   H HB   . VAL   A  1 39  ? 14.863 31.428  -20.380 0.00 63.79  ? 65   VAL   A HB   1 
ATOM   504   H HG11 . VAL   A  1 39  ? 16.510 29.585  -20.858 0.00 62.71  ? 65   VAL   A HG11 1 
ATOM   505   H HG12 . VAL   A  1 39  ? 15.152 29.170  -19.809 0.00 63.13  ? 65   VAL   A HG12 1 
ATOM   506   H HG13 . VAL   A  1 39  ? 15.140 28.654  -21.522 0.00 62.62  ? 65   VAL   A HG13 1 
ATOM   507   H HG21 . VAL   A  1 39  ? 16.503 31.626  -22.119 0.00 63.69  ? 65   VAL   A HG21 1 
ATOM   508   H HG22 . VAL   A  1 39  ? 15.502 30.665  -23.238 0.00 63.41  ? 65   VAL   A HG22 1 
ATOM   509   H HG23 . VAL   A  1 39  ? 14.960 32.283  -22.720 0.00 64.63  ? 65   VAL   A HG23 1 
ATOM   510   N N    . THR   A  1 40  ? 12.345 28.352  -20.885 1.00 42.30  ? 66   THR   A N    1 
ATOM   511   C CA   . THR   A  1 40  ? 11.730 27.338  -20.023 1.00 41.46  ? 66   THR   A CA   1 
ATOM   512   C C    . THR   A  1 40  ? 12.717 26.227  -19.638 1.00 39.94  ? 66   THR   A C    1 
ATOM   513   O O    . THR   A  1 40  ? 12.459 25.524  -18.675 1.00 40.11  ? 66   THR   A O    1 
ATOM   514   C CB   . THR   A  1 40  ? 10.504 26.726  -20.703 1.00 42.97  ? 66   THR   A CB   1 
ATOM   515   O OG1  . THR   A  1 40  ? 10.920 26.032  -21.879 1.00 43.87  ? 66   THR   A OG1  1 
ATOM   516   C CG2  . THR   A  1 40  ? 9.448  27.765  -21.051 1.00 43.93  ? 66   THR   A CG2  1 
ATOM   517   H H    . THR   A  1 40  ? 12.572 27.993  -21.807 0.00 58.20  ? 66   THR   A H    1 
ATOM   518   H HA   . THR   A  1 40  ? 11.383 27.793  -19.097 0.00 57.93  ? 66   THR   A HA   1 
ATOM   519   H HB   . THR   A  1 40  ? 10.048 26.010  -20.021 0.00 59.28  ? 66   THR   A HB   1 
ATOM   520   H HG1  . THR   A  1 40  ? 10.126 25.684  -22.362 0.00 59.93  ? 66   THR   A HG1  1 
ATOM   521   H HG21 . THR   A  1 40  ? 8.583  27.278  -21.500 0.00 61.63  ? 66   THR   A HG21 1 
ATOM   522   H HG22 . THR   A  1 40  ? 9.127  28.282  -20.149 0.00 62.05  ? 66   THR   A HG22 1 
ATOM   523   H HG23 . THR   A  1 40  ? 9.844  28.493  -21.758 0.00 61.66  ? 66   THR   A HG23 1 
ATOM   524   N N    . GLU   A  1 41  ? 13.805 26.022  -20.397 1.00 38.65  ? 67   GLU   A N    1 
ATOM   525   C CA   . GLU   A  1 41  ? 14.794 24.984  -20.081 1.00 37.76  ? 67   GLU   A CA   1 
ATOM   526   C C    . GLU   A  1 41  ? 16.167 25.615  -20.214 1.00 36.60  ? 67   GLU   A C    1 
ATOM   527   O O    . GLU   A  1 41  ? 16.485 26.166  -21.265 1.00 36.80  ? 67   GLU   A O    1 
ATOM   528   C CB   . GLU   A  1 41  ? 14.653 23.773  -21.019 1.00 39.58  ? 67   GLU   A CB   1 
ATOM   529   C CG   . GLU   A  1 41  ? 13.235 23.218  -21.067 1.00 43.78  ? 67   GLU   A CG   1 
ATOM   530   C CD   . GLU   A  1 41  ? 13.044 21.885  -21.767 1.00 48.45  ? 67   GLU   A CD   1 
ATOM   531   O OE1  . GLU   A  1 41  ? 14.040 21.316  -22.268 1.00 49.48  ? 67   GLU   A OE1  1 
ATOM   532   O OE2  . GLU   A  1 41  ? 11.886 21.411  -21.820 1.00 49.43  ? 67   GLU   A OE2  1 
ATOM   533   H H    . GLU   A  1 41  ? 14.033 26.537  -21.242 0.00 52.52  ? 67   GLU   A H    1 
ATOM   534   H HA   . GLU   A  1 41  ? 14.675 24.632  -19.058 0.00 50.55  ? 67   GLU   A HA   1 
ATOM   535   H HB2  . GLU   A  1 41  ? 14.932 24.084  -22.024 0.00 52.01  ? 67   GLU   A HB2  1 
ATOM   536   H HB3  . GLU   A  1 41  ? 15.319 22.985  -20.671 0.00 51.53  ? 67   GLU   A HB3  1 
ATOM   537   H HG2  . GLU   A  1 41  ? 12.867 23.109  -20.049 0.00 57.66  ? 67   GLU   A HG2  1 
ATOM   538   H HG3  . GLU   A  1 41  ? 12.610 23.936  -21.595 0.00 57.97  ? 67   GLU   A HG3  1 
ATOM   539   N N    . LEU   A  1 42  ? 16.957 25.591  -19.144 1.00 34.89  ? 68   LEU   A N    1 
ATOM   540   C CA   . LEU   A  1 42  ? 18.262 26.224  -19.136 1.00 34.19  ? 68   LEU   A CA   1 
ATOM   541   C C    . LEU   A  1 42  ? 19.336 25.180  -18.918 1.00 32.93  ? 68   LEU   A C    1 
ATOM   542   O O    . LEU   A  1 42  ? 19.339 24.503  -17.890 1.00 33.36  ? 68   LEU   A O    1 
ATOM   543   C CB   . LEU   A  1 42  ? 18.278 27.283  -18.023 1.00 34.88  ? 68   LEU   A CB   1 
ATOM   544   C CG   . LEU   A  1 42  ? 19.566 28.064  -17.761 1.00 36.66  ? 68   LEU   A CG   1 
ATOM   545   C CD1  . LEU   A  1 42  ? 20.136 28.682  -19.036 1.00 37.20  ? 68   LEU   A CD1  1 
ATOM   546   C CD2  . LEU   A  1 42  ? 19.297 29.168  -16.742 1.00 37.29  ? 68   LEU   A CD2  1 
ATOM   547   H H    . LEU   A  1 42  ? 16.725 25.139  -18.265 0.00 46.74  ? 68   LEU   A H    1 
ATOM   548   H HA   . LEU   A  1 42  ? 18.452 26.730  -20.081 0.00 45.84  ? 68   LEU   A HA   1 
ATOM   549   H HB2  . LEU   A  1 42  ? 17.518 28.020  -18.275 0.00 47.91  ? 68   LEU   A HB2  1 
ATOM   550   H HB3  . LEU   A  1 42  ? 18.007 26.794  -17.089 0.00 47.32  ? 68   LEU   A HB3  1 
ATOM   551   H HG   . LEU   A  1 42  ? 20.313 27.393  -17.339 0.00 49.01  ? 68   LEU   A HG   1 
ATOM   552   H HD11 . LEU   A  1 42  ? 20.969 29.332  -18.774 0.00 50.24  ? 68   LEU   A HD11 1 
ATOM   553   H HD12 . LEU   A  1 42  ? 20.487 27.889  -19.695 0.00 49.46  ? 68   LEU   A HD12 1 
ATOM   554   H HD13 . LEU   A  1 42  ? 19.355 29.257  -19.532 0.00 50.55  ? 68   LEU   A HD13 1 
ATOM   555   H HD21 . LEU   A  1 42  ? 20.224 29.703  -16.543 0.00 51.18  ? 68   LEU   A HD21 1 
ATOM   556   H HD22 . LEU   A  1 42  ? 18.555 29.852  -17.150 0.00 51.65  ? 68   LEU   A HD22 1 
ATOM   557   H HD23 . LEU   A  1 42  ? 18.921 28.718  -15.823 0.00 51.18  ? 68   LEU   A HD23 1 
ATOM   558   N N    . ASP   A  1 43  ? 20.219 25.019  -19.912 1.00 31.10  ? 69   ASP   A N    1 
ATOM   559   C CA   . ASP   A  1 43  ? 21.307 24.068  -19.839 1.00 30.02  ? 69   ASP   A CA   1 
ATOM   560   C C    . ASP   A  1 43  ? 22.600 24.804  -19.587 1.00 28.97  ? 69   ASP   A C    1 
ATOM   561   O O    . ASP   A  1 43  ? 23.150 25.390  -20.503 1.00 28.91  ? 69   ASP   A O    1 
ATOM   562   C CB   . ASP   A  1 43  ? 21.384 23.230  -21.127 1.00 30.99  ? 69   ASP   A CB   1 
ATOM   563   C CG   . ASP   A  1 43  ? 22.429 22.124  -21.115 1.00 35.61  ? 69   ASP   A CG   1 
ATOM   564   O OD1  . ASP   A  1 43  ? 23.174 22.009  -20.108 1.00 35.03  ? 69   ASP   A OD1  1 
ATOM   565   O OD2  . ASP   A  1 43  ? 22.494 21.363  -22.100 1.00 37.98  ? 69   ASP   A OD2  1 
ATOM   566   H H    . ASP   A  1 43  ? 20.204 25.536  -20.785 0.00 40.89  ? 69   ASP   A H    1 
ATOM   567   H HA   . ASP   A  1 43  ? 21.144 23.396  -19.003 0.00 38.62  ? 69   ASP   A HA   1 
ATOM   568   H HB2  . ASP   A  1 43  ? 20.416 22.755  -21.280 0.00 39.38  ? 69   ASP   A HB2  1 
ATOM   569   H HB3  . ASP   A  1 43  ? 21.600 23.884  -21.970 0.00 39.44  ? 69   ASP   A HB3  1 
ATOM   570   N N    . LEU   A  1 44  ? 23.089 24.768  -18.352 1.00 28.12  ? 70   LEU   A N    1 
ATOM   571   C CA   . LEU   A  1 44  ? 24.357 25.393  -17.965 1.00 28.47  ? 70   LEU   A CA   1 
ATOM   572   C C    . LEU   A  1 44  ? 25.443 24.360  -17.643 1.00 27.76  ? 70   LEU   A C    1 
ATOM   573   O O    . LEU   A  1 44  ? 26.408 24.695  -16.953 1.00 27.75  ? 70   LEU   A O    1 
ATOM   574   C CB   . LEU   A  1 44  ? 24.127 26.284  -16.732 1.00 28.80  ? 70   LEU   A CB   1 
ATOM   575   C CG   . LEU   A  1 44  ? 23.423 27.602  -16.982 1.00 30.89  ? 70   LEU   A CG   1 
ATOM   576   C CD1  . LEU   A  1 44  ? 22.839 28.130  -15.705 1.00 31.57  ? 70   LEU   A CD1  1 
ATOM   577   C CD2  . LEU   A  1 44  ? 24.387 28.628  -17.549 1.00 31.29  ? 70   LEU   A CD2  1 
ATOM   578   H H    . LEU   A  1 44  ? 22.631 24.299  -17.578 0.00 36.61  ? 70   LEU   A H    1 
ATOM   579   H HA   . LEU   A  1 44  ? 24.737 26.000  -18.783 0.00 37.12  ? 70   LEU   A HA   1 
ATOM   580   H HB2  . LEU   A  1 44  ? 23.540 25.729  -16.003 0.00 38.19  ? 70   LEU   A HB2  1 
ATOM   581   H HB3  . LEU   A  1 44  ? 25.086 26.549  -16.289 0.00 38.20  ? 70   LEU   A HB3  1 
ATOM   582   H HG   . LEU   A  1 44  ? 22.610 27.469  -17.694 0.00 41.44  ? 70   LEU   A HG   1 
ATOM   583   H HD11 . LEU   A  1 44  ? 22.381 29.096  -15.907 0.00 43.53  ? 70   LEU   A HD11 1 
ATOM   584   H HD12 . LEU   A  1 44  ? 22.084 27.436  -15.339 0.00 42.85  ? 70   LEU   A HD12 1 
ATOM   585   H HD13 . LEU   A  1 44  ? 23.632 28.239  -14.966 0.00 42.97  ? 70   LEU   A HD13 1 
ATOM   586   H HD21 . LEU   A  1 44  ? 23.812 29.470  -17.931 0.00 42.65  ? 70   LEU   A HD21 1 
ATOM   587   H HD22 . LEU   A  1 44  ? 25.039 28.970  -16.748 0.00 42.33  ? 70   LEU   A HD22 1 
ATOM   588   H HD23 . LEU   A  1 44  ? 24.991 28.201  -18.348 0.00 41.63  ? 70   LEU   A HD23 1 
ATOM   589   N N    . SER   A  1 45  ? 25.309 23.118  -18.151 1.00 26.94  ? 71   SER   A N    1 
ATOM   590   C CA   . SER   A  1 45  ? 26.257 22.051  -17.862 1.00 27.80  ? 71   SER   A CA   1 
ATOM   591   C C    . SER   A  1 45  ? 27.655 22.322  -18.439 1.00 28.45  ? 71   SER   A C    1 
ATOM   592   O O    . SER   A  1 45  ? 27.787 23.060  -19.402 1.00 28.26  ? 71   SER   A O    1 
ATOM   593   C CB   . SER   A  1 45  ? 25.729 20.710  -18.380 1.00 29.11  ? 71   SER   A CB   1 
ATOM   594   O OG   . SER   A  1 45  ? 25.729 20.654  -19.799 1.00 31.55  ? 71   SER   A OG   1 
ATOM   595   H H    . SER   A  1 45  ? 24.569 22.827  -18.782 0.00 33.89  ? 71   SER   A H    1 
ATOM   596   H HA   . SER   A  1 45  ? 26.360 21.967  -16.781 0.00 34.60  ? 71   SER   A HA   1 
ATOM   597   H HB2  . SER   A  1 45  ? 26.365 19.913  -17.999 0.00 35.13  ? 71   SER   A HB2  1 
ATOM   598   H HB3  . SER   A  1 45  ? 24.710 20.570  -18.022 0.00 35.68  ? 71   SER   A HB3  1 
ATOM   599   H HG   . SER   A  1 45  ? 25.233 21.425  -20.181 0.00 38.47  ? 71   SER   A HG   1 
ATOM   600   N N    . ASP   A  1 46  ? 28.699 21.742  -17.830 1.00 28.90  ? 72   ASP   A N    1 
ATOM   601   C CA   . ASP   A  1 46  ? 30.089 21.867  -18.292 1.00 29.96  ? 72   ASP   A CA   1 
ATOM   602   C C    . ASP   A  1 46  ? 30.624 23.302  -18.360 1.00 30.04  ? 72   ASP   A C    1 
ATOM   603   O O    . ASP   A  1 46  ? 31.321 23.672  -19.309 1.00 29.86  ? 72   ASP   A O    1 
ATOM   604   C CB   . ASP   A  1 46  ? 30.270 21.163  -19.644 1.00 32.96  ? 72   ASP   A CB   1 
ATOM   605   C CG   . ASP   A  1 46  ? 29.841 19.725  -19.612 1.00 40.93  ? 72   ASP   A CG   1 
ATOM   606   O OD1  . ASP   A  1 46  ? 30.542 18.915  -18.969 1.00 42.63  ? 72   ASP   A OD1  1 
ATOM   607   O OD2  . ASP   A  1 46  ? 28.809 19.401  -20.239 1.00 45.16  ? 72   ASP   A OD2  1 
ATOM   608   H H    . ASP   A  1 46  ? 28.609 21.166  -16.999 0.00 35.20  ? 72   ASP   A H    1 
ATOM   609   H HA   . ASP   A  1 46  ? 30.719 21.337  -17.579 0.00 36.16  ? 72   ASP   A HA   1 
ATOM   610   H HB2  . ASP   A  1 46  ? 29.685 21.678  -20.404 0.00 39.48  ? 72   ASP   A HB2  1 
ATOM   611   H HB3  . ASP   A  1 46  ? 31.324 21.172  -19.915 0.00 39.18  ? 72   ASP   A HB3  1 
ATOM   612   N N    . ASN   A  1 47  ? 30.333 24.098  -17.340 1.00 30.30  ? 73   ASN   A N    1 
ATOM   613   C CA   . ASN   A  1 47  ? 30.853 25.460  -17.245 1.00 30.97  ? 73   ASN   A CA   1 
ATOM   614   C C    . ASN   A  1 47  ? 31.781 25.533  -15.992 1.00 32.15  ? 73   ASN   A C    1 
ATOM   615   O O    . ASN   A  1 47  ? 32.188 24.486  -15.485 1.00 32.19  ? 73   ASN   A O    1 
ATOM   616   C CB   . ASN   A  1 47  ? 29.669 26.456  -17.249 1.00 31.52  ? 73   ASN   A CB   1 
ATOM   617   C CG   . ASN   A  1 47  ? 29.172 26.777  -18.639 1.00 33.20  ? 73   ASN   A CG   1 
ATOM   618   O OD1  . ASN   A  1 47  ? 29.937 27.228  -19.496 1.00 33.49  ? 73   ASN   A OD1  1 
ATOM   619   N ND2  . ASN   A  1 47  ? 27.890 26.558  -18.898 1.00 32.86  ? 73   ASN   A ND2  1 
ATOM   620   H H    . ASN   A  1 47  ? 29.749 23.832  -16.554 0.00 37.91  ? 73   ASN   A H    1 
ATOM   621   H HA   . ASN   A  1 47  ? 31.498 25.684  -18.093 0.00 39.02  ? 73   ASN   A HA   1 
ATOM   622   H HB2  . ASN   A  1 47  ? 28.815 26.005  -16.750 0.00 40.45  ? 73   ASN   A HB2  1 
ATOM   623   H HB3  . ASN   A  1 47  ? 29.950 27.386  -16.758 0.00 40.96  ? 73   ASN   A HB3  1 
ATOM   624   H HD21 . ASN   A  1 47  ? 27.528 26.766  -19.823 0.00 42.01  ? 73   ASN   A HD21 1 
ATOM   625   H HD22 . ASN   A  1 47  ? 27.261 26.193  -18.189 0.00 42.08  ? 73   ASN   A HD22 1 
ATOM   626   N N    . PHE   A  1 48  ? 32.195 26.730  -15.563 1.00 33.00  ? 74   PHE   A N    1 
ATOM   627   C CA   . PHE   A  1 48  ? 33.041 26.914  -14.382 1.00 34.29  ? 74   PHE   A CA   1 
ATOM   628   C C    . PHE   A  1 48  ? 32.272 27.593  -13.233 1.00 33.66  ? 74   PHE   A C    1 
ATOM   629   O O    . PHE   A  1 48  ? 32.887 28.292  -12.433 1.00 33.98  ? 74   PHE   A O    1 
ATOM   630   C CB   . PHE   A  1 48  ? 34.278 27.758  -14.748 1.00 35.49  ? 74   PHE   A CB   1 
ATOM   631   C CG   . PHE   A  1 48  ? 35.052 27.283  -15.954 1.00 37.41  ? 74   PHE   A CG   1 
ATOM   632   C CD1  . PHE   A  1 48  ? 35.304 25.937  -16.150 1.00 39.13  ? 74   PHE   A CD1  1 
ATOM   633   C CD2  . PHE   A  1 48  ? 35.658 28.189  -16.807 1.00 39.01  ? 74   PHE   A CD2  1 
ATOM   634   C CE1  . PHE   A  1 48  ? 36.089 25.506  -17.212 1.00 40.12  ? 74   PHE   A CE1  1 
ATOM   635   C CE2  . PHE   A  1 48  ? 36.459 27.754  -17.854 1.00 40.07  ? 74   PHE   A CE2  1 
ATOM   636   C CZ   . PHE   A  1 48  ? 36.648 26.415  -18.064 1.00 39.94  ? 74   PHE   A CZ   1 
ATOM   637   H H    . PHE   A  1 48  ? 31.974 27.603  -16.032 0.00 42.78  ? 74   PHE   A H    1 
ATOM   638   H HA   . PHE   A  1 48  ? 33.401 25.959  -14.005 0.00 43.94  ? 74   PHE   A HA   1 
ATOM   639   H HB2  . PHE   A  1 48  ? 33.955 28.780  -14.940 0.00 46.49  ? 74   PHE   A HB2  1 
ATOM   640   H HB3  . PHE   A  1 48  ? 34.969 27.746  -13.906 0.00 46.20  ? 74   PHE   A HB3  1 
ATOM   641   H HD1  . PHE   A  1 48  ? 34.876 25.207  -15.493 0.00 48.95  ? 74   PHE   A HD1  1 
ATOM   642   H HD2  . PHE   A  1 48  ? 35.517 29.246  -16.652 0.00 50.45  ? 74   PHE   A HD2  1 
ATOM   643   H HE1  . PHE   A  1 48  ? 36.244 24.452  -17.373 0.00 49.31  ? 74   PHE   A HE1  1 
ATOM   644   H HE2  . PHE   A  1 48  ? 36.887 28.469  -18.536 0.00 50.85  ? 74   PHE   A HE2  1 
ATOM   645   H HZ   . PHE   A  1 48  ? 37.247 26.077  -18.892 0.00 49.46  ? 74   PHE   A HZ   1 
ATOM   646   N N    . ILE   A  1 49  ? 30.940 27.422  -13.169 1.00 32.54  ? 75   ILE   A N    1 
ATOM   647   C CA   . ILE   A  1 49  ? 30.120 28.016  -12.113 1.00 31.68  ? 75   ILE   A CA   1 
ATOM   648   C C    . ILE   A  1 49  ? 30.469 27.359  -10.767 1.00 31.40  ? 75   ILE   A C    1 
ATOM   649   O O    . ILE   A  1 49  ? 30.463 26.133  -10.669 1.00 31.17  ? 75   ILE   A O    1 
ATOM   650   C CB   . ILE   A  1 49  ? 28.606 27.878  -12.419 1.00 31.17  ? 75   ILE   A CB   1 
ATOM   651   C CG1  . ILE   A  1 49  ? 28.222 28.570  -13.766 1.00 30.82  ? 75   ILE   A CG1  1 
ATOM   652   C CG2  . ILE   A  1 49  ? 27.785 28.449  -11.266 1.00 31.22  ? 75   ILE   A CG2  1 
ATOM   653   C CD1  . ILE   A  1 49  ? 26.975 28.042  -14.401 1.00 31.17  ? 75   ILE   A CD1  1 
ATOM   654   H H    . ILE   A  1 49  ? 30.396 26.914  -13.858 0.00 42.59  ? 75   ILE   A H    1 
ATOM   655   H HA   . ILE   A  1 49  ? 30.348 29.079  -12.051 0.00 43.16  ? 75   ILE   A HA   1 
ATOM   656   H HB   . ILE   A  1 49  ? 28.382 26.815  -12.495 0.00 41.51  ? 75   ILE   A HB   1 
ATOM   657   H HG12 . ILE   A  1 49  ? 28.062 29.630  -13.571 0.00 42.31  ? 75   ILE   A HG12 1 
ATOM   658   H HG13 . ILE   A  1 49  ? 29.026 28.455  -14.491 0.00 41.32  ? 75   ILE   A HG13 1 
ATOM   659   H HG21 . ILE   A  1 49  ? 26.794 28.721  -11.622 0.00 43.04  ? 75   ILE   A HG21 1 
ATOM   660   H HG22 . ILE   A  1 49  ? 27.687 27.695  -10.487 0.00 42.68  ? 75   ILE   A HG22 1 
ATOM   661   H HG23 . ILE   A  1 49  ? 28.291 29.329  -10.870 0.00 43.34  ? 75   ILE   A HG23 1 
ATOM   662   H HD11 . ILE   A  1 49  ? 26.876 28.485  -15.391 0.00 41.88  ? 75   ILE   A HD11 1 
ATOM   663   H HD12 . ILE   A  1 49  ? 27.053 26.959  -14.484 0.00 41.28  ? 75   ILE   A HD12 1 
ATOM   664   H HD13 . ILE   A  1 49  ? 26.113 28.308  -13.792 0.00 42.29  ? 75   ILE   A HD13 1 
ATOM   665   N N    . THR   A  1 50  ? 30.775 28.181  -9.746  1.00 30.70  ? 76   THR   A N    1 
ATOM   666   C CA   . THR   A  1 50  ? 31.149 27.705  -8.412  1.00 31.02  ? 76   THR   A CA   1 
ATOM   667   C C    . THR   A  1 50  ? 30.076 27.986  -7.352  1.00 30.59  ? 76   THR   A C    1 
ATOM   668   O O    . THR   A  1 50  ? 30.117 27.364  -6.291  1.00 31.05  ? 76   THR   A O    1 
ATOM   669   C CB   . THR   A  1 50  ? 32.478 28.358  -7.994  1.00 32.60  ? 76   THR   A CB   1 
ATOM   670   O OG1  . THR   A  1 50  ? 32.342 29.779  -8.075  1.00 33.29  ? 76   THR   A OG1  1 
ATOM   671   C CG2  . THR   A  1 50  ? 33.658 27.898  -8.855  1.00 33.56  ? 76   THR   A CG2  1 
ATOM   672   H H    . THR   A  1 50  ? 30.768 29.194  -9.812  0.00 42.67  ? 76   THR   A H    1 
ATOM   673   H HA   . THR   A  1 50  ? 31.311 26.629  -8.425  0.00 42.13  ? 76   THR   A HA   1 
ATOM   674   H HB   . THR   A  1 50  ? 32.696 28.075  -6.965  0.00 45.15  ? 76   THR   A HB   1 
ATOM   675   H HG1  . THR   A  1 50  ? 31.977 30.151  -7.229  0.00 47.04  ? 76   THR   A HG1  1 
ATOM   676   H HG21 . THR   A  1 50  ? 34.485 28.597  -8.745  0.00 45.89  ? 76   THR   A HG21 1 
ATOM   677   H HG22 . THR   A  1 50  ? 33.995 26.917  -8.525  0.00 45.12  ? 76   THR   A HG22 1 
ATOM   678   H HG23 . THR   A  1 50  ? 33.378 27.845  -9.906  0.00 45.19  ? 76   THR   A HG23 1 
ATOM   679   N N    . HIS   A  1 51  ? 29.146 28.922  -7.602  1.00 30.16  ? 77   HIS   A N    1 
ATOM   680   C CA   . HIS   A  1 51  ? 28.127 29.286  -6.622  1.00 30.95  ? 77   HIS   A CA   1 
ATOM   681   C C    . HIS   A  1 51  ? 26.742 29.424  -7.235  1.00 31.88  ? 77   HIS   A C    1 
ATOM   682   O O    . HIS   A  1 51  ? 26.603 30.000  -8.319  1.00 32.26  ? 77   HIS   A O    1 
ATOM   683   C CB   . HIS   A  1 51  ? 28.479 30.645  -5.989  1.00 31.47  ? 77   HIS   A CB   1 
ATOM   684   C CG   . HIS   A  1 51  ? 29.682 30.615  -5.102  1.00 32.95  ? 77   HIS   A CG   1 
ATOM   685   N ND1  . HIS   A  1 51  ? 30.966 30.711  -5.620  1.00 34.44  ? 77   HIS   A ND1  1 
ATOM   686   C CD2  . HIS   A  1 51  ? 29.759 30.524  -3.755  1.00 33.70  ? 77   HIS   A CD2  1 
ATOM   687   C CE1  . HIS   A  1 51  ? 31.779 30.662  -4.575  1.00 34.83  ? 77   HIS   A CE1  1 
ATOM   688   N NE2  . HIS   A  1 51  ? 31.096 30.546  -3.432  1.00 34.73  ? 77   HIS   A NE2  1 
ATOM   689   H H    . HIS   A  1 51  ? 29.071 29.455  -8.463  0.00 42.76  ? 77   HIS   A H    1 
ATOM   690   H HA   . HIS   A  1 51  ? 28.075 28.546  -5.825  0.00 44.25  ? 77   HIS   A HA   1 
ATOM   691   H HB2  . HIS   A  1 51  ? 28.672 31.363  -6.785  0.00 46.02  ? 77   HIS   A HB2  1 
ATOM   692   H HB3  . HIS   A  1 51  ? 27.633 30.979  -5.389  0.00 46.43  ? 77   HIS   A HB3  1 
ATOM   693   H HD2  . HIS   A  1 51  ? 28.932 30.450  -3.067  0.00 49.54  ? 77   HIS   A HD2  1 
ATOM   694   H HE1  . HIS   A  1 51  ? 32.853 30.709  -4.638  0.00 50.07  ? 77   HIS   A HE1  1 
ATOM   695   H HE2  . HIS   A  1 51  ? 31.491 30.486  -2.499  0.00 50.78  ? 77   HIS   A HE2  1 
ATOM   696   N N    . ILE   A  1 52  ? 25.715 28.981  -6.484  1.00 31.82  ? 78   ILE   A N    1 
ATOM   697   C CA   . ILE   A  1 52  ? 24.305 29.148  -6.824  1.00 32.31  ? 78   ILE   A CA   1 
ATOM   698   C C    . ILE   A  1 52  ? 23.653 29.765  -5.587  1.00 33.68  ? 78   ILE   A C    1 
ATOM   699   O O    . ILE   A  1 52  ? 23.746 29.196  -4.499  1.00 33.56  ? 78   ILE   A O    1 
ATOM   700   C CB   . ILE   A  1 52  ? 23.582 27.834  -7.195  1.00 32.13  ? 78   ILE   A CB   1 
ATOM   701   C CG1  . ILE   A  1 52  ? 24.299 27.067  -8.337  1.00 32.11  ? 78   ILE   A CG1  1 
ATOM   702   C CG2  . ILE   A  1 52  ? 22.105 28.118  -7.529  1.00 32.33  ? 78   ILE   A CG2  1 
ATOM   703   C CD1  . ILE   A  1 52  ? 24.366 27.777  -9.660  1.00 33.02  ? 78   ILE   A CD1  1 
ATOM   704   H H    . ILE   A  1 52  ? 25.837 28.485  -5.606  0.00 45.66  ? 78   ILE   A H    1 
ATOM   705   H HA   . ILE   A  1 52  ? 24.200 29.844  -7.655  0.00 46.61  ? 78   ILE   A HA   1 
ATOM   706   H HB   . ILE   A  1 52  ? 23.594 27.199  -6.310  0.00 45.52  ? 78   ILE   A HB   1 
ATOM   707   H HG12 . ILE   A  1 52  ? 25.320 26.858  -8.024  0.00 44.45  ? 78   ILE   A HG12 1 
ATOM   708   H HG13 . ILE   A  1 52  ? 23.774 26.127  -8.498  0.00 44.22  ? 78   ILE   A HG13 1 
ATOM   709   H HG21 . ILE   A  1 52  ? 21.766 27.391  -8.265  0.00 45.63  ? 78   ILE   A HG21 1 
ATOM   710   H HG22 . ILE   A  1 52  ? 21.517 28.008  -6.621  0.00 46.53  ? 78   ILE   A HG22 1 
ATOM   711   H HG23 . ILE   A  1 52  ? 22.004 29.127  -7.927  0.00 46.61  ? 78   ILE   A HG23 1 
ATOM   712   H HD11 . ILE   A  1 52  ? 24.870 27.129  -10.375 0.00 45.05  ? 78   ILE   A HD11 1 
ATOM   713   H HD12 . ILE   A  1 52  ? 23.358 27.992  -10.012 0.00 45.90  ? 78   ILE   A HD12 1 
ATOM   714   H HD13 . ILE   A  1 52  ? 24.930 28.702  -9.551  0.00 46.10  ? 78   ILE   A HD13 1 
ATOM   715   N N    . THR   A  1 53  ? 23.011 30.924  -5.747  1.00 34.78  ? 79   THR   A N    1 
ATOM   716   C CA   . THR   A  1 53  ? 22.330 31.623  -4.654  1.00 36.08  ? 79   THR   A CA   1 
ATOM   717   C C    . THR   A  1 53  ? 20.845 31.890  -5.033  1.00 37.01  ? 79   THR   A C    1 
ATOM   718   O O    . THR   A  1 53  ? 20.426 31.561  -6.148  1.00 36.55  ? 79   THR   A O    1 
ATOM   719   C CB   . THR   A  1 53  ? 23.102 32.931  -4.324  1.00 37.94  ? 79   THR   A CB   1 
ATOM   720   O OG1  . THR   A  1 53  ? 22.874 33.888  -5.366  1.00 39.35  ? 79   THR   A OG1  1 
ATOM   721   C CG2  . THR   A  1 53  ? 24.601 32.701  -4.119  1.00 37.97  ? 79   THR   A CG2  1 
ATOM   722   H H    . THR   A  1 53  ? 22.939 31.417  -6.631  0.00 51.08  ? 79   THR   A H    1 
ATOM   723   H HA   . THR   A  1 53  ? 22.322 31.012  -3.752  0.00 53.53  ? 79   THR   A HA   1 
ATOM   724   H HB   . THR   A  1 53  ? 22.705 33.338  -3.394  0.00 57.22  ? 79   THR   A HB   1 
ATOM   725   H HG1  . THR   A  1 53  ? 23.359 34.731  -5.165  0.00 59.02  ? 79   THR   A HG1  1 
ATOM   726   H HG21 . THR   A  1 53  ? 25.057 33.598  -3.703  0.00 56.85  ? 79   THR   A HG21 1 
ATOM   727   H HG22 . THR   A  1 53  ? 24.759 31.869  -3.434  0.00 55.95  ? 79   THR   A HG22 1 
ATOM   728   H HG23 . THR   A  1 53  ? 25.082 32.477  -5.070  0.00 55.64  ? 79   THR   A HG23 1 
ATOM   729   N N    . ASN   A  1 54  ? 20.045 32.478  -4.107  1.00 37.84  ? 80   ASN   A N    1 
ATOM   730   C CA   . ASN   A  1 54  ? 18.656 32.839  -4.411  1.00 39.38  ? 80   ASN   A CA   1 
ATOM   731   C C    . ASN   A  1 54  ? 18.549 33.990  -5.463  1.00 39.83  ? 80   ASN   A C    1 
ATOM   732   O O    . ASN   A  1 54  ? 17.450 34.272  -5.935  1.00 40.37  ? 80   ASN   A O    1 
ATOM   733   C CB   . ASN   A  1 54  ? 17.853 33.158  -3.135  1.00 41.72  ? 80   ASN   A CB   1 
ATOM   734   C CG   . ASN   A  1 54  ? 18.317 34.348  -2.322  1.00 47.01  ? 80   ASN   A CG   1 
ATOM   735   O OD1  . ASN   A  1 54  ? 19.264 35.062  -2.675  1.00 48.85  ? 80   ASN   A OD1  1 
ATOM   736   N ND2  . ASN   A  1 54  ? 17.659 34.574  -1.189  1.00 48.64  ? 80   ASN   A ND2  1 
ATOM   737   H H    . ASN   A  1 54  ? 20.342 32.691  -3.161  0.00 57.34  ? 80   ASN   A H    1 
ATOM   738   H HA   . ASN   A  1 54  ? 18.176 31.968  -4.856  0.00 58.73  ? 80   ASN   A HA   1 
ATOM   739   H HB2  . ASN   A  1 54  ? 16.819 33.345  -3.422  0.00 63.30  ? 80   ASN   A HB2  1 
ATOM   740   H HB3  . ASN   A  1 54  ? 17.891 32.286  -2.483  0.00 62.65  ? 80   ASN   A HB3  1 
ATOM   741   H HD21 . ASN   A  1 54  ? 17.919 35.357  -0.598  0.00 73.69  ? 80   ASN   A HD21 1 
ATOM   742   H HD22 . ASN   A  1 54  ? 16.892 33.967  -0.916  0.00 72.95  ? 80   ASN   A HD22 1 
ATOM   743   N N    . GLU   A  1 55  ? 19.682 34.611  -5.853  1.00 39.62  ? 81   GLU   A N    1 
ATOM   744   C CA   . GLU   A  1 55  ? 19.736 35.639  -6.897  1.00 40.14  ? 81   GLU   A CA   1 
ATOM   745   C C    . GLU   A  1 55  ? 20.210 35.078  -8.264  1.00 39.50  ? 81   GLU   A C    1 
ATOM   746   O O    . GLU   A  1 55  ? 20.170 35.812  -9.253  1.00 39.61  ? 81   GLU   A O    1 
ATOM   747   C CB   . GLU   A  1 55  ? 20.688 36.763  -6.471  1.00 43.62  ? 81   GLU   A CB   1 
ATOM   748   C CG   . GLU   A  1 55  ? 20.226 37.504  -5.226  1.00 50.56  ? 81   GLU   A CG   1 
ATOM   749   C CD   . GLU   A  1 55  ? 21.062 38.726  -4.903  1.00 60.21  ? 81   GLU   A CD   1 
ATOM   750   O OE1  . GLU   A  1 55  ? 20.551 39.621  -4.191  1.00 61.65  ? 81   GLU   A OE1  1 
ATOM   751   O OE2  . GLU   A  1 55  ? 22.225 38.795  -5.368  1.00 63.71  ? 81   GLU   A OE2  1 
ATOM   752   H H    . GLU   A  1 55  ? 20.597 34.431  -5.453  0.00 59.71  ? 81   GLU   A H    1 
ATOM   753   H HA   . GLU   A  1 55  ? 18.754 36.086  -7.041  0.00 61.41  ? 81   GLU   A HA   1 
ATOM   754   H HB2  . GLU   A  1 55  ? 21.671 36.341  -6.271  0.00 65.30  ? 81   GLU   A HB2  1 
ATOM   755   H HB3  . GLU   A  1 55  ? 20.759 37.493  -7.277  0.00 66.01  ? 81   GLU   A HB3  1 
ATOM   756   H HG2  . GLU   A  1 55  ? 19.199 37.833  -5.375  0.00 75.55  ? 81   GLU   A HG2  1 
ATOM   757   H HG3  . GLU   A  1 55  ? 20.279 36.829  -4.373  0.00 74.92  ? 81   GLU   A HG3  1 
ATOM   758   N N    . SER   A  1 56  ? 20.674 33.815  -8.330  1.00 38.49  ? 82   SER   A N    1 
ATOM   759   C CA   . SER   A  1 56  ? 21.175 33.232  -9.582  1.00 38.52  ? 82   SER   A CA   1 
ATOM   760   C C    . SER   A  1 56  ? 20.111 33.128  -10.684 1.00 38.99  ? 82   SER   A C    1 
ATOM   761   O O    . SER   A  1 56  ? 20.392 33.472  -11.831 1.00 39.00  ? 82   SER   A O    1 
ATOM   762   C CB   . SER   A  1 56  ? 21.769 31.850  -9.325  1.00 38.58  ? 82   SER   A CB   1 
ATOM   763   O OG   . SER   A  1 56  ? 22.900 31.915  -8.475  1.00 39.26  ? 82   SER   A OG   1 
ATOM   764   H H    . SER   A  1 56  ? 20.730 33.173  -7.546  0.00 56.83  ? 82   SER   A H    1 
ATOM   765   H HA   . SER   A  1 56  ? 21.973 33.870  -9.961  0.00 56.28  ? 82   SER   A HA   1 
ATOM   766   H HB2  . SER   A  1 56  ? 21.012 31.221  -8.860  0.00 55.27  ? 82   SER   A HB2  1 
ATOM   767   H HB3  . SER   A  1 56  ? 22.071 31.420  -10.279 0.00 54.73  ? 82   SER   A HB3  1 
ATOM   768   H HG   . SER   A  1 56  ? 23.503 32.654  -8.747  0.00 56.34  ? 82   SER   A HG   1 
ATOM   769   N N    . PHE   A  1 57  ? 18.908 32.650  -10.347 1.00 39.31  ? 83   PHE   A N    1 
ATOM   770   C CA   . PHE   A  1 57  ? 17.815 32.500  -11.316 1.00 40.27  ? 83   PHE   A CA   1 
ATOM   771   C C    . PHE   A  1 57  ? 16.674 33.489  -11.017 1.00 42.20  ? 83   PHE   A C    1 
ATOM   772   O O    . PHE   A  1 57  ? 15.511 33.178  -11.267 1.00 41.91  ? 83   PHE   A O    1 
ATOM   773   C CB   . PHE   A  1 57  ? 17.307 31.050  -11.291 1.00 39.29  ? 83   PHE   A CB   1 
ATOM   774   C CG   . PHE   A  1 57  ? 18.408 30.056  -11.577 1.00 39.22  ? 83   PHE   A CG   1 
ATOM   775   C CD1  . PHE   A  1 57  ? 18.903 29.898  -12.861 1.00 39.59  ? 83   PHE   A CD1  1 
ATOM   776   C CD2  . PHE   A  1 57  ? 18.994 29.332  -10.554 1.00 39.58  ? 83   PHE   A CD2  1 
ATOM   777   C CE1  . PHE   A  1 57  ? 19.945 29.019  -13.116 1.00 40.02  ? 83   PHE   A CE1  1 
ATOM   778   C CE2  . PHE   A  1 57  ? 20.038 28.453  -10.814 1.00 39.89  ? 83   PHE   A CE2  1 
ATOM   779   C CZ   . PHE   A  1 57  ? 20.504 28.301  -12.093 1.00 39.76  ? 83   PHE   A CZ   1 
ATOM   780   H H    . PHE   A  1 57  ? 18.657 32.354  -9.408  0.00 57.32  ? 83   PHE   A H    1 
ATOM   781   H HA   . PHE   A  1 57  ? 18.168 32.704  -12.325 0.00 58.07  ? 83   PHE   A HA   1 
ATOM   782   H HB2  . PHE   A  1 57  ? 16.896 30.839  -10.305 0.00 56.69  ? 83   PHE   A HB2  1 
ATOM   783   H HB3  . PHE   A  1 57  ? 16.541 30.920  -12.054 0.00 56.42  ? 83   PHE   A HB3  1 
ATOM   784   H HD1  . PHE   A  1 57  ? 18.475 30.465  -13.670 0.00 55.49  ? 83   PHE   A HD1  1 
ATOM   785   H HD2  . PHE   A  1 57  ? 18.639 29.449  -9.543  0.00 55.92  ? 83   PHE   A HD2  1 
ATOM   786   H HE1  . PHE   A  1 57  ? 20.310 28.895  -14.122 0.00 54.48  ? 83   PHE   A HE1  1 
ATOM   787   H HE2  . PHE   A  1 57  ? 20.474 27.883  -10.010 0.00 54.80  ? 83   PHE   A HE2  1 
ATOM   788   H HZ   . PHE   A  1 57  ? 21.305 27.614  -12.299 0.00 53.67  ? 83   PHE   A HZ   1 
ATOM   789   N N    . GLN   A  1 58  ? 17.019 34.695  -10.530 1.00 43.87  ? 84   GLN   A N    1 
ATOM   790   C CA   . GLN   A  1 58  ? 16.035 35.721  -10.169 1.00 46.02  ? 84   GLN   A CA   1 
ATOM   791   C C    . GLN   A  1 58  ? 15.299 36.205  -11.425 1.00 47.29  ? 84   GLN   A C    1 
ATOM   792   O O    . GLN   A  1 58  ? 15.934 36.481  -12.445 1.00 47.67  ? 84   GLN   A O    1 
ATOM   793   C CB   . GLN   A  1 58  ? 16.735 36.929  -9.485  1.00 48.62  ? 84   GLN   A CB   1 
ATOM   794   C CG   . GLN   A  1 58  ? 16.098 37.408  -8.171  1.00 54.35  ? 84   GLN   A CG   1 
ATOM   795   C CD   . GLN   A  1 58  ? 16.653 38.738  -7.694  1.00 60.99  ? 84   GLN   A CD   1 
ATOM   796   O OE1  . GLN   A  1 58  ? 15.901 39.667  -7.362  1.00 62.31  ? 84   GLN   A OE1  1 
ATOM   797   N NE2  . GLN   A  1 58  ? 17.979 38.871  -7.635  1.00 62.50  ? 84   GLN   A NE2  1 
ATOM   798   H H    . GLN   A  1 58  ? 17.982 34.995  -10.415 0.00 64.40  ? 84   GLN   A H    1 
ATOM   799   H HA   . GLN   A  1 58  ? 15.309 35.266  -9.495  0.00 68.31  ? 84   GLN   A HA   1 
ATOM   800   H HB2  . GLN   A  1 58  ? 17.767 36.675  -9.254  0.00 71.63  ? 84   GLN   A HB2  1 
ATOM   801   H HB3  . GLN   A  1 58  ? 16.719 37.769  -10.178 0.00 72.43  ? 84   GLN   A HB3  1 
ATOM   802   H HG2  . GLN   A  1 58  ? 15.026 37.530  -8.323  0.00 80.35  ? 84   GLN   A HG2  1 
ATOM   803   H HG3  . GLN   A  1 58  ? 16.280 36.667  -7.395  0.00 79.64  ? 84   GLN   A HG3  1 
ATOM   804   H HE21 . GLN   A  1 58  ? 18.596 38.103  -7.878  0.00 89.50  ? 84   GLN   A HE21 1 
ATOM   805   H HE22 . GLN   A  1 58  ? 18.378 39.749  -7.317  0.00 90.94  ? 84   GLN   A HE22 1 
ATOM   806   N N    . GLY   A  1 59  ? 13.975 36.281  -11.346 1.00 47.78  ? 85   GLY   A N    1 
ATOM   807   C CA   . GLY   A  1 59  ? 13.145 36.725  -12.460 1.00 48.67  ? 85   GLY   A CA   1 
ATOM   808   C C    . GLY   A  1 59  ? 13.019 35.745  -13.616 1.00 49.29  ? 85   GLY   A C    1 
ATOM   809   O O    . GLY   A  1 59  ? 12.604 36.150  -14.705 1.00 50.02  ? 85   GLY   A O    1 
ATOM   810   H H    . GLY   A  1 59  ? 13.436 36.048  -10.518 0.00 71.40  ? 85   GLY   A H    1 
ATOM   811   H HA2  . GLY   A  1 59  ? 12.143 36.930  -12.087 0.00 73.24  ? 85   GLY   A HA2  1 
ATOM   812   H HA3  . GLY   A  1 59  ? 13.550 37.656  -12.854 0.00 72.99  ? 85   GLY   A HA3  1 
ATOM   813   N N    . LEU   A  1 60  ? 13.367 34.453  -13.406 1.00 48.55  ? 86   LEU   A N    1 
ATOM   814   C CA   . LEU   A  1 60  ? 13.265 33.428  -14.447 1.00 48.17  ? 86   LEU   A CA   1 
ATOM   815   C C    . LEU   A  1 60  ? 12.208 32.397  -14.011 1.00 47.64  ? 86   LEU   A C    1 
ATOM   816   O O    . LEU   A  1 60  ? 12.481 31.198  -13.964 1.00 47.19  ? 86   LEU   A O    1 
ATOM   817   C CB   . LEU   A  1 60  ? 14.634 32.741  -14.686 1.00 48.33  ? 86   LEU   A CB   1 
ATOM   818   C CG   . LEU   A  1 60  ? 15.816 33.620  -15.100 1.00 49.65  ? 86   LEU   A CG   1 
ATOM   819   C CD1  . LEU   A  1 60  ? 17.065 32.787  -15.270 1.00 50.07  ? 86   LEU   A CD1  1 
ATOM   820   C CD2  . LEU   A  1 60  ? 15.539 34.350  -16.408 1.00 50.43  ? 86   LEU   A CD2  1 
ATOM   821   H H    . LEU   A  1 60  ? 13.714 34.083  -12.527 0.00 70.42  ? 86   LEU   A H    1 
ATOM   822   H HA   . LEU   A  1 60  ? 12.935 33.856  -15.392 0.00 69.52  ? 86   LEU   A HA   1 
ATOM   823   H HB2  . LEU   A  1 60  ? 14.922 32.216  -13.776 0.00 68.24  ? 86   LEU   A HB2  1 
ATOM   824   H HB3  . LEU   A  1 60  ? 14.509 32.030  -15.498 0.00 67.92  ? 86   LEU   A HB3  1 
ATOM   825   H HG   . LEU   A  1 60  ? 16.001 34.363  -14.325 0.00 70.67  ? 86   LEU   A HG   1 
ATOM   826   H HD11 . LEU   A  1 60  ? 17.915 33.450  -15.420 0.00 69.69  ? 86   LEU   A HD11 1 
ATOM   827   H HD12 . LEU   A  1 60  ? 17.215 32.178  -14.380 0.00 69.36  ? 86   LEU   A HD12 1 
ATOM   828   H HD13 . LEU   A  1 60  ? 16.942 32.144  -16.140 0.00 69.07  ? 86   LEU   A HD13 1 
ATOM   829   H HD21 . LEU   A  1 60  ? 16.445 34.864  -16.726 0.00 71.28  ? 86   LEU   A HD21 1 
ATOM   830   H HD22 . LEU   A  1 60  ? 15.238 33.624  -17.162 0.00 70.84  ? 86   LEU   A HD22 1 
ATOM   831   H HD23 . LEU   A  1 60  ? 14.741 35.075  -16.251 0.00 72.14  ? 86   LEU   A HD23 1 
ATOM   832   N N    . GLN   A  1 61  ? 10.991 32.871  -13.713 1.00 47.42  ? 87   GLN   A N    1 
ATOM   833   C CA   . GLN   A  1 61  ? 9.887  32.021  -13.251 1.00 47.40  ? 87   GLN   A CA   1 
ATOM   834   C C    . GLN   A  1 61  ? 9.373  30.999  -14.263 1.00 46.44  ? 87   GLN   A C    1 
ATOM   835   O O    . GLN   A  1 61  ? 8.766  30.014  -13.848 1.00 46.67  ? 87   GLN   A O    1 
ATOM   836   C CB   . GLN   A  1 61  ? 8.711  32.888  -12.760 1.00 49.75  ? 87   GLN   A CB   1 
ATOM   837   C CG   . GLN   A  1 61  ? 9.031  33.740  -11.533 1.00 54.49  ? 87   GLN   A CG   1 
ATOM   838   C CD   . GLN   A  1 61  ? 9.470  32.890  -10.360 1.00 60.34  ? 87   GLN   A CD   1 
ATOM   839   O OE1  . GLN   A  1 61  ? 8.855  31.857  -10.052 1.00 61.94  ? 87   GLN   A OE1  1 
ATOM   840   N NE2  . GLN   A  1 61  ? 10.558 33.277  -9.697  1.00 61.21  ? 87   GLN   A NE2  1 
ATOM   841   H H    . GLN   A  1 61  ? 10.741 33.851  -13.796 0.00 69.88  ? 87   GLN   A H    1 
ATOM   842   H HA   . GLN   A  1 61  ? 10.257 31.434  -12.413 0.00 68.82  ? 87   GLN   A HA   1 
ATOM   843   H HB2  . GLN   A  1 61  ? 8.413  33.562  -13.562 0.00 73.61  ? 87   GLN   A HB2  1 
ATOM   844   H HB3  . GLN   A  1 61  ? 7.877  32.235  -12.506 0.00 73.23  ? 87   GLN   A HB3  1 
ATOM   845   H HG2  . GLN   A  1 61  ? 9.826  34.439  -11.790 0.00 79.59  ? 87   GLN   A HG2  1 
ATOM   846   H HG3  . GLN   A  1 61  ? 8.136  34.285  -11.237 0.00 80.40  ? 87   GLN   A HG3  1 
ATOM   847   H HE21 . GLN   A  1 61  ? 11.066 34.113  -9.969  0.00 87.35  ? 87   GLN   A HE21 1 
ATOM   848   H HE22 . GLN   A  1 61  ? 10.880 32.731  -8.904  0.00 86.80  ? 87   GLN   A HE22 1 
ATOM   849   N N    . ASN   A  1 62  ? 9.595  31.211  -15.567 1.00 45.40  ? 88   ASN   A N    1 
ATOM   850   C CA   . ASN   A  1 62  ? 9.160  30.244  -16.580 1.00 45.11  ? 88   ASN   A CA   1 
ATOM   851   C C    . ASN   A  1 62  ? 10.036 28.970  -16.610 1.00 42.71  ? 88   ASN   A C    1 
ATOM   852   O O    . ASN   A  1 62  ? 9.665  28.020  -17.302 1.00 42.74  ? 88   ASN   A O    1 
ATOM   853   C CB   . ASN   A  1 62  ? 9.121  30.898  -17.981 1.00 48.77  ? 88   ASN   A CB   1 
ATOM   854   C CG   . ASN   A  1 62  ? 7.928  31.723  -18.217 1.00 56.77  ? 88   ASN   A CG   1 
ATOM   855   O OD1  . ASN   A  1 62  ? 6.846  31.147  -18.381 1.00 58.17  ? 88   ASN   A OD1  1 
ATOM   856   N ND2  . ASN   A  1 62  ? 8.004  33.030  -18.436 1.00 61.27  ? 88   ASN   A ND2  1 
ATOM   857   H H    . ASN   A  1 62  ? 10.052 32.033  -15.947 0.00 66.19  ? 88   ASN   A H    1 
ATOM   858   H HA   . ASN   A  1 62  ? 8.153  29.911  -16.334 0.00 65.40  ? 88   ASN   A HA   1 
ATOM   859   H HB2  . ASN   A  1 62  ? 10.002 31.523  -18.121 0.00 69.60  ? 88   ASN   A HB2  1 
ATOM   860   H HB3  . ASN   A  1 62  ? 9.115  30.115  -18.737 0.00 69.07  ? 88   ASN   A HB3  1 
ATOM   861   H HD21 . ASN   A  1 62  ? 7.270  33.251  -17.791 0.00 87.03  ? 88   ASN   A HD21 1 
ATOM   862   H HD22 . ASN   A  1 62  ? 8.869  33.542  -18.574 0.00 86.32  ? 88   ASN   A HD22 1 
ATOM   863   N N    . LEU   A  1 63  ? 11.175 28.932  -15.882 1.00 40.48  ? 89   LEU   A N    1 
ATOM   864   C CA   . LEU   A  1 63  ? 12.037 27.751  -15.909 1.00 39.05  ? 89   LEU   A CA   1 
ATOM   865   C C    . LEU   A  1 63  ? 11.372 26.517  -15.317 1.00 37.16  ? 89   LEU   A C    1 
ATOM   866   O O    . LEU   A  1 63  ? 11.004 26.516  -14.146 1.00 37.05  ? 89   LEU   A O    1 
ATOM   867   C CB   . LEU   A  1 63  ? 13.364 27.983  -15.165 1.00 39.38  ? 89   LEU   A CB   1 
ATOM   868   C CG   . LEU   A  1 63  ? 14.354 28.963  -15.778 1.00 40.48  ? 89   LEU   A CG   1 
ATOM   869   C CD1  . LEU   A  1 63  ? 15.552 29.162  -14.856 1.00 41.07  ? 89   LEU   A CD1  1 
ATOM   870   C CD2  . LEU   A  1 63  ? 14.841 28.505  -17.139 1.00 40.61  ? 89   LEU   A CD2  1 
ATOM   871   H H    . LEU   A  1 63  ? 11.525 29.676  -15.287 0.00 58.36  ? 89   LEU   A H    1 
ATOM   872   H HA   . LEU   A  1 63  ? 12.267 27.537  -16.951 0.00 54.85  ? 89   LEU   A HA   1 
ATOM   873   H HB2  . LEU   A  1 63  ? 13.130 28.342  -14.163 0.00 55.86  ? 89   LEU   A HB2  1 
ATOM   874   H HB3  . LEU   A  1 63  ? 13.876 27.025  -15.086 0.00 54.68  ? 89   LEU   A HB3  1 
ATOM   875   H HG   . LEU   A  1 63  ? 13.842 29.914  -15.914 0.00 57.43  ? 89   LEU   A HG   1 
ATOM   876   H HD11 . LEU   A  1 63  ? 16.195 29.938  -15.268 0.00 57.41  ? 89   LEU   A HD11 1 
ATOM   877   H HD12 . LEU   A  1 63  ? 15.199 29.458  -13.868 0.00 57.78  ? 89   LEU   A HD12 1 
ATOM   878   H HD13 . LEU   A  1 63  ? 16.103 28.225  -14.789 0.00 56.58  ? 89   LEU   A HD13 1 
ATOM   879   H HD21 . LEU   A  1 63  ? 15.679 29.134  -17.435 0.00 56.19  ? 89   LEU   A HD21 1 
ATOM   880   H HD22 . LEU   A  1 63  ? 15.154 27.463  -17.079 0.00 55.54  ? 89   LEU   A HD22 1 
ATOM   881   H HD23 . LEU   A  1 63  ? 14.039 28.618  -17.866 0.00 56.45  ? 89   LEU   A HD23 1 
ATOM   882   N N    . THR   A  1 64  ? 11.251 25.462  -16.133 1.00 35.93  ? 90   THR   A N    1 
ATOM   883   C CA   . THR   A  1 64  ? 10.751 24.147  -15.745 1.00 35.21  ? 90   THR   A CA   1 
ATOM   884   C C    . THR   A  1 64  ? 11.910 23.132  -15.634 1.00 33.65  ? 90   THR   A C    1 
ATOM   885   O O    . THR   A  1 64  ? 11.705 22.067  -15.063 1.00 33.98  ? 90   THR   A O    1 
ATOM   886   C CB   . THR   A  1 64  ? 9.695  23.645  -16.736 1.00 36.82  ? 90   THR   A CB   1 
ATOM   887   O OG1  . THR   A  1 64  ? 10.314 23.325  -17.981 1.00 38.10  ? 90   THR   A OG1  1 
ATOM   888   C CG2  . THR   A  1 64  ? 8.576  24.651  -16.953 1.00 37.47  ? 90   THR   A CG2  1 
ATOM   889   H H    . THR   A  1 64  ? 11.498 25.489  -17.117 0.00 50.35  ? 90   THR   A H    1 
ATOM   890   H HA   . THR   A  1 64  ? 10.247 24.209  -14.784 0.00 49.79  ? 90   THR   A HA   1 
ATOM   891   H HB   . THR   A  1 64  ? 9.246  22.739  -16.333 0.00 51.21  ? 90   THR   A HB   1 
ATOM   892   H HG1  . THR   A  1 64  ? 10.647 24.151  -18.422 0.00 52.48  ? 90   THR   A HG1  1 
ATOM   893   H HG21 . THR   A  1 64  ? 7.785  24.198  -17.549 0.00 53.18  ? 90   THR   A HG21 1 
ATOM   894   H HG22 . THR   A  1 64  ? 8.164  24.964  -15.995 0.00 53.61  ? 90   THR   A HG22 1 
ATOM   895   H HG23 . THR   A  1 64  ? 8.949  25.528  -17.482 0.00 53.30  ? 90   THR   A HG23 1 
ATOM   896   N N    . LYS   A  1 65  ? 13.097 23.423  -16.206 1.00 32.41  ? 91   LYS   A N    1 
ATOM   897   C CA   . LYS   A  1 65  ? 14.225 22.504  -16.179 1.00 31.31  ? 91   LYS   A CA   1 
ATOM   898   C C    . LYS   A  1 65  ? 15.524 23.278  -16.101 1.00 29.98  ? 91   LYS   A C    1 
ATOM   899   O O    . LYS   A  1 65  ? 15.705 24.243  -16.837 1.00 30.72  ? 91   LYS   A O    1 
ATOM   900   C CB   . LYS   A  1 65  ? 14.211 21.623  -17.448 1.00 32.99  ? 91   LYS   A CB   1 
ATOM   901   C CG   . LYS   A  1 65  ? 15.442 20.726  -17.632 1.00 37.69  ? 91   LYS   A CG   1 
ATOM   902   C CD   . LYS   A  1 65  ? 15.250 19.753  -18.783 1.00 42.08  ? 91   LYS   A CD   1 
ATOM   903   C CE   . LYS   A  1 65  ? 16.482 18.919  -19.037 1.00 45.63  ? 91   LYS   A CE   1 
ATOM   904   N NZ   . LYS   A  1 65  ? 16.408 18.214  -20.343 1.00 47.02  ? 91   LYS   A NZ   1 
ATOM   905   H H    . LYS   A  1 65  ? 13.311 24.281  -16.706 0.00 44.86  ? 91   LYS   A H    1 
ATOM   906   H HA   . LYS   A  1 65  ? 14.162 21.853  -15.309 0.00 42.37  ? 91   LYS   A HA   1 
ATOM   907   H HB2  . LYS   A  1 65  ? 13.333 20.980  -17.417 0.00 43.96  ? 91   LYS   A HB2  1 
ATOM   908   H HB3  . LYS   A  1 65  ? 14.157 22.277  -18.316 0.00 44.06  ? 91   LYS   A HB3  1 
ATOM   909   H HG2  . LYS   A  1 65  ? 16.308 21.338  -17.878 0.00 48.60  ? 91   LYS   A HG2  1 
ATOM   910   H HG3  . LYS   A  1 65  ? 15.632 20.159  -16.722 0.00 48.54  ? 91   LYS   A HG3  1 
ATOM   911   H HD2  . LYS   A  1 65  ? 14.428 19.079  -18.546 0.00 53.54  ? 91   LYS   A HD2  1 
ATOM   912   H HD3  . LYS   A  1 65  ? 15.025 20.313  -19.689 0.00 53.65  ? 91   LYS   A HD3  1 
ATOM   913   H HE2  . LYS   A  1 65  ? 17.359 19.565  -19.052 0.00 56.90  ? 91   LYS   A HE2  1 
ATOM   914   H HE3  . LYS   A  1 65  ? 16.580 18.173  -18.249 0.00 56.75  ? 91   LYS   A HE3  1 
ATOM   915   H HZ1  . LYS   A  1 65  ? 17.245 17.657  -20.484 0.00 57.72  ? 91   LYS   A HZ1  1 
ATOM   916   H HZ2  . LYS   A  1 65  ? 15.599 17.601  -20.357 0.00 58.28  ? 91   LYS   A HZ2  1 
ATOM   917   H HZ3  . LYS   A  1 65  ? 16.325 18.887  -21.098 0.00 58.39  ? 91   LYS   A HZ3  1 
ATOM   918   N N    . ILE   A  1 66  ? 16.437 22.838  -15.230 1.00 28.30  ? 92   ILE   A N    1 
ATOM   919   C CA   . ILE   A  1 66  ? 17.770 23.413  -15.122 1.00 27.68  ? 92   ILE   A CA   1 
ATOM   920   C C    . ILE   A  1 66  ? 18.738 22.258  -15.125 1.00 26.88  ? 92   ILE   A C    1 
ATOM   921   O O    . ILE   A  1 66  ? 18.583 21.317  -14.339 1.00 26.77  ? 92   ILE   A O    1 
ATOM   922   C CB   . ILE   A  1 66  ? 17.982 24.291  -13.854 1.00 28.18  ? 92   ILE   A CB   1 
ATOM   923   C CG1  . ILE   A  1 66  ? 17.165 25.591  -13.947 1.00 28.96  ? 92   ILE   A CG1  1 
ATOM   924   C CG2  . ILE   A  1 66  ? 19.493 24.609  -13.671 1.00 28.38  ? 92   ILE   A CG2  1 
ATOM   925   C CD1  . ILE   A  1 66  ? 16.932 26.283  -12.615 1.00 30.37  ? 92   ILE   A CD1  1 
ATOM   926   H H    . ILE   A  1 66  ? 16.285 22.075  -14.579 0.00 38.24  ? 92   ILE   A H    1 
ATOM   927   H HA   . ILE   A  1 66  ? 17.981 24.035  -15.990 0.00 37.55  ? 92   ILE   A HA   1 
ATOM   928   H HB   . ILE   A  1 66  ? 17.642 23.729  -12.986 0.00 38.74  ? 92   ILE   A HB   1 
ATOM   929   H HG12 . ILE   A  1 66  ? 17.694 26.289  -14.593 0.00 40.54  ? 92   ILE   A HG12 1 
ATOM   930   H HG13 . ILE   A  1 66  ? 16.188 25.366  -14.372 0.00 40.63  ? 92   ILE   A HG13 1 
ATOM   931   H HG21 . ILE   A  1 66  ? 19.614 25.464  -13.008 0.00 39.22  ? 92   ILE   A HG21 1 
ATOM   932   H HG22 . ILE   A  1 66  ? 19.993 23.752  -13.224 0.00 38.27  ? 92   ILE   A HG22 1 
ATOM   933   H HG23 . ILE   A  1 66  ? 19.930 24.836  -14.642 0.00 38.46  ? 92   ILE   A HG23 1 
ATOM   934   H HD11 . ILE   A  1 66  ? 16.194 27.068  -12.768 0.00 43.52  ? 92   ILE   A HD11 1 
ATOM   935   H HD12 . ILE   A  1 66  ? 16.565 25.556  -11.892 0.00 42.83  ? 92   ILE   A HD12 1 
ATOM   936   H HD13 . ILE   A  1 66  ? 17.860 26.729  -12.259 0.00 42.94  ? 92   ILE   A HD13 1 
ATOM   937   N N    . ASN   A  1 67  ? 19.775 22.357  -15.959 1.00 26.07  ? 93   ASN   A N    1 
ATOM   938   C CA   . ASN   A  1 67  ? 20.824 21.360  -15.987 1.00 25.26  ? 93   ASN   A CA   1 
ATOM   939   C C    . ASN   A  1 67  ? 22.120 22.067  -15.577 1.00 24.94  ? 93   ASN   A C    1 
ATOM   940   O O    . ASN   A  1 67  ? 22.628 22.909  -16.300 1.00 25.00  ? 93   ASN   A O    1 
ATOM   941   C CB   . ASN   A  1 67  ? 20.900 20.679  -17.369 1.00 25.61  ? 93   ASN   A CB   1 
ATOM   942   C CG   . ASN   A  1 67  ? 22.057 19.733  -17.528 1.00 27.74  ? 93   ASN   A CG   1 
ATOM   943   O OD1  . ASN   A  1 67  ? 22.943 19.649  -16.681 1.00 28.59  ? 93   ASN   A OD1  1 
ATOM   944   N ND2  . ASN   A  1 67  ? 22.073 18.996  -18.627 1.00 27.60  ? 93   ASN   A ND2  1 
ATOM   945   H H    . ASN   A  1 67  ? 19.915 23.110  -16.624 0.00 34.51  ? 93   ASN   A H    1 
ATOM   946   H HA   . ASN   A  1 67  ? 20.625 20.577  -15.258 0.00 32.55  ? 93   ASN   A HA   1 
ATOM   947   H HB2  . ASN   A  1 67  ? 19.989 20.102  -17.512 0.00 32.54  ? 93   ASN   A HB2  1 
ATOM   948   H HB3  . ASN   A  1 67  ? 20.979 21.421  -18.158 0.00 32.67  ? 93   ASN   A HB3  1 
ATOM   949   H HD21 . ASN   A  1 67  ? 22.831 18.339  -18.786 0.00 33.32  ? 93   ASN   A HD21 1 
ATOM   950   H HD22 . ASN   A  1 67  ? 21.329 19.088  -19.311 0.00 33.88  ? 93   ASN   A HD22 1 
ATOM   951   N N    . LEU   A  1 68  ? 22.625 21.749  -14.387 1.00 24.52  ? 94   LEU   A N    1 
ATOM   952   C CA   . LEU   A  1 68  ? 23.873 22.315  -13.871 1.00 24.24  ? 94   LEU   A CA   1 
ATOM   953   C C    . LEU   A  1 68  ? 24.955 21.230  -13.715 1.00 24.60  ? 94   LEU   A C    1 
ATOM   954   O O    . LEU   A  1 68  ? 25.911 21.434  -12.979 1.00 25.50  ? 94   LEU   A O    1 
ATOM   955   C CB   . LEU   A  1 68  ? 23.580 23.022  -12.519 1.00 23.69  ? 94   LEU   A CB   1 
ATOM   956   C CG   . LEU   A  1 68  ? 23.112 24.477  -12.592 1.00 23.96  ? 94   LEU   A CG   1 
ATOM   957   C CD1  . LEU   A  1 68  ? 22.368 24.856  -11.327 1.00 24.20  ? 94   LEU   A CD1  1 
ATOM   958   C CD2  . LEU   A  1 68  ? 24.293 25.426  -12.855 1.00 24.17  ? 94   LEU   A CD2  1 
ATOM   959   H H    . LEU   A  1 68  ? 22.201 21.082  -13.752 0.00 31.80  ? 94   LEU   A H    1 
ATOM   960   H HA   . LEU   A  1 68  ? 24.281 23.040  -14.572 0.00 31.64  ? 94   LEU   A HA   1 
ATOM   961   H HB2  . LEU   A  1 68  ? 22.780 22.475  -12.023 0.00 31.66  ? 94   LEU   A HB2  1 
ATOM   962   H HB3  . LEU   A  1 68  ? 24.467 23.011  -11.889 0.00 31.58  ? 94   LEU   A HB3  1 
ATOM   963   H HG   . LEU   A  1 68  ? 22.415 24.587  -13.422 0.00 32.67  ? 94   LEU   A HG   1 
ATOM   964   H HD11 . LEU   A  1 68  ? 22.205 25.932  -11.317 0.00 34.18  ? 94   LEU   A HD11 1 
ATOM   965   H HD12 . LEU   A  1 68  ? 21.412 24.336  -11.311 0.00 33.62  ? 94   LEU   A HD12 1 
ATOM   966   H HD13 . LEU   A  1 68  ? 22.965 24.562  -10.465 0.00 33.58  ? 94   LEU   A HD13 1 
ATOM   967   H HD21 . LEU   A  1 68  ? 23.923 26.449  -12.886 0.00 33.61  ? 94   LEU   A HD21 1 
ATOM   968   H HD22 . LEU   A  1 68  ? 25.017 25.319  -12.048 0.00 33.06  ? 94   LEU   A HD22 1 
ATOM   969   H HD23 . LEU   A  1 68  ? 24.758 25.173  -13.806 0.00 32.59  ? 94   LEU   A HD23 1 
ATOM   970   N N    . ASN   A  1 69  ? 24.874 20.131  -14.486 1.00 24.35  ? 95   ASN   A N    1 
ATOM   971   C CA   . ASN   A  1 69  ? 25.858 19.052  -14.427 1.00 24.74  ? 95   ASN   A CA   1 
ATOM   972   C C    . ASN   A  1 69  ? 27.268 19.497  -14.726 1.00 25.51  ? 95   ASN   A C    1 
ATOM   973   O O    . ASN   A  1 69  ? 27.480 20.360  -15.572 1.00 24.72  ? 95   ASN   A O    1 
ATOM   974   C CB   . ASN   A  1 69  ? 25.500 17.947  -15.448 1.00 24.97  ? 95   ASN   A CB   1 
ATOM   975   C CG   . ASN   A  1 69  ? 24.222 17.175  -15.188 1.00 26.02  ? 95   ASN   A CG   1 
ATOM   976   O OD1  . ASN   A  1 69  ? 23.730 16.441  -16.061 1.00 27.62  ? 95   ASN   A OD1  1 
ATOM   977   N ND2  . ASN   A  1 69  ? 23.574 17.416  -14.079 1.00 23.16  ? 95   ASN   A ND2  1 
ATOM   978   H H    . ASN   A  1 69  ? 24.154 19.975  -15.183 0.00 30.41  ? 95   ASN   A H    1 
ATOM   979   H HA   . ASN   A  1 69  ? 25.867 18.624  -13.425 0.00 30.48  ? 95   ASN   A HA   1 
ATOM   980   H HB2  . ASN   A  1 69  ? 25.407 18.405  -16.432 0.00 30.10  ? 95   ASN   A HB2  1 
ATOM   981   H HB3  . ASN   A  1 69  ? 26.314 17.225  -15.463 0.00 29.74  ? 95   ASN   A HB3  1 
ATOM   982   H HD21 . ASN   A  1 69  ? 22.729 16.896  -13.880 0.00 28.49  ? 95   ASN   A HD21 1 
ATOM   983   H HD22 . ASN   A  1 69  ? 23.800 18.211  -13.492 0.00 28.80  ? 95   ASN   A HD22 1 
ATOM   984   N N    . HIS   A  1 70  ? 28.247 18.840  -14.083 1.00 26.52  ? 96   HIS   A N    1 
ATOM   985   C CA   . HIS   A  1 70  ? 29.664 19.065  -14.361 1.00 28.36  ? 96   HIS   A CA   1 
ATOM   986   C C    . HIS   A  1 70  ? 30.057 20.542  -14.180 1.00 29.46  ? 96   HIS   A C    1 
ATOM   987   O O    . HIS   A  1 70  ? 30.537 21.187  -15.101 1.00 29.04  ? 96   HIS   A O    1 
ATOM   988   C CB   . HIS   A  1 70  ? 30.025 18.559  -15.780 1.00 30.21  ? 96   HIS   A CB   1 
ATOM   989   C CG   . HIS   A  1 70  ? 29.279 17.336  -16.241 1.00 34.66  ? 96   HIS   A CG   1 
ATOM   990   N ND1  . HIS   A  1 70  ? 29.525 16.085  -15.698 1.00 37.33  ? 96   HIS   A ND1  1 
ATOM   991   C CD2  . HIS   A  1 70  ? 28.377 17.201  -17.244 1.00 36.12  ? 96   HIS   A CD2  1 
ATOM   992   C CE1  . HIS   A  1 70  ? 28.712 15.250  -16.323 1.00 37.75  ? 96   HIS   A CE1  1 
ATOM   993   N NE2  . HIS   A  1 70  ? 28.011 15.874  -17.273 1.00 37.44  ? 96   HIS   A NE2  1 
ATOM   994   H H    . HIS   A  1 70  ? 28.089 18.138  -13.367 0.00 32.12  ? 96   HIS   A H    1 
ATOM   995   H HA   . HIS   A  1 70  ? 30.248 18.485  -13.648 0.00 34.13  ? 96   HIS   A HA   1 
ATOM   996   H HB2  . HIS   A  1 70  ? 29.803 19.335  -16.510 0.00 36.04  ? 96   HIS   A HB2  1 
ATOM   997   H HB3  . HIS   A  1 70  ? 31.087 18.322  -15.806 0.00 35.71  ? 96   HIS   A HB3  1 
ATOM   998   H HD1  . HIS   A  1 70  ? 30.213 15.852  -14.989 0.00 43.75  ? 96   HIS   A HD1  1 
ATOM   999   H HD2  . HIS   A  1 70  ? 28.015 17.982  -17.892 0.00 42.61  ? 96   HIS   A HD2  1 
ATOM   1000  H HE1  . HIS   A  1 70  ? 28.624 14.201  -16.092 0.00 43.71  ? 96   HIS   A HE1  1 
ATOM   1001  N N    . ASN   A  1 71  ? 29.824 21.060  -12.977 1.00 30.57  ? 97   ASN   A N    1 
ATOM   1002  C CA   . ASN   A  1 71  ? 30.135 22.432  -12.586 1.00 32.63  ? 97   ASN   A CA   1 
ATOM   1003  C C    . ASN   A  1 71  ? 30.768 22.443  -11.178 1.00 36.18  ? 97   ASN   A C    1 
ATOM   1004  O O    . ASN   A  1 71  ? 30.110 21.977  -10.252 1.00 36.18  ? 97   ASN   A O    1 
ATOM   1005  C CB   . ASN   A  1 71  ? 28.837 23.252  -12.542 1.00 32.64  ? 97   ASN   A CB   1 
ATOM   1006  C CG   . ASN   A  1 71  ? 28.524 23.987  -13.813 1.00 33.85  ? 97   ASN   A CG   1 
ATOM   1007  O OD1  . ASN   A  1 71  ? 27.578 23.683  -14.546 1.00 35.20  ? 97   ASN   A OD1  1 
ATOM   1008  N ND2  . ASN   A  1 71  ? 29.368 24.932  -14.087 1.00 32.35  ? 97   ASN   A ND2  1 
ATOM   1009  H H    . ASN   A  1 71  ? 29.407 20.508  -12.238 0.00 37.96  ? 97   ASN   A H    1 
ATOM   1010  H HA   . ASN   A  1 71  ? 30.836 22.860  -13.301 0.00 40.95  ? 97   ASN   A HA   1 
ATOM   1011  H HB2  . ASN   A  1 71  ? 27.999 22.587  -12.340 0.00 41.42  ? 97   ASN   A HB2  1 
ATOM   1012  H HB3  . ASN   A  1 71  ? 28.917 23.986  -11.742 0.00 42.08  ? 97   ASN   A HB3  1 
ATOM   1013  H HD21 . ASN   A  1 71  ? 29.266 25.522  -14.901 0.00 41.60  ? 97   ASN   A HD21 1 
ATOM   1014  H HD22 . ASN   A  1 71  ? 30.149 25.074  -13.453 0.00 41.64  ? 97   ASN   A HD22 1 
ATOM   1015  N N    . PRO   A  1 72  ? 31.982 23.000  -10.953 1.00 38.79  ? 98   PRO   A N    1 
ATOM   1016  C CA   . PRO   A  1 72  ? 32.908 23.615  -11.923 1.00 40.89  ? 98   PRO   A CA   1 
ATOM   1017  C C    . PRO   A  1 72  ? 33.588 22.598  -12.843 1.00 43.91  ? 98   PRO   A C    1 
ATOM   1018  O O    . PRO   A  1 72  ? 33.456 21.392  -12.651 1.00 44.39  ? 98   PRO   A O    1 
ATOM   1019  C CB   . PRO   A  1 72  ? 33.926 24.357  -11.028 1.00 41.51  ? 98   PRO   A CB   1 
ATOM   1020  C CG   . PRO   A  1 72  ? 33.410 24.239  -9.603  1.00 41.49  ? 98   PRO   A CG   1 
ATOM   1021  C CD   . PRO   A  1 72  ? 32.560 23.017  -9.595  1.00 39.04  ? 98   PRO   A CD   1 
ATOM   1022  H HA   . PRO   A  1 72  ? 32.391 24.358  -12.528 0.00 51.60  ? 98   PRO   A HA   1 
ATOM   1023  H HB2  . PRO   A  1 72  ? 34.903 23.885  -11.118 0.00 52.41  ? 98   PRO   A HB2  1 
ATOM   1024  H HB3  . PRO   A  1 72  ? 33.979 25.403  -11.328 0.00 53.05  ? 98   PRO   A HB3  1 
ATOM   1025  H HG2  . PRO   A  1 72  ? 34.246 24.137  -8.913  0.00 53.21  ? 98   PRO   A HG2  1 
ATOM   1026  H HG3  . PRO   A  1 72  ? 32.809 25.114  -9.361  0.00 53.57  ? 98   PRO   A HG3  1 
ATOM   1027  H HD2  . PRO   A  1 72  ? 33.172 22.131  -9.431  0.00 49.31  ? 98   PRO   A HD2  1 
ATOM   1028  H HD3  . PRO   A  1 72  ? 31.792 23.118  -8.830  0.00 49.99  ? 98   PRO   A HD3  1 
ATOM   1029  N N    . ASN   A  1 73  ? 34.337 23.098  -13.836 1.00 45.74  ? 99   ASN   A N    1 
ATOM   1030  C CA   . ASN   A  1 73  ? 35.057 22.298  -14.833 1.00 47.87  ? 99   ASN   A CA   1 
ATOM   1031  C C    . ASN   A  1 73  ? 34.089 21.602  -15.795 1.00 49.03  ? 99   ASN   A C    1 
ATOM   1032  O O    . ASN   A  1 73  ? 33.771 22.149  -16.855 1.00 49.59  ? 99   ASN   A O    1 
ATOM   1033  C CB   . ASN   A  1 73  ? 35.999 21.285  -14.169 1.00 49.73  ? 99   ASN   A CB   1 
ATOM   1034  C CG   . ASN   A  1 73  ? 36.969 21.909  -13.194 1.00 54.14  ? 99   ASN   A CG   1 
ATOM   1035  O OD1  . ASN   A  1 73  ? 37.219 23.119  -13.214 1.00 55.75  ? 99   ASN   A OD1  1 
ATOM   1036  N ND2  . ASN   A  1 73  ? 37.546 21.093  -12.320 1.00 55.26  ? 99   ASN   A ND2  1 
ATOM   1037  H H    . ASN   A  1 73  ? 34.481 24.095  -13.954 0.00 56.80  ? 99   ASN   A H    1 
ATOM   1038  H HA   . ASN   A  1 73  ? 35.673 22.969  -15.429 0.00 58.46  ? 99   ASN   A HA   1 
ATOM   1039  H HB2  . ASN   A  1 73  ? 35.409 20.540  -13.637 0.00 60.22  ? 99   ASN   A HB2  1 
ATOM   1040  H HB3  . ASN   A  1 73  ? 36.585 20.798  -14.947 0.00 59.96  ? 99   ASN   A HB3  1 
ATOM   1041  H HD21 . ASN   A  1 73  ? 38.206 21.462  -11.642 0.00 67.81  ? 99   ASN   A HD21 1 
ATOM   1042  H HD22 . ASN   A  1 73  ? 37.332 20.101  -12.329 0.00 67.08  ? 99   ASN   A HD22 1 
ATOM   1043  N N    . GLY   A  1 87  ? 34.124 22.257  -5.652  1.00 38.77  ? 113  GLY   A N    1 
ATOM   1044  C CA   . GLY   A  1 87  ? 32.763 21.822  -5.947  1.00 38.55  ? 113  GLY   A CA   1 
ATOM   1045  C C    . GLY   A  1 87  ? 31.765 22.960  -5.995  1.00 37.76  ? 113  GLY   A C    1 
ATOM   1046  O O    . GLY   A  1 87  ? 32.067 24.077  -5.563  1.00 38.50  ? 113  GLY   A O    1 
ATOM   1047  H HA2  . GLY   A  1 87  ? 32.750 21.314  -6.910  0.00 49.24  ? 113  GLY   A HA2  1 
ATOM   1048  H HA3  . GLY   A  1 87  ? 32.435 21.125  -5.178  0.00 49.78  ? 113  GLY   A HA3  1 
ATOM   1049  N N    . LEU   A  1 88  ? 30.555 22.678  -6.495  1.00 35.92  ? 114  LEU   A N    1 
ATOM   1050  C CA   . LEU   A  1 88  ? 29.488 23.669  -6.592  1.00 34.26  ? 114  LEU   A CA   1 
ATOM   1051  C C    . LEU   A  1 88  ? 28.923 23.941  -5.201  1.00 33.05  ? 114  LEU   A C    1 
ATOM   1052  O O    . LEU   A  1 88  ? 28.527 23.006  -4.502  1.00 32.87  ? 114  LEU   A O    1 
ATOM   1053  C CB   . LEU   A  1 88  ? 28.372 23.147  -7.507  1.00 33.92  ? 114  LEU   A CB   1 
ATOM   1054  C CG   . LEU   A  1 88  ? 27.216 24.111  -7.824  1.00 34.80  ? 114  LEU   A CG   1 
ATOM   1055  C CD1  . LEU   A  1 88  ? 27.716 25.359  -8.555  1.00 34.54  ? 114  LEU   A CD1  1 
ATOM   1056  C CD2  . LEU   A  1 88  ? 26.147 23.416  -8.659  1.00 35.34  ? 114  LEU   A CD2  1 
ATOM   1057  H H    . LEU   A  1 88  ? 30.287 21.764  -6.844  0.00 46.44  ? 114  LEU   A H    1 
ATOM   1058  H HA   . LEU   A  1 88  ? 29.892 24.589  -7.011  0.00 45.64  ? 114  LEU   A HA   1 
ATOM   1059  H HB2  . LEU   A  1 88  ? 28.818 22.848  -8.455  0.00 44.10  ? 114  LEU   A HB2  1 
ATOM   1060  H HB3  . LEU   A  1 88  ? 27.931 22.278  -7.023  0.00 44.43  ? 114  LEU   A HB3  1 
ATOM   1061  H HG   . LEU   A  1 88  ? 26.744 24.432  -6.897  0.00 46.63  ? 114  LEU   A HG   1 
ATOM   1062  H HD11 . LEU   A  1 88  ? 26.935 25.714  -9.225  0.00 46.15  ? 114  LEU   A HD11 1 
ATOM   1063  H HD12 . LEU   A  1 88  ? 27.951 26.127  -7.820  0.00 46.64  ? 114  LEU   A HD12 1 
ATOM   1064  H HD13 . LEU   A  1 88  ? 28.609 25.107  -9.126  0.00 45.65  ? 114  LEU   A HD13 1 
ATOM   1065  H HD21 . LEU   A  1 88  ? 25.265 24.052  -8.707  0.00 46.75  ? 114  LEU   A HD21 1 
ATOM   1066  H HD22 . LEU   A  1 88  ? 26.538 23.254  -9.662  0.00 45.91  ? 114  LEU   A HD22 1 
ATOM   1067  H HD23 . LEU   A  1 88  ? 25.896 22.460  -8.200  0.00 46.10  ? 114  LEU   A HD23 1 
ATOM   1068  N N    . ASN   A  1 89  ? 28.871 25.209  -4.805  1.00 31.78  ? 115  ASN   A N    1 
ATOM   1069  C CA   . ASN   A  1 89  ? 28.335 25.576  -3.496  1.00 30.93  ? 115  ASN   A CA   1 
ATOM   1070  C C    . ASN   A  1 89  ? 26.946 26.200  -3.737  1.00 30.11  ? 115  ASN   A C    1 
ATOM   1071  O O    . ASN   A  1 89  ? 26.829 27.257  -4.350  1.00 29.44  ? 115  ASN   A O    1 
ATOM   1072  C CB   . ASN   A  1 89  ? 29.352 26.450  -2.718  1.00 31.71  ? 115  ASN   A CB   1 
ATOM   1073  C CG   . ASN   A  1 89  ? 28.807 27.423  -1.764  1.00 35.05  ? 115  ASN   A CG   1 
ATOM   1074  O OD1  . ASN   A  1 89  ? 27.647 27.298  -1.327  1.00 35.04  ? 115  ASN   A OD1  1 
ATOM   1075  N ND2  . ASN   A  1 89  ? 29.610 28.345  -1.235  1.00 37.07  ? 115  ASN   A ND2  1 
ATOM   1076  H H    . ASN   A  1 89  ? 29.169 26.001  -5.366  0.00 43.98  ? 115  ASN   A H    1 
ATOM   1077  H HA   . ASN   A  1 89  ? 28.196 24.687  -2.885  0.00 43.36  ? 115  ASN   A HA   1 
ATOM   1078  H HB2  . ASN   A  1 89  ? 30.007 25.787  -2.155  0.00 44.93  ? 115  ASN   A HB2  1 
ATOM   1079  H HB3  . ASN   A  1 89  ? 29.945 27.015  -3.437  0.00 45.05  ? 115  ASN   A HB3  1 
ATOM   1080  H HD21 . ASN   A  1 89  ? 28.900 28.994  -1.502  0.00 53.39  ? 115  ASN   A HD21 1 
ATOM   1081  H HD22 . ASN   A  1 89  ? 30.608 28.397  -1.404  0.00 52.97  ? 115  ASN   A HD22 1 
ATOM   1082  N N    . ILE   A  1 90  ? 25.901 25.489  -3.292  1.00 30.06  ? 116  ILE   A N    1 
ATOM   1083  C CA   . ILE   A  1 90  ? 24.512 25.893  -3.428  1.00 30.74  ? 116  ILE   A CA   1 
ATOM   1084  C C    . ILE   A  1 90  ? 24.012 26.282  -2.039  1.00 32.30  ? 116  ILE   A C    1 
ATOM   1085  O O    . ILE   A  1 90  ? 24.040 25.454  -1.125  1.00 32.56  ? 116  ILE   A O    1 
ATOM   1086  C CB   . ILE   A  1 90  ? 23.659 24.729  -4.000  1.00 30.47  ? 116  ILE   A CB   1 
ATOM   1087  C CG1  . ILE   A  1 90  ? 24.275 24.200  -5.328  1.00 31.22  ? 116  ILE   A CG1  1 
ATOM   1088  C CG2  . ILE   A  1 90  ? 22.197 25.175  -4.186  1.00 30.62  ? 116  ILE   A CG2  1 
ATOM   1089  C CD1  . ILE   A  1 90  ? 23.563 23.029  -5.930  1.00 32.54  ? 116  ILE   A CD1  1 
ATOM   1090  H H    . ILE   A  1 90  ? 25.987 24.597  -2.815  0.00 42.58  ? 116  ILE   A H    1 
ATOM   1091  H HA   . ILE   A  1 90  ? 24.416 26.745  -4.099  0.00 44.22  ? 116  ILE   A HA   1 
ATOM   1092  H HB   . ILE   A  1 90  ? 23.669 23.913  -3.279  0.00 42.94  ? 116  ILE   A HB   1 
ATOM   1093  H HG12 . ILE   A  1 90  ? 24.273 25.000  -6.066  0.00 43.28  ? 116  ILE   A HG12 1 
ATOM   1094  H HG13 . ILE   A  1 90  ? 25.299 23.878  -5.146  0.00 42.89  ? 116  ILE   A HG13 1 
ATOM   1095  H HG21 . ILE   A  1 90  ? 21.615 24.352  -4.596  0.00 43.27  ? 116  ILE   A HG21 1 
ATOM   1096  H HG22 . ILE   A  1 90  ? 21.764 25.455  -3.227  0.00 44.25  ? 116  ILE   A HG22 1 
ATOM   1097  H HG23 . ILE   A  1 90  ? 22.171 26.024  -4.867  0.00 43.88  ? 116  ILE   A HG23 1 
ATOM   1098  H HD11 . ILE   A  1 90  ? 24.278 22.473  -6.535  0.00 43.56  ? 116  ILE   A HD11 1 
ATOM   1099  H HD12 . ILE   A  1 90  ? 23.174 22.398  -5.132  0.00 44.17  ? 116  ILE   A HD12 1 
ATOM   1100  H HD13 . ILE   A  1 90  ? 22.746 23.389  -6.553  0.00 44.26  ? 116  ILE   A HD13 1 
ATOM   1101  N N    . THR   A  1 91  ? 23.522 27.509  -1.889  1.00 32.86  ? 117  THR   A N    1 
ATOM   1102  C CA   . THR   A  1 91  ? 22.998 27.971  -0.605  1.00 34.07  ? 117  THR   A CA   1 
ATOM   1103  C C    . THR   A  1 91  ? 21.610 27.384  -0.345  1.00 34.39  ? 117  THR   A C    1 
ATOM   1104  O O    . THR   A  1 91  ? 20.918 26.970  -1.281  1.00 33.47  ? 117  THR   A O    1 
ATOM   1105  C CB   . THR   A  1 91  ? 22.926 29.495  -0.608  1.00 36.83  ? 117  THR   A CB   1 
ATOM   1106  O OG1  . THR   A  1 91  ? 22.086 29.889  -1.696  1.00 38.84  ? 117  THR   A OG1  1 
ATOM   1107  C CG2  . THR   A  1 91  ? 24.302 30.147  -0.739  1.00 37.38  ? 117  THR   A CG2  1 
ATOM   1108  H H    . THR   A  1 91  ? 23.464 28.198  -2.632  0.00 48.25  ? 117  THR   A H    1 
ATOM   1109  H HA   . THR   A  1 91  ? 23.662 27.667  0.202   0.00 50.49  ? 117  THR   A HA   1 
ATOM   1110  H HB   . THR   A  1 91  ? 22.480 29.829  0.327   0.00 55.28  ? 117  THR   A HB   1 
ATOM   1111  H HG1  . THR   A  1 91  ? 21.892 30.861  -1.635  0.00 57.63  ? 117  THR   A HG1  1 
ATOM   1112  H HG21 . THR   A  1 91  ? 24.208 31.228  -0.650  0.00 56.03  ? 117  THR   A HG21 1 
ATOM   1113  H HG22 . THR   A  1 91  ? 24.965 29.783  0.045   0.00 55.35  ? 117  THR   A HG22 1 
ATOM   1114  H HG23 . THR   A  1 91  ? 24.739 29.914  -1.709  0.00 54.75  ? 117  THR   A HG23 1 
ATOM   1115  N N    . ASP   A  1 92  ? 21.197 27.363  0.935   1.00 35.52  ? 118  ASP   A N    1 
ATOM   1116  C CA   . ASP   A  1 92  ? 19.880 26.874  1.364   1.00 37.29  ? 118  ASP   A CA   1 
ATOM   1117  C C    . ASP   A  1 92  ? 18.786 27.706  0.678   1.00 37.43  ? 118  ASP   A C    1 
ATOM   1118  O O    . ASP   A  1 92  ? 18.821 28.934  0.733   1.00 38.05  ? 118  ASP   A O    1 
ATOM   1119  C CB   . ASP   A  1 92  ? 19.762 26.996  2.904   1.00 41.57  ? 118  ASP   A CB   1 
ATOM   1120  C CG   . ASP   A  1 92  ? 18.474 26.480  3.539   1.00 50.63  ? 118  ASP   A CG   1 
ATOM   1121  O OD1  . ASP   A  1 92  ? 17.559 26.071  2.790   1.00 52.97  ? 118  ASP   A OD1  1 
ATOM   1122  O OD2  . ASP   A  1 92  ? 18.378 26.497  4.793   1.00 54.35  ? 118  ASP   A OD2  1 
ATOM   1123  H H    . ASP   A  1 92  ? 21.774 27.694  1.702   0.00 53.24  ? 118  ASP   A H    1 
ATOM   1124  H HA   . ASP   A  1 92  ? 19.770 25.826  1.089   0.00 54.57  ? 118  ASP   A HA   1 
ATOM   1125  H HB2  . ASP   A  1 92  ? 20.586 26.445  3.355   0.00 60.81  ? 118  ASP   A HB2  1 
ATOM   1126  H HB3  . ASP   A  1 92  ? 19.848 28.049  3.167   0.00 61.76  ? 118  ASP   A HB3  1 
ATOM   1127  N N    . GLY   A  1 93  ? 17.841 27.036  0.033   1.00 37.09  ? 119  GLY   A N    1 
ATOM   1128  C CA   . GLY   A  1 93  ? 16.736 27.694  -0.651  1.00 37.40  ? 119  GLY   A CA   1 
ATOM   1129  C C    . GLY   A  1 93  ? 17.115 28.480  -1.895  1.00 37.73  ? 119  GLY   A C    1 
ATOM   1130  O O    . GLY   A  1 93  ? 16.367 29.373  -2.285  1.00 38.24  ? 119  GLY   A O    1 
ATOM   1131  H H    . GLY   A  1 93  ? 17.804 26.024  -0.037  0.00 54.49  ? 119  GLY   A H    1 
ATOM   1132  H HA2  . GLY   A  1 93  ? 16.005 26.941  -0.942  0.00 55.50  ? 119  GLY   A HA2  1 
ATOM   1133  H HA3  . GLY   A  1 93  ? 16.252 28.381  0.041   0.00 56.60  ? 119  GLY   A HA3  1 
ATOM   1134  N N    . ALA   A  1 94  ? 18.238 28.147  -2.562  1.00 37.45  ? 120  ALA   A N    1 
ATOM   1135  C CA   . ALA   A  1 94  ? 18.649 28.881  -3.764  1.00 37.69  ? 120  ALA   A CA   1 
ATOM   1136  C C    . ALA   A  1 94  ? 17.617 28.787  -4.902  1.00 37.65  ? 120  ALA   A C    1 
ATOM   1137  O O    . ALA   A  1 94  ? 17.389 29.782  -5.591  1.00 38.34  ? 120  ALA   A O    1 
ATOM   1138  C CB   . ALA   A  1 94  ? 19.998 28.391  -4.257  1.00 37.58  ? 120  ALA   A CB   1 
ATOM   1139  H H    . ALA   A  1 94  ? 18.857 27.382  -2.314  0.00 54.48  ? 120  ALA   A H    1 
ATOM   1140  H HA   . ALA   A  1 94  ? 18.759 29.933  -3.506  0.00 55.79  ? 120  ALA   A HA   1 
ATOM   1141  H HB1  . ALA   A  1 94  ? 20.374 29.118  -4.975  0.00 54.26  ? 120  ALA   A HB1  1 
ATOM   1142  H HB2  . ALA   A  1 94  ? 20.686 28.314  -3.415  0.00 54.29  ? 120  ALA   A HB2  1 
ATOM   1143  H HB3  . ALA   A  1 94  ? 19.875 27.419  -4.733  0.00 53.54  ? 120  ALA   A HB3  1 
ATOM   1144  N N    . PHE   A  1 95  ? 17.015 27.605  -5.103  1.00 36.63  ? 121  PHE   A N    1 
ATOM   1145  C CA   . PHE   A  1 95  ? 16.023 27.366  -6.162  1.00 36.40  ? 121  PHE   A CA   1 
ATOM   1146  C C    . PHE   A  1 95  ? 14.571 27.448  -5.659  1.00 37.16  ? 121  PHE   A C    1 
ATOM   1147  O O    . PHE   A  1 95  ? 13.663 27.145  -6.427  1.00 37.05  ? 121  PHE   A O    1 
ATOM   1148  C CB   . PHE   A  1 95  ? 16.227 25.944  -6.743  1.00 35.33  ? 121  PHE   A CB   1 
ATOM   1149  C CG   . PHE   A  1 95  ? 17.587 25.614  -7.287  1.00 34.86  ? 121  PHE   A CG   1 
ATOM   1150  C CD1  . PHE   A  1 95  ? 17.876 25.804  -8.626  1.00 35.35  ? 121  PHE   A CD1  1 
ATOM   1151  C CD2  . PHE   A  1 95  ? 18.511 24.937  -6.513  1.00 34.84  ? 121  PHE   A CD2  1 
ATOM   1152  C CE1  . PHE   A  1 95  ? 19.108 25.433  -9.146  1.00 35.45  ? 121  PHE   A CE1  1 
ATOM   1153  C CE2  . PHE   A  1 95  ? 19.752 24.587  -7.031  1.00 35.34  ? 121  PHE   A CE2  1 
ATOM   1154  C CZ   . PHE   A  1 95  ? 20.043 24.841  -8.343  1.00 35.25  ? 121  PHE   A CZ   1 
ATOM   1155  H H    . PHE   A  1 95  ? 17.198 26.777  -4.545  0.00 52.86  ? 121  PHE   A H    1 
ATOM   1156  H HA   . PHE   A  1 95  ? 16.149 28.079  -6.976  0.00 52.85  ? 121  PHE   A HA   1 
ATOM   1157  H HB2  . PHE   A  1 95  ? 16.077 25.229  -5.938  0.00 50.41  ? 121  PHE   A HB2  1 
ATOM   1158  H HB3  . PHE   A  1 95  ? 15.507 25.767  -7.541  0.00 50.39  ? 121  PHE   A HB3  1 
ATOM   1159  H HD1  . PHE   A  1 95  ? 17.155 26.289  -9.263  0.00 49.66  ? 121  PHE   A HD1  1 
ATOM   1160  H HD2  . PHE   A  1 95  ? 18.304 24.751  -5.472  0.00 49.08  ? 121  PHE   A HD2  1 
ATOM   1161  H HE1  . PHE   A  1 95  ? 19.340 25.637  -10.179 0.00 48.58  ? 121  PHE   A HE1  1 
ATOM   1162  H HE2  . PHE   A  1 95  ? 20.480 24.104  -6.404  0.00 48.50  ? 121  PHE   A HE2  1 
ATOM   1163  H HZ   . PHE   A  1 95  ? 20.997 24.549  -8.751  0.00 47.77  ? 121  PHE   A HZ   1 
ATOM   1164  N N    . LEU   A  1 96  ? 14.343 27.818  -4.386  1.00 38.18  ? 122  LEU   A N    1 
ATOM   1165  C CA   . LEU   A  1 96  ? 13.007 27.834  -3.785  1.00 39.21  ? 122  LEU   A CA   1 
ATOM   1166  C C    . LEU   A  1 96  ? 12.006 28.736  -4.506  1.00 40.40  ? 122  LEU   A C    1 
ATOM   1167  O O    . LEU   A  1 96  ? 10.837 28.367  -4.606  1.00 40.49  ? 122  LEU   A O    1 
ATOM   1168  C CB   . LEU   A  1 96  ? 13.110 28.229  -2.296  1.00 39.21  ? 122  LEU   A CB   1 
ATOM   1169  C CG   . LEU   A  1 96  ? 11.870 27.991  -1.422  1.00 40.58  ? 122  LEU   A CG   1 
ATOM   1170  C CD1  . LEU   A  1 96  ? 11.543 26.501  -1.312  1.00 40.78  ? 122  LEU   A CD1  1 
ATOM   1171  C CD2  . LEU   A  1 96  ? 12.080 28.567  -0.033  1.00 40.98  ? 122  LEU   A CD2  1 
ATOM   1172  H H    . LEU   A  1 96  ? 15.069 28.139  -3.754  0.00 56.38  ? 122  LEU   A H    1 
ATOM   1173  H HA   . LEU   A  1 96  ? 12.620 26.818  -3.843  0.00 57.74  ? 122  LEU   A HA   1 
ATOM   1174  H HB2  . LEU   A  1 96  ? 13.924 27.666  -1.843  0.00 58.42  ? 122  LEU   A HB2  1 
ATOM   1175  H HB3  . LEU   A  1 96  ? 13.338 29.293  -2.245  0.00 59.40  ? 122  LEU   A HB3  1 
ATOM   1176  H HG   . LEU   A  1 96  ? 11.009 28.492  -1.861  0.00 61.59  ? 122  LEU   A HG   1 
ATOM   1177  H HD11 . LEU   A  1 96  ? 10.839 26.351  -0.495  0.00 61.20  ? 122  LEU   A HD11 1 
ATOM   1178  H HD12 . LEU   A  1 96  ? 11.087 26.163  -2.242  0.00 60.38  ? 122  LEU   A HD12 1 
ATOM   1179  H HD13 . LEU   A  1 96  ? 12.461 25.947  -1.122  0.00 60.15  ? 122  LEU   A HD13 1 
ATOM   1180  H HD21 . LEU   A  1 96  ? 11.170 28.436  0.551   0.00 62.87  ? 122  LEU   A HD21 1 
ATOM   1181  H HD22 . LEU   A  1 96  ? 12.906 28.043  0.446   0.00 61.97  ? 122  LEU   A HD22 1 
ATOM   1182  H HD23 . LEU   A  1 96  ? 12.316 29.627  -0.118  0.00 62.87  ? 122  LEU   A HD23 1 
ATOM   1183  N N    . ASN   A  1 97  ? 12.448 29.900  -5.010  1.00 41.49  ? 123  ASN   A N    1 
ATOM   1184  C CA   . ASN   A  1 97  ? 11.556 30.854  -5.687  1.00 42.94  ? 123  ASN   A CA   1 
ATOM   1185  C C    . ASN   A  1 97  ? 11.060 30.388  -7.073  1.00 43.19  ? 123  ASN   A C    1 
ATOM   1186  O O    . ASN   A  1 97  ? 10.129 30.987  -7.603  1.00 43.78  ? 123  ASN   A O    1 
ATOM   1187  C CB   . ASN   A  1 97  ? 12.218 32.252  -5.784  1.00 45.37  ? 123  ASN   A CB   1 
ATOM   1188  C CG   . ASN   A  1 97  ? 13.068 32.502  -7.024  1.00 50.97  ? 123  ASN   A CG   1 
ATOM   1189  O OD1  . ASN   A  1 97  ? 12.773 33.395  -7.832  1.00 53.15  ? 123  ASN   A OD1  1 
ATOM   1190  N ND2  . ASN   A  1 97  ? 14.129 31.721  -7.212  1.00 52.10  ? 123  ASN   A ND2  1 
ATOM   1191  H H    . ASN   A  1 97  ? 13.414 30.206  -4.966  0.00 61.74  ? 123  ASN   A H    1 
ATOM   1192  H HA   . ASN   A  1 97  ? 10.669 30.978  -5.068  0.00 64.97  ? 123  ASN   A HA   1 
ATOM   1193  H HB2  . ASN   A  1 97  ? 11.425 32.998  -5.788  0.00 68.62  ? 123  ASN   A HB2  1 
ATOM   1194  H HB3  . ASN   A  1 97  ? 12.851 32.410  -4.912  0.00 67.96  ? 123  ASN   A HB3  1 
ATOM   1195  H HD21 . ASN   A  1 97  ? 14.720 31.857  -8.026  0.00 74.04  ? 123  ASN   A HD21 1 
ATOM   1196  H HD22 . ASN   A  1 97  ? 14.348 30.991  -6.542  0.00 74.10  ? 123  ASN   A HD22 1 
ATOM   1197  N N    . LEU   A  1 98  ? 11.693 29.371  -7.674  1.00 42.62  ? 124  LEU   A N    1 
ATOM   1198  C CA   . LEU   A  1 98  ? 11.304 28.878  -8.997  1.00 42.46  ? 124  LEU   A CA   1 
ATOM   1199  C C    . LEU   A  1 98  ? 10.111 27.926  -8.842  1.00 42.66  ? 124  LEU   A C    1 
ATOM   1200  O O    . LEU   A  1 98  ? 10.282 26.720  -8.635  1.00 43.10  ? 124  LEU   A O    1 
ATOM   1201  C CB   . LEU   A  1 98  ? 12.500 28.181  -9.658  1.00 42.37  ? 124  LEU   A CB   1 
ATOM   1202  C CG   . LEU   A  1 98  ? 13.760 29.037  -9.816  1.00 43.19  ? 124  LEU   A CG   1 
ATOM   1203  C CD1  . LEU   A  1 98  ? 14.903 28.192  -10.342 1.00 43.44  ? 124  LEU   A CD1  1 
ATOM   1204  C CD2  . LEU   A  1 98  ? 13.509 30.243  -10.724 1.00 43.32  ? 124  LEU   A CD2  1 
ATOM   1205  H H    . LEU   A  1 98  ? 12.478 28.864  -7.279  0.00 61.97  ? 124  LEU   A H    1 
ATOM   1206  H HA   . LEU   A  1 98  ? 11.000 29.705  -9.636  0.00 62.21  ? 124  LEU   A HA   1 
ATOM   1207  H HB2  . LEU   A  1 98  ? 12.781 27.315  -9.060  0.00 60.20  ? 124  LEU   A HB2  1 
ATOM   1208  H HB3  . LEU   A  1 98  ? 12.201 27.855  -10.653 0.00 60.32  ? 124  LEU   A HB3  1 
ATOM   1209  H HG   . LEU   A  1 98  ? 14.062 29.415  -8.841  0.00 61.92  ? 124  LEU   A HG   1 
ATOM   1210  H HD11 . LEU   A  1 98  ? 15.765 28.825  -10.544 0.00 60.83  ? 124  LEU   A HD11 1 
ATOM   1211  H HD12 . LEU   A  1 98  ? 15.159 27.444  -9.594  0.00 60.54  ? 124  LEU   A HD12 1 
ATOM   1212  H HD13 . LEU   A  1 98  ? 14.570 27.703  -11.256 0.00 60.46  ? 124  LEU   A HD13 1 
ATOM   1213  H HD21 . LEU   A  1 98  ? 14.461 30.716  -10.963 0.00 62.12  ? 124  LEU   A HD21 1 
ATOM   1214  H HD22 . LEU   A  1 98  ? 13.022 29.905  -11.638 0.00 62.03  ? 124  LEU   A HD22 1 
ATOM   1215  H HD23 . LEU   A  1 98  ? 12.873 30.958  -10.204 0.00 63.06  ? 124  LEU   A HD23 1 
ATOM   1216  N N    . LYS   A  1 99  ? 8.898  28.482  -8.957  1.00 42.03  ? 125  LYS   A N    1 
ATOM   1217  C CA   . LYS   A  1 99  ? 7.645  27.766  -8.718  1.00 42.08  ? 125  LYS   A CA   1 
ATOM   1218  C C    . LYS   A  1 99  ? 7.232  26.726  -9.764  1.00 41.12  ? 125  LYS   A C    1 
ATOM   1219  O O    . LYS   A  1 99  ? 6.415  25.875  -9.420  1.00 41.34  ? 125  LYS   A O    1 
ATOM   1220  C CB   . LYS   A  1 99  ? 6.499  28.769  -8.514  1.00 45.28  ? 125  LYS   A CB   1 
ATOM   1221  C CG   . LYS   A  1 99  ? 6.671  29.641  -7.269  1.00 51.23  ? 125  LYS   A CG   1 
ATOM   1222  C CD   . LYS   A  1 99  ? 6.231  28.939  -5.978  1.00 57.25  ? 125  LYS   A CD   1 
ATOM   1223  C CE   . LYS   A  1 99  ? 4.740  29.038  -5.748  1.00 62.72  ? 125  LYS   A CE   1 
ATOM   1224  N NZ   . LYS   A  1 99  ? 4.332  28.382  -4.478  1.00 66.01  ? 125  LYS   A NZ   1 
ATOM   1225  H H    . LYS   A  1 99  ? 8.755  29.451  -9.224  0.00 62.64  ? 125  LYS   A H    1 
ATOM   1226  H HA   . LYS   A  1 99  ? 7.769  27.215  -7.788  0.00 62.27  ? 125  LYS   A HA   1 
ATOM   1227  H HB2  . LYS   A  1 99  ? 6.439  29.427  -9.380  0.00 67.57  ? 125  LYS   A HB2  1 
ATOM   1228  H HB3  . LYS   A  1 99  ? 5.568  28.215  -8.410  0.00 67.56  ? 125  LYS   A HB3  1 
ATOM   1229  H HG2  . LYS   A  1 99  ? 7.716  29.923  -7.155  0.00 74.99  ? 125  LYS   A HG2  1 
ATOM   1230  H HG3  . LYS   A  1 99  ? 6.063  30.537  -7.386  0.00 76.08  ? 125  LYS   A HG3  1 
ATOM   1231  H HD2  . LYS   A  1 99  ? 6.486  27.881  -6.017  0.00 81.96  ? 125  LYS   A HD2  1 
ATOM   1232  H HD3  . LYS   A  1 99  ? 6.731  29.411  -5.134  0.00 82.97  ? 125  LYS   A HD3  1 
ATOM   1233  H HE2  . LYS   A  1 99  ? 4.456  30.088  -5.692  0.00 90.91  ? 125  LYS   A HE2  1 
ATOM   1234  H HE3  . LYS   A  1 99  ? 4.208  28.552  -6.565  0.00 89.89  ? 125  LYS   A HE3  1 
ATOM   1235  H HZ1  . LYS   A  1 99  ? 3.328  28.466  -4.352  0.00 94.90  ? 125  LYS   A HZ1  1 
ATOM   1236  H HZ2  . LYS   A  1 99  ? 4.581  27.399  -4.499  0.00 93.61  ? 125  LYS   A HZ2  1 
ATOM   1237  H HZ3  . LYS   A  1 99  ? 4.799  28.826  -3.693  0.00 94.54  ? 125  LYS   A HZ3  1 
ATOM   1238  N N    . ASN   A  1 100 ? 7.746  26.772  -11.009 1.00 40.23  ? 126  ASN   A N    1 
ATOM   1239  C CA   . ASN   A  1 100 ? 7.421  25.750  -12.023 1.00 40.04  ? 126  ASN   A CA   1 
ATOM   1240  C C    . ASN   A  1 100 ? 8.631  24.830  -12.312 1.00 38.62  ? 126  ASN   A C    1 
ATOM   1241  O O    . ASN   A  1 100 ? 8.591  24.100  -13.299 1.00 38.31  ? 126  ASN   A O    1 
ATOM   1242  C CB   . ASN   A  1 100 ? 6.919  26.407  -13.337 1.00 42.36  ? 126  ASN   A CB   1 
ATOM   1243  C CG   . ASN   A  1 100 ? 6.185  25.456  -14.300 1.00 47.00  ? 126  ASN   A CG   1 
ATOM   1244  O OD1  . ASN   A  1 100 ? 6.402  24.222  -14.309 1.00 47.51  ? 126  ASN   A OD1  1 
ATOM   1245  N ND2  . ASN   A  1 100 ? 5.303  26.006  -15.151 1.00 47.87  ? 126  ASN   A ND2  1 
ATOM   1246  H H    . ASN   A  1 100 ? 8.372  27.495  -11.349 0.00 59.03  ? 126  ASN   A H    1 
ATOM   1247  H HA   . ASN   A  1 100 ? 6.614  25.109  -11.672 0.00 58.32  ? 126  ASN   A HA   1 
ATOM   1248  H HB2  . ASN   A  1 100 ? 6.235  27.213  -13.077 0.00 62.11  ? 126  ASN   A HB2  1 
ATOM   1249  H HB3  . ASN   A  1 100 ? 7.777  26.815  -13.870 0.00 60.98  ? 126  ASN   A HB3  1 
ATOM   1250  H HD21 . ASN   A  1 100 ? 4.796  25.418  -15.804 0.00 68.07  ? 126  ASN   A HD21 1 
ATOM   1251  H HD22 . ASN   A  1 100 ? 5.147  27.009  -15.147 0.00 68.81  ? 126  ASN   A HD22 1 
ATOM   1252  N N    . LEU   A  1 101 ? 9.690  24.840  -11.469 1.00 37.49  ? 127  LEU   A N    1 
ATOM   1253  C CA   . LEU   A  1 101 ? 10.852 23.989  -11.704 1.00 36.67  ? 127  LEU   A CA   1 
ATOM   1254  C C    . LEU   A  1 101 ? 10.449 22.539  -11.461 1.00 36.15  ? 127  LEU   A C    1 
ATOM   1255  O O    . LEU   A  1 101 ? 10.020 22.204  -10.362 1.00 36.42  ? 127  LEU   A O    1 
ATOM   1256  C CB   . LEU   A  1 101 ? 12.026 24.387  -10.799 1.00 36.60  ? 127  LEU   A CB   1 
ATOM   1257  C CG   . LEU   A  1 101 ? 13.354 23.668  -11.079 1.00 37.22  ? 127  LEU   A CG   1 
ATOM   1258  C CD1  . LEU   A  1 101 ? 13.918 24.057  -12.443 1.00 37.36  ? 127  LEU   A CD1  1 
ATOM   1259  C CD2  . LEU   A  1 101 ? 14.363 23.958  -9.979  1.00 37.84  ? 127  LEU   A CD2  1 
ATOM   1260  H H    . LEU   A  1 101 ? 9.770  25.403  -10.629 0.00 54.18  ? 127  LEU   A H    1 
ATOM   1261  H HA   . LEU   A  1 101 ? 11.177 24.111  -12.735 0.00 51.50  ? 127  LEU   A HA   1 
ATOM   1262  H HB2  . LEU   A  1 101 ? 12.200 25.456  -10.913 0.00 52.06  ? 127  LEU   A HB2  1 
ATOM   1263  H HB3  . LEU   A  1 101 ? 11.750 24.177  -9.767  0.00 51.89  ? 127  LEU   A HB3  1 
ATOM   1264  H HG   . LEU   A  1 101 ? 13.193 22.591  -11.085 0.00 51.02  ? 127  LEU   A HG   1 
ATOM   1265  H HD11 . LEU   A  1 101 ? 14.964 23.757  -12.492 0.00 50.75  ? 127  LEU   A HD11 1 
ATOM   1266  H HD12 . LEU   A  1 101 ? 13.361 23.539  -13.223 0.00 51.07  ? 127  LEU   A HD12 1 
ATOM   1267  H HD13 . LEU   A  1 101 ? 13.834 25.134  -12.577 0.00 51.79  ? 127  LEU   A HD13 1 
ATOM   1268  H HD21 . LEU   A  1 101 ? 15.277 23.399  -10.176 0.00 51.62  ? 127  LEU   A HD21 1 
ATOM   1269  H HD22 . LEU   A  1 101 ? 14.579 25.026  -9.969  0.00 52.68  ? 127  LEU   A HD22 1 
ATOM   1270  H HD23 . LEU   A  1 101 ? 13.944 23.655  -9.021  0.00 52.50  ? 127  LEU   A HD23 1 
ATOM   1271  N N    . ARG   A  1 102 ? 10.548 21.701  -12.497 1.00 35.09  ? 128  ARG   A N    1 
ATOM   1272  C CA   . ARG   A  1 102 ? 10.189 20.292  -12.464 1.00 34.80  ? 128  ARG   A CA   1 
ATOM   1273  C C    . ARG   A  1 102 ? 11.418 19.388  -12.511 1.00 33.38  ? 128  ARG   A C    1 
ATOM   1274  O O    . ARG   A  1 102 ? 11.445 18.366  -11.834 1.00 33.44  ? 128  ARG   A O    1 
ATOM   1275  C CB   . ARG   A  1 102 ? 9.276  19.953  -13.662 1.00 36.80  ? 128  ARG   A CB   1 
ATOM   1276  C CG   . ARG   A  1 102 ? 7.973  20.749  -13.738 1.00 41.83  ? 128  ARG   A CG   1 
ATOM   1277  C CD   . ARG   A  1 102 ? 7.015  20.367  -12.634 1.00 47.65  ? 128  ARG   A CD   1 
ATOM   1278  N NE   . ARG   A  1 102 ? 5.799  21.180  -12.629 1.00 53.68  ? 128  ARG   A NE   1 
ATOM   1279  C CZ   . ARG   A  1 102 ? 4.884  21.157  -11.662 1.00 57.43  ? 128  ARG   A CZ   1 
ATOM   1280  N NH1  . ARG   A  1 102 ? 5.035  20.353  -10.609 1.00 56.96  ? 128  ARG   A NH1  1 
ATOM   1281  N NH2  . ARG   A  1 102 ? 3.808  21.931  -11.739 1.00 58.43  ? 128  ARG   A NH2  1 
ATOM   1282  H H    . ARG   A  1 102 ? 10.887 21.985  -13.411 0.00 48.60  ? 128  ARG   A H    1 
ATOM   1283  H HA   . ARG   A  1 102 ? 9.660  20.061  -11.542 0.00 48.35  ? 128  ARG   A HA   1 
ATOM   1284  H HB2  . ARG   A  1 102 ? 9.830  20.141  -14.581 0.00 50.11  ? 128  ARG   A HB2  1 
ATOM   1285  H HB3  . ARG   A  1 102 ? 9.015  18.897  -13.610 0.00 50.15  ? 128  ARG   A HB3  1 
ATOM   1286  H HG2  . ARG   A  1 102 ? 8.183  21.815  -13.653 0.00 57.78  ? 128  ARG   A HG2  1 
ATOM   1287  H HG3  . ARG   A  1 102 ? 7.486  20.541  -14.689 0.00 57.36  ? 128  ARG   A HG3  1 
ATOM   1288  H HD2  . ARG   A  1 102 ? 6.730  19.322  -12.752 0.00 64.54  ? 128  ARG   A HD2  1 
ATOM   1289  H HD3  . ARG   A  1 102 ? 7.481  20.524  -11.664 0.00 64.86  ? 128  ARG   A HD3  1 
ATOM   1290  H HE   . ARG   A  1 102 ? 5.649  21.805  -13.415 0.00 73.25  ? 128  ARG   A HE   1 
ATOM   1291  H HH11 . ARG   A  1 102 ? 5.838  19.738  -10.515 0.00 76.76  ? 128  ARG   A HH11 1 
ATOM   1292  H HH12 . ARG   A  1 102 ? 4.324  20.340  -9.886  0.00 77.91  ? 128  ARG   A HH12 1 
ATOM   1293  H HH21 . ARG   A  1 102 ? 3.678  22.549  -12.533 0.00 80.48  ? 128  ARG   A HH21 1 
ATOM   1294  H HH22 . ARG   A  1 102 ? 3.110  21.914  -11.003 0.00 80.79  ? 128  ARG   A HH22 1 
ATOM   1295  N N    . GLU   A  1 103 ? 12.414 19.730  -13.330 1.00 32.23  ? 129  GLU   A N    1 
ATOM   1296  C CA   . GLU   A  1 103 ? 13.597 18.894  -13.490 1.00 31.36  ? 129  GLU   A CA   1 
ATOM   1297  C C    . GLU   A  1 103 ? 14.854 19.639  -13.078 1.00 30.55  ? 129  GLU   A C    1 
ATOM   1298  O O    . GLU   A  1 103 ? 15.104 20.726  -13.579 1.00 31.38  ? 129  GLU   A O    1 
ATOM   1299  C CB   . GLU   A  1 103 ? 13.675 18.423  -14.949 1.00 33.12  ? 129  GLU   A CB   1 
ATOM   1300  C CG   . GLU   A  1 103 ? 14.783 17.419  -15.239 1.00 38.34  ? 129  GLU   A CG   1 
ATOM   1301  C CD   . GLU   A  1 103 ? 14.733 16.801  -16.629 1.00 45.76  ? 129  GLU   A CD   1 
ATOM   1302  O OE1  . GLU   A  1 103 ? 13.746 17.038  -17.365 1.00 47.52  ? 129  GLU   A OE1  1 
ATOM   1303  O OE2  . GLU   A  1 103 ? 15.689 16.075  -16.983 1.00 47.32  ? 129  GLU   A OE2  1 
ATOM   1304  H H    . GLU   A  1 103 ? 12.429 20.567  -13.904 0.00 43.84  ? 129  GLU   A H    1 
ATOM   1305  H HA   . GLU   A  1 103 ? 13.523 17.999  -12.875 0.00 41.59  ? 129  GLU   A HA   1 
ATOM   1306  H HB2  . GLU   A  1 103 ? 12.725 17.949  -15.191 0.00 43.54  ? 129  GLU   A HB2  1 
ATOM   1307  H HB3  . GLU   A  1 103 ? 13.819 19.289  -15.592 0.00 43.56  ? 129  GLU   A HB3  1 
ATOM   1308  H HG2  . GLU   A  1 103 ? 15.747 17.917  -15.148 0.00 48.72  ? 129  GLU   A HG2  1 
ATOM   1309  H HG3  . GLU   A  1 103 ? 14.720 16.609  -14.514 0.00 48.73  ? 129  GLU   A HG3  1 
ATOM   1310  N N    . LEU   A  1 104 ? 15.652 19.051  -12.171 1.00 28.82  ? 130  LEU   A N    1 
ATOM   1311  C CA   . LEU   A  1 104 ? 16.899 19.641  -11.712 1.00 27.79  ? 130  LEU   A CA   1 
ATOM   1312  C C    . LEU   A  1 104 ? 18.001 18.593  -11.786 1.00 26.50  ? 130  LEU   A C    1 
ATOM   1313  O O    . LEU   A  1 104 ? 17.943 17.575  -11.095 1.00 26.19  ? 130  LEU   A O    1 
ATOM   1314  C CB   . LEU   A  1 104 ? 16.735 20.165  -10.271 1.00 28.31  ? 130  LEU   A CB   1 
ATOM   1315  C CG   . LEU   A  1 104 ? 17.942 20.869  -9.630  1.00 29.86  ? 130  LEU   A CG   1 
ATOM   1316  C CD1  . LEU   A  1 104 ? 18.513 21.993  -10.528 1.00 30.11  ? 130  LEU   A CD1  1 
ATOM   1317  C CD2  . LEU   A  1 104 ? 17.549 21.441  -8.272  1.00 30.48  ? 130  LEU   A CD2  1 
ATOM   1318  H H    . LEU   A  1 104 ? 15.457 18.156  -11.734 0.00 38.18  ? 130  LEU   A H    1 
ATOM   1319  H HA   . LEU   A  1 104 ? 17.173 20.475  -12.355 0.00 37.16  ? 130  LEU   A HA   1 
ATOM   1320  H HB2  . LEU   A  1 104 ? 15.914 20.880  -10.269 0.00 38.84  ? 130  LEU   A HB2  1 
ATOM   1321  H HB3  . LEU   A  1 104 ? 16.480 19.323  -9.630  0.00 38.20  ? 130  LEU   A HB3  1 
ATOM   1322  H HG   . LEU   A  1 104 ? 18.733 20.141  -9.463  0.00 39.77  ? 130  LEU   A HG   1 
ATOM   1323  H HD11 . LEU   A  1 104 ? 19.237 22.571  -9.957  0.00 40.82  ? 130  LEU   A HD11 1 
ATOM   1324  H HD12 . LEU   A  1 104 ? 19.005 21.546  -11.391 0.00 40.08  ? 130  LEU   A HD12 1 
ATOM   1325  H HD13 . LEU   A  1 104 ? 17.697 22.636  -10.857 0.00 41.06  ? 130  LEU   A HD13 1 
ATOM   1326  H HD21 . LEU   A  1 104 ? 18.409 21.944  -7.831  0.00 41.80  ? 130  LEU   A HD21 1 
ATOM   1327  H HD22 . LEU   A  1 104 ? 16.736 22.151  -8.409  0.00 42.22  ? 130  LEU   A HD22 1 
ATOM   1328  H HD23 . LEU   A  1 104 ? 17.226 20.626  -7.627  0.00 41.64  ? 130  LEU   A HD23 1 
ATOM   1329  N N    . LEU   A  1 105 ? 18.990 18.824  -12.664 1.00 25.66  ? 131  LEU   A N    1 
ATOM   1330  C CA   . LEU   A  1 105 ? 20.088 17.898  -12.840 1.00 25.26  ? 131  LEU   A CA   1 
ATOM   1331  C C    . LEU   A  1 105 ? 21.328 18.528  -12.226 1.00 25.01  ? 131  LEU   A C    1 
ATOM   1332  O O    . LEU   A  1 105 ? 21.746 19.605  -12.638 1.00 24.54  ? 131  LEU   A O    1 
ATOM   1333  C CB   . LEU   A  1 105 ? 20.283 17.554  -14.342 1.00 25.44  ? 131  LEU   A CB   1 
ATOM   1334  C CG   . LEU   A  1 105 ? 19.024 17.264  -15.147 1.00 27.04  ? 131  LEU   A CG   1 
ATOM   1335  C CD1  . LEU   A  1 105 ? 19.371 16.966  -16.597 1.00 27.35  ? 131  LEU   A CD1  1 
ATOM   1336  C CD2  . LEU   A  1 105 ? 18.251 16.087  -14.543 1.00 27.58  ? 131  LEU   A CD2  1 
ATOM   1337  H H    . LEU   A  1 105 ? 19.053 19.642  -13.260 0.00 33.52  ? 131  LEU   A H    1 
ATOM   1338  H HA   . LEU   A  1 105 ? 19.886 16.960  -12.328 0.00 32.06  ? 131  LEU   A HA   1 
ATOM   1339  H HB2  . LEU   A  1 105 ? 20.855 18.334  -14.840 0.00 31.95  ? 131  LEU   A HB2  1 
ATOM   1340  H HB3  . LEU   A  1 105 ? 20.817 16.608  -14.392 0.00 31.46  ? 131  LEU   A HB3  1 
ATOM   1341  H HG   . LEU   A  1 105 ? 18.375 18.138  -15.140 0.00 34.41  ? 131  LEU   A HG   1 
ATOM   1342  H HD11 . LEU   A  1 105 ? 18.452 16.783  -17.152 0.00 33.94  ? 131  LEU   A HD11 1 
ATOM   1343  H HD12 . LEU   A  1 105 ? 19.896 17.822  -17.018 0.00 33.90  ? 131  LEU   A HD12 1 
ATOM   1344  H HD13 . LEU   A  1 105 ? 20.010 16.085  -16.631 0.00 33.36  ? 131  LEU   A HD13 1 
ATOM   1345  H HD21 . LEU   A  1 105 ? 17.433 15.827  -15.214 0.00 34.56  ? 131  LEU   A HD21 1 
ATOM   1346  H HD22 . LEU   A  1 105 ? 18.921 15.236  -14.428 0.00 34.08  ? 131  LEU   A HD22 1 
ATOM   1347  H HD23 . LEU   A  1 105 ? 17.848 16.379  -13.574 0.00 34.93  ? 131  LEU   A HD23 1 
ATOM   1348  N N    . LEU   A  1 106 ? 21.893 17.872  -11.209 1.00 25.18  ? 132  LEU   A N    1 
ATOM   1349  C CA   . LEU   A  1 106 ? 23.057 18.366  -10.489 1.00 25.78  ? 132  LEU   A CA   1 
ATOM   1350  C C    . LEU   A  1 106 ? 24.096 17.250  -10.348 1.00 26.11  ? 132  LEU   A C    1 
ATOM   1351  O O    . LEU   A  1 106 ? 24.620 17.006  -9.265  1.00 26.98  ? 132  LEU   A O    1 
ATOM   1352  C CB   . LEU   A  1 106 ? 22.637 18.889  -9.099  1.00 25.85  ? 132  LEU   A CB   1 
ATOM   1353  C CG   . LEU   A  1 106 ? 21.811 20.162  -9.048  1.00 28.06  ? 132  LEU   A CG   1 
ATOM   1354  C CD1  . LEU   A  1 106 ? 21.122 20.292  -7.690  1.00 28.69  ? 132  LEU   A CD1  1 
ATOM   1355  C CD2  . LEU   A  1 106 ? 22.682 21.398  -9.275  1.00 29.04  ? 132  LEU   A CD2  1 
ATOM   1356  H H    . LEU   A  1 106 ? 21.562 16.981  -10.853 0.00 31.92  ? 132  LEU   A H    1 
ATOM   1357  H HA   . LEU   A  1 106 ? 23.539 19.169  -11.043 0.00 32.95  ? 132  LEU   A HA   1 
ATOM   1358  H HB2  . LEU   A  1 106 ? 22.059 18.111  -8.604  0.00 33.62  ? 132  LEU   A HB2  1 
ATOM   1359  H HB3  . LEU   A  1 106 ? 23.535 19.099  -8.521  0.00 33.71  ? 132  LEU   A HB3  1 
ATOM   1360  H HG   . LEU   A  1 106 ? 21.044 20.133  -9.822  0.00 36.91  ? 132  LEU   A HG   1 
ATOM   1361  H HD11 . LEU   A  1 106 ? 20.625 21.259  -7.638  0.00 38.85  ? 132  LEU   A HD11 1 
ATOM   1362  H HD12 . LEU   A  1 106 ? 20.392 19.491  -7.584  0.00 38.21  ? 132  LEU   A HD12 1 
ATOM   1363  H HD13 . LEU   A  1 106 ? 21.874 20.218  -6.906  0.00 38.36  ? 132  LEU   A HD13 1 
ATOM   1364  H HD21 . LEU   A  1 106 ? 22.038 22.265  -9.413  0.00 38.85  ? 132  LEU   A HD21 1 
ATOM   1365  H HD22 . LEU   A  1 106 ? 23.309 21.540  -8.398  0.00 38.58  ? 132  LEU   A HD22 1 
ATOM   1366  H HD23 . LEU   A  1 106 ? 23.313 21.255  -10.150 0.00 37.95  ? 132  LEU   A HD23 1 
ATOM   1367  N N    . GLU   A  1 107 ? 24.413 16.599  -11.451 1.00 25.35  ? 133  GLU   A N    1 
ATOM   1368  C CA   . GLU   A  1 107 ? 25.374 15.511  -11.464 1.00 25.32  ? 133  GLU   A CA   1 
ATOM   1369  C C    . GLU   A  1 107 ? 26.808 16.002  -11.532 1.00 25.80  ? 133  GLU   A C    1 
ATOM   1370  O O    . GLU   A  1 107 ? 27.070 17.030  -12.138 1.00 26.03  ? 133  GLU   A O    1 
ATOM   1371  C CB   . GLU   A  1 107 ? 25.118 14.594  -12.662 1.00 25.46  ? 133  GLU   A CB   1 
ATOM   1372  C CG   . GLU   A  1 107 ? 23.675 14.125  -12.779 1.00 26.87  ? 133  GLU   A CG   1 
ATOM   1373  C CD   . GLU   A  1 107 ? 23.425 13.164  -13.921 1.00 28.55  ? 133  GLU   A CD   1 
ATOM   1374  O OE1  . GLU   A  1 107 ? 24.395 12.796  -14.626 1.00 29.10  ? 133  GLU   A OE1  1 
ATOM   1375  O OE2  . GLU   A  1 107 ? 22.248 12.791  -14.123 1.00 27.60  ? 133  GLU   A OE2  1 
ATOM   1376  H H    . GLU   A  1 107 ? 24.007 16.780  -12.361 0.00 31.16  ? 133  GLU   A H    1 
ATOM   1377  H HA   . GLU   A  1 107 ? 25.258 14.909  -10.564 0.00 30.79  ? 133  GLU   A HA   1 
ATOM   1378  H HB2  . GLU   A  1 107 ? 25.371 15.129  -13.576 0.00 30.25  ? 133  GLU   A HB2  1 
ATOM   1379  H HB3  . GLU   A  1 107 ? 25.755 13.717  -12.560 0.00 30.03  ? 133  GLU   A HB3  1 
ATOM   1380  H HG2  . GLU   A  1 107 ? 23.371 13.658  -11.844 0.00 32.30  ? 133  GLU   A HG2  1 
ATOM   1381  H HG3  . GLU   A  1 107 ? 23.029 14.980  -12.970 0.00 32.48  ? 133  GLU   A HG3  1 
ATOM   1382  N N    . ASP   A  1 108 ? 27.737 15.238  -10.947 1.00 25.79  ? 134  ASP   A N    1 
ATOM   1383  C CA   . ASP   A  1 108 ? 29.164 15.523  -11.033 1.00 26.51  ? 134  ASP   A CA   1 
ATOM   1384  C C    . ASP   A  1 108 ? 29.518 16.925  -10.544 1.00 26.52  ? 134  ASP   A C    1 
ATOM   1385  O O    . ASP   A  1 108 ? 30.248 17.660  -11.211 1.00 26.83  ? 134  ASP   A O    1 
ATOM   1386  C CB   . ASP   A  1 108 ? 29.623 15.297  -12.481 1.00 29.06  ? 134  ASP   A CB   1 
ATOM   1387  C CG   . ASP   A  1 108 ? 31.120 15.233  -12.676 1.00 36.03  ? 134  ASP   A CG   1 
ATOM   1388  O OD1  . ASP   A  1 108 ? 31.842 14.997  -11.676 1.00 37.66  ? 134  ASP   A OD1  1 
ATOM   1389  O OD2  . ASP   A  1 108 ? 31.574 15.410  -13.831 1.00 39.01  ? 134  ASP   A OD2  1 
ATOM   1390  H H    . ASP   A  1 108 ? 27.528 14.406  -10.405 0.00 30.93  ? 134  ASP   A H    1 
ATOM   1391  H HA   . ASP   A  1 108 ? 29.680 14.813  -10.389 0.00 31.68  ? 134  ASP   A HA   1 
ATOM   1392  H HB2  . ASP   A  1 108 ? 29.205 14.354  -12.829 0.00 34.01  ? 134  ASP   A HB2  1 
ATOM   1393  H HB3  . ASP   A  1 108 ? 29.240 16.107  -13.099 0.00 34.44  ? 134  ASP   A HB3  1 
ATOM   1394  N N    . ASN   A  1 109 ? 29.004 17.282  -9.368  1.00 25.88  ? 135  ASN   A N    1 
ATOM   1395  C CA   . ASN   A  1 109 ? 29.228 18.596  -8.781  1.00 26.31  ? 135  ASN   A CA   1 
ATOM   1396  C C    . ASN   A  1 109 ? 29.958 18.540  -7.427  1.00 26.77  ? 135  ASN   A C    1 
ATOM   1397  O O    . ASN   A  1 109 ? 30.043 19.571  -6.770  1.00 26.64  ? 135  ASN   A O    1 
ATOM   1398  C CB   . ASN   A  1 109 ? 27.868 19.293  -8.603  1.00 27.32  ? 135  ASN   A CB   1 
ATOM   1399  C CG   . ASN   A  1 109 ? 27.185 19.721  -9.875  1.00 31.11  ? 135  ASN   A CG   1 
ATOM   1400  O OD1  . ASN   A  1 109 ? 25.976 19.577  -10.029 1.00 33.36  ? 135  ASN   A OD1  1 
ATOM   1401  N ND2  . ASN   A  1 109 ? 27.885 20.364  -10.750 1.00 30.47  ? 135  ASN   A ND2  1 
ATOM   1402  H H    . ASN   A  1 109 ? 28.433 16.674  -8.789  0.00 32.08  ? 135  ASN   A H    1 
ATOM   1403  H HA   . ASN   A  1 109 ? 29.856 19.200  -9.432  0.00 33.13  ? 135  ASN   A HA   1 
ATOM   1404  H HB2  . ASN   A  1 109 ? 27.190 18.569  -8.156  0.00 34.80  ? 135  ASN   A HB2  1 
ATOM   1405  H HB3  . ASN   A  1 109 ? 27.963 20.168  -7.963  0.00 35.35  ? 135  ASN   A HB3  1 
ATOM   1406  H HD21 . ASN   A  1 109 ? 27.450 20.665  -11.616 0.00 38.34  ? 135  ASN   A HD21 1 
ATOM   1407  H HD22 . ASN   A  1 109 ? 28.814 20.686  -10.501 0.00 38.48  ? 135  ASN   A HD22 1 
ATOM   1408  N N    . GLN   A  1 110 ? 30.467 17.363  -7.001  1.00 27.37  ? 136  GLN   A N    1 
ATOM   1409  C CA   . GLN   A  1 110 ? 31.124 17.196  -5.700  1.00 28.78  ? 136  GLN   A CA   1 
ATOM   1410  C C    . GLN   A  1 110 ? 30.275 17.728  -4.536  1.00 28.81  ? 136  GLN   A C    1 
ATOM   1411  O O    . GLN   A  1 110 ? 30.834 18.237  -3.567  1.00 29.20  ? 136  GLN   A O    1 
ATOM   1412  C CB   . GLN   A  1 110 ? 32.523 17.845  -5.698  1.00 32.04  ? 136  GLN   A CB   1 
ATOM   1413  C CG   . GLN   A  1 110 ? 33.459 17.265  -6.767  1.00 38.77  ? 136  GLN   A CG   1 
ATOM   1414  C CD   . GLN   A  1 110 ? 34.927 17.425  -6.436  1.00 47.49  ? 136  GLN   A CD   1 
ATOM   1415  O OE1  . GLN   A  1 110 ? 35.316 18.082  -5.465  1.00 50.77  ? 136  GLN   A OE1  1 
ATOM   1416  N NE2  . GLN   A  1 110 ? 35.787 16.808  -7.236  1.00 49.44  ? 136  GLN   A NE2  1 
ATOM   1417  H H    . GLN   A  1 110 ? 30.455 16.503  -7.539  0.00 34.02  ? 136  GLN   A H    1 
ATOM   1418  H HA   . GLN   A  1 110 ? 31.269 16.131  -5.529  0.00 36.23  ? 136  GLN   A HA   1 
ATOM   1419  H HB2  . GLN   A  1 110 ? 32.422 18.913  -5.881  0.00 40.88  ? 136  GLN   A HB2  1 
ATOM   1420  H HB3  . GLN   A  1 110 ? 32.983 17.670  -4.726  0.00 40.85  ? 136  GLN   A HB3  1 
ATOM   1421  H HG2  . GLN   A  1 110 ? 33.256 16.201  -6.876  0.00 47.70  ? 136  GLN   A HG2  1 
ATOM   1422  H HG3  . GLN   A  1 110 ? 33.274 17.774  -7.712  0.00 47.91  ? 136  GLN   A HG3  1 
ATOM   1423  H HE21 . GLN   A  1 110 ? 35.447 16.262  -8.021  0.00 60.12  ? 136  GLN   A HE21 1 
ATOM   1424  H HE22 . GLN   A  1 110 ? 36.784 16.880  -7.062  0.00 60.67  ? 136  GLN   A HE22 1 
ATOM   1425  N N    . LEU   A  1 111 ? 28.934 17.619  -4.623  1.00 27.78  ? 137  LEU   A N    1 
ATOM   1426  C CA   . LEU   A  1 111 ? 28.069 18.117  -3.552  1.00 27.83  ? 137  LEU   A CA   1 
ATOM   1427  C C    . LEU   A  1 111 ? 28.264 17.286  -2.282  1.00 28.30  ? 137  LEU   A C    1 
ATOM   1428  O O    . LEU   A  1 111 ? 28.239 16.062  -2.353  1.00 27.76  ? 137  LEU   A O    1 
ATOM   1429  C CB   . LEU   A  1 111 ? 26.591 18.067  -3.970  1.00 27.85  ? 137  LEU   A CB   1 
ATOM   1430  C CG   . LEU   A  1 111 ? 26.198 18.969  -5.143  1.00 29.34  ? 137  LEU   A CG   1 
ATOM   1431  C CD1  . LEU   A  1 111 ? 24.795 18.661  -5.617  1.00 29.87  ? 137  LEU   A CD1  1 
ATOM   1432  C CD2  . LEU   A  1 111 ? 26.320 20.429  -4.795  1.00 30.34  ? 137  LEU   A CD2  1 
ATOM   1433  H H    . LEU   A  1 111 ? 28.432 17.188  -5.391  0.00 35.62  ? 137  LEU   A H    1 
ATOM   1434  H HA   . LEU   A  1 111 ? 28.339 19.153  -3.357  0.00 37.12  ? 137  LEU   A HA   1 
ATOM   1435  H HB2  . LEU   A  1 111 ? 26.345 17.044  -4.253  0.00 36.30  ? 137  LEU   A HB2  1 
ATOM   1436  H HB3  . LEU   A  1 111 ? 25.983 18.355  -3.114  0.00 37.21  ? 137  LEU   A HB3  1 
ATOM   1437  H HG   . LEU   A  1 111 ? 26.891 18.775  -5.959  0.00 38.04  ? 137  LEU   A HG   1 
ATOM   1438  H HD11 . LEU   A  1 111 ? 24.547 19.319  -6.448  0.00 39.06  ? 137  LEU   A HD11 1 
ATOM   1439  H HD12 . LEU   A  1 111 ? 24.752 17.623  -5.942  0.00 38.58  ? 137  LEU   A HD12 1 
ATOM   1440  H HD13 . LEU   A  1 111 ? 24.101 18.820  -4.794  0.00 39.50  ? 137  LEU   A HD13 1 
ATOM   1441  H HD21 . LEU   A  1 111 ? 25.825 21.022  -5.562  0.00 40.38  ? 137  LEU   A HD21 1 
ATOM   1442  H HD22 . LEU   A  1 111 ? 25.852 20.603  -3.827  0.00 40.82  ? 137  LEU   A HD22 1 
ATOM   1443  H HD23 . LEU   A  1 111 ? 27.373 20.705  -4.758  0.00 40.33  ? 137  LEU   A HD23 1 
ATOM   1444  N N    . PRO   A  1 112 ? 28.469 17.920  -1.111  1.00 28.87  ? 138  PRO   A N    1 
ATOM   1445  C CA   . PRO   A  1 112 ? 28.622 17.137  0.128   1.00 28.79  ? 138  PRO   A CA   1 
ATOM   1446  C C    . PRO   A  1 112 ? 27.301 16.679  0.750   1.00 29.03  ? 138  PRO   A C    1 
ATOM   1447  O O    . PRO   A  1 112 ? 27.306 15.803  1.614   1.00 29.08  ? 138  PRO   A O    1 
ATOM   1448  C CB   . PRO   A  1 112 ? 29.321 18.121  1.058   1.00 29.83  ? 138  PRO   A CB   1 
ATOM   1449  C CG   . PRO   A  1 112 ? 28.752 19.454  0.657   1.00 30.58  ? 138  PRO   A CG   1 
ATOM   1450  C CD   . PRO   A  1 112 ? 28.515 19.371  -0.839  1.00 28.72  ? 138  PRO   A CD   1 
ATOM   1451  H HA   . PRO   A  1 112 ? 29.273 16.277  -0.022  0.00 38.51  ? 138  PRO   A HA   1 
ATOM   1452  H HB2  . PRO   A  1 112 ? 29.079 17.889  2.094   0.00 41.21  ? 138  PRO   A HB2  1 
ATOM   1453  H HB3  . PRO   A  1 112 ? 30.396 18.090  0.892   0.00 40.69  ? 138  PRO   A HB3  1 
ATOM   1454  H HG2  . PRO   A  1 112 ? 27.815 19.624  1.186   0.00 42.46  ? 138  PRO   A HG2  1 
ATOM   1455  H HG3  . PRO   A  1 112 ? 29.469 20.241  0.886   0.00 42.44  ? 138  PRO   A HG3  1 
ATOM   1456  H HD2  . PRO   A  1 112 ? 27.565 19.836  -1.097  0.00 39.40  ? 138  PRO   A HD2  1 
ATOM   1457  H HD3  . PRO   A  1 112 ? 29.346 19.831  -1.373  0.00 39.12  ? 138  PRO   A HD3  1 
ATOM   1458  N N    . GLN   A  1 113 ? 26.180 17.307  0.366   1.00 28.43  ? 139  GLN   A N    1 
ATOM   1459  C CA   . GLN   A  1 113 ? 24.856 17.008  0.906   1.00 29.05  ? 139  GLN   A CA   1 
ATOM   1460  C C    . GLN   A  1 113 ? 23.804 17.238  -0.174  1.00 29.22  ? 139  GLN   A C    1 
ATOM   1461  O O    . GLN   A  1 113 ? 24.044 17.980  -1.137  1.00 28.71  ? 139  GLN   A O    1 
ATOM   1462  C CB   . GLN   A  1 113 ? 24.529 17.989  2.066   1.00 30.65  ? 139  GLN   A CB   1 
ATOM   1463  C CG   . GLN   A  1 113 ? 25.413 17.889  3.304   1.00 37.12  ? 139  GLN   A CG   1 
ATOM   1464  C CD   . GLN   A  1 113 ? 25.228 16.608  4.096   1.00 44.85  ? 139  GLN   A CD   1 
ATOM   1465  O OE1  . GLN   A  1 113 ? 24.255 15.864  3.924   1.00 47.31  ? 139  GLN   A OE1  1 
ATOM   1466  N NE2  . GLN   A  1 113 ? 26.176 16.314  4.978   1.00 45.75  ? 139  GLN   A NE2  1 
ATOM   1467  H H    . GLN   A  1 113 ? 26.151 18.056  -0.318  0.00 38.85  ? 139  GLN   A H    1 
ATOM   1468  H HA   . GLN   A  1 113 ? 24.784 15.981  1.260   0.00 39.70  ? 139  GLN   A HA   1 
ATOM   1469  H HB2  . GLN   A  1 113 ? 24.634 19.004  1.685   0.00 42.88  ? 139  GLN   A HB2  1 
ATOM   1470  H HB3  . GLN   A  1 113 ? 23.497 17.832  2.377   0.00 42.91  ? 139  GLN   A HB3  1 
ATOM   1471  H HG2  . GLN   A  1 113 ? 26.456 17.947  2.998   0.00 50.60  ? 139  GLN   A HG2  1 
ATOM   1472  H HG3  . GLN   A  1 113 ? 25.179 18.721  3.966   0.00 51.47  ? 139  GLN   A HG3  1 
ATOM   1473  H HE21 . GLN   A  1 113 ? 26.972 16.933  5.095   0.00 61.51  ? 139  GLN   A HE21 1 
ATOM   1474  H HE22 . GLN   A  1 113 ? 26.103 15.469  5.536   0.00 61.31  ? 139  GLN   A HE22 1 
ATOM   1475  N N    . ILE   A  1 114 ? 22.579 16.724  0.048   1.00 29.70  ? 140  ILE   A N    1 
ATOM   1476  C CA   . ILE   A  1 114 ? 21.452 17.062  -0.819  1.00 30.43  ? 140  ILE   A CA   1 
ATOM   1477  C C    . ILE   A  1 114 ? 21.151 18.559  -0.529  1.00 31.37  ? 140  ILE   A C    1 
ATOM   1478  O O    . ILE   A  1 114 ? 21.088 18.914  0.651   1.00 31.84  ? 140  ILE   A O    1 
ATOM   1479  C CB   . ILE   A  1 114 ? 20.203 16.205  -0.509  1.00 30.65  ? 140  ILE   A CB   1 
ATOM   1480  C CG1  . ILE   A  1 114 ? 20.498 14.709  -0.790  1.00 30.95  ? 140  ILE   A CG1  1 
ATOM   1481  C CG2  . ILE   A  1 114 ? 18.979 16.731  -1.308  1.00 30.92  ? 140  ILE   A CG2  1 
ATOM   1482  C CD1  . ILE   A  1 114 ? 19.358 13.743  -0.518  1.00 31.67  ? 140  ILE   A CD1  1 
ATOM   1483  H H    . ILE   A  1 114 ? 22.349 16.101  0.817   0.00 40.71  ? 140  ILE   A H    1 
ATOM   1484  H HA   . ILE   A  1 114 ? 21.729 16.891  -1.857  0.00 40.95  ? 140  ILE   A HA   1 
ATOM   1485  H HB   . ILE   A  1 114 ? 19.978 16.308  0.551   0.00 42.29  ? 140  ILE   A HB   1 
ATOM   1486  H HG12 . ILE   A  1 114 ? 20.800 14.595  -1.829  0.00 41.02  ? 140  ILE   A HG12 1 
ATOM   1487  H HG13 . ILE   A  1 114 ? 21.313 14.407  -0.135  0.00 41.50  ? 140  ILE   A HG13 1 
ATOM   1488  H HG21 . ILE   A  1 114 ? 18.173 16.000  -1.287  0.00 42.23  ? 140  ILE   A HG21 1 
ATOM   1489  H HG22 . ILE   A  1 114 ? 18.618 17.653  -0.855  0.00 42.84  ? 140  ILE   A HG22 1 
ATOM   1490  H HG23 . ILE   A  1 114 ? 19.285 16.919  -2.336  0.00 41.88  ? 140  ILE   A HG23 1 
ATOM   1491  H HD11 . ILE   A  1 114 ? 19.772 12.748  -0.362  0.00 42.10  ? 140  ILE   A HD11 1 
ATOM   1492  H HD12 . ILE   A  1 114 ? 18.821 14.068  0.372   0.00 42.97  ? 140  ILE   A HD12 1 
ATOM   1493  H HD13 . ILE   A  1 114 ? 18.687 13.733  -1.376  0.00 42.25  ? 140  ILE   A HD13 1 
ATOM   1494  N N    . PRO   A  1 115 ? 21.048 19.458  -1.534  1.00 31.57  ? 141  PRO   A N    1 
ATOM   1495  C CA   . PRO   A  1 115 ? 20.778 20.873  -1.213  1.00 31.47  ? 141  PRO   A CA   1 
ATOM   1496  C C    . PRO   A  1 115 ? 19.511 21.060  -0.384  1.00 32.16  ? 141  PRO   A C    1 
ATOM   1497  O O    . PRO   A  1 115 ? 18.514 20.378  -0.615  1.00 32.56  ? 141  PRO   A O    1 
ATOM   1498  C CB   . PRO   A  1 115 ? 20.645 21.538  -2.588  1.00 31.95  ? 141  PRO   A CB   1 
ATOM   1499  C CG   . PRO   A  1 115 ? 21.365 20.645  -3.521  1.00 32.70  ? 141  PRO   A CG   1 
ATOM   1500  C CD   . PRO   A  1 115 ? 21.162 19.251  -2.993  1.00 30.91  ? 141  PRO   A CD   1 
ATOM   1501  H HA   . PRO   A  1 115 ? 21.631 21.303  -0.691  0.00 44.36  ? 141  PRO   A HA   1 
ATOM   1502  H HB2  . PRO   A  1 115 ? 19.592 21.611  -2.854  0.00 44.71  ? 141  PRO   A HB2  1 
ATOM   1503  H HB3  . PRO   A  1 115 ? 21.110 22.523  -2.563  0.00 44.86  ? 141  PRO   A HB3  1 
ATOM   1504  H HG2  . PRO   A  1 115 ? 20.943 20.746  -4.520  0.00 44.35  ? 141  PRO   A HG2  1 
ATOM   1505  H HG3  . PRO   A  1 115 ? 22.423 20.901  -3.519  0.00 44.45  ? 141  PRO   A HG3  1 
ATOM   1506  H HD2  . PRO   A  1 115 ? 20.247 18.816  -3.390  0.00 41.99  ? 141  PRO   A HD2  1 
ATOM   1507  H HD3  . PRO   A  1 115 ? 22.040 18.658  -3.242  0.00 41.60  ? 141  PRO   A HD3  1 
ATOM   1508  N N    . SER   A  1 116 ? 19.572 21.957  0.608   1.00 32.07  ? 142  SER   A N    1 
ATOM   1509  C CA   . SER   A  1 116 ? 18.448 22.262  1.485   1.00 32.27  ? 142  SER   A CA   1 
ATOM   1510  C C    . SER   A  1 116 ? 17.481 23.232  0.810   1.00 31.96  ? 142  SER   A C    1 
ATOM   1511  O O    . SER   A  1 116 ? 17.899 24.102  0.041   1.00 31.57  ? 142  SER   A O    1 
ATOM   1512  C CB   . SER   A  1 116 ? 18.952 22.901  2.775   1.00 33.91  ? 142  SER   A CB   1 
ATOM   1513  O OG   . SER   A  1 116 ? 19.776 22.002  3.499   1.00 36.67  ? 142  SER   A OG   1 
ATOM   1514  H H    . SER   A  1 116 ? 20.407 22.493  0.825   0.00 46.48  ? 142  SER   A H    1 
ATOM   1515  H HA   . SER   A  1 116 ? 17.915 21.347  1.742   0.00 47.06  ? 142  SER   A HA   1 
ATOM   1516  H HB2  . SER   A  1 116 ? 19.533 23.788  2.524   0.00 50.55  ? 142  SER   A HB2  1 
ATOM   1517  H HB3  . SER   A  1 116 ? 18.100 23.180  3.392   0.00 50.15  ? 142  SER   A HB3  1 
ATOM   1518  H HG   . SER   A  1 116 ? 20.398 22.507  4.086   0.00 53.57  ? 142  SER   A HG   1 
ATOM   1519  N N    . GLY   A  1 117 ? 16.206 23.100  1.148   1.00 32.04  ? 143  GLY   A N    1 
ATOM   1520  C CA   . GLY   A  1 117 ? 15.163 23.981  0.645   1.00 32.52  ? 143  GLY   A CA   1 
ATOM   1521  C C    . GLY   A  1 117 ? 14.946 23.916  -0.851  1.00 32.70  ? 143  GLY   A C    1 
ATOM   1522  O O    . GLY   A  1 117 ? 14.820 24.961  -1.496  1.00 33.12  ? 143  GLY   A O    1 
ATOM   1523  H H    . GLY   A  1 117 ? 15.854 22.390  1.783   0.00 47.91  ? 143  GLY   A H    1 
ATOM   1524  H HA2  . GLY   A  1 117 ? 14.222 23.724  1.131   0.00 49.42  ? 143  GLY   A HA2  1 
ATOM   1525  H HA3  . GLY   A  1 117 ? 15.410 25.009  0.904   0.00 49.52  ? 143  GLY   A HA3  1 
ATOM   1526  N N    . LEU   A  1 118 ? 14.913 22.702  -1.423  1.00 32.01  ? 144  LEU   A N    1 
ATOM   1527  C CA   . LEU   A  1 118 ? 14.650 22.549  -2.857  1.00 32.09  ? 144  LEU   A CA   1 
ATOM   1528  C C    . LEU   A  1 118 ? 13.152 22.782  -3.112  1.00 32.97  ? 144  LEU   A C    1 
ATOM   1529  O O    . LEU   A  1 118 ? 12.326 22.525  -2.225  1.00 33.25  ? 144  LEU   A O    1 
ATOM   1530  C CB   . LEU   A  1 118 ? 15.049 21.148  -3.353  1.00 31.98  ? 144  LEU   A CB   1 
ATOM   1531  C CG   . LEU   A  1 118 ? 16.544 20.894  -3.541  1.00 33.27  ? 144  LEU   A CG   1 
ATOM   1532  C CD1  . LEU   A  1 118 ? 16.815 19.409  -3.730  1.00 34.05  ? 144  LEU   A CD1  1 
ATOM   1533  C CD2  . LEU   A  1 118 ? 17.108 21.706  -4.708  1.00 33.71  ? 144  LEU   A CD2  1 
ATOM   1534  H H    . LEU   A  1 118 ? 15.063 21.831  -0.924  0.00 46.84  ? 144  LEU   A H    1 
ATOM   1535  H HA   . LEU   A  1 118 ? 15.226 23.297  -3.399  0.00 46.69  ? 144  LEU   A HA   1 
ATOM   1536  H HB2  . LEU   A  1 118 ? 14.700 20.411  -2.632  0.00 45.71  ? 144  LEU   A HB2  1 
ATOM   1537  H HB3  . LEU   A  1 118 ? 14.560 20.970  -4.310  0.00 45.43  ? 144  LEU   A HB3  1 
ATOM   1538  H HG   . LEU   A  1 118 ? 17.066 21.211  -2.640  0.00 46.88  ? 144  LEU   A HG   1 
ATOM   1539  H HD11 . LEU   A  1 118 ? 17.887 19.255  -3.851  0.00 46.37  ? 144  LEU   A HD11 1 
ATOM   1540  H HD12 . LEU   A  1 118 ? 16.462 18.866  -2.854  0.00 46.95  ? 144  LEU   A HD12 1 
ATOM   1541  H HD13 . LEU   A  1 118 ? 16.289 19.063  -4.618  0.00 46.50  ? 144  LEU   A HD13 1 
ATOM   1542  H HD21 . LEU   A  1 118 ? 18.082 21.303  -4.983  0.00 46.38  ? 144  LEU   A HD21 1 
ATOM   1543  H HD22 . LEU   A  1 118 ? 16.428 21.641  -5.556  0.00 46.80  ? 144  LEU   A HD22 1 
ATOM   1544  H HD23 . LEU   A  1 118 ? 17.227 22.744  -4.404  0.00 47.44  ? 144  LEU   A HD23 1 
ATOM   1545  N N    . PRO   A  1 119 ? 12.776 23.278  -4.311  1.00 33.17  ? 145  PRO   A N    1 
ATOM   1546  C CA   . PRO   A  1 119 ? 11.364 23.564  -4.562  1.00 33.68  ? 145  PRO   A CA   1 
ATOM   1547  C C    . PRO   A  1 119 ? 10.503 22.316  -4.589  1.00 34.38  ? 145  PRO   A C    1 
ATOM   1548  O O    . PRO   A  1 119 ? 10.859 21.319  -5.213  1.00 33.81  ? 145  PRO   A O    1 
ATOM   1549  C CB   . PRO   A  1 119 ? 11.364 24.278  -5.922  1.00 34.27  ? 145  PRO   A CB   1 
ATOM   1550  C CG   . PRO   A  1 119 ? 12.642 23.958  -6.547  1.00 34.40  ? 145  PRO   A CG   1 
ATOM   1551  C CD   . PRO   A  1 119 ? 13.618 23.680  -5.448  1.00 32.72  ? 145  PRO   A CD   1 
ATOM   1552  H HA   . PRO   A  1 119 ? 10.997 24.257  -3.806  0.00 50.42  ? 145  PRO   A HA   1 
ATOM   1553  H HB2  . PRO   A  1 119 ? 10.540 23.907  -6.528  0.00 50.33  ? 145  PRO   A HB2  1 
ATOM   1554  H HB3  . PRO   A  1 119 ? 11.277 25.354  -5.770  0.00 50.97  ? 145  PRO   A HB3  1 
ATOM   1555  H HG2  . PRO   A  1 119 ? 12.528 23.094  -7.197  0.00 49.13  ? 145  PRO   A HG2  1 
ATOM   1556  H HG3  . PRO   A  1 119 ? 12.976 24.817  -7.128  0.00 49.81  ? 145  PRO   A HG3  1 
ATOM   1557  H HD2  . PRO   A  1 119 ? 14.319 22.894  -5.723  0.00 46.82  ? 145  PRO   A HD2  1 
ATOM   1558  H HD3  . PRO   A  1 119 ? 14.116 24.605  -5.166  0.00 47.88  ? 145  PRO   A HD3  1 
ATOM   1559  N N    . GLU   A  1 120 ? 9.334  22.423  -3.963  1.00 34.88  ? 146  GLU   A N    1 
ATOM   1560  C CA   . GLU   A  1 120 ? 8.330  21.355  -3.850  1.00 35.95  ? 146  GLU   A CA   1 
ATOM   1561  C C    . GLU   A  1 120 ? 7.724  20.949  -5.218  1.00 36.04  ? 146  GLU   A C    1 
ATOM   1562  O O    . GLU   A  1 120 ? 7.142  19.869  -5.327  1.00 36.28  ? 146  GLU   A O    1 
ATOM   1563  C CB   . GLU   A  1 120 ? 7.214  21.824  -2.897  1.00 39.51  ? 146  GLU   A CB   1 
ATOM   1564  C CG   . GLU   A  1 120 ? 6.337  20.735  -2.337  1.00 46.74  ? 146  GLU   A CG   1 
ATOM   1565  C CD   . GLU   A  1 120 ? 5.420  21.243  -1.244  1.00 55.45  ? 146  GLU   A CD   1 
ATOM   1566  O OE1  . GLU   A  1 120 ? 5.825  21.194  -0.060  1.00 57.28  ? 146  GLU   A OE1  1 
ATOM   1567  O OE2  . GLU   A  1 120 ? 4.301  21.701  -1.569  1.00 58.29  ? 146  GLU   A OE2  1 
ATOM   1568  H H    . GLU   A  1 120 ? 9.051  23.299  -3.535  0.00 52.28  ? 146  GLU   A H    1 
ATOM   1569  H HA   . GLU   A  1 120 ? 8.801  20.473  -3.419  0.00 52.43  ? 146  GLU   A HA   1 
ATOM   1570  H HB2  . GLU   A  1 120 ? 7.668  22.326  -2.044  0.00 58.47  ? 146  GLU   A HB2  1 
ATOM   1571  H HB3  . GLU   A  1 120 ? 6.571  22.520  -3.433  0.00 58.59  ? 146  GLU   A HB3  1 
ATOM   1572  H HG2  . GLU   A  1 120 ? 5.719  20.327  -3.135  0.00 66.75  ? 146  GLU   A HG2  1 
ATOM   1573  H HG3  . GLU   A  1 120 ? 6.964  19.951  -1.915  0.00 66.47  ? 146  GLU   A HG3  1 
ATOM   1574  N N    . SER   A  1 121 ? 7.870  21.787  -6.258  1.00 35.48  ? 147  SER   A N    1 
ATOM   1575  C CA   . SER   A  1 121 ? 7.371  21.459  -7.592  1.00 35.22  ? 147  SER   A CA   1 
ATOM   1576  C C    . SER   A  1 121 ? 8.227  20.405  -8.326  1.00 34.28  ? 147  SER   A C    1 
ATOM   1577  O O    . SER   A  1 121 ? 7.832  19.972  -9.407  1.00 34.15  ? 147  SER   A O    1 
ATOM   1578  C CB   . SER   A  1 121 ? 7.313  22.722  -8.445  1.00 36.78  ? 147  SER   A CB   1 
ATOM   1579  O OG   . SER   A  1 121 ? 8.613  23.265  -8.620  1.00 38.99  ? 147  SER   A OG   1 
ATOM   1580  H H    . SER   A  1 121 ? 8.314  22.698  -6.213  0.00 52.23  ? 147  SER   A H    1 
ATOM   1581  H HA   . SER   A  1 121 ? 6.356  21.072  -7.513  0.00 51.71  ? 147  SER   A HA   1 
ATOM   1582  H HB2  . SER   A  1 121 ? 6.875  22.482  -9.413  0.00 53.53  ? 147  SER   A HB2  1 
ATOM   1583  H HB3  . SER   A  1 121 ? 6.694  23.458  -7.935  0.00 54.43  ? 147  SER   A HB3  1 
ATOM   1584  H HG   . SER   A  1 121 ? 9.011  22.973  -9.481  0.00 55.41  ? 147  SER   A HG   1 
ATOM   1585  N N    . LEU   A  1 122 ? 9.407  20.020  -7.793  1.00 33.51  ? 148  LEU   A N    1 
ATOM   1586  C CA   . LEU   A  1 122 ? 10.275 19.063  -8.479  1.00 32.87  ? 148  LEU   A CA   1 
ATOM   1587  C C    . LEU   A  1 122 ? 9.638  17.697  -8.703  1.00 32.40  ? 148  LEU   A C    1 
ATOM   1588  O O    . LEU   A  1 122 ? 9.115  17.112  -7.766  1.00 32.63  ? 148  LEU   A O    1 
ATOM   1589  C CB   . LEU   A  1 122 ? 11.589 18.839  -7.700  1.00 32.96  ? 148  LEU   A CB   1 
ATOM   1590  C CG   . LEU   A  1 122 ? 12.596 19.990  -7.664  1.00 34.38  ? 148  LEU   A CG   1 
ATOM   1591  C CD1  . LEU   A  1 122 ? 13.792 19.638  -6.754  1.00 34.63  ? 148  LEU   A CD1  1 
ATOM   1592  C CD2  . LEU   A  1 122 ? 13.082 20.364  -9.068  1.00 34.66  ? 148  LEU   A CD2  1 
ATOM   1593  H H    . LEU   A  1 122 ? 9.785  20.341  -6.908  0.00 48.00  ? 148  LEU   A H    1 
ATOM   1594  H HA   . LEU   A  1 122 ? 10.516 19.474  -9.457  0.00 45.92  ? 148  LEU   A HA   1 
ATOM   1595  H HB2  . LEU   A  1 122 ? 11.340 18.596  -6.669  0.00 46.08  ? 148  LEU   A HB2  1 
ATOM   1596  H HB3  . LEU   A  1 122 ? 12.100 17.989  -8.150  0.00 45.16  ? 148  LEU   A HB3  1 
ATOM   1597  H HG   . LEU   A  1 122 ? 12.094 20.855  -7.234  0.00 48.25  ? 148  LEU   A HG   1 
ATOM   1598  H HD11 . LEU   A  1 122 ? 14.467 20.492  -6.707  0.00 47.71  ? 148  LEU   A HD11 1 
ATOM   1599  H HD12 . LEU   A  1 122 ? 13.422 19.401  -5.758  0.00 47.89  ? 148  LEU   A HD12 1 
ATOM   1600  H HD13 . LEU   A  1 122 ? 14.313 18.778  -7.173  0.00 46.94  ? 148  LEU   A HD13 1 
ATOM   1601  H HD21 . LEU   A  1 122 ? 13.975 20.980  -8.978  0.00 47.49  ? 148  LEU   A HD21 1 
ATOM   1602  H HD22 . LEU   A  1 122 ? 13.308 19.455  -9.623  0.00 46.94  ? 148  LEU   A HD22 1 
ATOM   1603  H HD23 . LEU   A  1 122 ? 12.306 20.932  -9.578  0.00 47.92  ? 148  LEU   A HD23 1 
ATOM   1604  N N    . THR   A  1 123 ? 9.722  17.184  -9.940  1.00 31.61  ? 149  THR   A N    1 
ATOM   1605  C CA   . THR   A  1 123 ? 9.300  15.830  -10.316 1.00 31.22  ? 149  THR   A CA   1 
ATOM   1606  C C    . THR   A  1 123 ? 10.543 14.964  -10.654 1.00 30.12  ? 149  THR   A C    1 
ATOM   1607  O O    . THR   A  1 123 ? 10.452 13.746  -10.604 1.00 30.11  ? 149  THR   A O    1 
ATOM   1608  C CB   . THR   A  1 123 ? 8.322  15.852  -11.488 1.00 33.07  ? 149  THR   A CB   1 
ATOM   1609  O OG1  . THR   A  1 123 ? 8.989  16.396  -12.626 1.00 34.78  ? 149  THR   A OG1  1 
ATOM   1610  C CG2  . THR   A  1 123 ? 7.050  16.647  -11.179 1.00 33.46  ? 149  THR   A CG2  1 
ATOM   1611  H H    . THR   A  1 123 ? 10.075 17.705  -10.736 0.00 43.59  ? 149  THR   A H    1 
ATOM   1612  H HA   . THR   A  1 123 ? 8.754  15.366  -9.498  0.00 43.14  ? 149  THR   A HA   1 
ATOM   1613  H HB   . THR   A  1 123 ? 8.013  14.828  -11.696 0.00 45.02  ? 149  THR   A HB   1 
ATOM   1614  H HG1  . THR   A  1 123 ? 9.407  15.687  -13.183 0.00 46.46  ? 149  THR   A HG1  1 
ATOM   1615  H HG21 . THR   A  1 123 ? 6.351  16.567  -12.010 0.00 46.79  ? 149  THR   A HG21 1 
ATOM   1616  H HG22 . THR   A  1 123 ? 6.576  16.255  -10.280 0.00 46.93  ? 149  THR   A HG22 1 
ATOM   1617  H HG23 . THR   A  1 123 ? 7.290  17.697  -11.022 0.00 46.96  ? 149  THR   A HG23 1 
ATOM   1618  N N    . GLU   A  1 124 ? 11.686 15.575  -11.032 1.00 29.07  ? 150  GLU   A N    1 
ATOM   1619  C CA   . GLU   A  1 124 ? 12.890 14.833  -11.375 1.00 28.77  ? 150  GLU   A CA   1 
ATOM   1620  C C    . GLU   A  1 124 ? 14.095 15.524  -10.759 1.00 27.54  ? 150  GLU   A C    1 
ATOM   1621  O O    . GLU   A  1 124 ? 14.309 16.711  -11.001 1.00 27.19  ? 150  GLU   A O    1 
ATOM   1622  C CB   . GLU   A  1 124 ? 13.024 14.751  -12.905 1.00 32.65  ? 150  GLU   A CB   1 
ATOM   1623  C CG   . GLU   A  1 124 ? 11.981 13.839  -13.533 1.00 40.95  ? 150  GLU   A CG   1 
ATOM   1624  C CD   . GLU   A  1 124 ? 11.316 14.326  -14.807 1.00 51.47  ? 150  GLU   A CD   1 
ATOM   1625  O OE1  . GLU   A  1 124 ? 10.137 14.747  -14.742 1.00 54.31  ? 150  GLU   A OE1  1 
ATOM   1626  O OE2  . GLU   A  1 124 ? 11.964 14.258  -15.876 1.00 53.54  ? 150  GLU   A OE2  1 
ATOM   1627  H H    . GLU   A  1 124 ? 11.806 16.578  -11.122 0.00 39.37  ? 150  GLU   A H    1 
ATOM   1628  H HA   . GLU   A  1 124 ? 12.849 13.820  -10.980 0.00 37.75  ? 150  GLU   A HA   1 
ATOM   1629  H HB2  . GLU   A  1 124 ? 12.900 15.747  -13.327 0.00 42.50  ? 150  GLU   A HB2  1 
ATOM   1630  H HB3  . GLU   A  1 124 ? 14.009 14.358  -13.155 0.00 41.70  ? 150  GLU   A HB3  1 
ATOM   1631  H HG2  . GLU   A  1 124 ? 12.477 12.904  -13.788 0.00 51.66  ? 150  GLU   A HG2  1 
ATOM   1632  H HG3  . GLU   A  1 124 ? 11.194 13.649  -12.806 0.00 52.56  ? 150  GLU   A HG3  1 
ATOM   1633  N N    . LEU   A  1 125 ? 14.876 14.786  -9.954  1.00 26.45  ? 151  LEU   A N    1 
ATOM   1634  C CA   . LEU   A  1 125 ? 16.064 15.316  -9.294  1.00 25.85  ? 151  LEU   A CA   1 
ATOM   1635  C C    . LEU   A  1 125 ? 17.185 14.335  -9.504  1.00 25.23  ? 151  LEU   A C    1 
ATOM   1636  O O    . LEU   A  1 125 ? 17.066 13.185  -9.079  1.00 25.55  ? 151  LEU   A O    1 
ATOM   1637  C CB   . LEU   A  1 125 ? 15.790 15.476  -7.779  1.00 25.80  ? 151  LEU   A CB   1 
ATOM   1638  C CG   . LEU   A  1 125 ? 16.976 15.881  -6.881  1.00 26.80  ? 151  LEU   A CG   1 
ATOM   1639  C CD1  . LEU   A  1 125 ? 17.573 17.215  -7.315  1.00 27.36  ? 151  LEU   A CD1  1 
ATOM   1640  C CD2  . LEU   A  1 125 ? 16.539 15.957  -5.412  1.00 27.12  ? 151  LEU   A CD2  1 
ATOM   1641  H H    . LEU   A  1 125 ? 14.715 13.808  -9.738  0.00 34.61  ? 151  LEU   A H    1 
ATOM   1642  H HA   . LEU   A  1 125 ? 16.352 16.282  -9.707  0.00 34.17  ? 151  LEU   A HA   1 
ATOM   1643  H HB2  . LEU   A  1 125 ? 15.020 16.236  -7.653  0.00 35.05  ? 151  LEU   A HB2  1 
ATOM   1644  H HB3  . LEU   A  1 125 ? 15.416 14.524  -7.403  0.00 34.45  ? 151  LEU   A HB3  1 
ATOM   1645  H HG   . LEU   A  1 125 ? 17.759 15.128  -6.940  0.00 35.27  ? 151  LEU   A HG   1 
ATOM   1646  H HD11 . LEU   A  1 125 ? 18.326 17.519  -6.589  0.00 36.70  ? 151  LEU   A HD11 1 
ATOM   1647  H HD12 . LEU   A  1 125 ? 18.035 17.100  -8.294  0.00 36.14  ? 151  LEU   A HD12 1 
ATOM   1648  H HD13 . LEU   A  1 125 ? 16.781 17.960  -7.364  0.00 37.07  ? 151  LEU   A HD13 1 
ATOM   1649  H HD21 . LEU   A  1 125 ? 17.397 16.237  -4.801  0.00 36.77  ? 151  LEU   A HD21 1 
ATOM   1650  H HD22 . LEU   A  1 125 ? 15.753 16.704  -5.314  0.00 37.25  ? 151  LEU   A HD22 1 
ATOM   1651  H HD23 . LEU   A  1 125 ? 16.166 14.981  -5.103  0.00 36.62  ? 151  LEU   A HD23 1 
ATOM   1652  N N    . SER   A  1 126 ? 18.274 14.754  -10.163 1.00 24.80  ? 152  SER   A N    1 
ATOM   1653  C CA   . SER   A  1 126 ? 19.418 13.875  -10.350 1.00 24.68  ? 152  SER   A CA   1 
ATOM   1654  C C    . SER   A  1 126 ? 20.614 14.404  -9.592  1.00 24.30  ? 152  SER   A C    1 
ATOM   1655  O O    . SER   A  1 126 ? 21.063 15.515  -9.848  1.00 24.39  ? 152  SER   A O    1 
ATOM   1656  C CB   . SER   A  1 126 ? 19.766 13.707  -11.824 1.00 25.72  ? 152  SER   A CB   1 
ATOM   1657  O OG   . SER   A  1 126 ? 20.791 12.732  -11.938 1.00 26.73  ? 152  SER   A OG   1 
ATOM   1658  H H    . SER   A  1 126 ? 18.390 15.676  -10.570 0.00 31.89  ? 152  SER   A H    1 
ATOM   1659  H HA   . SER   A  1 126 ? 19.180 12.889  -9.954  0.00 30.87  ? 152  SER   A HA   1 
ATOM   1660  H HB2  . SER   A  1 126 ? 18.885 13.370  -12.368 0.00 31.75  ? 152  SER   A HB2  1 
ATOM   1661  H HB3  . SER   A  1 126 ? 20.124 14.652  -12.228 0.00 31.83  ? 152  SER   A HB3  1 
ATOM   1662  H HG   . SER   A  1 126 ? 21.039 12.610  -12.892 0.00 32.11  ? 152  SER   A HG   1 
ATOM   1663  N N    . LEU   A  1 127 ? 21.152 13.587  -8.683  1.00 23.54  ? 153  LEU   A N    1 
ATOM   1664  C CA   . LEU   A  1 127 ? 22.324 13.899  -7.878  1.00 23.51  ? 153  LEU   A CA   1 
ATOM   1665  C C    . LEU   A  1 127 ? 23.410 12.820  -8.057  1.00 22.91  ? 153  LEU   A C    1 
ATOM   1666  O O    . LEU   A  1 127 ? 24.220 12.586  -7.150  1.00 22.87  ? 153  LEU   A O    1 
ATOM   1667  C CB   . LEU   A  1 127 ? 21.871 14.027  -6.419  1.00 24.16  ? 153  LEU   A CB   1 
ATOM   1668  C CG   . LEU   A  1 127 ? 20.966 15.233  -6.114  1.00 26.40  ? 153  LEU   A CG   1 
ATOM   1669  C CD1  . LEU   A  1 127 ? 20.138 14.968  -4.883  1.00 27.13  ? 153  LEU   A CD1  1 
ATOM   1670  C CD2  . LEU   A  1 127 ? 21.795 16.503  -5.935  1.00 27.53  ? 153  LEU   A CD2  1 
ATOM   1671  H H    . LEU   A  1 127 ? 20.782 12.667  -8.467  0.00 29.47  ? 153  LEU   A H    1 
ATOM   1672  H HA   . LEU   A  1 127 ? 22.760 14.847  -8.187  0.00 29.70  ? 153  LEU   A HA   1 
ATOM   1673  H HB2  . LEU   A  1 127 ? 21.304 13.133  -6.166  0.00 30.89  ? 153  LEU   A HB2  1 
ATOM   1674  H HB3  . LEU   A  1 127 ? 22.742 14.112  -5.771  0.00 31.01  ? 153  LEU   A HB3  1 
ATOM   1675  H HG   . LEU   A  1 127 ? 20.269 15.407  -6.933  0.00 34.26  ? 153  LEU   A HG   1 
ATOM   1676  H HD11 . LEU   A  1 127 ? 19.697 15.902  -4.538  0.00 36.16  ? 153  LEU   A HD11 1 
ATOM   1677  H HD12 . LEU   A  1 127 ? 19.352 14.257  -5.132  0.00 35.53  ? 153  LEU   A HD12 1 
ATOM   1678  H HD13 . LEU   A  1 127 ? 20.790 14.548  -4.120  0.00 35.64  ? 153  LEU   A HD13 1 
ATOM   1679  H HD21 . LEU   A  1 127 ? 21.121 17.347  -5.792  0.00 36.41  ? 153  LEU   A HD21 1 
ATOM   1680  H HD22 . LEU   A  1 127 ? 22.430 16.386  -5.058  0.00 36.05  ? 153  LEU   A HD22 1 
ATOM   1681  H HD23 . LEU   A  1 127 ? 22.411 16.668  -6.817  0.00 35.58  ? 153  LEU   A HD23 1 
ATOM   1682  N N    . ILE   A  1 128 ? 23.492 12.234  -9.266  1.00 22.34  ? 154  ILE   A N    1 
ATOM   1683  C CA   . ILE   A  1 128 ? 24.480 11.212  -9.608  1.00 22.05  ? 154  ILE   A CA   1 
ATOM   1684  C C    . ILE   A  1 128 ? 25.892 11.786  -9.505  1.00 22.33  ? 154  ILE   A C    1 
ATOM   1685  O O    . ILE   A  1 128 ? 26.100 12.945  -9.839  1.00 23.30  ? 154  ILE   A O    1 
ATOM   1686  C CB   . ILE   A  1 128 ? 24.200 10.656  -11.050 1.00 22.07  ? 154  ILE   A CB   1 
ATOM   1687  C CG1  . ILE   A  1 128 ? 22.894 9.824   -11.080 1.00 22.63  ? 154  ILE   A CG1  1 
ATOM   1688  C CG2  . ILE   A  1 128 ? 25.379 9.845   -11.605 1.00 22.29  ? 154  ILE   A CG2  1 
ATOM   1689  C CD1  . ILE   A  1 128 ? 22.354 9.558   -12.530 1.00 23.41  ? 154  ILE   A CD1  1 
ATOM   1690  H H    . ILE   A  1 128 ? 22.886 12.478  -10.043 0.00 27.10  ? 154  ILE   A H    1 
ATOM   1691  H HA   . ILE   A  1 128 ? 24.392 10.386  -8.903  0.00 26.31  ? 154  ILE   A HA   1 
ATOM   1692  H HB   . ILE   A  1 128 ? 24.069 11.494  -11.731 0.00 25.90  ? 154  ILE   A HB   1 
ATOM   1693  H HG12 . ILE   A  1 128 ? 23.084 8.860   -10.612 0.00 26.47  ? 154  ILE   A HG12 1 
ATOM   1694  H HG13 . ILE   A  1 128 ? 22.115 10.352  -10.532 0.00 26.98  ? 154  ILE   A HG13 1 
ATOM   1695  H HG21 . ILE   A  1 128 ? 25.142 9.542   -12.622 0.00 25.34  ? 154  ILE   A HG21 1 
ATOM   1696  H HG22 . ILE   A  1 128 ? 26.285 10.449  -11.641 0.00 25.59  ? 154  ILE   A HG22 1 
ATOM   1697  H HG23 . ILE   A  1 128 ? 25.539 8.970   -10.978 0.00 25.58  ? 154  ILE   A HG23 1 
ATOM   1698  H HD11 . ILE   A  1 128 ? 21.335 9.178   -12.492 0.00 27.37  ? 154  ILE   A HD11 1 
ATOM   1699  H HD12 . ILE   A  1 128 ? 22.379 10.489  -13.093 0.00 27.27  ? 154  ILE   A HD12 1 
ATOM   1700  H HD13 . ILE   A  1 128 ? 22.988 8.819   -13.017 0.00 26.83  ? 154  ILE   A HD13 1 
ATOM   1701  N N    . GLN   A  1 129 ? 26.860 10.975  -9.081  1.00 20.86  ? 155  GLN   A N    1 
ATOM   1702  C CA   . GLN   A  1 129 ? 28.262 11.367  -9.049  1.00 21.49  ? 155  GLN   A CA   1 
ATOM   1703  C C    . GLN   A  1 129 ? 28.555 12.614  -8.200  1.00 22.62  ? 155  GLN   A C    1 
ATOM   1704  O O    . GLN   A  1 129 ? 29.219 13.546  -8.646  1.00 22.99  ? 155  GLN   A O    1 
ATOM   1705  C CB   . GLN   A  1 129 ? 28.819 11.520  -10.495 1.00 21.49  ? 155  GLN   A CB   1 
ATOM   1706  C CG   . GLN   A  1 129 ? 29.258 10.193  -11.141 1.00 21.89  ? 155  GLN   A CG   1 
ATOM   1707  C CD   . GLN   A  1 129 ? 30.525 9.635   -10.510 1.00 25.17  ? 155  GLN   A CD   1 
ATOM   1708  O OE1  . GLN   A  1 129 ? 31.155 10.249  -9.626  1.00 25.78  ? 155  GLN   A OE1  1 
ATOM   1709  N NE2  . GLN   A  1 129 ? 30.939 8.449   -10.934 1.00 25.58  ? 155  GLN   A NE2  1 
ATOM   1710  H H    . GLN   A  1 129 ? 26.701 10.030  -8.748  0.00 24.51  ? 155  GLN   A H    1 
ATOM   1711  H HA   . GLN   A  1 129 ? 28.799 10.562  -8.548  0.00 25.22  ? 155  GLN   A HA   1 
ATOM   1712  H HB2  . GLN   A  1 129 ? 28.056 11.955  -11.139 0.00 24.88  ? 155  GLN   A HB2  1 
ATOM   1713  H HB3  . GLN   A  1 129 ? 29.694 12.167  -10.501 0.00 24.94  ? 155  GLN   A HB3  1 
ATOM   1714  H HG2  . GLN   A  1 129 ? 28.461 9.461   -11.020 0.00 24.81  ? 155  GLN   A HG2  1 
ATOM   1715  H HG3  . GLN   A  1 129 ? 29.453 10.359  -12.200 0.00 24.59  ? 155  GLN   A HG3  1 
ATOM   1716  H HE21 . GLN   A  1 129 ? 30.416 7.954   -11.650 0.00 28.65  ? 155  GLN   A HE21 1 
ATOM   1717  H HE22 . GLN   A  1 129 ? 31.778 8.034   -10.541 0.00 28.88  ? 155  GLN   A HE22 1 
ATOM   1718  N N    . ASN   A  1 130 ? 28.129 12.576  -6.945  1.00 22.51  ? 156  ASN   A N    1 
ATOM   1719  C CA   . ASN   A  1 130 ? 28.442 13.615  -5.972  1.00 22.93  ? 156  ASN   A CA   1 
ATOM   1720  C C    . ASN   A  1 130 ? 29.111 12.940  -4.738  1.00 22.75  ? 156  ASN   A C    1 
ATOM   1721  O O    . ASN   A  1 130 ? 29.572 11.801  -4.861  1.00 22.55  ? 156  ASN   A O    1 
ATOM   1722  C CB   . ASN   A  1 130 ? 27.160 14.399  -5.641  1.00 23.79  ? 156  ASN   A CB   1 
ATOM   1723  C CG   . ASN   A  1 130 ? 26.797 15.363  -6.736  1.00 24.58  ? 156  ASN   A CG   1 
ATOM   1724  O OD1  . ASN   A  1 130 ? 27.511 16.322  -6.993  1.00 25.33  ? 156  ASN   A OD1  1 
ATOM   1725  N ND2  . ASN   A  1 130 ? 25.697 15.144  -7.395  1.00 24.35  ? 156  ASN   A ND2  1 
ATOM   1726  H H    . ASN   A  1 130 ? 27.560 11.827  -6.565  0.00 27.46  ? 156  ASN   A H    1 
ATOM   1727  H HA   . ASN   A  1 130 ? 29.181 14.308  -6.370  0.00 28.52  ? 156  ASN   A HA   1 
ATOM   1728  H HB2  . ASN   A  1 130 ? 26.346 13.691  -5.495  0.00 29.97  ? 156  ASN   A HB2  1 
ATOM   1729  H HB3  . ASN   A  1 130 ? 27.301 14.985  -4.735  0.00 30.49  ? 156  ASN   A HB3  1 
ATOM   1730  H HD21 . ASN   A  1 130 ? 25.423 15.775  -8.141  0.00 30.56  ? 156  ASN   A HD21 1 
ATOM   1731  H HD22 . ASN   A  1 130 ? 25.107 14.351  -7.165  0.00 30.47  ? 156  ASN   A HD22 1 
ATOM   1732  N N    . ASN   A  1 131 ? 29.238 13.647  -3.596  1.00 22.71  ? 157  ASN   A N    1 
ATOM   1733  C CA   . ASN   A  1 131 ? 29.815 13.105  -2.364  1.00 23.74  ? 157  ASN   A CA   1 
ATOM   1734  C C    . ASN   A  1 131 ? 28.733 13.056  -1.271  1.00 24.11  ? 157  ASN   A C    1 
ATOM   1735  O O    . ASN   A  1 131 ? 29.015 13.356  -0.121  1.00 24.83  ? 157  ASN   A O    1 
ATOM   1736  C CB   . ASN   A  1 131 ? 30.988 13.986  -1.925  1.00 25.12  ? 157  ASN   A CB   1 
ATOM   1737  C CG   . ASN   A  1 131 ? 32.065 14.108  -2.973  1.00 28.68  ? 157  ASN   A CG   1 
ATOM   1738  O OD1  . ASN   A  1 131 ? 32.299 13.190  -3.774  1.00 28.92  ? 157  ASN   A OD1  1 
ATOM   1739  N ND2  . ASN   A  1 131 ? 32.751 15.235  -3.002  1.00 30.25  ? 157  ASN   A ND2  1 
ATOM   1740  H H    . ASN   A  1 131 ? 28.981 14.623  -3.497  0.00 29.37  ? 157  ASN   A H    1 
ATOM   1741  H HA   . ASN   A  1 131 ? 30.189 12.092  -2.509  0.00 30.21  ? 157  ASN   A HA   1 
ATOM   1742  H HB2  . ASN   A  1 131 ? 30.607 14.980  -1.699  0.00 32.94  ? 157  ASN   A HB2  1 
ATOM   1743  H HB3  . ASN   A  1 131 ? 31.448 13.553  -1.037  0.00 32.77  ? 157  ASN   A HB3  1 
ATOM   1744  H HD21 . ASN   A  1 131 ? 33.484 15.358  -3.694  0.00 38.36  ? 157  ASN   A HD21 1 
ATOM   1745  H HD22 . ASN   A  1 131 ? 32.557 15.980  -2.342  0.00 39.08  ? 157  ASN   A HD22 1 
ATOM   1746  N N    . ILE   A  1 132 ? 27.504 12.678  -1.639  1.00 24.07  ? 158  ILE   A N    1 
ATOM   1747  C CA   . ILE   A  1 132 ? 26.368 12.635  -0.732  1.00 24.98  ? 158  ILE   A CA   1 
ATOM   1748  C C    . ILE   A  1 132 ? 26.319 11.267  -0.066  1.00 25.86  ? 158  ILE   A C    1 
ATOM   1749  O O    . ILE   A  1 132 ? 26.108 10.266  -0.745  1.00 25.34  ? 158  ILE   A O    1 
ATOM   1750  C CB   . ILE   A  1 132 ? 25.050 12.949  -1.476  1.00 25.42  ? 158  ILE   A CB   1 
ATOM   1751  C CG1  . ILE   A  1 132 ? 25.088 14.385  -2.059  1.00 26.85  ? 158  ILE   A CG1  1 
ATOM   1752  C CG2  . ILE   A  1 132 ? 23.842 12.777  -0.530  1.00 25.92  ? 158  ILE   A CG2  1 
ATOM   1753  C CD1  . ILE   A  1 132 ? 23.998 14.673  -3.099  1.00 28.25  ? 158  ILE   A CD1  1 
ATOM   1754  H H    . ILE   A  1 132 ? 27.265 12.368  -2.576  0.00 30.88  ? 158  ILE   A H    1 
ATOM   1755  H HA   . ILE   A  1 132 ? 26.484 13.393  0.040   0.00 33.32  ? 158  ILE   A HA   1 
ATOM   1756  H HB   . ILE   A  1 132 ? 24.938 12.246  -2.300  0.00 32.84  ? 158  ILE   A HB   1 
ATOM   1757  H HG12 . ILE   A  1 132 ? 24.959 15.091  -1.240  0.00 35.77  ? 158  ILE   A HG12 1 
ATOM   1758  H HG13 . ILE   A  1 132 ? 26.047 14.562  -2.543  0.00 34.98  ? 158  ILE   A HG13 1 
ATOM   1759  H HG21 . ILE   A  1 132 ? 22.939 13.073  -1.061  0.00 34.43  ? 158  ILE   A HG21 1 
ATOM   1760  H HG22 . ILE   A  1 132 ? 23.735 11.734  -0.234  0.00 34.23  ? 158  ILE   A HG22 1 
ATOM   1761  H HG23 . ILE   A  1 132 ? 23.984 13.404  0.348   0.00 34.89  ? 158  ILE   A HG23 1 
ATOM   1762  H HD11 . ILE   A  1 132 ? 24.258 15.584  -3.637  0.00 36.81  ? 158  ILE   A HD11 1 
ATOM   1763  H HD12 . ILE   A  1 132 ? 23.937 13.833  -3.789  0.00 36.27  ? 158  ILE   A HD12 1 
ATOM   1764  H HD13 . ILE   A  1 132 ? 23.043 14.810  -2.594  0.00 37.12  ? 158  ILE   A HD13 1 
ATOM   1765  N N    . TYR   A  1 133 ? 26.513 11.232  1.265   1.00 26.15  ? 159  TYR   A N    1 
ATOM   1766  C CA   . TYR   A  1 133 ? 26.508 9.980   2.036   1.00 26.96  ? 159  TYR   A CA   1 
ATOM   1767  C C    . TYR   A  1 133 ? 25.349 9.904   3.034   1.00 29.21  ? 159  TYR   A C    1 
ATOM   1768  O O    . TYR   A  1 133 ? 25.289 8.949   3.789   1.00 30.31  ? 159  TYR   A O    1 
ATOM   1769  C CB   . TYR   A  1 133 ? 27.858 9.813   2.780   1.00 26.24  ? 159  TYR   A CB   1 
ATOM   1770  C CG   . TYR   A  1 133 ? 29.060 10.082  1.897   1.00 27.15  ? 159  TYR   A CG   1 
ATOM   1771  C CD1  . TYR   A  1 133 ? 29.159 9.517   0.635   1.00 27.64  ? 159  TYR   A CD1  1 
ATOM   1772  C CD2  . TYR   A  1 133 ? 30.052 10.971  2.289   1.00 27.93  ? 159  TYR   A CD2  1 
ATOM   1773  C CE1  . TYR   A  1 133 ? 30.180 9.868   -0.234  1.00 28.44  ? 159  TYR   A CE1  1 
ATOM   1774  C CE2  . TYR   A  1 133 ? 31.125 11.267  1.458   1.00 28.57  ? 159  TYR   A CE2  1 
ATOM   1775  C CZ   . TYR   A  1 133 ? 31.187 10.711  0.195   1.00 29.31  ? 159  TYR   A CZ   1 
ATOM   1776  O OH   . TYR   A  1 133 ? 32.212 11.006  -0.672  1.00 31.17  ? 159  TYR   A OH   1 
ATOM   1777  H H    . TYR   A  1 133 ? 26.677 12.051  1.842   0.00 35.09  ? 159  TYR   A H    1 
ATOM   1778  H HA   . TYR   A  1 133 ? 26.407 9.125   1.370   0.00 35.22  ? 159  TYR   A HA   1 
ATOM   1779  H HB2  . TYR   A  1 133 ? 27.885 10.507  3.619   0.00 35.50  ? 159  TYR   A HB2  1 
ATOM   1780  H HB3  . TYR   A  1 133 ? 27.934 8.789   3.144   0.00 34.92  ? 159  TYR   A HB3  1 
ATOM   1781  H HD1  . TYR   A  1 133 ? 28.375 8.870   0.279   0.00 35.38  ? 159  TYR   A HD1  1 
ATOM   1782  H HD2  . TYR   A  1 133 ? 30.007 11.421  3.266   0.00 37.47  ? 159  TYR   A HD2  1 
ATOM   1783  H HE1  . TYR   A  1 133 ? 30.245 9.404   -1.203  0.00 35.76  ? 159  TYR   A HE1  1 
ATOM   1784  H HE2  . TYR   A  1 133 ? 31.882 11.957  1.792   0.00 37.67  ? 159  TYR   A HE2  1 
ATOM   1785  H HH   . TYR   A  1 133 ? 32.885 11.591  -0.237  0.00 39.83  ? 159  TYR   A HH   1 
ATOM   1786  N N    . ASN   A  1 134 ? 24.448 10.890  3.050   1.00 29.94  ? 160  ASN   A N    1 
ATOM   1787  C CA   . ASN   A  1 134 ? 23.353 10.958  3.992   1.00 31.36  ? 160  ASN   A CA   1 
ATOM   1788  C C    . ASN   A  1 134 ? 22.104 11.388  3.227   1.00 31.30  ? 160  ASN   A C    1 
ATOM   1789  O O    . ASN   A  1 134 ? 22.124 12.437  2.585   1.00 31.73  ? 160  ASN   A O    1 
ATOM   1790  C CB   . ASN   A  1 134 ? 23.717 11.991  5.082   1.00 33.84  ? 160  ASN   A CB   1 
ATOM   1791  C CG   . ASN   A  1 134 ? 22.962 11.855  6.373   1.00 39.98  ? 160  ASN   A CG   1 
ATOM   1792  O OD1  . ASN   A  1 134 ? 22.229 10.885  6.623   1.00 41.95  ? 160  ASN   A OD1  1 
ATOM   1793  N ND2  . ASN   A  1 134 ? 23.120 12.847  7.235   1.00 42.16  ? 160  ASN   A ND2  1 
ATOM   1794  H H    . ASN   A  1 134 ? 24.443 11.671  2.401   0.00 40.01  ? 160  ASN   A H    1 
ATOM   1795  H HA   . ASN   A  1 134 ? 23.177 9.988   4.452   0.00 42.39  ? 160  ASN   A HA   1 
ATOM   1796  H HB2  . ASN   A  1 134 ? 24.775 11.879  5.314   0.00 46.00  ? 160  ASN   A HB2  1 
ATOM   1797  H HB3  . ASN   A  1 134 ? 23.539 12.995  4.699   0.00 46.19  ? 160  ASN   A HB3  1 
ATOM   1798  H HD21 . ASN   A  1 134 ? 22.636 12.822  8.127   0.00 57.85  ? 160  ASN   A HD21 1 
ATOM   1799  H HD22 . ASN   A  1 134 ? 23.716 13.634  7.001   0.00 57.38  ? 160  ASN   A HD22 1 
ATOM   1800  N N    . ILE   A  1 135 ? 21.050 10.554  3.243   1.00 30.69  ? 161  ILE   A N    1 
ATOM   1801  C CA   . ILE   A  1 135 ? 19.769 10.831  2.588   1.00 31.11  ? 161  ILE   A CA   1 
ATOM   1802  C C    . ILE   A  1 135 ? 18.789 11.088  3.733   1.00 31.95  ? 161  ILE   A C    1 
ATOM   1803  O O    . ILE   A  1 135 ? 18.398 10.143  4.418   1.00 31.81  ? 161  ILE   A O    1 
ATOM   1804  C CB   . ILE   A  1 135 ? 19.316 9.638   1.696   1.00 31.12  ? 161  ILE   A CB   1 
ATOM   1805  C CG1  . ILE   A  1 135 ? 20.473 9.111   0.793   1.00 32.13  ? 161  ILE   A CG1  1 
ATOM   1806  C CG2  . ILE   A  1 135 ? 18.068 9.999   0.879   1.00 31.20  ? 161  ILE   A CG2  1 
ATOM   1807  C CD1  . ILE   A  1 135 ? 21.133 10.088  -0.062  1.00 33.61  ? 161  ILE   A CD1  1 
ATOM   1808  H H    . ILE   A  1 135 ? 21.055 9.653   3.712   0.00 41.52  ? 161  ILE   A H    1 
ATOM   1809  H HA   . ILE   A  1 135 ? 19.833 11.722  1.964   0.00 42.04  ? 161  ILE   A HA   1 
ATOM   1810  H HB   . ILE   A  1 135 ? 19.034 8.813   2.348   0.00 41.69  ? 161  ILE   A HB   1 
ATOM   1811  H HG12 . ILE   A  1 135 ? 21.239 8.664   1.426   0.00 42.07  ? 161  ILE   A HG12 1 
ATOM   1812  H HG13 . ILE   A  1 135 ? 20.067 8.340   0.140   0.00 41.72  ? 161  ILE   A HG13 1 
ATOM   1813  H HG21 . ILE   A  1 135 ? 17.879 9.211   0.152   0.00 41.27  ? 161  ILE   A HG21 1 
ATOM   1814  H HG22 . ILE   A  1 135 ? 17.213 10.086  1.547   0.00 42.16  ? 161  ILE   A HG22 1 
ATOM   1815  H HG23 . ILE   A  1 135 ? 18.238 10.945  0.367   0.00 41.66  ? 161  ILE   A HG23 1 
ATOM   1816  H HD11 . ILE   A  1 135 ? 21.866 9.573   -0.681  0.00 43.12  ? 161  ILE   A HD11 1 
ATOM   1817  H HD12 . ILE   A  1 135 ? 20.378 10.554  -0.691  0.00 43.61  ? 161  ILE   A HD12 1 
ATOM   1818  H HD13 . ILE   A  1 135 ? 21.635 10.838  0.548   0.00 43.91  ? 161  ILE   A HD13 1 
ATOM   1819  N N    . THR   A  1 136 ? 18.436 12.365  3.972   1.00 32.38  ? 162  THR   A N    1 
ATOM   1820  C CA   . THR   A  1 136 ? 17.605 12.752  5.109   1.00 33.23  ? 162  THR   A CA   1 
ATOM   1821  C C    . THR   A  1 136 ? 16.244 13.304  4.723   1.00 33.26  ? 162  THR   A C    1 
ATOM   1822  O O    . THR   A  1 136 ? 16.055 13.779  3.603   1.00 32.74  ? 162  THR   A O    1 
ATOM   1823  C CB   . THR   A  1 136 ? 18.367 13.795  5.955   1.00 35.14  ? 162  THR   A CB   1 
ATOM   1824  O OG1  . THR   A  1 136 ? 18.465 15.014  5.216   1.00 36.59  ? 162  THR   A OG1  1 
ATOM   1825  C CG2  . THR   A  1 136 ? 19.751 13.324  6.360   1.00 35.45  ? 162  THR   A CG2  1 
ATOM   1826  H H    . THR   A  1 136 ? 18.707 13.151  3.390   0.00 44.78  ? 162  THR   A H    1 
ATOM   1827  H HA   . THR   A  1 136 ? 17.431 11.893  5.754   0.00 46.76  ? 162  THR   A HA   1 
ATOM   1828  H HB   . THR   A  1 136 ? 17.801 13.985  6.867   0.00 50.08  ? 162  THR   A HB   1 
ATOM   1829  H HG1  . THR   A  1 136 ? 18.963 15.694  5.742   0.00 51.60  ? 162  THR   A HG1  1 
ATOM   1830  H HG21 . THR   A  1 136 ? 20.169 14.001  7.103   0.00 50.08  ? 162  THR   A HG21 1 
ATOM   1831  H HG22 . THR   A  1 136 ? 19.697 12.322  6.783   0.00 49.53  ? 162  THR   A HG22 1 
ATOM   1832  H HG23 . THR   A  1 136 ? 20.413 13.310  5.495   0.00 49.08  ? 162  THR   A HG23 1 
ATOM   1833  N N    . LYS   A  1 137 ? 15.305 13.261  5.683   1.00 33.94  ? 163  LYS   A N    1 
ATOM   1834  C CA   . LYS   A  1 137 ? 13.957 13.808  5.541   1.00 35.54  ? 163  LYS   A CA   1 
ATOM   1835  C C    . LYS   A  1 137 ? 14.012 15.310  5.271   1.00 36.99  ? 163  LYS   A C    1 
ATOM   1836  O O    . LYS   A  1 137 ? 13.221 15.814  4.481   1.00 36.94  ? 163  LYS   A O    1 
ATOM   1837  C CB   . LYS   A  1 137 ? 13.121 13.527  6.803   1.00 36.68  ? 163  LYS   A CB   1 
ATOM   1838  C CG   . LYS   A  1 137 ? 12.779 12.056  6.970   1.00 40.15  ? 163  LYS   A CG   1 
ATOM   1839  C CD   . LYS   A  1 137 ? 11.793 11.795  8.103   1.00 45.46  ? 163  LYS   A CD   1 
ATOM   1840  C CE   . LYS   A  1 137 ? 11.312 10.364  8.068   1.00 49.76  ? 163  LYS   A CE   1 
ATOM   1841  N NZ   . LYS   A  1 137 ? 10.461 10.022  9.239   1.00 52.55  ? 163  LYS   A NZ   1 
ATOM   1842  H H    . LYS   A  1 137 ? 15.468 12.845  6.594   0.00 48.75  ? 163  LYS   A H    1 
ATOM   1843  H HA   . LYS   A  1 137 ? 13.450 13.352  4.693   0.00 50.58  ? 163  LYS   A HA   1 
ATOM   1844  H HB2  . LYS   A  1 137 ? 13.674 13.851  7.683   0.00 53.34  ? 163  LYS   A HB2  1 
ATOM   1845  H HB3  . LYS   A  1 137 ? 12.185 14.079  6.733   0.00 53.44  ? 163  LYS   A HB3  1 
ATOM   1846  H HG2  . LYS   A  1 137 ? 12.319 11.705  6.048   0.00 56.54  ? 163  LYS   A HG2  1 
ATOM   1847  H HG3  . LYS   A  1 137 ? 13.690 11.496  7.174   0.00 56.56  ? 163  LYS   A HG3  1 
ATOM   1848  H HD2  . LYS   A  1 137 ? 12.286 11.970  9.058   0.00 64.33  ? 163  LYS   A HD2  1 
ATOM   1849  H HD3  . LYS   A  1 137 ? 10.931 12.451  7.992   0.00 64.44  ? 163  LYS   A HD3  1 
ATOM   1850  H HE2  . LYS   A  1 137 ? 10.725 10.207  7.164   0.00 68.68  ? 163  LYS   A HE2  1 
ATOM   1851  H HE3  . LYS   A  1 137 ? 12.175 9.699   8.074   0.00 68.47  ? 163  LYS   A HE3  1 
ATOM   1852  H HZ1  . LYS   A  1 137 ? 10.145 9.060   9.168   0.00 72.83  ? 163  LYS   A HZ1  1 
ATOM   1853  H HZ2  . LYS   A  1 137 ? 10.990 10.135  10.098  0.00 73.24  ? 163  LYS   A HZ2  1 
ATOM   1854  H HZ3  . LYS   A  1 137 ? 9.651  10.633  9.266   0.00 73.46  ? 163  LYS   A HZ3  1 
ATOM   1855  N N    . GLU   A  1 138 ? 14.961 16.018  5.907   1.00 38.12  ? 164  GLU   A N    1 
ATOM   1856  C CA   . GLU   A  1 138 ? 15.152 17.455  5.707   1.00 39.46  ? 164  GLU   A CA   1 
ATOM   1857  C C    . GLU   A  1 138 ? 15.418 17.766  4.221   1.00 39.37  ? 164  GLU   A C    1 
ATOM   1858  O O    . GLU   A  1 138 ? 14.905 18.750  3.699   1.00 39.61  ? 164  GLU   A O    1 
ATOM   1859  C CB   . GLU   A  1 138 ? 16.337 17.955  6.560   1.00 43.37  ? 164  GLU   A CB   1 
ATOM   1860  C CG   . GLU   A  1 138 ? 16.387 19.465  6.734   1.00 51.49  ? 164  GLU   A CG   1 
ATOM   1861  C CD   . GLU   A  1 138 ? 17.736 20.092  6.439   1.00 61.59  ? 164  GLU   A CD   1 
ATOM   1862  O OE1  . GLU   A  1 138 ? 18.759 19.588  6.959   1.00 62.84  ? 164  GLU   A OE1  1 
ATOM   1863  O OE2  . GLU   A  1 138 ? 17.767 21.100  5.695   1.00 65.88  ? 164  GLU   A OE2  1 
ATOM   1864  H H    . GLU   A  1 138 ? 15.610 15.617  6.576   0.00 54.61  ? 164  GLU   A H    1 
ATOM   1865  H HA   . GLU   A  1 138 ? 14.249 17.981  6.012   0.00 57.22  ? 164  GLU   A HA   1 
ATOM   1866  H HB2  . GLU   A  1 138 ? 16.270 17.523  7.558   0.00 61.88  ? 164  GLU   A HB2  1 
ATOM   1867  H HB3  . GLU   A  1 138 ? 17.262 17.635  6.083   0.00 60.99  ? 164  GLU   A HB3  1 
ATOM   1868  H HG2  . GLU   A  1 138 ? 15.658 19.927  6.070   0.00 72.04  ? 164  GLU   A HG2  1 
ATOM   1869  H HG3  . GLU   A  1 138 ? 16.138 19.700  7.767   0.00 72.64  ? 164  GLU   A HG3  1 
ATOM   1870  N N    . GLY   A  1 139 ? 16.184 16.908  3.557   1.00 39.02  ? 165  GLY   A N    1 
ATOM   1871  C CA   . GLY   A  1 139 ? 16.530 17.082  2.157   1.00 39.56  ? 165  GLY   A CA   1 
ATOM   1872  C C    . GLY   A  1 139 ? 15.457 16.749  1.134   1.00 39.79  ? 165  GLY   A C    1 
ATOM   1873  O O    . GLY   A  1 139 ? 15.280 17.524  0.190   1.00 39.94  ? 165  GLY   A O    1 
ATOM   1874  H H    . GLY   A  1 139 ? 16.605 16.079  3.965   0.00 54.45  ? 165  GLY   A H    1 
ATOM   1875  H HA2  . GLY   A  1 139 ? 16.835 18.115  1.992   0.00 54.97  ? 165  GLY   A HA2  1 
ATOM   1876  H HA3  . GLY   A  1 139 ? 17.391 16.451  1.939   0.00 54.19  ? 165  GLY   A HA3  1 
ATOM   1877  N N    . ILE   A  1 140 ? 14.758 15.588  1.265   1.00 39.58  ? 166  ILE   A N    1 
ATOM   1878  C CA   . ILE   A  1 140 ? 13.807 15.172  0.222   1.00 40.18  ? 166  ILE   A CA   1 
ATOM   1879  C C    . ILE   A  1 140 ? 12.363 14.847  0.657   1.00 40.88  ? 166  ILE   A C    1 
ATOM   1880  O O    . ILE   A  1 140 ? 11.547 14.648  -0.242  1.00 40.91  ? 166  ILE   A O    1 
ATOM   1881  C CB   . ILE   A  1 140 ? 14.374 13.960  -0.566  1.00 40.69  ? 166  ILE   A CB   1 
ATOM   1882  C CG1  . ILE   A  1 140 ? 14.437 12.680  0.294   1.00 41.54  ? 166  ILE   A CG1  1 
ATOM   1883  C CG2  . ILE   A  1 140 ? 15.750 14.288  -1.158  1.00 41.08  ? 166  ILE   A CG2  1 
ATOM   1884  C CD1  . ILE   A  1 140 ? 14.684 11.441  -0.511  1.00 43.04  ? 166  ILE   A CD1  1 
ATOM   1885  H H    . ILE   A  1 140 ? 14.834 14.950  2.050   0.00 54.45  ? 166  ILE   A H    1 
ATOM   1886  H HA   . ILE   A  1 140 ? 13.710 15.972  -0.510  0.00 54.89  ? 166  ILE   A HA   1 
ATOM   1887  H HB   . ILE   A  1 140 ? 13.705 13.765  -1.403  0.00 54.48  ? 166  ILE   A HB   1 
ATOM   1888  H HG12 . ILE   A  1 140 ? 15.252 12.779  1.009   0.00 55.56  ? 166  ILE   A HG12 1 
ATOM   1889  H HG13 . ILE   A  1 140 ? 13.500 12.524  0.827   0.00 55.99  ? 166  ILE   A HG13 1 
ATOM   1890  H HG21 . ILE   A  1 140 ? 16.007 13.538  -1.905  0.00 54.00  ? 166  ILE   A HG21 1 
ATOM   1891  H HG22 . ILE   A  1 140 ? 15.710 15.273  -1.620  0.00 54.73  ? 166  ILE   A HG22 1 
ATOM   1892  H HG23 . ILE   A  1 140 ? 16.493 14.282  -0.362  0.00 54.65  ? 166  ILE   A HG23 1 
ATOM   1893  H HD11 . ILE   A  1 140 ? 14.544 10.563  0.116   0.00 56.67  ? 166  ILE   A HD11 1 
ATOM   1894  H HD12 . ILE   A  1 140 ? 13.984 11.413  -1.344  0.00 56.61  ? 166  ILE   A HD12 1 
ATOM   1895  H HD13 . ILE   A  1 140 ? 15.706 11.458  -0.887  0.00 56.20  ? 166  ILE   A HD13 1 
ATOM   1896  N N    . SER   A  1 141 ? 12.030 14.756  1.966   1.00 41.31  ? 167  SER   A N    1 
ATOM   1897  C CA   . SER   A  1 141 ? 10.656 14.398  2.348   1.00 42.26  ? 167  SER   A CA   1 
ATOM   1898  C C    . SER   A  1 141 ? 9.618  15.475  2.004   1.00 41.82  ? 167  SER   A C    1 
ATOM   1899  O O    . SER   A  1 141 ? 8.461  15.124  1.786   1.00 41.99  ? 167  SER   A O    1 
ATOM   1900  C CB   . SER   A  1 141 ? 10.572 13.986  3.815   1.00 45.12  ? 167  SER   A CB   1 
ATOM   1901  O OG   . SER   A  1 141 ? 11.240 12.740  3.998   1.00 48.36  ? 167  SER   A OG   1 
ATOM   1902  H H    . SER   A  1 141 ? 12.660 14.916  2.745   0.00 57.46  ? 167  SER   A H    1 
ATOM   1903  H HA   . SER   A  1 141 ? 10.366 13.537  1.747   0.00 58.56  ? 167  SER   A HA   1 
ATOM   1904  H HB2  . SER   A  1 141 ? 11.051 14.744  4.433   0.00 63.20  ? 167  SER   A HB2  1 
ATOM   1905  H HB3  . SER   A  1 141 ? 9.522  13.893  4.090   0.00 63.32  ? 167  SER   A HB3  1 
ATOM   1906  H HG   . SER   A  1 141 ? 10.754 12.167  4.648   0.00 66.46  ? 167  SER   A HG   1 
ATOM   1907  N N    . ARG   A  1 142 ? 10.017 16.750  1.878   1.00 41.44  ? 168  ARG   A N    1 
ATOM   1908  C CA   . ARG   A  1 142 ? 9.086  17.800  1.430   1.00 41.76  ? 168  ARG   A CA   1 
ATOM   1909  C C    . ARG   A  1 142 ? 8.850  17.753  -0.103  1.00 40.97  ? 168  ARG   A C    1 
ATOM   1910  O O    . ARG   A  1 142 ? 7.921  18.392  -0.587  1.00 40.92  ? 168  ARG   A O    1 
ATOM   1911  C CB   . ARG   A  1 142 ? 9.586  19.206  1.847   1.00 44.50  ? 168  ARG   A CB   1 
ATOM   1912  C CG   . ARG   A  1 142 ? 9.211  19.591  3.276   1.00 50.19  ? 168  ARG   A CG   1 
ATOM   1913  C CD   . ARG   A  1 142 ? 9.979  20.791  3.799   1.00 55.95  ? 168  ARG   A CD   1 
ATOM   1914  N NE   . ARG   A  1 142 ? 11.343 20.429  4.184   1.00 60.77  ? 168  ARG   A NE   1 
ATOM   1915  C CZ   . ARG   A  1 142 ? 12.134 21.158  4.971   1.00 64.22  ? 168  ARG   A CZ   1 
ATOM   1916  N NH1  . ARG   A  1 142 ? 11.708 22.317  5.469   1.00 64.36  ? 168  ARG   A NH1  1 
ATOM   1917  N NH2  . ARG   A  1 142 ? 13.358 20.735  5.265   1.00 64.63  ? 168  ARG   A NH2  1 
ATOM   1918  H H    . ARG   A  1 142 ? 10.945 17.087  2.118   0.00 58.72  ? 168  ARG   A H    1 
ATOM   1919  H HA   . ARG   A  1 142 ? 8.112  17.631  1.887   0.00 60.31  ? 168  ARG   A HA   1 
ATOM   1920  H HB2  . ARG   A  1 142 ? 10.670 19.257  1.761   0.00 63.22  ? 168  ARG   A HB2  1 
ATOM   1921  H HB3  . ARG   A  1 142 ? 9.141  19.946  1.184   0.00 63.89  ? 168  ARG   A HB3  1 
ATOM   1922  H HG2  . ARG   A  1 142 ? 8.151  19.838  3.306   0.00 71.86  ? 168  ARG   A HG2  1 
ATOM   1923  H HG3  . ARG   A  1 142 ? 9.415  18.747  3.934   0.00 71.15  ? 168  ARG   A HG3  1 
ATOM   1924  H HD2  . ARG   A  1 142 ? 10.032 21.561  3.031   0.00 78.70  ? 168  ARG   A HD2  1 
ATOM   1925  H HD3  . ARG   A  1 142 ? 9.449  21.157  4.677   0.00 79.40  ? 168  ARG   A HD3  1 
ATOM   1926  H HE   . ARG   A  1 142 ? 11.705 19.551  3.827   0.00 83.31  ? 168  ARG   A HE   1 
ATOM   1927  H HH11 . ARG   A  1 142 ? 10.787 22.692  5.265   0.00 89.97  ? 168  ARG   A HH11 1 
ATOM   1928  H HH12 . ARG   A  1 142 ? 12.325 22.861  6.063   0.00 89.86  ? 168  ARG   A HH12 1 
ATOM   1929  H HH21 . ARG   A  1 142 ? 13.691 19.851  4.894   0.00 87.87  ? 168  ARG   A HH21 1 
ATOM   1930  H HH22 . ARG   A  1 142 ? 13.966 21.285  5.863   0.00 88.83  ? 168  ARG   A HH22 1 
ATOM   1931  N N    . LEU   A  1 143 ? 9.648  16.981  -0.864  1.00 40.15  ? 169  LEU   A N    1 
ATOM   1932  C CA   . LEU   A  1 143 ? 9.493  16.893  -2.312  1.00 39.38  ? 169  LEU   A CA   1 
ATOM   1933  C C    . LEU   A  1 143 ? 8.464  15.817  -2.676  1.00 38.68  ? 169  LEU   A C    1 
ATOM   1934  O O    . LEU   A  1 143 ? 8.781  14.835  -3.340  1.00 38.64  ? 169  LEU   A O    1 
ATOM   1935  C CB   . LEU   A  1 143 ? 10.855 16.636  -2.975  1.00 39.45  ? 169  LEU   A CB   1 
ATOM   1936  C CG   . LEU   A  1 143 ? 12.009 17.549  -2.558  1.00 41.00  ? 169  LEU   A CG   1 
ATOM   1937  C CD1  . LEU   A  1 143 ? 13.282 17.172  -3.299  1.00 41.62  ? 169  LEU   A CD1  1 
ATOM   1938  C CD2  . LEU   A  1 143 ? 11.673 19.019  -2.811  1.00 41.56  ? 169  LEU   A CD2  1 
ATOM   1939  H H    . LEU   A  1 143 ? 10.407 16.406  -0.515  0.00 56.16  ? 169  LEU   A H    1 
ATOM   1940  H HA   . LEU   A  1 143 ? 9.122  17.839  -2.703  0.00 55.54  ? 169  LEU   A HA   1 
ATOM   1941  H HB2  . LEU   A  1 143 ? 11.167 15.607  -2.803  0.00 53.99  ? 169  LEU   A HB2  1 
ATOM   1942  H HB3  . LEU   A  1 143 ? 10.716 16.824  -4.038  0.00 54.21  ? 169  LEU   A HB3  1 
ATOM   1943  H HG   . LEU   A  1 143 ? 12.196 17.432  -1.492  0.00 56.56  ? 169  LEU   A HG   1 
ATOM   1944  H HD11 . LEU   A  1 143 ? 14.088 17.832  -2.980  0.00 56.32  ? 169  LEU   A HD11 1 
ATOM   1945  H HD12 . LEU   A  1 143 ? 13.533 16.138  -3.067  0.00 55.86  ? 169  LEU   A HD12 1 
ATOM   1946  H HD13 . LEU   A  1 143 ? 13.114 17.281  -4.370  0.00 56.00  ? 169  LEU   A HD13 1 
ATOM   1947  H HD21 . LEU   A  1 143 ? 12.548 19.628  -2.590  0.00 57.62  ? 169  LEU   A HD21 1 
ATOM   1948  H HD22 . LEU   A  1 143 ? 11.390 19.142  -3.856  0.00 57.43  ? 169  LEU   A HD22 1 
ATOM   1949  H HD23 . LEU   A  1 143 ? 10.851 19.321  -2.164  0.00 58.25  ? 169  LEU   A HD23 1 
ATOM   1950  N N    . ILE   A  1 144 ? 7.209  16.064  -2.307  1.00 38.27  ? 170  ILE   A N    1 
ATOM   1951  C CA   . ILE   A  1 144 ? 6.110  15.114  -2.486  1.00 38.30  ? 170  ILE   A CA   1 
ATOM   1952  C C    . ILE   A  1 144 ? 5.709  14.847  -3.953  1.00 36.99  ? 170  ILE   A C    1 
ATOM   1953  O O    . ILE   A  1 144 ? 5.078  13.818  -4.192  1.00 36.93  ? 170  ILE   A O    1 
ATOM   1954  C CB   . ILE   A  1 144 ? 4.864  15.491  -1.634  1.00 39.65  ? 170  ILE   A CB   1 
ATOM   1955  C CG1  . ILE   A  1 144 ? 4.038  16.669  -2.226  1.00 41.23  ? 170  ILE   A CG1  1 
ATOM   1956  C CG2  . ILE   A  1 144 ? 5.246  15.755  -0.173  1.00 40.60  ? 170  ILE   A CG2  1 
ATOM   1957  C CD1  . ILE   A  1 144 ? 4.741  17.876  -2.600  1.00 43.12  ? 170  ILE   A CD1  1 
ATOM   1958  H H    . ILE   A  1 144 ? 6.930  16.948  -1.894  0.00 55.04  ? 170  ILE   A H    1 
ATOM   1959  H HA   . ILE   A  1 144 ? 6.459  14.159  -2.100  0.00 54.27  ? 170  ILE   A HA   1 
ATOM   1960  H HB   . ILE   A  1 144 ? 4.205  14.625  -1.638  0.00 57.23  ? 170  ILE   A HB   1 
ATOM   1961  H HG12 . ILE   A  1 144 ? 3.492  16.319  -3.101  0.00 59.59  ? 170  ILE   A HG12 1 
ATOM   1962  H HG13 . ILE   A  1 144 ? 3.324  16.983  -1.468  0.00 60.44  ? 170  ILE   A HG13 1 
ATOM   1963  H HG21 . ILE   A  1 144 ? 4.341  15.764  0.432   0.00 59.40  ? 170  ILE   A HG21 1 
ATOM   1964  H HG22 . ILE   A  1 144 ? 5.912  14.964  0.166   0.00 58.30  ? 170  ILE   A HG22 1 
ATOM   1965  H HG23 . ILE   A  1 144 ? 5.750  16.717  -0.092  0.00 58.87  ? 170  ILE   A HG23 1 
ATOM   1966  H HD11 . ILE   A  1 144 ? 4.015  18.597  -2.972  0.00 62.53  ? 170  ILE   A HD11 1 
ATOM   1967  H HD12 . ILE   A  1 144 ? 5.245  18.288  -1.727  0.00 62.21  ? 170  ILE   A HD12 1 
ATOM   1968  H HD13 . ILE   A  1 144 ? 5.467  17.661  -3.382  0.00 61.34  ? 170  ILE   A HD13 1 
ATOM   1969  N N    . ASN   A  1 145 ? 6.091  15.706  -4.924  1.00 35.71  ? 171  ASN   A N    1 
ATOM   1970  C CA   . ASN   A  1 145 ? 5.780  15.474  -6.337  1.00 35.04  ? 171  ASN   A CA   1 
ATOM   1971  C C    . ASN   A  1 145 ? 6.913  14.695  -7.062  1.00 34.78  ? 171  ASN   A C    1 
ATOM   1972  O O    . ASN   A  1 145 ? 6.810  14.498  -8.275  1.00 35.16  ? 171  ASN   A O    1 
ATOM   1973  C CB   . ASN   A  1 145 ? 5.517  16.807  -7.049  1.00 35.65  ? 171  ASN   A CB   1 
ATOM   1974  C CG   . ASN   A  1 145 ? 4.301  17.532  -6.511  1.00 38.36  ? 171  ASN   A CG   1 
ATOM   1975  O OD1  . ASN   A  1 145 ? 3.198  16.977  -6.473  1.00 39.63  ? 171  ASN   A OD1  1 
ATOM   1976  N ND2  . ASN   A  1 145 ? 4.464  18.778  -6.077  1.00 38.02  ? 171  ASN   A ND2  1 
ATOM   1977  H H    . ASN   A  1 145 ? 6.634  16.550  -4.774  0.00 51.09  ? 171  ASN   A H    1 
ATOM   1978  H HA   . ASN   A  1 145 ? 4.869  14.883  -6.426  0.00 50.06  ? 171  ASN   A HA   1 
ATOM   1979  H HB2  . ASN   A  1 145 ? 6.392  17.446  -6.941  0.00 50.87  ? 171  ASN   A HB2  1 
ATOM   1980  H HB3  . ASN   A  1 145 ? 5.329  16.618  -8.105  0.00 50.77  ? 171  ASN   A HB3  1 
ATOM   1981  H HD21 . ASN   A  1 145 ? 3.666  19.288  -5.710  0.00 56.09  ? 171  ASN   A HD21 1 
ATOM   1982  H HD22 . ASN   A  1 145 ? 5.373  19.227  -6.103  0.00 55.12  ? 171  ASN   A HD22 1 
ATOM   1983  N N    . LEU   A  1 146 ? 7.987  14.268  -6.355  1.00 33.51  ? 172  LEU   A N    1 
ATOM   1984  C CA   . LEU   A  1 146 ? 9.081  13.536  -6.995  1.00 32.92  ? 172  LEU   A CA   1 
ATOM   1985  C C    . LEU   A  1 146 ? 8.595  12.252  -7.657  1.00 32.17  ? 172  LEU   A C    1 
ATOM   1986  O O    . LEU   A  1 146 ? 7.888  11.463  -7.034  1.00 31.85  ? 172  LEU   A O    1 
ATOM   1987  C CB   . LEU   A  1 146 ? 10.211 13.165  -6.004  1.00 32.86  ? 172  LEU   A CB   1 
ATOM   1988  C CG   . LEU   A  1 146 ? 11.379 14.142  -5.815  1.00 34.11  ? 172  LEU   A CG   1 
ATOM   1989  C CD1  . LEU   A  1 146 ? 12.444 13.534  -4.895  1.00 34.85  ? 172  LEU   A CD1  1 
ATOM   1990  C CD2  . LEU   A  1 146 ? 12.003 14.560  -7.139  1.00 33.99  ? 172  LEU   A CD2  1 
ATOM   1991  H H    . LEU   A  1 146 ? 8.126  14.426  -5.362  0.00 46.90  ? 172  LEU   A H    1 
ATOM   1992  H HA   . LEU   A  1 146 ? 9.494  14.171  -7.775  0.00 44.90  ? 172  LEU   A HA   1 
ATOM   1993  H HB2  . LEU   A  1 146 ? 9.779  12.992  -5.020  0.00 45.10  ? 172  LEU   A HB2  1 
ATOM   1994  H HB3  . LEU   A  1 146 ? 10.649 12.233  -6.355  0.00 44.17  ? 172  LEU   A HB3  1 
ATOM   1995  H HG   . LEU   A  1 146 ? 10.995 15.040  -5.339  0.00 46.69  ? 172  LEU   A HG   1 
ATOM   1996  H HD11 . LEU   A  1 146 ? 13.209 14.280  -4.688  0.00 46.74  ? 172  LEU   A HD11 1 
ATOM   1997  H HD12 . LEU   A  1 146 ? 11.972 13.217  -3.966  0.00 47.06  ? 172  LEU   A HD12 1 
ATOM   1998  H HD13 . LEU   A  1 146 ? 12.890 12.675  -5.394  0.00 46.15  ? 172  LEU   A HD13 1 
ATOM   1999  H HD21 . LEU   A  1 146 ? 13.031 14.872  -6.965  0.00 45.28  ? 172  LEU   A HD21 1 
ATOM   2000  H HD22 . LEU   A  1 146 ? 11.979 13.716  -7.828  0.00 45.07  ? 172  LEU   A HD22 1 
ATOM   2001  H HD23 . LEU   A  1 146 ? 11.440 15.396  -7.551  0.00 45.87  ? 172  LEU   A HD23 1 
ATOM   2002  N N    . LYS   A  1 147 ? 8.979  12.065  -8.922  1.00 31.34  ? 173  LYS   A N    1 
ATOM   2003  C CA   . LYS   A  1 147 ? 8.673  10.897  -9.743  1.00 31.21  ? 173  LYS   A CA   1 
ATOM   2004  C C    . LYS   A  1 147 ? 9.972  10.110  -9.968  1.00 29.85  ? 173  LYS   A C    1 
ATOM   2005  O O    . LYS   A  1 147 ? 9.960  8.886   -9.862  1.00 29.97  ? 173  LYS   A O    1 
ATOM   2006  C CB   . LYS   A  1 147 ? 8.079  11.335  -11.093 1.00 34.52  ? 173  LYS   A CB   1 
ATOM   2007  C CG   . LYS   A  1 147 ? 7.460  10.193  -11.899 1.00 41.22  ? 173  LYS   A CG   1 
ATOM   2008  C CD   . LYS   A  1 147 ? 7.066  10.618  -13.324 1.00 47.39  ? 173  LYS   A CD   1 
ATOM   2009  C CE   . LYS   A  1 147 ? 8.190  10.421  -14.317 1.00 52.40  ? 173  LYS   A CE   1 
ATOM   2010  N NZ   . LYS   A  1 147 ? 7.770  10.722  -15.716 1.00 55.33  ? 173  LYS   A NZ   1 
ATOM   2011  H H    . LYS   A  1 147 ? 9.520  12.748  -9.440  0.00 42.16  ? 173  LYS   A H    1 
ATOM   2012  H HA   . LYS   A  1 147 ? 7.955  10.250  -9.242  0.00 42.04  ? 173  LYS   A HA   1 
ATOM   2013  H HB2  . LYS   A  1 147 ? 7.302  12.075  -10.911 0.00 46.42  ? 173  LYS   A HB2  1 
ATOM   2014  H HB3  . LYS   A  1 147 ? 8.871  11.774  -11.697 0.00 45.49  ? 173  LYS   A HB3  1 
ATOM   2015  H HG2  . LYS   A  1 147 ? 8.173  9.375   -11.981 0.00 53.19  ? 173  LYS   A HG2  1 
ATOM   2016  H HG3  . LYS   A  1 147 ? 6.559  9.852   -11.391 0.00 54.14  ? 173  LYS   A HG3  1 
ATOM   2017  H HD2  . LYS   A  1 147 ? 6.218  10.020  -13.653 0.00 61.31  ? 173  LYS   A HD2  1 
ATOM   2018  H HD3  . LYS   A  1 147 ? 6.797  11.673  -13.319 0.00 61.54  ? 173  LYS   A HD3  1 
ATOM   2019  H HE2  . LYS   A  1 147 ? 9.011  11.088  -14.058 0.00 66.29  ? 173  LYS   A HE2  1 
ATOM   2020  H HE3  . LYS   A  1 147 ? 8.526  9.386   -14.286 0.00 66.04  ? 173  LYS   A HE3  1 
ATOM   2021  H HZ1  . LYS   A  1 147 ? 8.554  10.597  -16.349 0.00 69.50  ? 173  LYS   A HZ1  1 
ATOM   2022  H HZ2  . LYS   A  1 147 ? 7.021  10.096  -15.994 0.00 70.11  ? 173  LYS   A HZ2  1 
ATOM   2023  H HZ3  . LYS   A  1 147 ? 7.440  11.679  -15.781 0.00 70.37  ? 173  LYS   A HZ3  1 
ATOM   2024  N N    . ASN   A  1 148 ? 11.080 10.794  -10.305 1.00 28.64  ? 174  ASN   A N    1 
ATOM   2025  C CA   . ASN   A  1 148 ? 12.356 10.123  -10.546 1.00 28.62  ? 174  ASN   A CA   1 
ATOM   2026  C C    . ASN   A  1 148 ? 13.447 10.723  -9.662  1.00 28.46  ? 174  ASN   A C    1 
ATOM   2027  O O    . ASN   A  1 148 ? 13.678 11.929  -9.710  1.00 28.82  ? 174  ASN   A O    1 
ATOM   2028  C CB   . ASN   A  1 148 ? 12.764 10.238  -12.014 1.00 29.85  ? 174  ASN   A CB   1 
ATOM   2029  C CG   . ASN   A  1 148 ? 11.731 9.744   -13.016 1.00 33.67  ? 174  ASN   A CG   1 
ATOM   2030  O OD1  . ASN   A  1 148 ? 10.888 8.893   -12.729 1.00 34.46  ? 174  ASN   A OD1  1 
ATOM   2031  N ND2  . ASN   A  1 148 ? 11.807 10.228  -14.240 1.00 34.92  ? 174  ASN   A ND2  1 
ATOM   2032  H H    . ASN   A  1 148 ? 11.120 11.800  -10.429 0.00 37.81  ? 174  ASN   A H    1 
ATOM   2033  H HA   . ASN   A  1 148 ? 12.280 9.066   -10.298 0.00 36.71  ? 174  ASN   A HA   1 
ATOM   2034  H HB2  . ASN   A  1 148 ? 12.969 11.285  -12.227 0.00 38.05  ? 174  ASN   A HB2  1 
ATOM   2035  H HB3  . ASN   A  1 148 ? 13.669 9.653   -12.168 0.00 37.43  ? 174  ASN   A HB3  1 
ATOM   2036  H HD21 . ASN   A  1 148 ? 11.137 9.929   -14.942 0.00 44.00  ? 174  ASN   A HD21 1 
ATOM   2037  H HD22 . ASN   A  1 148 ? 12.541 10.881  -14.490 0.00 43.77  ? 174  ASN   A HD22 1 
ATOM   2038  N N    . LEU   A  1 149 ? 14.118 9.885   -8.863  1.00 27.52  ? 175  LEU   A N    1 
ATOM   2039  C CA   . LEU   A  1 149 ? 15.180 10.337  -7.972  1.00 27.22  ? 175  LEU   A CA   1 
ATOM   2040  C C    . LEU   A  1 149 ? 16.431 9.513   -8.232  1.00 26.98  ? 175  LEU   A C    1 
ATOM   2041  O O    . LEU   A  1 149 ? 16.423 8.302   -8.002  1.00 27.03  ? 175  LEU   A O    1 
ATOM   2042  C CB   . LEU   A  1 149 ? 14.739 10.196  -6.498  1.00 27.20  ? 175  LEU   A CB   1 
ATOM   2043  C CG   . LEU   A  1 149 ? 15.778 10.594  -5.436  1.00 27.91  ? 175  LEU   A CG   1 
ATOM   2044  C CD1  . LEU   A  1 149 ? 16.306 12.027  -5.662  1.00 27.63  ? 175  LEU   A CD1  1 
ATOM   2045  C CD2  . LEU   A  1 149 ? 15.196 10.442  -4.031  1.00 28.16  ? 175  LEU   A CD2  1 
ATOM   2046  H H    . LEU   A  1 149 ? 13.951 8.885   -8.806  0.00 35.13  ? 175  LEU   A H    1 
ATOM   2047  H HA   . LEU   A  1 149 ? 15.409 11.384  -8.160  0.00 35.06  ? 175  LEU   A HA   1 
ATOM   2048  H HB2  . LEU   A  1 149 ? 13.855 10.812  -6.344  0.00 35.88  ? 175  LEU   A HB2  1 
ATOM   2049  H HB3  . LEU   A  1 149 ? 14.483 9.153   -6.318  0.00 35.30  ? 175  LEU   A HB3  1 
ATOM   2050  H HG   . LEU   A  1 149 ? 16.631 9.919   -5.496  0.00 35.91  ? 175  LEU   A HG   1 
ATOM   2051  H HD11 . LEU   A  1 149 ? 16.876 12.336  -4.786  0.00 36.32  ? 175  LEU   A HD11 1 
ATOM   2052  H HD12 . LEU   A  1 149 ? 16.953 12.037  -6.537  0.00 35.70  ? 175  LEU   A HD12 1 
ATOM   2053  H HD13 . LEU   A  1 149 ? 15.461 12.696  -5.813  0.00 36.53  ? 175  LEU   A HD13 1 
ATOM   2054  H HD21 . LEU   A  1 149 ? 15.945 10.740  -3.298  0.00 37.29  ? 175  LEU   A HD21 1 
ATOM   2055  H HD22 . LEU   A  1 149 ? 14.317 11.078  -3.942  0.00 37.66  ? 175  LEU   A HD22 1 
ATOM   2056  H HD23 . LEU   A  1 149 ? 14.918 9.400   -3.874  0.00 37.10  ? 175  LEU   A HD23 1 
ATOM   2057  N N    . TYR   A  1 150 ? 17.503 10.171  -8.724  1.00 26.38  ? 176  TYR   A N    1 
ATOM   2058  C CA   . TYR   A  1 150 ? 18.757 9.499   -9.015  1.00 26.61  ? 176  TYR   A CA   1 
ATOM   2059  C C    . TYR   A  1 150 ? 19.819 9.917   -8.020  1.00 27.03  ? 176  TYR   A C    1 
ATOM   2060  O O    . TYR   A  1 150 ? 20.180 11.089  -7.962  1.00 27.38  ? 176  TYR   A O    1 
ATOM   2061  C CB   . TYR   A  1 150 ? 19.251 9.795   -10.438 1.00 26.75  ? 176  TYR   A CB   1 
ATOM   2062  C CG   . TYR   A  1 150 ? 18.217 9.611   -11.526 1.00 27.76  ? 176  TYR   A CG   1 
ATOM   2063  C CD1  . TYR   A  1 150 ? 17.292 10.607  -11.810 1.00 28.85  ? 176  TYR   A CD1  1 
ATOM   2064  C CD2  . TYR   A  1 150 ? 18.211 8.471   -12.318 1.00 28.99  ? 176  TYR   A CD2  1 
ATOM   2065  C CE1  . TYR   A  1 150 ? 16.348 10.448  -12.815 1.00 30.24  ? 176  TYR   A CE1  1 
ATOM   2066  C CE2  . TYR   A  1 150 ? 17.275 8.304   -13.332 1.00 30.33  ? 176  TYR   A CE2  1 
ATOM   2067  C CZ   . TYR   A  1 150 ? 16.334 9.289   -13.567 1.00 31.77  ? 176  TYR   A CZ   1 
ATOM   2068  O OH   . TYR   A  1 150 ? 15.408 9.151   -14.573 1.00 34.83  ? 176  TYR   A OH   1 
ATOM   2069  H H    . TYR   A  1 150 ? 17.522 11.165  -8.928  0.00 33.17  ? 176  TYR   A H    1 
ATOM   2070  H HA   . TYR   A  1 150 ? 18.628 8.422   -8.942  0.00 32.56  ? 176  TYR   A HA   1 
ATOM   2071  H HB2  . TYR   A  1 150 ? 19.660 10.799  -10.518 0.00 32.57  ? 176  TYR   A HB2  1 
ATOM   2072  H HB3  . TYR   A  1 150 ? 20.046 9.077   -10.630 0.00 32.08  ? 176  TYR   A HB3  1 
ATOM   2073  H HD1  . TYR   A  1 150 ? 17.283 11.504  -11.215 0.00 35.72  ? 176  TYR   A HD1  1 
ATOM   2074  H HD2  . TYR   A  1 150 ? 18.925 7.687   -12.131 0.00 34.44  ? 176  TYR   A HD2  1 
ATOM   2075  H HE1  . TYR   A  1 150 ? 15.621 11.222  -13.001 0.00 37.45  ? 176  TYR   A HE1  1 
ATOM   2076  H HE2  . TYR   A  1 150 ? 17.278 7.399   -13.916 0.00 36.07  ? 176  TYR   A HE2  1 
ATOM   2077  H HH   . TYR   A  1 150 ? 15.483 8.262   -15.006 0.00 41.97  ? 176  TYR   A HH   1 
ATOM   2078  N N    . LEU   A  1 151 ? 20.320 8.965   -7.243  1.00 26.44  ? 177  LEU   A N    1 
ATOM   2079  C CA   . LEU   A  1 151 ? 21.378 9.182   -6.259  1.00 26.31  ? 177  LEU   A CA   1 
ATOM   2080  C C    . LEU   A  1 151 ? 22.566 8.216   -6.474  1.00 25.83  ? 177  LEU   A C    1 
ATOM   2081  O O    . LEU   A  1 151 ? 23.396 8.050   -5.577  1.00 26.11  ? 177  LEU   A O    1 
ATOM   2082  C CB   . LEU   A  1 151 ? 20.767 8.980   -4.860  1.00 26.85  ? 177  LEU   A CB   1 
ATOM   2083  C CG   . LEU   A  1 151 ? 19.754 10.032  -4.411  1.00 28.63  ? 177  LEU   A CG   1 
ATOM   2084  C CD1  . LEU   A  1 151 ? 18.834 9.474   -3.327  1.00 29.32  ? 177  LEU   A CD1  1 
ATOM   2085  C CD2  . LEU   A  1 151 ? 20.462 11.242  -3.872  1.00 29.79  ? 177  LEU   A CD2  1 
ATOM   2086  H H    . LEU   A  1 151 ? 20.002 8.001   -7.256  0.00 32.40  ? 177  LEU   A H    1 
ATOM   2087  H HA   . LEU   A  1 151 ? 21.773 10.194  -6.332  0.00 32.60  ? 177  LEU   A HA   1 
ATOM   2088  H HB2  . LEU   A  1 151 ? 20.251 8.022   -4.859  0.00 33.56  ? 177  LEU   A HB2  1 
ATOM   2089  H HB3  . LEU   A  1 151 ? 21.561 8.971   -4.116  0.00 33.72  ? 177  LEU   A HB3  1 
ATOM   2090  H HG   . LEU   A  1 151 ? 19.129 10.347  -5.245  0.00 36.33  ? 177  LEU   A HG   1 
ATOM   2091  H HD11 . LEU   A  1 151 ? 18.203 10.279  -2.954  0.00 38.10  ? 177  LEU   A HD11 1 
ATOM   2092  H HD12 . LEU   A  1 151 ? 18.216 8.688   -3.759  0.00 37.48  ? 177  LEU   A HD12 1 
ATOM   2093  H HD13 . LEU   A  1 151 ? 19.442 9.070   -2.520  0.00 37.68  ? 177  LEU   A HD13 1 
ATOM   2094  H HD21 . LEU   A  1 151 ? 19.748 12.059  -3.778  0.00 38.47  ? 177  LEU   A HD21 1 
ATOM   2095  H HD22 . LEU   A  1 151 ? 20.872 10.998  -2.893  0.00 38.25  ? 177  LEU   A HD22 1 
ATOM   2096  H HD23 . LEU   A  1 151 ? 21.275 11.525  -4.536  0.00 37.75  ? 177  LEU   A HD23 1 
ATOM   2097  N N    . ALA   A  1 152 ? 22.681 7.615   -7.669  1.00 24.43  ? 178  ALA   A N    1 
ATOM   2098  C CA   . ALA   A  1 152 ? 23.715 6.640   -7.948  1.00 24.03  ? 178  ALA   A CA   1 
ATOM   2099  C C    . ALA   A  1 152 ? 25.140 7.221   -7.998  1.00 23.44  ? 178  ALA   A C    1 
ATOM   2100  O O    . ALA   A  1 152 ? 25.323 8.424   -8.191  1.00 23.97  ? 178  ALA   A O    1 
ATOM   2101  C CB   . ALA   A  1 152 ? 23.391 5.915   -9.261  1.00 24.32  ? 178  ALA   A CB   1 
ATOM   2102  H H    . ALA   A  1 152 ? 22.086 7.809   -8.468  0.00 29.18  ? 178  ALA   A H    1 
ATOM   2103  H HA   . ALA   A  1 152 ? 23.697 5.893   -7.157  0.00 28.49  ? 178  ALA   A HA   1 
ATOM   2104  H HB1  . ALA   A  1 152 ? 24.134 5.137   -9.428  0.00 28.03  ? 178  ALA   A HB1  1 
ATOM   2105  H HB2  . ALA   A  1 152 ? 22.399 5.472   -9.186  0.00 28.43  ? 178  ALA   A HB2  1 
ATOM   2106  H HB3  . ALA   A  1 152 ? 23.417 6.628   -10.083 0.00 28.18  ? 178  ALA   A HB3  1 
ATOM   2107  N N    . TRP   A  1 153 ? 26.136 6.363   -7.773  1.00 22.08  ? 179  TRP   A N    1 
ATOM   2108  C CA   . TRP   A  1 153 ? 27.547 6.695   -7.919  1.00 22.04  ? 179  TRP   A CA   1 
ATOM   2109  C C    . TRP   A  1 153 ? 28.047 7.803   -6.974  1.00 22.96  ? 179  TRP   A C    1 
ATOM   2110  O O    . TRP   A  1 153 ? 28.771 8.696   -7.412  1.00 23.66  ? 179  TRP   A O    1 
ATOM   2111  C CB   . TRP   A  1 153 ? 27.847 7.049   -9.395  1.00 20.99  ? 179  TRP   A CB   1 
ATOM   2112  C CG   . TRP   A  1 153 ? 27.662 5.914   -10.341 1.00 20.65  ? 179  TRP   A CG   1 
ATOM   2113  C CD1  . TRP   A  1 153 ? 26.546 5.624   -11.071 1.00 21.58  ? 179  TRP   A CD1  1 
ATOM   2114  C CD2  . TRP   A  1 153 ? 28.676 5.000   -10.774 1.00 20.22  ? 179  TRP   A CD2  1 
ATOM   2115  N NE1  . TRP   A  1 153 ? 26.794 4.557   -11.903 1.00 21.40  ? 179  TRP   A NE1  1 
ATOM   2116  C CE2  . TRP   A  1 153 ? 28.113 4.196   -11.786 1.00 20.63  ? 179  TRP   A CE2  1 
ATOM   2117  C CE3  . TRP   A  1 153 ? 30.014 4.790   -10.406 1.00 20.73  ? 179  TRP   A CE3  1 
ATOM   2118  C CZ2  . TRP   A  1 153 ? 28.822 3.164   -12.394 1.00 20.69  ? 179  TRP   A CZ2  1 
ATOM   2119  C CZ3  . TRP   A  1 153 ? 30.732 3.795   -11.049 1.00 21.19  ? 179  TRP   A CZ3  1 
ATOM   2120  C CH2  . TRP   A  1 153 ? 30.140 3.003   -12.036 1.00 21.02  ? 179  TRP   A CH2  1 
ATOM   2121  H H    . TRP   A  1 153 ? 25.981 5.410   -7.459  0.00 25.67  ? 179  TRP   A H    1 
ATOM   2122  H HA   . TRP   A  1 153 ? 28.125 5.803   -7.686  0.00 25.38  ? 179  TRP   A HA   1 
ATOM   2123  H HB2  . TRP   A  1 153 ? 27.213 7.872   -9.721  0.00 23.94  ? 179  TRP   A HB2  1 
ATOM   2124  H HB3  . TRP   A  1 153 ? 28.893 7.341   -9.483  0.00 23.75  ? 179  TRP   A HB3  1 
ATOM   2125  H HD1  . TRP   A  1 153 ? 25.606 6.142   -10.996 0.00 24.24  ? 179  TRP   A HD1  1 
ATOM   2126  H HE1  . TRP   A  1 153 ? 26.110 4.143   -12.569 0.00 23.34  ? 179  TRP   A HE1  1 
ATOM   2127  H HE3  . TRP   A  1 153 ? 30.497 5.440   -9.698  0.00 23.00  ? 179  TRP   A HE3  1 
ATOM   2128  H HZ2  . TRP   A  1 153 ? 28.359 2.524   -13.120 0.00 21.97  ? 179  TRP   A HZ2  1 
ATOM   2129  H HZ3  . TRP   A  1 153 ? 31.767 3.640   -10.795 0.00 23.01  ? 179  TRP   A HZ3  1 
ATOM   2130  H HH2  . TRP   A  1 153 ? 30.711 2.206   -12.480 0.00 22.32  ? 179  TRP   A HH2  1 
ATOM   2131  N N    . ASN   A  1 154 ? 27.676 7.740   -5.687  1.00 22.74  ? 180  ASN   A N    1 
ATOM   2132  C CA   . ASN   A  1 154 ? 28.211 8.682   -4.703  1.00 23.28  ? 180  ASN   A CA   1 
ATOM   2133  C C    . ASN   A  1 154 ? 29.314 8.007   -3.862  1.00 24.54  ? 180  ASN   A C    1 
ATOM   2134  O O    . ASN   A  1 154 ? 30.189 8.714   -3.371  1.00 25.36  ? 180  ASN   A O    1 
ATOM   2135  C CB   . ASN   A  1 154 ? 27.107 9.317   -3.826  1.00 23.80  ? 180  ASN   A CB   1 
ATOM   2136  C CG   . ASN   A  1 154 ? 26.377 10.455  -4.520  1.00 26.17  ? 180  ASN   A CG   1 
ATOM   2137  O OD1  . ASN   A  1 154 ? 26.508 11.614  -4.146  1.00 25.73  ? 180  ASN   A OD1  1 
ATOM   2138  N ND2  . ASN   A  1 154 ? 25.654 10.165  -5.585  1.00 27.22  ? 180  ASN   A ND2  1 
ATOM   2139  H H    . ASN   A  1 154 ? 27.027 7.060   -5.304  0.00 27.25  ? 180  ASN   A H    1 
ATOM   2140  H HA   . ASN   A  1 154 ? 28.714 9.498   -5.220  0.00 28.22  ? 180  ASN   A HA   1 
ATOM   2141  H HB2  . ASN   A  1 154 ? 26.371 8.556   -3.570  0.00 29.44  ? 180  ASN   A HB2  1 
ATOM   2142  H HB3  . ASN   A  1 154 ? 27.562 9.714   -2.920  0.00 29.79  ? 180  ASN   A HB3  1 
ATOM   2143  H HD21 . ASN   A  1 154 ? 25.153 10.899  -6.075  0.00 33.35  ? 180  ASN   A HD21 1 
ATOM   2144  H HD22 . ASN   A  1 154 ? 25.601 9.206   -5.914  0.00 32.98  ? 180  ASN   A HD22 1 
ATOM   2145  N N    . CYS   A  1 155 ? 29.308 6.668   -3.715  1.00 24.23  ? 181  CYS   A N    1 
ATOM   2146  C CA   . CYS   A  1 155 ? 30.345 5.981   -2.946  1.00 24.98  ? 181  CYS   A CA   1 
ATOM   2147  C C    . CYS   A  1 155 ? 30.578 4.591   -3.536  1.00 24.68  ? 181  CYS   A C    1 
ATOM   2148  O O    . CYS   A  1 155 ? 29.731 3.717   -3.402  1.00 24.49  ? 181  CYS   A O    1 
ATOM   2149  C CB   . CYS   A  1 155 ? 29.965 5.906   -1.474  1.00 26.37  ? 181  CYS   A CB   1 
ATOM   2150  S SG   . CYS   A  1 155 ? 31.221 5.121   -0.439  1.00 31.81  ? 181  CYS   A SG   1 
ATOM   2151  H H    . CYS   A  1 155 ? 28.605 6.040   -4.091  0.00 29.17  ? 181  CYS   A H    1 
ATOM   2152  H HA   . CYS   A  1 155 ? 31.272 6.542   -3.045  0.00 30.37  ? 181  CYS   A HA   1 
ATOM   2153  H HB2  . CYS   A  1 155 ? 29.815 6.918   -1.100  0.00 32.89  ? 181  CYS   A HB2  1 
ATOM   2154  H HB3  . CYS   A  1 155 ? 29.042 5.337   -1.371  0.00 32.60  ? 181  CYS   A HB3  1 
ATOM   2155  N N    . TYR   A  1 156 ? 31.722 4.388   -4.204  1.00 24.30  ? 182  TYR   A N    1 
ATOM   2156  C CA   . TYR   A  1 156 ? 31.966 3.139   -4.921  1.00 24.68  ? 182  TYR   A CA   1 
ATOM   2157  C C    . TYR   A  1 156 ? 33.451 2.915   -5.203  1.00 24.91  ? 182  TYR   A C    1 
ATOM   2158  O O    . TYR   A  1 156 ? 34.243 3.846   -5.090  1.00 24.89  ? 182  TYR   A O    1 
ATOM   2159  C CB   . TYR   A  1 156 ? 31.194 3.202   -6.263  1.00 24.50  ? 182  TYR   A CB   1 
ATOM   2160  C CG   . TYR   A  1 156 ? 31.632 4.382   -7.104  1.00 25.02  ? 182  TYR   A CG   1 
ATOM   2161  C CD1  . TYR   A  1 156 ? 31.122 5.652   -6.873  1.00 25.90  ? 182  TYR   A CD1  1 
ATOM   2162  C CD2  . TYR   A  1 156 ? 32.681 4.265   -8.002  1.00 26.19  ? 182  TYR   A CD2  1 
ATOM   2163  C CE1  . TYR   A  1 156 ? 31.609 6.760   -7.553  1.00 26.67  ? 182  TYR   A CE1  1 
ATOM   2164  C CE2  . TYR   A  1 156 ? 33.150 5.356   -8.715  1.00 27.03  ? 182  TYR   A CE2  1 
ATOM   2165  C CZ   . TYR   A  1 156 ? 32.615 6.606   -8.485  1.00 27.76  ? 182  TYR   A CZ   1 
ATOM   2166  O OH   . TYR   A  1 156 ? 33.077 7.692   -9.186  1.00 29.76  ? 182  TYR   A OH   1 
ATOM   2167  H H    . TYR   A  1 156 ? 32.488 5.050   -4.261  0.00 28.92  ? 182  TYR   A H    1 
ATOM   2168  H HA   . TYR   A  1 156 ? 31.603 2.287   -4.348  0.00 29.10  ? 182  TYR   A HA   1 
ATOM   2169  H HB2  . TYR   A  1 156 ? 31.388 2.293   -6.830  0.00 28.06  ? 182  TYR   A HB2  1 
ATOM   2170  H HB3  . TYR   A  1 156 ? 30.127 3.300   -6.064  0.00 28.43  ? 182  TYR   A HB3  1 
ATOM   2171  H HD1  . TYR   A  1 156 ? 30.347 5.783   -6.135  0.00 30.35  ? 182  TYR   A HD1  1 
ATOM   2172  H HD2  . TYR   A  1 156 ? 33.112 3.297   -8.182  0.00 29.72  ? 182  TYR   A HD2  1 
ATOM   2173  H HE1  . TYR   A  1 156 ? 31.170 7.730   -7.388  0.00 31.11  ? 182  TYR   A HE1  1 
ATOM   2174  H HE2  . TYR   A  1 156 ? 33.941 5.222   -9.433  0.00 30.52  ? 182  TYR   A HE2  1 
ATOM   2175  H HH   . TYR   A  1 156 ? 33.808 7.437   -9.807  0.00 33.97  ? 182  TYR   A HH   1 
ATOM   2176  N N    . PHE   A  1 157 ? 33.822 1.671   -5.577  1.00 24.63  ? 183  PHE   A N    1 
ATOM   2177  C CA   . PHE   A  1 157 ? 35.185 1.287   -5.950  1.00 24.93  ? 183  PHE   A CA   1 
ATOM   2178  C C    . PHE   A  1 157 ? 36.185 1.695   -4.830  1.00 25.64  ? 183  PHE   A C    1 
ATOM   2179  O O    . PHE   A  1 157 ? 35.881 1.424   -3.669  1.00 25.51  ? 183  PHE   A O    1 
ATOM   2180  C CB   . PHE   A  1 157 ? 35.517 1.867   -7.355  1.00 24.28  ? 183  PHE   A CB   1 
ATOM   2181  C CG   . PHE   A  1 157 ? 34.696 1.416   -8.540  1.00 24.56  ? 183  PHE   A CG   1 
ATOM   2182  C CD1  . PHE   A  1 157 ? 33.774 0.388   -8.423  1.00 25.58  ? 183  PHE   A CD1  1 
ATOM   2183  C CD2  . PHE   A  1 157 ? 34.808 2.057   -9.761  1.00 25.16  ? 183  PHE   A CD2  1 
ATOM   2184  C CE1  . PHE   A  1 157 ? 32.986 0.011   -9.510  1.00 26.10  ? 183  PHE   A CE1  1 
ATOM   2185  C CE2  . PHE   A  1 157 ? 34.030 1.669   -10.843 1.00 25.76  ? 183  PHE   A CE2  1 
ATOM   2186  C CZ   . PHE   A  1 157 ? 33.139 0.636   -10.712 1.00 25.79  ? 183  PHE   A CZ   1 
ATOM   2187  H H    . PHE   A  1 157 ? 33.169 0.896   -5.628  0.00 28.51  ? 183  PHE   A H    1 
ATOM   2188  H HA   . PHE   A  1 157 ? 35.228 0.202   -6.029  0.00 28.78  ? 183  PHE   A HA   1 
ATOM   2189  H HB2  . PHE   A  1 157 ? 35.411 2.949   -7.300  0.00 27.71  ? 183  PHE   A HB2  1 
ATOM   2190  H HB3  . PHE   A  1 157 ? 36.547 1.626   -7.601  0.00 27.59  ? 183  PHE   A HB3  1 
ATOM   2191  H HD1  . PHE   A  1 157 ? 33.641 -0.132  -7.490  0.00 29.03  ? 183  PHE   A HD1  1 
ATOM   2192  H HD2  . PHE   A  1 157 ? 35.510 2.865   -9.875  0.00 27.96  ? 183  PHE   A HD2  1 
ATOM   2193  H HE1  . PHE   A  1 157 ? 32.287 -0.804  -9.412  0.00 29.08  ? 183  PHE   A HE1  1 
ATOM   2194  H HE2  . PHE   A  1 157 ? 34.141 2.166   -11.792 0.00 28.09  ? 183  PHE   A HE2  1 
ATOM   2195  H HZ   . PHE   A  1 157 ? 32.537 0.337   -11.553 0.00 28.14  ? 183  PHE   A HZ   1 
ATOM   2196  N N    . ASN   A  1 158 ? 37.324 2.374   -5.133  1.00 26.26  ? 184  ASN   A N    1 
ATOM   2197  C CA   . ASN   A  1 158 ? 38.262 2.821   -4.111  1.00 26.81  ? 184  ASN   A CA   1 
ATOM   2198  C C    . ASN   A  1 158 ? 38.115 4.308   -3.797  1.00 27.72  ? 184  ASN   A C    1 
ATOM   2199  O O    . ASN   A  1 158 ? 39.025 4.893   -3.215  1.00 28.22  ? 184  ASN   A O    1 
ATOM   2200  C CB   . ASN   A  1 158 ? 39.698 2.500   -4.515  1.00 27.33  ? 184  ASN   A CB   1 
ATOM   2201  C CG   . ASN   A  1 158 ? 39.960 1.025   -4.726  1.00 29.18  ? 184  ASN   A CG   1 
ATOM   2202  O OD1  . ASN   A  1 158 ? 40.558 0.626   -5.723  1.00 28.50  ? 184  ASN   A OD1  1 
ATOM   2203  N ND2  . ASN   A  1 158 ? 39.583 0.176   -3.765  1.00 29.87  ? 184  ASN   A ND2  1 
ATOM   2204  H H    . ASN   A  1 158 ? 37.624 2.640   -6.064  0.00 30.60  ? 184  ASN   A H    1 
ATOM   2205  H HA   . ASN   A  1 158 ? 38.064 2.301   -3.175  0.00 32.32  ? 184  ASN   A HA   1 
ATOM   2206  H HB2  . ASN   A  1 158 ? 39.925 3.016   -5.446  0.00 32.35  ? 184  ASN   A HB2  1 
ATOM   2207  H HB3  . ASN   A  1 158 ? 40.380 2.828   -3.731  0.00 33.03  ? 184  ASN   A HB3  1 
ATOM   2208  H HD21 . ASN   A  1 158 ? 39.751 -0.817  -3.890  0.00 35.82  ? 184  ASN   A HD21 1 
ATOM   2209  H HD22 . ASN   A  1 158 ? 39.166 0.505   -2.901  0.00 36.14  ? 184  ASN   A HD22 1 
ATOM   2210  N N    . LYS   A  1 159 ? 36.942 4.916   -4.082  1.00 27.80  ? 185  LYS   A N    1 
ATOM   2211  C CA   . LYS   A  1 159 ? 36.709 6.310   -3.710  1.00 27.98  ? 185  LYS   A CA   1 
ATOM   2212  C C    . LYS   A  1 159 ? 36.731 6.406   -2.163  1.00 28.70  ? 185  LYS   A C    1 
ATOM   2213  O O    . LYS   A  1 159 ? 36.264 5.482   -1.487  1.00 27.94  ? 185  LYS   A O    1 
ATOM   2214  C CB   . LYS   A  1 159 ? 35.345 6.780   -4.239  1.00 27.87  ? 185  LYS   A CB   1 
ATOM   2215  C CG   . LYS   A  1 159 ? 35.063 8.255   -3.996  1.00 29.10  ? 185  LYS   A CG   1 
ATOM   2216  C CD   . LYS   A  1 159 ? 33.659 8.631   -4.395  1.00 30.54  ? 185  LYS   A CD   1 
ATOM   2217  C CE   . LYS   A  1 159 ? 33.316 10.003  -3.883  1.00 32.58  ? 185  LYS   A CE   1 
ATOM   2218  N NZ   . LYS   A  1 159 ? 32.018 10.481  -4.420  1.00 33.96  ? 185  LYS   A NZ   1 
ATOM   2219  H H    . LYS   A  1 159 ? 36.150 4.486   -4.547  0.00 33.04  ? 185  LYS   A H    1 
ATOM   2220  H HA   . LYS   A  1 159 ? 37.491 6.944   -4.124  0.00 33.77  ? 185  LYS   A HA   1 
ATOM   2221  H HB2  . LYS   A  1 159 ? 35.308 6.607   -5.313  0.00 33.06  ? 185  LYS   A HB2  1 
ATOM   2222  H HB3  . LYS   A  1 159 ? 34.564 6.203   -3.746  0.00 33.55  ? 185  LYS   A HB3  1 
ATOM   2223  H HG2  . LYS   A  1 159 ? 35.174 8.495   -2.939  0.00 35.69  ? 185  LYS   A HG2  1 
ATOM   2224  H HG3  . LYS   A  1 159 ? 35.754 8.853   -4.589  0.00 35.16  ? 185  LYS   A HG3  1 
ATOM   2225  H HD2  . LYS   A  1 159 ? 33.580 8.638   -5.481  0.00 36.47  ? 185  LYS   A HD2  1 
ATOM   2226  H HD3  . LYS   A  1 159 ? 32.954 7.919   -3.967  0.00 36.89  ? 185  LYS   A HD3  1 
ATOM   2227  H HE2  . LYS   A  1 159 ? 33.245 9.973   -2.797  0.00 40.16  ? 185  LYS   A HE2  1 
ATOM   2228  H HE3  . LYS   A  1 159 ? 34.091 10.704  -4.190  0.00 39.78  ? 185  LYS   A HE3  1 
ATOM   2229  H HZ1  . LYS   A  1 159 ? 31.817 11.409  -4.063  0.00 41.66  ? 185  LYS   A HZ1  1 
ATOM   2230  H HZ2  . LYS   A  1 159 ? 32.055 10.518  -5.434  0.00 40.97  ? 185  LYS   A HZ2  1 
ATOM   2231  H HZ3  . LYS   A  1 159 ? 31.274 9.851   -4.139  0.00 41.32  ? 185  LYS   A HZ3  1 
ATOM   2232  N N    . VAL   A  1 160 ? 37.319 7.475   -1.620  1.00 30.19  ? 186  VAL   A N    1 
ATOM   2233  C CA   . VAL   A  1 160 ? 37.341 7.677   -0.172  1.00 31.86  ? 186  VAL   A CA   1 
ATOM   2234  C C    . VAL   A  1 160 ? 35.967 8.236   0.125   1.00 33.16  ? 186  VAL   A C    1 
ATOM   2235  O O    . VAL   A  1 160 ? 35.649 9.341   -0.330  1.00 33.84  ? 186  VAL   A O    1 
ATOM   2236  C CB   . VAL   A  1 160 ? 38.466 8.635   0.287   1.00 33.35  ? 186  VAL   A CB   1 
ATOM   2237  C CG1  . VAL   A  1 160 ? 38.425 8.828   1.806   1.00 33.77  ? 186  VAL   A CG1  1 
ATOM   2238  C CG2  . VAL   A  1 160 ? 39.837 8.117   -0.158  1.00 33.98  ? 186  VAL   A CG2  1 
ATOM   2239  H H    . VAL   A  1 160 ? 37.781 8.210   -2.146  0.00 37.40  ? 186  VAL   A H    1 
ATOM   2240  H HA   . VAL   A  1 160 ? 37.477 6.730   0.348   0.00 40.20  ? 186  VAL   A HA   1 
ATOM   2241  H HB   . VAL   A  1 160 ? 38.313 9.608   -0.177  0.00 42.30  ? 186  VAL   A HB   1 
ATOM   2242  H HG11 . VAL   A  1 160 ? 39.354 9.294   2.130   0.00 43.89  ? 186  VAL   A HG11 1 
ATOM   2243  H HG12 . VAL   A  1 160 ? 37.590 9.478   2.066   0.00 43.71  ? 186  VAL   A HG12 1 
ATOM   2244  H HG13 . VAL   A  1 160 ? 38.308 7.858   2.285   0.00 43.60  ? 186  VAL   A HG13 1 
ATOM   2245  H HG21 . VAL   A  1 160 ? 40.612 8.777   0.229   0.00 43.34  ? 186  VAL   A HG21 1 
ATOM   2246  H HG22 . VAL   A  1 160 ? 39.978 7.109   0.228   0.00 43.01  ? 186  VAL   A HG22 1 
ATOM   2247  H HG23 . VAL   A  1 160 ? 39.881 8.108   -1.246  0.00 42.51  ? 186  VAL   A HG23 1 
ATOM   2248  N N    . CYS   A  1 161 ? 35.111 7.444   0.769   1.00 33.25  ? 187  CYS   A N    1 
ATOM   2249  C CA   . CYS   A  1 161 ? 33.738 7.857   1.015   1.00 33.75  ? 187  CYS   A CA   1 
ATOM   2250  C C    . CYS   A  1 161 ? 33.132 7.095   2.181   1.00 35.18  ? 187  CYS   A C    1 
ATOM   2251  O O    . CYS   A  1 161 ? 33.596 6.016   2.539   1.00 35.61  ? 187  CYS   A O    1 
ATOM   2252  C CB   . CYS   A  1 161 ? 32.902 7.690   -0.255  1.00 33.30  ? 187  CYS   A CB   1 
ATOM   2253  S SG   . CYS   A  1 161 ? 32.963 6.032   -0.985  1.00 32.67  ? 187  CYS   A SG   1 
ATOM   2254  H H    . CYS   A  1 161 ? 35.332 6.521   1.131   0.00 42.02  ? 187  CYS   A H    1 
ATOM   2255  H HA   . CYS   A  1 161 ? 33.721 8.912   1.285   0.00 43.03  ? 187  CYS   A HA   1 
ATOM   2256  H HB2  . CYS   A  1 161 ? 31.862 7.908   -0.017  0.00 41.74  ? 187  CYS   A HB2  1 
ATOM   2257  H HB3  . CYS   A  1 161 ? 33.261 8.394   -1.005  0.00 41.42  ? 187  CYS   A HB3  1 
ATOM   2258  N N    . GLU   A  1 162 ? 32.085 7.667   2.770   1.00 35.66  ? 188  GLU   A N    1 
ATOM   2259  C CA   . GLU   A  1 162 ? 31.390 7.072   3.903   1.00 36.31  ? 188  GLU   A CA   1 
ATOM   2260  C C    . GLU   A  1 162 ? 30.277 6.153   3.432   1.00 36.03  ? 188  GLU   A C    1 
ATOM   2261  O O    . GLU   A  1 162 ? 29.727 6.336   2.345   1.00 35.71  ? 188  GLU   A O    1 
ATOM   2262  C CB   . GLU   A  1 162 ? 30.747 8.174   4.790   1.00 39.60  ? 188  GLU   A CB   1 
ATOM   2263  C CG   . GLU   A  1 162 ? 31.561 8.601   5.999   1.00 46.64  ? 188  GLU   A CG   1 
ATOM   2264  C CD   . GLU   A  1 162 ? 32.848 9.325   5.674   1.00 54.52  ? 188  GLU   A CD   1 
ATOM   2265  O OE1  . GLU   A  1 162 ? 32.925 9.943   4.587   1.00 56.72  ? 188  GLU   A OE1  1 
ATOM   2266  O OE2  . GLU   A  1 162 ? 33.782 9.278   6.509   1.00 56.54  ? 188  GLU   A OE2  1 
ATOM   2267  H H    . GLU   A  1 162 ? 31.686 8.544   2.453   0.00 45.75  ? 188  GLU   A H    1 
ATOM   2268  H HA   . GLU   A  1 162 ? 32.082 6.478   4.500   0.00 47.10  ? 188  GLU   A HA   1 
ATOM   2269  H HB2  . GLU   A  1 162 ? 30.526 9.059   4.195   0.00 51.37  ? 188  GLU   A HB2  1 
ATOM   2270  H HB3  . GLU   A  1 162 ? 29.809 7.776   5.177   0.00 51.62  ? 188  GLU   A HB3  1 
ATOM   2271  H HG2  . GLU   A  1 162 ? 30.952 9.267   6.608   0.00 61.00  ? 188  GLU   A HG2  1 
ATOM   2272  H HG3  . GLU   A  1 162 ? 31.819 7.714   6.575   0.00 60.69  ? 188  GLU   A HG3  1 
ATOM   2273  N N    . LYS   A  1 163 ? 29.875 5.208   4.305   1.00 36.19  ? 189  LYS   A N    1 
ATOM   2274  C CA   . LYS   A  1 163 ? 28.723 4.346   4.047   1.00 36.73  ? 189  LYS   A CA   1 
ATOM   2275  C C    . LYS   A  1 163 ? 27.471 5.240   3.991   1.00 35.97  ? 189  LYS   A C    1 
ATOM   2276  O O    . LYS   A  1 163 ? 27.406 6.234   4.712   1.00 35.77  ? 189  LYS   A O    1 
ATOM   2277  C CB   . LYS   A  1 163 ? 28.562 3.289   5.159   1.00 39.49  ? 189  LYS   A CB   1 
ATOM   2278  C CG   . LYS   A  1 163 ? 29.655 2.235   5.154   1.00 45.78  ? 189  LYS   A CG   1 
ATOM   2279  C CD   . LYS   A  1 163 ? 29.463 1.211   6.263   1.00 52.31  ? 189  LYS   A CD   1 
ATOM   2280  C CE   . LYS   A  1 163 ? 30.472 0.082   6.191   1.00 57.52  ? 189  LYS   A CE   1 
ATOM   2281  N NZ   . LYS   A  1 163 ? 30.232 -0.823  5.027   1.00 60.42  ? 189  LYS   A NZ   1 
ATOM   2282  H H    . LYS   A  1 163 ? 30.335 5.023   5.190   0.00 47.07  ? 189  LYS   A H    1 
ATOM   2283  H HA   . LYS   A  1 163 ? 28.844 3.847   3.089   0.00 46.68  ? 189  LYS   A HA   1 
ATOM   2284  H HB2  . LYS   A  1 163 ? 28.575 3.786   6.128   0.00 51.36  ? 189  LYS   A HB2  1 
ATOM   2285  H HB3  . LYS   A  1 163 ? 27.610 2.778   5.021   0.00 50.79  ? 189  LYS   A HB3  1 
ATOM   2286  H HG2  . LYS   A  1 163 ? 29.643 1.712   4.199   0.00 57.80  ? 189  LYS   A HG2  1 
ATOM   2287  H HG3  . LYS   A  1 163 ? 30.619 2.720   5.303   0.00 58.37  ? 189  LYS   A HG3  1 
ATOM   2288  H HD2  . LYS   A  1 163 ? 29.578 1.705   7.226   0.00 67.04  ? 189  LYS   A HD2  1 
ATOM   2289  H HD3  . LYS   A  1 163 ? 28.466 0.780   6.181   0.00 66.51  ? 189  LYS   A HD3  1 
ATOM   2290  H HE2  . LYS   A  1 163 ? 31.470 0.505   6.089   0.00 72.67  ? 189  LYS   A HE2  1 
ATOM   2291  H HE3  . LYS   A  1 163 ? 30.408 -0.511  7.102   0.00 73.11  ? 189  LYS   A HE3  1 
ATOM   2292  H HZ1  . LYS   A  1 163 ? 30.871 -1.611  5.065   0.00 75.60  ? 189  LYS   A HZ1  1 
ATOM   2293  H HZ2  . LYS   A  1 163 ? 29.279 -1.171  5.049   0.00 75.63  ? 189  LYS   A HZ2  1 
ATOM   2294  H HZ3  . LYS   A  1 163 ? 30.382 -0.325  4.156   0.00 75.23  ? 189  LYS   A HZ3  1 
ATOM   2295  N N    . THR   A  1 164 ? 26.519 4.926   3.115   1.00 35.49  ? 190  THR   A N    1 
ATOM   2296  C CA   . THR   A  1 164 ? 25.321 5.754   2.953   1.00 35.93  ? 190  THR   A CA   1 
ATOM   2297  C C    . THR   A  1 164 ? 24.328 5.556   4.089   1.00 36.53  ? 190  THR   A C    1 
ATOM   2298  O O    . THR   A  1 164 ? 23.856 4.443   4.312   1.00 37.21  ? 190  THR   A O    1 
ATOM   2299  C CB   . THR   A  1 164 ? 24.630 5.438   1.618   1.00 37.21  ? 190  THR   A CB   1 
ATOM   2300  O OG1  . THR   A  1 164 ? 25.594 5.414   0.570   1.00 37.82  ? 190  THR   A OG1  1 
ATOM   2301  C CG2  . THR   A  1 164 ? 23.529 6.432   1.275   1.00 38.09  ? 190  THR   A CG2  1 
ATOM   2302  H H    . THR   A  1 164 ? 26.544 4.114   2.507   0.00 45.11  ? 190  THR   A H    1 
ATOM   2303  H HA   . THR   A  1 164 ? 25.621 6.800   2.925   0.00 46.29  ? 190  THR   A HA   1 
ATOM   2304  H HB   . THR   A  1 164 ? 24.172 4.454   1.697   0.00 47.13  ? 190  THR   A HB   1 
ATOM   2305  H HG1  . THR   A  1 164 ? 26.049 6.295   0.507   0.00 47.43  ? 190  THR   A HG1  1 
ATOM   2306  H HG21 . THR   A  1 164 ? 23.228 6.301   0.237   0.00 48.00  ? 190  THR   A HG21 1 
ATOM   2307  H HG22 . THR   A  1 164 ? 22.658 6.271   1.909   0.00 48.74  ? 190  THR   A HG22 1 
ATOM   2308  H HG23 . THR   A  1 164 ? 23.887 7.451   1.415   0.00 48.57  ? 190  THR   A HG23 1 
ATOM   2309  N N    . ASN   A  1 165 ? 23.968 6.643   4.773   1.00 35.97  ? 191  ASN   A N    1 
ATOM   2310  C CA   . ASN   A  1 165 ? 22.987 6.598   5.838   1.00 36.04  ? 191  ASN   A CA   1 
ATOM   2311  C C    . ASN   A  1 165 ? 21.647 7.021   5.244   1.00 35.25  ? 191  ASN   A C    1 
ATOM   2312  O O    . ASN   A  1 165 ? 21.482 8.189   4.893   1.00 35.42  ? 191  ASN   A O    1 
ATOM   2313  C CB   . ASN   A  1 165 ? 23.381 7.531   6.985   1.00 37.81  ? 191  ASN   A CB   1 
ATOM   2314  C CG   . ASN   A  1 165 ? 22.345 7.557   8.079   1.00 42.28  ? 191  ASN   A CG   1 
ATOM   2315  O OD1  . ASN   A  1 165 ? 21.905 6.513   8.561   1.00 43.69  ? 191  ASN   A OD1  1 
ATOM   2316  N ND2  . ASN   A  1 165 ? 21.887 8.737   8.469   1.00 44.35  ? 191  ASN   A ND2  1 
ATOM   2317  H H    . ASN   A  1 165 ? 24.319 7.577   4.591   0.00 47.33  ? 191  ASN   A H    1 
ATOM   2318  H HA   . ASN   A  1 165 ? 22.898 5.593   6.248   0.00 48.00  ? 191  ASN   A HA   1 
ATOM   2319  H HB2  . ASN   A  1 165 ? 24.314 7.177   7.420   0.00 50.76  ? 191  ASN   A HB2  1 
ATOM   2320  H HB3  . ASN   A  1 165 ? 23.517 8.539   6.594   0.00 50.74  ? 191  ASN   A HB3  1 
ATOM   2321  H HD21 . ASN   A  1 165 ? 21.189 8.784   9.205   0.00 60.21  ? 191  ASN   A HD21 1 
ATOM   2322  H HD22 . ASN   A  1 165 ? 22.225 9.596   8.046   0.00 59.66  ? 191  ASN   A HD22 1 
ATOM   2323  N N    . ILE   A  1 166 ? 20.704 6.078   5.123   1.00 34.37  ? 192  ILE   A N    1 
ATOM   2324  C CA   . ILE   A  1 166 ? 19.362 6.359   4.624   1.00 34.27  ? 192  ILE   A CA   1 
ATOM   2325  C C    . ILE   A  1 166 ? 18.505 6.563   5.871   1.00 34.68  ? 192  ILE   A C    1 
ATOM   2326  O O    . ILE   A  1 166 ? 18.355 5.615   6.648   1.00 34.70  ? 192  ILE   A O    1 
ATOM   2327  C CB   . ILE   A  1 166 ? 18.817 5.181   3.759   1.00 34.56  ? 192  ILE   A CB   1 
ATOM   2328  C CG1  . ILE   A  1 166 ? 19.796 4.755   2.625   1.00 35.88  ? 192  ILE   A CG1  1 
ATOM   2329  C CG2  . ILE   A  1 166 ? 17.425 5.517   3.211   1.00 35.06  ? 192  ILE   A CG2  1 
ATOM   2330  C CD1  . ILE   A  1 166 ? 19.929 5.656   1.490   1.00 37.26  ? 192  ILE   A CD1  1 
ATOM   2331  H H    . ILE   A  1 166 ? 20.841 5.102   5.362   0.00 45.82  ? 192  ILE   A H    1 
ATOM   2332  H HA   . ILE   A  1 166 ? 19.346 7.265   4.021   0.00 45.77  ? 192  ILE   A HA   1 
ATOM   2333  H HB   . ILE   A  1 166 ? 18.704 4.317   4.412   0.00 45.93  ? 192  ILE   A HB   1 
ATOM   2334  H HG12 . ILE   A  1 166 ? 20.792 4.609   3.041   0.00 46.59  ? 192  ILE   A HG12 1 
ATOM   2335  H HG13 . ILE   A  1 166 ? 19.442 3.806   2.227   0.00 46.41  ? 192  ILE   A HG13 1 
ATOM   2336  H HG21 . ILE   A  1 166 ? 17.152 4.766   2.471   0.00 46.14  ? 192  ILE   A HG21 1 
ATOM   2337  H HG22 . ILE   A  1 166 ? 16.695 5.511   4.019   0.00 46.98  ? 192  ILE   A HG22 1 
ATOM   2338  H HG23 . ILE   A  1 166 ? 17.464 6.498   2.743   0.00 46.46  ? 192  ILE   A HG23 1 
ATOM   2339  H HD11 . ILE   A  1 166 ? 20.774 5.336   0.883   0.00 47.51  ? 192  ILE   A HD11 1 
ATOM   2340  H HD12 . ILE   A  1 166 ? 19.019 5.623   0.894   0.00 47.90  ? 192  ILE   A HD12 1 
ATOM   2341  H HD13 . ILE   A  1 166 ? 20.097 6.669   1.854   0.00 48.23  ? 192  ILE   A HD13 1 
ATOM   2342  N N    . GLU   A  1 167 ? 17.979 7.782   6.105   1.00 34.56  ? 193  GLU   A N    1 
ATOM   2343  C CA   . GLU   A  1 167 ? 17.153 8.022   7.290   1.00 35.31  ? 193  GLU   A CA   1 
ATOM   2344  C C    . GLU   A  1 167 ? 15.862 7.191   7.204   1.00 35.23  ? 193  GLU   A C    1 
ATOM   2345  O O    . GLU   A  1 167 ? 15.223 7.159   6.155   1.00 34.97  ? 193  GLU   A O    1 
ATOM   2346  C CB   . GLU   A  1 167 ? 16.832 9.519   7.459   1.00 37.92  ? 193  GLU   A CB   1 
ATOM   2347  C CG   . GLU   A  1 167 ? 16.290 9.846   8.838   1.00 42.22  ? 193  GLU   A CG   1 
ATOM   2348  C CD   . GLU   A  1 167 ? 15.787 11.262  9.001   1.00 48.34  ? 193  GLU   A CD   1 
ATOM   2349  O OE1  . GLU   A  1 167 ? 16.259 12.152  8.258   1.00 48.35  ? 193  GLU   A OE1  1 
ATOM   2350  O OE2  . GLU   A  1 167 ? 14.920 11.479  9.878   1.00 50.15  ? 193  GLU   A OE2  1 
ATOM   2351  H H    . GLU   A  1 167 ? 18.106 8.594   5.510   0.00 47.28  ? 193  GLU   A H    1 
ATOM   2352  H HA   . GLU   A  1 167 ? 17.715 7.690   8.162   0.00 49.27  ? 193  GLU   A HA   1 
ATOM   2353  H HB2  . GLU   A  1 167 ? 17.745 10.096  7.313   0.00 52.55  ? 193  GLU   A HB2  1 
ATOM   2354  H HB3  . GLU   A  1 167 ? 16.084 9.814   6.725   0.00 52.61  ? 193  GLU   A HB3  1 
ATOM   2355  H HG2  . GLU   A  1 167 ? 15.457 9.184   9.072   0.00 58.85  ? 193  GLU   A HG2  1 
ATOM   2356  H HG3  . GLU   A  1 167 ? 17.086 9.698   9.566   0.00 58.81  ? 193  GLU   A HG3  1 
ATOM   2357  N N    . ASP   A  1 168 ? 15.495 6.495   8.298   1.00 34.95  ? 194  ASP   A N    1 
ATOM   2358  C CA   . ASP   A  1 168 ? 14.323 5.613   8.308   1.00 35.12  ? 194  ASP   A CA   1 
ATOM   2359  C C    . ASP   A  1 168 ? 13.047 6.298   7.806   1.00 34.74  ? 194  ASP   A C    1 
ATOM   2360  O O    . ASP   A  1 168 ? 12.690 7.355   8.308   1.00 35.04  ? 194  ASP   A O    1 
ATOM   2361  C CB   . ASP   A  1 168 ? 14.091 5.046   9.714   1.00 37.17  ? 194  ASP   A CB   1 
ATOM   2362  C CG   . ASP   A  1 168 ? 13.052 3.951   9.723   1.00 42.99  ? 194  ASP   A CG   1 
ATOM   2363  O OD1  . ASP   A  1 168 ? 13.320 2.872   9.136   1.00 43.82  ? 194  ASP   A OD1  1 
ATOM   2364  O OD2  . ASP   A  1 168 ? 11.971 4.169   10.306  1.00 45.14  ? 194  ASP   A OD2  1 
ATOM   2365  H H    . ASP   A  1 168 ? 15.987 6.531   9.185   0.00 49.48  ? 194  ASP   A H    1 
ATOM   2366  H HA   . ASP   A  1 168 ? 14.535 4.769   7.653   0.00 49.04  ? 194  ASP   A HA   1 
ATOM   2367  H HB2  . ASP   A  1 168 ? 15.019 4.620   10.091  0.00 52.49  ? 194  ASP   A HB2  1 
ATOM   2368  H HB3  . ASP   A  1 168 ? 13.750 5.845   10.371  0.00 53.16  ? 194  ASP   A HB3  1 
ATOM   2369  N N    . GLY   A  1 169 ? 12.408 5.720   6.790   1.00 34.32  ? 195  GLY   A N    1 
ATOM   2370  C CA   . GLY   A  1 169 ? 11.187 6.272   6.217   1.00 34.22  ? 195  GLY   A CA   1 
ATOM   2371  C C    . GLY   A  1 169 ? 11.379 7.503   5.351   1.00 34.33  ? 195  GLY   A C    1 
ATOM   2372  O O    . GLY   A  1 169 ? 10.392 8.154   5.009   1.00 34.95  ? 195  GLY   A O    1 
ATOM   2373  H H    . GLY   A  1 169 ? 12.710 4.866   6.332   0.00 48.03  ? 195  GLY   A H    1 
ATOM   2374  H HA2  . GLY   A  1 169 ? 10.706 5.513   5.603   0.00 48.33  ? 195  GLY   A HA2  1 
ATOM   2375  H HA3  . GLY   A  1 169 ? 10.501 6.531   7.022   0.00 49.19  ? 195  GLY   A HA3  1 
ATOM   2376  N N    . VAL   A  1 170 ? 12.628 7.826   4.943   1.00 33.41  ? 196  VAL   A N    1 
ATOM   2377  C CA   . VAL   A  1 170 ? 12.869 9.020   4.126   1.00 33.42  ? 196  VAL   A CA   1 
ATOM   2378  C C    . VAL   A  1 170 ? 12.061 9.023   2.813   1.00 33.45  ? 196  VAL   A C    1 
ATOM   2379  O O    . VAL   A  1 170 ? 11.520 10.067  2.434   1.00 33.35  ? 196  VAL   A O    1 
ATOM   2380  C CB   . VAL   A  1 170 ? 14.383 9.250   3.868   1.00 34.05  ? 196  VAL   A CB   1 
ATOM   2381  C CG1  . VAL   A  1 170 ? 14.978 8.192   2.948   1.00 34.21  ? 196  VAL   A CG1  1 
ATOM   2382  C CG2  . VAL   A  1 170 ? 14.637 10.639  3.309   1.00 34.55  ? 196  VAL   A CG2  1 
ATOM   2383  H H    . VAL   A  1 170 ? 13.469 7.297   5.151   0.00 46.65  ? 196  VAL   A H    1 
ATOM   2384  H HA   . VAL   A  1 170 ? 12.498 9.862   4.706   0.00 47.36  ? 196  VAL   A HA   1 
ATOM   2385  H HB   . VAL   A  1 170 ? 14.906 9.183   4.821   0.00 47.28  ? 196  VAL   A HB   1 
ATOM   2386  H HG11 . VAL   A  1 170 ? 16.060 8.322   2.944   0.00 46.21  ? 196  VAL   A HG11 1 
ATOM   2387  H HG12 . VAL   A  1 170 ? 14.722 7.202   3.322   0.00 46.49  ? 196  VAL   A HG12 1 
ATOM   2388  H HG13 . VAL   A  1 170 ? 14.598 8.323   1.937   0.00 46.22  ? 196  VAL   A HG13 1 
ATOM   2389  H HG21 . VAL   A  1 170 ? 15.707 10.770  3.159   0.00 47.38  ? 196  VAL   A HG21 1 
ATOM   2390  H HG22 . VAL   A  1 170 ? 14.107 10.776  2.369   0.00 47.53  ? 196  VAL   A HG22 1 
ATOM   2391  H HG23 . VAL   A  1 170 ? 14.285 11.359  4.045   0.00 48.29  ? 196  VAL   A HG23 1 
ATOM   2392  N N    . PHE   A  1 171 ? 11.968 7.872   2.133   1.00 33.06  ? 197  PHE   A N    1 
ATOM   2393  C CA   . PHE   A  1 171 ? 11.227 7.788   0.868   1.00 33.38  ? 197  PHE   A CA   1 
ATOM   2394  C C    . PHE   A  1 171 ? 9.727  7.492   1.044   1.00 35.34  ? 197  PHE   A C    1 
ATOM   2395  O O    . PHE   A  1 171 ? 8.973  7.620   0.076   1.00 35.48  ? 197  PHE   A O    1 
ATOM   2396  C CB   . PHE   A  1 171 ? 11.825 6.688   -0.026  1.00 32.00  ? 197  PHE   A CB   1 
ATOM   2397  C CG   . PHE   A  1 171 ? 13.319 6.766   -0.208  1.00 31.02  ? 197  PHE   A CG   1 
ATOM   2398  C CD1  . PHE   A  1 171 ? 13.897 7.828   -0.885  1.00 30.86  ? 197  PHE   A CD1  1 
ATOM   2399  C CD2  . PHE   A  1 171 ? 14.146 5.766   0.275   1.00 30.93  ? 197  PHE   A CD2  1 
ATOM   2400  C CE1  . PHE   A  1 171 ? 15.270 7.885   -1.076  1.00 31.18  ? 197  PHE   A CE1  1 
ATOM   2401  C CE2  . PHE   A  1 171 ? 15.518 5.816   0.058   1.00 31.38  ? 197  PHE   A CE2  1 
ATOM   2402  C CZ   . PHE   A  1 171 ? 16.070 6.876   -0.611  1.00 30.96  ? 197  PHE   A CZ   1 
ATOM   2403  H H    . PHE   A  1 171 ? 12.375 6.992   2.434   0.00 45.42  ? 197  PHE   A H    1 
ATOM   2404  H HA   . PHE   A  1 171 ? 11.320 8.729   0.330   0.00 45.75  ? 197  PHE   A HA   1 
ATOM   2405  H HB2  . PHE   A  1 171 ? 11.586 5.719   0.410   0.00 43.44  ? 197  PHE   A HB2  1 
ATOM   2406  H HB3  . PHE   A  1 171 ? 11.372 6.761   -1.014  0.00 43.21  ? 197  PHE   A HB3  1 
ATOM   2407  H HD1  . PHE   A  1 171 ? 13.274 8.617   -1.272  0.00 41.51  ? 197  PHE   A HD1  1 
ATOM   2408  H HD2  . PHE   A  1 171 ? 13.723 4.917   0.786   0.00 41.49  ? 197  PHE   A HD2  1 
ATOM   2409  H HE1  . PHE   A  1 171 ? 15.706 8.717   -1.605  0.00 41.08  ? 197  PHE   A HE1  1 
ATOM   2410  H HE2  . PHE   A  1 171 ? 16.152 5.035   0.442   0.00 41.25  ? 197  PHE   A HE2  1 
ATOM   2411  H HZ   . PHE   A  1 171 ? 17.138 6.931   -0.750  0.00 40.38  ? 197  PHE   A HZ   1 
ATOM   2412  N N    . GLU   A  1 172 ? 9.309  7.048   2.242   1.00 36.55  ? 198  GLU   A N    1 
ATOM   2413  C CA   . GLU   A  1 172 ? 7.935  6.624   2.542   1.00 38.14  ? 198  GLU   A CA   1 
ATOM   2414  C C    . GLU   A  1 172 ? 6.855  7.611   2.125   1.00 39.32  ? 198  GLU   A C    1 
ATOM   2415  O O    . GLU   A  1 172 ? 5.805  7.185   1.643   1.00 40.28  ? 198  GLU   A O    1 
ATOM   2416  C CB   . GLU   A  1 172 ? 7.798  6.338   4.050   1.00 41.18  ? 198  GLU   A CB   1 
ATOM   2417  C CG   . GLU   A  1 172 ? 6.562  5.562   4.447   1.00 45.74  ? 198  GLU   A CG   1 
ATOM   2418  C CD   . GLU   A  1 172 ? 6.581  5.167   5.913   1.00 49.90  ? 198  GLU   A CD   1 
ATOM   2419  O OE1  . GLU   A  1 172 ? 7.142  5.933   6.731   1.00 50.08  ? 198  GLU   A OE1  1 
ATOM   2420  O OE2  . GLU   A  1 172 ? 6.049  4.083   6.242   1.00 51.24  ? 198  GLU   A OE2  1 
ATOM   2421  H H    . GLU   A  1 172 ? 9.930  6.971   3.040   0.00 50.66  ? 198  GLU   A H    1 
ATOM   2422  H HA   . GLU   A  1 172 ? 7.751  5.690   2.014   0.00 52.76  ? 198  GLU   A HA   1 
ATOM   2423  H HB2  . GLU   A  1 172 ? 8.655  5.755   4.384   0.00 56.96  ? 198  GLU   A HB2  1 
ATOM   2424  H HB3  . GLU   A  1 172 ? 7.777  7.292   4.574   0.00 57.67  ? 198  GLU   A HB3  1 
ATOM   2425  H HG2  . GLU   A  1 172 ? 5.678  6.174   4.280   0.00 63.64  ? 198  GLU   A HG2  1 
ATOM   2426  H HG3  . GLU   A  1 172 ? 6.508  4.652   3.850   0.00 62.86  ? 198  GLU   A HG3  1 
ATOM   2427  N N    . THR   A  1 173 ? 7.071  8.913   2.355   1.00 39.22  ? 199  THR   A N    1 
ATOM   2428  C CA   . THR   A  1 173 ? 6.086  9.943   2.013   1.00 39.69  ? 199  THR   A CA   1 
ATOM   2429  C C    . THR   A  1 173 ? 6.165  10.419  0.559   1.00 38.85  ? 199  THR   A C    1 
ATOM   2430  O O    . THR   A  1 173 ? 5.353  11.245  0.151   1.00 38.60  ? 199  THR   A O    1 
ATOM   2431  C CB   . THR   A  1 173 ? 6.219  11.116  2.987   1.00 42.59  ? 199  THR   A CB   1 
ATOM   2432  O OG1  . THR   A  1 173 ? 7.529  11.672  2.850   1.00 44.56  ? 199  THR   A OG1  1 
ATOM   2433  C CG2  . THR   A  1 173 ? 5.977  10.696  4.426   1.00 43.18  ? 199  THR   A CG2  1 
ATOM   2434  H H    . THR   A  1 173 ? 7.914  9.285   2.783   0.00 55.03  ? 199  THR   A H    1 
ATOM   2435  H HA   . THR   A  1 173 ? 5.085  9.539   2.158   0.00 56.62  ? 199  THR   A HA   1 
ATOM   2436  H HB   . THR   A  1 173 ? 5.479  11.874  2.737   0.00 60.74  ? 199  THR   A HB   1 
ATOM   2437  H HG1  . THR   A  1 173 ? 7.637  12.438  3.473   0.00 62.64  ? 199  THR   A HG1  1 
ATOM   2438  H HG21 . THR   A  1 173 ? 5.957  11.573  5.070   0.00 62.06  ? 199  THR   A HG21 1 
ATOM   2439  H HG22 . THR   A  1 173 ? 5.025  10.173  4.506   0.00 61.87  ? 199  THR   A HG22 1 
ATOM   2440  H HG23 . THR   A  1 173 ? 6.770  10.031  4.767   0.00 61.19  ? 199  THR   A HG23 1 
ATOM   2441  N N    . LEU   A  1 174 ? 7.108  9.894   -0.240  1.00 38.23  ? 200  LEU   A N    1 
ATOM   2442  C CA   . LEU   A  1 174 ? 7.208  10.244  -1.653  1.00 38.23  ? 200  LEU   A CA   1 
ATOM   2443  C C    . LEU   A  1 174 ? 6.262  9.288   -2.397  1.00 37.89  ? 200  LEU   A C    1 
ATOM   2444  O O    . LEU   A  1 174 ? 6.701  8.377   -3.103  1.00 38.14  ? 200  LEU   A O    1 
ATOM   2445  C CB   . LEU   A  1 174 ? 8.655  10.109  -2.155  1.00 38.21  ? 200  LEU   A CB   1 
ATOM   2446  C CG   . LEU   A  1 174 ? 9.668  11.207  -1.784  1.00 40.55  ? 200  LEU   A CG   1 
ATOM   2447  C CD1  . LEU   A  1 174 ? 9.631  11.583  -0.334  1.00 41.71  ? 200  LEU   A CD1  1 
ATOM   2448  C CD2  . LEU   A  1 174 ? 11.078 10.808  -2.188  1.00 41.00  ? 200  LEU   A CD2  1 
ATOM   2449  H H    . LEU   A  1 174 ? 7.811  9.224   0.053   0.00 52.90  ? 200  LEU   A H    1 
ATOM   2450  H HA   . LEU   A  1 174 ? 6.885  11.269  -1.825  0.00 53.20  ? 200  LEU   A HA   1 
ATOM   2451  H HB2  . LEU   A  1 174 ? 9.066  9.143   -1.866  0.00 51.74  ? 200  LEU   A HB2  1 
ATOM   2452  H HB3  . LEU   A  1 174 ? 8.597  10.184  -3.237  0.00 51.75  ? 200  LEU   A HB3  1 
ATOM   2453  H HG   . LEU   A  1 174 ? 9.415  12.101  -2.351  0.00 55.00  ? 200  LEU   A HG   1 
ATOM   2454  H HD11 . LEU   A  1 174 ? 10.506 12.192  -0.117  0.00 56.82  ? 200  LEU   A HD11 1 
ATOM   2455  H HD12 . LEU   A  1 174 ? 8.724  12.152  -0.138  0.00 57.45  ? 200  LEU   A HD12 1 
ATOM   2456  H HD13 . LEU   A  1 174 ? 9.642  10.678  0.272   0.00 56.86  ? 200  LEU   A HD13 1 
ATOM   2457  H HD21 . LEU   A  1 174 ? 11.755 11.642  -2.004  0.00 54.69  ? 200  LEU   A HD21 1 
ATOM   2458  H HD22 . LEU   A  1 174 ? 11.390 9.940   -1.612  0.00 54.56  ? 200  LEU   A HD22 1 
ATOM   2459  H HD23 . LEU   A  1 174 ? 11.078 10.562  -3.249  0.00 54.23  ? 200  LEU   A HD23 1 
ATOM   2460  N N    . THR   A  1 175 ? 4.952  9.526   -2.239  1.00 37.01  ? 201  THR   A N    1 
ATOM   2461  C CA   . THR   A  1 175 ? 3.890  8.660   -2.754  1.00 36.63  ? 201  THR   A CA   1 
ATOM   2462  C C    . THR   A  1 175 ? 3.648  8.759   -4.280  1.00 35.77  ? 201  THR   A C    1 
ATOM   2463  O O    . THR   A  1 175 ? 2.793  8.042   -4.791  1.00 35.50  ? 201  THR   A O    1 
ATOM   2464  C CB   . THR   A  1 175 ? 2.610  8.890   -1.954  1.00 37.76  ? 201  THR   A CB   1 
ATOM   2465  O OG1  . THR   A  1 175 ? 2.131  10.214  -2.188  1.00 38.88  ? 201  THR   A OG1  1 
ATOM   2466  C CG2  . THR   A  1 175 ? 2.825  8.663   -0.454  1.00 38.36  ? 201  THR   A CG2  1 
ATOM   2467  H H    . THR   A  1 175 ? 4.598  10.352  -1.765  0.00 52.52  ? 201  THR   A H    1 
ATOM   2468  H HA   . THR   A  1 175 ? 4.189  7.631   -2.560  0.00 51.36  ? 201  THR   A HA   1 
ATOM   2469  H HB   . THR   A  1 175 ? 1.852  8.182   -2.286  0.00 54.05  ? 201  THR   A HB   1 
ATOM   2470  H HG1  . THR   A  1 175 ? 1.300  10.374  -1.667  0.00 56.41  ? 201  THR   A HG1  1 
ATOM   2471  H HG21 . THR   A  1 175 ? 1.865  8.656   0.061   0.00 55.58  ? 201  THR   A HG21 1 
ATOM   2472  H HG22 . THR   A  1 175 ? 3.325  7.710   -0.287  0.00 54.54  ? 201  THR   A HG22 1 
ATOM   2473  H HG23 . THR   A  1 175 ? 3.435  9.462   -0.034  0.00 54.99  ? 201  THR   A HG23 1 
ATOM   2474  N N    . ASN   A  1 176 ? 4.409  9.584   -5.008  1.00 35.06  ? 202  ASN   A N    1 
ATOM   2475  C CA   . ASN   A  1 176 ? 4.355  9.619   -6.478  1.00 34.66  ? 202  ASN   A CA   1 
ATOM   2476  C C    . ASN   A  1 176 ? 5.692  9.109   -7.094  1.00 32.48  ? 202  ASN   A C    1 
ATOM   2477  O O    . ASN   A  1 176 ? 5.867  9.187   -8.313  1.00 31.97  ? 202  ASN   A O    1 
ATOM   2478  C CB   . ASN   A  1 176 ? 4.058  11.045  -6.964  1.00 37.83  ? 202  ASN   A CB   1 
ATOM   2479  C CG   . ASN   A  1 176 ? 2.779  11.631  -6.416  1.00 43.75  ? 202  ASN   A CG   1 
ATOM   2480  O OD1  . ASN   A  1 176 ? 2.764  12.745  -5.884  1.00 46.35  ? 202  ASN   A OD1  1 
ATOM   2481  N ND2  . ASN   A  1 176 ? 1.669  10.910  -6.533  1.00 45.10  ? 202  ASN   A ND2  1 
ATOM   2482  H H    . ASN   A  1 176 ? 5.066  10.256  -4.624  0.00 49.10  ? 202  ASN   A H    1 
ATOM   2483  H HA   . ASN   A  1 176 ? 3.564  8.974   -6.855  0.00 48.45  ? 202  ASN   A HA   1 
ATOM   2484  H HB2  . ASN   A  1 176 ? 4.877  11.695  -6.660  0.00 52.37  ? 202  ASN   A HB2  1 
ATOM   2485  H HB3  . ASN   A  1 176 ? 3.975  11.039  -8.050  0.00 52.29  ? 202  ASN   A HB3  1 
ATOM   2486  H HD21 . ASN   A  1 176 ? 0.792  11.278  -6.176  0.00 63.16  ? 202  ASN   A HD21 1 
ATOM   2487  H HD22 . ASN   A  1 176 ? 1.680  10.006  -6.993  0.00 62.16  ? 202  ASN   A HD22 1 
ATOM   2488  N N    . LEU   A  1 177 ? 6.637  8.591   -6.263  1.00 30.70  ? 203  LEU   A N    1 
ATOM   2489  C CA   . LEU   A  1 177 ? 7.940  8.146   -6.733  1.00 29.66  ? 203  LEU   A CA   1 
ATOM   2490  C C    . LEU   A  1 177 ? 7.802  6.869   -7.536  1.00 28.78  ? 203  LEU   A C    1 
ATOM   2491  O O    . LEU   A  1 177 ? 7.305  5.873   -7.018  1.00 27.86  ? 203  LEU   A O    1 
ATOM   2492  C CB   . LEU   A  1 177 ? 8.879  7.909   -5.543  1.00 29.33  ? 203  LEU   A CB   1 
ATOM   2493  C CG   . LEU   A  1 177 ? 10.371 7.766   -5.851  1.00 30.19  ? 203  LEU   A CG   1 
ATOM   2494  C CD1  . LEU   A  1 177 ? 10.937 9.066   -6.451  1.00 31.23  ? 203  LEU   A CD1  1 
ATOM   2495  C CD2  . LEU   A  1 177 ? 11.137 7.371   -4.589  1.00 29.95  ? 203  LEU   A CD2  1 
ATOM   2496  H H    . LEU   A  1 177 ? 6.510  8.451   -5.266  0.00 42.62  ? 203  LEU   A H    1 
ATOM   2497  H HA   . LEU   A  1 177 ? 8.357  8.927   -7.365  0.00 40.15  ? 203  LEU   A HA   1 
ATOM   2498  H HB2  . LEU   A  1 177 ? 8.784  8.765   -4.882  0.00 40.19  ? 203  LEU   A HB2  1 
ATOM   2499  H HB3  . LEU   A  1 177 ? 8.565  7.011   -5.013  0.00 39.88  ? 203  LEU   A HB3  1 
ATOM   2500  H HG   . LEU   A  1 177 ? 10.513 6.973   -6.583  0.00 39.73  ? 203  LEU   A HG   1 
ATOM   2501  H HD11 . LEU   A  1 177 ? 12.023 9.048   -6.376  0.00 40.88  ? 203  LEU   A HD11 1 
ATOM   2502  H HD12 . LEU   A  1 177 ? 10.651 9.131   -7.499  0.00 41.13  ? 203  LEU   A HD12 1 
ATOM   2503  H HD13 . LEU   A  1 177 ? 10.542 9.921   -5.903  0.00 41.76  ? 203  LEU   A HD13 1 
ATOM   2504  H HD21 . LEU   A  1 177 ? 12.200 7.314   -4.814  0.00 39.39  ? 203  LEU   A HD21 1 
ATOM   2505  H HD22 . LEU   A  1 177 ? 10.962 8.122   -3.819  0.00 40.28  ? 203  LEU   A HD22 1 
ATOM   2506  H HD23 . LEU   A  1 177 ? 10.777 6.402   -4.246  0.00 39.88  ? 203  LEU   A HD23 1 
ATOM   2507  N N    . GLU   A  1 178 ? 8.246  6.916   -8.799  1.00 28.56  ? 204  GLU   A N    1 
ATOM   2508  C CA   . GLU   A  1 178 ? 8.200  5.803   -9.737  1.00 28.86  ? 204  GLU   A CA   1 
ATOM   2509  C C    . GLU   A  1 178 ? 9.595  5.231   -9.998  1.00 28.56  ? 204  GLU   A C    1 
ATOM   2510  O O    . GLU   A  1 178 ? 9.693  4.046   -10.275 1.00 28.55  ? 204  GLU   A O    1 
ATOM   2511  C CB   . GLU   A  1 178 ? 7.560  6.260   -11.059 1.00 31.07  ? 204  GLU   A CB   1 
ATOM   2512  C CG   . GLU   A  1 178 ? 6.102  6.655   -10.901 1.00 36.21  ? 204  GLU   A CG   1 
ATOM   2513  C CD   . GLU   A  1 178 ? 5.413  7.050   -12.192 1.00 44.38  ? 204  GLU   A CD   1 
ATOM   2514  O OE1  . GLU   A  1 178 ? 6.118  7.332   -13.186 1.00 46.36  ? 204  GLU   A OE1  1 
ATOM   2515  O OE2  . GLU   A  1 178 ? 4.162  7.085   -12.209 1.00 48.38  ? 204  GLU   A OE2  1 
ATOM   2516  H H    . GLU   A  1 178 ? 8.655  7.745   -9.215  0.00 38.02  ? 204  GLU   A H    1 
ATOM   2517  H HA   . GLU   A  1 178 ? 7.582  4.999   -9.340  0.00 38.30  ? 204  GLU   A HA   1 
ATOM   2518  H HB2  . GLU   A  1 178 ? 8.112  7.119   -11.436 0.00 40.66  ? 204  GLU   A HB2  1 
ATOM   2519  H HB3  . GLU   A  1 178 ? 7.611  5.443   -11.776 0.00 40.52  ? 204  GLU   A HB3  1 
ATOM   2520  H HG2  . GLU   A  1 178 ? 5.557  5.813   -10.478 0.00 47.93  ? 204  GLU   A HG2  1 
ATOM   2521  H HG3  . GLU   A  1 178 ? 6.038  7.507   -10.225 0.00 48.07  ? 204  GLU   A HG3  1 
ATOM   2522  N N    . LEU   A  1 179 ? 10.663 6.049   -9.939  1.00 27.53  ? 205  LEU   A N    1 
ATOM   2523  C CA   . LEU   A  1 179 ? 12.015 5.563   -10.172 1.00 26.74  ? 205  LEU   A CA   1 
ATOM   2524  C C    . LEU   A  1 179 ? 12.934 6.011   -9.036  1.00 26.47  ? 205  LEU   A C    1 
ATOM   2525  O O    . LEU   A  1 179 ? 12.990 7.202   -8.707  1.00 26.96  ? 205  LEU   A O    1 
ATOM   2526  C CB   . LEU   A  1 179 ? 12.544 6.062   -11.529 1.00 26.75  ? 205  LEU   A CB   1 
ATOM   2527  C CG   . LEU   A  1 179 ? 13.934 5.571   -11.974 1.00 28.95  ? 205  LEU   A CG   1 
ATOM   2528  C CD1  . LEU   A  1 179 ? 14.076 5.663   -13.499 1.00 29.50  ? 205  LEU   A CD1  1 
ATOM   2529  C CD2  . LEU   A  1 179 ? 15.059 6.371   -11.332 1.00 30.14  ? 205  LEU   A CD2  1 
ATOM   2530  H H    . LEU   A  1 179 ? 10.623 7.045   -9.745  0.00 35.74  ? 205  LEU   A H    1 
ATOM   2531  H HA   . LEU   A  1 179 ? 12.028 4.476   -10.201 0.00 33.76  ? 205  LEU   A HA   1 
ATOM   2532  H HB2  . LEU   A  1 179 ? 11.836 5.747   -12.294 0.00 33.60  ? 205  LEU   A HB2  1 
ATOM   2533  H HB3  . LEU   A  1 179 ? 12.578 7.149   -11.513 0.00 33.73  ? 205  LEU   A HB3  1 
ATOM   2534  H HG   . LEU   A  1 179 ? 14.055 4.530   -11.681 0.00 35.42  ? 205  LEU   A HG   1 
ATOM   2535  H HD11 . LEU   A  1 179 ? 15.072 5.332   -13.787 0.00 35.44  ? 205  LEU   A HD11 1 
ATOM   2536  H HD12 . LEU   A  1 179 ? 13.329 5.022   -13.964 0.00 35.95  ? 205  LEU   A HD12 1 
ATOM   2537  H HD13 . LEU   A  1 179 ? 13.924 6.694   -13.810 0.00 36.02  ? 205  LEU   A HD13 1 
ATOM   2538  H HD21 . LEU   A  1 179 ? 16.009 6.047   -11.755 0.00 36.43  ? 205  LEU   A HD21 1 
ATOM   2539  H HD22 . LEU   A  1 179 ? 14.908 7.430   -11.534 0.00 37.04  ? 205  LEU   A HD22 1 
ATOM   2540  H HD23 . LEU   A  1 179 ? 15.065 6.192   -10.258 0.00 37.08  ? 205  LEU   A HD23 1 
ATOM   2541  N N    . LEU   A  1 180 ? 13.631 5.053   -8.423  1.00 25.63  ? 206  LEU   A N    1 
ATOM   2542  C CA   . LEU   A  1 180 ? 14.581 5.339   -7.361  1.00 25.51  ? 206  LEU   A CA   1 
ATOM   2543  C C    . LEU   A  1 180 ? 15.852 4.620   -7.727  1.00 25.05  ? 206  LEU   A C    1 
ATOM   2544  O O    . LEU   A  1 180 ? 15.844 3.392   -7.856  1.00 25.99  ? 206  LEU   A O    1 
ATOM   2545  C CB   . LEU   A  1 180 ? 14.066 4.849   -5.998  1.00 25.79  ? 206  LEU   A CB   1 
ATOM   2546  C CG   . LEU   A  1 180 ? 15.031 4.981   -4.805  1.00 27.65  ? 206  LEU   A CG   1 
ATOM   2547  C CD1  . LEU   A  1 180 ? 15.437 6.438   -4.582  1.00 27.93  ? 206  LEU   A CD1  1 
ATOM   2548  C CD2  . LEU   A  1 180 ? 14.401 4.405   -3.541  1.00 28.03  ? 206  LEU   A CD2  1 
ATOM   2549  H H    . LEU   A  1 180 ? 13.557 4.062   -8.632  0.00 32.21  ? 206  LEU   A H    1 
ATOM   2550  H HA   . LEU   A  1 180 ? 14.784 6.406   -7.299  0.00 32.37  ? 206  LEU   A HA   1 
ATOM   2551  H HB2  . LEU   A  1 180 ? 13.178 5.425   -5.749  0.00 33.48  ? 206  LEU   A HB2  1 
ATOM   2552  H HB3  . LEU   A  1 180 ? 13.805 3.796   -6.087  0.00 32.96  ? 206  LEU   A HB3  1 
ATOM   2553  H HG   . LEU   A  1 180 ? 15.938 4.409   -4.998  0.00 34.95  ? 206  LEU   A HG   1 
ATOM   2554  H HD11 . LEU   A  1 180 ? 15.970 6.515   -3.636  0.00 36.01  ? 206  LEU   A HD11 1 
ATOM   2555  H HD12 . LEU   A  1 180 ? 16.088 6.758   -5.395  0.00 35.49  ? 206  LEU   A HD12 1 
ATOM   2556  H HD13 . LEU   A  1 180 ? 14.540 7.056   -4.559  0.00 36.24  ? 206  LEU   A HD13 1 
ATOM   2557  H HD21 . LEU   A  1 180 ? 15.113 4.487   -2.721  0.00 36.34  ? 206  LEU   A HD21 1 
ATOM   2558  H HD22 . LEU   A  1 180 ? 13.499 4.968   -3.308  0.00 36.71  ? 206  LEU   A HD22 1 
ATOM   2559  H HD23 . LEU   A  1 180 ? 14.153 3.359   -3.714  0.00 36.16  ? 206  LEU   A HD23 1 
ATOM   2560  N N    . SER   A  1 181 ? 16.940 5.358   -7.913  1.00 23.23  ? 207  SER   A N    1 
ATOM   2561  C CA   . SER   A  1 181 ? 18.222 4.734   -8.214  1.00 22.56  ? 207  SER   A CA   1 
ATOM   2562  C C    . SER   A  1 181 ? 19.234 5.066   -7.147  1.00 22.98  ? 207  SER   A C    1 
ATOM   2563  O O    . SER   A  1 181 ? 19.586 6.234   -6.986  1.00 22.49  ? 207  SER   A O    1 
ATOM   2564  C CB   . SER   A  1 181 ? 18.738 5.163   -9.577  1.00 21.60  ? 207  SER   A CB   1 
ATOM   2565  O OG   . SER   A  1 181 ? 20.028 4.610   -9.784  1.00 22.08  ? 207  SER   A OG   1 
ATOM   2566  H H    . SER   A  1 181 ? 16.976 6.372   -7.866  0.00 28.84  ? 207  SER   A H    1 
ATOM   2567  H HA   . SER   A  1 181 ? 18.108 3.653   -8.233  0.00 27.28  ? 207  SER   A HA   1 
ATOM   2568  H HB2  . SER   A  1 181 ? 18.062 4.795   -10.348 0.00 25.75  ? 207  SER   A HB2  1 
ATOM   2569  H HB3  . SER   A  1 181 ? 18.803 6.248   -9.622  0.00 25.95  ? 207  SER   A HB3  1 
ATOM   2570  H HG   . SER   A  1 181 ? 20.378 4.890   -10.670 0.00 25.71  ? 207  SER   A HG   1 
ATOM   2571  N N    . LEU   A  1 182 ? 19.689 4.039   -6.406  1.00 23.28  ? 208  LEU   A N    1 
ATOM   2572  C CA   . LEU   A  1 182 ? 20.718 4.169   -5.371  1.00 23.17  ? 208  LEU   A CA   1 
ATOM   2573  C C    . LEU   A  1 182 ? 21.952 3.315   -5.677  1.00 22.04  ? 208  LEU   A C    1 
ATOM   2574  O O    . LEU   A  1 182 ? 22.786 3.126   -4.800  1.00 21.18  ? 208  LEU   A O    1 
ATOM   2575  C CB   . LEU   A  1 182 ? 20.140 3.739   -4.013  1.00 24.63  ? 208  LEU   A CB   1 
ATOM   2576  C CG   . LEU   A  1 182 ? 19.002 4.583   -3.459  1.00 27.19  ? 208  LEU   A CG   1 
ATOM   2577  C CD1  . LEU   A  1 182 ? 18.182 3.776   -2.443  1.00 27.44  ? 208  LEU   A CD1  1 
ATOM   2578  C CD2  . LEU   A  1 182 ? 19.556 5.841   -2.797  1.00 28.71  ? 208  LEU   A CD2  1 
ATOM   2579  H H    . LEU   A  1 182 ? 19.356 3.085   -6.500  0.00 28.27  ? 208  LEU   A H    1 
ATOM   2580  H HA   . LEU   A  1 182 ? 21.058 5.200   -5.296  0.00 28.39  ? 208  LEU   A HA   1 
ATOM   2581  H HB2  . LEU   A  1 182 ? 19.773 2.720   -4.103  0.00 30.47  ? 208  LEU   A HB2  1 
ATOM   2582  H HB3  . LEU   A  1 182 ? 20.929 3.781   -3.265  0.00 30.63  ? 208  LEU   A HB3  1 
ATOM   2583  H HG   . LEU   A  1 182 ? 18.328 4.887   -4.259  0.00 34.08  ? 208  LEU   A HG   1 
ATOM   2584  H HD11 . LEU   A  1 182 ? 17.416 4.421   -2.016  0.00 35.26  ? 208  LEU   A HD11 1 
ATOM   2585  H HD12 . LEU   A  1 182 ? 17.711 2.935   -2.951  0.00 34.70  ? 208  LEU   A HD12 1 
ATOM   2586  H HD13 . LEU   A  1 182 ? 18.845 3.414   -1.659  0.00 34.92  ? 208  LEU   A HD13 1 
ATOM   2587  H HD21 . LEU   A  1 182 ? 18.755 6.574   -2.712  0.00 36.56  ? 208  LEU   A HD21 1 
ATOM   2588  H HD22 . LEU   A  1 182 ? 19.912 5.576   -1.802  0.00 36.46  ? 208  LEU   A HD22 1 
ATOM   2589  H HD23 . LEU   A  1 182 ? 20.379 6.246   -3.381  0.00 35.93  ? 208  LEU   A HD23 1 
ATOM   2590  N N    . SER   A  1 183 ? 22.112 2.867   -6.922  1.00 21.50  ? 209  SER   A N    1 
ATOM   2591  C CA   . SER   A  1 183 ? 23.240 2.040   -7.332  1.00 21.46  ? 209  SER   A CA   1 
ATOM   2592  C C    . SER   A  1 183 ? 24.599 2.668   -7.043  1.00 21.43  ? 209  SER   A C    1 
ATOM   2593  O O    . SER   A  1 183 ? 24.703 3.893   -6.996  1.00 21.74  ? 209  SER   A O    1 
ATOM   2594  C CB   . SER   A  1 183 ? 23.146 1.765   -8.831  1.00 21.28  ? 209  SER   A CB   1 
ATOM   2595  O OG   . SER   A  1 183 ? 21.902 1.133   -9.088  1.00 22.12  ? 209  SER   A OG   1 
ATOM   2596  H H    . SER   A  1 183 ? 21.461 3.085   -7.670  0.00 25.36  ? 209  SER   A H    1 
ATOM   2597  H HA   . SER   A  1 183 ? 23.188 1.086   -6.810  0.00 25.10  ? 209  SER   A HA   1 
ATOM   2598  H HB2  . SER   A  1 183 ? 23.191 2.707   -9.375  0.00 24.29  ? 209  SER   A HB2  1 
ATOM   2599  H HB3  . SER   A  1 183 ? 23.968 1.116   -9.130  0.00 24.12  ? 209  SER   A HB3  1 
ATOM   2600  H HG   . SER   A  1 183 ? 21.816 0.936   -10.057 0.00 25.26  ? 209  SER   A HG   1 
ATOM   2601  N N    . PHE   A  1 184 ? 25.641 1.841   -6.882  1.00 20.43  ? 210  PHE   A N    1 
ATOM   2602  C CA   . PHE   A  1 184 ? 27.010 2.321   -6.677  1.00 21.15  ? 210  PHE   A CA   1 
ATOM   2603  C C    . PHE   A  1 184 ? 27.115 3.263   -5.483  1.00 22.09  ? 210  PHE   A C    1 
ATOM   2604  O O    . PHE   A  1 184 ? 27.631 4.379   -5.565  1.00 22.09  ? 210  PHE   A O    1 
ATOM   2605  C CB   . PHE   A  1 184 ? 27.580 2.939   -7.981  1.00 20.71  ? 210  PHE   A CB   1 
ATOM   2606  C CG   . PHE   A  1 184 ? 27.726 1.915   -9.076  1.00 20.50  ? 210  PHE   A CG   1 
ATOM   2607  C CD1  . PHE   A  1 184 ? 26.666 1.622   -9.917  1.00 20.82  ? 210  PHE   A CD1  1 
ATOM   2608  C CD2  . PHE   A  1 184 ? 28.896 1.185   -9.210  1.00 21.07  ? 210  PHE   A CD2  1 
ATOM   2609  C CE1  . PHE   A  1 184 ? 26.792 0.648   -10.903 1.00 21.45  ? 210  PHE   A CE1  1 
ATOM   2610  C CE2  . PHE   A  1 184 ? 29.030 0.237   -10.218 1.00 21.51  ? 210  PHE   A CE2  1 
ATOM   2611  C CZ   . PHE   A  1 184 ? 27.966 -0.055  -11.026 1.00 21.22  ? 210  PHE   A CZ   1 
ATOM   2612  H H    . PHE   A  1 184 ? 25.565 0.829   -6.875  0.00 23.50  ? 210  PHE   A H    1 
ATOM   2613  H HA   . PHE   A  1 184 ? 27.632 1.460   -6.435  0.00 24.32  ? 210  PHE   A HA   1 
ATOM   2614  H HB2  . PHE   A  1 184 ? 26.911 3.716   -8.348  0.00 23.47  ? 210  PHE   A HB2  1 
ATOM   2615  H HB3  . PHE   A  1 184 ? 28.568 3.355   -7.791  0.00 23.45  ? 210  PHE   A HB3  1 
ATOM   2616  H HD1  . PHE   A  1 184 ? 25.738 2.156   -9.813  0.00 23.21  ? 210  PHE   A HD1  1 
ATOM   2617  H HD2  . PHE   A  1 184 ? 29.732 1.397   -8.567  0.00 23.44  ? 210  PHE   A HD2  1 
ATOM   2618  H HE1  . PHE   A  1 184 ? 25.963 0.438   -11.558 0.00 23.41  ? 210  PHE   A HE1  1 
ATOM   2619  H HE2  . PHE   A  1 184 ? 29.949 -0.316  -10.316 0.00 23.41  ? 210  PHE   A HE2  1 
ATOM   2620  H HZ   . PHE   A  1 184 ? 28.069 -0.792  -11.804 0.00 22.81  ? 210  PHE   A HZ   1 
ATOM   2621  N N    . ASN   A  1 185 ? 26.571 2.777   -4.374  1.00 22.93  ? 211  ASN   A N    1 
ATOM   2622  C CA   . ASN   A  1 185 ? 26.606 3.372   -3.042  1.00 23.54  ? 211  ASN   A CA   1 
ATOM   2623  C C    . ASN   A  1 185 ? 26.770 2.197   -2.065  1.00 25.08  ? 211  ASN   A C    1 
ATOM   2624  O O    . ASN   A  1 185 ? 26.391 1.084   -2.423  1.00 25.25  ? 211  ASN   A O    1 
ATOM   2625  C CB   . ASN   A  1 185 ? 25.304 4.116   -2.745  1.00 23.60  ? 211  ASN   A CB   1 
ATOM   2626  C CG   . ASN   A  1 185 ? 25.194 5.431   -3.485  1.00 25.25  ? 211  ASN   A CG   1 
ATOM   2627  O OD1  . ASN   A  1 185 ? 26.078 6.291   -3.382  1.00 26.40  ? 211  ASN   A OD1  1 
ATOM   2628  N ND2  . ASN   A  1 185 ? 24.124 5.632   -4.236  1.00 24.30  ? 211  ASN   A ND2  1 
ATOM   2629  H H    . ASN   A  1 185 ? 26.044 1.909   -4.386  0.00 27.30  ? 211  ASN   A H    1 
ATOM   2630  H HA   . ASN   A  1 185 ? 27.454 4.048   -2.936  0.00 28.59  ? 211  ASN   A HA   1 
ATOM   2631  H HB2  . ASN   A  1 185 ? 24.467 3.477   -3.024  0.00 28.87  ? 211  ASN   A HB2  1 
ATOM   2632  H HB3  . ASN   A  1 185 ? 25.261 4.333   -1.679  0.00 29.35  ? 211  ASN   A HB3  1 
ATOM   2633  H HD21 . ASN   A  1 185 ? 24.026 6.505   -4.743  0.00 29.60  ? 211  ASN   A HD21 1 
ATOM   2634  H HD22 . ASN   A  1 185 ? 23.398 4.926   -4.309  0.00 29.62  ? 211  ASN   A HD22 1 
ATOM   2635  N N    . SER   A  1 186 ? 27.334 2.409   -0.871  1.00 25.58  ? 212  SER   A N    1 
ATOM   2636  C CA   . SER   A  1 186 ? 27.460 1.319   0.092   1.00 27.08  ? 212  SER   A CA   1 
ATOM   2637  C C    . SER   A  1 186 ? 26.220 1.336   0.985   1.00 27.79  ? 212  SER   A C    1 
ATOM   2638  O O    . SER   A  1 186 ? 26.169 2.102   1.950   1.00 28.02  ? 212  SER   A O    1 
ATOM   2639  C CB   . SER   A  1 186 ? 28.745 1.450   0.901   1.00 29.62  ? 212  SER   A CB   1 
ATOM   2640  O OG   . SER   A  1 186 ? 28.793 0.476   1.932   1.00 33.74  ? 212  SER   A OG   1 
ATOM   2641  H H    . SER   A  1 186 ? 27.699 3.302   -0.555  0.00 31.82  ? 212  SER   A H    1 
ATOM   2642  H HA   . SER   A  1 186 ? 27.504 0.358   -0.418  0.00 33.47  ? 212  SER   A HA   1 
ATOM   2643  H HB2  . SER   A  1 186 ? 29.593 1.293   0.236   0.00 36.72  ? 212  SER   A HB2  1 
ATOM   2644  H HB3  . SER   A  1 186 ? 28.794 2.447   1.330   0.00 37.28  ? 212  SER   A HB3  1 
ATOM   2645  H HG   . SER   A  1 186 ? 28.420 -0.390  1.618   0.00 42.14  ? 212  SER   A HG   1 
ATOM   2646  N N    . LEU   A  1 187 ? 25.213 0.512   0.655   1.00 27.75  ? 213  LEU   A N    1 
ATOM   2647  C CA   . LEU   A  1 187 ? 23.956 0.462   1.414   1.00 28.35  ? 213  LEU   A CA   1 
ATOM   2648  C C    . LEU   A  1 187 ? 23.897 -0.677  2.440   1.00 29.60  ? 213  LEU   A C    1 
ATOM   2649  O O    . LEU   A  1 187 ? 23.277 -0.491  3.484   1.00 29.95  ? 213  LEU   A O    1 
ATOM   2650  C CB   . LEU   A  1 187 ? 22.748 0.307   0.470   1.00 28.02  ? 213  LEU   A CB   1 
ATOM   2651  C CG   . LEU   A  1 187 ? 22.596 1.304   -0.689  1.00 29.05  ? 213  LEU   A CG   1 
ATOM   2652  C CD1  . LEU   A  1 187 ? 21.289 1.071   -1.398  1.00 29.07  ? 213  LEU   A CD1  1 
ATOM   2653  C CD2  . LEU   A  1 187 ? 22.679 2.742   -0.214  1.00 29.58  ? 213  LEU   A CD2  1 
ATOM   2654  H H    . LEU   A  1 187 ? 25.235 -0.130  -0.130  0.00 34.55  ? 213  LEU   A H    1 
ATOM   2655  H HA   . LEU   A  1 187 ? 23.818 1.392   1.961   0.00 36.33  ? 213  LEU   A HA   1 
ATOM   2656  H HB2  . LEU   A  1 187 ? 22.784 -0.692  0.039   0.00 35.22  ? 213  LEU   A HB2  1 
ATOM   2657  H HB3  . LEU   A  1 187 ? 21.846 0.393   1.074   0.00 35.80  ? 213  LEU   A HB3  1 
ATOM   2658  H HG   . LEU   A  1 187 ? 23.408 1.164   -1.402  0.00 35.94  ? 213  LEU   A HG   1 
ATOM   2659  H HD11 . LEU   A  1 187 ? 21.253 1.695   -2.289  0.00 36.03  ? 213  LEU   A HD11 1 
ATOM   2660  H HD12 . LEU   A  1 187 ? 21.223 0.020   -1.677  0.00 36.14  ? 213  LEU   A HD12 1 
ATOM   2661  H HD13 . LEU   A  1 187 ? 20.471 1.328   -0.727  0.00 36.69  ? 213  LEU   A HD13 1 
ATOM   2662  H HD21 . LEU   A  1 187 ? 22.324 3.399   -1.007  0.00 37.08  ? 213  LEU   A HD21 1 
ATOM   2663  H HD22 . LEU   A  1 187 ? 22.065 2.861   0.678   0.00 37.69  ? 213  LEU   A HD22 1 
ATOM   2664  H HD23 . LEU   A  1 187 ? 23.720 2.969   0.008   0.00 37.21  ? 213  LEU   A HD23 1 
ATOM   2665  N N    . SER   A  1 188 ? 24.440 -1.874  2.112   1.00 30.28  ? 214  SER   A N    1 
ATOM   2666  C CA   . SER   A  1 188 ? 24.413 -3.066  2.985   1.00 31.67  ? 214  SER   A CA   1 
ATOM   2667  C C    . SER   A  1 188 ? 23.041 -3.769  3.069   1.00 32.35  ? 214  SER   A C    1 
ATOM   2668  O O    . SER   A  1 188 ? 23.004 -4.988  3.207   1.00 33.24  ? 214  SER   A O    1 
ATOM   2669  C CB   . SER   A  1 188 ? 24.924 -2.755  4.394   1.00 33.98  ? 214  SER   A CB   1 
ATOM   2670  O OG   . SER   A  1 188 ? 26.306 -2.431  4.389   1.00 37.84  ? 214  SER   A OG   1 
ATOM   2671  H H    . SER   A  1 188 ? 24.906 -2.054  1.228   0.00 38.09  ? 214  SER   A H    1 
ATOM   2672  H HA   . SER   A  1 188 ? 25.094 -3.797  2.551   0.00 40.27  ? 214  SER   A HA   1 
ATOM   2673  H HB2  . SER   A  1 188 ? 24.360 -1.930  4.825   0.00 44.07  ? 214  SER   A HB2  1 
ATOM   2674  H HB3  . SER   A  1 188 ? 24.787 -3.643  5.009   0.00 44.11  ? 214  SER   A HB3  1 
ATOM   2675  H HG   . SER   A  1 188 ? 26.609 -2.226  5.312   0.00 48.74  ? 214  SER   A HG   1 
ATOM   2676  N N    . HIS   A  1 189 ? 21.935 -3.031  3.036   1.00 32.12  ? 215  HIS   A N    1 
ATOM   2677  C CA   . HIS   A  1 189 ? 20.589 -3.612  3.098   1.00 33.11  ? 215  HIS   A CA   1 
ATOM   2678  C C    . HIS   A  1 189 ? 19.638 -2.829  2.213   1.00 31.83  ? 215  HIS   A C    1 
ATOM   2679  O O    . HIS   A  1 189 ? 19.822 -1.629  2.023   1.00 31.41  ? 215  HIS   A O    1 
ATOM   2680  C CB   . HIS   A  1 189 ? 20.049 -3.569  4.544   1.00 35.94  ? 215  HIS   A CB   1 
ATOM   2681  C CG   . HIS   A  1 189 ? 20.960 -4.217  5.540   1.00 42.54  ? 215  HIS   A CG   1 
ATOM   2682  N ND1  . HIS   A  1 189 ? 20.840 -5.560  5.869   1.00 45.74  ? 215  HIS   A ND1  1 
ATOM   2683  C CD2  . HIS   A  1 189 ? 22.010 -3.694  6.220   1.00 44.52  ? 215  HIS   A CD2  1 
ATOM   2684  C CE1  . HIS   A  1 189 ? 21.802 -5.804  6.748   1.00 46.42  ? 215  HIS   A CE1  1 
ATOM   2685  N NE2  . HIS   A  1 189 ? 22.533 -4.711  6.985   1.00 46.04  ? 215  HIS   A NE2  1 
ATOM   2686  H H    . HIS   A  1 189 ? 21.917 -2.018  2.986   0.00 41.36  ? 215  HIS   A H    1 
ATOM   2687  H HA   . HIS   A  1 189 ? 20.593 -4.647  2.757   0.00 42.67  ? 215  HIS   A HA   1 
ATOM   2688  H HB2  . HIS   A  1 189 ? 19.917 -2.528  4.836   0.00 47.01  ? 215  HIS   A HB2  1 
ATOM   2689  H HB3  . HIS   A  1 189 ? 19.091 -4.086  4.579   0.00 47.04  ? 215  HIS   A HB3  1 
ATOM   2690  H HD2  . HIS   A  1 189 ? 22.366 -2.679  6.168   0.00 57.51  ? 215  HIS   A HD2  1 
ATOM   2691  H HE1  . HIS   A  1 189 ? 21.967 -6.757  7.219   0.00 60.44  ? 215  HIS   A HE1  1 
ATOM   2692  H HE2  . HIS   A  1 189 ? 23.326 -4.641  7.614   0.00 59.91  ? 215  HIS   A HE2  1 
ATOM   2693  N N    . VAL   A  1 190 ? 18.563 -3.481  1.735   1.00 31.33  ? 216  VAL   A N    1 
ATOM   2694  C CA   . VAL   A  1 190 ? 17.527 -2.798  0.955   1.00 31.68  ? 216  VAL   A CA   1 
ATOM   2695  C C    . VAL   A  1 190 ? 16.839 -1.807  1.911   1.00 32.41  ? 216  VAL   A C    1 
ATOM   2696  O O    . VAL   A  1 190 ? 16.493 -2.219  3.022   1.00 31.98  ? 216  VAL   A O    1 
ATOM   2697  C CB   . VAL   A  1 190 ? 16.486 -3.795  0.384   1.00 32.07  ? 216  VAL   A CB   1 
ATOM   2698  C CG1  . VAL   A  1 190 ? 15.295 -3.058  -0.247  1.00 32.17  ? 216  VAL   A CG1  1 
ATOM   2699  C CG2  . VAL   A  1 190 ? 17.139 -4.745  -0.617  1.00 32.19  ? 216  VAL   A CG2  1 
ATOM   2700  H H    . VAL   A  1 190 ? 18.387 -4.470  1.885   0.00 40.59  ? 216  VAL   A H    1 
ATOM   2701  H HA   . VAL   A  1 190 ? 18.000 -2.292  0.115   0.00 40.44  ? 216  VAL   A HA   1 
ATOM   2702  H HB   . VAL   A  1 190 ? 16.099 -4.398  1.204   0.00 41.72  ? 216  VAL   A HB   1 
ATOM   2703  H HG11 . VAL   A  1 190 ? 14.695 -3.776  -0.804  0.00 41.48  ? 216  VAL   A HG11 1 
ATOM   2704  H HG12 . VAL   A  1 190 ? 14.675 -2.611  0.529   0.00 41.96  ? 216  VAL   A HG12 1 
ATOM   2705  H HG13 . VAL   A  1 190 ? 15.668 -2.290  -0.923  0.00 41.22  ? 216  VAL   A HG13 1 
ATOM   2706  H HG21 . VAL   A  1 190 ? 16.373 -5.364  -1.083  0.00 41.03  ? 216  VAL   A HG21 1 
ATOM   2707  H HG22 . VAL   A  1 190 ? 17.661 -4.162  -1.373  0.00 40.60  ? 216  VAL   A HG22 1 
ATOM   2708  H HG23 . VAL   A  1 190 ? 17.850 -5.379  -0.088  0.00 41.03  ? 216  VAL   A HG23 1 
ATOM   2709  N N    . PRO   A  1 191 ? 16.698 -0.510  1.559   1.00 32.93  ? 217  PRO   A N    1 
ATOM   2710  C CA   . PRO   A  1 191 ? 16.073 0.418   2.509   1.00 33.11  ? 217  PRO   A CA   1 
ATOM   2711  C C    . PRO   A  1 191 ? 14.629 0.039   2.824   1.00 33.51  ? 217  PRO   A C    1 
ATOM   2712  O O    . PRO   A  1 191 ? 13.867 -0.252  1.899   1.00 33.66  ? 217  PRO   A O    1 
ATOM   2713  C CB   . PRO   A  1 191 ? 16.114 1.777   1.801   1.00 33.75  ? 217  PRO   A CB   1 
ATOM   2714  C CG   . PRO   A  1 191 ? 16.912 1.599   0.576   1.00 33.93  ? 217  PRO   A CG   1 
ATOM   2715  C CD   . PRO   A  1 191 ? 17.090 0.158   0.298   1.00 32.26  ? 217  PRO   A CD   1 
ATOM   2716  H HA   . PRO   A  1 191 ? 16.681 0.473   3.410   0.00 43.81  ? 217  PRO   A HA   1 
ATOM   2717  H HB2  . PRO   A  1 191 ? 15.102 2.092   1.551   0.00 44.39  ? 217  PRO   A HB2  1 
ATOM   2718  H HB3  . PRO   A  1 191 ? 16.585 2.507   2.456   0.00 44.41  ? 217  PRO   A HB3  1 
ATOM   2719  H HG2  . PRO   A  1 191 ? 16.393 2.073   -0.255  0.00 43.63  ? 217  PRO   A HG2  1 
ATOM   2720  H HG3  . PRO   A  1 191 ? 17.885 2.068   0.718   0.00 43.63  ? 217  PRO   A HG3  1 
ATOM   2721  H HD2  . PRO   A  1 191 ? 16.440 -0.146  -0.521  0.00 41.34  ? 217  PRO   A HD2  1 
ATOM   2722  H HD3  . PRO   A  1 191 ? 18.139 -0.023  0.068   0.00 41.17  ? 217  PRO   A HD3  1 
ATOM   2723  N N    . PRO   A  1 192 ? 14.219 0.053   4.105   1.00 33.11  ? 218  PRO   A N    1 
ATOM   2724  C CA   . PRO   A  1 192 ? 12.811 -0.230  4.410   1.00 33.05  ? 218  PRO   A CA   1 
ATOM   2725  C C    . PRO   A  1 192 ? 11.905 0.967   4.085   1.00 32.77  ? 218  PRO   A C    1 
ATOM   2726  O O    . PRO   A  1 192 ? 12.382 2.069   3.798   1.00 32.84  ? 218  PRO   A O    1 
ATOM   2727  C CB   . PRO   A  1 192 ? 12.828 -0.540  5.911   1.00 34.23  ? 218  PRO   A CB   1 
ATOM   2728  C CG   . PRO   A  1 192 ? 14.017 0.161   6.445   1.00 34.58  ? 218  PRO   A CG   1 
ATOM   2729  C CD   . PRO   A  1 192 ? 14.993 0.372   5.323   1.00 32.70  ? 218  PRO   A CD   1 
ATOM   2730  H HA   . PRO   A  1 192 ? 12.461 -1.113  3.876   0.00 44.93  ? 218  PRO   A HA   1 
ATOM   2731  H HB2  . PRO   A  1 192 ? 11.919 -0.163  6.377   0.00 47.58  ? 218  PRO   A HB2  1 
ATOM   2732  H HB3  . PRO   A  1 192 ? 12.919 -1.615  6.058   0.00 47.06  ? 218  PRO   A HB3  1 
ATOM   2733  H HG2  . PRO   A  1 192 ? 13.707 1.120   6.856   0.00 47.80  ? 218  PRO   A HG2  1 
ATOM   2734  H HG3  . PRO   A  1 192 ? 14.469 -0.453  7.223   0.00 47.64  ? 218  PRO   A HG3  1 
ATOM   2735  H HD2  . PRO   A  1 192 ? 15.325 1.410   5.299   0.00 44.49  ? 218  PRO   A HD2  1 
ATOM   2736  H HD3  . PRO   A  1 192 ? 15.833 -0.313  5.428   0.00 44.29  ? 218  PRO   A HD3  1 
ATOM   2737  N N    . LYS   A  1 193 ? 10.584 0.742   4.134   1.00 32.31  ? 219  LYS   A N    1 
ATOM   2738  C CA   . LYS   A  1 193 ? 9.563  1.772   3.941   1.00 32.57  ? 219  LYS   A CA   1 
ATOM   2739  C C    . LYS   A  1 193 ? 9.657  2.492   2.599   1.00 31.97  ? 219  LYS   A C    1 
ATOM   2740  O O    . LYS   A  1 193 ? 9.664  3.728   2.533   1.00 31.81  ? 219  LYS   A O    1 
ATOM   2741  C CB   . LYS   A  1 193 ? 9.588  2.770   5.108   1.00 34.52  ? 219  LYS   A CB   1 
ATOM   2742  C CG   . LYS   A  1 193 ? 9.335  2.109   6.444   1.00 38.71  ? 219  LYS   A CG   1 
ATOM   2743  C CD   . LYS   A  1 193 ? 9.561  3.074   7.587   1.00 41.96  ? 219  LYS   A CD   1 
ATOM   2744  C CE   . LYS   A  1 193 ? 9.338  2.399   8.909   1.00 44.48  ? 219  LYS   A CE   1 
ATOM   2745  N NZ   . LYS   A  1 193 ? 9.461  3.359   10.028  1.00 46.38  ? 219  LYS   A NZ   1 
ATOM   2746  H H    . LYS   A  1 193 ? 10.186 -0.174  4.313   0.00 44.99  ? 219  LYS   A H    1 
ATOM   2747  H HA   . LYS   A  1 193 ? 8.590  1.283   3.967   0.00 45.86  ? 219  LYS   A HA   1 
ATOM   2748  H HB2  . LYS   A  1 193 ? 10.562 3.254   5.148   0.00 48.22  ? 219  LYS   A HB2  1 
ATOM   2749  H HB3  . LYS   A  1 193 ? 8.802  3.511   4.967   0.00 48.79  ? 219  LYS   A HB3  1 
ATOM   2750  H HG2  . LYS   A  1 193 ? 8.302  1.767   6.486   0.00 54.38  ? 219  LYS   A HG2  1 
ATOM   2751  H HG3  . LYS   A  1 193 ? 10.015 1.270   6.584   0.00 53.77  ? 219  LYS   A HG3  1 
ATOM   2752  H HD2  . LYS   A  1 193 ? 10.587 3.439   7.555   0.00 58.18  ? 219  LYS   A HD2  1 
ATOM   2753  H HD3  . LYS   A  1 193 ? 8.860  3.903   7.501   0.00 58.81  ? 219  LYS   A HD3  1 
ATOM   2754  H HE2  . LYS   A  1 193 ? 8.335  1.975   8.931   0.00 62.37  ? 219  LYS   A HE2  1 
ATOM   2755  H HE3  . LYS   A  1 193 ? 10.083 1.616   9.045   0.00 61.78  ? 219  LYS   A HE3  1 
ATOM   2756  H HZ1  . LYS   A  1 193 ? 9.310  2.883   10.912  0.00 65.33  ? 219  LYS   A HZ1  1 
ATOM   2757  H HZ2  . LYS   A  1 193 ? 10.387 3.774   10.030  0.00 64.70  ? 219  LYS   A HZ2  1 
ATOM   2758  H HZ3  . LYS   A  1 193 ? 8.770  4.096   9.928   0.00 65.24  ? 219  LYS   A HZ3  1 
ATOM   2759  N N    . LEU   A  1 194 ? 9.670  1.710   1.527   1.00 31.39  ? 220  LEU   A N    1 
ATOM   2760  C CA   . LEU   A  1 194 ? 9.694  2.277   0.184   1.00 31.47  ? 220  LEU   A CA   1 
ATOM   2761  C C    . LEU   A  1 194 ? 8.252  2.496   -0.253  1.00 31.83  ? 220  LEU   A C    1 
ATOM   2762  O O    . LEU   A  1 194 ? 7.367  1.723   0.133   1.00 31.68  ? 220  LEU   A O    1 
ATOM   2763  C CB   . LEU   A  1 194 ? 10.427 1.343   -0.786  1.00 31.18  ? 220  LEU   A CB   1 
ATOM   2764  C CG   . LEU   A  1 194 ? 11.906 1.129   -0.503  1.00 32.80  ? 220  LEU   A CG   1 
ATOM   2765  C CD1  . LEU   A  1 194 ? 12.493 0.125   -1.478  1.00 33.36  ? 220  LEU   A CD1  1 
ATOM   2766  C CD2  . LEU   A  1 194 ? 12.685 2.444   -0.557  1.00 33.24  ? 220  LEU   A CD2  1 
ATOM   2767  H H    . LEU   A  1 194 ? 9.643  0.695   1.554   0.00 43.11  ? 220  LEU   A H    1 
ATOM   2768  H HA   . LEU   A  1 194 ? 10.207 3.236   0.201   0.00 42.82  ? 220  LEU   A HA   1 
ATOM   2769  H HB2  . LEU   A  1 194 ? 9.947  0.366   -0.756  0.00 41.95  ? 220  LEU   A HB2  1 
ATOM   2770  H HB3  . LEU   A  1 194 ? 10.344 1.760   -1.788  0.00 41.61  ? 220  LEU   A HB3  1 
ATOM   2771  H HG   . LEU   A  1 194 ? 12.017 0.718   0.499   0.00 43.65  ? 220  LEU   A HG   1 
ATOM   2772  H HD11 . LEU   A  1 194 ? 13.536 -0.057  -1.221  0.00 43.22  ? 220  LEU   A HD11 1 
ATOM   2773  H HD12 . LEU   A  1 194 ? 11.928 -0.804  -1.412  0.00 43.61  ? 220  LEU   A HD12 1 
ATOM   2774  H HD13 . LEU   A  1 194 ? 12.423 0.531   -2.486  0.00 43.20  ? 220  LEU   A HD13 1 
ATOM   2775  H HD21 . LEU   A  1 194 ? 13.749 2.223   -0.641  0.00 43.40  ? 220  LEU   A HD21 1 
ATOM   2776  H HD22 . LEU   A  1 194 ? 12.354 3.019   -1.420  0.00 43.65  ? 220  LEU   A HD22 1 
ATOM   2777  H HD23 . LEU   A  1 194 ? 12.505 3.004   0.359   0.00 44.21  ? 220  LEU   A HD23 1 
ATOM   2778  N N    . PRO   A  1 195 ? 7.975  3.561   -1.025  1.00 32.43  ? 221  PRO   A N    1 
ATOM   2779  C CA   . PRO   A  1 195 ? 6.583  3.811   -1.432  1.00 33.24  ? 221  PRO   A CA   1 
ATOM   2780  C C    . PRO   A  1 195 ? 6.113  2.796   -2.466  1.00 34.09  ? 221  PRO   A C    1 
ATOM   2781  O O    . PRO   A  1 195 ? 6.868  2.436   -3.378  1.00 34.83  ? 221  PRO   A O    1 
ATOM   2782  C CB   . PRO   A  1 195 ? 6.626  5.227   -2.003  1.00 33.91  ? 221  PRO   A CB   1 
ATOM   2783  C CG   . PRO   A  1 195 ? 8.029  5.395   -2.481  1.00 33.81  ? 221  PRO   A CG   1 
ATOM   2784  C CD   . PRO   A  1 195 ? 8.897  4.575   -1.573  1.00 31.78  ? 221  PRO   A CD   1 
ATOM   2785  H HA   . PRO   A  1 195 ? 5.925  3.801   -0.565  0.00 46.44  ? 221  PRO   A HA   1 
ATOM   2786  H HB2  . PRO   A  1 195 ? 5.922  5.311   -2.829  0.00 46.79  ? 221  PRO   A HB2  1 
ATOM   2787  H HB3  . PRO   A  1 195 ? 6.396  5.947   -1.218  0.00 47.19  ? 221  PRO   A HB3  1 
ATOM   2788  H HG2  . PRO   A  1 195 ? 8.103  5.045   -3.509  0.00 45.52  ? 221  PRO   A HG2  1 
ATOM   2789  H HG3  . PRO   A  1 195 ? 8.307  6.446   -2.419  0.00 46.01  ? 221  PRO   A HG3  1 
ATOM   2790  H HD2  . PRO   A  1 195 ? 9.691  4.094   -2.142  0.00 42.74  ? 221  PRO   A HD2  1 
ATOM   2791  H HD3  . PRO   A  1 195 ? 9.300  5.195   -0.773  0.00 43.50  ? 221  PRO   A HD3  1 
ATOM   2792  N N    . SER   A  1 196 ? 4.863  2.339   -2.321  1.00 33.85  ? 222  SER   A N    1 
ATOM   2793  C CA   . SER   A  1 196 ? 4.257  1.353   -3.215  1.00 34.41  ? 222  SER   A CA   1 
ATOM   2794  C C    . SER   A  1 196 ? 4.029  1.872   -4.650  1.00 33.68  ? 222  SER   A C    1 
ATOM   2795  O O    . SER   A  1 196 ? 3.668  1.088   -5.526  1.00 34.31  ? 222  SER   A O    1 
ATOM   2796  C CB   . SER   A  1 196 ? 2.944  0.852   -2.625  1.00 36.98  ? 222  SER   A CB   1 
ATOM   2797  O OG   . SER   A  1 196 ? 2.114  1.950   -2.289  1.00 40.87  ? 222  SER   A OG   1 
ATOM   2798  H H    . SER   A  1 196 ? 4.239  2.646   -1.582  0.00 47.43  ? 222  SER   A H    1 
ATOM   2799  H HA   . SER   A  1 196 ? 4.926  0.497   -3.286  0.00 47.07  ? 222  SER   A HA   1 
ATOM   2800  H HB2  . SER   A  1 196 ? 2.431  0.223   -3.351  0.00 51.27  ? 222  SER   A HB2  1 
ATOM   2801  H HB3  . SER   A  1 196 ? 3.159  0.279   -1.724  0.00 51.38  ? 222  SER   A HB3  1 
ATOM   2802  H HG   . SER   A  1 196 ? 1.263  1.623   -1.895  0.00 57.06  ? 222  SER   A HG   1 
ATOM   2803  N N    . SER   A  1 197 ? 4.240  3.173   -4.897  1.00 32.09  ? 223  SER   A N    1 
ATOM   2804  C CA   . SER   A  1 197 ? 4.153  3.738   -6.243  1.00 31.02  ? 223  SER   A CA   1 
ATOM   2805  C C    . SER   A  1 197 ? 5.369  3.321   -7.105  1.00 30.23  ? 223  SER   A C    1 
ATOM   2806  O O    . SER   A  1 197 ? 5.326  3.501   -8.323  1.00 30.43  ? 223  SER   A O    1 
ATOM   2807  C CB   . SER   A  1 197 ? 4.106  5.262   -6.164  1.00 31.12  ? 223  SER   A CB   1 
ATOM   2808  O OG   . SER   A  1 197 ? 5.180  5.757   -5.376  1.00 30.99  ? 223  SER   A OG   1 
ATOM   2809  H H    . SER   A  1 197 ? 4.464  3.866   -4.189  0.00 44.64  ? 223  SER   A H    1 
ATOM   2810  H HA   . SER   A  1 197 ? 3.242  3.396   -6.731  0.00 43.22  ? 223  SER   A HA   1 
ATOM   2811  H HB2  . SER   A  1 197 ? 4.175  5.674   -7.170  0.00 43.16  ? 223  SER   A HB2  1 
ATOM   2812  H HB3  . SER   A  1 197 ? 3.166  5.564   -5.704  0.00 43.97  ? 223  SER   A HB3  1 
ATOM   2813  H HG   . SER   A  1 197 ? 5.974  5.940   -5.944  0.00 42.52  ? 223  SER   A HG   1 
ATOM   2814  N N    . LEU   A  1 198 ? 6.467  2.816   -6.495  1.00 29.21  ? 224  LEU   A N    1 
ATOM   2815  C CA   . LEU   A  1 198 ? 7.666  2.476   -7.252  1.00 28.88  ? 224  LEU   A CA   1 
ATOM   2816  C C    . LEU   A  1 198 ? 7.422  1.528   -8.421  1.00 27.76  ? 224  LEU   A C    1 
ATOM   2817  O O    . LEU   A  1 198 ? 6.703  0.538   -8.288  1.00 26.93  ? 224  LEU   A O    1 
ATOM   2818  C CB   . LEU   A  1 198 ? 8.752  1.859   -6.356  1.00 29.46  ? 224  LEU   A CB   1 
ATOM   2819  C CG   . LEU   A  1 198 ? 9.605  2.817   -5.528  1.00 31.53  ? 224  LEU   A CG   1 
ATOM   2820  C CD1  . LEU   A  1 198 ? 10.573 2.042   -4.636  1.00 31.95  ? 224  LEU   A CD1  1 
ATOM   2821  C CD2  . LEU   A  1 198 ? 10.379 3.788   -6.424  1.00 31.67  ? 224  LEU   A CD2  1 
ATOM   2822  H H    . LEU   A  1 198 ? 6.559  2.658   -5.496  0.00 39.75  ? 224  LEU   A H    1 
ATOM   2823  H HA   . LEU   A  1 198 ? 8.029  3.415   -7.667  0.00 38.29  ? 224  LEU   A HA   1 
ATOM   2824  H HB2  . LEU   A  1 198 ? 8.276  1.165   -5.664  0.00 39.15  ? 224  LEU   A HB2  1 
ATOM   2825  H HB3  . LEU   A  1 198 ? 9.432  1.301   -6.997  0.00 38.37  ? 224  LEU   A HB3  1 
ATOM   2826  H HG   . LEU   A  1 198 ? 8.951  3.402   -4.885  0.00 41.83  ? 224  LEU   A HG   1 
ATOM   2827  H HD11 . LEU   A  1 198 ? 11.085 2.741   -3.975  0.00 41.72  ? 224  LEU   A HD11 1 
ATOM   2828  H HD12 . LEU   A  1 198 ? 10.010 1.317   -4.050  0.00 41.93  ? 224  LEU   A HD12 1 
ATOM   2829  H HD13 . LEU   A  1 198 ? 11.298 1.528   -5.265  0.00 41.15  ? 224  LEU   A HD13 1 
ATOM   2830  H HD21 . LEU   A  1 198 ? 11.241 4.158   -5.871  0.00 40.98  ? 224  LEU   A HD21 1 
ATOM   2831  H HD22 . LEU   A  1 198 ? 10.707 3.269   -7.324  0.00 40.67  ? 224  LEU   A HD22 1 
ATOM   2832  H HD23 . LEU   A  1 198 ? 9.735  4.625   -6.688  0.00 41.38  ? 224  LEU   A HD23 1 
ATOM   2833  N N    . ARG   A  1 199 ? 8.051  1.855   -9.555  1.00 27.36  ? 225  ARG   A N    1 
ATOM   2834  C CA   . ARG   A  1 199 ? 8.032  1.097   -10.794 1.00 27.72  ? 225  ARG   A CA   1 
ATOM   2835  C C    . ARG   A  1 199 ? 9.442  0.575   -11.099 1.00 25.93  ? 225  ARG   A C    1 
ATOM   2836  O O    . ARG   A  1 199 ? 9.573  -0.548  -11.557 1.00 25.86  ? 225  ARG   A O    1 
ATOM   2837  C CB   . ARG   A  1 199 ? 7.489  1.966   -11.950 1.00 31.48  ? 225  ARG   A CB   1 
ATOM   2838  C CG   . ARG   A  1 199 ? 5.983  2.200   -11.822 1.00 37.28  ? 225  ARG   A CG   1 
ATOM   2839  C CD   . ARG   A  1 199 ? 5.415  3.112   -12.878 1.00 44.08  ? 225  ARG   A CD   1 
ATOM   2840  N NE   . ARG   A  1 199 ? 3.954  3.106   -12.831 1.00 49.63  ? 225  ARG   A NE   1 
ATOM   2841  C CZ   . ARG   A  1 199 ? 3.170  3.894   -13.561 1.00 54.46  ? 225  ARG   A CZ   1 
ATOM   2842  N NH1  . ARG   A  1 199 ? 3.700  4.771   -14.412 1.00 55.56  ? 225  ARG   A NH1  1 
ATOM   2843  N NH2  . ARG   A  1 199 ? 1.852  3.815   -13.449 1.00 55.34  ? 225  ARG   A NH2  1 
ATOM   2844  H H    . ARG   A  1 199 ? 8.603  2.702   -9.648  0.00 35.70  ? 225  ARG   A H    1 
ATOM   2845  H HA   . ARG   A  1 199 ? 7.368  0.242   -10.705 0.00 36.21  ? 225  ARG   A HA   1 
ATOM   2846  H HB2  . ARG   A  1 199 ? 7.985  2.935   -11.937 0.00 40.48  ? 225  ARG   A HB2  1 
ATOM   2847  H HB3  . ARG   A  1 199 ? 7.674  1.461   -12.896 0.00 40.30  ? 225  ARG   A HB3  1 
ATOM   2848  H HG2  . ARG   A  1 199 ? 5.478  1.239   -11.902 0.00 48.38  ? 225  ARG   A HG2  1 
ATOM   2849  H HG3  . ARG   A  1 199 ? 5.775  2.643   -10.849 0.00 48.58  ? 225  ARG   A HG3  1 
ATOM   2850  H HD2  . ARG   A  1 199 ? 5.760  4.129   -12.701 0.00 56.60  ? 225  ARG   A HD2  1 
ATOM   2851  H HD3  . ARG   A  1 199 ? 5.729  2.770   -13.862 0.00 56.26  ? 225  ARG   A HD3  1 
ATOM   2852  H HE   . ARG   A  1 199 ? 3.511  2.455   -12.190 0.00 64.22  ? 225  ARG   A HE   1 
ATOM   2853  H HH11 . ARG   A  1 199 ? 4.702  4.862   -14.531 0.00 70.71  ? 225  ARG   A HH11 1 
ATOM   2854  H HH12 . ARG   A  1 199 ? 3.088  5.364   -14.964 0.00 71.53  ? 225  ARG   A HH12 1 
ATOM   2855  H HH21 . ARG   A  1 199 ? 1.442  3.154   -12.796 0.00 72.12  ? 225  ARG   A HH21 1 
ATOM   2856  H HH22 . ARG   A  1 199 ? 1.250  4.416   -14.002 0.00 72.22  ? 225  ARG   A HH22 1 
ATOM   2857  N N    . LYS   A  1 200 ? 10.486 1.358   -10.829 1.00 24.61  ? 226  LYS   A N    1 
ATOM   2858  C CA   . LYS   A  1 200 ? 11.862 0.970   -11.114 1.00 24.38  ? 226  LYS   A CA   1 
ATOM   2859  C C    . LYS   A  1 200 ? 12.732 1.223   -9.905  1.00 23.94  ? 226  LYS   A C    1 
ATOM   2860  O O    . LYS   A  1 200 ? 12.850 2.366   -9.466  1.00 23.82  ? 226  LYS   A O    1 
ATOM   2861  C CB   . LYS   A  1 200 ? 12.398 1.747   -12.331 1.00 24.66  ? 226  LYS   A CB   1 
ATOM   2862  C CG   . LYS   A  1 200 ? 11.478 1.638   -13.543 1.00 26.57  ? 226  LYS   A CG   1 
ATOM   2863  C CD   . LYS   A  1 200 ? 12.175 1.945   -14.868 1.00 28.80  ? 226  LYS   A CD   1 
ATOM   2864  C CE   . LYS   A  1 200 ? 11.212 1.724   -16.010 1.00 31.86  ? 226  LYS   A CE   1 
ATOM   2865  N NZ   . LYS   A  1 200 ? 11.872 1.778   -17.339 1.00 33.99  ? 226  LYS   A NZ   1 
ATOM   2866  H H    . LYS   A  1 200 ? 10.418 2.285   -10.421 0.00 31.49  ? 226  LYS   A H    1 
ATOM   2867  H HA   . LYS   A  1 200 ? 11.915 -0.090  -11.350 0.00 30.29  ? 226  LYS   A HA   1 
ATOM   2868  H HB2  . LYS   A  1 200 ? 12.487 2.801   -12.076 0.00 30.52  ? 226  LYS   A HB2  1 
ATOM   2869  H HB3  . LYS   A  1 200 ? 13.371 1.347   -12.609 0.00 29.98  ? 226  LYS   A HB3  1 
ATOM   2870  H HG2  . LYS   A  1 200 ? 11.089 0.622   -13.590 0.00 32.84  ? 226  LYS   A HG2  1 
ATOM   2871  H HG3  . LYS   A  1 200 ? 10.657 2.343   -13.425 0.00 33.18  ? 226  LYS   A HG3  1 
ATOM   2872  H HD2  . LYS   A  1 200 ? 12.493 2.986   -14.881 0.00 35.00  ? 226  LYS   A HD2  1 
ATOM   2873  H HD3  . LYS   A  1 200 ? 13.028 1.282   -14.993 0.00 34.64  ? 226  LYS   A HD3  1 
ATOM   2874  H HE2  . LYS   A  1 200 ? 10.751 0.743   -15.904 0.00 38.96  ? 226  LYS   A HE2  1 
ATOM   2875  H HE3  . LYS   A  1 200 ? 10.445 2.497   -15.986 0.00 39.23  ? 226  LYS   A HE3  1 
ATOM   2876  H HZ1  . LYS   A  1 200 ? 11.190 1.615   -18.072 0.00 41.14  ? 226  LYS   A HZ1  1 
ATOM   2877  H HZ2  . LYS   A  1 200 ? 12.296 2.689   -17.480 0.00 40.90  ? 226  LYS   A HZ2  1 
ATOM   2878  H HZ3  . LYS   A  1 200 ? 12.595 1.068   -17.394 0.00 40.66  ? 226  LYS   A HZ3  1 
ATOM   2879  N N    . LEU   A  1 201 ? 13.354 0.161   -9.379  1.00 23.62  ? 227  LEU   A N    1 
ATOM   2880  C CA   . LEU   A  1 201 ? 14.233 0.253   -8.216  1.00 23.23  ? 227  LEU   A CA   1 
ATOM   2881  C C    . LEU   A  1 201 ? 15.621 -0.223  -8.600  1.00 22.23  ? 227  LEU   A C    1 
ATOM   2882  O O    . LEU   A  1 201 ? 15.792 -1.405  -8.926  1.00 22.89  ? 227  LEU   A O    1 
ATOM   2883  C CB   . LEU   A  1 201 ? 13.657 -0.588  -7.064  1.00 23.41  ? 227  LEU   A CB   1 
ATOM   2884  C CG   . LEU   A  1 201 ? 14.437 -0.630  -5.757  1.00 24.64  ? 227  LEU   A CG   1 
ATOM   2885  C CD1  . LEU   A  1 201 ? 14.706 0.778   -5.212  1.00 24.51  ? 227  LEU   A CD1  1 
ATOM   2886  C CD2  . LEU   A  1 201 ? 13.680 -1.480  -4.711  1.00 25.26  ? 227  LEU   A CD2  1 
ATOM   2887  H H    . LEU   A  1 201 ? 13.273 -0.786  -9.735  0.00 29.23  ? 227  LEU   A H    1 
ATOM   2888  H HA   . LEU   A  1 201 ? 14.305 1.286   -7.881  0.00 29.00  ? 227  LEU   A HA   1 
ATOM   2889  H HB2  . LEU   A  1 201 ? 12.673 -0.190  -6.824  0.00 29.90  ? 227  LEU   A HB2  1 
ATOM   2890  H HB3  . LEU   A  1 201 ? 13.554 -1.615  -7.410  0.00 29.41  ? 227  LEU   A HB3  1 
ATOM   2891  H HG   . LEU   A  1 201 ? 15.396 -1.115  -5.929  0.00 30.75  ? 227  LEU   A HG   1 
ATOM   2892  H HD11 . LEU   A  1 201 ? 15.093 0.698   -4.197  0.00 31.27  ? 227  LEU   A HD11 1 
ATOM   2893  H HD12 . LEU   A  1 201 ? 15.444 1.270   -5.844  0.00 30.75  ? 227  LEU   A HD12 1 
ATOM   2894  H HD13 . LEU   A  1 201 ? 13.776 1.344   -5.215  0.00 31.42  ? 227  LEU   A HD13 1 
ATOM   2895  H HD21 . LEU   A  1 201 ? 14.242 -1.480  -3.778  0.00 32.43  ? 227  LEU   A HD21 1 
ATOM   2896  H HD22 . LEU   A  1 201 ? 12.694 -1.048  -4.552  0.00 32.69  ? 227  LEU   A HD22 1 
ATOM   2897  H HD23 . LEU   A  1 201 ? 13.585 -2.497  -5.087  0.00 32.22  ? 227  LEU   A HD23 1 
ATOM   2898  N N    . PHE   A  1 202 ? 16.614 0.693   -8.603  1.00 20.79  ? 228  PHE   A N    1 
ATOM   2899  C CA   . PHE   A  1 202 ? 17.987 0.329   -8.942  1.00 20.47  ? 228  PHE   A CA   1 
ATOM   2900  C C    . PHE   A  1 202 ? 18.878 0.266   -7.704  1.00 20.86  ? 228  PHE   A C    1 
ATOM   2901  O O    . PHE   A  1 202 ? 19.118 1.288   -7.063  1.00 20.84  ? 228  PHE   A O    1 
ATOM   2902  C CB   . PHE   A  1 202 ? 18.604 1.235   -10.035 1.00 20.00  ? 228  PHE   A CB   1 
ATOM   2903  C CG   . PHE   A  1 202 ? 17.812 1.345   -11.319 1.00 21.19  ? 228  PHE   A CG   1 
ATOM   2904  C CD1  . PHE   A  1 202 ? 16.697 2.161   -11.397 1.00 22.13  ? 228  PHE   A CD1  1 
ATOM   2905  C CD2  . PHE   A  1 202 ? 18.253 0.727   -12.480 1.00 21.63  ? 228  PHE   A CD2  1 
ATOM   2906  C CE1  . PHE   A  1 202 ? 16.028 2.342   -12.606 1.00 22.82  ? 228  PHE   A CE1  1 
ATOM   2907  C CE2  . PHE   A  1 202 ? 17.569 0.897   -13.682 1.00 22.45  ? 228  PHE   A CE2  1 
ATOM   2908  C CZ   . PHE   A  1 202 ? 16.453 1.689   -13.734 1.00 22.39  ? 228  PHE   A CZ   1 
ATOM   2909  H H    . PHE   A  1 202 ? 16.497 1.677   -8.381  0.00 25.34  ? 228  PHE   A H    1 
ATOM   2910  H HA   . PHE   A  1 202 ? 17.972 -0.668  -9.369  0.00 24.20  ? 228  PHE   A HA   1 
ATOM   2911  H HB2  . PHE   A  1 202 ? 18.794 2.239   -9.668  0.00 23.54  ? 228  PHE   A HB2  1 
ATOM   2912  H HB3  . PHE   A  1 202 ? 19.564 0.795   -10.302 0.00 23.11  ? 228  PHE   A HB3  1 
ATOM   2913  H HD1  . PHE   A  1 202 ? 16.362 2.687   -10.518 0.00 26.57  ? 228  PHE   A HD1  1 
ATOM   2914  H HD2  . PHE   A  1 202 ? 19.129 0.103   -12.458 0.00 24.65  ? 228  PHE   A HD2  1 
ATOM   2915  H HE1  . PHE   A  1 202 ? 15.142 2.951   -12.646 0.00 27.34  ? 228  PHE   A HE1  1 
ATOM   2916  H HE2  . PHE   A  1 202 ? 17.901 0.386   -14.569 0.00 25.55  ? 228  PHE   A HE2  1 
ATOM   2917  H HZ   . PHE   A  1 202 ? 15.915 1.804   -14.661 0.00 26.11  ? 228  PHE   A HZ   1 
ATOM   2918  N N    . LEU   A  1 203 ? 19.410 -0.933  -7.402  1.00 20.61  ? 229  LEU   A N    1 
ATOM   2919  C CA   . LEU   A  1 203 ? 20.272 -1.191  -6.253  1.00 21.16  ? 229  LEU   A CA   1 
ATOM   2920  C C    . LEU   A  1 203 ? 21.504 -1.995  -6.684  1.00 21.73  ? 229  LEU   A C    1 
ATOM   2921  O O    . LEU   A  1 203 ? 21.949 -2.892  -5.968  1.00 21.65  ? 229  LEU   A O    1 
ATOM   2922  C CB   . LEU   A  1 203 ? 19.471 -1.981  -5.206  1.00 21.38  ? 229  LEU   A CB   1 
ATOM   2923  C CG   . LEU   A  1 203 ? 18.231 -1.301  -4.661  1.00 22.98  ? 229  LEU   A CG   1 
ATOM   2924  C CD1  . LEU   A  1 203 ? 17.335 -2.312  -3.962  1.00 23.37  ? 229  LEU   A CD1  1 
ATOM   2925  C CD2  . LEU   A  1 203 ? 18.608 -0.166  -3.733  1.00 23.75  ? 229  LEU   A CD2  1 
ATOM   2926  H H    . LEU   A  1 203 ? 19.255 -1.769  -7.954  0.00 24.40  ? 229  LEU   A H    1 
ATOM   2927  H HA   . LEU   A  1 203 ? 20.631 -0.263  -5.811  0.00 25.42  ? 229  LEU   A HA   1 
ATOM   2928  H HB2  . LEU   A  1 203 ? 19.143 -2.903  -5.681  0.00 25.96  ? 229  LEU   A HB2  1 
ATOM   2929  H HB3  . LEU   A  1 203 ? 20.114 -2.208  -4.357  0.00 26.16  ? 229  LEU   A HB3  1 
ATOM   2930  H HG   . LEU   A  1 203 ? 17.656 -0.874  -5.481  0.00 28.31  ? 229  LEU   A HG   1 
ATOM   2931  H HD11 . LEU   A  1 203 ? 16.530 -1.788  -3.447  0.00 29.63  ? 229  LEU   A HD11 1 
ATOM   2932  H HD12 . LEU   A  1 203 ? 16.918 -2.990  -4.705  0.00 29.13  ? 229  LEU   A HD12 1 
ATOM   2933  H HD13 . LEU   A  1 203 ? 17.941 -2.866  -3.248  0.00 29.34  ? 229  LEU   A HD13 1 
ATOM   2934  H HD21 . LEU   A  1 203 ? 17.702 0.253   -3.295  0.00 29.93  ? 229  LEU   A HD21 1 
ATOM   2935  H HD22 . LEU   A  1 203 ? 19.265 -0.537  -2.948  0.00 29.67  ? 229  LEU   A HD22 1 
ATOM   2936  H HD23 . LEU   A  1 203 ? 19.113 0.595   -4.322  0.00 29.32  ? 229  LEU   A HD23 1 
ATOM   2937  N N    . SER   A  1 204 ? 22.081 -1.650  -7.849  1.00 21.37  ? 230  SER   A N    1 
ATOM   2938  C CA   . SER   A  1 204 ? 23.255 -2.347  -8.342  1.00 20.96  ? 230  SER   A CA   1 
ATOM   2939  C C    . SER   A  1 204 ? 24.499 -1.935  -7.562  1.00 20.98  ? 230  SER   A C    1 
ATOM   2940  O O    . SER   A  1 204 ? 24.629 -0.774  -7.245  1.00 22.02  ? 230  SER   A O    1 
ATOM   2941  C CB   . SER   A  1 204 ? 23.473 -2.051  -9.829  1.00 21.38  ? 230  SER   A CB   1 
ATOM   2942  O OG   . SER   A  1 204 ? 24.669 -2.669  -10.277 1.00 23.04  ? 230  SER   A OG   1 
ATOM   2943  H H    . SER   A  1 204 ? 21.772 -0.892  -8.448  0.00 24.69  ? 230  SER   A H    1 
ATOM   2944  H HA   . SER   A  1 204 ? 23.115 -3.422  -8.233  0.00 24.03  ? 230  SER   A HA   1 
ATOM   2945  H HB2  . SER   A  1 204 ? 22.634 -2.450  -10.396 0.00 24.05  ? 230  SER   A HB2  1 
ATOM   2946  H HB3  . SER   A  1 204 ? 23.549 -0.976  -9.986  0.00 24.01  ? 230  SER   A HB3  1 
ATOM   2947  H HG   . SER   A  1 204 ? 24.649 -3.637  -10.060 0.00 25.84  ? 230  SER   A HG   1 
ATOM   2948  N N    . ASN   A  1 205 ? 25.426 -2.863  -7.269  1.00 19.99  ? 231  ASN   A N    1 
ATOM   2949  C CA   . ASN   A  1 205 ? 26.701 -2.541  -6.611  1.00 20.24  ? 231  ASN   A CA   1 
ATOM   2950  C C    . ASN   A  1 205 ? 26.500 -1.740  -5.319  1.00 21.20  ? 231  ASN   A C    1 
ATOM   2951  O O    . ASN   A  1 205 ? 27.073 -0.660  -5.152  1.00 21.05  ? 231  ASN   A O    1 
ATOM   2952  C CB   . ASN   A  1 205 ? 27.611 -1.781  -7.601  1.00 19.85  ? 231  ASN   A CB   1 
ATOM   2953  C CG   . ASN   A  1 205 ? 28.189 -2.652  -8.675  1.00 20.80  ? 231  ASN   A CG   1 
ATOM   2954  O OD1  . ASN   A  1 205 ? 29.378 -2.936  -8.657  1.00 22.71  ? 231  ASN   A OD1  1 
ATOM   2955  N ND2  . ASN   A  1 205 ? 27.377 -3.072  -9.642  1.00 19.15  ? 231  ASN   A ND2  1 
ATOM   2956  H H    . ASN   A  1 205 ? 25.322 -3.852  -7.475  0.00 22.79  ? 231  ASN   A H    1 
ATOM   2957  H HA   . ASN   A  1 205 ? 27.204 -3.469  -6.345  0.00 23.22  ? 231  ASN   A HA   1 
ATOM   2958  H HB2  . ASN   A  1 205 ? 27.053 -0.978  -8.080  0.00 22.24  ? 231  ASN   A HB2  1 
ATOM   2959  H HB3  . ASN   A  1 205 ? 28.462 -1.367  -7.061  0.00 22.42  ? 231  ASN   A HB3  1 
ATOM   2960  H HD21 . ASN   A  1 205 ? 27.734 -3.663  -10.386 0.00 20.75  ? 231  ASN   A HD21 1 
ATOM   2961  H HD22 . ASN   A  1 205 ? 26.401 -2.793  -9.641  0.00 21.05  ? 231  ASN   A HD22 1 
ATOM   2962  N N    . THR   A  1 206 ? 25.631 -2.263  -4.440  1.00 21.31  ? 232  THR   A N    1 
ATOM   2963  C CA   . THR   A  1 206 ? 25.279 -1.631  -3.169  1.00 22.55  ? 232  THR   A CA   1 
ATOM   2964  C C    . THR   A  1 206 ? 25.683 -2.434  -1.937  1.00 23.94  ? 232  THR   A C    1 
ATOM   2965  O O    . THR   A  1 206 ? 25.283 -2.053  -0.832  1.00 24.45  ? 232  THR   A O    1 
ATOM   2966  C CB   . THR   A  1 206 ? 23.770 -1.343  -3.132  1.00 24.21  ? 232  THR   A CB   1 
ATOM   2967  O OG1  . THR   A  1 206 ? 23.051 -2.557  -3.369  1.00 24.68  ? 232  THR   A OG1  1 
ATOM   2968  C CG2  . THR   A  1 206 ? 23.358 -0.255  -4.121  1.00 24.93  ? 232  THR   A CG2  1 
ATOM   2969  H H    . THR   A  1 206 ? 25.155 -3.148  -4.584  0.00 25.25  ? 232  THR   A H    1 
ATOM   2970  H HA   . THR   A  1 206 ? 25.793 -0.675  -3.082  0.00 27.17  ? 232  THR   A HA   1 
ATOM   2971  H HB   . THR   A  1 206 ? 23.492 -0.990  -2.141  0.00 29.75  ? 232  THR   A HB   1 
ATOM   2972  H HG1  . THR   A  1 206 ? 23.025 -2.774  -4.338  0.00 29.63  ? 232  THR   A HG1  1 
ATOM   2973  H HG21 . THR   A  1 206 ? 22.286 -0.078  -4.051  0.00 30.20  ? 232  THR   A HG21 1 
ATOM   2974  H HG22 . THR   A  1 206 ? 23.887 0.670   -3.897  0.00 30.04  ? 232  THR   A HG22 1 
ATOM   2975  H HG23 . THR   A  1 206 ? 23.601 -0.563  -5.137  0.00 29.63  ? 232  THR   A HG23 1 
ATOM   2976  N N    . GLN   A  1 207 ? 26.491 -3.502  -2.098  1.00 24.06  ? 233  GLN   A N    1 
ATOM   2977  C CA   . GLN   A  1 207 ? 26.928 -4.364  -0.997  1.00 26.09  ? 233  GLN   A CA   1 
ATOM   2978  C C    . GLN   A  1 207 ? 25.770 -5.003  -0.221  1.00 26.76  ? 233  GLN   A C    1 
ATOM   2979  O O    . GLN   A  1 207 ? 25.900 -5.227  0.980   1.00 27.22  ? 233  GLN   A O    1 
ATOM   2980  C CB   . GLN   A  1 207 ? 27.887 -3.626  -0.056  1.00 29.13  ? 233  GLN   A CB   1 
ATOM   2981  C CG   . GLN   A  1 207 ? 29.121 -3.084  -0.772  1.00 34.57  ? 233  GLN   A CG   1 
ATOM   2982  C CD   . GLN   A  1 207 ? 30.053 -2.336  0.154   1.00 41.73  ? 233  GLN   A CD   1 
ATOM   2983  O OE1  . GLN   A  1 207 ? 29.681 -1.902  1.249   1.00 44.01  ? 233  GLN   A OE1  1 
ATOM   2984  N NE2  . GLN   A  1 207 ? 31.290 -2.154  -0.277  1.00 44.38  ? 233  GLN   A NE2  1 
ATOM   2985  H H    . GLN   A  1 207 ? 26.876 -3.801  -2.988  0.00 28.93  ? 233  GLN   A H    1 
ATOM   2986  H HA   . GLN   A  1 207 ? 27.494 -5.185  -1.432  0.00 31.92  ? 233  GLN   A HA   1 
ATOM   2987  H HB2  . GLN   A  1 207 ? 27.359 -2.795  0.408   0.00 36.20  ? 233  GLN   A HB2  1 
ATOM   2988  H HB3  . GLN   A  1 207 ? 28.246 -4.311  0.710   0.00 36.31  ? 233  GLN   A HB3  1 
ATOM   2989  H HG2  . GLN   A  1 207 ? 29.670 -3.915  -1.210  0.00 42.05  ? 233  GLN   A HG2  1 
ATOM   2990  H HG3  . GLN   A  1 207 ? 28.811 -2.392  -1.553  0.00 41.90  ? 233  GLN   A HG3  1 
ATOM   2991  H HE21 . GLN   A  1 207 ? 31.571 -2.503  -1.188  0.00 53.72  ? 233  GLN   A HE21 1 
ATOM   2992  H HE22 . GLN   A  1 207 ? 31.959 -1.659  0.304   0.00 54.31  ? 233  GLN   A HE22 1 
ATOM   2993  N N    . ILE   A  1 208 ? 24.660 -5.329  -0.907  1.00 26.90  ? 234  ILE   A N    1 
ATOM   2994  C CA   . ILE   A  1 208 ? 23.528 -6.006  -0.268  1.00 28.13  ? 234  ILE   A CA   1 
ATOM   2995  C C    . ILE   A  1 208 ? 23.788 -7.509  -0.452  1.00 29.56  ? 234  ILE   A C    1 
ATOM   2996  O O    . ILE   A  1 208 ? 23.771 -8.001  -1.578  1.00 31.54  ? 234  ILE   A O    1 
ATOM   2997  C CB   . ILE   A  1 208 ? 22.172 -5.559  -0.875  1.00 28.66  ? 234  ILE   A CB   1 
ATOM   2998  C CG1  . ILE   A  1 208 ? 21.997 -4.024  -0.742  1.00 29.31  ? 234  ILE   A CG1  1 
ATOM   2999  C CG2  . ILE   A  1 208 ? 21.013 -6.294  -0.167  1.00 29.47  ? 234  ILE   A CG2  1 
ATOM   3000  C CD1  . ILE   A  1 208 ? 20.680 -3.441  -1.350  1.00 30.56  ? 234  ILE   A CD1  1 
ATOM   3001  H H    . ILE   A  1 208 ? 24.518 -5.154  -1.896  0.00 32.98  ? 234  ILE   A H    1 
ATOM   3002  H HA   . ILE   A  1 208 ? 23.494 -5.777  0.795   0.00 35.58  ? 234  ILE   A HA   1 
ATOM   3003  H HB   . ILE   A  1 208 ? 22.159 -5.823  -1.931  0.00 35.41  ? 234  ILE   A HB   1 
ATOM   3004  H HG12 . ILE   A  1 208 ? 22.009 -3.766  0.316   0.00 36.93  ? 234  ILE   A HG12 1 
ATOM   3005  H HG13 . ILE   A  1 208 ? 22.823 -3.526  -1.248  0.00 36.25  ? 234  ILE   A HG13 1 
ATOM   3006  H HG21 . ILE   A  1 208 ? 20.064 -5.993  -0.606  0.00 37.19  ? 234  ILE   A HG21 1 
ATOM   3007  H HG22 . ILE   A  1 208 ? 21.122 -7.371  -0.288  0.00 37.21  ? 234  ILE   A HG22 1 
ATOM   3008  H HG23 . ILE   A  1 208 ? 21.030 -6.038  0.890   0.00 37.57  ? 234  ILE   A HG23 1 
ATOM   3009  H HD11 . ILE   A  1 208 ? 20.781 -2.359  -1.429  0.00 38.01  ? 234  ILE   A HD11 1 
ATOM   3010  H HD12 . ILE   A  1 208 ? 20.521 -3.875  -2.336  0.00 37.76  ? 234  ILE   A HD12 1 
ATOM   3011  H HD13 . ILE   A  1 208 ? 19.845 -3.683  -0.694  0.00 38.44  ? 234  ILE   A HD13 1 
ATOM   3012  N N    . LYS   A  1 209 ? 24.036 -8.234  0.637   1.00 28.45  ? 235  LYS   A N    1 
ATOM   3013  C CA   . LYS   A  1 209 ? 24.379 -9.651  0.568   1.00 28.61  ? 235  LYS   A CA   1 
ATOM   3014  C C    . LYS   A  1 209 ? 23.174 -10.592 0.712   1.00 28.76  ? 235  LYS   A C    1 
ATOM   3015  O O    . LYS   A  1 209 ? 23.257 -11.756 0.303   1.00 28.32  ? 235  LYS   A O    1 
ATOM   3016  C CB   . LYS   A  1 209 ? 25.410 -9.966  1.667   1.00 30.24  ? 235  LYS   A CB   1 
ATOM   3017  C CG   . LYS   A  1 209 ? 26.669 -9.098  1.587   1.00 35.16  ? 235  LYS   A CG   1 
ATOM   3018  C CD   . LYS   A  1 209 ? 27.586 -9.313  2.779   1.00 40.98  ? 235  LYS   A CD   1 
ATOM   3019  C CE   . LYS   A  1 209 ? 28.701 -8.295  2.850   1.00 46.02  ? 235  LYS   A CE   1 
ATOM   3020  N NZ   . LYS   A  1 209 ? 29.722 -8.497  1.788   1.00 47.95  ? 235  LYS   A NZ   1 
ATOM   3021  H H    . LYS   A  1 209 ? 24.008 -7.871  1.584   0.00 36.35  ? 235  LYS   A H    1 
ATOM   3022  H HA   . LYS   A  1 209 ? 24.861 -9.874  -0.383  0.00 35.95  ? 235  LYS   A HA   1 
ATOM   3023  H HB2  . LYS   A  1 209 ? 24.946 -9.799  2.638   0.00 39.03  ? 235  LYS   A HB2  1 
ATOM   3024  H HB3  . LYS   A  1 209 ? 25.716 -11.007 1.575   0.00 38.72  ? 235  LYS   A HB3  1 
ATOM   3025  H HG2  . LYS   A  1 209 ? 27.221 -9.353  0.684   0.00 43.97  ? 235  LYS   A HG2  1 
ATOM   3026  H HG3  . LYS   A  1 209 ? 26.392 -8.045  1.571   0.00 44.21  ? 235  LYS   A HG3  1 
ATOM   3027  H HD2  . LYS   A  1 209 ? 27.003 -9.234  3.695   0.00 52.16  ? 235  LYS   A HD2  1 
ATOM   3028  H HD3  . LYS   A  1 209 ? 28.037 -10.302 2.706   0.00 51.86  ? 235  LYS   A HD3  1 
ATOM   3029  H HE2  . LYS   A  1 209 ? 28.286 -7.295  2.734   0.00 57.56  ? 235  LYS   A HE2  1 
ATOM   3030  H HE3  . LYS   A  1 209 ? 29.198 -8.381  3.814   0.00 58.10  ? 235  LYS   A HE3  1 
ATOM   3031  H HZ1  . LYS   A  1 209 ? 30.489 -7.844  1.916   0.00 59.56  ? 235  LYS   A HZ1  1 
ATOM   3032  H HZ2  . LYS   A  1 209 ? 30.088 -9.442  1.831   0.00 59.72  ? 235  LYS   A HZ2  1 
ATOM   3033  H HZ3  . LYS   A  1 209 ? 29.313 -8.346  0.872   0.00 59.21  ? 235  LYS   A HZ3  1 
ATOM   3034  N N    . TYR   A  1 210 ? 22.084 -10.111 1.324   1.00 29.04  ? 236  TYR   A N    1 
ATOM   3035  C CA   . TYR   A  1 210 ? 20.902 -10.922 1.580   1.00 29.63  ? 236  TYR   A CA   1 
ATOM   3036  C C    . TYR   A  1 210 ? 19.633 -10.173 1.198   1.00 28.33  ? 236  TYR   A C    1 
ATOM   3037  O O    . TYR   A  1 210 ? 19.510 -8.981  1.476   1.00 28.31  ? 236  TYR   A O    1 
ATOM   3038  C CB   . TYR   A  1 210 ? 20.877 -11.297 3.077   1.00 31.38  ? 236  TYR   A CB   1 
ATOM   3039  C CG   . TYR   A  1 210 ? 19.609 -11.997 3.515   1.00 34.10  ? 236  TYR   A CG   1 
ATOM   3040  C CD1  . TYR   A  1 210 ? 19.273 -13.246 3.014   1.00 35.92  ? 236  TYR   A CD1  1 
ATOM   3041  C CD2  . TYR   A  1 210 ? 18.803 -11.461 4.510   1.00 35.49  ? 236  TYR   A CD2  1 
ATOM   3042  C CE1  . TYR   A  1 210 ? 18.104 -13.889 3.400   1.00 37.00  ? 236  TYR   A CE1  1 
ATOM   3043  C CE2  . TYR   A  1 210 ? 17.666 -12.126 4.954   1.00 36.99  ? 236  TYR   A CE2  1 
ATOM   3044  C CZ   . TYR   A  1 210 ? 17.326 -13.349 4.404   1.00 38.45  ? 236  TYR   A CZ   1 
ATOM   3045  O OH   . TYR   A  1 210 ? 16.219 -14.041 4.834   1.00 41.24  ? 236  TYR   A OH   1 
ATOM   3046  H H    . TYR   A  1 210 ? 21.981 -9.160  1.663   0.00 37.45  ? 236  TYR   A H    1 
ATOM   3047  H HA   . TYR   A  1 210 ? 20.938 -11.844 1.002   0.00 38.40  ? 236  TYR   A HA   1 
ATOM   3048  H HB2  . TYR   A  1 210 ? 21.711 -11.968 3.278   0.00 41.29  ? 236  TYR   A HB2  1 
ATOM   3049  H HB3  . TYR   A  1 210 ? 20.989 -10.388 3.665   0.00 41.31  ? 236  TYR   A HB3  1 
ATOM   3050  H HD1  . TYR   A  1 210 ? 19.877 -13.679 2.234   0.00 46.89  ? 236  TYR   A HD1  1 
ATOM   3051  H HD2  . TYR   A  1 210 ? 19.059 -10.512 4.951   0.00 47.07  ? 236  TYR   A HD2  1 
ATOM   3052  H HE1  . TYR   A  1 210 ? 17.865 -14.858 2.994   0.00 49.04  ? 236  TYR   A HE1  1 
ATOM   3053  H HE2  . TYR   A  1 210 ? 17.051 -11.678 5.718   0.00 49.70  ? 236  TYR   A HE2  1 
ATOM   3054  H HH   . TYR   A  1 210 ? 15.764 -13.556 5.572   0.00 55.30  ? 236  TYR   A HH   1 
ATOM   3055  N N    . ILE   A  1 211 ? 18.690 -10.878 0.554   1.00 27.36  ? 237  ILE   A N    1 
ATOM   3056  C CA   . ILE   A  1 211 ? 17.389 -10.332 0.201   1.00 27.46  ? 237  ILE   A CA   1 
ATOM   3057  C C    . ILE   A  1 211 ? 16.374 -11.143 0.993   1.00 27.66  ? 237  ILE   A C    1 
ATOM   3058  O O    . ILE   A  1 211 ? 16.223 -12.343 0.770   1.00 27.52  ? 237  ILE   A O    1 
ATOM   3059  C CB   . ILE   A  1 211 ? 17.097 -10.391 -1.318  1.00 28.03  ? 237  ILE   A CB   1 
ATOM   3060  C CG1  . ILE   A  1 211 ? 18.229 -9.724  -2.148  1.00 28.76  ? 237  ILE   A CG1  1 
ATOM   3061  C CG2  . ILE   A  1 211 ? 15.744 -9.764  -1.623  1.00 28.24  ? 237  ILE   A CG2  1 
ATOM   3062  C CD1  . ILE   A  1 211 ? 18.426 -8.207  -1.915  1.00 30.07  ? 237  ILE   A CD1  1 
ATOM   3063  H H    . ILE   A  1 211 ? 18.801 -11.844 0.263   0.00 35.77  ? 237  ILE   A H    1 
ATOM   3064  H HA   . ILE   A  1 211 ? 17.311 -9.293  0.514   0.00 35.95  ? 237  ILE   A HA   1 
ATOM   3065  H HB   . ILE   A  1 211 ? 17.028 -11.430 -1.627  0.00 36.24  ? 237  ILE   A HB   1 
ATOM   3066  H HG12 . ILE   A  1 211 ? 19.176 -10.218 -1.931  0.00 36.42  ? 237  ILE   A HG12 1 
ATOM   3067  H HG13 . ILE   A  1 211 ? 17.990 -9.856  -3.202  0.00 36.21  ? 237  ILE   A HG13 1 
ATOM   3068  H HG21 . ILE   A  1 211 ? 15.614 -9.762  -2.704  0.00 36.28  ? 237  ILE   A HG21 1 
ATOM   3069  H HG22 . ILE   A  1 211 ? 14.954 -10.357 -1.165  0.00 36.99  ? 237  ILE   A HG22 1 
ATOM   3070  H HG23 . ILE   A  1 211 ? 15.713 -8.748  -1.233  0.00 36.61  ? 237  ILE   A HG23 1 
ATOM   3071  H HD11 . ILE   A  1 211 ? 19.255 -7.870  -2.536  0.00 37.53  ? 237  ILE   A HD11 1 
ATOM   3072  H HD12 . ILE   A  1 211 ? 17.524 -7.669  -2.203  0.00 37.98  ? 237  ILE   A HD12 1 
ATOM   3073  H HD13 . ILE   A  1 211 ? 18.659 -8.019  -0.869  0.00 38.21  ? 237  ILE   A HD13 1 
ATOM   3074  N N    . SER   A  1 212 ? 15.720 -10.496 1.945   1.00 27.51  ? 238  SER   A N    1 
ATOM   3075  C CA   . SER   A  1 212 ? 14.729 -11.131 2.803   1.00 27.96  ? 238  SER   A CA   1 
ATOM   3076  C C    . SER   A  1 212 ? 13.346 -11.171 2.134   1.00 27.91  ? 238  SER   A C    1 
ATOM   3077  O O    . SER   A  1 212 ? 13.117 -10.547 1.098   1.00 28.07  ? 238  SER   A O    1 
ATOM   3078  C CB   . SER   A  1 212 ? 14.652 -10.385 4.135   1.00 29.55  ? 238  SER   A CB   1 
ATOM   3079  O OG   . SER   A  1 212 ? 13.991 -9.141  3.993   1.00 31.34  ? 238  SER   A OG   1 
ATOM   3080  H H    . SER   A  1 212 ? 15.844 -9.511  2.158   0.00 36.95  ? 238  SER   A H    1 
ATOM   3081  H HA   . SER   A  1 212 ? 15.028 -12.156 3.020   0.00 38.32  ? 238  SER   A HA   1 
ATOM   3082  H HB2  . SER   A  1 212 ? 14.105 -10.996 4.852   0.00 41.00  ? 238  SER   A HB2  1 
ATOM   3083  H HB3  . SER   A  1 212 ? 15.664 -10.207 4.496   0.00 40.40  ? 238  SER   A HB3  1 
ATOM   3084  H HG   . SER   A  1 212 ? 13.949 -8.676  4.869   0.00 42.96  ? 238  SER   A HG   1 
ATOM   3085  N N    . GLU   A  1 213 ? 12.420 -11.896 2.758   1.00 28.10  ? 239  GLU   A N    1 
ATOM   3086  C CA   . GLU   A  1 213 ? 11.045 -11.993 2.281   1.00 28.58  ? 239  GLU   A CA   1 
ATOM   3087  C C    . GLU   A  1 213 ? 10.343 -10.617 2.270   1.00 29.53  ? 239  GLU   A C    1 
ATOM   3088  O O    . GLU   A  1 213 ? 9.568  -10.357 1.357   1.00 30.81  ? 239  GLU   A O    1 
ATOM   3089  C CB   . GLU   A  1 213 ? 10.272 -12.978 3.172   1.00 30.25  ? 239  GLU   A CB   1 
ATOM   3090  C CG   . GLU   A  1 213 ? 8.884  -13.338 2.671   1.00 33.40  ? 239  GLU   A CG   1 
ATOM   3091  C CD   . GLU   A  1 213 ? 8.221  -14.479 3.419   1.00 36.97  ? 239  GLU   A CD   1 
ATOM   3092  O OE1  . GLU   A  1 213 ? 8.897  -15.139 4.242   1.00 38.49  ? 239  GLU   A OE1  1 
ATOM   3093  O OE2  . GLU   A  1 213 ? 7.014  -14.708 3.190   1.00 38.20  ? 239  GLU   A OE2  1 
ATOM   3094  H H    . GLU   A  1 213 ? 12.611 -12.416 3.608   0.00 39.35  ? 239  GLU   A H    1 
ATOM   3095  H HA   . GLU   A  1 213 ? 11.037 -12.394 1.269   0.00 39.55  ? 239  GLU   A HA   1 
ATOM   3096  H HB2  . GLU   A  1 213 ? 10.855 -13.896 3.228   0.00 42.52  ? 239  GLU   A HB2  1 
ATOM   3097  H HB3  . GLU   A  1 213 ? 10.167 -12.543 4.165   0.00 42.86  ? 239  GLU   A HB3  1 
ATOM   3098  H HG2  . GLU   A  1 213 ? 8.220  -12.484 2.777   0.00 46.78  ? 239  GLU   A HG2  1 
ATOM   3099  H HG3  . GLU   A  1 213 ? 8.944  -13.598 1.616   0.00 46.31  ? 239  GLU   A HG3  1 
ATOM   3100  N N    . GLU   A  1 214 ? 10.640 -9.731  3.242   1.00 29.08  ? 240  GLU   A N    1 
ATOM   3101  C CA   . GLU   A  1 214 ? 10.001 -8.412  3.375   1.00 29.88  ? 240  GLU   A CA   1 
ATOM   3102  C C    . GLU   A  1 214 ? 10.663 -7.250  2.635   1.00 29.42  ? 240  GLU   A C    1 
ATOM   3103  O O    . GLU   A  1 214 ? 10.091 -6.168  2.648   1.00 29.45  ? 240  GLU   A O    1 
ATOM   3104  C CB   . GLU   A  1 214 ? 9.932  -8.013  4.871   1.00 33.89  ? 240  GLU   A CB   1 
ATOM   3105  C CG   . GLU   A  1 214 ? 9.250  -9.012  5.789   1.00 42.48  ? 240  GLU   A CG   1 
ATOM   3106  C CD   . GLU   A  1 214 ? 8.224  -8.437  6.754   1.00 54.30  ? 240  GLU   A CD   1 
ATOM   3107  O OE1  . GLU   A  1 214 ? 7.366  -7.635  6.316   1.00 57.00  ? 240  GLU   A OE1  1 
ATOM   3108  O OE2  . GLU   A  1 214 ? 8.264  -8.813  7.949   1.00 57.33  ? 240  GLU   A OE2  1 
ATOM   3109  H H    . GLU   A  1 214 ? 11.323 -9.903  3.973   0.00 40.69  ? 240  GLU   A H    1 
ATOM   3110  H HA   . GLU   A  1 214 ? 8.975  -8.464  3.016   0.00 41.98  ? 240  GLU   A HA   1 
ATOM   3111  H HB2  . GLU   A  1 214 ? 10.952 -7.891  5.234   0.00 46.89  ? 240  GLU   A HB2  1 
ATOM   3112  H HB3  . GLU   A  1 214 ? 9.408  -7.063  4.960   0.00 47.26  ? 240  GLU   A HB3  1 
ATOM   3113  H HG2  . GLU   A  1 214 ? 8.750  -9.775  5.195   0.00 58.00  ? 240  GLU   A HG2  1 
ATOM   3114  H HG3  . GLU   A  1 214 ? 10.022 -9.484  6.396   0.00 58.11  ? 240  GLU   A HG3  1 
ATOM   3115  N N    . ASP   A  1 215 ? 11.861 -7.415  2.053   1.00 29.53  ? 241  ASP   A N    1 
ATOM   3116  C CA   . ASP   A  1 215 ? 12.553 -6.282  1.408   1.00 30.39  ? 241  ASP   A CA   1 
ATOM   3117  C C    . ASP   A  1 215 ? 11.731 -5.551  0.326   1.00 30.95  ? 241  ASP   A C    1 
ATOM   3118  O O    . ASP   A  1 215 ? 11.885 -4.334  0.190   1.00 32.13  ? 241  ASP   A O    1 
ATOM   3119  C CB   . ASP   A  1 215 ? 13.926 -6.705  0.851   1.00 31.25  ? 241  ASP   A CB   1 
ATOM   3120  C CG   . ASP   A  1 215 ? 15.001 -6.867  1.918   1.00 36.01  ? 241  ASP   A CG   1 
ATOM   3121  O OD1  . ASP   A  1 215 ? 14.813 -6.354  3.040   1.00 36.99  ? 241  ASP   A OD1  1 
ATOM   3122  O OD2  . ASP   A  1 215 ? 16.034 -7.503  1.631   1.00 38.58  ? 241  ASP   A OD2  1 
ATOM   3123  H H    . ASP   A  1 215 ? 12.377 -8.288  2.017   0.00 40.11  ? 241  ASP   A H    1 
ATOM   3124  H HA   . ASP   A  1 215 ? 12.725 -5.540  2.188   0.00 40.95  ? 241  ASP   A HA   1 
ATOM   3125  H HB2  . ASP   A  1 215 ? 13.824 -7.655  0.327   0.00 41.13  ? 241  ASP   A HB2  1 
ATOM   3126  H HB3  . ASP   A  1 215 ? 14.267 -5.940  0.156   0.00 40.87  ? 241  ASP   A HB3  1 
ATOM   3127  N N    . PHE   A  1 216 ? 10.850 -6.247  -0.407  1.00 30.47  ? 242  PHE   A N    1 
ATOM   3128  C CA   . PHE   A  1 216 ? 10.034 -5.610  -1.464  1.00 31.29  ? 242  PHE   A CA   1 
ATOM   3129  C C    . PHE   A  1 216 ? 8.526  -5.917  -1.326  1.00 34.04  ? 242  PHE   A C    1 
ATOM   3130  O O    . PHE   A  1 216 ? 7.803  -5.811  -2.319  1.00 34.69  ? 242  PHE   A O    1 
ATOM   3131  C CB   . PHE   A  1 216 ? 10.482 -6.142  -2.837  1.00 30.19  ? 242  PHE   A CB   1 
ATOM   3132  C CG   . PHE   A  1 216 ? 11.972 -6.158  -3.068  1.00 29.60  ? 242  PHE   A CG   1 
ATOM   3133  C CD1  . PHE   A  1 216 ? 12.701 -4.980  -3.082  1.00 29.94  ? 242  PHE   A CD1  1 
ATOM   3134  C CD2  . PHE   A  1 216 ? 12.638 -7.346  -3.312  1.00 29.68  ? 242  PHE   A CD2  1 
ATOM   3135  C CE1  . PHE   A  1 216 ? 14.070 -4.995  -3.295  1.00 29.98  ? 242  PHE   A CE1  1 
ATOM   3136  C CE2  . PHE   A  1 216 ? 14.002 -7.354  -3.537  1.00 30.17  ? 242  PHE   A CE2  1 
ATOM   3137  C CZ   . PHE   A  1 216 ? 14.713 -6.181  -3.518  1.00 29.77  ? 242  PHE   A CZ   1 
ATOM   3138  H H    . PHE   A  1 216 ? 10.676 -7.242  -0.304  0.00 40.91  ? 242  PHE   A H    1 
ATOM   3139  H HA   . PHE   A  1 216 ? 10.150 -4.528  -1.462  0.00 41.62  ? 242  PHE   A HA   1 
ATOM   3140  H HB2  . PHE   A  1 216 ? 10.111 -7.159  -2.951  0.00 39.94  ? 242  PHE   A HB2  1 
ATOM   3141  H HB3  . PHE   A  1 216 ? 10.052 -5.508  -3.609  0.00 39.71  ? 242  PHE   A HB3  1 
ATOM   3142  H HD1  . PHE   A  1 216 ? 12.204 -4.044  -2.881  0.00 38.89  ? 242  PHE   A HD1  1 
ATOM   3143  H HD2  . PHE   A  1 216 ? 12.094 -8.276  -3.330  0.00 38.65  ? 242  PHE   A HD2  1 
ATOM   3144  H HE1  . PHE   A  1 216 ? 14.627 -4.073  -3.282  0.00 38.10  ? 242  PHE   A HE1  1 
ATOM   3145  H HE2  . PHE   A  1 216 ? 14.504 -8.282  -3.738  0.00 38.42  ? 242  PHE   A HE2  1 
ATOM   3146  H HZ   . PHE   A  1 216 ? 15.773 -6.191  -3.703  0.00 37.48  ? 242  PHE   A HZ   1 
ATOM   3147  N N    . LYS   A  1 217 ? 8.049  -6.335  -0.140  1.00 35.36  ? 243  LYS   A N    1 
ATOM   3148  C CA   . LYS   A  1 217 ? 6.661  -6.811  0.027   1.00 36.96  ? 243  LYS   A CA   1 
ATOM   3149  C C    . LYS   A  1 217 ? 5.511  -5.912  -0.500  1.00 37.29  ? 243  LYS   A C    1 
ATOM   3150  O O    . LYS   A  1 217 ? 4.515  -6.462  -0.998  1.00 38.35  ? 243  LYS   A O    1 
ATOM   3151  C CB   . LYS   A  1 217 ? 6.347  -7.155  1.507   1.00 39.90  ? 243  LYS   A CB   1 
ATOM   3152  C CG   . LYS   A  1 217 ? 6.357  -8.655  1.796   1.00 44.40  ? 243  LYS   A CG   1 
ATOM   3153  C CD   . LYS   A  1 217 ? 6.193  -9.000  3.251   1.00 48.00  ? 243  LYS   A CD   1 
ATOM   3154  C CE   . LYS   A  1 217 ? 6.685  -10.407 3.427   1.00 50.98  ? 243  LYS   A CE   1 
ATOM   3155  N NZ   . LYS   A  1 217 ? 6.444  -10.962 4.777   1.00 53.14  ? 243  LYS   A NZ   1 
ATOM   3156  H H    . LYS   A  1 217 ? 8.596  -6.353  0.714   0.00 47.78  ? 243  LYS   A H    1 
ATOM   3157  H HA   . LYS   A  1 217 ? 6.613  -7.714  -0.583  0.00 50.09  ? 243  LYS   A HA   1 
ATOM   3158  H HB2  . LYS   A  1 217 ? 7.069  -6.680  2.170   0.00 54.32  ? 243  LYS   A HB2  1 
ATOM   3159  H HB3  . LYS   A  1 217 ? 5.349  -6.790  1.743   0.00 54.83  ? 243  LYS   A HB3  1 
ATOM   3160  H HG2  . LYS   A  1 217 ? 5.541  -9.122  1.248   0.00 60.03  ? 243  LYS   A HG2  1 
ATOM   3161  H HG3  . LYS   A  1 217 ? 7.307  -9.063  1.453   0.00 59.44  ? 243  LYS   A HG3  1 
ATOM   3162  H HD2  . LYS   A  1 217 ? 6.797  -8.333  3.865   0.00 64.77  ? 243  LYS   A HD2  1 
ATOM   3163  H HD3  . LYS   A  1 217 ? 5.143  -8.942  3.532   0.00 65.30  ? 243  LYS   A HD3  1 
ATOM   3164  H HE2  . LYS   A  1 217 ? 6.196  -11.053 2.701   0.00 68.37  ? 243  LYS   A HE2  1 
ATOM   3165  H HE3  . LYS   A  1 217 ? 7.758  -10.392 3.252   0.00 67.98  ? 243  LYS   A HE3  1 
ATOM   3166  H HZ1  . LYS   A  1 217 ? 5.495  -11.315 4.836   0.00 72.06  ? 243  LYS   A HZ1  1 
ATOM   3167  H HZ2  . LYS   A  1 217 ? 7.087  -11.726 4.958   0.00 71.61  ? 243  LYS   A HZ2  1 
ATOM   3168  H HZ3  . LYS   A  1 217 ? 6.586  -10.244 5.480   0.00 71.80  ? 243  LYS   A HZ3  1 
ATOM   3169  N N    . GLY   A  1 218 ? 5.597  -4.597  -0.306  1.00 35.89  ? 244  GLY   A N    1 
ATOM   3170  C CA   . GLY   A  1 218 ? 4.537  -3.683  -0.741  1.00 35.00  ? 244  GLY   A CA   1 
ATOM   3171  C C    . GLY   A  1 218 ? 4.692  -3.124  -2.149  1.00 33.97  ? 244  GLY   A C    1 
ATOM   3172  O O    . GLY   A  1 218 ? 3.834  -2.366  -2.612  1.00 34.73  ? 244  GLY   A O    1 
ATOM   3173  H H    . GLY   A  1 218 ? 6.381  -4.135  0.142   0.00 49.02  ? 244  GLY   A H    1 
ATOM   3174  H HA2  . GLY   A  1 218 ? 3.567  -4.173  -0.676  0.00 48.90  ? 244  GLY   A HA2  1 
ATOM   3175  H HA3  . GLY   A  1 218 ? 4.518  -2.834  -0.058  0.00 48.68  ? 244  GLY   A HA3  1 
ATOM   3176  N N    . LEU   A  1 219 ? 5.760  -3.498  -2.853  1.00 32.07  ? 245  LEU   A N    1 
ATOM   3177  C CA   . LEU   A  1 219 ? 6.047  -2.976  -4.189  1.00 30.92  ? 245  LEU   A CA   1 
ATOM   3178  C C    . LEU   A  1 219 ? 5.296  -3.731  -5.303  1.00 30.35  ? 245  LEU   A C    1 
ATOM   3179  O O    . LEU   A  1 219 ? 5.906  -4.282  -6.217  1.00 30.19  ? 245  LEU   A O    1 
ATOM   3180  C CB   . LEU   A  1 219 ? 7.572  -2.978  -4.416  1.00 30.63  ? 245  LEU   A CB   1 
ATOM   3181  C CG   . LEU   A  1 219 ? 8.418  -2.270  -3.319  1.00 31.39  ? 245  LEU   A CG   1 
ATOM   3182  C CD1  . LEU   A  1 219 ? 9.889  -2.273  -3.663  1.00 31.34  ? 245  LEU   A CD1  1 
ATOM   3183  C CD2  . LEU   A  1 219 ? 7.954  -0.825  -3.106  1.00 31.96  ? 245  LEU   A CD2  1 
ATOM   3184  H H    . LEU   A  1 219 ? 6.448  -4.179  -2.547  0.00 43.60  ? 245  LEU   A H    1 
ATOM   3185  H HA   . LEU   A  1 219 ? 5.718  -1.939  -4.245  0.00 42.12  ? 245  LEU   A HA   1 
ATOM   3186  H HB2  . LEU   A  1 219 ? 7.919  -4.009  -4.480  0.00 40.76  ? 245  LEU   A HB2  1 
ATOM   3187  H HB3  . LEU   A  1 219 ? 7.776  -2.459  -5.351  0.00 40.61  ? 245  LEU   A HB3  1 
ATOM   3188  H HG   . LEU   A  1 219 ? 8.300  -2.801  -2.376  0.00 42.13  ? 245  LEU   A HG   1 
ATOM   3189  H HD11 . LEU   A  1 219 ? 10.462 -2.030  -2.770  0.00 41.19  ? 245  LEU   A HD11 1 
ATOM   3190  H HD12 . LEU   A  1 219 ? 10.171 -3.254  -4.041  0.00 40.90  ? 245  LEU   A HD12 1 
ATOM   3191  H HD13 . LEU   A  1 219 ? 10.068 -1.520  -4.429  0.00 40.87  ? 245  LEU   A HD13 1 
ATOM   3192  H HD21 . LEU   A  1 219 ? 8.765  -0.252  -2.661  0.00 42.68  ? 245  LEU   A HD21 1 
ATOM   3193  H HD22 . LEU   A  1 219 ? 7.675  -0.402  -4.070  0.00 42.70  ? 245  LEU   A HD22 1 
ATOM   3194  H HD23 . LEU   A  1 219 ? 7.092  -0.828  -2.440  0.00 43.36  ? 245  LEU   A HD23 1 
ATOM   3195  N N    . ILE   A  1 220 ? 3.966  -3.650  -5.266  1.00 29.94  ? 246  ILE   A N    1 
ATOM   3196  C CA   . ILE   A  1 220 ? 3.073  -4.342  -6.198  1.00 30.60  ? 246  ILE   A CA   1 
ATOM   3197  C C    . ILE   A  1 220 ? 3.046  -3.757  -7.628  1.00 30.48  ? 246  ILE   A C    1 
ATOM   3198  O O    . ILE   A  1 220 ? 2.513  -4.427  -8.508  1.00 30.79  ? 246  ILE   A O    1 
ATOM   3199  C CB   . ILE   A  1 220 ? 1.624  -4.456  -5.630  1.00 32.10  ? 246  ILE   A CB   1 
ATOM   3200  C CG1  . ILE   A  1 220 ? 0.911  -3.079  -5.539  1.00 33.21  ? 246  ILE   A CG1  1 
ATOM   3201  C CG2  . ILE   A  1 220 ? 1.642  -5.192  -4.266  1.00 32.99  ? 246  ILE   A CG2  1 
ATOM   3202  C CD1  . ILE   A  1 220 ? -0.578 -3.184  -5.102  1.00 35.88  ? 246  ILE   A CD1  1 
ATOM   3203  H H    . ILE   A  1 220 ? 3.481  -3.087  -4.575  0.00 41.81  ? 246  ILE   A H    1 
ATOM   3204  H HA   . ILE   A  1 220 ? 3.441  -5.363  -6.295  0.00 42.19  ? 246  ILE   A HA   1 
ATOM   3205  H HB   . ILE   A  1 220 ? 1.050  -5.071  -6.321  0.00 45.13  ? 246  ILE   A HB   1 
ATOM   3206  H HG12 . ILE   A  1 220 ? 1.428  -2.459  -4.808  0.00 46.68  ? 246  ILE   A HG12 1 
ATOM   3207  H HG13 . ILE   A  1 220 ? 0.917  -2.586  -6.510  0.00 46.54  ? 246  ILE   A HG13 1 
ATOM   3208  H HG21 . ILE   A  1 220 ? 0.625  -5.470  -3.992  0.00 46.97  ? 246  ILE   A HG21 1 
ATOM   3209  H HG22 . ILE   A  1 220 ? 2.258  -6.087  -4.354  0.00 46.09  ? 246  ILE   A HG22 1 
ATOM   3210  H HG23 . ILE   A  1 220 ? 2.059  -4.528  -3.510  0.00 46.39  ? 246  ILE   A HG23 1 
ATOM   3211  H HD11 . ILE   A  1 220 ? -1.047 -2.208  -5.216  0.00 51.08  ? 246  ILE   A HD11 1 
ATOM   3212  H HD12 . ILE   A  1 220 ? -1.082 -3.918  -5.729  0.00 50.93  ? 246  ILE   A HD12 1 
ATOM   3213  H HD13 . ILE   A  1 220 ? -0.627 -3.495  -4.059  0.00 51.08  ? 246  ILE   A HD13 1 
ATOM   3214  N N    . ASN   A  1 221 ? 3.557  -2.535  -7.865  1.00 29.77  ? 247  ASN   A N    1 
ATOM   3215  C CA   . ASN   A  1 221 ? 3.626  -1.954  -9.224  1.00 29.64  ? 247  ASN   A CA   1 
ATOM   3216  C C    . ASN   A  1 221 ? 5.044  -2.028  -9.821  1.00 27.99  ? 247  ASN   A C    1 
ATOM   3217  O O    . ASN   A  1 221 ? 5.267  -1.474  -10.902 1.00 28.07  ? 247  ASN   A O    1 
ATOM   3218  C CB   . ASN   A  1 221 ? 3.187  -0.479  -9.206  1.00 32.14  ? 247  ASN   A CB   1 
ATOM   3219  C CG   . ASN   A  1 221 ? 1.739  -0.252  -9.077  1.00 38.23  ? 247  ASN   A CG   1 
ATOM   3220  O OD1  . ASN   A  1 221 ? 0.938  -1.178  -9.238  1.00 37.98  ? 247  ASN   A OD1  1 
ATOM   3221  N ND2  . ASN   A  1 221 ? 1.313  0.995   -8.983  1.00 43.48  ? 247  ASN   A ND2  1 
ATOM   3222  H H    . ASN   A  1 221 ? 3.930  -1.922  -7.148  0.00 40.83  ? 247  ASN   A H    1 
ATOM   3223  H HA   . ASN   A  1 221 ? 2.969  -2.491  -9.905  0.00 40.53  ? 247  ASN   A HA   1 
ATOM   3224  H HB2  . ASN   A  1 221 ? 3.672  0.022   -8.369  0.00 43.64  ? 247  ASN   A HB2  1 
ATOM   3225  H HB3  . ASN   A  1 221 ? 3.485  0.004   -10.134 0.00 43.38  ? 247  ASN   A HB3  1 
ATOM   3226  H HD21 . ASN   A  1 221 ? 0.682  0.752   -8.244  0.00 58.84  ? 247  ASN   A HD21 1 
ATOM   3227  H HD22 . ASN   A  1 221 ? 1.915  1.810   -9.021  0.00 58.15  ? 247  ASN   A HD22 1 
ATOM   3228  N N    . LEU   A  1 222 ? 6.005  -2.678  -9.134  1.00 26.35  ? 248  LEU   A N    1 
ATOM   3229  C CA   . LEU   A  1 222 ? 7.386  -2.729  -9.607  1.00 25.26  ? 248  LEU   A CA   1 
ATOM   3230  C C    . LEU   A  1 222 ? 7.497  -3.489  -10.919 1.00 24.49  ? 248  LEU   A C    1 
ATOM   3231  O O    . LEU   A  1 222 ? 7.062  -4.636  -10.995 1.00 24.78  ? 248  LEU   A O    1 
ATOM   3232  C CB   . LEU   A  1 222 ? 8.305  -3.379  -8.547  1.00 24.96  ? 248  LEU   A CB   1 
ATOM   3233  C CG   . LEU   A  1 222 ? 9.789  -3.003  -8.621  1.00 25.75  ? 248  LEU   A CG   1 
ATOM   3234  C CD1  . LEU   A  1 222 ? 10.005 -1.523  -8.235  1.00 25.89  ? 248  LEU   A CD1  1 
ATOM   3235  C CD2  . LEU   A  1 222 ? 10.631 -3.925  -7.729  1.00 26.07  ? 248  LEU   A CD2  1 
ATOM   3236  H H    . LEU   A  1 222 ? 5.857  -3.191  -8.272  0.00 35.56  ? 248  LEU   A H    1 
ATOM   3237  H HA   . LEU   A  1 222 ? 7.709  -1.706  -9.770  0.00 33.21  ? 248  LEU   A HA   1 
ATOM   3238  H HB2  . LEU   A  1 222 ? 7.957  -3.091  -7.557  0.00 33.19  ? 248  LEU   A HB2  1 
ATOM   3239  H HB3  . LEU   A  1 222 ? 8.241  -4.462  -8.645  0.00 32.84  ? 248  LEU   A HB3  1 
ATOM   3240  H HG   . LEU   A  1 222 ? 10.130 -3.129  -9.648  0.00 32.84  ? 248  LEU   A HG   1 
ATOM   3241  H HD11 . LEU   A  1 222 ? 11.058 -1.377  -8.000  0.00 33.08  ? 248  LEU   A HD11 1 
ATOM   3242  H HD12 . LEU   A  1 222 ? 9.739  -0.885  -9.077  0.00 33.34  ? 248  LEU   A HD12 1 
ATOM   3243  H HD13 . LEU   A  1 222 ? 9.393  -1.276  -7.369  0.00 33.84  ? 248  LEU   A HD13 1 
ATOM   3244  H HD21 . LEU   A  1 222 ? 11.681 -3.652  -7.826  0.00 33.08  ? 248  LEU   A HD21 1 
ATOM   3245  H HD22 . LEU   A  1 222 ? 10.312 -3.806  -6.695  0.00 33.83  ? 248  LEU   A HD22 1 
ATOM   3246  H HD23 . LEU   A  1 222 ? 10.486 -4.957  -8.047  0.00 33.47  ? 248  LEU   A HD23 1 
ATOM   3247  N N    . THR   A  1 223 ? 8.043  -2.830  -11.958 1.00 23.30  ? 249  THR   A N    1 
ATOM   3248  C CA   . THR   A  1 223 ? 8.275  -3.420  -13.271 1.00 23.21  ? 249  THR   A CA   1 
ATOM   3249  C C    . THR   A  1 223 ? 9.785  -3.719  -13.477 1.00 23.12  ? 249  THR   A C    1 
ATOM   3250  O O    . THR   A  1 223 ? 10.118 -4.537  -14.333 1.00 23.68  ? 249  THR   A O    1 
ATOM   3251  C CB   . THR   A  1 223 ? 7.728  -2.534  -14.387 1.00 24.12  ? 249  THR   A CB   1 
ATOM   3252  O OG1  . THR   A  1 223 ? 8.493  -1.334  -14.448 1.00 24.61  ? 249  THR   A OG1  1 
ATOM   3253  C CG2  . THR   A  1 223 ? 6.238  -2.239  -14.223 1.00 24.31  ? 249  THR   A CG2  1 
ATOM   3254  H H    . THR   A  1 223 ? 8.343  -1.862  -11.917 0.00 30.18  ? 249  THR   A H    1 
ATOM   3255  H HA   . THR   A  1 223 ? 7.707  -4.342  -13.366 0.00 30.07  ? 249  THR   A HA   1 
ATOM   3256  H HB   . THR   A  1 223 ? 7.846  -3.060  -15.332 0.00 30.80  ? 249  THR   A HB   1 
ATOM   3257  H HG1  . THR   A  1 223 ? 8.261  -0.745  -13.683 0.00 31.52  ? 249  THR   A HG1  1 
ATOM   3258  H HG21 . THR   A  1 223 ? 5.867  -1.701  -15.094 0.00 31.96  ? 249  THR   A HG21 1 
ATOM   3259  H HG22 . THR   A  1 223 ? 5.682  -3.169  -14.118 0.00 32.15  ? 249  THR   A HG22 1 
ATOM   3260  H HG23 . THR   A  1 223 ? 6.070  -1.629  -13.337 0.00 32.12  ? 249  THR   A HG23 1 
ATOM   3261  N N    . LEU   A  1 224 ? 10.700 -3.052  -12.731 1.00 22.00  ? 250  LEU   A N    1 
ATOM   3262  C CA   . LEU   A  1 224 ? 12.129 -3.296  -12.871 1.00 21.17  ? 250  LEU   A CA   1 
ATOM   3263  C C    . LEU   A  1 224 ? 12.783 -3.382  -11.514 1.00 21.93  ? 250  LEU   A C    1 
ATOM   3264  O O    . LEU   A  1 224 ? 12.514 -2.543  -10.644 1.00 22.58  ? 250  LEU   A O    1 
ATOM   3265  C CB   . LEU   A  1 224 ? 12.812 -2.192  -13.711 1.00 20.55  ? 250  LEU   A CB   1 
ATOM   3266  C CG   . LEU   A  1 224 ? 14.342 -2.324  -13.909 1.00 21.17  ? 250  LEU   A CG   1 
ATOM   3267  C CD1  . LEU   A  1 224 ? 14.754 -1.777  -15.248 1.00 21.57  ? 250  LEU   A CD1  1 
ATOM   3268  C CD2  . LEU   A  1 224 ? 15.121 -1.607  -12.801 1.00 21.52  ? 250  LEU   A CD2  1 
ATOM   3269  H H    . LEU   A  1 224 ? 10.486 -2.337  -12.044 0.00 27.74  ? 250  LEU   A H    1 
ATOM   3270  H HA   . LEU   A  1 224 ? 12.296 -4.243  -13.379 0.00 25.87  ? 250  LEU   A HA   1 
ATOM   3271  H HB2  . LEU   A  1 224 ? 12.355 -2.188  -14.700 0.00 24.87  ? 250  LEU   A HB2  1 
ATOM   3272  H HB3  . LEU   A  1 224 ? 12.630 -1.232  -13.233 0.00 25.04  ? 250  LEU   A HB3  1 
ATOM   3273  H HG   . LEU   A  1 224 ? 14.638 -3.372  -13.889 0.00 25.00  ? 250  LEU   A HG   1 
ATOM   3274  H HD11 . LEU   A  1 224 ? 15.839 -1.820  -15.330 0.00 24.88  ? 250  LEU   A HD11 1 
ATOM   3275  H HD12 . LEU   A  1 224 ? 14.301 -2.379  -16.034 0.00 25.25  ? 250  LEU   A HD12 1 
ATOM   3276  H HD13 . LEU   A  1 224 ? 14.416 -0.745  -15.329 0.00 25.35  ? 250  LEU   A HD13 1 
ATOM   3277  H HD21 . LEU   A  1 224 ? 16.187 -1.744  -12.972 0.00 25.13  ? 250  LEU   A HD21 1 
ATOM   3278  H HD22 . LEU   A  1 224 ? 14.877 -0.546  -12.830 0.00 25.58  ? 250  LEU   A HD22 1 
ATOM   3279  H HD23 . LEU   A  1 224 ? 14.843 -2.027  -11.835 0.00 25.74  ? 250  LEU   A HD23 1 
ATOM   3280  N N    . LEU   A  1 225 ? 13.670 -4.379  -11.345 1.00 20.91  ? 251  LEU   A N    1 
ATOM   3281  C CA   . LEU   A  1 225 ? 14.462 -4.560  -10.150 1.00 20.68  ? 251  LEU   A CA   1 
ATOM   3282  C C    . LEU   A  1 225 ? 15.878 -4.878  -10.603 1.00 21.33  ? 251  LEU   A C    1 
ATOM   3283  O O    . LEU   A  1 225 ? 16.091 -5.837  -11.352 1.00 21.67  ? 251  LEU   A O    1 
ATOM   3284  C CB   . LEU   A  1 225 ? 13.919 -5.698  -9.264  1.00 20.29  ? 251  LEU   A CB   1 
ATOM   3285  C CG   . LEU   A  1 225 ? 14.699 -5.977  -7.966  1.00 21.96  ? 251  LEU   A CG   1 
ATOM   3286  C CD1  . LEU   A  1 225 ? 14.776 -4.731  -7.081  1.00 22.27  ? 251  LEU   A CD1  1 
ATOM   3287  C CD2  . LEU   A  1 225 ? 14.064 -7.135  -7.189  1.00 22.38  ? 251  LEU   A CD2  1 
ATOM   3288  H H    . LEU   A  1 225 ? 13.855 -5.091  -12.044 0.00 25.31  ? 251  LEU   A H    1 
ATOM   3289  H HA   . LEU   A  1 225 ? 14.476 -3.635  -9.576  0.00 25.32  ? 251  LEU   A HA   1 
ATOM   3290  H HB2  . LEU   A  1 225 ? 12.905 -5.439  -8.962  0.00 25.51  ? 251  LEU   A HB2  1 
ATOM   3291  H HB3  . LEU   A  1 225 ? 13.904 -6.618  -9.846  0.00 25.07  ? 251  LEU   A HB3  1 
ATOM   3292  H HG   . LEU   A  1 225 ? 15.716 -6.278  -8.214  0.00 26.91  ? 251  LEU   A HG   1 
ATOM   3293  H HD11 . LEU   A  1 225 ? 15.119 -5.021  -6.089  0.00 27.92  ? 251  LEU   A HD11 1 
ATOM   3294  H HD12 . LEU   A  1 225 ? 15.482 -4.025  -7.516  0.00 27.43  ? 251  LEU   A HD12 1 
ATOM   3295  H HD13 . LEU   A  1 225 ? 13.787 -4.279  -7.016  0.00 28.05  ? 251  LEU   A HD13 1 
ATOM   3296  H HD21 . LEU   A  1 225 ? 14.665 -7.344  -6.305  0.00 28.24  ? 251  LEU   A HD21 1 
ATOM   3297  H HD22 . LEU   A  1 225 ? 13.055 -6.852  -6.893  0.00 28.53  ? 251  LEU   A HD22 1 
ATOM   3298  H HD23 . LEU   A  1 225 ? 14.029 -8.014  -7.830  0.00 28.09  ? 251  LEU   A HD23 1 
ATOM   3299  N N    . ASP   A  1 226 ? 16.842 -4.081  -10.152 1.00 21.19  ? 252  ASP   A N    1 
ATOM   3300  C CA   . ASP   A  1 226 ? 18.235 -4.296  -10.503 1.00 21.57  ? 252  ASP   A CA   1 
ATOM   3301  C C    . ASP   A  1 226 ? 19.021 -4.546  -9.231  1.00 21.75  ? 252  ASP   A C    1 
ATOM   3302  O O    . ASP   A  1 226 ? 19.261 -3.611  -8.470  1.00 22.02  ? 252  ASP   A O    1 
ATOM   3303  C CB   . ASP   A  1 226 ? 18.781 -3.092  -11.300 1.00 21.50  ? 252  ASP   A CB   1 
ATOM   3304  C CG   . ASP   A  1 226 ? 20.268 -3.112  -11.597 1.00 24.49  ? 252  ASP   A CG   1 
ATOM   3305  O OD1  . ASP   A  1 226 ? 20.897 -4.182  -11.425 1.00 24.66  ? 252  ASP   A OD1  1 
ATOM   3306  O OD2  . ASP   A  1 226 ? 20.798 -2.067  -12.049 1.00 25.08  ? 252  ASP   A OD2  1 
ATOM   3307  H H    . ASP   A  1 226 ? 16.699 -3.283  -9.542  0.00 25.31  ? 252  ASP   A H    1 
ATOM   3308  H HA   . ASP   A  1 226 ? 18.322 -5.182  -11.125 0.00 25.07  ? 252  ASP   A HA   1 
ATOM   3309  H HB2  . ASP   A  1 226 ? 18.263 -3.056  -12.257 0.00 24.69  ? 252  ASP   A HB2  1 
ATOM   3310  H HB3  . ASP   A  1 226 ? 18.581 -2.177  -10.752 0.00 24.94  ? 252  ASP   A HB3  1 
ATOM   3311  N N    . LEU   A  1 227 ? 19.396 -5.817  -8.992  1.00 21.42  ? 253  LEU   A N    1 
ATOM   3312  C CA   . LEU   A  1 227 ? 20.223 -6.220  -7.849  1.00 21.49  ? 253  LEU   A CA   1 
ATOM   3313  C C    . LEU   A  1 227 ? 21.620 -6.675  -8.313  1.00 21.16  ? 253  LEU   A C    1 
ATOM   3314  O O    . LEU   A  1 227 ? 22.303 -7.386  -7.574  1.00 21.07  ? 253  LEU   A O    1 
ATOM   3315  C CB   . LEU   A  1 227 ? 19.529 -7.371  -7.087  1.00 21.84  ? 253  LEU   A CB   1 
ATOM   3316  C CG   . LEU   A  1 227 ? 18.298 -7.010  -6.268  1.00 24.50  ? 253  LEU   A CG   1 
ATOM   3317  C CD1  . LEU   A  1 227 ? 17.575 -8.280  -5.809  1.00 24.65  ? 253  LEU   A CD1  1 
ATOM   3318  C CD2  . LEU   A  1 227 ? 18.676 -6.146  -5.054  1.00 25.32  ? 253  LEU   A CD2  1 
ATOM   3319  H H    . LEU   A  1 227 ? 19.132 -6.599  -9.582  0.00 25.13  ? 253  LEU   A H    1 
ATOM   3320  H HA   . LEU   A  1 227 ? 20.377 -5.386  -7.167  0.00 25.49  ? 253  LEU   A HA   1 
ATOM   3321  H HB2  . LEU   A  1 227 ? 19.200 -8.106  -7.819  0.00 26.17  ? 253  LEU   A HB2  1 
ATOM   3322  H HB3  . LEU   A  1 227 ? 20.232 -7.836  -6.398  0.00 26.32  ? 253  LEU   A HB3  1 
ATOM   3323  H HG   . LEU   A  1 227 ? 17.614 -6.434  -6.890  0.00 29.82  ? 253  LEU   A HG   1 
ATOM   3324  H HD11 . LEU   A  1 227 ? 16.762 -8.014  -5.135  0.00 30.80  ? 253  LEU   A HD11 1 
ATOM   3325  H HD12 . LEU   A  1 227 ? 17.174 -8.789  -6.685  0.00 30.36  ? 253  LEU   A HD12 1 
ATOM   3326  H HD13 . LEU   A  1 227 ? 18.291 -8.925  -5.304  0.00 30.50  ? 253  LEU   A HD13 1 
ATOM   3327  H HD21 . LEU   A  1 227 ? 17.819 -6.072  -4.387  0.00 31.45  ? 253  LEU   A HD21 1 
ATOM   3328  H HD22 . LEU   A  1 227 ? 19.513 -6.606  -4.530  0.00 31.08  ? 253  LEU   A HD22 1 
ATOM   3329  H HD23 . LEU   A  1 227 ? 18.952 -5.151  -5.394  0.00 30.87  ? 253  LEU   A HD23 1 
ATOM   3330  N N    . SER   A  1 228 ? 22.088 -6.224  -9.496  1.00 20.50  ? 254  SER   A N    1 
ATOM   3331  C CA   . SER   A  1 228 ? 23.384 -6.642  -10.006 1.00 20.07  ? 254  SER   A CA   1 
ATOM   3332  C C    . SER   A  1 228 ? 24.567 -6.132  -9.188  1.00 20.41  ? 254  SER   A C    1 
ATOM   3333  O O    . SER   A  1 228 ? 24.460 -5.141  -8.498  1.00 20.30  ? 254  SER   A O    1 
ATOM   3334  C CB   . SER   A  1 228 ? 23.539 -6.216  -11.473 1.00 20.10  ? 254  SER   A CB   1 
ATOM   3335  O OG   . SER   A  1 228 ? 23.465 -4.810  -11.632 1.00 20.70  ? 254  SER   A OG   1 
ATOM   3336  H H    . SER   A  1 228 ? 21.611 -5.569  -10.106 0.00 23.34  ? 254  SER   A H    1 
ATOM   3337  H HA   . SER   A  1 228 ? 23.421 -7.730  -9.986  0.00 22.73  ? 254  SER   A HA   1 
ATOM   3338  H HB2  . SER   A  1 228 ? 24.506 -6.559  -11.836 0.00 22.08  ? 254  SER   A HB2  1 
ATOM   3339  H HB3  . SER   A  1 228 ? 22.743 -6.676  -12.057 0.00 22.31  ? 254  SER   A HB3  1 
ATOM   3340  H HG   . SER   A  1 228 ? 22.522 -4.507  -11.562 0.00 23.03  ? 254  SER   A HG   1 
ATOM   3341  N N    . GLY   A  1 229 ? 25.689 -6.825  -9.274  1.00 20.26  ? 255  GLY   A N    1 
ATOM   3342  C CA   . GLY   A  1 229 ? 26.906 -6.429  -8.587  1.00 20.68  ? 255  GLY   A CA   1 
ATOM   3343  C C    . GLY   A  1 229 ? 26.924 -6.596  -7.081  1.00 20.46  ? 255  GLY   A C    1 
ATOM   3344  O O    . GLY   A  1 229 ? 27.822 -6.063  -6.429  1.00 20.78  ? 255  GLY   A O    1 
ATOM   3345  H H    . GLY   A  1 229 ? 25.793 -7.672  -9.824  0.00 22.69  ? 255  GLY   A H    1 
ATOM   3346  H HA2  . GLY   A  1 229 ? 27.734 -7.008  -8.993  0.00 23.17  ? 255  GLY   A HA2  1 
ATOM   3347  H HA3  . GLY   A  1 229 ? 27.104 -5.381  -8.805  0.00 23.15  ? 255  GLY   A HA3  1 
ATOM   3348  N N    . ASN   A  1 230 ? 25.948 -7.336  -6.507  1.00 20.24  ? 256  ASN   A N    1 
ATOM   3349  C CA   . ASN   A  1 230 ? 25.881 -7.591  -5.058  1.00 20.29  ? 256  ASN   A CA   1 
ATOM   3350  C C    . ASN   A  1 230 ? 26.385 -9.005  -4.890  1.00 21.19  ? 256  ASN   A C    1 
ATOM   3351  O O    . ASN   A  1 230 ? 25.795 -9.916  -5.463  1.00 22.46  ? 256  ASN   A O    1 
ATOM   3352  C CB   . ASN   A  1 230 ? 24.457 -7.393  -4.570  1.00 20.86  ? 256  ASN   A CB   1 
ATOM   3353  C CG   . ASN   A  1 230 ? 24.061 -5.937  -4.672  1.00 22.55  ? 256  ASN   A CG   1 
ATOM   3354  O OD1  . ASN   A  1 230 ? 24.730 -5.072  -4.114  1.00 23.57  ? 256  ASN   A OD1  1 
ATOM   3355  N ND2  . ASN   A  1 230 ? 23.006 -5.614  -5.411  1.00 22.23  ? 256  ASN   A ND2  1 
ATOM   3356  H H    . ASN   A  1 230 ? 25.190 -7.777  -7.017  0.00 23.49  ? 256  ASN   A H    1 
ATOM   3357  H HA   . ASN   A  1 230 ? 26.534 -6.915  -4.508  0.00 24.11  ? 256  ASN   A HA   1 
ATOM   3358  H HB2  . ASN   A  1 230 ? 23.780 -7.992  -5.175  0.00 24.96  ? 256  ASN   A HB2  1 
ATOM   3359  H HB3  . ASN   A  1 230 ? 24.391 -7.690  -3.524  0.00 25.37  ? 256  ASN   A HB3  1 
ATOM   3360  H HD21 . ASN   A  1 230 ? 22.729 -4.641  -5.492  0.00 26.43  ? 256  ASN   A HD21 1 
ATOM   3361  H HD22 . ASN   A  1 230 ? 22.471 -6.327  -5.896  0.00 26.44  ? 256  ASN   A HD22 1 
ATOM   3362  N N    . CYS   A  1 231 ? 27.533 -9.181  -4.210  1.00 20.12  ? 257  CYS   A N    1 
ATOM   3363  C CA   . CYS   A  1 231 ? 28.329 -10.414 -4.186  1.00 20.73  ? 257  CYS   A CA   1 
ATOM   3364  C C    . CYS   A  1 231 ? 28.873 -10.626 -5.597  1.00 21.38  ? 257  CYS   A C    1 
ATOM   3365  O O    . CYS   A  1 231 ? 28.547 -11.608 -6.259  1.00 21.27  ? 257  CYS   A O    1 
ATOM   3366  C CB   . CYS   A  1 231 ? 27.540 -11.618 -3.698  1.00 21.55  ? 257  CYS   A CB   1 
ATOM   3367  S SG   . CYS   A  1 231 ? 27.063 -11.507 -1.965  1.00 27.26  ? 257  CYS   A SG   1 
ATOM   3368  H H    . CYS   A  1 231 ? 27.950 -8.458  -3.633  0.00 24.24  ? 257  CYS   A H    1 
ATOM   3369  H HA   . CYS   A  1 231 ? 29.196 -10.283 -3.542  0.00 25.19  ? 257  CYS   A HA   1 
ATOM   3370  H HB2  . CYS   A  1 231 ? 26.636 -11.739 -4.295  0.00 26.29  ? 257  CYS   A HB2  1 
ATOM   3371  H HB3  . CYS   A  1 231 ? 28.164 -12.504 -3.800  0.00 26.50  ? 257  CYS   A HB3  1 
ATOM   3372  N N    . PRO   A  1 232 ? 29.725 -9.704  -6.068  1.00 21.49  ? 258  PRO   A N    1 
ATOM   3373  C CA   . PRO   A  1 232 ? 30.201 -9.801  -7.454  1.00 21.76  ? 258  PRO   A CA   1 
ATOM   3374  C C    . PRO   A  1 232 ? 31.164 -10.927 -7.790  1.00 21.48  ? 258  PRO   A C    1 
ATOM   3375  O O    . PRO   A  1 232 ? 31.815 -11.480 -6.911  1.00 21.47  ? 258  PRO   A O    1 
ATOM   3376  C CB   . PRO   A  1 232 ? 30.874 -8.443  -7.681  1.00 22.59  ? 258  PRO   A CB   1 
ATOM   3377  C CG   . PRO   A  1 232 ? 31.350 -8.046  -6.306  1.00 22.95  ? 258  PRO   A CG   1 
ATOM   3378  C CD   . PRO   A  1 232 ? 30.226 -8.481  -5.407  1.00 20.56  ? 258  PRO   A CD   1 
ATOM   3379  H HA   . PRO   A  1 232 ? 29.343 -9.873  -8.121  0.00 24.96  ? 258  PRO   A HA   1 
ATOM   3380  H HB2  . PRO   A  1 232 ? 31.712 -8.551  -8.368  0.00 25.65  ? 258  PRO   A HB2  1 
ATOM   3381  H HB3  . PRO   A  1 232 ? 30.145 -7.730  -8.060  0.00 25.67  ? 258  PRO   A HB3  1 
ATOM   3382  H HG2  . PRO   A  1 232 ? 32.272 -8.572  -6.068  0.00 26.77  ? 258  PRO   A HG2  1 
ATOM   3383  H HG3  . PRO   A  1 232 ? 31.495 -6.968  -6.259  0.00 26.53  ? 258  PRO   A HG3  1 
ATOM   3384  H HD2  . PRO   A  1 232 ? 30.622 -8.697  -4.416  0.00 24.46  ? 258  PRO   A HD2  1 
ATOM   3385  H HD3  . PRO   A  1 232 ? 29.447 -7.722  -5.370  0.00 24.07  ? 258  PRO   A HD3  1 
ATOM   3386  N N    . ARG   A  1 233 ? 31.224 -11.268 -9.097  1.00 21.04  ? 259  ARG   A N    1 
ATOM   3387  C CA   . ARG   A  1 233 ? 32.173 -12.238 -9.638  1.00 21.51  ? 259  ARG   A CA   1 
ATOM   3388  C C    . ARG   A  1 233 ? 33.359 -11.332 -10.020 1.00 21.31  ? 259  ARG   A C    1 
ATOM   3389  O O    . ARG   A  1 233 ? 33.220 -10.512 -10.918 1.00 19.99  ? 259  ARG   A O    1 
ATOM   3390  C CB   . ARG   A  1 233 ? 31.581 -12.986 -10.851 1.00 22.86  ? 259  ARG   A CB   1 
ATOM   3391  C CG   . ARG   A  1 233 ? 32.633 -13.543 -11.803 1.00 25.11  ? 259  ARG   A CG   1 
ATOM   3392  C CD   . ARG   A  1 233 ? 32.058 -14.488 -12.830 1.00 27.23  ? 259  ARG   A CD   1 
ATOM   3393  N NE   . ARG   A  1 233 ? 33.109 -14.889 -13.773 1.00 29.53  ? 259  ARG   A NE   1 
ATOM   3394  C CZ   . ARG   A  1 233 ? 33.088 -15.978 -14.535 1.00 28.10  ? 259  ARG   A CZ   1 
ATOM   3395  N NH1  . ARG   A  1 233 ? 32.049 -16.805 -14.498 1.00 23.41  ? 259  ARG   A NH1  1 
ATOM   3396  N NH2  . ARG   A  1 233 ? 34.108 -16.247 -15.348 1.00 28.14  ? 259  ARG   A NH2  1 
ATOM   3397  H H    . ARG   A  1 233 ? 30.624 -10.855 -9.804  0.00 23.75  ? 259  ARG   A H    1 
ATOM   3398  H HA   . ARG   A  1 233 ? 32.479 -12.963 -8.886  0.00 24.95  ? 259  ARG   A HA   1 
ATOM   3399  H HB2  . ARG   A  1 233 ? 30.989 -13.824 -10.487 0.00 26.33  ? 259  ARG   A HB2  1 
ATOM   3400  H HB3  . ARG   A  1 233 ? 30.951 -12.312 -11.429 0.00 25.79  ? 259  ARG   A HB3  1 
ATOM   3401  H HG2  . ARG   A  1 233 ? 33.092 -12.721 -12.351 0.00 28.34  ? 259  ARG   A HG2  1 
ATOM   3402  H HG3  . ARG   A  1 233 ? 33.387 -14.082 -11.230 0.00 28.92  ? 259  ARG   A HG3  1 
ATOM   3403  H HD2  . ARG   A  1 233 ? 31.685 -15.363 -12.300 0.00 31.51  ? 259  ARG   A HD2  1 
ATOM   3404  H HD3  . ARG   A  1 233 ? 31.259 -13.996 -13.381 0.00 30.95  ? 259  ARG   A HD3  1 
ATOM   3405  H HE   . ARG   A  1 233 ? 33.932 -14.297 -13.827 0.00 33.68  ? 259  ARG   A HE   1 
ATOM   3406  H HH11 . ARG   A  1 233 ? 31.237 -16.641 -13.913 0.00 26.93  ? 259  ARG   A HH11 1 
ATOM   3407  H HH12 . ARG   A  1 233 ? 32.046 -17.623 -15.099 0.00 26.96  ? 259  ARG   A HH12 1 
ATOM   3408  H HH21 . ARG   A  1 233 ? 34.915 -15.633 -15.380 0.00 32.05  ? 259  ARG   A HH21 1 
ATOM   3409  H HH22 . ARG   A  1 233 ? 34.092 -17.078 -15.932 0.00 32.33  ? 259  ARG   A HH22 1 
ATOM   3410  N N    . CYS   A  1 234 ? 34.488 -11.457 -9.325  1.00 21.30  ? 260  CYS   A N    1 
ATOM   3411  C CA   . CYS   A  1 234 ? 35.598 -10.517 -9.460  1.00 22.77  ? 260  CYS   A CA   1 
ATOM   3412  C C    . CYS   A  1 234 ? 36.775 -10.946 -10.303 1.00 22.71  ? 260  CYS   A C    1 
ATOM   3413  O O    . CYS   A  1 234 ? 37.633 -10.086 -10.542 1.00 22.92  ? 260  CYS   A O    1 
ATOM   3414  C CB   . CYS   A  1 234 ? 36.075 -10.114 -8.069  1.00 24.91  ? 260  CYS   A CB   1 
ATOM   3415  S SG   . CYS   A  1 234 ? 34.851 -9.147  -7.151  1.00 30.35  ? 260  CYS   A SG   1 
ATOM   3416  H H    . CYS   A  1 234 ? 34.666 -12.204 -8.662  0.00 24.67  ? 260  CYS   A H    1 
ATOM   3417  H HA   . CYS   A  1 234 ? 35.231 -9.614  -9.942  0.00 25.64  ? 260  CYS   A HA   1 
ATOM   3418  H HB2  . CYS   A  1 234 ? 36.291 -11.011 -7.491  0.00 29.23  ? 260  CYS   A HB2  1 
ATOM   3419  H HB3  . CYS   A  1 234 ? 36.975 -9.507  -8.147  0.00 28.83  ? 260  CYS   A HB3  1 
ATOM   3420  N N    . PHE   A  1 235 ? 36.866 -12.208 -10.768 1.00 21.63  ? 261  PHE   A N    1 
ATOM   3421  C CA   . PHE   A  1 235 ? 38.024 -12.601 -11.565 1.00 21.05  ? 261  PHE   A CA   1 
ATOM   3422  C C    . PHE   A  1 235 ? 38.104 -11.768 -12.858 1.00 19.60  ? 261  PHE   A C    1 
ATOM   3423  O O    . PHE   A  1 235 ? 37.101 -11.589 -13.530 1.00 19.44  ? 261  PHE   A O    1 
ATOM   3424  C CB   . PHE   A  1 235 ? 38.013 -14.097 -11.881 1.00 21.54  ? 261  PHE   A CB   1 
ATOM   3425  C CG   . PHE   A  1 235 ? 39.167 -14.494 -12.772 1.00 22.23  ? 261  PHE   A CG   1 
ATOM   3426  C CD1  . PHE   A  1 235 ? 40.472 -14.414 -12.318 1.00 22.86  ? 261  PHE   A CD1  1 
ATOM   3427  C CD2  . PHE   A  1 235 ? 38.954 -14.839 -14.095 1.00 23.10  ? 261  PHE   A CD2  1 
ATOM   3428  C CE1  . PHE   A  1 235 ? 41.537 -14.692 -13.165 1.00 23.45  ? 261  PHE   A CE1  1 
ATOM   3429  C CE2  . PHE   A  1 235 ? 40.020 -15.162 -14.926 1.00 23.47  ? 261  PHE   A CE2  1 
ATOM   3430  C CZ   . PHE   A  1 235 ? 41.302 -15.089 -14.454 1.00 23.24  ? 261  PHE   A CZ   1 
ATOM   3431  H H    . PHE   A  1 235 ? 36.193 -12.951 -10.609 0.00 24.77  ? 261  PHE   A H    1 
ATOM   3432  H HA   . PHE   A  1 235 ? 38.920 -12.404 -10.978 0.00 24.11  ? 261  PHE   A HA   1 
ATOM   3433  H HB2  . PHE   A  1 235 ? 38.095 -14.658 -10.952 0.00 25.14  ? 261  PHE   A HB2  1 
ATOM   3434  H HB3  . PHE   A  1 235 ? 37.081 -14.345 -12.386 0.00 24.60  ? 261  PHE   A HB3  1 
ATOM   3435  H HD1  . PHE   A  1 235 ? 40.667 -14.099 -11.306 0.00 26.81  ? 261  PHE   A HD1  1 
ATOM   3436  H HD2  . PHE   A  1 235 ? 37.949 -14.904 -14.475 0.00 26.21  ? 261  PHE   A HD2  1 
ATOM   3437  H HE1  . PHE   A  1 235 ? 42.545 -14.658 -12.788 0.00 27.57  ? 261  PHE   A HE1  1 
ATOM   3438  H HE2  . PHE   A  1 235 ? 39.837 -15.457 -15.945 0.00 26.68  ? 261  PHE   A HE2  1 
ATOM   3439  H HZ   . PHE   A  1 235 ? 42.128 -15.334 -15.099 0.00 26.87  ? 261  PHE   A HZ   1 
ATOM   3440  N N    . ASN   A  1 236 ? 39.265 -11.184 -13.122 1.00 19.01  ? 262  ASN   A N    1 
ATOM   3441  C CA   . ASN   A  1 236 ? 39.496 -10.374 -14.308 1.00 19.17  ? 262  ASN   A CA   1 
ATOM   3442  C C    . ASN   A  1 236 ? 38.554 -9.159  -14.433 1.00 20.23  ? 262  ASN   A C    1 
ATOM   3443  O O    . ASN   A  1 236 ? 38.268 -8.720  -15.550 1.00 20.35  ? 262  ASN   A O    1 
ATOM   3444  C CB   . ASN   A  1 236 ? 39.379 -11.243 -15.561 1.00 19.23  ? 262  ASN   A CB   1 
ATOM   3445  C CG   . ASN   A  1 236 ? 40.021 -10.589 -16.760 1.00 19.12  ? 262  ASN   A CG   1 
ATOM   3446  O OD1  . ASN   A  1 236 ? 41.131 -10.046 -16.658 1.00 19.27  ? 262  ASN   A OD1  1 
ATOM   3447  N ND2  . ASN   A  1 236 ? 39.330 -10.589 -17.889 1.00 19.29  ? 262  ASN   A ND2  1 
ATOM   3448  H H    . ASN   A  1 236 ? 40.088 -11.254 -12.530 0.00 21.15  ? 262  ASN   A H    1 
ATOM   3449  H HA   . ASN   A  1 236 ? 40.512 -9.989  -14.236 0.00 20.74  ? 262  ASN   A HA   1 
ATOM   3450  H HB2  . ASN   A  1 236 ? 39.886 -12.190 -15.381 0.00 20.91  ? 262  ASN   A HB2  1 
ATOM   3451  H HB3  . ASN   A  1 236 ? 38.324 -11.418 -15.766 0.00 20.52  ? 262  ASN   A HB3  1 
ATOM   3452  H HD21 . ASN   A  1 236 ? 39.726 -10.161 -18.720 0.00 19.90  ? 262  ASN   A HD21 1 
ATOM   3453  H HD22 . ASN   A  1 236 ? 38.406 -11.009 -17.937 0.00 20.09  ? 262  ASN   A HD22 1 
ATOM   3454  N N    . ALA   A  1 237 ? 38.101 -8.593  -13.297 1.00 20.14  ? 263  ALA   A N    1 
ATOM   3455  C CA   . ALA   A  1 237 ? 37.198 -7.453  -13.354 1.00 21.25  ? 263  ALA   A CA   1 
ATOM   3456  C C    . ALA   A  1 237 ? 37.925 -6.227  -13.877 1.00 21.54  ? 263  ALA   A C    1 
ATOM   3457  O O    . ALA   A  1 237 ? 39.041 -5.960  -13.425 1.00 21.63  ? 263  ALA   A O    1 
ATOM   3458  C CB   . ALA   A  1 237 ? 36.642 -7.155  -11.967 1.00 21.87  ? 263  ALA   A CB   1 
ATOM   3459  H H    . ALA   A  1 237 ? 38.347 -8.882  -12.356 0.00 21.96  ? 263  ALA   A H    1 
ATOM   3460  H HA   . ALA   A  1 237 ? 36.356 -7.716  -13.993 0.00 22.58  ? 263  ALA   A HA   1 
ATOM   3461  H HB1  . ALA   A  1 237 ? 35.964 -6.306  -12.033 0.00 23.63  ? 263  ALA   A HB1  1 
ATOM   3462  H HB2  . ALA   A  1 237 ? 36.106 -8.030  -11.603 0.00 23.95  ? 263  ALA   A HB2  1 
ATOM   3463  H HB3  . ALA   A  1 237 ? 37.469 -6.919  -11.299 0.00 23.98  ? 263  ALA   A HB3  1 
ATOM   3464  N N    . PRO   A  1 238 ? 37.299 -5.432  -14.774 1.00 22.06  ? 264  PRO   A N    1 
ATOM   3465  C CA   . PRO   A  1 238 ? 37.943 -4.193  -15.244 1.00 22.41  ? 264  PRO   A CA   1 
ATOM   3466  C C    . PRO   A  1 238 ? 37.716 -2.994  -14.299 1.00 23.76  ? 264  PRO   A C    1 
ATOM   3467  O O    . PRO   A  1 238 ? 37.786 -1.845  -14.730 1.00 24.44  ? 264  PRO   A O    1 
ATOM   3468  C CB   . PRO   A  1 238 ? 37.289 -3.986  -16.616 1.00 22.98  ? 264  PRO   A CB   1 
ATOM   3469  C CG   . PRO   A  1 238 ? 35.896 -4.502  -16.427 1.00 23.33  ? 264  PRO   A CG   1 
ATOM   3470  C CD   . PRO   A  1 238 ? 35.990 -5.634  -15.430 1.00 21.75  ? 264  PRO   A CD   1 
ATOM   3471  H HA   . PRO   A  1 238 ? 39.013 -4.330  -15.400 0.00 23.49  ? 264  PRO   A HA   1 
ATOM   3472  H HB2  . PRO   A  1 238 ? 37.281 -2.936  -16.902 0.00 23.65  ? 264  PRO   A HB2  1 
ATOM   3473  H HB3  . PRO   A  1 238 ? 37.815 -4.579  -17.362 0.00 23.70  ? 264  PRO   A HB3  1 
ATOM   3474  H HG2  . PRO   A  1 238 ? 35.263 -3.705  -16.039 0.00 24.22  ? 264  PRO   A HG2  1 
ATOM   3475  H HG3  . PRO   A  1 238 ? 35.512 -4.864  -17.379 0.00 24.04  ? 264  PRO   A HG3  1 
ATOM   3476  H HD2  . PRO   A  1 238 ? 35.181 -5.571  -14.705 0.00 22.74  ? 264  PRO   A HD2  1 
ATOM   3477  H HD3  . PRO   A  1 238 ? 35.977 -6.583  -15.964 0.00 22.60  ? 264  PRO   A HD3  1 
ATOM   3478  N N    . PHE   A  1 239 ? 37.427 -3.251  -13.013 1.00 23.73  ? 265  PHE   A N    1 
ATOM   3479  C CA   . PHE   A  1 239 ? 37.200 -2.213  -11.998 1.00 24.65  ? 265  PHE   A CA   1 
ATOM   3480  C C    . PHE   A  1 239 ? 37.549 -2.797  -10.612 1.00 24.66  ? 265  PHE   A C    1 
ATOM   3481  O O    . PHE   A  1 239 ? 37.625 -4.026  -10.484 1.00 23.80  ? 265  PHE   A O    1 
ATOM   3482  C CB   . PHE   A  1 239 ? 35.730 -1.723  -12.021 1.00 25.08  ? 265  PHE   A CB   1 
ATOM   3483  C CG   . PHE   A  1 239 ? 34.731 -2.851  -11.901 1.00 26.53  ? 265  PHE   A CG   1 
ATOM   3484  C CD1  . PHE   A  1 239 ? 34.329 -3.563  -13.014 1.00 27.76  ? 265  PHE   A CD1  1 
ATOM   3485  C CD2  . PHE   A  1 239 ? 34.255 -3.245  -10.667 1.00 27.60  ? 265  PHE   A CD2  1 
ATOM   3486  C CE1  . PHE   A  1 239 ? 33.467 -4.648  -12.894 1.00 28.26  ? 265  PHE   A CE1  1 
ATOM   3487  C CE2  . PHE   A  1 239 ? 33.382 -4.317  -10.554 1.00 28.38  ? 265  PHE   A CE2  1 
ATOM   3488  C CZ   . PHE   A  1 239 ? 32.983 -4.999  -11.672 1.00 28.14  ? 265  PHE   A CZ   1 
ATOM   3489  H H    . PHE   A  1 239 ? 37.328 -4.186  -12.632 0.00 25.60  ? 265  PHE   A H    1 
ATOM   3490  H HA   . PHE   A  1 239 ? 37.858 -1.372  -12.207 0.00 26.73  ? 265  PHE   A HA   1 
ATOM   3491  H HB2  . PHE   A  1 239 ? 35.572 -1.042  -11.187 0.00 27.40  ? 265  PHE   A HB2  1 
ATOM   3492  H HB3  . PHE   A  1 239 ? 35.544 -1.208  -12.962 0.00 26.94  ? 265  PHE   A HB3  1 
ATOM   3493  H HD1  . PHE   A  1 239 ? 34.710 -3.293  -13.984 0.00 29.95  ? 265  PHE   A HD1  1 
ATOM   3494  H HD2  . PHE   A  1 239 ? 34.566 -2.713  -9.784  0.00 30.81  ? 265  PHE   A HD2  1 
ATOM   3495  H HE1  . PHE   A  1 239 ? 33.142 -5.179  -13.773 0.00 30.72  ? 265  PHE   A HE1  1 
ATOM   3496  H HE2  . PHE   A  1 239 ? 32.999 -4.597  -9.589  0.00 31.88  ? 265  PHE   A HE2  1 
ATOM   3497  H HZ   . PHE   A  1 239 ? 32.293 -5.821  -11.579 0.00 31.15  ? 265  PHE   A HZ   1 
ATOM   3498  N N    . PRO   A  1 240 ? 37.782 -1.970  -9.564  1.00 25.86  ? 266  PRO   A N    1 
ATOM   3499  C CA   . PRO   A  1 240 ? 38.065 -2.539  -8.232  1.00 27.02  ? 266  PRO   A CA   1 
ATOM   3500  C C    . PRO   A  1 240 ? 36.845 -3.321  -7.742  1.00 28.30  ? 266  PRO   A C    1 
ATOM   3501  O O    . PRO   A  1 240 ? 35.746 -2.780  -7.687  1.00 29.06  ? 266  PRO   A O    1 
ATOM   3502  C CB   . PRO   A  1 240 ? 38.349 -1.305  -7.369  1.00 27.75  ? 266  PRO   A CB   1 
ATOM   3503  C CG   . PRO   A  1 240 ? 38.679 -0.238  -8.332  1.00 27.81  ? 266  PRO   A CG   1 
ATOM   3504  C CD   . PRO   A  1 240 ? 37.770 -0.498  -9.503  1.00 25.79  ? 266  PRO   A CD   1 
ATOM   3505  H HA   . PRO   A  1 240 ? 38.946 -3.178  -8.264  0.00 30.86  ? 266  PRO   A HA   1 
ATOM   3506  H HB2  . PRO   A  1 240 ? 37.470 -1.037  -6.785  0.00 32.03  ? 266  PRO   A HB2  1 
ATOM   3507  H HB3  . PRO   A  1 240 ? 39.194 -1.507  -6.713  0.00 32.22  ? 266  PRO   A HB3  1 
ATOM   3508  H HG2  . PRO   A  1 240 ? 38.540 0.743   -7.885  0.00 31.84  ? 266  PRO   A HG2  1 
ATOM   3509  H HG3  . PRO   A  1 240 ? 39.717 -0.357  -8.639  0.00 31.71  ? 266  PRO   A HG3  1 
ATOM   3510  H HD2  . PRO   A  1 240 ? 36.766 -0.128  -9.300  0.00 28.84  ? 266  PRO   A HD2  1 
ATOM   3511  H HD3  . PRO   A  1 240 ? 38.196 -0.044  -10.396 0.00 28.61  ? 266  PRO   A HD3  1 
ATOM   3512  N N    . CYS   A  1 241 ? 37.022 -4.609  -7.497  1.00 28.64  ? 267  CYS   A N    1 
ATOM   3513  C CA   . CYS   A  1 241 ? 35.935 -5.531  -7.206  1.00 29.29  ? 267  CYS   A CA   1 
ATOM   3514  C C    . CYS   A  1 241 ? 36.171 -6.225  -5.870  1.00 30.33  ? 267  CYS   A C    1 
ATOM   3515  O O    . CYS   A  1 241 ? 37.221 -6.828  -5.685  1.00 30.60  ? 267  CYS   A O    1 
ATOM   3516  C CB   . CYS   A  1 241 ? 35.847 -6.540  -8.351  1.00 29.32  ? 267  CYS   A CB   1 
ATOM   3517  S SG   . CYS   A  1 241 ? 34.359 -7.566  -8.340  1.00 31.28  ? 267  CYS   A SG   1 
ATOM   3518  H H    . CYS   A  1 241 ? 37.931 -5.061  -7.485  0.00 33.07  ? 267  CYS   A H    1 
ATOM   3519  H HA   . CYS   A  1 241 ? 34.982 -5.008  -7.155  0.00 33.76  ? 267  CYS   A HA   1 
ATOM   3520  H HB2  . CYS   A  1 241 ? 35.860 -5.994  -9.292  0.00 33.27  ? 267  CYS   A HB2  1 
ATOM   3521  H HB3  . CYS   A  1 241 ? 36.713 -7.200  -8.302  0.00 33.74  ? 267  CYS   A HB3  1 
ATOM   3522  N N    . VAL   A  1 242 ? 35.193 -6.160  -4.953  1.00 30.95  ? 268  VAL   A N    1 
ATOM   3523  C CA   . VAL   A  1 242 ? 35.291 -6.809  -3.644  1.00 31.30  ? 268  VAL   A CA   1 
ATOM   3524  C C    . VAL   A  1 242 ? 34.236 -7.916  -3.613  1.00 30.55  ? 268  VAL   A C    1 
ATOM   3525  O O    . VAL   A  1 242 ? 33.041 -7.604  -3.585  1.00 30.16  ? 268  VAL   A O    1 
ATOM   3526  C CB   . VAL   A  1 242 ? 35.057 -5.813  -2.476  1.00 32.71  ? 268  VAL   A CB   1 
ATOM   3527  C CG1  . VAL   A  1 242 ? 35.128 -6.535  -1.127  1.00 33.57  ? 268  VAL   A CG1  1 
ATOM   3528  C CG2  . VAL   A  1 242 ? 36.057 -4.660  -2.527  1.00 33.10  ? 268  VAL   A CG2  1 
ATOM   3529  H H    . VAL   A  1 242 ? 34.314 -5.669  -5.086  0.00 36.44  ? 268  VAL   A H    1 
ATOM   3530  H HA   . VAL   A  1 242 ? 36.283 -7.232  -3.497  0.00 37.68  ? 268  VAL   A HA   1 
ATOM   3531  H HB   . VAL   A  1 242 ? 34.060 -5.383  -2.570  0.00 39.40  ? 268  VAL   A HB   1 
ATOM   3532  H HG11 . VAL   A  1 242 ? 35.302 -5.804  -0.338  0.00 41.40  ? 268  VAL   A HG11 1 
ATOM   3533  H HG12 . VAL   A  1 242 ? 34.184 -7.045  -0.936  0.00 41.20  ? 268  VAL   A HG12 1 
ATOM   3534  H HG13 . VAL   A  1 242 ? 35.943 -7.257  -1.149  0.00 41.27  ? 268  VAL   A HG13 1 
ATOM   3535  H HG21 . VAL   A  1 242 ? 35.880 -3.997  -1.681  0.00 40.24  ? 268  VAL   A HG21 1 
ATOM   3536  H HG22 . VAL   A  1 242 ? 37.067 -5.065  -2.480  0.00 40.11  ? 268  VAL   A HG22 1 
ATOM   3537  H HG23 . VAL   A  1 242 ? 35.920 -4.105  -3.453  0.00 39.59  ? 268  VAL   A HG23 1 
ATOM   3538  N N    . PRO   A  1 243 ? 34.627 -9.198  -3.628  1.00 30.22  ? 269  PRO   A N    1 
ATOM   3539  C CA   . PRO   A  1 243 ? 33.611 -10.257 -3.576  1.00 30.23  ? 269  PRO   A CA   1 
ATOM   3540  C C    . PRO   A  1 243 ? 33.039 -10.440 -2.183  1.00 30.38  ? 269  PRO   A C    1 
ATOM   3541  O O    . PRO   A  1 243 ? 33.654 -10.032 -1.194  1.00 30.84  ? 269  PRO   A O    1 
ATOM   3542  C CB   . PRO   A  1 243 ? 34.382 -11.513 -3.986  1.00 31.00  ? 269  PRO   A CB   1 
ATOM   3543  C CG   . PRO   A  1 243 ? 35.792 -11.241 -3.641  1.00 31.86  ? 269  PRO   A CG   1 
ATOM   3544  C CD   . PRO   A  1 243 ? 35.996 -9.752  -3.637  1.00 30.22  ? 269  PRO   A CD   1 
ATOM   3545  H HA   . PRO   A  1 243 ? 32.806 -10.081 -4.287  0.00 36.30  ? 269  PRO   A HA   1 
ATOM   3546  H HB2  . PRO   A  1 243 ? 34.010 -12.357 -3.410  0.00 37.96  ? 269  PRO   A HB2  1 
ATOM   3547  H HB3  . PRO   A  1 243 ? 34.267 -11.690 -5.054  0.00 37.29  ? 269  PRO   A HB3  1 
ATOM   3548  H HG2  . PRO   A  1 243 ? 36.005 -11.647 -2.654  0.00 39.28  ? 269  PRO   A HG2  1 
ATOM   3549  H HG3  . PRO   A  1 243 ? 36.440 -11.708 -4.381  0.00 38.72  ? 269  PRO   A HG3  1 
ATOM   3550  H HD2  . PRO   A  1 243 ? 36.534 -9.446  -2.741  0.00 36.97  ? 269  PRO   A HD2  1 
ATOM   3551  H HD3  . PRO   A  1 243 ? 36.523 -9.445  -4.539  0.00 36.33  ? 269  PRO   A HD3  1 
ATOM   3552  N N    . CYS   A  1 244 ? 31.899 -11.130 -2.093  1.00 30.05  ? 270  CYS   A N    1 
ATOM   3553  C CA   . CYS   A  1 244 ? 31.355 -11.521 -0.797  1.00 30.37  ? 270  CYS   A CA   1 
ATOM   3554  C C    . CYS   A  1 244 ? 32.309 -12.584 -0.200  1.00 32.10  ? 270  CYS   A C    1 
ATOM   3555  O O    . CYS   A  1 244 ? 33.065 -13.207 -0.950  1.00 31.89  ? 270  CYS   A O    1 
ATOM   3556  C CB   . CYS   A  1 244 ? 29.925 -12.035 -0.930  1.00 29.42  ? 270  CYS   A CB   1 
ATOM   3557  S SG   . CYS   A  1 244 ? 28.700 -10.707 -1.069  1.00 28.97  ? 270  CYS   A SG   1 
ATOM   3558  H H    . CYS   A  1 244 ? 31.346 -11.418 -2.893  0.00 36.76  ? 270  CYS   A H    1 
ATOM   3559  H HA   . CYS   A  1 244 ? 31.338 -10.660 -0.130  0.00 38.03  ? 270  CYS   A HA   1 
ATOM   3560  H HB2  . CYS   A  1 244 ? 29.836 -12.671 -1.809  0.00 36.61  ? 270  CYS   A HB2  1 
ATOM   3561  H HB3  . CYS   A  1 244 ? 29.682 -12.612 -0.039  0.00 37.25  ? 270  CYS   A HB3  1 
ATOM   3562  N N    . ASP   A  1 245 ? 32.358 -12.734 1.128   1.00 33.42  ? 271  ASP   A N    1 
ATOM   3563  C CA   . ASP   A  1 245 ? 33.315 -13.655 1.766   1.00 35.49  ? 271  ASP   A CA   1 
ATOM   3564  C C    . ASP   A  1 245 ? 33.306 -15.071 1.151   1.00 35.90  ? 271  ASP   A C    1 
ATOM   3565  O O    . ASP   A  1 245 ? 32.243 -15.643 0.950   1.00 36.24  ? 271  ASP   A O    1 
ATOM   3566  C CB   . ASP   A  1 245 ? 33.102 -13.682 3.288   1.00 38.98  ? 271  ASP   A CB   1 
ATOM   3567  C CG   . ASP   A  1 245 ? 33.502 -12.379 3.993   1.00 46.60  ? 271  ASP   A CG   1 
ATOM   3568  O OD1  . ASP   A  1 245 ? 34.020 -11.455 3.309   1.00 47.11  ? 271  ASP   A OD1  1 
ATOM   3569  O OD2  . ASP   A  1 245 ? 33.308 -12.287 5.225   1.00 49.91  ? 271  ASP   A OD2  1 
ATOM   3570  H H    . ASP   A  1 245 ? 31.740 -12.254 1.775   0.00 42.72  ? 271  ASP   A H    1 
ATOM   3571  H HA   . ASP   A  1 245 ? 34.311 -13.251 1.596   0.00 45.46  ? 271  ASP   A HA   1 
ATOM   3572  H HB2  . ASP   A  1 245 ? 32.049 -13.874 3.490   0.00 50.43  ? 271  ASP   A HB2  1 
ATOM   3573  H HB3  . ASP   A  1 245 ? 33.704 -14.485 3.711   0.00 50.76  ? 271  ASP   A HB3  1 
ATOM   3574  N N    . GLY   A  1 246 ? 34.481 -15.539 0.730   1.00 36.00  ? 272  GLY   A N    1 
ATOM   3575  C CA   . GLY   A  1 246 ? 34.635 -16.820 0.047   1.00 36.47  ? 272  GLY   A CA   1 
ATOM   3576  C C    . GLY   A  1 246 ? 34.078 -16.844 -1.372  1.00 36.36  ? 272  GLY   A C    1 
ATOM   3577  O O    . GLY   A  1 246 ? 33.788 -17.915 -1.912  1.00 36.98  ? 272  GLY   A O    1 
ATOM   3578  H H    . GLY   A  1 246 ? 35.367 -15.058 0.854   0.00 46.25  ? 272  GLY   A H    1 
ATOM   3579  H HA2  . GLY   A  1 246 ? 35.692 -17.076 0.000   0.00 47.01  ? 272  GLY   A HA2  1 
ATOM   3580  H HA3  . GLY   A  1 246 ? 34.125 -17.591 0.623   0.00 47.28  ? 272  GLY   A HA3  1 
ATOM   3581  N N    . GLY   A  1 247 ? 33.929 -15.674 -1.989  1.00 35.44  ? 273  GLY   A N    1 
ATOM   3582  C CA   . GLY   A  1 247 ? 33.314 -15.560 -3.312  1.00 34.44  ? 273  GLY   A CA   1 
ATOM   3583  C C    . GLY   A  1 247 ? 31.867 -16.029 -3.326  1.00 32.96  ? 273  GLY   A C    1 
ATOM   3584  O O    . GLY   A  1 247 ? 31.371 -16.454 -4.374  1.00 32.32  ? 273  GLY   A O    1 
ATOM   3585  H H    . GLY   A  1 247 ? 34.237 -14.779 -1.623  0.00 44.46  ? 273  GLY   A H    1 
ATOM   3586  H HA2  . GLY   A  1 247 ? 33.335 -14.525 -3.647  0.00 42.44  ? 273  GLY   A HA2  1 
ATOM   3587  H HA3  . GLY   A  1 247 ? 33.878 -16.162 -4.023  0.00 42.75  ? 273  GLY   A HA3  1 
ATOM   3588  N N    . ALA   A  1 248 ? 31.182 -15.974 -2.149  1.00 31.67  ? 274  ALA   A N    1 
ATOM   3589  C CA   . ALA   A  1 248 ? 29.817 -16.468 -1.971  1.00 30.62  ? 274  ALA   A CA   1 
ATOM   3590  C C    . ALA   A  1 248 ? 28.791 -15.766 -2.860  1.00 29.14  ? 274  ALA   A C    1 
ATOM   3591  O O    . ALA   A  1 248 ? 28.970 -14.620 -3.243  1.00 28.57  ? 274  ALA   A O    1 
ATOM   3592  C CB   . ALA   A  1 248 ? 29.395 -16.337 -0.507  1.00 30.82  ? 274  ALA   A CB   1 
ATOM   3593  H H    . ALA   A  1 248 ? 31.555 -15.551 -1.306  0.00 40.12  ? 274  ALA   A H    1 
ATOM   3594  H HA   . ALA   A  1 248 ? 29.810 -17.526 -2.226  0.00 39.03  ? 274  ALA   A HA   1 
ATOM   3595  H HB1  . ALA   A  1 248 ? 28.378 -16.714 -0.403  0.00 39.71  ? 274  ALA   A HB1  1 
ATOM   3596  H HB2  . ALA   A  1 248 ? 30.076 -16.921 0.110   0.00 39.94  ? 274  ALA   A HB2  1 
ATOM   3597  H HB3  . ALA   A  1 248 ? 29.440 -15.289 -0.215  0.00 39.41  ? 274  ALA   A HB3  1 
ATOM   3598  N N    . SER   A  1 249 ? 27.703 -16.480 -3.150  1.00 28.22  ? 275  SER   A N    1 
ATOM   3599  C CA   . SER   A  1 249 ? 26.574 -15.991 -3.929  1.00 27.82  ? 275  SER   A CA   1 
ATOM   3600  C C    . SER   A  1 249 ? 25.764 -14.988 -3.114  1.00 26.98  ? 275  SER   A C    1 
ATOM   3601  O O    . SER   A  1 249 ? 25.784 -15.018 -1.875  1.00 26.42  ? 275  SER   A O    1 
ATOM   3602  C CB   . SER   A  1 249 ? 25.659 -17.168 -4.268  1.00 29.91  ? 275  SER   A CB   1 
ATOM   3603  O OG   . SER   A  1 249 ? 24.528 -16.787 -5.026  1.00 33.14  ? 275  SER   A OG   1 
ATOM   3604  H H    . SER   A  1 249 ? 27.601 -17.432 -2.814  0.00 35.97  ? 275  SER   A H    1 
ATOM   3605  H HA   . SER   A  1 249 ? 26.893 -15.533 -4.861  0.00 34.39  ? 275  SER   A HA   1 
ATOM   3606  H HB2  . SER   A  1 249 ? 26.231 -17.886 -4.853  0.00 37.54  ? 275  SER   A HB2  1 
ATOM   3607  H HB3  . SER   A  1 249 ? 25.334 -17.636 -3.340  0.00 38.01  ? 275  SER   A HB3  1 
ATOM   3608  H HG   . SER   A  1 249 ? 23.746 -16.600 -4.442  0.00 41.43  ? 275  SER   A HG   1 
ATOM   3609  N N    . ILE   A  1 250 ? 24.939 -14.169 -3.802  1.00 26.28  ? 276  ILE   A N    1 
ATOM   3610  C CA   . ILE   A  1 250 ? 23.932 -13.343 -3.126  1.00 26.01  ? 276  ILE   A CA   1 
ATOM   3611  C C    . ILE   A  1 250 ? 22.909 -14.354 -2.546  1.00 25.96  ? 276  ILE   A C    1 
ATOM   3612  O O    . ILE   A  1 250 ? 22.655 -15.396 -3.167  1.00 25.93  ? 276  ILE   A O    1 
ATOM   3613  C CB   . ILE   A  1 250 ? 23.222 -12.368 -4.102  1.00 26.24  ? 276  ILE   A CB   1 
ATOM   3614  C CG1  . ILE   A  1 250 ? 22.386 -11.322 -3.327  1.00 26.99  ? 276  ILE   A CG1  1 
ATOM   3615  C CG2  . ILE   A  1 250 ? 22.336 -13.129 -5.128  1.00 26.52  ? 276  ILE   A CG2  1 
ATOM   3616  C CD1  . ILE   A  1 250 ? 21.763 -10.224 -4.222  1.00 26.63  ? 276  ILE   A CD1  1 
ATOM   3617  H H    . ILE   A  1 250 ? 24.959 -14.061 -4.811  0.00 32.38  ? 276  ILE   A H    1 
ATOM   3618  H HA   . ILE   A  1 250 ? 24.387 -12.776 -2.315  0.00 32.65  ? 276  ILE   A HA   1 
ATOM   3619  H HB   . ILE   A  1 250 ? 23.997 -11.829 -4.643  0.00 32.06  ? 276  ILE   A HB   1 
ATOM   3620  H HG12 . ILE   A  1 250 ? 21.569 -11.828 -2.815  0.00 33.85  ? 276  ILE   A HG12 1 
ATOM   3621  H HG13 . ILE   A  1 250 ? 23.029 -10.831 -2.598  0.00 33.57  ? 276  ILE   A HG13 1 
ATOM   3622  H HG21 . ILE   A  1 250 ? 21.910 -12.423 -5.840  0.00 32.42  ? 276  ILE   A HG21 1 
ATOM   3623  H HG22 . ILE   A  1 250 ? 22.955 -13.851 -5.657  0.00 32.60  ? 276  ILE   A HG22 1 
ATOM   3624  H HG23 . ILE   A  1 250 ? 21.522 -13.645 -4.624  0.00 33.06  ? 276  ILE   A HG23 1 
ATOM   3625  H HD11 . ILE   A  1 250 ? 21.464 -9.384  -3.597  0.00 32.85  ? 276  ILE   A HD11 1 
ATOM   3626  H HD12 . ILE   A  1 250 ? 22.499 -9.907  -4.959  0.00 32.34  ? 276  ILE   A HD12 1 
ATOM   3627  H HD13 . ILE   A  1 250 ? 20.891 -10.636 -4.728  0.00 32.76  ? 276  ILE   A HD13 1 
ATOM   3628  N N    . ASN   A  1 251 ? 22.393 -14.084 -1.359  1.00 25.78  ? 277  ASN   A N    1 
ATOM   3629  C CA   . ASN   A  1 251 ? 21.455 -14.995 -0.704  1.00 27.09  ? 277  ASN   A CA   1 
ATOM   3630  C C    . ASN   A  1 251 ? 20.060 -14.424 -0.851  1.00 27.15  ? 277  ASN   A C    1 
ATOM   3631  O O    . ASN   A  1 251 ? 19.739 -13.486 -0.149  1.00 27.39  ? 277  ASN   A O    1 
ATOM   3632  C CB   . ASN   A  1 251 ? 21.847 -15.155 0.768   1.00 29.35  ? 277  ASN   A CB   1 
ATOM   3633  C CG   . ASN   A  1 251 ? 21.000 -16.142 1.526   1.00 34.89  ? 277  ASN   A CG   1 
ATOM   3634  O OD1  . ASN   A  1 251 ? 19.952 -16.611 1.057   1.00 37.03  ? 277  ASN   A OD1  1 
ATOM   3635  N ND2  . ASN   A  1 251 ? 21.439 -16.477 2.726   1.00 35.75  ? 277  ASN   A ND2  1 
ATOM   3636  H H    . ASN   A  1 251 ? 22.592 -13.244 -0.825  0.00 33.16  ? 277  ASN   A H    1 
ATOM   3637  H HA   . ASN   A  1 251 ? 21.476 -15.985 -1.158  0.00 35.33  ? 277  ASN   A HA   1 
ATOM   3638  H HB2  . ASN   A  1 251 ? 22.876 -15.511 0.808   0.00 38.46  ? 277  ASN   A HB2  1 
ATOM   3639  H HB3  . ASN   A  1 251 ? 21.778 -14.191 1.269   0.00 38.48  ? 277  ASN   A HB3  1 
ATOM   3640  H HD21 . ASN   A  1 251 ? 20.914 -17.135 3.292   0.00 47.68  ? 277  ASN   A HD21 1 
ATOM   3641  H HD22 . ASN   A  1 251 ? 22.297 -16.072 3.087   0.00 47.19  ? 277  ASN   A HD22 1 
ATOM   3642  N N    . ILE   A  1 252 ? 19.254 -14.943 -1.792  1.00 27.16  ? 278  ILE   A N    1 
ATOM   3643  C CA   . ILE   A  1 252 ? 17.900 -14.450 -2.008  1.00 27.86  ? 278  ILE   A CA   1 
ATOM   3644  C C    . ILE   A  1 252 ? 16.911 -15.439 -1.417  1.00 29.57  ? 278  ILE   A C    1 
ATOM   3645  O O    . ILE   A  1 252 ? 16.858 -16.586 -1.861  1.00 30.92  ? 278  ILE   A O    1 
ATOM   3646  C CB   . ILE   A  1 252 ? 17.596 -14.172 -3.510  1.00 27.69  ? 278  ILE   A CB   1 
ATOM   3647  C CG1  . ILE   A  1 252 ? 18.510 -13.071 -4.071  1.00 28.03  ? 278  ILE   A CG1  1 
ATOM   3648  C CG2  . ILE   A  1 252 ? 16.120 -13.775 -3.695  1.00 27.90  ? 278  ILE   A CG2  1 
ATOM   3649  C CD1  . ILE   A  1 252 ? 18.651 -13.086 -5.639  1.00 28.61  ? 278  ILE   A CD1  1 
ATOM   3650  H H    . ILE   A  1 252 ? 19.513 -15.704 -2.412  0.00 35.24  ? 278  ILE   A H    1 
ATOM   3651  H HA   . ILE   A  1 252 ? 17.778 -13.511 -1.473  0.00 36.27  ? 278  ILE   A HA   1 
ATOM   3652  H HB   . ILE   A  1 252 ? 17.777 -15.086 -4.074  0.00 35.57  ? 278  ILE   A HB   1 
ATOM   3653  H HG12 . ILE   A  1 252 ? 18.088 -12.107 -3.795  0.00 35.46  ? 278  ILE   A HG12 1 
ATOM   3654  H HG13 . ILE   A  1 252 ? 19.505 -13.167 -3.639  0.00 35.41  ? 278  ILE   A HG13 1 
ATOM   3655  H HG21 . ILE   A  1 252 ? 16.003 -13.220 -4.624  0.00 35.70  ? 278  ILE   A HG21 1 
ATOM   3656  H HG22 . ILE   A  1 252 ? 15.510 -14.676 -3.744  0.00 36.35  ? 278  ILE   A HG22 1 
ATOM   3657  H HG23 . ILE   A  1 252 ? 15.810 -13.157 -2.854  0.00 36.23  ? 278  ILE   A HG23 1 
ATOM   3658  H HD11 . ILE   A  1 252 ? 19.462 -12.418 -5.922  0.00 35.32  ? 278  ILE   A HD11 1 
ATOM   3659  H HD12 . ILE   A  1 252 ? 18.874 -14.101 -5.967  0.00 35.72  ? 278  ILE   A HD12 1 
ATOM   3660  H HD13 . ILE   A  1 252 ? 17.723 -12.744 -6.095  0.00 35.68  ? 278  ILE   A HD13 1 
ATOM   3661  N N    . ASP   A  1 253 ? 16.096 -14.995 -0.446  1.00 29.24  ? 279  ASP   A N    1 
ATOM   3662  C CA   . ASP   A  1 253 ? 15.089 -15.854 0.171   1.00 29.64  ? 279  ASP   A CA   1 
ATOM   3663  C C    . ASP   A  1 253 ? 14.104 -16.388 -0.879  1.00 29.87  ? 279  ASP   A C    1 
ATOM   3664  O O    . ASP   A  1 253 ? 13.770 -15.682 -1.830  1.00 29.64  ? 279  ASP   A O    1 
ATOM   3665  C CB   . ASP   A  1 253 ? 14.329 -15.091 1.261   1.00 31.19  ? 279  ASP   A CB   1 
ATOM   3666  C CG   . ASP   A  1 253 ? 13.367 -15.970 2.034   1.00 36.04  ? 279  ASP   A CG   1 
ATOM   3667  O OD1  . ASP   A  1 253 ? 13.830 -16.687 2.946   1.00 37.37  ? 279  ASP   A OD1  1 
ATOM   3668  O OD2  . ASP   A  1 253 ? 12.152 -15.968 1.700   1.00 35.94  ? 279  ASP   A OD2  1 
ATOM   3669  H H    . ASP   A  1 253 ? 16.101 -14.051 -0.073  0.00 38.83  ? 279  ASP   A H    1 
ATOM   3670  H HA   . ASP   A  1 253 ? 15.596 -16.697 0.638   0.00 40.21  ? 279  ASP   A HA   1 
ATOM   3671  H HB2  . ASP   A  1 253 ? 15.043 -14.675 1.970   0.00 42.23  ? 279  ASP   A HB2  1 
ATOM   3672  H HB3  . ASP   A  1 253 ? 13.753 -14.291 0.797   0.00 42.07  ? 279  ASP   A HB3  1 
ATOM   3673  N N    . ARG   A  1 254 ? 13.692 -17.654 -0.723  1.00 30.18  ? 280  ARG   A N    1 
ATOM   3674  C CA   . ARG   A  1 254 ? 12.745 -18.345 -1.614  1.00 31.24  ? 280  ARG   A CA   1 
ATOM   3675  C C    . ARG   A  1 254 ? 11.497 -17.490 -1.937  1.00 30.33  ? 280  ARG   A C    1 
ATOM   3676  O O    . ARG   A  1 254 ? 11.029 -17.515 -3.079  1.00 30.98  ? 280  ARG   A O    1 
ATOM   3677  C CB   . ARG   A  1 254 ? 12.390 -19.726 -0.990  1.00 34.57  ? 280  ARG   A CB   1 
ATOM   3678  C CG   . ARG   A  1 254 ? 10.961 -20.277 -1.173  1.00 41.73  ? 280  ARG   A CG   1 
ATOM   3679  C CD   . ARG   A  1 254 ? 10.762 -20.810 -2.572  1.00 47.58  ? 280  ARG   A CD   1 
ATOM   3680  N NE   . ARG   A  1 254 ? 9.390  -21.278 -2.813  1.00 51.98  ? 280  ARG   A NE   1 
ATOM   3681  C CZ   . ARG   A  1 254 ? 8.360  -20.506 -3.166  1.00 53.82  ? 280  ARG   A CZ   1 
ATOM   3682  N NH1  . ARG   A  1 254 ? 8.518  -19.192 -3.306  1.00 51.91  ? 280  ARG   A NH1  1 
ATOM   3683  N NH2  . ARG   A  1 254 ? 7.161  -21.041 -3.370  1.00 54.59  ? 280  ARG   A NH2  1 
ATOM   3684  H H    . ARG   A  1 254 ? 14.048 -18.241 0.023   0.00 41.39  ? 280  ARG   A H    1 
ATOM   3685  H HA   . ARG   A  1 254 ? 13.247 -18.543 -2.561  0.00 42.16  ? 280  ARG   A HA   1 
ATOM   3686  H HB2  . ARG   A  1 254 ? 13.061 -20.466 -1.423  0.00 47.08  ? 280  ARG   A HB2  1 
ATOM   3687  H HB3  . ARG   A  1 254 ? 12.558 -19.678 0.084   0.00 47.46  ? 280  ARG   A HB3  1 
ATOM   3688  H HG2  . ARG   A  1 254 ? 10.828 -21.115 -0.492  0.00 56.75  ? 280  ARG   A HG2  1 
ATOM   3689  H HG3  . ARG   A  1 254 ? 10.207 -19.519 -0.967  0.00 56.36  ? 280  ARG   A HG3  1 
ATOM   3690  H HD2  . ARG   A  1 254 ? 11.033 -20.051 -3.305  0.00 62.59  ? 280  ARG   A HD2  1 
ATOM   3691  H HD3  . ARG   A  1 254 ? 11.416 -21.671 -2.697  0.00 63.12  ? 280  ARG   A HD3  1 
ATOM   3692  H HE   . ARG   A  1 254 ? 9.226  -22.276 -2.727  0.00 69.27  ? 280  ARG   A HE   1 
ATOM   3693  H HH11 . ARG   A  1 254 ? 9.405  -18.727 -3.147  0.00 68.01  ? 280  ARG   A HH11 1 
ATOM   3694  H HH12 . ARG   A  1 254 ? 7.716  -18.625 -3.561  0.00 68.46  ? 280  ARG   A HH12 1 
ATOM   3695  H HH21 . ARG   A  1 254 ? 7.022  -22.042 -3.269  0.00 72.95  ? 280  ARG   A HH21 1 
ATOM   3696  H HH22 . ARG   A  1 254 ? 6.375  -20.454 -3.631  0.00 72.64  ? 280  ARG   A HH22 1 
ATOM   3697  N N    . PHE   A  1 255 ? 11.011 -16.688 -0.959  1.00 29.24  ? 281  PHE   A N    1 
ATOM   3698  C CA   . PHE   A  1 255 ? 9.814  -15.847 -1.116  1.00 29.48  ? 281  PHE   A CA   1 
ATOM   3699  C C    . PHE   A  1 255 ? 10.076 -14.350 -1.373  1.00 27.67  ? 281  PHE   A C    1 
ATOM   3700  O O    . PHE   A  1 255 ? 9.120  -13.587 -1.380  1.00 26.66  ? 281  PHE   A O    1 
ATOM   3701  C CB   . PHE   A  1 255 ? 8.951  -15.978 0.152   1.00 31.06  ? 281  PHE   A CB   1 
ATOM   3702  C CG   . PHE   A  1 255 ? 8.445  -17.370 0.412   1.00 33.13  ? 281  PHE   A CG   1 
ATOM   3703  C CD1  . PHE   A  1 255 ? 7.654  -18.018 -0.517  1.00 34.75  ? 281  PHE   A CD1  1 
ATOM   3704  C CD2  . PHE   A  1 255 ? 8.699  -18.002 1.615   1.00 34.90  ? 281  PHE   A CD2  1 
ATOM   3705  C CE1  . PHE   A  1 255 ? 7.128  -19.275 -0.250  1.00 35.61  ? 281  PHE   A CE1  1 
ATOM   3706  C CE2  . PHE   A  1 255 ? 8.186  -19.265 1.876   1.00 35.99  ? 281  PHE   A CE2  1 
ATOM   3707  C CZ   . PHE   A  1 255 ? 7.436  -19.910 0.922   1.00 35.91  ? 281  PHE   A CZ   1 
ATOM   3708  H H    . PHE   A  1 255 ? 11.430 -16.604 -0.039  0.00 40.57  ? 281  PHE   A H    1 
ATOM   3709  H HA   . PHE   A  1 255 ? 9.219  -16.208 -1.954  0.00 40.89  ? 281  PHE   A HA   1 
ATOM   3710  H HB2  . PHE   A  1 255 ? 9.568  -15.700 1.005   0.00 43.47  ? 281  PHE   A HB2  1 
ATOM   3711  H HB3  . PHE   A  1 255 ? 8.083  -15.326 0.084   0.00 43.60  ? 281  PHE   A HB3  1 
ATOM   3712  H HD1  . PHE   A  1 255 ? 7.425  -17.531 -1.454  0.00 48.24  ? 281  PHE   A HD1  1 
ATOM   3713  H HD2  . PHE   A  1 255 ? 9.292  -17.511 2.367   0.00 49.05  ? 281  PHE   A HD2  1 
ATOM   3714  H HE1  . PHE   A  1 255 ? 6.529  -19.772 -0.996  0.00 50.28  ? 281  PHE   A HE1  1 
ATOM   3715  H HE2  . PHE   A  1 255 ? 8.403  -19.747 2.813   0.00 51.34  ? 281  PHE   A HE2  1 
ATOM   3716  H HZ   . PHE   A  1 255 ? 7.020  -20.883 1.126   0.00 51.44  ? 281  PHE   A HZ   1 
ATOM   3717  N N    . ALA   A  1 256 ? 11.330 -13.927 -1.606  1.00 27.05  ? 282  ALA   A N    1 
ATOM   3718  C CA   . ALA   A  1 256 ? 11.658 -12.512 -1.837  1.00 27.13  ? 282  ALA   A CA   1 
ATOM   3719  C C    . ALA   A  1 256 ? 10.882 -11.817 -2.963  1.00 26.87  ? 282  ALA   A C    1 
ATOM   3720  O O    . ALA   A  1 256 ? 10.676 -10.605 -2.886  1.00 26.97  ? 282  ALA   A O    1 
ATOM   3721  C CB   . ALA   A  1 256 ? 13.149 -12.356 -2.087  1.00 27.07  ? 282  ALA   A CB   1 
ATOM   3722  H H    . ALA   A  1 256 ? 12.143 -14.534 -1.638  0.00 36.82  ? 282  ALA   A H    1 
ATOM   3723  H HA   . ALA   A  1 256 ? 11.437 -11.953 -0.930  0.00 36.90  ? 282  ALA   A HA   1 
ATOM   3724  H HB1  . ALA   A  1 256 ? 13.328 -11.347 -2.455  0.00 35.73  ? 282  ALA   A HB1  1 
ATOM   3725  H HB2  . ALA   A  1 256 ? 13.690 -12.518 -1.155  0.00 36.20  ? 282  ALA   A HB2  1 
ATOM   3726  H HB3  . ALA   A  1 256 ? 13.470 -13.078 -2.837  0.00 35.84  ? 282  ALA   A HB3  1 
ATOM   3727  N N    . PHE   A  1 257 ? 10.529 -12.533 -4.031  1.00 27.10  ? 283  PHE   A N    1 
ATOM   3728  C CA   . PHE   A  1 257 ? 9.827  -11.919 -5.166  1.00 28.07  ? 283  PHE   A CA   1 
ATOM   3729  C C    . PHE   A  1 257 ? 8.399  -12.465 -5.327  1.00 28.12  ? 283  PHE   A C    1 
ATOM   3730  O O    . PHE   A  1 257 ? 7.813  -12.316 -6.406  1.00 27.75  ? 283  PHE   A O    1 
ATOM   3731  C CB   . PHE   A  1 257 ? 10.622 -12.170 -6.459  1.00 29.27  ? 283  PHE   A CB   1 
ATOM   3732  C CG   . PHE   A  1 257 ? 12.114 -11.903 -6.403  1.00 31.37  ? 283  PHE   A CG   1 
ATOM   3733  C CD1  . PHE   A  1 257 ? 12.615 -10.779 -5.765  1.00 32.99  ? 283  PHE   A CD1  1 
ATOM   3734  C CD2  . PHE   A  1 257 ? 13.001 -12.708 -7.089  1.00 33.10  ? 283  PHE   A CD2  1 
ATOM   3735  C CE1  . PHE   A  1 257 ? 13.980 -10.504 -5.772  1.00 33.99  ? 283  PHE   A CE1  1 
ATOM   3736  C CE2  . PHE   A  1 257 ? 14.358 -12.421 -7.112  1.00 34.09  ? 283  PHE   A CE2  1 
ATOM   3737  C CZ   . PHE   A  1 257 ? 14.842 -11.326 -6.444  1.00 33.90  ? 283  PHE   A CZ   1 
ATOM   3738  H H    . PHE   A  1 257 ? 10.715 -13.524 -4.153  0.00 36.41  ? 283  PHE   A H    1 
ATOM   3739  H HA   . PHE   A  1 257 ? 9.751  -10.839 -5.044  0.00 37.27  ? 283  PHE   A HA   1 
ATOM   3740  H HB2  . PHE   A  1 257 ? 10.486 -13.212 -6.741  0.00 38.39  ? 283  PHE   A HB2  1 
ATOM   3741  H HB3  . PHE   A  1 257 ? 10.215 -11.528 -7.240  0.00 38.11  ? 283  PHE   A HB3  1 
ATOM   3742  H HD1  . PHE   A  1 257 ? 11.949 -10.117 -5.238  0.00 42.32  ? 283  PHE   A HD1  1 
ATOM   3743  H HD2  . PHE   A  1 257 ? 12.623 -13.546 -7.643  0.00 42.15  ? 283  PHE   A HD2  1 
ATOM   3744  H HE1  . PHE   A  1 257 ? 14.359 -9.645  -5.243  0.00 42.76  ? 283  PHE   A HE1  1 
ATOM   3745  H HE2  . PHE   A  1 257 ? 15.035 -13.073 -7.637  0.00 42.57  ? 283  PHE   A HE2  1 
ATOM   3746  H HZ   . PHE   A  1 257 ? 15.898 -11.120 -6.441  0.00 42.11  ? 283  PHE   A HZ   1 
ATOM   3747  N N    . GLN   A  1 258 ? 7.813  -13.061 -4.255  1.00 27.97  ? 284  GLN   A N    1 
ATOM   3748  C CA   . GLN   A  1 258 ? 6.486  -13.670 -4.348  1.00 28.40  ? 284  GLN   A CA   1 
ATOM   3749  C C    . GLN   A  1 258 ? 5.363  -12.688 -4.701  1.00 29.65  ? 284  GLN   A C    1 
ATOM   3750  O O    . GLN   A  1 258 ? 4.363  -13.115 -5.267  1.00 30.19  ? 284  GLN   A O    1 
ATOM   3751  C CB   . GLN   A  1 258 ? 6.144  -14.449 -3.054  1.00 29.04  ? 284  GLN   A CB   1 
ATOM   3752  C CG   . GLN   A  1 258 ? 5.791  -13.565 -1.865  1.00 30.93  ? 284  GLN   A CG   1 
ATOM   3753  C CD   . GLN   A  1 258 ? 5.573  -14.369 -0.600  1.00 32.85  ? 284  GLN   A CD   1 
ATOM   3754  O OE1  . GLN   A  1 258 ? 5.234  -15.567 -0.636  1.00 32.11  ? 284  GLN   A OE1  1 
ATOM   3755  N NE2  . GLN   A  1 258 ? 5.758  -13.722 0.548   1.00 32.36  ? 284  GLN   A NE2  1 
ATOM   3756  H H    . GLN   A  1 258 ? 8.216  -13.114 -3.325  0.00 38.47  ? 284  GLN   A H    1 
ATOM   3757  H HA   . GLN   A  1 258 ? 6.527  -14.401 -5.154  0.00 39.36  ? 284  GLN   A HA   1 
ATOM   3758  H HB2  . GLN   A  1 258 ? 5.287  -15.088 -3.261  0.00 41.24  ? 284  GLN   A HB2  1 
ATOM   3759  H HB3  . GLN   A  1 258 ? 7.000  -15.060 -2.773  0.00 40.70  ? 284  GLN   A HB3  1 
ATOM   3760  H HG2  . GLN   A  1 258 ? 6.606  -12.864 -1.692  0.00 43.04  ? 284  GLN   A HG2  1 
ATOM   3761  H HG3  . GLN   A  1 258 ? 4.867  -13.022 -2.061  0.00 43.66  ? 284  GLN   A HG3  1 
ATOM   3762  H HE21 . GLN   A  1 258 ? 6.023  -12.742 0.548   0.00 45.62  ? 284  GLN   A HE21 1 
ATOM   3763  H HE22 . GLN   A  1 258 ? 5.621  -14.209 1.428   0.00 46.28  ? 284  GLN   A HE22 1 
ATOM   3764  N N    . ASN   A  1 259 ? 5.494  -11.406 -4.329  1.00 30.42  ? 285  ASN   A N    1 
ATOM   3765  C CA   . ASN   A  1 259 ? 4.480  -10.382 -4.622  1.00 31.83  ? 285  ASN   A CA   1 
ATOM   3766  C C    . ASN   A  1 259 ? 4.879  -9.449  -5.771  1.00 30.49  ? 285  ASN   A C    1 
ATOM   3767  O O    . ASN   A  1 259 ? 4.171  -8.470  -5.998  1.00 31.10  ? 285  ASN   A O    1 
ATOM   3768  C CB   . ASN   A  1 259 ? 4.209  -9.533  -3.379  1.00 36.39  ? 285  ASN   A CB   1 
ATOM   3769  C CG   . ASN   A  1 259 ? 3.647  -10.313 -2.232  1.00 45.86  ? 285  ASN   A CG   1 
ATOM   3770  O OD1  . ASN   A  1 259 ? 2.691  -11.081 -2.399  1.00 49.51  ? 285  ASN   A OD1  1 
ATOM   3771  N ND2  . ASN   A  1 259 ? 4.190  -10.112 -1.025  1.00 47.93  ? 285  ASN   A ND2  1 
ATOM   3772  H H    . ASN   A  1 259 ? 6.287  -11.038 -3.812  0.00 41.73  ? 285  ASN   A H    1 
ATOM   3773  H HA   . ASN   A  1 259 ? 3.539  -10.851 -4.902  0.00 44.30  ? 285  ASN   A HA   1 
ATOM   3774  H HB2  . ASN   A  1 259 ? 5.145  -9.070  -3.068  0.00 49.35  ? 285  ASN   A HB2  1 
ATOM   3775  H HB3  . ASN   A  1 259 ? 3.482  -8.757  -3.615  0.00 49.92  ? 285  ASN   A HB3  1 
ATOM   3776  H HD21 . ASN   A  1 259 ? 3.834  -10.623 -0.224  0.00 64.70  ? 285  ASN   A HD21 1 
ATOM   3777  H HD22 . ASN   A  1 259 ? 4.948  -9.448  -0.901  0.00 63.93  ? 285  ASN   A HD22 1 
ATOM   3778  N N    . LEU   A  1 260 ? 5.988  -9.723  -6.492  1.00 29.00  ? 286  LEU   A N    1 
ATOM   3779  C CA   . LEU   A  1 260 ? 6.426  -8.863  -7.596  1.00 28.03  ? 286  LEU   A CA   1 
ATOM   3780  C C    . LEU   A  1 260 ? 5.796  -9.347  -8.911  1.00 26.92  ? 286  LEU   A C    1 
ATOM   3781  O O    . LEU   A  1 260 ? 6.489  -9.682  -9.868  1.00 25.64  ? 286  LEU   A O    1 
ATOM   3782  C CB   . LEU   A  1 260 ? 7.962  -8.826  -7.687  1.00 28.04  ? 286  LEU   A CB   1 
ATOM   3783  C CG   . LEU   A  1 260 ? 8.694  -8.266  -6.453  1.00 30.25  ? 286  LEU   A CG   1 
ATOM   3784  C CD1  . LEU   A  1 260 ? 10.200 -8.237  -6.674  1.00 31.11  ? 286  LEU   A CD1  1 
ATOM   3785  C CD2  . LEU   A  1 260 ? 8.220  -6.853  -6.112  1.00 31.05  ? 286  LEU   A CD2  1 
ATOM   3786  H H    . LEU   A  1 260 ? 6.600  -10.519 -6.345  0.00 39.22  ? 286  LEU   A H    1 
ATOM   3787  H HA   . LEU   A  1 260 ? 6.078  -7.842  -7.445  0.00 37.78  ? 286  LEU   A HA   1 
ATOM   3788  H HB2  . LEU   A  1 260 ? 8.325  -9.840  -7.848  0.00 36.98  ? 286  LEU   A HB2  1 
ATOM   3789  H HB3  . LEU   A  1 260 ? 8.244  -8.201  -8.533  0.00 36.71  ? 286  LEU   A HB3  1 
ATOM   3790  H HG   . LEU   A  1 260 ? 8.491  -8.908  -5.597  0.00 40.00  ? 286  LEU   A HG   1 
ATOM   3791  H HD11 . LEU   A  1 260 ? 10.690 -7.932  -5.750  0.00 40.13  ? 286  LEU   A HD11 1 
ATOM   3792  H HD12 . LEU   A  1 260 ? 10.535 -9.232  -6.961  0.00 40.00  ? 286  LEU   A HD12 1 
ATOM   3793  H HD13 . LEU   A  1 260 ? 10.427 -7.525  -7.466  0.00 39.77  ? 286  LEU   A HD13 1 
ATOM   3794  H HD21 . LEU   A  1 260 ? 8.924  -6.402  -5.415  0.00 40.69  ? 286  LEU   A HD21 1 
ATOM   3795  H HD22 . LEU   A  1 260 ? 8.169  -6.264  -7.026  0.00 40.57  ? 286  LEU   A HD22 1 
ATOM   3796  H HD23 . LEU   A  1 260 ? 7.236  -6.912  -5.649  0.00 41.30  ? 286  LEU   A HD23 1 
ATOM   3797  N N    . THR   A  1 261 ? 4.463  -9.331  -8.941  1.00 26.90  ? 287  THR   A N    1 
ATOM   3798  C CA   . THR   A  1 261 ? 3.652  -9.805  -10.066 1.00 27.37  ? 287  THR   A CA   1 
ATOM   3799  C C    . THR   A  1 261 ? 3.819  -8.980  -11.344 1.00 26.00  ? 287  THR   A C    1 
ATOM   3800  O O    . THR   A  1 261 ? 3.612  -9.507  -12.440 1.00 26.40  ? 287  THR   A O    1 
ATOM   3801  C CB   . THR   A  1 261 ? 2.164  -9.833  -9.656  1.00 30.65  ? 287  THR   A CB   1 
ATOM   3802  O OG1  . THR   A  1 261 ? 2.016  -10.650 -8.483  1.00 32.69  ? 287  THR   A OG1  1 
ATOM   3803  C CG2  . THR   A  1 261 ? 1.273  -10.349 -10.759 1.00 32.09  ? 287  THR   A CG2  1 
ATOM   3804  H H    . THR   A  1 261 ? 3.916  -8.971  -8.164  0.00 37.30  ? 287  THR   A H    1 
ATOM   3805  H HA   . THR   A  1 261 ? 3.950  -10.828 -10.292 0.00 37.63  ? 287  THR   A HA   1 
ATOM   3806  H HB   . THR   A  1 261 ? 1.848  -8.818  -9.419  0.00 42.53  ? 287  THR   A HB   1 
ATOM   3807  H HG1  . THR   A  1 261 ? 1.109  -10.532 -8.096  0.00 45.74  ? 287  THR   A HG1  1 
ATOM   3808  H HG21 . THR   A  1 261 ? 0.323  -10.679 -10.342 0.00 45.04  ? 287  THR   A HG21 1 
ATOM   3809  H HG22 . THR   A  1 261 ? 1.070  -9.560  -11.482 0.00 44.37  ? 287  THR   A HG22 1 
ATOM   3810  H HG23 . THR   A  1 261 ? 1.751  -11.186 -11.265 0.00 44.23  ? 287  THR   A HG23 1 
ATOM   3811  N N    . GLN   A  1 262 ? 4.183  -7.708  -11.218 1.00 24.48  ? 288  GLN   A N    1 
ATOM   3812  C CA   . GLN   A  1 262 ? 4.329  -6.834  -12.372 1.00 24.49  ? 288  GLN   A CA   1 
ATOM   3813  C C    . GLN   A  1 262 ? 5.755  -6.708  -12.908 1.00 24.35  ? 288  GLN   A C    1 
ATOM   3814  O O    . GLN   A  1 262 ? 5.969  -5.931  -13.844 1.00 24.98  ? 288  GLN   A O    1 
ATOM   3815  C CB   . GLN   A  1 262 ? 3.745  -5.447  -12.019 1.00 25.60  ? 288  GLN   A CB   1 
ATOM   3816  C CG   . GLN   A  1 262 ? 2.277  -5.513  -11.550 1.00 27.89  ? 288  GLN   A CG   1 
ATOM   3817  C CD   . GLN   A  1 262 ? 1.399  -6.222  -12.550 1.00 31.17  ? 288  GLN   A CD   1 
ATOM   3818  O OE1  . GLN   A  1 262 ? 0.810  -7.274  -12.273 1.00 33.83  ? 288  GLN   A OE1  1 
ATOM   3819  N NE2  . GLN   A  1 262 ? 1.328  -5.675  -13.738 1.00 30.28  ? 288  GLN   A NE2  1 
ATOM   3820  H H    . GLN   A  1 262 ? 4.375  -7.241  -10.338 0.00 33.66  ? 288  GLN   A H    1 
ATOM   3821  H HA   . GLN   A  1 262 ? 3.746  -7.226  -13.203 0.00 33.50  ? 288  GLN   A HA   1 
ATOM   3822  H HB2  . GLN   A  1 262 ? 4.335  -5.011  -11.215 0.00 34.78  ? 288  GLN   A HB2  1 
ATOM   3823  H HB3  . GLN   A  1 262 ? 3.781  -4.805  -12.898 0.00 34.78  ? 288  GLN   A HB3  1 
ATOM   3824  H HG2  . GLN   A  1 262 ? 2.218  -6.045  -10.601 0.00 38.67  ? 288  GLN   A HG2  1 
ATOM   3825  H HG3  . GLN   A  1 262 ? 1.900  -4.498  -11.434 0.00 38.67  ? 288  GLN   A HG3  1 
ATOM   3826  H HE21 . GLN   A  1 262 ? 1.786  -4.786  -13.911 0.00 41.25  ? 288  GLN   A HE21 1 
ATOM   3827  H HE22 . GLN   A  1 262 ? 0.749  -6.098  -14.456 0.00 41.75  ? 288  GLN   A HE22 1 
ATOM   3828  N N    . LEU   A  1 263 ? 6.714  -7.491  -12.386 1.00 23.38  ? 289  LEU   A N    1 
ATOM   3829  C CA   . LEU   A  1 263 ? 8.092  -7.392  -12.852 1.00 24.14  ? 289  LEU   A CA   1 
ATOM   3830  C C    . LEU   A  1 263 ? 8.239  -7.809  -14.327 1.00 23.84  ? 289  LEU   A C    1 
ATOM   3831  O O    . LEU   A  1 263 ? 7.721  -8.849  -14.732 1.00 23.65  ? 289  LEU   A O    1 
ATOM   3832  C CB   . LEU   A  1 263 ? 9.058  -8.202  -11.947 1.00 24.86  ? 289  LEU   A CB   1 
ATOM   3833  C CG   . LEU   A  1 263 ? 10.470 -7.621  -11.769 1.00 26.34  ? 289  LEU   A CG   1 
ATOM   3834  C CD1  . LEU   A  1 263 ? 10.443 -6.368  -10.868 1.00 26.55  ? 289  LEU   A CD1  1 
ATOM   3835  C CD2  . LEU   A  1 263 ? 11.413 -8.652  -11.170 1.00 26.90  ? 289  LEU   A CD2  1 
ATOM   3836  H H    . LEU   A  1 263 ? 6.565  -8.202  -11.678 0.00 31.20  ? 289  LEU   A H    1 
ATOM   3837  H HA   . LEU   A  1 263 ? 8.358  -6.340  -12.787 0.00 31.07  ? 289  LEU   A HA   1 
ATOM   3838  H HB2  . LEU   A  1 263 ? 8.630  -8.286  -10.948 0.00 32.27  ? 289  LEU   A HB2  1 
ATOM   3839  H HB3  . LEU   A  1 263 ? 9.168  -9.196  -12.376 0.00 31.90  ? 289  LEU   A HB3  1 
ATOM   3840  H HG   . LEU   A  1 263 ? 10.860 -7.329  -12.744 0.00 32.82  ? 289  LEU   A HG   1 
ATOM   3841  H HD11 . LEU   A  1 263 ? 11.471 -6.084  -10.649 0.00 33.17  ? 289  LEU   A HD11 1 
ATOM   3842  H HD12 . LEU   A  1 263 ? 9.956  -5.542  -11.384 0.00 33.54  ? 289  LEU   A HD12 1 
ATOM   3843  H HD13 . LEU   A  1 263 ? 9.916  -6.596  -9.943  0.00 33.89  ? 289  LEU   A HD13 1 
ATOM   3844  H HD21 . LEU   A  1 263 ? 12.400 -8.199  -11.096 0.00 33.34  ? 289  LEU   A HD21 1 
ATOM   3845  H HD22 . LEU   A  1 263 ? 11.055 -8.933  -10.180 0.00 34.04  ? 289  LEU   A HD22 1 
ATOM   3846  H HD23 . LEU   A  1 263 ? 11.450 -9.524  -11.820 0.00 33.65  ? 289  LEU   A HD23 1 
ATOM   3847  N N    . ARG   A  1 264 ? 8.849  -6.927  -15.135 1.00 23.84  ? 290  ARG   A N    1 
ATOM   3848  C CA   . ARG   A  1 264 ? 9.176  -7.142  -16.552 1.00 23.70  ? 290  ARG   A CA   1 
ATOM   3849  C C    . ARG   A  1 264 ? 10.706 -7.260  -16.714 1.00 23.06  ? 290  ARG   A C    1 
ATOM   3850  O O    . ARG   A  1 264 ? 11.152 -7.942  -17.627 1.00 22.75  ? 290  ARG   A O    1 
ATOM   3851  C CB   . ARG   A  1 264 ? 8.676  -5.984  -17.456 1.00 24.59  ? 290  ARG   A CB   1 
ATOM   3852  C CG   . ARG   A  1 264 ? 7.301  -6.180  -18.099 1.00 26.24  ? 290  ARG   A CG   1 
ATOM   3853  C CD   . ARG   A  1 264 ? 6.196  -6.009  -17.088 1.00 27.96  ? 290  ARG   A CD   1 
ATOM   3854  N NE   . ARG   A  1 264 ? 4.861  -6.195  -17.670 1.00 29.77  ? 290  ARG   A NE   1 
ATOM   3855  C CZ   . ARG   A  1 264 ? 3.724  -6.084  -16.986 1.00 32.56  ? 290  ARG   A CZ   1 
ATOM   3856  N NH1  . ARG   A  1 264 ? 3.746  -5.782  -15.692 1.00 31.10  ? 290  ARG   A NH1  1 
ATOM   3857  N NH2  . ARG   A  1 264 ? 2.552  -6.268  -17.594 1.00 32.55  ? 290  ARG   A NH2  1 
ATOM   3858  H H    . ARG   A  1 264 ? 9.140  -6.008  -14.819 0.00 30.07  ? 290  ARG   A H    1 
ATOM   3859  H HA   . ARG   A  1 264 ? 8.732  -8.070  -16.906 0.00 29.94  ? 290  ARG   A HA   1 
ATOM   3860  H HB2  . ARG   A  1 264 ? 8.630  -5.071  -16.864 0.00 30.89  ? 290  ARG   A HB2  1 
ATOM   3861  H HB3  . ARG   A  1 264 ? 9.393  -5.848  -18.263 0.00 30.45  ? 290  ARG   A HB3  1 
ATOM   3862  H HG2  . ARG   A  1 264 ? 7.162  -5.437  -18.882 0.00 33.28  ? 290  ARG   A HG2  1 
ATOM   3863  H HG3  . ARG   A  1 264 ? 7.232  -7.184  -18.514 0.00 33.38  ? 290  ARG   A HG3  1 
ATOM   3864  H HD2  . ARG   A  1 264 ? 6.322  -6.744  -16.295 0.00 36.05  ? 290  ARG   A HD2  1 
ATOM   3865  H HD3  . ARG   A  1 264 ? 6.246  -5.003  -16.676 0.00 35.97  ? 290  ARG   A HD3  1 
ATOM   3866  H HE   . ARG   A  1 264 ? 4.809  -6.405  -18.661 0.00 38.66  ? 290  ARG   A HE   1 
ATOM   3867  H HH11 . ARG   A  1 264 ? 4.618  -5.661  -15.187 0.00 40.68  ? 290  ARG   A HH11 1 
ATOM   3868  H HH12 . ARG   A  1 264 ? 2.877  -5.754  -15.170 0.00 41.53  ? 290  ARG   A HH12 1 
ATOM   3869  H HH21 . ARG   A  1 264 ? 2.524  -6.493  -18.583 0.00 43.14  ? 290  ARG   A HH21 1 
ATOM   3870  H HH22 . ARG   A  1 264 ? 1.683  -6.212  -17.073 0.00 43.69  ? 290  ARG   A HH22 1 
ATOM   3871  N N    . TYR   A  1 265 ? 11.511 -6.558  -15.880 1.00 22.80  ? 291  TYR   A N    1 
ATOM   3872  C CA   . TYR   A  1 265 ? 12.975 -6.561  -15.987 1.00 22.50  ? 291  TYR   A CA   1 
ATOM   3873  C C    . TYR   A  1 265 ? 13.590 -6.967  -14.669 1.00 21.68  ? 291  TYR   A C    1 
ATOM   3874  O O    . TYR   A  1 265 ? 13.270 -6.368  -13.647 1.00 21.34  ? 291  TYR   A O    1 
ATOM   3875  C CB   . TYR   A  1 265 ? 13.487 -5.151  -16.321 1.00 23.43  ? 291  TYR   A CB   1 
ATOM   3876  C CG   . TYR   A  1 265 ? 13.007 -4.631  -17.657 1.00 25.93  ? 291  TYR   A CG   1 
ATOM   3877  C CD1  . TYR   A  1 265 ? 11.745 -4.079  -17.798 1.00 27.71  ? 291  TYR   A CD1  1 
ATOM   3878  C CD2  . TYR   A  1 265 ? 13.835 -4.654  -18.771 1.00 27.89  ? 291  TYR   A CD2  1 
ATOM   3879  C CE1  . TYR   A  1 265 ? 11.294 -3.611  -19.028 1.00 29.24  ? 291  TYR   A CE1  1 
ATOM   3880  C CE2  . TYR   A  1 265 ? 13.393 -4.197  -20.007 1.00 29.19  ? 291  TYR   A CE2  1 
ATOM   3881  C CZ   . TYR   A  1 265 ? 12.111 -3.700  -20.137 1.00 30.72  ? 291  TYR   A CZ   1 
ATOM   3882  O OH   . TYR   A  1 265 ? 11.676 -3.212  -21.348 1.00 34.35  ? 291  TYR   A OH   1 
ATOM   3883  H H    . TYR   A  1 265 ? 11.180 -5.963  -15.128 0.00 28.01  ? 291  TYR   A H    1 
ATOM   3884  H HA   . TYR   A  1 265 ? 13.315 -7.239  -16.766 0.00 26.76  ? 291  TYR   A HA   1 
ATOM   3885  H HB2  . TYR   A  1 265 ? 13.139 -4.461  -15.554 0.00 27.95  ? 291  TYR   A HB2  1 
ATOM   3886  H HB3  . TYR   A  1 265 ? 14.576 -5.168  -16.334 0.00 27.40  ? 291  TYR   A HB3  1 
ATOM   3887  H HD1  . TYR   A  1 265 ? 11.088 -4.045  -16.948 0.00 33.62  ? 291  TYR   A HD1  1 
ATOM   3888  H HD2  . TYR   A  1 265 ? 14.820 -5.082  -18.689 0.00 32.38  ? 291  TYR   A HD2  1 
ATOM   3889  H HE1  . TYR   A  1 265 ? 10.299 -3.210  -19.121 0.00 35.52  ? 291  TYR   A HE1  1 
ATOM   3890  H HE2  . TYR   A  1 265 ? 14.049 -4.256  -20.861 0.00 33.94  ? 291  TYR   A HE2  1 
ATOM   3891  H HH   . TYR   A  1 265 ? 12.321 -3.423  -22.072 0.00 40.64  ? 291  TYR   A HH   1 
ATOM   3892  N N    . LEU   A  1 266 ? 14.518 -7.929  -14.694 1.00 21.03  ? 292  LEU   A N    1 
ATOM   3893  C CA   . LEU   A  1 266 ? 15.221 -8.357  -13.501 1.00 20.64  ? 292  LEU   A CA   1 
ATOM   3894  C C    . LEU   A  1 266 ? 16.690 -8.463  -13.850 1.00 19.52  ? 292  LEU   A C    1 
ATOM   3895  O O    . LEU   A  1 266 ? 17.049 -9.184  -14.789 1.00 19.44  ? 292  LEU   A O    1 
ATOM   3896  C CB   . LEU   A  1 266 ? 14.695 -9.717  -12.996 1.00 21.83  ? 292  LEU   A CB   1 
ATOM   3897  C CG   . LEU   A  1 266 ? 15.413 -10.322 -11.774 1.00 23.48  ? 292  LEU   A CG   1 
ATOM   3898  C CD1  . LEU   A  1 266 ? 15.381 -9.380  -10.556 1.00 23.74  ? 292  LEU   A CD1  1 
ATOM   3899  C CD2  . LEU   A  1 266 ? 14.805 -11.653 -11.421 1.00 24.24  ? 292  LEU   A CD2  1 
ATOM   3900  H H    . LEU   A  1 266 ? 14.804 -8.428  -15.530 0.00 24.81  ? 292  LEU   A H    1 
ATOM   3901  H HA   . LEU   A  1 266 ? 15.101 -7.617  -12.713 0.00 24.63  ? 292  LEU   A HA   1 
ATOM   3902  H HB2  . LEU   A  1 266 ? 13.646 -9.598  -12.730 0.00 26.71  ? 292  LEU   A HB2  1 
ATOM   3903  H HB3  . LEU   A  1 266 ? 14.780 -10.435 -13.811 0.00 26.29  ? 292  LEU   A HB3  1 
ATOM   3904  H HG   . LEU   A  1 266 ? 16.457 -10.510 -12.020 0.00 28.13  ? 292  LEU   A HG   1 
ATOM   3905  H HD11 . LEU   A  1 266 ? 15.814 -9.897  -9.700  0.00 29.00  ? 292  LEU   A HD11 1 
ATOM   3906  H HD12 . LEU   A  1 266 ? 15.972 -8.489  -10.765 0.00 28.58  ? 292  LEU   A HD12 1 
ATOM   3907  H HD13 . LEU   A  1 266 ? 14.351 -9.109  -10.333 0.00 29.19  ? 292  LEU   A HD13 1 
ATOM   3908  H HD21 . LEU   A  1 266 ? 15.248 -12.020 -10.496 0.00 29.90  ? 292  LEU   A HD21 1 
ATOM   3909  H HD22 . LEU   A  1 266 ? 13.729 -11.532 -11.302 0.00 30.09  ? 292  LEU   A HD22 1 
ATOM   3910  H HD23 . LEU   A  1 266 ? 15.017 -12.346 -12.234 0.00 29.68  ? 292  LEU   A HD23 1 
ATOM   3911  N N    . ASN   A  1 267 ? 17.536 -7.739  -13.123 1.00 18.56  ? 293  ASN   A N    1 
ATOM   3912  C CA   . ASN   A  1 267 ? 18.968 -7.785  -13.361 1.00 19.31  ? 293  ASN   A CA   1 
ATOM   3913  C C    . ASN   A  1 267 ? 19.691 -8.393  -12.168 1.00 19.79  ? 293  ASN   A C    1 
ATOM   3914  O O    . ASN   A  1 267 ? 19.778 -7.779  -11.110 1.00 19.65  ? 293  ASN   A O    1 
ATOM   3915  C CB   . ASN   A  1 267 ? 19.507 -6.385  -13.688 1.00 19.41  ? 293  ASN   A CB   1 
ATOM   3916  C CG   . ASN   A  1 267 ? 20.849 -6.383  -14.384 1.00 20.32  ? 293  ASN   A CG   1 
ATOM   3917  O OD1  . ASN   A  1 267 ? 21.587 -7.364  -14.326 1.00 19.66  ? 293  ASN   A OD1  1 
ATOM   3918  N ND2  . ASN   A  1 267 ? 21.276 -5.255  -14.941 1.00 21.14  ? 293  ASN   A ND2  1 
ATOM   3919  H H    . ASN   A  1 267 ? 17.269 -7.118  -12.366 0.00 21.58  ? 293  ASN   A H    1 
ATOM   3920  H HA   . ASN   A  1 267 ? 19.174 -8.415  -14.223 0.00 21.80  ? 293  ASN   A HA   1 
ATOM   3921  H HB2  . ASN   A  1 267 ? 18.755 -5.907  -14.314 0.00 21.78  ? 293  ASN   A HB2  1 
ATOM   3922  H HB3  . ASN   A  1 267 ? 19.650 -5.824  -12.767 0.00 21.86  ? 293  ASN   A HB3  1 
ATOM   3923  H HD21 . ASN   A  1 267 ? 22.191 -5.186  -15.373 0.00 22.90  ? 293  ASN   A HD21 1 
ATOM   3924  N N    . LEU   A  1 268 ? 20.202 -9.611  -12.345 1.00 20.04  ? 294  LEU   A N    1 
ATOM   3925  C CA   . LEU   A  1 268 ? 21.004 -10.307 -11.330 1.00 20.28  ? 294  LEU   A CA   1 
ATOM   3926  C C    . LEU   A  1 268 ? 22.418 -10.577 -11.871 1.00 19.39  ? 294  LEU   A C    1 
ATOM   3927  O O    . LEU   A  1 268 ? 23.050 -11.572 -11.493 1.00 19.54  ? 294  LEU   A O    1 
ATOM   3928  C CB   . LEU   A  1 268 ? 20.294 -11.608 -10.902 1.00 21.25  ? 294  LEU   A CB   1 
ATOM   3929  C CG   . LEU   A  1 268 ? 18.968 -11.426 -10.134 1.00 24.13  ? 294  LEU   A CG   1 
ATOM   3930  C CD1  . LEU   A  1 268 ? 18.176 -12.743 -10.104 1.00 24.93  ? 294  LEU   A CD1  1 
ATOM   3931  C CD2  . LEU   A  1 268 ? 19.215 -10.988 -8.702  1.00 24.82  ? 294  LEU   A CD2  1 
ATOM   3932  H H    . LEU   A  1 268 ? 20.080 -10.163 -13.189 0.00 22.89  ? 294  LEU   A H    1 
ATOM   3933  H HA   . LEU   A  1 268 ? 21.142 -9.674  -10.457 0.00 23.47  ? 294  LEU   A HA   1 
ATOM   3934  H HB2  . LEU   A  1 268 ? 20.066 -12.179 -11.801 0.00 24.93  ? 294  LEU   A HB2  1 
ATOM   3935  H HB3  . LEU   A  1 268 ? 20.952 -12.184 -10.253 0.00 25.09  ? 294  LEU   A HB3  1 
ATOM   3936  H HG   . LEU   A  1 268 ? 18.357 -10.672 -10.629 0.00 28.75  ? 294  LEU   A HG   1 
ATOM   3937  H HD11 . LEU   A  1 268 ? 17.279 -12.601 -9.503  0.00 30.51  ? 294  LEU   A HD11 1 
ATOM   3938  H HD12 . LEU   A  1 268 ? 17.904 -13.018 -11.122 0.00 30.09  ? 294  LEU   A HD12 1 
ATOM   3939  H HD13 . LEU   A  1 268 ? 18.800 -13.519 -9.660  0.00 30.30  ? 294  LEU   A HD13 1 
ATOM   3940  H HD21 . LEU   A  1 268 ? 18.258 -10.754 -8.237  0.00 30.17  ? 294  LEU   A HD21 1 
ATOM   3941  H HD22 . LEU   A  1 268 ? 19.687 -11.809 -8.165  0.00 30.05  ? 294  LEU   A HD22 1 
ATOM   3942  H HD23 . LEU   A  1 268 ? 19.863 -10.116 -8.672  0.00 29.65  ? 294  LEU   A HD23 1 
ATOM   3943  N N    . SER   A  1 269 ? 22.947 -9.664  -12.727 1.00 18.76  ? 295  SER   A N    1 
ATOM   3944  C CA   . SER   A  1 269 ? 24.290 -9.815  -13.250 1.00 19.22  ? 295  SER   A CA   1 
ATOM   3945  C C    . SER   A  1 269 ? 25.288 -9.654  -12.115 1.00 19.56  ? 295  SER   A C    1 
ATOM   3946  O O    . SER   A  1 269 ? 25.102 -8.822  -11.234 1.00 19.12  ? 295  SER   A O    1 
ATOM   3947  C CB   . SER   A  1 269 ? 24.599 -8.768  -14.321 1.00 20.44  ? 295  SER   A CB   1 
ATOM   3948  O OG   . SER   A  1 269 ? 23.738 -8.908  -15.437 1.00 23.13  ? 295  SER   A OG   1 
ATOM   3949  H H    . SER   A  1 269 ? 22.483 -8.822  -13.052 0.00 20.75  ? 295  SER   A H    1 
ATOM   3950  H HA   . SER   A  1 269 ? 24.398 -10.803 -13.694 0.00 21.16  ? 295  SER   A HA   1 
ATOM   3951  H HB2  . SER   A  1 269 ? 24.465 -7.775  -13.894 0.00 22.18  ? 295  SER   A HB2  1 
ATOM   3952  H HB3  . SER   A  1 269 ? 25.629 -8.893  -14.652 0.00 22.01  ? 295  SER   A HB3  1 
ATOM   3953  H HG   . SER   A  1 269 ? 22.834 -8.563  -15.215 0.00 25.50  ? 295  SER   A HG   1 
ATOM   3954  N N    . SER   A  1 270 ? 26.343 -10.429 -12.145 1.00 19.29  ? 296  SER   A N    1 
ATOM   3955  C CA   . SER   A  1 270 ? 27.411 -10.375 -11.164 1.00 19.84  ? 296  SER   A CA   1 
ATOM   3956  C C    . SER   A  1 270 ? 26.947 -10.424 -9.701  1.00 20.27  ? 296  SER   A C    1 
ATOM   3957  O O    . SER   A  1 270 ? 27.309 -9.585  -8.896  1.00 20.59  ? 296  SER   A O    1 
ATOM   3958  C CB   . SER   A  1 270 ? 28.306 -9.163  -11.422 1.00 21.09  ? 296  SER   A CB   1 
ATOM   3959  O OG   . SER   A  1 270 ? 29.593 -9.334  -10.844 1.00 22.38  ? 296  SER   A OG   1 
ATOM   3960  H H    . SER   A  1 270 ? 26.506 -11.131 -12.861 0.00 21.23  ? 296  SER   A H    1 
ATOM   3961  H HA   . SER   A  1 270 ? 27.998 -11.280 -11.323 0.00 22.13  ? 296  SER   A HA   1 
ATOM   3962  H HB2  . SER   A  1 270 ? 28.426 -9.047  -12.498 0.00 22.99  ? 296  SER   A HB2  1 
ATOM   3963  H HB3  . SER   A  1 270 ? 27.841 -8.267  -11.013 0.00 23.27  ? 296  SER   A HB3  1 
ATOM   3964  H HG   . SER   A  1 270 ? 30.153 -8.534  -11.023 0.00 24.72  ? 296  SER   A HG   1 
ATOM   3965  N N    . THR   A  1 271 ? 26.087 -11.365 -9.402  1.00 20.04  ? 297  THR   A N    1 
ATOM   3966  C CA   . THR   A  1 271 ? 25.673 -11.734 -8.050  1.00 20.32  ? 297  THR   A CA   1 
ATOM   3967  C C    . THR   A  1 271 ? 26.259 -13.103 -7.593  1.00 21.03  ? 297  THR   A C    1 
ATOM   3968  O O    . THR   A  1 271 ? 25.858 -13.625 -6.531  1.00 21.52  ? 297  THR   A O    1 
ATOM   3969  C CB   . THR   A  1 271 ? 24.154 -11.676 -7.951  1.00 21.30  ? 297  THR   A CB   1 
ATOM   3970  O OG1  . THR   A  1 271 ? 23.575 -12.628 -8.837  1.00 21.51  ? 297  THR   A OG1  1 
ATOM   3971  C CG2  . THR   A  1 271 ? 23.611 -10.283 -8.237  1.00 21.98  ? 297  THR   A CG2  1 
ATOM   3972  H H    . THR   A  1 271 ? 25.499 -11.763 -10.119 0.00 22.95  ? 297  THR   A H    1 
ATOM   3973  H HA   . THR   A  1 271 ? 26.052 -10.999 -7.343  0.00 23.83  ? 297  THR   A HA   1 
ATOM   3974  H HB   . THR   A  1 271 ? 23.868 -11.935 -6.934  0.00 25.51  ? 297  THR   A HB   1 
ATOM   3975  H HG1  . THR   A  1 271 ? 23.610 -12.313 -9.779  0.00 25.12  ? 297  THR   A HG1  1 
ATOM   3976  H HG21 . THR   A  1 271 ? 22.537 -10.262 -8.062  0.00 25.94  ? 297  THR   A HG21 1 
ATOM   3977  H HG22 . THR   A  1 271 ? 24.091 -9.558  -7.581  0.00 25.76  ? 297  THR   A HG22 1 
ATOM   3978  H HG23 . THR   A  1 271 ? 23.800 -10.002 -9.272  0.00 25.42  ? 297  THR   A HG23 1 
ATOM   3979  N N    . SER   A  1 272 ? 27.251 -13.638 -8.339  1.00 21.39  ? 298  SER   A N    1 
ATOM   3980  C CA   . SER   A  1 272 ? 27.930 -14.900 -8.073  1.00 22.49  ? 298  SER   A CA   1 
ATOM   3981  C C    . SER   A  1 272 ? 26.974 -16.082 -7.914  1.00 23.62  ? 298  SER   A C    1 
ATOM   3982  O O    . SER   A  1 272 ? 27.225 -16.964 -7.086  1.00 24.16  ? 298  SER   A O    1 
ATOM   3983  C CB   . SER   A  1 272 ? 28.858 -14.757 -6.864  1.00 23.61  ? 298  SER   A CB   1 
ATOM   3984  O OG   . SER   A  1 272 ? 29.918 -13.866 -7.168  1.00 25.55  ? 298  SER   A OG   1 
ATOM   3985  H H    . SER   A  1 272 ? 27.634 -13.193 -9.166  0.00 24.90  ? 298  SER   A H    1 
ATOM   3986  H HA   . SER   A  1 272 ? 28.543 -15.134 -8.943  0.00 26.66  ? 298  SER   A HA   1 
ATOM   3987  H HB2  . SER   A  1 272 ? 28.316 -14.309 -6.034  0.00 28.64  ? 298  SER   A HB2  1 
ATOM   3988  H HB3  . SER   A  1 272 ? 29.284 -15.718 -6.580  0.00 28.77  ? 298  SER   A HB3  1 
ATOM   3989  H HG   . SER   A  1 272 ? 29.593 -12.928 -7.164  0.00 30.30  ? 298  SER   A HG   1 
ATOM   3990  N N    . LEU   A  1 273 ? 25.874 -16.104 -8.692  1.00 23.31  ? 299  LEU   A N    1 
ATOM   3991  C CA   . LEU   A  1 273 ? 24.928 -17.200 -8.624  1.00 23.21  ? 299  LEU   A CA   1 
ATOM   3992  C C    . LEU   A  1 273 ? 25.441 -18.473 -9.288  1.00 23.75  ? 299  LEU   A C    1 
ATOM   3993  O O    . LEU   A  1 273 ? 25.946 -18.425 -10.412 1.00 23.29  ? 299  LEU   A O    1 
ATOM   3994  C CB   . LEU   A  1 273 ? 23.605 -16.821 -9.318  1.00 23.03  ? 299  LEU   A CB   1 
ATOM   3995  C CG   . LEU   A  1 273 ? 22.712 -15.827 -8.596  1.00 24.70  ? 299  LEU   A CG   1 
ATOM   3996  C CD1  . LEU   A  1 273 ? 21.671 -15.247 -9.570  1.00 25.44  ? 299  LEU   A CD1  1 
ATOM   3997  C CD2  . LEU   A  1 273 ? 22.041 -16.461 -7.370  1.00 24.82  ? 299  LEU   A CD2  1 
ATOM   3998  H H    . LEU   A  1 273 ? 25.560 -15.351 -9.293  0.00 27.82  ? 299  LEU   A H    1 
ATOM   3999  H HA   . LEU   A  1 273 ? 24.716 -17.401 -7.575  0.00 28.73  ? 299  LEU   A HA   1 
ATOM   4000  H HB2  . LEU   A  1 273 ? 23.829 -16.408 -10.301 0.00 27.69  ? 299  LEU   A HB2  1 
ATOM   4001  H HB3  . LEU   A  1 273 ? 23.025 -17.733 -9.454  0.00 28.33  ? 299  LEU   A HB3  1 
ATOM   4002  H HG   . LEU   A  1 273 ? 23.326 -15.000 -8.241  0.00 29.91  ? 299  LEU   A HG   1 
ATOM   4003  H HD11 . LEU   A  1 273 ? 21.018 -14.568 -9.023  0.00 30.86  ? 299  LEU   A HD11 1 
ATOM   4004  H HD12 . LEU   A  1 273 ? 22.185 -14.706 -10.362 0.00 30.40  ? 299  LEU   A HD12 1 
ATOM   4005  H HD13 . LEU   A  1 273 ? 21.090 -16.062 -9.997  0.00 30.97  ? 299  LEU   A HD13 1 
ATOM   4006  H HD21 . LEU   A  1 273 ? 21.278 -15.781 -6.996  0.00 30.85  ? 299  LEU   A HD21 1 
ATOM   4007  H HD22 . LEU   A  1 273 ? 21.583 -17.408 -7.656  0.00 31.04  ? 299  LEU   A HD22 1 
ATOM   4008  H HD23 . LEU   A  1 273 ? 22.784 -16.625 -6.589  0.00 30.95  ? 299  LEU   A HD23 1 
ATOM   4009  N N    A ARG   A  1 274 ? 25.309 -19.610 -8.589  0.50 23.83  ? 300  ARG   A N    1 
ATOM   4010  N N    B ARG   A  1 274 ? 25.303 -19.604 -8.582  0.50 23.86  ? 300  ARG   A N    1 
ATOM   4011  C CA   A ARG   A  1 274 ? 25.607 -20.953 -9.108  0.50 24.45  ? 300  ARG   A CA   1 
ATOM   4012  C CA   B ARG   A  1 274 ? 25.624 -20.952 -9.065  0.50 24.51  ? 300  ARG   A CA   1 
ATOM   4013  C C    A ARG   A  1 274 ? 24.279 -21.714 -9.360  0.50 25.85  ? 300  ARG   A C    1 
ATOM   4014  C C    B ARG   A  1 274 ? 24.320 -21.785 -9.261  0.50 25.81  ? 300  ARG   A C    1 
ATOM   4015  O O    A ARG   A  1 274 ? 24.224 -22.562 -10.251 0.50 26.24  ? 300  ARG   A O    1 
ATOM   4016  O O    B ARG   A  1 274 ? 24.325 -22.752 -10.020 0.50 26.14  ? 300  ARG   A O    1 
ATOM   4017  C CB   A ARG   A  1 274 ? 26.452 -21.771 -8.117  0.50 24.91  ? 300  ARG   A CB   1 
ATOM   4018  C CB   B ARG   A  1 274 ? 26.580 -21.656 -8.083  0.50 25.12  ? 300  ARG   A CB   1 
ATOM   4019  C CG   A ARG   A  1 274 ? 27.947 -21.476 -8.141  0.50 25.12  ? 300  ARG   A CG   1 
ATOM   4020  C CG   B ARG   A  1 274 ? 28.009 -21.140 -8.179  0.50 25.75  ? 300  ARG   A CG   1 
ATOM   4021  C CD   A ARG   A  1 274 ? 28.272 -20.164 -7.474  0.50 25.38  ? 300  ARG   A CD   1 
ATOM   4022  C CD   B ARG   A  1 274 ? 28.956 -21.697 -7.129  0.50 27.02  ? 300  ARG   A CD   1 
ATOM   4023  N NE   A ARG   A  1 274 ? 29.710 -20.005 -7.250  0.50 25.38  ? 300  ARG   A NE   1 
ATOM   4024  N NE   B ARG   A  1 274 ? 30.269 -21.039 -7.184  0.50 27.43  ? 300  ARG   A NE   1 
ATOM   4025  C CZ   A ARG   A  1 274 ? 30.254 -19.148 -6.388  0.50 25.28  ? 300  ARG   A CZ   1 
ATOM   4026  C CZ   B ARG   A  1 274 ? 31.221 -21.286 -8.085  0.50 26.42  ? 300  ARG   A CZ   1 
ATOM   4027  N NH1  A ARG   A  1 274 ? 31.577 -19.080 -6.255  0.50 25.30  ? 300  ARG   A NH1  1 
ATOM   4028  N NH1  B ARG   A  1 274 ? 32.373 -20.630 -8.037  0.50 25.97  ? 300  ARG   A NH1  1 
ATOM   4029  N NH2  A ARG   A  1 274 ? 29.483 -18.346 -5.656  0.50 22.48  ? 300  ARG   A NH2  1 
ATOM   4030  N NH2  B ARG   A  1 274 ? 31.020 -22.175 -9.054  0.50 24.60  ? 300  ARG   A NH2  1 
ATOM   4031  H H    A ARG   A  1 274 ? 24.990 -19.631 -7.626  0.00 30.08  ? 300  ARG   A H    1 
ATOM   4032  H H    B ARG   A  1 274 ? 24.964 -19.616 -7.626  0.00 30.11  ? 300  ARG   A H    1 
ATOM   4033  H HA   A ARG   A  1 274 ? 26.141 -20.893 -10.055 0.00 30.54  ? 300  ARG   A HA   1 
ATOM   4034  H HA   B ARG   A  1 274 ? 26.107 -20.897 -10.040 0.00 30.62  ? 300  ARG   A HA   1 
ATOM   4035  H HB2  A ARG   A  1 274 ? 26.085 -21.600 -7.106  0.00 32.07  ? 300  ARG   A HB2  1 
ATOM   4036  H HB2  B ARG   A  1 274 ? 26.231 -21.499 -7.063  0.00 32.30  ? 300  ARG   A HB2  1 
ATOM   4037  H HB3  A ARG   A  1 274 ? 26.333 -22.825 -8.364  0.00 32.17  ? 300  ARG   A HB3  1 
ATOM   4038  H HB3  B ARG   A  1 274 ? 26.593 -22.721 -8.308  0.00 32.38  ? 300  ARG   A HB3  1 
ATOM   4039  H HG2  A ARG   A  1 274 ? 28.466 -22.262 -7.595  0.00 32.32  ? 300  ARG   A HG2  1 
ATOM   4040  H HG2  B ARG   A  1 274 ? 28.404 -21.449 -9.145  0.00 32.38  ? 300  ARG   A HG2  1 
ATOM   4041  H HG3  A ARG   A  1 274 ? 28.295 -21.457 -9.172  0.00 31.63  ? 300  ARG   A HG3  1 
ATOM   4042  H HG3  B ARG   A  1 274 ? 28.008 -20.054 -8.099  0.00 32.20  ? 300  ARG   A HG3  1 
ATOM   4043  H HD2  A ARG   A  1 274 ? 27.924 -19.341 -8.097  0.00 31.54  ? 300  ARG   A HD2  1 
ATOM   4044  H HD2  B ARG   A  1 274 ? 28.534 -21.510 -6.143  0.00 34.73  ? 300  ARG   A HD2  1 
ATOM   4045  H HD3  A ARG   A  1 274 ? 27.764 -20.156 -6.511  0.00 32.23  ? 300  ARG   A HD3  1 
ATOM   4046  H HD3  B ARG   A  1 274 ? 29.084 -22.768 -7.277  0.00 34.85  ? 300  ARG   A HD3  1 
ATOM   4047  H HE   A ARG   A  1 274 ? 30.331 -20.603 -7.786  0.00 31.96  ? 300  ARG   A HE   1 
ATOM   4048  H HE   B ARG   A  1 274 ? 30.467 -20.351 -6.465  0.00 34.72  ? 300  ARG   A HE   1 
ATOM   4049  H HH11 A ARG   A  1 274 ? 32.178 -19.688 -6.802  0.00 31.86  ? 300  ARG   A HH11 1 
ATOM   4050  H HH11 B ARG   A  1 274 ? 32.543 -19.944 -7.307  0.00 32.63  ? 300  ARG   A HH11 1 
ATOM   4051  H HH12 A ARG   A  1 274 ? 31.993 -18.426 -5.599  0.00 31.82  ? 300  ARG   A HH12 1 
ATOM   4052  H HH12 B ARG   A  1 274 ? 33.097 -20.813 -8.725  0.00 32.54  ? 300  ARG   A HH12 1 
ATOM   4053  H HH21 A ARG   A  1 274 ? 28.471 -18.340 -5.726  0.00 28.39  ? 300  ARG   A HH21 1 
ATOM   4054  H HH21 B ARG   A  1 274 ? 30.157 -22.702 -9.134  0.00 31.42  ? 300  ARG   A HH21 1 
ATOM   4055  H HH22 A ARG   A  1 274 ? 29.921 -17.695 -5.012  0.00 28.39  ? 300  ARG   A HH22 1 
ATOM   4056  H HH22 B ARG   A  1 274 ? 31.754 -22.348 -9.733  0.00 31.14  ? 300  ARG   A HH22 1 
ATOM   4057  N N    . LYS   A  1 275 ? 23.219 -21.406 -8.582  1.00 26.43  ? 301  LYS   A N    1 
ATOM   4058  C CA   . LYS   A  1 275 ? 21.912 -22.037 -8.668  1.00 28.15  ? 301  LYS   A CA   1 
ATOM   4059  C C    . LYS   A  1 275 ? 20.865 -20.920 -8.784  1.00 28.49  ? 301  LYS   A C    1 
ATOM   4060  O O    . LYS   A  1 275 ? 21.002 -19.872 -8.163  1.00 28.87  ? 301  LYS   A O    1 
ATOM   4061  C CB   . LYS   A  1 275 ? 21.624 -22.827 -7.376  1.00 31.66  ? 301  LYS   A CB   1 
ATOM   4062  C CG   . LYS   A  1 275 ? 22.672 -23.881 -7.020  1.00 39.38  ? 301  LYS   A CG   1 
ATOM   4063  C CD   . LYS   A  1 275 ? 22.526 -25.162 -7.847  1.00 46.19  ? 301  LYS   A CD   1 
ATOM   4064  C CE   . LYS   A  1 275 ? 23.448 -26.249 -7.338  1.00 50.82  ? 301  LYS   A CE   1 
ATOM   4065  N NZ   . LYS   A  1 275 ? 23.167 -27.561 -7.976  1.00 53.70  ? 301  LYS   A NZ   1 
ATOM   4066  H H    . LYS   A  1 275 ? 23.208 -20.677 -7.876  0.00 33.66  ? 301  LYS   A H    1 
ATOM   4067  H HA   . LYS   A  1 275 ? 21.822 -22.703 -9.525  0.00 36.20  ? 301  LYS   A HA   1 
ATOM   4068  H HB2  . LYS   A  1 275 ? 21.572 -22.124 -6.547  0.00 40.97  ? 301  LYS   A HB2  1 
ATOM   4069  H HB3  . LYS   A  1 275 ? 20.666 -23.333 -7.486  0.00 41.29  ? 301  LYS   A HB3  1 
ATOM   4070  H HG2  . LYS   A  1 275 ? 23.675 -23.488 -7.182  0.00 50.31  ? 301  LYS   A HG2  1 
ATOM   4071  H HG3  . LYS   A  1 275 ? 22.550 -24.146 -5.972  0.00 51.00  ? 301  LYS   A HG3  1 
ATOM   4072  H HD2  . LYS   A  1 275 ? 21.502 -25.525 -7.777  0.00 59.37  ? 301  LYS   A HD2  1 
ATOM   4073  H HD3  . LYS   A  1 275 ? 22.784 -24.954 -8.884  0.00 58.71  ? 301  LYS   A HD3  1 
ATOM   4074  H HE2  . LYS   A  1 275 ? 24.479 -25.978 -7.561  0.00 64.83  ? 301  LYS   A HE2  1 
ATOM   4075  H HE3  . LYS   A  1 275 ? 23.313 -26.362 -6.263  0.00 65.45  ? 301  LYS   A HE3  1 
ATOM   4076  H HZ1  . LYS   A  1 275 ? 23.809 -28.263 -7.623  0.00 69.31  ? 301  LYS   A HZ1  1 
ATOM   4077  H HZ2  . LYS   A  1 275 ? 22.216 -27.850 -7.770  0.00 69.29  ? 301  LYS   A HZ2  1 
ATOM   4078  H HZ3  . LYS   A  1 275 ? 23.278 -27.488 -8.982  0.00 68.70  ? 301  LYS   A HZ3  1 
ATOM   4079  N N    . ILE   A  1 276 ? 19.824 -21.152 -9.564  1.00 28.15  ? 302  ILE   A N    1 
ATOM   4080  C CA   . ILE   A  1 276 ? 18.715 -20.235 -9.698  1.00 28.63  ? 302  ILE   A CA   1 
ATOM   4081  C C    . ILE   A  1 276 ? 17.521 -20.998 -9.154  1.00 28.73  ? 302  ILE   A C    1 
ATOM   4082  O O    . ILE   A  1 276 ? 17.214 -22.092 -9.649  1.00 28.78  ? 302  ILE   A O    1 
ATOM   4083  C CB   . ILE   A  1 276 ? 18.504 -19.803 -11.162 1.00 29.95  ? 302  ILE   A CB   1 
ATOM   4084  C CG1  . ILE   A  1 276 ? 19.753 -19.034 -11.666 1.00 31.40  ? 302  ILE   A CG1  1 
ATOM   4085  C CG2  . ILE   A  1 276 ? 17.242 -18.930 -11.266 1.00 30.77  ? 302  ILE   A CG2  1 
ATOM   4086  C CD1  . ILE   A  1 276 ? 19.750 -18.738 -13.085 1.00 33.35  ? 302  ILE   A CD1  1 
ATOM   4087  H H    . ILE   A  1 276 ? 19.723 -21.980 -10.145 0.00 36.15  ? 302  ILE   A H    1 
ATOM   4088  H HA   . ILE   A  1 276 ? 18.863 -19.338 -9.099  0.00 36.27  ? 302  ILE   A HA   1 
ATOM   4089  H HB   . ILE   A  1 276 ? 18.363 -20.691 -11.777 0.00 37.82  ? 302  ILE   A HB   1 
ATOM   4090  H HG12 . ILE   A  1 276 ? 19.819 -18.087 -11.131 0.00 38.63  ? 302  ILE   A HG12 1 
ATOM   4091  H HG13 . ILE   A  1 276 ? 20.647 -19.624 -11.471 0.00 38.86  ? 302  ILE   A HG13 1 
ATOM   4092  H HG21 . ILE   A  1 276 ? 17.165 -18.499 -12.263 0.00 38.32  ? 302  ILE   A HG21 1 
ATOM   4093  H HG22 . ILE   A  1 276 ? 16.357 -19.539 -11.089 0.00 39.03  ? 302  ILE   A HG22 1 
ATOM   4094  H HG23 . ILE   A  1 276 ? 17.300 -18.137 -10.521 0.00 38.51  ? 302  ILE   A HG23 1 
ATOM   4095  H HD11 . ILE   A  1 276 ? 20.775 -18.542 -13.395 0.00 40.49  ? 302  ILE   A HD11 1 
ATOM   4096  H HD12 . ILE   A  1 276 ? 19.346 -19.588 -13.633 0.00 41.03  ? 302  ILE   A HD12 1 
ATOM   4097  H HD13 . ILE   A  1 276 ? 19.144 -17.852 -13.265 0.00 40.63  ? 302  ILE   A HD13 1 
ATOM   4098  N N    . ASN   A  1 277 ? 16.868 -20.452 -8.124  1.00 28.19  ? 303  ASN   A N    1 
ATOM   4099  C CA   . ASN   A  1 277 ? 15.693 -21.092 -7.558  1.00 27.44  ? 303  ASN   A CA   1 
ATOM   4100  C C    . ASN   A  1 277 ? 14.515 -20.808 -8.494  1.00 27.03  ? 303  ASN   A C    1 
ATOM   4101  O O    . ASN   A  1 277 ? 14.094 -19.664 -8.603  1.00 26.77  ? 303  ASN   A O    1 
ATOM   4102  C CB   . ASN   A  1 277 ? 15.426 -20.550 -6.155  1.00 28.10  ? 303  ASN   A CB   1 
ATOM   4103  C CG   . ASN   A  1 277 ? 14.358 -21.299 -5.411  1.00 31.09  ? 303  ASN   A CG   1 
ATOM   4104  O OD1  . ASN   A  1 277 ? 13.595 -22.081 -5.987  1.00 32.00  ? 303  ASN   A OD1  1 
ATOM   4105  N ND2  . ASN   A  1 277 ? 14.287 -21.083 -4.104  1.00 31.54  ? 303  ASN   A ND2  1 
ATOM   4106  H H    . ASN   A  1 277 ? 17.122 -19.583 -7.665  0.00 36.50  ? 303  ASN   A H    1 
ATOM   4107  H HA   . ASN   A  1 277 ? 15.843 -22.167 -7.479  0.00 36.75  ? 303  ASN   A HA   1 
ATOM   4108  H HB2  . ASN   A  1 277 ? 16.344 -20.627 -5.575  0.00 37.40  ? 303  ASN   A HB2  1 
ATOM   4109  H HB3  . ASN   A  1 277 ? 15.122 -19.505 -6.215  0.00 37.19  ? 303  ASN   A HB3  1 
ATOM   4110  H HD21 . ASN   A  1 277 ? 13.585 -21.562 -3.549  0.00 43.01  ? 303  ASN   A HD21 1 
ATOM   4111  H HD22 . ASN   A  1 277 ? 14.931 -20.439 -3.656  0.00 42.30  ? 303  ASN   A HD22 1 
ATOM   4112  N N    . ALA   A  1 278 ? 13.982 -21.844 -9.165  1.00 27.10  ? 304  ALA   A N    1 
ATOM   4113  C CA   . ALA   A  1 278 ? 12.844 -21.699 -10.079 1.00 27.90  ? 304  ALA   A CA   1 
ATOM   4114  C C    . ALA   A  1 278 ? 11.638 -21.015 -9.406  1.00 28.54  ? 304  ALA   A C    1 
ATOM   4115  O O    . ALA   A  1 278 ? 10.885 -20.310 -10.082 1.00 29.30  ? 304  ALA   A O    1 
ATOM   4116  C CB   . ALA   A  1 278 ? 12.425 -23.063 -10.605 1.00 28.05  ? 304  ALA   A CB   1 
ATOM   4117  H H    . ALA   A  1 278 ? 14.316 -22.799 -9.093  0.00 36.58  ? 304  ALA   A H    1 
ATOM   4118  H HA   . ALA   A  1 278 ? 13.144 -21.088 -10.928 0.00 36.94  ? 304  ALA   A HA   1 
ATOM   4119  H HB1  . ALA   A  1 278 ? 11.580 -22.942 -11.282 0.00 38.14  ? 304  ALA   A HB1  1 
ATOM   4120  H HB2  . ALA   A  1 278 ? 13.264 -23.511 -11.135 0.00 37.87  ? 304  ALA   A HB2  1 
ATOM   4121  H HB3  . ALA   A  1 278 ? 12.138 -23.693 -9.764  0.00 38.51  ? 304  ALA   A HB3  1 
ATOM   4122  N N    . ALA   A  1 279 ? 11.468 -21.218 -8.089  1.00 27.90  ? 305  ALA   A N    1 
ATOM   4123  C CA   . ALA   A  1 279 ? 10.375 -20.619 -7.319  1.00 27.93  ? 305  ALA   A CA   1 
ATOM   4124  C C    . ALA   A  1 279 ? 10.406 -19.087 -7.292  1.00 27.59  ? 305  ALA   A C    1 
ATOM   4125  O O    . ALA   A  1 279 ? 9.357  -18.476 -7.105  1.00 27.62  ? 305  ALA   A O    1 
ATOM   4126  C CB   . ALA   A  1 279 ? 10.375 -21.164 -5.905  1.00 28.30  ? 305  ALA   A CB   1 
ATOM   4127  H H    . ALA   A  1 279 ? 12.069 -21.814 -7.528  0.00 38.17  ? 305  ALA   A H    1 
ATOM   4128  H HA   . ALA   A  1 279 ? 9.433  -20.913 -7.782  0.00 38.71  ? 305  ALA   A HA   1 
ATOM   4129  H HB1  . ALA   A  1 279 ? 9.576  -20.685 -5.340  0.00 39.59  ? 305  ALA   A HB1  1 
ATOM   4130  H HB2  . ALA   A  1 279 ? 10.210 -22.240 -5.942  0.00 39.71  ? 305  ALA   A HB2  1 
ATOM   4131  H HB3  . ALA   A  1 279 ? 11.336 -20.951 -5.439  0.00 39.08  ? 305  ALA   A HB3  1 
ATOM   4132  N N    . TRP   A  1 280 ? 11.574 -18.459 -7.528  1.00 27.54  ? 306  TRP   A N    1 
ATOM   4133  C CA   . TRP   A  1 280 ? 11.671 -16.997 -7.608  1.00 28.25  ? 306  TRP   A CA   1 
ATOM   4134  C C    . TRP   A  1 280 ? 10.747 -16.428 -8.700  1.00 28.59  ? 306  TRP   A C    1 
ATOM   4135  O O    . TRP   A  1 280 ? 10.285 -15.303 -8.571  1.00 28.33  ? 306  TRP   A O    1 
ATOM   4136  C CB   . TRP   A  1 280 ? 13.115 -16.561 -7.951  1.00 28.26  ? 306  TRP   A CB   1 
ATOM   4137  C CG   . TRP   A  1 280 ? 14.136 -16.789 -6.872  1.00 29.31  ? 306  TRP   A CG   1 
ATOM   4138  C CD1  . TRP   A  1 280 ? 13.916 -16.935 -5.531  1.00 30.24  ? 306  TRP   A CD1  1 
ATOM   4139  C CD2  . TRP   A  1 280 ? 15.552 -16.850 -7.056  1.00 29.65  ? 306  TRP   A CD2  1 
ATOM   4140  N NE1  . TRP   A  1 280 ? 15.107 -17.156 -4.879  1.00 30.72  ? 306  TRP   A NE1  1 
ATOM   4141  C CE2  . TRP   A  1 280 ? 16.132 -17.074 -5.789  1.00 30.50  ? 306  TRP   A CE2  1 
ATOM   4142  C CE3  . TRP   A  1 280 ? 16.389 -16.756 -8.179  1.00 30.12  ? 306  TRP   A CE3  1 
ATOM   4143  C CZ2  . TRP   A  1 280 ? 17.508 -17.220 -5.618  1.00 31.06  ? 306  TRP   A CZ2  1 
ATOM   4144  C CZ3  . TRP   A  1 280 ? 17.752 -16.875 -8.001  1.00 30.83  ? 306  TRP   A CZ3  1 
ATOM   4145  C CH2  . TRP   A  1 280 ? 18.297 -17.111 -6.734  1.00 30.93  ? 306  TRP   A CH2  1 
ATOM   4146  H H    . TRP   A  1 280 ? 12.462 -18.932 -7.663  0.00 36.74  ? 306  TRP   A H    1 
ATOM   4147  H HA   . TRP   A  1 280 ? 11.382 -16.558 -6.654  0.00 37.56  ? 306  TRP   A HA   1 
ATOM   4148  H HB2  . TRP   A  1 280 ? 13.441 -17.124 -8.825  0.00 36.60  ? 306  TRP   A HB2  1 
ATOM   4149  H HB3  . TRP   A  1 280 ? 13.118 -15.502 -8.200  0.00 36.46  ? 306  TRP   A HB3  1 
ATOM   4150  H HD1  . TRP   A  1 280 ? 12.948 -16.953 -5.059  0.00 39.97  ? 306  TRP   A HD1  1 
ATOM   4151  H HE1  . TRP   A  1 280 ? 15.220 -17.296 -3.853  0.00 40.35  ? 306  TRP   A HE1  1 
ATOM   4152  H HE3  . TRP   A  1 280 ? 15.976 -16.584 -9.162  0.00 37.95  ? 306  TRP   A HE3  1 
ATOM   4153  H HZ2  . TRP   A  1 280 ? 17.935 -17.383 -4.641  0.00 39.96  ? 306  TRP   A HZ2  1 
ATOM   4154  H HZ3  . TRP   A  1 280 ? 18.405 -16.809 -8.857  0.00 38.37  ? 306  TRP   A HZ3  1 
ATOM   4155  H HH2  . TRP   A  1 280 ? 19.365 -17.202 -6.630  0.00 38.95  ? 306  TRP   A HH2  1 
ATOM   4156  N N    . PHE   A  1 281 ? 10.495 -17.201 -9.773  1.00 29.57  ? 307  PHE   A N    1 
ATOM   4157  C CA   . PHE   A  1 281 ? 9.689  -16.769 -10.925 1.00 30.87  ? 307  PHE   A CA   1 
ATOM   4158  C C    . PHE   A  1 281 ? 8.257  -17.312 -10.924 1.00 32.26  ? 307  PHE   A C    1 
ATOM   4159  O O    . PHE   A  1 281 ? 7.543  -17.100 -11.905 1.00 32.59  ? 307  PHE   A O    1 
ATOM   4160  C CB   . PHE   A  1 281 ? 10.401 -17.195 -12.225 1.00 30.64  ? 307  PHE   A CB   1 
ATOM   4161  C CG   . PHE   A  1 281 ? 11.850 -16.781 -12.270 1.00 30.95  ? 307  PHE   A CG   1 
ATOM   4162  C CD1  . PHE   A  1 281 ? 12.200 -15.458 -12.462 1.00 31.38  ? 307  PHE   A CD1  1 
ATOM   4163  C CD2  . PHE   A  1 281 ? 12.855 -17.687 -11.984 1.00 31.49  ? 307  PHE   A CD2  1 
ATOM   4164  C CE1  . PHE   A  1 281 ? 13.532 -15.069 -12.465 1.00 31.93  ? 307  PHE   A CE1  1 
ATOM   4165  C CE2  . PHE   A  1 281 ? 14.188 -17.291 -11.978 1.00 32.14  ? 307  PHE   A CE2  1 
ATOM   4166  C CZ   . PHE   A  1 281 ? 14.517 -15.984 -12.211 1.00 31.71  ? 307  PHE   A CZ   1 
ATOM   4167  H H    . PHE   A  1 281 ? 10.843 -18.146 -9.889  0.00 39.01  ? 307  PHE   A H    1 
ATOM   4168  H HA   . PHE   A  1 281 ? 9.624  -15.682 -10.945 0.00 40.21  ? 307  PHE   A HA   1 
ATOM   4169  H HB2  . PHE   A  1 281 ? 10.356 -18.280 -12.307 0.00 40.07  ? 307  PHE   A HB2  1 
ATOM   4170  H HB3  . PHE   A  1 281 ? 9.898  -16.737 -13.076 0.00 39.72  ? 307  PHE   A HB3  1 
ATOM   4171  H HD1  . PHE   A  1 281 ? 11.434 -14.729 -12.665 0.00 39.70  ? 307  PHE   A HD1  1 
ATOM   4172  H HD2  . PHE   A  1 281 ? 12.609 -18.717 -11.798 0.00 40.57  ? 307  PHE   A HD2  1 
ATOM   4173  H HE1  . PHE   A  1 281 ? 13.786 -14.043 -12.655 0.00 39.48  ? 307  PHE   A HE1  1 
ATOM   4174  H HE2  . PHE   A  1 281 ? 14.963 -18.013 -11.787 0.00 40.49  ? 307  PHE   A HE2  1 
ATOM   4175  H HZ   . PHE   A  1 281 ? 15.550 -15.681 -12.212 0.00 39.16  ? 307  PHE   A HZ   1 
ATOM   4176  N N    . LYS   A  1 282 ? 7.823  -17.978 -9.837  1.00 32.67  ? 308  LYS   A N    1 
ATOM   4177  C CA   . LYS   A  1 282 ? 6.486  -18.574 -9.743  1.00 33.91  ? 308  LYS   A CA   1 
ATOM   4178  C C    . LYS   A  1 282 ? 5.368  -17.546 -9.935  1.00 33.66  ? 308  LYS   A C    1 
ATOM   4179  O O    . LYS   A  1 282 ? 4.356  -17.878 -10.550 1.00 34.33  ? 308  LYS   A O    1 
ATOM   4180  C CB   . LYS   A  1 282 ? 6.327  -19.297 -8.387  1.00 37.56  ? 308  LYS   A CB   1 
ATOM   4181  C CG   . LYS   A  1 282 ? 5.145  -20.247 -8.293  1.00 44.91  ? 308  LYS   A CG   1 
ATOM   4182  C CD   . LYS   A  1 282 ? 4.957  -20.718 -6.853  1.00 51.77  ? 308  LYS   A CD   1 
ATOM   4183  C CE   . LYS   A  1 282 ? 4.064  -21.937 -6.724  1.00 57.57  ? 308  LYS   A CE   1 
ATOM   4184  N NZ   . LYS   A  1 282 ? 4.835  -23.210 -6.779  1.00 61.19  ? 308  LYS   A NZ   1 
ATOM   4185  H H    . LYS   A  1 282 ? 8.373  -18.105 -8.993  0.00 43.76  ? 308  LYS   A H    1 
ATOM   4186  H HA   . LYS   A  1 282 ? 6.383  -19.320 -10.529 0.00 46.05  ? 308  LYS   A HA   1 
ATOM   4187  H HB2  . LYS   A  1 282 ? 7.220  -19.889 -8.195  0.00 50.69  ? 308  LYS   A HB2  1 
ATOM   4188  H HB3  . LYS   A  1 282 ? 6.210  -18.548 -7.605  0.00 50.85  ? 308  LYS   A HB3  1 
ATOM   4189  H HG2  . LYS   A  1 282 ? 4.230  -19.747 -8.607  0.00 60.59  ? 308  LYS   A HG2  1 
ATOM   4190  H HG3  . LYS   A  1 282 ? 5.332  -21.120 -8.918  0.00 60.46  ? 308  LYS   A HG3  1 
ATOM   4191  H HD2  . LYS   A  1 282 ? 5.930  -20.967 -6.432  0.00 68.91  ? 308  LYS   A HD2  1 
ATOM   4192  H HD3  . LYS   A  1 282 ? 4.504  -19.911 -6.279  0.00 69.23  ? 308  LYS   A HD3  1 
ATOM   4193  H HE2  . LYS   A  1 282 ? 3.544  -21.897 -5.768  0.00 77.27  ? 308  LYS   A HE2  1 
ATOM   4194  H HE3  . LYS   A  1 282 ? 3.344  -21.939 -7.541  0.00 77.02  ? 308  LYS   A HE3  1 
ATOM   4195  H HZ1  . LYS   A  1 282 ? 4.203  -24.002 -6.722  0.00 81.78  ? 308  LYS   A HZ1  1 
ATOM   4196  H HZ2  . LYS   A  1 282 ? 5.352  -23.262 -7.651  0.00 80.88  ? 308  LYS   A HZ2  1 
ATOM   4197  H HZ3  . LYS   A  1 282 ? 5.490  -23.255 -6.005  0.00 81.15  ? 308  LYS   A HZ3  1 
ATOM   4198  N N    . ASN   A  1 283 ? 5.535  -16.317 -9.410  1.00 32.62  ? 309  ASN   A N    1 
ATOM   4199  C CA   . ASN   A  1 283 ? 4.511  -15.275 -9.515  1.00 31.87  ? 309  ASN   A CA   1 
ATOM   4200  C C    . ASN   A  1 283 ? 4.966  -14.079 -10.367 1.00 29.80  ? 309  ASN   A C    1 
ATOM   4201  O O    . ASN   A  1 283 ? 4.498  -12.971 -10.129 1.00 29.06  ? 309  ASN   A O    1 
ATOM   4202  C CB   . ASN   A  1 283 ? 4.098  -14.812 -8.120  1.00 34.35  ? 309  ASN   A CB   1 
ATOM   4203  C CG   . ASN   A  1 283 ? 3.575  -15.931 -7.251  1.00 39.70  ? 309  ASN   A CG   1 
ATOM   4204  O OD1  . ASN   A  1 283 ? 2.776  -16.761 -7.691  1.00 41.26  ? 309  ASN   A OD1  1 
ATOM   4205  N ND2  . ASN   A  1 283 ? 3.990  -15.973 -5.991  1.00 41.18  ? 309  ASN   A ND2  1 
ATOM   4206  H H    . ASN   A  1 283 ? 6.360  -16.017 -8.899  0.00 44.00  ? 309  ASN   A H    1 
ATOM   4207  H HA   . ASN   A  1 283 ? 3.617  -15.673 -9.992  0.00 44.00  ? 309  ASN   A HA   1 
ATOM   4208  H HB2  . ASN   A  1 283 ? 4.963  -14.362 -7.634  0.00 46.60  ? 309  ASN   A HB2  1 
ATOM   4209  H HB3  . ASN   A  1 283 ? 3.294  -14.082 -8.202  0.00 47.19  ? 309  ASN   A HB3  1 
ATOM   4210  H HD21 . ASN   A  1 283 ? 3.662  -16.715 -5.380  0.00 56.19  ? 309  ASN   A HD21 1 
ATOM   4211  H HD22 . ASN   A  1 283 ? 4.626  -15.273 -5.624  0.00 55.37  ? 309  ASN   A HD22 1 
ATOM   4212  N N    . MET   A  1 284 ? 5.828  -14.316 -11.392 1.00 28.82  ? 310  MET   A N    1 
ATOM   4213  C CA   . MET   A  1 284 ? 6.288  -13.294 -12.342 1.00 28.21  ? 310  MET   A CA   1 
ATOM   4214  C C    . MET   A  1 284 ? 5.798  -13.711 -13.753 1.00 27.87  ? 310  MET   A C    1 
ATOM   4215  O O    . MET   A  1 284 ? 6.606  -14.074 -14.623 1.00 28.12  ? 310  MET   A O    1 
ATOM   4216  C CB   . MET   A  1 284 ? 7.828  -13.193 -12.361 1.00 28.73  ? 310  MET   A CB   1 
ATOM   4217  C CG   . MET   A  1 284 ? 8.442  -12.358 -11.303 1.00 31.28  ? 310  MET   A CG   1 
ATOM   4218  S SD   . MET   A  1 284 ? 10.234 -12.275 -11.617 1.00 33.39  ? 310  MET   A SD   1 
ATOM   4219  C CE   . MET   A  1 284 ? 10.782 -12.118 -9.987  1.00 28.76  ? 310  MET   A CE   1 
ATOM   4220  H H    . MET   A  1 284 ? 6.222  -15.229 -11.598 0.00 38.87  ? 310  MET   A H    1 
ATOM   4221  H HA   . MET   A  1 284 ? 5.874  -12.317 -12.097 0.00 37.69  ? 310  MET   A HA   1 
ATOM   4222  H HB2  . MET   A  1 284 ? 8.255  -14.193 -12.289 0.00 37.63  ? 310  MET   A HB2  1 
ATOM   4223  H HB3  . MET   A  1 284 ? 8.110  -12.731 -13.304 0.00 37.28  ? 310  MET   A HB3  1 
ATOM   4224  H HG2  . MET   A  1 284 ? 8.026  -11.352 -11.341 0.00 40.48  ? 310  MET   A HG2  1 
ATOM   4225  H HG3  . MET   A  1 284 ? 8.279  -12.809 -10.326 0.00 40.78  ? 310  MET   A HG3  1 
ATOM   4226  H HE1  . MET   A  1 284 ? 11.868 -12.042 -9.985  0.00 36.42  ? 310  MET   A HE1  1 
ATOM   4227  H HE2  . MET   A  1 284 ? 10.346 -11.221 -9.549  0.00 36.91  ? 310  MET   A HE2  1 
ATOM   4228  H HE3  . MET   A  1 284 ? 10.471 -12.996 -9.424  0.00 37.16  ? 310  MET   A HE3  1 
ATOM   4229  N N    . PRO   A  1 285 ? 4.476  -13.647 -14.015 1.00 26.89  ? 311  PRO   A N    1 
ATOM   4230  C CA   . PRO   A  1 285 ? 3.973  -14.083 -15.324 1.00 26.61  ? 311  PRO   A CA   1 
ATOM   4231  C C    . PRO   A  1 285 ? 4.352  -13.192 -16.502 1.00 26.34  ? 311  PRO   A C    1 
ATOM   4232  O O    . PRO   A  1 285 ? 4.267  -13.655 -17.630 1.00 26.81  ? 311  PRO   A O    1 
ATOM   4233  C CB   . PRO   A  1 285 ? 2.449  -14.124 -15.115 1.00 27.25  ? 311  PRO   A CB   1 
ATOM   4234  C CG   . PRO   A  1 285 ? 2.191  -13.121 -14.074 1.00 27.70  ? 311  PRO   A CG   1 
ATOM   4235  C CD   . PRO   A  1 285 ? 3.368  -13.227 -13.136 1.00 26.21  ? 311  PRO   A CD   1 
ATOM   4236  H HA   . PRO   A  1 285 ? 4.318  -15.094 -15.532 0.00 36.49  ? 311  PRO   A HA   1 
ATOM   4237  H HB2  . PRO   A  1 285 ? 1.944  -13.862 -16.044 0.00 38.12  ? 311  PRO   A HB2  1 
ATOM   4238  H HB3  . PRO   A  1 285 ? 2.154  -15.117 -14.779 0.00 38.38  ? 311  PRO   A HB3  1 
ATOM   4239  H HG2  . PRO   A  1 285 ? 2.146  -12.130 -14.525 0.00 38.45  ? 311  PRO   A HG2  1 
ATOM   4240  H HG3  . PRO   A  1 285 ? 1.262  -13.355 -13.557 0.00 39.18  ? 311  PRO   A HG3  1 
ATOM   4241  H HD2  . PRO   A  1 285 ? 3.584  -12.258 -12.690 0.00 36.21  ? 311  PRO   A HD2  1 
ATOM   4242  H HD3  . PRO   A  1 285 ? 3.181  -13.985 -12.377 0.00 36.72  ? 311  PRO   A HD3  1 
ATOM   4243  N N    . HIS   A  1 286 ? 4.768  -11.941 -16.254 1.00 25.61  ? 312  HIS   A N    1 
ATOM   4244  C CA   . HIS   A  1 286 ? 5.110  -10.997 -17.315 1.00 25.66  ? 312  HIS   A CA   1 
ATOM   4245  C C    . HIS   A  1 286 ? 6.624  -10.772 -17.496 1.00 25.50  ? 312  HIS   A C    1 
ATOM   4246  O O    . HIS   A  1 286 ? 6.978  -9.857  -18.244 1.00 26.37  ? 312  HIS   A O    1 
ATOM   4247  C CB   . HIS   A  1 286 ? 4.467  -9.631  -17.012 1.00 25.64  ? 312  HIS   A CB   1 
ATOM   4248  C CG   . HIS   A  1 286 ? 3.000  -9.678  -16.715 1.00 27.78  ? 312  HIS   A CG   1 
ATOM   4249  N ND1  . HIS   A  1 286 ? 2.058  -9.745  -17.728 1.00 29.48  ? 312  HIS   A ND1  1 
ATOM   4250  C CD2  . HIS   A  1 286 ? 2.354  -9.607  -15.525 1.00 28.82  ? 312  HIS   A CD2  1 
ATOM   4251  C CE1  . HIS   A  1 286 ? 0.877  -9.733  -17.129 1.00 30.20  ? 312  HIS   A CE1  1 
ATOM   4252  N NE2  . HIS   A  1 286 ? 1.006  -9.651  -15.804 1.00 30.48  ? 312  HIS   A NE2  1 
ATOM   4253  H H    . HIS   A  1 286 ? 4.876  -11.538 -15.329 0.00 34.46  ? 312  HIS   A H    1 
ATOM   4254  H HA   . HIS   A  1 286 ? 4.709  -11.332 -18.270 0.00 34.28  ? 312  HIS   A HA   1 
ATOM   4255  H HB2  . HIS   A  1 286 ? 4.966  -9.198  -16.147 0.00 34.09  ? 312  HIS   A HB2  1 
ATOM   4256  H HB3  . HIS   A  1 286 ? 4.593  -8.977  -17.873 0.00 34.07  ? 312  HIS   A HB3  1 
ATOM   4257  H HD1  . HIS   A  1 286 ? 2.237  -9.793  -18.726 0.00 39.85  ? 312  HIS   A HD1  1 
ATOM   4258  H HD2  . HIS   A  1 286 ? 2.808  -9.531  -14.552 0.00 39.15  ? 312  HIS   A HD2  1 
ATOM   4259  H HE1  . HIS   A  1 286 ? -0.068 -9.777  -17.642 0.00 42.01  ? 312  HIS   A HE1  1 
ATOM   4260  N N    . LEU   A  1 287 ? 7.531  -11.539 -16.819 1.00 24.37  ? 313  LEU   A N    1 
ATOM   4261  C CA   . LEU   A  1 287 ? 8.976  -11.271 -16.939 1.00 23.45  ? 313  LEU   A CA   1 
ATOM   4262  C C    . LEU   A  1 287 ? 9.431  -11.318 -18.399 1.00 22.47  ? 313  LEU   A C    1 
ATOM   4263  O O    . LEU   A  1 287 ? 9.196  -12.314 -19.076 1.00 21.96  ? 313  LEU   A O    1 
ATOM   4264  C CB   . LEU   A  1 287 ? 9.838  -12.217 -16.076 1.00 23.50  ? 313  LEU   A CB   1 
ATOM   4265  C CG   . LEU   A  1 287 ? 11.318 -11.800 -15.924 1.00 25.36  ? 313  LEU   A CG   1 
ATOM   4266  C CD1  . LEU   A  1 287 ? 11.466 -10.501 -15.109 1.00 25.80  ? 313  LEU   A CD1  1 
ATOM   4267  C CD2  . LEU   A  1 287 ? 12.135 -12.902 -15.286 1.00 26.47  ? 313  LEU   A CD2  1 
ATOM   4268  H H    . LEU   A  1 287 ? 7.307  -12.320 -16.211 0.00 31.94  ? 313  LEU   A H    1 
ATOM   4269  H HA   . LEU   A  1 287 ? 9.135  -10.263 -16.564 0.00 29.75  ? 313  LEU   A HA   1 
ATOM   4270  H HB2  . LEU   A  1 287 ? 9.415  -12.255 -15.074 0.00 30.17  ? 313  LEU   A HB2  1 
ATOM   4271  H HB3  . LEU   A  1 287 ? 9.818  -13.209 -16.522 0.00 30.00  ? 313  LEU   A HB3  1 
ATOM   4272  H HG   . LEU   A  1 287 ? 11.747 -11.617 -16.909 0.00 31.23  ? 313  LEU   A HG   1 
ATOM   4273  H HD11 . LEU   A  1 287 ? 12.502 -10.395 -14.790 0.00 31.60  ? 313  LEU   A HD11 1 
ATOM   4274  H HD12 . LEU   A  1 287 ? 11.201 -9.654  -15.740 0.00 31.82  ? 313  LEU   A HD12 1 
ATOM   4275  H HD13 . LEU   A  1 287 ? 10.812 -10.543 -14.240 0.00 32.28  ? 313  LEU   A HD13 1 
ATOM   4276  H HD21 . LEU   A  1 287 ? 13.168 -12.572 -15.186 0.00 32.47  ? 313  LEU   A HD21 1 
ATOM   4277  H HD22 . LEU   A  1 287 ? 11.721 -13.131 -14.305 0.00 33.17  ? 313  LEU   A HD22 1 
ATOM   4278  H HD23 . LEU   A  1 287 ? 12.095 -13.782 -15.925 0.00 32.94  ? 313  LEU   A HD23 1 
ATOM   4279  N N    . LYS   A  1 288 ? 10.025 -10.222 -18.875 1.00 21.77  ? 314  LYS   A N    1 
ATOM   4280  C CA   . LYS   A  1 288 ? 10.424 -10.025 -20.272 1.00 22.19  ? 314  LYS   A CA   1 
ATOM   4281  C C    . LYS   A  1 288 ? 11.937 -10.034 -20.497 1.00 21.11  ? 314  LYS   A C    1 
ATOM   4282  O O    . LYS   A  1 288 ? 12.376 -10.496 -21.559 1.00 21.07  ? 314  LYS   A O    1 
ATOM   4283  C CB   . LYS   A  1 288 ? 9.861  -8.679  -20.747 1.00 25.87  ? 314  LYS   A CB   1 
ATOM   4284  C CG   . LYS   A  1 288 ? 9.878  -8.479  -22.253 1.00 32.44  ? 314  LYS   A CG   1 
ATOM   4285  C CD   . LYS   A  1 288 ? 9.205  -7.176  -22.659 1.00 39.36  ? 314  LYS   A CD   1 
ATOM   4286  C CE   . LYS   A  1 288 ? 10.166 -6.014  -22.584 1.00 45.63  ? 314  LYS   A CE   1 
ATOM   4287  N NZ   . LYS   A  1 288 ? 9.500  -4.721  -22.918 1.00 49.56  ? 314  LYS   A NZ   1 
ATOM   4288  H H    . LYS   A  1 288 ? 10.257 -9.417  -18.303 0.00 27.02  ? 314  LYS   A H    1 
ATOM   4289  H HA   . LYS   A  1 288 ? 9.980  -10.797 -20.898 0.00 27.60  ? 314  LYS   A HA   1 
ATOM   4290  H HB2  . LYS   A  1 288 ? 8.829  -8.601  -20.409 0.00 32.25  ? 314  LYS   A HB2  1 
ATOM   4291  H HB3  . LYS   A  1 288 ? 10.454 -7.883  -20.300 0.00 31.54  ? 314  LYS   A HB3  1 
ATOM   4292  H HG2  . LYS   A  1 288 ? 10.906 -8.450  -22.610 0.00 39.15  ? 314  LYS   A HG2  1 
ATOM   4293  H HG3  . LYS   A  1 288 ? 9.339  -9.298  -22.726 0.00 39.87  ? 314  LYS   A HG3  1 
ATOM   4294  H HD2  . LYS   A  1 288 ? 8.855  -7.257  -23.687 0.00 48.14  ? 314  LYS   A HD2  1 
ATOM   4295  H HD3  . LYS   A  1 288 ? 8.366  -6.971  -21.995 0.00 48.39  ? 314  LYS   A HD3  1 
ATOM   4296  H HE2  . LYS   A  1 288 ? 10.561 -5.937  -21.572 0.00 54.97  ? 314  LYS   A HE2  1 
ATOM   4297  H HE3  . LYS   A  1 288 ? 10.977 -6.169  -23.293 0.00 54.73  ? 314  LYS   A HE3  1 
ATOM   4298  H HZ1  . LYS   A  1 288 ? 10.169 -3.960  -22.856 0.00 59.70  ? 314  LYS   A HZ1  1 
ATOM   4299  H HZ2  . LYS   A  1 288 ? 9.129  -4.755  -23.862 0.00 60.11  ? 314  LYS   A HZ2  1 
ATOM   4300  H HZ3  . LYS   A  1 288 ? 8.736  -4.547  -22.272 0.00 60.34  ? 314  LYS   A HZ3  1 
ATOM   4301  N N    . VAL   A  1 289 ? 12.719 -9.438  -19.577 1.00 20.32  ? 315  VAL   A N    1 
ATOM   4302  C CA   . VAL   A  1 289 ? 14.180 -9.351  -19.708 1.00 20.95  ? 315  VAL   A CA   1 
ATOM   4303  C C    . VAL   A  1 289 ? 14.817 -9.867  -18.425 1.00 21.64  ? 315  VAL   A C    1 
ATOM   4304  O O    . VAL   A  1 289 ? 14.492 -9.385  -17.332 1.00 22.66  ? 315  VAL   A O    1 
ATOM   4305  C CB   . VAL   A  1 289 ? 14.649 -7.905  -20.032 1.00 21.58  ? 315  VAL   A CB   1 
ATOM   4306  C CG1  . VAL   A  1 289 ? 16.173 -7.833  -20.196 1.00 22.34  ? 315  VAL   A CG1  1 
ATOM   4307  C CG2  . VAL   A  1 289 ? 13.934 -7.357  -21.270 1.00 21.85  ? 315  VAL   A CG2  1 
ATOM   4308  H H    . VAL   A  1 289 ? 12.370 -9.002  -18.730 0.00 24.41  ? 315  VAL   A H    1 
ATOM   4309  H HA   . VAL   A  1 289 ? 14.518 -9.983  -20.527 0.00 24.41  ? 315  VAL   A HA   1 
ATOM   4310  H HB   . VAL   A  1 289 ? 14.382 -7.264  -19.193 0.00 25.04  ? 315  VAL   A HB   1 
ATOM   4311  H HG11 . VAL   A  1 289 ? 16.442 -6.898  -20.685 0.00 25.14  ? 315  VAL   A HG11 1 
ATOM   4312  H HG12 . VAL   A  1 289 ? 16.645 -7.871  -19.216 0.00 25.32  ? 315  VAL   A HG12 1 
ATOM   4313  H HG13 . VAL   A  1 289 ? 16.508 -8.676  -20.798 0.00 25.30  ? 315  VAL   A HG13 1 
ATOM   4314  H HG21 . VAL   A  1 289 ? 14.376 -6.403  -21.553 0.00 25.09  ? 315  VAL   A HG21 1 
ATOM   4315  H HG22 . VAL   A  1 289 ? 14.032 -8.069  -22.087 0.00 25.32  ? 315  VAL   A HG22 1 
ATOM   4316  H HG23 . VAL   A  1 289 ? 12.880 -7.209  -21.037 0.00 25.70  ? 315  VAL   A HG23 1 
ATOM   4317  N N    . LEU   A  1 290 ? 15.690 -10.869 -18.554 1.00 20.12  ? 316  LEU   A N    1 
ATOM   4318  C CA   . LEU   A  1 290 ? 16.385 -11.470 -17.423 1.00 19.62  ? 316  LEU   A CA   1 
ATOM   4319  C C    . LEU   A  1 290 ? 17.887 -11.406 -17.717 1.00 19.49  ? 316  LEU   A C    1 
ATOM   4320  O O    . LEU   A  1 290 ? 18.367 -12.011 -18.683 1.00 18.91  ? 316  LEU   A O    1 
ATOM   4321  C CB   . LEU   A  1 290 ? 15.920 -12.922 -17.211 1.00 19.30  ? 316  LEU   A CB   1 
ATOM   4322  C CG   . LEU   A  1 290 ? 16.587 -13.710 -16.069 1.00 20.49  ? 316  LEU   A CG   1 
ATOM   4323  C CD1  . LEU   A  1 290 ? 16.556 -12.944 -14.736 1.00 20.75  ? 316  LEU   A CD1  1 
ATOM   4324  C CD2  . LEU   A  1 290 ? 15.939 -15.075 -15.913 1.00 21.13  ? 316  LEU   A CD2  1 
ATOM   4325  H H    . LEU   A  1 290 ? 15.946 -11.293 -19.440 0.00 23.28  ? 316  LEU   A H    1 
ATOM   4326  H HA   . LEU   A  1 290 ? 16.182 -10.908 -16.513 0.00 22.90  ? 316  LEU   A HA   1 
ATOM   4327  H HB2  . LEU   A  1 290 ? 14.850 -12.908 -17.010 0.00 23.16  ? 316  LEU   A HB2  1 
ATOM   4328  H HB3  . LEU   A  1 290 ? 16.103 -13.473 -18.132 0.00 22.78  ? 316  LEU   A HB3  1 
ATOM   4329  H HG   . LEU   A  1 290 ? 17.628 -13.885 -16.332 0.00 24.11  ? 316  LEU   A HG   1 
ATOM   4330  H HD11 . LEU   A  1 290 ? 16.881 -13.606 -13.934 0.00 24.93  ? 316  LEU   A HD11 1 
ATOM   4331  H HD12 . LEU   A  1 290 ? 17.231 -12.093 -14.795 0.00 24.42  ? 316  LEU   A HD12 1 
ATOM   4332  H HD13 . LEU   A  1 290 ? 15.540 -12.602 -14.546 0.00 24.99  ? 316  LEU   A HD13 1 
ATOM   4333  H HD21 . LEU   A  1 290 ? 16.400 -15.598 -15.076 0.00 25.74  ? 316  LEU   A HD21 1 
ATOM   4334  H HD22 . LEU   A  1 290 ? 14.875 -14.941 -15.726 0.00 25.92  ? 316  LEU   A HD22 1 
ATOM   4335  H HD23 . LEU   A  1 290 ? 16.087 -15.641 -16.831 0.00 25.59  ? 316  LEU   A HD23 1 
ATOM   4336  N N    . ASP   A  1 291 ? 18.605 -10.613 -16.933 1.00 19.40  ? 317  ASP   A N    1 
ATOM   4337  C CA   . ASP   A  1 291 ? 20.036 -10.438 -17.094 1.00 20.48  ? 317  ASP   A CA   1 
ATOM   4338  C C    . ASP   A  1 291 ? 20.744 -11.250 -16.001 1.00 20.39  ? 317  ASP   A C    1 
ATOM   4339  O O    . ASP   A  1 291 ? 20.534 -11.009 -14.799 1.00 20.39  ? 317  ASP   A O    1 
ATOM   4340  C CB   . ASP   A  1 291 ? 20.374 -8.941  -17.004 1.00 23.93  ? 317  ASP   A CB   1 
ATOM   4341  C CG   . ASP   A  1 291 ? 21.588 -8.544  -17.793 1.00 33.58  ? 317  ASP   A CG   1 
ATOM   4342  O OD1  . ASP   A  1 291 ? 22.479 -9.399  -17.973 1.00 35.57  ? 317  ASP   A OD1  1 
ATOM   4343  O OD2  . ASP   A  1 291 ? 21.672 -7.366  -18.204 1.00 37.32  ? 317  ASP   A OD2  1 
ATOM   4344  H H    . ASP   A  1 291 ? 18.225 -10.068 -16.166 0.00 22.02  ? 317  ASP   A H    1 
ATOM   4345  H HA   . ASP   A  1 291 ? 20.336 -10.821 -18.069 0.00 22.69  ? 317  ASP   A HA   1 
ATOM   4346  H HB2  . ASP   A  1 291 ? 19.527 -8.363  -17.370 0.00 26.77  ? 317  ASP   A HB2  1 
ATOM   4347  H HB3  . ASP   A  1 291 ? 20.590 -8.680  -15.970 0.00 26.78  ? 317  ASP   A HB3  1 
ATOM   4348  N N    . LEU   A  1 292 ? 21.529 -12.256 -16.420 1.00 19.58  ? 318  LEU   A N    1 
ATOM   4349  C CA   . LEU   A  1 292 ? 22.281 -13.135 -15.519 1.00 19.40  ? 318  LEU   A CA   1 
ATOM   4350  C C    . LEU   A  1 292 ? 23.749 -13.234 -15.948 1.00 18.97  ? 318  LEU   A C    1 
ATOM   4351  O O    . LEU   A  1 292 ? 24.380 -14.286 -15.806 1.00 19.35  ? 318  LEU   A O    1 
ATOM   4352  C CB   . LEU   A  1 292 ? 21.653 -14.530 -15.536 1.00 19.80  ? 318  LEU   A CB   1 
ATOM   4353  C CG   . LEU   A  1 292 ? 20.260 -14.657 -14.918 1.00 21.86  ? 318  LEU   A CG   1 
ATOM   4354  C CD1  . LEU   A  1 292 ? 19.590 -15.935 -15.415 1.00 22.75  ? 318  LEU   A CD1  1 
ATOM   4355  C CD2  . LEU   A  1 292 ? 20.344 -14.678 -13.397 1.00 22.21  ? 318  LEU   A CD2  1 
ATOM   4356  H H    . LEU   A  1 292 ? 21.668 -12.495 -17.397 0.00 21.72  ? 318  LEU   A H    1 
ATOM   4357  H HA   . LEU   A  1 292 ? 22.279 -12.740 -14.504 0.00 21.90  ? 318  LEU   A HA   1 
ATOM   4358  H HB2  . LEU   A  1 292 ? 21.583 -14.863 -16.571 0.00 22.61  ? 318  LEU   A HB2  1 
ATOM   4359  H HB3  . LEU   A  1 292 ? 22.287 -15.213 -14.972 0.00 22.82  ? 318  LEU   A HB3  1 
ATOM   4360  H HG   . LEU   A  1 292 ? 19.646 -13.808 -15.213 0.00 25.44  ? 318  LEU   A HG   1 
ATOM   4361  H HD11 . LEU   A  1 292 ? 18.663 -16.085 -14.864 0.00 27.28  ? 318  LEU   A HD11 1 
ATOM   4362  H HD12 . LEU   A  1 292 ? 19.381 -15.838 -16.480 0.00 26.83  ? 318  LEU   A HD12 1 
ATOM   4363  H HD13 . LEU   A  1 292 ? 20.262 -16.775 -15.245 0.00 27.06  ? 318  LEU   A HD13 1 
ATOM   4364  H HD21 . LEU   A  1 292 ? 19.341 -14.546 -12.993 0.00 26.46  ? 318  LEU   A HD21 1 
ATOM   4365  H HD22 . LEU   A  1 292 ? 20.737 -15.644 -13.085 0.00 26.42  ? 318  LEU   A HD22 1 
ATOM   4366  H HD23 . LEU   A  1 292 ? 20.998 -13.888 -13.035 0.00 25.99  ? 318  LEU   A HD23 1 
ATOM   4367  N N    . GLU   A  1 293 ? 24.309 -12.127 -16.409 1.00 18.78  ? 319  GLU   A N    1 
ATOM   4368  C CA   . GLU   A  1 293 ? 25.700 -12.100 -16.856 1.00 18.93  ? 319  GLU   A CA   1 
ATOM   4369  C C    . GLU   A  1 293 ? 26.650 -12.170 -15.686 1.00 18.54  ? 319  GLU   A C    1 
ATOM   4370  O O    . GLU   A  1 293 ? 26.286 -11.763 -14.587 1.00 18.59  ? 319  GLU   A O    1 
ATOM   4371  C CB   . GLU   A  1 293 ? 26.006 -10.788 -17.598 1.00 21.23  ? 319  GLU   A CB   1 
ATOM   4372  C CG   . GLU   A  1 293 ? 25.095 -10.491 -18.757 1.00 26.57  ? 319  GLU   A CG   1 
ATOM   4373  C CD   . GLU   A  1 293 ? 25.271 -9.072  -19.246 1.00 32.72  ? 319  GLU   A CD   1 
ATOM   4374  O OE1  . GLU   A  1 293 ? 24.472 -8.209  -18.815 1.00 33.50  ? 319  GLU   A OE1  1 
ATOM   4375  O OE2  . GLU   A  1 293 ? 26.213 -8.816  -20.031 1.00 33.44  ? 319  GLU   A OE2  1 
ATOM   4376  H H    . GLU   A  1 293 ? 23.855 -11.219 -16.419 0.00 20.30  ? 319  GLU   A H    1 
ATOM   4377  H HA   . GLU   A  1 293 ? 25.896 -12.933 -17.531 0.00 20.36  ? 319  GLU   A HA   1 
ATOM   4378  H HB2  . GLU   A  1 293 ? 25.922 -9.964  -16.892 0.00 22.68  ? 319  GLU   A HB2  1 
ATOM   4379  H HB3  . GLU   A  1 293 ? 27.023 -10.836 -17.986 0.00 22.53  ? 319  GLU   A HB3  1 
ATOM   4380  H HG2  . GLU   A  1 293 ? 25.293 -11.180 -19.574 0.00 28.99  ? 319  GLU   A HG2  1 
ATOM   4381  H HG3  . GLU   A  1 293 ? 24.054 -10.586 -18.450 0.00 29.22  ? 319  GLU   A HG3  1 
ATOM   4382  N N    . PHE   A  1 294 ? 27.894 -12.587 -15.927 1.00 18.15  ? 320  PHE   A N    1 
ATOM   4383  C CA   . PHE   A  1 294 ? 28.937 -12.567 -14.909 1.00 18.95  ? 320  PHE   A CA   1 
ATOM   4384  C C    . PHE   A  1 294 ? 28.561 -13.333 -13.648 1.00 19.14  ? 320  PHE   A C    1 
ATOM   4385  O O    . PHE   A  1 294 ? 28.773 -12.858 -12.536 1.00 18.82  ? 320  PHE   A O    1 
ATOM   4386  C CB   . PHE   A  1 294 ? 29.358 -11.117 -14.599 1.00 19.25  ? 320  PHE   A CB   1 
ATOM   4387  C CG   . PHE   A  1 294 ? 30.001 -10.434 -15.791 1.00 20.37  ? 320  PHE   A CG   1 
ATOM   4388  C CD1  . PHE   A  1 294 ? 31.334 -10.659 -16.105 1.00 21.11  ? 320  PHE   A CD1  1 
ATOM   4389  C CD2  . PHE   A  1 294 ? 29.277 -9.562  -16.584 1.00 21.11  ? 320  PHE   A CD2  1 
ATOM   4390  C CE1  . PHE   A  1 294 ? 31.930 -10.025 -17.195 1.00 21.93  ? 320  PHE   A CE1  1 
ATOM   4391  C CE2  . PHE   A  1 294 ? 29.877 -8.924  -17.672 1.00 22.21  ? 320  PHE   A CE2  1 
ATOM   4392  C CZ   . PHE   A  1 294 ? 31.195 -9.168  -17.974 1.00 21.74  ? 320  PHE   A CZ   1 
ATOM   4393  H H    . PHE   A  1 294 ? 28.209 -12.944 -16.824 0.00 19.30  ? 320  PHE   A H    1 
ATOM   4394  H HA   . PHE   A  1 294 ? 29.810 -13.068 -15.322 0.00 20.45  ? 320  PHE   A HA   1 
ATOM   4395  H HB2  . PHE   A  1 294 ? 28.488 -10.536 -14.296 0.00 20.62  ? 320  PHE   A HB2  1 
ATOM   4396  H HB3  . PHE   A  1 294 ? 30.098 -11.114 -13.801 0.00 20.73  ? 320  PHE   A HB3  1 
ATOM   4397  H HD1  . PHE   A  1 294 ? 31.914 -11.335 -15.503 0.00 22.59  ? 320  PHE   A HD1  1 
ATOM   4398  H HD2  . PHE   A  1 294 ? 28.244 -9.366  -16.355 0.00 22.30  ? 320  PHE   A HD2  1 
ATOM   4399  H HE1  . PHE   A  1 294 ? 32.964 -10.217 -17.432 0.00 23.00  ? 320  PHE   A HE1  1 
ATOM   4400  H HE2  . PHE   A  1 294 ? 29.301 -8.251  -18.285 0.00 23.07  ? 320  PHE   A HE2  1 
ATOM   4401  H HZ   . PHE   A  1 294 ? 31.656 -8.676  -18.815 0.00 22.34  ? 320  PHE   A HZ   1 
ATOM   4402  N N    . ASN   A  1 295 ? 28.003 -14.519 -13.837 1.00 19.05  ? 321  ASN   A N    1 
ATOM   4403  C CA   . ASN   A  1 295 ? 27.664 -15.430 -12.751 1.00 19.61  ? 321  ASN   A CA   1 
ATOM   4404  C C    . ASN   A  1 295 ? 28.444 -16.745 -12.979 1.00 20.77  ? 321  ASN   A C    1 
ATOM   4405  O O    . ASN   A  1 295 ? 29.413 -16.738 -13.747 1.00 21.42  ? 321  ASN   A O    1 
ATOM   4406  C CB   . ASN   A  1 295 ? 26.127 -15.624 -12.702 1.00 19.70  ? 321  ASN   A CB   1 
ATOM   4407  C CG   . ASN   A  1 295 ? 25.347 -14.481 -12.140 1.00 20.22  ? 321  ASN   A CG   1 
ATOM   4408  O OD1  . ASN   A  1 295 ? 24.403 -13.954 -12.757 1.00 20.77  ? 321  ASN   A OD1  1 
ATOM   4409  N ND2  . ASN   A  1 295 ? 25.730 -14.023 -10.985 1.00 18.51  ? 321  ASN   A ND2  1 
ATOM   4410  H H    . ASN   A  1 295 ? 27.774 -14.901 -14.749 0.00 21.22  ? 321  ASN   A H    1 
ATOM   4411  H HA   . ASN   A  1 295 ? 28.025 -15.041 -11.801 0.00 22.52  ? 321  ASN   A HA   1 
ATOM   4412  H HB2  . ASN   A  1 295 ? 25.760 -15.825 -13.707 0.00 22.61  ? 321  ASN   A HB2  1 
ATOM   4413  H HB3  . ASN   A  1 295 ? 25.891 -16.456 -12.042 0.00 23.09  ? 321  ASN   A HB3  1 
ATOM   4414  H HD21 . ASN   A  1 295 ? 25.142 -13.317 -10.565 0.00 21.35  ? 321  ASN   A HD21 1 
ATOM   4415  H HD22 . ASN   A  1 295 ? 26.557 -14.358 -10.503 0.00 21.45  ? 321  ASN   A HD22 1 
ATOM   4416  N N    . TYR   A  1 296 ? 28.077 -17.850 -12.302 1.00 20.88  ? 322  TYR   A N    1 
ATOM   4417  C CA   . TYR   A  1 296 ? 28.746 -19.126 -12.479 1.00 21.99  ? 322  TYR   A CA   1 
ATOM   4418  C C    . TYR   A  1 296 ? 27.682 -20.159 -12.891 1.00 22.52  ? 322  TYR   A C    1 
ATOM   4419  O O    . TYR   A  1 296 ? 27.568 -21.226 -12.283 1.00 23.01  ? 322  TYR   A O    1 
ATOM   4420  C CB   . TYR   A  1 296 ? 29.395 -19.515 -11.155 1.00 22.12  ? 322  TYR   A CB   1 
ATOM   4421  C CG   . TYR   A  1 296 ? 30.379 -18.500 -10.619 1.00 23.53  ? 322  TYR   A CG   1 
ATOM   4422  C CD1  . TYR   A  1 296 ? 31.668 -18.416 -11.129 1.00 24.62  ? 322  TYR   A CD1  1 
ATOM   4423  C CD2  . TYR   A  1 296 ? 30.052 -17.686 -9.539  1.00 24.81  ? 322  TYR   A CD2  1 
ATOM   4424  C CE1  . TYR   A  1 296 ? 32.608 -17.557 -10.574 1.00 26.04  ? 322  TYR   A CE1  1 
ATOM   4425  C CE2  . TYR   A  1 296 ? 30.965 -16.786 -9.012  1.00 25.70  ? 322  TYR   A CE2  1 
ATOM   4426  C CZ   . TYR   A  1 296 ? 32.258 -16.754 -9.502  1.00 27.07  ? 322  TYR   A CZ   1 
ATOM   4427  O OH   . TYR   A  1 296 ? 33.196 -15.915 -8.943  1.00 28.39  ? 322  TYR   A OH   1 
ATOM   4428  H H    . TYR   A  1 296 ? 27.352 -17.889 -11.593 0.00 24.89  ? 322  TYR   A H    1 
ATOM   4429  H HA   . TYR   A  1 296 ? 29.513 -19.090 -13.251 0.00 26.12  ? 322  TYR   A HA   1 
ATOM   4430  H HB2  . TYR   A  1 296 ? 28.590 -19.572 -10.425 0.00 27.08  ? 322  TYR   A HB2  1 
ATOM   4431  H HB3  . TYR   A  1 296 ? 29.901 -20.474 -11.252 0.00 27.14  ? 322  TYR   A HB3  1 
ATOM   4432  H HD1  . TYR   A  1 296 ? 31.961 -19.071 -11.932 0.00 29.51  ? 322  TYR   A HD1  1 
ATOM   4433  H HD2  . TYR   A  1 296 ? 29.060 -17.726 -9.123  0.00 30.05  ? 322  TYR   A HD2  1 
ATOM   4434  H HE1  . TYR   A  1 296 ? 33.608 -17.519 -10.973 0.00 31.01  ? 322  TYR   A HE1  1 
ATOM   4435  H HE2  . TYR   A  1 296 ? 30.687 -16.184 -8.164  0.00 30.92  ? 322  TYR   A HE2  1 
ATOM   4436  H HH   . TYR   A  1 296 ? 32.803 -15.384 -8.202  0.00 33.95  ? 322  TYR   A HH   1 
ATOM   4437  N N    . LEU   A  1 297 ? 26.911 -19.836 -13.931 1.00 22.46  ? 323  LEU   A N    1 
ATOM   4438  C CA   . LEU   A  1 297 ? 25.752 -20.626 -14.332 1.00 22.83  ? 323  LEU   A CA   1 
ATOM   4439  C C    . LEU   A  1 297 ? 25.929 -21.640 -15.477 1.00 23.70  ? 323  LEU   A C    1 
ATOM   4440  O O    . LEU   A  1 297 ? 24.912 -22.048 -16.038 1.00 23.63  ? 323  LEU   A O    1 
ATOM   4441  C CB   . LEU   A  1 297 ? 24.613 -19.648 -14.692 1.00 22.58  ? 323  LEU   A CB   1 
ATOM   4442  C CG   . LEU   A  1 297 ? 24.167 -18.721 -13.552 1.00 23.53  ? 323  LEU   A CG   1 
ATOM   4443  C CD1  . LEU   A  1 297 ? 23.308 -17.586 -14.094 1.00 24.04  ? 323  LEU   A CD1  1 
ATOM   4444  C CD2  . LEU   A  1 297 ? 23.407 -19.501 -12.462 1.00 24.08  ? 323  LEU   A CD2  1 
ATOM   4445  H H    . LEU   A  1 297 ? 27.075 -19.029 -14.524 0.00 26.55  ? 323  LEU   A H    1 
ATOM   4446  H HA   . LEU   A  1 297 ? 25.418 -21.220 -13.484 0.00 28.05  ? 323  LEU   A HA   1 
ATOM   4447  H HB2  . LEU   A  1 297 ? 24.948 -19.015 -15.512 0.00 26.72  ? 323  LEU   A HB2  1 
ATOM   4448  H HB3  . LEU   A  1 297 ? 23.727 -20.196 -15.007 0.00 27.33  ? 323  LEU   A HB3  1 
ATOM   4449  H HG   . LEU   A  1 297 ? 25.045 -18.280 -13.087 0.00 28.07  ? 323  LEU   A HG   1 
ATOM   4450  H HD11 . LEU   A  1 297 ? 22.839 -17.054 -13.268 0.00 28.59  ? 323  LEU   A HD11 1 
ATOM   4451  H HD12 . LEU   A  1 297 ? 23.942 -16.904 -14.658 0.00 28.14  ? 323  LEU   A HD12 1 
ATOM   4452  H HD13 . LEU   A  1 297 ? 22.552 -18.002 -14.758 0.00 28.63  ? 323  LEU   A HD13 1 
ATOM   4453  H HD21 . LEU   A  1 297 ? 23.037 -18.795 -11.720 0.00 29.41  ? 323  LEU   A HD21 1 
ATOM   4454  H HD22 . LEU   A  1 297 ? 22.567 -20.001 -12.941 0.00 29.60  ? 323  LEU   A HD22 1 
ATOM   4455  H HD23 . LEU   A  1 297 ? 24.061 -20.221 -11.974 0.00 29.66  ? 323  LEU   A HD23 1 
ATOM   4456  N N    . VAL   A  1 298 ? 27.147 -22.148 -15.764 1.00 24.26  ? 324  VAL   A N    1 
ATOM   4457  C CA   . VAL   A  1 298 ? 27.308 -23.204 -16.793 1.00 24.90  ? 324  VAL   A CA   1 
ATOM   4458  C C    . VAL   A  1 298 ? 26.429 -24.445 -16.445 1.00 25.19  ? 324  VAL   A C    1 
ATOM   4459  O O    . VAL   A  1 298 ? 25.756 -24.975 -17.326 1.00 24.77  ? 324  VAL   A O    1 
ATOM   4460  C CB   . VAL   A  1 298 ? 28.809 -23.586 -17.012 1.00 25.23  ? 324  VAL   A CB   1 
ATOM   4461  C CG1  . VAL   A  1 298 ? 28.971 -24.955 -17.690 1.00 25.49  ? 324  VAL   A CG1  1 
ATOM   4462  C CG2  . VAL   A  1 298 ? 29.539 -22.504 -17.811 1.00 25.95  ? 324  VAL   A CG2  1 
ATOM   4463  H H    . VAL   A  1 298 ? 28.010 -21.861 -15.315 0.00 29.46  ? 324  VAL   A H    1 
ATOM   4464  H HA   . VAL   A  1 298 ? 26.907 -22.814 -17.729 0.00 30.29  ? 324  VAL   A HA   1 
ATOM   4465  H HB   . VAL   A  1 298 ? 29.295 -23.655 -16.040 0.00 31.12  ? 324  VAL   A HB   1 
ATOM   4466  H HG11 . VAL   A  1 298 ? 29.993 -25.042 -18.055 0.00 31.68  ? 324  VAL   A HG11 1 
ATOM   4467  H HG12 . VAL   A  1 298 ? 28.789 -25.749 -16.967 0.00 32.19  ? 324  VAL   A HG12 1 
ATOM   4468  H HG13 . VAL   A  1 298 ? 28.278 -25.035 -18.526 0.00 31.69  ? 324  VAL   A HG13 1 
ATOM   4469  H HG21 . VAL   A  1 298 ? 30.594 -22.761 -17.882 0.00 31.31  ? 324  VAL   A HG21 1 
ATOM   4470  H HG22 . VAL   A  1 298 ? 29.103 -22.446 -18.808 0.00 31.12  ? 324  VAL   A HG22 1 
ATOM   4471  H HG23 . VAL   A  1 298 ? 29.423 -21.549 -17.301 0.00 30.98  ? 324  VAL   A HG23 1 
ATOM   4472  N N    . GLY   A  1 299 ? 26.443 -24.870 -15.182 1.00 25.90  ? 325  GLY   A N    1 
ATOM   4473  C CA   . GLY   A  1 299 ? 25.631 -25.996 -14.716 1.00 26.38  ? 325  GLY   A CA   1 
ATOM   4474  C C    . GLY   A  1 299 ? 24.147 -25.726 -14.894 1.00 26.62  ? 325  GLY   A C    1 
ATOM   4475  O O    . GLY   A  1 299 ? 23.418 -26.572 -15.418 1.00 27.16  ? 325  GLY   A O    1 
ATOM   4476  H H    . GLY   A  1 299 ? 27.020 -24.464 -14.452 0.00 32.65  ? 325  GLY   A H    1 
ATOM   4477  H HA2  . GLY   A  1 299 ? 25.891 -26.891 -15.278 0.00 34.21  ? 325  GLY   A HA2  1 
ATOM   4478  H HA3  . GLY   A  1 299 ? 25.827 -26.176 -13.660 0.00 34.17  ? 325  GLY   A HA3  1 
ATOM   4479  N N    . GLU   A  1 300 ? 23.696 -24.514 -14.514 1.00 25.72  ? 326  GLU   A N    1 
ATOM   4480  C CA   . GLU   A  1 300 ? 22.295 -24.114 -14.681 1.00 25.17  ? 326  GLU   A CA   1 
ATOM   4481  C C    . GLU   A  1 300 ? 21.891 -24.018 -16.149 1.00 24.89  ? 326  GLU   A C    1 
ATOM   4482  O O    . GLU   A  1 300 ? 20.750 -24.323 -16.472 1.00 25.00  ? 326  GLU   A O    1 
ATOM   4483  C CB   . GLU   A  1 300 ? 22.011 -22.772 -13.978 1.00 27.19  ? 326  GLU   A CB   1 
ATOM   4484  C CG   . GLU   A  1 300 ? 21.722 -22.898 -12.491 1.00 31.53  ? 326  GLU   A CG   1 
ATOM   4485  C CD   . GLU   A  1 300 ? 20.368 -23.484 -12.145 1.00 36.51  ? 326  GLU   A CD   1 
ATOM   4486  O OE1  . GLU   A  1 300 ? 19.528 -23.662 -13.055 1.00 39.05  ? 326  GLU   A OE1  1 
ATOM   4487  O OE2  . GLU   A  1 300 ? 20.138 -23.733 -10.944 1.00 37.22  ? 326  GLU   A OE2  1 
ATOM   4488  H H    . GLU   A  1 300 ? 24.280 -23.809 -14.077 0.00 32.49  ? 326  GLU   A H    1 
ATOM   4489  H HA   . GLU   A  1 300 ? 21.674 -24.894 -14.241 0.00 32.57  ? 326  GLU   A HA   1 
ATOM   4490  H HB2  . GLU   A  1 300 ? 22.879 -22.124 -14.081 0.00 33.80  ? 326  GLU   A HB2  1 
ATOM   4491  H HB3  . GLU   A  1 300 ? 21.157 -22.296 -14.457 0.00 34.06  ? 326  GLU   A HB3  1 
ATOM   4492  H HG2  . GLU   A  1 300 ? 22.477 -23.547 -12.051 0.00 39.96  ? 326  GLU   A HG2  1 
ATOM   4493  H HG3  . GLU   A  1 300 ? 21.770 -21.918 -12.021 0.00 39.48  ? 326  GLU   A HG3  1 
ATOM   4494  N N    . ILE   A  1 301 ? 22.804 -23.614 -17.044 1.00 23.99  ? 327  ILE   A N    1 
ATOM   4495  C CA   . ILE   A  1 301 ? 22.506 -23.554 -18.471 1.00 23.95  ? 327  ILE   A CA   1 
ATOM   4496  C C    . ILE   A  1 301 ? 22.272 -24.973 -19.010 1.00 24.99  ? 327  ILE   A C    1 
ATOM   4497  O O    . ILE   A  1 301 ? 21.450 -25.146 -19.905 1.00 25.09  ? 327  ILE   A O    1 
ATOM   4498  C CB   . ILE   A  1 301 ? 23.610 -22.785 -19.269 1.00 23.20  ? 327  ILE   A CB   1 
ATOM   4499  C CG1  . ILE   A  1 301 ? 23.601 -21.284 -18.885 1.00 23.52  ? 327  ILE   A CG1  1 
ATOM   4500  C CG2  . ILE   A  1 301 ? 23.386 -22.950 -20.784 1.00 23.39  ? 327  ILE   A CG2  1 
ATOM   4501  C CD1  . ILE   A  1 301 ? 24.865 -20.478 -19.274 1.00 24.42  ? 327  ILE   A CD1  1 
ATOM   4502  H H    . ILE   A  1 301 ? 23.750 -23.326 -16.813 0.00 29.86  ? 327  ILE   A H    1 
ATOM   4503  H HA   . ILE   A  1 301 ? 21.579 -23.001 -18.611 0.00 29.79  ? 327  ILE   A HA   1 
ATOM   4504  H HB   . ILE   A  1 301 ? 24.582 -23.205 -19.015 0.00 28.48  ? 327  ILE   A HB   1 
ATOM   4505  H HG12 . ILE   A  1 301 ? 22.746 -20.818 -19.373 0.00 28.23  ? 327  ILE   A HG12 1 
ATOM   4506  H HG13 . ILE   A  1 301 ? 23.490 -21.196 -17.806 0.00 28.43  ? 327  ILE   A HG13 1 
ATOM   4507  H HG21 . ILE   A  1 301 ? 23.948 -22.188 -21.321 0.00 28.18  ? 327  ILE   A HG21 1 
ATOM   4508  H HG22 . ILE   A  1 301 ? 23.739 -23.931 -21.098 0.00 28.90  ? 327  ILE   A HG22 1 
ATOM   4509  H HG23 . ILE   A  1 301 ? 22.324 -22.847 -21.003 0.00 28.72  ? 327  ILE   A HG23 1 
ATOM   4510  H HD11 . ILE   A  1 301 ? 24.848 -19.525 -18.748 0.00 28.65  ? 327  ILE   A HD11 1 
ATOM   4511  H HD12 . ILE   A  1 301 ? 25.749 -21.046 -18.986 0.00 29.02  ? 327  ILE   A HD12 1 
ATOM   4512  H HD13 . ILE   A  1 301 ? 24.867 -20.302 -20.348 0.00 28.72  ? 327  ILE   A HD13 1 
ATOM   4513  N N    . ALA   A  1 302 ? 22.985 -25.981 -18.483 1.00 25.58  ? 328  ALA   A N    1 
ATOM   4514  C CA   . ALA   A  1 302 ? 22.806 -27.369 -18.906 1.00 26.77  ? 328  ALA   A CA   1 
ATOM   4515  C C    . ALA   A  1 302 ? 21.541 -28.040 -18.305 1.00 28.64  ? 328  ALA   A C    1 
ATOM   4516  O O    . ALA   A  1 302 ? 21.063 -29.012 -18.879 1.00 28.50  ? 328  ALA   A O    1 
ATOM   4517  C CB   . ALA   A  1 302 ? 24.039 -28.180 -18.509 1.00 26.53  ? 328  ALA   A CB   1 
ATOM   4518  H H    . ALA   A  1 302 ? 23.710 -25.871 -17.782 0.00 32.68  ? 328  ALA   A H    1 
ATOM   4519  H HA   . ALA   A  1 302 ? 22.722 -27.412 -19.991 0.00 34.69  ? 328  ALA   A HA   1 
ATOM   4520  H HB1  . ALA   A  1 302 ? 23.923 -29.200 -18.874 0.00 35.20  ? 328  ALA   A HB1  1 
ATOM   4521  H HB2  . ALA   A  1 302 ? 24.921 -27.724 -18.956 0.00 34.37  ? 328  ALA   A HB2  1 
ATOM   4522  H HB3  . ALA   A  1 302 ? 24.130 -28.183 -17.424 0.00 34.85  ? 328  ALA   A HB3  1 
ATOM   4523  N N    . SER   A  1 303 ? 21.027 -27.579 -17.151 1.00 30.59  ? 329  SER   A N    1 
ATOM   4524  C CA   . SER   A  1 303 ? 19.905 -28.266 -16.490 1.00 33.23  ? 329  SER   A CA   1 
ATOM   4525  C C    . SER   A  1 303 ? 18.953 -27.326 -15.746 1.00 35.49  ? 329  SER   A C    1 
ATOM   4526  O O    . SER   A  1 303 ? 18.422 -27.679 -14.681 1.00 37.25  ? 329  SER   A O    1 
ATOM   4527  C CB   . SER   A  1 303 ? 20.477 -29.276 -15.497 1.00 35.48  ? 329  SER   A CB   1 
ATOM   4528  O OG   . SER   A  1 303 ? 21.017 -28.607 -14.368 1.00 38.77  ? 329  SER   A OG   1 
ATOM   4529  H H    . SER   A  1 303 ? 21.354 -26.757 -16.655 0.00 39.56  ? 329  SER   A H    1 
ATOM   4530  H HA   . SER   A  1 303 ? 19.307 -28.812 -17.219 0.00 43.95  ? 329  SER   A HA   1 
ATOM   4531  H HB2  . SER   A  1 303 ? 19.690 -29.955 -15.173 0.00 47.40  ? 329  SER   A HB2  1 
ATOM   4532  H HB3  . SER   A  1 303 ? 21.273 -29.837 -15.985 0.00 46.98  ? 329  SER   A HB3  1 
ATOM   4533  H HG   . SER   A  1 303 ? 21.807 -28.065 -14.630 0.00 50.16  ? 329  SER   A HG   1 
ATOM   4534  N N    . GLY   A  1 304 ? 18.707 -26.174 -16.326 1.00 35.29  ? 330  GLY   A N    1 
ATOM   4535  C CA   . GLY   A  1 304 ? 17.905 -25.131 -15.712 1.00 36.01  ? 330  GLY   A CA   1 
ATOM   4536  C C    . GLY   A  1 304 ? 16.423 -25.377 -15.567 1.00 35.64  ? 330  GLY   A C    1 
ATOM   4537  O O    . GLY   A  1 304 ? 15.670 -25.210 -16.527 1.00 36.40  ? 330  GLY   A O    1 
ATOM   4538  H H    . GLY   A  1 304 ? 19.039 -25.918 -17.250 0.00 45.22  ? 330  GLY   A H    1 
ATOM   4539  H HA2  . GLY   A  1 304 ? 18.312 -24.924 -14.724 0.00 46.13  ? 330  GLY   A HA2  1 
ATOM   4540  H HA3  . GLY   A  1 304 ? 18.020 -24.226 -16.306 0.00 45.71  ? 330  GLY   A HA3  1 
ATOM   4541  N N    . ALA   A  1 305 ? 15.987 -25.697 -14.347 1.00 34.71  ? 331  ALA   A N    1 
ATOM   4542  C CA   . ALA   A  1 305 ? 14.569 -25.833 -14.041 1.00 34.30  ? 331  ALA   A CA   1 
ATOM   4543  C C    . ALA   A  1 305 ? 13.880 -24.455 -14.139 1.00 33.36  ? 331  ALA   A C    1 
ATOM   4544  O O    . ALA   A  1 305 ? 12.708 -24.397 -14.507 1.00 33.35  ? 331  ALA   A O    1 
ATOM   4545  C CB   . ALA   A  1 305 ? 14.389 -26.396 -12.639 1.00 34.53  ? 331  ALA   A CB   1 
ATOM   4546  H H    . ALA   A  1 305 ? 16.589 -25.876 -13.549 0.00 45.51  ? 331  ALA   A H    1 
ATOM   4547  H HA   . ALA   A  1 305 ? 14.099 -26.511 -14.753 0.00 45.74  ? 331  ALA   A HA   1 
ATOM   4548  H HB1  . ALA   A  1 305 ? 13.325 -26.503 -12.434 0.00 46.56  ? 331  ALA   A HB1  1 
ATOM   4549  H HB2  . ALA   A  1 305 ? 14.874 -27.370 -12.584 0.00 46.49  ? 331  ALA   A HB2  1 
ATOM   4550  H HB3  . ALA   A  1 305 ? 14.841 -25.714 -11.920 0.00 45.91  ? 331  ALA   A HB3  1 
ATOM   4551  N N    . PHE   A  1 306 ? 14.597 -23.349 -13.820 1.00 32.56  ? 332  PHE   A N    1 
ATOM   4552  C CA   . PHE   A  1 306 ? 14.021 -22.001 -13.905 1.00 32.86  ? 332  PHE   A CA   1 
ATOM   4553  C C    . PHE   A  1 306 ? 13.567 -21.639 -15.333 1.00 33.16  ? 332  PHE   A C    1 
ATOM   4554  O O    . PHE   A  1 306 ? 12.705 -20.782 -15.489 1.00 33.93  ? 332  PHE   A O    1 
ATOM   4555  C CB   . PHE   A  1 306 ? 15.011 -20.939 -13.382 1.00 32.48  ? 332  PHE   A CB   1 
ATOM   4556  C CG   . PHE   A  1 306 ? 16.117 -20.582 -14.348 1.00 32.84  ? 332  PHE   A CG   1 
ATOM   4557  C CD1  . PHE   A  1 306 ? 17.211 -21.409 -14.508 1.00 33.40  ? 332  PHE   A CD1  1 
ATOM   4558  C CD2  . PHE   A  1 306 ? 16.043 -19.435 -15.118 1.00 33.66  ? 332  PHE   A CD2  1 
ATOM   4559  C CE1  . PHE   A  1 306 ? 18.214 -21.091 -15.408 1.00 34.11  ? 332  PHE   A CE1  1 
ATOM   4560  C CE2  . PHE   A  1 306 ? 17.055 -19.115 -16.013 1.00 34.22  ? 332  PHE   A CE2  1 
ATOM   4561  C CZ   . PHE   A  1 306 ? 18.133 -19.942 -16.151 1.00 34.13  ? 332  PHE   A CZ   1 
ATOM   4562  H H    . PHE   A  1 306 ? 15.559 -23.355 -13.496 0.00 42.23  ? 332  PHE   A H    1 
ATOM   4563  H HA   . PHE   A  1 306 ? 13.140 -21.966 -13.266 0.00 42.80  ? 332  PHE   A HA   1 
ATOM   4564  H HB2  . PHE   A  1 306 ? 14.451 -20.029 -13.171 0.00 41.36  ? 332  PHE   A HB2  1 
ATOM   4565  H HB3  . PHE   A  1 306 ? 15.472 -21.298 -12.463 0.00 41.60  ? 332  PHE   A HB3  1 
ATOM   4566  H HD1  . PHE   A  1 306 ? 17.283 -22.313 -13.928 0.00 42.37  ? 332  PHE   A HD1  1 
ATOM   4567  H HD2  . PHE   A  1 306 ? 15.198 -18.775 -15.017 0.00 41.92  ? 332  PHE   A HD2  1 
ATOM   4568  H HE1  . PHE   A  1 306 ? 19.065 -21.739 -15.513 0.00 42.40  ? 332  PHE   A HE1  1 
ATOM   4569  H HE2  . PHE   A  1 306 ? 16.991 -18.215 -16.599 0.00 41.75  ? 332  PHE   A HE2  1 
ATOM   4570  H HZ   . PHE   A  1 306 ? 18.916 -19.692 -16.845 0.00 41.61  ? 332  PHE   A HZ   1 
ATOM   4571  N N    . LEU   A  1 307 ? 14.150 -22.277 -16.364 1.00 33.00  ? 333  LEU   A N    1 
ATOM   4572  C CA   . LEU   A  1 307 ? 13.794 -22.022 -17.761 1.00 33.14  ? 333  LEU   A CA   1 
ATOM   4573  C C    . LEU   A  1 307 ? 12.347 -22.426 -18.081 1.00 32.88  ? 333  LEU   A C    1 
ATOM   4574  O O    . LEU   A  1 307 ? 11.782 -21.911 -19.051 1.00 33.39  ? 333  LEU   A O    1 
ATOM   4575  C CB   . LEU   A  1 307 ? 14.759 -22.759 -18.697 1.00 33.85  ? 333  LEU   A CB   1 
ATOM   4576  C CG   . LEU   A  1 307 ? 16.245 -22.381 -18.591 1.00 35.76  ? 333  LEU   A CG   1 
ATOM   4577  C CD1  . LEU   A  1 307 ? 17.115 -23.478 -19.146 1.00 36.64  ? 333  LEU   A CD1  1 
ATOM   4578  C CD2  . LEU   A  1 307 ? 16.534 -21.100 -19.300 1.00 36.46  ? 333  LEU   A CD2  1 
ATOM   4579  H H    . LEU   A  1 307 ? 14.875 -22.980 -16.260 0.00 42.41  ? 333  LEU   A H    1 
ATOM   4580  H HA   . LEU   A  1 307 ? 13.880 -20.953 -17.951 0.00 42.00  ? 333  LEU   A HA   1 
ATOM   4581  H HB2  . LEU   A  1 307 ? 14.691 -23.820 -18.467 0.00 43.56  ? 333  LEU   A HB2  1 
ATOM   4582  H HB3  . LEU   A  1 307 ? 14.447 -22.586 -19.727 0.00 43.08  ? 333  LEU   A HB3  1 
ATOM   4583  H HG   . LEU   A  1 307 ? 16.518 -22.249 -17.545 0.00 44.89  ? 333  LEU   A HG   1 
ATOM   4584  H HD11 . LEU   A  1 307 ? 18.153 -23.151 -19.119 0.00 45.72  ? 333  LEU   A HD11 1 
ATOM   4585  H HD12 . LEU   A  1 307 ? 16.994 -24.372 -18.535 0.00 46.52  ? 333  LEU   A HD12 1 
ATOM   4586  H HD13 . LEU   A  1 307 ? 16.816 -23.685 -20.172 0.00 46.15  ? 333  LEU   A HD13 1 
ATOM   4587  H HD21 . LEU   A  1 307 ? 17.560 -20.806 -19.085 0.00 44.83  ? 333  LEU   A HD21 1 
ATOM   4588  H HD22 . LEU   A  1 307 ? 16.421 -21.271 -20.370 0.00 45.16  ? 333  LEU   A HD22 1 
ATOM   4589  H HD23 . LEU   A  1 307 ? 15.849 -20.323 -18.967 0.00 45.12  ? 333  LEU   A HD23 1 
ATOM   4590  N N    . THR   A  1 308 ? 11.741 -23.342 -17.282 1.00 31.50  ? 334  THR   A N    1 
ATOM   4591  C CA   . THR   A  1 308 ? 10.348 -23.748 -17.496 1.00 31.16  ? 334  THR   A CA   1 
ATOM   4592  C C    . THR   A  1 308 ? 9.347  -22.701 -16.926 1.00 30.62  ? 334  THR   A C    1 
ATOM   4593  O O    . THR   A  1 308 ? 8.181  -22.752 -17.261 1.00 30.56  ? 334  THR   A O    1 
ATOM   4594  C CB   . THR   A  1 308 ? 10.089 -25.145 -16.883 1.00 32.28  ? 334  THR   A CB   1 
ATOM   4595  O OG1  . THR   A  1 308 ? 10.066 -25.036 -15.464 1.00 33.69  ? 334  THR   A OG1  1 
ATOM   4596  C CG2  . THR   A  1 308 ? 11.148 -26.181 -17.296 1.00 32.80  ? 334  THR   A CG2  1 
ATOM   4597  H H    . THR   A  1 308 ? 12.179 -23.796 -16.487 0.00 41.69  ? 334  THR   A H    1 
ATOM   4598  H HA   . THR   A  1 308 ? 10.160 -23.835 -18.565 0.00 41.78  ? 334  THR   A HA   1 
ATOM   4599  H HB   . THR   A  1 308 ? 9.119  -25.504 -17.225 0.00 44.24  ? 334  THR   A HB   1 
ATOM   4600  H HG1  . THR   A  1 308 ? 10.956 -24.760 -15.123 0.00 45.21  ? 334  THR   A HG1  1 
ATOM   4601  H HG21 . THR   A  1 308 ? 10.822 -27.178 -17.004 0.00 44.98  ? 334  THR   A HG21 1 
ATOM   4602  H HG22 . THR   A  1 308 ? 11.300 -26.157 -18.373 0.00 44.27  ? 334  THR   A HG22 1 
ATOM   4603  H HG23 . THR   A  1 308 ? 12.096 -25.969 -16.803 0.00 44.09  ? 334  THR   A HG23 1 
ATOM   4604  N N    . MET   A  1 309 ? 9.807  -21.753 -16.098 1.00 30.30  ? 335  MET   A N    1 
ATOM   4605  C CA   . MET   A  1 309 ? 8.977  -20.739 -15.443 1.00 29.78  ? 335  MET   A CA   1 
ATOM   4606  C C    . MET   A  1 309 ? 8.884  -19.421 -16.214 1.00 28.90  ? 335  MET   A C    1 
ATOM   4607  O O    . MET   A  1 309 ? 8.272  -18.482 -15.701 1.00 29.20  ? 335  MET   A O    1 
ATOM   4608  C CB   . MET   A  1 309 ? 9.632  -20.404 -14.086 1.00 30.38  ? 335  MET   A CB   1 
ATOM   4609  C CG   . MET   A  1 309 ? 9.885  -21.607 -13.185 1.00 32.93  ? 335  MET   A CG   1 
ATOM   4610  S SD   . MET   A  1 309 ? 8.398  -22.566 -12.830 1.00 38.14  ? 335  MET   A SD   1 
ATOM   4611  C CE   . MET   A  1 309 ? 7.419  -21.348 -12.042 1.00 32.05  ? 335  MET   A CE   1 
ATOM   4612  H H    . MET   A  1 309 ? 10.786 -21.646 -15.855 0.00 40.02  ? 335  MET   A H    1 
ATOM   4613  H HA   . MET   A  1 309 ? 7.970  -21.116 -15.274 0.00 40.32  ? 335  MET   A HA   1 
ATOM   4614  H HB2  . MET   A  1 309 ? 10.595 -19.932 -14.273 0.00 39.85  ? 335  MET   A HB2  1 
ATOM   4615  H HB3  . MET   A  1 309 ? 8.995  -19.707 -13.545 0.00 40.46  ? 335  MET   A HB3  1 
ATOM   4616  H HG2  . MET   A  1 309 ? 10.608 -22.270 -13.654 0.00 43.72  ? 335  MET   A HG2  1 
ATOM   4617  H HG3  . MET   A  1 309 ? 10.281 -21.250 -12.235 0.00 43.72  ? 335  MET   A HG3  1 
ATOM   4618  H HE1  . MET   A  1 309 ? 6.610  -21.836 -11.501 0.00 44.32  ? 335  MET   A HE1  1 
ATOM   4619  H HE2  . MET   A  1 309 ? 8.043  -20.784 -11.350 0.00 43.46  ? 335  MET   A HE2  1 
ATOM   4620  H HE3  . MET   A  1 309 ? 7.011  -20.680 -12.800 0.00 43.61  ? 335  MET   A HE3  1 
ATOM   4621  N N    . LEU   A  1 310 ? 9.464  -19.333 -17.426 1.00 27.39  ? 336  LEU   A N    1 
ATOM   4622  C CA   . LEU   A  1 310 ? 9.581  -18.077 -18.155 1.00 26.66  ? 336  LEU   A CA   1 
ATOM   4623  C C    . LEU   A  1 310 ? 9.017  -18.128 -19.594 1.00 26.09  ? 336  LEU   A C    1 
ATOM   4624  O O    . LEU   A  1 310 ? 9.742  -17.853 -20.551 1.00 25.91  ? 336  LEU   A O    1 
ATOM   4625  C CB   . LEU   A  1 310 ? 11.094 -17.754 -18.168 1.00 26.92  ? 336  LEU   A CB   1 
ATOM   4626  C CG   . LEU   A  1 310 ? 11.756 -17.571 -16.795 1.00 28.95  ? 336  LEU   A CG   1 
ATOM   4627  C CD1  . LEU   A  1 310 ? 13.246 -17.371 -16.918 1.00 29.27  ? 336  LEU   A CD1  1 
ATOM   4628  C CD2  . LEU   A  1 310 ? 11.126 -16.408 -16.040 1.00 30.27  ? 336  LEU   A CD2  1 
ATOM   4629  H H    . LEU   A  1 310 ? 9.853  -20.115 -17.942 0.00 36.17  ? 336  LEU   A H    1 
ATOM   4630  H HA   . LEU   A  1 310 ? 9.058  -17.274 -17.641 0.00 34.84  ? 336  LEU   A HA   1 
ATOM   4631  H HB2  . LEU   A  1 310 ? 11.607 -18.573 -18.669 0.00 34.48  ? 336  LEU   A HB2  1 
ATOM   4632  H HB3  . LEU   A  1 310 ? 11.265 -16.836 -18.721 0.00 34.14  ? 336  LEU   A HB3  1 
ATOM   4633  H HG   . LEU   A  1 310 ? 11.603 -18.468 -16.196 0.00 37.13  ? 336  LEU   A HG   1 
ATOM   4634  H HD11 . LEU   A  1 310 ? 13.696 -17.442 -15.929 0.00 36.60  ? 336  LEU   A HD11 1 
ATOM   4635  H HD12 . LEU   A  1 310 ? 13.660 -18.138 -17.572 0.00 36.61  ? 336  LEU   A HD12 1 
ATOM   4636  H HD13 . LEU   A  1 310 ? 13.436 -16.385 -17.337 0.00 36.26  ? 336  LEU   A HD13 1 
ATOM   4637  H HD21 . LEU   A  1 310 ? 11.808 -16.079 -15.257 0.00 38.16  ? 336  LEU   A HD21 1 
ATOM   4638  H HD22 . LEU   A  1 310 ? 10.929 -15.599 -16.743 0.00 38.19  ? 336  LEU   A HD22 1 
ATOM   4639  H HD23 . LEU   A  1 310 ? 10.192 -16.745 -15.594 0.00 38.84  ? 336  LEU   A HD23 1 
ATOM   4640  N N    . PRO   A  1 311 ? 7.717  -18.432 -19.765 1.00 25.69  ? 337  PRO   A N    1 
ATOM   4641  C CA   . PRO   A  1 311 ? 7.160  -18.528 -21.125 1.00 25.79  ? 337  PRO   A CA   1 
ATOM   4642  C C    . PRO   A  1 311 ? 6.970  -17.208 -21.888 1.00 25.88  ? 337  PRO   A C    1 
ATOM   4643  O O    . PRO   A  1 311 ? 6.834  -17.251 -23.110 1.00 25.93  ? 337  PRO   A O    1 
ATOM   4644  C CB   . PRO   A  1 311 ? 5.822  -19.240 -20.904 1.00 26.52  ? 337  PRO   A CB   1 
ATOM   4645  C CG   . PRO   A  1 311 ? 5.411  -18.833 -19.534 1.00 27.06  ? 337  PRO   A CG   1 
ATOM   4646  C CD   . PRO   A  1 311 ? 6.703  -18.774 -18.746 1.00 25.23  ? 337  PRO   A CD   1 
ATOM   4647  H HA   . PRO   A  1 311 ? 7.785  -19.181 -21.732 0.00 34.56  ? 337  PRO   A HA   1 
ATOM   4648  H HB2  . PRO   A  1 311 ? 5.096  -18.907 -21.643 0.00 36.53  ? 337  PRO   A HB2  1 
ATOM   4649  H HB3  . PRO   A  1 311 ? 5.963  -20.318 -20.956 0.00 36.57  ? 337  PRO   A HB3  1 
ATOM   4650  H HG2  . PRO   A  1 311 ? 4.937  -17.853 -19.572 0.00 37.05  ? 337  PRO   A HG2  1 
ATOM   4651  H HG3  . PRO   A  1 311 ? 4.735  -19.577 -19.115 0.00 37.63  ? 337  PRO   A HG3  1 
ATOM   4652  H HD2  . PRO   A  1 311 ? 6.652  -17.995 -17.988 0.00 34.24  ? 337  PRO   A HD2  1 
ATOM   4653  H HD3  . PRO   A  1 311 ? 6.922  -19.744 -18.303 0.00 34.59  ? 337  PRO   A HD3  1 
ATOM   4654  N N    . ARG   A  1 312 ? 6.982  -16.056 -21.195 1.00 25.56  ? 338  ARG   A N    1 
ATOM   4655  C CA   . ARG   A  1 312 ? 6.853  -14.729 -21.820 1.00 25.74  ? 338  ARG   A CA   1 
ATOM   4656  C C    . ARG   A  1 312 ? 8.201  -13.988 -21.924 1.00 24.34  ? 338  ARG   A C    1 
ATOM   4657  O O    . ARG   A  1 312 ? 8.215  -12.842 -22.377 1.00 24.75  ? 338  ARG   A O    1 
ATOM   4658  C CB   . ARG   A  1 312 ? 5.850  -13.860 -21.012 1.00 28.54  ? 338  ARG   A CB   1 
ATOM   4659  C CG   . ARG   A  1 312 ? 4.553  -13.499 -21.740 1.00 35.90  ? 338  ARG   A CG   1 
ATOM   4660  C CD   . ARG   A  1 312 ? 3.328  -13.844 -20.937 1.00 41.94  ? 338  ARG   A CD   1 
ATOM   4661  N NE   . ARG   A  1 312 ? 3.162  -15.290 -20.788 1.00 48.02  ? 338  ARG   A NE   1 
ATOM   4662  C CZ   . ARG   A  1 312 ? 2.132  -15.874 -20.174 1.00 50.77  ? 338  ARG   A CZ   1 
ATOM   4663  N NH1  . ARG   A  1 312 ? 1.158  -15.137 -19.642 1.00 51.51  ? 338  ARG   A NH1  1 
ATOM   4664  N NH2  . ARG   A  1 312 ? 2.069  -17.199 -20.085 1.00 49.92  ? 338  ARG   A NH2  1 
ATOM   4665  H H    . ARG   A  1 312 ? 7.101  -16.005 -20.189 0.00 33.83  ? 338  ARG   A H    1 
ATOM   4666  H HA   . ARG   A  1 312 ? 6.513  -14.850 -22.847 0.00 33.94  ? 338  ARG   A HA   1 
ATOM   4667  H HB2  . ARG   A  1 312 ? 5.570  -14.395 -20.106 0.00 37.73  ? 338  ARG   A HB2  1 
ATOM   4668  H HB3  . ARG   A  1 312 ? 6.331  -12.925 -20.726 0.00 37.11  ? 338  ARG   A HB3  1 
ATOM   4669  H HG2  . ARG   A  1 312 ? 4.540  -12.426 -21.930 0.00 46.67  ? 338  ARG   A HG2  1 
ATOM   4670  H HG3  . ARG   A  1 312 ? 4.486  -14.039 -22.683 0.00 46.96  ? 338  ARG   A HG3  1 
ATOM   4671  H HD2  . ARG   A  1 312 ? 3.417  -13.412 -19.941 0.00 54.67  ? 338  ARG   A HD2  1 
ATOM   4672  H HD3  . ARG   A  1 312 ? 2.446  -13.453 -21.441 0.00 55.12  ? 338  ARG   A HD3  1 
ATOM   4673  H HE   . ARG   A  1 312 ? 3.882  -15.886 -21.183 0.00 62.20  ? 338  ARG   A HE   1 
ATOM   4674  H HH11 . ARG   A  1 312 ? 1.169  -14.124 -19.687 0.00 67.41  ? 338  ARG   A HH11 1 
ATOM   4675  H HH12 . ARG   A  1 312 ? 0.380  -15.594 -19.177 0.00 68.13  ? 338  ARG   A HH12 1 
ATOM   4676  H HH21 . ARG   A  1 312 ? 2.803  -17.774 -20.486 0.00 65.46  ? 338  ARG   A HH21 1 
ATOM   4677  H HH22 . ARG   A  1 312 ? 1.285  -17.644 -19.619 0.00 66.21  ? 338  ARG   A HH22 1 
ATOM   4678  N N    . LEU   A  1 313 ? 9.322  -14.615 -21.514 1.00 22.33  ? 339  LEU   A N    1 
ATOM   4679  C CA   . LEU   A  1 313 ? 10.617 -13.967 -21.573 1.00 21.59  ? 339  LEU   A CA   1 
ATOM   4680  C C    . LEU   A  1 313 ? 11.045 -13.732 -23.021 1.00 21.04  ? 339  LEU   A C    1 
ATOM   4681  O O    . LEU   A  1 313 ? 10.941 -14.633 -23.845 1.00 21.05  ? 339  LEU   A O    1 
ATOM   4682  C CB   . LEU   A  1 313 ? 11.663 -14.807 -20.833 1.00 21.43  ? 339  LEU   A CB   1 
ATOM   4683  C CG   . LEU   A  1 313 ? 13.001 -14.137 -20.553 1.00 22.36  ? 339  LEU   A CG   1 
ATOM   4684  C CD1  . LEU   A  1 313 ? 12.895 -13.245 -19.298 1.00 22.90  ? 339  LEU   A CD1  1 
ATOM   4685  C CD2  . LEU   A  1 313 ? 14.093 -15.188 -20.366 1.00 22.06  ? 339  LEU   A CD2  1 
ATOM   4686  H H    . LEU   A  1 313 ? 9.362  -15.565 -21.158 0.00 28.87  ? 339  LEU   A H    1 
ATOM   4687  H HA   . LEU   A  1 313 ? 10.545 -13.008 -21.065 0.00 27.02  ? 339  LEU   A HA   1 
ATOM   4688  H HB2  . LEU   A  1 313 ? 11.224 -14.998 -19.857 0.00 27.04  ? 339  LEU   A HB2  1 
ATOM   4689  H HB3  . LEU   A  1 313 ? 11.837 -15.737 -21.372 0.00 26.90  ? 339  LEU   A HB3  1 
ATOM   4690  H HG   . LEU   A  1 313 ? 13.302 -13.506 -21.388 0.00 27.03  ? 339  LEU   A HG   1 
ATOM   4691  H HD11 . LEU   A  1 313 ? 13.851 -12.743 -19.151 0.00 27.52  ? 339  LEU   A HD11 1 
ATOM   4692  H HD12 . LEU   A  1 313 ? 12.110 -12.505 -19.440 0.00 28.04  ? 339  LEU   A HD12 1 
ATOM   4693  H HD13 . LEU   A  1 313 ? 12.675 -13.865 -18.431 0.00 28.18  ? 339  LEU   A HD13 1 
ATOM   4694  H HD21 . LEU   A  1 313 ? 15.022 -14.686 -20.101 0.00 26.46  ? 339  LEU   A HD21 1 
ATOM   4695  H HD22 . LEU   A  1 313 ? 13.797 -15.873 -19.574 0.00 27.15  ? 339  LEU   A HD22 1 
ATOM   4696  H HD23 . LEU   A  1 313 ? 14.218 -15.732 -21.301 0.00 26.85  ? 339  LEU   A HD23 1 
ATOM   4697  N N    . GLU   A  1 314 ? 11.496 -12.519 -23.324 1.00 20.18  ? 340  GLU   A N    1 
ATOM   4698  C CA   . GLU   A  1 314 ? 11.932 -12.138 -24.667 1.00 19.83  ? 340  GLU   A CA   1 
ATOM   4699  C C    . GLU   A  1 314 ? 13.453 -12.000 -24.771 1.00 19.72  ? 340  GLU   A C    1 
ATOM   4700  O O    . GLU   A  1 314 ? 13.998 -12.304 -25.833 1.00 19.61  ? 340  GLU   A O    1 
ATOM   4701  C CB   . GLU   A  1 314 ? 11.249 -10.834 -25.088 1.00 21.78  ? 340  GLU   A CB   1 
ATOM   4702  C CG   . GLU   A  1 314 ? 9.745  -10.987 -25.244 1.00 28.10  ? 340  GLU   A CG   1 
ATOM   4703  C CD   . GLU   A  1 314 ? 9.010  -9.700  -25.558 1.00 35.34  ? 340  GLU   A CD   1 
ATOM   4704  O OE1  . GLU   A  1 314 ? 9.675  -8.713  -25.944 1.00 37.78  ? 340  GLU   A OE1  1 
ATOM   4705  O OE2  . GLU   A  1 314 ? 7.770  -9.674  -25.396 1.00 37.05  ? 340  GLU   A OE2  1 
ATOM   4706  H H    . GLU   A  1 314 ? 11.579 -11.762 -22.654 0.00 24.64  ? 340  GLU   A H    1 
ATOM   4707  H HA   . GLU   A  1 314 ? 11.627 -12.893 -25.389 0.00 24.32  ? 340  GLU   A HA   1 
ATOM   4708  H HB2  . GLU   A  1 314 ? 11.435 -10.073 -24.333 0.00 26.30  ? 340  GLU   A HB2  1 
ATOM   4709  H HB3  . GLU   A  1 314 ? 11.657 -10.517 -26.047 0.00 26.25  ? 340  GLU   A HB3  1 
ATOM   4710  H HG2  . GLU   A  1 314 ? 9.549  -11.681 -26.060 0.00 34.84  ? 340  GLU   A HG2  1 
ATOM   4711  H HG3  . GLU   A  1 314 ? 9.326  -11.381 -24.318 0.00 34.91  ? 340  GLU   A HG3  1 
ATOM   4712  N N    . ILE   A  1 315 ? 14.141 -11.525 -23.719 1.00 19.19  ? 341  ILE   A N    1 
ATOM   4713  C CA   . ILE   A  1 315 ? 15.600 -11.371 -23.773 1.00 19.95  ? 341  ILE   A CA   1 
ATOM   4714  C C    . ILE   A  1 315 ? 16.230 -12.088 -22.591 1.00 19.90  ? 341  ILE   A C    1 
ATOM   4715  O O    . ILE   A  1 315 ? 15.875 -11.821 -21.447 1.00 20.63  ? 341  ILE   A O    1 
ATOM   4716  C CB   . ILE   A  1 315 ? 16.031 -9.879  -23.812 1.00 20.90  ? 341  ILE   A CB   1 
ATOM   4717  C CG1  . ILE   A  1 315 ? 15.287 -9.124  -24.964 1.00 21.87  ? 341  ILE   A CG1  1 
ATOM   4718  C CG2  . ILE   A  1 315 ? 17.567 -9.775  -23.951 1.00 21.90  ? 341  ILE   A CG2  1 
ATOM   4719  C CD1  . ILE   A  1 315 ? 15.569 -7.634  -25.049 1.00 23.64  ? 341  ILE   A CD1  1 
ATOM   4720  H H    . ILE   A  1 315 ? 13.730 -11.234 -22.838 0.00 22.60  ? 341  ILE   A H    1 
ATOM   4721  H HA   . ILE   A  1 315 ? 15.988 -11.830 -24.680 0.00 22.81  ? 341  ILE   A HA   1 
ATOM   4722  H HB   . ILE   A  1 315 ? 15.745 -9.423  -22.865 0.00 23.74  ? 341  ILE   A HB   1 
ATOM   4723  H HG12 . ILE   A  1 315 ? 15.583 -9.570  -25.912 0.00 24.86  ? 341  ILE   A HG12 1 
ATOM   4724  H HG13 . ILE   A  1 315 ? 14.212 -9.230  -24.828 0.00 25.29  ? 341  ILE   A HG13 1 
ATOM   4725  H HG21 . ILE   A  1 315 ? 17.858 -8.733  -24.069 0.00 24.17  ? 341  ILE   A HG21 1 
ATOM   4726  H HG22 . ILE   A  1 315 ? 18.047 -10.165 -23.054 0.00 24.37  ? 341  ILE   A HG22 1 
ATOM   4727  H HG23 . ILE   A  1 315 ? 17.882 -10.348 -24.821 0.00 24.35  ? 341  ILE   A HG23 1 
ATOM   4728  H HD11 . ILE   A  1 315 ? 14.803 -7.164  -25.665 0.00 26.96  ? 341  ILE   A HD11 1 
ATOM   4729  H HD12 . ILE   A  1 315 ? 15.555 -7.208  -24.047 0.00 26.77  ? 341  ILE   A HD12 1 
ATOM   4730  H HD13 . ILE   A  1 315 ? 16.545 -7.477  -25.507 0.00 26.44  ? 341  ILE   A HD13 1 
ATOM   4731  N N    . LEU   A  1 316 ? 17.175 -12.980 -22.867 1.00 19.27  ? 342  LEU   A N    1 
ATOM   4732  C CA   . LEU   A  1 316 ? 17.868 -13.734 -21.839 1.00 18.82  ? 342  LEU   A CA   1 
ATOM   4733  C C    . LEU   A  1 316 ? 19.353 -13.493 -22.035 1.00 18.50  ? 342  LEU   A C    1 
ATOM   4734  O O    . LEU   A  1 316 ? 19.882 -13.815 -23.100 1.00 18.65  ? 342  LEU   A O    1 
ATOM   4735  C CB   . LEU   A  1 316 ? 17.528 -15.234 -21.976 1.00 18.76  ? 342  LEU   A CB   1 
ATOM   4736  C CG   . LEU   A  1 316 ? 18.256 -16.198 -21.009 1.00 19.94  ? 342  LEU   A CG   1 
ATOM   4737  C CD1  . LEU   A  1 316 ? 18.062 -15.778 -19.524 1.00 19.78  ? 342  LEU   A CD1  1 
ATOM   4738  C CD2  . LEU   A  1 316 ? 17.764 -17.641 -21.217 1.00 20.58  ? 342  LEU   A CD2  1 
ATOM   4739  H H    . LEU   A  1 316 ? 17.493 -13.209 -23.803 0.00 21.85  ? 342  LEU   A H    1 
ATOM   4740  H HA   . LEU   A  1 316 ? 17.581 -13.397 -20.844 0.00 21.52  ? 342  LEU   A HA   1 
ATOM   4741  H HB2  . LEU   A  1 316 ? 16.459 -15.361 -21.814 0.00 22.12  ? 342  LEU   A HB2  1 
ATOM   4742  H HB3  . LEU   A  1 316 ? 17.779 -15.546 -22.989 0.00 21.73  ? 342  LEU   A HB3  1 
ATOM   4743  H HG   . LEU   A  1 316 ? 19.323 -16.181 -21.224 0.00 23.05  ? 342  LEU   A HG   1 
ATOM   4744  H HD11 . LEU   A  1 316 ? 18.454 -16.567 -18.884 0.00 23.37  ? 342  LEU   A HD11 1 
ATOM   4745  H HD12 . LEU   A  1 316 ? 18.609 -14.855 -19.338 0.00 22.88  ? 342  LEU   A HD12 1 
ATOM   4746  H HD13 . LEU   A  1 316 ? 17.001 -15.633 -19.328 0.00 23.46  ? 342  LEU   A HD13 1 
ATOM   4747  H HD21 . LEU   A  1 316 ? 18.297 -18.299 -20.531 0.00 24.69  ? 342  LEU   A HD21 1 
ATOM   4748  H HD22 . LEU   A  1 316 ? 16.695 -17.685 -21.016 0.00 24.88  ? 342  LEU   A HD22 1 
ATOM   4749  H HD23 . LEU   A  1 316 ? 17.961 -17.938 -22.246 0.00 24.54  ? 342  LEU   A HD23 1 
ATOM   4750  N N    . ASP   A  1 317 ? 20.023 -12.870 -21.055 1.00 18.49  ? 343  ASP   A N    1 
ATOM   4751  C CA   . ASP   A  1 317 ? 21.464 -12.611 -21.171 1.00 18.47  ? 343  ASP   A CA   1 
ATOM   4752  C C    . ASP   A  1 317 ? 22.245 -13.476 -20.189 1.00 18.50  ? 343  ASP   A C    1 
ATOM   4753  O O    . ASP   A  1 317 ? 22.177 -13.266 -18.976 1.00 18.18  ? 343  ASP   A O    1 
ATOM   4754  C CB   . ASP   A  1 317 ? 21.793 -11.112 -20.995 1.00 19.26  ? 343  ASP   A CB   1 
ATOM   4755  C CG   . ASP   A  1 317 ? 23.171 -10.738 -21.534 1.00 24.04  ? 343  ASP   A CG   1 
ATOM   4756  O OD1  . ASP   A  1 317 ? 24.060 -11.609 -21.553 1.00 24.46  ? 343  ASP   A OD1  1 
ATOM   4757  O OD2  . ASP   A  1 317 ? 23.352 -9.577  -21.964 1.00 25.97  ? 343  ASP   A OD2  1 
ATOM   4758  H H    . ASP   A  1 317 ? 19.614 -12.540 -20.186 0.00 20.51  ? 343  ASP   A H    1 
ATOM   4759  H HA   . ASP   A  1 317 ? 21.787 -12.890 -22.170 0.00 19.92  ? 343  ASP   A HA   1 
ATOM   4760  H HB2  . ASP   A  1 317 ? 21.053 -10.527 -21.541 0.00 20.65  ? 343  ASP   A HB2  1 
ATOM   4761  H HB3  . ASP   A  1 317 ? 21.758 -10.854 -19.938 0.00 20.72  ? 343  ASP   A HB3  1 
ATOM   4762  N N    . LEU   A  1 318 ? 22.961 -14.468 -20.710 1.00 18.35  ? 344  LEU   A N    1 
ATOM   4763  C CA   . LEU   A  1 318 ? 23.776 -15.375 -19.904 1.00 19.18  ? 344  LEU   A CA   1 
ATOM   4764  C C    . LEU   A  1 318 ? 25.274 -15.210 -20.229 1.00 19.15  ? 344  LEU   A C    1 
ATOM   4765  O O    . LEU   A  1 318 ? 26.048 -16.144 -20.028 1.00 19.38  ? 344  LEU   A O    1 
ATOM   4766  C CB   . LEU   A  1 318 ? 23.311 -16.822 -20.171 1.00 19.12  ? 344  LEU   A CB   1 
ATOM   4767  C CG   . LEU   A  1 318 ? 21.990 -17.233 -19.519 1.00 20.63  ? 344  LEU   A CG   1 
ATOM   4768  C CD1  . LEU   A  1 318 ? 21.360 -18.385 -20.286 1.00 21.45  ? 344  LEU   A CD1  1 
ATOM   4769  C CD2  . LEU   A  1 318 ? 22.203 -17.608 -18.043 1.00 21.10  ? 344  LEU   A CD2  1 
ATOM   4770  H H    . LEU   A  1 318 ? 23.009 -14.677 -21.703 0.00 19.98  ? 344  LEU   A H    1 
ATOM   4771  H HA   . LEU   A  1 318 ? 23.657 -15.166 -18.841 0.00 21.29  ? 344  LEU   A HA   1 
ATOM   4772  H HB2  . LEU   A  1 318 ? 23.199 -16.957 -21.246 0.00 21.50  ? 344  LEU   A HB2  1 
ATOM   4773  H HB3  . LEU   A  1 318 ? 24.060 -17.519 -19.798 0.00 21.67  ? 344  LEU   A HB3  1 
ATOM   4774  H HG   . LEU   A  1 318 ? 21.283 -16.405 -19.549 0.00 23.66  ? 344  LEU   A HG   1 
ATOM   4775  H HD11 . LEU   A  1 318 ? 20.708 -18.951 -19.621 0.00 25.47  ? 344  LEU   A HD11 1 
ATOM   4776  H HD12 . LEU   A  1 318 ? 20.778 -17.983 -21.113 0.00 25.03  ? 344  LEU   A HD12 1 
ATOM   4777  H HD13 . LEU   A  1 318 ? 22.150 -19.022 -20.679 0.00 25.12  ? 344  LEU   A HD13 1 
ATOM   4778  H HD21 . LEU   A  1 318 ? 21.241 -17.853 -17.596 0.00 24.86  ? 344  LEU   A HD21 1 
ATOM   4779  H HD22 . LEU   A  1 318 ? 22.863 -18.472 -17.988 0.00 24.71  ? 344  LEU   A HD22 1 
ATOM   4780  H HD23 . LEU   A  1 318 ? 22.649 -16.769 -17.512 0.00 24.33  ? 344  LEU   A HD23 1 
ATOM   4781  N N    . SER   A  1 319 ? 25.692 -14.017 -20.685 1.00 18.75  ? 345  SER   A N    1 
ATOM   4782  C CA   . SER   A  1 319 ? 27.079 -13.789 -21.066 1.00 18.85  ? 345  SER   A CA   1 
ATOM   4783  C C    . SER   A  1 319 ? 28.048 -13.849 -19.891 1.00 19.61  ? 345  SER   A C    1 
ATOM   4784  O O    . SER   A  1 319 ? 27.673 -13.581 -18.752 1.00 20.97  ? 345  SER   A O    1 
ATOM   4785  C CB   . SER   A  1 319 ? 27.234 -12.438 -21.759 1.00 19.03  ? 345  SER   A CB   1 
ATOM   4786  O OG   . SER   A  1 319 ? 26.466 -12.386 -22.951 1.00 20.17  ? 345  SER   A OG   1 
ATOM   4787  H H    . SER   A  1 319 ? 25.110 -13.192 -20.786 0.00 19.88  ? 345  SER   A H    1 
ATOM   4788  H HA   . SER   A  1 319 ? 27.365 -14.558 -21.782 0.00 19.93  ? 345  SER   A HA   1 
ATOM   4789  H HB2  . SER   A  1 319 ? 26.887 -11.651 -21.093 0.00 19.65  ? 345  SER   A HB2  1 
ATOM   4790  H HB3  . SER   A  1 319 ? 28.293 -12.272 -21.946 0.00 19.53  ? 345  SER   A HB3  1 
ATOM   4791  H HG   . SER   A  1 319 ? 25.511 -12.216 -22.734 0.00 21.15  ? 345  SER   A HG   1 
ATOM   4792  N N    . PHE   A  1 320 ? 29.288 -14.214 -20.185 1.00 18.29  ? 346  PHE   A N    1 
ATOM   4793  C CA   . PHE   A  1 320 ? 30.392 -14.286 -19.259 1.00 19.03  ? 346  PHE   A CA   1 
ATOM   4794  C C    . PHE   A  1 320 ? 30.100 -15.120 -18.017 1.00 19.61  ? 346  PHE   A C    1 
ATOM   4795  O O    . PHE   A  1 320 ? 30.345 -14.704 -16.881 1.00 19.77  ? 346  PHE   A O    1 
ATOM   4796  C CB   . PHE   A  1 320 ? 30.874 -12.865 -18.916 1.00 19.28  ? 346  PHE   A CB   1 
ATOM   4797  C CG   . PHE   A  1 320 ? 31.589 -12.234 -20.092 1.00 20.73  ? 346  PHE   A CG   1 
ATOM   4798  C CD1  . PHE   A  1 320 ? 32.876 -12.624 -20.430 1.00 21.95  ? 346  PHE   A CD1  1 
ATOM   4799  C CD2  . PHE   A  1 320 ? 30.947 -11.313 -20.901 1.00 22.02  ? 346  PHE   A CD2  1 
ATOM   4800  C CE1  . PHE   A  1 320 ? 33.507 -12.107 -21.560 1.00 22.90  ? 346  PHE   A CE1  1 
ATOM   4801  C CE2  . PHE   A  1 320 ? 31.595 -10.770 -22.015 1.00 22.77  ? 346  PHE   A CE2  1 
ATOM   4802  C CZ   . PHE   A  1 320 ? 32.865 -11.173 -22.335 1.00 22.75  ? 346  PHE   A CZ   1 
ATOM   4803  H H    . PHE   A  1 320 ? 29.571 -14.478 -21.124 0.00 19.12  ? 346  PHE   A H    1 
ATOM   4804  H HA   . PHE   A  1 320 ? 31.200 -14.818 -19.761 0.00 20.18  ? 346  PHE   A HA   1 
ATOM   4805  H HB2  . PHE   A  1 320 ? 30.027 -12.237 -18.644 0.00 20.11  ? 346  PHE   A HB2  1 
ATOM   4806  H HB3  . PHE   A  1 320 ? 31.590 -12.902 -18.098 0.00 20.27  ? 346  PHE   A HB3  1 
ATOM   4807  H HD1  . PHE   A  1 320 ? 33.377 -13.368 -19.837 0.00 23.29  ? 346  PHE   A HD1  1 
ATOM   4808  H HD2  . PHE   A  1 320 ? 29.944 -11.000 -20.664 0.00 22.89  ? 346  PHE   A HD2  1 
ATOM   4809  H HE1  . PHE   A  1 320 ? 34.513 -12.406 -21.801 0.00 23.95  ? 346  PHE   A HE1  1 
ATOM   4810  H HE2  . PHE   A  1 320 ? 31.093 -10.041 -22.627 0.00 23.32  ? 346  PHE   A HE2  1 
ATOM   4811  H HZ   . PHE   A  1 320 ? 33.367 -10.746 -23.188 0.00 23.28  ? 346  PHE   A HZ   1 
ATOM   4812  N N    . ASN   A  1 321 ? 29.644 -16.344 -18.252 1.00 19.52  ? 347  ASN   A N    1 
ATOM   4813  C CA   . ASN   A  1 321 ? 29.467 -17.320 -17.184 1.00 20.29  ? 347  ASN   A CA   1 
ATOM   4814  C C    . ASN   A  1 321 ? 30.564 -18.429 -17.293 1.00 21.25  ? 347  ASN   A C    1 
ATOM   4815  O O    . ASN   A  1 321 ? 30.459 -19.455 -16.621 1.00 21.18  ? 347  ASN   A O    1 
ATOM   4816  C CB   . ASN   A  1 321 ? 28.045 -17.907 -17.248 1.00 20.29  ? 347  ASN   A CB   1 
ATOM   4817  C CG   . ASN   A  1 321 ? 27.031 -17.061 -16.518 1.00 22.34  ? 347  ASN   A CG   1 
ATOM   4818  O OD1  . ASN   A  1 321 ? 26.751 -17.293 -15.351 1.00 22.93  ? 347  ASN   A OD1  1 
ATOM   4819  N ND2  . ASN   A  1 321 ? 26.479 -16.049 -17.161 1.00 22.81  ? 347  ASN   A ND2  1 
ATOM   4820  H H    . ASN   A  1 321 ? 29.411 -16.696 -19.175 0.00 21.43  ? 347  ASN   A H    1 
ATOM   4821  H HA   . ASN   A  1 321 ? 29.614 -16.858 -16.209 0.00 22.85  ? 347  ASN   A HA   1 
ATOM   4822  H HB2  . ASN   A  1 321 ? 27.732 -17.993 -18.288 0.00 22.98  ? 347  ASN   A HB2  1 
ATOM   4823  H HB3  . ASN   A  1 321 ? 28.028 -18.891 -16.783 0.00 23.45  ? 347  ASN   A HB3  1 
ATOM   4824  H HD21 . ASN   A  1 321 ? 25.793 -15.467 -16.694 0.00 25.73  ? 347  ASN   A HD21 1 
ATOM   4825  H HD22 . ASN   A  1 321 ? 26.742 -15.853 -18.122 0.00 25.51  ? 347  ASN   A HD22 1 
ATOM   4826  N N    . TYR   A  1 322 ? 31.640 -18.203 -18.082 1.00 21.17  ? 348  TYR   A N    1 
ATOM   4827  C CA   . TYR   A  1 322 ? 32.690 -19.190 -18.258 1.00 21.53  ? 348  TYR   A CA   1 
ATOM   4828  C C    . TYR   A  1 322 ? 33.300 -19.681 -16.949 1.00 23.29  ? 348  TYR   A C    1 
ATOM   4829  O O    . TYR   A  1 322 ? 33.332 -18.960 -15.948 1.00 23.50  ? 348  TYR   A O    1 
ATOM   4830  C CB   . TYR   A  1 322 ? 33.806 -18.642 -19.166 1.00 20.81  ? 348  TYR   A CB   1 
ATOM   4831  C CG   . TYR   A  1 322 ? 34.666 -17.558 -18.552 1.00 20.33  ? 348  TYR   A CG   1 
ATOM   4832  C CD1  . TYR   A  1 322 ? 34.415 -16.217 -18.808 1.00 20.30  ? 348  TYR   A CD1  1 
ATOM   4833  C CD2  . TYR   A  1 322 ? 35.817 -17.875 -17.844 1.00 20.66  ? 348  TYR   A CD2  1 
ATOM   4834  C CE1  . TYR   A  1 322 ? 35.233 -15.220 -18.292 1.00 20.92  ? 348  TYR   A CE1  1 
ATOM   4835  C CE2  . TYR   A  1 322 ? 36.614 -16.889 -17.283 1.00 21.22  ? 348  TYR   A CE2  1 
ATOM   4836  C CZ   . TYR   A  1 322 ? 36.339 -15.562 -17.536 1.00 21.80  ? 348  TYR   A CZ   1 
ATOM   4837  O OH   . TYR   A  1 322 ? 37.172 -14.591 -17.034 1.00 23.46  ? 348  TYR   A OH   1 
ATOM   4838  H H    . TYR   A  1 322 ? 31.813 -17.344 -18.594 0.00 23.60  ? 348  TYR   A H    1 
ATOM   4839  H HA   . TYR   A  1 322 ? 32.255 -20.051 -18.763 0.00 24.86  ? 348  TYR   A HA   1 
ATOM   4840  H HB2  . TYR   A  1 322 ? 34.465 -19.467 -19.433 0.00 23.72  ? 348  TYR   A HB2  1 
ATOM   4841  H HB3  . TYR   A  1 322 ? 33.353 -18.235 -20.069 0.00 23.21  ? 348  TYR   A HB3  1 
ATOM   4842  H HD1  . TYR   A  1 322 ? 33.554 -15.943 -19.396 0.00 22.02  ? 348  TYR   A HD1  1 
ATOM   4843  H HD2  . TYR   A  1 322 ? 36.038 -18.908 -17.633 0.00 23.71  ? 348  TYR   A HD2  1 
ATOM   4844  H HE1  . TYR   A  1 322 ? 35.004 -14.184 -18.479 0.00 22.47  ? 348  TYR   A HE1  1 
ATOM   4845  H HE2  . TYR   A  1 322 ? 37.489 -17.161 -16.715 0.00 24.09  ? 348  TYR   A HE2  1 
ATOM   4846  H HH   . TYR   A  1 322 ? 36.916 -14.384 -16.097 0.00 26.09  ? 348  TYR   A HH   1 
ATOM   4847  N N    . ILE   A  1 323 ? 33.810 -20.905 -16.975 1.00 23.79  ? 349  ILE   A N    1 
ATOM   4848  C CA   . ILE   A  1 323 ? 34.509 -21.486 -15.836 1.00 25.44  ? 349  ILE   A CA   1 
ATOM   4849  C C    . ILE   A  1 323 ? 35.986 -21.197 -16.089 1.00 26.22  ? 349  ILE   A C    1 
ATOM   4850  O O    . ILE   A  1 323 ? 36.533 -21.655 -17.095 1.00 25.40  ? 349  ILE   A O    1 
ATOM   4851  C CB   . ILE   A  1 323 ? 34.229 -23.011 -15.705 1.00 26.42  ? 349  ILE   A CB   1 
ATOM   4852  C CG1  . ILE   A  1 323 ? 32.768 -23.279 -15.298 1.00 28.11  ? 349  ILE   A CG1  1 
ATOM   4853  C CG2  . ILE   A  1 323 ? 35.205 -23.655 -14.692 1.00 26.92  ? 349  ILE   A CG2  1 
ATOM   4854  C CD1  . ILE   A  1 323 ? 32.253 -24.754 -15.644 1.00 29.58  ? 349  ILE   A CD1  1 
ATOM   4855  H H    . ILE   A  1 323 ? 33.770 -21.515 -17.785 0.00 28.26  ? 349  ILE   A H    1 
ATOM   4856  H HA   . ILE   A  1 323 ? 34.202 -21.015 -14.905 0.00 30.58  ? 349  ILE   A HA   1 
ATOM   4857  H HB   . ILE   A  1 323 ? 34.348 -23.470 -16.682 0.00 32.37  ? 349  ILE   A HB   1 
ATOM   4858  H HG12 . ILE   A  1 323 ? 32.676 -23.140 -14.223 0.00 34.68  ? 349  ILE   A HG12 1 
ATOM   4859  H HG13 . ILE   A  1 323 ? 32.118 -22.577 -15.818 0.00 34.15  ? 349  ILE   A HG13 1 
ATOM   4860  H HG21 . ILE   A  1 323 ? 34.787 -24.588 -14.319 0.00 33.91  ? 349  ILE   A HG21 1 
ATOM   4861  H HG22 . ILE   A  1 323 ? 36.150 -23.865 -15.192 0.00 33.51  ? 349  ILE   A HG22 1 
ATOM   4862  H HG23 . ILE   A  1 323 ? 35.365 -22.966 -13.865 0.00 33.38  ? 349  ILE   A HG23 1 
ATOM   4863  H HD11 . ILE   A  1 323 ? 31.197 -24.826 -15.390 0.00 36.89  ? 349  ILE   A HD11 1 
ATOM   4864  H HD12 . ILE   A  1 323 ? 32.389 -24.934 -16.709 0.00 36.72  ? 349  ILE   A HD12 1 
ATOM   4865  H HD13 . ILE   A  1 323 ? 32.814 -25.489 -15.071 0.00 37.25  ? 349  ILE   A HD13 1 
ATOM   4866  N N    . LYS   A  1 324 ? 36.640 -20.431 -15.198 1.00 27.21  ? 350  LYS   A N    1 
ATOM   4867  C CA   . LYS   A  1 324 ? 38.069 -20.110 -15.321 1.00 28.87  ? 350  LYS   A CA   1 
ATOM   4868  C C    . LYS   A  1 324 ? 38.901 -21.404 -15.460 1.00 29.74  ? 350  LYS   A C    1 
ATOM   4869  O O    . LYS   A  1 324 ? 38.696 -22.340 -14.693 1.00 29.99  ? 350  LYS   A O    1 
ATOM   4870  C CB   . LYS   A  1 324 ? 38.535 -19.324 -14.070 1.00 31.74  ? 350  LYS   A CB   1 
ATOM   4871  C CG   . LYS   A  1 324 ? 40.010 -18.921 -14.099 1.00 37.12  ? 350  LYS   A CG   1 
ATOM   4872  C CD   . LYS   A  1 324 ? 40.495 -18.289 -12.793 1.00 41.23  ? 350  LYS   A CD   1 
ATOM   4873  C CE   . LYS   A  1 324 ? 42.007 -18.244 -12.767 1.00 45.15  ? 350  LYS   A CE   1 
ATOM   4874  N NZ   . LYS   A  1 324 ? 42.535 -17.637 -11.521 1.00 47.88  ? 350  LYS   A NZ   1 
ATOM   4875  H H    . LYS   A  1 324 ? 36.208 -20.013 -14.380 0.00 32.57  ? 350  LYS   A H    1 
ATOM   4876  H HA   . LYS   A  1 324 ? 38.223 -19.487 -16.201 0.00 34.18  ? 350  LYS   A HA   1 
ATOM   4877  H HB2  . LYS   A  1 324 ? 37.948 -18.408 -14.002 0.00 37.69  ? 350  LYS   A HB2  1 
ATOM   4878  H HB3  . LYS   A  1 324 ? 38.375 -19.934 -13.184 0.00 38.43  ? 350  LYS   A HB3  1 
ATOM   4879  H HG2  . LYS   A  1 324 ? 40.635 -19.794 -14.280 0.00 44.89  ? 350  LYS   A HG2  1 
ATOM   4880  H HG3  . LYS   A  1 324 ? 40.159 -18.193 -14.896 0.00 44.15  ? 350  LYS   A HG3  1 
ATOM   4881  H HD2  . LYS   A  1 324 ? 40.118 -17.270 -12.722 0.00 49.28  ? 350  LYS   A HD2  1 
ATOM   4882  H HD3  . LYS   A  1 324 ? 40.151 -18.887 -11.950 0.00 49.99  ? 350  LYS   A HD3  1 
ATOM   4883  H HE2  . LYS   A  1 324 ? 42.398 -19.258 -12.836 0.00 54.96  ? 350  LYS   A HE2  1 
ATOM   4884  H HE3  . LYS   A  1 324 ? 42.360 -17.650 -13.609 0.00 54.23  ? 350  LYS   A HE3  1 
ATOM   4885  H HZ1  . LYS   A  1 324 ? 43.550 -17.632 -11.542 0.00 58.24  ? 350  LYS   A HZ1  1 
ATOM   4886  H HZ2  . LYS   A  1 324 ? 42.205 -16.681 -11.434 0.00 57.73  ? 350  LYS   A HZ2  1 
ATOM   4887  H HZ3  . LYS   A  1 324 ? 42.225 -18.170 -10.715 0.00 58.39  ? 350  LYS   A HZ3  1 
ATOM   4888  N N    . GLY   A  1 325 ? 39.753 -21.468 -16.474 1.00 29.69  ? 351  GLY   A N    1 
ATOM   4889  C CA   . GLY   A  1 325 ? 40.580 -22.651 -16.693 1.00 29.97  ? 351  GLY   A CA   1 
ATOM   4890  C C    . GLY   A  1 325 ? 39.912 -23.774 -17.471 1.00 29.60  ? 351  GLY   A C    1 
ATOM   4891  O O    . GLY   A  1 325 ? 40.589 -24.733 -17.840 1.00 29.93  ? 351  GLY   A O    1 
ATOM   4892  H H    . GLY   A  1 325 ? 39.903 -20.732 -17.156 0.00 35.61  ? 351  GLY   A H    1 
ATOM   4893  H HA2  . GLY   A  1 325 ? 41.463 -22.350 -17.255 0.00 36.76  ? 351  GLY   A HA2  1 
ATOM   4894  H HA3  . GLY   A  1 325 ? 40.921 -23.048 -15.738 0.00 37.26  ? 351  GLY   A HA3  1 
ATOM   4895  N N    . SER   A  1 326 ? 38.606 -23.652 -17.797 1.00 28.02  ? 352  SER   A N    1 
ATOM   4896  C CA   . SER   A  1 326 ? 37.893 -24.686 -18.550 1.00 27.43  ? 352  SER   A CA   1 
ATOM   4897  C C    . SER   A  1 326 ? 37.546 -24.187 -19.952 1.00 26.69  ? 352  SER   A C    1 
ATOM   4898  O O    . SER   A  1 326 ? 36.838 -23.197 -20.087 1.00 26.17  ? 352  SER   A O    1 
ATOM   4899  C CB   . SER   A  1 326 ? 36.609 -25.056 -17.827 1.00 29.20  ? 352  SER   A CB   1 
ATOM   4900  O OG   . SER   A  1 326 ? 35.870 -26.045 -18.522 1.00 31.97  ? 352  SER   A OG   1 
ATOM   4901  H H    . SER   A  1 326 ? 38.017 -22.858 -17.567 0.00 34.15  ? 352  SER   A H    1 
ATOM   4902  H HA   . SER   A  1 326 ? 38.489 -25.594 -18.635 0.00 34.49  ? 352  SER   A HA   1 
ATOM   4903  H HB2  . SER   A  1 326 ? 36.837 -25.397 -16.818 0.00 36.67  ? 352  SER   A HB2  1 
ATOM   4904  H HB3  . SER   A  1 326 ? 36.023 -24.143 -17.805 0.00 35.90  ? 352  SER   A HB3  1 
ATOM   4905  H HG   . SER   A  1 326 ? 35.047 -26.269 -18.013 0.00 40.05  ? 352  SER   A HG   1 
ATOM   4906  N N    . TYR   A  1 327 ? 38.004 -24.896 -20.990 1.00 26.01  ? 353  TYR   A N    1 
ATOM   4907  C CA   . TYR   A  1 327 ? 37.753 -24.547 -22.389 1.00 25.65  ? 353  TYR   A CA   1 
ATOM   4908  C C    . TYR   A  1 327 ? 37.141 -25.813 -23.009 1.00 26.08  ? 353  TYR   A C    1 
ATOM   4909  O O    . TYR   A  1 327 ? 37.835 -26.582 -23.668 1.00 26.70  ? 353  TYR   A O    1 
ATOM   4910  C CB   . TYR   A  1 327 ? 39.101 -24.154 -23.026 1.00 24.94  ? 353  TYR   A CB   1 
ATOM   4911  C CG   . TYR   A  1 327 ? 39.108 -23.654 -24.461 1.00 24.36  ? 353  TYR   A CG   1 
ATOM   4912  C CD1  . TYR   A  1 327 ? 37.961 -23.134 -25.050 1.00 24.59  ? 353  TYR   A CD1  1 
ATOM   4913  C CD2  . TYR   A  1 327 ? 40.293 -23.580 -25.181 1.00 24.81  ? 353  TYR   A CD2  1 
ATOM   4914  C CE1  . TYR   A  1 327 ? 37.990 -22.594 -26.331 1.00 25.00  ? 353  TYR   A CE1  1 
ATOM   4915  C CE2  . TYR   A  1 327 ? 40.322 -23.098 -26.482 1.00 25.23  ? 353  TYR   A CE2  1 
ATOM   4916  C CZ   . TYR   A  1 327 ? 39.169 -22.599 -27.055 1.00 25.70  ? 353  TYR   A CZ   1 
ATOM   4917  O OH   . TYR   A  1 327 ? 39.213 -22.120 -28.352 1.00 26.22  ? 353  TYR   A OH   1 
ATOM   4918  H H    . TYR   A  1 327 ? 38.564 -25.737 -20.895 0.00 32.52  ? 353  TYR   A H    1 
ATOM   4919  H HA   . TYR   A  1 327 ? 37.070 -23.704 -22.473 0.00 30.89  ? 353  TYR   A HA   1 
ATOM   4920  H HB2  . TYR   A  1 327 ? 39.522 -23.352 -22.422 0.00 30.10  ? 353  TYR   A HB2  1 
ATOM   4921  H HB3  . TYR   A  1 327 ? 39.771 -25.010 -22.980 0.00 30.79  ? 353  TYR   A HB3  1 
ATOM   4922  H HD1  . TYR   A  1 327 ? 37.025 -23.125 -24.523 0.00 29.18  ? 353  TYR   A HD1  1 
ATOM   4923  H HD2  . TYR   A  1 327 ? 41.196 -23.971 -24.745 0.00 30.18  ? 353  TYR   A HD2  1 
ATOM   4924  H HE1  . TYR   A  1 327 ? 37.075 -22.244 -26.779 0.00 29.15  ? 353  TYR   A HE1  1 
ATOM   4925  H HE2  . TYR   A  1 327 ? 41.247 -23.085 -27.032 0.00 30.12  ? 353  TYR   A HE2  1 
ATOM   4926  H HH   . TYR   A  1 327 ? 38.323 -21.785 -28.637 0.00 30.42  ? 353  TYR   A HH   1 
ATOM   4927  N N    . PRO   A  1 328 ? 35.863 -26.111 -22.700 1.00 26.30  ? 354  PRO   A N    1 
ATOM   4928  C CA   . PRO   A  1 328 ? 35.266 -27.365 -23.186 1.00 26.88  ? 354  PRO   A CA   1 
ATOM   4929  C C    . PRO   A  1 328 ? 35.096 -27.439 -24.686 1.00 27.99  ? 354  PRO   A C    1 
ATOM   4930  O O    . PRO   A  1 328 ? 35.115 -26.417 -25.373 1.00 27.35  ? 354  PRO   A O    1 
ATOM   4931  C CB   . PRO   A  1 328 ? 33.908 -27.405 -22.477 1.00 27.66  ? 354  PRO   A CB   1 
ATOM   4932  C CG   . PRO   A  1 328 ? 33.571 -25.958 -22.261 1.00 27.64  ? 354  PRO   A CG   1 
ATOM   4933  C CD   . PRO   A  1 328 ? 34.894 -25.341 -21.893 1.00 25.49  ? 354  PRO   A CD   1 
ATOM   4934  H HA   . PRO   A  1 328 ? 35.860 -28.215 -22.854 0.00 34.33  ? 354  PRO   A HA   1 
ATOM   4935  H HB2  . PRO   A  1 328 ? 33.170 -27.886 -23.116 0.00 35.00  ? 354  PRO   A HB2  1 
ATOM   4936  H HB3  . PRO   A  1 328 ? 34.001 -27.928 -21.526 0.00 35.19  ? 354  PRO   A HB3  1 
ATOM   4937  H HG2  . PRO   A  1 328 ? 33.180 -25.527 -23.181 0.00 33.86  ? 354  PRO   A HG2  1 
ATOM   4938  H HG3  . PRO   A  1 328 ? 32.854 -25.861 -21.447 0.00 34.17  ? 354  PRO   A HG3  1 
ATOM   4939  H HD2  . PRO   A  1 328 ? 34.886 -24.290 -22.177 0.00 30.86  ? 354  PRO   A HD2  1 
ATOM   4940  H HD3  . PRO   A  1 328 ? 35.093 -25.471 -20.831 0.00 31.53  ? 354  PRO   A HD3  1 
ATOM   4941  N N    . GLN   A  1 329 ? 34.950 -28.665 -25.195 1.00 28.62  ? 355  GLN   A N    1 
ATOM   4942  C CA   . GLN   A  1 329 ? 34.772 -28.867 -26.619 1.00 29.30  ? 355  GLN   A CA   1 
ATOM   4943  C C    . GLN   A  1 329 ? 33.443 -28.297 -27.094 1.00 28.42  ? 355  GLN   A C    1 
ATOM   4944  O O    . GLN   A  1 329 ? 33.401 -27.687 -28.158 1.00 28.26  ? 355  GLN   A O    1 
ATOM   4945  C CB   . GLN   A  1 329 ? 34.847 -30.364 -26.968 1.00 32.98  ? 355  GLN   A CB   1 
ATOM   4946  C CG   . GLN   A  1 329 ? 36.241 -30.960 -26.836 1.00 38.76  ? 355  GLN   A CG   1 
ATOM   4947  C CD   . GLN   A  1 329 ? 36.350 -32.299 -27.536 1.00 46.29  ? 355  GLN   A CD   1 
ATOM   4948  O OE1  . GLN   A  1 329 ? 35.371 -33.046 -27.663 1.00 48.52  ? 355  GLN   A OE1  1 
ATOM   4949  N NE2  . GLN   A  1 329 ? 37.548 -32.646 -27.996 1.00 47.71  ? 355  GLN   A NE2  1 
ATOM   4950  H H    . GLN   A  1 329 ? 34.954 -29.517 -24.645 0.00 36.89  ? 355  GLN   A H    1 
ATOM   4951  H HA   . GLN   A  1 329 ? 35.570 -28.355 -27.154 0.00 37.00  ? 355  GLN   A HA   1 
ATOM   4952  H HB2  . GLN   A  1 329 ? 34.177 -30.921 -26.316 0.00 42.77  ? 355  GLN   A HB2  1 
ATOM   4953  H HB3  . GLN   A  1 329 ? 34.535 -30.490 -28.004 0.00 42.49  ? 355  GLN   A HB3  1 
ATOM   4954  H HG2  . GLN   A  1 329 ? 36.962 -30.276 -27.281 0.00 49.44  ? 355  GLN   A HG2  1 
ATOM   4955  H HG3  . GLN   A  1 329 ? 36.467 -31.109 -25.781 0.00 49.92  ? 355  GLN   A HG3  1 
ATOM   4956  H HE21 . GLN   A  1 329 ? 38.346 -32.032 -27.867 0.00 61.28  ? 355  GLN   A HE21 1 
ATOM   4957  H HE22 . GLN   A  1 329 ? 37.668 -33.535 -28.472 0.00 62.09  ? 355  GLN   A HE22 1 
ATOM   4958  N N    . HIS   A  1 330 ? 32.357 -28.486 -26.323 1.00 27.20  ? 356  HIS   A N    1 
ATOM   4959  C CA   . HIS   A  1 330 ? 31.032 -28.059 -26.762 1.00 27.46  ? 356  HIS   A CA   1 
ATOM   4960  C C    . HIS   A  1 330 ? 30.258 -27.245 -25.729 1.00 26.49  ? 356  HIS   A C    1 
ATOM   4961  O O    . HIS   A  1 330 ? 30.583 -27.275 -24.543 1.00 26.60  ? 356  HIS   A O    1 
ATOM   4962  C CB   . HIS   A  1 330 ? 30.212 -29.315 -27.155 1.00 29.26  ? 356  HIS   A CB   1 
ATOM   4963  C CG   . HIS   A  1 330 ? 30.940 -30.192 -28.134 1.00 32.69  ? 356  HIS   A CG   1 
ATOM   4964  N ND1  . HIS   A  1 330 ? 31.317 -31.484 -27.805 1.00 34.85  ? 356  HIS   A ND1  1 
ATOM   4965  C CD2  . HIS   A  1 330 ? 31.453 -29.885 -29.348 1.00 33.81  ? 356  HIS   A CD2  1 
ATOM   4966  C CE1  . HIS   A  1 330 ? 31.986 -31.945 -28.851 1.00 35.51  ? 356  HIS   A CE1  1 
ATOM   4967  N NE2  . HIS   A  1 330 ? 32.098 -31.014 -29.804 1.00 35.37  ? 356  HIS   A NE2  1 
ATOM   4968  H H    . HIS   A  1 330 ? 32.360 -28.933 -25.412 0.00 34.81  ? 356  HIS   A H    1 
ATOM   4969  H HA   . HIS   A  1 330 ? 31.110 -27.437 -27.652 0.00 34.32  ? 356  HIS   A HA   1 
ATOM   4970  H HB2  . HIS   A  1 330 ? 30.010 -29.902 -26.261 0.00 37.80  ? 356  HIS   A HB2  1 
ATOM   4971  H HB3  . HIS   A  1 330 ? 29.277 -28.999 -27.615 0.00 37.35  ? 356  HIS   A HB3  1 
ATOM   4972  H HD1  . HIS   A  1 330 ? 31.120 -31.977 -26.940 0.00 45.58  ? 356  HIS   A HD1  1 
ATOM   4973  H HD2  . HIS   A  1 330 ? 31.372 -28.940 -29.858 0.00 42.68  ? 356  HIS   A HD2  1 
ATOM   4974  H HE1  . HIS   A  1 330 ? 32.387 -32.942 -28.925 0.00 46.89  ? 356  HIS   A HE1  1 
ATOM   4975  N N    . ILE   A  1 331 ? 29.235 -26.509 -26.202 1.00 25.17  ? 357  ILE   A N    1 
ATOM   4976  C CA   . ILE   A  1 331 ? 28.309 -25.789 -25.337 1.00 24.96  ? 357  ILE   A CA   1 
ATOM   4977  C C    . ILE   A  1 331 ? 27.202 -26.789 -24.941 1.00 25.27  ? 357  ILE   A C    1 
ATOM   4978  O O    . ILE   A  1 331 ? 26.775 -27.598 -25.767 1.00 25.38  ? 357  ILE   A O    1 
ATOM   4979  C CB   . ILE   A  1 331 ? 27.748 -24.472 -25.973 1.00 25.17  ? 357  ILE   A CB   1 
ATOM   4980  C CG1  . ILE   A  1 331 ? 26.976 -23.658 -24.919 1.00 25.11  ? 357  ILE   A CG1  1 
ATOM   4981  C CG2  . ILE   A  1 331 ? 26.867 -24.711 -27.223 1.00 25.87  ? 357  ILE   A CG2  1 
ATOM   4982  C CD1  . ILE   A  1 331 ? 26.708 -22.180 -25.329 1.00 25.79  ? 357  ILE   A CD1  1 
ATOM   4983  H H    . ILE   A  1 331 ? 29.046 -26.407 -27.193 0.00 31.21  ? 357  ILE   A H    1 
ATOM   4984  H HA   . ILE   A  1 331 ? 28.836 -25.502 -24.428 0.00 30.67  ? 357  ILE   A HA   1 
ATOM   4985  H HB   . ILE   A  1 331 ? 28.602 -23.872 -26.285 0.00 30.16  ? 357  ILE   A HB   1 
ATOM   4986  H HG12 . ILE   A  1 331 ? 26.010 -24.133 -24.751 0.00 30.51  ? 357  ILE   A HG12 1 
ATOM   4987  H HG13 . ILE   A  1 331 ? 27.543 -23.642 -23.990 0.00 30.19  ? 357  ILE   A HG13 1 
ATOM   4988  H HG21 . ILE   A  1 331 ? 26.684 -23.755 -27.712 0.00 31.11  ? 357  ILE   A HG21 1 
ATOM   4989  H HG22 . ILE   A  1 331 ? 27.367 -25.379 -27.922 0.00 31.73  ? 357  ILE   A HG22 1 
ATOM   4990  H HG23 . ILE   A  1 331 ? 25.918 -25.145 -26.915 0.00 31.79  ? 357  ILE   A HG23 1 
ATOM   4991  H HD11 . ILE   A  1 331 ? 26.284 -21.650 -24.477 0.00 30.33  ? 357  ILE   A HD11 1 
ATOM   4992  H HD12 . ILE   A  1 331 ? 27.648 -21.716 -25.625 0.00 30.16  ? 357  ILE   A HD12 1 
ATOM   4993  H HD13 . ILE   A  1 331 ? 26.004 -22.159 -26.160 0.00 30.49  ? 357  ILE   A HD13 1 
ATOM   4994  N N    . ASN   A  1 332 ? 26.783 -26.767 -23.671 1.00 24.70  ? 358  ASN   A N    1 
ATOM   4995  C CA   . ASN   A  1 332 ? 25.757 -27.673 -23.172 1.00 25.70  ? 358  ASN   A CA   1 
ATOM   4996  C C    . ASN   A  1 332 ? 24.491 -26.871 -22.793 1.00 25.62  ? 358  ASN   A C    1 
ATOM   4997  O O    . ASN   A  1 332 ? 24.404 -26.304 -21.701 1.00 25.35  ? 358  ASN   A O    1 
ATOM   4998  C CB   . ASN   A  1 332 ? 26.302 -28.495 -22.003 1.00 26.75  ? 358  ASN   A CB   1 
ATOM   4999  C CG   . ASN   A  1 332 ? 25.390 -29.612 -21.563 1.00 31.32  ? 358  ASN   A CG   1 
ATOM   5000  O OD1  . ASN   A  1 332 ? 24.269 -29.770 -22.055 1.00 33.32  ? 358  ASN   A OD1  1 
ATOM   5001  N ND2  . ASN   A  1 332 ? 25.851 -30.425 -20.616 1.00 32.66  ? 358  ASN   A ND2  1 
ATOM   5002  H H    . ASN   A  1 332 ? 27.137 -26.131 -22.964 0.00 30.87  ? 358  ASN   A H    1 
ATOM   5003  H HA   . ASN   A  1 332 ? 25.479 -28.387 -23.946 0.00 33.22  ? 358  ASN   A HA   1 
ATOM   5004  H HB2  . ASN   A  1 332 ? 27.246 -28.944 -22.308 0.00 34.68  ? 358  ASN   A HB2  1 
ATOM   5005  H HB3  . ASN   A  1 332 ? 26.471 -27.840 -21.149 0.00 34.31  ? 358  ASN   A HB3  1 
ATOM   5006  H HD21 . ASN   A  1 332 ? 25.278 -31.194 -20.284 0.00 43.27  ? 358  ASN   A HD21 1 
ATOM   5007  H HD22 . ASN   A  1 332 ? 26.777 -30.276 -20.228 0.00 42.66  ? 358  ASN   A HD22 1 
ATOM   5008  N N    . ILE   A  1 333 ? 23.517 -26.850 -23.717 1.00 25.65  ? 359  ILE   A N    1 
ATOM   5009  C CA   . ILE   A  1 333 ? 22.240 -26.130 -23.598 1.00 26.27  ? 359  ILE   A CA   1 
ATOM   5010  C C    . ILE   A  1 333 ? 21.128 -27.102 -23.194 1.00 25.93  ? 359  ILE   A C    1 
ATOM   5011  O O    . ILE   A  1 333 ? 20.865 -28.054 -23.922 1.00 25.81  ? 359  ILE   A O    1 
ATOM   5012  C CB   . ILE   A  1 333 ? 21.915 -25.482 -24.982 1.00 27.57  ? 359  ILE   A CB   1 
ATOM   5013  C CG1  . ILE   A  1 333 ? 22.998 -24.463 -25.404 1.00 28.74  ? 359  ILE   A CG1  1 
ATOM   5014  C CG2  . ILE   A  1 333 ? 20.543 -24.849 -24.991 1.00 28.82  ? 359  ILE   A CG2  1 
ATOM   5015  C CD1  . ILE   A  1 333 ? 23.242 -23.316 -24.440 1.00 30.44  ? 359  ILE   A CD1  1 
ATOM   5016  H H    . ILE   A  1 333 ? 23.590 -27.346 -24.599 0.00 32.89  ? 359  ILE   A H    1 
ATOM   5017  H HA   . ILE   A  1 333 ? 22.306 -25.348 -22.844 0.00 33.04  ? 359  ILE   A HA   1 
ATOM   5018  H HB   . ILE   A  1 333 ? 21.901 -26.274 -25.729 0.00 34.96  ? 359  ILE   A HB   1 
ATOM   5019  H HG12 . ILE   A  1 333 ? 23.944 -24.987 -25.525 0.00 35.47  ? 359  ILE   A HG12 1 
ATOM   5020  H HG13 . ILE   A  1 333 ? 22.713 -24.025 -26.359 0.00 35.25  ? 359  ILE   A HG13 1 
ATOM   5021  H HG21 . ILE   A  1 333 ? 20.483 -24.130 -25.806 0.00 35.83  ? 359  ILE   A HG21 1 
ATOM   5022  H HG22 . ILE   A  1 333 ? 19.787 -25.618 -25.139 0.00 36.61  ? 359  ILE   A HG22 1 
ATOM   5023  H HG23 . ILE   A  1 333 ? 20.383 -24.346 -24.039 0.00 35.99  ? 359  ILE   A HG23 1 
ATOM   5024  H HD11 . ILE   A  1 333 ? 23.861 -22.570 -24.936 0.00 36.58  ? 359  ILE   A HD11 1 
ATOM   5025  H HD12 . ILE   A  1 333 ? 22.293 -22.870 -24.147 0.00 36.98  ? 359  ILE   A HD12 1 
ATOM   5026  H HD13 . ILE   A  1 333 ? 23.764 -23.691 -23.561 0.00 37.10  ? 359  ILE   A HD13 1 
ATOM   5027  N N    . SER   A  1 334 ? 20.459 -26.846 -22.066 1.00 25.68  ? 360  SER   A N    1 
ATOM   5028  C CA   . SER   A  1 334 ? 19.368 -27.701 -21.594 1.00 26.09  ? 360  SER   A CA   1 
ATOM   5029  C C    . SER   A  1 334 ? 18.241 -27.814 -22.602 1.00 27.10  ? 360  SER   A C    1 
ATOM   5030  O O    . SER   A  1 334 ? 17.907 -26.831 -23.268 1.00 26.65  ? 360  SER   A O    1 
ATOM   5031  C CB   . SER   A  1 334 ? 18.767 -27.120 -20.317 1.00 26.28  ? 360  SER   A CB   1 
ATOM   5032  O OG   . SER   A  1 334 ? 17.689 -27.912 -19.841 1.00 26.56  ? 360  SER   A OG   1 
ATOM   5033  H H    . SER   A  1 334 ? 20.650 -26.056 -21.458 0.00 33.01  ? 360  SER   A H    1 
ATOM   5034  H HA   . SER   A  1 334 ? 19.755 -28.695 -21.376 0.00 34.89  ? 360  SER   A HA   1 
ATOM   5035  H HB2  . SER   A  1 334 ? 19.540 -27.081 -19.550 0.00 34.57  ? 360  SER   A HB2  1 
ATOM   5036  H HB3  . SER   A  1 334 ? 18.402 -26.116 -20.526 0.00 34.29  ? 360  SER   A HB3  1 
ATOM   5037  H HG   . SER   A  1 334 ? 17.330 -27.526 -19.000 0.00 35.62  ? 360  SER   A HG   1 
ATOM   5038  N N    . ARG   A  1 335 ? 17.580 -28.986 -22.642 1.00 27.98  ? 361  ARG   A N    1 
ATOM   5039  C CA   . ARG   A  1 335 ? 16.369 -29.157 -23.450 1.00 29.27  ? 361  ARG   A CA   1 
ATOM   5040  C C    . ARG   A  1 335 ? 15.268 -28.162 -22.994 1.00 28.84  ? 361  ARG   A C    1 
ATOM   5041  O O    . ARG   A  1 335 ? 14.407 -27.812 -23.803 1.00 29.77  ? 361  ARG   A O    1 
ATOM   5042  C CB   . ARG   A  1 335 ? 15.824 -30.588 -23.339 1.00 32.48  ? 361  ARG   A CB   1 
ATOM   5043  C CG   . ARG   A  1 335 ? 16.584 -31.627 -24.161 1.00 39.52  ? 361  ARG   A CG   1 
ATOM   5044  C CD   . ARG   A  1 335 ? 15.790 -32.926 -24.250 1.00 46.36  ? 361  ARG   A CD   1 
ATOM   5045  N NE   . ARG   A  1 335 ? 16.445 -33.949 -25.070 1.00 52.71  ? 361  ARG   A NE   1 
ATOM   5046  C CZ   . ARG   A  1 335 ? 17.462 -34.715 -24.673 1.00 57.36  ? 361  ARG   A CZ   1 
ATOM   5047  N NH1  . ARG   A  1 335 ? 17.978 -35.621 -25.495 1.00 57.87  ? 361  ARG   A NH1  1 
ATOM   5048  N NH2  . ARG   A  1 335 ? 17.981 -34.570 -23.456 1.00 58.27  ? 361  ARG   A NH2  1 
ATOM   5049  H H    . ARG   A  1 335 ? 17.866 -29.820 -22.140 0.00 38.07  ? 361  ARG   A H    1 
ATOM   5050  H HA   . ARG   A  1 335 ? 16.601 -28.954 -24.495 0.00 39.42  ? 361  ARG   A HA   1 
ATOM   5051  H HB2  . ARG   A  1 335 ? 15.852 -30.904 -22.297 0.00 44.50  ? 361  ARG   A HB2  1 
ATOM   5052  H HB3  . ARG   A  1 335 ? 14.793 -30.587 -23.688 0.00 44.59  ? 361  ARG   A HB3  1 
ATOM   5053  H HG2  . ARG   A  1 335 ? 16.736 -31.248 -25.171 0.00 52.81  ? 361  ARG   A HG2  1 
ATOM   5054  H HG3  . ARG   A  1 335 ? 17.540 -31.840 -23.685 0.00 52.97  ? 361  ARG   A HG3  1 
ATOM   5055  H HD2  . ARG   A  1 335 ? 15.619 -33.320 -23.249 0.00 62.47  ? 361  ARG   A HD2  1 
ATOM   5056  H HD3  . ARG   A  1 335 ? 14.832 -32.708 -24.719 0.00 62.31  ? 361  ARG   A HD3  1 
ATOM   5057  H HE   . ARG   A  1 335 ? 16.076 -34.097 -26.004 0.00 70.36  ? 361  ARG   A HE   1 
ATOM   5058  H HH11 . ARG   A  1 335 ? 17.595 -35.745 -26.427 0.00 77.13  ? 361  ARG   A HH11 1 
ATOM   5059  H HH12 . ARG   A  1 335 ? 18.755 -36.202 -25.195 0.00 77.15  ? 361  ARG   A HH12 1 
ATOM   5060  H HH21 . ARG   A  1 335 ? 17.624 -33.889 -22.793 0.00 76.60  ? 361  ARG   A HH21 1 
ATOM   5061  H HH22 . ARG   A  1 335 ? 18.758 -35.157 -23.171 0.00 77.07  ? 361  ARG   A HH22 1 
ATOM   5062  N N    . ASN   A  1 336 ? 15.304 -27.704 -21.714 1.00 27.46  ? 362  ASN   A N    1 
ATOM   5063  C CA   . ASN   A  1 336 ? 14.341 -26.745 -21.169 1.00 27.13  ? 362  ASN   A CA   1 
ATOM   5064  C C    . ASN   A  1 336 ? 14.377 -25.368 -21.855 1.00 26.06  ? 362  ASN   A C    1 
ATOM   5065  O O    . ASN   A  1 336 ? 13.445 -24.588 -21.654 1.00 26.02  ? 362  ASN   A O    1 
ATOM   5066  C CB   . ASN   A  1 336 ? 14.520 -26.580 -19.656 1.00 28.10  ? 362  ASN   A CB   1 
ATOM   5067  C CG   . ASN   A  1 336 ? 14.109 -27.783 -18.848 1.00 32.13  ? 362  ASN   A CG   1 
ATOM   5068  O OD1  . ASN   A  1 336 ? 13.236 -28.563 -19.245 1.00 32.03  ? 362  ASN   A OD1  1 
ATOM   5069  N ND2  . ASN   A  1 336 ? 14.713 -27.943 -17.676 1.00 34.00  ? 362  ASN   A ND2  1 
ATOM   5070  H H    . ASN   A  1 336 ? 15.990 -28.000 -21.026 0.00 37.09  ? 362  ASN   A H    1 
ATOM   5071  H HA   . ASN   A  1 336 ? 13.341 -27.140 -21.344 0.00 37.05  ? 362  ASN   A HA   1 
ATOM   5072  H HB2  . ASN   A  1 336 ? 15.561 -26.346 -19.440 0.00 37.35  ? 362  ASN   A HB2  1 
ATOM   5073  H HB3  . ASN   A  1 336 ? 13.876 -25.766 -19.331 0.00 37.59  ? 362  ASN   A HB3  1 
ATOM   5074  H HD21 . ASN   A  1 336 ? 14.474 -28.738 -17.092 0.00 45.99  ? 362  ASN   A HD21 1 
ATOM   5075  H HD22 . ASN   A  1 336 ? 15.407 -27.275 -17.357 0.00 45.06  ? 362  ASN   A HD22 1 
ATOM   5076  N N    . PHE   A  1 337 ? 15.424 -25.052 -22.644 1.00 24.73  ? 363  PHE   A N    1 
ATOM   5077  C CA   . PHE   A  1 337 ? 15.430 -23.806 -23.425 1.00 24.71  ? 363  PHE   A CA   1 
ATOM   5078  C C    . PHE   A  1 337 ? 14.245 -23.804 -24.445 1.00 25.43  ? 363  PHE   A C    1 
ATOM   5079  O O    . PHE   A  1 337 ? 13.784 -22.732 -24.831 1.00 25.58  ? 363  PHE   A O    1 
ATOM   5080  C CB   . PHE   A  1 337 ? 16.768 -23.588 -24.170 1.00 23.97  ? 363  PHE   A CB   1 
ATOM   5081  C CG   . PHE   A  1 337 ? 17.836 -22.866 -23.367 1.00 23.86  ? 363  PHE   A CG   1 
ATOM   5082  C CD1  . PHE   A  1 337 ? 18.630 -23.553 -22.460 1.00 23.91  ? 363  PHE   A CD1  1 
ATOM   5083  C CD2  . PHE   A  1 337 ? 17.991 -21.493 -23.466 1.00 24.27  ? 363  PHE   A CD2  1 
ATOM   5084  C CE1  . PHE   A  1 337 ? 19.614 -22.895 -21.735 1.00 24.37  ? 363  PHE   A CE1  1 
ATOM   5085  C CE2  . PHE   A  1 337 ? 18.967 -20.834 -22.725 1.00 24.75  ? 363  PHE   A CE2  1 
ATOM   5086  C CZ   . PHE   A  1 337 ? 19.763 -21.538 -21.857 1.00 24.27  ? 363  PHE   A CZ   1 
ATOM   5087  H H    . PHE   A  1 337 ? 16.268 -25.608 -22.743 0.00 32.62  ? 363  PHE   A H    1 
ATOM   5088  H HA   . PHE   A  1 337 ? 15.260 -22.971 -22.747 0.00 31.84  ? 363  PHE   A HA   1 
ATOM   5089  H HB2  . PHE   A  1 337 ? 17.177 -24.545 -24.490 0.00 30.98  ? 363  PHE   A HB2  1 
ATOM   5090  H HB3  . PHE   A  1 337 ? 16.561 -22.976 -25.047 0.00 30.53  ? 363  PHE   A HB3  1 
ATOM   5091  H HD1  . PHE   A  1 337 ? 18.523 -24.621 -22.364 0.00 30.69  ? 363  PHE   A HD1  1 
ATOM   5092  H HD2  . PHE   A  1 337 ? 17.379 -20.934 -24.152 0.00 29.97  ? 363  PHE   A HD2  1 
ATOM   5093  H HE1  . PHE   A  1 337 ? 20.232 -23.444 -21.044 0.00 30.49  ? 363  PHE   A HE1  1 
ATOM   5094  H HE2  . PHE   A  1 337 ? 19.092 -19.769 -22.826 0.00 29.79  ? 363  PHE   A HE2  1 
ATOM   5095  H HZ   . PHE   A  1 337 ? 20.512 -21.024 -21.278 0.00 29.42  ? 363  PHE   A HZ   1 
ATOM   5096  N N    . SER   A  1 338 ? 13.756 -24.993 -24.862 1.00 24.94  ? 364  SER   A N    1 
ATOM   5097  C CA   . SER   A  1 338 ? 12.605 -25.125 -25.753 1.00 25.23  ? 364  SER   A CA   1 
ATOM   5098  C C    . SER   A  1 338 ? 11.286 -24.594 -25.133 1.00 25.25  ? 364  SER   A C    1 
ATOM   5099  O O    . SER   A  1 338 ? 10.295 -24.437 -25.858 1.00 25.69  ? 364  SER   A O    1 
ATOM   5100  C CB   . SER   A  1 338 ? 12.411 -26.588 -26.152 1.00 26.61  ? 364  SER   A CB   1 
ATOM   5101  O OG   . SER   A  1 338 ? 11.918 -27.365 -25.071 1.00 28.69  ? 364  SER   A OG   1 
ATOM   5102  H H    . SER   A  1 338 ? 14.160 -25.886 -24.596 0.00 33.54  ? 364  SER   A H    1 
ATOM   5103  H HA   . SER   A  1 338 ? 12.798 -24.555 -26.661 0.00 33.80  ? 364  SER   A HA   1 
ATOM   5104  H HB2  . SER   A  1 338 ? 11.692 -26.634 -26.970 0.00 36.69  ? 364  SER   A HB2  1 
ATOM   5105  H HB3  . SER   A  1 338 ? 13.364 -27.000 -26.480 0.00 36.28  ? 364  SER   A HB3  1 
ATOM   5106  H HG   . SER   A  1 338 ? 12.399 -27.150 -24.228 0.00 39.15  ? 364  SER   A HG   1 
ATOM   5107  N N    . LYS   A  1 339 ? 11.265 -24.357 -23.811 1.00 24.54  ? 365  LYS   A N    1 
ATOM   5108  C CA   . LYS   A  1 339 ? 10.105 -23.825 -23.100 1.00 24.36  ? 365  LYS   A CA   1 
ATOM   5109  C C    . LYS   A  1 339 ? 10.061 -22.294 -23.116 1.00 23.71  ? 365  LYS   A C    1 
ATOM   5110  O O    . LYS   A  1 339 ? 9.057  -21.733 -22.677 1.00 23.24  ? 365  LYS   A O    1 
ATOM   5111  C CB   . LYS   A  1 339 ? 10.106 -24.316 -21.639 1.00 26.86  ? 365  LYS   A CB   1 
ATOM   5112  C CG   . LYS   A  1 339 ? 10.180 -25.836 -21.474 1.00 32.67  ? 365  LYS   A CG   1 
ATOM   5113  C CD   . LYS   A  1 339 ? 8.969  -26.547 -22.075 1.00 39.05  ? 365  LYS   A CD   1 
ATOM   5114  C CE   . LYS   A  1 339 ? 8.965  -28.023 -21.755 1.00 43.98  ? 365  LYS   A CE   1 
ATOM   5115  N NZ   . LYS   A  1 339 ? 8.106  -28.778 -22.702 1.00 47.17  ? 365  LYS   A NZ   1 
ATOM   5116  H H    . LYS   A  1 339 ? 12.046 -24.529 -23.185 0.00 33.22  ? 365  LYS   A H    1 
ATOM   5117  H HA   . LYS   A  1 339 ? 9.188  -24.172 -23.572 0.00 33.89  ? 365  LYS   A HA   1 
ATOM   5118  H HB2  . LYS   A  1 339 ? 10.967 -23.889 -21.125 0.00 36.20  ? 365  LYS   A HB2  1 
ATOM   5119  H HB3  . LYS   A  1 339 ? 9.189  -23.979 -21.159 0.00 36.89  ? 365  LYS   A HB3  1 
ATOM   5120  H HG2  . LYS   A  1 339 ? 11.077 -26.220 -21.957 0.00 44.01  ? 365  LYS   A HG2  1 
ATOM   5121  H HG3  . LYS   A  1 339 ? 10.201 -26.072 -20.412 0.00 44.34  ? 365  LYS   A HG3  1 
ATOM   5122  H HD2  . LYS   A  1 339 ? 8.059  -26.106 -21.671 0.00 52.77  ? 365  LYS   A HD2  1 
ATOM   5123  H HD3  . LYS   A  1 339 ? 8.988  -26.443 -23.159 0.00 52.51  ? 365  LYS   A HD3  1 
ATOM   5124  H HE2  . LYS   A  1 339 ? 9.980  -28.410 -21.833 0.00 58.94  ? 365  LYS   A HE2  1 
ATOM   5125  H HE3  . LYS   A  1 339 ? 8.579  -28.171 -20.748 0.00 59.38  ? 365  LYS   A HE3  1 
ATOM   5126  H HZ1  . LYS   A  1 339 ? 8.078  -29.758 -22.438 0.00 64.08  ? 365  LYS   A HZ1  1 
ATOM   5127  H HZ2  . LYS   A  1 339 ? 7.162  -28.404 -22.687 0.00 63.84  ? 365  LYS   A HZ2  1 
ATOM   5128  H HZ3  . LYS   A  1 339 ? 8.475  -28.703 -23.645 0.00 63.44  ? 365  LYS   A HZ3  1 
ATOM   5129  N N    . LEU   A  1 340 ? 11.137 -21.609 -23.591 1.00 23.06  ? 366  LEU   A N    1 
ATOM   5130  C CA   . LEU   A  1 340 ? 11.163 -20.159 -23.687 1.00 22.85  ? 366  LEU   A CA   1 
ATOM   5131  C C    . LEU   A  1 340 ? 10.455 -19.754 -24.987 1.00 23.30  ? 366  LEU   A C    1 
ATOM   5132  O O    . LEU   A  1 340 ? 11.064 -19.171 -25.891 1.00 22.78  ? 366  LEU   A O    1 
ATOM   5133  C CB   . LEU   A  1 340 ? 12.605 -19.651 -23.670 1.00 22.57  ? 366  LEU   A CB   1 
ATOM   5134  C CG   . LEU   A  1 340 ? 13.439 -19.997 -22.429 1.00 23.85  ? 366  LEU   A CG   1 
ATOM   5135  C CD1  . LEU   A  1 340 ? 14.903 -19.581 -22.646 1.00 24.32  ? 366  LEU   A CD1  1 
ATOM   5136  C CD2  . LEU   A  1 340 ? 12.865 -19.329 -21.181 1.00 23.98  ? 366  LEU   A CD2  1 
ATOM   5137  H H    . LEU   A  1 340 ? 12.004 -22.032 -23.905 0.00 30.53  ? 366  LEU   A H    1 
ATOM   5138  H HA   . LEU   A  1 340 ? 10.623 -19.710 -22.856 0.00 30.04  ? 366  LEU   A HA   1 
ATOM   5139  H HB2  . LEU   A  1 340 ? 13.136 -20.031 -24.542 0.00 28.88  ? 366  LEU   A HB2  1 
ATOM   5140  H HB3  . LEU   A  1 340 ? 12.560 -18.565 -23.700 0.00 28.65  ? 366  LEU   A HB3  1 
ATOM   5141  H HG   . LEU   A  1 340 ? 13.419 -21.074 -22.269 0.00 30.73  ? 366  LEU   A HG   1 
ATOM   5142  H HD11 . LEU   A  1 340 ? 15.449 -19.671 -21.709 0.00 30.26  ? 366  LEU   A HD11 1 
ATOM   5143  H HD12 . LEU   A  1 340 ? 15.347 -20.229 -23.399 0.00 30.38  ? 366  LEU   A HD12 1 
ATOM   5144  H HD13 . LEU   A  1 340 ? 14.926 -18.547 -22.988 0.00 30.01  ? 366  LEU   A HD13 1 
ATOM   5145  H HD21 . LEU   A  1 340 ? 13.558 -19.467 -20.353 0.00 30.44  ? 366  LEU   A HD21 1 
ATOM   5146  H HD22 . LEU   A  1 340 ? 12.726 -18.267 -21.375 0.00 30.30  ? 366  LEU   A HD22 1 
ATOM   5147  H HD23 . LEU   A  1 340 ? 11.911 -19.791 -20.931 0.00 31.05  ? 366  LEU   A HD23 1 
ATOM   5148  N N    . LEU   A  1 341 ? 9.131  -19.998 -25.017 1.00 23.77  ? 367  LEU   A N    1 
ATOM   5149  C CA   . LEU   A  1 341 ? 8.277  -19.790 -26.189 1.00 23.85  ? 367  LEU   A CA   1 
ATOM   5150  C C    . LEU   A  1 341 ? 8.393  -18.392 -26.821 1.00 23.24  ? 367  LEU   A C    1 
ATOM   5151  O O    . LEU   A  1 341 ? 8.405  -18.292 -28.042 1.00 23.84  ? 367  LEU   A O    1 
ATOM   5152  C CB   . LEU   A  1 341 ? 6.798  -20.070 -25.856 1.00 24.42  ? 367  LEU   A CB   1 
ATOM   5153  C CG   . LEU   A  1 341 ? 6.425  -21.427 -25.220 1.00 27.28  ? 367  LEU   A CG   1 
ATOM   5154  C CD1  . LEU   A  1 341 ? 4.916  -21.528 -25.050 1.00 28.28  ? 367  LEU   A CD1  1 
ATOM   5155  C CD2  . LEU   A  1 341 ? 6.940  -22.608 -26.052 1.00 28.35  ? 367  LEU   A CD2  1 
ATOM   5156  H H    . LEU   A  1 341 ? 8.632  -20.316 -24.195 0.00 32.08  ? 367  LEU   A H    1 
ATOM   5157  H HA   . LEU   A  1 341 ? 8.578  -20.511 -26.947 0.00 32.29  ? 367  LEU   A HA   1 
ATOM   5158  H HB2  . LEU   A  1 341 ? 6.461  -19.298 -25.167 0.00 33.47  ? 367  LEU   A HB2  1 
ATOM   5159  H HB3  . LEU   A  1 341 ? 6.228  -19.989 -26.780 0.00 33.81  ? 367  LEU   A HB3  1 
ATOM   5160  H HG   . LEU   A  1 341 ? 6.866  -21.504 -24.228 0.00 37.41  ? 367  LEU   A HG   1 
ATOM   5161  H HD11 . LEU   A  1 341 ? 4.674  -22.486 -24.593 0.00 39.92  ? 367  LEU   A HD11 1 
ATOM   5162  H HD12 . LEU   A  1 341 ? 4.578  -20.717 -24.406 0.00 39.39  ? 367  LEU   A HD12 1 
ATOM   5163  H HD13 . LEU   A  1 341 ? 4.441  -21.452 -26.027 0.00 39.72  ? 367  LEU   A HD13 1 
ATOM   5164  H HD21 . LEU   A  1 341 ? 6.552  -23.533 -25.628 0.00 39.54  ? 367  LEU   A HD21 1 
ATOM   5165  H HD22 . LEU   A  1 341 ? 6.598  -22.492 -27.079 0.00 39.20  ? 367  LEU   A HD22 1 
ATOM   5166  H HD23 . LEU   A  1 341 ? 8.028  -22.620 -26.017 0.00 38.59  ? 367  LEU   A HD23 1 
ATOM   5167  N N    . SER   A  1 342 ? 8.480  -17.329 -26.008 1.00 22.75  ? 368  SER   A N    1 
ATOM   5168  C CA   . SER   A  1 342 ? 8.543  -15.951 -26.518 1.00 22.71  ? 368  SER   A CA   1 
ATOM   5169  C C    . SER   A  1 342 ? 9.960  -15.401 -26.725 1.00 22.21  ? 368  SER   A C    1 
ATOM   5170  O O    . SER   A  1 342 ? 10.092 -14.216 -27.047 1.00 22.08  ? 368  SER   A O    1 
ATOM   5171  C CB   . SER   A  1 342 ? 7.800  -15.009 -25.569 1.00 24.65  ? 368  SER   A CB   1 
ATOM   5172  O OG   . SER   A  1 342 ? 6.469  -15.442 -25.356 1.00 27.93  ? 368  SER   A OG   1 
ATOM   5173  H H    . SER   A  1 342 ? 8.506  -17.387 -24.994 0.00 30.06  ? 368  SER   A H    1 
ATOM   5174  H HA   . SER   A  1 342 ? 8.029  -15.892 -27.476 0.00 29.89  ? 368  SER   A HA   1 
ATOM   5175  H HB2  . SER   A  1 342 ? 8.322  -14.985 -24.613 0.00 31.85  ? 368  SER   A HB2  1 
ATOM   5176  H HB3  . SER   A  1 342 ? 7.764  -14.010 -26.001 0.00 31.90  ? 368  SER   A HB3  1 
ATOM   5177  H HG   . SER   A  1 342 ? 6.445  -16.122 -24.632 0.00 36.86  ? 368  SER   A HG   1 
ATOM   5178  N N    . LEU   A  1 343 ? 11.015 -16.217 -26.539 1.00 21.28  ? 369  LEU   A N    1 
ATOM   5179  C CA   . LEU   A  1 343 ? 12.385 -15.719 -26.668 1.00 20.87  ? 369  LEU   A CA   1 
ATOM   5180  C C    . LEU   A  1 343 ? 12.674 -15.087 -28.028 1.00 20.68  ? 369  LEU   A C    1 
ATOM   5181  O O    . LEU   A  1 343 ? 12.376 -15.677 -29.064 1.00 21.06  ? 369  LEU   A O    1 
ATOM   5182  C CB   . LEU   A  1 343 ? 13.427 -16.821 -26.393 1.00 20.94  ? 369  LEU   A CB   1 
ATOM   5183  C CG   . LEU   A  1 343 ? 14.841 -16.331 -26.011 1.00 22.60  ? 369  LEU   A CG   1 
ATOM   5184  C CD1  . LEU   A  1 343 ? 14.808 -15.493 -24.702 1.00 22.48  ? 369  LEU   A CD1  1 
ATOM   5185  C CD2  . LEU   A  1 343 ? 15.791 -17.516 -25.885 1.00 23.42  ? 369  LEU   A CD2  1 
ATOM   5186  H H    . LEU   A  1 343 ? 10.956 -17.206 -26.322 0.00 27.29  ? 369  LEU   A H    1 
ATOM   5187  H HA   . LEU   A  1 343 ? 12.488 -14.950 -25.907 0.00 25.68  ? 369  LEU   A HA   1 
ATOM   5188  H HB2  . LEU   A  1 343 ? 13.076 -17.445 -25.574 0.00 26.18  ? 369  LEU   A HB2  1 
ATOM   5189  H HB3  . LEU   A  1 343 ? 13.528 -17.425 -27.293 0.00 26.03  ? 369  LEU   A HB3  1 
ATOM   5190  H HG   . LEU   A  1 343 ? 15.221 -15.689 -26.806 0.00 27.02  ? 369  LEU   A HG   1 
ATOM   5191  H HD11 . LEU   A  1 343 ? 15.796 -15.492 -24.245 0.00 26.68  ? 369  LEU   A HD11 1 
ATOM   5192  H HD12 . LEU   A  1 343 ? 14.530 -14.468 -24.945 0.00 26.82  ? 369  LEU   A HD12 1 
ATOM   5193  H HD13 . LEU   A  1 343 ? 14.080 -15.928 -24.019 0.00 27.32  ? 369  LEU   A HD13 1 
ATOM   5194  H HD21 . LEU   A  1 343 ? 16.721 -17.192 -25.421 0.00 27.95  ? 369  LEU   A HD21 1 
ATOM   5195  H HD22 . LEU   A  1 343 ? 15.318 -18.283 -25.273 0.00 28.67  ? 369  LEU   A HD22 1 
ATOM   5196  H HD23 . LEU   A  1 343 ? 15.993 -17.908 -26.881 0.00 28.35  ? 369  LEU   A HD23 1 
ATOM   5197  N N    . ARG   A  1 344 ? 13.229 -13.877 -28.002 1.00 20.40  ? 370  ARG   A N    1 
ATOM   5198  C CA   . ARG   A  1 344 ? 13.593 -13.093 -29.175 1.00 20.78  ? 370  ARG   A CA   1 
ATOM   5199  C C    . ARG   A  1 344 ? 15.110 -12.961 -29.301 1.00 21.04  ? 370  ARG   A C    1 
ATOM   5200  O O    . ARG   A  1 344 ? 15.617 -12.901 -30.423 1.00 21.31  ? 370  ARG   A O    1 
ATOM   5201  C CB   . ARG   A  1 344 ? 12.987 -11.685 -29.091 1.00 22.31  ? 370  ARG   A CB   1 
ATOM   5202  C CG   . ARG   A  1 344 ? 11.468 -11.641 -29.145 1.00 26.68  ? 370  ARG   A CG   1 
ATOM   5203  C CD   . ARG   A  1 344 ? 11.001 -10.196 -29.228 1.00 31.10  ? 370  ARG   A CD   1 
ATOM   5204  N NE   . ARG   A  1 344 ? 9.545  -10.056 -29.169 1.00 35.61  ? 370  ARG   A NE   1 
ATOM   5205  C CZ   . ARG   A  1 344 ? 8.706  -10.224 -30.193 1.00 40.37  ? 370  ARG   A CZ   1 
ATOM   5206  N NH1  . ARG   A  1 344 ? 9.163  -10.586 -31.391 1.00 41.28  ? 370  ARG   A NH1  1 
ATOM   5207  N NH2  . ARG   A  1 344 ? 7.399  -10.058 -30.022 1.00 41.69  ? 370  ARG   A NH2  1 
ATOM   5208  H H    . ARG   A  1 344 ? 13.436 -13.383 -27.140 0.00 24.45  ? 370  ARG   A H    1 
ATOM   5209  H HA   . ARG   A  1 344 ? 13.219 -13.562 -30.083 0.00 25.09  ? 370  ARG   A HA   1 
ATOM   5210  H HB2  . ARG   A  1 344 ? 13.295 -11.226 -28.153 0.00 26.41  ? 370  ARG   A HB2  1 
ATOM   5211  H HB3  . ARG   A  1 344 ? 13.361 -11.096 -29.927 0.00 26.41  ? 370  ARG   A HB3  1 
ATOM   5212  H HG2  . ARG   A  1 344 ? 11.119 -12.170 -30.030 0.00 32.71  ? 370  ARG   A HG2  1 
ATOM   5213  H HG3  . ARG   A  1 344 ? 11.056 -12.088 -28.241 0.00 32.65  ? 370  ARG   A HG3  1 
ATOM   5214  H HD2  . ARG   A  1 344 ? 11.408 -9.660  -28.373 0.00 37.43  ? 370  ARG   A HD2  1 
ATOM   5215  H HD3  . ARG   A  1 344 ? 11.373 -9.740  -30.144 0.00 37.52  ? 370  ARG   A HD3  1 
ATOM   5216  H HE   . ARG   A  1 344 ? 9.149  -9.777  -28.277 0.00 43.78  ? 370  ARG   A HE   1 
ATOM   5217  H HH11 . ARG   A  1 344 ? 10.149 -10.736 -31.574 0.00 50.48  ? 370  ARG   A HH11 1 
ATOM   5218  H HH12 . ARG   A  1 344 ? 8.508  -10.723 -32.154 0.00 51.24  ? 370  ARG   A HH12 1 
ATOM   5219  H HH21 . ARG   A  1 344 ? 7.030  -9.785  -29.117 0.00 52.06  ? 370  ARG   A HH21 1 
ATOM   5220  H HH22 . ARG   A  1 344 ? 6.764  -10.196 -30.801 0.00 52.35  ? 370  ARG   A HH22 1 
ATOM   5221  N N    . ALA   A  1 345 ? 15.837 -12.837 -28.168 1.00 20.21  ? 371  ALA   A N    1 
ATOM   5222  C CA   . ALA   A  1 345 ? 17.287 -12.656 -28.226 1.00 20.29  ? 371  ALA   A CA   1 
ATOM   5223  C C    . ALA   A  1 345 ? 17.948 -13.440 -27.117 1.00 20.77  ? 371  ALA   A C    1 
ATOM   5224  O O    . ALA   A  1 345 ? 17.515 -13.363 -25.961 1.00 21.43  ? 371  ALA   A O    1 
ATOM   5225  C CB   . ALA   A  1 345 ? 17.636 -11.182 -28.091 1.00 20.13  ? 371  ALA   A CB   1 
ATOM   5226  H H    . ALA   A  1 345 ? 15.460 -12.840 -27.226 0.00 23.44  ? 371  ALA   A H    1 
ATOM   5227  H HA   . ALA   A  1 345 ? 17.681 -13.012 -29.176 0.00 22.92  ? 371  ALA   A HA   1 
ATOM   5228  H HB1  . ALA   A  1 345 ? 18.718 -11.067 -28.133 0.00 22.06  ? 371  ALA   A HB1  1 
ATOM   5229  H HB2  . ALA   A  1 345 ? 17.173 -10.634 -28.910 0.00 22.43  ? 371  ALA   A HB2  1 
ATOM   5230  H HB3  . ALA   A  1 345 ? 17.259 -10.815 -27.137 0.00 22.43  ? 371  ALA   A HB3  1 
ATOM   5231  N N    . LEU   A  1 346 ? 19.001 -14.191 -27.465 1.00 19.66  ? 372  LEU   A N    1 
ATOM   5232  C CA   . LEU   A  1 346 ? 19.746 -14.972 -26.499 1.00 19.08  ? 372  LEU   A CA   1 
ATOM   5233  C C    . LEU   A  1 346 ? 21.206 -14.544 -26.575 1.00 18.55  ? 372  LEU   A C    1 
ATOM   5234  O O    . LEU   A  1 346 ? 21.834 -14.652 -27.642 1.00 18.16  ? 372  LEU   A O    1 
ATOM   5235  C CB   . LEU   A  1 346 ? 19.611 -16.465 -26.809 1.00 19.26  ? 372  LEU   A CB   1 
ATOM   5236  C CG   . LEU   A  1 346 ? 20.394 -17.433 -25.901 1.00 21.36  ? 372  LEU   A CG   1 
ATOM   5237  C CD1  . LEU   A  1 346 ? 20.011 -17.250 -24.408 1.00 21.76  ? 372  LEU   A CD1  1 
ATOM   5238  C CD2  . LEU   A  1 346 ? 20.145 -18.879 -26.333 1.00 22.15  ? 372  LEU   A CD2  1 
ATOM   5239  H H    . LEU   A  1 346 ? 19.365 -14.270 -28.409 0.00 21.97  ? 372  LEU   A H    1 
ATOM   5240  H HA   . LEU   A  1 346 ? 19.378 -14.790 -25.490 0.00 21.42  ? 372  LEU   A HA   1 
ATOM   5241  H HB2  . LEU   A  1 346 ? 18.559 -16.737 -26.745 0.00 22.32  ? 372  LEU   A HB2  1 
ATOM   5242  H HB3  . LEU   A  1 346 ? 19.961 -16.631 -27.826 0.00 21.93  ? 372  LEU   A HB3  1 
ATOM   5243  H HG   . LEU   A  1 346 ? 21.462 -17.247 -25.999 0.00 24.31  ? 372  LEU   A HG   1 
ATOM   5244  H HD11 . LEU   A  1 346 ? 20.442 -18.066 -23.830 0.00 25.33  ? 372  LEU   A HD11 1 
ATOM   5245  H HD12 . LEU   A  1 346 ? 20.410 -16.302 -24.051 0.00 24.83  ? 372  LEU   A HD12 1 
ATOM   5246  H HD13 . LEU   A  1 346 ? 18.926 -17.259 -24.315 0.00 25.42  ? 372  LEU   A HD13 1 
ATOM   5247  H HD21 . LEU   A  1 346 ? 20.680 -19.551 -25.664 0.00 26.14  ? 372  LEU   A HD21 1 
ATOM   5248  H HD22 . LEU   A  1 346 ? 19.076 -19.084 -26.287 0.00 26.35  ? 372  LEU   A HD22 1 
ATOM   5249  H HD23 . LEU   A  1 346 ? 20.503 -19.008 -27.354 0.00 25.98  ? 372  LEU   A HD23 1 
ATOM   5250  N N    . HIS   A  1 347 ? 21.737 -14.029 -25.460 1.00 17.83  ? 373  HIS   A N    1 
ATOM   5251  C CA   . HIS   A  1 347 ? 23.123 -13.598 -25.416 1.00 18.11  ? 373  HIS   A CA   1 
ATOM   5252  C C    . HIS   A  1 347 ? 23.951 -14.608 -24.640 1.00 18.11  ? 373  HIS   A C    1 
ATOM   5253  O O    . HIS   A  1 347 ? 23.699 -14.847 -23.456 1.00 18.18  ? 373  HIS   A O    1 
ATOM   5254  C CB   . HIS   A  1 347 ? 23.265 -12.180 -24.846 1.00 18.72  ? 373  HIS   A CB   1 
ATOM   5255  C CG   . HIS   A  1 347 ? 22.395 -11.187 -25.546 1.00 20.94  ? 373  HIS   A CG   1 
ATOM   5256  N ND1  . HIS   A  1 347 ? 22.863 -10.472 -26.632 1.00 22.43  ? 373  HIS   A ND1  1 
ATOM   5257  C CD2  . HIS   A  1 347 ? 21.100 -10.859 -25.327 1.00 22.23  ? 373  HIS   A CD2  1 
ATOM   5258  C CE1  . HIS   A  1 347 ? 21.845 -9.729  -27.046 1.00 23.21  ? 373  HIS   A CE1  1 
ATOM   5259  N NE2  . HIS   A  1 347 ? 20.763 -9.925  -26.286 1.00 23.51  ? 373  HIS   A NE2  1 
ATOM   5260  H H    . HIS   A  1 347 ? 21.241 -13.900 -24.584 0.00 19.33  ? 373  HIS   A H    1 
ATOM   5261  H HA   . HIS   A  1 347 ? 23.515 -13.553 -26.427 0.00 19.07  ? 373  HIS   A HA   1 
ATOM   5262  H HB2  . HIS   A  1 347 ? 23.052 -12.155 -23.781 0.00 19.72  ? 373  HIS   A HB2  1 
ATOM   5263  H HB3  . HIS   A  1 347 ? 24.294 -11.861 -25.006 0.00 19.37  ? 373  HIS   A HB3  1 
ATOM   5264  H HD2  . HIS   A  1 347 ? 20.456 -11.253 -24.556 0.00 24.26  ? 373  HIS   A HD2  1 
ATOM   5265  H HE1  . HIS   A  1 347 ? 21.888 -9.055  -27.886 0.00 24.66  ? 373  HIS   A HE1  1 
ATOM   5266  H HE2  . HIS   A  1 347 ? 19.861 -9.471  -26.394 0.00 25.59  ? 373  HIS   A HE2  1 
ATOM   5267  N N    . LEU   A  1 348 ? 24.914 -15.228 -25.320 1.00 17.69  ? 374  LEU   A N    1 
ATOM   5268  C CA   . LEU   A  1 348 ? 25.791 -16.228 -24.721 1.00 18.96  ? 374  LEU   A CA   1 
ATOM   5269  C C    . LEU   A  1 348 ? 27.245 -15.890 -25.043 1.00 19.29  ? 374  LEU   A C    1 
ATOM   5270  O O    . LEU   A  1 348 ? 28.004 -16.758 -25.464 1.00 19.86  ? 374  LEU   A O    1 
ATOM   5271  C CB   . LEU   A  1 348 ? 25.417 -17.641 -25.234 1.00 20.01  ? 374  LEU   A CB   1 
ATOM   5272  C CG   . LEU   A  1 348 ? 24.178 -18.297 -24.611 1.00 22.12  ? 374  LEU   A CG   1 
ATOM   5273  C CD1  . LEU   A  1 348 ? 23.694 -19.436 -25.488 1.00 22.81  ? 374  LEU   A CD1  1 
ATOM   5274  C CD2  . LEU   A  1 348 ? 24.483 -18.851 -23.213 1.00 22.81  ? 374  LEU   A CD2  1 
ATOM   5275  H H    . LEU   A  1 348 ? 25.125 -15.062 -26.299 0.00 18.66  ? 374  LEU   A H    1 
ATOM   5276  H HA   . LEU   A  1 348 ? 25.699 -16.219 -23.637 0.00 20.54  ? 374  LEU   A HA   1 
ATOM   5277  H HB2  . LEU   A  1 348 ? 25.246 -17.578 -26.308 0.00 22.11  ? 374  LEU   A HB2  1 
ATOM   5278  H HB3  . LEU   A  1 348 ? 26.240 -18.326 -25.039 0.00 22.25  ? 374  LEU   A HB3  1 
ATOM   5279  H HG   . LEU   A  1 348 ? 23.379 -17.562 -24.528 0.00 25.00  ? 374  LEU   A HG   1 
ATOM   5280  H HD11 . LEU   A  1 348 ? 22.875 -19.950 -24.986 0.00 26.65  ? 374  LEU   A HD11 1 
ATOM   5281  H HD12 . LEU   A  1 348 ? 23.351 -19.030 -26.438 0.00 26.22  ? 374  LEU   A HD12 1 
ATOM   5282  H HD13 . LEU   A  1 348 ? 24.519 -20.128 -25.656 0.00 26.42  ? 374  LEU   A HD13 1 
ATOM   5283  H HD21 . LEU   A  1 348 ? 23.583 -19.317 -22.814 0.00 26.44  ? 374  LEU   A HD21 1 
ATOM   5284  H HD22 . LEU   A  1 348 ? 25.276 -19.594 -23.289 0.00 26.25  ? 374  LEU   A HD22 1 
ATOM   5285  H HD23 . LEU   A  1 348 ? 24.796 -18.042 -22.557 0.00 25.88  ? 374  LEU   A HD23 1 
ATOM   5286  N N    . ARG   A  1 349 ? 27.643 -14.623 -24.841 1.00 19.11  ? 375  ARG   A N    1 
ATOM   5287  C CA   . ARG   A  1 349 ? 29.056 -14.264 -25.015 1.00 19.54  ? 375  ARG   A CA   1 
ATOM   5288  C C    . ARG   A  1 349 ? 29.829 -14.873 -23.839 1.00 18.89  ? 375  ARG   A C    1 
ATOM   5289  O O    . ARG   A  1 349 ? 29.237 -15.112 -22.809 1.00 18.90  ? 375  ARG   A O    1 
ATOM   5290  C CB   . ARG   A  1 349 ? 29.267 -12.749 -24.984 1.00 21.75  ? 375  ARG   A CB   1 
ATOM   5291  C CG   . ARG   A  1 349 ? 28.515 -11.995 -26.056 1.00 28.30  ? 375  ARG   A CG   1 
ATOM   5292  C CD   . ARG   A  1 349 ? 29.151 -10.646 -26.327 1.00 34.72  ? 375  ARG   A CD   1 
ATOM   5293  N NE   . ARG   A  1 349 ? 29.177 -9.812  -25.132 1.00 40.04  ? 375  ARG   A NE   1 
ATOM   5294  C CZ   . ARG   A  1 349 ? 29.856 -8.673  -25.016 1.00 44.78  ? 375  ARG   A CZ   1 
ATOM   5295  N NH1  . ARG   A  1 349 ? 30.568 -8.204  -26.040 1.00 44.63  ? 375  ARG   A NH1  1 
ATOM   5296  N NH2  . ARG   A  1 349 ? 29.820 -7.986  -23.880 1.00 45.91  ? 375  ARG   A NH2  1 
ATOM   5297  H H    . ARG   A  1 349 ? 27.043 -13.860 -24.547 0.00 19.89  ? 375  ARG   A H    1 
ATOM   5298  H HA   . ARG   A  1 349 ? 29.448 -14.657 -25.952 0.00 20.28  ? 375  ARG   A HA   1 
ATOM   5299  H HB2  . ARG   A  1 349 ? 28.937 -12.350 -24.029 0.00 22.57  ? 375  ARG   A HB2  1 
ATOM   5300  H HB3  . ARG   A  1 349 ? 30.329 -12.549 -25.116 0.00 22.42  ? 375  ARG   A HB3  1 
ATOM   5301  H HG2  . ARG   A  1 349 ? 28.533 -12.571 -26.980 0.00 30.34  ? 375  ARG   A HG2  1 
ATOM   5302  H HG3  . ARG   A  1 349 ? 27.489 -11.832 -25.731 0.00 30.36  ? 375  ARG   A HG3  1 
ATOM   5303  H HD2  . ARG   A  1 349 ? 30.178 -10.801 -26.657 0.00 37.54  ? 375  ARG   A HD2  1 
ATOM   5304  H HD3  . ARG   A  1 349 ? 28.591 -10.125 -27.102 0.00 37.54  ? 375  ARG   A HD3  1 
ATOM   5305  H HE   . ARG   A  1 349 ? 28.639 -10.126 -24.330 0.00 44.10  ? 375  ARG   A HE   1 
ATOM   5306  H HH11 . ARG   A  1 349 ? 30.626 -8.700  -26.924 0.00 49.03  ? 375  ARG   A HH11 1 
ATOM   5307  H HH12 . ARG   A  1 349 ? 31.080 -7.334  -25.937 0.00 48.87  ? 375  ARG   A HH12 1 
ATOM   5308  H HH21 . ARG   A  1 349 ? 29.272 -8.327  -23.096 0.00 50.91  ? 375  ARG   A HH21 1 
ATOM   5309  H HH22 . ARG   A  1 349 ? 30.329 -7.113  -23.794 0.00 50.60  ? 375  ARG   A HH22 1 
ATOM   5310  N N    . GLY   A  1 350 ? 31.119 -15.107 -23.988 1.00 18.03  ? 376  GLY   A N    1 
ATOM   5311  C CA   . GLY   A  1 350 ? 31.955 -15.549 -22.880 1.00 18.32  ? 376  GLY   A CA   1 
ATOM   5312  C C    . GLY   A  1 350 ? 31.537 -16.779 -22.087 1.00 18.32  ? 376  GLY   A C    1 
ATOM   5313  O O    . GLY   A  1 350 ? 31.783 -16.831 -20.887 1.00 17.97  ? 376  GLY   A O    1 
ATOM   5314  H H    . GLY   A  1 350 ? 31.620 -15.003 -24.866 0.00 18.48  ? 376  GLY   A H    1 
ATOM   5315  H HA2  . GLY   A  1 350 ? 32.954 -15.745 -23.269 0.00 19.12  ? 376  GLY   A HA2  1 
ATOM   5316  H HA3  . GLY   A  1 350 ? 32.041 -14.727 -22.171 0.00 18.98  ? 376  GLY   A HA3  1 
ATOM   5317  N N    . TYR   A  1 351 ? 30.902 -17.768 -22.739 1.00 18.07  ? 377  TYR   A N    1 
ATOM   5318  C CA   . TYR   A  1 351 ? 30.645 -19.106 -22.183 1.00 19.50  ? 377  TYR   A CA   1 
ATOM   5319  C C    . TYR   A  1 351 ? 31.985 -19.871 -22.301 1.00 19.57  ? 377  TYR   A C    1 
ATOM   5320  O O    . TYR   A  1 351 ? 32.438 -20.498 -21.330 1.00 19.31  ? 377  TYR   A O    1 
ATOM   5321  C CB   . TYR   A  1 351 ? 29.541 -19.837 -22.983 1.00 20.06  ? 377  TYR   A CB   1 
ATOM   5322  C CG   . TYR   A  1 351 ? 29.245 -21.236 -22.487 1.00 20.45  ? 377  TYR   A CG   1 
ATOM   5323  C CD1  . TYR   A  1 351 ? 30.036 -22.313 -22.868 1.00 21.08  ? 377  TYR   A CD1  1 
ATOM   5324  C CD2  . TYR   A  1 351 ? 28.109 -21.501 -21.729 1.00 21.15  ? 377  TYR   A CD2  1 
ATOM   5325  C CE1  . TYR   A  1 351 ? 29.753 -23.603 -22.446 1.00 21.62  ? 377  TYR   A CE1  1 
ATOM   5326  C CE2  . TYR   A  1 351 ? 27.792 -22.797 -21.336 1.00 22.15  ? 377  TYR   A CE2  1 
ATOM   5327  C CZ   . TYR   A  1 351 ? 28.634 -23.842 -21.677 1.00 22.85  ? 377  TYR   A CZ   1 
ATOM   5328  O OH   . TYR   A  1 351 ? 28.332 -25.133 -21.352 1.00 24.96  ? 377  TYR   A OH   1 
ATOM   5329  H H    . TYR   A  1 351 ? 30.551 -17.673 -23.686 0.00 19.42  ? 377  TYR   A H    1 
ATOM   5330  H HA   . TYR   A  1 351 ? 30.355 -19.045 -21.136 0.00 21.83  ? 377  TYR   A HA   1 
ATOM   5331  H HB2  . TYR   A  1 351 ? 28.623 -19.255 -22.922 0.00 22.51  ? 377  TYR   A HB2  1 
ATOM   5332  H HB3  . TYR   A  1 351 ? 29.854 -19.916 -24.023 0.00 22.56  ? 377  TYR   A HB3  1 
ATOM   5333  H HD1  . TYR   A  1 351 ? 30.916 -22.133 -23.462 0.00 24.58  ? 377  TYR   A HD1  1 
ATOM   5334  H HD2  . TYR   A  1 351 ? 27.456 -20.693 -21.453 0.00 24.54  ? 377  TYR   A HD2  1 
ATOM   5335  H HE1  . TYR   A  1 351 ? 30.384 -24.422 -22.747 0.00 26.23  ? 377  TYR   A HE1  1 
ATOM   5336  H HE2  . TYR   A  1 351 ? 26.916 -22.974 -20.736 0.00 26.69  ? 377  TYR   A HE2  1 
ATOM   5337  H HH   . TYR   A  1 351 ? 27.550 -25.173 -20.742 0.00 30.91  ? 377  TYR   A HH   1 
ATOM   5338  N N    . VAL   A  1 352 ? 32.625 -19.784 -23.503 1.00 19.48  ? 378  VAL   A N    1 
ATOM   5339  C CA   . VAL   A  1 352 ? 33.953 -20.306 -23.852 1.00 20.56  ? 378  VAL   A CA   1 
ATOM   5340  C C    . VAL   A  1 352 ? 33.902 -21.791 -24.196 1.00 21.15  ? 378  VAL   A C    1 
ATOM   5341  O O    . VAL   A  1 352 ? 33.814 -22.634 -23.317 1.00 21.43  ? 378  VAL   A O    1 
ATOM   5342  C CB   . VAL   A  1 352 ? 35.048 -19.978 -22.801 1.00 21.26  ? 378  VAL   A CB   1 
ATOM   5343  C CG1  . VAL   A  1 352 ? 36.419 -20.471 -23.269 1.00 22.14  ? 378  VAL   A CG1  1 
ATOM   5344  C CG2  . VAL   A  1 352 ? 35.091 -18.473 -22.533 1.00 21.26  ? 378  VAL   A CG2  1 
ATOM   5345  H H    . VAL   A  1 352 ? 32.199 -19.339 -24.311 0.00 21.54  ? 378  VAL   A H    1 
ATOM   5346  H HA   . VAL   A  1 352 ? 34.263 -19.779 -24.753 0.00 22.94  ? 378  VAL   A HA   1 
ATOM   5347  H HB   . VAL   A  1 352 ? 34.811 -20.482 -21.866 0.00 24.32  ? 378  VAL   A HB   1 
ATOM   5348  H HG11 . VAL   A  1 352 ? 37.173 -20.018 -22.628 0.00 25.22  ? 378  VAL   A HG11 1 
ATOM   5349  H HG12 . VAL   A  1 352 ? 36.469 -21.554 -23.165 0.00 25.69  ? 378  VAL   A HG12 1 
ATOM   5350  H HG13 . VAL   A  1 352 ? 36.577 -20.180 -24.307 0.00 25.08  ? 378  VAL   A HG13 1 
ATOM   5351  H HG21 . VAL   A  1 352 ? 35.778 -18.288 -21.710 0.00 23.62  ? 378  VAL   A HG21 1 
ATOM   5352  H HG22 . VAL   A  1 352 ? 35.444 -17.967 -23.431 0.00 23.32  ? 378  VAL   A HG22 1 
ATOM   5353  H HG23 . VAL   A  1 352 ? 34.099 -18.110 -22.269 0.00 23.46  ? 378  VAL   A HG23 1 
ATOM   5354  N N    . PHE   A  1 353 ? 33.931 -22.092 -25.495 1.00 21.24  ? 379  PHE   A N    1 
ATOM   5355  C CA   . PHE   A  1 353 ? 33.890 -23.462 -26.007 1.00 22.09  ? 379  PHE   A CA   1 
ATOM   5356  C C    . PHE   A  1 353 ? 34.522 -23.501 -27.398 1.00 22.99  ? 379  PHE   A C    1 
ATOM   5357  O O    . PHE   A  1 353 ? 34.602 -22.476 -28.076 1.00 23.16  ? 379  PHE   A O    1 
ATOM   5358  C CB   . PHE   A  1 353 ? 32.462 -24.038 -26.008 1.00 21.23  ? 379  PHE   A CB   1 
ATOM   5359  C CG   . PHE   A  1 353 ? 31.471 -23.303 -26.883 1.00 20.57  ? 379  PHE   A CG   1 
ATOM   5360  C CD1  . PHE   A  1 353 ? 30.907 -22.111 -26.467 1.00 20.44  ? 379  PHE   A CD1  1 
ATOM   5361  C CD2  . PHE   A  1 353 ? 31.051 -23.845 -28.088 1.00 20.62  ? 379  PHE   A CD2  1 
ATOM   5362  C CE1  . PHE   A  1 353 ? 29.969 -21.452 -27.257 1.00 21.11  ? 379  PHE   A CE1  1 
ATOM   5363  C CE2  . PHE   A  1 353 ? 30.110 -23.184 -28.876 1.00 21.22  ? 379  PHE   A CE2  1 
ATOM   5364  C CZ   . PHE   A  1 353 ? 29.584 -21.986 -28.458 1.00 21.16  ? 379  PHE   A CZ   1 
ATOM   5365  H H    . PHE   A  1 353 ? 33.969 -21.393 -26.230 0.00 24.25  ? 379  PHE   A H    1 
ATOM   5366  H HA   . PHE   A  1 353 ? 34.499 -24.099 -25.367 0.00 26.42  ? 379  PHE   A HA   1 
ATOM   5367  H HB2  . PHE   A  1 353 ? 32.506 -25.071 -26.348 0.00 25.75  ? 379  PHE   A HB2  1 
ATOM   5368  H HB3  . PHE   A  1 353 ? 32.079 -24.010 -24.988 0.00 25.37  ? 379  PHE   A HB3  1 
ATOM   5369  H HD1  . PHE   A  1 353 ? 31.208 -21.681 -25.526 0.00 23.49  ? 379  PHE   A HD1  1 
ATOM   5370  H HD2  . PHE   A  1 353 ? 31.463 -24.780 -28.429 0.00 24.86  ? 379  PHE   A HD2  1 
ATOM   5371  H HE1  . PHE   A  1 353 ? 29.555 -20.514 -26.928 0.00 23.89  ? 379  PHE   A HE1  1 
ATOM   5372  H HE2  . PHE   A  1 353 ? 29.806 -23.605 -29.820 0.00 25.16  ? 379  PHE   A HE2  1 
ATOM   5373  H HZ   . PHE   A  1 353 ? 28.859 -21.475 -29.070 0.00 24.33  ? 379  PHE   A HZ   1 
ATOM   5374  N N    . GLN   A  1 354 ? 35.014 -24.677 -27.797 1.00 22.99  ? 380  GLN   A N    1 
ATOM   5375  C CA   . GLN   A  1 354 ? 35.782 -24.826 -29.032 1.00 23.68  ? 380  GLN   A CA   1 
ATOM   5376  C C    . GLN   A  1 354 ? 34.981 -25.046 -30.299 1.00 24.00  ? 380  GLN   A C    1 
ATOM   5377  O O    . GLN   A  1 354 ? 35.450 -24.641 -31.353 1.00 23.84  ? 380  GLN   A O    1 
ATOM   5378  C CB   . GLN   A  1 354 ? 36.797 -25.990 -28.894 1.00 25.30  ? 380  GLN   A CB   1 
ATOM   5379  C CG   . GLN   A  1 354 ? 37.676 -25.917 -27.647 1.00 27.66  ? 380  GLN   A CG   1 
ATOM   5380  C CD   . GLN   A  1 354 ? 38.524 -27.159 -27.474 1.00 33.31  ? 380  GLN   A CD   1 
ATOM   5381  O OE1  . GLN   A  1 354 ? 38.970 -27.777 -28.445 1.00 35.38  ? 380  GLN   A OE1  1 
ATOM   5382  N NE2  . GLN   A  1 354 ? 38.781 -27.549 -26.236 1.00 32.98  ? 380  GLN   A NE2  1 
ATOM   5383  H H    . GLN   A  1 354 ? 34.884 -25.546 -27.288 0.00 28.05  ? 380  GLN   A H    1 
ATOM   5384  H HA   . GLN   A  1 354 ? 36.379 -23.925 -29.168 0.00 28.14  ? 380  GLN   A HA   1 
ATOM   5385  H HB2  . GLN   A  1 354 ? 36.249 -26.930 -28.864 0.00 31.47  ? 380  GLN   A HB2  1 
ATOM   5386  H HB3  . GLN   A  1 354 ? 37.454 -25.978 -29.763 0.00 31.06  ? 380  GLN   A HB3  1 
ATOM   5387  H HG2  . GLN   A  1 354 ? 38.343 -25.060 -27.733 0.00 33.59  ? 380  GLN   A HG2  1 
ATOM   5388  H HG3  . GLN   A  1 354 ? 37.048 -25.814 -26.764 0.00 33.89  ? 380  GLN   A HG3  1 
ATOM   5389  H HE21 . GLN   A  1 354 ? 38.422 -27.028 -25.443 0.00 41.02  ? 380  GLN   A HE21 1 
ATOM   5390  H HE22 . GLN   A  1 354 ? 39.346 -28.377 -26.078 0.00 41.74  ? 380  GLN   A HE22 1 
ATOM   5391  N N    . GLU   A  1 355 ? 33.829 -25.730 -30.232 1.00 24.50  ? 381  GLU   A N    1 
ATOM   5392  C CA   . GLU   A  1 355 ? 33.092 -26.079 -31.447 1.00 25.90  ? 381  GLU   A CA   1 
ATOM   5393  C C    . GLU   A  1 355 ? 31.579 -26.005 -31.264 1.00 26.29  ? 381  GLU   A C    1 
ATOM   5394  O O    . GLU   A  1 355 ? 31.066 -26.525 -30.277 1.00 26.36  ? 381  GLU   A O    1 
ATOM   5395  C CB   . GLU   A  1 355 ? 33.484 -27.515 -31.831 1.00 29.36  ? 381  GLU   A CB   1 
ATOM   5396  C CG   . GLU   A  1 355 ? 32.895 -28.022 -33.135 1.00 38.27  ? 381  GLU   A CG   1 
ATOM   5397  C CD   . GLU   A  1 355 ? 33.254 -29.461 -33.470 1.00 47.25  ? 381  GLU   A CD   1 
ATOM   5398  O OE1  . GLU   A  1 355 ? 33.739 -30.192 -32.573 1.00 48.53  ? 381  GLU   A OE1  1 
ATOM   5399  O OE2  . GLU   A  1 355 ? 33.033 -29.860 -34.637 1.00 49.77  ? 381  GLU   A OE2  1 
ATOM   5400  H H    . GLU   A  1 355 ? 33.392 -26.056 -29.376 0.00 30.04  ? 381  GLU   A H    1 
ATOM   5401  H HA   . GLU   A  1 355 ? 33.362 -25.419 -32.270 0.00 31.45  ? 381  GLU   A HA   1 
ATOM   5402  H HB2  . GLU   A  1 355 ? 34.569 -27.568 -31.915 0.00 36.62  ? 381  GLU   A HB2  1 
ATOM   5403  H HB3  . GLU   A  1 355 ? 33.147 -28.176 -31.034 0.00 36.91  ? 381  GLU   A HB3  1 
ATOM   5404  H HG2  . GLU   A  1 355 ? 31.808 -27.975 -33.095 0.00 47.55  ? 381  GLU   A HG2  1 
ATOM   5405  H HG3  . GLU   A  1 355 ? 33.261 -27.396 -33.947 0.00 47.29  ? 381  GLU   A HG3  1 
ATOM   5406  N N    . LEU   A  1 356 ? 30.859 -25.442 -32.256 1.00 26.18  ? 382  LEU   A N    1 
ATOM   5407  C CA   . LEU   A  1 356 ? 29.404 -25.407 -32.218 1.00 26.55  ? 382  LEU   A CA   1 
ATOM   5408  C C    . LEU   A  1 356 ? 28.883 -26.452 -33.210 1.00 27.42  ? 382  LEU   A C    1 
ATOM   5409  O O    . LEU   A  1 356 ? 29.137 -26.340 -34.406 1.00 26.21  ? 382  LEU   A O    1 
ATOM   5410  C CB   . LEU   A  1 356 ? 28.856 -24.009 -32.558 1.00 26.33  ? 382  LEU   A CB   1 
ATOM   5411  C CG   . LEU   A  1 356 ? 27.329 -23.838 -32.409 1.00 26.88  ? 382  LEU   A CG   1 
ATOM   5412  C CD1  . LEU   A  1 356 ? 26.857 -24.057 -30.955 1.00 26.88  ? 382  LEU   A CD1  1 
ATOM   5413  C CD2  . LEU   A  1 356 ? 26.892 -22.469 -32.906 1.00 27.24  ? 382  LEU   A CD2  1 
ATOM   5414  H H    . LEU   A  1 356 ? 31.251 -25.016 -33.089 0.00 31.71  ? 382  LEU   A H    1 
ATOM   5415  H HA   . LEU   A  1 356 ? 29.057 -25.673 -31.221 0.00 32.54  ? 382  LEU   A HA   1 
ATOM   5416  H HB2  . LEU   A  1 356 ? 29.336 -23.280 -31.907 0.00 31.24  ? 382  LEU   A HB2  1 
ATOM   5417  H HB3  . LEU   A  1 356 ? 29.102 -23.788 -33.595 0.00 31.55  ? 382  LEU   A HB3  1 
ATOM   5418  H HG   . LEU   A  1 356 ? 26.824 -24.585 -33.019 0.00 32.76  ? 382  LEU   A HG   1 
ATOM   5419  H HD11 . LEU   A  1 356 ? 25.843 -23.674 -30.851 0.00 32.41  ? 382  LEU   A HD11 1 
ATOM   5420  H HD12 . LEU   A  1 356 ? 26.865 -25.123 -30.734 0.00 32.90  ? 382  LEU   A HD12 1 
ATOM   5421  H HD13 . LEU   A  1 356 ? 27.528 -23.528 -30.279 0.00 32.14  ? 382  LEU   A HD13 1 
ATOM   5422  H HD21 . LEU   A  1 356 ? 25.808 -22.392 -32.832 0.00 32.41  ? 382  LEU   A HD21 1 
ATOM   5423  H HD22 . LEU   A  1 356 ? 27.363 -21.705 -32.291 0.00 31.91  ? 382  LEU   A HD22 1 
ATOM   5424  H HD23 . LEU   A  1 356 ? 27.200 -22.356 -33.944 0.00 32.27  ? 382  LEU   A HD23 1 
ATOM   5425  N N    . ARG   A  1 357 ? 28.177 -27.473 -32.705 1.00 29.73  ? 383  ARG   A N    1 
ATOM   5426  C CA   . ARG   A  1 357 ? 27.615 -28.541 -33.542 1.00 32.07  ? 383  ARG   A CA   1 
ATOM   5427  C C    . ARG   A  1 357 ? 26.116 -28.334 -33.683 1.00 33.59  ? 383  ARG   A C    1 
ATOM   5428  O O    . ARG   A  1 357 ? 25.491 -27.736 -32.801 1.00 33.40  ? 383  ARG   A O    1 
ATOM   5429  C CB   . ARG   A  1 357 ? 27.859 -29.921 -32.915 1.00 34.02  ? 383  ARG   A CB   1 
ATOM   5430  C CG   . ARG   A  1 357 ? 29.297 -30.224 -32.542 1.00 38.14  ? 383  ARG   A CG   1 
ATOM   5431  C CD   . ARG   A  1 357 ? 29.397 -31.602 -31.902 1.00 42.14  ? 383  ARG   A CD   1 
ATOM   5432  N NE   . ARG   A  1 357 ? 28.702 -31.660 -30.613 1.00 44.94  ? 383  ARG   A NE   1 
ATOM   5433  C CZ   . ARG   A  1 357 ? 28.628 -32.739 -29.838 1.00 48.05  ? 383  ARG   A CZ   1 
ATOM   5434  N NH1  . ARG   A  1 357 ? 29.217 -33.874 -30.207 1.00 48.58  ? 383  ARG   A NH1  1 
ATOM   5435  N NH2  . ARG   A  1 357 ? 27.965 -32.694 -28.687 1.00 47.18  ? 383  ARG   A NH2  1 
ATOM   5436  H H    . ARG   A  1 357 ? 27.973 -27.595 -31.718 0.00 37.37  ? 383  ARG   A H    1 
ATOM   5437  H HA   . ARG   A  1 357 ? 28.060 -28.542 -34.536 0.00 40.80  ? 383  ARG   A HA   1 
ATOM   5438  H HB2  . ARG   A  1 357 ? 27.252 -29.985 -32.014 0.00 43.81  ? 383  ARG   A HB2  1 
ATOM   5439  H HB3  . ARG   A  1 357 ? 27.538 -30.683 -33.624 0.00 44.25  ? 383  ARG   A HB3  1 
ATOM   5440  H HG2  . ARG   A  1 357 ? 29.914 -30.215 -33.440 0.00 48.71  ? 383  ARG   A HG2  1 
ATOM   5441  H HG3  . ARG   A  1 357 ? 29.658 -29.490 -31.823 0.00 48.27  ? 383  ARG   A HG3  1 
ATOM   5442  H HD2  . ARG   A  1 357 ? 28.945 -32.338 -32.565 0.00 54.72  ? 383  ARG   A HD2  1 
ATOM   5443  H HD3  . ARG   A  1 357 ? 30.446 -31.842 -31.732 0.00 54.30  ? 383  ARG   A HD3  1 
ATOM   5444  H HE   . ARG   A  1 357 ? 28.246 -30.814 -30.286 0.00 57.19  ? 383  ARG   A HE   1 
ATOM   5445  H HH11 . ARG   A  1 357 ? 29.725 -33.952 -31.082 0.00 63.28  ? 383  ARG   A HH11 1 
ATOM   5446  H HH12 . ARG   A  1 357 ? 29.149 -34.692 -29.609 0.00 63.73  ? 383  ARG   A HH12 1 
ATOM   5447  H HH21 . ARG   A  1 357 ? 27.517 -31.834 -28.386 0.00 60.47  ? 383  ARG   A HH21 1 
ATOM   5448  H HH22 . ARG   A  1 357 ? 27.912 -33.516 -28.094 0.00 61.41  ? 383  ARG   A HH22 1 
ATOM   5449  N N    . GLU   A  1 358 ? 25.526 -28.870 -34.760 1.00 35.09  ? 384  GLU   A N    1 
ATOM   5450  C CA   . GLU   A  1 358 ? 24.087 -28.737 -34.990 1.00 36.85  ? 384  GLU   A CA   1 
ATOM   5451  C C    . GLU   A  1 358 ? 23.258 -29.319 -33.838 1.00 37.55  ? 384  GLU   A C    1 
ATOM   5452  O O    . GLU   A  1 358 ? 22.289 -28.687 -33.410 1.00 38.50  ? 384  GLU   A O    1 
ATOM   5453  C CB   . GLU   A  1 358 ? 23.700 -29.391 -36.326 1.00 40.41  ? 384  GLU   A CB   1 
ATOM   5454  C CG   . GLU   A  1 358 ? 22.216 -29.298 -36.634 1.00 46.92  ? 384  GLU   A CG   1 
ATOM   5455  C CD   . GLU   A  1 358 ? 21.881 -29.318 -38.111 1.00 54.56  ? 384  GLU   A CD   1 
ATOM   5456  O OE1  . GLU   A  1 358 ? 22.566 -30.041 -38.871 1.00 55.75  ? 384  GLU   A OE1  1 
ATOM   5457  O OE2  . GLU   A  1 358 ? 20.924 -28.613 -38.508 1.00 57.48  ? 384  GLU   A OE2  1 
ATOM   5458  H H    . GLU   A  1 358 ? 26.007 -29.408 -35.475 0.00 45.20  ? 384  GLU   A H    1 
ATOM   5459  H HA   . GLU   A  1 358 ? 23.853 -27.676 -35.050 0.00 46.75  ? 384  GLU   A HA   1 
ATOM   5460  H HB2  . GLU   A  1 358 ? 24.242 -28.890 -37.128 0.00 51.78  ? 384  GLU   A HB2  1 
ATOM   5461  H HB3  . GLU   A  1 358 ? 23.972 -30.445 -36.295 0.00 52.54  ? 384  GLU   A HB3  1 
ATOM   5462  H HG2  . GLU   A  1 358 ? 21.707 -30.142 -36.170 0.00 60.60  ? 384  GLU   A HG2  1 
ATOM   5463  H HG3  . GLU   A  1 358 ? 21.833 -28.365 -36.224 0.00 59.67  ? 384  GLU   A HG3  1 
ATOM   5464  N N    . ASP   A  1 359 ? 23.649 -30.483 -33.306 1.00 37.15  ? 385  ASP   A N    1 
ATOM   5465  C CA   . ASP   A  1 359 ? 22.922 -31.095 -32.188 1.00 37.56  ? 385  ASP   A CA   1 
ATOM   5466  C C    . ASP   A  1 359 ? 22.910 -30.204 -30.932 1.00 35.97  ? 385  ASP   A C    1 
ATOM   5467  O O    . ASP   A  1 359 ? 21.994 -30.325 -30.117 1.00 36.01  ? 385  ASP   A O    1 
ATOM   5468  C CB   . ASP   A  1 359 ? 23.529 -32.460 -31.802 1.00 40.88  ? 385  ASP   A CB   1 
ATOM   5469  C CG   . ASP   A  1 359 ? 23.152 -33.622 -32.706 1.00 48.18  ? 385  ASP   A CG   1 
ATOM   5470  O OD1  . ASP   A  1 359 ? 22.418 -33.395 -33.695 1.00 49.91  ? 385  ASP   A OD1  1 
ATOM   5471  O OD2  . ASP   A  1 359 ? 23.598 -34.759 -32.426 1.00 51.22  ? 385  ASP   A OD2  1 
ATOM   5472  H H    . ASP   A  1 359 ? 24.437 -31.029 -33.638 0.00 48.59  ? 385  ASP   A H    1 
ATOM   5473  H HA   . ASP   A  1 359 ? 21.896 -31.281 -32.498 0.00 49.59  ? 385  ASP   A HA   1 
ATOM   5474  H HB2  . ASP   A  1 359 ? 24.615 -32.381 -31.801 0.00 53.67  ? 385  ASP   A HB2  1 
ATOM   5475  H HB3  . ASP   A  1 359 ? 23.188 -32.710 -30.799 0.00 54.03  ? 385  ASP   A HB3  1 
ATOM   5476  N N    . ASP   A  1 360 ? 23.920 -29.330 -30.760 1.00 34.18  ? 386  ASP   A N    1 
ATOM   5477  C CA   . ASP   A  1 360 ? 24.013 -28.518 -29.549 1.00 33.40  ? 386  ASP   A CA   1 
ATOM   5478  C C    . ASP   A  1 360 ? 22.931 -27.431 -29.412 1.00 32.10  ? 386  ASP   A C    1 
ATOM   5479  O O    . ASP   A  1 360 ? 22.592 -27.097 -28.285 1.00 31.61  ? 386  ASP   A O    1 
ATOM   5480  C CB   . ASP   A  1 360 ? 25.407 -27.902 -29.392 1.00 34.82  ? 386  ASP   A CB   1 
ATOM   5481  C CG   . ASP   A  1 360 ? 26.525 -28.923 -29.427 1.00 40.43  ? 386  ASP   A CG   1 
ATOM   5482  O OD1  . ASP   A  1 360 ? 26.336 -30.035 -28.892 1.00 40.04  ? 386  ASP   A OD1  1 
ATOM   5483  O OD2  . ASP   A  1 360 ? 27.586 -28.610 -29.991 1.00 44.30  ? 386  ASP   A OD2  1 
ATOM   5484  H H    . ASP   A  1 360 ? 24.655 -29.148 -31.436 0.00 43.89  ? 386  ASP   A H    1 
ATOM   5485  H HA   . ASP   A  1 360 ? 23.876 -29.181 -28.696 0.00 42.99  ? 386  ASP   A HA   1 
ATOM   5486  H HB2  . ASP   A  1 360 ? 25.574 -27.194 -30.202 0.00 43.53  ? 386  ASP   A HB2  1 
ATOM   5487  H HB3  . ASP   A  1 360 ? 25.457 -27.386 -28.434 0.00 43.59  ? 386  ASP   A HB3  1 
ATOM   5488  N N    . PHE   A  1 361 ? 22.375 -26.912 -30.522 1.00 31.14  ? 387  PHE   A N    1 
ATOM   5489  C CA   . PHE   A  1 361 ? 21.336 -25.880 -30.453 1.00 30.54  ? 387  PHE   A CA   1 
ATOM   5490  C C    . PHE   A  1 361 ? 19.933 -26.393 -30.825 1.00 30.33  ? 387  PHE   A C    1 
ATOM   5491  O O    . PHE   A  1 361 ? 19.034 -25.584 -31.049 1.00 30.10  ? 387  PHE   A O    1 
ATOM   5492  C CB   . PHE   A  1 361 ? 21.753 -24.669 -31.317 1.00 29.72  ? 387  PHE   A CB   1 
ATOM   5493  C CG   . PHE   A  1 361 ? 22.655 -23.624 -30.691 1.00 29.57  ? 387  PHE   A CG   1 
ATOM   5494  C CD1  . PHE   A  1 361 ? 23.159 -23.782 -29.407 1.00 30.57  ? 387  PHE   A CD1  1 
ATOM   5495  C CD2  . PHE   A  1 361 ? 22.967 -22.462 -31.374 1.00 29.90  ? 387  PHE   A CD2  1 
ATOM   5496  C CE1  . PHE   A  1 361 ? 23.951 -22.797 -28.830 1.00 31.00  ? 387  PHE   A CE1  1 
ATOM   5497  C CE2  . PHE   A  1 361 ? 23.734 -21.473 -30.781 1.00 30.33  ? 387  PHE   A CE2  1 
ATOM   5498  C CZ   . PHE   A  1 361 ? 24.227 -21.650 -29.518 1.00 30.38  ? 387  PHE   A CZ   1 
ATOM   5499  H H    . PHE   A  1 361 ? 22.607 -27.192 -31.470 0.00 39.63  ? 387  PHE   A H    1 
ATOM   5500  H HA   . PHE   A  1 361 ? 21.202 -25.537 -29.430 0.00 38.35  ? 387  PHE   A HA   1 
ATOM   5501  H HB2  . PHE   A  1 361 ? 22.272 -25.041 -32.199 0.00 37.06  ? 387  PHE   A HB2  1 
ATOM   5502  H HB3  . PHE   A  1 361 ? 20.862 -24.134 -31.643 0.00 36.95  ? 387  PHE   A HB3  1 
ATOM   5503  H HD1  . PHE   A  1 361 ? 22.989 -24.672 -28.831 0.00 37.67  ? 387  PHE   A HD1  1 
ATOM   5504  H HD2  . PHE   A  1 361 ? 22.554 -22.296 -32.356 0.00 36.12  ? 387  PHE   A HD2  1 
ATOM   5505  H HE1  . PHE   A  1 361 ? 24.353 -22.942 -27.842 0.00 37.26  ? 387  PHE   A HE1  1 
ATOM   5506  H HE2  . PHE   A  1 361 ? 23.955 -20.570 -31.326 0.00 35.68  ? 387  PHE   A HE2  1 
ATOM   5507  H HZ   . PHE   A  1 361 ? 24.854 -20.898 -29.074 0.00 35.66  ? 387  PHE   A HZ   1 
ATOM   5508  N N    . GLN   A  1 362 ? 19.707 -27.721 -30.767 1.00 30.35  ? 388  GLN   A N    1 
ATOM   5509  C CA   . GLN   A  1 362 ? 18.381 -28.287 -31.060 1.00 30.91  ? 388  GLN   A CA   1 
ATOM   5510  C C    . GLN   A  1 362 ? 17.283 -27.712 -30.147 1.00 30.08  ? 388  GLN   A C    1 
ATOM   5511  O O    . GLN   A  1 362 ? 16.199 -27.428 -30.653 1.00 30.41  ? 388  GLN   A O    1 
ATOM   5512  C CB   . GLN   A  1 362 ? 18.365 -29.823 -30.958 1.00 34.07  ? 388  GLN   A CB   1 
ATOM   5513  C CG   . GLN   A  1 362 ? 19.268 -30.502 -31.960 1.00 41.71  ? 388  GLN   A CG   1 
ATOM   5514  C CD   . GLN   A  1 362 ? 18.728 -30.490 -33.366 1.00 50.07  ? 388  GLN   A CD   1 
ATOM   5515  O OE1  . GLN   A  1 362 ? 17.589 -30.900 -33.626 1.00 52.96  ? 388  GLN   A OE1  1 
ATOM   5516  N NE2  . GLN   A  1 362 ? 19.539 -30.034 -34.312 1.00 51.53  ? 388  GLN   A NE2  1 
ATOM   5517  H H    . GLN   A  1 362 ? 20.392 -28.413 -30.482 0.00 39.65  ? 388  GLN   A H    1 
ATOM   5518  H HA   . GLN   A  1 362 ? 18.133 -28.024 -32.087 0.00 40.77  ? 388  GLN   A HA   1 
ATOM   5519  H HB2  . GLN   A  1 362 ? 18.694 -30.139 -29.970 0.00 45.34  ? 388  GLN   A HB2  1 
ATOM   5520  H HB3  . GLN   A  1 362 ? 17.348 -30.172 -31.126 0.00 45.77  ? 388  GLN   A HB3  1 
ATOM   5521  H HG2  . GLN   A  1 362 ? 20.209 -29.957 -31.953 0.00 54.17  ? 388  GLN   A HG2  1 
ATOM   5522  H HG3  . GLN   A  1 362 ? 19.427 -31.537 -31.662 0.00 55.16  ? 388  GLN   A HG3  1 
ATOM   5523  H HE21 . GLN   A  1 362 ? 20.477 -29.715 -34.091 0.00 65.95  ? 388  GLN   A HE21 1 
ATOM   5524  H HE22 . GLN   A  1 362 ? 19.217 -30.007 -35.274 0.00 66.53  ? 388  GLN   A HE22 1 
ATOM   5525  N N    . PRO   A  1 363 ? 17.514 -27.504 -28.827 1.00 29.06  ? 389  PRO   A N    1 
ATOM   5526  C CA   . PRO   A  1 363 ? 16.454 -26.927 -27.985 1.00 28.40  ? 389  PRO   A CA   1 
ATOM   5527  C C    . PRO   A  1 363 ? 15.946 -25.542 -28.414 1.00 28.34  ? 389  PRO   A C    1 
ATOM   5528  O O    . PRO   A  1 363 ? 14.813 -25.209 -28.103 1.00 28.61  ? 389  PRO   A O    1 
ATOM   5529  C CB   . PRO   A  1 363 ? 17.113 -26.859 -26.602 1.00 28.98  ? 389  PRO   A CB   1 
ATOM   5530  C CG   . PRO   A  1 363 ? 18.202 -27.890 -26.640 1.00 29.62  ? 389  PRO   A CG   1 
ATOM   5531  C CD   . PRO   A  1 363 ? 18.733 -27.759 -28.029 1.00 28.40  ? 389  PRO   A CD   1 
ATOM   5532  H HA   . PRO   A  1 363 ? 15.609 -27.612 -27.937 0.00 38.05  ? 389  PRO   A HA   1 
ATOM   5533  H HB2  . PRO   A  1 363 ? 17.532 -25.866 -26.448 0.00 37.43  ? 389  PRO   A HB2  1 
ATOM   5534  H HB3  . PRO   A  1 363 ? 16.375 -27.088 -25.836 0.00 38.27  ? 389  PRO   A HB3  1 
ATOM   5535  H HG2  . PRO   A  1 363 ? 18.968 -27.662 -25.902 0.00 38.64  ? 389  PRO   A HG2  1 
ATOM   5536  H HG3  . PRO   A  1 363 ? 17.787 -28.884 -26.485 0.00 39.50  ? 389  PRO   A HG3  1 
ATOM   5537  H HD2  . PRO   A  1 363 ? 19.410 -26.909 -28.092 0.00 36.76  ? 389  PRO   A HD2  1 
ATOM   5538  H HD3  . PRO   A  1 363 ? 19.229 -28.682 -28.323 0.00 37.63  ? 389  PRO   A HD3  1 
ATOM   5539  N N    . LEU   A  1 364 ? 16.743 -24.755 -29.139 1.00 28.05  ? 390  LEU   A N    1 
ATOM   5540  C CA   . LEU   A  1 364 ? 16.350 -23.411 -29.584 1.00 28.63  ? 390  LEU   A CA   1 
ATOM   5541  C C    . LEU   A  1 364 ? 15.672 -23.355 -30.969 1.00 29.09  ? 390  LEU   A C    1 
ATOM   5542  O O    . LEU   A  1 364 ? 15.145 -22.299 -31.337 1.00 29.32  ? 390  LEU   A O    1 
ATOM   5543  C CB   . LEU   A  1 364 ? 17.622 -22.551 -29.685 1.00 28.59  ? 390  LEU   A CB   1 
ATOM   5544  C CG   . LEU   A  1 364 ? 18.539 -22.482 -28.460 1.00 29.50  ? 390  LEU   A CG   1 
ATOM   5545  C CD1  . LEU   A  1 364 ? 19.890 -21.882 -28.834 1.00 29.27  ? 390  LEU   A CD1  1 
ATOM   5546  C CD2  . LEU   A  1 364 ? 17.900 -21.689 -27.349 1.00 29.80  ? 390  LEU   A CD2  1 
ATOM   5547  H H    . LEU   A  1 364 ? 17.677 -25.009 -29.444 0.00 35.97  ? 390  LEU   A H    1 
ATOM   5548  H HA   . LEU   A  1 364 ? 15.675 -22.951 -28.865 0.00 36.40  ? 390  LEU   A HA   1 
ATOM   5549  H HB2  . LEU   A  1 364 ? 18.220 -22.934 -30.510 0.00 35.68  ? 390  LEU   A HB2  1 
ATOM   5550  H HB3  . LEU   A  1 364 ? 17.320 -21.529 -29.912 0.00 35.39  ? 390  LEU   A HB3  1 
ATOM   5551  H HG   . LEU   A  1 364 ? 18.726 -23.487 -28.084 0.00 36.79  ? 390  LEU   A HG   1 
ATOM   5552  H HD11 . LEU   A  1 364 ? 20.507 -21.820 -27.938 0.00 35.47  ? 390  LEU   A HD11 1 
ATOM   5553  H HD12 . LEU   A  1 364 ? 20.372 -22.524 -29.570 0.00 35.79  ? 390  LEU   A HD12 1 
ATOM   5554  H HD13 . LEU   A  1 364 ? 19.736 -20.888 -29.252 0.00 35.34  ? 390  LEU   A HD13 1 
ATOM   5555  H HD21 . LEU   A  1 364 ? 18.531 -21.755 -26.464 0.00 36.56  ? 390  LEU   A HD21 1 
ATOM   5556  H HD22 . LEU   A  1 364 ? 17.820 -20.650 -27.667 0.00 36.35  ? 390  LEU   A HD22 1 
ATOM   5557  H HD23 . LEU   A  1 364 ? 16.910 -22.086 -27.135 0.00 37.10  ? 390  LEU   A HD23 1 
ATOM   5558  N N    . MET   A  1 365 ? 15.755 -24.437 -31.764 1.00 28.81  ? 391  MET   A N    1 
ATOM   5559  C CA   . MET   A  1 365 ? 15.364 -24.410 -33.172 1.00 29.69  ? 391  MET   A CA   1 
ATOM   5560  C C    . MET   A  1 365 ? 13.879 -24.303 -33.475 1.00 30.23  ? 391  MET   A C    1 
ATOM   5561  O O    . MET   A  1 365 ? 13.540 -23.944 -34.606 1.00 30.63  ? 391  MET   A O    1 
ATOM   5562  C CB   . MET   A  1 365 ? 15.954 -25.629 -33.901 1.00 30.69  ? 391  MET   A CB   1 
ATOM   5563  C CG   . MET   A  1 365 ? 17.456 -25.513 -34.097 1.00 33.24  ? 391  MET   A CG   1 
ATOM   5564  S SD   . MET   A  1 365 ? 18.253 -27.024 -34.665 1.00 39.56  ? 391  MET   A SD   1 
ATOM   5565  C CE   . MET   A  1 365 ? 19.955 -26.495 -34.594 1.00 34.97  ? 391  MET   A CE   1 
ATOM   5566  H H    . MET   A  1 365 ? 16.097 -25.343 -31.461 0.00 37.57  ? 391  MET   A H    1 
ATOM   5567  H HA   . MET   A  1 365 ? 15.810 -23.514 -33.604 0.00 38.15  ? 391  MET   A HA   1 
ATOM   5568  H HB2  . MET   A  1 365 ? 15.749 -26.537 -33.334 0.00 40.60  ? 391  MET   A HB2  1 
ATOM   5569  H HB3  . MET   A  1 365 ? 15.501 -25.706 -34.888 0.00 40.47  ? 391  MET   A HB3  1 
ATOM   5570  H HG2  . MET   A  1 365 ? 17.651 -24.738 -34.837 0.00 42.47  ? 391  MET   A HG2  1 
ATOM   5571  H HG3  . MET   A  1 365 ? 17.913 -25.236 -33.148 0.00 42.46  ? 391  MET   A HG3  1 
ATOM   5572  H HE1  . MET   A  1 365 ? 20.590 -27.377 -34.523 0.00 44.95  ? 391  MET   A HE1  1 
ATOM   5573  H HE2  . MET   A  1 365 ? 20.194 -25.935 -35.497 0.00 44.49  ? 391  MET   A HE2  1 
ATOM   5574  H HE3  . MET   A  1 365 ? 20.102 -25.869 -33.715 0.00 44.30  ? 391  MET   A HE3  1 
ATOM   5575  N N    . GLN   A  1 366 ? 13.008 -24.577 -32.514 1.00 30.28  ? 392  GLN   A N    1 
ATOM   5576  C CA   . GLN   A  1 366 ? 11.570 -24.453 -32.729 1.00 31.95  ? 392  GLN   A CA   1 
ATOM   5577  C C    . GLN   A  1 366 ? 11.003 -23.172 -32.063 1.00 31.27  ? 392  GLN   A C    1 
ATOM   5578  O O    . GLN   A  1 366 ? 9.789  -23.000 -32.083 1.00 31.75  ? 392  GLN   A O    1 
ATOM   5579  C CB   . GLN   A  1 366 ? 10.861 -25.723 -32.203 1.00 35.38  ? 392  GLN   A CB   1 
ATOM   5580  C CG   . GLN   A  1 366 ? 9.619  -26.156 -32.986 1.00 43.92  ? 392  GLN   A CG   1 
ATOM   5581  C CD   . GLN   A  1 366 ? 8.993  -27.434 -32.450 1.00 53.54  ? 392  GLN   A CD   1 
ATOM   5582  O OE1  . GLN   A  1 366 ? 9.596  -28.186 -31.669 1.00 56.74  ? 392  GLN   A OE1  1 
ATOM   5583  N NE2  . GLN   A  1 366 ? 7.759  -27.712 -32.866 1.00 55.19  ? 392  GLN   A NE2  1 
ATOM   5584  H H    . GLN   A  1 366 ? 13.250 -24.891 -31.580 0.00 40.08  ? 392  GLN   A H    1 
ATOM   5585  H HA   . GLN   A  1 366 ? 11.371 -24.359 -33.796 0.00 42.76  ? 392  GLN   A HA   1 
ATOM   5586  H HB2  . GLN   A  1 366 ? 11.578 -26.542 -32.235 0.00 47.54  ? 392  GLN   A HB2  1 
ATOM   5587  H HB3  . GLN   A  1 366 ? 10.556 -25.547 -31.173 0.00 47.42  ? 392  GLN   A HB3  1 
ATOM   5588  H HG2  . GLN   A  1 366 ? 8.871  -25.367 -32.929 0.00 58.45  ? 392  GLN   A HG2  1 
ATOM   5589  H HG3  . GLN   A  1 366 ? 9.898  -26.329 -34.024 0.00 58.53  ? 392  GLN   A HG3  1 
ATOM   5590  H HE21 . GLN   A  1 366 ? 7.284  -27.083 -33.504 0.00 73.43  ? 392  GLN   A HE21 1 
ATOM   5591  H HE22 . GLN   A  1 366 ? 7.293  -28.552 -32.538 0.00 73.97  ? 392  GLN   A HE22 1 
ATOM   5592  N N    . LEU   A  1 367 ? 11.859 -22.274 -31.494 1.00 29.59  ? 393  LEU   A N    1 
ATOM   5593  C CA   . LEU   A  1 367 ? 11.386 -21.040 -30.866 1.00 28.46  ? 393  LEU   A CA   1 
ATOM   5594  C C    . LEU   A  1 367 ? 11.034 -20.097 -32.012 1.00 28.20  ? 393  LEU   A C    1 
ATOM   5595  O O    . LEU   A  1 367 ? 11.897 -19.794 -32.834 1.00 28.52  ? 393  LEU   A O    1 
ATOM   5596  C CB   . LEU   A  1 367 ? 12.445 -20.465 -29.912 1.00 27.59  ? 393  LEU   A CB   1 
ATOM   5597  C CG   . LEU   A  1 367 ? 12.836 -21.391 -28.735 1.00 28.44  ? 393  LEU   A CG   1 
ATOM   5598  C CD1  . LEU   A  1 367 ? 13.896 -20.762 -27.870 1.00 28.63  ? 393  LEU   A CD1  1 
ATOM   5599  C CD2  . LEU   A  1 367 ? 11.627 -21.761 -27.872 1.00 29.38  ? 393  LEU   A CD2  1 
ATOM   5600  H H    . LEU   A  1 367 ? 12.869 -22.371 -31.454 0.00 38.39  ? 393  LEU   A H    1 
ATOM   5601  H HA   . LEU   A  1 367 ? 10.497 -21.263 -30.281 0.00 37.46  ? 393  LEU   A HA   1 
ATOM   5602  H HB2  . LEU   A  1 367 ? 13.351 -20.257 -30.480 0.00 35.03  ? 393  LEU   A HB2  1 
ATOM   5603  H HB3  . LEU   A  1 367 ? 12.062 -19.538 -29.488 0.00 35.22  ? 393  LEU   A HB3  1 
ATOM   5604  H HG   . LEU   A  1 367 ? 13.247 -22.316 -29.135 0.00 36.72  ? 393  LEU   A HG   1 
ATOM   5605  H HD11 . LEU   A  1 367 ? 14.183 -21.460 -27.085 0.00 36.27  ? 393  LEU   A HD11 1 
ATOM   5606  H HD12 . LEU   A  1 367 ? 14.759 -20.528 -28.491 0.00 35.80  ? 393  LEU   A HD12 1 
ATOM   5607  H HD13 . LEU   A  1 367 ? 13.497 -19.850 -27.429 0.00 35.97  ? 393  LEU   A HD13 1 
ATOM   5608  H HD21 . LEU   A  1 367 ? 11.974 -22.172 -26.925 0.00 38.18  ? 393  LEU   A HD21 1 
ATOM   5609  H HD22 . LEU   A  1 367 ? 11.032 -20.865 -27.696 0.00 38.10  ? 393  LEU   A HD22 1 
ATOM   5610  H HD23 . LEU   A  1 367 ? 11.033 -22.508 -28.394 0.00 38.69  ? 393  LEU   A HD23 1 
ATOM   5611  N N    . PRO   A  1 368 ? 9.740  -19.750 -32.180 1.00 27.69  ? 394  PRO   A N    1 
ATOM   5612  C CA   . PRO   A  1 368 ? 9.338  -19.018 -33.388 1.00 27.16  ? 394  PRO   A CA   1 
ATOM   5613  C C    . PRO   A  1 368 ? 9.838  -17.591 -33.532 1.00 26.05  ? 394  PRO   A C    1 
ATOM   5614  O O    . PRO   A  1 368 ? 9.992  -17.149 -34.670 1.00 26.31  ? 394  PRO   A O    1 
ATOM   5615  C CB   . PRO   A  1 368 ? 7.805  -19.072 -33.350 1.00 28.02  ? 394  PRO   A CB   1 
ATOM   5616  C CG   . PRO   A  1 368 ? 7.461  -19.269 -31.927 1.00 28.76  ? 394  PRO   A CG   1 
ATOM   5617  C CD   . PRO   A  1 368 ? 8.572  -20.073 -31.329 1.00 27.18  ? 394  PRO   A CD   1 
ATOM   5618  H HA   . PRO   A  1 368 ? 9.667  -19.577 -34.263 0.00 36.03  ? 394  PRO   A HA   1 
ATOM   5619  H HB2  . PRO   A  1 368 ? 7.393  -18.132 -33.716 0.00 37.56  ? 394  PRO   A HB2  1 
ATOM   5620  H HB3  . PRO   A  1 368 ? 7.451  -19.910 -33.948 0.00 38.09  ? 394  PRO   A HB3  1 
ATOM   5621  H HG2  . PRO   A  1 368 ? 7.391  -18.297 -31.442 0.00 38.28  ? 394  PRO   A HG2  1 
ATOM   5622  H HG3  . PRO   A  1 368 ? 6.517  -19.806 -31.853 0.00 39.16  ? 394  PRO   A HG3  1 
ATOM   5623  H HD2  . PRO   A  1 368 ? 8.748  -19.747 -30.305 0.00 36.13  ? 394  PRO   A HD2  1 
ATOM   5624  H HD3  . PRO   A  1 368 ? 8.347  -21.137 -31.380 0.00 36.84  ? 394  PRO   A HD3  1 
ATOM   5625  N N    . ASN   A  1 369 ? 10.108 -16.875 -32.436 1.00 24.83  ? 395  ASN   A N    1 
ATOM   5626  C CA   . ASN   A  1 369 ? 10.560 -15.482 -32.542 1.00 24.23  ? 395  ASN   A CA   1 
ATOM   5627  C C    . ASN   A  1 369 ? 12.014 -15.253 -32.187 1.00 22.66  ? 395  ASN   A C    1 
ATOM   5628  O O    . ASN   A  1 369 ? 12.408 -14.099 -32.083 1.00 21.58  ? 395  ASN   A O    1 
ATOM   5629  C CB   . ASN   A  1 369 ? 9.643  -14.592 -31.697 1.00 25.57  ? 395  ASN   A CB   1 
ATOM   5630  C CG   . ASN   A  1 369 ? 8.246  -14.663 -32.140 1.00 30.11  ? 395  ASN   A CG   1 
ATOM   5631  O OD1  . ASN   A  1 369 ? 7.984  -14.823 -33.350 1.00 31.32  ? 395  ASN   A OD1  1 
ATOM   5632  N ND2  . ASN   A  1 369 ? 7.261  -14.382 -31.341 1.00 32.37  ? 395  ASN   A ND2  1 
ATOM   5633  H H    . ASN   A  1 369 ? 10.021 -17.207 -31.481 0.00 32.14  ? 395  ASN   A H    1 
ATOM   5634  H HA   . ASN   A  1 369 ? 10.466 -15.135 -33.569 0.00 30.90  ? 395  ASN   A HA   1 
ATOM   5635  H HB2  . ASN   A  1 369 ? 9.688  -14.916 -30.658 0.00 32.53  ? 395  ASN   A HB2  1 
ATOM   5636  H HB3  . ASN   A  1 369 ? 9.955  -13.552 -31.781 0.00 32.22  ? 395  ASN   A HB3  1 
ATOM   5637  H HD21 . ASN   A  1 369 ? 6.750  -15.206 -31.590 0.00 42.14  ? 395  ASN   A HD21 1 
ATOM   5638  H HD22 . ASN   A  1 369 ? 7.370  -13.986 -30.414 0.00 41.51  ? 395  ASN   A HD22 1 
ATOM   5639  N N    . LEU   A  1 370 ? 12.817 -16.323 -32.024 1.00 22.26  ? 396  LEU   A N    1 
ATOM   5640  C CA   . LEU   A  1 370 ? 14.229 -16.166 -31.705 1.00 22.46  ? 396  LEU   A CA   1 
ATOM   5641  C C    . LEU   A  1 370 ? 14.939 -15.604 -32.940 1.00 23.18  ? 396  LEU   A C    1 
ATOM   5642  O O    . LEU   A  1 370 ? 15.196 -16.335 -33.893 1.00 23.78  ? 396  LEU   A O    1 
ATOM   5643  C CB   . LEU   A  1 370 ? 14.830 -17.516 -31.268 1.00 22.42  ? 396  LEU   A CB   1 
ATOM   5644  C CG   . LEU   A  1 370 ? 16.326 -17.510 -30.865 1.00 24.08  ? 396  LEU   A CG   1 
ATOM   5645  C CD1  . LEU   A  1 370 ? 16.623 -16.455 -29.802 1.00 24.17  ? 396  LEU   A CD1  1 
ATOM   5646  C CD2  . LEU   A  1 370 ? 16.736 -18.879 -30.318 1.00 24.58  ? 396  LEU   A CD2  1 
ATOM   5647  H H    . LEU   A  1 370 ? 12.531 -17.293 -32.107 0.00 28.15  ? 396  LEU   A H    1 
ATOM   5648  H HA   . LEU   A  1 370 ? 14.328 -15.460 -30.882 0.00 27.19  ? 396  LEU   A HA   1 
ATOM   5649  H HB2  . LEU   A  1 370 ? 14.269 -17.874 -30.405 0.00 27.78  ? 396  LEU   A HB2  1 
ATOM   5650  H HB3  . LEU   A  1 370 ? 14.719 -18.228 -32.085 0.00 27.83  ? 396  LEU   A HB3  1 
ATOM   5651  H HG   . LEU   A  1 370 ? 16.940 -17.299 -31.738 0.00 28.83  ? 396  LEU   A HG   1 
ATOM   5652  H HD11 . LEU   A  1 370 ? 17.623 -16.629 -29.407 0.00 28.45  ? 396  LEU   A HD11 1 
ATOM   5653  H HD12 . LEU   A  1 370 ? 16.579 -15.467 -30.258 0.00 28.49  ? 396  LEU   A HD12 1 
ATOM   5654  H HD13 . LEU   A  1 370 ? 15.887 -16.536 -29.003 0.00 28.93  ? 396  LEU   A HD13 1 
ATOM   5655  H HD21 . LEU   A  1 370 ? 17.822 -18.917 -30.243 0.00 29.59  ? 396  LEU   A HD21 1 
ATOM   5656  H HD22 . LEU   A  1 370 ? 16.296 -19.008 -29.330 0.00 30.01  ? 396  LEU   A HD22 1 
ATOM   5657  H HD23 . LEU   A  1 370 ? 16.376 -19.656 -30.992 0.00 30.28  ? 396  LEU   A HD23 1 
ATOM   5658  N N    . SER   A  1 371 ? 15.168 -14.291 -32.954 1.00 23.18  ? 397  SER   A N    1 
ATOM   5659  C CA   . SER   A  1 371 ? 15.765 -13.616 -34.101 1.00 23.49  ? 397  SER   A CA   1 
ATOM   5660  C C    . SER   A  1 371 ? 17.231 -13.238 -33.894 1.00 22.36  ? 397  SER   A C    1 
ATOM   5661  O O    . SER   A  1 371 ? 17.923 -13.012 -34.885 1.00 22.44  ? 397  SER   A O    1 
ATOM   5662  C CB   . SER   A  1 371 ? 14.942 -12.388 -34.488 1.00 26.86  ? 397  SER   A CB   1 
ATOM   5663  O OG   . SER   A  1 371 ? 15.016 -11.365 -33.507 1.00 30.84  ? 397  SER   A OG   1 
ATOM   5664  H H    . SER   A  1 371 ? 14.945 -13.666 -32.186 0.00 27.51  ? 397  SER   A H    1 
ATOM   5665  H HA   . SER   A  1 371 ? 15.716 -14.267 -34.970 0.00 27.99  ? 397  SER   A HA   1 
ATOM   5666  H HB2  . SER   A  1 371 ? 15.315 -11.998 -35.434 0.00 31.73  ? 397  SER   A HB2  1 
ATOM   5667  H HB3  . SER   A  1 371 ? 13.900 -12.686 -34.594 0.00 32.28  ? 397  SER   A HB3  1 
ATOM   5668  H HG   . SER   A  1 371 ? 15.134 -11.733 -32.592 0.00 36.28  ? 397  SER   A HG   1 
ATOM   5669  N N    . THR   A  1 372 ? 17.718 -13.155 -32.637 1.00 21.17  ? 398  THR   A N    1 
ATOM   5670  C CA   . THR   A  1 372 ? 19.106 -12.797 -32.367 1.00 21.32  ? 398  THR   A CA   1 
ATOM   5671  C C    . THR   A  1 372 ? 19.813 -13.868 -31.546 1.00 20.16  ? 398  THR   A C    1 
ATOM   5672  O O    . THR   A  1 372 ? 19.302 -14.274 -30.497 1.00 19.24  ? 398  THR   A O    1 
ATOM   5673  C CB   . THR   A  1 372 ? 19.179 -11.447 -31.619 1.00 23.79  ? 398  THR   A CB   1 
ATOM   5674  O OG1  . THR   A  1 372 ? 18.705 -10.421 -32.483 1.00 25.72  ? 398  THR   A OG1  1 
ATOM   5675  C CG2  . THR   A  1 372 ? 20.605 -11.091 -31.177 1.00 24.43  ? 398  THR   A CG2  1 
ATOM   5676  H H    . THR   A  1 372 ? 17.180 -13.322 -31.792 0.00 24.28  ? 398  THR   A H    1 
ATOM   5677  H HA   . THR   A  1 372 ? 19.657 -12.683 -33.300 0.00 23.71  ? 398  THR   A HA   1 
ATOM   5678  H HB   . THR   A  1 372 ? 18.548 -11.494 -30.732 0.00 26.62  ? 398  THR   A HB   1 
ATOM   5679  H HG1  . THR   A  1 372 ? 18.559 -9.582  -31.973 0.00 28.67  ? 398  THR   A HG1  1 
ATOM   5680  H HG21 . THR   A  1 372 ? 20.680 -10.019 -30.994 0.00 26.58  ? 398  THR   A HG21 1 
ATOM   5681  H HG22 . THR   A  1 372 ? 20.854 -11.608 -30.251 0.00 26.79  ? 398  THR   A HG22 1 
ATOM   5682  H HG23 . THR   A  1 372 ? 21.319 -11.370 -31.950 0.00 26.69  ? 398  THR   A HG23 1 
ATOM   5683  N N    . ILE   A  1 373 ? 21.005 -14.297 -32.013 1.00 19.70  ? 399  ILE   A N    1 
ATOM   5684  C CA   . ILE   A  1 373 ? 21.867 -15.242 -31.295 1.00 20.36  ? 399  ILE   A CA   1 
ATOM   5685  C C    . ILE   A  1 373 ? 23.219 -14.569 -31.221 1.00 19.54  ? 399  ILE   A C    1 
ATOM   5686  O O    . ILE   A  1 373 ? 23.797 -14.216 -32.259 1.00 19.36  ? 399  ILE   A O    1 
ATOM   5687  C CB   . ILE   A  1 373 ? 21.953 -16.673 -31.928 1.00 22.27  ? 399  ILE   A CB   1 
ATOM   5688  C CG1  . ILE   A  1 373 ? 22.965 -17.565 -31.161 1.00 24.14  ? 399  ILE   A CG1  1 
ATOM   5689  C CG2  . ILE   A  1 373 ? 22.325 -16.639 -33.413 1.00 23.17  ? 399  ILE   A CG2  1 
ATOM   5690  C CD1  . ILE   A  1 373 ? 22.623 -17.796 -29.723 1.00 26.90  ? 399  ILE   A CD1  1 
ATOM   5691  H H    . ILE   A  1 373 ? 21.409 -13.996 -32.895 0.00 21.59  ? 399  ILE   A H    1 
ATOM   5692  H HA   . ILE   A  1 373 ? 21.491 -15.358 -30.280 0.00 22.59  ? 399  ILE   A HA   1 
ATOM   5693  H HB   . ILE   A  1 373 ? 20.970 -17.134 -31.842 0.00 25.54  ? 399  ILE   A HB   1 
ATOM   5694  H HG12 . ILE   A  1 373 ? 22.976 -18.542 -31.644 0.00 27.78  ? 399  ILE   A HG12 1 
ATOM   5695  H HG13 . ILE   A  1 373 ? 23.964 -17.135 -31.214 0.00 27.15  ? 399  ILE   A HG13 1 
ATOM   5696  H HG21 . ILE   A  1 373 ? 22.276 -17.655 -33.803 0.00 26.61  ? 399  ILE   A HG21 1 
ATOM   5697  H HG22 . ILE   A  1 373 ? 21.628 -16.001 -33.953 0.00 26.25  ? 399  ILE   A HG22 1 
ATOM   5698  H HG23 . ILE   A  1 373 ? 23.341 -16.261 -33.515 0.00 25.96  ? 399  ILE   A HG23 1 
ATOM   5699  H HD11 . ILE   A  1 373 ? 23.225 -18.621 -29.344 0.00 30.98  ? 399  ILE   A HD11 1 
ATOM   5700  H HD12 . ILE   A  1 373 ? 22.840 -16.893 -29.154 0.00 30.55  ? 399  ILE   A HD12 1 
ATOM   5701  H HD13 . ILE   A  1 373 ? 21.564 -18.041 -29.644 0.00 31.16  ? 399  ILE   A HD13 1 
ATOM   5702  N N    . ASN   A  1 374 ? 23.705 -14.342 -29.994 1.00 18.56  ? 400  ASN   A N    1 
ATOM   5703  C CA   . ASN   A  1 374 ? 24.969 -13.654 -29.808 1.00 18.81  ? 400  ASN   A CA   1 
ATOM   5704  C C    . ASN   A  1 374 ? 25.979 -14.592 -29.136 1.00 18.53  ? 400  ASN   A C    1 
ATOM   5705  O O    . ASN   A  1 374 ? 25.819 -14.956 -27.969 1.00 17.79  ? 400  ASN   A O    1 
ATOM   5706  C CB   . ASN   A  1 374 ? 24.713 -12.335 -29.059 1.00 19.32  ? 400  ASN   A CB   1 
ATOM   5707  C CG   . ASN   A  1 374 ? 25.915 -11.630 -28.506 1.00 22.87  ? 400  ASN   A CG   1 
ATOM   5708  O OD1  . ASN   A  1 374 ? 27.051 -11.886 -28.899 1.00 23.66  ? 400  ASN   A OD1  1 
ATOM   5709  N ND2  . ASN   A  1 374 ? 25.680 -10.685 -27.594 1.00 23.72  ? 400  ASN   A ND2  1 
ATOM   5710  H H    . ASN   A  1 374 ? 23.259 -14.619 -29.126 0.00 19.87  ? 400  ASN   A H    1 
ATOM   5711  H HA   . ASN   A  1 374 ? 25.390 -13.380 -30.771 0.00 19.51  ? 400  ASN   A HA   1 
ATOM   5712  H HB2  . ASN   A  1 374 ? 24.275 -11.647 -29.781 0.00 19.94  ? 400  ASN   A HB2  1 
ATOM   5713  H HB3  . ASN   A  1 374 ? 23.990 -12.490 -28.263 0.00 20.17  ? 400  ASN   A HB3  1 
ATOM   5714  H HD21 . ASN   A  1 374 ? 26.451 -10.171 -27.181 0.00 24.62  ? 400  ASN   A HD21 1 
ATOM   5715  H HD22 . ASN   A  1 374 ? 24.727 -10.472 -27.317 0.00 24.94  ? 400  ASN   A HD22 1 
ATOM   5716  N N    . LEU   A  1 375 ? 26.986 -15.030 -29.919 1.00 18.23  ? 401  LEU   A N    1 
ATOM   5717  C CA   . LEU   A  1 375 ? 28.055 -15.889 -29.432 1.00 18.23  ? 401  LEU   A CA   1 
ATOM   5718  C C    . LEU   A  1 375 ? 29.415 -15.198 -29.562 1.00 18.25  ? 401  LEU   A C    1 
ATOM   5719  O O    . LEU   A  1 375 ? 30.411 -15.872 -29.782 1.00 18.47  ? 401  LEU   A O    1 
ATOM   5720  C CB   . LEU   A  1 375 ? 28.058 -17.230 -30.189 1.00 18.27  ? 401  LEU   A CB   1 
ATOM   5721  C CG   . LEU   A  1 375 ? 26.827 -18.118 -30.001 1.00 20.65  ? 401  LEU   A CG   1 
ATOM   5722  C CD1  . LEU   A  1 375 ? 26.725 -19.145 -31.149 1.00 21.92  ? 401  LEU   A CD1  1 
ATOM   5723  C CD2  . LEU   A  1 375 ? 26.889 -18.846 -28.660 1.00 21.01  ? 401  LEU   A CD2  1 
ATOM   5724  H H    . LEU   A  1 375 ? 27.084 -14.808 -30.905 0.00 18.91  ? 401  LEU   A H    1 
ATOM   5725  H HA   . LEU   A  1 375 ? 27.922 -16.085 -28.370 0.00 19.15  ? 401  LEU   A HA   1 
ATOM   5726  H HB2  . LEU   A  1 375 ? 28.169 -17.031 -31.253 0.00 19.44  ? 401  LEU   A HB2  1 
ATOM   5727  H HB3  . LEU   A  1 375 ? 28.903 -17.825 -29.845 0.00 19.59  ? 401  LEU   A HB3  1 
ATOM   5728  H HG   . LEU   A  1 375 ? 25.924 -17.510 -30.013 0.00 22.72  ? 401  LEU   A HG   1 
ATOM   5729  H HD11 . LEU   A  1 375 ? 25.950 -19.871 -30.909 0.00 25.02  ? 401  LEU   A HD11 1 
ATOM   5730  H HD12 . LEU   A  1 375 ? 26.476 -18.622 -32.071 0.00 24.57  ? 401  LEU   A HD12 1 
ATOM   5731  H HD13 . LEU   A  1 375 ? 27.687 -19.645 -31.255 0.00 24.72  ? 401  LEU   A HD13 1 
ATOM   5732  H HD21 . LEU   A  1 375 ? 25.881 -19.147 -28.382 0.00 23.67  ? 401  LEU   A HD21 1 
ATOM   5733  H HD22 . LEU   A  1 375 ? 27.513 -19.731 -28.775 0.00 23.66  ? 401  LEU   A HD22 1 
ATOM   5734  H HD23 . LEU   A  1 375 ? 27.306 -18.205 -27.886 0.00 23.19  ? 401  LEU   A HD23 1 
ATOM   5735  N N    . GLY   A  1 376 ? 29.465 -13.891 -29.323 1.00 18.72  ? 402  GLY   A N    1 
ATOM   5736  C CA   . GLY   A  1 376 ? 30.731 -13.170 -29.353 1.00 18.96  ? 402  GLY   A CA   1 
ATOM   5737  C C    . GLY   A  1 376 ? 31.647 -13.612 -28.223 1.00 18.26  ? 402  GLY   A C    1 
ATOM   5738  O O    . GLY   A  1 376 ? 31.170 -14.016 -27.164 1.00 17.85  ? 402  GLY   A O    1 
ATOM   5739  H H    . GLY   A  1 376 ? 28.669 -13.303 -29.096 0.00 18.93  ? 402  GLY   A H    1 
ATOM   5740  H HA2  . GLY   A  1 376 ? 31.229 -13.344 -30.306 0.00 18.99  ? 402  GLY   A HA2  1 
ATOM   5741  H HA3  . GLY   A  1 376 ? 30.544 -12.102 -29.250 0.00 18.77  ? 402  GLY   A HA3  1 
ATOM   5742  N N    . ILE   A  1 377 ? 32.968 -13.564 -28.445 1.00 17.20  ? 403  ILE   A N    1 
ATOM   5743  C CA   . ILE   A  1 377 ? 33.982 -13.805 -27.406 1.00 17.84  ? 403  ILE   A CA   1 
ATOM   5744  C C    . ILE   A  1 377 ? 33.827 -15.169 -26.703 1.00 17.86  ? 403  ILE   A C    1 
ATOM   5745  O O    . ILE   A  1 377 ? 33.726 -15.245 -25.477 1.00 18.79  ? 403  ILE   A O    1 
ATOM   5746  C CB   . ILE   A  1 377 ? 34.037 -12.619 -26.366 1.00 19.00  ? 403  ILE   A CB   1 
ATOM   5747  C CG1  . ILE   A  1 377 ? 33.867 -11.219 -27.047 1.00 19.94  ? 403  ILE   A CG1  1 
ATOM   5748  C CG2  . ILE   A  1 377 ? 35.356 -12.653 -25.554 1.00 19.63  ? 403  ILE   A CG2  1 
ATOM   5749  C CD1  . ILE   A  1 377 ? 33.630 -10.052 -26.049 1.00 21.66  ? 403  ILE   A CD1  1 
ATOM   5750  H H    . ILE   A  1 377 ? 33.376 -13.356 -29.351 0.00 16.78  ? 403  ILE   A H    1 
ATOM   5751  H HA   . ILE   A  1 377 ? 34.945 -13.835 -27.917 0.00 17.69  ? 403  ILE   A HA   1 
ATOM   5752  H HB   . ILE   A  1 377 ? 33.209 -12.737 -25.668 0.00 18.98  ? 403  ILE   A HB   1 
ATOM   5753  H HG12 . ILE   A  1 377 ? 34.768 -10.995 -27.616 0.00 19.59  ? 403  ILE   A HG12 1 
ATOM   5754  H HG13 . ILE   A  1 377 ? 33.004 -11.229 -27.712 0.00 19.67  ? 403  ILE   A HG13 1 
ATOM   5755  H HG21 . ILE   A  1 377 ? 35.321 -11.895 -24.772 0.00 19.61  ? 403  ILE   A HG21 1 
ATOM   5756  H HG22 . ILE   A  1 377 ? 35.483 -13.632 -25.094 0.00 19.98  ? 403  ILE   A HG22 1 
ATOM   5757  H HG23 . ILE   A  1 377 ? 36.187 -12.452 -26.228 0.00 19.62  ? 403  ILE   A HG23 1 
ATOM   5758  H HD11 . ILE   A  1 377 ? 33.314 -9.172  -26.608 0.00 21.40  ? 403  ILE   A HD11 1 
ATOM   5759  H HD12 . ILE   A  1 377 ? 32.857 -10.341 -25.338 0.00 21.71  ? 403  ILE   A HD12 1 
ATOM   5760  H HD13 . ILE   A  1 377 ? 34.559 -9.835  -25.523 0.00 21.57  ? 403  ILE   A HD13 1 
ATOM   5761  N N    . ASN   A  1 378 ? 33.816 -16.236 -27.485 1.00 17.49  ? 404  ASN   A N    1 
ATOM   5762  C CA   . ASN   A  1 378 ? 33.739 -17.598 -26.944 1.00 18.16  ? 404  ASN   A CA   1 
ATOM   5763  C C    . ASN   A  1 378 ? 34.946 -18.458 -27.328 1.00 18.59  ? 404  ASN   A C    1 
ATOM   5764  O O    . ASN   A  1 378 ? 34.978 -19.635 -26.965 1.00 18.54  ? 404  ASN   A O    1 
ATOM   5765  C CB   . ASN   A  1 378 ? 32.447 -18.274 -27.437 1.00 18.29  ? 404  ASN   A CB   1 
ATOM   5766  C CG   . ASN   A  1 378 ? 31.244 -17.924 -26.613 1.00 18.91  ? 404  ASN   A CG   1 
ATOM   5767  O OD1  . ASN   A  1 378 ? 31.202 -18.251 -25.443 1.00 19.65  ? 404  ASN   A OD1  1 
ATOM   5768  N ND2  . ASN   A  1 378 ? 30.245 -17.288 -27.189 1.00 17.87  ? 404  ASN   A ND2  1 
ATOM   5769  H H    . ASN   A  1 378 ? 33.853 -16.200 -28.498 0.00 17.91  ? 404  ASN   A H    1 
ATOM   5770  H HA   . ASN   A  1 378 ? 33.732 -17.575 -25.855 0.00 19.25  ? 404  ASN   A HA   1 
ATOM   5771  H HB2  . ASN   A  1 378 ? 32.270 -18.003 -28.477 0.00 19.46  ? 404  ASN   A HB2  1 
ATOM   5772  H HB3  . ASN   A  1 378 ? 32.550 -19.353 -27.334 0.00 19.94  ? 404  ASN   A HB3  1 
ATOM   5773  H HD21 . ASN   A  1 378 ? 29.423 -17.047 -26.644 0.00 18.89  ? 404  ASN   A HD21 1 
ATOM   5774  H HD22 . ASN   A  1 378 ? 30.284 -17.046 -28.173 0.00 18.77  ? 404  ASN   A HD22 1 
ATOM   5775  N N    . PHE   A  1 379 ? 35.946 -17.889 -28.045 1.00 18.49  ? 405  PHE   A N    1 
ATOM   5776  C CA   . PHE   A  1 379 ? 37.109 -18.623 -28.540 1.00 19.05  ? 405  PHE   A CA   1 
ATOM   5777  C C    . PHE   A  1 379 ? 36.678 -19.852 -29.364 1.00 19.41  ? 405  PHE   A C    1 
ATOM   5778  O O    . PHE   A  1 379 ? 37.320 -20.891 -29.304 1.00 19.45  ? 405  PHE   A O    1 
ATOM   5779  C CB   . PHE   A  1 379 ? 38.091 -18.952 -27.387 1.00 19.26  ? 405  PHE   A CB   1 
ATOM   5780  C CG   . PHE   A  1 379 ? 38.717 -17.696 -26.820 1.00 19.76  ? 405  PHE   A CG   1 
ATOM   5781  C CD1  . PHE   A  1 379 ? 39.796 -17.091 -27.456 1.00 19.57  ? 405  PHE   A CD1  1 
ATOM   5782  C CD2  . PHE   A  1 379 ? 38.165 -17.064 -25.713 1.00 20.27  ? 405  PHE   A CD2  1 
ATOM   5783  C CE1  . PHE   A  1 379 ? 40.292 -15.869 -27.011 1.00 19.73  ? 405  PHE   A CE1  1 
ATOM   5784  C CE2  . PHE   A  1 379 ? 38.691 -15.864 -25.246 1.00 20.61  ? 405  PHE   A CE2  1 
ATOM   5785  C CZ   . PHE   A  1 379 ? 39.753 -15.277 -25.896 1.00 19.90  ? 405  PHE   A CZ   1 
ATOM   5786  H H    . PHE   A  1 379 ? 35.986 -16.906 -28.297 0.00 19.32  ? 405  PHE   A H    1 
ATOM   5787  H HA   . PHE   A  1 379 ? 37.617 -17.954 -29.232 0.00 20.36  ? 405  PHE   A HA   1 
ATOM   5788  H HB2  . PHE   A  1 379 ? 37.560 -19.462 -26.585 0.00 21.24  ? 405  PHE   A HB2  1 
ATOM   5789  H HB3  . PHE   A  1 379 ? 38.902 -19.576 -27.759 0.00 21.30  ? 405  PHE   A HB3  1 
ATOM   5790  H HD1  . PHE   A  1 379 ? 40.220 -17.540 -28.337 0.00 21.05  ? 405  PHE   A HD1  1 
ATOM   5791  H HD2  . PHE   A  1 379 ? 37.316 -17.503 -25.215 0.00 21.89  ? 405  PHE   A HD2  1 
ATOM   5792  H HE1  . PHE   A  1 379 ? 41.148 -15.428 -27.493 0.00 20.74  ? 405  PHE   A HE1  1 
ATOM   5793  H HE2  . PHE   A  1 379 ? 38.262 -15.392 -24.377 0.00 21.80  ? 405  PHE   A HE2  1 
ATOM   5794  H HZ   . PHE   A  1 379 ? 40.170 -14.358 -25.520 0.00 20.70  ? 405  PHE   A HZ   1 
ATOM   5795  N N    . ILE   A  1 380 ? 35.551 -19.731 -30.113 1.00 19.32  ? 406  ILE   A N    1 
ATOM   5796  C CA   . ILE   A  1 380 ? 35.035 -20.821 -30.933 1.00 19.66  ? 406  ILE   A CA   1 
ATOM   5797  C C    . ILE   A  1 380 ? 35.979 -20.974 -32.114 1.00 21.40  ? 406  ILE   A C    1 
ATOM   5798  O O    . ILE   A  1 380 ? 36.226 -20.000 -32.817 1.00 22.14  ? 406  ILE   A O    1 
ATOM   5799  C CB   . ILE   A  1 380 ? 33.588 -20.550 -31.445 1.00 18.77  ? 406  ILE   A CB   1 
ATOM   5800  C CG1  . ILE   A  1 380 ? 32.582 -20.472 -30.275 1.00 19.31  ? 406  ILE   A CG1  1 
ATOM   5801  C CG2  . ILE   A  1 380 ? 33.163 -21.646 -32.425 1.00 18.82  ? 406  ILE   A CG2  1 
ATOM   5802  C CD1  . ILE   A  1 380 ? 31.284 -19.699 -30.617 1.00 20.72  ? 406  ILE   A CD1  1 
ATOM   5803  H H    . ILE   A  1 380 ? 34.996 -18.885 -30.185 0.00 20.90  ? 406  ILE   A H    1 
ATOM   5804  H HA   . ILE   A  1 380 ? 35.027 -21.741 -30.351 0.00 22.36  ? 406  ILE   A HA   1 
ATOM   5805  H HB   . ILE   A  1 380 ? 33.586 -19.598 -31.973 0.00 20.51  ? 406  ILE   A HB   1 
ATOM   5806  H HG12 . ILE   A  1 380 ? 32.303 -21.482 -29.980 0.00 21.89  ? 406  ILE   A HG12 1 
ATOM   5807  H HG13 . ILE   A  1 380 ? 33.066 -19.962 -29.444 0.00 21.31  ? 406  ILE   A HG13 1 
ATOM   5808  H HG21 . ILE   A  1 380 ? 32.076 -21.700 -32.471 0.00 21.42  ? 406  ILE   A HG21 1 
ATOM   5809  H HG22 . ILE   A  1 380 ? 33.547 -21.414 -33.417 0.00 21.28  ? 406  ILE   A HG22 1 
ATOM   5810  H HG23 . ILE   A  1 380 ? 33.562 -22.600 -32.083 0.00 21.72  ? 406  ILE   A HG23 1 
ATOM   5811  H HD11 . ILE   A  1 380 ? 30.727 -19.530 -29.697 0.00 22.94  ? 406  ILE   A HD11 1 
ATOM   5812  H HD12 . ILE   A  1 380 ? 31.547 -18.746 -31.072 0.00 22.63  ? 406  ILE   A HD12 1 
ATOM   5813  H HD13 . ILE   A  1 380 ? 30.678 -20.286 -31.306 0.00 23.22  ? 406  ILE   A HD13 1 
ATOM   5814  N N    . LYS   A  1 381 ? 36.460 -22.187 -32.362 1.00 21.82  ? 407  LYS   A N    1 
ATOM   5815  C CA   . LYS   A  1 381 ? 37.371 -22.476 -33.469 1.00 23.43  ? 407  LYS   A CA   1 
ATOM   5816  C C    . LYS   A  1 381 ? 36.622 -23.003 -34.709 1.00 25.34  ? 407  LYS   A C    1 
ATOM   5817  O O    . LYS   A  1 381 ? 37.136 -22.876 -35.824 1.00 25.41  ? 407  LYS   A O    1 
ATOM   5818  C CB   . LYS   A  1 381 ? 38.365 -23.572 -33.036 1.00 25.92  ? 407  LYS   A CB   1 
ATOM   5819  C CG   . LYS   A  1 381 ? 39.278 -23.204 -31.867 1.00 29.50  ? 407  LYS   A CG   1 
ATOM   5820  C CD   . LYS   A  1 381 ? 40.134 -24.410 -31.504 1.00 33.63  ? 407  LYS   A CD   1 
ATOM   5821  C CE   . LYS   A  1 381 ? 41.155 -24.123 -30.433 1.00 38.59  ? 407  LYS   A CE   1 
ATOM   5822  N NZ   . LYS   A  1 381 ? 41.934 -25.346 -30.050 1.00 40.22  ? 407  LYS   A NZ   1 
ATOM   5823  H H    . LYS   A  1 381 ? 36.231 -23.008 -31.811 0.00 25.49  ? 407  LYS   A H    1 
ATOM   5824  H HA   . LYS   A  1 381 ? 37.941 -21.591 -33.749 0.00 26.94  ? 407  LYS   A HA   1 
ATOM   5825  H HB2  . LYS   A  1 381 ? 37.804 -24.460 -32.749 0.00 31.12  ? 407  LYS   A HB2  1 
ATOM   5826  H HB3  . LYS   A  1 381 ? 39.004 -23.807 -33.886 0.00 30.92  ? 407  LYS   A HB3  1 
ATOM   5827  H HG2  . LYS   A  1 381 ? 39.933 -22.385 -32.157 0.00 34.65  ? 407  LYS   A HG2  1 
ATOM   5828  H HG3  . LYS   A  1 381 ? 38.679 -22.931 -30.999 0.00 34.78  ? 407  LYS   A HG3  1 
ATOM   5829  H HD2  . LYS   A  1 381 ? 39.485 -25.206 -31.141 0.00 40.81  ? 407  LYS   A HD2  1 
ATOM   5830  H HD3  . LYS   A  1 381 ? 40.667 -24.746 -32.393 0.00 40.73  ? 407  LYS   A HD3  1 
ATOM   5831  H HE2  . LYS   A  1 381 ? 41.857 -23.376 -30.802 0.00 46.19  ? 407  LYS   A HE2  1 
ATOM   5832  H HE3  . LYS   A  1 381 ? 40.646 -23.752 -29.544 0.00 46.22  ? 407  LYS   A HE3  1 
ATOM   5833  H HZ1  . LYS   A  1 381 ? 42.636 -25.107 -29.356 0.00 49.05  ? 407  LYS   A HZ1  1 
ATOM   5834  H HZ2  . LYS   A  1 381 ? 41.310 -26.045 -29.661 0.00 49.31  ? 407  LYS   A HZ2  1 
ATOM   5835  H HZ3  . LYS   A  1 381 ? 42.395 -25.733 -30.867 0.00 49.29  ? 407  LYS   A HZ3  1 
ATOM   5836  N N    . GLN   A  1 382 ? 35.460 -23.666 -34.517 1.00 26.18  ? 408  GLN   A N    1 
ATOM   5837  C CA   . GLN   A  1 382 ? 34.714 -24.279 -35.622 1.00 27.53  ? 408  GLN   A CA   1 
ATOM   5838  C C    . GLN   A  1 382 ? 33.203 -24.250 -35.409 1.00 27.90  ? 408  GLN   A C    1 
ATOM   5839  O O    . GLN   A  1 382 ? 32.717 -24.492 -34.301 1.00 27.41  ? 408  GLN   A O    1 
ATOM   5840  C CB   . GLN   A  1 382 ? 35.131 -25.757 -35.773 1.00 30.53  ? 408  GLN   A CB   1 
ATOM   5841  C CG   . GLN   A  1 382 ? 36.360 -26.010 -36.645 1.00 35.48  ? 408  GLN   A CG   1 
ATOM   5842  H H    . GLN   A  1 382 ? 35.015 -23.810 -33.616 0.00 31.10  ? 408  GLN   A H    1 
ATOM   5843  H HA   . GLN   A  1 382 ? 34.922 -23.749 -36.551 0.00 32.85  ? 408  GLN   A HA   1 
ATOM   5844  H HB2  . GLN   A  1 382 ? 35.347 -26.154 -34.782 0.00 37.44  ? 408  GLN   A HB2  1 
ATOM   5845  H HB3  . GLN   A  1 382 ? 34.300 -26.306 -36.212 0.00 37.60  ? 408  GLN   A HB3  1 
ATOM   5846  N N    . ILE   A  1 383 ? 32.452 -24.028 -36.490 1.00 28.26  ? 409  ILE   A N    1 
ATOM   5847  C CA   . ILE   A  1 383 ? 30.996 -24.026 -36.433 1.00 28.89  ? 409  ILE   A CA   1 
ATOM   5848  C C    . ILE   A  1 383 ? 30.452 -24.837 -37.601 1.00 28.64  ? 409  ILE   A C    1 
ATOM   5849  O O    . ILE   A  1 383 ? 30.915 -24.668 -38.726 1.00 28.14  ? 409  ILE   A O    1 
ATOM   5850  C CB   . ILE   A  1 383 ? 30.452 -22.567 -36.490 1.00 29.94  ? 409  ILE   A CB   1 
ATOM   5851  C CG1  . ILE   A  1 383 ? 30.969 -21.771 -35.268 1.00 31.45  ? 409  ILE   A CG1  1 
ATOM   5852  C CG2  . ILE   A  1 383 ? 28.891 -22.550 -36.597 1.00 30.39  ? 409  ILE   A CG2  1 
ATOM   5853  C CD1  . ILE   A  1 383 ? 30.423 -20.376 -35.064 1.00 32.85  ? 409  ILE   A CD1  1 
ATOM   5854  H H    . ILE   A  1 383 ? 32.814 -23.851 -37.422 0.00 33.90  ? 409  ILE   A H    1 
ATOM   5855  H HA   . ILE   A  1 383 ? 30.649 -24.481 -35.507 0.00 34.90  ? 409  ILE   A HA   1 
ATOM   5856  H HB   . ILE   A  1 383 ? 30.853 -22.098 -37.387 0.00 35.29  ? 409  ILE   A HB   1 
ATOM   5857  H HG12 . ILE   A  1 383 ? 30.743 -22.339 -34.367 0.00 36.98  ? 409  ILE   A HG12 1 
ATOM   5858  H HG13 . ILE   A  1 383 ? 32.049 -21.666 -35.359 0.00 36.70  ? 409  ILE   A HG13 1 
ATOM   5859  H HG21 . ILE   A  1 383 ? 28.529 -21.523 -36.582 0.00 35.77  ? 409  ILE   A HG21 1 
ATOM   5860  H HG22 . ILE   A  1 383 ? 28.572 -23.006 -37.533 0.00 36.45  ? 409  ILE   A HG22 1 
ATOM   5861  H HG23 . ILE   A  1 383 ? 28.475 -23.101 -35.755 0.00 36.34  ? 409  ILE   A HG23 1 
ATOM   5862  H HD11 . ILE   A  1 383 ? 31.024 -19.868 -34.311 0.00 37.70  ? 409  ILE   A HD11 1 
ATOM   5863  H HD12 . ILE   A  1 383 ? 30.484 -19.850 -36.015 0.00 37.85  ? 409  ILE   A HD12 1 
ATOM   5864  H HD13 . ILE   A  1 383 ? 29.389 -20.433 -34.727 0.00 38.06  ? 409  ILE   A HD13 1 
ATOM   5865  N N    . ASP   A  1 384 ? 29.450 -25.674 -37.345 1.00 29.08  ? 410  ASP   A N    1 
ATOM   5866  C CA   . ASP   A  1 384 ? 28.739 -26.387 -38.404 1.00 30.60  ? 410  ASP   A CA   1 
ATOM   5867  C C    . ASP   A  1 384 ? 27.685 -25.357 -38.828 1.00 30.04  ? 410  ASP   A C    1 
ATOM   5868  O O    . ASP   A  1 384 ? 26.621 -25.304 -38.225 1.00 29.35  ? 410  ASP   A O    1 
ATOM   5869  C CB   . ASP   A  1 384 ? 28.053 -27.671 -37.876 1.00 34.76  ? 410  ASP   A CB   1 
ATOM   5870  C CG   . ASP   A  1 384 ? 28.909 -28.934 -37.873 1.00 44.55  ? 410  ASP   A CG   1 
ATOM   5871  O OD1  . ASP   A  1 384 ? 30.048 -28.890 -38.402 1.00 46.96  ? 410  ASP   A OD1  1 
ATOM   5872  O OD2  . ASP   A  1 384 ? 28.432 -29.975 -37.357 1.00 48.37  ? 410  ASP   A OD2  1 
ATOM   5873  H H    . ASP   A  1 384 ? 29.102 -25.868 -36.411 0.00 35.95  ? 410  ASP   A H    1 
ATOM   5874  H HA   . ASP   A  1 384 ? 29.379 -26.616 -39.254 0.00 38.41  ? 410  ASP   A HA   1 
ATOM   5875  H HB2  . ASP   A  1 384 ? 27.701 -27.510 -36.858 0.00 43.75  ? 410  ASP   A HB2  1 
ATOM   5876  H HB3  . ASP   A  1 384 ? 27.197 -27.882 -38.516 0.00 44.20  ? 410  ASP   A HB3  1 
ATOM   5877  N N    . PHE   A  1 385 ? 28.006 -24.492 -39.792 1.00 30.20  ? 411  PHE   A N    1 
ATOM   5878  C CA   . PHE   A  1 385 ? 27.104 -23.408 -40.194 1.00 31.26  ? 411  PHE   A CA   1 
ATOM   5879  C C    . PHE   A  1 385 ? 25.715 -23.846 -40.684 1.00 32.11  ? 411  PHE   A C    1 
ATOM   5880  O O    . PHE   A  1 385 ? 24.778 -23.048 -40.590 1.00 32.22  ? 411  PHE   A O    1 
ATOM   5881  C CB   . PHE   A  1 385 ? 27.767 -22.508 -41.247 1.00 31.28  ? 411  PHE   A CB   1 
ATOM   5882  C CG   . PHE   A  1 385 ? 28.885 -21.652 -40.704 1.00 32.04  ? 411  PHE   A CG   1 
ATOM   5883  C CD1  . PHE   A  1 385 ? 28.616 -20.435 -40.103 1.00 32.80  ? 411  PHE   A CD1  1 
ATOM   5884  C CD2  . PHE   A  1 385 ? 30.199 -22.084 -40.758 1.00 32.86  ? 411  PHE   A CD2  1 
ATOM   5885  C CE1  . PHE   A  1 385 ? 29.637 -19.672 -39.559 1.00 33.25  ? 411  PHE   A CE1  1 
ATOM   5886  C CE2  . PHE   A  1 385 ? 31.219 -21.319 -40.215 1.00 33.51  ? 411  PHE   A CE2  1 
ATOM   5887  C CZ   . PHE   A  1 385 ? 30.931 -20.120 -39.613 1.00 33.27  ? 411  PHE   A CZ   1 
ATOM   5888  H H    . PHE   A  1 385 ? 28.878 -24.521 -40.311 0.00 37.15  ? 411  PHE   A H    1 
ATOM   5889  H HA   . PHE   A  1 385 ? 26.922 -22.799 -39.309 0.00 37.82  ? 411  PHE   A HA   1 
ATOM   5890  H HB2  . PHE   A  1 385 ? 28.160 -23.120 -42.058 0.00 38.19  ? 411  PHE   A HB2  1 
ATOM   5891  H HB3  . PHE   A  1 385 ? 27.004 -21.831 -41.626 0.00 37.77  ? 411  PHE   A HB3  1 
ATOM   5892  H HD1  . PHE   A  1 385 ? 27.599 -20.087 -40.037 0.00 38.61  ? 411  PHE   A HD1  1 
ATOM   5893  H HD2  . PHE   A  1 385 ? 30.429 -23.035 -41.209 0.00 39.66  ? 411  PHE   A HD2  1 
ATOM   5894  H HE1  . PHE   A  1 385 ? 29.413 -18.725 -39.098 0.00 38.32  ? 411  PHE   A HE1  1 
ATOM   5895  H HE2  . PHE   A  1 385 ? 32.238 -21.666 -40.269 0.00 39.61  ? 411  PHE   A HE2  1 
ATOM   5896  H HZ   . PHE   A  1 385 ? 31.727 -19.513 -39.214 0.00 38.42  ? 411  PHE   A HZ   1 
ATOM   5897  N N    . LYS   A  1 386 ? 25.559 -25.092 -41.171 1.00 32.26  ? 412  LYS   A N    1 
ATOM   5898  C CA   . LYS   A  1 386 ? 24.252 -25.576 -41.621 1.00 33.19  ? 412  LYS   A CA   1 
ATOM   5899  C C    . LYS   A  1 386 ? 23.185 -25.521 -40.520 1.00 33.19  ? 412  LYS   A C    1 
ATOM   5900  O O    . LYS   A  1 386 ? 22.003 -25.523 -40.838 1.00 33.21  ? 412  LYS   A O    1 
ATOM   5901  C CB   . LYS   A  1 386 ? 24.352 -27.019 -42.154 1.00 35.93  ? 412  LYS   A CB   1 
ATOM   5902  C CG   . LYS   A  1 386 ? 24.674 -28.079 -41.103 1.00 41.99  ? 412  LYS   A CG   1 
ATOM   5903  C CD   . LYS   A  1 386 ? 24.966 -29.433 -41.757 1.00 48.57  ? 412  LYS   A CD   1 
ATOM   5904  C CE   . LYS   A  1 386 ? 25.361 -30.484 -40.741 1.00 53.74  ? 412  LYS   A CE   1 
ATOM   5905  N NZ   . LYS   A  1 386 ? 25.609 -31.813 -41.368 1.00 56.54  ? 412  LYS   A NZ   1 
ATOM   5906  H H    . LYS   A  1 386 ? 26.306 -25.770 -41.278 0.00 40.69  ? 412  LYS   A H    1 
ATOM   5907  H HA   . LYS   A  1 386 ? 23.911 -24.946 -42.440 0.00 42.07  ? 412  LYS   A HA   1 
ATOM   5908  H HB2  . LYS   A  1 386 ? 23.398 -27.287 -42.607 0.00 46.57  ? 412  LYS   A HB2  1 
ATOM   5909  H HB3  . LYS   A  1 386 ? 25.135 -27.056 -42.911 0.00 46.18  ? 412  LYS   A HB3  1 
ATOM   5910  H HG2  . LYS   A  1 386 ? 25.553 -27.773 -40.538 0.00 53.33  ? 412  LYS   A HG2  1 
ATOM   5911  H HG3  . LYS   A  1 386 ? 23.823 -28.217 -40.438 0.00 53.83  ? 412  LYS   A HG3  1 
ATOM   5912  H HD2  . LYS   A  1 386 ? 24.073 -29.781 -42.275 0.00 62.81  ? 412  LYS   A HD2  1 
ATOM   5913  H HD3  . LYS   A  1 386 ? 25.788 -29.320 -42.463 0.00 62.31  ? 412  LYS   A HD3  1 
ATOM   5914  H HE2  . LYS   A  1 386 ? 26.276 -30.170 -40.241 0.00 68.53  ? 412  LYS   A HE2  1 
ATOM   5915  H HE3  . LYS   A  1 386 ? 24.558 -30.598 -40.014 0.00 68.98  ? 412  LYS   A HE3  1 
ATOM   5916  H HZ1  . LYS   A  1 386 ? 25.889 -32.484 -40.660 0.00 73.31  ? 412  LYS   A HZ1  1 
ATOM   5917  H HZ2  . LYS   A  1 386 ? 24.763 -32.145 -41.820 0.00 73.48  ? 412  LYS   A HZ2  1 
ATOM   5918  H HZ3  . LYS   A  1 386 ? 26.346 -31.736 -42.061 0.00 73.06  ? 412  LYS   A HZ3  1 
ATOM   5919  N N    . LEU   A  1 387 ? 23.583 -25.481 -39.239 1.00 32.82  ? 413  LEU   A N    1 
ATOM   5920  C CA   . LEU   A  1 387 ? 22.623 -25.457 -38.141 1.00 32.83  ? 413  LEU   A CA   1 
ATOM   5921  C C    . LEU   A  1 387 ? 21.738 -24.205 -38.113 1.00 32.64  ? 413  LEU   A C    1 
ATOM   5922  O O    . LEU   A  1 387 ? 20.593 -24.305 -37.681 1.00 32.42  ? 413  LEU   A O    1 
ATOM   5923  C CB   . LEU   A  1 387 ? 23.354 -25.650 -36.796 1.00 33.28  ? 413  LEU   A CB   1 
ATOM   5924  C CG   . LEU   A  1 387 ? 24.120 -24.455 -36.212 1.00 35.21  ? 413  LEU   A CG   1 
ATOM   5925  C CD1  . LEU   A  1 387 ? 23.239 -23.597 -35.329 1.00 35.66  ? 413  LEU   A CD1  1 
ATOM   5926  C CD2  . LEU   A  1 387 ? 25.276 -24.919 -35.359 1.00 36.26  ? 413  LEU   A CD2  1 
ATOM   5927  H H    . LEU   A  1 387 ? 24.550 -25.460 -38.932 0.00 41.17  ? 413  LEU   A H    1 
ATOM   5928  H HA   . LEU   A  1 387 ? 21.957 -26.310 -38.262 0.00 42.02  ? 413  LEU   A HA   1 
ATOM   5929  H HB2  . LEU   A  1 387 ? 22.621 -25.964 -36.054 0.00 41.99  ? 413  LEU   A HB2  1 
ATOM   5930  H HB3  . LEU   A  1 387 ? 24.078 -26.449 -36.948 0.00 42.04  ? 413  LEU   A HB3  1 
ATOM   5931  H HG   . LEU   A  1 387 ? 24.516 -23.834 -37.015 0.00 43.12  ? 413  LEU   A HG   1 
ATOM   5932  H HD11 . LEU   A  1 387 ? 23.826 -22.767 -34.939 0.00 43.15  ? 413  LEU   A HD11 1 
ATOM   5933  H HD12 . LEU   A  1 387 ? 22.413 -23.215 -35.927 0.00 43.71  ? 413  LEU   A HD12 1 
ATOM   5934  H HD13 . LEU   A  1 387 ? 22.858 -24.202 -34.507 0.00 43.87  ? 413  LEU   A HD13 1 
ATOM   5935  H HD21 . LEU   A  1 387 ? 25.812 -24.037 -35.012 0.00 44.08  ? 413  LEU   A HD21 1 
ATOM   5936  H HD22 . LEU   A  1 387 ? 24.893 -25.486 -34.512 0.00 44.80  ? 413  LEU   A HD22 1 
ATOM   5937  H HD23 . LEU   A  1 387 ? 25.943 -25.539 -35.957 0.00 44.80  ? 413  LEU   A HD23 1 
ATOM   5938  N N    . PHE   A  1 388 ? 22.241 -23.045 -38.592 1.00 32.28  ? 414  PHE   A N    1 
ATOM   5939  C CA   . PHE   A  1 388 ? 21.481 -21.794 -38.539 1.00 32.60  ? 414  PHE   A CA   1 
ATOM   5940  C C    . PHE   A  1 388 ? 20.224 -21.782 -39.417 1.00 34.49  ? 414  PHE   A C    1 
ATOM   5941  O O    . PHE   A  1 388 ? 19.239 -21.154 -39.029 1.00 35.18  ? 414  PHE   A O    1 
ATOM   5942  C CB   . PHE   A  1 388 ? 22.381 -20.595 -38.856 1.00 31.47  ? 414  PHE   A CB   1 
ATOM   5943  C CG   . PHE   A  1 388 ? 23.494 -20.416 -37.845 1.00 31.10  ? 414  PHE   A CG   1 
ATOM   5944  C CD1  . PHE   A  1 388 ? 23.210 -20.098 -36.527 1.00 31.65  ? 414  PHE   A CD1  1 
ATOM   5945  C CD2  . PHE   A  1 388 ? 24.820 -20.549 -38.218 1.00 31.20  ? 414  PHE   A CD2  1 
ATOM   5946  C CE1  . PHE   A  1 388 ? 24.230 -19.954 -35.596 1.00 32.24  ? 414  PHE   A CE1  1 
ATOM   5947  C CE2  . PHE   A  1 388 ? 25.840 -20.370 -37.289 1.00 31.58  ? 414  PHE   A CE2  1 
ATOM   5948  C CZ   . PHE   A  1 388 ? 25.539 -20.070 -35.989 1.00 31.46  ? 414  PHE   A CZ   1 
ATOM   5949  H H    . PHE   A  1 388 ? 23.153 -22.950 -39.028 0.00 39.75  ? 414  PHE   A H    1 
ATOM   5950  H HA   . PHE   A  1 388 ? 21.135 -21.672 -37.514 0.00 39.88  ? 414  PHE   A HA   1 
ATOM   5951  H HB2  . PHE   A  1 388 ? 22.825 -20.734 -39.841 0.00 38.11  ? 414  PHE   A HB2  1 
ATOM   5952  H HB3  . PHE   A  1 388 ? 21.775 -19.690 -38.849 0.00 37.84  ? 414  PHE   A HB3  1 
ATOM   5953  H HD1  . PHE   A  1 388 ? 22.185 -20.005 -36.212 0.00 37.75  ? 414  PHE   A HD1  1 
ATOM   5954  H HD2  . PHE   A  1 388 ? 25.071 -20.778 -39.240 0.00 37.28  ? 414  PHE   A HD2  1 
ATOM   5955  H HE1  . PHE   A  1 388 ? 23.994 -19.707 -34.574 0.00 37.84  ? 414  PHE   A HE1  1 
ATOM   5956  H HE2  . PHE   A  1 388 ? 26.868 -20.478 -37.592 0.00 37.12  ? 414  PHE   A HE2  1 
ATOM   5957  H HZ   . PHE   A  1 388 ? 26.330 -19.943 -35.268 0.00 36.66  ? 414  PHE   A HZ   1 
ATOM   5958  N N    . GLN   A  1 389 ? 20.228 -22.486 -40.560 1.00 35.36  ? 415  GLN   A N    1 
ATOM   5959  C CA   . GLN   A  1 389 ? 19.036 -22.545 -41.408 1.00 37.17  ? 415  GLN   A CA   1 
ATOM   5960  C C    . GLN   A  1 389 ? 17.924 -23.392 -40.752 1.00 38.18  ? 415  GLN   A C    1 
ATOM   5961  O O    . GLN   A  1 389 ? 16.759 -23.215 -41.109 1.00 38.14  ? 415  GLN   A O    1 
ATOM   5962  C CB   . GLN   A  1 389 ? 19.373 -23.040 -42.831 1.00 40.05  ? 415  GLN   A CB   1 
ATOM   5963  C CG   . GLN   A  1 389 ? 19.513 -24.555 -42.988 1.00 45.53  ? 415  GLN   A CG   1 
ATOM   5964  C CD   . GLN   A  1 389 ? 20.243 -24.971 -44.257 1.00 51.58  ? 415  GLN   A CD   1 
ATOM   5965  O OE1  . GLN   A  1 389 ? 21.021 -25.932 -44.251 1.00 53.79  ? 415  GLN   A OE1  1 
ATOM   5966  N NE2  . GLN   A  1 389 ? 20.016 -24.287 -45.382 1.00 52.21  ? 415  GLN   A NE2  1 
ATOM   5967  H H    . GLN   A  1 389 ? 21.021 -23.005 -40.924 0.00 44.24  ? 415  GLN   A H    1 
ATOM   5968  H HA   . GLN   A  1 389 ? 18.645 -21.535 -41.523 0.00 46.59  ? 415  GLN   A HA   1 
ATOM   5969  H HB2  . GLN   A  1 389 ? 18.577 -22.718 -43.501 0.00 50.88  ? 415  GLN   A HB2  1 
ATOM   5970  H HB3  . GLN   A  1 389 ? 20.313 -22.589 -43.145 0.00 50.28  ? 415  GLN   A HB3  1 
ATOM   5971  H HG2  . GLN   A  1 389 ? 20.069 -24.949 -42.138 0.00 57.72  ? 415  GLN   A HG2  1 
ATOM   5972  H HG3  . GLN   A  1 389 ? 18.522 -25.005 -43.024 0.00 58.34  ? 415  GLN   A HG3  1 
ATOM   5973  H HE21 . GLN   A  1 389 ? 19.354 -23.518 -45.410 0.00 66.05  ? 415  GLN   A HE21 1 
ATOM   5974  H HE22 . GLN   A  1 389 ? 20.497 -24.559 -46.233 0.00 66.34  ? 415  GLN   A HE22 1 
ATOM   5975  N N    . ASN   A  1 390 ? 18.261 -24.293 -39.797 1.00 38.75  ? 416  ASN   A N    1 
ATOM   5976  C CA   . ASN   A  1 390 ? 17.230 -25.077 -39.116 1.00 40.24  ? 416  ASN   A CA   1 
ATOM   5977  C C    . ASN   A  1 390 ? 16.541 -24.304 -37.967 1.00 39.00  ? 416  ASN   A C    1 
ATOM   5978  O O    . ASN   A  1 390 ? 15.622 -24.846 -37.355 1.00 39.33  ? 416  ASN   A O    1 
ATOM   5979  C CB   . ASN   A  1 390 ? 17.775 -26.438 -38.633 1.00 44.71  ? 416  ASN   A CB   1 
ATOM   5980  C CG   . ASN   A  1 390 ? 16.762 -27.515 -38.577 1.00 54.43  ? 416  ASN   A CG   1 
ATOM   5981  O OD1  . ASN   A  1 390 ? 15.765 -27.453 -39.322 1.00 56.54  ? 416  ASN   A OD1  1 
ATOM   5982  N ND2  . ASN   A  1 390 ? 16.795 -28.446 -37.637 1.00 59.46  ? 416  ASN   A ND2  1 
ATOM   5983  H H    . ASN   A  1 390 ? 19.205 -24.503 -39.489 0.00 49.18  ? 416  ASN   A H    1 
ATOM   5984  H HA   . ASN   A  1 390 ? 16.455 -25.257 -39.860 0.00 52.15  ? 416  ASN   A HA   1 
ATOM   5985  H HB2  . ASN   A  1 390 ? 18.560 -26.764 -39.314 0.00 57.48  ? 416  ASN   A HB2  1 
ATOM   5986  H HB3  . ASN   A  1 390 ? 18.185 -26.313 -37.632 0.00 57.12  ? 416  ASN   A HB3  1 
ATOM   5987  H HD21 . ASN   A  1 390 ? 16.642 -29.190 -38.289 0.00 76.73  ? 416  ASN   A HD21 1 
ATOM   5988  H HD22 . ASN   A  1 390 ? 17.441 -28.444 -36.855 0.00 75.92  ? 416  ASN   A HD22 1 
ATOM   5989  N N    . PHE   A  1 391 ? 16.962 -23.054 -37.670 1.00 37.33  ? 417  PHE   A N    1 
ATOM   5990  C CA   . PHE   A  1 391 ? 16.258 -22.219 -36.688 1.00 36.61  ? 417  PHE   A CA   1 
ATOM   5991  C C    . PHE   A  1 391 ? 14.998 -21.686 -37.371 1.00 36.40  ? 417  PHE   A C    1 
ATOM   5992  O O    . PHE   A  1 391 ? 14.982 -21.556 -38.597 1.00 36.25  ? 417  PHE   A O    1 
ATOM   5993  C CB   . PHE   A  1 391 ? 17.113 -21.023 -36.226 1.00 35.53  ? 417  PHE   A CB   1 
ATOM   5994  C CG   . PHE   A  1 391 ? 18.040 -21.312 -35.076 1.00 35.41  ? 417  PHE   A CG   1 
ATOM   5995  C CD1  . PHE   A  1 391 ? 19.199 -22.043 -35.266 1.00 36.03  ? 417  PHE   A CD1  1 
ATOM   5996  C CD2  . PHE   A  1 391 ? 17.772 -20.821 -33.810 1.00 35.82  ? 417  PHE   A CD2  1 
ATOM   5997  C CE1  . PHE   A  1 391 ? 20.070 -22.275 -34.214 1.00 36.66  ? 417  PHE   A CE1  1 
ATOM   5998  C CE2  . PHE   A  1 391 ? 18.653 -21.042 -32.765 1.00 36.40  ? 417  PHE   A CE2  1 
ATOM   5999  C CZ   . PHE   A  1 391 ? 19.790 -21.777 -32.969 1.00 36.32  ? 417  PHE   A CZ   1 
ATOM   6000  H H    . PHE   A  1 391 ? 17.780 -22.609 -38.073 0.00 46.92  ? 417  PHE   A H    1 
ATOM   6001  H HA   . PHE   A  1 391 ? 15.962 -22.811 -35.823 0.00 46.37  ? 417  PHE   A HA   1 
ATOM   6002  H HB2  . PHE   A  1 391 ? 17.712 -20.663 -37.060 0.00 43.91  ? 417  PHE   A HB2  1 
ATOM   6003  H HB3  . PHE   A  1 391 ? 16.437 -20.229 -35.911 0.00 44.00  ? 417  PHE   A HB3  1 
ATOM   6004  H HD1  . PHE   A  1 391 ? 19.433 -22.427 -36.245 0.00 44.58  ? 417  PHE   A HD1  1 
ATOM   6005  H HD2  . PHE   A  1 391 ? 16.886 -20.235 -33.636 0.00 43.99  ? 417  PHE   A HD2  1 
ATOM   6006  H HE1  . PHE   A  1 391 ? 20.965 -22.849 -34.371 0.00 44.95  ? 417  PHE   A HE1  1 
ATOM   6007  H HE2  . PHE   A  1 391 ? 18.427 -20.666 -31.782 0.00 44.27  ? 417  PHE   A HE2  1 
ATOM   6008  H HZ   . PHE   A  1 391 ? 20.461 -21.969 -32.149 0.00 44.16  ? 417  PHE   A HZ   1 
ATOM   6009  N N    . SER   A  1 392 ? 13.960 -21.334 -36.593 1.00 36.42  ? 418  SER   A N    1 
ATOM   6010  C CA   . SER   A  1 392 ? 12.713 -20.862 -37.198 1.00 36.78  ? 418  SER   A CA   1 
ATOM   6011  C C    . SER   A  1 392 ? 12.880 -19.570 -38.020 1.00 35.73  ? 418  SER   A C    1 
ATOM   6012  O O    . SER   A  1 392 ? 12.461 -19.538 -39.174 1.00 36.14  ? 418  SER   A O    1 
ATOM   6013  C CB   . SER   A  1 392 ? 11.609 -20.691 -36.161 1.00 39.27  ? 418  SER   A CB   1 
ATOM   6014  O OG   . SER   A  1 392 ? 10.383 -20.473 -36.847 1.00 43.68  ? 418  SER   A OG   1 
ATOM   6015  H H    . SER   A  1 392 ? 13.956 -21.366 -35.579 0.00 46.26  ? 418  SER   A H    1 
ATOM   6016  H HA   . SER   A  1 392 ? 12.408 -21.654 -37.882 0.00 47.67  ? 418  SER   A HA   1 
ATOM   6017  H HB2  . SER   A  1 392 ? 11.535 -21.596 -35.560 0.00 50.70  ? 418  SER   A HB2  1 
ATOM   6018  H HB3  . SER   A  1 392 ? 11.839 -19.835 -35.528 0.00 49.95  ? 418  SER   A HB3  1 
ATOM   6019  H HG   . SER   A  1 392 ? 9.817  -19.805 -36.379 0.00 56.14  ? 418  SER   A HG   1 
ATOM   6020  N N    . ASN   A  1 393 ? 13.463 -18.508 -37.439 1.00 34.33  ? 419  ASN   A N    1 
ATOM   6021  C CA   . ASN   A  1 393 ? 13.659 -17.251 -38.167 1.00 33.25  ? 419  ASN   A CA   1 
ATOM   6022  C C    . ASN   A  1 393 ? 14.783 -16.378 -37.577 1.00 30.48  ? 419  ASN   A C    1 
ATOM   6023  O O    . ASN   A  1 393 ? 14.516 -15.306 -37.021 1.00 30.11  ? 419  ASN   A O    1 
ATOM   6024  C CB   . ASN   A  1 393 ? 12.339 -16.467 -38.230 1.00 35.85  ? 419  ASN   A CB   1 
ATOM   6025  C CG   . ASN   A  1 393 ? 12.425 -15.200 -39.061 1.00 41.11  ? 419  ASN   A CG   1 
ATOM   6026  O OD1  . ASN   A  1 393 ? 13.201 -15.112 -40.028 1.00 42.35  ? 419  ASN   A OD1  1 
ATOM   6027  N ND2  . ASN   A  1 393 ? 11.632 -14.191 -38.705 1.00 42.37  ? 419  ASN   A ND2  1 
ATOM   6028  H H    . ASN   A  1 393 ? 13.802 -18.489 -36.482 0.00 42.96  ? 419  ASN   A H    1 
ATOM   6029  H HA   . ASN   A  1 393 ? 13.955 -17.488 -39.188 0.00 41.70  ? 419  ASN   A HA   1 
ATOM   6030  H HB2  . ASN   A  1 393 ? 11.574 -17.098 -38.678 0.00 45.55  ? 419  ASN   A HB2  1 
ATOM   6031  H HB3  . ASN   A  1 393 ? 12.040 -16.202 -37.217 0.00 44.88  ? 419  ASN   A HB3  1 
ATOM   6032  H HD21 . ASN   A  1 393 ? 11.651 -13.325 -39.235 0.00 52.55  ? 419  ASN   A HD21 1 
ATOM   6033  H HD22 . ASN   A  1 393 ? 10.999 -14.285 -37.917 0.00 52.83  ? 419  ASN   A HD22 1 
ATOM   6034  N N    . LEU   A  1 394 ? 16.040 -16.817 -37.727 1.00 28.80  ? 420  LEU   A N    1 
ATOM   6035  C CA   . LEU   A  1 394 ? 17.170 -16.009 -37.271 1.00 27.55  ? 420  LEU   A CA   1 
ATOM   6036  C C    . LEU   A  1 394 ? 17.338 -14.800 -38.211 1.00 25.88  ? 420  LEU   A C    1 
ATOM   6037  O O    . LEU   A  1 394 ? 17.245 -14.955 -39.427 1.00 25.97  ? 420  LEU   A O    1 
ATOM   6038  C CB   . LEU   A  1 394 ? 18.485 -16.811 -37.227 1.00 27.71  ? 420  LEU   A CB   1 
ATOM   6039  C CG   . LEU   A  1 394 ? 18.729 -17.675 -35.997 1.00 28.77  ? 420  LEU   A CG   1 
ATOM   6040  C CD1  . LEU   A  1 394 ? 19.958 -18.545 -36.203 1.00 29.39  ? 420  LEU   A CD1  1 
ATOM   6041  C CD2  . LEU   A  1 394 ? 18.849 -16.814 -34.713 1.00 29.08  ? 420  LEU   A CD2  1 
ATOM   6042  H H    . LEU   A  1 394 ? 16.289 -17.704 -38.152 0.00 35.47  ? 420  LEU   A H    1 
ATOM   6043  H HA   . LEU   A  1 394 ? 16.953 -15.625 -36.277 0.00 32.93  ? 420  LEU   A HA   1 
ATOM   6044  H HB2  . LEU   A  1 394 ? 18.525 -17.465 -38.098 0.00 33.40  ? 420  LEU   A HB2  1 
ATOM   6045  H HB3  . LEU   A  1 394 ? 19.309 -16.101 -37.288 0.00 32.68  ? 420  LEU   A HB3  1 
ATOM   6046  H HG   . LEU   A  1 394 ? 17.876 -18.340 -35.865 0.00 34.83  ? 420  LEU   A HG   1 
ATOM   6047  H HD11 . LEU   A  1 394 ? 20.590 -18.525 -35.316 0.00 34.83  ? 420  LEU   A HD11 1 
ATOM   6048  H HD12 . LEU   A  1 394 ? 19.639 -19.568 -36.394 0.00 35.54  ? 420  LEU   A HD12 1 
ATOM   6049  H HD13 . LEU   A  1 394 ? 20.514 -18.173 -37.062 0.00 34.97  ? 420  LEU   A HD13 1 
ATOM   6050  H HD21 . LEU   A  1 394 ? 19.320 -17.397 -33.922 0.00 34.35  ? 420  LEU   A HD21 1 
ATOM   6051  H HD22 . LEU   A  1 394 ? 19.442 -15.926 -34.929 0.00 33.97  ? 420  LEU   A HD22 1 
ATOM   6052  H HD23 . LEU   A  1 394 ? 17.853 -16.527 -34.379 0.00 34.52  ? 420  LEU   A HD23 1 
ATOM   6053  N N    . GLU   A  1 395 ? 17.537 -13.603 -37.643 1.00 24.44  ? 421  GLU   A N    1 
ATOM   6054  C CA   . GLU   A  1 395 ? 17.786 -12.358 -38.391 1.00 24.00  ? 421  GLU   A CA   1 
ATOM   6055  C C    . GLU   A  1 395 ? 19.196 -11.804 -38.090 1.00 22.46  ? 421  GLU   A C    1 
ATOM   6056  O O    . GLU   A  1 395 ? 19.740 -11.063 -38.911 1.00 21.82  ? 421  GLU   A O    1 
ATOM   6057  C CB   . GLU   A  1 395 ? 16.728 -11.292 -38.062 1.00 27.89  ? 421  GLU   A CB   1 
ATOM   6058  C CG   . GLU   A  1 395 ? 15.301 -11.707 -38.390 1.00 37.16  ? 421  GLU   A CG   1 
ATOM   6059  C CD   . GLU   A  1 395 ? 14.244 -10.756 -37.853 1.00 50.56  ? 421  GLU   A CD   1 
ATOM   6060  O OE1  . GLU   A  1 395 ? 14.437 -9.522  -37.967 1.00 54.17  ? 421  GLU   A OE1  1 
ATOM   6061  O OE2  . GLU   A  1 395 ? 13.223 -11.246 -37.315 1.00 54.43  ? 421  GLU   A OE2  1 
ATOM   6062  H H    . GLU   A  1 395 ? 17.512 -13.452 -36.639 0.00 28.53  ? 421  GLU   A H    1 
ATOM   6063  H HA   . GLU   A  1 395 ? 17.735 -12.542 -39.463 0.00 28.11  ? 421  GLU   A HA   1 
ATOM   6064  H HB2  . GLU   A  1 395 ? 16.773 -11.071 -36.996 0.00 32.47  ? 421  GLU   A HB2  1 
ATOM   6065  H HB3  . GLU   A  1 395 ? 16.950 -10.394 -38.637 0.00 32.50  ? 421  GLU   A HB3  1 
ATOM   6066  H HG2  . GLU   A  1 395 ? 15.193 -11.747 -39.473 0.00 44.60  ? 421  GLU   A HG2  1 
ATOM   6067  H HG3  . GLU   A  1 395 ? 15.100 -12.688 -37.964 0.00 44.59  ? 421  GLU   A HG3  1 
ATOM   6068  N N    . ILE   A  1 396 ? 19.766 -12.117 -36.905 1.00 21.45  ? 422  ILE   A N    1 
ATOM   6069  C CA   . ILE   A  1 396 ? 21.091 -11.644 -36.500 1.00 20.98  ? 422  ILE   A CA   1 
ATOM   6070  C C    . ILE   A  1 396 ? 21.879 -12.817 -35.940 1.00 20.49  ? 422  ILE   A C    1 
ATOM   6071  O O    . ILE   A  1 396 ? 21.538 -13.324 -34.871 1.00 20.89  ? 422  ILE   A O    1 
ATOM   6072  C CB   . ILE   A  1 396 ? 20.972 -10.504 -35.452 1.00 21.59  ? 422  ILE   A CB   1 
ATOM   6073  C CG1  . ILE   A  1 396 ? 20.337 -9.243  -36.087 1.00 22.70  ? 422  ILE   A CG1  1 
ATOM   6074  C CG2  . ILE   A  1 396 ? 22.359 -10.172 -34.837 1.00 21.55  ? 422  ILE   A CG2  1 
ATOM   6075  C CD1  . ILE   A  1 396 ? 19.926 -8.161  -35.063 1.00 24.35  ? 422  ILE   A CD1  1 
ATOM   6076  H H    . ILE   A  1 396 ? 19.330 -12.690 -36.189 0.00 24.19  ? 422  ILE   A H    1 
ATOM   6077  H HA   . ILE   A  1 396 ? 21.634 -11.249 -37.358 0.00 22.85  ? 422  ILE   A HA   1 
ATOM   6078  H HB   . ILE   A  1 396 ? 20.319 -10.847 -34.650 0.00 23.60  ? 422  ILE   A HB   1 
ATOM   6079  H HG12 . ILE   A  1 396 ? 21.056 -8.796  -36.773 0.00 24.58  ? 422  ILE   A HG12 1 
ATOM   6080  H HG13 . ILE   A  1 396 ? 19.440 -9.529  -36.633 0.00 25.13  ? 422  ILE   A HG13 1 
ATOM   6081  H HG21 . ILE   A  1 396 ? 22.335 -9.199  -34.352 0.00 22.76  ? 422  ILE   A HG21 1 
ATOM   6082  H HG22 . ILE   A  1 396 ? 22.610 -10.924 -34.090 0.00 22.97  ? 422  ILE   A HG22 1 
ATOM   6083  H HG23 . ILE   A  1 396 ? 23.106 -10.170 -35.631 0.00 22.83  ? 422  ILE   A HG23 1 
ATOM   6084  H HD11 . ILE   A  1 396 ? 19.160 -7.529  -35.512 0.00 26.81  ? 422  ILE   A HD11 1 
ATOM   6085  H HD12 . ILE   A  1 396 ? 19.538 -8.643  -34.165 0.00 26.76  ? 422  ILE   A HD12 1 
ATOM   6086  H HD13 . ILE   A  1 396 ? 20.791 -7.548  -34.817 0.00 26.31  ? 422  ILE   A HD13 1 
ATOM   6087  N N    . ILE   A  1 397 ? 22.935 -13.247 -36.659 1.00 19.29  ? 423  ILE   A N    1 
ATOM   6088  C CA   . ILE   A  1 397 ? 23.807 -14.326 -36.212 1.00 18.92  ? 423  ILE   A CA   1 
ATOM   6089  C C    . ILE   A  1 397 ? 25.112 -13.614 -35.893 1.00 19.24  ? 423  ILE   A C    1 
ATOM   6090  O O    . ILE   A  1 397 ? 25.857 -13.260 -36.806 1.00 18.79  ? 423  ILE   A O    1 
ATOM   6091  C CB   . ILE   A  1 397 ? 23.992 -15.423 -37.298 1.00 20.09  ? 423  ILE   A CB   1 
ATOM   6092  C CG1  . ILE   A  1 397 ? 22.632 -16.015 -37.744 1.00 20.76  ? 423  ILE   A CG1  1 
ATOM   6093  C CG2  . ILE   A  1 397 ? 24.937 -16.529 -36.766 1.00 20.72  ? 423  ILE   A CG2  1 
ATOM   6094  C CD1  . ILE   A  1 397 ? 22.696 -16.767 -39.086 1.00 22.49  ? 423  ILE   A CD1  1 
ATOM   6095  H H    . ILE   A  1 397 ? 23.204 -12.867 -37.561 0.00 20.81  ? 423  ILE   A H    1 
ATOM   6096  H HA   . ILE   A  1 397 ? 23.425 -14.798 -35.309 0.00 20.57  ? 423  ILE   A HA   1 
ATOM   6097  H HB   . ILE   A  1 397 ? 24.461 -14.971 -38.171 0.00 22.09  ? 423  ILE   A HB   1 
ATOM   6098  H HG12 . ILE   A  1 397 ? 22.305 -16.719 -36.980 0.00 23.72  ? 423  ILE   A HG12 1 
ATOM   6099  H HG13 . ILE   A  1 397 ? 21.895 -15.222 -37.855 0.00 23.49  ? 423  ILE   A HG13 1 
ATOM   6100  H HG21 . ILE   A  1 397 ? 24.809 -17.442 -37.344 0.00 23.39  ? 423  ILE   A HG21 1 
ATOM   6101  H HG22 . ILE   A  1 397 ? 25.964 -16.184 -36.873 0.00 22.77  ? 423  ILE   A HG22 1 
ATOM   6102  H HG23 . ILE   A  1 397 ? 24.715 -16.719 -35.716 0.00 23.04  ? 423  ILE   A HG23 1 
ATOM   6103  H HD11 . ILE   A  1 397 ? 21.680 -16.921 -39.445 0.00 26.30  ? 423  ILE   A HD11 1 
ATOM   6104  H HD12 . ILE   A  1 397 ? 23.259 -16.171 -39.804 0.00 25.76  ? 423  ILE   A HD12 1 
ATOM   6105  H HD13 . ILE   A  1 397 ? 23.179 -17.732 -38.943 0.00 26.12  ? 423  ILE   A HD13 1 
ATOM   6106  N N    . TYR   A  1 398 ? 25.337 -13.300 -34.609 1.00 18.83  ? 424  TYR   A N    1 
ATOM   6107  C CA   . TYR   A  1 398 ? 26.511 -12.550 -34.209 1.00 18.93  ? 424  TYR   A CA   1 
ATOM   6108  C C    . TYR   A  1 398 ? 27.604 -13.474 -33.664 1.00 18.13  ? 424  TYR   A C    1 
ATOM   6109  O O    . TYR   A  1 398 ? 27.446 -14.070 -32.598 1.00 17.51  ? 424  TYR   A O    1 
ATOM   6110  C CB   . TYR   A  1 398 ? 26.098 -11.444 -33.237 1.00 19.57  ? 424  TYR   A CB   1 
ATOM   6111  C CG   . TYR   A  1 398 ? 27.201 -10.481 -32.877 1.00 21.06  ? 424  TYR   A CG   1 
ATOM   6112  C CD1  . TYR   A  1 398 ? 27.432 -9.339  -33.636 1.00 22.20  ? 424  TYR   A CD1  1 
ATOM   6113  C CD2  . TYR   A  1 398 ? 27.956 -10.659 -31.727 1.00 22.17  ? 424  TYR   A CD2  1 
ATOM   6114  C CE1  . TYR   A  1 398 ? 28.418 -8.427  -33.279 1.00 23.37  ? 424  TYR   A CE1  1 
ATOM   6115  C CE2  . TYR   A  1 398 ? 28.939 -9.753  -31.362 1.00 23.22  ? 424  TYR   A CE2  1 
ATOM   6116  C CZ   . TYR   A  1 398 ? 29.132 -8.611  -32.112 1.00 24.84  ? 424  TYR   A CZ   1 
ATOM   6117  O OH   . TYR   A  1 398 ? 30.131 -7.726  -31.774 1.00 28.71  ? 424  TYR   A OH   1 
ATOM   6118  H H    . TYR   A  1 398 ? 24.730 -13.556 -33.836 0.00 19.81  ? 424  TYR   A H    1 
ATOM   6119  H HA   . TYR   A  1 398 ? 26.916 -12.038 -35.078 0.00 19.28  ? 424  TYR   A HA   1 
ATOM   6120  H HB2  . TYR   A  1 398 ? 25.310 -10.861 -33.710 0.00 20.01  ? 424  TYR   A HB2  1 
ATOM   6121  H HB3  . TYR   A  1 398 ? 25.719 -11.873 -32.314 0.00 20.08  ? 424  TYR   A HB3  1 
ATOM   6122  H HD1  . TYR   A  1 398 ? 26.846 -9.164  -34.523 0.00 22.64  ? 424  TYR   A HD1  1 
ATOM   6123  H HD2  . TYR   A  1 398 ? 27.782 -11.525 -31.111 0.00 22.79  ? 424  TYR   A HD2  1 
ATOM   6124  H HE1  . TYR   A  1 398 ? 28.585 -7.550  -33.881 0.00 23.51  ? 424  TYR   A HE1  1 
ATOM   6125  H HE2  . TYR   A  1 398 ? 29.512 -9.924  -30.464 0.00 23.54  ? 424  TYR   A HE2  1 
ATOM   6126  H HH   . TYR   A  1 398 ? 30.454 -7.893  -30.848 0.00 29.72  ? 424  TYR   A HH   1 
ATOM   6127  N N    . LEU   A  1 399 ? 28.702 -13.623 -34.440 1.00 17.46  ? 425  LEU   A N    1 
ATOM   6128  C CA   . LEU   A  1 399 ? 29.827 -14.500 -34.092 1.00 18.14  ? 425  LEU   A CA   1 
ATOM   6129  C C    . LEU   A  1 399 ? 31.161 -13.723 -34.056 1.00 19.07  ? 425  LEU   A C    1 
ATOM   6130  O O    . LEU   A  1 399 ? 32.227 -14.340 -34.196 1.00 20.11  ? 425  LEU   A O    1 
ATOM   6131  C CB   . LEU   A  1 399 ? 29.919 -15.628 -35.144 1.00 18.20  ? 425  LEU   A CB   1 
ATOM   6132  C CG   . LEU   A  1 399 ? 28.641 -16.434 -35.373 1.00 20.92  ? 425  LEU   A CG   1 
ATOM   6133  C CD1  . LEU   A  1 399 ? 28.772 -17.340 -36.594 1.00 21.24  ? 425  LEU   A CD1  1 
ATOM   6134  C CD2  . LEU   A  1 399 ? 28.256 -17.207 -34.121 1.00 22.43  ? 425  LEU   A CD2  1 
ATOM   6135  H H    . LEU   A  1 399 ? 28.839 -13.149 -35.328 0.00 17.51  ? 425  LEU   A H    1 
ATOM   6136  H HA   . LEU   A  1 399 ? 29.682 -14.955 -33.113 0.00 18.58  ? 425  LEU   A HA   1 
ATOM   6137  H HB2  . LEU   A  1 399 ? 30.185 -15.174 -36.097 0.00 18.82  ? 425  LEU   A HB2  1 
ATOM   6138  H HB3  . LEU   A  1 399 ? 30.694 -16.332 -34.844 0.00 19.02  ? 425  LEU   A HB3  1 
ATOM   6139  H HG   . LEU   A  1 399 ? 27.827 -15.743 -35.583 0.00 22.48  ? 425  LEU   A HG   1 
ATOM   6140  H HD11 . LEU   A  1 399 ? 28.026 -18.132 -36.558 0.00 23.64  ? 425  LEU   A HD11 1 
ATOM   6141  H HD12 . LEU   A  1 399 ? 28.616 -16.734 -37.484 0.00 23.20  ? 425  LEU   A HD12 1 
ATOM   6142  H HD13 . LEU   A  1 399 ? 29.777 -17.757 -36.614 0.00 23.34  ? 425  LEU   A HD13 1 
ATOM   6143  H HD21 . LEU   A  1 399 ? 27.522 -17.972 -34.367 0.00 24.94  ? 425  LEU   A HD21 1 
ATOM   6144  H HD22 . LEU   A  1 399 ? 29.143 -17.659 -33.680 0.00 24.60  ? 425  LEU   A HD22 1 
ATOM   6145  H HD23 . LEU   A  1 399 ? 27.811 -16.492 -33.432 0.00 24.40  ? 425  LEU   A HD23 1 
ATOM   6146  N N    . SER   A  1 400 ? 31.111 -12.399 -33.852 1.00 17.89  ? 426  SER   A N    1 
ATOM   6147  C CA   . SER   A  1 400 ? 32.295 -11.553 -33.852 1.00 17.91  ? 426  SER   A CA   1 
ATOM   6148  C C    . SER   A  1 400 ? 33.224 -11.939 -32.711 1.00 18.73  ? 426  SER   A C    1 
ATOM   6149  O O    . SER   A  1 400 ? 32.754 -12.318 -31.637 1.00 18.80  ? 426  SER   A O    1 
ATOM   6150  C CB   . SER   A  1 400 ? 31.899 -10.086 -33.689 1.00 17.81  ? 426  SER   A CB   1 
ATOM   6151  O OG   . SER   A  1 400 ? 33.003 -9.194  -33.666 1.00 18.08  ? 426  SER   A OG   1 
ATOM   6152  H H    . SER   A  1 400 ? 30.254 -11.891 -33.657 0.00 17.51  ? 426  SER   A H    1 
ATOM   6153  H HA   . SER   A  1 400 ? 32.820 -11.670 -34.799 0.00 17.32  ? 426  SER   A HA   1 
ATOM   6154  H HB2  . SER   A  1 400 ? 31.250 -9.810  -34.520 0.00 16.93  ? 426  SER   A HB2  1 
ATOM   6155  H HB3  . SER   A  1 400 ? 31.354 -9.979  -32.753 0.00 16.90  ? 426  SER   A HB3  1 
ATOM   6156  H HG   . SER   A  1 400 ? 33.768 -9.567  -34.179 0.00 17.02  ? 426  SER   A HG   1 
ATOM   6157  N N    . GLU   A  1 401 ? 34.528 -11.858 -32.957 1.00 18.16  ? 427  GLU   A N    1 
ATOM   6158  C CA   . GLU   A  1 401 ? 35.546 -12.083 -31.938 1.00 18.50  ? 427  GLU   A CA   1 
ATOM   6159  C C    . GLU   A  1 401 ? 35.591 -13.514 -31.433 1.00 19.36  ? 427  GLU   A C    1 
ATOM   6160  O O    . GLU   A  1 401 ? 35.341 -13.794 -30.261 1.00 20.04  ? 427  GLU   A O    1 
ATOM   6161  C CB   . GLU   A  1 401 ? 35.368 -11.078 -30.787 1.00 20.51  ? 427  GLU   A CB   1 
ATOM   6162  C CG   . GLU   A  1 401 ? 36.599 -10.919 -29.913 1.00 23.37  ? 427  GLU   A CG   1 
ATOM   6163  C CD   . GLU   A  1 401 ? 37.786 -10.365 -30.680 1.00 26.30  ? 427  GLU   A CD   1 
ATOM   6164  O OE1  . GLU   A  1 401 ? 38.678 -11.153 -31.065 1.00 29.82  ? 427  GLU   A OE1  1 
ATOM   6165  O OE2  . GLU   A  1 401 ? 37.819 -9.137  -30.905 1.00 26.41  ? 427  GLU   A OE2  1 
ATOM   6166  H H    . GLU   A  1 401 ? 34.920 -11.631 -33.866 0.00 17.49  ? 427  GLU   A H    1 
ATOM   6167  H HA   . GLU   A  1 401 ? 36.505 -11.901 -32.422 0.00 17.93  ? 427  GLU   A HA   1 
ATOM   6168  H HB2  . GLU   A  1 401 ? 35.153 -10.102 -31.220 0.00 19.97  ? 427  GLU   A HB2  1 
ATOM   6169  H HB3  . GLU   A  1 401 ? 34.536 -11.381 -30.153 0.00 20.26  ? 427  GLU   A HB3  1 
ATOM   6170  H HG2  . GLU   A  1 401 ? 36.364 -10.215 -29.115 0.00 23.48  ? 427  GLU   A HG2  1 
ATOM   6171  H HG3  . GLU   A  1 401 ? 36.882 -11.881 -29.489 0.00 23.82  ? 427  GLU   A HG3  1 
ATOM   6172  N N    . ASN   A  1 402 ? 35.926 -14.418 -32.323 1.00 18.66  ? 428  ASN   A N    1 
ATOM   6173  C CA   . ASN   A  1 402 ? 36.099 -15.831 -31.996 1.00 19.22  ? 428  ASN   A CA   1 
ATOM   6174  C C    . ASN   A  1 402 ? 37.423 -16.272 -32.683 1.00 20.69  ? 428  ASN   A C    1 
ATOM   6175  O O    . ASN   A  1 402 ? 38.280 -15.409 -32.926 1.00 21.00  ? 428  ASN   A O    1 
ATOM   6176  C CB   . ASN   A  1 402 ? 34.809 -16.608 -32.427 1.00 18.85  ? 428  ASN   A CB   1 
ATOM   6177  C CG   . ASN   A  1 402 ? 33.742 -16.539 -31.353 1.00 18.08  ? 428  ASN   A CG   1 
ATOM   6178  O OD1  . ASN   A  1 402 ? 33.944 -17.048 -30.245 1.00 17.31  ? 428  ASN   A OD1  1 
ATOM   6179  N ND2  . ASN   A  1 402 ? 32.628 -15.884 -31.638 1.00 17.47  ? 428  ASN   A ND2  1 
ATOM   6180  H H    . ASN   A  1 402 ? 36.099 -14.206 -33.300 0.00 18.69  ? 428  ASN   A H    1 
ATOM   6181  H HA   . ASN   A  1 402 ? 36.265 -15.960 -30.927 0.00 19.85  ? 428  ASN   A HA   1 
ATOM   6182  H HB2  . ASN   A  1 402 ? 34.423 -16.162 -33.343 0.00 19.49  ? 428  ASN   A HB2  1 
ATOM   6183  H HB3  . ASN   A  1 402 ? 35.011 -17.664 -32.594 0.00 19.94  ? 428  ASN   A HB3  1 
ATOM   6184  H HD21 . ASN   A  1 402 ? 31.891 -15.819 -30.943 0.00 17.80  ? 428  ASN   A HD21 1 
ATOM   6185  H HD22 . ASN   A  1 402 ? 32.497 -15.445 -32.545 0.00 17.68  ? 428  ASN   A HD22 1 
ATOM   6186  N N    . ARG   A  1 403 ? 37.622 -17.571 -32.935 1.00 21.38  ? 429  ARG   A N    1 
ATOM   6187  C CA   . ARG   A  1 403 ? 38.810 -18.113 -33.610 1.00 22.41  ? 429  ARG   A CA   1 
ATOM   6188  C C    . ARG   A  1 403 ? 38.375 -18.916 -34.844 1.00 22.01  ? 429  ARG   A C    1 
ATOM   6189  O O    . ARG   A  1 403 ? 38.968 -19.949 -35.148 1.00 21.35  ? 429  ARG   A O    1 
ATOM   6190  C CB   . ARG   A  1 403 ? 39.580 -19.034 -32.644 1.00 23.81  ? 429  ARG   A CB   1 
ATOM   6191  C CG   . ARG   A  1 403 ? 39.936 -18.397 -31.334 1.00 29.59  ? 429  ARG   A CG   1 
ATOM   6192  C CD   . ARG   A  1 403 ? 41.036 -17.367 -31.442 1.00 35.61  ? 429  ARG   A CD   1 
ATOM   6193  N NE   . ARG   A  1 403 ? 42.329 -17.968 -31.786 1.00 40.45  ? 429  ARG   A NE   1 
ATOM   6194  C CZ   . ARG   A  1 403 ? 43.489 -17.324 -31.749 1.00 42.83  ? 429  ARG   A CZ   1 
ATOM   6195  N NH1  . ARG   A  1 403 ? 44.615 -17.954 -32.070 1.00 42.53  ? 429  ARG   A NH1  1 
ATOM   6196  N NH2  . ARG   A  1 403 ? 43.540 -16.051 -31.365 1.00 42.48  ? 429  ARG   A NH2  1 
ATOM   6197  H H    . ARG   A  1 403 ? 36.997 -18.314 -32.642 0.00 23.21  ? 429  ARG   A H    1 
ATOM   6198  H HA   . ARG   A  1 403 ? 39.473 -17.319 -33.953 0.00 24.24  ? 429  ARG   A HA   1 
ATOM   6199  H HB2  . ARG   A  1 403 ? 38.960 -19.903 -32.428 0.00 26.77  ? 429  ARG   A HB2  1 
ATOM   6200  H HB3  . ARG   A  1 403 ? 40.503 -19.356 -33.125 0.00 26.69  ? 429  ARG   A HB3  1 
ATOM   6201  H HG2  . ARG   A  1 403 ? 39.066 -17.881 -30.935 0.00 33.01  ? 429  ARG   A HG2  1 
ATOM   6202  H HG3  . ARG   A  1 403 ? 40.263 -19.169 -30.639 0.00 33.56  ? 429  ARG   A HG3  1 
ATOM   6203  H HD2  . ARG   A  1 403 ? 40.790 -16.623 -32.197 0.00 39.95  ? 429  ARG   A HD2  1 
ATOM   6204  H HD3  . ARG   A  1 403 ? 41.141 -16.882 -30.472 0.00 40.10  ? 429  ARG   A HD3  1 
ATOM   6205  H HE   . ARG   A  1 403 ? 42.337 -18.941 -32.073 0.00 46.71  ? 429  ARG   A HE   1 
ATOM   6206  H HH11 . ARG   A  1 403 ? 44.594 -18.927 -32.358 0.00 49.50  ? 429  ARG   A HH11 1 
ATOM   6207  H HH12 . ARG   A  1 403 ? 45.503 -17.464 -32.037 0.00 49.13  ? 429  ARG   A HH12 1 
ATOM   6208  H HH21 . ARG   A  1 403 ? 42.706 -15.533 -31.109 0.00 48.07  ? 429  ARG   A HH21 1 
ATOM   6209  H HH22 . ARG   A  1 403 ? 44.436 -15.575 -31.335 0.00 48.31  ? 429  ARG   A HH22 1 
ATOM   6210  N N    . ILE   A  1 404 ? 37.314 -18.465 -35.538 1.00 21.91  ? 430  ILE   A N    1 
ATOM   6211  C CA   . ILE   A  1 404 ? 36.794 -19.196 -36.678 1.00 23.05  ? 430  ILE   A CA   1 
ATOM   6212  C C    . ILE   A  1 404 ? 37.811 -19.065 -37.806 1.00 24.51  ? 430  ILE   A C    1 
ATOM   6213  O O    . ILE   A  1 404 ? 38.298 -17.972 -38.089 1.00 24.30  ? 430  ILE   A O    1 
ATOM   6214  C CB   . ILE   A  1 404 ? 35.379 -18.712 -37.053 1.00 23.75  ? 430  ILE   A CB   1 
ATOM   6215  C CG1  . ILE   A  1 404 ? 34.391 -19.017 -35.885 1.00 24.71  ? 430  ILE   A CG1  1 
ATOM   6216  C CG2  . ILE   A  1 404 ? 34.918 -19.385 -38.350 1.00 24.10  ? 430  ILE   A CG2  1 
ATOM   6217  C CD1  . ILE   A  1 404 ? 33.116 -18.123 -35.887 1.00 25.60  ? 430  ILE   A CD1  1 
ATOM   6218  H H    . ILE   A  1 404 ? 36.822 -17.598 -35.348 0.00 23.68  ? 430  ILE   A H    1 
ATOM   6219  H HA   . ILE   A  1 404 ? 36.704 -20.247 -36.406 0.00 26.03  ? 430  ILE   A HA   1 
ATOM   6220  H HB   . ILE   A  1 404 ? 35.406 -17.635 -37.217 0.00 25.99  ? 430  ILE   A HB   1 
ATOM   6221  H HG12 . ILE   A  1 404 ? 34.064 -20.052 -35.970 0.00 27.94  ? 430  ILE   A HG12 1 
ATOM   6222  H HG13 . ILE   A  1 404 ? 34.887 -18.869 -34.927 0.00 27.45  ? 430  ILE   A HG13 1 
ATOM   6223  H HG21 . ILE   A  1 404 ? 33.838 -19.275 -38.438 0.00 27.12  ? 430  ILE   A HG21 1 
ATOM   6224  H HG22 . ILE   A  1 404 ? 35.399 -18.909 -39.202 0.00 27.02  ? 430  ILE   A HG22 1 
ATOM   6225  H HG23 . ILE   A  1 404 ? 35.182 -20.441 -38.315 0.00 27.51  ? 430  ILE   A HG23 1 
ATOM   6226  H HD11 . ILE   A  1 404 ? 32.584 -18.262 -34.948 0.00 28.39  ? 430  ILE   A HD11 1 
ATOM   6227  H HD12 . ILE   A  1 404 ? 33.415 -17.081 -35.995 0.00 28.02  ? 430  ILE   A HD12 1 
ATOM   6228  H HD13 . ILE   A  1 404 ? 32.480 -18.415 -36.721 0.00 28.55  ? 430  ILE   A HD13 1 
ATOM   6229  N N    . SER   A  1 405 ? 38.209 -20.191 -38.353 1.00 25.55  ? 431  SER   A N    1 
ATOM   6230  C CA   . SER   A  1 405 ? 39.224 -20.236 -39.392 1.00 27.85  ? 431  SER   A CA   1 
ATOM   6231  C C    . SER   A  1 405 ? 38.614 -20.811 -40.685 1.00 29.59  ? 431  SER   A C    1 
ATOM   6232  O O    . SER   A  1 405 ? 37.453 -21.214 -40.668 1.00 29.89  ? 431  SER   A O    1 
ATOM   6233  C CB   . SER   A  1 405 ? 40.400 -21.061 -38.872 1.00 29.37  ? 431  SER   A CB   1 
ATOM   6234  O OG   . SER   A  1 405 ? 40.017 -22.418 -38.757 1.00 32.38  ? 431  SER   A OG   1 
ATOM   6235  H H    . SER   A  1 405 ? 37.850 -21.109 -38.112 0.00 29.52  ? 431  SER   A H    1 
ATOM   6236  H HA   . SER   A  1 405 ? 39.598 -19.239 -39.620 0.00 31.75  ? 431  SER   A HA   1 
ATOM   6237  H HB2  . SER   A  1 405 ? 41.259 -20.969 -39.534 0.00 34.34  ? 431  SER   A HB2  1 
ATOM   6238  H HB3  . SER   A  1 405 ? 40.666 -20.694 -37.882 0.00 34.06  ? 431  SER   A HB3  1 
ATOM   6239  H HG   . SER   A  1 405 ? 39.493 -22.557 -37.925 0.00 38.37  ? 431  SER   A HG   1 
ATOM   6240  N N    . PRO   A  1 406 ? 39.329 -20.801 -41.829 1.00 31.07  ? 432  PRO   A N    1 
ATOM   6241  C CA   . PRO   A  1 406 ? 38.744 -21.346 -43.067 1.00 33.05  ? 432  PRO   A CA   1 
ATOM   6242  C C    . PRO   A  1 406 ? 38.151 -22.760 -42.927 1.00 35.98  ? 432  PRO   A C    1 
ATOM   6243  O O    . PRO   A  1 406 ? 38.771 -23.647 -42.347 1.00 36.31  ? 432  PRO   A O    1 
ATOM   6244  C CB   . PRO   A  1 406 ? 39.912 -21.282 -44.060 1.00 33.12  ? 432  PRO   A CB   1 
ATOM   6245  C CG   . PRO   A  1 406 ? 40.774 -20.155 -43.537 1.00 32.57  ? 432  PRO   A CG   1 
ATOM   6246  C CD   . PRO   A  1 406 ? 40.712 -20.335 -42.055 1.00 30.51  ? 432  PRO   A CD   1 
ATOM   6247  H HA   . PRO   A  1 406 ? 37.966 -20.668 -43.416 0.00 38.94  ? 432  PRO   A HA   1 
ATOM   6248  H HB2  . PRO   A  1 406 ? 40.457 -22.225 -44.054 0.00 39.84  ? 432  PRO   A HB2  1 
ATOM   6249  H HB3  . PRO   A  1 406 ? 39.538 -21.054 -45.056 0.00 39.47  ? 432  PRO   A HB3  1 
ATOM   6250  H HG2  . PRO   A  1 406 ? 41.794 -20.254 -43.907 0.00 38.43  ? 432  PRO   A HG2  1 
ATOM   6251  H HG3  . PRO   A  1 406 ? 40.337 -19.200 -43.822 0.00 37.92  ? 432  PRO   A HG3  1 
ATOM   6252  H HD2  . PRO   A  1 406 ? 41.429 -21.106 -41.778 0.00 36.01  ? 432  PRO   A HD2  1 
ATOM   6253  H HD3  . PRO   A  1 406 ? 40.903 -19.392 -41.545 0.00 35.28  ? 432  PRO   A HD3  1 
ATOM   6254  N N    . LEU   A  1 407 ? 36.925 -22.947 -43.439 1.00 37.78  ? 433  LEU   A N    1 
ATOM   6255  C CA   . LEU   A  1 407 ? 36.192 -24.208 -43.343 1.00 40.25  ? 433  LEU   A CA   1 
ATOM   6256  C C    . LEU   A  1 407 ? 36.933 -25.351 -44.048 1.00 41.74  ? 433  LEU   A C    1 
ATOM   6257  O O    . LEU   A  1 407 ? 37.572 -25.136 -45.078 1.00 42.50  ? 433  LEU   A O    1 
ATOM   6258  C CB   . LEU   A  1 407 ? 34.783 -24.031 -43.942 1.00 41.17  ? 433  LEU   A CB   1 
ATOM   6259  C CG   . LEU   A  1 407 ? 33.743 -25.098 -43.595 1.00 43.82  ? 433  LEU   A CG   1 
ATOM   6260  C CD1  . LEU   A  1 407 ? 32.351 -24.557 -43.801 1.00 44.63  ? 433  LEU   A CD1  1 
ATOM   6261  C CD2  . LEU   A  1 407 ? 33.931 -26.359 -44.438 1.00 44.97  ? 433  LEU   A CD2  1 
ATOM   6262  H H    . LEU   A  1 407 ? 36.438 -22.233 -43.971 0.00 45.35  ? 433  LEU   A H    1 
ATOM   6263  H HA   . LEU   A  1 407 ? 36.083 -24.472 -42.292 0.00 49.04  ? 433  LEU   A HA   1 
ATOM   6264  H HB2  . LEU   A  1 407 ? 34.379 -23.081 -43.595 0.00 49.76  ? 433  LEU   A HB2  1 
ATOM   6265  H HB3  . LEU   A  1 407 ? 34.876 -24.006 -45.027 0.00 50.39  ? 433  LEU   A HB3  1 
ATOM   6266  H HG   . LEU   A  1 407 ? 33.840 -25.375 -42.546 0.00 53.83  ? 433  LEU   A HG   1 
ATOM   6267  H HD11 . LEU   A  1 407 ? 31.631 -25.352 -43.619 0.00 55.10  ? 433  LEU   A HD11 1 
ATOM   6268  H HD12 . LEU   A  1 407 ? 32.179 -23.741 -43.101 0.00 54.24  ? 433  LEU   A HD12 1 
ATOM   6269  H HD13 . LEU   A  1 407 ? 32.260 -24.197 -44.825 0.00 54.72  ? 433  LEU   A HD13 1 
ATOM   6270  H HD21 . LEU   A  1 407 ? 33.158 -27.079 -44.175 0.00 56.34  ? 433  LEU   A HD21 1 
ATOM   6271  H HD22 . LEU   A  1 407 ? 33.851 -26.099 -45.492 0.00 56.06  ? 433  LEU   A HD22 1 
ATOM   6272  H HD23 . LEU   A  1 407 ? 34.913 -26.783 -44.231 0.00 56.13  ? 433  LEU   A HD23 1 
ATOM   6273  N N    . PHE   A  1 433 ? 35.374 10.348  -14.398 1.00 39.61  ? 459  PHE   A N    1 
ATOM   6274  C CA   . PHE   A  1 433 ? 34.949 8.958   -14.202 1.00 39.37  ? 459  PHE   A CA   1 
ATOM   6275  C C    . PHE   A  1 433 ? 35.032 8.115   -15.498 1.00 37.92  ? 459  PHE   A C    1 
ATOM   6276  O O    . PHE   A  1 433 ? 34.847 8.644   -16.586 1.00 38.72  ? 459  PHE   A O    1 
ATOM   6277  C CB   . PHE   A  1 433 ? 33.544 8.887   -13.571 1.00 39.74  ? 459  PHE   A CB   1 
ATOM   6278  C CG   . PHE   A  1 433 ? 32.514 9.868   -14.074 1.00 40.65  ? 459  PHE   A CG   1 
ATOM   6279  C CD1  . PHE   A  1 433 ? 31.719 9.564   -15.165 1.00 41.73  ? 459  PHE   A CD1  1 
ATOM   6280  C CD2  . PHE   A  1 433 ? 32.262 11.040  -13.388 1.00 41.49  ? 459  PHE   A CD2  1 
ATOM   6281  C CE1  . PHE   A  1 433 ? 30.736 10.441  -15.597 1.00 42.50  ? 459  PHE   A CE1  1 
ATOM   6282  C CE2  . PHE   A  1 433 ? 31.264 11.904  -13.809 1.00 42.31  ? 459  PHE   A CE2  1 
ATOM   6283  C CZ   . PHE   A  1 433 ? 30.500 11.594  -14.904 1.00 42.21  ? 459  PHE   A CZ   1 
ATOM   6284  H HA   . PHE   A  1 433 ? 35.621 8.514   -13.471 0.00 44.66  ? 459  PHE   A HA   1 
ATOM   6285  H HB2  . PHE   A  1 433 ? 33.145 7.889   -13.747 0.00 44.97  ? 459  PHE   A HB2  1 
ATOM   6286  H HB3  . PHE   A  1 433 ? 33.647 9.045   -12.499 0.00 45.46  ? 459  PHE   A HB3  1 
ATOM   6287  H HD1  . PHE   A  1 433 ? 31.883 8.652   -15.706 0.00 47.08  ? 459  PHE   A HD1  1 
ATOM   6288  H HD2  . PHE   A  1 433 ? 32.844 11.281  -12.513 0.00 48.01  ? 459  PHE   A HD2  1 
ATOM   6289  H HE1  . PHE   A  1 433 ? 30.139 10.205  -16.458 0.00 48.25  ? 459  PHE   A HE1  1 
ATOM   6290  H HE2  . PHE   A  1 433 ? 31.092 12.823  -13.283 0.00 49.23  ? 459  PHE   A HE2  1 
ATOM   6291  H HZ   . PHE   A  1 433 ? 29.746 12.278  -15.250 0.00 48.63  ? 459  PHE   A HZ   1 
ATOM   6292  N N    . GLU   A  1 434 ? 35.286 6.803   -15.365 1.00 35.69  ? 460  GLU   A N    1 
ATOM   6293  C CA   . GLU   A  1 434 ? 35.440 5.861   -16.491 1.00 33.67  ? 460  GLU   A CA   1 
ATOM   6294  C C    . GLU   A  1 434 ? 34.125 5.294   -17.059 1.00 31.50  ? 460  GLU   A C    1 
ATOM   6295  O O    . GLU   A  1 434 ? 34.073 4.964   -18.242 1.00 31.13  ? 460  GLU   A O    1 
ATOM   6296  C CB   . GLU   A  1 434 ? 36.315 4.680   -16.019 1.00 34.24  ? 460  GLU   A CB   1 
ATOM   6297  C CG   . GLU   A  1 434 ? 36.515 3.555   -17.027 1.00 36.89  ? 460  GLU   A CG   1 
ATOM   6298  C CD   . GLU   A  1 434 ? 37.244 2.335   -16.498 1.00 39.40  ? 460  GLU   A CD   1 
ATOM   6299  O OE1  . GLU   A  1 434 ? 37.322 1.324   -17.238 1.00 40.83  ? 460  GLU   A OE1  1 
ATOM   6300  O OE2  . GLU   A  1 434 ? 37.725 2.381   -15.342 1.00 37.77  ? 460  GLU   A OE2  1 
ATOM   6301  H H    . GLU   A  1 434 ? 35.388 6.358   -14.459 0.00 39.71  ? 460  GLU   A H    1 
ATOM   6302  H HA   . GLU   A  1 434 ? 35.967 6.358   -17.304 0.00 36.65  ? 460  GLU   A HA   1 
ATOM   6303  H HB2  . GLU   A  1 434 ? 37.300 5.062   -15.755 0.00 37.57  ? 460  GLU   A HB2  1 
ATOM   6304  H HB3  . GLU   A  1 434 ? 35.848 4.236   -15.141 0.00 37.59  ? 460  GLU   A HB3  1 
ATOM   6305  H HG2  . GLU   A  1 434 ? 35.550 3.188   -17.375 0.00 40.23  ? 460  GLU   A HG2  1 
ATOM   6306  H HG3  . GLU   A  1 434 ? 37.081 3.941   -17.873 0.00 40.21  ? 460  GLU   A HG3  1 
ATOM   6307  N N    . PHE   A  1 435 ? 33.130 5.042   -16.198 1.00 29.50  ? 461  PHE   A N    1 
ATOM   6308  C CA   . PHE   A  1 435 ? 31.877 4.407   -16.595 1.00 28.00  ? 461  PHE   A CA   1 
ATOM   6309  C C    . PHE   A  1 435 ? 30.746 5.412   -16.678 1.00 27.26  ? 461  PHE   A C    1 
ATOM   6310  O O    . PHE   A  1 435 ? 30.525 6.172   -15.734 1.00 27.57  ? 461  PHE   A O    1 
ATOM   6311  C CB   . PHE   A  1 435 ? 31.531 3.291   -15.583 1.00 27.36  ? 461  PHE   A CB   1 
ATOM   6312  C CG   . PHE   A  1 435 ? 32.592 2.217   -15.531 1.00 27.02  ? 461  PHE   A CG   1 
ATOM   6313  C CD1  . PHE   A  1 435 ? 32.628 1.210   -16.478 1.00 27.61  ? 461  PHE   A CD1  1 
ATOM   6314  C CD2  . PHE   A  1 435 ? 33.581 2.243   -14.565 1.00 27.62  ? 461  PHE   A CD2  1 
ATOM   6315  C CE1  . PHE   A  1 435 ? 33.621 0.241   -16.447 1.00 28.16  ? 461  PHE   A CE1  1 
ATOM   6316  C CE2  . PHE   A  1 435 ? 34.569 1.272   -14.535 1.00 28.29  ? 461  PHE   A CE2  1 
ATOM   6317  C CZ   . PHE   A  1 435 ? 34.583 0.277   -15.476 1.00 27.79  ? 461  PHE   A CZ   1 
ATOM   6318  H H    . PHE   A  1 435 ? 33.164 5.262   -15.207 0.00 32.00  ? 461  PHE   A H    1 
ATOM   6319  H HA   . PHE   A  1 435 ? 31.989 3.929   -17.566 0.00 29.64  ? 461  PHE   A HA   1 
ATOM   6320  H HB2  . PHE   A  1 435 ? 31.435 3.726   -14.589 0.00 29.50  ? 461  PHE   A HB2  1 
ATOM   6321  H HB3  . PHE   A  1 435 ? 30.592 2.826   -15.878 0.00 29.21  ? 461  PHE   A HB3  1 
ATOM   6322  H HD1  . PHE   A  1 435 ? 31.879 1.177   -17.250 0.00 29.09  ? 461  PHE   A HD1  1 
ATOM   6323  H HD2  . PHE   A  1 435 ? 33.581 3.023   -13.821 0.00 29.87  ? 461  PHE   A HD2  1 
ATOM   6324  H HE1  . PHE   A  1 435 ? 33.630 -0.543  -17.186 0.00 29.68  ? 461  PHE   A HE1  1 
ATOM   6325  H HE2  . PHE   A  1 435 ? 35.325 1.300   -13.768 0.00 30.60  ? 461  PHE   A HE2  1 
ATOM   6326  H HZ   . PHE   A  1 435 ? 35.348 -0.478  -15.448 0.00 29.60  ? 461  PHE   A HZ   1 
ATOM   6327  N N    . ASP   A  1 436 ? 30.019 5.408   -17.795 1.00 25.76  ? 462  ASP   A N    1 
ATOM   6328  C CA   . ASP   A  1 436 ? 28.900 6.310   -17.998 1.00 25.04  ? 462  ASP   A CA   1 
ATOM   6329  C C    . ASP   A  1 436 ? 27.776 5.875   -17.044 1.00 24.50  ? 462  ASP   A C    1 
ATOM   6330  O O    . ASP   A  1 436 ? 27.251 4.774   -17.196 1.00 24.09  ? 462  ASP   A O    1 
ATOM   6331  C CB   . ASP   A  1 436 ? 28.431 6.241   -19.458 1.00 26.38  ? 462  ASP   A CB   1 
ATOM   6332  C CG   . ASP   A  1 436 ? 27.233 7.105   -19.801 1.00 30.60  ? 462  ASP   A CG   1 
ATOM   6333  O OD1  . ASP   A  1 436 ? 26.722 7.810   -18.901 1.00 29.28  ? 462  ASP   A OD1  1 
ATOM   6334  O OD2  . ASP   A  1 436 ? 26.802 7.075   -20.970 1.00 34.12  ? 462  ASP   A OD2  1 
ATOM   6335  H H    . ASP   A  1 436 ? 30.185 4.783   -18.577 0.00 26.98  ? 462  ASP   A H    1 
ATOM   6336  H HA   . ASP   A  1 436 ? 29.220 7.331   -17.799 0.00 26.65  ? 462  ASP   A HA   1 
ATOM   6337  H HB2  . ASP   A  1 436 ? 29.254 6.558   -20.097 0.00 27.76  ? 462  ASP   A HB2  1 
ATOM   6338  H HB3  . ASP   A  1 436 ? 28.168 5.212   -19.693 0.00 27.79  ? 462  ASP   A HB3  1 
ATOM   6339  N N    . PRO   A  1 437 ? 27.381 6.719   -16.073 1.00 24.25  ? 463  PRO   A N    1 
ATOM   6340  C CA   . PRO   A  1 437 ? 26.323 6.293   -15.135 1.00 24.47  ? 463  PRO   A CA   1 
ATOM   6341  C C    . PRO   A  1 437 ? 24.935 6.123   -15.741 1.00 23.69  ? 463  PRO   A C    1 
ATOM   6342  O O    . PRO   A  1 437 ? 24.080 5.533   -15.088 1.00 23.39  ? 463  PRO   A O    1 
ATOM   6343  C CB   . PRO   A  1 437 ? 26.328 7.373   -14.050 1.00 25.59  ? 463  PRO   A CB   1 
ATOM   6344  C CG   . PRO   A  1 437 ? 27.033 8.527   -14.622 1.00 26.12  ? 463  PRO   A CG   1 
ATOM   6345  C CD   . PRO   A  1 437 ? 27.906 8.058   -15.747 1.00 24.05  ? 463  PRO   A CD   1 
ATOM   6346  H HA   . PRO   A  1 437 ? 26.610 5.352   -14.669 0.00 26.63  ? 463  PRO   A HA   1 
ATOM   6347  H HB2  . PRO   A  1 437 ? 25.293 7.616   -13.816 0.00 28.66  ? 463  PRO   A HB2  1 
ATOM   6348  H HB3  . PRO   A  1 437 ? 26.846 7.003   -13.166 0.00 28.48  ? 463  PRO   A HB3  1 
ATOM   6349  H HG2  . PRO   A  1 437 ? 26.300 9.242   -14.992 0.00 29.17  ? 463  PRO   A HG2  1 
ATOM   6350  H HG3  . PRO   A  1 437 ? 27.643 8.989   -13.847 0.00 29.21  ? 463  PRO   A HG3  1 
ATOM   6351  H HD2  . PRO   A  1 437 ? 27.799 8.725   -16.602 0.00 26.07  ? 463  PRO   A HD2  1 
ATOM   6352  H HD3  . PRO   A  1 437 ? 28.942 7.991   -15.421 0.00 26.06  ? 463  PRO   A HD3  1 
ATOM   6353  N N    . HIS   A  1 438 ? 24.701 6.632   -16.974 1.00 23.44  ? 464  HIS   A N    1 
ATOM   6354  C CA   . HIS   A  1 438 ? 23.426 6.494   -17.666 1.00 24.12  ? 464  HIS   A CA   1 
ATOM   6355  C C    . HIS   A  1 438 ? 23.407 5.312   -18.663 1.00 25.16  ? 464  HIS   A C    1 
ATOM   6356  O O    . HIS   A  1 438 ? 22.432 5.183   -19.406 1.00 25.41  ? 464  HIS   A O    1 
ATOM   6357  C CB   . HIS   A  1 438 ? 23.082 7.814   -18.378 1.00 25.33  ? 464  HIS   A CB   1 
ATOM   6358  C CG   . HIS   A  1 438 ? 23.005 8.965   -17.429 1.00 28.22  ? 464  HIS   A CG   1 
ATOM   6359  N ND1  . HIS   A  1 438 ? 21.902 9.156   -16.624 1.00 30.28  ? 464  HIS   A ND1  1 
ATOM   6360  C CD2  . HIS   A  1 438 ? 23.929 9.905   -17.134 1.00 29.55  ? 464  HIS   A CD2  1 
ATOM   6361  C CE1  . HIS   A  1 438 ? 22.168 10.223  -15.892 1.00 30.91  ? 464  HIS   A CE1  1 
ATOM   6362  N NE2  . HIS   A  1 438 ? 23.377 10.709  -16.171 1.00 30.79  ? 464  HIS   A NE2  1 
ATOM   6363  H H    . HIS   A  1 438 ? 25.379 7.156   -17.519 0.00 25.27  ? 464  HIS   A H    1 
ATOM   6364  H HA   . HIS   A  1 438 ? 22.633 6.316   -16.942 0.00 26.57  ? 464  HIS   A HA   1 
ATOM   6365  H HB2  . HIS   A  1 438 ? 23.850 8.034   -19.118 0.00 27.70  ? 464  HIS   A HB2  1 
ATOM   6366  H HB3  . HIS   A  1 438 ? 22.111 7.725   -18.864 0.00 28.05  ? 464  HIS   A HB3  1 
ATOM   6367  H HD2  . HIS   A  1 438 ? 24.910 10.005  -17.573 0.00 33.17  ? 464  HIS   A HD2  1 
ATOM   6368  H HE1  . HIS   A  1 438 ? 21.494 10.640  -15.162 0.00 36.07  ? 464  HIS   A HE1  1 
ATOM   6369  H HE2  . HIS   A  1 438 ? 23.808 11.526  -15.755 0.00 35.52  ? 464  HIS   A HE2  1 
ATOM   6370  N N    . SER   A  1 439 ? 24.453 4.460   -18.679 1.00 25.65  ? 465  SER   A N    1 
ATOM   6371  C CA   . SER   A  1 439 ? 24.555 3.291   -19.564 1.00 26.76  ? 465  SER   A CA   1 
ATOM   6372  C C    . SER   A  1 439 ? 24.501 1.985   -18.745 1.00 25.63  ? 465  SER   A C    1 
ATOM   6373  O O    . SER   A  1 439 ? 24.622 1.993   -17.518 1.00 25.17  ? 465  SER   A O    1 
ATOM   6374  C CB   . SER   A  1 439 ? 25.884 3.320   -20.334 1.00 30.72  ? 465  SER   A CB   1 
ATOM   6375  O OG   . SER   A  1 439 ? 25.948 4.375   -21.280 1.00 36.57  ? 465  SER   A OG   1 
ATOM   6376  H H    . SER   A  1 439 ? 25.265 4.539   -18.076 0.00 27.52  ? 465  SER   A H    1 
ATOM   6377  H HA   . SER   A  1 439 ? 23.744 3.276   -20.290 0.00 28.69  ? 465  SER   A HA   1 
ATOM   6378  H HB2  . SER   A  1 439 ? 26.699 3.428   -19.620 0.00 33.05  ? 465  SER   A HB2  1 
ATOM   6379  H HB3  . SER   A  1 439 ? 26.004 2.381   -20.870 0.00 32.91  ? 465  SER   A HB3  1 
ATOM   6380  H HG   . SER   A  1 439 ? 26.834 4.377   -21.728 0.00 39.84  ? 465  SER   A HG   1 
ATOM   6381  N N    . ASN   A  1 440 ? 24.364 0.860   -19.448 1.00 25.04  ? 466  ASN   A N    1 
ATOM   6382  C CA   . ASN   A  1 440 ? 24.388 -0.462  -18.844 1.00 24.56  ? 466  ASN   A CA   1 
ATOM   6383  C C    . ASN   A  1 440 ? 25.854 -0.742  -18.496 1.00 24.63  ? 466  ASN   A C    1 
ATOM   6384  O O    . ASN   A  1 440 ? 26.735 -0.594  -19.349 1.00 24.80  ? 466  ASN   A O    1 
ATOM   6385  C CB   . ASN   A  1 440 ? 23.868 -1.490  -19.841 1.00 24.68  ? 466  ASN   A CB   1 
ATOM   6386  C CG   . ASN   A  1 440 ? 23.508 -2.810  -19.213 1.00 24.07  ? 466  ASN   A CG   1 
ATOM   6387  O OD1  . ASN   A  1 440 ? 24.374 -3.554  -18.739 1.00 23.09  ? 466  ASN   A OD1  1 
ATOM   6388  N ND2  . ASN   A  1 440 ? 22.218 -3.135  -19.204 1.00 24.44  ? 466  ASN   A ND2  1 
ATOM   6389  H H    . ASN   A  1 440 ? 24.247 0.846   -20.456 0.00 26.37  ? 466  ASN   A H    1 
ATOM   6390  H HA   . ASN   A  1 440 ? 23.774 -0.488  -17.946 0.00 26.19  ? 466  ASN   A HA   1 
ATOM   6391  H HB2  . ASN   A  1 440 ? 22.986 -1.085  -20.336 0.00 26.16  ? 466  ASN   A HB2  1 
ATOM   6392  H HB3  . ASN   A  1 440 ? 24.641 -1.680  -20.585 0.00 25.82  ? 466  ASN   A HB3  1 
ATOM   6393  H HD21 . ASN   A  1 440 ? 21.930 -4.015  -18.791 0.00 26.33  ? 466  ASN   A HD21 1 
ATOM   6394  H HD22 . ASN   A  1 440 ? 21.517 -2.516  -19.599 0.00 26.27  ? 466  ASN   A HD22 1 
ATOM   6395  N N    . PHE   A  1 441 ? 26.116 -1.117  -17.250 1.00 23.68  ? 467  PHE   A N    1 
ATOM   6396  C CA   . PHE   A  1 441 ? 27.470 -1.387  -16.772 1.00 23.36  ? 467  PHE   A CA   1 
ATOM   6397  C C    . PHE   A  1 441 ? 28.032 -2.723  -17.258 1.00 23.63  ? 467  PHE   A C    1 
ATOM   6398  O O    . PHE   A  1 441 ? 29.249 -2.833  -17.392 1.00 24.47  ? 467  PHE   A O    1 
ATOM   6399  C CB   . PHE   A  1 441 ? 27.467 -1.373  -15.226 1.00 22.96  ? 467  PHE   A CB   1 
ATOM   6400  C CG   . PHE   A  1 441 ? 28.809 -1.528  -14.546 1.00 23.27  ? 467  PHE   A CG   1 
ATOM   6401  C CD1  . PHE   A  1 441 ? 29.719 -0.486  -14.533 1.00 23.69  ? 467  PHE   A CD1  1 
ATOM   6402  C CD2  . PHE   A  1 441 ? 29.110 -2.669  -13.821 1.00 24.02  ? 467  PHE   A CD2  1 
ATOM   6403  C CE1  . PHE   A  1 441 ? 30.928 -0.605  -13.864 1.00 24.59  ? 467  PHE   A CE1  1 
ATOM   6404  C CE2  . PHE   A  1 441 ? 30.316 -2.782  -13.140 1.00 24.98  ? 467  PHE   A CE2  1 
ATOM   6405  C CZ   . PHE   A  1 441 ? 31.231 -1.760  -13.189 1.00 24.66  ? 467  PHE   A CZ   1 
ATOM   6406  H H    . PHE   A  1 441 ? 25.406 -1.251  -16.538 0.00 25.09  ? 467  PHE   A H    1 
ATOM   6407  H HA   . PHE   A  1 441 ? 28.136 -0.595  -17.112 0.00 24.26  ? 467  PHE   A HA   1 
ATOM   6408  H HB2  . PHE   A  1 441 ? 27.050 -0.422  -14.900 0.00 24.32  ? 467  PHE   A HB2  1 
ATOM   6409  H HB3  . PHE   A  1 441 ? 26.827 -2.183  -14.879 0.00 24.36  ? 467  PHE   A HB3  1 
ATOM   6410  H HD1  . PHE   A  1 441 ? 29.497 0.417   -15.074 0.00 24.95  ? 467  PHE   A HD1  1 
ATOM   6411  H HD2  . PHE   A  1 441 ? 28.408 -3.484  -13.787 0.00 25.73  ? 467  PHE   A HD2  1 
ATOM   6412  H HE1  . PHE   A  1 441 ? 31.641 0.201   -13.896 0.00 26.15  ? 467  PHE   A HE1  1 
ATOM   6413  H HE2  . PHE   A  1 441 ? 30.553 -3.690  -12.612 0.00 27.02  ? 467  PHE   A HE2  1 
ATOM   6414  H HZ   . PHE   A  1 441 ? 32.169 -1.848  -12.668 0.00 26.50  ? 467  PHE   A HZ   1 
ATOM   6415  N N    . TYR   A  1 442 ? 27.183 -3.752  -17.460 1.00 23.05  ? 468  TYR   A N    1 
ATOM   6416  C CA   . TYR   A  1 442 ? 27.673 -5.091  -17.804 1.00 23.02  ? 468  TYR   A CA   1 
ATOM   6417  C C    . TYR   A  1 442 ? 27.788 -5.414  -19.300 1.00 24.14  ? 468  TYR   A C    1 
ATOM   6418  O O    . TYR   A  1 442 ? 28.534 -6.332  -19.636 1.00 24.42  ? 468  TYR   A O    1 
ATOM   6419  C CB   . TYR   A  1 442 ? 26.814 -6.146  -17.083 1.00 21.93  ? 468  TYR   A CB   1 
ATOM   6420  C CG   . TYR   A  1 442 ? 27.032 -6.065  -15.591 1.00 21.62  ? 468  TYR   A CG   1 
ATOM   6421  C CD1  . TYR   A  1 442 ? 28.227 -6.482  -15.023 1.00 21.83  ? 468  TYR   A CD1  1 
ATOM   6422  C CD2  . TYR   A  1 442 ? 26.124 -5.411  -14.773 1.00 22.33  ? 468  TYR   A CD2  1 
ATOM   6423  C CE1  . TYR   A  1 442 ? 28.488 -6.309  -13.673 1.00 22.89  ? 468  TYR   A CE1  1 
ATOM   6424  C CE2  . TYR   A  1 442 ? 26.368 -5.248  -13.413 1.00 23.08  ? 468  TYR   A CE2  1 
ATOM   6425  C CZ   . TYR   A  1 442 ? 27.527 -5.749  -12.857 1.00 23.95  ? 468  TYR   A CZ   1 
ATOM   6426  O OH   . TYR   A  1 442 ? 27.789 -5.549  -11.523 1.00 26.02  ? 468  TYR   A OH   1 
ATOM   6427  H H    . TYR   A  1 442 ? 26.172 -3.691  -17.391 0.00 24.13  ? 468  TYR   A H    1 
ATOM   6428  H HA   . TYR   A  1 442 ? 28.694 -5.189  -17.439 0.00 23.91  ? 468  TYR   A HA   1 
ATOM   6429  H HB2  . TYR   A  1 442 ? 25.760 -5.977  -17.295 0.00 23.01  ? 468  TYR   A HB2  1 
ATOM   6430  H HB3  . TYR   A  1 442 ? 27.112 -7.138  -17.418 0.00 22.93  ? 468  TYR   A HB3  1 
ATOM   6431  H HD1  . TYR   A  1 442 ? 28.968 -6.952  -15.646 0.00 22.94  ? 468  TYR   A HD1  1 
ATOM   6432  H HD2  . TYR   A  1 442 ? 25.202 -5.044  -15.190 0.00 23.86  ? 468  TYR   A HD2  1 
ATOM   6433  H HE1  . TYR   A  1 442 ? 29.402 -6.697  -13.254 0.00 24.64  ? 468  TYR   A HE1  1 
ATOM   6434  H HE2  . TYR   A  1 442 ? 25.629 -4.779  -12.786 0.00 25.18  ? 468  TYR   A HE2  1 
ATOM   6435  H HH   . TYR   A  1 442 ? 28.739 -5.749  -11.314 0.00 28.81  ? 468  TYR   A HH   1 
ATOM   6436  N N    . HIS   A  1 443 ? 27.150 -4.651  -20.196 1.00 24.66  ? 469  HIS   A N    1 
ATOM   6437  C CA   . HIS   A  1 443 ? 27.332 -4.860  -21.640 1.00 25.01  ? 469  HIS   A CA   1 
ATOM   6438  C C    . HIS   A  1 443 ? 27.062 -3.572  -22.401 1.00 25.51  ? 469  HIS   A C    1 
ATOM   6439  O O    . HIS   A  1 443 ? 26.362 -2.696  -21.904 1.00 24.78  ? 469  HIS   A O    1 
ATOM   6440  C CB   . HIS   A  1 443 ? 26.438 -5.998  -22.159 1.00 25.51  ? 469  HIS   A CB   1 
ATOM   6441  C CG   . HIS   A  1 443 ? 24.981 -5.776  -21.921 1.00 27.18  ? 469  HIS   A CG   1 
ATOM   6442  N ND1  . HIS   A  1 443 ? 24.319 -6.396  -20.883 1.00 28.58  ? 469  HIS   A ND1  1 
ATOM   6443  C CD2  . HIS   A  1 443 ? 24.104 -4.993  -22.592 1.00 28.22  ? 469  HIS   A CD2  1 
ATOM   6444  C CE1  . HIS   A  1 443 ? 23.064 -5.981  -20.952 1.00 29.26  ? 469  HIS   A CE1  1 
ATOM   6445  N NE2  . HIS   A  1 443 ? 22.889 -5.137  -21.969 1.00 29.44  ? 469  HIS   A NE2  1 
ATOM   6446  H H    . HIS   A  1 443 ? 26.503 -3.901  -19.974 0.00 25.65  ? 469  HIS   A H    1 
ATOM   6447  H HA   . HIS   A  1 443 ? 28.368 -5.130  -21.842 0.00 25.70  ? 469  HIS   A HA   1 
ATOM   6448  H HB2  . HIS   A  1 443 ? 26.588 -6.100  -23.232 0.00 26.47  ? 469  HIS   A HB2  1 
ATOM   6449  H HB3  . HIS   A  1 443 ? 26.720 -6.921  -21.656 0.00 26.69  ? 469  HIS   A HB3  1 
ATOM   6450  H HD2  . HIS   A  1 443 ? 24.318 -4.378  -23.449 0.00 29.92  ? 469  HIS   A HD2  1 
ATOM   6451  H HE1  . HIS   A  1 443 ? 22.280 -6.289  -20.278 0.00 32.01  ? 469  HIS   A HE1  1 
ATOM   6452  H HE2  . HIS   A  1 443 ? 22.020 -4.683  -22.230 0.00 31.96  ? 469  HIS   A HE2  1 
ATOM   6453  N N    . PHE   A  1 444 ? 27.620 -3.468  -23.626 1.00 26.03  ? 470  PHE   A N    1 
ATOM   6454  C CA   . PHE   A  1 444 ? 27.388 -2.313  -24.493 1.00 27.04  ? 470  PHE   A CA   1 
ATOM   6455  C C    . PHE   A  1 444 ? 25.930 -2.360  -24.964 1.00 26.03  ? 470  PHE   A C    1 
ATOM   6456  O O    . PHE   A  1 444 ? 25.380 -3.445  -25.130 1.00 25.65  ? 470  PHE   A O    1 
ATOM   6457  C CB   . PHE   A  1 444 ? 28.313 -2.354  -25.729 1.00 28.64  ? 470  PHE   A CB   1 
ATOM   6458  C CG   . PHE   A  1 444 ? 29.794 -2.397  -25.448 1.00 31.48  ? 470  PHE   A CG   1 
ATOM   6459  C CD1  . PHE   A  1 444 ? 30.383 -1.469  -24.607 1.00 33.52  ? 470  PHE   A CD1  1 
ATOM   6460  C CD2  . PHE   A  1 444 ? 30.610 -3.321  -26.081 1.00 33.12  ? 470  PHE   A CD2  1 
ATOM   6461  C CE1  . PHE   A  1 444 ? 31.760 -1.476  -24.392 1.00 34.75  ? 470  PHE   A CE1  1 
ATOM   6462  C CE2  . PHE   A  1 444 ? 31.987 -3.325  -25.864 1.00 34.30  ? 470  PHE   A CE2  1 
ATOM   6463  C CZ   . PHE   A  1 444 ? 32.550 -2.405  -25.021 1.00 34.49  ? 470  PHE   A CZ   1 
ATOM   6464  H H    . PHE   A  1 444 ? 28.211 -4.184  -24.035 0.00 26.66  ? 470  PHE   A H    1 
ATOM   6465  H HA   . PHE   A  1 444 ? 27.561 -1.387  -23.946 0.00 27.86  ? 470  PHE   A HA   1 
ATOM   6466  H HB2  . PHE   A  1 444 ? 28.058 -3.237  -26.313 0.00 29.58  ? 470  PHE   A HB2  1 
ATOM   6467  H HB3  . PHE   A  1 444 ? 28.124 -1.463  -26.325 0.00 29.51  ? 470  PHE   A HB3  1 
ATOM   6468  H HD1  . PHE   A  1 444 ? 29.772 -0.728  -24.118 0.00 35.35  ? 470  PHE   A HD1  1 
ATOM   6469  H HD2  . PHE   A  1 444 ? 30.183 -4.043  -26.755 0.00 34.75  ? 470  PHE   A HD2  1 
ATOM   6470  H HE1  . PHE   A  1 444 ? 32.204 -0.759  -23.722 0.00 36.67  ? 470  PHE   A HE1  1 
ATOM   6471  H HE2  . PHE   A  1 444 ? 32.606 -4.060  -26.348 0.00 36.01  ? 470  PHE   A HE2  1 
ATOM   6472  H HZ   . PHE   A  1 444 ? 33.611 -2.423  -24.836 0.00 36.22  ? 470  PHE   A HZ   1 
ATOM   6473  N N    . THR   A  1 445 ? 25.302 -1.199  -25.160 1.00 26.24  ? 471  THR   A N    1 
ATOM   6474  C CA   . THR   A  1 445 ? 23.906 -1.130  -25.605 1.00 27.79  ? 471  THR   A CA   1 
ATOM   6475  C C    . THR   A  1 445 ? 23.749 -0.763  -27.095 1.00 28.03  ? 471  THR   A C    1 
ATOM   6476  O O    . THR   A  1 445 ? 22.618 -0.739  -27.587 1.00 28.05  ? 471  THR   A O    1 
ATOM   6477  C CB   . THR   A  1 445 ? 23.126 -0.160  -24.704 1.00 29.96  ? 471  THR   A CB   1 
ATOM   6478  O OG1  . THR   A  1 445 ? 23.775 1.115   -24.747 1.00 32.00  ? 471  THR   A OG1  1 
ATOM   6479  C CG2  . THR   A  1 445 ? 23.059 -0.638  -23.270 1.00 30.24  ? 471  THR   A CG2  1 
ATOM   6480  H H    . THR   A  1 445 ? 25.729 -0.291  -25.012 0.00 27.07  ? 471  THR   A H    1 
ATOM   6481  H HA   . THR   A  1 445 ? 23.434 -2.104  -25.486 0.00 29.35  ? 471  THR   A HA   1 
ATOM   6482  H HB   . THR   A  1 445 ? 22.108 -0.058  -25.073 0.00 32.25  ? 471  THR   A HB   1 
ATOM   6483  H HG1  . THR   A  1 445 ? 23.282 1.757   -24.171 0.00 34.57  ? 471  THR   A HG1  1 
ATOM   6484  H HG21 . THR   A  1 445 ? 22.426 0.029   -22.685 0.00 32.70  ? 471  THR   A HG21 1 
ATOM   6485  H HG22 . THR   A  1 445 ? 22.644 -1.643  -23.232 0.00 32.60  ? 471  THR   A HG22 1 
ATOM   6486  H HG23 . THR   A  1 445 ? 24.055 -0.651  -22.831 0.00 32.35  ? 471  THR   A HG23 1 
ATOM   6487  N N    . ARG   A  1 446 ? 24.853 -0.523  -27.818 1.00 28.20  ? 472  ARG   A N    1 
ATOM   6488  C CA   . ARG   A  1 446 ? 24.766 -0.214  -29.254 1.00 29.07  ? 472  ARG   A CA   1 
ATOM   6489  C C    . ARG   A  1 446 ? 24.274 -1.453  -30.030 1.00 28.18  ? 472  ARG   A C    1 
ATOM   6490  O O    . ARG   A  1 446 ? 24.486 -2.577  -29.561 1.00 27.22  ? 472  ARG   A O    1 
ATOM   6491  C CB   . ARG   A  1 446 ? 26.126 0.244   -29.810 1.00 31.41  ? 472  ARG   A CB   1 
ATOM   6492  C CG   . ARG   A  1 446 ? 27.220 -0.826  -29.806 1.00 36.25  ? 472  ARG   A CG   1 
ATOM   6493  C CD   . ARG   A  1 446 ? 28.381 -0.421  -30.699 1.00 40.81  ? 472  ARG   A CD   1 
ATOM   6494  N NE   . ARG   A  1 446 ? 29.494 -1.373  -30.655 1.00 45.01  ? 472  ARG   A NE   1 
ATOM   6495  C CZ   . ARG   A  1 446 ? 29.546 -2.531  -31.312 1.00 47.62  ? 472  ARG   A CZ   1 
ATOM   6496  N NH1  . ARG   A  1 446 ? 28.519 -2.929  -32.059 1.00 46.85  ? 472  ARG   A NH1  1 
ATOM   6497  N NH2  . ARG   A  1 446 ? 30.618 -3.309  -31.214 1.00 47.81  ? 472  ARG   A NH2  1 
ATOM   6498  H H    . ARG   A  1 446 ? 25.801 -0.513  -27.457 0.00 29.27  ? 472  ARG   A H    1 
ATOM   6499  H HA   . ARG   A  1 446 ? 24.061 0.606   -29.373 0.00 30.61  ? 472  ARG   A HA   1 
ATOM   6500  H HB2  . ARG   A  1 446 ? 25.987 0.567   -30.840 0.00 33.03  ? 472  ARG   A HB2  1 
ATOM   6501  H HB3  . ARG   A  1 446 ? 26.484 1.080   -29.210 0.00 32.98  ? 472  ARG   A HB3  1 
ATOM   6502  H HG2  . ARG   A  1 446 ? 27.596 -0.945  -28.792 0.00 38.60  ? 472  ARG   A HG2  1 
ATOM   6503  H HG3  . ARG   A  1 446 ? 26.847 -1.776  -30.184 0.00 38.71  ? 472  ARG   A HG3  1 
ATOM   6504  H HD2  . ARG   A  1 446 ? 28.041 -0.315  -31.728 0.00 43.96  ? 472  ARG   A HD2  1 
ATOM   6505  H HD3  . ARG   A  1 446 ? 28.761 0.536   -30.345 0.00 43.87  ? 472  ARG   A HD3  1 
ATOM   6506  H HE   . ARG   A  1 446 ? 30.304 -1.104  -30.105 0.00 48.73  ? 472  ARG   A HE   1 
ATOM   6507  H HH11 . ARG   A  1 446 ? 27.678 -2.371  -32.162 0.00 51.32  ? 472  ARG   A HH11 1 
ATOM   6508  H HH12 . ARG   A  1 446 ? 28.571 -3.819  -32.544 0.00 51.28  ? 472  ARG   A HH12 1 
ATOM   6509  H HH21 . ARG   A  1 446 ? 31.408 -3.023  -30.644 0.00 52.05  ? 472  ARG   A HH21 1 
ATOM   6510  H HH22 . ARG   A  1 446 ? 30.653 -4.198  -31.702 0.00 52.20  ? 472  ARG   A HH22 1 
ATOM   6511  N N    . PRO   A  1 447 ? 23.661 -1.299  -31.226 1.00 28.00  ? 473  PRO   A N    1 
ATOM   6512  C CA   . PRO   A  1 447 ? 23.219 -2.499  -31.970 1.00 26.84  ? 473  PRO   A CA   1 
ATOM   6513  C C    . PRO   A  1 447 ? 24.388 -3.442  -32.273 1.00 25.47  ? 473  PRO   A C    1 
ATOM   6514  O O    . PRO   A  1 447 ? 25.522 -2.986  -32.424 1.00 25.21  ? 473  PRO   A O    1 
ATOM   6515  C CB   . PRO   A  1 447 ? 22.605 -1.933  -33.258 1.00 28.01  ? 473  PRO   A CB   1 
ATOM   6516  C CG   . PRO   A  1 447 ? 22.352 -0.479  -32.991 1.00 29.07  ? 473  PRO   A CG   1 
ATOM   6517  C CD   . PRO   A  1 447 ? 23.348 -0.048  -31.961 1.00 27.86  ? 473  PRO   A CD   1 
ATOM   6518  H HA   . PRO   A  1 447 ? 22.455 -3.032  -31.404 0.00 28.34  ? 473  PRO   A HA   1 
ATOM   6519  H HB2  . PRO   A  1 447 ? 23.307 -2.050  -34.081 0.00 29.60  ? 473  PRO   A HB2  1 
ATOM   6520  H HB3  . PRO   A  1 447 ? 21.671 -2.448  -33.475 0.00 29.98  ? 473  PRO   A HB3  1 
ATOM   6521  H HG2  . PRO   A  1 447 ? 22.486 0.084   -33.914 0.00 31.04  ? 473  PRO   A HG2  1 
ATOM   6522  H HG3  . PRO   A  1 447 ? 21.339 -0.355  -32.611 0.00 31.28  ? 473  PRO   A HG3  1 
ATOM   6523  H HD2  . PRO   A  1 447 ? 24.241 0.345   -32.444 0.00 29.14  ? 473  PRO   A HD2  1 
ATOM   6524  H HD3  . PRO   A  1 447 ? 22.885 0.691   -31.310 0.00 29.44  ? 473  PRO   A HD3  1 
ATOM   6525  N N    . LEU   A  1 448 ? 24.135 -4.755  -32.280 1.00 24.34  ? 474  LEU   A N    1 
ATOM   6526  C CA   . LEU   A  1 448 ? 25.201 -5.730  -32.569 1.00 24.03  ? 474  LEU   A CA   1 
ATOM   6527  C C    . LEU   A  1 448 ? 25.732 -5.535  -33.991 1.00 23.79  ? 474  LEU   A C    1 
ATOM   6528  O O    . LEU   A  1 448 ? 26.935 -5.589  -34.230 1.00 23.48  ? 474  LEU   A O    1 
ATOM   6529  C CB   . LEU   A  1 448 ? 24.654 -7.161  -32.427 1.00 23.74  ? 474  LEU   A CB   1 
ATOM   6530  C CG   . LEU   A  1 448 ? 24.242 -7.587  -31.019 1.00 24.20  ? 474  LEU   A CG   1 
ATOM   6531  C CD1  . LEU   A  1 448 ? 23.609 -8.944  -31.044 1.00 25.16  ? 474  LEU   A CD1  1 
ATOM   6532  C CD2  . LEU   A  1 448 ? 25.437 -7.580  -30.065 1.00 24.68  ? 474  LEU   A CD2  1 
ATOM   6533  H H    . LEU   A  1 448 ? 23.225 -5.166  -32.098 0.00 25.31  ? 474  LEU   A H    1 
ATOM   6534  H HA   . LEU   A  1 448 ? 26.032 -5.583  -31.880 0.00 24.42  ? 474  LEU   A HA   1 
ATOM   6535  H HB2  . LEU   A  1 448 ? 23.781 -7.255  -33.069 0.00 24.73  ? 474  LEU   A HB2  1 
ATOM   6536  H HB3  . LEU   A  1 448 ? 25.425 -7.852  -32.764 0.00 24.47  ? 474  LEU   A HB3  1 
ATOM   6537  H HG   . LEU   A  1 448 ? 23.506 -6.882  -30.637 0.00 25.22  ? 474  LEU   A HG   1 
ATOM   6538  H HD11 . LEU   A  1 448 ? 23.281 -9.210  -30.039 0.00 26.71  ? 474  LEU   A HD11 1 
ATOM   6539  H HD12 . LEU   A  1 448 ? 22.754 -8.923  -31.718 0.00 26.81  ? 474  LEU   A HD12 1 
ATOM   6540  H HD13 . LEU   A  1 448 ? 24.342 -9.668  -31.399 0.00 26.60  ? 474  LEU   A HD13 1 
ATOM   6541  H HD21 . LEU   A  1 448 ? 25.175 -8.129  -29.162 0.00 25.62  ? 474  LEU   A HD21 1 
ATOM   6542  H HD22 . LEU   A  1 448 ? 26.289 -8.048  -30.556 0.00 25.43  ? 474  LEU   A HD22 1 
ATOM   6543  H HD23 . LEU   A  1 448 ? 25.676 -6.551  -29.805 0.00 25.34  ? 474  LEU   A HD23 1 
ATOM   6544  N N    . ILE   A  1 449 ? 24.818 -5.284  -34.919 1.00 23.53  ? 475  ILE   A N    1 
ATOM   6545  C CA   . ILE   A  1 449 ? 25.107 -5.083  -36.328 1.00 24.43  ? 475  ILE   A CA   1 
ATOM   6546  C C    . ILE   A  1 449 ? 24.659 -3.685  -36.712 1.00 24.43  ? 475  ILE   A C    1 
ATOM   6547  O O    . ILE   A  1 449 ? 23.647 -3.208  -36.204 1.00 24.89  ? 475  ILE   A O    1 
ATOM   6548  C CB   . ILE   A  1 449 ? 24.396 -6.235  -37.102 1.00 25.81  ? 475  ILE   A CB   1 
ATOM   6549  C CG1  . ILE   A  1 449 ? 25.118 -7.584  -36.672 1.00 26.68  ? 475  ILE   A CG1  1 
ATOM   6550  C CG2  . ILE   A  1 449 ? 24.411 -5.980  -38.639 1.00 26.15  ? 475  ILE   A CG2  1 
ATOM   6551  C CD1  . ILE   A  1 449 ? 24.835 -8.771  -37.382 1.00 28.15  ? 475  ILE   A CD1  1 
ATOM   6552  H H    . ILE   A  1 449 ? 23.823 -5.230  -34.728 0.00 24.34  ? 475  ILE   A H    1 
ATOM   6553  H HA   . ILE   A  1 449 ? 26.177 -5.144  -36.521 0.00 25.05  ? 475  ILE   A HA   1 
ATOM   6554  H HB   . ILE   A  1 449 ? 23.348 -6.303  -36.812 0.00 27.43  ? 475  ILE   A HB   1 
ATOM   6555  H HG12 . ILE   A  1 449 ? 26.193 -7.431  -36.746 0.00 28.02  ? 475  ILE   A HG12 1 
ATOM   6556  H HG13 . ILE   A  1 449 ? 24.861 -7.788  -35.633 0.00 28.23  ? 475  ILE   A HG13 1 
ATOM   6557  H HG21 . ILE   A  1 449 ? 24.029 -6.858  -39.156 0.00 27.99  ? 475  ILE   A HG21 1 
ATOM   6558  H HG22 . ILE   A  1 449 ? 23.775 -5.129  -38.875 0.00 27.84  ? 475  ILE   A HG22 1 
ATOM   6559  H HG23 . ILE   A  1 449 ? 25.433 -5.775  -38.955 0.00 27.55  ? 475  ILE   A HG23 1 
ATOM   6560  H HD11 . ILE   A  1 449 ? 25.235 -9.618  -36.825 0.00 30.31  ? 475  ILE   A HD11 1 
ATOM   6561  H HD12 . ILE   A  1 449 ? 23.755 -8.869  -37.485 0.00 30.56  ? 475  ILE   A HD12 1 
ATOM   6562  H HD13 . ILE   A  1 449 ? 25.311 -8.715  -38.359 0.00 30.31  ? 475  ILE   A HD13 1 
ATOM   6563  N N    . LYS   A  1 450 ? 25.420 -2.990  -37.586 1.00 23.64  ? 476  LYS   A N    1 
ATOM   6564  C CA   . LYS   A  1 450 ? 25.064 -1.630  -38.000 1.00 24.11  ? 476  LYS   A CA   1 
ATOM   6565  C C    . LYS   A  1 450 ? 23.639 -1.585  -38.551 1.00 23.84  ? 476  LYS   A C    1 
ATOM   6566  O O    . LYS   A  1 450 ? 23.298 -2.468  -39.346 1.00 23.43  ? 476  LYS   A O    1 
ATOM   6567  C CB   . LYS   A  1 450 ? 26.003 -1.107  -39.100 1.00 26.33  ? 476  LYS   A CB   1 
ATOM   6568  C CG   . LYS   A  1 450 ? 27.379 -0.689  -38.626 1.00 33.84  ? 476  LYS   A CG   1 
ATOM   6569  C CD   . LYS   A  1 450 ? 28.078 0.074   -39.735 1.00 39.91  ? 476  LYS   A CD   1 
ATOM   6570  C CE   . LYS   A  1 450 ? 29.565 0.213   -39.531 1.00 45.38  ? 476  LYS   A CE   1 
ATOM   6571  N NZ   . LYS   A  1 450 ? 30.255 0.721   -40.756 1.00 48.50  ? 476  LYS   A NZ   1 
ATOM   6572  H H    . LYS   A  1 450 ? 26.271 -3.342  -38.012 0.00 24.06  ? 476  LYS   A H    1 
ATOM   6573  H HA   . LYS   A  1 450 ? 25.171 -0.983  -37.133 0.00 24.68  ? 476  LYS   A HA   1 
ATOM   6574  H HB2  . LYS   A  1 450 ? 26.130 -1.885  -39.852 0.00 27.43  ? 476  LYS   A HB2  1 
ATOM   6575  H HB3  . LYS   A  1 450 ? 25.539 -0.235  -39.558 0.00 27.48  ? 476  LYS   A HB3  1 
ATOM   6576  H HG2  . LYS   A  1 450 ? 27.286 -0.036  -37.760 0.00 35.98  ? 476  LYS   A HG2  1 
ATOM   6577  H HG3  . LYS   A  1 450 ? 27.964 -1.574  -38.382 0.00 35.94  ? 476  LYS   A HG3  1 
ATOM   6578  H HD2  . LYS   A  1 450 ? 27.908 -0.433  -40.683 0.00 43.43  ? 476  LYS   A HD2  1 
ATOM   6579  H HD3  . LYS   A  1 450 ? 27.659 1.078   -39.782 0.00 43.39  ? 476  LYS   A HD3  1 
ATOM   6580  H HE2  . LYS   A  1 450 ? 29.749 0.918   -38.722 0.00 49.52  ? 476  LYS   A HE2  1 
ATOM   6581  H HE3  . LYS   A  1 450 ? 29.989 -0.760  -39.285 0.00 49.53  ? 476  LYS   A HE3  1 
ATOM   6582  H HZ1  . LYS   A  1 450 ? 31.244 0.848   -40.569 0.00 53.21  ? 476  LYS   A HZ1  1 
ATOM   6583  H HZ2  . LYS   A  1 450 ? 30.146 0.056   -41.515 0.00 53.46  ? 476  LYS   A HZ2  1 
ATOM   6584  H HZ3  . LYS   A  1 450 ? 29.854 1.610   -41.036 0.00 53.46  ? 476  LYS   A HZ3  1 
ATOM   6585  N N    . PRO   A  1 451 ? 22.766 -0.665  -38.088 1.00 24.42  ? 477  PRO   A N    1 
ATOM   6586  C CA   . PRO   A  1 451 ? 21.383 -0.675  -38.602 1.00 24.71  ? 477  PRO   A CA   1 
ATOM   6587  C C    . PRO   A  1 451 ? 21.278 -0.606  -40.122 1.00 24.75  ? 477  PRO   A C    1 
ATOM   6588  O O    . PRO   A  1 451 ? 20.373 -1.203  -40.687 1.00 24.80  ? 477  PRO   A O    1 
ATOM   6589  C CB   . PRO   A  1 451 ? 20.734 0.557   -37.953 1.00 25.31  ? 477  PRO   A CB   1 
ATOM   6590  C CG   . PRO   A  1 451 ? 21.585 0.887   -36.791 1.00 25.94  ? 477  PRO   A CG   1 
ATOM   6591  C CD   . PRO   A  1 451 ? 22.975 0.414   -37.095 1.00 23.86  ? 477  PRO   A CD   1 
ATOM   6592  H HA   . PRO   A  1 451 ? 20.869 -1.571  -38.257 0.00 26.58  ? 477  PRO   A HA   1 
ATOM   6593  H HB2  . PRO   A  1 451 ? 20.715 1.379   -38.665 0.00 27.41  ? 477  PRO   A HB2  1 
ATOM   6594  H HB3  . PRO   A  1 451 ? 19.725 0.305   -37.630 0.00 27.58  ? 477  PRO   A HB3  1 
ATOM   6595  H HG2  . PRO   A  1 451 ? 21.580 1.966   -36.640 0.00 27.74  ? 477  PRO   A HG2  1 
ATOM   6596  H HG3  . PRO   A  1 451 ? 21.198 0.379   -35.909 0.00 27.75  ? 477  PRO   A HG3  1 
ATOM   6597  H HD2  . PRO   A  1 451 ? 23.567 1.222   -37.524 0.00 24.79  ? 477  PRO   A HD2  1 
ATOM   6598  H HD3  . PRO   A  1 451 ? 23.405 0.031   -36.170 0.00 24.71  ? 477  PRO   A HD3  1 
ATOM   6599  N N    . GLN   A  1 452 ? 22.203 0.106   -40.782 1.00 24.63  ? 478  GLN   A N    1 
ATOM   6600  C CA   . GLN   A  1 452 ? 22.181 0.237   -42.237 1.00 24.86  ? 478  GLN   A CA   1 
ATOM   6601  C C    . GLN   A  1 452 ? 22.402 -1.107  -42.940 1.00 24.33  ? 478  GLN   A C    1 
ATOM   6602  O O    . GLN   A  1 452 ? 21.875 -1.316  -44.028 1.00 24.36  ? 478  GLN   A O    1 
ATOM   6603  C CB   . GLN   A  1 452 ? 23.223 1.271   -42.711 1.00 26.67  ? 478  GLN   A CB   1 
ATOM   6604  C CG   . GLN   A  1 452 ? 22.922 2.708   -42.247 1.00 29.32  ? 478  GLN   A CG   1 
ATOM   6605  C CD   . GLN   A  1 452 ? 23.636 3.094   -40.966 1.00 31.69  ? 478  GLN   A CD   1 
ATOM   6606  O OE1  . GLN   A  1 452 ? 23.897 2.268   -40.091 1.00 32.14  ? 478  GLN   A OE1  1 
ATOM   6607  N NE2  . GLN   A  1 452 ? 23.956 4.373   -40.816 1.00 32.44  ? 478  GLN   A NE2  1 
ATOM   6608  H H    . GLN   A  1 452 ? 22.968 0.609   -40.343 0.00 26.15  ? 478  GLN   A H    1 
ATOM   6609  H HA   . GLN   A  1 452 ? 21.199 0.599   -42.538 0.00 27.23  ? 478  GLN   A HA   1 
ATOM   6610  H HB2  . GLN   A  1 452 ? 24.206 0.985   -42.341 0.00 28.56  ? 478  GLN   A HB2  1 
ATOM   6611  H HB3  . GLN   A  1 452 ? 23.231 1.276   -43.800 0.00 29.04  ? 478  GLN   A HB3  1 
ATOM   6612  H HG2  . GLN   A  1 452 ? 23.234 3.390   -43.038 0.00 32.17  ? 478  GLN   A HG2  1 
ATOM   6613  H HG3  . GLN   A  1 452 ? 21.852 2.810   -42.075 0.00 32.38  ? 478  GLN   A HG3  1 
ATOM   6614  H HE21 . GLN   A  1 452 ? 23.722 5.052   -41.534 0.00 35.70  ? 478  GLN   A HE21 1 
ATOM   6615  H HE22 . GLN   A  1 452 ? 24.437 4.680   -39.977 0.00 35.30  ? 478  GLN   A HE22 1 
ATOM   6616  N N    . CYS   A  1 453 ? 23.172 -2.011  -42.321 1.00 23.99  ? 479  CYS   A N    1 
ATOM   6617  C CA   . CYS   A  1 453 ? 23.437 -3.343  -42.850 1.00 24.39  ? 479  CYS   A CA   1 
ATOM   6618  C C    . CYS   A  1 453 ? 22.263 -4.272  -42.487 1.00 25.12  ? 479  CYS   A C    1 
ATOM   6619  O O    . CYS   A  1 453 ? 21.708 -4.921  -43.375 1.00 25.62  ? 479  CYS   A O    1 
ATOM   6620  C CB   . CYS   A  1 453 ? 24.766 -3.846  -42.292 1.00 24.34  ? 479  CYS   A CB   1 
ATOM   6621  S SG   . CYS   A  1 453 ? 25.464 -5.291  -43.142 1.00 25.10  ? 479  CYS   A SG   1 
ATOM   6622  H H    . CYS   A  1 453 ? 23.645 -1.846  -41.438 0.00 25.39  ? 479  CYS   A H    1 
ATOM   6623  H HA   . CYS   A  1 453 ? 23.524 -3.301  -43.935 0.00 26.36  ? 479  CYS   A HA   1 
ATOM   6624  H HB2  . CYS   A  1 453 ? 25.461 -3.022  -42.437 0.00 25.58  ? 479  CYS   A HB2  1 
ATOM   6625  H HB3  . CYS   A  1 453 ? 24.657 -4.083  -41.234 0.00 25.66  ? 479  CYS   A HB3  1 
ATOM   6626  N N    . ALA   A  1 454 ? 21.844 -4.297  -41.207 1.00 25.33  ? 480  ALA   A N    1 
ATOM   6627  C CA   . ALA   A  1 454 ? 20.737 -5.148  -40.773 1.00 25.65  ? 480  ALA   A CA   1 
ATOM   6628  C C    . ALA   A  1 454 ? 19.412 -4.828  -41.487 1.00 25.71  ? 480  ALA   A C    1 
ATOM   6629  O O    . ALA   A  1 454 ? 18.611 -5.743  -41.669 1.00 25.53  ? 480  ALA   A O    1 
ATOM   6630  C CB   . ALA   A  1 454 ? 20.547 -5.061  -39.257 1.00 25.52  ? 480  ALA   A CB   1 
ATOM   6631  H H    . ALA   A  1 454 ? 22.257 -3.750  -40.458 0.00 27.32  ? 480  ALA   A H    1 
ATOM   6632  H HA   . ALA   A  1 454 ? 20.988 -6.182  -41.007 0.00 28.33  ? 480  ALA   A HA   1 
ATOM   6633  H HB1  . ALA   A  1 454 ? 19.703 -5.686  -38.966 0.00 28.22  ? 480  ALA   A HB1  1 
ATOM   6634  H HB2  . ALA   A  1 454 ? 21.453 -5.415  -38.767 0.00 27.68  ? 480  ALA   A HB2  1 
ATOM   6635  H HB3  . ALA   A  1 454 ? 20.359 -4.023  -38.985 0.00 27.90  ? 480  ALA   A HB3  1 
ATOM   6636  N N    . ALA   A  1 455 ? 19.179 -3.555  -41.884 1.00 25.70  ? 481  ALA   A N    1 
ATOM   6637  C CA   . ALA   A  1 455 ? 17.949 -3.146  -42.595 1.00 26.18  ? 481  ALA   A CA   1 
ATOM   6638  C C    . ALA   A  1 455 ? 17.725 -3.925  -43.880 1.00 26.25  ? 481  ALA   A C    1 
ATOM   6639  O O    . ALA   A  1 455 ? 16.584 -4.027  -44.331 1.00 27.05  ? 481  ALA   A O    1 
ATOM   6640  C CB   . ALA   A  1 455 ? 18.002 -1.664  -42.929 1.00 26.63  ? 481  ALA   A CB   1 
ATOM   6641  H H    . ALA   A  1 455 ? 19.811 -2.779  -41.718 0.00 28.58  ? 481  ALA   A H    1 
ATOM   6642  H HA   . ALA   A  1 455 ? 17.092 -3.312  -41.945 0.00 30.12  ? 481  ALA   A HA   1 
ATOM   6643  H HB1  . ALA   A  1 455 ? 17.090 -1.385  -43.455 0.00 30.87  ? 481  ALA   A HB1  1 
ATOM   6644  H HB2  . ALA   A  1 455 ? 18.088 -1.094  -42.005 0.00 30.26  ? 481  ALA   A HB2  1 
ATOM   6645  H HB3  . ALA   A  1 455 ? 18.868 -1.476  -43.563 0.00 30.27  ? 481  ALA   A HB3  1 
ATOM   6646  N N    . TYR   A  1 456 ? 18.806 -4.442  -44.498 1.00 24.73  ? 482  TYR   A N    1 
ATOM   6647  C CA   . TYR   A  1 456 ? 18.695 -5.215  -45.722 1.00 24.03  ? 482  TYR   A CA   1 
ATOM   6648  C C    . TYR   A  1 456 ? 18.163 -6.620  -45.535 1.00 22.96  ? 482  TYR   A C    1 
ATOM   6649  O O    . TYR   A  1 456 ? 17.712 -7.190  -46.517 1.00 22.56  ? 482  TYR   A O    1 
ATOM   6650  C CB   . TYR   A  1 456 ? 20.040 -5.274  -46.461 1.00 23.78  ? 482  TYR   A CB   1 
ATOM   6651  C CG   . TYR   A  1 456 ? 20.326 -4.028  -47.257 1.00 24.21  ? 482  TYR   A CG   1 
ATOM   6652  C CD1  . TYR   A  1 456 ? 19.618 -3.743  -48.422 1.00 24.52  ? 482  TYR   A CD1  1 
ATOM   6653  C CD2  . TYR   A  1 456 ? 21.297 -3.126  -46.847 1.00 24.64  ? 482  TYR   A CD2  1 
ATOM   6654  C CE1  . TYR   A  1 456 ? 19.888 -2.604  -49.169 1.00 25.11  ? 482  TYR   A CE1  1 
ATOM   6655  C CE2  . TYR   A  1 456 ? 21.581 -1.987  -47.590 1.00 25.56  ? 482  TYR   A CE2  1 
ATOM   6656  C CZ   . TYR   A  1 456 ? 20.881 -1.733  -48.753 1.00 26.21  ? 482  TYR   A CZ   1 
ATOM   6657  O OH   . TYR   A  1 456 ? 21.151 -0.579  -49.442 1.00 28.01  ? 482  TYR   A OH   1 
ATOM   6658  H H    . TYR   A  1 456 ? 19.760 -4.329  -44.173 0.00 27.95  ? 482  TYR   A H    1 
ATOM   6659  H HA   . TYR   A  1 456 ? 17.959 -4.726  -46.359 0.00 28.19  ? 482  TYR   A HA   1 
ATOM   6660  H HB2  . TYR   A  1 456 ? 20.853 -5.435  -45.754 0.00 26.88  ? 482  TYR   A HB2  1 
ATOM   6661  H HB3  . TYR   A  1 456 ? 20.015 -6.099  -47.171 0.00 27.51  ? 482  TYR   A HB3  1 
ATOM   6662  H HD1  . TYR   A  1 456 ? 18.861 -4.430  -48.761 0.00 29.00  ? 482  TYR   A HD1  1 
ATOM   6663  H HD2  . TYR   A  1 456 ? 21.861 -3.323  -45.950 0.00 27.48  ? 482  TYR   A HD2  1 
ATOM   6664  H HE1  . TYR   A  1 456 ? 19.330 -2.412  -50.070 0.00 29.75  ? 482  TYR   A HE1  1 
ATOM   6665  H HE2  . TYR   A  1 456 ? 22.340 -1.300  -47.257 0.00 28.62  ? 482  TYR   A HE2  1 
ATOM   6666  H HH   . TYR   A  1 456 ? 20.543 -0.484  -50.221 0.00 32.80  ? 482  TYR   A HH   1 
ATOM   6667  N N    . GLY   A  1 457 ? 18.216 -7.176  -44.332 1.00 22.16  ? 483  GLY   A N    1 
ATOM   6668  C CA   . GLY   A  1 457 ? 17.714 -8.527  -44.104 1.00 22.35  ? 483  GLY   A CA   1 
ATOM   6669  C C    . GLY   A  1 457 ? 18.606 -9.318  -43.177 1.00 22.18  ? 483  GLY   A C    1 
ATOM   6670  O O    . GLY   A  1 457 ? 19.280 -8.727  -42.328 1.00 22.77  ? 483  GLY   A O    1 
ATOM   6671  H H    . GLY   A  1 457 ? 18.607 -6.747  -43.500 0.00 25.34  ? 483  GLY   A H    1 
ATOM   6672  H HA2  . GLY   A  1 457 ? 16.724 -8.473  -43.653 0.00 26.46  ? 483  GLY   A HA2  1 
ATOM   6673  H HA3  . GLY   A  1 457 ? 17.635 -9.081  -45.039 0.00 26.52  ? 483  GLY   A HA3  1 
ATOM   6674  N N    . LYS   A  1 458 ? 18.611 -10.655 -43.330 1.00 21.18  ? 484  LYS   A N    1 
ATOM   6675  C CA   . LYS   A  1 458 ? 19.370 -11.546 -42.439 1.00 20.91  ? 484  LYS   A CA   1 
ATOM   6676  C C    . LYS   A  1 458 ? 20.849 -11.192 -42.418 1.00 20.42  ? 484  LYS   A C    1 
ATOM   6677  O O    . LYS   A  1 458 ? 21.485 -11.084 -43.473 1.00 19.92  ? 484  LYS   A O    1 
ATOM   6678  C CB   . LYS   A  1 458 ? 19.213 -13.022 -42.825 1.00 22.66  ? 484  LYS   A CB   1 
ATOM   6679  C CG   . LYS   A  1 458 ? 17.787 -13.591 -42.797 1.00 27.11  ? 484  LYS   A CG   1 
ATOM   6680  C CD   . LYS   A  1 458 ? 17.870 -15.097 -43.128 1.00 33.45  ? 484  LYS   A CD   1 
ATOM   6681  C CE   . LYS   A  1 458 ? 16.812 -15.999 -42.520 1.00 38.48  ? 484  LYS   A CE   1 
ATOM   6682  N NZ   . LYS   A  1 458 ? 15.478 -15.835 -43.130 1.00 40.19  ? 484  LYS   A NZ   1 
ATOM   6683  H H    . LYS   A  1 458 ? 18.101 -11.139 -44.062 0.00 25.11  ? 484  LYS   A H    1 
ATOM   6684  H HA   . LYS   A  1 458 ? 18.973 -11.427 -41.432 0.00 24.11  ? 484  LYS   A HA   1 
ATOM   6685  H HB2  . LYS   A  1 458 ? 19.604 -13.162 -43.832 0.00 27.11  ? 484  LYS   A HB2  1 
ATOM   6686  H HB3  . LYS   A  1 458 ? 19.804 -13.600 -42.117 0.00 26.60  ? 484  LYS   A HB3  1 
ATOM   6687  H HG2  . LYS   A  1 458 ? 17.333 -13.441 -41.818 0.00 31.97  ? 484  LYS   A HG2  1 
ATOM   6688  H HG3  . LYS   A  1 458 ? 17.187 -13.116 -43.575 0.00 32.43  ? 484  LYS   A HG3  1 
ATOM   6689  H HD2  . LYS   A  1 458 ? 17.809 -15.213 -44.209 0.00 40.66  ? 484  LYS   A HD2  1 
ATOM   6690  H HD3  . LYS   A  1 458 ? 18.826 -15.485 -42.778 0.00 40.28  ? 484  LYS   A HD3  1 
ATOM   6691  H HE2  . LYS   A  1 458 ? 17.116 -17.033 -42.674 0.00 47.15  ? 484  LYS   A HE2  1 
ATOM   6692  H HE3  . LYS   A  1 458 ? 16.735 -15.788 -41.454 0.00 46.74  ? 484  LYS   A HE3  1 
ATOM   6693  H HZ1  . LYS   A  1 458 ? 14.810 -16.408 -42.623 0.00 49.86  ? 484  LYS   A HZ1  1 
ATOM   6694  H HZ2  . LYS   A  1 458 ? 15.179 -14.866 -43.087 0.00 49.40  ? 484  LYS   A HZ2  1 
ATOM   6695  H HZ3  . LYS   A  1 458 ? 15.491 -16.140 -44.098 0.00 49.80  ? 484  LYS   A HZ3  1 
ATOM   6696  N N    . ALA   A  1 459 ? 21.406 -11.079 -41.205 1.00 19.77  ? 485  ALA   A N    1 
ATOM   6697  C CA   . ALA   A  1 459 ? 22.782 -10.667 -41.017 1.00 19.70  ? 485  ALA   A CA   1 
ATOM   6698  C C    . ALA   A  1 459 ? 23.636 -11.733 -40.361 1.00 18.64  ? 485  ALA   A C    1 
ATOM   6699  O O    . ALA   A  1 459 ? 23.209 -12.395 -39.407 1.00 18.33  ? 485  ALA   A O    1 
ATOM   6700  C CB   . ALA   A  1 459 ? 22.814 -9.404  -40.185 1.00 20.15  ? 485  ALA   A CB   1 
ATOM   6701  H H    . ALA   A  1 459 ? 20.926 -11.280 -40.333 0.00 21.98  ? 485  ALA   A H    1 
ATOM   6702  H HA   . ALA   A  1 459 ? 23.229 -10.418 -41.979 0.00 21.38  ? 485  ALA   A HA   1 
ATOM   6703  H HB1  . ALA   A  1 459 ? 23.845 -9.061  -40.109 0.00 21.27  ? 485  ALA   A HB1  1 
ATOM   6704  H HB2  . ALA   A  1 459 ? 22.207 -8.643  -40.674 0.00 21.68  ? 485  ALA   A HB2  1 
ATOM   6705  H HB3  . ALA   A  1 459 ? 22.407 -9.627  -39.200 0.00 21.58  ? 485  ALA   A HB3  1 
ATOM   6706  N N    . LEU   A  1 460 ? 24.870 -11.860 -40.855 1.00 17.46  ? 486  LEU   A N    1 
ATOM   6707  C CA   . LEU   A  1 460 ? 25.852 -12.795 -40.326 1.00 17.38  ? 486  LEU   A CA   1 
ATOM   6708  C C    . LEU   A  1 460 ? 27.107 -11.985 -40.052 1.00 17.25  ? 486  LEU   A C    1 
ATOM   6709  O O    . LEU   A  1 460 ? 27.692 -11.422 -40.984 1.00 16.31  ? 486  LEU   A O    1 
ATOM   6710  C CB   . LEU   A  1 460 ? 26.143 -13.874 -41.367 1.00 18.03  ? 486  LEU   A CB   1 
ATOM   6711  C CG   . LEU   A  1 460 ? 27.290 -14.850 -41.047 1.00 18.65  ? 486  LEU   A CG   1 
ATOM   6712  C CD1  . LEU   A  1 460 ? 27.036 -15.590 -39.697 1.00 19.65  ? 486  LEU   A CD1  1 
ATOM   6713  C CD2  . LEU   A  1 460 ? 27.420 -15.856 -42.151 1.00 18.48  ? 486  LEU   A CD2  1 
ATOM   6714  H H    . LEU   A  1 460 ? 25.231 -11.318 -41.634 0.00 18.37  ? 486  LEU   A H    1 
ATOM   6715  H HA   . LEU   A  1 460 ? 25.506 -13.263 -39.406 0.00 18.34  ? 486  LEU   A HA   1 
ATOM   6716  H HB2  . LEU   A  1 460 ? 25.241 -14.470 -41.497 0.00 19.77  ? 486  LEU   A HB2  1 
ATOM   6717  H HB3  . LEU   A  1 460 ? 26.390 -13.384 -42.308 0.00 19.40  ? 486  LEU   A HB3  1 
ATOM   6718  H HG   . LEU   A  1 460 ? 28.238 -14.319 -40.975 0.00 19.88  ? 486  LEU   A HG   1 
ATOM   6719  H HD11 . LEU   A  1 460 ? 27.740 -16.416 -39.616 0.00 21.55  ? 486  LEU   A HD11 1 
ATOM   6720  H HD12 . LEU   A  1 460 ? 27.186 -14.893 -38.875 0.00 21.13  ? 486  LEU   A HD12 1 
ATOM   6721  H HD13 . LEU   A  1 460 ? 26.014 -15.967 -39.686 0.00 21.73  ? 486  LEU   A HD13 1 
ATOM   6722  H HD21 . LEU   A  1 460 ? 28.319 -16.449 -41.989 0.00 20.40  ? 486  LEU   A HD21 1 
ATOM   6723  H HD22 . LEU   A  1 460 ? 26.540 -16.497 -42.107 0.00 20.72  ? 486  LEU   A HD22 1 
ATOM   6724  H HD23 . LEU   A  1 460 ? 27.470 -15.341 -43.109 0.00 20.40  ? 486  LEU   A HD23 1 
ATOM   6725  N N    . ASP   A  1 461 ? 27.491 -11.877 -38.776 1.00 17.83  ? 487  ASP   A N    1 
ATOM   6726  C CA   . ASP   A  1 461 ? 28.669 -11.112 -38.405 1.00 17.96  ? 487  ASP   A CA   1 
ATOM   6727  C C    . ASP   A  1 461 ? 29.796 -12.065 -38.004 1.00 17.60  ? 487  ASP   A C    1 
ATOM   6728  O O    . ASP   A  1 461 ? 29.734 -12.686 -36.956 1.00 17.33  ? 487  ASP   A O    1 
ATOM   6729  C CB   . ASP   A  1 461 ? 28.335 -10.118 -37.280 1.00 19.32  ? 487  ASP   A CB   1 
ATOM   6730  C CG   . ASP   A  1 461 ? 29.441 -9.127  -36.968 1.00 24.24  ? 487  ASP   A CG   1 
ATOM   6731  O OD1  . ASP   A  1 461 ? 30.616 -9.443  -37.231 1.00 23.27  ? 487  ASP   A OD1  1 
ATOM   6732  O OD2  . ASP   A  1 461 ? 29.129 -8.035  -36.465 1.00 27.90  ? 487  ASP   A OD2  1 
ATOM   6733  H H    . ASP   A  1 461 ? 27.011 -12.299 -37.987 0.00 18.24  ? 487  ASP   A H    1 
ATOM   6734  H HA   . ASP   A  1 461 ? 29.008 -10.534 -39.261 0.00 17.86  ? 487  ASP   A HA   1 
ATOM   6735  H HB2  . ASP   A  1 461 ? 27.452 -9.548  -37.567 0.00 19.37  ? 487  ASP   A HB2  1 
ATOM   6736  H HB3  . ASP   A  1 461 ? 28.138 -10.664 -36.359 0.00 19.37  ? 487  ASP   A HB3  1 
ATOM   6737  N N    . LEU   A  1 462 ? 30.810 -12.181 -38.863 1.00 17.06  ? 488  LEU   A N    1 
ATOM   6738  C CA   . LEU   A  1 462 ? 31.995 -13.005 -38.621 1.00 17.43  ? 488  LEU   A CA   1 
ATOM   6739  C C    . LEU   A  1 462 ? 33.248 -12.123 -38.483 1.00 17.54  ? 488  LEU   A C    1 
ATOM   6740  O O    . LEU   A  1 462 ? 34.369 -12.590 -38.749 1.00 18.31  ? 488  LEU   A O    1 
ATOM   6741  C CB   . LEU   A  1 462 ? 32.166 -13.999 -39.794 1.00 18.02  ? 488  LEU   A CB   1 
ATOM   6742  C CG   . LEU   A  1 462 ? 31.210 -15.190 -39.802 1.00 19.83  ? 488  LEU   A CG   1 
ATOM   6743  C CD1  . LEU   A  1 462 ? 31.115 -15.789 -41.199 1.00 20.22  ? 488  LEU   A CD1  1 
ATOM   6744  C CD2  . LEU   A  1 462 ? 31.639 -16.255 -38.779 1.00 20.51  ? 488  LEU   A CD2  1 
ATOM   6745  H H    . LEU   A  1 462 ? 30.845 -11.701 -39.756 0.00 16.85  ? 488  LEU   A H    1 
ATOM   6746  H HA   . LEU   A  1 462 ? 31.892 -13.566 -37.694 0.00 17.43  ? 488  LEU   A HA   1 
ATOM   6747  H HB2  . LEU   A  1 462 ? 32.018 -13.458 -40.727 0.00 18.42  ? 488  LEU   A HB2  1 
ATOM   6748  H HB3  . LEU   A  1 462 ? 33.171 -14.417 -39.774 0.00 18.48  ? 488  LEU   A HB3  1 
ATOM   6749  H HG   . LEU   A  1 462 ? 30.209 -14.857 -39.529 0.00 21.00  ? 488  LEU   A HG   1 
ATOM   6750  H HD11 . LEU   A  1 462 ? 30.493 -16.681 -41.160 0.00 22.17  ? 488  LEU   A HD11 1 
ATOM   6751  H HD12 . LEU   A  1 462 ? 30.673 -15.055 -41.871 0.00 21.77  ? 488  LEU   A HD12 1 
ATOM   6752  H HD13 . LEU   A  1 462 ? 32.116 -16.049 -41.541 0.00 21.87  ? 488  LEU   A HD13 1 
ATOM   6753  H HD21 . LEU   A  1 462 ? 30.940 -17.088 -38.836 0.00 22.32  ? 488  LEU   A HD21 1 
ATOM   6754  H HD22 . LEU   A  1 462 ? 32.641 -16.602 -39.023 0.00 22.05  ? 488  LEU   A HD22 1 
ATOM   6755  H HD23 . LEU   A  1 462 ? 31.628 -15.837 -37.775 0.00 21.78  ? 488  LEU   A HD23 1 
ATOM   6756  N N    . SER   A  1 463 ? 33.077 -10.855 -38.053 1.00 16.34  ? 489  SER   A N    1 
ATOM   6757  C CA   . SER   A  1 463 ? 34.199 -9.956  -37.909 1.00 16.08  ? 489  SER   A CA   1 
ATOM   6758  C C    . SER   A  1 463 ? 35.111 -10.403 -36.787 1.00 15.99  ? 489  SER   A C    1 
ATOM   6759  O O    . SER   A  1 463 ? 34.685 -11.118 -35.878 1.00 14.62  ? 489  SER   A O    1 
ATOM   6760  C CB   . SER   A  1 463 ? 33.719 -8.537  -37.638 1.00 16.44  ? 489  SER   A CB   1 
ATOM   6761  O OG   . SER   A  1 463 ? 33.011 -8.452  -36.411 1.00 18.27  ? 489  SER   A OG   1 
ATOM   6762  H H    . SER   A  1 463 ? 32.191 -10.441 -37.782 0.00 15.41  ? 489  SER   A H    1 
ATOM   6763  H HA   . SER   A  1 463 ? 34.775 -9.946  -38.834 0.00 14.92  ? 489  SER   A HA   1 
ATOM   6764  H HB2  . SER   A  1 463 ? 34.578 -7.868  -37.603 0.00 14.90  ? 489  SER   A HB2  1 
ATOM   6765  H HB3  . SER   A  1 463 ? 33.062 -8.264  -38.461 0.00 15.12  ? 489  SER   A HB3  1 
ATOM   6766  H HG   . SER   A  1 463 ? 32.100 -8.833  -36.515 0.00 17.35  ? 489  SER   A HG   1 
ATOM   6767  N N    . LEU   A  1 464 ? 36.390 -10.000 -36.865 1.00 16.27  ? 490  LEU   A N    1 
ATOM   6768  C CA   . LEU   A  1 464 ? 37.356 -10.319 -35.827 1.00 17.59  ? 490  LEU   A CA   1 
ATOM   6769  C C    . LEU   A  1 464 ? 37.492 -11.816 -35.582 1.00 18.03  ? 490  LEU   A C    1 
ATOM   6770  O O    . LEU   A  1 464 ? 37.451 -12.284 -34.446 1.00 18.62  ? 490  LEU   A O    1 
ATOM   6771  C CB   . LEU   A  1 464 ? 37.039 -9.542  -34.536 1.00 18.41  ? 490  LEU   A CB   1 
ATOM   6772  C CG   . LEU   A  1 464 ? 37.083 -7.998  -34.685 1.00 19.71  ? 490  LEU   A CG   1 
ATOM   6773  C CD1  . LEU   A  1 464 ? 36.192 -7.325  -33.656 1.00 20.36  ? 490  LEU   A CD1  1 
ATOM   6774  C CD2  . LEU   A  1 464 ? 38.509 -7.485  -34.574 1.00 20.58  ? 490  LEU   A CD2  1 
ATOM   6775  H H    . LEU   A  1 464 ? 36.773 -9.456  -37.632 0.00 14.90  ? 490  LEU   A H    1 
ATOM   6776  H HA   . LEU   A  1 464 ? 38.329 -9.972  -36.170 0.00 16.53  ? 490  LEU   A HA   1 
ATOM   6777  H HB2  . LEU   A  1 464 ? 36.047 -9.815  -34.180 0.00 17.41  ? 490  LEU   A HB2  1 
ATOM   6778  H HB3  . LEU   A  1 464 ? 37.775 -9.808  -33.778 0.00 17.41  ? 490  LEU   A HB3  1 
ATOM   6779  H HG   . LEU   A  1 464 ? 36.707 -7.691  -35.660 0.00 18.64  ? 490  LEU   A HG   1 
ATOM   6780  H HD11 . LEU   A  1 464 ? 36.266 -6.246  -33.778 0.00 19.17  ? 490  LEU   A HD11 1 
ATOM   6781  H HD12 . LEU   A  1 464 ? 35.163 -7.645  -33.813 0.00 19.39  ? 490  LEU   A HD12 1 
ATOM   6782  H HD13 . LEU   A  1 464 ? 36.524 -7.609  -32.659 0.00 19.35  ? 490  LEU   A HD13 1 
ATOM   6783  H HD21 . LEU   A  1 464 ? 38.502 -6.402  -34.693 0.00 19.48  ? 490  LEU   A HD21 1 
ATOM   6784  H HD22 . LEU   A  1 464 ? 38.907 -7.743  -33.593 0.00 19.67  ? 490  LEU   A HD22 1 
ATOM   6785  H HD23 . LEU   A  1 464 ? 39.116 -7.939  -35.355 0.00 19.74  ? 490  LEU   A HD23 1 
ATOM   6786  N N    . ASN   A  1 465 ? 37.647 -12.565 -36.666 1.00 17.17  ? 491  ASN   A N    1 
ATOM   6787  C CA   . ASN   A  1 465 ? 37.915 -13.999 -36.602 1.00 17.37  ? 491  ASN   A CA   1 
ATOM   6788  C C    . ASN   A  1 465 ? 39.229 -14.215 -37.408 1.00 18.41  ? 491  ASN   A C    1 
ATOM   6789  O O    . ASN   A  1 465 ? 40.015 -13.264 -37.554 1.00 18.61  ? 491  ASN   A O    1 
ATOM   6790  C CB   . ASN   A  1 465 ? 36.679 -14.786 -37.122 1.00 17.95  ? 491  ASN   A CB   1 
ATOM   6791  C CG   . ASN   A  1 465 ? 35.632 -14.980 -36.056 1.00 20.30  ? 491  ASN   A CG   1 
ATOM   6792  O OD1  . ASN   A  1 465 ? 35.795 -15.844 -35.195 1.00 22.12  ? 491  ASN   A OD1  1 
ATOM   6793  N ND2  . ASN   A  1 465 ? 34.560 -14.196 -36.057 1.00 18.09  ? 491  ASN   A ND2  1 
ATOM   6794  H H    . ASN   A  1 465 ? 37.601 -12.211 -37.616 0.00 16.58  ? 491  ASN   A H    1 
ATOM   6795  H HA   . ASN   A  1 465 ? 38.128 -14.310 -35.580 0.00 17.27  ? 491  ASN   A HA   1 
ATOM   6796  H HB2  . ASN   A  1 465 ? 36.238 -14.232 -37.948 0.00 18.05  ? 491  ASN   A HB2  1 
ATOM   6797  H HB3  . ASN   A  1 465 ? 36.956 -15.782 -37.460 0.00 18.46  ? 491  ASN   A HB3  1 
ATOM   6798  H HD21 . ASN   A  1 465 ? 33.847 -14.321 -35.346 0.00 18.16  ? 491  ASN   A HD21 1 
ATOM   6799  H HD22 . ASN   A  1 465 ? 34.447 -13.478 -36.765 0.00 17.99  ? 491  ASN   A HD22 1 
ATOM   6800  N N    . SER   A  1 466 ? 39.505 -15.431 -37.874 1.00 19.41  ? 492  SER   A N    1 
ATOM   6801  C CA   . SER   A  1 466 ? 40.704 -15.766 -38.630 1.00 20.38  ? 492  SER   A CA   1 
ATOM   6802  C C    . SER   A  1 466 ? 40.321 -16.469 -39.939 1.00 20.32  ? 492  SER   A C    1 
ATOM   6803  O O    . SER   A  1 466 ? 40.943 -17.464 -40.309 1.00 20.19  ? 492  SER   A O    1 
ATOM   6804  C CB   . SER   A  1 466 ? 41.585 -16.679 -37.781 1.00 22.82  ? 492  SER   A CB   1 
ATOM   6805  O OG   . SER   A  1 466 ? 41.889 -16.049 -36.554 1.00 27.16  ? 492  SER   A OG   1 
ATOM   6806  H H    . SER   A  1 466 ? 38.948 -16.260 -37.698 0.00 20.43  ? 492  SER   A H    1 
ATOM   6807  H HA   . SER   A  1 466 ? 41.275 -14.875 -38.883 0.00 21.38  ? 492  SER   A HA   1 
ATOM   6808  H HB2  . SER   A  1 466 ? 41.052 -17.609 -37.590 0.00 25.07  ? 492  SER   A HB2  1 
ATOM   6809  H HB3  . SER   A  1 466 ? 42.513 -16.887 -38.308 0.00 25.00  ? 492  SER   A HB3  1 
ATOM   6810  H HG   . SER   A  1 466 ? 41.182 -16.238 -35.883 0.00 29.75  ? 492  SER   A HG   1 
ATOM   6811  N N    . ILE   A  1 467 ? 39.295 -15.966 -40.643 1.00 20.03  ? 493  ILE   A N    1 
ATOM   6812  C CA   . ILE   A  1 467 ? 38.906 -16.545 -41.938 1.00 20.12  ? 493  ILE   A CA   1 
ATOM   6813  C C    . ILE   A  1 467 ? 39.818 -15.809 -42.929 1.00 20.94  ? 493  ILE   A C    1 
ATOM   6814  O O    . ILE   A  1 467 ? 39.387 -14.881 -43.628 1.00 21.48  ? 493  ILE   A O    1 
ATOM   6815  C CB   . ILE   A  1 467 ? 37.393 -16.360 -42.199 1.00 20.10  ? 493  ILE   A CB   1 
ATOM   6816  C CG1  . ILE   A  1 467 ? 36.561 -17.009 -41.049 1.00 20.68  ? 493  ILE   A CG1  1 
ATOM   6817  C CG2  . ILE   A  1 467 ? 36.992 -16.974 -43.566 1.00 20.61  ? 493  ILE   A CG2  1 
ATOM   6818  C CD1  . ILE   A  1 467 ? 35.037 -16.714 -41.159 1.00 21.15  ? 493  ILE   A CD1  1 
ATOM   6819  H H    . ILE   A  1 467 ? 38.730 -15.171 -40.363 0.00 21.05  ? 493  ILE   A H    1 
ATOM   6820  H HA   . ILE   A  1 467 ? 39.124 -17.611 -41.978 0.00 22.12  ? 493  ILE   A HA   1 
ATOM   6821  H HB   . ILE   A  1 467 ? 37.170 -15.294 -42.219 0.00 21.37  ? 493  ILE   A HB   1 
ATOM   6822  H HG12 . ILE   A  1 467 ? 36.696 -18.089 -41.081 0.00 22.82  ? 493  ILE   A HG12 1 
ATOM   6823  H HG13 . ILE   A  1 467 ? 36.892 -16.622 -40.087 0.00 22.22  ? 493  ILE   A HG13 1 
ATOM   6824  H HG21 . ILE   A  1 467 ? 35.950 -16.740 -43.779 0.00 22.66  ? 493  ILE   A HG21 1 
ATOM   6825  H HG22 . ILE   A  1 467 ? 37.615 -16.561 -44.357 0.00 22.66  ? 493  ILE   A HG22 1 
ATOM   6826  H HG23 . ILE   A  1 467 ? 37.125 -18.054 -43.519 0.00 23.04  ? 493  ILE   A HG23 1 
ATOM   6827  H HD11 . ILE   A  1 467 ? 34.566 -16.989 -40.218 0.00 22.96  ? 493  ILE   A HD11 1 
ATOM   6828  H HD12 . ILE   A  1 467 ? 34.891 -15.653 -41.357 0.00 22.67  ? 493  ILE   A HD12 1 
ATOM   6829  H HD13 . ILE   A  1 467 ? 34.613 -17.308 -41.967 0.00 23.28  ? 493  ILE   A HD13 1 
ATOM   6830  N N    A PHE   A  1 468 ? 41.104 -16.182 -42.929 0.50 20.49  ? 494  PHE   A N    1 
ATOM   6831  N N    B PHE   A  1 468 ? 41.096 -16.222 -42.948 0.50 21.22  ? 494  PHE   A N    1 
ATOM   6832  C CA   A PHE   A  1 468 ? 42.122 -15.536 -43.764 0.50 20.70  ? 494  PHE   A CA   1 
ATOM   6833  C CA   B PHE   A  1 468 ? 42.171 -15.652 -43.785 0.50 22.20  ? 494  PHE   A CA   1 
ATOM   6834  C C    A PHE   A  1 468 ? 42.014 -15.863 -45.266 0.50 22.31  ? 494  PHE   A C    1 
ATOM   6835  C C    B PHE   A  1 468 ? 41.959 -15.838 -45.273 0.50 23.05  ? 494  PHE   A C    1 
ATOM   6836  O O    A PHE   A  1 468 ? 42.728 -15.253 -46.065 0.50 22.40  ? 494  PHE   A O    1 
ATOM   6837  O O    B PHE   A  1 468 ? 42.612 -15.164 -46.072 0.50 23.25  ? 494  PHE   A O    1 
ATOM   6838  C CB   A PHE   A  1 468 ? 43.537 -15.860 -43.247 0.50 19.92  ? 494  PHE   A CB   1 
ATOM   6839  C CB   B PHE   A  1 468 ? 43.494 -16.381 -43.505 0.50 22.49  ? 494  PHE   A CB   1 
ATOM   6840  C CG   A PHE   A  1 468 ? 43.938 -17.316 -43.322 0.50 19.85  ? 494  PHE   A CG   1 
ATOM   6841  C CG   B PHE   A  1 468 ? 43.886 -16.481 -42.062 0.50 23.67  ? 494  PHE   A CG   1 
ATOM   6842  C CD1  A PHE   A  1 468 ? 44.479 -17.844 -44.479 0.50 20.34  ? 494  PHE   A CD1  1 
ATOM   6843  C CD1  B PHE   A  1 468 ? 44.040 -15.349 -41.298 0.50 24.79  ? 494  PHE   A CD1  1 
ATOM   6844  C CD2  A PHE   A  1 468 ? 43.789 -18.150 -42.227 0.50 20.35  ? 494  PHE   A CD2  1 
ATOM   6845  C CD2  B PHE   A  1 468 ? 44.110 -17.711 -41.472 0.50 24.90  ? 494  PHE   A CD2  1 
ATOM   6846  C CE1  A PHE   A  1 468 ? 44.849 -19.184 -44.545 0.50 21.04  ? 494  PHE   A CE1  1 
ATOM   6847  C CE1  B PHE   A  1 468 ? 44.417 -15.434 -39.965 0.50 25.66  ? 494  PHE   A CE1  1 
ATOM   6848  C CE2  A PHE   A  1 468 ? 44.167 -19.485 -42.292 0.50 20.84  ? 494  PHE   A CE2  1 
ATOM   6849  C CE2  B PHE   A  1 468 ? 44.488 -17.797 -40.141 0.50 25.99  ? 494  PHE   A CE2  1 
ATOM   6850  C CZ   A PHE   A  1 468 ? 44.688 -19.995 -43.452 0.50 20.58  ? 494  PHE   A CZ   1 
ATOM   6851  C CZ   B PHE   A  1 468 ? 44.652 -16.657 -39.400 0.50 25.57  ? 494  PHE   A CZ   1 
ATOM   6852  H H    A PHE   A  1 468 ? 41.459 -16.929 -42.342 0.00 22.50  ? 494  PHE   A H    1 
ATOM   6853  H H    B PHE   A  1 468 ? 41.399 -17.014 -42.392 0.00 23.40  ? 494  PHE   A H    1 
ATOM   6854  H HA   A PHE   A  1 468 ? 41.990 -14.463 -43.640 0.00 22.16  ? 494  PHE   A HA   1 
ATOM   6855  H HA   B PHE   A  1 468 ? 42.294 -14.592 -43.571 0.00 24.00  ? 494  PHE   A HA   1 
ATOM   6856  H HB2  A PHE   A  1 468 ? 44.257 -15.292 -43.834 0.00 21.70  ? 494  PHE   A HB2  1 
ATOM   6857  H HB2  B PHE   A  1 468 ? 43.419 -17.390 -43.908 0.00 25.40  ? 494  PHE   A HB2  1 
ATOM   6858  H HB3  A PHE   A  1 468 ? 43.600 -15.557 -42.203 0.00 21.53  ? 494  PHE   A HB3  1 
ATOM   6859  H HB3  B PHE   A  1 468 ? 44.291 -15.847 -44.020 0.00 24.96  ? 494  PHE   A HB3  1 
ATOM   6860  H HD1  A PHE   A  1 468 ? 44.603 -17.215 -45.344 0.00 23.08  ? 494  PHE   A HD1  1 
ATOM   6861  H HD1  B PHE   A  1 468 ? 43.880 -14.408 -41.782 0.00 27.02  ? 494  PHE   A HD1  1 
ATOM   6862  H HD2  A PHE   A  1 468 ? 43.375 -17.760 -41.312 0.00 22.68  ? 494  PHE   A HD2  1 
ATOM   6863  H HD2  B PHE   A  1 468 ? 43.997 -18.614 -42.048 0.00 28.61  ? 494  PHE   A HD2  1 
ATOM   6864  H HE1  A PHE   A  1 468 ? 45.264 -19.583 -45.455 0.00 24.90  ? 494  PHE   A HE1  1 
ATOM   6865  H HE1  B PHE   A  1 468 ? 44.543 -14.538 -39.382 0.00 28.02  ? 494  PHE   A HE1  1 
ATOM   6866  H HE2  A PHE   A  1 468 ? 44.039 -20.123 -41.434 0.00 24.23  ? 494  PHE   A HE2  1 
ATOM   6867  H HE2  B PHE   A  1 468 ? 44.658 -18.762 -39.693 0.00 29.88  ? 494  PHE   A HE2  1 
ATOM   6868  H HZ   A PHE   A  1 468 ? 44.981 -21.031 -43.502 0.00 24.64  ? 494  PHE   A HZ   1 
ATOM   6869  H HZ   B PHE   A  1 468 ? 44.930 -16.728 -38.362 0.00 28.62  ? 494  PHE   A HZ   1 
ATOM   6870  N N    . PHE   A  1 469 ? 41.188 -16.861 -45.638 1.00 23.26  ? 495  PHE   A N    1 
ATOM   6871  C CA   . PHE   A  1 469 ? 40.956 -17.255 -47.022 1.00 25.72  ? 495  PHE   A CA   1 
ATOM   6872  C C    . PHE   A  1 469 ? 39.561 -17.864 -47.072 1.00 26.84  ? 495  PHE   A C    1 
ATOM   6873  O O    . PHE   A  1 469 ? 39.216 -18.662 -46.198 1.00 27.63  ? 495  PHE   A O    1 
ATOM   6874  C CB   . PHE   A  1 469 ? 42.011 -18.304 -47.432 1.00 26.52  ? 495  PHE   A CB   1 
ATOM   6875  C CG   . PHE   A  1 469 ? 41.843 -18.899 -48.809 1.00 28.09  ? 495  PHE   A CG   1 
ATOM   6876  C CD1  . PHE   A  1 469 ? 42.386 -18.277 -49.920 1.00 29.31  ? 495  PHE   A CD1  1 
ATOM   6877  C CD2  . PHE   A  1 469 ? 41.231 -20.133 -48.980 1.00 29.24  ? 495  PHE   A CD2  1 
ATOM   6878  C CE1  . PHE   A  1 469 ? 42.280 -18.852 -51.187 1.00 30.15  ? 495  PHE   A CE1  1 
ATOM   6879  C CE2  . PHE   A  1 469 ? 41.121 -20.705 -50.246 1.00 30.32  ? 495  PHE   A CE2  1 
ATOM   6880  C CZ   . PHE   A  1 469 ? 41.612 -20.042 -51.348 1.00 30.10  ? 495  PHE   A CZ   1 
ATOM   6881  H H    . PHE   A  1 469 ? 40.698 -17.458 -44.979 0.00 26.31  ? 495  PHE   A H    1 
ATOM   6882  H HA   . PHE   A  1 469 ? 41.009 -16.400 -47.694 0.00 29.36  ? 495  PHE   A HA   1 
ATOM   6883  H HB2  . PHE   A  1 469 ? 42.992 -17.833 -47.399 0.00 30.89  ? 495  PHE   A HB2  1 
ATOM   6884  H HB3  . PHE   A  1 469 ? 41.978 -19.123 -46.714 0.00 31.18  ? 495  PHE   A HB3  1 
ATOM   6885  H HD1  . PHE   A  1 469 ? 42.889 -17.331 -49.806 0.00 34.49  ? 495  PHE   A HD1  1 
ATOM   6886  H HD2  . PHE   A  1 469 ? 40.816 -20.645 -48.128 0.00 35.23  ? 495  PHE   A HD2  1 
ATOM   6887  H HE1  . PHE   A  1 469 ? 42.676 -18.337 -52.046 0.00 36.34  ? 495  PHE   A HE1  1 
ATOM   6888  H HE2  . PHE   A  1 469 ? 40.608 -21.644 -50.369 0.00 37.41  ? 495  PHE   A HE2  1 
ATOM   6889  H HZ   . PHE   A  1 469 ? 41.537 -20.490 -52.325 0.00 37.14  ? 495  PHE   A HZ   1 
ATOM   6890  N N    . ILE   A  1 470 ? 38.741 -17.424 -48.019 1.00 26.63  ? 496  ILE   A N    1 
ATOM   6891  C CA   . ILE   A  1 470 ? 37.385 -17.914 -48.217 1.00 27.27  ? 496  ILE   A CA   1 
ATOM   6892  C C    . ILE   A  1 470 ? 37.487 -19.011 -49.266 1.00 29.64  ? 496  ILE   A C    1 
ATOM   6893  O O    . ILE   A  1 470 ? 37.778 -18.719 -50.431 1.00 29.31  ? 496  ILE   A O    1 
ATOM   6894  C CB   . ILE   A  1 470 ? 36.442 -16.771 -48.666 1.00 26.66  ? 496  ILE   A CB   1 
ATOM   6895  C CG1  . ILE   A  1 470 ? 36.367 -15.657 -47.585 1.00 27.32  ? 496  ILE   A CG1  1 
ATOM   6896  C CG2  . ILE   A  1 470 ? 35.052 -17.323 -48.983 1.00 26.77  ? 496  ILE   A CG2  1 
ATOM   6897  C CD1  . ILE   A  1 470 ? 35.833 -14.336 -48.080 1.00 28.31  ? 496  ILE   A CD1  1 
ATOM   6898  H H    . ILE   A  1 470 ? 39.000 -16.704 -48.684 0.00 30.69  ? 496  ILE   A H    1 
ATOM   6899  H HA   . ILE   A  1 470 ? 36.978 -18.328 -47.296 0.00 31.76  ? 496  ILE   A HA   1 
ATOM   6900  H HB   . ILE   A  1 470 ? 36.845 -16.334 -49.578 0.00 30.83  ? 496  ILE   A HB   1 
ATOM   6901  H HG12 . ILE   A  1 470 ? 35.709 -15.997 -46.787 0.00 30.98  ? 496  ILE   A HG12 1 
ATOM   6902  H HG13 . ILE   A  1 470 ? 37.361 -15.467 -47.183 0.00 30.84  ? 496  ILE   A HG13 1 
ATOM   6903  H HG21 . ILE   A  1 470 ? 34.379 -16.491 -49.180 0.00 31.03  ? 496  ILE   A HG21 1 
ATOM   6904  H HG22 . ILE   A  1 470 ? 35.092 -17.957 -49.868 0.00 31.64  ? 496  ILE   A HG22 1 
ATOM   6905  H HG23 . ILE   A  1 470 ? 34.697 -17.894 -48.127 0.00 31.26  ? 496  ILE   A HG23 1 
ATOM   6906  H HD11 . ILE   A  1 470 ? 36.080 -13.563 -47.355 0.00 31.55  ? 496  ILE   A HD11 1 
ATOM   6907  H HD12 . ILE   A  1 470 ? 36.291 -14.102 -49.040 0.00 32.02  ? 496  ILE   A HD12 1 
ATOM   6908  H HD13 . ILE   A  1 470 ? 34.752 -14.410 -48.192 0.00 32.02  ? 496  ILE   A HD13 1 
ATOM   6909  N N    . GLY   A  1 471 ? 37.302 -20.253 -48.832 1.00 31.67  ? 497  GLY   A N    1 
ATOM   6910  C CA   . GLY   A  1 471 ? 37.329 -21.424 -49.697 1.00 34.32  ? 497  GLY   A CA   1 
ATOM   6911  C C    . GLY   A  1 471 ? 35.978 -21.672 -50.348 1.00 36.33  ? 497  GLY   A C    1 
ATOM   6912  O O    . GLY   A  1 471 ? 34.971 -21.073 -49.951 1.00 36.69  ? 497  GLY   A O    1 
ATOM   6913  H H    . GLY   A  1 471 ? 37.137 -20.494 -47.860 0.00 37.98  ? 497  GLY   A H    1 
ATOM   6914  H HA2  . GLY   A  1 471 ? 38.084 -21.293 -50.471 0.00 42.04  ? 497  GLY   A HA2  1 
ATOM   6915  H HA3  . GLY   A  1 471 ? 37.592 -22.301 -49.108 0.00 42.16  ? 497  GLY   A HA3  1 
ATOM   6916  N N    . PRO   A  1 472 ? 35.914 -22.602 -51.316 1.00 37.42  ? 498  PRO   A N    1 
ATOM   6917  C CA   . PRO   A  1 472 ? 34.644 -22.839 -52.017 1.00 38.10  ? 498  PRO   A CA   1 
ATOM   6918  C C    . PRO   A  1 472 ? 33.452 -23.303 -51.175 1.00 38.60  ? 498  PRO   A C    1 
ATOM   6919  O O    . PRO   A  1 472 ? 32.336 -23.110 -51.633 1.00 39.64  ? 498  PRO   A O    1 
ATOM   6920  C CB   . PRO   A  1 472 ? 35.005 -23.882 -53.084 1.00 39.17  ? 498  PRO   A CB   1 
ATOM   6921  C CG   . PRO   A  1 472 ? 36.305 -24.463 -52.661 1.00 39.68  ? 498  PRO   A CG   1 
ATOM   6922  C CD   . PRO   A  1 472 ? 37.015 -23.389 -51.906 1.00 37.61  ? 498  PRO   A CD   1 
ATOM   6923  H HA   . PRO   A  1 472 ? 34.350 -21.925 -52.529 0.00 47.49  ? 498  PRO   A HA   1 
ATOM   6924  H HB2  . PRO   A  1 472 ? 34.233 -24.650 -53.120 0.00 50.16  ? 498  PRO   A HB2  1 
ATOM   6925  H HB3  . PRO   A  1 472 ? 35.103 -23.398 -54.053 0.00 49.80  ? 498  PRO   A HB3  1 
ATOM   6926  H HG2  . PRO   A  1 472 ? 36.126 -25.326 -52.020 0.00 50.71  ? 498  PRO   A HG2  1 
ATOM   6927  H HG3  . PRO   A  1 472 ? 36.877 -24.755 -53.540 0.00 50.82  ? 498  PRO   A HG3  1 
ATOM   6928  H HD2  . PRO   A  1 472 ? 37.638 -23.828 -51.128 0.00 47.25  ? 498  PRO   A HD2  1 
ATOM   6929  H HD3  . PRO   A  1 472 ? 37.602 -22.772 -52.585 0.00 47.14  ? 498  PRO   A HD3  1 
ATOM   6930  N N    . ASN   A  1 473 ? 33.649 -23.869 -49.967 1.00 38.02  ? 499  ASN   A N    1 
ATOM   6931  C CA   . ASN   A  1 473 ? 32.533 -24.339 -49.124 1.00 37.88  ? 499  ASN   A CA   1 
ATOM   6932  C C    . ASN   A  1 473 ? 32.276 -23.468 -47.890 1.00 36.21  ? 499  ASN   A C    1 
ATOM   6933  O O    . ASN   A  1 473 ? 31.433 -23.840 -47.079 1.00 36.49  ? 499  ASN   A O    1 
ATOM   6934  C CB   . ASN   A  1 473 ? 32.808 -25.772 -48.642 1.00 40.45  ? 499  ASN   A CB   1 
ATOM   6935  C CG   . ASN   A  1 473 ? 33.160 -26.719 -49.761 1.00 45.75  ? 499  ASN   A CG   1 
ATOM   6936  O OD1  . ASN   A  1 473 ? 32.566 -26.675 -50.847 1.00 46.72  ? 499  ASN   A OD1  1 
ATOM   6937  N ND2  . ASN   A  1 473 ? 34.138 -27.595 -49.529 1.00 47.63  ? 499  ASN   A ND2  1 
ATOM   6938  H H    . ASN   A  1 473 ? 34.560 -24.025 -49.546 0.00 47.55  ? 499  ASN   A H    1 
ATOM   6939  H HA   . ASN   A  1 473 ? 31.609 -24.373 -49.698 0.00 47.81  ? 499  ASN   A HA   1 
ATOM   6940  H HB2  . ASN   A  1 473 ? 33.630 -25.743 -47.929 0.00 50.96  ? 499  ASN   A HB2  1 
ATOM   6941  H HB3  . ASN   A  1 473 ? 31.915 -26.164 -48.158 0.00 51.34  ? 499  ASN   A HB3  1 
ATOM   6942  H HD21 . ASN   A  1 473 ? 34.403 -28.252 -50.255 0.00 61.35  ? 499  ASN   A HD21 1 
ATOM   6943  H HD22 . ASN   A  1 473 ? 34.613 -27.619 -48.632 0.00 60.62  ? 499  ASN   A HD22 1 
ATOM   6944  N N    . GLN   A  1 474 ? 32.972 -22.326 -47.733 1.00 34.64  ? 500  GLN   A N    1 
ATOM   6945  C CA   . GLN   A  1 474 ? 32.832 -21.483 -46.540 1.00 33.58  ? 500  GLN   A CA   1 
ATOM   6946  C C    . GLN   A  1 474 ? 31.393 -21.090 -46.204 1.00 33.09  ? 500  GLN   A C    1 
ATOM   6947  O O    . GLN   A  1 474 ? 31.012 -21.134 -45.034 1.00 33.15  ? 500  GLN   A O    1 
ATOM   6948  C CB   . GLN   A  1 474 ? 33.686 -20.203 -46.684 1.00 33.87  ? 500  GLN   A CB   1 
ATOM   6949  C CG   . GLN   A  1 474 ? 33.726 -19.298 -45.443 1.00 34.15  ? 500  GLN   A CG   1 
ATOM   6950  C CD   . GLN   A  1 474 ? 34.332 -20.001 -44.249 1.00 35.76  ? 500  GLN   A CD   1 
ATOM   6951  O OE1  . GLN   A  1 474 ? 35.464 -20.489 -44.313 1.00 35.76  ? 500  GLN   A OE1  1 
ATOM   6952  N NE2  . GLN   A  1 474 ? 33.600 -20.097 -43.142 1.00 34.90  ? 500  GLN   A NE2  1 
ATOM   6953  H H    . GLN   A  1 474 ? 33.630 -21.948 -48.407 0.00 42.39  ? 500  GLN   A H    1 
ATOM   6954  H HA   . GLN   A  1 474 ? 33.219 -22.055 -45.698 0.00 40.64  ? 500  GLN   A HA   1 
ATOM   6955  H HB2  . GLN   A  1 474 ? 34.712 -20.488 -46.913 0.00 40.49  ? 500  GLN   A HB2  1 
ATOM   6956  H HB3  . GLN   A  1 474 ? 33.276 -19.617 -47.505 0.00 40.37  ? 500  GLN   A HB3  1 
ATOM   6957  H HG2  . GLN   A  1 474 ? 34.362 -18.443 -45.669 0.00 39.85  ? 500  GLN   A HG2  1 
ATOM   6958  H HG3  . GLN   A  1 474 ? 32.727 -18.945 -45.195 0.00 40.06  ? 500  GLN   A HG3  1 
ATOM   6959  H HE21 . GLN   A  1 474 ? 32.663 -19.708 -43.100 0.00 40.90  ? 500  GLN   A HE21 1 
ATOM   6960  H HE22 . GLN   A  1 474 ? 33.987 -20.562 -42.327 0.00 41.02  ? 500  GLN   A HE22 1 
ATOM   6961  N N    . PHE   A  1 475 ? 30.613 -20.669 -47.206 1.00 32.31  ? 501  PHE   A N    1 
ATOM   6962  C CA   . PHE   A  1 475 ? 29.254 -20.178 -46.972 1.00 32.44  ? 501  PHE   A CA   1 
ATOM   6963  C C    . PHE   A  1 475 ? 28.153 -21.143 -47.409 1.00 33.69  ? 501  PHE   A C    1 
ATOM   6964  O O    . PHE   A  1 475 ? 27.014 -20.728 -47.633 1.00 34.13  ? 501  PHE   A O    1 
ATOM   6965  C CB   . PHE   A  1 475 ? 29.108 -18.804 -47.654 1.00 31.68  ? 501  PHE   A CB   1 
ATOM   6966  C CG   . PHE   A  1 475 ? 30.104 -17.800 -47.113 1.00 31.71  ? 501  PHE   A CG   1 
ATOM   6967  C CD1  . PHE   A  1 475 ? 30.118 -17.467 -45.768 1.00 32.17  ? 501  PHE   A CD1  1 
ATOM   6968  C CD2  . PHE   A  1 475 ? 31.036 -17.205 -47.943 1.00 32.30  ? 501  PHE   A CD2  1 
ATOM   6969  C CE1  . PHE   A  1 475 ? 31.041 -16.560 -45.268 1.00 32.74  ? 501  PHE   A CE1  1 
ATOM   6970  C CE2  . PHE   A  1 475 ? 31.950 -16.283 -47.439 1.00 33.05  ? 501  PHE   A CE2  1 
ATOM   6971  C CZ   . PHE   A  1 475 ? 31.953 -15.976 -46.107 1.00 32.70  ? 501  PHE   A CZ   1 
ATOM   6972  H H    . PHE   A  1 475 ? 30.895 -20.649 -48.180 0.00 39.27  ? 501  PHE   A H    1 
ATOM   6973  H HA   . PHE   A  1 475 ? 29.114 -20.022 -45.905 0.00 38.94  ? 501  PHE   A HA   1 
ATOM   6974  H HB2  . PHE   A  1 475 ? 29.277 -18.921 -48.723 0.00 38.22  ? 501  PHE   A HB2  1 
ATOM   6975  H HB3  . PHE   A  1 475 ? 28.111 -18.405 -47.475 0.00 37.93  ? 501  PHE   A HB3  1 
ATOM   6976  H HD1  . PHE   A  1 475 ? 29.414 -17.934 -45.100 0.00 37.66  ? 501  PHE   A HD1  1 
ATOM   6977  H HD2  . PHE   A  1 475 ? 31.045 -17.435 -48.995 0.00 38.28  ? 501  PHE   A HD2  1 
ATOM   6978  H HE1  . PHE   A  1 475 ? 31.046 -16.318 -44.219 0.00 37.48  ? 501  PHE   A HE1  1 
ATOM   6979  H HE2  . PHE   A  1 475 ? 32.664 -15.816 -48.094 0.00 38.28  ? 501  PHE   A HE2  1 
ATOM   6980  H HZ   . PHE   A  1 475 ? 32.672 -15.278 -45.715 0.00 37.23  ? 501  PHE   A HZ   1 
ATOM   6981  N N    . GLU   A  1 476 ? 28.464 -22.436 -47.453 1.00 34.33  ? 502  GLU   A N    1 
ATOM   6982  C CA   . GLU   A  1 476 ? 27.498 -23.455 -47.840 1.00 35.58  ? 502  GLU   A CA   1 
ATOM   6983  C C    . GLU   A  1 476 ? 26.467 -23.661 -46.721 1.00 36.19  ? 502  GLU   A C    1 
ATOM   6984  O O    . GLU   A  1 476 ? 26.798 -23.500 -45.540 1.00 36.85  ? 502  GLU   A O    1 
ATOM   6985  C CB   . GLU   A  1 476 ? 28.230 -24.778 -48.112 1.00 38.37  ? 502  GLU   A CB   1 
ATOM   6986  C CG   . GLU   A  1 476 ? 27.363 -25.857 -48.733 1.00 45.97  ? 502  GLU   A CG   1 
ATOM   6987  C CD   . GLU   A  1 476 ? 28.072 -27.172 -48.996 1.00 55.76  ? 502  GLU   A CD   1 
ATOM   6988  O OE1  . GLU   A  1 476 ? 29.203 -27.359 -48.489 1.00 57.50  ? 502  GLU   A OE1  1 
ATOM   6989  O OE2  . GLU   A  1 476 ? 27.487 -28.025 -49.703 1.00 58.70  ? 502  GLU   A OE2  1 
ATOM   6990  H H    . GLU   A  1 476 ? 29.371 -22.817 -47.203 0.00 42.54  ? 502  GLU   A H    1 
ATOM   6991  H HA   . GLU   A  1 476 ? 26.983 -23.151 -48.749 0.00 44.92  ? 502  GLU   A HA   1 
ATOM   6992  H HB2  . GLU   A  1 476 ? 29.062 -24.587 -48.789 0.00 48.57  ? 502  GLU   A HB2  1 
ATOM   6993  H HB3  . GLU   A  1 476 ? 28.608 -25.157 -47.164 0.00 48.53  ? 502  GLU   A HB3  1 
ATOM   6994  H HG2  . GLU   A  1 476 ? 26.526 -26.077 -48.071 0.00 58.62  ? 502  GLU   A HG2  1 
ATOM   6995  H HG3  . GLU   A  1 476 ? 26.987 -25.493 -49.688 0.00 58.67  ? 502  GLU   A HG3  1 
ATOM   6996  N N    . ASN   A  1 477 ? 25.229 -24.030 -47.098 1.00 35.73  ? 503  ASN   A N    1 
ATOM   6997  C CA   . ASN   A  1 477 ? 24.140 -24.349 -46.168 1.00 36.09  ? 503  ASN   A CA   1 
ATOM   6998  C C    . ASN   A  1 477 ? 23.731 -23.181 -45.249 1.00 36.17  ? 503  ASN   A C    1 
ATOM   6999  O O    . ASN   A  1 477 ? 23.183 -23.398 -44.167 1.00 36.31  ? 503  ASN   A O    1 
ATOM   7000  C CB   . ASN   A  1 477 ? 24.523 -25.572 -45.326 1.00 37.66  ? 503  ASN   A CB   1 
ATOM   7001  C CG   . ASN   A  1 477 ? 25.021 -26.735 -46.149 1.00 41.65  ? 503  ASN   A CG   1 
ATOM   7002  O OD1  . ASN   A  1 477 ? 24.415 -27.102 -47.161 1.00 42.54  ? 503  ASN   A OD1  1 
ATOM   7003  N ND2  . ASN   A  1 477 ? 26.141 -27.337 -45.749 1.00 43.16  ? 503  ASN   A ND2  1 
ATOM   7004  H H    . ASN   A  1 477 ? 24.949 -24.120 -48.070 0.00 45.75  ? 503  ASN   A H    1 
ATOM   7005  H HA   . ASN   A  1 477 ? 23.262 -24.620 -46.753 0.00 46.45  ? 503  ASN   A HA   1 
ATOM   7006  H HB2  . ASN   A  1 477 ? 25.294 -25.279 -44.615 0.00 47.75  ? 503  ASN   A HB2  1 
ATOM   7007  H HB3  . ASN   A  1 477 ? 23.641 -25.916 -44.787 0.00 48.42  ? 503  ASN   A HB3  1 
ATOM   7008  H HD21 . ASN   A  1 477 ? 26.503 -28.123 -46.280 0.00 55.84  ? 503  ASN   A HD21 1 
ATOM   7009  H HD22 . ASN   A  1 477 ? 26.634 -27.023 -44.920 0.00 54.98  ? 503  ASN   A HD22 1 
ATOM   7010  N N    . LEU   A  1 478 ? 23.947 -21.957 -45.706 1.00 35.84  ? 504  LEU   A N    1 
ATOM   7011  C CA   . LEU   A  1 478 ? 23.636 -20.755 -44.945 1.00 36.36  ? 504  LEU   A CA   1 
ATOM   7012  C C    . LEU   A  1 478 ? 22.268 -20.234 -45.388 1.00 35.94  ? 504  LEU   A C    1 
ATOM   7013  O O    . LEU   A  1 478 ? 21.895 -20.447 -46.544 1.00 36.36  ? 504  LEU   A O    1 
ATOM   7014  C CB   . LEU   A  1 478 ? 24.724 -19.701 -45.268 1.00 37.38  ? 504  LEU   A CB   1 
ATOM   7015  C CG   . LEU   A  1 478 ? 25.436 -18.923 -44.156 1.00 39.80  ? 504  LEU   A CG   1 
ATOM   7016  C CD1  . LEU   A  1 478 ? 25.717 -19.768 -42.941 1.00 40.60  ? 504  LEU   A CD1  1 
ATOM   7017  C CD2  . LEU   A  1 478 ? 26.734 -18.385 -44.672 1.00 40.51  ? 504  LEU   A CD2  1 
ATOM   7018  H H    . LEU   A  1 478 ? 24.291 -21.757 -46.641 0.00 44.71  ? 504  LEU   A H    1 
ATOM   7019  H HA   . LEU   A  1 478 ? 23.615 -20.974 -43.879 0.00 44.59  ? 504  LEU   A HA   1 
ATOM   7020  H HB2  . LEU   A  1 478 ? 25.528 -20.183 -45.823 0.00 45.51  ? 504  LEU   A HB2  1 
ATOM   7021  H HB3  . LEU   A  1 478 ? 24.265 -18.954 -45.914 0.00 45.38  ? 504  LEU   A HB3  1 
ATOM   7022  H HG   . LEU   A  1 478 ? 24.824 -18.075 -43.854 0.00 47.47  ? 504  LEU   A HG   1 
ATOM   7023  H HD11 . LEU   A  1 478 ? 26.563 -19.352 -42.396 0.00 48.22  ? 504  LEU   A HD11 1 
ATOM   7024  H HD12 . LEU   A  1 478 ? 24.836 -19.778 -42.300 0.00 48.70  ? 504  LEU   A HD12 1 
ATOM   7025  H HD13 . LEU   A  1 478 ? 25.939 -20.773 -43.296 0.00 49.00  ? 504  LEU   A HD13 1 
ATOM   7026  H HD21 . LEU   A  1 478 ? 27.029 -17.513 -44.092 0.00 47.73  ? 504  LEU   A HD21 1 
ATOM   7027  H HD22 . LEU   A  1 478 ? 27.488 -19.162 -44.564 0.00 48.25  ? 504  LEU   A HD22 1 
ATOM   7028  H HD23 . LEU   A  1 478 ? 26.616 -18.110 -45.719 0.00 48.32  ? 504  LEU   A HD23 1 
ATOM   7029  N N    . PRO   A  1 479 ? 21.499 -19.530 -44.525 1.00 34.88  ? 505  PRO   A N    1 
ATOM   7030  C CA   . PRO   A  1 479 ? 20.247 -18.923 -45.019 1.00 34.10  ? 505  PRO   A CA   1 
ATOM   7031  C C    . PRO   A  1 479 ? 20.547 -17.777 -46.022 1.00 33.34  ? 505  PRO   A C    1 
ATOM   7032  O O    . PRO   A  1 479 ? 21.719 -17.516 -46.340 1.00 33.39  ? 505  PRO   A O    1 
ATOM   7033  C CB   . PRO   A  1 479 ? 19.543 -18.454 -43.743 1.00 35.22  ? 505  PRO   A CB   1 
ATOM   7034  C CG   . PRO   A  1 479 ? 20.603 -18.322 -42.714 1.00 35.93  ? 505  PRO   A CG   1 
ATOM   7035  C CD   . PRO   A  1 479 ? 21.797 -19.134 -43.132 1.00 34.40  ? 505  PRO   A CD   1 
ATOM   7036  H HA   . PRO   A  1 479 ? 19.625 -19.673 -45.504 0.00 42.77  ? 505  PRO   A HA   1 
ATOM   7037  H HB2  . PRO   A  1 479 ? 19.060 -17.496 -43.929 0.00 43.27  ? 505  PRO   A HB2  1 
ATOM   7038  H HB3  . PRO   A  1 479 ? 18.810 -19.201 -43.441 0.00 43.74  ? 505  PRO   A HB3  1 
ATOM   7039  H HG2  . PRO   A  1 479 ? 20.880 -17.272 -42.636 0.00 43.24  ? 505  PRO   A HG2  1 
ATOM   7040  H HG3  . PRO   A  1 479 ? 20.222 -18.682 -41.759 0.00 43.60  ? 505  PRO   A HG3  1 
ATOM   7041  H HD2  . PRO   A  1 479 ? 22.694 -18.519 -43.093 0.00 41.48  ? 505  PRO   A HD2  1 
ATOM   7042  H HD3  . PRO   A  1 479 ? 21.893 -20.015 -42.499 0.00 42.12  ? 505  PRO   A HD3  1 
ATOM   7043  N N    . ASP   A  1 480 ? 19.501 -17.132 -46.574 1.00 32.20  ? 506  ASP   A N    1 
ATOM   7044  C CA   . ASP   A  1 480 ? 19.681 -16.053 -47.549 1.00 31.52  ? 506  ASP   A CA   1 
ATOM   7045  C C    . ASP   A  1 480 ? 20.240 -14.824 -46.834 1.00 28.95  ? 506  ASP   A C    1 
ATOM   7046  O O    . ASP   A  1 480 ? 19.484 -13.958 -46.396 1.00 29.29  ? 506  ASP   A O    1 
ATOM   7047  C CB   . ASP   A  1 480 ? 18.347 -15.732 -48.264 1.00 34.27  ? 506  ASP   A CB   1 
ATOM   7048  C CG   . ASP   A  1 480 ? 18.445 -14.654 -49.340 1.00 39.54  ? 506  ASP   A CG   1 
ATOM   7049  O OD1  . ASP   A  1 480 ? 19.528 -14.037 -49.473 1.00 40.85  ? 506  ASP   A OD1  1 
ATOM   7050  O OD2  . ASP   A  1 480 ? 17.440 -14.429 -50.045 1.00 41.37  ? 506  ASP   A OD2  1 
ATOM   7051  H H    . ASP   A  1 480 ? 18.530 -17.335 -46.362 0.00 40.25  ? 506  ASP   A H    1 
ATOM   7052  H HA   . ASP   A  1 480 ? 20.395 -16.362 -48.312 0.00 39.04  ? 506  ASP   A HA   1 
ATOM   7053  H HB2  . ASP   A  1 480 ? 17.996 -16.641 -48.751 0.00 43.29  ? 506  ASP   A HB2  1 
ATOM   7054  H HB3  . ASP   A  1 480 ? 17.612 -15.408 -47.529 0.00 42.74  ? 506  ASP   A HB3  1 
ATOM   7055  N N    . ILE   A  1 481 ? 21.572 -14.754 -46.721 1.00 26.40  ? 507  ILE   A N    1 
ATOM   7056  C CA   . ILE   A  1 481 ? 22.232 -13.658 -46.037 1.00 25.02  ? 507  ILE   A CA   1 
ATOM   7057  C C    . ILE   A  1 481 ? 22.216 -12.413 -46.909 1.00 24.18  ? 507  ILE   A C    1 
ATOM   7058  O O    . ILE   A  1 481 ? 22.641 -12.475 -48.060 1.00 25.39  ? 507  ILE   A O    1 
ATOM   7059  C CB   . ILE   A  1 481 ? 23.681 -14.051 -45.635 1.00 24.99  ? 507  ILE   A CB   1 
ATOM   7060  C CG1  . ILE   A  1 481 ? 23.698 -15.291 -44.679 1.00 24.95  ? 507  ILE   A CG1  1 
ATOM   7061  C CG2  . ILE   A  1 481 ? 24.402 -12.865 -45.004 1.00 25.15  ? 507  ILE   A CG2  1 
ATOM   7062  C CD1  . ILE   A  1 481 ? 22.944 -15.142 -43.338 1.00 25.13  ? 507  ILE   A CD1  1 
ATOM   7063  H H    . ILE   A  1 481 ? 22.210 -15.447 -47.101 0.00 31.84  ? 507  ILE   A H    1 
ATOM   7064  H HA   . ILE   A  1 481 ? 21.689 -13.429 -45.122 0.00 29.37  ? 507  ILE   A HA   1 
ATOM   7065  H HB   . ILE   A  1 481 ? 24.220 -14.320 -46.543 0.00 29.22  ? 507  ILE   A HB   1 
ATOM   7066  H HG12 . ILE   A  1 481 ? 23.263 -16.140 -45.203 0.00 29.61  ? 507  ILE   A HG12 1 
ATOM   7067  H HG13 . ILE   A  1 481 ? 24.736 -15.520 -44.439 0.00 28.95  ? 507  ILE   A HG13 1 
ATOM   7068  H HG21 . ILE   A  1 481 ? 25.227 -13.232 -44.398 0.00 28.49  ? 507  ILE   A HG21 1 
ATOM   7069  H HG22 . ILE   A  1 481 ? 24.794 -12.222 -45.791 0.00 28.62  ? 507  ILE   A HG22 1 
ATOM   7070  H HG23 . ILE   A  1 481 ? 23.700 -12.310 -44.382 0.00 28.61  ? 507  ILE   A HG23 1 
ATOM   7071  H HD11 . ILE   A  1 481 ? 23.168 -16.007 -42.714 0.00 29.35  ? 507  ILE   A HD11 1 
ATOM   7072  H HD12 . ILE   A  1 481 ? 23.268 -14.233 -42.833 0.00 28.86  ? 507  ILE   A HD12 1 
ATOM   7073  H HD13 . ILE   A  1 481 ? 21.873 -15.102 -43.530 0.00 29.56  ? 507  ILE   A HD13 1 
ATOM   7074  N N    . ALA   A  1 482 ? 21.739 -11.291 -46.349 1.00 22.57  ? 508  ALA   A N    1 
ATOM   7075  C CA   . ALA   A  1 482 ? 21.697 -9.972  -46.983 1.00 22.27  ? 508  ALA   A CA   1 
ATOM   7076  C C    . ALA   A  1 482 ? 22.810 -9.045  -46.453 1.00 21.60  ? 508  ALA   A C    1 
ATOM   7077  O O    . ALA   A  1 482 ? 23.229 -8.123  -47.157 1.00 20.65  ? 508  ALA   A O    1 
ATOM   7078  C CB   . ALA   A  1 482 ? 20.359 -9.321  -46.698 1.00 22.02  ? 508  ALA   A CB   1 
ATOM   7079  H H    . ALA   A  1 482 ? 21.352 -11.261 -45.410 0.00 26.09  ? 508  ALA   A H    1 
ATOM   7080  H HA   . ALA   A  1 482 ? 21.796 -10.060 -48.064 0.00 25.96  ? 508  ALA   A HA   1 
ATOM   7081  H HB1  . ALA   A  1 482 ? 20.283 -8.405  -47.281 0.00 25.64  ? 508  ALA   A HB1  1 
ATOM   7082  H HB2  . ALA   A  1 482 ? 19.563 -10.010 -46.978 0.00 26.08  ? 508  ALA   A HB2  1 
ATOM   7083  H HB3  . ALA   A  1 482 ? 20.296 -9.091  -45.635 0.00 25.41  ? 508  ALA   A HB3  1 
ATOM   7084  N N    . CYS   A  1 483 ? 23.232 -9.240  -45.194 1.00 20.62  ? 509  CYS   A N    1 
ATOM   7085  C CA   . CYS   A  1 483 ? 24.209 -8.380  -44.543 1.00 21.00  ? 509  CYS   A CA   1 
ATOM   7086  C C    . CYS   A  1 483 ? 25.328 -9.281  -44.032 1.00 21.05  ? 509  CYS   A C    1 
ATOM   7087  O O    . CYS   A  1 483 ? 25.074 -10.164 -43.216 1.00 21.76  ? 509  CYS   A O    1 
ATOM   7088  C CB   . CYS   A  1 483 ? 23.513 -7.613  -43.417 1.00 21.49  ? 509  CYS   A CB   1 
ATOM   7089  S SG   . CYS   A  1 483 ? 24.618 -6.876  -42.180 1.00 24.91  ? 509  CYS   A SG   1 
ATOM   7090  H H    . CYS   A  1 483 ? 22.907 -9.986  -44.587 0.00 22.93  ? 509  CYS   A H    1 
ATOM   7091  H HA   . CYS   A  1 483 ? 24.633 -7.656  -45.237 0.00 22.71  ? 509  CYS   A HA   1 
ATOM   7092  H HB2  . CYS   A  1 483 ? 22.934 -6.805  -43.862 0.00 23.35  ? 509  CYS   A HB2  1 
ATOM   7093  H HB3  . CYS   A  1 483 ? 22.842 -8.297  -42.897 0.00 23.41  ? 509  CYS   A HB3  1 
ATOM   7094  N N    . LEU   A  1 484 ? 26.558 -9.088  -44.534 1.00 20.57  ? 510  LEU   A N    1 
ATOM   7095  C CA   . LEU   A  1 484 ? 27.675 -9.948  -44.155 1.00 20.21  ? 510  LEU   A CA   1 
ATOM   7096  C C    . LEU   A  1 484 ? 28.846 -9.112  -43.709 1.00 19.62  ? 510  LEU   A C    1 
ATOM   7097  O O    . LEU   A  1 484 ? 29.300 -8.227  -44.442 1.00 19.47  ? 510  LEU   A O    1 
ATOM   7098  C CB   . LEU   A  1 484 ? 28.091 -10.805 -45.361 1.00 20.61  ? 510  LEU   A CB   1 
ATOM   7099  C CG   . LEU   A  1 484 ? 29.303 -11.732 -45.164 1.00 23.14  ? 510  LEU   A CG   1 
ATOM   7100  C CD1  . LEU   A  1 484 ? 29.046 -12.759 -44.026 1.00 24.04  ? 510  LEU   A CD1  1 
ATOM   7101  C CD2  . LEU   A  1 484 ? 29.632 -12.465 -46.466 1.00 24.01  ? 510  LEU   A CD2  1 
ATOM   7102  H H    . LEU   A  1 484 ? 26.810 -8.358  -45.193 0.00 21.83  ? 510  LEU   A H    1 
ATOM   7103  H HA   . LEU   A  1 484 ? 27.386 -10.611 -43.342 0.00 21.38  ? 510  LEU   A HA   1 
ATOM   7104  H HB2  . LEU   A  1 484 ? 27.246 -11.435 -45.639 0.00 22.46  ? 510  LEU   A HB2  1 
ATOM   7105  H HB3  . LEU   A  1 484 ? 28.328 -10.137 -46.189 0.00 22.10  ? 510  LEU   A HB3  1 
ATOM   7106  H HG   . LEU   A  1 484 ? 30.184 -11.149 -44.899 0.00 24.83  ? 510  LEU   A HG   1 
ATOM   7107  H HD11 . LEU   A  1 484 ? 29.851 -13.492 -44.016 0.00 26.36  ? 510  LEU   A HD11 1 
ATOM   7108  H HD12 . LEU   A  1 484 ? 29.022 -12.236 -43.070 0.00 26.02  ? 510  LEU   A HD12 1 
ATOM   7109  H HD13 . LEU   A  1 484 ? 28.092 -13.255 -44.203 0.00 26.59  ? 510  LEU   A HD13 1 
ATOM   7110  H HD21 . LEU   A  1 484 ? 30.395 -13.217 -46.273 0.00 26.58  ? 510  LEU   A HD21 1 
ATOM   7111  H HD22 . LEU   A  1 484 ? 28.725 -12.938 -46.840 0.00 26.87  ? 510  LEU   A HD22 1 
ATOM   7112  H HD23 . LEU   A  1 484 ? 30.004 -11.748 -47.196 0.00 26.46  ? 510  LEU   A HD23 1 
ATOM   7113  N N    . ASN   A  1 485 ? 29.375 -9.413  -42.527 1.00 18.78  ? 511  ASN   A N    1 
ATOM   7114  C CA   . ASN   A  1 485 ? 30.523 -8.699  -42.022 1.00 18.58  ? 511  ASN   A CA   1 
ATOM   7115  C C    . ASN   A  1 485 ? 31.712 -9.653  -41.863 1.00 18.41  ? 511  ASN   A C    1 
ATOM   7116  O O    . ASN   A  1 485 ? 31.657 -10.587 -41.079 1.00 18.28  ? 511  ASN   A O    1 
ATOM   7117  C CB   . ASN   A  1 485 ? 30.175 -7.953  -40.726 1.00 18.98  ? 511  ASN   A CB   1 
ATOM   7118  C CG   . ASN   A  1 485 ? 31.224 -7.066  -40.214 1.00 19.76  ? 511  ASN   A CG   1 
ATOM   7119  O OD1  . ASN   A  1 485 ? 32.278 -6.887  -40.849 1.00 18.49  ? 511  ASN   A OD1  1 
ATOM   7120  N ND2  . ASN   A  1 485 ? 30.957 -6.329  -39.156 1.00 20.68  ? 511  ASN   A ND2  1 
ATOM   7121  H H    . ASN   A  1 485 ? 29.036 -10.139 -41.903 0.00 19.08  ? 511  ASN   A H    1 
ATOM   7122  H HA   . ASN   A  1 485 ? 30.829 -7.930  -42.728 0.00 18.33  ? 511  ASN   A HA   1 
ATOM   7123  H HB2  . ASN   A  1 485 ? 29.285 -7.350  -40.898 0.00 18.68  ? 511  ASN   A HB2  1 
ATOM   7124  H HB3  . ASN   A  1 485 ? 29.982 -8.674  -39.935 0.00 18.68  ? 511  ASN   A HB3  1 
ATOM   7125  H HD21 . ASN   A  1 485 ? 31.813 -6.652  -38.771 0.00 20.09  ? 511  ASN   A HD21 1 
ATOM   7126  H HD22 . ASN   A  1 485 ? 30.048 -6.312  -38.708 0.00 20.24  ? 511  ASN   A HD22 1 
ATOM   7127  N N    . LEU   A  1 486 ? 32.752 -9.444  -42.677 1.00 18.12  ? 512  LEU   A N    1 
ATOM   7128  C CA   . LEU   A  1 486 ? 34.006 -10.197 -42.623 1.00 18.69  ? 512  LEU   A CA   1 
ATOM   7129  C C    . LEU   A  1 486 ? 35.174 -9.243  -42.267 1.00 18.50  ? 512  LEU   A C    1 
ATOM   7130  O O    . LEU   A  1 486 ? 36.332 -9.517  -42.603 1.00 19.12  ? 512  LEU   A O    1 
ATOM   7131  C CB   . LEU   A  1 486 ? 34.255 -10.870 -43.980 1.00 19.43  ? 512  LEU   A CB   1 
ATOM   7132  C CG   . LEU   A  1 486 ? 33.324 -12.035 -44.324 1.00 22.30  ? 512  LEU   A CG   1 
ATOM   7133  C CD1  . LEU   A  1 486 ? 33.387 -12.342 -45.801 1.00 23.13  ? 512  LEU   A CD1  1 
ATOM   7134  C CD2  . LEU   A  1 486 ? 33.698 -13.306 -43.524 1.00 23.46  ? 512  LEU   A CD2  1 
ATOM   7135  H H    . LEU   A  1 486 ? 32.761 -8.743  -43.413 0.00 17.80  ? 512  LEU   A H    1 
ATOM   7136  H HA   . LEU   A  1 486 ? 33.965 -10.964 -41.853 0.00 18.62  ? 512  LEU   A HA   1 
ATOM   7137  H HB2  . LEU   A  1 486 ? 34.141 -10.118 -44.759 0.00 19.72  ? 512  LEU   A HB2  1 
ATOM   7138  H HB3  . LEU   A  1 486 ? 35.270 -11.264 -44.007 0.00 19.79  ? 512  LEU   A HB3  1 
ATOM   7139  H HG   . LEU   A  1 486 ? 32.296 -11.770 -44.083 0.00 23.58  ? 512  LEU   A HG   1 
ATOM   7140  H HD11 . LEU   A  1 486 ? 32.718 -13.171 -46.024 0.00 25.21  ? 512  LEU   A HD11 1 
ATOM   7141  H HD12 . LEU   A  1 486 ? 33.072 -11.463 -46.361 0.00 24.82  ? 512  LEU   A HD12 1 
ATOM   7142  H HD13 . LEU   A  1 486 ? 34.410 -12.605 -46.062 0.00 24.93  ? 512  LEU   A HD13 1 
ATOM   7143  H HD21 . LEU   A  1 486 ? 33.075 -14.131 -43.867 0.00 25.47  ? 512  LEU   A HD21 1 
ATOM   7144  H HD22 . LEU   A  1 486 ? 34.747 -13.540 -43.694 0.00 25.17  ? 512  LEU   A HD22 1 
ATOM   7145  H HD23 . LEU   A  1 486 ? 33.522 -13.135 -42.464 0.00 24.97  ? 512  LEU   A HD23 1 
ATOM   7146  N N    . SER   A  1 487 ? 34.883 -8.135  -41.569 1.00 17.46  ? 513  SER   A N    1 
ATOM   7147  C CA   . SER   A  1 487 ? 35.904 -7.175  -41.177 1.00 16.82  ? 513  SER   A CA   1 
ATOM   7148  C C    . SER   A  1 487 ? 36.944 -7.834  -40.286 1.00 16.30  ? 513  SER   A C    1 
ATOM   7149  O O    . SER   A  1 487 ? 36.589 -8.690  -39.487 1.00 16.61  ? 513  SER   A O    1 
ATOM   7150  C CB   . SER   A  1 487 ? 35.271 -6.022  -40.402 1.00 18.45  ? 513  SER   A CB   1 
ATOM   7151  O OG   . SER   A  1 487 ? 36.231 -5.085  -39.949 1.00 21.59  ? 513  SER   A OG   1 
ATOM   7152  H H    . SER   A  1 487 ? 33.950 -7.893  -41.252 0.00 16.48  ? 513  SER   A H    1 
ATOM   7153  H HA   . SER   A  1 487 ? 36.392 -6.776  -42.065 0.00 15.51  ? 513  SER   A HA   1 
ATOM   7154  H HB2  . SER   A  1 487 ? 34.565 -5.511  -41.055 0.00 17.28  ? 513  SER   A HB2  1 
ATOM   7155  H HB3  . SER   A  1 487 ? 34.745 -6.430  -39.540 0.00 17.24  ? 513  SER   A HB3  1 
ATOM   7156  H HG   . SER   A  1 487 ? 36.938 -4.952  -40.634 0.00 20.83  ? 513  SER   A HG   1 
ATOM   7157  N N    . ALA   A  1 488 ? 38.217 -7.415  -40.403 1.00 15.72  ? 514  ALA   A N    1 
ATOM   7158  C CA   . ALA   A  1 488 ? 39.296 -7.870  -39.513 1.00 15.89  ? 514  ALA   A CA   1 
ATOM   7159  C C    . ALA   A  1 488 ? 39.423 -9.387  -39.389 1.00 16.57  ? 514  ALA   A C    1 
ATOM   7160  O O    . ALA   A  1 488 ? 39.377 -9.942  -38.295 1.00 17.67  ? 514  ALA   A O    1 
ATOM   7161  C CB   . ALA   A  1 488 ? 39.151 -7.219  -38.129 1.00 16.18  ? 514  ALA   A CB   1 
ATOM   7162  H H    . ALA   A  1 488 ? 38.532 -6.754  -41.106 0.00 14.05  ? 514  ALA   A H    1 
ATOM   7163  H HA   . ALA   A  1 488 ? 40.237 -7.513  -39.929 0.00 14.31  ? 514  ALA   A HA   1 
ATOM   7164  H HB1  . ALA   A  1 488 ? 40.017 -7.476  -37.521 0.00 14.49  ? 514  ALA   A HB1  1 
ATOM   7165  H HB2  . ALA   A  1 488 ? 39.094 -6.139  -38.253 0.00 14.30  ? 514  ALA   A HB2  1 
ATOM   7166  H HB3  . ALA   A  1 488 ? 38.243 -7.589  -37.655 0.00 14.47  ? 514  ALA   A HB3  1 
ATOM   7167  N N    . ASN   A  1 489 ? 39.560 -10.052 -40.518 1.00 16.27  ? 515  ASN   A N    1 
ATOM   7168  C CA   . ASN   A  1 489 ? 39.804 -11.493 -40.591 1.00 16.88  ? 515  ASN   A CA   1 
ATOM   7169  C C    . ASN   A  1 489 ? 41.185 -11.807 -41.170 1.00 17.89  ? 515  ASN   A C    1 
ATOM   7170  O O    . ASN   A  1 489 ? 41.431 -12.959 -41.521 1.00 18.07  ? 515  ASN   A O    1 
ATOM   7171  C CB   . ASN   A  1 489 ? 38.705 -12.174 -41.427 1.00 16.69  ? 515  ASN   A CB   1 
ATOM   7172  C CG   . ASN   A  1 489 ? 37.523 -12.575 -40.571 1.00 18.34  ? 515  ASN   A CG   1 
ATOM   7173  O OD1  . ASN   A  1 489 ? 37.536 -13.632 -39.943 1.00 18.70  ? 515  ASN   A OD1  1 
ATOM   7174  N ND2  . ASN   A  1 489 ? 36.533 -11.715 -40.459 1.00 18.10  ? 515  ASN   A ND2  1 
ATOM   7175  H H    . ASN   A  1 489 ? 39.518 -9.609  -41.431 0.00 15.27  ? 515  ASN   A H    1 
ATOM   7176  H HA   . ASN   A  1 489 ? 39.824 -11.915 -39.587 0.00 16.35  ? 515  ASN   A HA   1 
ATOM   7177  H HB2  . ASN   A  1 489 ? 38.361 -11.491 -42.202 0.00 16.25  ? 515  ASN   A HB2  1 
ATOM   7178  H HB3  . ASN   A  1 489 ? 39.080 -13.086 -41.889 0.00 16.62  ? 515  ASN   A HB3  1 
ATOM   7179  H HD21 . ASN   A  1 489 ? 35.723 -11.949 -39.895 0.00 17.83  ? 515  ASN   A HD21 1 
ATOM   7180  H HD22 . ASN   A  1 489 ? 36.577 -10.817 -40.932 0.00 17.66  ? 515  ASN   A HD22 1 
ATOM   7181  N N    . SER   A  1 490 ? 42.101 -10.803 -41.244 1.00 18.92  ? 516  SER   A N    1 
ATOM   7182  C CA   . SER   A  1 490 ? 43.450 -10.947 -41.779 1.00 19.66  ? 516  SER   A CA   1 
ATOM   7183  C C    . SER   A  1 490 ? 43.443 -11.597 -43.170 1.00 19.42  ? 516  SER   A C    1 
ATOM   7184  O O    . SER   A  1 490 ? 44.358 -12.337 -43.519 1.00 18.87  ? 516  SER   A O    1 
ATOM   7185  C CB   A SER   A  1 490 ? 44.340 -11.726 -40.816 0.50 22.31  ? 516  SER   A CB   1 
ATOM   7186  C CB   B SER   A  1 490 ? 44.295 -11.742 -40.791 0.50 20.57  ? 516  SER   A CB   1 
ATOM   7187  O OG   A SER   A  1 490 ? 44.080 -13.120 -40.776 0.50 26.08  ? 516  SER   A OG   1 
ATOM   7188  O OG   B SER   A  1 490 ? 44.268 -11.153 -39.502 0.50 21.40  ? 516  SER   A OG   1 
ATOM   7189  H H    . SER   A  1 490 ? 41.935 -9.857  -40.917 0.00 18.55  ? 516  SER   A H    1 
ATOM   7190  H HA   . SER   A  1 490 ? 43.877 -9.951  -41.892 0.00 19.70  ? 516  SER   A HA   1 
ATOM   7191  H HB2  A SER   A  1 490 ? 45.373 -11.583 -41.128 0.00 23.37  ? 516  SER   A HB2  1 
ATOM   7192  H HB2  B SER   A  1 490 ? 43.859 -12.731 -40.678 0.00 21.37  ? 516  SER   A HB2  1 
ATOM   7193  H HB3  A SER   A  1 490 ? 44.203 -11.320 -39.815 0.00 23.07  ? 516  SER   A HB3  1 
ATOM   7194  H HB3  B SER   A  1 490 ? 45.323 -11.806 -41.142 0.00 21.32  ? 516  SER   A HB3  1 
ATOM   7195  H HG   A SER   A  1 490 ? 43.107 -13.307 -40.840 0.00 28.07  ? 516  SER   A HG   1 
ATOM   7196  H HG   B SER   A  1 490 ? 44.560 -11.808 -38.816 0.00 22.07  ? 516  SER   A HG   1 
ATOM   7197  N N    . ASN   A  1 491 ? 42.397 -11.300 -43.966 1.00 18.91  ? 517  ASN   A N    1 
ATOM   7198  C CA   . ASN   A  1 491 ? 42.223 -11.897 -45.268 1.00 19.18  ? 517  ASN   A CA   1 
ATOM   7199  C C    . ASN   A  1 491 ? 43.135 -11.235 -46.301 1.00 18.55  ? 517  ASN   A C    1 
ATOM   7200  O O    . ASN   A  1 491 ? 42.995 -10.059 -46.569 1.00 18.31  ? 517  ASN   A O    1 
ATOM   7201  C CB   . ASN   A  1 491 ? 40.746 -11.838 -45.682 1.00 20.42  ? 517  ASN   A CB   1 
ATOM   7202  C CG   . ASN   A  1 491 ? 40.457 -12.724 -46.874 1.00 22.41  ? 517  ASN   A CG   1 
ATOM   7203  O OD1  . ASN   A  1 491 ? 41.239 -12.792 -47.799 1.00 23.10  ? 517  ASN   A OD1  1 
ATOM   7204  N ND2  . ASN   A  1 491 ? 39.365 -13.474 -46.863 1.00 23.41  ? 517  ASN   A ND2  1 
ATOM   7205  H H    . ASN   A  1 491 ? 41.667 -10.633 -43.738 0.00 19.00  ? 517  ASN   A H    1 
ATOM   7206  H HA   . ASN   A  1 491 ? 42.506 -12.946 -45.221 0.00 20.15  ? 517  ASN   A HA   1 
ATOM   7207  H HB2  . ASN   A  1 491 ? 40.136 -12.168 -44.842 0.00 21.27  ? 517  ASN   A HB2  1 
ATOM   7208  H HB3  . ASN   A  1 491 ? 40.488 -10.815 -45.949 0.00 21.12  ? 517  ASN   A HB3  1 
ATOM   7209  H HD21 . ASN   A  1 491 ? 39.158 -14.073 -47.656 0.00 25.81  ? 517  ASN   A HD21 1 
ATOM   7210  H HD22 . ASN   A  1 491 ? 38.731 -13.455 -46.070 0.00 25.35  ? 517  ASN   A HD22 1 
ATOM   7211  N N    . ALA   A  1 492 ? 44.039 -12.004 -46.893 1.00 18.67  ? 518  ALA   A N    1 
ATOM   7212  C CA   . ALA   A  1 492 ? 44.975 -11.500 -47.895 1.00 20.06  ? 518  ALA   A CA   1 
ATOM   7213  C C    . ALA   A  1 492 ? 44.757 -12.158 -49.269 1.00 20.03  ? 518  ALA   A C    1 
ATOM   7214  O O    . ALA   A  1 492 ? 45.665 -12.120 -50.103 1.00 20.19  ? 518  ALA   A O    1 
ATOM   7215  C CB   . ALA   A  1 492 ? 46.399 -11.775 -47.422 1.00 20.71  ? 518  ALA   A CB   1 
ATOM   7216  H H    . ALA   A  1 492 ? 44.162 -12.994 -46.705 0.00 19.90  ? 518  ALA   A H    1 
ATOM   7217  H HA   . ALA   A  1 492 ? 44.872 -10.424 -48.024 0.00 21.19  ? 518  ALA   A HA   1 
ATOM   7218  H HB1  . ALA   A  1 492 ? 47.093 -11.191 -48.025 0.00 22.40  ? 518  ALA   A HB1  1 
ATOM   7219  H HB2  . ALA   A  1 492 ? 46.483 -11.490 -46.375 0.00 22.15  ? 518  ALA   A HB2  1 
ATOM   7220  H HB3  . ALA   A  1 492 ? 46.610 -12.837 -47.537 0.00 22.70  ? 518  ALA   A HB3  1 
ATOM   7221  N N    . GLN   A  1 493 ? 43.567 -12.719 -49.533 1.00 19.85  ? 519  GLN   A N    1 
ATOM   7222  C CA   . GLN   A  1 493 ? 43.335 -13.431 -50.788 1.00 20.20  ? 519  GLN   A CA   1 
ATOM   7223  C C    . GLN   A  1 493 ? 43.023 -12.493 -51.972 1.00 21.06  ? 519  GLN   A C    1 
ATOM   7224  O O    . GLN   A  1 493 ? 42.690 -11.324 -51.783 1.00 21.24  ? 519  GLN   A O    1 
ATOM   7225  C CB   . GLN   A  1 493 ? 42.217 -14.493 -50.614 1.00 21.28  ? 519  GLN   A CB   1 
ATOM   7226  C CG   . GLN   A  1 493 ? 40.793 -13.997 -50.885 1.00 23.73  ? 519  GLN   A CG   1 
ATOM   7227  C CD   . GLN   A  1 493 ? 39.793 -15.059 -50.520 1.00 25.77  ? 519  GLN   A CD   1 
ATOM   7228  O OE1  . GLN   A  1 493 ? 39.217 -15.034 -49.442 1.00 24.61  ? 519  GLN   A OE1  1 
ATOM   7229  N NE2  . GLN   A  1 493 ? 39.591 -16.037 -51.403 1.00 25.76  ? 519  GLN   A NE2  1 
ATOM   7230  H H    . GLN   A  1 493 ? 42.752 -12.684 -48.930 0.00 21.51  ? 519  GLN   A H    1 
ATOM   7231  H HA   . GLN   A  1 493 ? 44.235 -13.986 -51.050 0.00 22.83  ? 519  GLN   A HA   1 
ATOM   7232  H HB2  . GLN   A  1 493 ? 42.411 -15.311 -51.306 0.00 24.47  ? 519  GLN   A HB2  1 
ATOM   7233  H HB3  . GLN   A  1 493 ? 42.245 -14.870 -49.592 0.00 23.96  ? 519  GLN   A HB3  1 
ATOM   7234  H HG2  . GLN   A  1 493 ? 40.595 -13.111 -50.283 0.00 26.47  ? 519  GLN   A HG2  1 
ATOM   7235  H HG3  . GLN   A  1 493 ? 40.662 -13.781 -51.944 0.00 27.03  ? 519  GLN   A HG3  1 
ATOM   7236  H HE21 . GLN   A  1 493 ? 40.106 -16.049 -52.277 0.00 30.24  ? 519  GLN   A HE21 1 
ATOM   7237  H HE22 . GLN   A  1 493 ? 38.924 -16.774 -51.197 0.00 30.22  ? 519  GLN   A HE22 1 
ATOM   7238  N N    . VAL   A  1 494 ? 43.093 -13.054 -53.179 1.00 21.12  ? 520  VAL   A N    1 
ATOM   7239  C CA   . VAL   A  1 494 ? 42.699 -12.393 -54.404 1.00 21.72  ? 520  VAL   A CA   1 
ATOM   7240  C C    . VAL   A  1 494 ? 41.288 -12.902 -54.652 1.00 22.82  ? 520  VAL   A C    1 
ATOM   7241  O O    . VAL   A  1 494 ? 41.123 -14.040 -55.099 1.00 23.71  ? 520  VAL   A O    1 
ATOM   7242  C CB   . VAL   A  1 494 ? 43.633 -12.747 -55.592 1.00 22.34  ? 520  VAL   A CB   1 
ATOM   7243  C CG1  . VAL   A  1 494 ? 43.104 -12.166 -56.906 1.00 22.47  ? 520  VAL   A CG1  1 
ATOM   7244  C CG2  . VAL   A  1 494 ? 45.055 -12.264 -55.326 1.00 22.82  ? 520  VAL   A CG2  1 
ATOM   7245  H H    . VAL   A  1 494 ? 43.426 -14.000 -53.331 0.00 24.40  ? 520  VAL   A H    1 
ATOM   7246  H HA   . VAL   A  1 494 ? 42.683 -11.311 -54.290 0.00 24.57  ? 520  VAL   A HA   1 
ATOM   7247  H HB   . VAL   A  1 494 ? 43.676 -13.830 -55.703 0.00 26.43  ? 520  VAL   A HB   1 
ATOM   7248  H HG11 . VAL   A  1 494 ? 43.889 -12.221 -57.659 0.00 26.68  ? 520  VAL   A HG11 1 
ATOM   7249  H HG12 . VAL   A  1 494 ? 42.247 -12.748 -57.244 0.00 26.65  ? 520  VAL   A HG12 1 
ATOM   7250  H HG13 . VAL   A  1 494 ? 42.813 -11.129 -56.743 0.00 26.09  ? 520  VAL   A HG13 1 
ATOM   7251  H HG21 . VAL   A  1 494 ? 45.683 -12.512 -56.181 0.00 26.89  ? 520  VAL   A HG21 1 
ATOM   7252  H HG22 . VAL   A  1 494 ? 45.040 -11.186 -55.176 0.00 26.21  ? 520  VAL   A HG22 1 
ATOM   7253  H HG23 . VAL   A  1 494 ? 45.441 -12.758 -54.437 0.00 26.48  ? 520  VAL   A HG23 1 
ATOM   7254  N N    . LEU   A  1 495 ? 40.262 -12.087 -54.343 1.00 22.02  ? 521  LEU   A N    1 
ATOM   7255  C CA   . LEU   A  1 495 ? 38.866 -12.445 -54.624 1.00 22.32  ? 521  LEU   A CA   1 
ATOM   7256  C C    . LEU   A  1 495 ? 38.726 -12.503 -56.159 1.00 23.03  ? 521  LEU   A C    1 
ATOM   7257  O O    . LEU   A  1 495 ? 39.315 -11.678 -56.863 1.00 22.16  ? 521  LEU   A O    1 
ATOM   7258  C CB   . LEU   A  1 495 ? 37.905 -11.427 -54.018 1.00 22.10  ? 521  LEU   A CB   1 
ATOM   7259  C CG   . LEU   A  1 495 ? 37.910 -11.377 -52.474 1.00 23.55  ? 521  LEU   A CG   1 
ATOM   7260  C CD1  . LEU   A  1 495 ? 37.212 -10.134 -51.972 1.00 24.29  ? 521  LEU   A CD1  1 
ATOM   7261  C CD2  . LEU   A  1 495 ? 37.276 -12.625 -51.875 1.00 24.65  ? 521  LEU   A CD2  1 
ATOM   7262  H H    . LEU   A  1 495 ? 40.371 -11.177 -53.907 0.00 24.75  ? 521  LEU   A H    1 
ATOM   7263  H HA   . LEU   A  1 495 ? 38.651 -13.434 -54.224 0.00 25.81  ? 521  LEU   A HA   1 
ATOM   7264  H HB2  . LEU   A  1 495 ? 38.173 -10.436 -54.381 0.00 24.83  ? 521  LEU   A HB2  1 
ATOM   7265  H HB3  . LEU   A  1 495 ? 36.893 -11.669 -54.339 0.00 25.17  ? 521  LEU   A HB3  1 
ATOM   7266  H HG   . LEU   A  1 495 ? 38.939 -11.332 -52.120 0.00 26.20  ? 521  LEU   A HG   1 
ATOM   7267  H HD11 . LEU   A  1 495 ? 37.226 -10.126 -50.883 0.00 26.56  ? 521  LEU   A HD11 1 
ATOM   7268  H HD12 . LEU   A  1 495 ? 37.731 -9.257  -52.356 0.00 26.70  ? 521  LEU   A HD12 1 
ATOM   7269  H HD13 . LEU   A  1 495 ? 36.185 -10.145 -52.333 0.00 26.96  ? 521  LEU   A HD13 1 
ATOM   7270  H HD21 . LEU   A  1 495 ? 37.129 -12.472 -50.807 0.00 27.54  ? 521  LEU   A HD21 1 
ATOM   7271  H HD22 . LEU   A  1 495 ? 36.317 -12.810 -52.358 0.00 28.03  ? 521  LEU   A HD22 1 
ATOM   7272  H HD23 . LEU   A  1 495 ? 37.941 -13.473 -52.027 0.00 28.07  ? 521  LEU   A HD23 1 
ATOM   7273  N N    . SER   A  1 496 ? 38.051 -13.535 -56.667 1.00 23.90  ? 522  SER   A N    1 
ATOM   7274  C CA   . SER   A  1 496 ? 38.015 -13.786 -58.092 1.00 25.86  ? 522  SER   A CA   1 
ATOM   7275  C C    . SER   A  1 496 ? 36.636 -14.093 -58.691 1.00 26.15  ? 522  SER   A C    1 
ATOM   7276  O O    . SER   A  1 496 ? 36.573 -14.595 -59.812 1.00 26.25  ? 522  SER   A O    1 
ATOM   7277  C CB   . SER   A  1 496 ? 38.979 -14.924 -58.386 1.00 28.59  ? 522  SER   A CB   1 
ATOM   7278  O OG   . SER   A  1 496 ? 38.522 -16.095 -57.729 1.00 32.40  ? 522  SER   A OG   1 
ATOM   7279  H H    . SER   A  1 496 ? 37.521 -14.204 -56.118 0.00 28.50  ? 522  SER   A H    1 
ATOM   7280  H HA   . SER   A  1 496 ? 38.382 -12.917 -58.634 0.00 31.22  ? 522  SER   A HA   1 
ATOM   7281  H HB2  . SER   A  1 496 ? 39.046 -15.089 -59.460 0.00 35.38  ? 522  SER   A HB2  1 
ATOM   7282  H HB3  . SER   A  1 496 ? 39.960 -14.656 -57.998 0.00 34.76  ? 522  SER   A HB3  1 
ATOM   7283  H HG   . SER   A  1 496 ? 38.858 -16.123 -56.795 0.00 39.46  ? 522  SER   A HG   1 
ATOM   7284  N N    . GLY   A  1 497 ? 35.563 -13.739 -57.995 1.00 25.83  ? 523  GLY   A N    1 
ATOM   7285  C CA   . GLY   A  1 497 ? 34.215 -13.924 -58.517 1.00 26.58  ? 523  GLY   A CA   1 
ATOM   7286  C C    . GLY   A  1 497 ? 33.492 -15.228 -58.235 1.00 26.56  ? 523  GLY   A C    1 
ATOM   7287  O O    . GLY   A  1 497 ? 32.454 -15.464 -58.850 1.00 26.67  ? 523  GLY   A O    1 
ATOM   7288  H H    . GLY   A  1 497 ? 35.578 -13.318 -57.072 0.00 30.97  ? 523  GLY   A H    1 
ATOM   7289  H HA2  . GLY   A  1 497 ? 33.593 -13.134 -58.099 0.00 32.33  ? 523  GLY   A HA2  1 
ATOM   7290  H HA3  . GLY   A  1 497 ? 34.219 -13.782 -59.597 0.00 32.95  ? 523  GLY   A HA3  1 
ATOM   7291  N N    . THR   A  1 498 ? 33.999 -16.079 -57.327 1.00 26.22  ? 524  THR   A N    1 
ATOM   7292  C CA   . THR   A  1 498 ? 33.325 -17.353 -56.982 1.00 27.36  ? 524  THR   A CA   1 
ATOM   7293  C C    . THR   A  1 498 ? 33.154 -17.574 -55.475 1.00 26.94  ? 524  THR   A C    1 
ATOM   7294  O O    . THR   A  1 498 ? 32.393 -18.458 -55.082 1.00 27.96  ? 524  THR   A O    1 
ATOM   7295  C CB   . THR   A  1 498 ? 34.147 -18.534 -57.508 1.00 29.96  ? 524  THR   A CB   1 
ATOM   7296  O OG1  . THR   A  1 498 ? 35.465 -18.451 -56.944 1.00 31.10  ? 524  THR   A OG1  1 
ATOM   7297  C CG2  . THR   A  1 498 ? 34.221 -18.568 -59.027 1.00 31.11  ? 524  THR   A CG2  1 
ATOM   7298  H H    . THR   A  1 498 ? 34.887 -15.943 -56.854 0.00 32.21  ? 524  THR   A H    1 
ATOM   7299  H HA   . THR   A  1 498 ? 32.335 -17.408 -57.432 0.00 34.52  ? 524  THR   A HA   1 
ATOM   7300  H HB   . THR   A  1 498 ? 33.681 -19.463 -57.184 0.00 38.17  ? 524  THR   A HB   1 
ATOM   7301  H HG1  . THR   A  1 498 ? 36.023 -19.203 -57.276 0.00 39.29  ? 524  THR   A HG1  1 
ATOM   7302  H HG21 . THR   A  1 498 ? 34.756 -19.459 -59.353 0.00 40.18  ? 524  THR   A HG21 1 
ATOM   7303  H HG22 . THR   A  1 498 ? 33.217 -18.585 -59.450 0.00 40.03  ? 524  THR   A HG22 1 
ATOM   7304  H HG23 . THR   A  1 498 ? 34.746 -17.688 -59.397 0.00 39.52  ? 524  THR   A HG23 1 
ATOM   7305  N N    . GLU   A  1 499 ? 33.863 -16.808 -54.641 1.00 25.56  ? 525  GLU   A N    1 
ATOM   7306  C CA   . GLU   A  1 499 ? 33.872 -16.990 -53.194 1.00 25.51  ? 525  GLU   A CA   1 
ATOM   7307  C C    . GLU   A  1 499 ? 32.514 -16.864 -52.519 1.00 25.97  ? 525  GLU   A C    1 
ATOM   7308  O O    . GLU   A  1 499 ? 32.288 -17.513 -51.493 1.00 26.48  ? 525  GLU   A O    1 
ATOM   7309  C CB   . GLU   A  1 499 ? 34.864 -16.010 -52.530 1.00 26.58  ? 525  GLU   A CB   1 
ATOM   7310  C CG   . GLU   A  1 499 ? 36.324 -16.274 -52.872 1.00 30.25  ? 525  GLU   A CG   1 
ATOM   7311  C CD   . GLU   A  1 499 ? 36.793 -15.860 -54.253 1.00 32.07  ? 525  GLU   A CD   1 
ATOM   7312  O OE1  . GLU   A  1 499 ? 36.132 -15.005 -54.885 1.00 30.58  ? 525  GLU   A OE1  1 
ATOM   7313  O OE2  . GLU   A  1 499 ? 37.839 -16.375 -54.701 1.00 35.01  ? 525  GLU   A OE2  1 
ATOM   7314  H H    . GLU   A  1 499 ? 34.424 -16.017 -54.935 0.00 30.91  ? 525  GLU   A H    1 
ATOM   7315  H HA   . GLU   A  1 499 ? 34.230 -17.997 -52.989 0.00 30.99  ? 525  GLU   A HA   1 
ATOM   7316  H HB2  . GLU   A  1 499 ? 34.611 -14.991 -52.819 0.00 31.20  ? 525  GLU   A HB2  1 
ATOM   7317  H HB3  . GLU   A  1 499 ? 34.765 -16.109 -51.451 0.00 31.19  ? 525  GLU   A HB3  1 
ATOM   7318  H HG2  . GLU   A  1 499 ? 36.943 -15.744 -52.151 0.00 35.54  ? 525  GLU   A HG2  1 
ATOM   7319  H HG3  . GLU   A  1 499 ? 36.507 -17.343 -52.782 0.00 36.25  ? 525  GLU   A HG3  1 
ATOM   7320  N N    . PHE   A  1 500 ? 31.625 -16.019 -53.045 1.00 25.97  ? 526  PHE   A N    1 
ATOM   7321  C CA   . PHE   A  1 500 ? 30.315 -15.772 -52.439 1.00 26.32  ? 526  PHE   A CA   1 
ATOM   7322  C C    . PHE   A  1 500 ? 29.144 -16.391 -53.209 1.00 27.58  ? 526  PHE   A C    1 
ATOM   7323  O O    . PHE   A  1 500 ? 28.003 -16.041 -52.937 1.00 28.30  ? 526  PHE   A O    1 
ATOM   7324  C CB   . PHE   A  1 500 ? 30.116 -14.259 -52.289 1.00 26.02  ? 526  PHE   A CB   1 
ATOM   7325  C CG   . PHE   A  1 500 ? 31.153 -13.622 -51.392 1.00 26.22  ? 526  PHE   A CG   1 
ATOM   7326  C CD1  . PHE   A  1 500 ? 31.030 -13.682 -50.017 1.00 26.63  ? 526  PHE   A CD1  1 
ATOM   7327  C CD2  . PHE   A  1 500 ? 32.285 -13.023 -51.927 1.00 26.66  ? 526  PHE   A CD2  1 
ATOM   7328  C CE1  . PHE   A  1 500 ? 32.003 -13.125 -49.191 1.00 27.08  ? 526  PHE   A CE1  1 
ATOM   7329  C CE2  . PHE   A  1 500 ? 33.251 -12.461 -51.099 1.00 27.35  ? 526  PHE   A CE2  1 
ATOM   7330  C CZ   . PHE   A  1 500 ? 33.099 -12.507 -49.737 1.00 26.95  ? 526  PHE   A CZ   1 
ATOM   7331  H H    . PHE   A  1 500 ? 31.777 -15.480 -53.891 0.00 31.21  ? 526  PHE   A H    1 
ATOM   7332  H HA   . PHE   A  1 500 ? 30.285 -16.186 -51.432 0.00 31.39  ? 526  PHE   A HA   1 
ATOM   7333  H HB2  . PHE   A  1 500 ? 30.181 -13.793 -53.271 0.00 30.84  ? 526  PHE   A HB2  1 
ATOM   7334  H HB3  . PHE   A  1 500 ? 29.142 -14.062 -51.842 0.00 30.69  ? 526  PHE   A HB3  1 
ATOM   7335  H HD1  . PHE   A  1 500 ? 30.167 -14.159 -49.580 0.00 30.72  ? 526  PHE   A HD1  1 
ATOM   7336  H HD2  . PHE   A  1 500 ? 32.410 -12.974 -52.995 0.00 31.00  ? 526  PHE   A HD2  1 
ATOM   7337  H HE1  . PHE   A  1 500 ? 31.884 -13.160 -48.122 0.00 30.45  ? 526  PHE   A HE1  1 
ATOM   7338  H HE2  . PHE   A  1 500 ? 34.115 -11.980 -51.527 0.00 31.02  ? 526  PHE   A HE2  1 
ATOM   7339  H HZ   . PHE   A  1 500 ? 33.849 -12.075 -49.097 0.00 30.03  ? 526  PHE   A HZ   1 
ATOM   7340  N N    . SER   A  1 501 ? 29.406 -17.363 -54.101 1.00 28.48  ? 527  SER   A N    1 
ATOM   7341  C CA   . SER   A  1 501 ? 28.357 -18.000 -54.902 1.00 29.57  ? 527  SER   A CA   1 
ATOM   7342  C C    . SER   A  1 501 ? 27.263 -18.729 -54.093 1.00 29.38  ? 527  SER   A C    1 
ATOM   7343  O O    . SER   A  1 501 ? 26.154 -18.856 -54.600 1.00 30.08  ? 527  SER   A O    1 
ATOM   7344  C CB   . SER   A  1 501 ? 28.977 -18.946 -55.927 1.00 32.78  ? 527  SER   A CB   1 
ATOM   7345  O OG   . SER   A  1 501 ? 29.896 -19.836 -55.312 1.00 37.19  ? 527  SER   A OG   1 
ATOM   7346  H H    . SER   A  1 501 ? 30.329 -17.746 -54.280 0.00 35.27  ? 527  SER   A H    1 
ATOM   7347  H HA   . SER   A  1 501 ? 27.850 -17.217 -55.463 0.00 37.20  ? 527  SER   A HA   1 
ATOM   7348  H HB2  . SER   A  1 501 ? 28.183 -19.525 -56.396 0.00 42.10  ? 527  SER   A HB2  1 
ATOM   7349  H HB3  . SER   A  1 501 ? 29.499 -18.357 -56.680 0.00 41.53  ? 527  SER   A HB3  1 
ATOM   7350  H HG   . SER   A  1 501 ? 30.796 -19.420 -55.266 0.00 46.57  ? 527  SER   A HG   1 
ATOM   7351  N N    . ALA   A  1 502 ? 27.542 -19.187 -52.857 1.00 28.73  ? 528  ALA   A N    1 
ATOM   7352  C CA   . ALA   A  1 502 ? 26.521 -19.853 -52.028 1.00 28.32  ? 528  ALA   A CA   1 
ATOM   7353  C C    . ALA   A  1 502 ? 25.568 -18.855 -51.334 1.00 27.64  ? 528  ALA   A C    1 
ATOM   7354  O O    . ALA   A  1 502 ? 24.480 -19.244 -50.905 1.00 27.09  ? 528  ALA   A O    1 
ATOM   7355  C CB   . ALA   A  1 502 ? 27.184 -20.733 -50.997 1.00 28.71  ? 528  ALA   A CB   1 
ATOM   7356  H H    . ALA   A  1 502 ? 28.449 -19.121 -52.408 0.00 35.83  ? 528  ALA   A H    1 
ATOM   7357  H HA   . ALA   A  1 502 ? 25.915 -20.505 -52.656 0.00 36.40  ? 528  ALA   A HA   1 
ATOM   7358  H HB1  . ALA   A  1 502 ? 26.415 -21.243 -50.419 0.00 36.41  ? 528  ALA   A HB1  1 
ATOM   7359  H HB2  . ALA   A  1 502 ? 27.812 -21.461 -51.508 0.00 36.54  ? 528  ALA   A HB2  1 
ATOM   7360  H HB3  . ALA   A  1 502 ? 27.792 -20.113 -50.339 0.00 35.70  ? 528  ALA   A HB3  1 
ATOM   7361  N N    . ILE   A  1 503 ? 25.971 -17.577 -51.212 1.00 27.42  ? 529  ILE   A N    1 
ATOM   7362  C CA   . ILE   A  1 503 ? 25.139 -16.514 -50.633 1.00 27.50  ? 529  ILE   A CA   1 
ATOM   7363  C C    . ILE   A  1 503 ? 25.192 -15.366 -51.655 1.00 27.85  ? 529  ILE   A C    1 
ATOM   7364  O O    . ILE   A  1 503 ? 25.795 -14.333 -51.395 1.00 27.40  ? 529  ILE   A O    1 
ATOM   7365  C CB   . ILE   A  1 503 ? 25.632 -16.097 -49.208 1.00 28.39  ? 529  ILE   A CB   1 
ATOM   7366  C CG1  . ILE   A  1 503 ? 27.162 -15.876 -49.168 1.00 29.67  ? 529  ILE   A CG1  1 
ATOM   7367  C CG2  . ILE   A  1 503 ? 25.213 -17.149 -48.158 1.00 28.85  ? 529  ILE   A CG2  1 
ATOM   7368  C CD1  . ILE   A  1 503 ? 27.642 -15.225 -47.884 1.00 31.06  ? 529  ILE   A CD1  1 
ATOM   7369  H H    . ILE   A  1 503 ? 26.878 -17.238 -51.517 0.00 33.65  ? 529  ILE   A H    1 
ATOM   7370  H HA   . ILE   A  1 503 ? 24.098 -16.826 -50.565 0.00 33.96  ? 529  ILE   A HA   1 
ATOM   7371  H HB   . ILE   A  1 503 ? 25.151 -15.156 -48.943 0.00 33.88  ? 529  ILE   A HB   1 
ATOM   7372  H HG12 . ILE   A  1 503 ? 27.662 -16.840 -49.251 0.00 35.48  ? 529  ILE   A HG12 1 
ATOM   7373  H HG13 . ILE   A  1 503 ? 27.465 -15.233 -49.993 0.00 35.21  ? 529  ILE   A HG13 1 
ATOM   7374  H HG21 . ILE   A  1 503 ? 25.367 -16.748 -47.157 0.00 34.42  ? 529  ILE   A HG21 1 
ATOM   7375  H HG22 . ILE   A  1 503 ? 24.160 -17.393 -48.295 0.00 35.17  ? 529  ILE   A HG22 1 
ATOM   7376  H HG23 . ILE   A  1 503 ? 25.820 -18.042 -48.295 0.00 34.99  ? 529  ILE   A HG23 1 
ATOM   7377  H HD11 . ILE   A  1 503 ? 28.691 -14.955 -48.004 0.00 36.12  ? 529  ILE   A HD11 1 
ATOM   7378  H HD12 . ILE   A  1 503 ? 27.046 -14.334 -47.692 0.00 36.17  ? 529  ILE   A HD12 1 
ATOM   7379  H HD13 . ILE   A  1 503 ? 27.542 -15.928 -47.059 0.00 36.39  ? 529  ILE   A HD13 1 
ATOM   7380  N N    . PRO   A  1 504 ? 24.613 -15.561 -52.859 1.00 28.13  ? 530  PRO   A N    1 
ATOM   7381  C CA   . PRO   A  1 504 ? 24.753 -14.546 -53.914 1.00 28.32  ? 530  PRO   A CA   1 
ATOM   7382  C C    . PRO   A  1 504 ? 23.864 -13.313 -53.782 1.00 28.31  ? 530  PRO   A C    1 
ATOM   7383  O O    . PRO   A  1 504 ? 23.998 -12.401 -54.601 1.00 29.15  ? 530  PRO   A O    1 
ATOM   7384  C CB   . PRO   A  1 504 ? 24.436 -15.338 -55.190 1.00 29.09  ? 530  PRO   A CB   1 
ATOM   7385  C CG   . PRO   A  1 504 ? 23.475 -16.381 -54.753 1.00 29.57  ? 530  PRO   A CG   1 
ATOM   7386  C CD   . PRO   A  1 504 ? 23.867 -16.744 -53.341 1.00 27.82  ? 530  PRO   A CD   1 
ATOM   7387  H HA   . PRO   A  1 504 ? 25.791 -14.222 -53.988 0.00 34.77  ? 530  PRO   A HA   1 
ATOM   7388  H HB2  . PRO   A  1 504 ? 23.984 -14.687 -55.936 0.00 36.88  ? 530  PRO   A HB2  1 
ATOM   7389  H HB3  . PRO   A  1 504 ? 25.348 -15.792 -55.577 0.00 36.74  ? 530  PRO   A HB3  1 
ATOM   7390  H HG2  . PRO   A  1 504 ? 22.462 -15.978 -54.778 0.00 37.86  ? 530  PRO   A HG2  1 
ATOM   7391  H HG3  . PRO   A  1 504 ? 23.556 -17.248 -55.408 0.00 38.17  ? 530  PRO   A HG3  1 
ATOM   7392  H HD2  . PRO   A  1 504 ? 22.980 -16.902 -52.729 0.00 35.27  ? 530  PRO   A HD2  1 
ATOM   7393  H HD3  . PRO   A  1 504 ? 24.513 -17.621 -53.341 0.00 35.29  ? 530  PRO   A HD3  1 
ATOM   7394  N N    . HIS   A  1 505 ? 22.967 -13.269 -52.777 1.00 27.16  ? 531  HIS   A N    1 
ATOM   7395  C CA   . HIS   A  1 505 ? 22.068 -12.133 -52.591 1.00 26.51  ? 531  HIS   A CA   1 
ATOM   7396  C C    . HIS   A  1 505 ? 22.505 -11.207 -51.457 1.00 24.76  ? 531  HIS   A C    1 
ATOM   7397  O O    . HIS   A  1 505 ? 21.685 -10.473 -50.912 1.00 24.82  ? 531  HIS   A O    1 
ATOM   7398  C CB   . HIS   A  1 505 ? 20.625 -12.637 -52.404 1.00 28.12  ? 531  HIS   A CB   1 
ATOM   7399  C CG   . HIS   A  1 505 ? 20.215 -13.560 -53.511 1.00 32.48  ? 531  HIS   A CG   1 
ATOM   7400  N ND1  . HIS   A  1 505 ? 20.097 -13.110 -54.818 1.00 35.12  ? 531  HIS   A ND1  1 
ATOM   7401  C CD2  . HIS   A  1 505 ? 19.993 -14.894 -53.490 1.00 34.44  ? 531  HIS   A CD2  1 
ATOM   7402  C CE1  . HIS   A  1 505 ? 19.780 -14.171 -55.545 1.00 35.99  ? 531  HIS   A CE1  1 
ATOM   7403  N NE2  . HIS   A  1 505 ? 19.694 -15.268 -54.788 1.00 35.87  ? 531  HIS   A NE2  1 
ATOM   7404  H H    . HIS   A  1 505 ? 22.836 -13.991 -52.075 0.00 33.48  ? 531  HIS   A H    1 
ATOM   7405  H HA   . HIS   A  1 505 ? 22.056 -11.530 -53.497 0.00 32.75  ? 531  HIS   A HA   1 
ATOM   7406  H HB2  . HIS   A  1 505 ? 20.551 -13.179 -51.462 0.00 34.91  ? 531  HIS   A HB2  1 
ATOM   7407  H HB3  . HIS   A  1 505 ? 19.942 -11.788 -52.409 0.00 35.07  ? 531  HIS   A HB3  1 
ATOM   7408  H HD1  . HIS   A  1 505 ? 20.227 -12.160 -55.151 0.00 44.32  ? 531  HIS   A HD1  1 
ATOM   7409  H HD2  . HIS   A  1 505 ? 20.039 -15.541 -52.629 0.00 43.61  ? 531  HIS   A HD2  1 
ATOM   7410  H HE1  . HIS   A  1 505 ? 19.614 -14.152 -56.609 0.00 46.55  ? 531  HIS   A HE1  1 
ATOM   7411  N N    . VAL   A  1 506 ? 23.816 -11.171 -51.142 1.00 23.27  ? 532  VAL   A N    1 
ATOM   7412  C CA   . VAL   A  1 506 ? 24.337 -10.240 -50.144 1.00 22.80  ? 532  VAL   A CA   1 
ATOM   7413  C C    . VAL   A  1 506 ? 24.144 -8.810  -50.725 1.00 22.28  ? 532  VAL   A C    1 
ATOM   7414  O O    . VAL   A  1 506 ? 24.440 -8.577  -51.890 1.00 22.45  ? 532  VAL   A O    1 
ATOM   7415  C CB   . VAL   A  1 506 ? 25.827 -10.519 -49.814 1.00 23.00  ? 532  VAL   A CB   1 
ATOM   7416  C CG1  . VAL   A  1 506 ? 26.416 -9.399  -48.945 1.00 23.26  ? 532  VAL   A CG1  1 
ATOM   7417  C CG2  . VAL   A  1 506 ? 25.992 -11.878 -49.132 1.00 23.24  ? 532  VAL   A CG2  1 
ATOM   7418  H H    . VAL   A  1 506 ? 24.533 -11.750 -51.567 0.00 27.68  ? 532  VAL   A H    1 
ATOM   7419  H HA   . VAL   A  1 506 ? 23.767 -10.342 -49.221 0.00 26.41  ? 532  VAL   A HA   1 
ATOM   7420  H HB   . VAL   A  1 506 ? 26.394 -10.544 -50.743 0.00 26.45  ? 532  VAL   A HB   1 
ATOM   7421  H HG11 . VAL   A  1 506 ? 27.302 -9.774  -48.434 0.00 25.87  ? 532  VAL   A HG11 1 
ATOM   7422  H HG12 . VAL   A  1 506 ? 26.701 -8.561  -49.580 0.00 26.04  ? 532  VAL   A HG12 1 
ATOM   7423  H HG13 . VAL   A  1 506 ? 25.671 -9.084  -48.217 0.00 26.04  ? 532  VAL   A HG13 1 
ATOM   7424  H HG21 . VAL   A  1 506 ? 27.049 -12.053 -48.935 0.00 26.50  ? 532  VAL   A HG21 1 
ATOM   7425  H HG22 . VAL   A  1 506 ? 25.437 -11.875 -48.194 0.00 26.62  ? 532  VAL   A HG22 1 
ATOM   7426  H HG23 . VAL   A  1 506 ? 25.606 -12.658 -49.786 0.00 27.15  ? 532  VAL   A HG23 1 
ATOM   7427  N N    . LYS   A  1 507 ? 23.559 -7.930  -49.940 1.00 21.49  ? 533  LYS   A N    1 
ATOM   7428  C CA   . LYS   A  1 507 ? 23.257 -6.561  -50.321 1.00 22.06  ? 533  LYS   A CA   1 
ATOM   7429  C C    . LYS   A  1 507 ? 24.268 -5.594  -49.727 1.00 21.97  ? 533  LYS   A C    1 
ATOM   7430  O O    . LYS   A  1 507 ? 24.554 -4.571  -50.347 1.00 22.47  ? 533  LYS   A O    1 
ATOM   7431  C CB   . LYS   A  1 507 ? 21.866 -6.179  -49.791 1.00 24.31  ? 533  LYS   A CB   1 
ATOM   7432  C CG   . LYS   A  1 507 ? 20.729 -7.085  -50.243 1.00 29.13  ? 533  LYS   A CG   1 
ATOM   7433  C CD   . LYS   A  1 507 ? 20.299 -6.818  -51.673 1.00 32.93  ? 533  LYS   A CD   1 
ATOM   7434  C CE   . LYS   A  1 507 ? 19.077 -7.629  -52.083 1.00 36.67  ? 533  LYS   A CE   1 
ATOM   7435  N NZ   . LYS   A  1 507 ? 17.826 -7.207  -51.391 1.00 38.65  ? 533  LYS   A NZ   1 
ATOM   7436  H H    . LYS   A  1 507 ? 23.269 -8.135  -48.989 0.00 24.53  ? 533  LYS   A H    1 
ATOM   7437  H HA   . LYS   A  1 507 ? 23.253 -6.442  -51.403 0.00 25.59  ? 533  LYS   A HA   1 
ATOM   7438  H HB2  . LYS   A  1 507 ? 21.891 -6.203  -48.703 0.00 27.96  ? 533  LYS   A HB2  1 
ATOM   7439  H HB3  . LYS   A  1 507 ? 21.636 -5.168  -50.125 0.00 28.28  ? 533  LYS   A HB3  1 
ATOM   7440  H HG2  . LYS   A  1 507 ? 21.025 -8.130  -50.169 0.00 34.63  ? 533  LYS   A HG2  1 
ATOM   7441  H HG3  . LYS   A  1 507 ? 19.868 -6.904  -49.601 0.00 34.68  ? 533  LYS   A HG3  1 
ATOM   7442  H HD2  . LYS   A  1 507 ? 20.052 -5.763  -51.782 0.00 39.63  ? 533  LYS   A HD2  1 
ATOM   7443  H HD3  . LYS   A  1 507 ? 21.123 -7.078  -52.335 0.00 39.61  ? 533  LYS   A HD3  1 
ATOM   7444  H HE2  . LYS   A  1 507 ? 18.904 -7.509  -53.150 0.00 45.13  ? 533  LYS   A HE2  1 
ATOM   7445  H HE3  . LYS   A  1 507 ? 19.254 -8.678  -51.850 0.00 44.80  ? 533  LYS   A HE3  1 
ATOM   7446  H HZ1  . LYS   A  1 507 ? 17.036 -7.731  -51.756 0.00 47.79  ? 533  LYS   A HZ1  1 
ATOM   7447  H HZ2  . LYS   A  1 507 ? 17.900 -7.380  -50.394 0.00 47.04  ? 533  LYS   A HZ2  1 
ATOM   7448  H HZ3  . LYS   A  1 507 ? 17.663 -6.217  -51.543 0.00 47.31  ? 533  LYS   A HZ3  1 
ATOM   7449  N N    . TYR   A  1 508 ? 24.756 -5.879  -48.496 1.00 21.12  ? 534  TYR   A N    1 
ATOM   7450  C CA   . TYR   A  1 508 ? 25.677 -5.011  -47.768 1.00 20.96  ? 534  TYR   A CA   1 
ATOM   7451  C C    . TYR   A  1 508 ? 26.842 -5.891  -47.294 1.00 19.54  ? 534  TYR   A C    1 
ATOM   7452  O O    . TYR   A  1 508 ? 26.654 -6.783  -46.463 1.00 18.81  ? 534  TYR   A O    1 
ATOM   7453  C CB   . TYR   A  1 508 ? 24.942 -4.344  -46.586 1.00 21.42  ? 534  TYR   A CB   1 
ATOM   7454  C CG   . TYR   A  1 508 ? 25.684 -3.204  -45.914 1.00 22.63  ? 534  TYR   A CG   1 
ATOM   7455  C CD1  . TYR   A  1 508 ? 26.939 -3.400  -45.354 1.00 23.78  ? 534  TYR   A CD1  1 
ATOM   7456  C CD2  . TYR   A  1 508 ? 25.067 -1.978  -45.700 1.00 23.84  ? 534  TYR   A CD2  1 
ATOM   7457  C CE1  . TYR   A  1 508 ? 27.595 -2.383  -44.672 1.00 24.80  ? 534  TYR   A CE1  1 
ATOM   7458  C CE2  . TYR   A  1 508 ? 25.694 -0.971  -44.976 1.00 25.12  ? 534  TYR   A CE2  1 
ATOM   7459  C CZ   . TYR   A  1 508 ? 26.971 -1.168  -44.489 1.00 26.09  ? 534  TYR   A CZ   1 
ATOM   7460  O OH   . TYR   A  1 508 ? 27.637 -0.174  -43.821 1.00 28.04  ? 534  TYR   A OH   1 
ATOM   7461  H H    . TYR   A  1 508 ? 24.519 -6.716  -47.972 0.00 23.32  ? 534  TYR   A H    1 
ATOM   7462  H HA   . TYR   A  1 508 ? 26.068 -4.224  -48.411 0.00 22.58  ? 534  TYR   A HA   1 
ATOM   7463  H HB2  . TYR   A  1 508 ? 23.999 -3.949  -46.961 0.00 23.29  ? 534  TYR   A HB2  1 
ATOM   7464  H HB3  . TYR   A  1 508 ? 24.738 -5.096  -45.826 0.00 22.98  ? 534  TYR   A HB3  1 
ATOM   7465  H HD1  . TYR   A  1 508 ? 27.437 -4.345  -45.476 0.00 25.10  ? 534  TYR   A HD1  1 
ATOM   7466  H HD2  . TYR   A  1 508 ? 24.071 -1.812  -46.068 0.00 25.88  ? 534  TYR   A HD2  1 
ATOM   7467  H HE1  . TYR   A  1 508 ? 28.582 -2.546  -44.276 0.00 25.77  ? 534  TYR   A HE1  1 
ATOM   7468  H HE2  . TYR   A  1 508 ? 25.211 -0.015  -44.868 0.00 26.86  ? 534  TYR   A HE2  1 
ATOM   7469  H HH   . TYR   A  1 508 ? 27.069 0.636   -43.733 0.00 29.77  ? 534  TYR   A HH   1 
ATOM   7470  N N    . LEU   A  1 509 ? 28.022 -5.664  -47.876 1.00 18.85  ? 535  LEU   A N    1 
ATOM   7471  C CA   . LEU   A  1 509 ? 29.213 -6.444  -47.575 1.00 19.11  ? 535  LEU   A CA   1 
ATOM   7472  C C    . LEU   A  1 509 ? 30.298 -5.578  -46.938 1.00 18.50  ? 535  LEU   A C    1 
ATOM   7473  O O    . LEU   A  1 509 ? 30.784 -4.629  -47.558 1.00 17.94  ? 535  LEU   A O    1 
ATOM   7474  C CB   . LEU   A  1 509 ? 29.734 -7.072  -48.876 1.00 18.92  ? 535  LEU   A CB   1 
ATOM   7475  C CG   . LEU   A  1 509 ? 31.050 -7.858  -48.779 1.00 19.79  ? 535  LEU   A CG   1 
ATOM   7476  C CD1  . LEU   A  1 509 ? 30.948 -9.013  -47.768 1.00 20.08  ? 535  LEU   A CD1  1 
ATOM   7477  C CD2  . LEU   A  1 509 ? 31.450 -8.398  -50.138 1.00 20.06  ? 535  LEU   A CD2  1 
ATOM   7478  H H    . LEU   A  1 509 ? 28.189 -4.939  -48.567 0.00 19.71  ? 535  LEU   A H    1 
ATOM   7479  H HA   . LEU   A  1 509 ? 28.972 -7.254  -46.890 0.00 19.84  ? 535  LEU   A HA   1 
ATOM   7480  H HB2  . LEU   A  1 509 ? 28.972 -7.747  -49.264 0.00 20.19  ? 535  LEU   A HB2  1 
ATOM   7481  H HB3  . LEU   A  1 509 ? 29.910 -6.267  -49.587 0.00 19.89  ? 535  LEU   A HB3  1 
ATOM   7482  H HG   . LEU   A  1 509 ? 31.829 -7.169  -48.464 0.00 20.54  ? 535  LEU   A HG   1 
ATOM   7483  H HD11 . LEU   A  1 509 ? 31.822 -9.656  -47.865 0.00 21.19  ? 535  LEU   A HD11 1 
ATOM   7484  H HD12 . LEU   A  1 509 ? 30.905 -8.603  -46.760 0.00 20.89  ? 535  LEU   A HD12 1 
ATOM   7485  H HD13 . LEU   A  1 509 ? 30.040 -9.575  -47.979 0.00 21.44  ? 535  LEU   A HD13 1 
ATOM   7486  H HD21 . LEU   A  1 509 ? 32.376 -8.963  -50.041 0.00 21.45  ? 535  LEU   A HD21 1 
ATOM   7487  H HD22 . LEU   A  1 509 ? 30.658 -9.045  -50.511 0.00 21.80  ? 535  LEU   A HD22 1 
ATOM   7488  H HD23 . LEU   A  1 509 ? 31.598 -7.562  -50.820 0.00 21.48  ? 535  LEU   A HD23 1 
ATOM   7489  N N    . ASP   A  1 510 ? 30.711 -5.940  -45.710 1.00 18.04  ? 536  ASP   A N    1 
ATOM   7490  C CA   . ASP   A  1 510 ? 31.770 -5.225  -45.011 1.00 17.86  ? 536  ASP   A CA   1 
ATOM   7491  C C    . ASP   A  1 510 ? 33.052 -6.099  -45.032 1.00 17.31  ? 536  ASP   A C    1 
ATOM   7492  O O    . ASP   A  1 510 ? 33.075 -7.180  -44.454 1.00 16.40  ? 536  ASP   A O    1 
ATOM   7493  C CB   . ASP   A  1 510 ? 31.298 -4.843  -43.587 1.00 19.05  ? 536  ASP   A CB   1 
ATOM   7494  C CG   . ASP   A  1 510 ? 32.313 -4.069  -42.758 1.00 21.61  ? 536  ASP   A CG   1 
ATOM   7495  O OD1  . ASP   A  1 510 ? 33.510 -4.234  -42.993 1.00 23.41  ? 536  ASP   A OD1  1 
ATOM   7496  O OD2  . ASP   A  1 510 ? 31.895 -3.319  -41.852 1.00 21.68  ? 536  ASP   A OD2  1 
ATOM   7497  H H    . ASP   A  1 510 ? 30.336 -6.719  -45.179 0.00 17.95  ? 536  ASP   A H    1 
ATOM   7498  H HA   . ASP   A  1 510 ? 31.995 -4.294  -45.526 0.00 17.28  ? 536  ASP   A HA   1 
ATOM   7499  H HB2  . ASP   A  1 510 ? 30.416 -4.213  -43.686 0.00 18.61  ? 536  ASP   A HB2  1 
ATOM   7500  H HB3  . ASP   A  1 510 ? 31.039 -5.739  -43.029 0.00 18.60  ? 536  ASP   A HB3  1 
ATOM   7501  N N    . LEU   A  1 511 ? 34.078 -5.662  -45.791 1.00 17.50  ? 537  LEU   A N    1 
ATOM   7502  C CA   . LEU   A  1 511 ? 35.369 -6.360  -45.863 1.00 18.26  ? 537  LEU   A CA   1 
ATOM   7503  C C    . LEU   A  1 511 ? 36.499 -5.475  -45.319 1.00 18.04  ? 537  LEU   A C    1 
ATOM   7504  O O    . LEU   A  1 511 ? 37.661 -5.672  -45.681 1.00 17.64  ? 537  LEU   A O    1 
ATOM   7505  C CB   . LEU   A  1 511 ? 35.702 -6.747  -47.319 1.00 18.81  ? 537  LEU   A CB   1 
ATOM   7506  C CG   . LEU   A  1 511 ? 34.894 -7.879  -47.938 1.00 20.93  ? 537  LEU   A CG   1 
ATOM   7507  C CD1  . LEU   A  1 511 ? 35.105 -7.901  -49.460 1.00 21.19  ? 537  LEU   A CD1  1 
ATOM   7508  C CD2  . LEU   A  1 511 ? 35.262 -9.237  -47.360 1.00 21.61  ? 537  LEU   A CD2  1 
ATOM   7509  H H    . LEU   A  1 511 ? 34.047 -4.829  -46.371 0.00 16.83  ? 537  LEU   A H    1 
ATOM   7510  H HA   . LEU   A  1 511 ? 35.350 -7.248  -45.234 0.00 17.79  ? 537  LEU   A HA   1 
ATOM   7511  H HB2  . LEU   A  1 511 ? 35.558 -5.868  -47.946 0.00 18.71  ? 537  LEU   A HB2  1 
ATOM   7512  H HB3  . LEU   A  1 511 ? 36.743 -7.057  -47.374 0.00 18.72  ? 537  LEU   A HB3  1 
ATOM   7513  H HG   . LEU   A  1 511 ? 33.842 -7.713  -47.722 0.00 21.63  ? 537  LEU   A HG   1 
ATOM   7514  H HD11 . LEU   A  1 511 ? 34.689 -8.822  -49.864 0.00 22.51  ? 537  LEU   A HD11 1 
ATOM   7515  H HD12 . LEU   A  1 511 ? 34.603 -7.040  -49.900 0.00 22.21  ? 537  LEU   A HD12 1 
ATOM   7516  H HD13 . LEU   A  1 511 ? 36.173 -7.851  -49.668 0.00 22.19  ? 537  LEU   A HD13 1 
ATOM   7517  H HD21 . LEU   A  1 511 ? 34.400 -9.896  -47.451 0.00 22.76  ? 537  LEU   A HD21 1 
ATOM   7518  H HD22 . LEU   A  1 511 ? 36.083 -9.643  -47.951 0.00 22.68  ? 537  LEU   A HD22 1 
ATOM   7519  H HD23 . LEU   A  1 511 ? 35.575 -9.170  -46.321 0.00 22.33  ? 537  LEU   A HD23 1 
ATOM   7520  N N    . THR   A  1 512 ? 36.179 -4.551  -44.404 1.00 17.41  ? 538  THR   A N    1 
ATOM   7521  C CA   . THR   A  1 512 ? 37.160 -3.611  -43.903 1.00 17.03  ? 538  THR   A CA   1 
ATOM   7522  C C    . THR   A  1 512 ? 38.232 -4.264  -43.048 1.00 16.67  ? 538  THR   A C    1 
ATOM   7523  O O    . THR   A  1 512 ? 38.028 -5.353  -42.509 1.00 14.76  ? 538  THR   A O    1 
ATOM   7524  C CB   . THR   A  1 512 ? 36.484 -2.494  -43.095 1.00 19.07  ? 538  THR   A CB   1 
ATOM   7525  O OG1  . THR   A  1 512 ? 35.959 -3.041  -41.876 1.00 21.30  ? 538  THR   A OG1  1 
ATOM   7526  C CG2  . THR   A  1 512 ? 35.412 -1.790  -43.873 1.00 18.93  ? 538  THR   A CG2  1 
ATOM   7527  H H    . THR   A  1 512 ? 35.271 -4.475  -43.956 0.00 16.22  ? 538  THR   A H    1 
ATOM   7528  H HA   . THR   A  1 512 ? 37.654 -3.143  -44.752 0.00 15.64  ? 538  THR   A HA   1 
ATOM   7529  H HB   . THR   A  1 512 ? 37.238 -1.750  -42.840 0.00 17.75  ? 538  THR   A HB   1 
ATOM   7530  H HG1  . THR   A  1 512 ? 35.194 -3.645  -42.064 0.00 20.58  ? 538  THR   A HG1  1 
ATOM   7531  H HG21 . THR   A  1 512 ? 35.103 -0.889  -43.345 0.00 17.70  ? 538  THR   A HG21 1 
ATOM   7532  H HG22 . THR   A  1 512 ? 35.787 -1.516  -44.857 0.00 17.89  ? 538  THR   A HG22 1 
ATOM   7533  H HG23 . THR   A  1 512 ? 34.543 -2.436  -43.993 0.00 17.91  ? 538  THR   A HG23 1 
ATOM   7534  N N    . ASN   A  1 513 ? 39.376 -3.581  -42.924 1.00 16.84  ? 539  ASN   A N    1 
ATOM   7535  C CA   . ASN   A  1 513 ? 40.433 -3.989  -42.016 1.00 17.25  ? 539  ASN   A CA   1 
ATOM   7536  C C    . ASN   A  1 513 ? 40.953 -5.388  -42.281 1.00 16.71  ? 539  ASN   A C    1 
ATOM   7537  O O    . ASN   A  1 513 ? 41.174 -6.151  -41.359 1.00 17.72  ? 539  ASN   A O    1 
ATOM   7538  C CB   . ASN   A  1 513 ? 39.955 -3.825  -40.565 1.00 18.68  ? 539  ASN   A CB   1 
ATOM   7539  C CG   . ASN   A  1 513 ? 39.696 -2.379  -40.216 1.00 21.98  ? 539  ASN   A CG   1 
ATOM   7540  O OD1  . ASN   A  1 513 ? 38.571 -1.898  -40.260 1.00 24.35  ? 539  ASN   A OD1  1 
ATOM   7541  N ND2  . ASN   A  1 513 ? 40.728 -1.645  -39.879 1.00 22.86  ? 539  ASN   A ND2  1 
ATOM   7542  H H    . ASN   A  1 513 ? 39.603 -2.761  -43.477 0.00 15.19  ? 539  ASN   A H    1 
ATOM   7543  H HA   . ASN   A  1 513 ? 41.271 -3.306  -42.152 0.00 15.62  ? 539  ASN   A HA   1 
ATOM   7544  H HB2  . ASN   A  1 513 ? 39.036 -4.389  -40.404 0.00 17.24  ? 539  ASN   A HB2  1 
ATOM   7545  H HB3  . ASN   A  1 513 ? 40.722 -4.185  -39.882 0.00 17.22  ? 539  ASN   A HB3  1 
ATOM   7546  H HD21 . ASN   A  1 513 ? 40.599 -0.667  -39.638 0.00 21.94  ? 539  ASN   A HD21 1 
ATOM   7547  H HD22 . ASN   A  1 513 ? 41.659 -2.049  -39.865 0.00 22.08  ? 539  ASN   A HD22 1 
ATOM   7548  N N    . ASN   A  1 514 ? 41.184 -5.709  -43.543 1.00 16.15  ? 540  ASN   A N    1 
ATOM   7549  C CA   . ASN   A  1 514 ? 41.792 -6.977  -43.943 1.00 15.39  ? 540  ASN   A CA   1 
ATOM   7550  C C    . ASN   A  1 514 ? 43.130 -6.610  -44.661 1.00 15.62  ? 540  ASN   A C    1 
ATOM   7551  O O    . ASN   A  1 514 ? 43.653 -5.515  -44.436 1.00 15.76  ? 540  ASN   A O    1 
ATOM   7552  C CB   . ASN   A  1 514 ? 40.778 -7.760  -44.814 1.00 15.60  ? 540  ASN   A CB   1 
ATOM   7553  C CG   . ASN   A  1 514 ? 39.748 -8.476  -43.970 1.00 17.61  ? 540  ASN   A CG   1 
ATOM   7554  O OD1  . ASN   A  1 514 ? 40.092 -9.385  -43.209 1.00 18.03  ? 540  ASN   A OD1  1 
ATOM   7555  N ND2  . ASN   A  1 514 ? 38.486 -8.094  -44.066 1.00 17.57  ? 540  ASN   A ND2  1 
ATOM   7556  H H    . ASN   A  1 514 ? 40.984 -5.100  -44.330 0.00 14.74  ? 540  ASN   A H    1 
ATOM   7557  H HA   . ASN   A  1 514 ? 42.059 -7.582  -43.077 0.00 14.11  ? 540  ASN   A HA   1 
ATOM   7558  H HB2  . ASN   A  1 514 ? 40.273 -7.061  -45.479 0.00 14.51  ? 540  ASN   A HB2  1 
ATOM   7559  H HB3  . ASN   A  1 514 ? 41.283 -8.524  -45.401 0.00 14.79  ? 540  ASN   A HB3  1 
ATOM   7560  H HD21 . ASN   A  1 514 ? 37.778 -8.560  -43.507 0.00 16.86  ? 540  ASN   A HD21 1 
ATOM   7561  H HD22 . ASN   A  1 514 ? 38.217 -7.341  -44.691 0.00 16.80  ? 540  ASN   A HD22 1 
ATOM   7562  N N    . ARG   A  1 515 ? 43.711 -7.522  -45.448 1.00 15.64  ? 541  ARG   A N    1 
ATOM   7563  C CA   . ARG   A  1 515 ? 44.924 -7.298  -46.252 1.00 16.48  ? 541  ARG   A CA   1 
ATOM   7564  C C    . ARG   A  1 515 ? 44.577 -7.735  -47.697 1.00 16.32  ? 541  ARG   A C    1 
ATOM   7565  O O    . ARG   A  1 515 ? 45.395 -8.363  -48.355 1.00 16.96  ? 541  ARG   A O    1 
ATOM   7566  C CB   . ARG   A  1 515 ? 46.074 -8.189  -45.709 1.00 19.63  ? 541  ARG   A CB   1 
ATOM   7567  C CG   . ARG   A  1 515 ? 46.438 -7.971  -44.243 1.00 25.17  ? 541  ARG   A CG   1 
ATOM   7568  C CD   . ARG   A  1 515 ? 47.076 -9.214  -43.627 1.00 30.17  ? 541  ARG   A CD   1 
ATOM   7569  N NE   . ARG   A  1 515 ? 48.460 -9.455  -44.061 1.00 36.44  ? 541  ARG   A NE   1 
ATOM   7570  C CZ   . ARG   A  1 515 ? 49.578 -9.249  -43.345 1.00 39.25  ? 541  ARG   A CZ   1 
ATOM   7571  N NH1  . ARG   A  1 515 ? 50.765 -9.551  -43.856 1.00 38.08  ? 541  ARG   A NH1  1 
ATOM   7572  N NH2  . ARG   A  1 515 ? 49.513 -8.734  -42.117 1.00 39.56  ? 541  ARG   A NH2  1 
ATOM   7573  H H    . ARG   A  1 515 ? 43.389 -8.481  -45.529 0.00 14.96  ? 541  ARG   A H    1 
ATOM   7574  H HA   . ARG   A  1 515 ? 45.233 -6.254  -46.252 0.00 15.82  ? 541  ARG   A HA   1 
ATOM   7575  H HB2  . ARG   A  1 515 ? 45.784 -9.230  -45.844 0.00 20.16  ? 541  ARG   A HB2  1 
ATOM   7576  H HB3  . ARG   A  1 515 ? 46.973 -7.985  -46.289 0.00 20.11  ? 541  ARG   A HB3  1 
ATOM   7577  H HG2  . ARG   A  1 515 ? 47.157 -7.156  -44.176 0.00 26.38  ? 541  ARG   A HG2  1 
ATOM   7578  H HG3  . ARG   A  1 515 ? 45.548 -7.730  -43.663 0.00 26.23  ? 541  ARG   A HG3  1 
ATOM   7579  H HD2  . ARG   A  1 515 ? 46.984 -9.167  -42.544 0.00 32.58  ? 541  ARG   A HD2  1 
ATOM   7580  H HD3  . ARG   A  1 515 ? 46.508 -10.082 -43.956 0.00 32.86  ? 541  ARG   A HD3  1 
ATOM   7581  H HE   . ARG   A  1 515 ? 48.573 -9.872  -44.980 0.00 40.76  ? 541  ARG   A HE   1 
ATOM   7582  H HH11 . ARG   A  1 515 ? 50.839 -9.948  -44.787 0.00 43.12  ? 541  ARG   A HH11 1 
ATOM   7583  H HH12 . ARG   A  1 515 ? 51.608 -9.383  -43.318 0.00 43.00  ? 541  ARG   A HH12 1 
ATOM   7584  H HH21 . ARG   A  1 515 ? 48.650 -8.460  -41.662 0.00 43.88  ? 541  ARG   A HH21 1 
ATOM   7585  H HH22 . ARG   A  1 515 ? 50.379 -8.572  -41.612 0.00 44.21  ? 541  ARG   A HH22 1 
ATOM   7586  N N    . LEU   A  1 516 ? 43.358 -7.444  -48.176 1.00 16.09  ? 542  LEU   A N    1 
ATOM   7587  C CA   . LEU   A  1 516 ? 42.893 -7.941  -49.469 1.00 16.28  ? 542  LEU   A CA   1 
ATOM   7588  C C    . LEU   A  1 516 ? 43.769 -7.516  -50.646 1.00 17.17  ? 542  LEU   A C    1 
ATOM   7589  O O    . LEU   A  1 516 ? 44.292 -6.408  -50.688 1.00 16.88  ? 542  LEU   A O    1 
ATOM   7590  C CB   . LEU   A  1 516 ? 41.422 -7.558  -49.694 1.00 16.55  ? 542  LEU   A CB   1 
ATOM   7591  C CG   . LEU   A  1 516 ? 40.420 -8.327  -48.801 1.00 18.49  ? 542  LEU   A CG   1 
ATOM   7592  C CD1  . LEU   A  1 516 ? 39.063 -7.683  -48.823 1.00 19.43  ? 542  LEU   A CD1  1 
ATOM   7593  C CD2  . LEU   A  1 516 ? 40.334 -9.817  -49.221 1.00 18.98  ? 542  LEU   A CD2  1 
ATOM   7594  H H    . LEU   A  1 516 ? 42.676 -6.861  -47.700 0.00 15.50  ? 542  LEU   A H    1 
ATOM   7595  H HA   . LEU   A  1 516 ? 42.969 -9.026  -49.398 0.00 16.45  ? 542  LEU   A HA   1 
ATOM   7596  H HB2  . LEU   A  1 516 ? 41.295 -6.494  -49.496 0.00 16.26  ? 542  LEU   A HB2  1 
ATOM   7597  H HB3  . LEU   A  1 516 ? 41.167 -7.760  -50.733 0.00 16.73  ? 542  LEU   A HB3  1 
ATOM   7598  H HG   . LEU   A  1 516 ? 40.772 -8.300  -47.771 0.00 18.58  ? 542  LEU   A HG   1 
ATOM   7599  H HD11 . LEU   A  1 516 ? 38.360 -8.346  -48.321 0.00 19.81  ? 542  LEU   A HD11 1 
ATOM   7600  H HD12 . LEU   A  1 516 ? 39.115 -6.730  -48.299 0.00 19.51  ? 542  LEU   A HD12 1 
ATOM   7601  H HD13 . LEU   A  1 516 ? 38.758 -7.527  -49.856 0.00 19.96  ? 542  LEU   A HD13 1 
ATOM   7602  H HD21 . LEU   A  1 516 ? 39.424 -10.258 -48.817 0.00 19.74  ? 542  LEU   A HD21 1 
ATOM   7603  H HD22 . LEU   A  1 516 ? 40.327 -9.886  -50.307 0.00 19.96  ? 542  LEU   A HD22 1 
ATOM   7604  H HD23 . LEU   A  1 516 ? 41.191 -10.354 -48.819 0.00 19.80  ? 542  LEU   A HD23 1 
ATOM   7605  N N    . ASP   A  1 517 ? 44.013 -8.462  -51.539 1.00 17.19  ? 543  ASP   A N    1 
ATOM   7606  C CA   . ASP   A  1 517 ? 44.861 -8.249  -52.701 1.00 17.49  ? 543  ASP   A CA   1 
ATOM   7607  C C    . ASP   A  1 517 ? 43.928 -8.120  -53.885 1.00 18.66  ? 543  ASP   A C    1 
ATOM   7608  O O    . ASP   A  1 517 ? 43.467 -9.125  -54.423 1.00 19.32  ? 543  ASP   A O    1 
ATOM   7609  C CB   . ASP   A  1 517 ? 45.812 -9.444  -52.841 1.00 17.70  ? 543  ASP   A CB   1 
ATOM   7610  C CG   . ASP   A  1 517 ? 46.810 -9.357  -53.983 1.00 20.38  ? 543  ASP   A CG   1 
ATOM   7611  O OD1  . ASP   A  1 517 ? 46.840 -8.305  -54.676 1.00 21.15  ? 543  ASP   A OD1  1 
ATOM   7612  O OD2  . ASP   A  1 517 ? 47.567 -10.335 -54.181 1.00 20.79  ? 543  ASP   A OD2  1 
ATOM   7613  H H    . ASP   A  1 517 ? 43.626 -9.400  -51.497 0.00 18.07  ? 543  ASP   A H    1 
ATOM   7614  H HA   . ASP   A  1 517 ? 45.459 -7.343  -52.609 0.00 18.38  ? 543  ASP   A HA   1 
ATOM   7615  H HB2  . ASP   A  1 517 ? 46.388 -9.526  -51.920 0.00 19.03  ? 543  ASP   A HB2  1 
ATOM   7616  H HB3  . ASP   A  1 517 ? 45.230 -10.354 -52.979 0.00 19.34  ? 543  ASP   A HB3  1 
ATOM   7617  N N    . PHE   A  1 518 ? 43.594 -6.881  -54.254 1.00 19.18  ? 544  PHE   A N    1 
ATOM   7618  C CA   . PHE   A  1 518 ? 42.694 -6.640  -55.375 1.00 19.74  ? 544  PHE   A CA   1 
ATOM   7619  C C    . PHE   A  1 518 ? 43.467 -6.856  -56.676 1.00 20.88  ? 544  PHE   A C    1 
ATOM   7620  O O    . PHE   A  1 518 ? 44.065 -5.923  -57.189 1.00 21.34  ? 544  PHE   A O    1 
ATOM   7621  C CB   . PHE   A  1 518 ? 42.079 -5.240  -55.271 1.00 19.35  ? 544  PHE   A CB   1 
ATOM   7622  C CG   . PHE   A  1 518 ? 41.206 -5.122  -54.040 1.00 20.31  ? 544  PHE   A CG   1 
ATOM   7623  C CD1  . PHE   A  1 518 ? 39.923 -5.658  -54.026 1.00 21.60  ? 544  PHE   A CD1  1 
ATOM   7624  C CD2  . PHE   A  1 518 ? 41.702 -4.578  -52.868 1.00 21.47  ? 544  PHE   A CD2  1 
ATOM   7625  C CE1  . PHE   A  1 518 ? 39.134 -5.582  -52.885 1.00 22.39  ? 544  PHE   A CE1  1 
ATOM   7626  C CE2  . PHE   A  1 518 ? 40.895 -4.468  -51.739 1.00 22.37  ? 544  PHE   A CE2  1 
ATOM   7627  C CZ   . PHE   A  1 518 ? 39.622 -4.978  -51.754 1.00 22.54  ? 544  PHE   A CZ   1 
ATOM   7628  H H    . PHE   A  1 518 ? 43.936 -6.037  -53.805 0.00 20.35  ? 544  PHE   A H    1 
ATOM   7629  H HA   . PHE   A  1 518 ? 41.876 -7.360  -55.354 0.00 21.57  ? 544  PHE   A HA   1 
ATOM   7630  H HB2  . PHE   A  1 518 ? 42.870 -4.494  -55.211 0.00 20.63  ? 544  PHE   A HB2  1 
ATOM   7631  H HB3  . PHE   A  1 518 ? 41.456 -5.059  -56.146 0.00 20.94  ? 544  PHE   A HB3  1 
ATOM   7632  H HD1  . PHE   A  1 518 ? 39.528 -6.118  -54.915 0.00 23.48  ? 544  PHE   A HD1  1 
ATOM   7633  H HD2  . PHE   A  1 518 ? 42.695 -4.158  -52.856 0.00 22.55  ? 544  PHE   A HD2  1 
ATOM   7634  H HE1  . PHE   A  1 518 ? 38.128 -5.968  -52.898 0.00 23.95  ? 544  PHE   A HE1  1 
ATOM   7635  H HE2  . PHE   A  1 518 ? 41.283 -4.016  -50.841 0.00 23.15  ? 544  PHE   A HE2  1 
ATOM   7636  H HZ   . PHE   A  1 518 ? 39.009 -4.920  -50.869 0.00 23.49  ? 544  PHE   A HZ   1 
ATOM   7637  N N    . ASP   A  1 519 ? 43.500 -8.114  -57.164 1.00 21.27  ? 545  ASP   A N    1 
ATOM   7638  C CA   . ASP   A  1 519 ? 44.282 -8.484  -58.337 1.00 22.00  ? 545  ASP   A CA   1 
ATOM   7639  C C    . ASP   A  1 519 ? 43.491 -9.299  -59.360 1.00 23.04  ? 545  ASP   A C    1 
ATOM   7640  O O    . ASP   A  1 519 ? 44.079 -10.102 -60.082 1.00 23.57  ? 545  ASP   A O    1 
ATOM   7641  C CB   . ASP   A  1 519 ? 45.515 -9.286  -57.878 1.00 23.17  ? 545  ASP   A CB   1 
ATOM   7642  C CG   . ASP   A  1 519 ? 46.591 -9.380  -58.931 1.00 25.88  ? 545  ASP   A CG   1 
ATOM   7643  O OD1  . ASP   A  1 519 ? 46.748 -8.419  -59.690 1.00 26.29  ? 545  ASP   A OD1  1 
ATOM   7644  O OD2  . ASP   A  1 519 ? 47.279 -10.425 -58.991 1.00 27.12  ? 545  ASP   A OD2  1 
ATOM   7645  H H    . ASP   A  1 519 ? 42.994 -8.894  -56.754 0.00 24.13  ? 545  ASP   A H    1 
ATOM   7646  H HA   . ASP   A  1 519 ? 44.619 -7.578  -58.836 0.00 25.39  ? 545  ASP   A HA   1 
ATOM   7647  H HB2  . ASP   A  1 519 ? 45.946 -8.802  -57.003 0.00 26.62  ? 545  ASP   A HB2  1 
ATOM   7648  H HB3  . ASP   A  1 519 ? 45.206 -10.299 -57.624 0.00 27.09  ? 545  ASP   A HB3  1 
ATOM   7649  N N    . ASN   A  1 520 ? 42.167 -9.115  -59.428 1.00 22.89  ? 546  ASN   A N    1 
ATOM   7650  C CA   . ASN   A  1 520 ? 41.351 -9.852  -60.392 1.00 23.18  ? 546  ASN   A CA   1 
ATOM   7651  C C    . ASN   A  1 520 ? 40.132 -9.015  -60.758 1.00 23.26  ? 546  ASN   A C    1 
ATOM   7652  O O    . ASN   A  1 520 ? 39.365 -8.659  -59.871 1.00 23.11  ? 546  ASN   A O    1 
ATOM   7653  C CB   . ASN   A  1 520 ? 40.934 -11.236 -59.833 1.00 24.54  ? 546  ASN   A CB   1 
ATOM   7654  C CG   . ASN   A  1 520 ? 40.323 -12.057 -60.881 1.00 29.60  ? 546  ASN   A CG   1 
ATOM   7655  O OD1  . ASN   A  1 520 ? 39.134 -11.884 -61.148 1.00 28.10  ? 546  ASN   A OD1  1 
ATOM   7656  N ND2  . ASN   A  1 520 ? 40.965 -13.059 -61.447 1.00 35.89  ? 546  ASN   A ND2  1 
ATOM   7657  H H    . ASN   A  1 520 ? 41.639 -8.470  -58.850 0.00 26.57  ? 546  ASN   A H    1 
ATOM   7658  H HA   . ASN   A  1 520 ? 41.927 -10.006 -61.303 0.00 28.06  ? 546  ASN   A HA   1 
ATOM   7659  H HB2  . ASN   A  1 520 ? 41.814 -11.753 -59.456 0.00 29.52  ? 546  ASN   A HB2  1 
ATOM   7660  H HB3  . ASN   A  1 520 ? 40.204 -11.099 -59.036 0.00 29.22  ? 546  ASN   A HB3  1 
ATOM   7661  H HD21 . ASN   A  1 520 ? 40.706 -12.683 -62.336 0.00 44.38  ? 546  ASN   A HD21 1 
ATOM   7662  H HD22 . ASN   A  1 520 ? 41.859 -13.431 -61.147 0.00 44.18  ? 546  ASN   A HD22 1 
ATOM   7663  N N    . ALA   A  1 521 ? 39.951 -8.700  -62.060 1.00 23.25  ? 547  ALA   A N    1 
ATOM   7664  C CA   . ALA   A  1 521 ? 38.830 -7.876  -62.531 1.00 23.61  ? 547  ALA   A CA   1 
ATOM   7665  C C    . ALA   A  1 521 ? 37.437 -8.457  -62.249 1.00 23.70  ? 547  ALA   A C    1 
ATOM   7666  O O    . ALA   A  1 521 ? 36.463 -7.724  -62.361 1.00 24.38  ? 547  ALA   A O    1 
ATOM   7667  C CB   . ALA   A  1 521 ? 38.978 -7.601  -64.024 1.00 23.40  ? 547  ALA   A CB   1 
ATOM   7668  H H    . ALA   A  1 521 ? 40.566 -9.000  -62.809 0.00 28.45  ? 547  ALA   A H    1 
ATOM   7669  H HA   . ALA   A  1 521 ? 38.883 -6.915  -62.021 0.00 28.26  ? 547  ALA   A HA   1 
ATOM   7670  H HB1  . ALA   A  1 521 ? 38.114 -7.039  -64.372 0.00 28.93  ? 547  ALA   A HB1  1 
ATOM   7671  H HB2  . ALA   A  1 521 ? 39.889 -7.027  -64.187 0.00 28.76  ? 547  ALA   A HB2  1 
ATOM   7672  H HB3  . ALA   A  1 521 ? 39.039 -8.550  -64.555 0.00 29.25  ? 547  ALA   A HB3  1 
ATOM   7673  N N    . SER   A  1 522 ? 37.324 -9.756  -61.931 1.00 23.35  ? 548  SER   A N    1 
ATOM   7674  C CA   . SER   A  1 522 ? 36.031 -10.391 -61.655 1.00 23.38  ? 548  SER   A CA   1 
ATOM   7675  C C    . SER   A  1 522 ? 35.699 -10.466 -60.153 1.00 22.72  ? 548  SER   A C    1 
ATOM   7676  O O    . SER   A  1 522 ? 34.689 -11.075 -59.800 1.00 21.93  ? 548  SER   A O    1 
ATOM   7677  C CB   . SER   A  1 522 ? 35.998 -11.802 -62.238 1.00 25.15  ? 548  SER   A CB   1 
ATOM   7678  O OG   . SER   A  1 522 ? 36.398 -11.801 -63.596 1.00 28.14  ? 548  SER   A OG   1 
ATOM   7679  H H    . SER   A  1 522 ? 38.101 -10.406 -61.868 0.00 28.66  ? 548  SER   A H    1 
ATOM   7680  H HA   . SER   A  1 522 ? 35.229 -9.837  -62.140 0.00 28.90  ? 548  SER   A HA   1 
ATOM   7681  H HB2  . SER   A  1 522 ? 36.676 -12.437 -61.670 0.00 31.37  ? 548  SER   A HB2  1 
ATOM   7682  H HB3  . SER   A  1 522 ? 34.984 -12.192 -62.177 0.00 31.65  ? 548  SER   A HB3  1 
ATOM   7683  H HG   . SER   A  1 522 ? 36.364 -12.723 -63.963 0.00 35.92  ? 548  SER   A HG   1 
ATOM   7684  N N    . ALA   A  1 523 ? 36.513 -9.869  -59.277 1.00 21.95  ? 549  ALA   A N    1 
ATOM   7685  C CA   . ALA   A  1 523 ? 36.270 -9.915  -57.831 1.00 21.71  ? 549  ALA   A CA   1 
ATOM   7686  C C    . ALA   A  1 523 ? 34.859 -9.469  -57.444 1.00 21.37  ? 549  ALA   A C    1 
ATOM   7687  O O    . ALA   A  1 523 ? 34.395 -8.450  -57.941 1.00 21.30  ? 549  ALA   A O    1 
ATOM   7688  C CB   . ALA   A  1 523 ? 37.280 -9.030  -57.110 1.00 21.56  ? 549  ALA   A CB   1 
ATOM   7689  H H    . ALA   A  1 523 ? 37.346 -9.343  -59.523 0.00 25.98  ? 549  ALA   A H    1 
ATOM   7690  H HA   . ALA   A  1 523 ? 36.418 -10.937 -57.486 0.00 25.47  ? 549  ALA   A HA   1 
ATOM   7691  H HB1  . ALA   A  1 523 ? 37.084 -9.069  -56.039 0.00 24.39  ? 549  ALA   A HB1  1 
ATOM   7692  H HB2  . ALA   A  1 523 ? 38.286 -9.393  -57.318 0.00 24.78  ? 549  ALA   A HB2  1 
ATOM   7693  H HB3  . ALA   A  1 523 ? 37.174 -8.008  -57.471 0.00 24.60  ? 549  ALA   A HB3  1 
ATOM   7694  N N    . LEU   A  1 524 ? 34.173 -10.235 -56.583 1.00 20.92  ? 550  LEU   A N    1 
ATOM   7695  C CA   . LEU   A  1 524 ? 32.855 -9.876  -56.045 1.00 21.61  ? 550  LEU   A CA   1 
ATOM   7696  C C    . LEU   A  1 524 ? 31.705 -9.779  -57.053 1.00 23.20  ? 550  LEU   A C    1 
ATOM   7697  O O    . LEU   A  1 524 ? 30.565 -9.592  -56.612 1.00 23.84  ? 550  LEU   A O    1 
ATOM   7698  C CB   . LEU   A  1 524 ? 32.954 -8.551  -55.267 1.00 21.44  ? 550  LEU   A CB   1 
ATOM   7699  C CG   . LEU   A  1 524 ? 33.976 -8.520  -54.135 1.00 21.60  ? 550  LEU   A CG   1 
ATOM   7700  C CD1  . LEU   A  1 524 ? 34.043 -7.157  -53.518 1.00 21.55  ? 550  LEU   A CD1  1 
ATOM   7701  C CD2  . LEU   A  1 524 ? 33.624 -9.546  -53.066 1.00 22.51  ? 550  LEU   A CD2  1 
ATOM   7702  H H    . LEU   A  1 524 ? 34.506 -11.128 -56.233 0.00 24.34  ? 550  LEU   A H    1 
ATOM   7703  H HA   . LEU   A  1 524 ? 32.565 -10.652 -55.339 0.00 25.01  ? 550  LEU   A HA   1 
ATOM   7704  H HB2  . LEU   A  1 524 ? 33.209 -7.752  -55.962 0.00 24.33  ? 550  LEU   A HB2  1 
ATOM   7705  H HB3  . LEU   A  1 524 ? 31.984 -8.334  -54.823 0.00 24.27  ? 550  LEU   A HB3  1 
ATOM   7706  H HG   . LEU   A  1 524 ? 34.965 -8.756  -54.526 0.00 24.11  ? 550  LEU   A HG   1 
ATOM   7707  H HD11 . LEU   A  1 524 ? 34.827 -7.141  -52.763 0.00 23.31  ? 550  LEU   A HD11 1 
ATOM   7708  H HD12 . LEU   A  1 524 ? 34.264 -6.426  -54.294 0.00 23.65  ? 550  LEU   A HD12 1 
ATOM   7709  H HD13 . LEU   A  1 524 ? 33.080 -6.934  -53.060 0.00 23.54  ? 550  LEU   A HD13 1 
ATOM   7710  H HD21 . LEU   A  1 524 ? 34.067 -9.247  -52.118 0.00 24.75  ? 550  LEU   A HD21 1 
ATOM   7711  H HD22 . LEU   A  1 524 ? 32.541 -9.604  -52.963 0.00 25.20  ? 550  LEU   A HD22 1 
ATOM   7712  H HD23 . LEU   A  1 524 ? 34.018 -10.515 -53.369 0.00 25.35  ? 550  LEU   A HD23 1 
ATOM   7713  N N    . THR   A  1 525 ? 31.960 -10.006 -58.358 1.00 23.79  ? 551  THR   A N    1 
ATOM   7714  C CA   . THR   A  1 525 ? 30.935 -9.891  -59.410 1.00 24.56  ? 551  THR   A CA   1 
ATOM   7715  C C    . THR   A  1 525 ? 29.819 -10.946 -59.311 1.00 24.89  ? 551  THR   A C    1 
ATOM   7716  O O    . THR   A  1 525 ? 28.771 -10.751 -59.908 1.00 25.00  ? 551  THR   A O    1 
ATOM   7717  C CB   . THR   A  1 525 ? 31.589 -9.875  -60.797 1.00 26.27  ? 551  THR   A CB   1 
ATOM   7718  O OG1  . THR   A  1 525 ? 32.262 -11.112 -61.007 1.00 27.06  ? 551  THR   A OG1  1 
ATOM   7719  C CG2  . THR   A  1 525 ? 32.553 -8.696  -60.973 1.00 27.16  ? 551  THR   A CG2  1 
ATOM   7720  H H    . THR   A  1 525 ? 32.865 -10.293 -58.719 0.00 28.57  ? 551  THR   A H    1 
ATOM   7721  H HA   . THR   A  1 525 ? 30.451 -8.923  -59.285 0.00 29.79  ? 551  THR   A HA   1 
ATOM   7722  H HB   . THR   A  1 525 ? 30.806 -9.774  -61.547 0.00 32.77  ? 551  THR   A HB   1 
ATOM   7723  H HG1  . THR   A  1 525 ? 33.115 -11.149 -60.500 0.00 33.29  ? 551  THR   A HG1  1 
ATOM   7724  H HG21 . THR   A  1 525 ? 32.794 -8.563  -62.026 0.00 33.43  ? 551  THR   A HG21 1 
ATOM   7725  H HG22 . THR   A  1 525 ? 32.097 -7.785  -60.588 0.00 32.86  ? 551  THR   A HG22 1 
ATOM   7726  H HG23 . THR   A  1 525 ? 33.475 -8.875  -60.423 0.00 32.82  ? 551  THR   A HG23 1 
ATOM   7727  N N    . GLU   A  1 526 ? 30.009 -12.026 -58.532 1.00 25.03  ? 552  GLU   A N    1 
ATOM   7728  C CA   . GLU   A  1 526 ? 28.947 -13.001 -58.264 1.00 25.53  ? 552  GLU   A CA   1 
ATOM   7729  C C    . GLU   A  1 526 ? 27.820 -12.385 -57.394 1.00 25.59  ? 552  GLU   A C    1 
ATOM   7730  O O    . GLU   A  1 526 ? 26.724 -12.936 -57.358 1.00 26.11  ? 552  GLU   A O    1 
ATOM   7731  C CB   . GLU   A  1 526 ? 29.499 -14.292 -57.605 1.00 26.75  ? 552  GLU   A CB   1 
ATOM   7732  C CG   . GLU   A  1 526 ? 29.971 -14.178 -56.155 1.00 26.95  ? 552  GLU   A CG   1 
ATOM   7733  C CD   . GLU   A  1 526 ? 31.406 -13.711 -55.990 1.00 28.46  ? 552  GLU   A CD   1 
ATOM   7734  O OE1  . GLU   A  1 526 ? 31.845 -12.854 -56.784 1.00 26.21  ? 552  GLU   A OE1  1 
ATOM   7735  O OE2  . GLU   A  1 526 ? 32.102 -14.208 -55.077 1.00 29.48  ? 552  GLU   A OE2  1 
ATOM   7736  H H    . GLU   A  1 526 ? 30.891 -12.273 -58.095 0.00 30.62  ? 552  GLU   A H    1 
ATOM   7737  H HA   . GLU   A  1 526 ? 28.502 -13.295 -59.214 0.00 32.31  ? 552  GLU   A HA   1 
ATOM   7738  H HB2  . GLU   A  1 526 ? 28.712 -15.045 -57.630 0.00 33.68  ? 552  GLU   A HB2  1 
ATOM   7739  H HB3  . GLU   A  1 526 ? 30.347 -14.638 -58.194 0.00 33.46  ? 552  GLU   A HB3  1 
ATOM   7740  H HG2  . GLU   A  1 526 ? 29.338 -13.495 -55.592 0.00 32.70  ? 552  GLU   A HG2  1 
ATOM   7741  H HG3  . GLU   A  1 526 ? 29.907 -15.167 -55.705 0.00 33.11  ? 552  GLU   A HG3  1 
ATOM   7742  N N    . LEU   A  1 527 ? 28.095 -11.270 -56.678 1.00 24.37  ? 553  LEU   A N    1 
ATOM   7743  C CA   . LEU   A  1 527 ? 27.120 -10.581 -55.853 1.00 23.51  ? 553  LEU   A CA   1 
ATOM   7744  C C    . LEU   A  1 527 ? 26.347 -9.570  -56.692 1.00 24.58  ? 553  LEU   A C    1 
ATOM   7745  O O    . LEU   A  1 527 ? 26.499 -8.364  -56.518 1.00 23.94  ? 553  LEU   A O    1 
ATOM   7746  C CB   . LEU   A  1 527 ? 27.818 -9.897  -54.650 1.00 22.45  ? 553  LEU   A CB   1 
ATOM   7747  C CG   . LEU   A  1 527 ? 28.525 -10.847 -53.678 1.00 22.37  ? 553  LEU   A CG   1 
ATOM   7748  C CD1  . LEU   A  1 527 ? 29.187 -10.076 -52.538 1.00 22.77  ? 553  LEU   A CD1  1 
ATOM   7749  C CD2  . LEU   A  1 527 ? 27.543 -11.867 -53.091 1.00 22.68  ? 553  LEU   A CD2  1 
ATOM   7750  H H    . LEU   A  1 527 ? 29.008 -10.829 -56.640 0.00 29.34  ? 553  LEU   A H    1 
ATOM   7751  H HA   . LEU   A  1 527 ? 26.393 -11.292 -55.463 0.00 28.58  ? 553  LEU   A HA   1 
ATOM   7752  H HB2  . LEU   A  1 527 ? 28.566 -9.200  -55.026 0.00 26.27  ? 553  LEU   A HB2  1 
ATOM   7753  H HB3  . LEU   A  1 527 ? 27.066 -9.351  -54.081 0.00 26.33  ? 553  LEU   A HB3  1 
ATOM   7754  H HG   . LEU   A  1 527 ? 29.301 -11.391 -54.213 0.00 26.26  ? 553  LEU   A HG   1 
ATOM   7755  H HD11 . LEU   A  1 527 ? 29.776 -10.765 -51.933 0.00 25.89  ? 553  LEU   A HD11 1 
ATOM   7756  H HD12 . LEU   A  1 527 ? 29.836 -9.309  -52.959 0.00 25.86  ? 553  LEU   A HD12 1 
ATOM   7757  H HD13 . LEU   A  1 527 ? 28.413 -9.615  -51.926 0.00 25.89  ? 553  LEU   A HD13 1 
ATOM   7758  H HD21 . LEU   A  1 527 ? 27.862 -12.135 -52.086 0.00 26.48  ? 553  LEU   A HD21 1 
ATOM   7759  H HD22 . LEU   A  1 527 ? 26.544 -11.433 -53.065 0.00 26.86  ? 553  LEU   A HD22 1 
ATOM   7760  H HD23 . LEU   A  1 527 ? 27.551 -12.750 -53.728 0.00 27.16  ? 553  LEU   A HD23 1 
ATOM   7761  N N    . SER   A  1 528 ? 25.443 -10.076 -57.543 1.00 25.75  ? 554  SER   A N    1 
ATOM   7762  C CA   . SER   A  1 528 ? 24.678 -9.251  -58.478 1.00 27.13  ? 554  SER   A CA   1 
ATOM   7763  C C    . SER   A  1 528 ? 23.762 -8.200  -57.819 1.00 26.46  ? 554  SER   A C    1 
ATOM   7764  O O    . SER   A  1 528 ? 23.550 -7.142  -58.407 1.00 26.93  ? 554  SER   A O    1 
ATOM   7765  C CB   . SER   A  1 528 ? 23.888 -10.129 -59.456 1.00 29.82  ? 554  SER   A CB   1 
ATOM   7766  O OG   . SER   A  1 528 ? 22.649 -10.584 -58.940 1.00 34.19  ? 554  SER   A OG   1 
ATOM   7767  H H    . SER   A  1 528 ? 25.217 -11.064 -57.591 0.00 32.21  ? 554  SER   A H    1 
ATOM   7768  H HA   . SER   A  1 528 ? 25.397 -8.696  -59.080 0.00 33.87  ? 554  SER   A HA   1 
ATOM   7769  H HB2  . SER   A  1 528 ? 23.683 -9.538  -60.348 0.00 38.19  ? 554  SER   A HB2  1 
ATOM   7770  H HB3  . SER   A  1 528 ? 24.492 -10.991 -59.735 0.00 38.03  ? 554  SER   A HB3  1 
ATOM   7771  H HG   . SER   A  1 528 ? 22.756 -10.882 -57.998 0.00 43.21  ? 554  SER   A HG   1 
ATOM   7772  N N    . ASP   A  1 529 ? 23.244 -8.468  -56.619 1.00 25.15  ? 555  ASP   A N    1 
ATOM   7773  C CA   . ASP   A  1 529 ? 22.375 -7.530  -55.915 1.00 24.28  ? 555  ASP   A CA   1 
ATOM   7774  C C    . ASP   A  1 529 ? 23.141 -6.601  -54.941 1.00 22.11  ? 555  ASP   A C    1 
ATOM   7775  O O    . ASP   A  1 529 ? 22.501 -5.911  -54.148 1.00 21.93  ? 555  ASP   A O    1 
ATOM   7776  C CB   . ASP   A  1 529 ? 21.318 -8.319  -55.117 1.00 26.79  ? 555  ASP   A CB   1 
ATOM   7777  C CG   . ASP   A  1 529 ? 20.338 -9.105  -55.961 1.00 34.60  ? 555  ASP   A CG   1 
ATOM   7778  O OD1  . ASP   A  1 529 ? 20.244 -8.828  -57.179 1.00 35.13  ? 555  ASP   A OD1  1 
ATOM   7779  O OD2  . ASP   A  1 529 ? 19.636 -9.973  -55.396 1.00 38.28  ? 555  ASP   A OD2  1 
ATOM   7780  H H    . ASP   A  1 529 ? 23.402 -9.330  -56.107 0.00 31.12  ? 555  ASP   A H    1 
ATOM   7781  H HA   . ASP   A  1 529 ? 21.849 -6.892  -56.624 0.00 30.31  ? 555  ASP   A HA   1 
ATOM   7782  H HB2  . ASP   A  1 529 ? 21.815 -9.011  -54.438 0.00 32.95  ? 555  ASP   A HB2  1 
ATOM   7783  H HB3  . ASP   A  1 529 ? 20.719 -7.614  -54.544 0.00 33.13  ? 555  ASP   A HB3  1 
ATOM   7784  N N    . LEU   A  1 530 ? 24.481 -6.571  -54.990 1.00 21.04  ? 556  LEU   A N    1 
ATOM   7785  C CA   . LEU   A  1 530 ? 25.256 -5.754  -54.050 1.00 20.39  ? 556  LEU   A CA   1 
ATOM   7786  C C    . LEU   A  1 530 ? 24.897 -4.259  -54.168 1.00 21.17  ? 556  LEU   A C    1 
ATOM   7787  O O    . LEU   A  1 530 ? 24.905 -3.711  -55.279 1.00 21.75  ? 556  LEU   A O    1 
ATOM   7788  C CB   . LEU   A  1 530 ? 26.756 -5.951  -54.300 1.00 19.79  ? 556  LEU   A CB   1 
ATOM   7789  C CG   . LEU   A  1 530 ? 27.717 -5.472  -53.189 1.00 20.61  ? 556  LEU   A CG   1 
ATOM   7790  C CD1  . LEU   A  1 530 ? 27.423 -6.165  -51.867 1.00 20.64  ? 556  LEU   A CD1  1 
ATOM   7791  C CD2  . LEU   A  1 530 ? 29.146 -5.730  -53.610 1.00 20.40  ? 556  LEU   A CD2  1 
ATOM   7792  H H    . LEU   A  1 530 ? 25.050 -7.066  -55.668 0.00 25.22  ? 556  LEU   A H    1 
ATOM   7793  H HA   . LEU   A  1 530 ? 25.005 -6.096  -53.047 0.00 23.53  ? 556  LEU   A HA   1 
ATOM   7794  H HB2  . LEU   A  1 530 ? 26.946 -7.015  -54.435 0.00 22.87  ? 556  LEU   A HB2  1 
ATOM   7795  H HB3  . LEU   A  1 530 ? 27.024 -5.421  -55.213 0.00 22.87  ? 556  LEU   A HB3  1 
ATOM   7796  H HG   . LEU   A  1 530 ? 27.595 -4.400  -53.044 0.00 22.99  ? 556  LEU   A HG   1 
ATOM   7797  H HD11 . LEU   A  1 530 ? 28.285 -6.062  -51.210 0.00 22.60  ? 556  LEU   A HD11 1 
ATOM   7798  H HD12 . LEU   A  1 530 ? 26.562 -5.692  -51.398 0.00 22.96  ? 556  LEU   A HD12 1 
ATOM   7799  H HD13 . LEU   A  1 530 ? 27.217 -7.217  -52.053 0.00 23.20  ? 556  LEU   A HD13 1 
ATOM   7800  H HD21 . LEU   A  1 530 ? 29.820 -5.483  -52.793 0.00 22.36  ? 556  LEU   A HD21 1 
ATOM   7801  H HD22 . LEU   A  1 530 ? 29.252 -6.782  -53.870 0.00 22.94  ? 556  LEU   A HD22 1 
ATOM   7802  H HD23 . LEU   A  1 530 ? 29.374 -5.112  -54.477 0.00 22.87  ? 556  LEU   A HD23 1 
ATOM   7803  N N    . GLU   A  1 531 ? 24.583 -3.619  -53.028 1.00 20.19  ? 557  GLU   A N    1 
ATOM   7804  C CA   . GLU   A  1 531 ? 24.202 -2.203  -52.935 1.00 20.30  ? 557  GLU   A CA   1 
ATOM   7805  C C    . GLU   A  1 531 ? 25.243 -1.386  -52.150 1.00 19.67  ? 557  GLU   A C    1 
ATOM   7806  O O    . GLU   A  1 531 ? 25.453 -0.215  -52.452 1.00 19.57  ? 557  GLU   A O    1 
ATOM   7807  C CB   . GLU   A  1 531 ? 22.826 -2.046  -52.273 1.00 22.15  ? 557  GLU   A CB   1 
ATOM   7808  C CG   . GLU   A  1 531 ? 21.711 -2.727  -53.062 1.00 26.92  ? 557  GLU   A CG   1 
ATOM   7809  C CD   . GLU   A  1 531 ? 20.292 -2.216  -52.878 1.00 32.48  ? 557  GLU   A CD   1 
ATOM   7810  O OE1  . GLU   A  1 531 ? 20.086 -1.223  -52.141 1.00 32.11  ? 557  GLU   A OE1  1 
ATOM   7811  O OE2  . GLU   A  1 531 ? 19.380 -2.809  -53.499 1.00 35.18  ? 557  GLU   A OE2  1 
ATOM   7812  H H    . GLU   A  1 531 ? 24.569 -4.077  -52.123 0.00 22.93  ? 557  GLU   A H    1 
ATOM   7813  H HA   . GLU   A  1 531 ? 24.100 -1.766  -53.926 0.00 23.53  ? 557  GLU   A HA   1 
ATOM   7814  H HB2  . GLU   A  1 531 ? 22.857 -2.490  -51.279 0.00 25.41  ? 557  GLU   A HB2  1 
ATOM   7815  H HB3  . GLU   A  1 531 ? 22.606 -0.982  -52.200 0.00 25.66  ? 557  GLU   A HB3  1 
ATOM   7816  H HG2  . GLU   A  1 531 ? 21.940 -2.639  -54.123 0.00 32.21  ? 557  GLU   A HG2  1 
ATOM   7817  H HG3  . GLU   A  1 531 ? 21.705 -3.781  -52.788 0.00 31.98  ? 557  GLU   A HG3  1 
ATOM   7818  N N    . VAL   A  1 532 ? 25.850 -1.979  -51.117 1.00 18.80  ? 558  VAL   A N    1 
ATOM   7819  C CA   . VAL   A  1 532 ? 26.831 -1.284  -50.295 1.00 19.01  ? 558  VAL   A CA   1 
ATOM   7820  C C    . VAL   A  1 532 ? 28.040 -2.182  -50.156 1.00 18.92  ? 558  VAL   A C    1 
ATOM   7821  O O    . VAL   A  1 532 ? 27.895 -3.347  -49.779 1.00 18.84  ? 558  VAL   A O    1 
ATOM   7822  C CB   . VAL   A  1 532 ? 26.256 -0.929  -48.907 1.00 19.77  ? 558  VAL   A CB   1 
ATOM   7823  C CG1  . VAL   A  1 532 ? 27.315 -0.226  -48.040 1.00 20.79  ? 558  VAL   A CG1  1 
ATOM   7824  C CG2  . VAL   A  1 532 ? 24.980 -0.086  -49.024 1.00 19.98  ? 558  VAL   A CG2  1 
ATOM   7825  H H    . VAL   A  1 532 ? 25.673 -2.930  -50.810 0.00 20.55  ? 558  VAL   A H    1 
ATOM   7826  H HA   . VAL   A  1 532 ? 27.145 -0.357  -50.772 0.00 20.31  ? 558  VAL   A HA   1 
ATOM   7827  H HB   . VAL   A  1 532 ? 25.986 -1.855  -48.401 0.00 21.00  ? 558  VAL   A HB   1 
ATOM   7828  H HG11 . VAL   A  1 532 ? 26.818 0.293   -47.222 0.00 21.72  ? 558  VAL   A HG11 1 
ATOM   7829  H HG12 . VAL   A  1 532 ? 27.995 -0.969  -47.626 0.00 21.59  ? 558  VAL   A HG12 1 
ATOM   7830  H HG13 . VAL   A  1 532 ? 27.866 0.485   -48.654 0.00 21.79  ? 558  VAL   A HG13 1 
ATOM   7831  H HG21 . VAL   A  1 532 ? 24.630 0.168   -48.024 0.00 21.44  ? 558  VAL   A HG21 1 
ATOM   7832  H HG22 . VAL   A  1 532 ? 25.195 0.821   -49.586 0.00 21.64  ? 558  VAL   A HG22 1 
ATOM   7833  H HG23 . VAL   A  1 532 ? 24.211 -0.664  -49.536 0.00 21.90  ? 558  VAL   A HG23 1 
ATOM   7834  N N    . LEU   A  1 533 ? 29.228 -1.646  -50.469 1.00 18.58  ? 559  LEU   A N    1 
ATOM   7835  C CA   . LEU   A  1 533 ? 30.475 -2.381  -50.361 1.00 18.32  ? 559  LEU   A CA   1 
ATOM   7836  C C    . LEU   A  1 533 ? 31.472 -1.527  -49.588 1.00 18.26  ? 559  LEU   A C    1 
ATOM   7837  O O    . LEU   A  1 533 ? 31.785 -0.406  -50.019 1.00 18.73  ? 559  LEU   A O    1 
ATOM   7838  C CB   . LEU   A  1 533 ? 31.012 -2.687  -51.762 1.00 18.39  ? 559  LEU   A CB   1 
ATOM   7839  C CG   . LEU   A  1 533 ? 32.347 -3.438  -51.842 1.00 19.53  ? 559  LEU   A CG   1 
ATOM   7840  C CD1  . LEU   A  1 533 ? 32.331 -4.734  -51.012 1.00 20.17  ? 559  LEU   A CD1  1 
ATOM   7841  C CD2  . LEU   A  1 533 ? 32.737 -3.720  -53.302 1.00 19.81  ? 559  LEU   A CD2  1 
ATOM   7842  H H    . LEU   A  1 533 ? 29.361 -0.695  -50.798 0.00 19.36  ? 559  LEU   A H    1 
ATOM   7843  H HA   . LEU   A  1 533 ? 30.321 -3.315  -49.825 0.00 18.83  ? 559  LEU   A HA   1 
ATOM   7844  H HB2  . LEU   A  1 533 ? 30.266 -3.278  -52.291 0.00 19.50  ? 559  LEU   A HB2  1 
ATOM   7845  H HB3  . LEU   A  1 533 ? 31.148 -1.742  -52.285 0.00 19.24  ? 559  LEU   A HB3  1 
ATOM   7846  H HG   . LEU   A  1 533 ? 33.115 -2.791  -51.426 0.00 20.20  ? 559  LEU   A HG   1 
ATOM   7847  H HD11 . LEU   A  1 533 ? 33.154 -5.371  -51.330 0.00 21.21  ? 559  LEU   A HD11 1 
ATOM   7848  H HD12 . LEU   A  1 533 ? 32.460 -4.473  -49.962 0.00 20.88  ? 559  LEU   A HD12 1 
ATOM   7849  H HD13 . LEU   A  1 533 ? 31.381 -5.248  -51.143 0.00 21.39  ? 559  LEU   A HD13 1 
ATOM   7850  H HD21 . LEU   A  1 533 ? 33.710 -4.208  -53.324 0.00 21.07  ? 559  LEU   A HD21 1 
ATOM   7851  H HD22 . LEU   A  1 533 ? 31.985 -4.371  -53.746 0.00 21.43  ? 559  LEU   A HD22 1 
ATOM   7852  H HD23 . LEU   A  1 533 ? 32.781 -2.780  -53.849 0.00 21.19  ? 559  LEU   A HD23 1 
ATOM   7853  N N    . ASP   A  1 534 ? 31.990 -2.059  -48.463 1.00 17.27  ? 560  ASP   A N    1 
ATOM   7854  C CA   . ASP   A  1 534 ? 32.970 -1.339  -47.647 1.00 17.40  ? 560  ASP   A CA   1 
ATOM   7855  C C    . ASP   A  1 534 ? 34.335 -2.050  -47.721 1.00 17.25  ? 560  ASP   A C    1 
ATOM   7856  O O    . ASP   A  1 534 ? 34.497 -3.140  -47.183 1.00 17.04  ? 560  ASP   A O    1 
ATOM   7857  C CB   . ASP   A  1 534 ? 32.472 -1.192  -46.187 1.00 18.25  ? 560  ASP   A CB   1 
ATOM   7858  C CG   . ASP   A  1 534 ? 33.126 -0.046  -45.418 1.00 21.37  ? 560  ASP   A CG   1 
ATOM   7859  O OD1  . ASP   A  1 534 ? 34.184 0.468   -45.884 1.00 20.61  ? 560  ASP   A OD1  1 
ATOM   7860  O OD2  . ASP   A  1 534 ? 32.608 0.319   -44.337 1.00 21.56  ? 560  ASP   A OD2  1 
ATOM   7861  H H    . ASP   A  1 534 ? 31.759 -2.976  -48.098 0.00 16.96  ? 560  ASP   A H    1 
ATOM   7862  H HA   . ASP   A  1 534 ? 33.097 -0.335  -48.049 0.00 16.78  ? 560  ASP   A HA   1 
ATOM   7863  H HB2  . ASP   A  1 534 ? 31.399 -1.009  -46.204 0.00 17.71  ? 560  ASP   A HB2  1 
ATOM   7864  H HB3  . ASP   A  1 534 ? 32.679 -2.108  -45.637 0.00 17.51  ? 560  ASP   A HB3  1 
ATOM   7865  N N    . LEU   A  1 535 ? 35.301 -1.441  -48.446 1.00 17.33  ? 561  LEU   A N    1 
ATOM   7866  C CA   . LEU   A  1 535 ? 36.671 -1.970  -48.584 1.00 17.81  ? 561  LEU   A CA   1 
ATOM   7867  C C    . LEU   A  1 535 ? 37.694 -1.122  -47.806 1.00 17.62  ? 561  LEU   A C    1 
ATOM   7868  O O    . LEU   A  1 535 ? 38.892 -1.188  -48.108 1.00 18.15  ? 561  LEU   A O    1 
ATOM   7869  C CB   . LEU   A  1 535 ? 37.076 -2.000  -50.071 1.00 18.63  ? 561  LEU   A CB   1 
ATOM   7870  C CG   . LEU   A  1 535 ? 36.122 -2.714  -51.019 1.00 20.71  ? 561  LEU   A CG   1 
ATOM   7871  C CD1  . LEU   A  1 535 ? 36.642 -2.672  -52.453 1.00 21.10  ? 561  LEU   A CD1  1 
ATOM   7872  C CD2  . LEU   A  1 535 ? 35.895 -4.186  -50.583 1.00 21.35  ? 561  LEU   A CD2  1 
ATOM   7873  H H    . LEU   A  1 535 ? 35.164 -0.575  -48.957 0.00 16.67  ? 561  LEU   A H    1 
ATOM   7874  H HA   . LEU   A  1 535 ? 36.732 -2.986  -48.196 0.00 17.16  ? 561  LEU   A HA   1 
ATOM   7875  H HB2  . LEU   A  1 535 ? 37.176 -0.973  -50.420 0.00 18.39  ? 561  LEU   A HB2  1 
ATOM   7876  H HB3  . LEU   A  1 535 ? 38.035 -2.508  -50.158 0.00 18.41  ? 561  LEU   A HB3  1 
ATOM   7877  H HG   . LEU   A  1 535 ? 35.180 -2.174  -50.993 0.00 21.25  ? 561  LEU   A HG   1 
ATOM   7878  H HD11 . LEU   A  1 535 ? 35.916 -3.152  -53.108 0.00 22.23  ? 561  LEU   A HD11 1 
ATOM   7879  H HD12 . LEU   A  1 535 ? 36.779 -1.632  -52.747 0.00 21.95  ? 561  LEU   A HD12 1 
ATOM   7880  H HD13 . LEU   A  1 535 ? 37.593 -3.200  -52.500 0.00 21.98  ? 561  LEU   A HD13 1 
ATOM   7881  H HD21 . LEU   A  1 535 ? 35.394 -4.719  -51.389 0.00 22.34  ? 561  LEU   A HD21 1 
ATOM   7882  H HD22 . LEU   A  1 535 ? 36.860 -4.646  -50.374 0.00 22.00  ? 561  LEU   A HD22 1 
ATOM   7883  H HD23 . LEU   A  1 535 ? 35.274 -4.201  -49.689 0.00 21.91  ? 561  LEU   A HD23 1 
ATOM   7884  N N    . SER   A  1 536 ? 37.234 -0.315  -46.822 1.00 17.01  ? 562  SER   A N    1 
ATOM   7885  C CA   . SER   A  1 536 ? 38.109 0.555   -46.030 1.00 17.05  ? 562  SER   A CA   1 
ATOM   7886  C C    . SER   A  1 536 ? 39.229 -0.222  -45.359 1.00 16.86  ? 562  SER   A C    1 
ATOM   7887  O O    . SER   A  1 536 ? 39.021 -1.371  -44.966 1.00 16.05  ? 562  SER   A O    1 
ATOM   7888  C CB   . SER   A  1 536 ? 37.320 1.248   -44.923 1.00 18.34  ? 562  SER   A CB   1 
ATOM   7889  O OG   . SER   A  1 536 ? 36.316 2.110   -45.424 1.00 20.30  ? 562  SER   A OG   1 
ATOM   7890  H H    . SER   A  1 536 ? 36.260 -0.247  -46.543 0.00 15.76  ? 562  SER   A H    1 
ATOM   7891  H HA   . SER   A  1 536 ? 38.543 1.317   -46.676 0.00 15.67  ? 562  SER   A HA   1 
ATOM   7892  H HB2  . SER   A  1 536 ? 36.849 0.488   -44.301 0.00 16.97  ? 562  SER   A HB2  1 
ATOM   7893  H HB3  . SER   A  1 536 ? 38.010 1.835   -44.321 0.00 16.91  ? 562  SER   A HB3  1 
ATOM   7894  H HG   . SER   A  1 536 ? 35.581 1.581   -45.833 0.00 19.59  ? 562  SER   A HG   1 
ATOM   7895  N N    . TYR   A  1 537 ? 40.406 0.414   -45.202 1.00 16.51  ? 563  TYR   A N    1 
ATOM   7896  C CA   . TYR   A  1 537 ? 41.529 -0.190  -44.491 1.00 17.13  ? 563  TYR   A CA   1 
ATOM   7897  C C    . TYR   A  1 537 ? 41.983 -1.556  -45.040 1.00 16.42  ? 563  TYR   A C    1 
ATOM   7898  O O    . TYR   A  1 537 ? 42.111 -2.524  -44.296 1.00 16.55  ? 563  TYR   A O    1 
ATOM   7899  C CB   . TYR   A  1 537 ? 41.197 -0.283  -42.990 1.00 19.18  ? 563  TYR   A CB   1 
ATOM   7900  C CG   . TYR   A  1 537 ? 40.968 1.071   -42.362 1.00 22.35  ? 563  TYR   A CG   1 
ATOM   7901  C CD1  . TYR   A  1 537 ? 42.033 1.849   -41.934 1.00 24.44  ? 563  TYR   A CD1  1 
ATOM   7902  C CD2  . TYR   A  1 537 ? 39.686 1.554   -42.152 1.00 24.79  ? 563  TYR   A CD2  1 
ATOM   7903  C CE1  . TYR   A  1 537 ? 41.826 3.077   -41.312 1.00 26.19  ? 563  TYR   A CE1  1 
ATOM   7904  C CE2  . TYR   A  1 537 ? 39.468 2.790   -41.558 1.00 26.31  ? 563  TYR   A CE2  1 
ATOM   7905  C CZ   . TYR   A  1 537 ? 40.541 3.545   -41.129 1.00 27.97  ? 563  TYR   A CZ   1 
ATOM   7906  O OH   . TYR   A  1 537 ? 40.344 4.761   -40.515 1.00 31.89  ? 563  TYR   A OH   1 
ATOM   7907  H H    . TYR   A  1 537 ? 40.602 1.347   -45.551 0.00 14.85  ? 563  TYR   A H    1 
ATOM   7908  H HA   . TYR   A  1 537 ? 42.378 0.486   -44.586 0.00 15.54  ? 563  TYR   A HA   1 
ATOM   7909  H HB2  . TYR   A  1 537 ? 40.297 -0.873  -42.835 0.00 17.80  ? 563  TYR   A HB2  1 
ATOM   7910  H HB3  . TYR   A  1 537 ? 42.035 -0.739  -42.465 0.00 17.81  ? 563  TYR   A HB3  1 
ATOM   7911  H HD1  . TYR   A  1 537 ? 43.037 1.485   -42.064 0.00 24.05  ? 563  TYR   A HD1  1 
ATOM   7912  H HD2  . TYR   A  1 537 ? 38.843 0.968   -42.479 0.00 24.42  ? 563  TYR   A HD2  1 
ATOM   7913  H HE1  . TYR   A  1 537 ? 42.666 3.669   -40.989 0.00 26.06  ? 563  TYR   A HE1  1 
ATOM   7914  H HE2  . TYR   A  1 537 ? 38.460 3.138   -41.410 0.00 26.16  ? 563  TYR   A HE2  1 
ATOM   7915  H HH   . TYR   A  1 537 ? 39.377 4.975   -40.453 0.00 32.84  ? 563  TYR   A HH   1 
ATOM   7916  N N    . ASN   A  1 538 ? 42.237 -1.616  -46.358 1.00 14.90  ? 564  ASN   A N    1 
ATOM   7917  C CA   . ASN   A  1 538 ? 42.830 -2.778  -47.025 1.00 15.39  ? 564  ASN   A CA   1 
ATOM   7918  C C    . ASN   A  1 538 ? 44.050 -2.254  -47.820 1.00 16.21  ? 564  ASN   A C    1 
ATOM   7919  O O    . ASN   A  1 538 ? 44.213 -2.568  -48.992 1.00 17.10  ? 564  ASN   A O    1 
ATOM   7920  C CB   . ASN   A  1 538 ? 41.820 -3.444  -47.959 1.00 15.53  ? 564  ASN   A CB   1 
ATOM   7921  C CG   . ASN   A  1 538 ? 40.890 -4.374  -47.221 1.00 17.12  ? 564  ASN   A CG   1 
ATOM   7922  O OD1  . ASN   A  1 538 ? 41.299 -5.456  -46.828 1.00 17.04  ? 564  ASN   A OD1  1 
ATOM   7923  N ND2  . ASN   A  1 538 ? 39.645 -3.986  -47.020 1.00 17.23  ? 564  ASN   A ND2  1 
ATOM   7924  H H    . ASN   A  1 538 ? 42.038 -0.852  -46.996 0.00 13.24  ? 564  ASN   A H    1 
ATOM   7925  H HA   . ASN   A  1 538 ? 43.198 -3.506  -46.303 0.00 14.00  ? 564  ASN   A HA   1 
ATOM   7926  H HB2  . ASN   A  1 538 ? 41.236 -2.676  -48.464 0.00 14.35  ? 564  ASN   A HB2  1 
ATOM   7927  H HB3  . ASN   A  1 538 ? 42.338 -4.059  -48.693 0.00 14.57  ? 564  ASN   A HB3  1 
ATOM   7928  H HD21 . ASN   A  1 538 ? 39.004 -4.597  -46.523 0.00 16.26  ? 564  ASN   A HD21 1 
ATOM   7929  H HD22 . ASN   A  1 538 ? 39.324 -3.081  -47.348 0.00 16.23  ? 564  ASN   A HD22 1 
ATOM   7930  N N    . SER   A  1 539 ? 44.864 -1.412  -47.185 1.00 16.00  ? 565  SER   A N    1 
ATOM   7931  C CA   . SER   A  1 539 ? 46.003 -0.784  -47.847 1.00 17.33  ? 565  SER   A CA   1 
ATOM   7932  C C    . SER   A  1 539 ? 47.184 -1.717  -48.133 1.00 18.07  ? 565  SER   A C    1 
ATOM   7933  O O    . SER   A  1 539 ? 48.023 -1.363  -48.968 1.00 18.85  ? 565  SER   A O    1 
ATOM   7934  C CB   . SER   A  1 539 ? 46.515 0.362   -46.981 1.00 18.47  ? 565  SER   A CB   1 
ATOM   7935  O OG   . SER   A  1 539 ? 47.085 -0.185  -45.803 1.00 20.77  ? 565  SER   A OG   1 
ATOM   7936  H H    . SER   A  1 539 ? 44.774 -1.167  -46.204 0.00 14.62  ? 565  SER   A H    1 
ATOM   7937  H HA   . SER   A  1 539 ? 45.675 -0.360  -48.794 0.00 16.61  ? 565  SER   A HA   1 
ATOM   7938  H HB2  . SER   A  1 539 ? 47.297 0.883   -47.529 0.00 17.88  ? 565  SER   A HB2  1 
ATOM   7939  H HB3  . SER   A  1 539 ? 45.698 1.035   -46.726 0.00 17.60  ? 565  SER   A HB3  1 
ATOM   7940  H HG   . SER   A  1 539 ? 46.370 -0.409  -45.151 0.00 20.30  ? 565  SER   A HG   1 
ATOM   7941  N N    . HIS   A  1 540 ? 47.279 -2.876  -47.450 1.00 17.37  ? 566  HIS   A N    1 
ATOM   7942  C CA   . HIS   A  1 540 ? 48.435 -3.789  -47.551 1.00 18.20  ? 566  HIS   A CA   1 
ATOM   7943  C C    . HIS   A  1 540 ? 49.100 -3.877  -48.940 1.00 18.69  ? 566  HIS   A C    1 
ATOM   7944  O O    . HIS   A  1 540 ? 50.302 -3.613  -49.061 1.00 18.94  ? 566  HIS   A O    1 
ATOM   7945  C CB   . HIS   A  1 540 ? 48.074 -5.204  -47.076 1.00 18.98  ? 566  HIS   A CB   1 
ATOM   7946  C CG   . HIS   A  1 540 ? 49.266 -6.092  -46.912 1.00 20.98  ? 566  HIS   A CG   1 
ATOM   7947  N ND1  . HIS   A  1 540 ? 49.716 -6.468  -45.655 1.00 22.83  ? 566  HIS   A ND1  1 
ATOM   7948  C CD2  . HIS   A  1 540 ? 50.091 -6.619  -47.845 1.00 21.98  ? 566  HIS   A CD2  1 
ATOM   7949  C CE1  . HIS   A  1 540 ? 50.788 -7.215  -45.864 1.00 23.36  ? 566  HIS   A CE1  1 
ATOM   7950  N NE2  . HIS   A  1 540 ? 51.062 -7.320  -47.167 1.00 23.64  ? 566  HIS   A NE2  1 
ATOM   7951  H H    . HIS   A  1 540 ? 46.569 -3.216  -46.809 0.00 16.70  ? 566  HIS   A H    1 
ATOM   7952  H HA   . HIS   A  1 540 ? 49.187 -3.421  -46.854 0.00 18.06  ? 566  HIS   A HA   1 
ATOM   7953  H HB2  . HIS   A  1 540 ? 47.579 -5.145  -46.107 0.00 18.90  ? 566  HIS   A HB2  1 
ATOM   7954  H HB3  . HIS   A  1 540 ? 47.409 -5.664  -47.805 0.00 19.19  ? 566  HIS   A HB3  1 
ATOM   7955  H HD2  . HIS   A  1 540 ? 50.006 -6.510  -48.913 0.00 23.49  ? 566  HIS   A HD2  1 
ATOM   7956  H HE1  . HIS   A  1 540 ? 51.366 -7.680  -45.082 0.00 25.11  ? 566  HIS   A HE1  1 
ATOM   7957  H HE2  . HIS   A  1 540 ? 51.840 -7.824  -47.580 0.00 25.88  ? 566  HIS   A HE2  1 
ATOM   7958  N N    . TYR   A  1 541 ? 48.331 -4.227  -49.976 1.00 18.01  ? 567  TYR   A N    1 
ATOM   7959  C CA   . TYR   A  1 541 ? 48.897 -4.405  -51.311 1.00 17.90  ? 567  TYR   A CA   1 
ATOM   7960  C C    . TYR   A  1 541 ? 48.857 -3.140  -52.156 1.00 17.60  ? 567  TYR   A C    1 
ATOM   7961  O O    . TYR   A  1 541 ? 49.755 -2.940  -52.972 1.00 17.78  ? 567  TYR   A O    1 
ATOM   7962  C CB   . TYR   A  1 541 ? 48.233 -5.592  -52.031 1.00 17.71  ? 567  TYR   A CB   1 
ATOM   7963  C CG   . TYR   A  1 541 ? 48.693 -6.913  -51.469 1.00 18.47  ? 567  TYR   A CG   1 
ATOM   7964  C CD1  . TYR   A  1 541 ? 49.958 -7.407  -51.762 1.00 19.57  ? 567  TYR   A CD1  1 
ATOM   7965  C CD2  . TYR   A  1 541 ? 47.942 -7.581  -50.508 1.00 19.02  ? 567  TYR   A CD2  1 
ATOM   7966  C CE1  . TYR   A  1 541 ? 50.433 -8.571  -51.171 1.00 20.68  ? 567  TYR   A CE1  1 
ATOM   7967  C CE2  . TYR   A  1 541 ? 48.389 -8.771  -49.941 1.00 20.28  ? 567  TYR   A CE2  1 
ATOM   7968  C CZ   . TYR   A  1 541 ? 49.630 -9.273  -50.288 1.00 21.60  ? 567  TYR   A CZ   1 
ATOM   7969  O OH   . TYR   A  1 541 ? 50.093 -10.410 -49.655 1.00 23.00  ? 567  TYR   A OH   1 
ATOM   7970  H H    . TYR   A  1 541 ? 47.332 -4.394  -49.919 0.00 18.18  ? 567  TYR   A H    1 
ATOM   7971  H HA   . TYR   A  1 541 ? 49.953 -4.643  -51.183 0.00 18.66  ? 567  TYR   A HA   1 
ATOM   7972  H HB2  . TYR   A  1 541 ? 47.150 -5.530  -51.924 0.00 18.35  ? 567  TYR   A HB2  1 
ATOM   7973  H HB3  . TYR   A  1 541 ? 48.502 -5.564  -53.086 0.00 18.75  ? 567  TYR   A HB3  1 
ATOM   7974  H HD1  . TYR   A  1 541 ? 50.582 -6.879  -52.461 0.00 21.39  ? 567  TYR   A HD1  1 
ATOM   7975  H HD2  . TYR   A  1 541 ? 46.964 -7.214  -50.250 0.00 19.87  ? 567  TYR   A HD2  1 
ATOM   7976  H HE1  . TYR   A  1 541 ? 51.404 -8.949  -51.444 0.00 23.10  ? 567  TYR   A HE1  1 
ATOM   7977  H HE2  . TYR   A  1 541 ? 47.777 -9.292  -49.222 0.00 21.72  ? 567  TYR   A HE2  1 
ATOM   7978  H HH   . TYR   A  1 541 ? 51.043 -10.581 -49.889 0.00 25.93  ? 567  TYR   A HH   1 
ATOM   7979  N N    . PHE   A  1 542 ? 47.872 -2.250  -51.934 1.00 17.35  ? 568  PHE   A N    1 
ATOM   7980  C CA   . PHE   A  1 542 ? 47.841 -0.971  -52.666 1.00 17.88  ? 568  PHE   A CA   1 
ATOM   7981  C C    . PHE   A  1 542 ? 49.113 -0.145  -52.413 1.00 18.55  ? 568  PHE   A C    1 
ATOM   7982  O O    . PHE   A  1 542 ? 49.533 0.602   -53.307 1.00 18.98  ? 568  PHE   A O    1 
ATOM   7983  C CB   . PHE   A  1 542 ? 46.632 -0.120  -52.256 1.00 17.43  ? 568  PHE   A CB   1 
ATOM   7984  C CG   . PHE   A  1 542 ? 45.303 -0.556  -52.823 1.00 17.88  ? 568  PHE   A CG   1 
ATOM   7985  C CD1  . PHE   A  1 542 ? 45.098 -0.604  -54.193 1.00 18.83  ? 568  PHE   A CD1  1 
ATOM   7986  C CD2  . PHE   A  1 542 ? 44.248 -0.886  -51.986 1.00 18.76  ? 568  PHE   A CD2  1 
ATOM   7987  C CE1  . PHE   A  1 542 ? 43.865 -0.978  -54.713 1.00 19.75  ? 568  PHE   A CE1  1 
ATOM   7988  C CE2  . PHE   A  1 542 ? 43.014 -1.248  -52.509 1.00 19.47  ? 568  PHE   A CE2  1 
ATOM   7989  C CZ   . PHE   A  1 542 ? 42.836 -1.307  -53.866 1.00 19.11  ? 568  PHE   A CZ   1 
ATOM   7990  H H    . PHE   A  1 542 ? 47.097 -2.381  -51.291 0.00 17.38  ? 568  PHE   A H    1 
ATOM   7991  H HA   . PHE   A  1 542 ? 47.783 -1.176  -53.734 0.00 18.47  ? 568  PHE   A HA   1 
ATOM   7992  H HB2  . PHE   A  1 542 ? 46.556 -0.119  -51.169 0.00 17.21  ? 568  PHE   A HB2  1 
ATOM   7993  H HB3  . PHE   A  1 542 ? 46.808 0.898   -52.601 0.00 17.46  ? 568  PHE   A HB3  1 
ATOM   7994  H HD1  . PHE   A  1 542 ? 45.902 -0.348  -54.862 0.00 19.63  ? 568  PHE   A HD1  1 
ATOM   7995  H HD2  . PHE   A  1 542 ? 44.374 -0.841  -50.917 0.00 18.64  ? 568  PHE   A HD2  1 
ATOM   7996  H HE1  . PHE   A  1 542 ? 43.723 -1.026  -55.779 0.00 20.90  ? 568  PHE   A HE1  1 
ATOM   7997  H HE2  . PHE   A  1 542 ? 42.205 -1.515  -51.849 0.00 19.65  ? 568  PHE   A HE2  1 
ATOM   7998  H HZ   . PHE   A  1 542 ? 41.886 -1.612  -54.267 0.00 19.77  ? 568  PHE   A HZ   1 
ATOM   7999  N N    . ARG   A  1 543 ? 49.715 -0.266  -51.197 1.00 18.47  ? 569  ARG   A N    1 
ATOM   8000  C CA   . ARG   A  1 543 ? 50.947 0.452   -50.819 1.00 19.93  ? 569  ARG   A CA   1 
ATOM   8001  C C    . ARG   A  1 543 ? 52.179 0.050   -51.624 1.00 20.25  ? 569  ARG   A C    1 
ATOM   8002  O O    . ARG   A  1 543 ? 53.160 0.802   -51.659 1.00 20.88  ? 569  ARG   A O    1 
ATOM   8003  C CB   . ARG   A  1 543 ? 51.286 0.193   -49.337 1.00 22.14  ? 569  ARG   A CB   1 
ATOM   8004  C CG   . ARG   A  1 543 ? 50.324 0.809   -48.362 1.00 28.13  ? 569  ARG   A CG   1 
ATOM   8005  C CD   . ARG   A  1 543 ? 50.699 0.429   -46.940 1.00 32.29  ? 569  ARG   A CD   1 
ATOM   8006  N NE   . ARG   A  1 543 ? 49.744 0.950   -45.957 1.00 37.63  ? 569  ARG   A NE   1 
ATOM   8007  C CZ   . ARG   A  1 543 ? 49.718 2.200   -45.495 1.00 41.47  ? 569  ARG   A CZ   1 
ATOM   8008  N NH1  . ARG   A  1 543 ? 48.812 2.561   -44.593 1.00 42.31  ? 569  ARG   A NH1  1 
ATOM   8009  N NH2  . ARG   A  1 543 ? 50.593 3.102   -45.938 1.00 41.82  ? 569  ARG   A NH2  1 
ATOM   8010  H H    . ARG   A  1 543 ? 49.356 -0.848  -50.447 0.00 18.70  ? 569  ARG   A H    1 
ATOM   8011  H HA   . ARG   A  1 543 ? 50.791 1.522   -50.950 0.00 20.61  ? 569  ARG   A HA   1 
ATOM   8012  H HB2  . ARG   A  1 543 ? 51.301 -0.881  -49.159 0.00 23.20  ? 569  ARG   A HB2  1 
ATOM   8013  H HB3  . ARG   A  1 543 ? 52.270 0.609   -49.128 0.00 23.26  ? 569  ARG   A HB3  1 
ATOM   8014  H HG2  . ARG   A  1 543 ? 50.359 1.892   -48.442 0.00 29.98  ? 569  ARG   A HG2  1 
ATOM   8015  H HG3  . ARG   A  1 543 ? 49.320 0.440   -48.568 0.00 29.91  ? 569  ARG   A HG3  1 
ATOM   8016  H HD2  . ARG   A  1 543 ? 50.684 -0.657  -46.861 0.00 34.94  ? 569  ARG   A HD2  1 
ATOM   8017  H HD3  . ARG   A  1 543 ? 51.699 0.793   -46.708 0.00 35.02  ? 569  ARG   A HD3  1 
ATOM   8018  H HE   . ARG   A  1 543 ? 49.064 0.293   -45.587 0.00 40.89  ? 569  ARG   A HE   1 
ATOM   8019  H HH11 . ARG   A  1 543 ? 48.139 1.885   -44.244 0.00 46.17  ? 569  ARG   A HH11 1 
ATOM   8020  H HH12 . ARG   A  1 543 ? 48.785 3.514   -44.245 0.00 46.25  ? 569  ARG   A HH12 1 
ATOM   8021  H HH21 . ARG   A  1 543 ? 51.299 2.880   -46.632 0.00 46.31  ? 569  ARG   A HH21 1 
ATOM   8022  H HH22 . ARG   A  1 543 ? 50.551 4.051   -45.581 0.00 46.07  ? 569  ARG   A HH22 1 
ATOM   8023  N N    . ILE   A  1 544 ? 52.174 -1.161  -52.187 1.00 19.16  ? 570  ILE   A N    1 
ATOM   8024  C CA   . ILE   A  1 544 ? 53.324 -1.719  -52.878 1.00 18.87  ? 570  ILE   A CA   1 
ATOM   8025  C C    . ILE   A  1 544 ? 53.230 -1.361  -54.361 1.00 19.11  ? 570  ILE   A C    1 
ATOM   8026  O O    . ILE   A  1 544 ? 52.348 -1.873  -55.041 1.00 19.35  ? 570  ILE   A O    1 
ATOM   8027  C CB   . ILE   A  1 544 ? 53.379 -3.276  -52.691 1.00 19.16  ? 570  ILE   A CB   1 
ATOM   8028  C CG1  . ILE   A  1 544 ? 53.166 -3.684  -51.196 1.00 19.81  ? 570  ILE   A CG1  1 
ATOM   8029  C CG2  . ILE   A  1 544 ? 54.719 -3.827  -53.258 1.00 19.55  ? 570  ILE   A CG2  1 
ATOM   8030  C CD1  . ILE   A  1 544 ? 52.835 -5.143  -51.016 1.00 21.59  ? 570  ILE   A CD1  1 
ATOM   8031  H H    . ILE   A  1 544 ? 51.370 -1.781  -52.202 0.00 20.24  ? 570  ILE   A H    1 
ATOM   8032  H HA   . ILE   A  1 544 ? 54.243 -1.301  -52.466 0.00 20.44  ? 570  ILE   A HA   1 
ATOM   8033  H HB   . ILE   A  1 544 ? 52.568 -3.717  -53.267 0.00 20.89  ? 570  ILE   A HB   1 
ATOM   8034  H HG12 . ILE   A  1 544 ? 54.083 -3.483  -50.645 0.00 21.48  ? 570  ILE   A HG12 1 
ATOM   8035  H HG13 . ILE   A  1 544 ? 52.343 -3.122  -50.759 0.00 21.09  ? 570  ILE   A HG13 1 
ATOM   8036  H HG21 . ILE   A  1 544 ? 54.824 -4.880  -53.007 0.00 21.96  ? 570  ILE   A HG21 1 
ATOM   8037  H HG22 . ILE   A  1 544 ? 54.728 -3.717  -54.341 0.00 22.02  ? 570  ILE   A HG22 1 
ATOM   8038  H HG23 . ILE   A  1 544 ? 55.544 -3.262  -52.827 0.00 21.85  ? 570  ILE   A HG23 1 
ATOM   8039  H HD11 . ILE   A  1 544 ? 52.466 -5.294  -50.002 0.00 23.43  ? 570  ILE   A HD11 1 
ATOM   8040  H HD12 . ILE   A  1 544 ? 52.072 -5.433  -51.737 0.00 23.68  ? 570  ILE   A HD12 1 
ATOM   8041  H HD13 . ILE   A  1 544 ? 53.731 -5.741  -51.168 0.00 23.97  ? 570  ILE   A HD13 1 
ATOM   8042  N N    . ALA   A  1 545 ? 54.142 -0.521  -54.870 1.00 18.94  ? 571  ALA   A N    1 
ATOM   8043  C CA   . ALA   A  1 545 ? 54.091 -0.129  -56.282 1.00 19.51  ? 571  ALA   A CA   1 
ATOM   8044  C C    . ALA   A  1 545 ? 54.274 -1.296  -57.251 1.00 19.84  ? 571  ALA   A C    1 
ATOM   8045  O O    . ALA   A  1 545 ? 53.601 -1.339  -58.287 1.00 20.17  ? 571  ALA   A O    1 
ATOM   8046  C CB   . ALA   A  1 545 ? 55.143 0.941   -56.576 1.00 19.80  ? 571  ALA   A CB   1 
ATOM   8047  H H    . ALA   A  1 545 ? 54.909 -0.106  -54.350 0.00 20.92  ? 571  ALA   A H    1 
ATOM   8048  H HA   . ALA   A  1 545 ? 53.112 0.304   -56.471 0.00 21.68  ? 571  ALA   A HA   1 
ATOM   8049  H HB1  . ALA   A  1 545 ? 55.084 1.214   -57.628 0.00 22.62  ? 571  ALA   A HB1  1 
ATOM   8050  H HB2  . ALA   A  1 545 ? 54.945 1.813   -55.955 0.00 22.17  ? 571  ALA   A HB2  1 
ATOM   8051  H HB3  . ALA   A  1 545 ? 56.130 0.539   -56.352 0.00 22.59  ? 571  ALA   A HB3  1 
ATOM   8052  N N    . GLY   A  1 546 ? 55.189 -2.205  -56.921 1.00 19.17  ? 572  GLY   A N    1 
ATOM   8053  C CA   . GLY   A  1 546 ? 55.575 -3.308  -57.796 1.00 19.68  ? 572  GLY   A CA   1 
ATOM   8054  C C    . GLY   A  1 546 ? 54.577 -4.429  -57.999 1.00 19.91  ? 572  GLY   A C    1 
ATOM   8055  O O    . GLY   A  1 546 ? 54.804 -5.279  -58.869 1.00 20.40  ? 572  GLY   A O    1 
ATOM   8056  H H    . GLY   A  1 546 ? 55.702 -2.206  -56.046 0.00 21.95  ? 572  GLY   A H    1 
ATOM   8057  H HA2  . GLY   A  1 546 ? 55.812 -2.901  -58.778 0.00 23.33  ? 572  GLY   A HA2  1 
ATOM   8058  H HA3  . GLY   A  1 546 ? 56.486 -3.753  -57.398 0.00 23.27  ? 572  GLY   A HA3  1 
ATOM   8059  N N    . VAL   A  1 547 ? 53.515 -4.502  -57.170 1.00 19.27  ? 573  VAL   A N    1 
ATOM   8060  C CA   . VAL   A  1 547 ? 52.498 -5.530  -57.373 1.00 19.34  ? 573  VAL   A CA   1 
ATOM   8061  C C    . VAL   A  1 547 ? 51.361 -4.934  -58.194 1.00 19.63  ? 573  VAL   A C    1 
ATOM   8062  O O    . VAL   A  1 547 ? 51.186 -3.716  -58.222 1.00 19.72  ? 573  VAL   A O    1 
ATOM   8063  C CB   . VAL   A  1 547 ? 52.010 -6.201  -56.068 1.00 19.76  ? 573  VAL   A CB   1 
ATOM   8064  C CG1  . VAL   A  1 547 ? 53.204 -6.691  -55.241 1.00 20.73  ? 573  VAL   A CG1  1 
ATOM   8065  C CG2  . VAL   A  1 547 ? 51.099 -5.268  -55.255 1.00 19.58  ? 573  VAL   A CG2  1 
ATOM   8066  H H    . VAL   A  1 547 ? 53.341 -3.894  -56.376 0.00 21.87  ? 573  VAL   A H    1 
ATOM   8067  H HA   . VAL   A  1 547 ? 52.925 -6.328  -57.972 0.00 22.69  ? 573  VAL   A HA   1 
ATOM   8068  H HB   . VAL   A  1 547 ? 51.420 -7.077  -56.334 0.00 22.66  ? 573  VAL   A HB   1 
ATOM   8069  H HG11 . VAL   A  1 547 ? 52.834 -7.292  -54.412 0.00 23.68  ? 573  VAL   A HG11 1 
ATOM   8070  H HG12 . VAL   A  1 547 ? 53.852 -7.293  -55.877 0.00 24.21  ? 573  VAL   A HG12 1 
ATOM   8071  H HG13 . VAL   A  1 547 ? 53.752 -5.833  -54.856 0.00 23.67  ? 573  VAL   A HG13 1 
ATOM   8072  H HG21 . VAL   A  1 547 ? 51.067 -5.620  -54.225 0.00 21.63  ? 573  VAL   A HG21 1 
ATOM   8073  H HG22 . VAL   A  1 547 ? 51.500 -4.256  -55.292 0.00 21.72  ? 573  VAL   A HG22 1 
ATOM   8074  H HG23 . VAL   A  1 547 ? 50.094 -5.289  -55.674 0.00 21.76  ? 573  VAL   A HG23 1 
ATOM   8075  N N    . THR   A  1 548 ? 50.606 -5.778  -58.888 1.00 19.65  ? 574  THR   A N    1 
ATOM   8076  C CA   . THR   A  1 548 ? 49.489 -5.290  -59.707 1.00 20.02  ? 574  THR   A CA   1 
ATOM   8077  C C    . THR   A  1 548 ? 48.254 -4.995  -58.837 1.00 20.27  ? 574  THR   A C    1 
ATOM   8078  O O    . THR   A  1 548 ? 48.088 -5.591  -57.770 1.00 20.27  ? 574  THR   A O    1 
ATOM   8079  C CB   . THR   A  1 548 ? 49.221 -6.271  -60.859 1.00 21.04  ? 574  THR   A CB   1 
ATOM   8080  O OG1  . THR   A  1 548 ? 49.047 -7.562  -60.310 1.00 21.50  ? 574  THR   A OG1  1 
ATOM   8081  C CG2  . THR   A  1 548 ? 50.372 -6.305  -61.863 1.00 21.58  ? 574  THR   A CG2  1 
ATOM   8082  H H    . THR   A  1 548 ? 50.730 -6.785  -58.907 0.00 23.04  ? 574  THR   A H    1 
ATOM   8083  H HA   . THR   A  1 548 ? 49.774 -4.341  -60.159 0.00 23.29  ? 574  THR   A HA   1 
ATOM   8084  H HB   . THR   A  1 548 ? 48.311 -5.975  -61.378 0.00 24.99  ? 574  THR   A HB   1 
ATOM   8085  H HG1  . THR   A  1 548 ? 48.125 -7.673  -59.960 0.00 25.41  ? 574  THR   A HG1  1 
ATOM   8086  H HG21 . THR   A  1 548 ? 50.130 -6.986  -62.677 0.00 26.46  ? 574  THR   A HG21 1 
ATOM   8087  H HG22 . THR   A  1 548 ? 50.541 -5.310  -62.272 0.00 26.06  ? 574  THR   A HG22 1 
ATOM   8088  H HG23 . THR   A  1 548 ? 51.284 -6.648  -61.376 0.00 26.14  ? 574  THR   A HG23 1 
ATOM   8089  N N    . HIS   A  1 549 ? 47.428 -4.014  -59.260 1.00 19.66  ? 575  HIS   A N    1 
ATOM   8090  C CA   . HIS   A  1 549 ? 46.225 -3.617  -58.524 1.00 19.25  ? 575  HIS   A CA   1 
ATOM   8091  C C    . HIS   A  1 549 ? 45.102 -3.443  -59.538 1.00 19.56  ? 575  HIS   A C    1 
ATOM   8092  O O    . HIS   A  1 549 ? 45.273 -2.727  -60.514 1.00 19.77  ? 575  HIS   A O    1 
ATOM   8093  C CB   . HIS   A  1 549 ? 46.431 -2.292  -57.747 1.00 19.00  ? 575  HIS   A CB   1 
ATOM   8094  C CG   . HIS   A  1 549 ? 47.747 -2.174  -57.043 1.00 19.32  ? 575  HIS   A CG   1 
ATOM   8095  N ND1  . HIS   A  1 549 ? 48.839 -1.613  -57.657 1.00 20.11  ? 575  HIS   A ND1  1 
ATOM   8096  C CD2  . HIS   A  1 549 ? 48.098 -2.563  -55.802 1.00 20.40  ? 575  HIS   A CD2  1 
ATOM   8097  C CE1  . HIS   A  1 549 ? 49.816 -1.666  -56.777 1.00 20.73  ? 575  HIS   A CE1  1 
ATOM   8098  N NE2  . HIS   A  1 549 ? 49.425 -2.257  -55.658 1.00 20.97  ? 575  HIS   A NE2  1 
ATOM   8099  H H    . HIS   A  1 549 ? 47.574 -3.479  -60.109 0.00 22.48  ? 575  HIS   A H    1 
ATOM   8100  H HA   . HIS   A  1 549 ? 45.931 -4.387  -57.812 0.00 21.33  ? 575  HIS   A HA   1 
ATOM   8101  H HB2  . HIS   A  1 549 ? 46.350 -1.458  -58.440 0.00 20.88  ? 575  HIS   A HB2  1 
ATOM   8102  H HB3  . HIS   A  1 549 ? 45.649 -2.211  -56.992 0.00 20.52  ? 575  HIS   A HB3  1 
ATOM   8103  H HD2  . HIS   A  1 549 ? 47.460 -3.024  -55.067 0.00 21.96  ? 575  HIS   A HD2  1 
ATOM   8104  H HE1  . HIS   A  1 549 ? 50.807 -1.278  -56.945 0.00 23.02  ? 575  HIS   A HE1  1 
ATOM   8105  H HE2  . HIS   A  1 549 ? 49.999 -2.449  -54.844 0.00 22.82  ? 575  HIS   A HE2  1 
ATOM   8106  N N    . HIS   A  1 550 ? 43.941 -4.036  -59.267 1.00 19.59  ? 576  HIS   A N    1 
ATOM   8107  C CA   . HIS   A  1 550 ? 42.826 -4.020  -60.195 1.00 20.15  ? 576  HIS   A CA   1 
ATOM   8108  C C    . HIS   A  1 550 ? 41.511 -3.663  -59.498 1.00 20.88  ? 576  HIS   A C    1 
ATOM   8109  O O    . HIS   A  1 550 ? 41.052 -4.404  -58.615 1.00 20.07  ? 576  HIS   A O    1 
ATOM   8110  C CB   . HIS   A  1 550 ? 42.712 -5.414  -60.852 1.00 20.79  ? 576  HIS   A CB   1 
ATOM   8111  C CG   . HIS   A  1 550 ? 43.810 -5.712  -61.835 1.00 21.46  ? 576  HIS   A CG   1 
ATOM   8112  N ND1  . HIS   A  1 550 ? 43.791 -5.193  -63.113 1.00 23.76  ? 576  HIS   A ND1  1 
ATOM   8113  C CD2  . HIS   A  1 550 ? 44.918 -6.478  -61.693 1.00 22.03  ? 576  HIS   A CD2  1 
ATOM   8114  C CE1  . HIS   A  1 550 ? 44.890 -5.638  -63.710 1.00 23.97  ? 576  HIS   A CE1  1 
ATOM   8115  N NE2  . HIS   A  1 550 ? 45.604 -6.410  -62.888 1.00 23.46  ? 576  HIS   A NE2  1 
ATOM   8116  H H    . HIS   A  1 550 ? 43.739 -4.536  -58.407 0.00 21.82  ? 576  HIS   A H    1 
ATOM   8117  H HA   . HIS   A  1 550 ? 42.995 -3.298  -60.992 0.00 23.10  ? 576  HIS   A HA   1 
ATOM   8118  H HB2  . HIS   A  1 550 ? 42.747 -6.173  -60.072 0.00 24.00  ? 576  HIS   A HB2  1 
ATOM   8119  H HB3  . HIS   A  1 550 ? 41.764 -5.476  -61.384 0.00 24.30  ? 576  HIS   A HB3  1 
ATOM   8120  H HD2  . HIS   A  1 550 ? 45.211 -7.033  -60.821 0.00 25.97  ? 576  HIS   A HD2  1 
ATOM   8121  H HE1  . HIS   A  1 550 ? 45.169 -5.407  -64.724 0.00 29.33  ? 576  HIS   A HE1  1 
ATOM   8122  H HE2  . HIS   A  1 550 ? 46.485 -6.865  -63.106 0.00 28.49  ? 576  HIS   A HE2  1 
ATOM   8123  N N    . LEU   A  1 551 ? 40.873 -2.561  -59.941 1.00 21.64  ? 577  LEU   A N    1 
ATOM   8124  C CA   . LEU   A  1 551 ? 39.570 -2.151  -59.418 1.00 22.86  ? 577  LEU   A CA   1 
ATOM   8125  C C    . LEU   A  1 551 ? 38.461 -2.178  -60.502 1.00 23.67  ? 577  LEU   A C    1 
ATOM   8126  O O    . LEU   A  1 551 ? 37.396 -1.616  -60.270 1.00 24.46  ? 577  LEU   A O    1 
ATOM   8127  C CB   . LEU   A  1 551 ? 39.700 -0.748  -58.785 1.00 23.26  ? 577  LEU   A CB   1 
ATOM   8128  C CG   . LEU   A  1 551 ? 40.524 -0.692  -57.486 1.00 24.80  ? 577  LEU   A CG   1 
ATOM   8129  C CD1  . LEU   A  1 551 ? 40.650 0.748   -56.975 1.00 25.50  ? 577  LEU   A CD1  1 
ATOM   8130  C CD2  . LEU   A  1 551 ? 39.906 -1.578  -56.397 1.00 25.35  ? 577  LEU   A CD2  1 
ATOM   8131  H H    . LEU   A  1 551 ? 41.232 -1.938  -60.657 0.00 24.64  ? 577  LEU   A H    1 
ATOM   8132  H HA   . LEU   A  1 551 ? 39.239 -2.841  -58.644 0.00 25.63  ? 577  LEU   A HA   1 
ATOM   8133  H HB2  . LEU   A  1 551 ? 40.179 -0.085  -59.504 0.00 26.12  ? 577  LEU   A HB2  1 
ATOM   8134  H HB3  . LEU   A  1 551 ? 38.710 -0.366  -58.540 0.00 25.91  ? 577  LEU   A HB3  1 
ATOM   8135  H HG   . LEU   A  1 551 ? 41.527 -1.063  -57.691 0.00 27.46  ? 577  LEU   A HG   1 
ATOM   8136  H HD11 . LEU   A  1 551 ? 41.333 0.763   -56.127 0.00 27.77  ? 577  LEU   A HD11 1 
ATOM   8137  H HD12 . LEU   A  1 551 ? 41.039 1.375   -57.776 0.00 28.20  ? 577  LEU   A HD12 1 
ATOM   8138  H HD13 . LEU   A  1 551 ? 39.667 1.101   -56.667 0.00 27.94  ? 577  LEU   A HD13 1 
ATOM   8139  H HD21 . LEU   A  1 551 ? 40.144 -1.161  -55.420 0.00 27.53  ? 577  LEU   A HD21 1 
ATOM   8140  H HD22 . LEU   A  1 551 ? 38.826 -1.613  -56.532 0.00 27.91  ? 577  LEU   A HD22 1 
ATOM   8141  H HD23 . LEU   A  1 551 ? 40.321 -2.581  -56.483 0.00 27.93  ? 577  LEU   A HD23 1 
ATOM   8142  N N    . GLU   A  1 552 ? 38.673 -2.900  -61.628 1.00 22.74  ? 578  GLU   A N    1 
ATOM   8143  C CA   . GLU   A  1 552 ? 37.713 -2.995  -62.735 1.00 23.50  ? 578  GLU   A CA   1 
ATOM   8144  C C    . GLU   A  1 552 ? 36.361 -3.577  -62.351 1.00 23.79  ? 578  GLU   A C    1 
ATOM   8145  O O    . GLU   A  1 552 ? 35.382 -3.274  -63.020 1.00 24.38  ? 578  GLU   A O    1 
ATOM   8146  C CB   . GLU   A  1 552 ? 38.253 -3.868  -63.899 1.00 25.42  ? 578  GLU   A CB   1 
ATOM   8147  C CG   . GLU   A  1 552 ? 39.569 -3.424  -64.502 1.00 28.90  ? 578  GLU   A CG   1 
ATOM   8148  C CD   . GLU   A  1 552 ? 40.805 -3.982  -63.836 1.00 34.09  ? 578  GLU   A CD   1 
ATOM   8149  O OE1  . GLU   A  1 552 ? 40.700 -4.409  -62.668 1.00 36.32  ? 578  GLU   A OE1  1 
ATOM   8150  O OE2  . GLU   A  1 552 ? 41.881 -3.993  -64.475 1.00 34.72  ? 578  GLU   A OE2  1 
ATOM   8151  H H    . GLU   A  1 552 ? 39.499 -3.469  -61.781 0.00 26.57  ? 578  GLU   A H    1 
ATOM   8152  H HA   . GLU   A  1 552 ? 37.538 -1.994  -63.127 0.00 27.93  ? 578  GLU   A HA   1 
ATOM   8153  H HB2  . GLU   A  1 552 ? 38.365 -4.890  -63.541 0.00 30.67  ? 578  GLU   A HB2  1 
ATOM   8154  H HB3  . GLU   A  1 552 ? 37.516 -3.851  -64.701 0.00 31.04  ? 578  GLU   A HB3  1 
ATOM   8155  H HG2  . GLU   A  1 552 ? 39.593 -3.721  -65.549 0.00 35.38  ? 578  GLU   A HG2  1 
ATOM   8156  H HG3  . GLU   A  1 552 ? 39.639 -2.340  -64.423 0.00 34.77  ? 578  GLU   A HG3  1 
ATOM   8157  N N    . PHE   A  1 553 ? 36.306 -4.452  -61.331 1.00 23.75  ? 579  PHE   A N    1 
ATOM   8158  C CA   . PHE   A  1 553 ? 35.060 -5.111  -60.931 1.00 23.65  ? 579  PHE   A CA   1 
ATOM   8159  C C    . PHE   A  1 553 ? 33.935 -4.149  -60.562 1.00 24.80  ? 579  PHE   A C    1 
ATOM   8160  O O    . PHE   A  1 553 ? 32.777 -4.541  -60.661 1.00 26.12  ? 579  PHE   A O    1 
ATOM   8161  C CB   . PHE   A  1 553 ? 35.308 -6.073  -59.760 1.00 22.70  ? 579  PHE   A CB   1 
ATOM   8162  C CG   . PHE   A  1 553 ? 35.874 -5.421  -58.523 1.00 22.33  ? 579  PHE   A CG   1 
ATOM   8163  C CD1  . PHE   A  1 553 ? 35.045 -5.006  -57.499 1.00 22.81  ? 579  PHE   A CD1  1 
ATOM   8164  C CD2  . PHE   A  1 553 ? 37.242 -5.283  -58.360 1.00 22.72  ? 579  PHE   A CD2  1 
ATOM   8165  C CE1  . PHE   A  1 553 ? 35.573 -4.419  -56.355 1.00 23.52  ? 579  PHE   A CE1  1 
ATOM   8166  C CE2  . PHE   A  1 553 ? 37.763 -4.666  -57.233 1.00 23.25  ? 579  PHE   A CE2  1 
ATOM   8167  C CZ   . PHE   A  1 553 ? 36.928 -4.246  -56.236 1.00 23.20  ? 579  PHE   A CZ   1 
ATOM   8168  H H    . PHE   A  1 553 ? 37.114 -4.741  -60.790 0.00 27.77  ? 579  PHE   A H    1 
ATOM   8169  H HA   . PHE   A  1 553 ? 34.709 -5.709  -61.771 0.00 28.37  ? 579  PHE   A HA   1 
ATOM   8170  H HB2  . PHE   A  1 553 ? 34.364 -6.539  -59.484 0.00 26.61  ? 579  PHE   A HB2  1 
ATOM   8171  H HB3  . PHE   A  1 553 ? 36.014 -6.837  -60.082 0.00 26.69  ? 579  PHE   A HB3  1 
ATOM   8172  H HD1  . PHE   A  1 553 ? 33.979 -5.121  -57.594 0.00 25.97  ? 579  PHE   A HD1  1 
ATOM   8173  H HD2  . PHE   A  1 553 ? 37.906 -5.597  -59.148 0.00 26.05  ? 579  PHE   A HD2  1 
ATOM   8174  H HE1  . PHE   A  1 553 ? 34.916 -4.075  -55.573 0.00 25.98  ? 579  PHE   A HE1  1 
ATOM   8175  H HE2  . PHE   A  1 553 ? 38.829 -4.550  -57.128 0.00 25.88  ? 579  PHE   A HE2  1 
ATOM   8176  H HZ   . PHE   A  1 553 ? 37.337 -3.794  -55.348 0.00 25.30  ? 579  PHE   A HZ   1 
ATOM   8177  N N    . ILE   A  1 554 ? 34.258 -2.910  -60.134 1.00 24.54  ? 580  ILE   A N    1 
ATOM   8178  C CA   . ILE   A  1 554 ? 33.254 -1.912  -59.724 1.00 25.17  ? 580  ILE   A CA   1 
ATOM   8179  C C    . ILE   A  1 554 ? 32.166 -1.695  -60.810 1.00 25.60  ? 580  ILE   A C    1 
ATOM   8180  O O    . ILE   A  1 554 ? 30.992 -1.500  -60.491 1.00 25.35  ? 580  ILE   A O    1 
ATOM   8181  C CB   . ILE   A  1 554 ? 33.965 -0.577  -59.326 1.00 25.74  ? 580  ILE   A CB   1 
ATOM   8182  C CG1  . ILE   A  1 554 ? 34.784 -0.761  -58.018 1.00 27.15  ? 580  ILE   A CG1  1 
ATOM   8183  C CG2  . ILE   A  1 554 ? 32.954 0.580   -59.167 1.00 26.28  ? 580  ILE   A CG2  1 
ATOM   8184  C CD1  . ILE   A  1 554 ? 35.921 0.278   -57.840 1.00 28.71  ? 580  ILE   A CD1  1 
ATOM   8185  H H    . ILE   A  1 554 ? 35.212 -2.570  -60.061 0.00 28.41  ? 580  ILE   A H    1 
ATOM   8186  H HA   . ILE   A  1 554 ? 32.749 -2.285  -58.835 0.00 29.06  ? 580  ILE   A HA   1 
ATOM   8187  H HB   . ILE   A  1 554 ? 34.651 -0.301  -60.126 0.00 29.77  ? 580  ILE   A HB   1 
ATOM   8188  H HG12 . ILE   A  1 554 ? 34.112 -0.662  -57.167 0.00 30.61  ? 580  ILE   A HG12 1 
ATOM   8189  H HG13 . ILE   A  1 554 ? 35.242 -1.749  -58.009 0.00 30.81  ? 580  ILE   A HG13 1 
ATOM   8190  H HG21 . ILE   A  1 554 ? 33.419 1.393   -58.611 0.00 30.02  ? 580  ILE   A HG21 1 
ATOM   8191  H HG22 . ILE   A  1 554 ? 32.665 0.945   -60.151 0.00 30.65  ? 580  ILE   A HG22 1 
ATOM   8192  H HG23 . ILE   A  1 554 ? 32.081 0.217   -58.627 0.00 30.28  ? 580  ILE   A HG23 1 
ATOM   8193  H HD11 . ILE   A  1 554 ? 36.558 -0.035  -57.014 0.00 32.13  ? 580  ILE   A HD11 1 
ATOM   8194  H HD12 . ILE   A  1 554 ? 36.497 0.315   -58.763 0.00 32.65  ? 580  ILE   A HD12 1 
ATOM   8195  H HD13 . ILE   A  1 554 ? 35.496 1.256   -57.623 0.00 32.37  ? 580  ILE   A HD13 1 
ATOM   8196  N N    . GLN   A  1 555 ? 32.571 -1.744  -62.075 1.00 26.55  ? 581  GLN   A N    1 
ATOM   8197  C CA   . GLN   A  1 555 ? 31.686 -1.551  -63.237 1.00 28.06  ? 581  GLN   A CA   1 
ATOM   8198  C C    . GLN   A  1 555 ? 30.598 -2.619  -63.418 1.00 29.08  ? 581  GLN   A C    1 
ATOM   8199  O O    . GLN   A  1 555 ? 29.564 -2.339  -64.035 1.00 29.17  ? 581  GLN   A O    1 
ATOM   8200  C CB   . GLN   A  1 555 ? 32.555 -1.516  -64.508 1.00 30.64  ? 581  GLN   A CB   1 
ATOM   8201  C CG   . GLN   A  1 555 ? 31.844 -1.175  -65.793 1.00 36.83  ? 581  GLN   A CG   1 
ATOM   8202  C CD   . GLN   A  1 555 ? 32.857 -1.057  -66.910 1.00 42.03  ? 581  GLN   A CD   1 
ATOM   8203  O OE1  . GLN   A  1 555 ? 33.788 -1.877  -67.015 1.00 42.18  ? 581  GLN   A OE1  1 
ATOM   8204  N NE2  . GLN   A  1 555 ? 32.693 -0.045  -67.770 1.00 42.73  ? 581  GLN   A NE2  1 
ATOM   8205  H H    . GLN   A  1 555 ? 33.541 -1.918  -62.317 0.00 31.77  ? 581  GLN   A H    1 
ATOM   8206  H HA   . GLN   A  1 555 ? 31.192 -0.585  -63.145 0.00 34.21  ? 581  GLN   A HA   1 
ATOM   8207  H HB2  . GLN   A  1 555 ? 33.342 -0.777  -64.371 0.00 37.41  ? 581  GLN   A HB2  1 
ATOM   8208  H HB3  . GLN   A  1 555 ? 33.000 -2.503  -64.629 0.00 37.71  ? 581  GLN   A HB3  1 
ATOM   8209  H HG2  . GLN   A  1 555 ? 31.141 -1.961  -66.063 0.00 46.01  ? 581  GLN   A HG2  1 
ATOM   8210  H HG3  . GLN   A  1 555 ? 31.323 -0.226  -65.673 0.00 45.68  ? 581  GLN   A HG3  1 
ATOM   8211  H HE21 . GLN   A  1 555 ? 31.917 0.603   -67.672 0.00 53.47  ? 581  GLN   A HE21 1 
ATOM   8212  H HE22 . GLN   A  1 555 ? 33.347 0.071   -68.537 0.00 53.61  ? 581  GLN   A HE22 1 
ATOM   8213  N N    . ASN   A  1 556 ? 30.849 -3.850  -62.974 1.00 29.18  ? 582  ASN   A N    1 
ATOM   8214  C CA   . ASN   A  1 556 ? 29.918 -4.960  -63.203 1.00 30.28  ? 582  ASN   A CA   1 
ATOM   8215  C C    . ASN   A  1 556 ? 28.608 -4.930  -62.410 1.00 30.36  ? 582  ASN   A C    1 
ATOM   8216  O O    . ASN   A  1 556 ? 27.662 -5.636  -62.784 1.00 31.75  ? 582  ASN   A O    1 
ATOM   8217  C CB   . ASN   A  1 556 ? 30.620 -6.273  -62.927 1.00 32.96  ? 582  ASN   A CB   1 
ATOM   8218  C CG   . ASN   A  1 556 ? 31.731 -6.559  -63.855 1.00 39.30  ? 582  ASN   A CG   1 
ATOM   8219  O OD1  . ASN   A  1 556 ? 32.784 -5.903  -63.783 1.00 38.88  ? 582  ASN   A OD1  1 
ATOM   8220  N ND2  . ASN   A  1 556 ? 31.505 -7.413  -64.848 1.00 44.20  ? 582  ASN   A ND2  1 
ATOM   8221  H H    . ASN   A  1 556 ? 31.679 -4.109  -62.450 0.00 35.51  ? 582  ASN   A H    1 
ATOM   8222  H HA   . ASN   A  1 556 ? 29.648 -4.964  -64.258 0.00 38.04  ? 582  ASN   A HA   1 
ATOM   8223  H HB2  . ASN   A  1 556 ? 31.026 -6.239  -61.918 0.00 40.24  ? 582  ASN   A HB2  1 
ATOM   8224  H HB3  . ASN   A  1 556 ? 29.897 -7.084  -62.999 0.00 41.01  ? 582  ASN   A HB3  1 
ATOM   8225  H HD21 . ASN   A  1 556 ? 32.385 -7.865  -64.697 0.00 54.86  ? 582  ASN   A HD21 1 
ATOM   8226  H HD22 . ASN   A  1 556 ? 30.617 -7.869  -65.027 0.00 55.32  ? 582  ASN   A HD22 1 
ATOM   8227  N N    . PHE   A  1 557 ? 28.528 -4.134  -61.345 1.00 28.57  ? 583  PHE   A N    1 
ATOM   8228  C CA   . PHE   A  1 557 ? 27.333 -4.090  -60.509 1.00 28.33  ? 583  PHE   A CA   1 
ATOM   8229  C C    . PHE   A  1 557 ? 26.269 -3.131  -61.032 1.00 28.68  ? 583  PHE   A C    1 
ATOM   8230  O O    . PHE   A  1 557 ? 26.559 -1.950  -61.232 1.00 29.08  ? 583  PHE   A O    1 
ATOM   8231  C CB   . PHE   A  1 557 ? 27.720 -3.684  -59.090 1.00 27.46  ? 583  PHE   A CB   1 
ATOM   8232  C CG   . PHE   A  1 557 ? 28.744 -4.593  -58.465 1.00 27.08  ? 583  PHE   A CG   1 
ATOM   8233  C CD1  . PHE   A  1 557 ? 28.385 -5.841  -57.990 1.00 27.10  ? 583  PHE   A CD1  1 
ATOM   8234  C CD2  . PHE   A  1 557 ? 30.064 -4.199  -58.349 1.00 27.49  ? 583  PHE   A CD2  1 
ATOM   8235  C CE1  . PHE   A  1 557 ? 29.327 -6.680  -57.418 1.00 27.57  ? 583  PHE   A CE1  1 
ATOM   8236  C CE2  . PHE   A  1 557 ? 31.007 -5.042  -57.772 1.00 28.46  ? 583  PHE   A CE2  1 
ATOM   8237  C CZ   . PHE   A  1 557 ? 30.626 -6.268  -57.288 1.00 27.82  ? 583  PHE   A CZ   1 
ATOM   8238  H H    . PHE   A  1 557 ? 29.259 -3.500  -61.039 0.00 34.65  ? 583  PHE   A H    1 
ATOM   8239  H HA   . PHE   A  1 557 ? 26.901 -5.087  -60.442 0.00 34.87  ? 583  PHE   A HA   1 
ATOM   8240  H HB2  . PHE   A  1 557 ? 28.121 -2.671  -59.111 0.00 32.81  ? 583  PHE   A HB2  1 
ATOM   8241  H HB3  . PHE   A  1 557 ? 26.822 -3.729  -58.476 0.00 32.99  ? 583  PHE   A HB3  1 
ATOM   8242  H HD1  . PHE   A  1 557 ? 27.362 -6.168  -58.075 0.00 32.58  ? 583  PHE   A HD1  1 
ATOM   8243  H HD2  . PHE   A  1 557 ? 30.368 -3.230  -58.706 0.00 32.29  ? 583  PHE   A HD2  1 
ATOM   8244  H HE1  . PHE   A  1 557 ? 29.030 -7.645  -57.049 0.00 32.67  ? 583  PHE   A HE1  1 
ATOM   8245  H HE2  . PHE   A  1 557 ? 32.030 -4.718  -57.676 0.00 32.99  ? 583  PHE   A HE2  1 
ATOM   8246  H HZ   . PHE   A  1 557 ? 31.358 -6.924  -56.851 0.00 32.39  ? 583  PHE   A HZ   1 
ATOM   8247  N N    . THR   A  1 558 ? 25.027 -3.610  -61.182 1.00 28.05  ? 584  THR   A N    1 
ATOM   8248  C CA   . THR   A  1 558 ? 23.918 -2.776  -61.644 1.00 28.16  ? 584  THR   A CA   1 
ATOM   8249  C C    . THR   A  1 558 ? 23.170 -2.092  -60.502 1.00 27.61  ? 584  THR   A C    1 
ATOM   8250  O O    . THR   A  1 558 ? 22.452 -1.131  -60.769 1.00 28.59  ? 584  THR   A O    1 
ATOM   8251  C CB   . THR   A  1 558 ? 22.962 -3.584  -62.543 1.00 29.92  ? 584  THR   A CB   1 
ATOM   8252  O OG1  . THR   A  1 558 ? 22.214 -4.499  -61.743 1.00 31.95  ? 584  THR   A OG1  1 
ATOM   8253  C CG2  . THR   A  1 558 ? 23.693 -4.320  -63.661 1.00 29.77  ? 584  THR   A CG2  1 
ATOM   8254  H H    . THR   A  1 558 ? 24.753 -4.568  -60.986 0.00 35.24  ? 584  THR   A H    1 
ATOM   8255  H HA   . THR   A  1 558 ? 24.314 -1.984  -62.277 0.00 35.78  ? 584  THR   A HA   1 
ATOM   8256  H HB   . THR   A  1 558 ? 22.266 -2.892  -63.013 0.00 38.89  ? 584  THR   A HB   1 
ATOM   8257  H HG1  . THR   A  1 558 ? 22.811 -5.201  -61.373 0.00 40.72  ? 584  THR   A HG1  1 
ATOM   8258  H HG21 . THR   A  1 558 ? 22.972 -4.736  -64.362 0.00 39.23  ? 584  THR   A HG21 1 
ATOM   8259  H HG22 . THR   A  1 558 ? 24.352 -3.633  -64.190 0.00 38.60  ? 584  THR   A HG22 1 
ATOM   8260  H HG23 . THR   A  1 558 ? 24.288 -5.134  -63.251 0.00 38.41  ? 584  THR   A HG23 1 
ATOM   8261  N N    . ASN   A  1 559 ? 23.286 -2.574  -59.251 1.00 26.32  ? 585  ASN   A N    1 
ATOM   8262  C CA   . ASN   A  1 559 ? 22.576 -1.969  -58.116 1.00 26.42  ? 585  ASN   A CA   1 
ATOM   8263  C C    . ASN   A  1 559 ? 23.540 -1.360  -57.066 1.00 25.28  ? 585  ASN   A C    1 
ATOM   8264  O O    . ASN   A  1 559 ? 23.077 -1.028  -55.978 1.00 25.05  ? 585  ASN   A O    1 
ATOM   8265  C CB   . ASN   A  1 559 ? 21.721 -3.021  -57.394 1.00 28.85  ? 585  ASN   A CB   1 
ATOM   8266  C CG   . ASN   A  1 559 ? 20.753 -3.777  -58.259 1.00 34.91  ? 585  ASN   A CG   1 
ATOM   8267  O OD1  . ASN   A  1 559 ? 20.953 -4.961  -58.568 1.00 37.99  ? 585  ASN   A OD1  1 
ATOM   8268  N ND2  . ASN   A  1 559 ? 19.671 -3.124  -58.645 1.00 35.69  ? 585  ASN   A ND2  1 
ATOM   8269  H H    . ASN   A  1 559 ? 23.842 -3.380  -58.986 0.00 32.58  ? 585  ASN   A H    1 
ATOM   8270  H HA   . ASN   A  1 559 ? 21.905 -1.178  -58.447 0.00 32.97  ? 585  ASN   A HA   1 
ATOM   8271  H HB2  . ASN   A  1 559 ? 22.385 -3.749  -56.931 0.00 35.37  ? 585  ASN   A HB2  1 
ATOM   8272  H HB3  . ASN   A  1 559 ? 21.126 -2.528  -56.626 0.00 35.58  ? 585  ASN   A HB3  1 
ATOM   8273  H HD21 . ASN   A  1 559 ? 18.980 -3.588  -59.227 0.00 45.54  ? 585  ASN   A HD21 1 
ATOM   8274  H HD22 . ASN   A  1 559 ? 19.527 -2.160  -58.362 0.00 44.92  ? 585  ASN   A HD22 1 
ATOM   8275  N N    . LEU   A  1 560 ? 24.860 -1.265  -57.349 1.00 23.91  ? 586  LEU   A N    1 
ATOM   8276  C CA   . LEU   A  1 560 ? 25.803 -0.733  -56.371 1.00 23.46  ? 586  LEU   A CA   1 
ATOM   8277  C C    . LEU   A  1 560 ? 25.546 0.759   -56.163 1.00 22.81  ? 586  LEU   A C    1 
ATOM   8278  O O    . LEU   A  1 560 ? 25.636 1.530   -57.124 1.00 22.54  ? 586  LEU   A O    1 
ATOM   8279  C CB   . LEU   A  1 560 ? 27.247 -0.979  -56.805 1.00 23.33  ? 586  LEU   A CB   1 
ATOM   8280  C CG   . LEU   A  1 560 ? 28.347 -0.649  -55.786 1.00 23.87  ? 586  LEU   A CG   1 
ATOM   8281  C CD1  . LEU   A  1 560 ? 28.276 -1.572  -54.556 1.00 24.57  ? 586  LEU   A CD1  1 
ATOM   8282  C CD2  . LEU   A  1 560 ? 29.720 -0.744  -56.437 1.00 24.73  ? 586  LEU   A CD2  1 
ATOM   8283  H H    . LEU   A  1 560 ? 25.295 -1.530  -58.226 0.00 28.88  ? 586  LEU   A H    1 
ATOM   8284  H HA   . LEU   A  1 560 ? 25.665 -1.253  -55.427 0.00 27.32  ? 586  LEU   A HA   1 
ATOM   8285  H HB2  . LEU   A  1 560 ? 27.345 -2.039  -57.025 0.00 27.29  ? 586  LEU   A HB2  1 
ATOM   8286  H HB3  . LEU   A  1 560 ? 27.443 -0.402  -57.708 0.00 27.40  ? 586  LEU   A HB3  1 
ATOM   8287  H HG   . LEU   A  1 560 ? 28.227 0.376   -55.439 0.00 27.15  ? 586  LEU   A HG   1 
ATOM   8288  H HD11 . LEU   A  1 560 ? 29.195 -1.465  -53.982 0.00 27.44  ? 586  LEU   A HD11 1 
ATOM   8289  H HD12 . LEU   A  1 560 ? 27.430 -1.281  -53.935 0.00 27.78  ? 586  LEU   A HD12 1 
ATOM   8290  H HD13 . LEU   A  1 560 ? 28.163 -2.603  -54.885 0.00 27.98  ? 586  LEU   A HD13 1 
ATOM   8291  H HD21 . LEU   A  1 560 ? 30.482 -0.474  -55.708 0.00 27.82  ? 586  LEU   A HD21 1 
ATOM   8292  H HD22 . LEU   A  1 560 ? 29.879 -1.765  -56.779 0.00 28.32  ? 586  LEU   A HD22 1 
ATOM   8293  H HD23 . LEU   A  1 560 ? 29.762 -0.062  -57.285 0.00 28.42  ? 586  LEU   A HD23 1 
ATOM   8294  N N    . LYS   A  1 561 ? 25.223 1.147   -54.926 1.00 21.23  ? 587  LYS   A N    1 
ATOM   8295  C CA   . LYS   A  1 561 ? 24.920 2.536   -54.570 1.00 21.40  ? 587  LYS   A CA   1 
ATOM   8296  C C    . LYS   A  1 561 ? 26.063 3.216   -53.797 1.00 20.46  ? 587  LYS   A C    1 
ATOM   8297  O O    . LYS   A  1 561 ? 26.346 4.385   -54.044 1.00 20.10  ? 587  LYS   A O    1 
ATOM   8298  C CB   . LYS   A  1 561 ? 23.652 2.613   -53.694 1.00 23.16  ? 587  LYS   A CB   1 
ATOM   8299  C CG   . LYS   A  1 561 ? 22.359 2.193   -54.371 1.00 28.60  ? 587  LYS   A CG   1 
ATOM   8300  C CD   . LYS   A  1 561 ? 21.194 2.277   -53.371 1.00 34.99  ? 587  LYS   A CD   1 
ATOM   8301  C CE   . LYS   A  1 561 ? 19.849 1.987   -53.993 1.00 40.34  ? 587  LYS   A CE   1 
ATOM   8302  N NZ   . LYS   A  1 561 ? 19.819 0.671   -54.696 1.00 43.83  ? 587  LYS   A NZ   1 
ATOM   8303  H H    . LYS   A  1 561 ? 25.163 0.518   -54.131 0.00 24.34  ? 587  LYS   A H    1 
ATOM   8304  H HA   . LYS   A  1 561 ? 24.729 3.124   -55.466 0.00 25.07  ? 587  LYS   A HA   1 
ATOM   8305  H HB2  . LYS   A  1 561 ? 23.790 1.968   -52.828 0.00 26.66  ? 587  LYS   A HB2  1 
ATOM   8306  H HB3  . LYS   A  1 561 ? 23.526 3.642   -53.363 0.00 26.94  ? 587  LYS   A HB3  1 
ATOM   8307  H HG2  . LYS   A  1 561 ? 22.149 2.862   -55.205 0.00 34.41  ? 587  LYS   A HG2  1 
ATOM   8308  H HG3  . LYS   A  1 561 ? 22.452 1.166   -54.719 0.00 34.14  ? 587  LYS   A HG3  1 
ATOM   8309  H HD2  . LYS   A  1 561 ? 21.359 1.551   -52.577 0.00 41.53  ? 587  LYS   A HD2  1 
ATOM   8310  H HD3  . LYS   A  1 561 ? 21.160 3.282   -52.954 0.00 41.76  ? 587  LYS   A HD3  1 
ATOM   8311  H HE2  . LYS   A  1 561 ? 19.092 1.969   -53.210 0.00 48.93  ? 587  LYS   A HE2  1 
ATOM   8312  H HE3  . LYS   A  1 561 ? 19.618 2.764   -54.720 0.00 49.22  ? 587  LYS   A HE3  1 
ATOM   8313  H HZ1  . LYS   A  1 561 ? 18.857 0.397   -54.870 0.00 53.68  ? 587  LYS   A HZ1  1 
ATOM   8314  H HZ2  . LYS   A  1 561 ? 20.300 0.737   -55.588 0.00 53.39  ? 587  LYS   A HZ2  1 
ATOM   8315  H HZ3  . LYS   A  1 561 ? 20.269 -0.039  -54.128 0.00 52.94  ? 587  LYS   A HZ3  1 
ATOM   8316  N N    . VAL   A  1 562 ? 26.666 2.514   -52.825 1.00 18.97  ? 588  VAL   A N    1 
ATOM   8317  C CA   . VAL   A  1 562 ? 27.687 3.087   -51.952 1.00 19.01  ? 588  VAL   A CA   1 
ATOM   8318  C C    . VAL   A  1 562 ? 28.940 2.227   -51.959 1.00 19.06  ? 588  VAL   A C    1 
ATOM   8319  O O    . VAL   A  1 562 ? 28.867 1.013   -51.725 1.00 19.31  ? 588  VAL   A O    1 
ATOM   8320  C CB   . VAL   A  1 562 ? 27.133 3.241   -50.515 1.00 19.47  ? 588  VAL   A CB   1 
ATOM   8321  C CG1  . VAL   A  1 562 ? 28.169 3.893   -49.587 1.00 20.06  ? 588  VAL   A CG1  1 
ATOM   8322  C CG2  . VAL   A  1 562 ? 25.809 4.019   -50.508 1.00 19.83  ? 588  VAL   A CG2  1 
ATOM   8323  H H    . VAL   A  1 562 ? 26.455 1.545   -52.607 0.00 20.87  ? 588  VAL   A H    1 
ATOM   8324  H HA   . VAL   A  1 562 ? 27.962 4.082   -52.299 0.00 20.54  ? 588  VAL   A HA   1 
ATOM   8325  H HB   . VAL   A  1 562 ? 26.935 2.246   -50.118 0.00 20.75  ? 588  VAL   A HB   1 
ATOM   8326  H HG11 . VAL   A  1 562 ? 27.679 4.217   -48.671 0.00 21.04  ? 588  VAL   A HG11 1 
ATOM   8327  H HG12 . VAL   A  1 562 ? 28.943 3.168   -49.338 0.00 20.87  ? 588  VAL   A HG12 1 
ATOM   8328  H HG13 . VAL   A  1 562 ? 28.610 4.748   -50.097 0.00 21.18  ? 588  VAL   A HG13 1 
ATOM   8329  H HG21 . VAL   A  1 562 ? 25.541 4.276   -49.484 0.00 21.45  ? 588  VAL   A HG21 1 
ATOM   8330  H HG22 . VAL   A  1 562 ? 25.918 4.922   -51.107 0.00 21.77  ? 588  VAL   A HG22 1 
ATOM   8331  H HG23 . VAL   A  1 562 ? 25.025 3.392   -50.932 0.00 21.88  ? 588  VAL   A HG23 1 
ATOM   8332  N N    . LEU   A  1 563 ? 30.092 2.870   -52.193 1.00 18.46  ? 589  LEU   A N    1 
ATOM   8333  C CA   . LEU   A  1 563 ? 31.378 2.206   -52.209 1.00 18.77  ? 589  LEU   A CA   1 
ATOM   8334  C C    . LEU   A  1 563 ? 32.335 3.005   -51.359 1.00 18.19  ? 589  LEU   A C    1 
ATOM   8335  O O    . LEU   A  1 563 ? 32.528 4.201   -51.591 1.00 18.43  ? 589  LEU   A O    1 
ATOM   8336  C CB   . LEU   A  1 563 ? 31.916 2.113   -53.646 1.00 18.73  ? 589  LEU   A CB   1 
ATOM   8337  C CG   . LEU   A  1 563 ? 33.317 1.540   -53.808 1.00 19.23  ? 589  LEU   A CG   1 
ATOM   8338  C CD1  . LEU   A  1 563 ? 33.414 0.114   -53.261 1.00 18.99  ? 589  LEU   A CD1  1 
ATOM   8339  C CD2  . LEU   A  1 563 ? 33.740 1.589   -55.278 1.00 19.96  ? 589  LEU   A CD2  1 
ATOM   8340  H H    . LEU   A  1 563 ? 30.166 3.866   -52.370 0.00 19.44  ? 589  LEU   A H    1 
ATOM   8341  H HA   . LEU   A  1 563 ? 31.295 1.201   -51.801 0.00 19.45  ? 589  LEU   A HA   1 
ATOM   8342  H HB2  . LEU   A  1 563 ? 31.238 1.487   -54.224 0.00 20.03  ? 589  LEU   A HB2  1 
ATOM   8343  H HB3  . LEU   A  1 563 ? 31.927 3.116   -54.072 0.00 19.88  ? 589  LEU   A HB3  1 
ATOM   8344  H HG   . LEU   A  1 563 ? 34.017 2.156   -53.251 0.00 19.97  ? 589  LEU   A HG   1 
ATOM   8345  H HD11 . LEU   A  1 563 ? 34.369 -0.317  -53.561 0.00 19.76  ? 589  LEU   A HD11 1 
ATOM   8346  H HD12 . LEU   A  1 563 ? 33.348 0.143   -52.175 0.00 19.52  ? 589  LEU   A HD12 1 
ATOM   8347  H HD13 . LEU   A  1 563 ? 32.592 -0.473  -53.669 0.00 20.02  ? 589  LEU   A HD13 1 
ATOM   8348  H HD21 . LEU   A  1 563 ? 34.754 1.203   -55.368 0.00 21.31  ? 589  LEU   A HD21 1 
ATOM   8349  H HD22 . LEU   A  1 563 ? 33.056 0.974   -55.862 0.00 21.68  ? 589  LEU   A HD22 1 
ATOM   8350  H HD23 . LEU   A  1 563 ? 33.703 2.620   -55.624 0.00 21.50  ? 589  LEU   A HD23 1 
ATOM   8351  N N    . ASN   A  1 564 ? 32.967 2.339   -50.402 1.00 17.06  ? 590  ASN   A N    1 
ATOM   8352  C CA   . ASN   A  1 564 ? 33.926 2.991   -49.531 1.00 16.93  ? 590  ASN   A CA   1 
ATOM   8353  C C    . ASN   A  1 564 ? 35.308 2.391   -49.766 1.00 16.68  ? 590  ASN   A C    1 
ATOM   8354  O O    . ASN   A  1 564 ? 35.553 1.241   -49.421 1.00 16.35  ? 590  ASN   A O    1 
ATOM   8355  C CB   . ASN   A  1 564 ? 33.469 2.926   -48.056 1.00 16.49  ? 590  ASN   A CB   1 
ATOM   8356  C CG   . ASN   A  1 564 ? 34.263 3.836   -47.139 1.00 19.07  ? 590  ASN   A CG   1 
ATOM   8357  O OD1  . ASN   A  1 564 ? 35.386 4.197   -47.467 1.00 20.72  ? 590  ASN   A OD1  1 
ATOM   8358  N ND2  . ASN   A  1 564 ? 33.806 4.148   -45.924 1.00 19.99  ? 590  ASN   A ND2  1 
ATOM   8359  H H    . ASN   A  1 564 ? 32.843 1.353   -50.200 0.00 16.80  ? 590  ASN   A H    1 
ATOM   8360  H HA   . ASN   A  1 564 ? 33.993 4.047   -49.784 0.00 16.46  ? 590  ASN   A HA   1 
ATOM   8361  H HB2  . ASN   A  1 564 ? 32.419 3.215   -48.051 0.00 15.75  ? 590  ASN   A HB2  1 
ATOM   8362  H HB3  . ASN   A  1 564 ? 33.579 1.906   -47.692 0.00 15.52  ? 590  ASN   A HB3  1 
ATOM   8363  H HD21 . ASN   A  1 564 ? 34.340 4.721   -45.280 0.00 19.33  ? 590  ASN   A HD21 1 
ATOM   8364  N N    . LEU   A  1 565 ? 36.197 3.174   -50.410 1.00 17.11  ? 591  LEU   A N    1 
ATOM   8365  C CA   . LEU   A  1 565 ? 37.594 2.807   -50.632 1.00 17.50  ? 591  LEU   A CA   1 
ATOM   8366  C C    . LEU   A  1 565 ? 38.516 3.576   -49.674 1.00 17.69  ? 591  LEU   A C    1 
ATOM   8367  O O    . LEU   A  1 565 ? 39.691 3.733   -49.997 1.00 18.44  ? 591  LEU   A O    1 
ATOM   8368  C CB   . LEU   A  1 565 ? 38.005 3.138   -52.087 1.00 18.16  ? 591  LEU   A CB   1 
ATOM   8369  C CG   . LEU   A  1 565 ? 37.156 2.505   -53.180 1.00 20.26  ? 591  LEU   A CG   1 
ATOM   8370  C CD1  . LEU   A  1 565 ? 37.606 2.948   -54.559 1.00 21.16  ? 591  LEU   A CD1  1 
ATOM   8371  C CD2  . LEU   A  1 565 ? 37.195 0.972   -53.091 1.00 21.43  ? 591  LEU   A CD2  1 
ATOM   8372  H H    . LEU   A  1 565 ? 35.972 4.083   -50.804 0.00 16.68  ? 591  LEU   A H    1 
ATOM   8373  H HA   . LEU   A  1 565 ? 37.749 1.743   -50.461 0.00 16.93  ? 591  LEU   A HA   1 
ATOM   8374  H HB2  . LEU   A  1 565 ? 37.966 4.217   -52.222 0.00 18.10  ? 591  LEU   A HB2  1 
ATOM   8375  H HB3  . LEU   A  1 565 ? 39.023 2.787   -52.253 0.00 18.04  ? 591  LEU   A HB3  1 
ATOM   8376  H HG   . LEU   A  1 565 ? 36.131 2.843   -53.050 0.00 20.93  ? 591  LEU   A HG   1 
ATOM   8377  H HD11 . LEU   A  1 565 ? 36.917 2.548   -55.302 0.00 22.50  ? 591  LEU   A HD11 1 
ATOM   8378  H HD12 . LEU   A  1 565 ? 37.607 4.036   -54.600 0.00 22.28  ? 591  LEU   A HD12 1 
ATOM   8379  H HD13 . LEU   A  1 565 ? 38.609 2.569   -54.742 0.00 22.23  ? 591  LEU   A HD13 1 
ATOM   8380  H HD21 . LEU   A  1 565 ? 36.729 0.556   -53.984 0.00 22.55  ? 591  LEU   A HD21 1 
ATOM   8381  H HD22 . LEU   A  1 565 ? 38.232 0.648   -53.028 0.00 22.22  ? 591  LEU   A HD22 1 
ATOM   8382  H HD23 . LEU   A  1 565 ? 36.646 0.648   -52.208 0.00 22.12  ? 591  LEU   A HD23 1 
ATOM   8383  N N    . SER   A  1 566 ? 38.022 4.040   -48.508 1.00 17.24  ? 592  SER   A N    1 
ATOM   8384  C CA   . SER   A  1 566 ? 38.835 4.851   -47.613 1.00 17.62  ? 592  SER   A CA   1 
ATOM   8385  C C    . SER   A  1 566 ? 40.052 4.148   -47.005 1.00 17.16  ? 592  SER   A C    1 
ATOM   8386  O O    . SER   A  1 566 ? 40.056 2.925   -46.809 1.00 16.41  ? 592  SER   A O    1 
ATOM   8387  C CB   . SER   A  1 566 ? 37.996 5.458   -46.487 1.00 19.13  ? 592  SER   A CB   1 
ATOM   8388  O OG   . SER   A  1 566 ? 37.665 4.527   -45.463 1.00 20.48  ? 592  SER   A OG   1 
ATOM   8389  H H    . SER   A  1 566 ? 37.088 3.856   -48.155 0.00 16.23  ? 592  SER   A H    1 
ATOM   8390  H HA   . SER   A  1 566 ? 39.211 5.687   -48.201 0.00 16.68  ? 592  SER   A HA   1 
ATOM   8391  H HB2  . SER   A  1 566 ? 38.561 6.277   -46.044 0.00 18.22  ? 592  SER   A HB2  1 
ATOM   8392  H HB3  . SER   A  1 566 ? 37.072 5.844   -46.914 0.00 18.39  ? 592  SER   A HB3  1 
ATOM   8393  H HG   . SER   A  1 566 ? 37.427 3.650   -45.861 0.00 19.73  ? 592  SER   A HG   1 
ATOM   8394  N N    . HIS   A  1 567 ? 41.095 4.951   -46.736 1.00 16.68  ? 593  HIS   A N    1 
ATOM   8395  C CA   . HIS   A  1 567 ? 42.312 4.521   -46.057 1.00 16.67  ? 593  HIS   A CA   1 
ATOM   8396  C C    . HIS   A  1 567 ? 42.940 3.289   -46.683 1.00 16.75  ? 593  HIS   A C    1 
ATOM   8397  O O    . HIS   A  1 567 ? 43.378 2.372   -45.987 1.00 17.34  ? 593  HIS   A O    1 
ATOM   8398  C CB   . HIS   A  1 567 ? 42.010 4.320   -44.570 1.00 18.20  ? 593  HIS   A CB   1 
ATOM   8399  C CG   . HIS   A  1 567 ? 41.454 5.564   -43.946 1.00 21.33  ? 593  HIS   A CG   1 
ATOM   8400  N ND1  . HIS   A  1 567 ? 42.265 6.646   -43.654 1.00 23.46  ? 593  HIS   A ND1  1 
ATOM   8401  C CD2  . HIS   A  1 567 ? 40.176 5.886   -43.644 1.00 22.48  ? 593  HIS   A CD2  1 
ATOM   8402  C CE1  . HIS   A  1 567 ? 41.460 7.583   -43.174 1.00 24.06  ? 593  HIS   A CE1  1 
ATOM   8403  N NE2  . HIS   A  1 567 ? 40.198 7.161   -43.134 1.00 23.96  ? 593  HIS   A NE2  1 
ATOM   8404  H H    . HIS   A  1 567 ? 41.119 5.936   -46.981 0.00 15.35  ? 593  HIS   A H    1 
ATOM   8405  H HA   . HIS   A  1 567 ? 43.040 5.328   -46.133 0.00 15.23  ? 593  HIS   A HA   1 
ATOM   8406  H HB2  . HIS   A  1 567 ? 41.283 3.518   -44.449 0.00 16.75  ? 593  HIS   A HB2  1 
ATOM   8407  H HB3  . HIS   A  1 567 ? 42.931 4.073   -44.045 0.00 16.77  ? 593  HIS   A HB3  1 
ATOM   8408  H HD2  . HIS   A  1 567 ? 39.307 5.261   -43.780 0.00 21.87  ? 593  HIS   A HD2  1 
ATOM   8409  H HE1  . HIS   A  1 567 ? 41.783 8.561   -42.856 0.00 23.95  ? 593  HIS   A HE1  1 
ATOM   8410  H HE2  . HIS   A  1 567 ? 39.400 7.686   -42.791 0.00 23.73  ? 593  HIS   A HE2  1 
ATOM   8411  N N    . ASN   A  1 568 ? 42.986 3.290   -48.006 1.00 16.18  ? 594  ASN   A N    1 
ATOM   8412  C CA   . ASN   A  1 568 ? 43.604 2.227   -48.781 1.00 16.92  ? 594  ASN   A CA   1 
ATOM   8413  C C    . ASN   A  1 568 ? 44.956 2.642   -49.359 1.00 18.05  ? 594  ASN   A C    1 
ATOM   8414  O O    . ASN   A  1 568 ? 45.628 1.790   -49.936 1.00 18.78  ? 594  ASN   A O    1 
ATOM   8415  C CB   . ASN   A  1 568 ? 42.663 1.760   -49.884 1.00 16.87  ? 594  ASN   A CB   1 
ATOM   8416  C CG   . ASN   A  1 568 ? 41.706 0.721   -49.387 1.00 19.03  ? 594  ASN   A CG   1 
ATOM   8417  O OD1  . ASN   A  1 568 ? 42.143 -0.198  -48.733 1.00 20.84  ? 594  ASN   A OD1  1 
ATOM   8418  N ND2  . ASN   A  1 568 ? 40.427 0.804   -49.682 1.00 17.58  ? 594  ASN   A ND2  1 
ATOM   8419  H H    . ASN   A  1 568 ? 42.624 4.041   -48.585 0.00 14.94  ? 594  ASN   A H    1 
ATOM   8420  H HA   . ASN   A  1 568 ? 43.856 1.400   -48.117 0.00 15.81  ? 594  ASN   A HA   1 
ATOM   8421  H HB2  . ASN   A  1 568 ? 42.114 2.603   -50.301 0.00 16.05  ? 594  ASN   A HB2  1 
ATOM   8422  H HB3  . ASN   A  1 568 ? 43.245 1.260   -50.657 0.00 16.17  ? 594  ASN   A HB3  1 
ATOM   8423  H HD21 . ASN   A  1 568 ? 39.783 0.098   -49.339 0.00 16.78  ? 594  ASN   A HD21 1 
ATOM   8424  H HD22 . ASN   A  1 568 ? 40.077 1.573   -50.246 0.00 16.91  ? 594  ASN   A HD22 1 
ATOM   8425  N N    . ASN   A  1 569 ? 45.379 3.925   -49.209 1.00 18.03  ? 595  ASN   A N    1 
ATOM   8426  C CA   . ASN   A  1 569 ? 46.672 4.389   -49.718 1.00 18.82  ? 595  ASN   A CA   1 
ATOM   8427  C C    . ASN   A  1 569 ? 46.792 4.117   -51.232 1.00 17.90  ? 595  ASN   A C    1 
ATOM   8428  O O    . ASN   A  1 569 ? 47.868 3.763   -51.706 1.00 18.61  ? 595  ASN   A O    1 
ATOM   8429  C CB   . ASN   A  1 569 ? 47.808 3.683   -48.917 1.00 23.02  ? 595  ASN   A CB   1 
ATOM   8430  C CG   . ASN   A  1 569 ? 48.668 4.604   -48.102 1.00 33.36  ? 595  ASN   A CG   1 
ATOM   8431  O OD1  . ASN   A  1 569 ? 48.165 5.439   -47.328 1.00 37.22  ? 595  ASN   A OD1  1 
ATOM   8432  N ND2  . ASN   A  1 569 ? 49.980 4.514   -48.261 1.00 35.66  ? 595  ASN   A ND2  1 
ATOM   8433  H H    . ASN   A  1 569 ? 44.857 4.664   -48.751 0.00 17.30  ? 595  ASN   A H    1 
ATOM   8434  H HA   . ASN   A  1 569 ? 46.716 5.470   -49.588 0.00 18.54  ? 595  ASN   A HA   1 
ATOM   8435  H HB2  . ASN   A  1 569 ? 47.345 3.036   -48.176 0.00 23.40  ? 595  ASN   A HB2  1 
ATOM   8436  H HB3  . ASN   A  1 569 ? 48.438 3.080   -49.569 0.00 23.73  ? 595  ASN   A HB3  1 
ATOM   8437  H HD21 . ASN   A  1 569 ? 50.589 5.127   -47.728 0.00 38.94  ? 595  ASN   A HD21 1 
ATOM   8438  H HD22 . ASN   A  1 569 ? 50.386 3.890   -48.950 0.00 39.05  ? 595  ASN   A HD22 1 
ATOM   8439  N N    . ILE   A  1 570 ? 45.680 4.267   -51.973 1.00 16.28  ? 596  ILE   A N    1 
ATOM   8440  C CA   . ILE   A  1 570 ? 45.656 4.011   -53.412 1.00 16.38  ? 596  ILE   A CA   1 
ATOM   8441  C C    . ILE   A  1 570 ? 46.432 5.112   -54.132 1.00 16.60  ? 596  ILE   A C    1 
ATOM   8442  O O    . ILE   A  1 570 ? 46.086 6.284   -54.006 1.00 16.10  ? 596  ILE   A O    1 
ATOM   8443  C CB   . ILE   A  1 570 ? 44.192 3.937   -53.954 1.00 16.39  ? 596  ILE   A CB   1 
ATOM   8444  C CG1  . ILE   A  1 570 ? 43.413 2.771   -53.267 1.00 16.59  ? 596  ILE   A CG1  1 
ATOM   8445  C CG2  . ILE   A  1 570 ? 44.193 3.798   -55.501 1.00 16.33  ? 596  ILE   A CG2  1 
ATOM   8446  C CD1  . ILE   A  1 570 ? 41.874 2.734   -53.485 1.00 17.67  ? 596  ILE   A CD1  1 
ATOM   8447  H H    . ILE   A  1 570 ? 44.790 4.592   -51.610 0.00 15.69  ? 596  ILE   A H    1 
ATOM   8448  H HA   . ILE   A  1 570 ? 46.128 3.050   -53.612 0.00 16.30  ? 596  ILE   A HA   1 
ATOM   8449  H HB   . ILE   A  1 570 ? 43.690 4.871   -53.704 0.00 16.22  ? 596  ILE   A HB   1 
ATOM   8450  H HG12 . ILE   A  1 570 ? 43.821 1.822   -53.613 0.00 16.45  ? 596  ILE   A HG12 1 
ATOM   8451  H HG13 . ILE   A  1 570 ? 43.564 2.871   -52.195 0.00 16.12  ? 596  ILE   A HG13 1 
ATOM   8452  H HG21 . ILE   A  1 570 ? 43.236 3.407   -55.841 0.00 16.62  ? 596  ILE   A HG21 1 
ATOM   8453  H HG22 . ILE   A  1 570 ? 44.351 4.778   -55.949 0.00 16.69  ? 596  ILE   A HG22 1 
ATOM   8454  H HG23 . ILE   A  1 570 ? 44.996 3.123   -55.793 0.00 16.67  ? 596  ILE   A HG23 1 
ATOM   8455  H HD11 . ILE   A  1 570 ? 41.437 2.036   -52.772 0.00 17.51  ? 596  ILE   A HD11 1 
ATOM   8456  H HD12 . ILE   A  1 570 ? 41.471 3.733   -53.324 0.00 17.64  ? 596  ILE   A HD12 1 
ATOM   8457  H HD13 . ILE   A  1 570 ? 41.656 2.400   -54.498 0.00 17.91  ? 596  ILE   A HD13 1 
ATOM   8458  N N    . TYR   A  1 571 ? 47.499 4.734   -54.842 1.00 17.36  ? 597  TYR   A N    1 
ATOM   8459  C CA   . TYR   A  1 571 ? 48.296 5.670   -55.636 1.00 17.40  ? 597  TYR   A CA   1 
ATOM   8460  C C    . TYR   A  1 571 ? 48.684 5.142   -57.002 1.00 17.10  ? 597  TYR   A C    1 
ATOM   8461  O O    . TYR   A  1 571 ? 49.287 5.889   -57.754 1.00 16.77  ? 597  TYR   A O    1 
ATOM   8462  C CB   . TYR   A  1 571 ? 49.572 6.099   -54.896 1.00 18.10  ? 597  TYR   A CB   1 
ATOM   8463  C CG   . TYR   A  1 571 ? 50.654 5.049   -54.782 1.00 19.13  ? 597  TYR   A CG   1 
ATOM   8464  C CD1  . TYR   A  1 571 ? 50.571 4.052   -53.824 1.00 19.56  ? 597  TYR   A CD1  1 
ATOM   8465  C CD2  . TYR   A  1 571 ? 51.853 5.182   -55.473 1.00 20.24  ? 597  TYR   A CD2  1 
ATOM   8466  C CE1  . TYR   A  1 571 ? 51.618 3.177   -53.596 1.00 20.59  ? 597  TYR   A CE1  1 
ATOM   8467  C CE2  . TYR   A  1 571 ? 52.918 4.310   -55.250 1.00 21.07  ? 597  TYR   A CE2  1 
ATOM   8468  C CZ   . TYR   A  1 571 ? 52.798 3.316   -54.295 1.00 21.74  ? 597  TYR   A CZ   1 
ATOM   8469  O OH   . TYR   A  1 571 ? 53.834 2.470   -54.004 1.00 23.27  ? 597  TYR   A OH   1 
ATOM   8470  H H    . TYR   A  1 571 ? 47.870 3.789   -54.832 0.00 17.87  ? 597  TYR   A H    1 
ATOM   8471  H HA   . TYR   A  1 571 ? 47.715 6.574   -55.800 0.00 18.20  ? 597  TYR   A HA   1 
ATOM   8472  H HB2  . TYR   A  1 571 ? 49.989 6.988   -55.365 0.00 19.18  ? 597  TYR   A HB2  1 
ATOM   8473  H HB3  . TYR   A  1 571 ? 49.317 6.296   -53.858 0.00 18.75  ? 597  TYR   A HB3  1 
ATOM   8474  H HD1  . TYR   A  1 571 ? 49.672 3.961   -53.236 0.00 20.38  ? 597  TYR   A HD1  1 
ATOM   8475  H HD2  . TYR   A  1 571 ? 51.970 5.984   -56.183 0.00 22.17  ? 597  TYR   A HD2  1 
ATOM   8476  H HE1  . TYR   A  1 571 ? 51.514 2.406   -52.852 0.00 21.82  ? 597  TYR   A HE1  1 
ATOM   8477  H HE2  . TYR   A  1 571 ? 53.837 4.426   -55.799 0.00 23.37  ? 597  TYR   A HE2  1 
ATOM   8478  H HH   . TYR   A  1 571 ? 53.657 1.958   -53.171 0.00 25.50  ? 597  TYR   A HH   1 
ATOM   8479  N N    . THR   A  1 572 ? 48.386 3.870   -57.326 1.00 16.96  ? 598  THR   A N    1 
ATOM   8480  C CA   . THR   A  1 572 ? 48.746 3.294   -58.614 1.00 17.23  ? 598  THR   A CA   1 
ATOM   8481  C C    . THR   A  1 572 ? 47.823 2.123   -58.919 1.00 18.23  ? 598  THR   A C    1 
ATOM   8482  O O    . THR   A  1 572 ? 47.530 1.316   -58.028 1.00 18.79  ? 598  THR   A O    1 
ATOM   8483  C CB   . THR   A  1 572 ? 50.239 2.874   -58.637 1.00 17.83  ? 598  THR   A CB   1 
ATOM   8484  O OG1  . THR   A  1 572 ? 50.545 2.310   -59.921 1.00 18.61  ? 598  THR   A OG1  1 
ATOM   8485  C CG2  . THR   A  1 572 ? 50.599 1.875   -57.536 1.00 17.92  ? 598  THR   A CG2  1 
ATOM   8486  H H    . THR   A  1 572 ? 47.915 3.211   -56.713 0.00 17.85  ? 598  THR   A H    1 
ATOM   8487  H HA   . THR   A  1 572 ? 48.602 4.044   -59.390 0.00 18.93  ? 598  THR   A HA   1 
ATOM   8488  H HB   . THR   A  1 572 ? 50.852 3.762   -58.492 0.00 19.67  ? 598  THR   A HB   1 
ATOM   8489  H HG1  . THR   A  1 572 ? 51.499 2.040   -59.954 0.00 21.14  ? 598  THR   A HG1  1 
ATOM   8490  H HG21 . THR   A  1 572 ? 51.673 1.698   -57.570 0.00 19.71  ? 598  THR   A HG21 1 
ATOM   8491  H HG22 . THR   A  1 572 ? 50.343 2.272   -56.555 0.00 19.26  ? 598  THR   A HG22 1 
ATOM   8492  H HG23 . THR   A  1 572 ? 50.085 0.927   -57.687 0.00 19.57  ? 598  THR   A HG23 1 
ATOM   8493  N N    . LEU   A  1 573 ? 47.350 2.053   -60.170 1.00 18.91  ? 599  LEU   A N    1 
ATOM   8494  C CA   . LEU   A  1 573 ? 46.490 0.988   -60.677 1.00 19.58  ? 599  LEU   A CA   1 
ATOM   8495  C C    . LEU   A  1 573 ? 47.127 0.407   -61.957 1.00 20.67  ? 599  LEU   A C    1 
ATOM   8496  O O    . LEU   A  1 573 ? 47.925 1.081   -62.629 1.00 20.88  ? 599  LEU   A O    1 
ATOM   8497  C CB   . LEU   A  1 573 ? 45.068 1.511   -60.973 1.00 19.58  ? 599  LEU   A CB   1 
ATOM   8498  C CG   . LEU   A  1 573 ? 44.272 2.072   -59.765 1.00 19.90  ? 599  LEU   A CG   1 
ATOM   8499  C CD1  . LEU   A  1 573 ? 42.924 2.598   -60.202 1.00 20.04  ? 599  LEU   A CD1  1 
ATOM   8500  C CD2  . LEU   A  1 573 ? 44.048 1.016   -58.681 1.00 20.24  ? 599  LEU   A CD2  1 
ATOM   8501  H H    . LEU   A  1 573 ? 47.555 2.745   -60.883 0.00 21.31  ? 599  LEU   A H    1 
ATOM   8502  H HA   . LEU   A  1 573 ? 46.417 0.176   -59.960 0.00 21.89  ? 599  LEU   A HA   1 
ATOM   8503  H HB2  . LEU   A  1 573 ? 45.145 2.313   -61.707 0.00 22.26  ? 599  LEU   A HB2  1 
ATOM   8504  H HB3  . LEU   A  1 573 ? 44.483 0.694   -61.394 0.00 22.21  ? 599  LEU   A HB3  1 
ATOM   8505  H HG   . LEU   A  1 573 ? 44.831 2.896   -59.325 0.00 21.90  ? 599  LEU   A HG   1 
ATOM   8506  H HD11 . LEU   A  1 573 ? 42.420 3.049   -59.350 0.00 22.05  ? 599  LEU   A HD11 1 
ATOM   8507  H HD12 . LEU   A  1 573 ? 43.074 3.343   -60.984 0.00 22.54  ? 599  LEU   A HD12 1 
ATOM   8508  H HD13 . LEU   A  1 573 ? 42.330 1.772   -60.591 0.00 22.46  ? 599  LEU   A HD13 1 
ATOM   8509  H HD21 . LEU   A  1 573 ? 43.372 1.420   -57.928 0.00 21.91  ? 599  LEU   A HD21 1 
ATOM   8510  H HD22 . LEU   A  1 573 ? 43.611 0.126   -59.132 0.00 22.32  ? 599  LEU   A HD22 1 
ATOM   8511  H HD23 . LEU   A  1 573 ? 45.002 0.771   -58.216 0.00 22.06  ? 599  LEU   A HD23 1 
ATOM   8512  N N    . THR   A  1 574 ? 46.818 -0.864  -62.244 1.00 20.88  ? 600  THR   A N    1 
ATOM   8513  C CA   . THR   A  1 574 ? 47.360 -1.578  -63.390 1.00 22.39  ? 600  THR   A CA   1 
ATOM   8514  C C    . THR   A  1 574 ? 46.392 -1.506  -64.571 1.00 24.44  ? 600  THR   A C    1 
ATOM   8515  O O    . THR   A  1 574 ? 45.250 -1.928  -64.417 1.00 25.21  ? 600  THR   A O    1 
ATOM   8516  C CB   . THR   A  1 574 ? 47.588 -3.057  -63.016 1.00 22.52  ? 600  THR   A CB   1 
ATOM   8517  O OG1  . THR   A  1 574 ? 48.394 -3.114  -61.843 1.00 22.70  ? 600  THR   A OG1  1 
ATOM   8518  C CG2  . THR   A  1 574 ? 48.288 -3.834  -64.129 1.00 22.13  ? 600  THR   A CG2  1 
ATOM   8519  H H    . THR   A  1 574 ? 46.182 -1.427  -61.689 0.00 24.10  ? 600  THR   A H    1 
ATOM   8520  H HA   . THR   A  1 574 ? 48.321 -1.160  -63.684 0.00 26.70  ? 600  THR   A HA   1 
ATOM   8521  H HB   . THR   A  1 574 ? 46.632 -3.536  -62.813 0.00 26.72  ? 600  THR   A HB   1 
ATOM   8522  H HG1  . THR   A  1 574 ? 49.268 -2.673  -62.009 0.00 26.78  ? 600  THR   A HG1  1 
ATOM   8523  H HG21 . THR   A  1 574 ? 48.657 -4.782  -63.739 0.00 26.90  ? 600  THR   A HG21 1 
ATOM   8524  H HG22 . THR   A  1 574 ? 47.595 -4.044  -64.943 0.00 27.12  ? 600  THR   A HG22 1 
ATOM   8525  H HG23 . THR   A  1 574 ? 49.128 -3.259  -64.517 0.00 26.99  ? 600  THR   A HG23 1 
ATOM   8526  N N    . ASP   A  1 575 ? 46.852 -0.999  -65.731 1.00 25.04  ? 601  ASP   A N    1 
ATOM   8527  C CA   . ASP   A  1 575 ? 46.097 -0.929  -67.003 1.00 26.66  ? 601  ASP   A CA   1 
ATOM   8528  C C    . ASP   A  1 575 ? 44.817 -0.046  -66.997 1.00 27.50  ? 601  ASP   A C    1 
ATOM   8529  O O    . ASP   A  1 575 ? 44.714 0.844   -67.842 1.00 28.27  ? 601  ASP   A O    1 
ATOM   8530  C CB   . ASP   A  1 575 ? 45.726 -2.336  -67.506 1.00 28.25  ? 601  ASP   A CB   1 
ATOM   8531  C CG   . ASP   A  1 575 ? 46.908 -3.254  -67.723 1.00 31.91  ? 601  ASP   A CG   1 
ATOM   8532  O OD1  . ASP   A  1 575 ? 48.018 -2.740  -68.010 1.00 32.58  ? 601  ASP   A OD1  1 
ATOM   8533  O OD2  . ASP   A  1 575 ? 46.720 -4.486  -67.630 1.00 33.94  ? 601  ASP   A OD2  1 
ATOM   8534  H H    . ASP   A  1 575 ? 47.783 -0.607  -65.829 0.00 30.54  ? 601  ASP   A H    1 
ATOM   8535  H HA   . ASP   A  1 575 ? 46.784 -0.515  -67.740 0.00 33.15  ? 601  ASP   A HA   1 
ATOM   8536  H HB2  . ASP   A  1 575 ? 45.063 -2.810  -66.784 0.00 34.86  ? 601  ASP   A HB2  1 
ATOM   8537  H HB3  . ASP   A  1 575 ? 45.211 -2.237  -68.461 0.00 35.47  ? 601  ASP   A HB3  1 
ATOM   8538  N N    . LYS   A  1 576 ? 43.824 -0.330  -66.128 1.00 27.02  ? 602  LYS   A N    1 
ATOM   8539  C CA   . LYS   A  1 576 ? 42.606 0.473   -66.086 1.00 27.15  ? 602  LYS   A CA   1 
ATOM   8540  C C    . LYS   A  1 576 ? 42.775 1.487   -64.974 1.00 25.75  ? 602  LYS   A C    1 
ATOM   8541  O O    . LYS   A  1 576 ? 42.863 1.137   -63.791 1.00 26.19  ? 602  LYS   A O    1 
ATOM   8542  C CB   . LYS   A  1 576 ? 41.325 -0.367  -65.901 1.00 29.91  ? 602  LYS   A CB   1 
ATOM   8543  C CG   . LYS   A  1 576 ? 40.050 0.394   -66.328 1.00 35.75  ? 602  LYS   A CG   1 
ATOM   8544  C CD   . LYS   A  1 576 ? 38.801 -0.476  -66.206 1.00 41.85  ? 602  LYS   A CD   1 
ATOM   8545  C CE   . LYS   A  1 576 ? 37.610 -0.020  -67.017 1.00 46.59  ? 602  LYS   A CE   1 
ATOM   8546  N NZ   . LYS   A  1 576 ? 36.750 0.935   -66.286 1.00 49.47  ? 602  LYS   A NZ   1 
ATOM   8547  H H    . LYS   A  1 576 ? 43.843 -1.096  -65.462 0.00 32.68  ? 602  LYS   A H    1 
ATOM   8548  H HA   . LYS   A  1 576 ? 42.514 0.993   -67.038 0.00 33.30  ? 602  LYS   A HA   1 
ATOM   8549  H HB2  . LYS   A  1 576 ? 41.403 -1.263  -66.514 0.00 36.62  ? 602  LYS   A HB2  1 
ATOM   8550  H HB3  . LYS   A  1 576 ? 41.219 -0.643  -64.853 0.00 35.93  ? 602  LYS   A HB3  1 
ATOM   8551  H HG2  . LYS   A  1 576 ? 39.921 1.264   -65.686 0.00 43.19  ? 602  LYS   A HG2  1 
ATOM   8552  H HG3  . LYS   A  1 576 ? 40.158 0.706   -67.365 0.00 43.87  ? 602  LYS   A HG3  1 
ATOM   8553  H HD2  . LYS   A  1 576 ? 39.047 -1.485  -66.532 0.00 51.11  ? 602  LYS   A HD2  1 
ATOM   8554  H HD3  . LYS   A  1 576 ? 38.506 -0.494  -65.159 0.00 50.51  ? 602  LYS   A HD3  1 
ATOM   8555  H HE2  . LYS   A  1 576 ? 37.951 0.465   -67.930 0.00 57.31  ? 602  LYS   A HE2  1 
ATOM   8556  H HE3  . LYS   A  1 576 ? 37.003 -0.889  -67.266 0.00 57.19  ? 602  LYS   A HE3  1 
ATOM   8557  H HZ1  . LYS   A  1 576 ? 35.796 0.840   -66.617 0.00 60.37  ? 602  LYS   A HZ1  1 
ATOM   8558  H HZ2  . LYS   A  1 576 ? 36.765 0.765   -65.286 0.00 59.75  ? 602  LYS   A HZ2  1 
ATOM   8559  H HZ3  . LYS   A  1 576 ? 37.079 1.878   -66.466 0.00 60.20  ? 602  LYS   A HZ3  1 
ATOM   8560  N N    . TYR   A  1 577 ? 42.903 2.736   -65.361 1.00 24.43  ? 603  TYR   A N    1 
ATOM   8561  C CA   . TYR   A  1 577 ? 43.152 3.829   -64.422 1.00 24.90  ? 603  TYR   A CA   1 
ATOM   8562  C C    . TYR   A  1 577 ? 41.868 4.502   -63.901 1.00 25.48  ? 603  TYR   A C    1 
ATOM   8563  O O    . TYR   A  1 577 ? 41.944 5.308   -62.963 1.00 25.61  ? 603  TYR   A O    1 
ATOM   8564  C CB   . TYR   A  1 577 ? 44.035 4.870   -65.124 1.00 24.57  ? 603  TYR   A CB   1 
ATOM   8565  C CG   . TYR   A  1 577 ? 45.312 4.282   -65.684 1.00 25.23  ? 603  TYR   A CG   1 
ATOM   8566  C CD1  . TYR   A  1 577 ? 46.199 3.601   -64.868 1.00 26.28  ? 603  TYR   A CD1  1 
ATOM   8567  C CD2  . TYR   A  1 577 ? 45.614 4.377   -67.038 1.00 26.40  ? 603  TYR   A CD2  1 
ATOM   8568  C CE1  . TYR   A  1 577 ? 47.391 3.090   -65.363 1.00 27.10  ? 603  TYR   A CE1  1 
ATOM   8569  C CE2  . TYR   A  1 577 ? 46.801 3.862   -67.549 1.00 27.39  ? 603  TYR   A CE2  1 
ATOM   8570  C CZ   . TYR   A  1 577 ? 47.702 3.242   -66.700 1.00 28.43  ? 603  TYR   A CZ   1 
ATOM   8571  O OH   . TYR   A  1 577 ? 48.859 2.681   -67.194 1.00 29.82  ? 603  TYR   A OH   1 
ATOM   8572  H H    . TYR   A  1 577 ? 42.823 3.049   -66.323 0.00 29.68  ? 603  TYR   A H    1 
ATOM   8573  H HA   . TYR   A  1 577 ? 43.705 3.464   -63.558 0.00 29.22  ? 603  TYR   A HA   1 
ATOM   8574  H HB2  . TYR   A  1 577 ? 43.472 5.316   -65.943 0.00 29.69  ? 603  TYR   A HB2  1 
ATOM   8575  H HB3  . TYR   A  1 577 ? 44.310 5.639   -64.404 0.00 29.13  ? 603  TYR   A HB3  1 
ATOM   8576  H HD1  . TYR   A  1 577 ? 45.989 3.522   -63.814 0.00 31.00  ? 603  TYR   A HD1  1 
ATOM   8577  H HD2  . TYR   A  1 577 ? 44.943 4.899   -67.699 0.00 32.55  ? 603  TYR   A HD2  1 
ATOM   8578  H HE1  . TYR   A  1 577 ? 48.069 2.588   -64.694 0.00 32.43  ? 603  TYR   A HE1  1 
ATOM   8579  H HE2  . TYR   A  1 577 ? 47.028 3.965   -68.597 0.00 34.14  ? 603  TYR   A HE2  1 
ATOM   8580  H HH   . TYR   A  1 577 ? 49.311 2.126   -66.505 0.00 36.45  ? 603  TYR   A HH   1 
ATOM   8581  N N    . ASN   A  1 578 ? 40.701 4.146   -64.477 1.00 25.06  ? 604  ASN   A N    1 
ATOM   8582  C CA   . ASN   A  1 578 ? 39.423 4.748   -64.163 1.00 24.63  ? 604  ASN   A CA   1 
ATOM   8583  C C    . ASN   A  1 578 ? 38.447 3.868   -63.412 1.00 24.77  ? 604  ASN   A C    1 
ATOM   8584  O O    . ASN   A  1 578 ? 38.370 2.664   -63.651 1.00 25.03  ? 604  ASN   A O    1 
ATOM   8585  C CB   . ASN   A  1 578 ? 38.773 5.216   -65.459 1.00 25.35  ? 604  ASN   A CB   1 
ATOM   8586  C CG   . ASN   A  1 578 ? 39.589 6.257   -66.200 1.00 28.91  ? 604  ASN   A CG   1 
ATOM   8587  O OD1  . ASN   A  1 578 ? 40.218 7.131   -65.600 1.00 29.32  ? 604  ASN   A OD1  1 
ATOM   8588  N ND2  . ASN   A  1 578 ? 39.591 6.208   -67.524 1.00 29.95  ? 604  ASN   A ND2  1 
ATOM   8589  H H    . ASN   A  1 578 ? 40.608 3.422   -65.181 0.00 30.08  ? 604  ASN   A H    1 
ATOM   8590  H HA   . ASN   A  1 578 ? 39.600 5.617   -63.537 0.00 29.07  ? 604  ASN   A HA   1 
ATOM   8591  H HB2  . ASN   A  1 578 ? 38.635 4.353   -66.109 0.00 30.93  ? 604  ASN   A HB2  1 
ATOM   8592  H HB3  . ASN   A  1 578 ? 37.805 5.658   -65.225 0.00 30.70  ? 604  ASN   A HB3  1 
ATOM   8593  H HD21 . ASN   A  1 578 ? 40.126 6.890   -68.050 0.00 37.18  ? 604  ASN   A HD21 1 
ATOM   8594  H HD22 . ASN   A  1 578 ? 39.058 5.499   -68.017 0.00 37.20  ? 604  ASN   A HD22 1 
ATOM   8595  N N    . LEU   A  1 579 ? 37.683 4.496   -62.499 1.00 23.83  ? 605  LEU   A N    1 
ATOM   8596  C CA   . LEU   A  1 579 ? 36.589 3.859   -61.782 1.00 23.45  ? 605  LEU   A CA   1 
ATOM   8597  C C    . LEU   A  1 579 ? 35.339 4.141   -62.592 1.00 23.31  ? 605  LEU   A C    1 
ATOM   8598  O O    . LEU   A  1 579 ? 35.120 5.281   -63.008 1.00 24.68  ? 605  LEU   A O    1 
ATOM   8599  C CB   . LEU   A  1 579 ? 36.436 4.417   -60.362 1.00 24.03  ? 605  LEU   A CB   1 
ATOM   8600  C CG   . LEU   A  1 579 ? 37.678 4.390   -59.459 1.00 26.25  ? 605  LEU   A CG   1 
ATOM   8601  C CD1  . LEU   A  1 579 ? 37.303 4.768   -58.038 1.00 26.39  ? 605  LEU   A CD1  1 
ATOM   8602  C CD2  . LEU   A  1 579 ? 38.371 3.023   -59.479 1.00 27.39  ? 605  LEU   A CD2  1 
ATOM   8603  H H    . LEU   A  1 579 ? 37.790 5.474   -62.251 0.00 27.80  ? 605  LEU   A H    1 
ATOM   8604  H HA   . LEU   A  1 579 ? 36.736 2.782   -61.721 0.00 27.22  ? 605  LEU   A HA   1 
ATOM   8605  H HB2  . LEU   A  1 579 ? 36.120 5.456   -60.440 0.00 27.61  ? 605  LEU   A HB2  1 
ATOM   8606  H HB3  . LEU   A  1 579 ? 35.660 3.842   -59.857 0.00 27.43  ? 605  LEU   A HB3  1 
ATOM   8607  H HG   . LEU   A  1 579 ? 38.390 5.129   -59.824 0.00 29.84  ? 605  LEU   A HG   1 
ATOM   8608  H HD11 . LEU   A  1 579 ? 38.203 4.789   -57.426 0.00 29.30  ? 605  LEU   A HD11 1 
ATOM   8609  H HD12 . LEU   A  1 579 ? 36.840 5.754   -58.048 0.00 29.63  ? 605  LEU   A HD12 1 
ATOM   8610  H HD13 . LEU   A  1 579 ? 36.604 4.031   -57.647 0.00 29.47  ? 605  LEU   A HD13 1 
ATOM   8611  H HD21 . LEU   A  1 579 ? 39.096 2.980   -58.668 0.00 30.77  ? 605  LEU   A HD21 1 
ATOM   8612  H HD22 . LEU   A  1 579 ? 37.620 2.244   -59.356 0.00 31.08  ? 605  LEU   A HD22 1 
ATOM   8613  H HD23 . LEU   A  1 579 ? 38.884 2.899   -60.432 0.00 31.33  ? 605  LEU   A HD23 1 
ATOM   8614  N N    . GLU   A  1 580 ? 34.545 3.110   -62.865 1.00 21.65  ? 606  GLU   A N    1 
ATOM   8615  C CA   . GLU   A  1 580 ? 33.348 3.255   -63.685 1.00 21.41  ? 606  GLU   A CA   1 
ATOM   8616  C C    . GLU   A  1 580 ? 32.171 2.532   -63.073 1.00 21.21  ? 606  GLU   A C    1 
ATOM   8617  O O    . GLU   A  1 580 ? 32.320 1.429   -62.574 1.00 21.07  ? 606  GLU   A O    1 
ATOM   8618  C CB   . GLU   A  1 580 ? 33.617 2.717   -65.107 1.00 22.77  ? 606  GLU   A CB   1 
ATOM   8619  C CG   . GLU   A  1 580 ? 34.847 3.347   -65.734 1.00 29.11  ? 606  GLU   A CG   1 
ATOM   8620  C CD   . GLU   A  1 580 ? 35.038 3.077   -67.206 1.00 38.72  ? 606  GLU   A CD   1 
ATOM   8621  O OE1  . GLU   A  1 580 ? 34.624 1.988   -67.667 1.00 41.76  ? 606  GLU   A OE1  1 
ATOM   8622  O OE2  . GLU   A  1 580 ? 35.630 3.940   -67.894 1.00 41.55  ? 606  GLU   A OE2  1 
ATOM   8623  H H    . GLU   A  1 580 ? 34.695 2.162   -62.535 0.00 25.60  ? 606  GLU   A H    1 
ATOM   8624  H HA   . GLU   A  1 580 ? 33.083 4.306   -63.779 0.00 26.04  ? 606  GLU   A HA   1 
ATOM   8625  H HB2  . GLU   A  1 580 ? 33.777 1.641   -65.055 0.00 28.07  ? 606  GLU   A HB2  1 
ATOM   8626  H HB3  . GLU   A  1 580 ? 32.759 2.938   -65.740 0.00 28.49  ? 606  GLU   A HB3  1 
ATOM   8627  H HG2  . GLU   A  1 580 ? 34.799 4.426   -65.602 0.00 35.70  ? 606  GLU   A HG2  1 
ATOM   8628  H HG3  . GLU   A  1 580 ? 35.727 2.967   -65.217 0.00 35.42  ? 606  GLU   A HG3  1 
ATOM   8629  N N    . SER   A  1 581 ? 30.999 3.168   -63.113 1.00 20.60  ? 607  SER   A N    1 
ATOM   8630  C CA   . SER   A  1 581 ? 29.758 2.598   -62.608 1.00 20.24  ? 607  SER   A CA   1 
ATOM   8631  C C    . SER   A  1 581 ? 28.583 3.403   -63.105 1.00 21.63  ? 607  SER   A C    1 
ATOM   8632  O O    . SER   A  1 581 ? 28.525 4.608   -62.844 1.00 21.88  ? 607  SER   A O    1 
ATOM   8633  C CB   . SER   A  1 581 ? 29.712 2.605   -61.082 1.00 20.45  ? 607  SER   A CB   1 
ATOM   8634  O OG   . SER   A  1 581 ? 28.442 2.139   -60.643 1.00 20.90  ? 607  SER   A OG   1 
ATOM   8635  H H    . SER   A  1 581 ? 30.896 4.103   -63.495 0.00 25.38  ? 607  SER   A H    1 
ATOM   8636  H HA   . SER   A  1 581 ? 29.665 1.570   -62.955 0.00 24.99  ? 607  SER   A HA   1 
ATOM   8637  H HB2  . SER   A  1 581 ? 30.487 1.946   -60.696 0.00 24.23  ? 607  SER   A HB2  1 
ATOM   8638  H HB3  . SER   A  1 581 ? 29.868 3.621   -60.722 0.00 24.38  ? 607  SER   A HB3  1 
ATOM   8639  H HG   . SER   A  1 581 ? 28.198 1.303   -61.120 0.00 25.44  ? 607  SER   A HG   1 
ATOM   8640  N N    . LYS   A  1 582 ? 27.612 2.736   -63.737 1.00 22.00  ? 608  LYS   A N    1 
ATOM   8641  C CA   . LYS   A  1 582 ? 26.399 3.417   -64.165 1.00 23.24  ? 608  LYS   A CA   1 
ATOM   8642  C C    . LYS   A  1 582 ? 25.443 3.671   -62.983 1.00 23.80  ? 608  LYS   A C    1 
ATOM   8643  O O    . LYS   A  1 582 ? 24.604 4.559   -63.101 1.00 24.66  ? 608  LYS   A O    1 
ATOM   8644  C CB   . LYS   A  1 582 ? 25.698 2.606   -65.271 1.00 25.22  ? 608  LYS   A CB   1 
ATOM   8645  C CG   . LYS   A  1 582 ? 26.524 2.532   -66.551 1.00 30.96  ? 608  LYS   A CG   1 
ATOM   8646  C CD   . LYS   A  1 582 ? 25.800 1.777   -67.647 1.00 38.09  ? 608  LYS   A CD   1 
ATOM   8647  C CE   . LYS   A  1 582 ? 26.479 1.912   -68.993 1.00 43.02  ? 608  LYS   A CE   1 
ATOM   8648  N NZ   . LYS   A  1 582 ? 25.722 1.189   -70.055 1.00 45.91  ? 608  LYS   A NZ   1 
ATOM   8649  H H    . LYS   A  1 582 ? 27.625 1.744   -63.954 0.00 27.98  ? 608  LYS   A H    1 
ATOM   8650  H HA   . LYS   A  1 582 ? 26.657 4.385   -64.590 0.00 30.03  ? 608  LYS   A HA   1 
ATOM   8651  H HB2  . LYS   A  1 582 ? 25.516 1.591   -64.921 0.00 32.83  ? 608  LYS   A HB2  1 
ATOM   8652  H HB3  . LYS   A  1 582 ? 24.752 3.088   -65.513 0.00 33.32  ? 608  LYS   A HB3  1 
ATOM   8653  H HG2  . LYS   A  1 582 ? 26.722 3.540   -66.910 0.00 40.23  ? 608  LYS   A HG2  1 
ATOM   8654  H HG3  . LYS   A  1 582 ? 27.460 2.015   -66.347 0.00 39.77  ? 608  LYS   A HG3  1 
ATOM   8655  H HD2  . LYS   A  1 582 ? 25.772 0.720   -67.389 0.00 49.27  ? 608  LYS   A HD2  1 
ATOM   8656  H HD3  . LYS   A  1 582 ? 24.787 2.165   -67.738 0.00 49.72  ? 608  LYS   A HD3  1 
ATOM   8657  H HE2  . LYS   A  1 582 ? 26.528 2.965   -69.265 0.00 55.82  ? 608  LYS   A HE2  1 
ATOM   8658  H HE3  . LYS   A  1 582 ? 27.479 1.485   -68.935 0.00 55.40  ? 608  LYS   A HE3  1 
ATOM   8659  H HZ1  . LYS   A  1 582 ? 26.197 1.288   -70.947 0.00 60.20  ? 608  LYS   A HZ1  1 
ATOM   8660  H HZ2  . LYS   A  1 582 ? 25.654 0.203   -69.823 0.00 59.85  ? 608  LYS   A HZ2  1 
ATOM   8661  H HZ3  . LYS   A  1 582 ? 24.786 1.574   -70.135 0.00 60.24  ? 608  LYS   A HZ3  1 
ATOM   8662  N N    . SER   A  1 583 ? 25.579 2.940   -61.850 1.00 23.08  ? 609  SER   A N    1 
ATOM   8663  C CA   . SER   A  1 583 ? 24.674 3.060   -60.703 1.00 23.05  ? 609  SER   A CA   1 
ATOM   8664  C C    . SER   A  1 583 ? 25.182 3.843   -59.489 1.00 22.76  ? 609  SER   A C    1 
ATOM   8665  O O    . SER   A  1 583 ? 24.375 4.423   -58.771 1.00 23.52  ? 609  SER   A O    1 
ATOM   8666  C CB   . SER   A  1 583 ? 24.312 1.660   -60.210 1.00 24.75  ? 609  SER   A CB   1 
ATOM   8667  O OG   . SER   A  1 583 ? 25.471 0.912   -59.867 1.00 25.87  ? 609  SER   A OG   1 
ATOM   8668  H H    . SER   A  1 583 ? 26.303 2.246   -61.696 0.00 28.75  ? 609  SER   A H    1 
ATOM   8669  H HA   . SER   A  1 583 ? 23.743 3.528   -61.019 0.00 29.25  ? 609  SER   A HA   1 
ATOM   8670  H HB2  . SER   A  1 583 ? 23.668 1.750   -59.336 0.00 30.67  ? 609  SER   A HB2  1 
ATOM   8671  H HB3  . SER   A  1 583 ? 23.782 1.137   -61.005 0.00 31.24  ? 609  SER   A HB3  1 
ATOM   8672  H HG   . SER   A  1 583 ? 25.695 1.030   -58.906 0.00 31.27  ? 609  SER   A HG   1 
ATOM   8673  N N    . LEU   A  1 584 ? 26.477 3.759   -59.181 1.00 21.77  ? 610  LEU   A N    1 
ATOM   8674  C CA   . LEU   A  1 584 ? 27.043 4.319   -57.949 1.00 21.50  ? 610  LEU   A CA   1 
ATOM   8675  C C    . LEU   A  1 584 ? 26.612 5.757   -57.639 1.00 21.46  ? 610  LEU   A C    1 
ATOM   8676  O O    . LEU   A  1 584 ? 26.726 6.615   -58.512 1.00 22.04  ? 610  LEU   A O    1 
ATOM   8677  C CB   . LEU   A  1 584 ? 28.582 4.221   -57.965 1.00 21.34  ? 610  LEU   A CB   1 
ATOM   8678  C CG   . LEU   A  1 584 ? 29.271 4.361   -56.592 1.00 22.28  ? 610  LEU   A CG   1 
ATOM   8679  C CD1  . LEU   A  1 584 ? 29.089 3.097   -55.744 1.00 23.38  ? 610  LEU   A CD1  1 
ATOM   8680  C CD2  . LEU   A  1 584 ? 30.762 4.650   -56.747 1.00 22.51  ? 610  LEU   A CD2  1 
ATOM   8681  H H    . LEU   A  1 584 ? 27.162 3.305   -59.776 0.00 26.27  ? 610  LEU   A H    1 
ATOM   8682  H HA   . LEU   A  1 584 ? 26.673 3.698   -57.135 0.00 25.21  ? 610  LEU   A HA   1 
ATOM   8683  H HB2  . LEU   A  1 584 ? 28.876 3.254   -58.369 0.00 24.87  ? 610  LEU   A HB2  1 
ATOM   8684  H HB3  . LEU   A  1 584 ? 28.967 5.010   -58.608 0.00 24.99  ? 610  LEU   A HB3  1 
ATOM   8685  H HG   . LEU   A  1 584 ? 28.833 5.192   -56.042 0.00 25.36  ? 610  LEU   A HG   1 
ATOM   8686  H HD11 . LEU   A  1 584 ? 29.731 3.170   -54.867 0.00 26.08  ? 610  LEU   A HD11 1 
ATOM   8687  H HD12 . LEU   A  1 584 ? 28.052 3.016   -55.423 0.00 26.59  ? 610  LEU   A HD12 1 
ATOM   8688  H HD13 . LEU   A  1 584 ? 29.368 2.225   -56.333 0.00 26.56  ? 610  LEU   A HD13 1 
ATOM   8689  H HD21 . LEU   A  1 584 ? 31.190 4.835   -55.762 0.00 25.06  ? 610  LEU   A HD21 1 
ATOM   8690  H HD22 . LEU   A  1 584 ? 31.242 3.784   -57.200 0.00 25.44  ? 610  LEU   A HD22 1 
ATOM   8691  H HD23 . LEU   A  1 584 ? 30.902 5.522   -57.383 0.00 25.63  ? 610  LEU   A HD23 1 
ATOM   8692  N N    . VAL   A  1 585 ? 26.106 6.010   -56.414 1.00 20.70  ? 611  VAL   A N    1 
ATOM   8693  C CA   . VAL   A  1 585 ? 25.689 7.351   -56.001 1.00 21.93  ? 611  VAL   A CA   1 
ATOM   8694  C C    . VAL   A  1 585 ? 26.703 7.974   -55.030 1.00 21.46  ? 611  VAL   A C    1 
ATOM   8695  O O    . VAL   A  1 585 ? 26.847 9.192   -55.019 1.00 22.26  ? 611  VAL   A O    1 
ATOM   8696  C CB   . VAL   A  1 585 ? 24.245 7.404   -55.429 1.00 23.96  ? 611  VAL   A CB   1 
ATOM   8697  C CG1  . VAL   A  1 585 ? 23.269 6.665   -56.333 1.00 25.25  ? 611  VAL   A CG1  1 
ATOM   8698  C CG2  . VAL   A  1 585 ? 24.173 6.881   -54.012 1.00 25.19  ? 611  VAL   A CG2  1 
ATOM   8699  H H    . VAL   A  1 585 ? 25.974 5.312   -55.689 0.00 24.08  ? 611  VAL   A H    1 
ATOM   8700  H HA   . VAL   A  1 585 ? 25.655 7.986   -56.884 0.00 26.23  ? 611  VAL   A HA   1 
ATOM   8701  H HB   . VAL   A  1 585 ? 23.918 8.442   -55.387 0.00 28.78  ? 611  VAL   A HB   1 
ATOM   8702  H HG11 . VAL   A  1 585 ? 22.253 6.886   -56.009 0.00 30.94  ? 611  VAL   A HG11 1 
ATOM   8703  H HG12 . VAL   A  1 585 ? 23.416 6.991   -57.362 0.00 30.88  ? 611  VAL   A HG12 1 
ATOM   8704  H HG13 . VAL   A  1 585 ? 23.445 5.595   -56.255 0.00 30.46  ? 611  VAL   A HG13 1 
ATOM   8705  H HG21 . VAL   A  1 585 ? 23.148 6.580   -53.802 0.00 29.83  ? 611  VAL   A HG21 1 
ATOM   8706  H HG22 . VAL   A  1 585 ? 24.841 6.027   -53.910 0.00 29.32  ? 611  VAL   A HG22 1 
ATOM   8707  H HG23 . VAL   A  1 585 ? 24.466 7.670   -53.321 0.00 29.40  ? 611  VAL   A HG23 1 
ATOM   8708  N N    . GLU   A  1 586 ? 27.389 7.154   -54.203 1.00 19.42  ? 612  GLU   A N    1 
ATOM   8709  C CA   . GLU   A  1 586 ? 28.348 7.665   -53.225 1.00 18.79  ? 612  GLU   A CA   1 
ATOM   8710  C C    . GLU   A  1 586 ? 29.684 6.935   -53.287 1.00 18.14  ? 612  GLU   A C    1 
ATOM   8711  O O    . GLU   A  1 586 ? 29.719 5.704   -53.230 1.00 18.02  ? 612  GLU   A O    1 
ATOM   8712  C CB   . GLU   A  1 586 ? 27.764 7.547   -51.807 1.00 19.71  ? 612  GLU   A CB   1 
ATOM   8713  C CG   . GLU   A  1 586 ? 28.685 8.016   -50.684 1.00 21.22  ? 612  GLU   A CG   1 
ATOM   8714  C CD   . GLU   A  1 586 ? 28.084 7.885   -49.293 1.00 26.82  ? 612  GLU   A CD   1 
ATOM   8715  O OE1  . GLU   A  1 586 ? 26.995 7.280   -49.152 1.00 28.47  ? 612  GLU   A OE1  1 
ATOM   8716  O OE2  . GLU   A  1 586 ? 28.721 8.372   -48.334 1.00 27.28  ? 612  GLU   A OE2  1 
ATOM   8717  H H    . GLU   A  1 586 ? 27.289 6.145   -54.172 0.00 21.82  ? 612  GLU   A H    1 
ATOM   8718  H HA   . GLU   A  1 586 ? 28.541 8.721   -53.404 0.00 20.84  ? 612  GLU   A HA   1 
ATOM   8719  H HB2  . GLU   A  1 586 ? 26.850 8.137   -51.755 0.00 21.85  ? 612  GLU   A HB2  1 
ATOM   8720  H HB3  . GLU   A  1 586 ? 27.537 6.499   -51.625 0.00 21.48  ? 612  GLU   A HB3  1 
ATOM   8721  H HG2  . GLU   A  1 586 ? 29.595 7.418   -50.677 0.00 22.72  ? 612  GLU   A HG2  1 
ATOM   8722  H HG3  . GLU   A  1 586 ? 28.937 9.063   -50.845 0.00 23.09  ? 612  GLU   A HG3  1 
ATOM   8723  N N    . LEU   A  1 587 ? 30.784 7.706   -53.392 1.00 17.29  ? 613  LEU   A N    1 
ATOM   8724  C CA   . LEU   A  1 587 ? 32.130 7.164   -53.350 1.00 17.73  ? 613  LEU   A CA   1 
ATOM   8725  C C    . LEU   A  1 587 ? 32.877 7.841   -52.210 1.00 18.59  ? 613  LEU   A C    1 
ATOM   8726  O O    . LEU   A  1 587 ? 33.032 9.068   -52.218 1.00 19.71  ? 613  LEU   A O    1 
ATOM   8727  C CB   . LEU   A  1 587 ? 32.922 7.364   -54.663 1.00 17.30  ? 613  LEU   A CB   1 
ATOM   8728  C CG   . LEU   A  1 587 ? 34.402 6.885   -54.609 1.00 18.12  ? 613  LEU   A CG   1 
ATOM   8729  C CD1  . LEU   A  1 587 ? 34.486 5.381   -54.345 1.00 18.01  ? 613  LEU   A CD1  1 
ATOM   8730  C CD2  . LEU   A  1 587 ? 35.152 7.237   -55.873 1.00 19.71  ? 613  LEU   A CD2  1 
ATOM   8731  H H    . LEU   A  1 587 ? 30.769 8.714   -53.515 0.00 18.60  ? 613  LEU   A H    1 
ATOM   8732  H HA   . LEU   A  1 587 ? 32.088 6.096   -53.144 0.00 18.55  ? 613  LEU   A HA   1 
ATOM   8733  H HB2  . LEU   A  1 587 ? 32.423 6.810   -55.458 0.00 18.64  ? 613  LEU   A HB2  1 
ATOM   8734  H HB3  . LEU   A  1 587 ? 32.926 8.425   -54.908 0.00 18.56  ? 613  LEU   A HB3  1 
ATOM   8735  H HG   . LEU   A  1 587 ? 34.927 7.387   -53.798 0.00 18.89  ? 613  LEU   A HG   1 
ATOM   8736  H HD11 . LEU   A  1 587 ? 35.505 5.047   -54.532 0.00 18.72  ? 613  LEU   A HD11 1 
ATOM   8737  H HD12 . LEU   A  1 587 ? 34.222 5.184   -53.307 0.00 18.56  ? 613  LEU   A HD12 1 
ATOM   8738  H HD13 . LEU   A  1 587 ? 33.795 4.867   -55.011 0.00 19.04  ? 613  LEU   A HD13 1 
ATOM   8739  H HD21 . LEU   A  1 587 ? 36.202 6.976   -55.749 0.00 21.11  ? 613  LEU   A HD21 1 
ATOM   8740  H HD22 . LEU   A  1 587 ? 34.725 6.675   -56.702 0.00 21.53  ? 613  LEU   A HD22 1 
ATOM   8741  H HD23 . LEU   A  1 587 ? 35.055 8.305   -56.059 0.00 21.45  ? 613  LEU   A HD23 1 
ATOM   8742  N N    . VAL   A  1 588 ? 33.401 7.045   -51.274 1.00 17.80  ? 614  VAL   A N    1 
ATOM   8743  C CA   . VAL   A  1 588 ? 34.257 7.568   -50.233 1.00 17.42  ? 614  VAL   A CA   1 
ATOM   8744  C C    . VAL   A  1 588 ? 35.682 7.193   -50.626 1.00 17.01  ? 614  VAL   A C    1 
ATOM   8745  O O    . VAL   A  1 588 ? 36.028 6.010   -50.643 1.00 17.04  ? 614  VAL   A O    1 
ATOM   8746  C CB   . VAL   A  1 588 ? 33.885 7.084   -48.815 1.00 17.97  ? 614  VAL   A CB   1 
ATOM   8747  C CG1  . VAL   A  1 588 ? 34.778 7.734   -47.767 1.00 18.03  ? 614  VAL   A CG1  1 
ATOM   8748  C CG2  . VAL   A  1 588 ? 32.402 7.365   -48.528 1.00 18.31  ? 614  VAL   A CG2  1 
ATOM   8749  H H    . VAL   A  1 588 ? 33.254 6.043   -51.213 0.00 18.00  ? 614  VAL   A H    1 
ATOM   8750  H HA   . VAL   A  1 588 ? 34.190 8.651   -50.227 0.00 17.46  ? 614  VAL   A HA   1 
ATOM   8751  H HB   . VAL   A  1 588 ? 34.045 6.011   -48.734 0.00 17.60  ? 614  VAL   A HB   1 
ATOM   8752  H HG11 . VAL   A  1 588 ? 34.482 7.371   -46.784 0.00 17.40  ? 614  VAL   A HG11 1 
ATOM   8753  H HG12 . VAL   A  1 588 ? 35.822 7.485   -47.949 0.00 17.47  ? 614  VAL   A HG12 1 
ATOM   8754  H HG13 . VAL   A  1 588 ? 34.643 8.814   -47.815 0.00 17.71  ? 614  VAL   A HG13 1 
ATOM   8755  H HG21 . VAL   A  1 588 ? 32.201 7.152   -47.479 0.00 18.11  ? 614  VAL   A HG21 1 
ATOM   8756  H HG22 . VAL   A  1 588 ? 32.191 8.410   -48.746 0.00 18.48  ? 614  VAL   A HG22 1 
ATOM   8757  H HG23 . VAL   A  1 588 ? 31.787 6.722   -49.156 0.00 18.45  ? 614  VAL   A HG23 1 
ATOM   8758  N N    . PHE   A  1 589 ? 36.487 8.185   -51.000 1.00 17.11  ? 615  PHE   A N    1 
ATOM   8759  C CA   . PHE   A  1 589 ? 37.879 7.958   -51.428 1.00 17.53  ? 615  PHE   A CA   1 
ATOM   8760  C C    . PHE   A  1 589 ? 38.896 8.589   -50.440 1.00 17.47  ? 615  PHE   A C    1 
ATOM   8761  O O    . PHE   A  1 589 ? 40.054 8.817   -50.812 1.00 17.00  ? 615  PHE   A O    1 
ATOM   8762  C CB   . PHE   A  1 589 ? 38.088 8.555   -52.848 1.00 17.24  ? 615  PHE   A CB   1 
ATOM   8763  C CG   . PHE   A  1 589 ? 39.161 7.878   -53.676 1.00 18.69  ? 615  PHE   A CG   1 
ATOM   8764  C CD1  . PHE   A  1 589 ? 38.963 6.607   -54.191 1.00 19.74  ? 615  PHE   A CD1  1 
ATOM   8765  C CD2  . PHE   A  1 589 ? 40.369 8.513   -53.938 1.00 19.52  ? 615  PHE   A CD2  1 
ATOM   8766  C CE1  . PHE   A  1 589 ? 39.957 5.979   -54.931 1.00 20.77  ? 615  PHE   A CE1  1 
ATOM   8767  C CE2  . PHE   A  1 589 ? 41.352 7.885   -54.698 1.00 20.49  ? 615  PHE   A CE2  1 
ATOM   8768  C CZ   . PHE   A  1 589 ? 41.149 6.618   -55.168 1.00 20.19  ? 615  PHE   A CZ   1 
ATOM   8769  H H    . PHE   A  1 589 ? 36.219 9.163   -51.032 0.00 17.10  ? 615  PHE   A H    1 
ATOM   8770  H HA   . PHE   A  1 589 ? 38.088 6.890   -51.459 0.00 17.31  ? 615  PHE   A HA   1 
ATOM   8771  H HB2  . PHE   A  1 589 ? 37.151 8.470   -53.396 0.00 17.61  ? 615  PHE   A HB2  1 
ATOM   8772  H HB3  . PHE   A  1 589 ? 38.353 9.607   -52.748 0.00 17.50  ? 615  PHE   A HB3  1 
ATOM   8773  H HD1  . PHE   A  1 589 ? 38.040 6.089   -53.990 0.00 20.49  ? 615  PHE   A HD1  1 
ATOM   8774  H HD2  . PHE   A  1 589 ? 40.548 9.503   -53.558 0.00 20.30  ? 615  PHE   A HD2  1 
ATOM   8775  H HE1  . PHE   A  1 589 ? 39.791 4.987   -55.318 0.00 21.89  ? 615  PHE   A HE1  1 
ATOM   8776  H HE2  . PHE   A  1 589 ? 42.287 8.386   -54.887 0.00 21.61  ? 615  PHE   A HE2  1 
ATOM   8777  H HZ   . PHE   A  1 589 ? 41.908 6.138   -55.762 0.00 21.31  ? 615  PHE   A HZ   1 
ATOM   8778  N N    . SER   A  1 590 ? 38.492 8.840   -49.198 1.00 17.57  ? 616  SER   A N    1 
ATOM   8779  C CA   . SER   A  1 590 ? 39.360 9.497   -48.244 1.00 18.44  ? 616  SER   A CA   1 
ATOM   8780  C C    . SER   A  1 590 ? 40.539 8.631   -47.858 1.00 18.38  ? 616  SER   A C    1 
ATOM   8781  O O    . SER   A  1 590 ? 40.450 7.405   -47.931 1.00 19.04  ? 616  SER   A O    1 
ATOM   8782  C CB   . SER   A  1 590 ? 38.577 9.896   -47.002 1.00 21.82  ? 616  SER   A CB   1 
ATOM   8783  O OG   . SER   A  1 590 ? 37.888 8.769   -46.499 1.00 26.48  ? 616  SER   A OG   1 
ATOM   8784  H H    . SER   A  1 590 ? 37.587 8.585   -48.814 0.00 17.05  ? 616  SER   A H    1 
ATOM   8785  H HA   . SER   A  1 590 ? 39.747 10.410  -48.694 0.00 18.19  ? 616  SER   A HA   1 
ATOM   8786  H HB2  . SER   A  1 590 ? 39.265 10.269  -46.244 0.00 21.87  ? 616  SER   A HB2  1 
ATOM   8787  H HB3  . SER   A  1 590 ? 37.855 10.665  -47.269 0.00 22.14  ? 616  SER   A HB3  1 
ATOM   8788  H HG   . SER   A  1 590 ? 37.378 9.019   -45.684 0.00 27.32  ? 616  SER   A HG   1 
ATOM   8789  N N    . GLY   A  1 591 ? 41.644 9.258   -47.476 1.00 17.02  ? 617  GLY   A N    1 
ATOM   8790  C CA   . GLY   A  1 591 ? 42.810 8.514   -47.014 1.00 17.36  ? 617  GLY   A CA   1 
ATOM   8791  C C    . GLY   A  1 591 ? 43.525 7.747   -48.106 1.00 17.57  ? 617  GLY   A C    1 
ATOM   8792  O O    . GLY   A  1 591 ? 44.111 6.685   -47.848 1.00 17.63  ? 617  GLY   A O    1 
ATOM   8793  H H    . GLY   A  1 591 ? 41.777 10.265  -47.492 0.00 16.26  ? 617  GLY   A H    1 
ATOM   8794  H HA2  . GLY   A  1 591 ? 43.519 9.208   -46.568 0.00 16.44  ? 617  GLY   A HA2  1 
ATOM   8795  H HA3  . GLY   A  1 591 ? 42.501 7.804   -46.247 0.00 16.23  ? 617  GLY   A HA3  1 
ATOM   8796  N N    . ASN   A  1 592 ? 43.466 8.270   -49.330 1.00 17.55  ? 618  ASN   A N    1 
ATOM   8797  C CA   . ASN   A  1 592 ? 44.172 7.697   -50.467 1.00 17.52  ? 618  ASN   A CA   1 
ATOM   8798  C C    . ASN   A  1 592 ? 45.225 8.744   -50.915 1.00 17.62  ? 618  ASN   A C    1 
ATOM   8799  O O    . ASN   A  1 592 ? 45.531 9.664   -50.143 1.00 18.08  ? 618  ASN   A O    1 
ATOM   8800  C CB   . ASN   A  1 592 ? 43.151 7.274   -51.554 1.00 18.07  ? 618  ASN   A CB   1 
ATOM   8801  C CG   . ASN   A  1 592 ? 42.399 6.035   -51.113 1.00 18.90  ? 618  ASN   A CG   1 
ATOM   8802  O OD1  . ASN   A  1 592 ? 43.017 5.033   -50.754 1.00 19.14  ? 618  ASN   A OD1  1 
ATOM   8803  N ND2  . ASN   A  1 592 ? 41.072 6.074   -51.083 1.00 17.73  ? 618  ASN   A ND2  1 
ATOM   8804  H H    . ASN   A  1 592 ? 42.951 9.108   -49.580 0.00 17.09  ? 618  ASN   A H    1 
ATOM   8805  H HA   . ASN   A  1 592 ? 44.739 6.818   -50.165 0.00 17.02  ? 618  ASN   A HA   1 
ATOM   8806  H HB2  . ASN   A  1 592 ? 42.447 8.089   -51.717 0.00 17.99  ? 618  ASN   A HB2  1 
ATOM   8807  H HB3  . ASN   A  1 592 ? 43.668 7.033   -52.481 0.00 18.08  ? 618  ASN   A HB3  1 
ATOM   8808  H HD21 . ASN   A  1 592 ? 40.552 5.252   -50.789 0.00 17.23  ? 618  ASN   A HD21 1 
ATOM   8809  H HD22 . ASN   A  1 592 ? 40.570 6.914   -51.351 0.00 17.44  ? 618  ASN   A HD22 1 
ATOM   8810  N N    . ARG   A  1 593 ? 45.819 8.588   -52.094 1.00 17.53  ? 619  ARG   A N    1 
ATOM   8811  C CA   . ARG   A  1 593 ? 46.854 9.506   -52.544 1.00 17.34  ? 619  ARG   A CA   1 
ATOM   8812  C C    . ARG   A  1 593 ? 46.530 10.157  -53.875 1.00 17.85  ? 619  ARG   A C    1 
ATOM   8813  O O    . ARG   A  1 593 ? 47.310 10.048  -54.826 1.00 17.78  ? 619  ARG   A O    1 
ATOM   8814  C CB   . ARG   A  1 593 ? 48.210 8.780   -52.574 1.00 18.47  ? 619  ARG   A CB   1 
ATOM   8815  C CG   . ARG   A  1 593 ? 48.667 8.189   -51.225 1.00 20.66  ? 619  ARG   A CG   1 
ATOM   8816  C CD   . ARG   A  1 593 ? 48.962 9.249   -50.150 1.00 20.57  ? 619  ARG   A CD   1 
ATOM   8817  N NE   . ARG   A  1 593 ? 49.947 10.239  -50.603 1.00 21.36  ? 619  ARG   A NE   1 
ATOM   8818  C CZ   . ARG   A  1 593 ? 51.272 10.127  -50.486 1.00 22.61  ? 619  ARG   A CZ   1 
ATOM   8819  N NH1  . ARG   A  1 593 ? 51.813 9.042   -49.931 1.00 21.24  ? 619  ARG   A NH1  1 
ATOM   8820  N NH2  . ARG   A  1 593 ? 52.067 11.096  -50.925 1.00 21.44  ? 619  ARG   A NH2  1 
ATOM   8821  H H    . ARG   A  1 593 ? 45.633 7.835   -52.749 0.00 17.62  ? 619  ARG   A H    1 
ATOM   8822  H HA   . ARG   A  1 593 ? 46.949 10.342  -51.853 0.00 17.56  ? 619  ARG   A HA   1 
ATOM   8823  H HB2  . ARG   A  1 593 ? 48.077 7.965   -53.282 0.00 19.05  ? 619  ARG   A HB2  1 
ATOM   8824  H HB3  . ARG   A  1 593 ? 48.983 9.461   -52.929 0.00 19.21  ? 619  ARG   A HB3  1 
ATOM   8825  H HG2  . ARG   A  1 593 ? 47.895 7.525   -50.838 0.00 21.18  ? 619  ARG   A HG2  1 
ATOM   8826  H HG3  . ARG   A  1 593 ? 49.583 7.623   -51.387 0.00 21.47  ? 619  ARG   A HG3  1 
ATOM   8827  H HD2  . ARG   A  1 593 ? 48.044 9.790   -49.928 0.00 21.14  ? 619  ARG   A HD2  1 
ATOM   8828  H HD3  . ARG   A  1 593 ? 49.292 8.766   -49.232 0.00 21.07  ? 619  ARG   A HD3  1 
ATOM   8829  H HE   . ARG   A  1 593 ? 49.581 11.087  -51.024 0.00 22.58  ? 619  ARG   A HE   1 
ATOM   8830  H HH11 . ARG   A  1 593 ? 51.265 8.259   -49.592 0.00 22.16  ? 619  ARG   A HH11 1 
ATOM   8831  H HH12 . ARG   A  1 593 ? 52.824 8.979   -49.865 0.00 22.52  ? 619  ARG   A HH12 1 
ATOM   8832  H HH21 . ARG   A  1 593 ? 51.672 11.932  -51.345 0.00 23.12  ? 619  ARG   A HH21 1 
ATOM   8833  H HH22 . ARG   A  1 593 ? 53.075 11.011  -50.841 0.00 23.15  ? 619  ARG   A HH22 1 
ATOM   8834  N N    . LEU   A  1 594 ? 45.445 10.950  -53.911 1.00 17.92  ? 620  LEU   A N    1 
ATOM   8835  C CA   . LEU   A  1 594 ? 45.151 11.751  -55.097 1.00 18.63  ? 620  LEU   A CA   1 
ATOM   8836  C C    . LEU   A  1 594 ? 46.252 12.793  -55.369 1.00 18.95  ? 620  LEU   A C    1 
ATOM   8837  O O    . LEU   A  1 594 ? 46.368 13.254  -56.504 1.00 19.63  ? 620  LEU   A O    1 
ATOM   8838  C CB   . LEU   A  1 594 ? 43.771 12.413  -55.041 1.00 19.03  ? 620  LEU   A CB   1 
ATOM   8839  C CG   . LEU   A  1 594 ? 42.582 11.478  -55.247 1.00 20.68  ? 620  LEU   A CG   1 
ATOM   8840  C CD1  . LEU   A  1 594 ? 41.321 12.100  -54.726 1.00 21.27  ? 620  LEU   A CD1  1 
ATOM   8841  C CD2  . LEU   A  1 594 ? 42.412 11.125  -56.735 1.00 21.25  ? 620  LEU   A CD2  1 
ATOM   8842  H H    . LEU   A  1 594 ? 44.772 11.046  -53.158 0.00 18.48  ? 620  LEU   A H    1 
ATOM   8843  H HA   . LEU   A  1 594 ? 45.172 11.073  -55.945 0.00 19.97  ? 620  LEU   A HA   1 
ATOM   8844  H HB2  . LEU   A  1 594 ? 43.636 12.931  -54.096 0.00 20.27  ? 620  LEU   A HB2  1 
ATOM   8845  H HB3  . LEU   A  1 594 ? 43.732 13.144  -55.846 0.00 20.70  ? 620  LEU   A HB3  1 
ATOM   8846  H HG   . LEU   A  1 594 ? 42.735 10.549  -54.699 0.00 22.03  ? 620  LEU   A HG   1 
ATOM   8847  H HD11 . LEU   A  1 594 ? 40.506 11.414  -54.947 0.00 22.97  ? 620  LEU   A HD11 1 
ATOM   8848  H HD12 . LEU   A  1 594 ? 41.409 12.244  -53.650 0.00 22.77  ? 620  LEU   A HD12 1 
ATOM   8849  H HD13 . LEU   A  1 594 ? 41.158 13.055  -55.225 0.00 23.27  ? 620  LEU   A HD13 1 
ATOM   8850  H HD21 . LEU   A  1 594 ? 41.495 10.552  -56.859 0.00 23.27  ? 620  LEU   A HD21 1 
ATOM   8851  H HD22 . LEU   A  1 594 ? 42.352 12.041  -57.322 0.00 23.58  ? 620  LEU   A HD22 1 
ATOM   8852  H HD23 . LEU   A  1 594 ? 43.253 10.522  -57.069 0.00 23.29  ? 620  LEU   A HD23 1 
ATOM   8853  N N    . ASP   A  1 595 ? 47.102 13.131  -54.371 1.00 18.29  ? 621  ASP   A N    1 
ATOM   8854  C CA   . ASP   A  1 595 ? 48.258 14.012  -54.635 1.00 18.89  ? 621  ASP   A CA   1 
ATOM   8855  C C    . ASP   A  1 595 ? 49.206 13.327  -55.643 1.00 19.44  ? 621  ASP   A C    1 
ATOM   8856  O O    . ASP   A  1 595 ? 49.753 13.997  -56.521 1.00 20.55  ? 621  ASP   A O    1 
ATOM   8857  C CB   . ASP   A  1 595 ? 49.021 14.349  -53.343 1.00 19.67  ? 621  ASP   A CB   1 
ATOM   8858  C CG   . ASP   A  1 595 ? 49.667 13.154  -52.642 1.00 22.71  ? 621  ASP   A CG   1 
ATOM   8859  O OD1  . ASP   A  1 595 ? 48.972 12.112  -52.465 1.00 20.98  ? 621  ASP   A OD1  1 
ATOM   8860  O OD2  . ASP   A  1 595 ? 50.845 13.272  -52.230 1.00 23.33  ? 621  ASP   A OD2  1 
ATOM   8861  H H    . ASP   A  1 595 ? 47.001 12.854  -53.400 0.00 19.36  ? 621  ASP   A H    1 
ATOM   8862  H HA   . ASP   A  1 595 ? 47.915 14.945  -55.080 0.00 20.85  ? 621  ASP   A HA   1 
ATOM   8863  H HB2  . ASP   A  1 595 ? 49.813 15.058  -53.581 0.00 21.68  ? 621  ASP   A HB2  1 
ATOM   8864  H HB3  . ASP   A  1 595 ? 48.324 14.806  -52.641 0.00 21.31  ? 621  ASP   A HB3  1 
ATOM   8865  N N    . ILE   A  1 596 ? 49.355 11.987  -55.549 1.00 18.46  ? 622  ILE   A N    1 
ATOM   8866  C CA   . ILE   A  1 596 ? 50.176 11.220  -56.483 1.00 18.48  ? 622  ILE   A CA   1 
ATOM   8867  C C    . ILE   A  1 596 ? 49.390 10.938  -57.779 1.00 18.17  ? 622  ILE   A C    1 
ATOM   8868  O O    . ILE   A  1 596 ? 49.915 11.174  -58.867 1.00 17.69  ? 622  ILE   A O    1 
ATOM   8869  C CB   . ILE   A  1 596 ? 50.688 9.909   -55.820 1.00 19.06  ? 622  ILE   A CB   1 
ATOM   8870  C CG1  . ILE   A  1 596 ? 51.694 10.248  -54.690 1.00 20.74  ? 622  ILE   A CG1  1 
ATOM   8871  C CG2  . ILE   A  1 596 ? 51.304 8.969   -56.885 1.00 19.24  ? 622  ILE   A CG2  1 
ATOM   8872  C CD1  . ILE   A  1 596 ? 52.204 9.049   -53.864 1.00 22.36  ? 622  ILE   A CD1  1 
ATOM   8873  H H    . ILE   A  1 596 ? 48.926 11.414  -54.829 0.00 19.80  ? 622  ILE   A H    1 
ATOM   8874  H HA   . ILE   A  1 596 ? 51.054 11.805  -56.754 0.00 20.53  ? 622  ILE   A HA   1 
ATOM   8875  H HB   . ILE   A  1 596 ? 49.841 9.388   -55.377 0.00 20.50  ? 622  ILE   A HB   1 
ATOM   8876  H HG12 . ILE   A  1 596 ? 52.560 10.734  -55.137 0.00 22.97  ? 622  ILE   A HG12 1 
ATOM   8877  H HG13 . ILE   A  1 596 ? 51.218 10.935  -53.992 0.00 22.56  ? 622  ILE   A HG13 1 
ATOM   8878  H HG21 . ILE   A  1 596 ? 51.885 8.184   -56.404 0.00 21.11  ? 622  ILE   A HG21 1 
ATOM   8879  H HG22 . ILE   A  1 596 ? 50.509 8.498   -57.462 0.00 21.20  ? 622  ILE   A HG22 1 
ATOM   8880  H HG23 . ILE   A  1 596 ? 51.947 9.552   -57.544 0.00 21.49  ? 622  ILE   A HG23 1 
ATOM   8881  H HD11 . ILE   A  1 596 ? 52.593 9.419   -52.917 0.00 24.35  ? 622  ILE   A HD11 1 
ATOM   8882  H HD12 . ILE   A  1 596 ? 51.379 8.360   -53.688 0.00 24.23  ? 622  ILE   A HD12 1 
ATOM   8883  H HD13 . ILE   A  1 596 ? 53.001 8.547   -54.410 0.00 24.64  ? 622  ILE   A HD13 1 
ATOM   8884  N N    . LEU   A  1 597 ? 48.150 10.415  -57.675 1.00 19.15  ? 623  LEU   A N    1 
ATOM   8885  C CA   . LEU   A  1 597 ? 47.348 10.114  -58.873 1.00 20.56  ? 623  LEU   A CA   1 
ATOM   8886  C C    . LEU   A  1 597 ? 47.166 11.335  -59.782 1.00 21.25  ? 623  LEU   A C    1 
ATOM   8887  O O    . LEU   A  1 597 ? 47.231 11.210  -61.002 1.00 21.24  ? 623  LEU   A O    1 
ATOM   8888  C CB   . LEU   A  1 597 ? 45.969 9.537   -58.492 1.00 20.85  ? 623  LEU   A CB   1 
ATOM   8889  C CG   . LEU   A  1 597 ? 45.980 8.225   -57.684 1.00 21.29  ? 623  LEU   A CG   1 
ATOM   8890  C CD1  . LEU   A  1 597 ? 44.707 8.047   -56.826 1.00 21.65  ? 623  LEU   A CD1  1 
ATOM   8891  C CD2  . LEU   A  1 597 ? 46.136 7.040   -58.611 1.00 21.43  ? 623  LEU   A CD2  1 
ATOM   8892  H H    . LEU   A  1 597 ? 47.690 10.212  -56.794 0.00 20.82  ? 623  LEU   A H    1 
ATOM   8893  H HA   . LEU   A  1 597 ? 47.870 9.353   -59.450 0.00 23.13  ? 623  LEU   A HA   1 
ATOM   8894  H HB2  . LEU   A  1 597 ? 45.391 10.293  -57.968 0.00 23.05  ? 623  LEU   A HB2  1 
ATOM   8895  H HB3  . LEU   A  1 597 ? 45.454 9.312   -59.425 0.00 23.34  ? 623  LEU   A HB3  1 
ATOM   8896  H HG   . LEU   A  1 597 ? 46.821 8.238   -56.995 0.00 23.20  ? 623  LEU   A HG   1 
ATOM   8897  H HD11 . LEU   A  1 597 ? 44.721 7.054   -56.378 0.00 23.30  ? 623  LEU   A HD11 1 
ATOM   8898  H HD12 . LEU   A  1 597 ? 44.696 8.802   -56.042 0.00 23.35  ? 623  LEU   A HD12 1 
ATOM   8899  H HD13 . LEU   A  1 597 ? 43.831 8.156   -57.463 0.00 23.64  ? 623  LEU   A HD13 1 
ATOM   8900  H HD21 . LEU   A  1 597 ? 46.229 6.135   -58.012 0.00 23.47  ? 623  LEU   A HD21 1 
ATOM   8901  H HD22 . LEU   A  1 597 ? 45.259 6.969   -59.253 0.00 23.81  ? 623  LEU   A HD22 1 
ATOM   8902  H HD23 . LEU   A  1 597 ? 47.030 7.180   -59.216 0.00 23.89  ? 623  LEU   A HD23 1 
ATOM   8903  N N    . TRP   A  1 598 ? 46.956 12.517  -59.182 1.00 21.46  ? 624  TRP   A N    1 
ATOM   8904  C CA   . TRP   A  1 598 ? 46.775 13.758  -59.929 1.00 21.83  ? 624  TRP   A CA   1 
ATOM   8905  C C    . TRP   A  1 598 ? 48.036 14.621  -59.934 1.00 23.90  ? 624  TRP   A C    1 
ATOM   8906  O O    . TRP   A  1 598 ? 47.952 15.837  -60.100 1.00 24.64  ? 624  TRP   A O    1 
ATOM   8907  C CB   . TRP   A  1 598 ? 45.580 14.548  -59.383 1.00 20.71  ? 624  TRP   A CB   1 
ATOM   8908  C CG   . TRP   A  1 598 ? 44.244 13.933  -59.669 1.00 20.42  ? 624  TRP   A CG   1 
ATOM   8909  C CD1  . TRP   A  1 598 ? 43.900 13.160  -60.744 1.00 21.12  ? 624  TRP   A CD1  1 
ATOM   8910  C CD2  . TRP   A  1 598 ? 43.022 14.232  -58.985 1.00 19.72  ? 624  TRP   A CD2  1 
ATOM   8911  N NE1  . TRP   A  1 598 ? 42.557 12.863  -60.697 1.00 21.12  ? 624  TRP   A NE1  1 
ATOM   8912  C CE2  . TRP   A  1 598 ? 41.985 13.559  -59.663 1.00 20.36  ? 624  TRP   A CE2  1 
ATOM   8913  C CE3  . TRP   A  1 598 ? 42.702 15.027  -57.880 1.00 20.14  ? 624  TRP   A CE3  1 
ATOM   8914  C CZ2  . TRP   A  1 598 ? 40.671 13.575  -59.205 1.00 20.99  ? 624  TRP   A CZ2  1 
ATOM   8915  C CZ3  . TRP   A  1 598 ? 41.398 15.044  -57.432 1.00 20.70  ? 624  TRP   A CZ3  1 
ATOM   8916  C CH2  . TRP   A  1 598 ? 40.389 14.376  -58.126 1.00 21.09  ? 624  TRP   A CH2  1 
ATOM   8917  H H    . TRP   A  1 598 ? 46.896 12.642  -58.177 0.00 24.21  ? 624  TRP   A H    1 
ATOM   8918  H HA   . TRP   A  1 598 ? 46.563 13.537  -60.974 0.00 25.54  ? 624  TRP   A HA   1 
ATOM   8919  H HB2  . TRP   A  1 598 ? 45.681 14.642  -58.303 0.00 23.64  ? 624  TRP   A HB2  1 
ATOM   8920  H HB3  . TRP   A  1 598 ? 45.556 15.538  -59.835 0.00 24.22  ? 624  TRP   A HB3  1 
ATOM   8921  H HD1  . TRP   A  1 598 ? 44.593 12.747  -61.456 0.00 24.68  ? 624  TRP   A HD1  1 
ATOM   8922  H HE1  . TRP   A  1 598 ? 42.046 12.261  -61.376 0.00 24.62  ? 624  TRP   A HE1  1 
ATOM   8923  H HE3  . TRP   A  1 598 ? 43.469 15.572  -57.356 0.00 22.87  ? 624  TRP   A HE3  1 
ATOM   8924  H HZ2  . TRP   A  1 598 ? 39.892 13.038  -59.720 0.00 24.19  ? 624  TRP   A HZ2  1 
ATOM   8925  H HZ3  . TRP   A  1 598 ? 41.140 15.652  -56.582 0.00 23.43  ? 624  TRP   A HZ3  1 
ATOM   8926  H HH2  . TRP   A  1 598 ? 39.383 14.407  -57.746 0.00 24.04  ? 624  TRP   A HH2  1 
ATOM   8927  N N    . ASN   A  1 599 ? 49.218 13.996  -59.875 1.00 24.17  ? 625  ASN   A N    1 
ATOM   8928  C CA   . ASN   A  1 599 ? 50.487 14.722  -59.986 1.00 25.79  ? 625  ASN   A CA   1 
ATOM   8929  C C    . ASN   A  1 599 ? 50.519 15.465  -61.336 1.00 27.24  ? 625  ASN   A C    1 
ATOM   8930  O O    . ASN   A  1 599 ? 50.053 14.913  -62.341 1.00 27.63  ? 625  ASN   A O    1 
ATOM   8931  C CB   . ASN   A  1 599 ? 51.652 13.739  -59.902 1.00 27.37  ? 625  ASN   A CB   1 
ATOM   8932  C CG   . ASN   A  1 599 ? 52.984 14.385  -60.115 1.00 31.98  ? 625  ASN   A CG   1 
ATOM   8933  O OD1  . ASN   A  1 599 ? 53.471 14.474  -61.255 1.00 32.92  ? 625  ASN   A OD1  1 
ATOM   8934  N ND2  . ASN   A  1 599 ? 53.581 14.874  -59.033 1.00 32.02  ? 625  ASN   A ND2  1 
ATOM   8935  H H    . ASN   A  1 599 ? 49.329 12.993  -59.767 0.00 28.10  ? 625  ASN   A H    1 
ATOM   8936  H HA   . ASN   A  1 599 ? 50.572 15.442  -59.174 0.00 30.42  ? 625  ASN   A HA   1 
ATOM   8937  H HB2  . ASN   A  1 599 ? 51.647 13.263  -58.922 0.00 32.00  ? 625  ASN   A HB2  1 
ATOM   8938  H HB3  . ASN   A  1 599 ? 51.528 12.983  -60.675 0.00 32.40  ? 625  ASN   A HB3  1 
ATOM   8939  H HD21 . ASN   A  1 599 ? 54.487 15.315  -59.134 0.00 38.39  ? 625  ASN   A HD21 1 
ATOM   8940  H HD22 . ASN   A  1 599 ? 53.143 14.805  -58.120 0.00 37.85  ? 625  ASN   A HD22 1 
ATOM   8941  N N    . ASP   A  1 600 ? 50.967 16.728  -61.337 1.00 28.05  ? 626  ASP   A N    1 
ATOM   8942  C CA   . ASP   A  1 600 ? 50.986 17.575  -62.538 1.00 29.11  ? 626  ASP   A CA   1 
ATOM   8943  C C    . ASP   A  1 600 ? 51.644 16.941  -63.764 1.00 28.25  ? 626  ASP   A C    1 
ATOM   8944  O O    . ASP   A  1 600 ? 51.344 17.350  -64.882 1.00 28.74  ? 626  ASP   A O    1 
ATOM   8945  C CB   . ASP   A  1 600 ? 51.731 18.890  -62.255 1.00 32.48  ? 626  ASP   A CB   1 
ATOM   8946  C CG   . ASP   A  1 600 ? 51.030 19.844  -61.322 1.00 40.68  ? 626  ASP   A CG   1 
ATOM   8947  O OD1  . ASP   A  1 600 ? 49.791 19.743  -61.189 1.00 42.38  ? 626  ASP   A OD1  1 
ATOM   8948  O OD2  . ASP   A  1 600 ? 51.718 20.695  -60.718 1.00 44.22  ? 626  ASP   A OD2  1 
ATOM   8949  H H    . ASP   A  1 600 ? 51.343 17.185  -60.512 0.00 33.92  ? 626  ASP   A H    1 
ATOM   8950  H HA   . ASP   A  1 600 ? 49.960 17.809  -62.819 0.00 35.87  ? 626  ASP   A HA   1 
ATOM   8951  H HB2  . ASP   A  1 600 ? 52.696 18.651  -61.810 0.00 40.09  ? 626  ASP   A HB2  1 
ATOM   8952  H HB3  . ASP   A  1 600 ? 51.882 19.412  -63.198 0.00 40.58  ? 626  ASP   A HB3  1 
ATOM   8953  N N    . ASP   A  1 601 ? 52.585 16.015  -63.561 1.00 27.15  ? 627  ASP   A N    1 
ATOM   8954  C CA   . ASP   A  1 601 ? 53.324 15.397  -64.665 1.00 26.50  ? 627  ASP   A CA   1 
ATOM   8955  C C    . ASP   A  1 601 ? 52.718 14.058  -65.128 1.00 25.63  ? 627  ASP   A C    1 
ATOM   8956  O O    . ASP   A  1 601 ? 53.339 13.381  -65.937 1.00 25.19  ? 627  ASP   A O    1 
ATOM   8957  C CB   . ASP   A  1 601 ? 54.786 15.183  -64.235 1.00 27.96  ? 627  ASP   A CB   1 
ATOM   8958  C CG   . ASP   A  1 601 ? 55.447 16.435  -63.696 1.00 31.94  ? 627  ASP   A CG   1 
ATOM   8959  O OD1  . ASP   A  1 601 ? 55.451 17.452  -64.409 1.00 30.59  ? 627  ASP   A OD1  1 
ATOM   8960  O OD2  . ASP   A  1 601 ? 55.971 16.390  -62.547 1.00 35.66  ? 627  ASP   A OD2  1 
ATOM   8961  H H    . ASP   A  1 601 ? 52.866 15.666  -62.650 0.00 33.31  ? 627  ASP   A H    1 
ATOM   8962  H HA   . ASP   A  1 601 ? 53.346 16.064  -65.525 0.00 33.55  ? 627  ASP   A HA   1 
ATOM   8963  H HB2  . ASP   A  1 601 ? 54.822 14.420  -63.459 0.00 34.58  ? 627  ASP   A HB2  1 
ATOM   8964  H HB3  . ASP   A  1 601 ? 55.363 14.864  -65.101 0.00 35.25  ? 627  ASP   A HB3  1 
ATOM   8965  N N    . ASP   A  1 602 ? 51.513 13.688  -64.653 1.00 24.81  ? 628  ASP   A N    1 
ATOM   8966  C CA   . ASP   A  1 602 ? 50.870 12.438  -65.040 1.00 24.75  ? 628  ASP   A CA   1 
ATOM   8967  C C    . ASP   A  1 602 ? 49.441 12.703  -65.506 1.00 24.80  ? 628  ASP   A C    1 
ATOM   8968  O O    . ASP   A  1 602 ? 48.636 13.226  -64.739 1.00 24.79  ? 628  ASP   A O    1 
ATOM   8969  C CB   . ASP   A  1 602 ? 50.870 11.473  -63.834 1.00 25.47  ? 628  ASP   A CB   1 
ATOM   8970  C CG   . ASP   A  1 602 ? 50.431 10.054  -64.135 1.00 28.32  ? 628  ASP   A CG   1 
ATOM   8971  O OD1  . ASP   A  1 602 ? 50.124 9.761   -65.302 1.00 26.17  ? 628  ASP   A OD1  1 
ATOM   8972  O OD2  . ASP   A  1 602 ? 50.414 9.229   -63.201 1.00 32.10  ? 628  ASP   A OD2  1 
ATOM   8973  H H    . ASP   A  1 602 ? 50.947 14.233  -64.011 0.00 30.46  ? 628  ASP   A H    1 
ATOM   8974  H HA   . ASP   A  1 602 ? 51.411 11.964  -65.857 0.00 30.70  ? 628  ASP   A HA   1 
ATOM   8975  H HB2  . ASP   A  1 602 ? 51.881 11.422  -63.435 0.00 30.77  ? 628  ASP   A HB2  1 
ATOM   8976  H HB3  . ASP   A  1 602 ? 50.197 11.866  -63.073 0.00 30.53  ? 628  ASP   A HB3  1 
ATOM   8977  N N    . ASN   A  1 603 ? 49.116 12.312  -66.745 1.00 24.92  ? 629  ASN   A N    1 
ATOM   8978  C CA   . ASN   A  1 603 ? 47.757 12.464  -67.273 1.00 25.41  ? 629  ASN   A CA   1 
ATOM   8979  C C    . ASN   A  1 603 ? 46.915 11.185  -67.135 1.00 23.93  ? 629  ASN   A C    1 
ATOM   8980  O O    . ASN   A  1 603 ? 45.745 11.210  -67.529 1.00 23.83  ? 629  ASN   A O    1 
ATOM   8981  C CB   . ASN   A  1 603 ? 47.823 12.852  -68.763 1.00 28.74  ? 629  ASN   A CB   1 
ATOM   8982  C CG   . ASN   A  1 603 ? 48.388 14.234  -69.002 1.00 35.39  ? 629  ASN   A CG   1 
ATOM   8983  O OD1  . ASN   A  1 603 ? 48.327 15.116  -68.131 1.00 36.92  ? 629  ASN   A OD1  1 
ATOM   8984  N ND2  . ASN   A  1 603 ? 48.924 14.470  -70.204 1.00 37.27  ? 629  ASN   A ND2  1 
ATOM   8985  H H    . ASN   A  1 603 ? 49.762 11.882  -67.400 0.00 31.30  ? 629  ASN   A H    1 
ATOM   8986  H HA   . ASN   A  1 603 ? 47.227 13.256  -66.747 0.00 31.71  ? 629  ASN   A HA   1 
ATOM   8987  H HB2  . ASN   A  1 603 ? 48.446 12.132  -69.291 0.00 36.55  ? 629  ASN   A HB2  1 
ATOM   8988  H HB3  . ASN   A  1 603 ? 46.819 12.846  -69.183 0.00 36.56  ? 629  ASN   A HB3  1 
ATOM   8989  H HD21 . ASN   A  1 603 ? 49.317 15.383  -70.410 0.00 47.76  ? 629  ASN   A HD21 1 
ATOM   8990  H HD22 . ASN   A  1 603 ? 48.941 13.742  -70.911 0.00 47.67  ? 629  ASN   A HD22 1 
ATOM   8991  N N    . ARG   A  1 604 ? 47.476 10.070  -66.616 1.00 22.74  ? 630  ARG   A N    1 
ATOM   8992  C CA   . ARG   A  1 604 ? 46.758 8.791   -66.633 1.00 22.95  ? 630  ARG   A CA   1 
ATOM   8993  C C    . ARG   A  1 604 ? 45.466 8.722   -65.794 1.00 22.28  ? 630  ARG   A C    1 
ATOM   8994  O O    . ARG   A  1 604 ? 44.549 8.015   -66.207 1.00 22.51  ? 630  ARG   A O    1 
ATOM   8995  C CB   . ARG   A  1 604 ? 47.680 7.630   -66.242 1.00 23.37  ? 630  ARG   A CB   1 
ATOM   8996  C CG   . ARG   A  1 604 ? 48.822 7.394   -67.256 1.00 24.99  ? 630  ARG   A CG   1 
ATOM   8997  C CD   . ARG   A  1 604 ? 49.859 6.388   -66.756 1.00 26.73  ? 630  ARG   A CD   1 
ATOM   8998  N NE   . ARG   A  1 604 ? 50.428 6.832   -65.488 1.00 27.09  ? 630  ARG   A NE   1 
ATOM   8999  C CZ   . ARG   A  1 604 ? 50.939 6.043   -64.547 1.00 27.20  ? 630  ARG   A CZ   1 
ATOM   9000  N NH1  . ARG   A  1 604 ? 50.998 4.725   -64.729 1.00 26.39  ? 630  ARG   A NH1  1 
ATOM   9001  N NH2  . ARG   A  1 604 ? 51.366 6.562   -63.401 1.00 24.43  ? 630  ARG   A NH2  1 
ATOM   9002  H H    . ARG   A  1 604 ? 48.388 10.016  -66.174 0.00 27.95  ? 630  ARG   A H    1 
ATOM   9003  H HA   . ARG   A  1 604 ? 46.462 8.617   -67.667 0.00 28.56  ? 630  ARG   A HA   1 
ATOM   9004  H HB2  . ARG   A  1 604 ? 48.108 7.848   -65.265 0.00 28.21  ? 630  ARG   A HB2  1 
ATOM   9005  H HB3  . ARG   A  1 604 ? 47.088 6.718   -66.187 0.00 28.43  ? 630  ARG   A HB3  1 
ATOM   9006  H HG2  . ARG   A  1 604 ? 48.399 7.007   -68.182 0.00 31.19  ? 630  ARG   A HG2  1 
ATOM   9007  H HG3  . ARG   A  1 604 ? 49.339 8.333   -67.448 0.00 31.04  ? 630  ARG   A HG3  1 
ATOM   9008  H HD2  . ARG   A  1 604 ? 49.334 5.444   -66.624 0.00 32.72  ? 630  ARG   A HD2  1 
ATOM   9009  H HD3  . ARG   A  1 604 ? 50.658 6.287   -67.489 0.00 33.17  ? 630  ARG   A HD3  1 
ATOM   9010  H HE   . ARG   A  1 604 ? 50.378 7.826   -65.291 0.00 32.85  ? 630  ARG   A HE   1 
ATOM   9011  H HH11 . ARG   A  1 604 ? 50.685 4.266   -65.577 0.00 32.07  ? 630  ARG   A HH11 1 
ATOM   9012  H HH12 . ARG   A  1 604 ? 51.400 4.145   -63.999 0.00 31.62  ? 630  ARG   A HH12 1 
ATOM   9013  H HH21 . ARG   A  1 604 ? 51.332 7.564   -63.248 0.00 29.07  ? 630  ARG   A HH21 1 
ATOM   9014  H HH22 . ARG   A  1 604 ? 51.776 5.964   -62.690 0.00 28.90  ? 630  ARG   A HH22 1 
ATOM   9015  N N    . TYR   A  1 605 ? 45.388 9.436   -64.675 1.00 20.76  ? 631  TYR   A N    1 
ATOM   9016  C CA   . TYR   A  1 605 ? 44.226 9.396   -63.759 1.00 20.94  ? 631  TYR   A CA   1 
ATOM   9017  C C    . TYR   A  1 605 ? 43.372 10.660  -63.805 1.00 22.19  ? 631  TYR   A C    1 
ATOM   9018  O O    . TYR   A  1 605 ? 42.536 10.852  -62.928 1.00 22.28  ? 631  TYR   A O    1 
ATOM   9019  C CB   . TYR   A  1 605 ? 44.717 9.180   -62.316 1.00 19.74  ? 631  TYR   A CB   1 
ATOM   9020  C CG   . TYR   A  1 605 ? 45.535 7.922   -62.172 1.00 19.48  ? 631  TYR   A CG   1 
ATOM   9021  C CD1  . TYR   A  1 605 ? 44.923 6.693   -61.957 1.00 19.24  ? 631  TYR   A CD1  1 
ATOM   9022  C CD2  . TYR   A  1 605 ? 46.916 7.946   -62.325 1.00 19.82  ? 631  TYR   A CD2  1 
ATOM   9023  C CE1  . TYR   A  1 605 ? 45.671 5.529   -61.820 1.00 19.51  ? 631  TYR   A CE1  1 
ATOM   9024  C CE2  . TYR   A  1 605 ? 47.673 6.786   -62.208 1.00 20.05  ? 631  TYR   A CE2  1 
ATOM   9025  C CZ   . TYR   A  1 605 ? 47.046 5.577   -61.966 1.00 20.38  ? 631  TYR   A CZ   1 
ATOM   9026  O OH   . TYR   A  1 605 ? 47.780 4.418   -61.867 1.00 21.14  ? 631  TYR   A OH   1 
ATOM   9027  H H    . TYR   A  1 605 ? 46.121 10.059  -64.347 0.00 24.85  ? 631  TYR   A H    1 
ATOM   9028  H HA   . TYR   A  1 605 ? 43.582 8.553   -64.006 0.00 24.81  ? 631  TYR   A HA   1 
ATOM   9029  H HB2  . TYR   A  1 605 ? 45.337 10.025  -62.019 0.00 22.85  ? 631  TYR   A HB2  1 
ATOM   9030  H HB3  . TYR   A  1 605 ? 43.863 9.087   -61.647 0.00 22.63  ? 631  TYR   A HB3  1 
ATOM   9031  H HD1  . TYR   A  1 605 ? 43.854 6.648   -61.838 0.00 21.92  ? 631  TYR   A HD1  1 
ATOM   9032  H HD2  . TYR   A  1 605 ? 47.410 8.885   -62.510 0.00 23.07  ? 631  TYR   A HD2  1 
ATOM   9033  H HE1  . TYR   A  1 605 ? 45.177 4.588   -61.641 0.00 22.14  ? 631  TYR   A HE1  1 
ATOM   9034  H HE2  . TYR   A  1 605 ? 48.744 6.840   -62.316 0.00 23.25  ? 631  TYR   A HE2  1 
ATOM   9035  H HH   . TYR   A  1 605 ? 48.751 4.601   -61.963 0.00 24.39  ? 631  TYR   A HH   1 
ATOM   9036  N N    . ILE   A  1 606 ? 43.508 11.461  -64.874 1.00 23.22  ? 632  ILE   A N    1 
ATOM   9037  C CA   . ILE   A  1 606 ? 42.813 12.730  -65.012 1.00 24.88  ? 632  ILE   A CA   1 
ATOM   9038  C C    . ILE   A  1 606 ? 41.275 12.566  -65.111 1.00 24.20  ? 632  ILE   A C    1 
ATOM   9039  O O    . ILE   A  1 606 ? 40.562 13.521  -64.829 1.00 24.84  ? 632  ILE   A O    1 
ATOM   9040  C CB   . ILE   A  1 606 ? 43.416 13.553  -66.214 1.00 27.01  ? 632  ILE   A CB   1 
ATOM   9041  C CG1  . ILE   A  1 606 ? 43.281 15.064  -65.976 1.00 30.08  ? 632  ILE   A CG1  1 
ATOM   9042  C CG2  . ILE   A  1 606 ? 42.795 13.150  -67.550 1.00 27.33  ? 632  ILE   A CG2  1 
ATOM   9043  C CD1  . ILE   A  1 606 ? 44.392 15.661  -65.022 1.00 32.97  ? 632  ILE   A CD1  1 
ATOM   9044  H H    . ILE   A  1 606 ? 44.071 11.233  -65.687 0.00 28.40  ? 632  ILE   A H    1 
ATOM   9045  H HA   . ILE   A  1 606 ? 42.994 13.272  -64.084 0.00 30.15  ? 632  ILE   A HA   1 
ATOM   9046  H HB   . ILE   A  1 606 ? 44.483 13.360  -66.326 0.00 33.47  ? 632  ILE   A HB   1 
ATOM   9047  H HG12 . ILE   A  1 606 ? 43.355 15.577  -66.933 0.00 37.81  ? 632  ILE   A HG12 1 
ATOM   9048  H HG13 . ILE   A  1 606 ? 42.312 15.267  -65.523 0.00 37.28  ? 632  ILE   A HG13 1 
ATOM   9049  H HG21 . ILE   A  1 606 ? 43.442 13.503  -68.352 0.00 34.68  ? 632  ILE   A HG21 1 
ATOM   9050  H HG22 . ILE   A  1 606 ? 42.707 12.066  -67.595 0.00 34.19  ? 632  ILE   A HG22 1 
ATOM   9051  H HG23 . ILE   A  1 606 ? 41.815 13.612  -67.653 0.00 34.50  ? 632  ILE   A HG23 1 
ATOM   9052  H HD11 . ILE   A  1 606 ? 44.089 16.658  -64.705 0.00 40.70  ? 632  ILE   A HD11 1 
ATOM   9053  H HD12 . ILE   A  1 606 ? 44.523 15.011  -64.158 0.00 40.16  ? 632  ILE   A HD12 1 
ATOM   9054  H HD13 . ILE   A  1 606 ? 45.327 15.723  -65.576 0.00 40.79  ? 632  ILE   A HD13 1 
ATOM   9055  N N    . SER   A  1 607 ? 40.774 11.382  -65.486 1.00 23.33  ? 633  SER   A N    1 
ATOM   9056  C CA   . SER   A  1 607 ? 39.337 11.087  -65.558 1.00 22.93  ? 633  SER   A CA   1 
ATOM   9057  C C    . SER   A  1 607 ? 38.974 9.922   -64.611 1.00 22.45  ? 633  SER   A C    1 
ATOM   9058  O O    . SER   A  1 607 ? 37.994 9.223   -64.866 1.00 22.88  ? 633  SER   A O    1 
ATOM   9059  C CB   . SER   A  1 607 ? 38.952 10.699  -66.988 1.00 24.59  ? 633  SER   A CB   1 
ATOM   9060  O OG   . SER   A  1 607 ? 39.312 11.712  -67.907 1.00 27.75  ? 633  SER   A OG   1 
ATOM   9061  H H    . SER   A  1 607 ? 41.339 10.591  -65.780 0.00 28.59  ? 633  SER   A H    1 
ATOM   9062  H HA   . SER   A  1 607 ? 38.742 11.949  -65.266 0.00 28.31  ? 633  SER   A HA   1 
ATOM   9063  H HB2  . SER   A  1 607 ? 39.466 9.776   -67.256 0.00 30.71  ? 633  SER   A HB2  1 
ATOM   9064  H HB3  . SER   A  1 607 ? 37.874 10.557  -67.046 0.00 30.89  ? 633  SER   A HB3  1 
ATOM   9065  H HG   . SER   A  1 607 ? 39.364 12.593  -67.453 0.00 34.96  ? 633  SER   A HG   1 
ATOM   9066  N N    . ILE   A  1 608 ? 39.728 9.728   -63.520 1.00 21.45  ? 634  ILE   A N    1 
ATOM   9067  C CA   . ILE   A  1 608 ? 39.520 8.618   -62.585 1.00 21.17  ? 634  ILE   A CA   1 
ATOM   9068  C C    . ILE   A  1 608 ? 38.057 8.443   -62.109 1.00 20.68  ? 634  ILE   A C    1 
ATOM   9069  O O    . ILE   A  1 608 ? 37.613 7.306   -61.966 1.00 21.71  ? 634  ILE   A O    1 
ATOM   9070  C CB   . ILE   A  1 608 ? 40.505 8.699   -61.381 1.00 21.64  ? 634  ILE   A CB   1 
ATOM   9071  C CG1  . ILE   A  1 608 ? 40.447 7.405   -60.530 1.00 21.98  ? 634  ILE   A CG1  1 
ATOM   9072  C CG2  . ILE   A  1 608 ? 40.247 9.946   -60.502 1.00 22.30  ? 634  ILE   A CG2  1 
ATOM   9073  C CD1  . ILE   A  1 608 ? 41.604 7.267   -59.523 1.00 22.88  ? 634  ILE   A CD1  1 
ATOM   9074  H H    . ILE   A  1 608 ? 40.494 10.335  -63.245 0.00 25.45  ? 634  ILE   A H    1 
ATOM   9075  H HA   . ILE   A  1 608 ? 39.793 7.725   -63.138 0.00 24.88  ? 634  ILE   A HA   1 
ATOM   9076  H HB   . ILE   A  1 608 ? 41.514 8.783   -61.782 0.00 24.97  ? 634  ILE   A HB   1 
ATOM   9077  H HG12 . ILE   A  1 608 ? 39.523 7.395   -59.952 0.00 24.80  ? 634  ILE   A HG12 1 
ATOM   9078  H HG13 . ILE   A  1 608 ? 40.477 6.543   -61.194 0.00 25.09  ? 634  ILE   A HG13 1 
ATOM   9079  H HG21 . ILE   A  1 608 ? 41.088 10.075  -59.822 0.00 25.31  ? 634  ILE   A HG21 1 
ATOM   9080  H HG22 . ILE   A  1 608 ? 40.150 10.824  -61.138 0.00 25.86  ? 634  ILE   A HG22 1 
ATOM   9081  H HG23 . ILE   A  1 608 ? 39.334 9.796   -59.928 0.00 25.42  ? 634  ILE   A HG23 1 
ATOM   9082  H HD11 . ILE   A  1 608 ? 41.547 6.286   -59.055 0.00 25.45  ? 634  ILE   A HD11 1 
ATOM   9083  H HD12 . ILE   A  1 608 ? 42.549 7.374   -60.054 0.00 25.79  ? 634  ILE   A HD12 1 
ATOM   9084  H HD13 . ILE   A  1 608 ? 41.515 8.042   -58.763 0.00 25.48  ? 634  ILE   A HD13 1 
ATOM   9085  N N    . PHE   A  1 609 ? 37.326 9.516   -61.850 1.00 19.47  ? 635  PHE   A N    1 
ATOM   9086  C CA   . PHE   A  1 609 ? 35.935 9.426   -61.364 1.00 19.54  ? 635  PHE   A CA   1 
ATOM   9087  C C    . PHE   A  1 609 ? 34.871 9.786   -62.428 1.00 20.24  ? 635  PHE   A C    1 
ATOM   9088  O O    . PHE   A  1 609 ? 33.676 9.643   -62.148 1.00 20.58  ? 635  PHE   A O    1 
ATOM   9089  C CB   . PHE   A  1 609 ? 35.750 10.345  -60.153 1.00 19.10  ? 635  PHE   A CB   1 
ATOM   9090  C CG   . PHE   A  1 609 ? 36.764 10.131  -59.051 1.00 19.76  ? 635  PHE   A CG   1 
ATOM   9091  C CD1  . PHE   A  1 609 ? 37.031 8.859   -58.566 1.00 20.57  ? 635  PHE   A CD1  1 
ATOM   9092  C CD2  . PHE   A  1 609 ? 37.457 11.199  -58.509 1.00 20.61  ? 635  PHE   A CD2  1 
ATOM   9093  C CE1  . PHE   A  1 609 ? 37.977 8.665   -57.565 1.00 21.13  ? 635  PHE   A CE1  1 
ATOM   9094  C CE2  . PHE   A  1 609 ? 38.407 10.999  -57.515 1.00 20.80  ? 635  PHE   A CE2  1 
ATOM   9095  C CZ   . PHE   A  1 609 ? 38.642 9.738   -57.034 1.00 21.03  ? 635  PHE   A CZ   1 
ATOM   9096  H H    . PHE   A  1 609 ? 37.655 10.470  -61.961 0.00 22.90  ? 635  PHE   A H    1 
ATOM   9097  H HA   . PHE   A  1 609 ? 35.713 8.414   -61.028 0.00 22.67  ? 635  PHE   A HA   1 
ATOM   9098  H HB2  . PHE   A  1 609 ? 35.828 11.378  -60.489 0.00 22.31  ? 635  PHE   A HB2  1 
ATOM   9099  H HB3  . PHE   A  1 609 ? 34.763 10.171  -59.728 0.00 22.05  ? 635  PHE   A HB3  1 
ATOM   9100  H HD1  . PHE   A  1 609 ? 36.504 8.011   -58.968 0.00 23.11  ? 635  PHE   A HD1  1 
ATOM   9101  H HD2  . PHE   A  1 609 ? 37.276 12.196  -58.870 0.00 23.59  ? 635  PHE   A HD2  1 
ATOM   9102  H HE1  . PHE   A  1 609 ? 38.168 7.673   -57.190 0.00 23.08  ? 635  PHE   A HE1  1 
ATOM   9103  H HE2  . PHE   A  1 609 ? 38.931 11.839  -57.096 0.00 23.11  ? 635  PHE   A HE2  1 
ATOM   9104  H HZ   . PHE   A  1 609 ? 39.374 9.586   -56.259 0.00 22.82  ? 635  PHE   A HZ   1 
ATOM   9105  N N    . LYS   A  1 610 ? 35.280 10.223  -63.630 1.00 20.29  ? 636  LYS   A N    1 
ATOM   9106  C CA   . LYS   A  1 610 ? 34.345 10.637  -64.681 1.00 21.21  ? 636  LYS   A CA   1 
ATOM   9107  C C    . LYS   A  1 610 ? 33.306 9.566   -65.064 1.00 22.23  ? 636  LYS   A C    1 
ATOM   9108  O O    . LYS   A  1 610 ? 32.150 9.906   -65.323 1.00 22.07  ? 636  LYS   A O    1 
ATOM   9109  C CB   . LYS   A  1 610 ? 35.123 11.071  -65.936 1.00 23.93  ? 636  LYS   A CB   1 
ATOM   9110  C CG   . LYS   A  1 610 ? 34.238 11.717  -66.993 1.00 30.07  ? 636  LYS   A CG   1 
ATOM   9111  C CD   . LYS   A  1 610 ? 35.058 12.455  -68.039 1.00 35.81  ? 636  LYS   A CD   1 
ATOM   9112  C CE   . LYS   A  1 610 ? 34.173 13.240  -68.976 1.00 41.88  ? 636  LYS   A CE   1 
ATOM   9113  N NZ   . LYS   A  1 610 ? 34.978 14.090  -69.903 1.00 46.00  ? 636  LYS   A NZ   1 
ATOM   9114  H H    . LYS   A  1 610 ? 36.253 10.300  -63.909 0.00 24.71  ? 636  LYS   A H    1 
ATOM   9115  H HA   . LYS   A  1 610 ? 33.794 11.504  -64.323 0.00 26.51  ? 636  LYS   A HA   1 
ATOM   9116  H HB2  . LYS   A  1 610 ? 35.881 11.797  -65.645 0.00 29.98  ? 636  LYS   A HB2  1 
ATOM   9117  H HB3  . LYS   A  1 610 ? 35.596 10.196  -66.379 0.00 30.10  ? 636  LYS   A HB3  1 
ATOM   9118  H HG2  . LYS   A  1 610 ? 33.664 10.950  -67.509 0.00 38.35  ? 636  LYS   A HG2  1 
ATOM   9119  H HG3  . LYS   A  1 610 ? 33.570 12.432  -66.515 0.00 38.18  ? 636  LYS   A HG3  1 
ATOM   9120  H HD2  . LYS   A  1 610 ? 35.732 13.155  -67.547 0.00 45.22  ? 636  LYS   A HD2  1 
ATOM   9121  H HD3  . LYS   A  1 610 ? 35.624 11.735  -68.628 0.00 45.48  ? 636  LYS   A HD3  1 
ATOM   9122  H HE2  . LYS   A  1 610 ? 33.579 12.550  -69.573 0.00 53.66  ? 636  LYS   A HE2  1 
ATOM   9123  H HE3  . LYS   A  1 610 ? 33.523 13.893  -68.395 0.00 53.38  ? 636  LYS   A HE3  1 
ATOM   9124  H HZ1  . LYS   A  1 610 ? 34.361 14.641  -70.491 0.00 59.22  ? 636  LYS   A HZ1  1 
ATOM   9125  H HZ2  . LYS   A  1 610 ? 35.573 14.716  -69.370 0.00 58.52  ? 636  LYS   A HZ2  1 
ATOM   9126  H HZ3  . LYS   A  1 610 ? 35.559 13.503  -70.493 0.00 58.81  ? 636  LYS   A HZ3  1 
ATOM   9127  N N    . GLY   A  1 611 ? 33.730 8.304   -65.099 1.00 22.02  ? 637  GLY   A N    1 
ATOM   9128  C CA   . GLY   A  1 611 ? 32.872 7.174   -65.436 1.00 22.27  ? 637  GLY   A CA   1 
ATOM   9129  C C    . GLY   A  1 611 ? 31.862 6.797   -64.368 1.00 22.12  ? 637  GLY   A C    1 
ATOM   9130  O O    . GLY   A  1 611 ? 31.036 5.912   -64.596 1.00 22.44  ? 637  GLY   A O    1 
ATOM   9131  H H    . GLY   A  1 611 ? 34.688 8.024   -64.913 0.00 27.15  ? 637  GLY   A H    1 
ATOM   9132  H HA2  . GLY   A  1 611 ? 32.323 7.410   -66.347 0.00 28.39  ? 637  GLY   A HA2  1 
ATOM   9133  H HA3  . GLY   A  1 611 ? 33.493 6.305   -65.638 0.00 27.81  ? 637  GLY   A HA3  1 
ATOM   9134  N N    . LEU   A  1 612 ? 31.889 7.471   -63.197 1.00 21.24  ? 638  LEU   A N    1 
ATOM   9135  C CA   . LEU   A  1 612 ? 30.898 7.251   -62.146 1.00 20.80  ? 638  LEU   A CA   1 
ATOM   9136  C C    . LEU   A  1 612 ? 29.742 8.196   -62.518 1.00 21.73  ? 638  LEU   A C    1 
ATOM   9137  O O    . LEU   A  1 612 ? 29.510 9.225   -61.886 1.00 21.42  ? 638  LEU   A O    1 
ATOM   9138  C CB   . LEU   A  1 612 ? 31.510 7.555   -60.764 1.00 19.90  ? 638  LEU   A CB   1 
ATOM   9139  C CG   . LEU   A  1 612 ? 32.769 6.726   -60.440 1.00 20.03  ? 638  LEU   A CG   1 
ATOM   9140  C CD1  . LEU   A  1 612 ? 33.405 7.168   -59.122 1.00 19.36  ? 638  LEU   A CD1  1 
ATOM   9141  C CD2  . LEU   A  1 612 ? 32.464 5.240   -60.396 1.00 20.63  ? 638  LEU   A CD2  1 
ATOM   9142  H H    . LEU   A  1 612 ? 32.582 8.168   -62.943 0.00 25.85  ? 638  LEU   A H    1 
ATOM   9143  H HA   . LEU   A  1 612 ? 30.527 6.228   -62.153 0.00 25.30  ? 638  LEU   A HA   1 
ATOM   9144  H HB2  . LEU   A  1 612 ? 31.796 8.606   -60.727 0.00 23.67  ? 638  LEU   A HB2  1 
ATOM   9145  H HB3  . LEU   A  1 612 ? 30.768 7.344   -59.997 0.00 23.50  ? 638  LEU   A HB3  1 
ATOM   9146  H HG   . LEU   A  1 612 ? 33.513 6.888   -61.220 0.00 23.52  ? 638  LEU   A HG   1 
ATOM   9147  H HD11 . LEU   A  1 612 ? 34.349 6.641   -58.996 0.00 21.84  ? 638  LEU   A HD11 1 
ATOM   9148  H HD12 . LEU   A  1 612 ? 33.580 8.242   -59.156 0.00 22.14  ? 638  LEU   A HD12 1 
ATOM   9149  H HD13 . LEU   A  1 612 ? 32.729 6.923   -58.304 0.00 21.90  ? 638  LEU   A HD13 1 
ATOM   9150  H HD21 . LEU   A  1 612 ? 33.321 4.716   -59.976 0.00 23.74  ? 638  LEU   A HD21 1 
ATOM   9151  H HD22 . LEU   A  1 612 ? 31.584 5.074   -59.776 0.00 23.99  ? 638  LEU   A HD22 1 
ATOM   9152  H HD23 . LEU   A  1 612 ? 32.281 4.881   -61.408 0.00 24.41  ? 638  LEU   A HD23 1 
ATOM   9153  N N    . LYS   A  1 613 ? 29.042 7.828   -63.595 1.00 22.26  ? 639  LYS   A N    1 
ATOM   9154  C CA   . LYS   A  1 613 ? 28.034 8.653   -64.256 1.00 23.91  ? 639  LYS   A CA   1 
ATOM   9155  C C    . LYS   A  1 613 ? 26.821 9.034   -63.399 1.00 23.80  ? 639  LYS   A C    1 
ATOM   9156  O O    . LYS   A  1 613 ? 26.194 10.045  -63.689 1.00 24.58  ? 639  LYS   A O    1 
ATOM   9157  C CB   . LYS   A  1 613 ? 27.577 7.981   -65.563 1.00 26.89  ? 639  LYS   A CB   1 
ATOM   9158  C CG   . LYS   A  1 613 ? 28.723 7.834   -66.563 1.00 34.27  ? 639  LYS   A CG   1 
ATOM   9159  C CD   . LYS   A  1 613 ? 28.280 7.418   -67.952 1.00 41.90  ? 639  LYS   A CD   1 
ATOM   9160  C CE   . LYS   A  1 613 ? 29.439 7.482   -68.924 1.00 46.97  ? 639  LYS   A CE   1 
ATOM   9161  N NZ   . LYS   A  1 613 ? 29.035 7.105   -70.307 1.00 50.27  ? 639  LYS   A NZ   1 
ATOM   9162  H H    . LYS   A  1 613 ? 29.152 6.914   -64.022 0.00 28.12  ? 639  LYS   A H    1 
ATOM   9163  H HA   . LYS   A  1 613 ? 28.510 9.592   -64.532 0.00 30.74  ? 639  LYS   A HA   1 
ATOM   9164  H HB2  . LYS   A  1 613 ? 27.188 6.988   -65.342 0.00 34.72  ? 639  LYS   A HB2  1 
ATOM   9165  H HB3  . LYS   A  1 613 ? 26.802 8.590   -66.026 0.00 35.27  ? 639  LYS   A HB3  1 
ATOM   9166  H HG2  . LYS   A  1 613 ? 29.234 8.792   -66.652 0.00 43.77  ? 639  LYS   A HG2  1 
ATOM   9167  H HG3  . LYS   A  1 613 ? 29.416 7.079   -66.195 0.00 43.36  ? 639  LYS   A HG3  1 
ATOM   9168  H HD2  . LYS   A  1 613 ? 27.915 6.393   -67.923 0.00 53.59  ? 639  LYS   A HD2  1 
ATOM   9169  H HD3  . LYS   A  1 613 ? 27.499 8.092   -68.302 0.00 54.03  ? 639  LYS   A HD3  1 
ATOM   9170  H HE2  . LYS   A  1 613 ? 29.823 8.501   -68.952 0.00 59.83  ? 639  LYS   A HE2  1 
ATOM   9171  H HE3  . LYS   A  1 613 ? 30.219 6.795   -68.597 0.00 59.44  ? 639  LYS   A HE3  1 
ATOM   9172  H HZ1  . LYS   A  1 613 ? 29.833 7.168   -70.931 0.00 64.60  ? 639  LYS   A HZ1  1 
ATOM   9173  H HZ2  . LYS   A  1 613 ? 28.683 6.153   -70.317 0.00 64.53  ? 639  LYS   A HZ2  1 
ATOM   9174  H HZ3  . LYS   A  1 613 ? 28.306 7.729   -70.638 0.00 64.90  ? 639  LYS   A HZ3  1 
ATOM   9175  N N    . ASN   A  1 614 ? 26.497 8.262   -62.360 1.00 22.96  ? 640  ASN   A N    1 
ATOM   9176  C CA   . ASN   A  1 614 ? 25.348 8.545   -61.505 1.00 22.80  ? 640  ASN   A CA   1 
ATOM   9177  C C    . ASN   A  1 614 ? 25.762 9.137   -60.132 1.00 21.80  ? 640  ASN   A C    1 
ATOM   9178  O O    . ASN   A  1 614 ? 24.910 9.267   -59.258 1.00 21.77  ? 640  ASN   A O    1 
ATOM   9179  C CB   . ASN   A  1 614 ? 24.602 7.207   -61.289 1.00 23.92  ? 640  ASN   A CB   1 
ATOM   9180  C CG   . ASN   A  1 614 ? 23.175 7.327   -60.968 1.00 26.40  ? 640  ASN   A CG   1 
ATOM   9181  O OD1  . ASN   A  1 614 ? 22.482 8.153   -61.576 1.00 25.38  ? 640  ASN   A OD1  1 
ATOM   9182  N ND2  . ASN   A  1 614 ? 22.599 6.441   -60.176 1.00 29.04  ? 640  ASN   A ND2  1 
ATOM   9183  H H    . ASN   A  1 614 ? 27.003 7.427   -62.080 0.00 28.82  ? 640  ASN   A H    1 
ATOM   9184  H HA   . ASN   A  1 614 ? 24.679 9.253   -61.991 0.00 29.49  ? 640  ASN   A HA   1 
ATOM   9185  H HB2  . ASN   A  1 614 ? 24.685 6.618   -62.201 0.00 30.63  ? 640  ASN   A HB2  1 
ATOM   9186  H HB3  . ASN   A  1 614 ? 25.080 6.673   -60.468 0.00 29.87  ? 640  ASN   A HB3  1 
ATOM   9187  H HD21 . ASN   A  1 614 ? 22.214 7.214   -59.674 0.00 36.69  ? 640  ASN   A HD21 1 
ATOM   9188  H HD22 . ASN   A  1 614 ? 23.055 5.614   -59.805 0.00 36.31  ? 640  ASN   A HD22 1 
ATOM   9189  N N    . LEU   A  1 615 ? 27.046 9.496   -59.934 1.00 20.36  ? 641  LEU   A N    1 
ATOM   9190  C CA   . LEU   A  1 615 ? 27.555 9.918   -58.636 1.00 20.96  ? 641  LEU   A CA   1 
ATOM   9191  C C    . LEU   A  1 615 ? 27.016 11.254  -58.154 1.00 21.70  ? 641  LEU   A C    1 
ATOM   9192  O O    . LEU   A  1 615 ? 27.081 12.233  -58.889 1.00 22.09  ? 641  LEU   A O    1 
ATOM   9193  C CB   . LEU   A  1 615 ? 29.098 9.971   -58.648 1.00 20.72  ? 641  LEU   A CB   1 
ATOM   9194  C CG   . LEU   A  1 615 ? 29.790 9.720   -57.297 1.00 22.49  ? 641  LEU   A CG   1 
ATOM   9195  C CD1  . LEU   A  1 615 ? 29.754 8.232   -56.925 1.00 22.77  ? 641  LEU   A CD1  1 
ATOM   9196  C CD2  . LEU   A  1 615 ? 31.214 10.187  -57.328 1.00 23.93  ? 641  LEU   A CD2  1 
ATOM   9197  H H    . LEU   A  1 615 ? 27.745 9.537   -60.668 0.00 25.23  ? 641  LEU   A H    1 
ATOM   9198  H HA   . LEU   A  1 615 ? 27.238 9.160   -57.924 0.00 25.11  ? 641  LEU   A HA   1 
ATOM   9199  H HB2  . LEU   A  1 615 ? 29.489 9.245   -59.358 0.00 24.74  ? 641  LEU   A HB2  1 
ATOM   9200  H HB3  . LEU   A  1 615 ? 29.371 10.976  -58.962 0.00 24.89  ? 641  LEU   A HB3  1 
ATOM   9201  H HG   . LEU   A  1 615 ? 29.270 10.275  -56.517 0.00 26.18  ? 641  LEU   A HG   1 
ATOM   9202  H HD11 . LEU   A  1 615 ? 30.416 8.059   -56.078 0.00 25.86  ? 641  LEU   A HD11 1 
ATOM   9203  H HD12 . LEU   A  1 615 ? 28.739 7.951   -56.651 0.00 26.38  ? 641  LEU   A HD12 1 
ATOM   9204  H HD13 . LEU   A  1 615 ? 30.084 7.648   -57.782 0.00 26.39  ? 641  LEU   A HD13 1 
ATOM   9205  H HD21 . LEU   A  1 615 ? 31.622 10.069  -56.326 0.00 27.34  ? 641  LEU   A HD21 1 
ATOM   9206  H HD22 . LEU   A  1 615 ? 31.773 9.575   -58.034 0.00 27.75  ? 641  LEU   A HD22 1 
ATOM   9207  H HD23 . LEU   A  1 615 ? 31.251 11.232  -57.627 0.00 27.97  ? 641  LEU   A HD23 1 
ATOM   9208  N N    . THR   A  1 616 ? 26.518 11.297  -56.911 1.00 21.95  ? 642  THR   A N    1 
ATOM   9209  C CA   . THR   A  1 616 ? 26.022 12.523  -56.293 1.00 22.66  ? 642  THR   A CA   1 
ATOM   9210  C C    . THR   A  1 616 ? 26.870 12.931  -55.082 1.00 22.25  ? 642  THR   A C    1 
ATOM   9211  O O    . THR   A  1 616 ? 26.947 14.114  -54.791 1.00 22.57  ? 642  THR   A O    1 
ATOM   9212  C CB   . THR   A  1 616 ? 24.510 12.423  -55.973 1.00 25.04  ? 642  THR   A CB   1 
ATOM   9213  O OG1  . THR   A  1 616 ? 24.269 11.377  -55.037 1.00 26.70  ? 642  THR   A OG1  1 
ATOM   9214  C CG2  . THR   A  1 616 ? 23.672 12.225  -57.222 1.00 25.97  ? 642  THR   A CG2  1 
ATOM   9215  H H    . THR   A  1 616 ? 26.428 10.487  -56.305 0.00 26.21  ? 642  THR   A H    1 
ATOM   9216  H HA   . THR   A  1 616 ? 26.091 13.331  -57.015 0.00 27.89  ? 642  THR   A HA   1 
ATOM   9217  H HB   . THR   A  1 616 ? 24.190 13.359  -55.521 0.00 30.86  ? 642  THR   A HB   1 
ATOM   9218  H HG1  . THR   A  1 616 ? 23.300 11.322  -54.827 0.00 32.54  ? 642  THR   A HG1  1 
ATOM   9219  H HG21 . THR   A  1 616 ? 22.612 12.236  -56.968 0.00 32.70  ? 642  THR   A HG21 1 
ATOM   9220  H HG22 . THR   A  1 616 ? 23.874 13.016  -57.942 0.00 32.75  ? 642  THR   A HG22 1 
ATOM   9221  H HG23 . THR   A  1 616 ? 23.909 11.268  -57.679 0.00 32.32  ? 642  THR   A HG23 1 
ATOM   9222  N N    . ARG   A  1 617 ? 27.514 11.987  -54.382 1.00 21.72  ? 643  ARG   A N    1 
ATOM   9223  C CA   . ARG   A  1 617 ? 28.321 12.306  -53.205 1.00 22.18  ? 643  ARG   A CA   1 
ATOM   9224  C C    . ARG   A  1 617 ? 29.728 11.762  -53.387 1.00 21.91  ? 643  ARG   A C    1 
ATOM   9225  O O    . ARG   A  1 617 ? 29.899 10.564  -53.625 1.00 22.11  ? 643  ARG   A O    1 
ATOM   9226  C CB   . ARG   A  1 617 ? 27.676 11.721  -51.936 1.00 23.90  ? 643  ARG   A CB   1 
ATOM   9227  C CG   . ARG   A  1 617 ? 28.431 12.112  -50.671 1.00 30.89  ? 643  ARG   A CG   1 
ATOM   9228  C CD   . ARG   A  1 617 ? 27.721 11.727  -49.372 1.00 36.50  ? 643  ARG   A CD   1 
ATOM   9229  N NE   . ARG   A  1 617 ? 28.406 12.298  -48.201 1.00 41.43  ? 643  ARG   A NE   1 
ATOM   9230  C CZ   . ARG   A  1 617 ? 29.542 11.835  -47.674 1.00 44.33  ? 643  ARG   A CZ   1 
ATOM   9231  N NH1  . ARG   A  1 617 ? 30.150 10.775  -48.205 1.00 43.80  ? 643  ARG   A NH1  1 
ATOM   9232  N NH2  . ARG   A  1 617 ? 30.090 12.438  -46.623 1.00 44.48  ? 643  ARG   A NH2  1 
ATOM   9233  H H    . ARG   A  1 617 ? 27.488 10.994  -54.587 0.00 25.25  ? 643  ARG   A H    1 
ATOM   9234  H HA   . ARG   A  1 617 ? 28.387 13.383  -53.067 0.00 25.63  ? 643  ARG   A HA   1 
ATOM   9235  H HB2  . ARG   A  1 617 ? 26.657 12.095  -51.852 0.00 27.57  ? 643  ARG   A HB2  1 
ATOM   9236  H HB3  . ARG   A  1 617 ? 27.670 10.634  -52.007 0.00 27.10  ? 643  ARG   A HB3  1 
ATOM   9237  H HG2  . ARG   A  1 617 ? 29.402 11.619  -50.661 0.00 34.96  ? 643  ARG   A HG2  1 
ATOM   9238  H HG3  . ARG   A  1 617 ? 28.567 13.192  -50.668 0.00 35.44  ? 643  ARG   A HG3  1 
ATOM   9239  H HD2  . ARG   A  1 617 ? 26.710 12.129  -49.394 0.00 42.12  ? 643  ARG   A HD2  1 
ATOM   9240  H HD3  . ARG   A  1 617 ? 27.682 10.643  -49.273 0.00 41.60  ? 643  ARG   A HD3  1 
ATOM   9241  H HE   . ARG   A  1 617 ? 27.979 13.113  -47.772 0.00 47.61  ? 643  ARG   A HE   1 
ATOM   9242  H HH11 . ARG   A  1 617 ? 29.777 10.284  -49.010 0.00 49.80  ? 643  ARG   A HH11 1 
ATOM   9243  H HH12 . ARG   A  1 617 ? 31.014 10.439  -47.791 0.00 49.37  ? 643  ARG   A HH12 1 
ATOM   9244  H HH21 . ARG   A  1 617 ? 29.640 13.248  -46.209 0.00 50.68  ? 643  ARG   A HH21 1 
ATOM   9245  H HH22 . ARG   A  1 617 ? 30.954 12.086  -46.222 0.00 50.21  ? 643  ARG   A HH22 1 
ATOM   9246  N N    . LEU   A  1 618 ? 30.739 12.638  -53.266 1.00 21.00  ? 644  LEU   A N    1 
ATOM   9247  C CA   . LEU   A  1 618 ? 32.139 12.244  -53.428 1.00 20.85  ? 644  LEU   A CA   1 
ATOM   9248  C C    . LEU   A  1 618 ? 32.976 12.792  -52.274 1.00 20.31  ? 644  LEU   A C    1 
ATOM   9249  O O    . LEU   A  1 618 ? 32.917 13.992  -51.986 1.00 20.54  ? 644  LEU   A O    1 
ATOM   9250  C CB   . LEU   A  1 618 ? 32.654 12.767  -54.781 1.00 21.28  ? 644  LEU   A CB   1 
ATOM   9251  C CG   . LEU   A  1 618 ? 34.131 12.522  -55.112 1.00 22.91  ? 644  LEU   A CG   1 
ATOM   9252  C CD1  . LEU   A  1 618 ? 34.464 11.006  -55.148 1.00 23.17  ? 644  LEU   A CD1  1 
ATOM   9253  C CD2  . LEU   A  1 618 ? 34.501 13.157  -56.446 1.00 23.35  ? 644  LEU   A CD2  1 
ATOM   9254  H H    . LEU   A  1 618 ? 30.624 13.624  -53.058 0.00 23.78  ? 644  LEU   A H    1 
ATOM   9255  H HA   . LEU   A  1 618 ? 32.220 11.159  -53.420 0.00 22.93  ? 644  LEU   A HA   1 
ATOM   9256  H HB2  . LEU   A  1 618 ? 32.085 12.249  -55.549 0.00 24.20  ? 644  LEU   A HB2  1 
ATOM   9257  H HB3  . LEU   A  1 618 ? 32.468 13.838  -54.842 0.00 24.25  ? 644  LEU   A HB3  1 
ATOM   9258  H HG   . LEU   A  1 618 ? 34.757 12.978  -54.348 0.00 25.56  ? 644  LEU   A HG   1 
ATOM   9259  H HD11 . LEU   A  1 618 ? 35.504 10.892  -55.448 0.00 25.70  ? 644  LEU   A HD11 1 
ATOM   9260  H HD12 . LEU   A  1 618 ? 34.326 10.573  -54.158 0.00 25.48  ? 644  LEU   A HD12 1 
ATOM   9261  H HD13 . LEU   A  1 618 ? 33.821 10.513  -55.873 0.00 25.99  ? 644  LEU   A HD13 1 
ATOM   9262  H HD21 . LEU   A  1 618 ? 35.554 12.971  -56.650 0.00 26.58  ? 644  LEU   A HD21 1 
ATOM   9263  H HD22 . LEU   A  1 618 ? 33.887 12.716  -57.230 0.00 26.93  ? 644  LEU   A HD22 1 
ATOM   9264  H HD23 . LEU   A  1 618 ? 34.317 14.228  -56.393 0.00 26.93  ? 644  LEU   A HD23 1 
ATOM   9265  N N    . ASP   A  1 619 ? 33.755 11.928  -51.608 1.00 18.82  ? 645  ASP   A N    1 
ATOM   9266  C CA   . ASP   A  1 619 ? 34.606 12.372  -50.507 1.00 18.68  ? 645  ASP   A CA   1 
ATOM   9267  C C    . ASP   A  1 619 ? 36.074 12.162  -50.874 1.00 18.74  ? 645  ASP   A C    1 
ATOM   9268  O O    . ASP   A  1 619 ? 36.533 11.027  -50.963 1.00 18.46  ? 645  ASP   A O    1 
ATOM   9269  C CB   . ASP   A  1 619 ? 34.217 11.653  -49.198 1.00 19.38  ? 645  ASP   A CB   1 
ATOM   9270  C CG   . ASP   A  1 619 ? 34.971 12.080  -47.958 1.00 22.11  ? 645  ASP   A CG   1 
ATOM   9271  O OD1  . ASP   A  1 619 ? 35.900 12.891  -48.077 1.00 20.96  ? 645  ASP   A OD1  1 
ATOM   9272  O OD2  . ASP   A  1 619 ? 34.618 11.601  -46.854 1.00 25.46  ? 645  ASP   A OD2  1 
ATOM   9273  H H    . ASP   A  1 619 ? 33.822 10.934  -51.801 0.00 19.83  ? 645  ASP   A H    1 
ATOM   9274  H HA   . ASP   A  1 619 ? 34.466 13.437  -50.348 0.00 19.72  ? 645  ASP   A HA   1 
ATOM   9275  H HB2  . ASP   A  1 619 ? 33.154 11.801  -49.016 0.00 20.18  ? 645  ASP   A HB2  1 
ATOM   9276  H HB3  . ASP   A  1 619 ? 34.430 10.594  -49.310 0.00 19.86  ? 645  ASP   A HB3  1 
ATOM   9277  N N    . LEU   A  1 620 ? 36.786 13.273  -51.125 1.00 18.73  ? 646  LEU   A N    1 
ATOM   9278  C CA   . LEU   A  1 620 ? 38.210 13.317  -51.455 1.00 18.96  ? 646  LEU   A CA   1 
ATOM   9279  C C    . LEU   A  1 620 ? 39.053 13.842  -50.291 1.00 19.26  ? 646  LEU   A C    1 
ATOM   9280  O O    . LEU   A  1 620 ? 40.185 14.287  -50.520 1.00 19.47  ? 646  LEU   A O    1 
ATOM   9281  C CB   . LEU   A  1 620 ? 38.422 14.240  -52.675 1.00 19.99  ? 646  LEU   A CB   1 
ATOM   9282  C CG   . LEU   A  1 620 ? 37.564 13.974  -53.907 1.00 21.13  ? 646  LEU   A CG   1 
ATOM   9283  C CD1  . LEU   A  1 620 ? 37.988 14.854  -55.070 1.00 21.44  ? 646  LEU   A CD1  1 
ATOM   9284  C CD2  . LEU   A  1 620 ? 37.608 12.499  -54.306 1.00 21.74  ? 646  LEU   A CD2  1 
ATOM   9285  H H    . LEU   A  1 620 ? 36.385 14.205  -51.114 0.00 19.87  ? 646  LEU   A H    1 
ATOM   9286  H HA   . LEU   A  1 620 ? 38.578 12.321  -51.696 0.00 19.72  ? 646  LEU   A HA   1 
ATOM   9287  H HB2  . LEU   A  1 620 ? 38.230 15.266  -52.365 0.00 21.70  ? 646  LEU   A HB2  1 
ATOM   9288  H HB3  . LEU   A  1 620 ? 39.457 14.150  -53.000 0.00 21.51  ? 646  LEU   A HB3  1 
ATOM   9289  H HG   . LEU   A  1 620 ? 36.536 14.236  -53.663 0.00 23.29  ? 646  LEU   A HG   1 
ATOM   9290  H HD11 . LEU   A  1 620 ? 37.298 14.712  -55.901 0.00 24.23  ? 646  LEU   A HD11 1 
ATOM   9291  H HD12 . LEU   A  1 620 ? 37.975 15.895  -54.753 0.00 24.14  ? 646  LEU   A HD12 1 
ATOM   9292  H HD13 . LEU   A  1 620 ? 38.996 14.574  -55.374 0.00 23.92  ? 646  LEU   A HD13 1 
ATOM   9293  H HD21 . LEU   A  1 620 ? 37.482 12.417  -55.385 0.00 24.00  ? 646  LEU   A HD21 1 
ATOM   9294  H HD22 . LEU   A  1 620 ? 38.562 12.076  -54.000 0.00 23.52  ? 646  LEU   A HD22 1 
ATOM   9295  H HD23 . LEU   A  1 620 ? 36.798 11.976  -53.801 0.00 23.61  ? 646  LEU   A HD23 1 
ATOM   9296  N N    . SER   A  1 621 ? 38.544 13.763  -49.044 1.00 19.01  ? 647  SER   A N    1 
ATOM   9297  C CA   . SER   A  1 621 ? 39.291 14.258  -47.898 1.00 18.79  ? 647  SER   A CA   1 
ATOM   9298  C C    . SER   A  1 621 ? 40.530 13.422  -47.615 1.00 18.34  ? 647  SER   A C    1 
ATOM   9299  O O    . SER   A  1 621 ? 40.628 12.295  -48.079 1.00 17.98  ? 647  SER   A O    1 
ATOM   9300  C CB   . SER   A  1 621 ? 38.396 14.296  -46.656 1.00 19.22  ? 647  SER   A CB   1 
ATOM   9301  O OG   . SER   A  1 621 ? 38.080 12.997  -46.185 1.00 19.52  ? 647  SER   A OG   1 
ATOM   9302  H H    . SER   A  1 621 ? 37.647 13.358  -48.797 0.00 19.50  ? 647  SER   A H    1 
ATOM   9303  H HA   . SER   A  1 621 ? 39.614 15.279  -48.101 0.00 19.40  ? 647  SER   A HA   1 
ATOM   9304  H HB2  . SER   A  1 621 ? 38.921 14.834  -45.869 0.00 19.55  ? 647  SER   A HB2  1 
ATOM   9305  H HB3  . SER   A  1 621 ? 37.474 14.819  -46.908 0.00 19.77  ? 647  SER   A HB3  1 
ATOM   9306  H HG   . SER   A  1 621 ? 37.271 12.651  -46.647 0.00 19.67  ? 647  SER   A HG   1 
ATOM   9307  N N    . LEU   A  1 622 ? 41.486 13.975  -46.865 1.00 18.71  ? 648  LEU   A N    1 
ATOM   9308  C CA   . LEU   A  1 622 ? 42.686 13.237  -46.443 1.00 19.07  ? 648  LEU   A CA   1 
ATOM   9309  C C    . LEU   A  1 622 ? 43.445 12.589  -47.600 1.00 19.07  ? 648  LEU   A C    1 
ATOM   9310  O O    . LEU   A  1 622 ? 43.884 11.445  -47.492 1.00 19.50  ? 648  LEU   A O    1 
ATOM   9311  C CB   . LEU   A  1 622 ? 42.319 12.189  -45.360 1.00 19.37  ? 648  LEU   A CB   1 
ATOM   9312  C CG   . LEU   A  1 622 ? 41.779 12.729  -44.047 1.00 20.86  ? 648  LEU   A CG   1 
ATOM   9313  C CD1  . LEU   A  1 622 ? 41.292 11.573  -43.147 1.00 21.59  ? 648  LEU   A CD1  1 
ATOM   9314  C CD2  . LEU   A  1 622 ? 42.832 13.563  -43.315 1.00 20.93  ? 648  LEU   A CD2  1 
ATOM   9315  H H    . LEU   A  1 622 ? 41.463 14.935  -46.534 0.00 18.97  ? 648  LEU   A H    1 
ATOM   9316  H HA   . LEU   A  1 622 ? 43.383 13.953  -46.012 0.00 19.16  ? 648  LEU   A HA   1 
ATOM   9317  H HB2  . LEU   A  1 622 ? 41.562 11.516  -45.760 0.00 19.02  ? 648  LEU   A HB2  1 
ATOM   9318  H HB3  . LEU   A  1 622 ? 43.209 11.616  -45.106 0.00 18.99  ? 648  LEU   A HB3  1 
ATOM   9319  H HG   . LEU   A  1 622 ? 40.928 13.377  -44.253 0.00 20.97  ? 648  LEU   A HG   1 
ATOM   9320  H HD11 . LEU   A  1 622 ? 40.893 11.989  -42.223 0.00 21.41  ? 648  LEU   A HD11 1 
ATOM   9321  H HD12 . LEU   A  1 622 ? 40.515 11.019  -43.670 0.00 21.38  ? 648  LEU   A HD12 1 
ATOM   9322  H HD13 . LEU   A  1 622 ? 42.131 10.914  -42.928 0.00 21.31  ? 648  LEU   A HD13 1 
ATOM   9323  H HD21 . LEU   A  1 622 ? 42.477 13.765  -42.306 0.00 20.97  ? 648  LEU   A HD21 1 
ATOM   9324  H HD22 . LEU   A  1 622 ? 43.766 13.005  -43.279 0.00 20.94  ? 648  LEU   A HD22 1 
ATOM   9325  H HD23 . LEU   A  1 622 ? 42.981 14.506  -43.839 0.00 21.26  ? 648  LEU   A HD23 1 
ATOM   9326  N N    . ASN   A  1 623 ? 43.628 13.324  -48.694 1.00 18.26  ? 649  ASN   A N    1 
ATOM   9327  C CA   . ASN   A  1 623 ? 44.376 12.814  -49.844 1.00 18.27  ? 649  ASN   A CA   1 
ATOM   9328  C C    . ASN   A  1 623 ? 45.689 13.610  -50.104 1.00 18.07  ? 649  ASN   A C    1 
ATOM   9329  O O    . ASN   A  1 623 ? 46.286 13.465  -51.175 1.00 17.48  ? 649  ASN   A O    1 
ATOM   9330  C CB   . ASN   A  1 623 ? 43.475 12.796  -51.076 1.00 18.87  ? 649  ASN   A CB   1 
ATOM   9331  C CG   . ASN   A  1 623 ? 42.757 11.468  -51.289 1.00 21.19  ? 649  ASN   A CG   1 
ATOM   9332  O OD1  . ASN   A  1 623 ? 43.187 10.631  -52.100 1.00 20.75  ? 649  ASN   A OD1  1 
ATOM   9333  N ND2  . ASN   A  1 623 ? 41.681 11.236  -50.539 1.00 20.69  ? 649  ASN   A ND2  1 
ATOM   9334  H H    . ASN   A  1 623 ? 43.288 14.273  -48.814 0.00 18.62  ? 649  ASN   A H    1 
ATOM   9335  H HA   . ASN   A  1 623 ? 44.718 11.801  -49.635 0.00 18.36  ? 649  ASN   A HA   1 
ATOM   9336  H HB2  . ASN   A  1 623 ? 42.720 13.575  -50.982 0.00 19.58  ? 649  ASN   A HB2  1 
ATOM   9337  H HB3  . ASN   A  1 623 ? 44.094 12.987  -51.948 0.00 19.67  ? 649  ASN   A HB3  1 
ATOM   9338  H HD21 . ASN   A  1 623 ? 41.168 10.366  -50.642 0.00 21.19  ? 649  ASN   A HD21 1 
ATOM   9339  H HD22 . ASN   A  1 623 ? 41.377 11.929  -49.863 0.00 21.28  ? 649  ASN   A HD22 1 
ATOM   9340  N N    . ARG   A  1 624 ? 46.133 14.424  -49.111 1.00 18.50  ? 650  ARG   A N    1 
ATOM   9341  C CA   . ARG   A  1 624 ? 47.370 15.218  -49.163 1.00 19.80  ? 650  ARG   A CA   1 
ATOM   9342  C C    . ARG   A  1 624 ? 47.429 16.167  -50.352 1.00 20.74  ? 650  ARG   A C    1 
ATOM   9343  O O    . ARG   A  1 624 ? 48.515 16.512  -50.808 1.00 20.98  ? 650  ARG   A O    1 
ATOM   9344  C CB   . ARG   A  1 624 ? 48.593 14.282  -49.144 1.00 20.76  ? 650  ARG   A CB   1 
ATOM   9345  C CG   . ARG   A  1 624 ? 48.455 13.164  -48.114 1.00 24.16  ? 650  ARG   A CG   1 
ATOM   9346  C CD   . ARG   A  1 624 ? 49.770 12.484  -47.789 1.00 28.65  ? 650  ARG   A CD   1 
ATOM   9347  N NE   . ARG   A  1 624 ? 49.542 11.198  -47.124 1.00 32.41  ? 650  ARG   A NE   1 
ATOM   9348  C CZ   . ARG   A  1 624 ? 50.507 10.375  -46.714 1.00 34.84  ? 650  ARG   A CZ   1 
ATOM   9349  N NH1  . ARG   A  1 624 ? 51.786 10.700  -46.882 1.00 33.80  ? 650  ARG   A NH1  1 
ATOM   9350  N NH2  . ARG   A  1 624 ? 50.200 9.224   -46.130 1.00 35.32  ? 650  ARG   A NH2  1 
ATOM   9351  H H    . ARG   A  1 624 ? 45.653 14.557  -48.227 0.00 18.97  ? 650  ARG   A H    1 
ATOM   9352  H HA   . ARG   A  1 624 ? 47.417 15.828  -48.263 0.00 20.92  ? 650  ARG   A HA   1 
ATOM   9353  H HB2  . ARG   A  1 624 ? 48.700 13.820  -50.125 0.00 22.05  ? 650  ARG   A HB2  1 
ATOM   9354  H HB3  . ARG   A  1 624 ? 49.484 14.858  -48.902 0.00 22.15  ? 650  ARG   A HB3  1 
ATOM   9355  H HG2  . ARG   A  1 624 ? 48.050 13.577  -47.192 0.00 25.62  ? 650  ARG   A HG2  1 
ATOM   9356  H HG3  . ARG   A  1 624 ? 47.780 12.406  -48.511 0.00 25.57  ? 650  ARG   A HG3  1 
ATOM   9357  H HD2  . ARG   A  1 624 ? 50.320 12.300  -48.711 0.00 31.26  ? 650  ARG   A HD2  1 
ATOM   9358  H HD3  . ARG   A  1 624 ? 50.348 13.120  -47.121 0.00 31.21  ? 650  ARG   A HD3  1 
ATOM   9359  H HE   . ARG   A  1 624 ? 48.581 10.910  -46.974 0.00 35.14  ? 650  ARG   A HE   1 
ATOM   9360  H HH11 . ARG   A  1 624 ? 52.061 11.569  -47.328 0.00 37.43  ? 650  ARG   A HH11 1 
ATOM   9361  H HH12 . ARG   A  1 624 ? 52.511 10.066  -46.564 0.00 37.24  ? 650  ARG   A HH12 1 
ATOM   9362  H HH21 . ARG   A  1 624 ? 49.230 8.962   -45.989 0.00 38.38  ? 650  ARG   A HH21 1 
ATOM   9363  H HH22 . ARG   A  1 624 ? 50.934 8.600   -45.812 0.00 38.58  ? 650  ARG   A HH22 1 
ATOM   9364  N N    . LEU   A  1 625 ? 46.269 16.587  -50.864 1.00 21.51  ? 651  LEU   A N    1 
ATOM   9365  C CA   . LEU   A  1 625 ? 46.213 17.446  -52.036 1.00 22.33  ? 651  LEU   A CA   1 
ATOM   9366  C C    . LEU   A  1 625 ? 46.669 18.871  -51.761 1.00 23.61  ? 651  LEU   A C    1 
ATOM   9367  O O    . LEU   A  1 625 ? 46.166 19.509  -50.849 1.00 22.75  ? 651  LEU   A O    1 
ATOM   9368  C CB   . LEU   A  1 625 ? 44.768 17.465  -52.608 1.00 22.39  ? 651  LEU   A CB   1 
ATOM   9369  C CG   . LEU   A  1 625 ? 44.321 16.183  -53.338 1.00 22.53  ? 651  LEU   A CG   1 
ATOM   9370  C CD1  . LEU   A  1 625 ? 42.810 16.103  -53.428 1.00 22.82  ? 651  LEU   A CD1  1 
ATOM   9371  C CD2  . LEU   A  1 625 ? 44.904 16.132  -54.744 1.00 23.13  ? 651  LEU   A CD2  1 
ATOM   9372  H H    . LEU   A  1 625 ? 45.355 16.364  -50.482 0.00 23.29  ? 651  LEU   A H    1 
ATOM   9373  H HA   . LEU   A  1 625 ? 46.876 17.025  -52.791 0.00 24.90  ? 651  LEU   A HA   1 
ATOM   9374  H HB2  . LEU   A  1 625 ? 44.061 17.648  -51.801 0.00 24.86  ? 651  LEU   A HB2  1 
ATOM   9375  H HB3  . LEU   A  1 625 ? 44.704 18.281  -53.326 0.00 25.32  ? 651  LEU   A HB3  1 
ATOM   9376  H HG   . LEU   A  1 625 ? 44.672 15.308  -52.793 0.00 24.67  ? 651  LEU   A HG   1 
ATOM   9377  H HD11 . LEU   A  1 625 ? 42.535 15.205  -53.978 0.00 25.23  ? 651  LEU   A HD11 1 
ATOM   9378  H HD12 . LEU   A  1 625 ? 42.396 16.061  -52.422 0.00 25.10  ? 651  LEU   A HD12 1 
ATOM   9379  H HD13 . LEU   A  1 625 ? 42.439 16.985  -53.949 0.00 25.63  ? 651  LEU   A HD13 1 
ATOM   9380  H HD21 . LEU   A  1 625 ? 44.580 15.210  -55.223 0.00 25.87  ? 651  LEU   A HD21 1 
ATOM   9381  H HD22 . LEU   A  1 625 ? 44.534 16.987  -55.308 0.00 26.29  ? 651  LEU   A HD22 1 
ATOM   9382  H HD23 . LEU   A  1 625 ? 45.991 16.160  -54.702 0.00 26.01  ? 651  LEU   A HD23 1 
ATOM   9383  N N    . LYS   A  1 626 ? 47.627 19.365  -52.555 1.00 24.56  ? 652  LYS   A N    1 
ATOM   9384  C CA   . LYS   A  1 626 ? 48.095 20.759  -52.486 1.00 26.15  ? 652  LYS   A CA   1 
ATOM   9385  C C    . LYS   A  1 626 ? 47.349 21.609  -53.537 1.00 27.15  ? 652  LYS   A C    1 
ATOM   9386  O O    . LYS   A  1 626 ? 47.120 22.798  -53.333 1.00 27.32  ? 652  LYS   A O    1 
ATOM   9387  C CB   . LYS   A  1 626 ? 49.617 20.828  -52.668 1.00 28.56  ? 652  LYS   A CB   1 
ATOM   9388  C CG   . LYS   A  1 626 ? 50.360 20.241  -51.474 1.00 34.82  ? 652  LYS   A CG   1 
ATOM   9389  C CD   . LYS   A  1 626 ? 51.862 20.394  -51.600 1.00 41.51  ? 652  LYS   A CD   1 
ATOM   9390  C CE   . LYS   A  1 626 ? 52.575 19.863  -50.381 1.00 47.02  ? 652  LYS   A CE   1 
ATOM   9391  N NZ   . LYS   A  1 626 ? 54.054 19.869  -50.570 1.00 51.03  ? 652  LYS   A NZ   1 
ATOM   9392  H H    . LYS   A  1 626 ? 48.102 18.825  -53.270 0.00 28.20  ? 652  LYS   A H    1 
ATOM   9393  H HA   . LYS   A  1 626 ? 47.856 21.190  -51.514 0.00 30.46  ? 652  LYS   A HA   1 
ATOM   9394  H HB2  . LYS   A  1 626 ? 49.905 20.268  -53.556 0.00 33.61  ? 652  LYS   A HB2  1 
ATOM   9395  H HB3  . LYS   A  1 626 ? 49.913 21.871  -52.767 0.00 33.96  ? 652  LYS   A HB3  1 
ATOM   9396  H HG2  . LYS   A  1 626 ? 50.043 20.760  -50.570 0.00 40.80  ? 652  LYS   A HG2  1 
ATOM   9397  H HG3  . LYS   A  1 626 ? 50.131 19.178  -51.397 0.00 40.48  ? 652  LYS   A HG3  1 
ATOM   9398  H HD2  . LYS   A  1 626 ? 52.207 19.832  -52.467 0.00 49.11  ? 652  LYS   A HD2  1 
ATOM   9399  H HD3  . LYS   A  1 626 ? 52.109 21.450  -51.705 0.00 49.45  ? 652  LYS   A HD3  1 
ATOM   9400  H HE2  . LYS   A  1 626 ? 52.338 20.493  -49.525 0.00 55.51  ? 652  LYS   A HE2  1 
ATOM   9401  H HE3  . LYS   A  1 626 ? 52.257 18.838  -50.196 0.00 55.12  ? 652  LYS   A HE3  1 
ATOM   9402  H HZ1  . LYS   A  1 626 ? 54.511 19.514  -49.735 0.00 60.43  ? 652  LYS   A HZ1  1 
ATOM   9403  H HZ2  . LYS   A  1 626 ? 54.306 19.281  -51.357 0.00 60.54  ? 652  LYS   A HZ2  1 
ATOM   9404  H HZ3  . LYS   A  1 626 ? 54.379 20.814  -50.746 0.00 60.90  ? 652  LYS   A HZ3  1 
ATOM   9405  N N    . HIS   A  1 627 ? 46.975 20.991  -54.658 1.00 28.01  ? 653  HIS   A N    1 
ATOM   9406  C CA   . HIS   A  1 627 ? 46.154 21.606  -55.698 1.00 29.78  ? 653  HIS   A CA   1 
ATOM   9407  C C    . HIS   A  1 627 ? 45.553 20.491  -56.570 1.00 29.04  ? 653  HIS   A C    1 
ATOM   9408  O O    . HIS   A  1 627 ? 46.103 19.388  -56.630 1.00 29.55  ? 653  HIS   A O    1 
ATOM   9409  C CB   . HIS   A  1 627 ? 46.994 22.566  -56.549 1.00 33.11  ? 653  HIS   A CB   1 
ATOM   9410  C CG   . HIS   A  1 627 ? 48.073 21.870  -57.303 1.00 39.68  ? 653  HIS   A CG   1 
ATOM   9411  N ND1  . HIS   A  1 627 ? 49.254 21.497  -56.692 1.00 42.79  ? 653  HIS   A ND1  1 
ATOM   9412  C CD2  . HIS   A  1 627 ? 48.096 21.457  -58.590 1.00 42.29  ? 653  HIS   A CD2  1 
ATOM   9413  C CE1  . HIS   A  1 627 ? 49.967 20.887  -57.622 1.00 43.89  ? 653  HIS   A CE1  1 
ATOM   9414  N NE2  . HIS   A  1 627 ? 49.305 20.833  -58.781 1.00 44.16  ? 653  HIS   A NE2  1 
ATOM   9415  H H    . HIS   A  1 627 ? 47.286 20.054  -54.896 0.00 32.95  ? 653  HIS   A H    1 
ATOM   9416  H HA   . HIS   A  1 627 ? 45.340 22.168  -55.243 0.00 35.72  ? 653  HIS   A HA   1 
ATOM   9417  H HB2  . HIS   A  1 627 ? 46.345 23.061  -57.269 0.00 40.50  ? 653  HIS   A HB2  1 
ATOM   9418  H HB3  . HIS   A  1 627 ? 47.459 23.308  -55.901 0.00 40.31  ? 653  HIS   A HB3  1 
ATOM   9419  H HD1  . HIS   A  1 627 ? 49.519 21.661  -55.727 0.00 51.49  ? 653  HIS   A HD1  1 
ATOM   9420  H HD2  . HIS   A  1 627 ? 47.317 21.590  -59.321 0.00 51.57  ? 653  HIS   A HD2  1 
ATOM   9421  H HE1  . HIS   A  1 627 ? 50.953 20.482  -57.465 0.00 52.98  ? 653  HIS   A HE1  1 
ATOM   9422  N N    . ILE   A  1 628 ? 44.421 20.759  -57.207 1.00 27.70  ? 654  ILE   A N    1 
ATOM   9423  C CA   . ILE   A  1 628 ? 43.787 19.788  -58.093 1.00 26.61  ? 654  ILE   A CA   1 
ATOM   9424  C C    . ILE   A  1 628 ? 44.009 20.322  -59.500 1.00 25.77  ? 654  ILE   A C    1 
ATOM   9425  O O    . ILE   A  1 628 ? 43.630 21.472  -59.751 1.00 25.42  ? 654  ILE   A O    1 
ATOM   9426  C CB   . ILE   A  1 628 ? 42.278 19.628  -57.789 1.00 26.47  ? 654  ILE   A CB   1 
ATOM   9427  C CG1  . ILE   A  1 628 ? 42.079 19.036  -56.363 1.00 27.49  ? 654  ILE   A CG1  1 
ATOM   9428  C CG2  . ILE   A  1 628 ? 41.623 18.734  -58.864 1.00 26.62  ? 654  ILE   A CG2  1 
ATOM   9429  C CD1  . ILE   A  1 628 ? 40.740 19.279  -55.762 1.00 28.35  ? 654  ILE   A CD1  1 
ATOM   9430  H H    . ILE   A  1 628 ? 43.916 21.637  -57.131 0.00 33.49  ? 654  ILE   A H    1 
ATOM   9431  H HA   . ILE   A  1 628 ? 44.232 18.803  -57.971 0.00 31.56  ? 654  ILE   A HA   1 
ATOM   9432  H HB   . ILE   A  1 628 ? 41.811 20.611  -57.825 0.00 31.93  ? 654  ILE   A HB   1 
ATOM   9433  H HG12 . ILE   A  1 628 ? 42.222 17.958  -56.416 0.00 32.04  ? 654  ILE   A HG12 1 
ATOM   9434  H HG13 . ILE   A  1 628 ? 42.815 19.463  -55.684 0.00 32.25  ? 654  ILE   A HG13 1 
ATOM   9435  H HG21 . ILE   A  1 628 ? 40.631 18.423  -58.542 0.00 31.77  ? 654  ILE   A HG21 1 
ATOM   9436  H HG22 . ILE   A  1 628 ? 41.535 19.283  -59.800 0.00 32.29  ? 654  ILE   A HG22 1 
ATOM   9437  H HG23 . ILE   A  1 628 ? 42.248 17.855  -59.014 0.00 31.65  ? 654  ILE   A HG23 1 
ATOM   9438  H HD11 . ILE   A  1 628 ? 40.558 18.509  -55.015 0.00 32.95  ? 654  ILE   A HD11 1 
ATOM   9439  H HD12 . ILE   A  1 628 ? 40.743 20.259  -55.288 0.00 33.56  ? 654  ILE   A HD12 1 
ATOM   9440  H HD13 . ILE   A  1 628 ? 39.964 19.247  -56.526 0.00 33.50  ? 654  ILE   A HD13 1 
ATOM   9441  N N    . PRO   A  1 629 ? 44.575 19.547  -60.460 1.00 25.34  ? 655  PRO   A N    1 
ATOM   9442  C CA   . PRO   A  1 629 ? 44.724 20.090  -61.828 1.00 24.97  ? 655  PRO   A CA   1 
ATOM   9443  C C    . PRO   A  1 629 ? 43.366 20.500  -62.389 1.00 24.92  ? 655  PRO   A C    1 
ATOM   9444  O O    . PRO   A  1 629 ? 42.372 19.812  -62.144 1.00 24.90  ? 655  PRO   A O    1 
ATOM   9445  C CB   . PRO   A  1 629 ? 45.321 18.924  -62.619 1.00 25.63  ? 655  PRO   A CB   1 
ATOM   9446  C CG   . PRO   A  1 629 ? 45.905 18.018  -61.610 1.00 26.27  ? 655  PRO   A CG   1 
ATOM   9447  C CD   . PRO   A  1 629 ? 45.082 18.163  -60.376 1.00 24.97  ? 655  PRO   A CD   1 
ATOM   9448  H HA   . PRO   A  1 629 ? 45.410 20.935  -61.837 0.00 31.25  ? 655  PRO   A HA   1 
ATOM   9449  H HB2  . PRO   A  1 629 ? 44.533 18.418  -63.176 0.00 31.77  ? 655  PRO   A HB2  1 
ATOM   9450  H HB3  . PRO   A  1 629 ? 46.092 19.295  -63.292 0.00 32.03  ? 655  PRO   A HB3  1 
ATOM   9451  H HG2  . PRO   A  1 629 ? 45.864 16.993  -61.977 0.00 31.83  ? 655  PRO   A HG2  1 
ATOM   9452  H HG3  . PRO   A  1 629 ? 46.935 18.313  -61.416 0.00 32.00  ? 655  PRO   A HG3  1 
ATOM   9453  H HD2  . PRO   A  1 629 ? 44.260 17.449  -60.377 0.00 29.90  ? 655  PRO   A HD2  1 
ATOM   9454  H HD3  . PRO   A  1 629 ? 45.728 18.035  -59.509 0.00 29.81  ? 655  PRO   A HD3  1 
ATOM   9455  N N    . ASN   A  1 630 ? 43.294 21.630  -63.086 1.00 24.57  ? 656  ASN   A N    1 
ATOM   9456  C CA   . ASN   A  1 630 ? 42.021 22.129  -63.625 1.00 24.80  ? 656  ASN   A CA   1 
ATOM   9457  C C    . ASN   A  1 630 ? 41.264 21.077  -64.453 1.00 24.53  ? 656  ASN   A C    1 
ATOM   9458  O O    . ASN   A  1 630 ? 40.063 20.897  -64.260 1.00 24.39  ? 656  ASN   A O    1 
ATOM   9459  C CB   . ASN   A  1 630 ? 42.264 23.394  -64.439 1.00 25.51  ? 656  ASN   A CB   1 
ATOM   9460  C CG   . ASN   A  1 630 ? 42.836 24.523  -63.599 1.00 27.37  ? 656  ASN   A CG   1 
ATOM   9461  O OD1  . ASN   A  1 630 ? 42.395 24.777  -62.471 1.00 28.05  ? 656  ASN   A OD1  1 
ATOM   9462  N ND2  . ASN   A  1 630 ? 43.833 25.226  -64.114 1.00 27.74  ? 656  ASN   A ND2  1 
ATOM   9463  H H    . ASN   A  1 630 ? 44.104 22.192  -63.326 0.00 31.65  ? 656  ASN   A H    1 
ATOM   9464  H HA   . ASN   A  1 630 ? 41.381 22.395  -62.785 0.00 31.95  ? 656  ASN   A HA   1 
ATOM   9465  H HB2  . ASN   A  1 630 ? 42.960 23.160  -65.243 0.00 33.77  ? 656  ASN   A HB2  1 
ATOM   9466  H HB3  . ASN   A  1 630 ? 41.317 23.734  -64.856 0.00 33.95  ? 656  ASN   A HB3  1 
ATOM   9467  H HD21 . ASN   A  1 630 ? 44.236 25.990  -63.582 0.00 36.86  ? 656  ASN   A HD21 1 
ATOM   9468  H HD22 . ASN   A  1 630 ? 44.191 25.017  -65.041 0.00 36.97  ? 656  ASN   A HD22 1 
ATOM   9469  N N    . GLU   A  1 631 ? 41.985 20.318  -65.289 1.00 24.78  ? 657  GLU   A N    1 
ATOM   9470  C CA   . GLU   A  1 631 ? 41.378 19.269  -66.121 1.00 25.78  ? 657  GLU   A CA   1 
ATOM   9471  C C    . GLU   A  1 631 ? 40.821 18.135  -65.253 1.00 25.97  ? 657  GLU   A C    1 
ATOM   9472  O O    . GLU   A  1 631 ? 39.772 17.591  -65.590 1.00 26.90  ? 657  GLU   A O    1 
ATOM   9473  C CB   . GLU   A  1 631 ? 42.420 18.719  -67.106 1.00 29.40  ? 657  GLU   A CB   1 
ATOM   9474  C CG   . GLU   A  1 631 ? 41.880 17.790  -68.180 1.00 37.26  ? 657  GLU   A CG   1 
ATOM   9475  C CD   . GLU   A  1 631 ? 42.919 17.339  -69.197 1.00 45.54  ? 657  GLU   A CD   1 
ATOM   9476  O OE1  . GLU   A  1 631 ? 44.130 17.562  -68.960 1.00 47.91  ? 657  GLU   A OE1  1 
ATOM   9477  O OE2  . GLU   A  1 631 ? 42.519 16.761  -70.235 1.00 46.11  ? 657  GLU   A OE2  1 
ATOM   9478  H H    . GLU   A  1 631 ? 42.988 20.406  -65.419 0.00 32.10  ? 657  GLU   A H    1 
ATOM   9479  H HA   . GLU   A  1 631 ? 40.556 19.695  -66.695 0.00 33.73  ? 657  GLU   A HA   1 
ATOM   9480  H HB2  . GLU   A  1 631 ? 42.894 19.559  -67.612 0.00 38.21  ? 657  GLU   A HB2  1 
ATOM   9481  H HB3  . GLU   A  1 631 ? 43.167 18.167  -66.537 0.00 37.43  ? 657  GLU   A HB3  1 
ATOM   9482  H HG2  . GLU   A  1 631 ? 41.480 16.893  -67.710 0.00 47.11  ? 657  GLU   A HG2  1 
ATOM   9483  H HG3  . GLU   A  1 631 ? 41.089 18.306  -68.721 0.00 47.88  ? 657  GLU   A HG3  1 
ATOM   9484  N N    . ALA   A  1 632 ? 41.514 17.776  -64.147 1.00 24.77  ? 658  ALA   A N    1 
ATOM   9485  C CA   . ALA   A  1 632 ? 41.025 16.725  -63.257 1.00 24.85  ? 658  ALA   A CA   1 
ATOM   9486  C C    . ALA   A  1 632 ? 39.757 17.176  -62.542 1.00 24.08  ? 658  ALA   A C    1 
ATOM   9487  O O    . ALA   A  1 632 ? 38.848 16.363  -62.405 1.00 23.45  ? 658  ALA   A O    1 
ATOM   9488  C CB   . ALA   A  1 632 ? 42.079 16.332  -62.232 1.00 24.96  ? 658  ALA   A CB   1 
ATOM   9489  H H    . ALA   A  1 632 ? 42.402 18.175  -63.858 0.00 30.97  ? 658  ALA   A H    1 
ATOM   9490  H HA   . ALA   A  1 632 ? 40.796 15.841  -63.850 0.00 30.62  ? 658  ALA   A HA   1 
ATOM   9491  H HB1  . ALA   A  1 632 ? 41.698 15.510  -61.629 0.00 29.90  ? 658  ALA   A HB1  1 
ATOM   9492  H HB2  . ALA   A  1 632 ? 42.984 16.024  -62.752 0.00 30.31  ? 658  ALA   A HB2  1 
ATOM   9493  H HB3  . ALA   A  1 632 ? 42.289 17.192  -61.598 0.00 30.24  ? 658  ALA   A HB3  1 
ATOM   9494  N N    . PHE   A  1 633 ? 39.673 18.456  -62.097 1.00 23.66  ? 659  PHE   A N    1 
ATOM   9495  C CA   . PHE   A  1 633 ? 38.456 18.930  -61.422 1.00 24.25  ? 659  PHE   A CA   1 
ATOM   9496  C C    . PHE   A  1 633 ? 37.285 18.925  -62.415 1.00 23.59  ? 659  PHE   A C    1 
ATOM   9497  O O    . PHE   A  1 633 ? 36.178 18.509  -62.072 1.00 22.38  ? 659  PHE   A O    1 
ATOM   9498  C CB   . PHE   A  1 633 ? 38.636 20.353  -60.845 1.00 24.59  ? 659  PHE   A CB   1 
ATOM   9499  C CG   . PHE   A  1 633 ? 37.535 20.754  -59.892 1.00 25.24  ? 659  PHE   A CG   1 
ATOM   9500  C CD1  . PHE   A  1 633 ? 36.369 21.347  -60.360 1.00 26.34  ? 659  PHE   A CD1  1 
ATOM   9501  C CD2  . PHE   A  1 633 ? 37.631 20.472  -58.540 1.00 25.76  ? 659  PHE   A CD2  1 
ATOM   9502  C CE1  . PHE   A  1 633 ? 35.323 21.648  -59.489 1.00 26.93  ? 659  PHE   A CE1  1 
ATOM   9503  C CE2  . PHE   A  1 633 ? 36.600 20.804  -57.668 1.00 26.54  ? 659  PHE   A CE2  1 
ATOM   9504  C CZ   . PHE   A  1 633 ? 35.450 21.388  -58.151 1.00 26.60  ? 659  PHE   A CZ   1 
ATOM   9505  H H    . PHE   A  1 633 ? 40.406 19.154  -62.177 0.00 29.48  ? 659  PHE   A H    1 
ATOM   9506  H HA   . PHE   A  1 633 ? 38.217 18.255  -60.602 0.00 29.66  ? 659  PHE   A HA   1 
ATOM   9507  H HB2  . PHE   A  1 633 ? 39.579 20.405  -60.302 0.00 30.46  ? 659  PHE   A HB2  1 
ATOM   9508  H HB3  . PHE   A  1 633 ? 38.642 21.067  -61.667 0.00 31.17  ? 659  PHE   A HB3  1 
ATOM   9509  H HD1  . PHE   A  1 633 ? 36.255 21.541  -61.413 0.00 33.65  ? 659  PHE   A HD1  1 
ATOM   9510  H HD2  . PHE   A  1 633 ? 38.526 20.010  -58.154 0.00 31.22  ? 659  PHE   A HD2  1 
ATOM   9511  H HE1  . PHE   A  1 633 ? 34.431 22.124  -59.863 0.00 34.37  ? 659  PHE   A HE1  1 
ATOM   9512  H HE2  . PHE   A  1 633 ? 36.699 20.598  -56.615 0.00 32.14  ? 659  PHE   A HE2  1 
ATOM   9513  H HZ   . PHE   A  1 633 ? 34.656 21.651  -57.474 0.00 33.09  ? 659  PHE   A HZ   1 
ATOM   9514  N N    . LEU   A  1 634 ? 37.534 19.374  -63.644 1.00 23.42  ? 660  LEU   A N    1 
ATOM   9515  C CA   . LEU   A  1 634 ? 36.511 19.381  -64.679 1.00 24.57  ? 660  LEU   A CA   1 
ATOM   9516  C C    . LEU   A  1 634 ? 36.024 17.989  -65.050 1.00 24.64  ? 660  LEU   A C    1 
ATOM   9517  O O    . LEU   A  1 634 ? 34.919 17.880  -65.575 1.00 25.69  ? 660  LEU   A O    1 
ATOM   9518  C CB   . LEU   A  1 634 ? 37.020 20.104  -65.943 1.00 25.60  ? 660  LEU   A CB   1 
ATOM   9519  C CG   . LEU   A  1 634 ? 37.151 21.626  -65.836 1.00 28.74  ? 660  LEU   A CG   1 
ATOM   9520  C CD1  . LEU   A  1 634 ? 37.674 22.227  -67.147 1.00 29.56  ? 660  LEU   A CD1  1 
ATOM   9521  C CD2  . LEU   A  1 634 ? 35.822 22.246  -65.504 1.00 29.82  ? 660  LEU   A CD2  1 
ATOM   9522  H H    . LEU   A  1 634 ? 38.423 19.760  -63.944 0.00 30.15  ? 660  LEU   A H    1 
ATOM   9523  H HA   . LEU   A  1 634 ? 35.645 19.906  -64.278 0.00 32.08  ? 660  LEU   A HA   1 
ATOM   9524  H HB2  . LEU   A  1 634 ? 38.002 19.712  -66.201 0.00 33.61  ? 660  LEU   A HB2  1 
ATOM   9525  H HB3  . LEU   A  1 634 ? 36.333 19.890  -66.760 0.00 34.12  ? 660  LEU   A HB3  1 
ATOM   9526  H HG   . LEU   A  1 634 ? 37.852 21.873  -65.041 0.00 37.63  ? 660  LEU   A HG   1 
ATOM   9527  H HD11 . LEU   A  1 634 ? 37.854 23.292  -67.005 0.00 39.82  ? 660  LEU   A HD11 1 
ATOM   9528  H HD12 . LEU   A  1 634 ? 38.604 21.728  -67.417 0.00 39.36  ? 660  LEU   A HD12 1 
ATOM   9529  H HD13 . LEU   A  1 634 ? 36.931 22.075  -67.928 0.00 39.91  ? 660  LEU   A HD13 1 
ATOM   9530  H HD21 . LEU   A  1 634 ? 35.689 23.164  -66.074 0.00 40.09  ? 660  LEU   A HD21 1 
ATOM   9531  H HD22 . LEU   A  1 634 ? 35.051 21.526  -65.769 0.00 39.54  ? 660  LEU   A HD22 1 
ATOM   9532  H HD23 . LEU   A  1 634 ? 35.779 22.448  -64.437 0.00 39.23  ? 660  LEU   A HD23 1 
ATOM   9533  N N    . ASN   A  1 635 ? 36.825 16.930  -64.798 1.00 23.30  ? 661  ASN   A N    1 
ATOM   9534  C CA   . ASN   A  1 635 ? 36.403 15.566  -65.091 1.00 23.19  ? 661  ASN   A CA   1 
ATOM   9535  C C    . ASN   A  1 635 ? 35.689 14.889  -63.910 1.00 22.73  ? 661  ASN   A C    1 
ATOM   9536  O O    . ASN   A  1 635 ? 35.373 13.706  -64.017 1.00 22.70  ? 661  ASN   A O    1 
ATOM   9537  C CB   . ASN   A  1 635 ? 37.570 14.715  -65.616 1.00 24.41  ? 661  ASN   A CB   1 
ATOM   9538  C CG   . ASN   A  1 635 ? 38.107 15.111  -66.987 1.00 28.67  ? 661  ASN   A CG   1 
ATOM   9539  O OD1  . ASN   A  1 635 ? 39.292 14.905  -67.285 1.00 30.65  ? 661  ASN   A OD1  1 
ATOM   9540  N ND2  . ASN   A  1 635 ? 37.291 15.651  -67.890 1.00 28.12  ? 661  ASN   A ND2  1 
ATOM   9541  H H    . ASN   A  1 635 ? 37.760 16.988  -64.409 0.00 29.52  ? 661  ASN   A H    1 
ATOM   9542  H HA   . ASN   A  1 635 ? 35.628 15.582  -65.854 0.00 29.90  ? 661  ASN   A HA   1 
ATOM   9543  H HB2  . ASN   A  1 635 ? 38.395 14.778  -64.907 0.00 30.47  ? 661  ASN   A HB2  1 
ATOM   9544  H HB3  . ASN   A  1 635 ? 37.246 13.679  -65.701 0.00 30.70  ? 661  ASN   A HB3  1 
ATOM   9545  H HD21 . ASN   A  1 635 ? 37.680 15.903  -68.793 0.00 36.76  ? 661  ASN   A HD21 1 
ATOM   9546  H HD22 . ASN   A  1 635 ? 36.296 15.781  -67.748 0.00 36.51  ? 661  ASN   A HD22 1 
ATOM   9547  N N    . LEU   A  1 636 ? 35.353 15.630  -62.840 1.00 21.89  ? 662  LEU   A N    1 
ATOM   9548  C CA   . LEU   A  1 636 ? 34.537 15.060  -61.773 1.00 21.81  ? 662  LEU   A CA   1 
ATOM   9549  C C    . LEU   A  1 636 ? 33.103 14.954  -62.338 1.00 22.68  ? 662  LEU   A C    1 
ATOM   9550  O O    . LEU   A  1 636 ? 32.726 15.752  -63.214 1.00 22.75  ? 662  LEU   A O    1 
ATOM   9551  C CB   . LEU   A  1 636 ? 34.578 15.920  -60.505 1.00 21.35  ? 662  LEU   A CB   1 
ATOM   9552  C CG   . LEU   A  1 636 ? 35.951 16.079  -59.847 1.00 22.42  ? 662  LEU   A CG   1 
ATOM   9553  C CD1  . LEU   A  1 636 ? 35.859 16.988  -58.621 1.00 23.18  ? 662  LEU   A CD1  1 
ATOM   9554  C CD2  . LEU   A  1 636 ? 36.551 14.725  -59.442 1.00 22.45  ? 662  LEU   A CD2  1 
ATOM   9555  H H    . LEU   A  1 636 ? 35.613 16.598  -62.678 0.00 27.43  ? 662  LEU   A H    1 
ATOM   9556  H HA   . LEU   A  1 636 ? 34.930 14.074  -61.535 0.00 26.51  ? 662  LEU   A HA   1 
ATOM   9557  H HB2  . LEU   A  1 636 ? 34.218 16.917  -60.757 0.00 26.45  ? 662  LEU   A HB2  1 
ATOM   9558  H HB3  . LEU   A  1 636 ? 33.914 15.472  -59.767 0.00 25.85  ? 662  LEU   A HB3  1 
ATOM   9559  H HG   . LEU   A  1 636 ? 36.630 16.545  -60.560 0.00 27.21  ? 662  LEU   A HG   1 
ATOM   9560  H HD11 . LEU   A  1 636 ? 36.856 17.133  -58.208 0.00 27.55  ? 662  LEU   A HD11 1 
ATOM   9561  H HD12 . LEU   A  1 636 ? 35.436 17.945  -58.922 0.00 28.15  ? 662  LEU   A HD12 1 
ATOM   9562  H HD13 . LEU   A  1 636 ? 35.219 16.513  -57.878 0.00 27.52  ? 662  LEU   A HD13 1 
ATOM   9563  H HD21 . LEU   A  1 636 ? 37.387 14.895  -58.765 0.00 26.25  ? 662  LEU   A HD21 1 
ATOM   9564  H HD22 . LEU   A  1 636 ? 35.786 14.129  -58.946 0.00 26.34  ? 662  LEU   A HD22 1 
ATOM   9565  H HD23 . LEU   A  1 636 ? 36.907 14.213  -60.334 0.00 26.64  ? 662  LEU   A HD23 1 
ATOM   9566  N N    . PRO   A  1 637 ? 32.311 13.942  -61.940 1.00 23.59  ? 663  PRO   A N    1 
ATOM   9567  C CA   . PRO   A  1 637 ? 30.955 13.800  -62.521 1.00 23.99  ? 663  PRO   A CA   1 
ATOM   9568  C C    . PRO   A  1 637 ? 30.102 15.052  -62.397 1.00 25.00  ? 663  PRO   A C    1 
ATOM   9569  O O    . PRO   A  1 637 ? 29.985 15.585  -61.295 1.00 25.32  ? 663  PRO   A O    1 
ATOM   9570  C CB   . PRO   A  1 637 ? 30.336 12.648  -61.721 1.00 24.41  ? 663  PRO   A CB   1 
ATOM   9571  C CG   . PRO   A  1 637 ? 31.474 11.934  -61.120 1.00 24.74  ? 663  PRO   A CG   1 
ATOM   9572  C CD   . PRO   A  1 637 ? 32.593 12.885  -60.947 1.00 23.23  ? 663  PRO   A CD   1 
ATOM   9573  H HA   . PRO   A  1 637 ? 31.025 13.508  -63.567 0.00 30.47  ? 663  PRO   A HA   1 
ATOM   9574  H HB2  . PRO   A  1 637 ? 29.675 13.029  -60.944 0.00 30.26  ? 663  PRO   A HB2  1 
ATOM   9575  H HB3  . PRO   A  1 637 ? 29.787 11.992  -62.394 0.00 30.56  ? 663  PRO   A HB3  1 
ATOM   9576  H HG2  . PRO   A  1 637 ? 31.199 11.526  -60.150 0.00 29.79  ? 663  PRO   A HG2  1 
ATOM   9577  H HG3  . PRO   A  1 637 ? 31.775 11.129  -61.788 0.00 30.17  ? 663  PRO   A HG3  1 
ATOM   9578  H HD2  . PRO   A  1 637 ? 32.593 13.294  -59.938 0.00 27.94  ? 663  PRO   A HD2  1 
ATOM   9579  H HD3  . PRO   A  1 637 ? 33.520 12.361  -61.170 0.00 28.01  ? 663  PRO   A HD3  1 
ATOM   9580  N N    . ALA   A  1 638 ? 29.540 15.545  -63.526 1.00 24.99  ? 664  ALA   A N    1 
ATOM   9581  C CA   . ALA   A  1 638 ? 28.669 16.725  -63.509 1.00 25.92  ? 664  ALA   A CA   1 
ATOM   9582  C C    . ALA   A  1 638 ? 27.366 16.501  -62.702 1.00 26.14  ? 664  ALA   A C    1 
ATOM   9583  O O    . ALA   A  1 638 ? 26.674 17.466  -62.379 1.00 26.72  ? 664  ALA   A O    1 
ATOM   9584  C CB   . ALA   A  1 638 ? 28.334 17.142  -64.932 1.00 26.22  ? 664  ALA   A CB   1 
ATOM   9585  H H    . ALA   A  1 638 ? 29.665 15.147  -64.452 0.00 32.67  ? 664  ALA   A H    1 
ATOM   9586  H HA   . ALA   A  1 638 ? 29.212 17.547  -63.045 0.00 33.96  ? 664  ALA   A HA   1 
ATOM   9587  H HB1  . ALA   A  1 638 ? 27.692 18.021  -64.903 0.00 35.57  ? 664  ALA   A HB1  1 
ATOM   9588  H HB2  . ALA   A  1 638 ? 29.257 17.373  -65.462 0.00 35.18  ? 664  ALA   A HB2  1 
ATOM   9589  H HB3  . ALA   A  1 638 ? 27.819 16.322  -65.430 0.00 35.30  ? 664  ALA   A HB3  1 
ATOM   9590  N N    . SER   A  1 639 ? 27.076 15.241  -62.323 1.00 25.38  ? 665  SER   A N    1 
ATOM   9591  C CA   . SER   A  1 639 ? 25.917 14.871  -61.510 1.00 25.46  ? 665  SER   A CA   1 
ATOM   9592  C C    . SER   A  1 639 ? 26.123 15.178  -59.995 1.00 24.68  ? 665  SER   A C    1 
ATOM   9593  O O    . SER   A  1 639 ? 25.191 14.996  -59.220 1.00 24.81  ? 665  SER   A O    1 
ATOM   9594  C CB   . SER   A  1 639 ? 25.650 13.373  -61.671 1.00 26.44  ? 665  SER   A CB   1 
ATOM   9595  O OG   . SER   A  1 639 ? 26.829 12.630  -61.398 1.00 27.25  ? 665  SER   A OG   1 
ATOM   9596  H H    . SER   A  1 639 ? 27.649 14.442  -62.573 0.00 32.82  ? 665  SER   A H    1 
ATOM   9597  H HA   . SER   A  1 639 ? 25.039 15.414  -61.856 0.00 33.64  ? 665  SER   A HA   1 
ATOM   9598  H HB2  . SER   A  1 639 ? 24.859 13.067  -60.987 0.00 34.05  ? 665  SER   A HB2  1 
ATOM   9599  H HB3  . SER   A  1 639 ? 25.344 13.181  -62.698 0.00 34.55  ? 665  SER   A HB3  1 
ATOM   9600  H HG   . SER   A  1 639 ? 26.870 12.384  -60.437 0.00 34.10  ? 665  SER   A HG   1 
ATOM   9601  N N    . LEU   A  1 640 ? 27.337 15.572  -59.561 1.00 23.63  ? 666  LEU   A N    1 
ATOM   9602  C CA   . LEU   A  1 640 ? 27.599 15.811  -58.136 1.00 23.62  ? 666  LEU   A CA   1 
ATOM   9603  C C    . LEU   A  1 640 ? 26.671 16.823  -57.452 1.00 24.01  ? 666  LEU   A C    1 
ATOM   9604  O O    . LEU   A  1 640 ? 26.438 17.908  -57.976 1.00 24.15  ? 666  LEU   A O    1 
ATOM   9605  C CB   . LEU   A  1 640 ? 29.061 16.238  -57.903 1.00 23.44  ? 666  LEU   A CB   1 
ATOM   9606  C CG   . LEU   A  1 640 ? 30.155 15.175  -58.069 1.00 23.79  ? 666  LEU   A CG   1 
ATOM   9607  C CD1  . LEU   A  1 640 ? 31.529 15.796  -57.877 1.00 23.46  ? 666  LEU   A CD1  1 
ATOM   9608  C CD2  . LEU   A  1 640 ? 29.978 14.021  -57.084 1.00 24.74  ? 666  LEU   A CD2  1 
ATOM   9609  H H    . LEU   A  1 640 ? 28.153 15.713  -60.147 0.00 30.01  ? 666  LEU   A H    1 
ATOM   9610  H HA   . LEU   A  1 640 ? 27.470 14.867  -57.616 0.00 29.17  ? 666  LEU   A HA   1 
ATOM   9611  H HB2  . LEU   A  1 640 ? 29.292 17.050  -58.590 0.00 29.33  ? 666  LEU   A HB2  1 
ATOM   9612  H HB3  . LEU   A  1 640 ? 29.139 16.603  -56.880 0.00 28.73  ? 666  LEU   A HB3  1 
ATOM   9613  H HG   . LEU   A  1 640 ? 30.102 14.773  -59.079 0.00 29.17  ? 666  LEU   A HG   1 
ATOM   9614  H HD11 . LEU   A  1 640 ? 32.293 15.051  -58.093 0.00 28.06  ? 666  LEU   A HD11 1 
ATOM   9615  H HD12 . LEU   A  1 640 ? 31.634 16.643  -58.555 0.00 28.71  ? 666  LEU   A HD12 1 
ATOM   9616  H HD13 . LEU   A  1 640 ? 31.624 16.131  -56.845 0.00 28.08  ? 666  LEU   A HD13 1 
ATOM   9617  H HD21 . LEU   A  1 640 ? 30.911 13.462  -57.060 0.00 29.23  ? 666  LEU   A HD21 1 
ATOM   9618  H HD22 . LEU   A  1 640 ? 29.744 14.413  -56.095 0.00 29.41  ? 666  LEU   A HD22 1 
ATOM   9619  H HD23 . LEU   A  1 640 ? 29.181 13.363  -57.427 0.00 29.71  ? 666  LEU   A HD23 1 
ATOM   9620  N N    . THR   A  1 641 ? 26.150 16.456  -56.269 1.00 23.86  ? 667  THR   A N    1 
ATOM   9621  C CA   . THR   A  1 641 ? 25.377 17.355  -55.423 1.00 24.32  ? 667  THR   A CA   1 
ATOM   9622  C C    . THR   A  1 641 ? 26.183 17.686  -54.134 1.00 24.15  ? 667  THR   A C    1 
ATOM   9623  O O    . THR   A  1 641 ? 25.956 18.731  -53.529 1.00 24.74  ? 667  THR   A O    1 
ATOM   9624  C CB   . THR   A  1 641 ? 23.989 16.785  -55.082 1.00 25.78  ? 667  THR   A CB   1 
ATOM   9625  O OG1  . THR   A  1 641 ? 24.126 15.697  -54.174 1.00 27.45  ? 667  THR   A OG1  1 
ATOM   9626  C CG2  . THR   A  1 641 ? 23.185 16.401  -56.324 1.00 26.42  ? 667  THR   A CG2  1 
ATOM   9627  H H    . THR   A  1 641 ? 26.239 15.526  -55.872 0.00 29.43  ? 667  THR   A H    1 
ATOM   9628  H HA   . THR   A  1 641 ? 25.179 18.285  -55.949 0.00 31.07  ? 667  THR   A HA   1 
ATOM   9629  H HB   . THR   A  1 641 ? 23.419 17.560  -54.573 0.00 32.78  ? 667  THR   A HB   1 
ATOM   9630  H HG1  . THR   A  1 641 ? 24.864 15.095  -54.452 0.00 33.64  ? 667  THR   A HG1  1 
ATOM   9631  H HG21 . THR   A  1 641 ? 22.179 16.094  -56.040 0.00 33.98  ? 667  THR   A HG21 1 
ATOM   9632  H HG22 . THR   A  1 641 ? 23.118 17.253  -56.998 0.00 34.27  ? 667  THR   A HG22 1 
ATOM   9633  H HG23 . THR   A  1 641 ? 23.669 15.576  -56.842 0.00 33.59  ? 667  THR   A HG23 1 
ATOM   9634  N N    . GLU   A  1 642 ? 27.110 16.808  -53.711 1.00 23.53  ? 668  GLU   A N    1 
ATOM   9635  C CA   . GLU   A  1 642 ? 27.870 17.001  -52.483 1.00 23.21  ? 668  GLU   A CA   1 
ATOM   9636  C C    . GLU   A  1 642 ? 29.323 16.596  -52.724 1.00 22.74  ? 668  GLU   A C    1 
ATOM   9637  O O    . GLU   A  1 642 ? 29.581 15.453  -53.087 1.00 23.01  ? 668  GLU   A O    1 
ATOM   9638  C CB   . GLU   A  1 642 ? 27.224 16.116  -51.409 1.00 25.65  ? 668  GLU   A CB   1 
ATOM   9639  C CG   . GLU   A  1 642 ? 27.949 16.095  -50.080 1.00 29.50  ? 668  GLU   A CG   1 
ATOM   9640  C CD   . GLU   A  1 642 ? 27.252 15.285  -48.999 1.00 32.83  ? 668  GLU   A CD   1 
ATOM   9641  O OE1  . GLU   A  1 642 ? 26.086 14.875  -49.200 1.00 31.57  ? 668  GLU   A OE1  1 
ATOM   9642  O OE2  . GLU   A  1 642 ? 27.888 15.048  -47.949 1.00 35.31  ? 668  GLU   A OE2  1 
ATOM   9643  H H    . GLU   A  1 642 ? 27.351 15.942  -54.184 0.00 28.38  ? 668  GLU   A H    1 
ATOM   9644  H HA   . GLU   A  1 642 ? 27.841 18.037  -52.150 0.00 27.93  ? 668  GLU   A HA   1 
ATOM   9645  H HB2  . GLU   A  1 642 ? 26.215 16.487  -51.236 0.00 30.64  ? 668  GLU   A HB2  1 
ATOM   9646  H HB3  . GLU   A  1 642 ? 27.181 15.093  -51.781 0.00 30.14  ? 668  GLU   A HB3  1 
ATOM   9647  H HG2  . GLU   A  1 642 ? 28.936 15.654  -50.208 0.00 34.15  ? 668  GLU   A HG2  1 
ATOM   9648  H HG3  . GLU   A  1 642 ? 28.046 17.118  -49.721 0.00 34.65  ? 668  GLU   A HG3  1 
ATOM   9649  N N    . LEU   A  1 643 ? 30.269 17.517  -52.505 1.00 21.79  ? 669  LEU   A N    1 
ATOM   9650  C CA   . LEU   A  1 643 ? 31.689 17.266  -52.749 1.00 20.66  ? 669  LEU   A CA   1 
ATOM   9651  C C    . LEU   A  1 643 ? 32.505 17.683  -51.529 1.00 20.13  ? 669  LEU   A C    1 
ATOM   9652  O O    . LEU   A  1 643 ? 32.462 18.855  -51.137 1.00 19.68  ? 669  LEU   A O    1 
ATOM   9653  C CB   . LEU   A  1 643 ? 32.122 18.068  -53.982 1.00 20.54  ? 669  LEU   A CB   1 
ATOM   9654  C CG   . LEU   A  1 643 ? 33.615 18.077  -54.362 1.00 22.08  ? 669  LEU   A CG   1 
ATOM   9655  C CD1  . LEU   A  1 643 ? 34.168 16.646  -54.565 1.00 22.24  ? 669  LEU   A CD1  1 
ATOM   9656  C CD2  . LEU   A  1 643 ? 33.832 18.927  -55.612 1.00 22.38  ? 669  LEU   A CD2  1 
ATOM   9657  H H    . LEU   A  1 643 ? 30.085 18.450  -52.151 0.00 25.83  ? 669  LEU   A H    1 
ATOM   9658  H HA   . LEU   A  1 643 ? 31.874 16.212  -52.944 0.00 23.69  ? 669  LEU   A HA   1 
ATOM   9659  H HB2  . LEU   A  1 643 ? 31.579 17.676  -54.841 0.00 24.45  ? 669  LEU   A HB2  1 
ATOM   9660  H HB3  . LEU   A  1 643 ? 31.828 19.104  -53.826 0.00 24.56  ? 669  LEU   A HB3  1 
ATOM   9661  H HG   . LEU   A  1 643 ? 34.192 18.540  -53.564 0.00 25.77  ? 669  LEU   A HG   1 
ATOM   9662  H HD11 . LEU   A  1 643 ? 35.190 16.708  -54.935 0.00 25.64  ? 669  LEU   A HD11 1 
ATOM   9663  H HD12 . LEU   A  1 643 ? 34.154 16.118  -53.613 0.00 25.33  ? 669  LEU   A HD12 1 
ATOM   9664  H HD13 . LEU   A  1 643 ? 33.540 16.128  -55.288 0.00 25.84  ? 669  LEU   A HD13 1 
ATOM   9665  H HD21 . LEU   A  1 643 ? 34.874 18.850  -55.918 0.00 26.69  ? 669  LEU   A HD21 1 
ATOM   9666  H HD22 . LEU   A  1 643 ? 33.184 18.560  -56.406 0.00 27.01  ? 669  LEU   A HD22 1 
ATOM   9667  H HD23 . LEU   A  1 643 ? 33.586 19.962  -55.383 0.00 27.10  ? 669  LEU   A HD23 1 
ATOM   9668  N N    . HIS   A  1 644 ? 33.245 16.730  -50.933 1.00 19.53  ? 670  HIS   A N    1 
ATOM   9669  C CA   . HIS   A  1 644 ? 34.115 17.009  -49.797 1.00 19.57  ? 670  HIS   A CA   1 
ATOM   9670  C C    . HIS   A  1 644 ? 35.565 16.889  -50.229 1.00 19.25  ? 670  HIS   A C    1 
ATOM   9671  O O    . HIS   A  1 644 ? 35.951 15.905  -50.852 1.00 17.97  ? 670  HIS   A O    1 
ATOM   9672  C CB   . HIS   A  1 644 ? 33.861 16.068  -48.613 1.00 21.03  ? 670  HIS   A CB   1 
ATOM   9673  C CG   . HIS   A  1 644 ? 32.460 16.086  -48.096 1.00 25.03  ? 670  HIS   A CG   1 
ATOM   9674  N ND1  . HIS   A  1 644 ? 32.146 16.712  -46.909 1.00 27.42  ? 670  HIS   A ND1  1 
ATOM   9675  C CD2  . HIS   A  1 644 ? 31.346 15.501  -48.589 1.00 26.70  ? 670  HIS   A CD2  1 
ATOM   9676  C CE1  . HIS   A  1 644 ? 30.849 16.528  -46.735 1.00 28.25  ? 670  HIS   A CE1  1 
ATOM   9677  N NE2  . HIS   A  1 644 ? 30.330 15.790  -47.712 1.00 27.82  ? 670  HIS   A NE2  1 
ATOM   9678  H H    . HIS   A  1 644 ? 33.258 15.754  -51.211 0.00 21.61  ? 670  HIS   A H    1 
ATOM   9679  H HA   . HIS   A  1 644 ? 33.950 18.028  -49.459 0.00 21.80  ? 670  HIS   A HA   1 
ATOM   9680  H HB2  . HIS   A  1 644 ? 34.104 15.044  -48.882 0.00 22.66  ? 670  HIS   A HB2  1 
ATOM   9681  H HB3  . HIS   A  1 644 ? 34.509 16.378  -47.793 0.00 22.75  ? 670  HIS   A HB3  1 
ATOM   9682  H HD2  . HIS   A  1 644 ? 31.270 14.924  -49.491 0.00 30.00  ? 670  HIS   A HD2  1 
ATOM   9683  H HE1  . HIS   A  1 644 ? 30.283 16.925  -45.909 0.00 31.93  ? 670  HIS   A HE1  1 
ATOM   9684  H HE2  . HIS   A  1 644 ? 29.364 15.491  -47.785 0.00 31.53  ? 670  HIS   A HE2  1 
ATOM   9685  N N    . ILE   A  1 645 ? 36.344 17.928  -49.966 1.00 19.52  ? 671  ILE   A N    1 
ATOM   9686  C CA   . ILE   A  1 645 ? 37.786 17.954  -50.217 1.00 20.28  ? 671  ILE   A CA   1 
ATOM   9687  C C    . ILE   A  1 645 ? 38.476 18.502  -48.923 1.00 20.78  ? 671  ILE   A C    1 
ATOM   9688  O O    . ILE   A  1 645 ? 39.523 19.144  -48.993 1.00 21.39  ? 671  ILE   A O    1 
ATOM   9689  C CB   . ILE   A  1 645 ? 38.159 18.810  -51.478 1.00 20.86  ? 671  ILE   A CB   1 
ATOM   9690  C CG1  . ILE   A  1 645 ? 37.039 18.790  -52.594 1.00 21.50  ? 671  ILE   A CG1  1 
ATOM   9691  C CG2  . ILE   A  1 645 ? 39.541 18.375  -52.040 1.00 21.45  ? 671  ILE   A CG2  1 
ATOM   9692  C CD1  . ILE   A  1 645 ? 37.328 19.684  -53.855 1.00 22.67  ? 671  ILE   A CD1  1 
ATOM   9693  H H    . ILE   A  1 645 ? 36.006 18.803  -49.579 0.00 21.72  ? 671  ILE   A H    1 
ATOM   9694  H HA   . ILE   A  1 645 ? 38.134 16.928  -50.338 0.00 22.06  ? 671  ILE   A HA   1 
ATOM   9695  H HB   . ILE   A  1 645 ? 38.265 19.845  -51.158 0.00 23.71  ? 671  ILE   A HB   1 
ATOM   9696  H HG12 . ILE   A  1 645 ? 36.908 17.764  -52.934 0.00 24.36  ? 671  ILE   A HG12 1 
ATOM   9697  H HG13 . ILE   A  1 645 ? 36.106 19.157  -52.169 0.00 24.68  ? 671  ILE   A HG13 1 
ATOM   9698  H HG21 . ILE   A  1 645 ? 39.807 19.005  -52.886 0.00 24.40  ? 671  ILE   A HG21 1 
ATOM   9699  H HG22 . ILE   A  1 645 ? 40.287 18.476  -51.253 0.00 23.90  ? 671  ILE   A HG22 1 
ATOM   9700  H HG23 . ILE   A  1 645 ? 39.479 17.334  -52.357 0.00 23.87  ? 671  ILE   A HG23 1 
ATOM   9701  H HD11 . ILE   A  1 645 ? 36.414 19.779  -54.439 0.00 26.73  ? 671  ILE   A HD11 1 
ATOM   9702  H HD12 . ILE   A  1 645 ? 37.663 20.667  -53.527 0.00 26.67  ? 671  ILE   A HD12 1 
ATOM   9703  H HD13 . ILE   A  1 645 ? 38.100 19.209  -54.458 0.00 26.39  ? 671  ILE   A HD13 1 
ATOM   9704  N N    . ASN   A  1 646 ? 37.886 18.231  -47.752 1.00 20.01  ? 672  ASN   A N    1 
ATOM   9705  C CA   . ASN   A  1 646 ? 38.362 18.724  -46.483 1.00 20.17  ? 672  ASN   A CA   1 
ATOM   9706  C C    . ASN   A  1 646 ? 39.623 17.994  -46.027 1.00 20.11  ? 672  ASN   A C    1 
ATOM   9707  O O    . ASN   A  1 646 ? 39.915 16.903  -46.496 1.00 19.54  ? 672  ASN   A O    1 
ATOM   9708  C CB   . ASN   A  1 646 ? 37.250 18.624  -45.418 1.00 20.76  ? 672  ASN   A CB   1 
ATOM   9709  C CG   . ASN   A  1 646 ? 36.719 17.227  -45.218 1.00 22.93  ? 672  ASN   A CG   1 
ATOM   9710  O OD1  . ASN   A  1 646 ? 36.154 16.622  -46.147 1.00 23.92  ? 672  ASN   A OD1  1 
ATOM   9711  N ND2  . ASN   A  1 646 ? 36.892 16.670  -44.033 1.00 23.48  ? 672  ASN   A ND2  1 
ATOM   9712  H H    . ASN   A  1 646 ? 37.059 17.649  -47.674 0.00 21.57  ? 672  ASN   A H    1 
ATOM   9713  H HA   . ASN   A  1 646 ? 38.611 19.779  -46.589 0.00 22.10  ? 672  ASN   A HA   1 
ATOM   9714  H HB2  . ASN   A  1 646 ? 37.645 18.995  -44.473 0.00 22.39  ? 672  ASN   A HB2  1 
ATOM   9715  H HB3  . ASN   A  1 646 ? 36.416 19.248  -45.732 0.00 22.72  ? 672  ASN   A HB3  1 
ATOM   9716  H HD21 . ASN   A  1 646 ? 36.547 15.730  -43.867 0.00 24.78  ? 672  ASN   A HD21 1 
ATOM   9717  H HD22 . ASN   A  1 646 ? 37.367 17.164  -43.284 0.00 25.03  ? 672  ASN   A HD22 1 
ATOM   9718  N N    . ASP   A  1 647 ? 40.372 18.603  -45.111 1.00 20.48  ? 673  ASP   A N    1 
ATOM   9719  C CA   . ASP   A  1 647 ? 41.577 18.000  -44.554 1.00 21.07  ? 673  ASP   A CA   1 
ATOM   9720  C C    . ASP   A  1 647 ? 42.584 17.528  -45.621 1.00 20.66  ? 673  ASP   A C    1 
ATOM   9721  O O    . ASP   A  1 647 ? 43.046 16.387  -45.634 1.00 20.52  ? 673  ASP   A O    1 
ATOM   9722  C CB   . ASP   A  1 647 ? 41.194 16.884  -43.570 1.00 24.08  ? 673  ASP   A CB   1 
ATOM   9723  C CG   . ASP   A  1 647 ? 40.297 17.405  -42.460 1.00 30.30  ? 673  ASP   A CG   1 
ATOM   9724  O OD1  . ASP   A  1 647 ? 40.562 18.517  -41.953 1.00 29.74  ? 673  ASP   A OD1  1 
ATOM   9725  O OD2  . ASP   A  1 647 ? 39.334 16.703  -42.098 1.00 35.00  ? 673  ASP   A OD2  1 
ATOM   9726  H H    . ASP   A  1 647 ? 40.168 19.524  -44.735 0.00 22.10  ? 673  ASP   A H    1 
ATOM   9727  H HA   . ASP   A  1 647 ? 42.094 18.770  -43.983 0.00 22.50  ? 673  ASP   A HA   1 
ATOM   9728  H HB2  . ASP   A  1 647 ? 40.674 16.084  -44.096 0.00 25.41  ? 673  ASP   A HB2  1 
ATOM   9729  H HB3  . ASP   A  1 647 ? 42.101 16.503  -43.102 0.00 25.42  ? 673  ASP   A HB3  1 
ATOM   9730  N N    . ASN   A  1 648 ? 42.910 18.445  -46.509 1.00 20.52  ? 674  ASN   A N    1 
ATOM   9731  C CA   . ASN   A  1 648 ? 43.971 18.312  -47.502 1.00 20.51  ? 674  ASN   A CA   1 
ATOM   9732  C C    . ASN   A  1 648 ? 44.919 19.517  -47.165 1.00 21.53  ? 674  ASN   A C    1 
ATOM   9733  O O    . ASN   A  1 648 ? 44.905 19.982  -46.029 1.00 21.62  ? 674  ASN   A O    1 
ATOM   9734  C CB   . ASN   A  1 648 ? 43.354 18.318  -48.935 1.00 20.74  ? 674  ASN   A CB   1 
ATOM   9735  C CG   . ASN   A  1 648 ? 42.810 16.969  -49.324 1.00 21.12  ? 674  ASN   A CG   1 
ATOM   9736  O OD1  . ASN   A  1 648 ? 43.578 16.057  -49.614 1.00 21.49  ? 674  ASN   A OD1  1 
ATOM   9737  N ND2  . ASN   A  1 648 ? 41.486 16.797  -49.312 1.00 19.26  ? 674  ASN   A ND2  1 
ATOM   9738  H H    . ASN   A  1 648 ? 42.440 19.343  -46.576 0.00 22.27  ? 674  ASN   A H    1 
ATOM   9739  H HA   . ASN   A  1 648 ? 44.534 17.390  -47.362 0.00 21.86  ? 674  ASN   A HA   1 
ATOM   9740  H HB2  . ASN   A  1 648 ? 42.551 19.053  -48.972 0.00 22.77  ? 674  ASN   A HB2  1 
ATOM   9741  H HB3  . ASN   A  1 648 ? 44.112 18.572  -49.673 0.00 22.76  ? 674  ASN   A HB3  1 
ATOM   9742  H HD21 . ASN   A  1 648 ? 41.096 15.895  -49.571 0.00 20.30  ? 674  ASN   A HD21 1 
ATOM   9743  H HD22 . ASN   A  1 648 ? 40.865 17.553  -49.044 0.00 20.63  ? 674  ASN   A HD22 1 
ATOM   9744  N N    A MET   A  1 649 ? 45.753 19.968  -48.098 0.50 21.86  ? 675  MET   A N    1 
ATOM   9745  N N    B MET   A  1 649 ? 45.761 19.967  -48.099 0.50 21.90  ? 675  MET   A N    1 
ATOM   9746  C CA   A MET   A  1 649 ? 46.626 21.121  -47.897 0.50 22.98  ? 675  MET   A CA   1 
ATOM   9747  C CA   B MET   A  1 649 ? 46.637 21.124  -47.910 0.50 23.05  ? 675  MET   A CA   1 
ATOM   9748  C C    A MET   A  1 649 ? 46.441 22.067  -49.097 0.50 23.19  ? 675  MET   A C    1 
ATOM   9749  C C    B MET   A  1 649 ? 46.441 22.073  -49.103 0.50 23.22  ? 675  MET   A C    1 
ATOM   9750  O O    A MET   A  1 649 ? 47.419 22.585  -49.634 0.50 23.17  ? 675  MET   A O    1 
ATOM   9751  O O    B MET   A  1 649 ? 47.415 22.596  -49.645 0.50 23.18  ? 675  MET   A O    1 
ATOM   9752  C CB   A MET   A  1 649 ? 48.087 20.649  -47.764 0.50 24.14  ? 675  MET   A CB   1 
ATOM   9753  C CB   B MET   A  1 649 ? 48.102 20.659  -47.816 0.50 24.30  ? 675  MET   A CB   1 
ATOM   9754  C CG   A MET   A  1 649 ? 48.324 19.759  -46.550 0.50 27.14  ? 675  MET   A CG   1 
ATOM   9755  C CG   B MET   A  1 649 ? 48.387 19.822  -46.592 0.50 27.46  ? 675  MET   A CG   1 
ATOM   9756  S SD   A MET   A  1 649 ? 47.770 18.047  -46.770 0.50 32.53  ? 675  MET   A SD   1 
ATOM   9757  S SD   B MET   A  1 649 ? 50.085 19.204  -46.570 0.50 33.40  ? 675  MET   A SD   1 
ATOM   9758  C CE   A MET   A  1 649 ? 48.028 17.405  -45.128 0.50 33.19  ? 675  MET   A CE   1 
ATOM   9759  C CE   B MET   A  1 649 ? 49.948 17.864  -47.734 0.50 30.36  ? 675  MET   A CE   1 
ATOM   9760  H H    A MET   A  1 649 ? 45.880 19.543  -49.011 0.00 24.34  ? 675  MET   A H    1 
ATOM   9761  H H    B MET   A  1 649 ? 45.888 19.534  -49.008 0.00 24.38  ? 675  MET   A H    1 
ATOM   9762  H HA   A MET   A  1 649 ? 46.362 21.660  -46.989 0.00 26.10  ? 675  MET   A HA   1 
ATOM   9763  H HA   B MET   A  1 649 ? 46.391 21.660  -46.994 0.00 26.19  ? 675  MET   A HA   1 
ATOM   9764  H HB2  A MET   A  1 649 ? 48.362 20.085  -48.654 0.00 27.36  ? 675  MET   A HB2  1 
ATOM   9765  H HB2  B MET   A  1 649 ? 48.341 20.068  -48.699 0.00 27.54  ? 675  MET   A HB2  1 
ATOM   9766  H HB3  A MET   A  1 649 ? 48.736 21.517  -47.657 0.00 27.71  ? 675  MET   A HB3  1 
ATOM   9767  H HB3  B MET   A  1 649 ? 48.755 21.529  -47.762 0.00 27.91  ? 675  MET   A HB3  1 
ATOM   9768  H HG2  A MET   A  1 649 ? 49.392 19.736  -46.335 0.00 30.70  ? 675  MET   A HG2  1 
ATOM   9769  H HG2  B MET   A  1 649 ? 48.239 20.433  -45.703 0.00 31.11  ? 675  MET   A HG2  1 
ATOM   9770  H HG3  A MET   A  1 649 ? 47.787 20.176  -45.699 0.00 30.60  ? 675  MET   A HG3  1 
ATOM   9771  H HG3  B MET   A  1 649 ? 47.716 18.965  -46.572 0.00 30.72  ? 675  MET   A HG3  1 
ATOM   9772  H HE1  A MET   A  1 649 ? 47.752 16.352  -45.112 0.00 36.80  ? 675  MET   A HE1  1 
ATOM   9773  H HE1  B MET   A  1 649 ? 50.859 17.267  -47.693 0.00 34.24  ? 675  MET   A HE1  1 
ATOM   9774  H HE2  A MET   A  1 649 ? 49.079 17.518  -44.865 0.00 37.20  ? 675  MET   A HE2  1 
ATOM   9775  H HE2  B MET   A  1 649 ? 49.091 17.248  -47.468 0.00 33.99  ? 675  MET   A HE2  1 
ATOM   9776  H HE3  A MET   A  1 649 ? 47.408 17.963  -44.428 0.00 37.10  ? 675  MET   A HE3  1 
ATOM   9777  H HE3  B MET   A  1 649 ? 49.819 18.271  -48.736 0.00 34.49  ? 675  MET   A HE3  1 
ATOM   9778  N N    . LEU   A  1 650 ? 45.181 22.276  -49.536 1.00 23.21  ? 676  LEU   A N    1 
ATOM   9779  C CA   . LEU   A  1 650 ? 44.909 23.105  -50.708 1.00 24.55  ? 676  LEU   A CA   1 
ATOM   9780  C C    . LEU   A  1 650 ? 45.289 24.561  -50.490 1.00 26.01  ? 676  LEU   A C    1 
ATOM   9781  O O    . LEU   A  1 650 ? 44.803 25.172  -49.550 1.00 25.69  ? 676  LEU   A O    1 
ATOM   9782  C CB   . LEU   A  1 650 ? 43.425 23.039  -51.116 1.00 24.43  ? 676  LEU   A CB   1 
ATOM   9783  C CG   . LEU   A  1 650 ? 42.878 21.687  -51.572 1.00 24.83  ? 676  LEU   A CG   1 
ATOM   9784  C CD1  . LEU   A  1 650 ? 41.351 21.757  -51.748 1.00 25.26  ? 676  LEU   A CD1  1 
ATOM   9785  C CD2  . LEU   A  1 650 ? 43.533 21.221  -52.851 1.00 24.68  ? 676  LEU   A CD2  1 
ATOM   9786  H H    . LEU   A  1 650 ? 44.342 21.909  -49.097 0.00 26.66  ? 676  LEU   A H    1 
ATOM   9787  H HA   . LEU   A  1 650 ? 45.501 22.722  -51.538 0.00 28.93  ? 676  LEU   A HA   1 
ATOM   9788  H HB2  . LEU   A  1 650 ? 42.815 23.362  -50.275 0.00 28.79  ? 676  LEU   A HB2  1 
ATOM   9789  H HB3  . LEU   A  1 650 ? 43.277 23.737  -51.940 0.00 29.19  ? 676  LEU   A HB3  1 
ATOM   9790  H HG   . LEU   A  1 650 ? 43.090 20.944  -50.805 0.00 28.53  ? 676  LEU   A HG   1 
ATOM   9791  H HD11 . LEU   A  1 650 ? 40.982 20.761  -51.984 0.00 29.24  ? 676  LEU   A HD11 1 
ATOM   9792  H HD12 . LEU   A  1 650 ? 40.900 22.107  -50.821 0.00 29.50  ? 676  LEU   A HD12 1 
ATOM   9793  H HD13 . LEU   A  1 650 ? 41.115 22.446  -52.559 0.00 29.91  ? 676  LEU   A HD13 1 
ATOM   9794  H HD21 . LEU   A  1 650 ? 42.972 20.375  -53.246 0.00 28.62  ? 676  LEU   A HD21 1 
ATOM   9795  H HD22 . LEU   A  1 650 ? 43.533 22.038  -53.572 0.00 29.21  ? 676  LEU   A HD22 1 
ATOM   9796  H HD23 . LEU   A  1 650 ? 44.554 20.908  -52.636 0.00 28.68  ? 676  LEU   A HD23 1 
ATOM   9797  N N    . LYS   A  1 651 ? 46.156 25.105  -51.361 1.00 27.31  ? 677  LYS   A N    1 
ATOM   9798  C CA   . LYS   A  1 651 ? 46.550 26.514  -51.344 1.00 29.28  ? 677  LYS   A CA   1 
ATOM   9799  C C    . LYS   A  1 651 ? 45.723 27.322  -52.354 1.00 31.00  ? 677  LYS   A C    1 
ATOM   9800  O O    . LYS   A  1 651 ? 45.547 28.527  -52.159 1.00 32.37  ? 677  LYS   A O    1 
ATOM   9801  C CB   . LYS   A  1 651 ? 48.049 26.670  -51.646 1.00 32.43  ? 677  LYS   A CB   1 
ATOM   9802  C CG   . LYS   A  1 651 ? 48.939 26.157  -50.512 1.00 39.17  ? 677  LYS   A CG   1 
ATOM   9803  C CD   . LYS   A  1 651 ? 50.235 26.961  -50.362 1.00 45.83  ? 677  LYS   A CD   1 
ATOM   9804  C CE   . LYS   A  1 651 ? 50.967 26.605  -49.084 1.00 51.36  ? 677  LYS   A CE   1 
ATOM   9805  N NZ   . LYS   A  1 651 ? 52.351 27.168  -49.065 1.00 54.62  ? 677  LYS   A NZ   1 
ATOM   9806  H H    . LYS   A  1 651 ? 46.604 24.581  -52.107 0.00 33.05  ? 677  LYS   A H    1 
ATOM   9807  H HA   . LYS   A  1 651 ? 46.358 26.947  -50.363 0.00 36.04  ? 677  LYS   A HA   1 
ATOM   9808  H HB2  . LYS   A  1 651 ? 48.298 26.108  -52.545 0.00 39.93  ? 677  LYS   A HB2  1 
ATOM   9809  H HB3  . LYS   A  1 651 ? 48.262 27.727  -51.797 0.00 40.47  ? 677  LYS   A HB3  1 
ATOM   9810  H HG2  . LYS   A  1 651 ? 48.399 26.224  -49.569 0.00 47.65  ? 677  LYS   A HG2  1 
ATOM   9811  H HG3  . LYS   A  1 651 ? 49.206 25.120  -50.713 0.00 47.40  ? 677  LYS   A HG3  1 
ATOM   9812  H HD2  . LYS   A  1 651 ? 50.893 26.735  -51.200 0.00 56.23  ? 677  LYS   A HD2  1 
ATOM   9813  H HD3  . LYS   A  1 651 ? 50.008 28.025  -50.331 0.00 56.60  ? 677  LYS   A HD3  1 
ATOM   9814  H HE2  . LYS   A  1 651 ? 50.422 27.019  -48.237 0.00 62.62  ? 677  LYS   A HE2  1 
ATOM   9815  H HE3  . LYS   A  1 651 ? 51.036 25.521  -48.999 0.00 62.16  ? 677  LYS   A HE3  1 
ATOM   9816  H HZ1  . LYS   A  1 651 ? 52.804 26.940  -48.186 0.00 66.79  ? 677  LYS   A HZ1  1 
ATOM   9817  H HZ2  . LYS   A  1 651 ? 52.893 26.774  -49.827 0.00 66.90  ? 677  LYS   A HZ2  1 
ATOM   9818  H HZ3  . LYS   A  1 651 ? 52.318 28.177  -49.170 0.00 67.34  ? 677  LYS   A HZ3  1 
ATOM   9819  N N    . PHE   A  1 652 ? 45.223 26.678  -53.428 1.00 30.63  ? 678  PHE   A N    1 
ATOM   9820  C CA   . PHE   A  1 652 ? 44.407 27.324  -54.443 1.00 30.33  ? 678  PHE   A CA   1 
ATOM   9821  C C    . PHE   A  1 652 ? 43.171 26.466  -54.744 1.00 28.93  ? 678  PHE   A C    1 
ATOM   9822  O O    . PHE   A  1 652 ? 43.192 25.248  -54.573 1.00 28.78  ? 678  PHE   A O    1 
ATOM   9823  C CB   . PHE   A  1 652 ? 45.231 27.528  -55.731 1.00 30.75  ? 678  PHE   A CB   1 
ATOM   9824  H H    . PHE   A  1 652 ? 45.391 25.700  -53.639 0.00 37.69  ? 678  PHE   A H    1 
ATOM   9825  H HA   . PHE   A  1 652 ? 44.068 28.302  -54.104 0.00 38.49  ? 678  PHE   A HA   1 
ATOM   9826  N N    . PHE   A  1 653 ? 42.084 27.133  -55.150 1.00 27.71  ? 679  PHE   A N    1 
ATOM   9827  C CA   . PHE   A  1 653 ? 40.831 26.493  -55.550 1.00 26.89  ? 679  PHE   A CA   1 
ATOM   9828  C C    . PHE   A  1 653 ? 40.275 27.333  -56.677 1.00 26.82  ? 679  PHE   A C    1 
ATOM   9829  O O    . PHE   A  1 653 ? 40.066 28.526  -56.488 1.00 26.40  ? 679  PHE   A O    1 
ATOM   9830  C CB   . PHE   A  1 653 ? 39.806 26.405  -54.401 1.00 25.83  ? 679  PHE   A CB   1 
ATOM   9831  C CG   . PHE   A  1 653 ? 38.583 25.604  -54.791 1.00 25.53  ? 679  PHE   A CG   1 
ATOM   9832  C CD1  . PHE   A  1 653 ? 38.645 24.224  -54.899 1.00 26.08  ? 679  PHE   A CD1  1 
ATOM   9833  C CD2  . PHE   A  1 653 ? 37.399 26.238  -55.134 1.00 25.94  ? 679  PHE   A CD2  1 
ATOM   9834  C CE1  . PHE   A  1 653 ? 37.533 23.492  -55.304 1.00 26.41  ? 679  PHE   A CE1  1 
ATOM   9835  C CE2  . PHE   A  1 653 ? 36.297 25.507  -55.554 1.00 26.30  ? 679  PHE   A CE2  1 
ATOM   9836  C CZ   . PHE   A  1 653 ? 36.364 24.139  -55.623 1.00 25.83  ? 679  PHE   A CZ   1 
ATOM   9837  H H    . PHE   A  1 653 ? 42.050 28.148  -55.188 0.00 35.57  ? 679  PHE   A H    1 
ATOM   9838  H HA   . PHE   A  1 653 ? 41.026 25.486  -55.920 0.00 33.70  ? 679  PHE   A HA   1 
ATOM   9839  H HB2  . PHE   A  1 653 ? 40.274 25.908  -53.552 0.00 32.13  ? 679  PHE   A HB2  1 
ATOM   9840  H HB3  . PHE   A  1 653 ? 39.487 27.408  -54.123 0.00 32.94  ? 679  PHE   A HB3  1 
ATOM   9841  H HD1  . PHE   A  1 653 ? 39.560 23.707  -54.650 0.00 31.88  ? 679  PHE   A HD1  1 
ATOM   9842  H HD2  . PHE   A  1 653 ? 37.335 27.314  -55.089 0.00 33.47  ? 679  PHE   A HD2  1 
ATOM   9843  H HE1  . PHE   A  1 653 ? 37.588 22.417  -55.358 0.00 32.16  ? 679  PHE   A HE1  1 
ATOM   9844  H HE2  . PHE   A  1 653 ? 35.376 26.014  -55.797 0.00 33.79  ? 679  PHE   A HE2  1 
ATOM   9845  H HZ   . PHE   A  1 653 ? 35.502 23.574  -55.931 0.00 32.29  ? 679  PHE   A HZ   1 
ATOM   9846  N N    . ASN   A  1 654 ? 40.121 26.744  -57.865 1.00 26.96  ? 680  ASN   A N    1 
ATOM   9847  C CA   . ASN   A  1 654 ? 39.658 27.490  -59.027 1.00 28.18  ? 680  ASN   A CA   1 
ATOM   9848  C C    . ASN   A  1 654 ? 38.124 27.520  -58.979 1.00 28.44  ? 680  ASN   A C    1 
ATOM   9849  O O    . ASN   A  1 654 ? 37.467 26.571  -59.396 1.00 27.88  ? 680  ASN   A O    1 
ATOM   9850  C CB   . ASN   A  1 654 ? 40.228 26.851  -60.297 1.00 29.83  ? 680  ASN   A CB   1 
ATOM   9851  C CG   . ASN   A  1 654 ? 39.858 27.504  -61.573 1.00 33.54  ? 680  ASN   A CG   1 
ATOM   9852  O OD1  . ASN   A  1 654 ? 39.139 28.508  -61.587 1.00 33.38  ? 680  ASN   A OD1  1 
ATOM   9853  N ND2  . ASN   A  1 654 ? 40.466 27.048  -62.667 1.00 36.61  ? 680  ASN   A ND2  1 
ATOM   9854  H H    . ASN   A  1 654 ? 40.312 25.765  -58.053 0.00 34.47  ? 680  ASN   A H    1 
ATOM   9855  H HA   . ASN   A  1 654 ? 40.028 28.514  -58.995 0.00 37.36  ? 680  ASN   A HA   1 
ATOM   9856  H HB2  . ASN   A  1 654 ? 41.314 26.865  -60.227 0.00 38.87  ? 680  ASN   A HB2  1 
ATOM   9857  H HB3  . ASN   A  1 654 ? 39.882 25.819  -60.351 0.00 38.60  ? 680  ASN   A HB3  1 
ATOM   9858  H HD21 . ASN   A  1 654 ? 39.597 27.055  -63.166 0.00 48.14  ? 680  ASN   A HD21 1 
ATOM   9859  H HD22 . ASN   A  1 654 ? 41.151 26.300  -62.667 0.00 47.52  ? 680  ASN   A HD22 1 
ATOM   9860  N N    . TRP   A  1 655 ? 37.569 28.604  -58.401 1.00 28.81  ? 681  TRP   A N    1 
ATOM   9861  C CA   . TRP   A  1 655 ? 36.123 28.772  -58.221 1.00 29.02  ? 681  TRP   A CA   1 
ATOM   9862  C C    . TRP   A  1 655 ? 35.351 28.811  -59.537 1.00 29.31  ? 681  TRP   A C    1 
ATOM   9863  O O    . TRP   A  1 655 ? 34.173 28.449  -59.557 1.00 29.49  ? 681  TRP   A O    1 
ATOM   9864  C CB   . TRP   A  1 655 ? 35.823 30.051  -57.422 1.00 28.69  ? 681  TRP   A CB   1 
ATOM   9865  C CG   . TRP   A  1 655 ? 36.406 30.058  -56.043 1.00 28.16  ? 681  TRP   A CG   1 
ATOM   9866  C CD1  . TRP   A  1 655 ? 37.636 30.518  -55.678 1.00 28.54  ? 681  TRP   A CD1  1 
ATOM   9867  C CD2  . TRP   A  1 655 ? 35.830 29.473  -54.870 1.00 27.99  ? 681  TRP   A CD2  1 
ATOM   9868  N NE1  . TRP   A  1 655 ? 37.859 30.261  -54.349 1.00 28.38  ? 681  TRP   A NE1  1 
ATOM   9869  C CE2  . TRP   A  1 655 ? 36.763 29.622  -53.827 1.00 28.47  ? 681  TRP   A CE2  1 
ATOM   9870  C CE3  . TRP   A  1 655 ? 34.622 28.818  -54.604 1.00 28.69  ? 681  TRP   A CE3  1 
ATOM   9871  C CZ2  . TRP   A  1 655 ? 36.502 29.189  -52.527 1.00 29.00  ? 681  TRP   A CZ2  1 
ATOM   9872  C CZ3  . TRP   A  1 655 ? 34.362 28.398  -53.314 1.00 29.42  ? 681  TRP   A CZ3  1 
ATOM   9873  C CH2  . TRP   A  1 655 ? 35.305 28.563  -52.299 1.00 29.38  ? 681  TRP   A CH2  1 
ATOM   9874  H H    . TRP   A  1 655 ? 38.112 29.396  -58.071 0.00 38.49  ? 681  TRP   A H    1 
ATOM   9875  H HA   . TRP   A  1 655 ? 35.748 27.928  -57.644 0.00 38.30  ? 681  TRP   A HA   1 
ATOM   9876  H HB2  . TRP   A  1 655 ? 36.222 30.909  -57.961 0.00 39.30  ? 681  TRP   A HB2  1 
ATOM   9877  H HB3  . TRP   A  1 655 ? 34.741 30.141  -57.324 0.00 39.01  ? 681  TRP   A HB3  1 
ATOM   9878  H HD1  . TRP   A  1 655 ? 38.338 30.995  -56.340 0.00 38.47  ? 681  TRP   A HD1  1 
ATOM   9879  H HE1  . TRP   A  1 655 ? 38.705 30.538  -53.814 0.00 37.45  ? 681  TRP   A HE1  1 
ATOM   9880  H HE3  . TRP   A  1 655 ? 33.891 28.681  -55.382 0.00 37.98  ? 681  TRP   A HE3  1 
ATOM   9881  H HZ2  . TRP   A  1 655 ? 37.223 29.320  -51.740 0.00 37.36  ? 681  TRP   A HZ2  1 
ATOM   9882  H HZ3  . TRP   A  1 655 ? 33.435 27.898  -53.098 0.00 38.06  ? 681  TRP   A HZ3  1 
ATOM   9883  H HH2  . TRP   A  1 655 ? 35.075 28.214  -51.306 0.00 37.52  ? 681  TRP   A HH2  1 
ATOM   9884  N N    . THR   A  1 656 ? 35.993 29.266  -60.629 1.00 29.74  ? 682  THR   A N    1 
ATOM   9885  C CA   . THR   A  1 656 ? 35.351 29.348  -61.941 1.00 30.40  ? 682  THR   A CA   1 
ATOM   9886  C C    . THR   A  1 656 ? 34.821 27.995  -62.424 1.00 29.62  ? 682  THR   A C    1 
ATOM   9887  O O    . THR   A  1 656 ? 33.811 27.954  -63.124 1.00 29.59  ? 682  THR   A O    1 
ATOM   9888  C CB   . THR   A  1 656 ? 36.336 29.925  -62.979 1.00 33.25  ? 682  THR   A CB   1 
ATOM   9889  O OG1  . THR   A  1 656 ? 36.909 31.132  -62.463 1.00 35.39  ? 682  THR   A OG1  1 
ATOM   9890  C CG2  . THR   A  1 656 ? 35.673 30.221  -64.309 1.00 33.94  ? 682  THR   A CG2  1 
ATOM   9891  H H    . THR   A  1 656 ? 36.952 29.598  -60.623 0.00 40.56  ? 682  THR   A H    1 
ATOM   9892  H HA   . THR   A  1 656 ? 34.503 30.029  -61.872 0.00 42.37  ? 682  THR   A HA   1 
ATOM   9893  H HB   . THR   A  1 656 ? 37.131 29.201  -63.154 0.00 45.34  ? 682  THR   A HB   1 
ATOM   9894  H HG1  . THR   A  1 656 ? 36.189 31.745  -62.157 0.00 48.94  ? 682  THR   A HG1  1 
ATOM   9895  H HG21 . THR   A  1 656 ? 36.322 30.856  -64.909 0.00 47.68  ? 682  THR   A HG21 1 
ATOM   9896  H HG22 . THR   A  1 656 ? 35.492 29.296  -64.856 0.00 47.08  ? 682  THR   A HG22 1 
ATOM   9897  H HG23 . THR   A  1 656 ? 34.723 30.730  -64.148 0.00 47.67  ? 682  THR   A HG23 1 
ATOM   9898  N N    . LEU   A  1 657 ? 35.480 26.895  -62.034 1.00 29.08  ? 683  LEU   A N    1 
ATOM   9899  C CA   . LEU   A  1 657 ? 35.109 25.548  -62.463 1.00 29.65  ? 683  LEU   A CA   1 
ATOM   9900  C C    . LEU   A  1 657 ? 33.787 25.045  -61.882 1.00 30.68  ? 683  LEU   A C    1 
ATOM   9901  O O    . LEU   A  1 657 ? 33.252 24.061  -62.398 1.00 30.76  ? 683  LEU   A O    1 
ATOM   9902  C CB   . LEU   A  1 657 ? 36.261 24.578  -62.152 1.00 29.82  ? 683  LEU   A CB   1 
ATOM   9903  C CG   . LEU   A  1 657 ? 37.641 24.966  -62.736 1.00 32.07  ? 683  LEU   A CG   1 
ATOM   9904  C CD1  . LEU   A  1 657 ? 38.694 23.924  -62.426 1.00 32.12  ? 683  LEU   A CD1  1 
ATOM   9905  C CD2  . LEU   A  1 657 ? 37.587 25.251  -64.241 1.00 33.03  ? 683  LEU   A CD2  1 
ATOM   9906  H H    . LEU   A  1 657 ? 36.266 26.905  -61.394 0.00 38.92  ? 683  LEU   A H    1 
ATOM   9907  H HA   . LEU   A  1 657 ? 34.971 25.563  -63.542 0.00 39.98  ? 683  LEU   A HA   1 
ATOM   9908  H HB2  . LEU   A  1 657 ? 36.380 24.543  -61.069 0.00 38.75  ? 683  LEU   A HB2  1 
ATOM   9909  H HB3  . LEU   A  1 657 ? 36.001 23.582  -62.502 0.00 38.91  ? 683  LEU   A HB3  1 
ATOM   9910  H HG   . LEU   A  1 657 ? 37.967 25.887  -62.255 0.00 42.10  ? 683  LEU   A HG   1 
ATOM   9911  H HD11 . LEU   A  1 657 ? 39.664 24.284  -62.766 0.00 41.52  ? 683  LEU   A HD11 1 
ATOM   9912  H HD12 . LEU   A  1 657 ? 38.717 23.750  -61.352 0.00 40.98  ? 683  LEU   A HD12 1 
ATOM   9913  H HD13 . LEU   A  1 657 ? 38.439 23.002  -62.948 0.00 41.28  ? 683  LEU   A HD13 1 
ATOM   9914  H HD21 . LEU   A  1 657 ? 38.605 25.346  -64.617 0.00 43.75  ? 683  LEU   A HD21 1 
ATOM   9915  H HD22 . LEU   A  1 657 ? 37.084 24.422  -64.735 0.00 43.66  ? 683  LEU   A HD22 1 
ATOM   9916  H HD23 . LEU   A  1 657 ? 37.046 26.180  -64.414 0.00 44.23  ? 683  LEU   A HD23 1 
ATOM   9917  N N    . LEU   A  1 658 ? 33.217 25.727  -60.867 1.00 31.09  ? 684  LEU   A N    1 
ATOM   9918  C CA   . LEU   A  1 658 ? 31.912 25.318  -60.336 1.00 31.89  ? 684  LEU   A CA   1 
ATOM   9919  C C    . LEU   A  1 658 ? 30.773 25.493  -61.373 1.00 33.83  ? 684  LEU   A C    1 
ATOM   9920  O O    . LEU   A  1 658 ? 29.690 24.941  -61.167 1.00 33.93  ? 684  LEU   A O    1 
ATOM   9921  C CB   . LEU   A  1 658 ? 31.584 26.055  -59.028 1.00 31.21  ? 684  LEU   A CB   1 
ATOM   9922  C CG   . LEU   A  1 658 ? 32.570 25.840  -57.880 1.00 31.33  ? 684  LEU   A CG   1 
ATOM   9923  C CD1  . LEU   A  1 658 ? 32.151 26.620  -56.652 1.00 30.80  ? 684  LEU   A CD1  1 
ATOM   9924  C CD2  . LEU   A  1 658 ? 32.718 24.354  -57.530 1.00 32.20  ? 684  LEU   A CD2  1 
ATOM   9925  H H    . LEU   A  1 658 ? 33.613 26.538  -60.403 0.00 41.35  ? 684  LEU   A H    1 
ATOM   9926  H HA   . LEU   A  1 658 ? 31.952 24.253  -60.115 0.00 41.65  ? 684  LEU   A HA   1 
ATOM   9927  H HB2  . LEU   A  1 658 ? 31.551 27.123  -59.235 0.00 41.84  ? 684  LEU   A HB2  1 
ATOM   9928  H HB3  . LEU   A  1 658 ? 30.606 25.724  -58.682 0.00 41.30  ? 684  LEU   A HB3  1 
ATOM   9929  H HG   . LEU   A  1 658 ? 33.549 26.205  -58.187 0.00 40.86  ? 684  LEU   A HG   1 
ATOM   9930  H HD11 . LEU   A  1 658 ? 32.911 26.506  -55.880 0.00 39.88  ? 684  LEU   A HD11 1 
ATOM   9931  H HD12 . LEU   A  1 658 ? 32.043 27.670  -56.917 0.00 40.83  ? 684  LEU   A HD12 1 
ATOM   9932  H HD13 . LEU   A  1 658 ? 31.200 26.230  -56.292 0.00 40.22  ? 684  LEU   A HD13 1 
ATOM   9933  H HD21 . LEU   A  1 658 ? 33.200 24.261  -56.558 0.00 40.76  ? 684  LEU   A HD21 1 
ATOM   9934  H HD22 . LEU   A  1 658 ? 31.731 23.897  -57.507 0.00 41.17  ? 684  LEU   A HD22 1 
ATOM   9935  H HD23 . LEU   A  1 658 ? 33.336 23.869  -58.285 0.00 41.05  ? 684  LEU   A HD23 1 
ATOM   9936  N N    . GLN   A  1 659 ? 31.020 26.229  -62.481 1.00 35.02  ? 685  GLN   A N    1 
ATOM   9937  C CA   . GLN   A  1 659 ? 30.067 26.419  -63.584 1.00 36.38  ? 685  GLN   A CA   1 
ATOM   9938  C C    . GLN   A  1 659 ? 29.643 25.102  -64.205 1.00 37.23  ? 685  GLN   A C    1 
ATOM   9939  O O    . GLN   A  1 659 ? 28.508 24.991  -64.669 1.00 37.63  ? 685  GLN   A O    1 
ATOM   9940  C CB   . GLN   A  1 659 ? 30.707 27.245  -64.711 1.00 38.46  ? 685  GLN   A CB   1 
ATOM   9941  C CG   . GLN   A  1 659 ? 30.834 28.708  -64.411 1.00 42.56  ? 685  GLN   A CG   1 
ATOM   9942  C CD   . GLN   A  1 659 ? 31.419 29.430  -65.595 1.00 46.94  ? 685  GLN   A CD   1 
ATOM   9943  O OE1  . GLN   A  1 659 ? 32.630 29.376  -65.841 1.00 48.07  ? 685  GLN   A OE1  1 
ATOM   9944  N NE2  . GLN   A  1 659 ? 30.580 30.100  -66.370 1.00 47.70  ? 685  GLN   A NE2  1 
ATOM   9945  H H    . GLN   A  1 659 ? 31.887 26.734  -62.631 0.00 47.24  ? 685  GLN   A H    1 
ATOM   9946  H HA   . GLN   A  1 659 ? 29.180 26.934  -63.219 0.00 49.84  ? 685  GLN   A HA   1 
ATOM   9947  H HB2  . GLN   A  1 659 ? 31.702 26.857  -64.924 0.00 52.29  ? 685  GLN   A HB2  1 
ATOM   9948  H HB3  . GLN   A  1 659 ? 30.086 27.149  -65.600 0.00 53.08  ? 685  GLN   A HB3  1 
ATOM   9949  H HG2  . GLN   A  1 659 ? 29.840 29.103  -64.204 0.00 58.41  ? 685  GLN   A HG2  1 
ATOM   9950  H HG3  . GLN   A  1 659 ? 31.508 28.839  -63.565 0.00 57.62  ? 685  GLN   A HG3  1 
ATOM   9951  H HE21 . GLN   A  1 659 ? 29.585 30.117  -66.169 0.00 65.89  ? 685  GLN   A HE21 1 
ATOM   9952  H HE22 . GLN   A  1 659 ? 30.936 30.601  -67.178 0.00 66.14  ? 685  GLN   A HE22 1 
ATOM   9953  N N    . GLN   A  1 660 ? 30.572 24.130  -64.279 1.00 37.45  ? 686  GLN   A N    1 
ATOM   9954  C CA   . GLN   A  1 660 ? 30.300 22.814  -64.863 1.00 37.94  ? 686  GLN   A CA   1 
ATOM   9955  C C    . GLN   A  1 660 ? 29.579 21.865  -63.926 1.00 36.33  ? 686  GLN   A C    1 
ATOM   9956  O O    . GLN   A  1 660 ? 29.414 20.704  -64.298 1.00 36.74  ? 686  GLN   A O    1 
ATOM   9957  C CB   . GLN   A  1 660 ? 31.611 22.132  -65.284 1.00 41.34  ? 686  GLN   A CB   1 
ATOM   9958  C CG   . GLN   A  1 660 ? 32.598 22.991  -66.067 1.00 48.46  ? 686  GLN   A CG   1 
ATOM   9959  C CD   . GLN   A  1 660 ? 31.993 23.880  -67.092 1.00 56.34  ? 686  GLN   A CD   1 
ATOM   9960  O OE1  . GLN   A  1 660 ? 31.166 23.429  -67.875 1.00 58.71  ? 686  GLN   A OE1  1 
ATOM   9961  N NE2  . GLN   A  1 660 ? 32.401 25.139  -67.109 1.00 59.12  ? 686  GLN   A NE2  1 
ATOM   9962  H H    . GLN   A  1 660 ? 31.519 24.221  -63.925 0.00 49.69  ? 686  GLN   A H    1 
ATOM   9963  H HA   . GLN   A  1 660 ? 29.681 22.929  -65.751 0.00 50.95  ? 686  GLN   A HA   1 
ATOM   9964  H HB2  . GLN   A  1 660 ? 32.122 21.788  -64.386 0.00 53.52  ? 686  GLN   A HB2  1 
ATOM   9965  H HB3  . GLN   A  1 660 ? 31.371 21.277  -65.914 0.00 54.08  ? 686  GLN   A HB3  1 
ATOM   9966  H HG2  . GLN   A  1 660 ? 33.214 23.567  -65.378 0.00 62.81  ? 686  GLN   A HG2  1 
ATOM   9967  H HG3  . GLN   A  1 660 ? 33.210 22.311  -66.656 0.00 62.86  ? 686  GLN   A HG3  1 
ATOM   9968  H HE21 . GLN   A  1 660 ? 33.094 25.472  -66.447 0.00 76.76  ? 686  GLN   A HE21 1 
ATOM   9969  H HE22 . GLN   A  1 660 ? 32.018 25.788  -67.785 0.00 77.67  ? 686  GLN   A HE22 1 
ATOM   9970  N N    . PHE   A  1 661 ? 29.184 22.313  -62.715 1.00 34.70  ? 687  PHE   A N    1 
ATOM   9971  C CA   . PHE   A  1 661 ? 28.508 21.481  -61.729 1.00 33.82  ? 687  PHE   A CA   1 
ATOM   9972  C C    . PHE   A  1 661 ? 27.203 22.164  -61.337 1.00 32.67  ? 687  PHE   A C    1 
ATOM   9973  O O    . PHE   A  1 661 ? 27.106 22.742  -60.258 1.00 32.03  ? 687  PHE   A O    1 
ATOM   9974  C CB   . PHE   A  1 661 ? 29.431 21.262  -60.521 1.00 34.01  ? 687  PHE   A CB   1 
ATOM   9975  C CG   . PHE   A  1 661 ? 30.671 20.517  -60.934 1.00 34.87  ? 687  PHE   A CG   1 
ATOM   9976  C CD1  . PHE   A  1 661 ? 31.774 21.194  -61.422 1.00 35.58  ? 687  PHE   A CD1  1 
ATOM   9977  C CD2  . PHE   A  1 661 ? 30.690 19.134  -60.949 1.00 35.62  ? 687  PHE   A CD2  1 
ATOM   9978  C CE1  . PHE   A  1 661 ? 32.876 20.504  -61.898 1.00 36.48  ? 687  PHE   A CE1  1 
ATOM   9979  C CE2  . PHE   A  1 661 ? 31.801 18.449  -61.402 1.00 36.47  ? 687  PHE   A CE2  1 
ATOM   9980  C CZ   . PHE   A  1 661 ? 32.886 19.136  -61.876 1.00 36.47  ? 687  PHE   A CZ   1 
ATOM   9981  H H    . PHE   A  1 661 ? 29.312 23.263  -62.383 0.00 46.05  ? 687  PHE   A H    1 
ATOM   9982  H HA   . PHE   A  1 661 ? 28.280 20.494  -62.128 0.00 44.23  ? 687  PHE   A HA   1 
ATOM   9983  H HB2  . PHE   A  1 661 ? 29.720 22.217  -60.086 0.00 43.96  ? 687  PHE   A HB2  1 
ATOM   9984  H HB3  . PHE   A  1 661 ? 28.910 20.640  -59.796 0.00 43.55  ? 687  PHE   A HB3  1 
ATOM   9985  H HD1  . PHE   A  1 661 ? 31.764 22.270  -61.455 0.00 45.83  ? 687  PHE   A HD1  1 
ATOM   9986  H HD2  . PHE   A  1 661 ? 29.834 18.586  -60.595 0.00 44.88  ? 687  PHE   A HD2  1 
ATOM   9987  H HE1  . PHE   A  1 661 ? 33.740 21.045  -62.243 0.00 46.36  ? 687  PHE   A HE1  1 
ATOM   9988  H HE2  . PHE   A  1 661 ? 31.812 17.372  -61.383 0.00 45.37  ? 687  PHE   A HE2  1 
ATOM   9989  H HZ   . PHE   A  1 661 ? 33.759 18.599  -62.207 0.00 45.60  ? 687  PHE   A HZ   1 
ATOM   9990  N N    . PRO   A  1 662 ? 26.183 22.095  -62.221 1.00 32.31  ? 688  PRO   A N    1 
ATOM   9991  C CA   . PRO   A  1 662 ? 24.923 22.812  -61.957 1.00 32.33  ? 688  PRO   A CA   1 
ATOM   9992  C C    . PRO   A  1 662 ? 24.030 22.248  -60.863 1.00 32.34  ? 688  PRO   A C    1 
ATOM   9993  O O    . PRO   A  1 662 ? 23.053 22.897  -60.495 1.00 32.65  ? 688  PRO   A O    1 
ATOM   9994  C CB   . PRO   A  1 662 ? 24.217 22.785  -63.319 1.00 33.29  ? 688  PRO   A CB   1 
ATOM   9995  C CG   . PRO   A  1 662 ? 24.706 21.533  -63.959 1.00 33.65  ? 688  PRO   A CG   1 
ATOM   9996  C CD   . PRO   A  1 662 ? 26.152 21.423  -63.538 1.00 31.68  ? 688  PRO   A CD   1 
ATOM   9997  H HA   . PRO   A  1 662 ? 25.143 23.850  -61.711 0.00 44.45  ? 688  PRO   A HA   1 
ATOM   9998  H HB2  . PRO   A  1 662 ? 23.138 22.751  -63.181 0.00 46.42  ? 688  PRO   A HB2  1 
ATOM   9999  H HB3  . PRO   A  1 662 ? 24.509 23.656  -63.904 0.00 46.56  ? 688  PRO   A HB3  1 
ATOM   10000 H HG2  . PRO   A  1 662 ? 24.131 20.685  -63.592 0.00 45.93  ? 688  PRO   A HG2  1 
ATOM   10001 H HG3  . PRO   A  1 662 ? 24.624 21.618  -65.042 0.00 46.64  ? 688  PRO   A HG3  1 
ATOM   10002 H HD2  . PRO   A  1 662 ? 26.416 20.370  -63.449 0.00 42.66  ? 688  PRO   A HD2  1 
ATOM   10003 H HD3  . PRO   A  1 662 ? 26.797 21.939  -64.246 0.00 43.37  ? 688  PRO   A HD3  1 
ATOM   10004 N N    . ARG   A  1 663 ? 24.331 21.048  -60.366 1.00 31.79  ? 689  ARG   A N    1 
ATOM   10005 C CA   . ARG   A  1 663 ? 23.570 20.421  -59.288 1.00 32.04  ? 689  ARG   A CA   1 
ATOM   10006 C C    . ARG   A  1 663 ? 24.318 20.501  -57.933 1.00 30.75  ? 689  ARG   A C    1 
ATOM   10007 O O    . ARG   A  1 663 ? 23.799 19.985  -56.941 1.00 30.68  ? 689  ARG   A O    1 
ATOM   10008 C CB   . ARG   A  1 663 ? 23.322 18.945  -59.633 1.00 35.12  ? 689  ARG   A CB   1 
ATOM   10009 C CG   . ARG   A  1 663 ? 22.638 18.717  -60.986 1.00 40.99  ? 689  ARG   A CG   1 
ATOM   10010 C CD   . ARG   A  1 663 ? 21.127 18.695  -60.864 1.00 46.59  ? 689  ARG   A CD   1 
ATOM   10011 N NE   . ARG   A  1 663 ? 20.468 18.294  -62.110 1.00 51.48  ? 689  ARG   A NE   1 
ATOM   10012 C CZ   . ARG   A  1 663 ? 20.268 19.088  -63.163 1.00 55.55  ? 689  ARG   A CZ   1 
ATOM   10013 N NH1  . ARG   A  1 663 ? 19.647 18.624  -64.242 1.00 56.16  ? 689  ARG   A NH1  1 
ATOM   10014 N NH2  . ARG   A  1 663 ? 20.699 20.349  -63.151 1.00 55.65  ? 689  ARG   A NH2  1 
ATOM   10015 H H    . ARG   A  1 663 ? 25.092 20.459  -60.686 0.00 42.24  ? 689  ARG   A H    1 
ATOM   10016 H HA   . ARG   A  1 663 ? 22.597 20.895  -59.170 0.00 43.04  ? 689  ARG   A HA   1 
ATOM   10017 H HB2  . ARG   A  1 663 ? 24.276 18.421  -59.648 0.00 45.52  ? 689  ARG   A HB2  1 
ATOM   10018 H HB3  . ARG   A  1 663 ? 22.677 18.518  -58.867 0.00 45.83  ? 689  ARG   A HB3  1 
ATOM   10019 H HG2  . ARG   A  1 663 ? 22.903 19.500  -61.694 0.00 54.07  ? 689  ARG   A HG2  1 
ATOM   10020 H HG3  . ARG   A  1 663 ? 22.951 17.748  -61.374 0.00 53.42  ? 689  ARG   A HG3  1 
ATOM   10021 H HD2  . ARG   A  1 663 ? 20.847 17.958  -60.113 0.00 60.55  ? 689  ARG   A HD2  1 
ATOM   10022 H HD3  . ARG   A  1 663 ? 20.766 19.676  -60.559 0.00 61.27  ? 689  ARG   A HD3  1 
ATOM   10023 H HE   . ARG   A  1 663 ? 20.116 17.343  -62.160 0.00 67.28  ? 689  ARG   A HE   1 
ATOM   10024 H HH11 . ARG   A  1 663 ? 19.312 17.666  -64.269 0.00 74.15  ? 689  ARG   A HH11 1 
ATOM   10025 H HH12 . ARG   A  1 663 ? 19.503 19.225  -65.048 0.00 74.85  ? 689  ARG   A HH12 1 
ATOM   10026 H HH21 . ARG   A  1 663 ? 21.187 20.747  -62.356 0.00 72.97  ? 689  ARG   A HH21 1 
ATOM   10027 H HH22 . ARG   A  1 663 ? 20.548 20.935  -63.966 0.00 73.92  ? 689  ARG   A HH22 1 
ATOM   10028 N N    . LEU   A  1 664 ? 25.535 21.104  -57.880 1.00 29.40  ? 690  LEU   A N    1 
ATOM   10029 C CA   . LEU   A  1 664 ? 26.308 21.159  -56.637 1.00 28.77  ? 690  LEU   A CA   1 
ATOM   10030 C C    . LEU   A  1 664 ? 25.640 22.006  -55.560 1.00 28.71  ? 690  LEU   A C    1 
ATOM   10031 O O    . LEU   A  1 664 ? 25.535 23.219  -55.718 1.00 29.30  ? 690  LEU   A O    1 
ATOM   10032 C CB   . LEU   A  1 664 ? 27.731 21.660  -56.901 1.00 28.48  ? 690  LEU   A CB   1 
ATOM   10033 C CG   . LEU   A  1 664 ? 28.723 21.503  -55.727 1.00 29.25  ? 690  LEU   A CG   1 
ATOM   10034 C CD1  . LEU   A  1 664 ? 28.914 20.025  -55.343 1.00 29.64  ? 690  LEU   A CD1  1 
ATOM   10035 C CD2  . LEU   A  1 664 ? 30.059 22.142  -56.077 1.00 30.27  ? 690  LEU   A CD2  1 
ATOM   10036 H H    . LEU   A  1 664 ? 26.003 21.560  -58.656 0.00 38.79  ? 690  LEU   A H    1 
ATOM   10037 H HA   . LEU   A  1 664 ? 26.397 20.141  -56.267 0.00 36.71  ? 690  LEU   A HA   1 
ATOM   10038 H HB2  . LEU   A  1 664 ? 28.135 21.083  -57.728 0.00 36.63  ? 690  LEU   A HB2  1 
ATOM   10039 H HB3  . LEU   A  1 664 ? 27.694 22.713  -57.172 0.00 37.16  ? 690  LEU   A HB3  1 
ATOM   10040 H HG   . LEU   A  1 664 ? 28.339 22.022  -54.851 0.00 37.01  ? 690  LEU   A HG   1 
ATOM   10041 H HD11 . LEU   A  1 664 ? 29.832 19.919  -54.767 0.00 36.39  ? 690  LEU   A HD11 1 
ATOM   10042 H HD12 . LEU   A  1 664 ? 28.073 19.702  -54.732 0.00 36.73  ? 690  LEU   A HD12 1 
ATOM   10043 H HD13 . LEU   A  1 664 ? 28.968 19.424  -56.248 0.00 36.84  ? 690  LEU   A HD13 1 
ATOM   10044 H HD21 . LEU   A  1 664 ? 30.743 22.029  -55.236 0.00 37.77  ? 690  LEU   A HD21 1 
ATOM   10045 H HD22 . LEU   A  1 664 ? 30.468 21.652  -56.959 0.00 38.15  ? 690  LEU   A HD22 1 
ATOM   10046 H HD23 . LEU   A  1 664 ? 29.891 23.198  -56.279 0.00 38.67  ? 690  LEU   A HD23 1 
ATOM   10047 N N    . GLU   A  1 665 ? 25.230 21.359  -54.459 1.00 28.00  ? 691  GLU   A N    1 
ATOM   10048 C CA   . GLU   A  1 665 ? 24.560 21.959  -53.310 1.00 27.99  ? 691  GLU   A CA   1 
ATOM   10049 C C    . GLU   A  1 665 ? 25.494 22.143  -52.118 1.00 26.86  ? 691  GLU   A C    1 
ATOM   10050 O O    . GLU   A  1 665 ? 25.281 23.064  -51.332 1.00 27.10  ? 691  GLU   A O    1 
ATOM   10051 C CB   . GLU   A  1 665 ? 23.395 21.063  -52.853 1.00 31.60  ? 691  GLU   A CB   1 
ATOM   10052 C CG   . GLU   A  1 665 ? 22.264 20.972  -53.855 1.00 38.88  ? 691  GLU   A CG   1 
ATOM   10053 C CD   . GLU   A  1 665 ? 21.060 20.193  -53.356 1.00 48.55  ? 691  GLU   A CD   1 
ATOM   10054 O OE1  . GLU   A  1 665 ? 21.244 19.219  -52.591 1.00 50.21  ? 691  GLU   A OE1  1 
ATOM   10055 O OE2  . GLU   A  1 665 ? 19.927 20.553  -53.746 1.00 52.70  ? 691  GLU   A OE2  1 
ATOM   10056 H H    . GLU   A  1 665 ? 25.363 20.362  -54.327 0.00 35.64  ? 691  GLU   A H    1 
ATOM   10057 H HA   . GLU   A  1 665 ? 24.146 22.928  -53.583 0.00 36.73  ? 691  GLU   A HA   1 
ATOM   10058 H HB2  . GLU   A  1 665 ? 23.774 20.061  -52.664 0.00 39.93  ? 691  GLU   A HB2  1 
ATOM   10059 H HB3  . GLU   A  1 665 ? 22.986 21.466  -51.929 0.00 40.50  ? 691  GLU   A HB3  1 
ATOM   10060 H HG2  . GLU   A  1 665 ? 21.931 21.977  -54.103 0.00 50.34  ? 691  GLU   A HG2  1 
ATOM   10061 H HG3  . GLU   A  1 665 ? 22.631 20.479  -54.753 0.00 49.73  ? 691  GLU   A HG3  1 
ATOM   10062 N N    . LEU   A  1 666 ? 26.453 21.228  -51.922 1.00 25.34  ? 692  LEU   A N    1 
ATOM   10063 C CA   . LEU   A  1 666 ? 27.350 21.304  -50.774 1.00 24.92  ? 692  LEU   A CA   1 
ATOM   10064 C C    . LEU   A  1 666 ? 28.800 21.194  -51.198 1.00 24.11  ? 692  LEU   A C    1 
ATOM   10065 O O    . LEU   A  1 666 ? 29.182 20.220  -51.846 1.00 23.37  ? 692  LEU   A O    1 
ATOM   10066 C CB   . LEU   A  1 666 ? 27.015 20.192  -49.768 1.00 25.20  ? 692  LEU   A CB   1 
ATOM   10067 C CG   . LEU   A  1 666 ? 27.711 20.271  -48.399 1.00 27.10  ? 692  LEU   A CG   1 
ATOM   10068 C CD1  . LEU   A  1 666 ? 26.822 19.690  -47.325 1.00 28.19  ? 692  LEU   A CD1  1 
ATOM   10069 C CD2  . LEU   A  1 666 ? 29.018 19.535  -48.397 1.00 27.60  ? 692  LEU   A CD2  1 
ATOM   10070 H H    . LEU   A  1 666 ? 26.629 20.426  -52.520 0.00 31.65  ? 692  LEU   A H    1 
ATOM   10071 H HA   . LEU   A  1 666 ? 27.227 22.254  -50.256 0.00 31.12  ? 692  LEU   A HA   1 
ATOM   10072 H HB2  . LEU   A  1 666 ? 25.942 20.218  -49.585 0.00 30.95  ? 692  LEU   A HB2  1 
ATOM   10073 H HB3  . LEU   A  1 666 ? 27.275 19.236  -50.219 0.00 30.41  ? 692  LEU   A HB3  1 
ATOM   10074 H HG   . LEU   A  1 666 ? 27.923 21.303  -48.125 0.00 32.81  ? 692  LEU   A HG   1 
ATOM   10075 H HD11 . LEU   A  1 666 ? 27.376 19.655  -46.388 0.00 33.39  ? 692  LEU   A HD11 1 
ATOM   10076 H HD12 . LEU   A  1 666 ? 25.944 20.324  -47.211 0.00 34.12  ? 692  LEU   A HD12 1 
ATOM   10077 H HD13 . LEU   A  1 666 ? 26.520 18.686  -47.618 0.00 33.50  ? 692  LEU   A HD13 1 
ATOM   10078 H HD21 . LEU   A  1 666 ? 29.660 20.028  -47.671 0.00 32.49  ? 692  LEU   A HD21 1 
ATOM   10079 H HD22 . LEU   A  1 666 ? 28.853 18.506  -48.084 0.00 32.27  ? 692  LEU   A HD22 1 
ATOM   10080 H HD23 . LEU   A  1 666 ? 29.466 19.570  -49.389 0.00 32.71  ? 692  LEU   A HD23 1 
ATOM   10081 N N    . LEU   A  1 667 ? 29.622 22.171  -50.790 1.00 23.67  ? 693  LEU   A N    1 
ATOM   10082 C CA   . LEU   A  1 667 ? 31.046 22.164  -51.096 1.00 22.56  ? 693  LEU   A CA   1 
ATOM   10083 C C    . LEU   A  1 667 ? 31.782 22.287  -49.772 1.00 22.12  ? 693  LEU   A C    1 
ATOM   10084 O O    . LEU   A  1 667 ? 31.581 23.256  -49.042 1.00 22.46  ? 693  LEU   A O    1 
ATOM   10085 C CB   . LEU   A  1 667 ? 31.411 23.317  -52.052 1.00 22.02  ? 693  LEU   A CB   1 
ATOM   10086 C CG   . LEU   A  1 667 ? 32.896 23.452  -52.429 1.00 22.84  ? 693  LEU   A CG   1 
ATOM   10087 C CD1  . LEU   A  1 667 ? 33.485 22.122  -52.955 1.00 23.13  ? 693  LEU   A CD1  1 
ATOM   10088 C CD2  . LEU   A  1 667 ? 33.090 24.558  -53.433 1.00 22.85  ? 693  LEU   A CD2  1 
ATOM   10089 H H    . LEU   A  1 667 ? 29.340 22.978  -50.244 0.00 29.36  ? 693  LEU   A H    1 
ATOM   10090 H HA   . LEU   A  1 667 ? 31.325 21.223  -51.565 0.00 27.25  ? 693  LEU   A HA   1 
ATOM   10091 H HB2  . LEU   A  1 667 ? 30.852 23.190  -52.978 0.00 27.71  ? 693  LEU   A HB2  1 
ATOM   10092 H HB3  . LEU   A  1 667 ? 31.123 24.251  -51.574 0.00 27.76  ? 693  LEU   A HB3  1 
ATOM   10093 H HG   . LEU   A  1 667 ? 33.448 23.736  -51.535 0.00 28.10  ? 693  LEU   A HG   1 
ATOM   10094 H HD11 . LEU   A  1 667 ? 34.467 22.314  -53.384 0.00 28.16  ? 693  LEU   A HD11 1 
ATOM   10095 H HD12 . LEU   A  1 667 ? 33.583 21.420  -52.128 0.00 27.72  ? 693  LEU   A HD12 1 
ATOM   10096 H HD13 . LEU   A  1 667 ? 32.819 21.716  -53.715 0.00 28.31  ? 693  LEU   A HD13 1 
ATOM   10097 H HD21 . LEU   A  1 667 ? 34.148 24.635  -53.680 0.00 28.80  ? 693  LEU   A HD21 1 
ATOM   10098 H HD22 . LEU   A  1 667 ? 32.513 24.329  -54.328 0.00 29.12  ? 693  LEU   A HD22 1 
ATOM   10099 H HD23 . LEU   A  1 667 ? 32.740 25.493  -52.999 0.00 29.25  ? 693  LEU   A HD23 1 
ATOM   10100 N N    . ASP   A  1 668 ? 32.573 21.274  -49.425 1.00 21.52  ? 694  ASP   A N    1 
ATOM   10101 C CA   . ASP   A  1 668 ? 33.272 21.244  -48.152 1.00 22.12  ? 694  ASP   A CA   1 
ATOM   10102 C C    . ASP   A  1 668 ? 34.786 21.300  -48.370 1.00 22.40  ? 694  ASP   A C    1 
ATOM   10103 O O    . ASP   A  1 668 ? 35.391 20.334  -48.833 1.00 22.45  ? 694  ASP   A O    1 
ATOM   10104 C CB   . ASP   A  1 668 ? 32.810 20.021  -47.341 1.00 23.15  ? 694  ASP   A CB   1 
ATOM   10105 C CG   . ASP   A  1 668 ? 33.584 19.712  -46.087 1.00 27.10  ? 694  ASP   A CG   1 
ATOM   10106 O OD1  . ASP   A  1 668 ? 34.335 20.595  -45.625 1.00 27.67  ? 694  ASP   A OD1  1 
ATOM   10107 O OD2  . ASP   A  1 668 ? 33.408 18.592  -45.536 1.00 29.30  ? 694  ASP   A OD2  1 
ATOM   10108 H H    . ASP   A  1 668 ? 32.752 20.457  -49.997 0.00 25.16  ? 694  ASP   A H    1 
ATOM   10109 H HA   . ASP   A  1 668 ? 32.998 22.121  -47.574 0.00 26.00  ? 694  ASP   A HA   1 
ATOM   10110 H HB2  . ASP   A  1 668 ? 31.796 20.234  -47.013 0.00 26.70  ? 694  ASP   A HB2  1 
ATOM   10111 H HB3  . ASP   A  1 668 ? 32.784 19.132  -47.965 0.00 26.33  ? 694  ASP   A HB3  1 
ATOM   10112 N N    . LEU   A  1 669 ? 35.374 22.465  -48.078 1.00 21.65  ? 695  LEU   A N    1 
ATOM   10113 C CA   . LEU   A  1 669 ? 36.811 22.720  -48.213 1.00 21.61  ? 695  LEU   A CA   1 
ATOM   10114 C C    . LEU   A  1 669 ? 37.455 23.020  -46.845 1.00 21.01  ? 695  LEU   A C    1 
ATOM   10115 O O    . LEU   A  1 669 ? 38.504 23.646  -46.805 1.00 20.94  ? 695  LEU   A O    1 
ATOM   10116 C CB   . LEU   A  1 669 ? 37.037 23.915  -49.170 1.00 22.33  ? 695  LEU   A CB   1 
ATOM   10117 C CG   . LEU   A  1 669 ? 36.548 23.727  -50.606 1.00 23.60  ? 695  LEU   A CG   1 
ATOM   10118 C CD1  . LEU   A  1 669 ? 36.685 25.019  -51.415 1.00 23.99  ? 695  LEU   A CD1  1 
ATOM   10119 C CD2  . LEU   A  1 669 ? 37.279 22.596  -51.285 1.00 24.62  ? 695  LEU   A CD2  1 
ATOM   10120 H H    . LEU   A  1 669 ? 34.873 23.279  -47.736 0.00 25.60  ? 695  LEU   A H    1 
ATOM   10121 H HA   . LEU   A  1 669 ? 37.323 21.850  -48.617 0.00 24.89  ? 695  LEU   A HA   1 
ATOM   10122 H HB2  . LEU   A  1 669 ? 36.507 24.776  -48.766 0.00 26.95  ? 695  LEU   A HB2  1 
ATOM   10123 H HB3  . LEU   A  1 669 ? 38.101 24.135  -49.229 0.00 26.61  ? 695  LEU   A HB3  1 
ATOM   10124 H HG   . LEU   A  1 669 ? 35.494 23.461  -50.575 0.00 28.42  ? 695  LEU   A HG   1 
ATOM   10125 H HD11 . LEU   A  1 669 ? 36.268 24.866  -52.409 0.00 29.68  ? 695  LEU   A HD11 1 
ATOM   10126 H HD12 . LEU   A  1 669 ? 36.144 25.815  -50.906 0.00 29.78  ? 695  LEU   A HD12 1 
ATOM   10127 H HD13 . LEU   A  1 669 ? 37.740 25.277  -51.492 0.00 29.49  ? 695  LEU   A HD13 1 
ATOM   10128 H HD21 . LEU   A  1 669 ? 37.106 22.653  -52.358 0.00 29.49  ? 695  LEU   A HD21 1 
ATOM   10129 H HD22 . LEU   A  1 669 ? 38.344 22.667  -51.069 0.00 29.13  ? 695  LEU   A HD22 1 
ATOM   10130 H HD23 . LEU   A  1 669 ? 36.878 21.660  -50.899 0.00 28.89  ? 695  LEU   A HD23 1 
ATOM   10131 N N    . ARG   A  1 670 ? 36.872 22.529  -45.747 1.00 20.44  ? 696  ARG   A N    1 
ATOM   10132 C CA   . ARG   A  1 670 ? 37.425 22.756  -44.415 1.00 21.06  ? 696  ARG   A CA   1 
ATOM   10133 C C    . ARG   A  1 670 ? 38.820 22.148  -44.256 1.00 21.88  ? 696  ARG   A C    1 
ATOM   10134 O O    . ARG   A  1 670 ? 39.148 21.198  -44.954 1.00 22.28  ? 696  ARG   A O    1 
ATOM   10135 C CB   . ARG   A  1 670 ? 36.529 22.117  -43.353 1.00 22.19  ? 696  ARG   A CB   1 
ATOM   10136 C CG   . ARG   A  1 670 ? 35.140 22.735  -43.235 1.00 22.97  ? 696  ARG   A CG   1 
ATOM   10137 C CD   . ARG   A  1 670 ? 34.273 21.912  -42.284 1.00 25.80  ? 696  ARG   A CD   1 
ATOM   10138 N NE   . ARG   A  1 670 ? 34.047 20.563  -42.803 1.00 29.15  ? 696  ARG   A NE   1 
ATOM   10139 C CZ   . ARG   A  1 670 ? 33.481 19.573  -42.122 1.00 34.25  ? 696  ARG   A CZ   1 
ATOM   10140 N NH1  . ARG   A  1 670 ? 33.057 19.768  -40.877 1.00 34.51  ? 696  ARG   A NH1  1 
ATOM   10141 N NH2  . ARG   A  1 670 ? 33.331 18.376  -42.681 1.00 34.99  ? 696  ARG   A NH2  1 
ATOM   10142 H H    . ARG   A  1 670 ? 36.043 21.945  -45.745 0.00 23.24  ? 696  ARG   A H    1 
ATOM   10143 H HA   . ARG   A  1 670 ? 37.486 23.826  -44.224 0.00 24.38  ? 696  ARG   A HA   1 
ATOM   10144 H HB2  . ARG   A  1 670 ? 36.423 21.060  -43.590 0.00 24.76  ? 696  ARG   A HB2  1 
ATOM   10145 H HB3  . ARG   A  1 670 ? 37.016 22.223  -42.385 0.00 25.01  ? 696  ARG   A HB3  1 
ATOM   10146 H HG2  . ARG   A  1 670 ? 35.228 23.742  -42.832 0.00 26.73  ? 696  ARG   A HG2  1 
ATOM   10147 H HG3  . ARG   A  1 670 ? 34.660 22.753  -44.212 0.00 26.57  ? 696  ARG   A HG3  1 
ATOM   10148 H HD2  . ARG   A  1 670 ? 34.780 21.829  -41.324 0.00 29.34  ? 696  ARG   A HD2  1 
ATOM   10149 H HD3  . ARG   A  1 670 ? 33.306 22.396  -42.156 0.00 29.81  ? 696  ARG   A HD3  1 
ATOM   10150 H HE   . ARG   A  1 670 ? 34.358 20.371  -43.749 0.00 33.13  ? 696  ARG   A HE   1 
ATOM   10151 H HH11 . ARG   A  1 670 ? 33.152 20.667  -40.417 0.00 39.53  ? 696  ARG   A HH11 1 
ATOM   10152 H HH12 . ARG   A  1 670 ? 32.620 19.005  -40.370 0.00 39.06  ? 696  ARG   A HH12 1 
ATOM   10153 H HH21 . ARG   A  1 670 ? 33.648 18.210  -43.630 0.00 39.54  ? 696  ARG   A HH21 1 
ATOM   10154 H HH22 . ARG   A  1 670 ? 32.892 17.621  -42.162 0.00 39.33  ? 696  ARG   A HH22 1 
ATOM   10155 N N    . GLY   A  1 671 ? 39.617 22.690  -43.342 1.00 21.85  ? 697  GLY   A N    1 
ATOM   10156 C CA   . GLY   A  1 671 ? 40.939 22.145  -43.039 1.00 21.96  ? 697  GLY   A CA   1 
ATOM   10157 C C    . GLY   A  1 671 ? 41.899 22.126  -44.211 1.00 22.39  ? 697  GLY   A C    1 
ATOM   10158 O O    . GLY   A  1 671 ? 42.503 21.094  -44.508 1.00 23.05  ? 697  GLY   A O    1 
ATOM   10159 H H    . GLY   A  1 671 ? 39.380 23.516  -42.805 0.00 24.96  ? 697  GLY   A H    1 
ATOM   10160 H HA2  . GLY   A  1 671 ? 41.392 22.737  -42.246 0.00 24.72  ? 697  GLY   A HA2  1 
ATOM   10161 H HA3  . GLY   A  1 671 ? 40.825 21.123  -42.680 0.00 24.20  ? 697  GLY   A HA3  1 
ATOM   10162 N N    . ASN   A  1 672 ? 42.037 23.258  -44.884 1.00 21.78  ? 698  ASN   A N    1 
ATOM   10163 C CA   . ASN   A  1 672 ? 42.973 23.417  -45.998 1.00 22.05  ? 698  ASN   A CA   1 
ATOM   10164 C C    . ASN   A  1 672 ? 43.843 24.694  -45.716 1.00 22.66  ? 698  ASN   A C    1 
ATOM   10165 O O    . ASN   A  1 672 ? 43.957 25.082  -44.554 1.00 22.58  ? 698  ASN   A O    1 
ATOM   10166 C CB   . ASN   A  1 672 ? 42.164 23.462  -47.320 1.00 22.40  ? 698  ASN   A CB   1 
ATOM   10167 C CG   . ASN   A  1 672 ? 41.795 22.078  -47.815 1.00 24.06  ? 698  ASN   A CG   1 
ATOM   10168 O OD1  . ASN   A  1 672 ? 42.679 21.274  -48.114 1.00 24.53  ? 698  ASN   A OD1  1 
ATOM   10169 N ND2  . ASN   A  1 672 ? 40.506 21.759  -47.910 1.00 22.78  ? 698  ASN   A ND2  1 
ATOM   10170 H H    . ASN   A  1 672 ? 41.514 24.104  -44.681 0.00 25.20  ? 698  ASN   A H    1 
ATOM   10171 H HA   . ASN   A  1 672 ? 43.668 22.579  -46.033 0.00 25.09  ? 698  ASN   A HA   1 
ATOM   10172 H HB2  . ASN   A  1 672 ? 41.249 24.026  -47.143 0.00 26.18  ? 698  ASN   A HB2  1 
ATOM   10173 H HB3  . ASN   A  1 672 ? 42.741 23.956  -48.097 0.00 26.25  ? 698  ASN   A HB3  1 
ATOM   10174 H HD21 . ASN   A  1 672 ? 40.241 20.836  -48.242 0.00 25.71  ? 698  ASN   A HD21 1 
ATOM   10175 H HD22 . ASN   A  1 672 ? 39.783 22.424  -47.656 0.00 26.19  ? 698  ASN   A HD22 1 
ATOM   10176 N N    . LYS   A  1 673 ? 44.505 25.286  -46.725 1.00 22.99  ? 699  LYS   A N    1 
ATOM   10177 C CA   . LYS   A  1 673 ? 45.332 26.482  -46.560 1.00 24.86  ? 699  LYS   A CA   1 
ATOM   10178 C C    . LYS   A  1 673 ? 44.893 27.578  -47.542 1.00 26.79  ? 699  LYS   A C    1 
ATOM   10179 O O    . LYS   A  1 673 ? 45.725 28.335  -48.027 1.00 26.86  ? 699  LYS   A O    1 
ATOM   10180 C CB   . LYS   A  1 673 ? 46.810 26.110  -46.800 1.00 26.61  ? 699  LYS   A CB   1 
ATOM   10181 C CG   . LYS   A  1 673 ? 47.296 25.012  -45.860 1.00 31.36  ? 699  LYS   A CG   1 
ATOM   10182 C CD   . LYS   A  1 673 ? 48.764 24.652  -46.055 1.00 38.14  ? 699  LYS   A CD   1 
ATOM   10183 C CE   . LYS   A  1 673 ? 49.214 23.670  -44.986 1.00 43.23  ? 699  LYS   A CE   1 
ATOM   10184 N NZ   . LYS   A  1 673 ? 50.553 23.084  -45.271 1.00 45.68  ? 699  LYS   A NZ   1 
ATOM   10185 H H    . LYS   A  1 673 ? 44.536 24.940  -47.678 0.00 27.29  ? 699  LYS   A H    1 
ATOM   10186 H HA   . LYS   A  1 673 ? 45.245 26.886  -45.552 0.00 30.12  ? 699  LYS   A HA   1 
ATOM   10187 H HB2  . LYS   A  1 673 ? 46.926 25.757  -47.824 0.00 32.06  ? 699  LYS   A HB2  1 
ATOM   10188 H HB3  . LYS   A  1 673 ? 47.438 26.984  -46.630 0.00 32.46  ? 699  LYS   A HB3  1 
ATOM   10189 H HG2  . LYS   A  1 673 ? 47.168 25.347  -44.832 0.00 37.32  ? 699  LYS   A HG2  1 
ATOM   10190 H HG3  . LYS   A  1 673 ? 46.718 24.105  -46.030 0.00 36.93  ? 699  LYS   A HG3  1 
ATOM   10191 H HD2  . LYS   A  1 673 ? 48.898 24.186  -47.031 0.00 45.38  ? 699  LYS   A HD2  1 
ATOM   10192 H HD3  . LYS   A  1 673 ? 49.372 25.552  -45.975 0.00 45.83  ? 699  LYS   A HD3  1 
ATOM   10193 H HE2  . LYS   A  1 673 ? 49.268 24.187  -44.029 0.00 51.26  ? 699  LYS   A HE2  1 
ATOM   10194 H HE3  . LYS   A  1 673 ? 48.495 22.854  -44.928 0.00 50.77  ? 699  LYS   A HE3  1 
ATOM   10195 H HZ1  . LYS   A  1 673 ? 50.804 22.421  -44.544 0.00 53.82  ? 699  LYS   A HZ1  1 
ATOM   10196 H HZ2  . LYS   A  1 673 ? 50.539 22.604  -46.165 0.00 53.97  ? 699  LYS   A HZ2  1 
ATOM   10197 H HZ3  . LYS   A  1 673 ? 51.253 23.818  -45.303 0.00 54.42  ? 699  LYS   A HZ3  1 
ATOM   10198 N N    . LEU   A  1 674 ? 43.594 27.633  -47.872 1.00 28.00  ? 700  LEU   A N    1 
ATOM   10199 C CA   . LEU   A  1 674 ? 43.088 28.588  -48.849 1.00 30.25  ? 700  LEU   A CA   1 
ATOM   10200 C C    . LEU   A  1 674 ? 43.280 30.017  -48.327 1.00 33.21  ? 700  LEU   A C    1 
ATOM   10201 O O    . LEU   A  1 674 ? 42.997 30.293  -47.161 1.00 32.33  ? 700  LEU   A O    1 
ATOM   10202 C CB   . LEU   A  1 674 ? 41.617 28.291  -49.175 1.00 30.01  ? 700  LEU   A CB   1 
ATOM   10203 C CG   . LEU   A  1 674 ? 41.349 26.902  -49.784 1.00 30.40  ? 700  LEU   A CG   1 
ATOM   10204 C CD1  . LEU   A  1 674 ? 39.862 26.652  -49.936 1.00 30.92  ? 700  LEU   A CD1  1 
ATOM   10205 C CD2  . LEU   A  1 674 ? 42.048 26.742  -51.127 1.00 30.33  ? 700  LEU   A CD2  1 
ATOM   10206 H H    . LEU   A  1 674 ? 42.871 27.057  -47.454 0.00 34.13  ? 700  LEU   A H    1 
ATOM   10207 H HA   . LEU   A  1 674 ? 43.676 28.489  -49.760 0.00 37.75  ? 700  LEU   A HA   1 
ATOM   10208 H HB2  . LEU   A  1 674 ? 41.038 28.361  -48.255 0.00 37.27  ? 700  LEU   A HB2  1 
ATOM   10209 H HB3  . LEU   A  1 674 ? 41.263 29.040  -49.882 0.00 37.80  ? 700  LEU   A HB3  1 
ATOM   10210 H HG   . LEU   A  1 674 ? 41.742 26.136  -49.117 0.00 36.88  ? 700  LEU   A HG   1 
ATOM   10211 H HD11 . LEU   A  1 674 ? 39.709 25.634  -50.289 0.00 37.57  ? 700  LEU   A HD11 1 
ATOM   10212 H HD12 . LEU   A  1 674 ? 39.380 26.786  -48.969 0.00 37.87  ? 700  LEU   A HD12 1 
ATOM   10213 H HD13 . LEU   A  1 674 ? 39.454 27.365  -50.652 0.00 38.38  ? 700  LEU   A HD13 1 
ATOM   10214 H HD21 . LEU   A  1 674 ? 41.636 25.873  -51.639 0.00 37.08  ? 700  LEU   A HD21 1 
ATOM   10215 H HD22 . LEU   A  1 674 ? 41.886 27.640  -51.722 0.00 37.83  ? 700  LEU   A HD22 1 
ATOM   10216 H HD23 . LEU   A  1 674 ? 43.113 26.588  -50.959 0.00 37.23  ? 700  LEU   A HD23 1 
ATOM   10217 N N    . LEU   A  1 675 ? 43.831 30.894  -49.179 1.00 36.12  ? 701  LEU   A N    1 
ATOM   10218 C CA   . LEU   A  1 675 ? 44.203 32.260  -48.816 1.00 39.76  ? 701  LEU   A CA   1 
ATOM   10219 C C    . LEU   A  1 675 ? 43.186 33.314  -49.202 1.00 42.66  ? 701  LEU   A C    1 
ATOM   10220 O O    . LEU   A  1 675 ? 43.200 34.398  -48.614 1.00 43.39  ? 701  LEU   A O    1 
ATOM   10221 C CB   . LEU   A  1 675 ? 45.562 32.595  -49.461 1.00 40.60  ? 701  LEU   A CB   1 
ATOM   10222 C CG   . LEU   A  1 675 ? 46.764 31.799  -48.925 1.00 43.01  ? 701  LEU   A CG   1 
ATOM   10223 C CD1  . LEU   A  1 675 ? 47.913 31.805  -49.917 1.00 43.96  ? 701  LEU   A CD1  1 
ATOM   10224 C CD2  . LEU   A  1 675 ? 47.233 32.353  -47.598 1.00 44.11  ? 701  LEU   A CD2  1 
ATOM   10225 H H    . LEU   A  1 675 ? 44.026 30.679  -50.151 0.00 45.87  ? 701  LEU   A H    1 
ATOM   10226 H HA   . LEU   A  1 675 ? 44.330 32.331  -47.737 0.00 50.76  ? 701  LEU   A HA   1 
ATOM   10227 H HB2  . LEU   A  1 675 ? 45.497 32.413  -50.532 0.00 52.18  ? 701  LEU   A HB2  1 
ATOM   10228 H HB3  . LEU   A  1 675 ? 45.767 33.651  -49.290 0.00 52.66  ? 701  LEU   A HB3  1 
ATOM   10229 H HG   . LEU   A  1 675 ? 46.485 30.758  -48.769 0.00 54.03  ? 701  LEU   A HG   1 
ATOM   10230 H HD11 . LEU   A  1 675 ? 48.746 31.239  -49.501 0.00 55.62  ? 701  LEU   A HD11 1 
ATOM   10231 H HD12 . LEU   A  1 675 ? 47.582 31.342  -50.845 0.00 55.78  ? 701  LEU   A HD12 1 
ATOM   10232 H HD13 . LEU   A  1 675 ? 48.215 32.835  -50.099 0.00 56.46  ? 701  LEU   A HD13 1 
ATOM   10233 H HD21 . LEU   A  1 675 ? 48.125 31.810  -47.288 0.00 55.77  ? 701  LEU   A HD21 1 
ATOM   10234 H HD22 . LEU   A  1 675 ? 47.470 33.410  -47.711 0.00 56.60  ? 701  LEU   A HD22 1 
ATOM   10235 H HD23 . LEU   A  1 675 ? 46.452 32.224  -46.850 0.00 55.86  ? 701  LEU   A HD23 1 
ATOM   10236 N N    . PHE   A  1 676 ? 42.345 33.043  -50.202 1.00 44.13  ? 702  PHE   A N    1 
ATOM   10237 C CA   . PHE   A  1 676 ? 41.343 34.009  -50.624 1.00 46.61  ? 702  PHE   A CA   1 
ATOM   10238 C C    . PHE   A  1 676 ? 40.140 33.337  -51.271 1.00 47.52  ? 702  PHE   A C    1 
ATOM   10239 O O    . PHE   A  1 676 ? 40.184 32.147  -51.601 1.00 48.13  ? 702  PHE   A O    1 
ATOM   10240 C CB   . PHE   A  1 676 ? 41.966 35.086  -51.545 1.00 47.89  ? 702  PHE   A CB   1 
ATOM   10241 C CG   . PHE   A  1 676 ? 42.809 34.541  -52.673 1.00 49.89  ? 702  PHE   A CG   1 
ATOM   10242 C CD1  . PHE   A  1 676 ? 42.224 34.102  -53.846 1.00 51.07  ? 702  PHE   A CD1  1 
ATOM   10243 C CD2  . PHE   A  1 676 ? 44.190 34.499  -52.570 1.00 51.26  ? 702  PHE   A CD2  1 
ATOM   10244 C CE1  . PHE   A  1 676 ? 43.002 33.594  -54.881 1.00 52.03  ? 702  PHE   A CE1  1 
ATOM   10245 C CE2  . PHE   A  1 676 ? 44.964 33.993  -53.608 1.00 52.24  ? 702  PHE   A CE2  1 
ATOM   10246 C CZ   . PHE   A  1 676 ? 44.365 33.557  -54.762 1.00 51.99  ? 702  PHE   A CZ   1 
ATOM   10247 H H    . PHE   A  1 676 ? 42.334 32.184  -50.744 0.00 56.35  ? 702  PHE   A H    1 
ATOM   10248 H HA   . PHE   A  1 676 ? 40.957 34.526  -49.747 0.00 60.51  ? 702  PHE   A HA   1 
ATOM   10249 H HB2  . PHE   A  1 676 ? 41.166 35.677  -51.986 0.00 63.03  ? 702  PHE   A HB2  1 
ATOM   10250 H HB3  . PHE   A  1 676 ? 42.600 35.732  -50.939 0.00 62.84  ? 702  PHE   A HB3  1 
ATOM   10251 H HD1  . PHE   A  1 676 ? 41.153 34.132  -53.947 0.00 66.32  ? 702  PHE   A HD1  1 
ATOM   10252 H HD2  . PHE   A  1 676 ? 44.669 34.838  -51.668 0.00 66.44  ? 702  PHE   A HD2  1 
ATOM   10253 H HE1  . PHE   A  1 676 ? 42.538 33.248  -55.786 0.00 67.29  ? 702  PHE   A HE1  1 
ATOM   10254 H HE2  . PHE   A  1 676 ? 46.036 33.960  -53.513 0.00 67.44  ? 702  PHE   A HE2  1 
ATOM   10255 H HZ   . PHE   A  1 676 ? 44.965 33.166  -55.566 0.00 67.08  ? 702  PHE   A HZ   1 
ATOM   10256 N N    . LEU   A  1 677 ? 39.048 34.109  -51.401 1.00 47.30  ? 703  LEU   A N    1 
ATOM   10257 C CA   . LEU   A  1 677 ? 37.776 33.686  -51.972 1.00 47.75  ? 703  LEU   A CA   1 
ATOM   10258 C C    . LEU   A  1 677 ? 37.482 34.502  -53.221 1.00 47.77  ? 703  LEU   A C    1 
ATOM   10259 O O    . LEU   A  1 677 ? 37.867 35.671  -53.303 1.00 47.69  ? 703  LEU   A O    1 
ATOM   10260 C CB   . LEU   A  1 677 ? 36.660 33.931  -50.936 1.00 48.34  ? 703  LEU   A CB   1 
ATOM   10261 C CG   . LEU   A  1 677 ? 36.135 32.761  -50.082 1.00 50.60  ? 703  LEU   A CG   1 
ATOM   10262 C CD1  . LEU   A  1 677 ? 37.214 31.764  -49.715 1.00 51.37  ? 703  LEU   A CD1  1 
ATOM   10263 C CD2  . LEU   A  1 677 ? 35.487 33.285  -48.816 1.00 51.49  ? 703  LEU   A CD2  1 
ATOM   10264 H H    . LEU   A  1 677 ? 39.045 35.086  -51.125 0.00 62.01  ? 703  LEU   A H    1 
ATOM   10265 H HA   . LEU   A  1 677 ? 37.800 32.636  -52.258 0.00 61.54  ? 703  LEU   A HA   1 
ATOM   10266 H HB2  . LEU   A  1 677 ? 37.009 34.686  -50.233 0.00 63.10  ? 703  LEU   A HB2  1 
ATOM   10267 H HB3  . LEU   A  1 677 ? 35.799 34.329  -51.471 0.00 63.29  ? 703  LEU   A HB3  1 
ATOM   10268 H HG   . LEU   A  1 677 ? 35.372 32.230  -50.648 0.00 64.77  ? 703  LEU   A HG   1 
ATOM   10269 H HD11 . LEU   A  1 677 ? 36.881 31.163  -48.871 0.00 64.66  ? 703  LEU   A HD11 1 
ATOM   10270 H HD12 . LEU   A  1 677 ? 37.409 31.114  -50.565 0.00 64.84  ? 703  LEU   A HD12 1 
ATOM   10271 H HD13 . LEU   A  1 677 ? 38.119 32.310  -49.452 0.00 65.21  ? 703  LEU   A HD13 1 
ATOM   10272 H HD21 . LEU   A  1 677 ? 35.001 32.465  -48.290 0.00 65.67  ? 703  LEU   A HD21 1 
ATOM   10273 H HD22 . LEU   A  1 677 ? 36.252 33.732  -48.185 0.00 66.04  ? 703  LEU   A HD22 1 
ATOM   10274 H HD23 . LEU   A  1 677 ? 34.748 34.038  -49.086 0.00 66.69  ? 703  LEU   A HD23 1 
ATOM   10275 N N    . THR   A  1 678 ? 36.782 33.899  -54.187 1.00 47.56  ? 704  THR   A N    1 
ATOM   10276 C CA   . THR   A  1 678 ? 36.428 34.598  -55.421 1.00 48.07  ? 704  THR   A CA   1 
ATOM   10277 C C    . THR   A  1 678 ? 35.441 35.740  -55.125 1.00 48.52  ? 704  THR   A C    1 
ATOM   10278 O O    . THR   A  1 678 ? 34.597 35.623  -54.232 1.00 48.47  ? 704  THR   A O    1 
ATOM   10279 C CB   . THR   A  1 678 ? 35.841 33.613  -56.458 1.00 48.96  ? 704  THR   A CB   1 
ATOM   10280 O OG1  . THR   A  1 678 ? 35.831 34.232  -57.755 1.00 49.99  ? 704  THR   A OG1  1 
ATOM   10281 C CG2  . THR   A  1 678 ? 34.446 33.096  -56.057 1.00 48.80  ? 704  THR   A CG2  1 
ATOM   10282 H H    . THR   A  1 678 ? 36.457 32.938  -54.141 0.00 62.02  ? 704  THR   A H    1 
ATOM   10283 H HA   . THR   A  1 678 ? 37.340 35.033  -55.830 0.00 64.04  ? 704  THR   A HA   1 
ATOM   10284 H HB   . THR   A  1 678 ? 36.492 32.741  -56.524 0.00 64.16  ? 704  THR   A HB   1 
ATOM   10285 H HG1  . THR   A  1 678 ? 34.986 34.718  -57.945 0.00 66.98  ? 704  THR   A HG1  1 
ATOM   10286 H HG21 . THR   A  1 678 ? 34.147 32.293  -56.728 0.00 64.13  ? 704  THR   A HG21 1 
ATOM   10287 H HG22 . THR   A  1 678 ? 34.468 32.713  -55.037 0.00 63.88  ? 704  THR   A HG22 1 
ATOM   10288 H HG23 . THR   A  1 678 ? 33.700 33.886  -56.123 0.00 64.92  ? 704  THR   A HG23 1 
ATOM   10289 N N    . ASP   A  1 679 ? 35.558 36.839  -55.877 1.00 48.92  ? 705  ASP   A N    1 
ATOM   10290 C CA   . ASP   A  1 679 ? 34.676 38.002  -55.720 1.00 49.87  ? 705  ASP   A CA   1 
ATOM   10291 C C    . ASP   A  1 679 ? 33.440 37.952  -56.646 1.00 49.84  ? 705  ASP   A C    1 
ATOM   10292 O O    . ASP   A  1 679 ? 32.728 38.951  -56.741 1.00 50.07  ? 705  ASP   A O    1 
ATOM   10293 C CB   . ASP   A  1 679 ? 35.475 39.303  -55.972 1.00 52.50  ? 705  ASP   A CB   1 
ATOM   10294 C CG   . ASP   A  1 679 ? 35.968 39.506  -57.395 1.00 58.33  ? 705  ASP   A CG   1 
ATOM   10295 O OD1  . ASP   A  1 679 ? 36.017 38.513  -58.156 1.00 59.43  ? 705  ASP   A OD1  1 
ATOM   10296 O OD2  . ASP   A  1 679 ? 36.329 40.654  -57.741 1.00 61.05  ? 705  ASP   A OD2  1 
ATOM   10297 H H    . ASP   A  1 679 ? 36.252 36.938  -56.610 0.00 66.51  ? 705  ASP   A H    1 
ATOM   10298 H HA   . ASP   A  1 679 ? 34.310 38.052  -54.695 0.00 68.26  ? 705  ASP   A HA   1 
ATOM   10299 H HB2  . ASP   A  1 679 ? 34.849 40.156  -55.715 0.00 72.89  ? 705  ASP   A HB2  1 
ATOM   10300 H HB3  . ASP   A  1 679 ? 36.352 39.293  -55.327 0.00 71.98  ? 705  ASP   A HB3  1 
ATOM   10301 N N    . SER   A  1 680 ? 33.172 36.802  -57.307 1.00 49.31  ? 706  SER   A N    1 
ATOM   10302 C CA   . SER   A  1 680 ? 32.070 36.661  -58.261 1.00 49.29  ? 706  SER   A CA   1 
ATOM   10303 C C    . SER   A  1 680 ? 31.542 35.216  -58.250 1.00 48.53  ? 706  SER   A C    1 
ATOM   10304 O O    . SER   A  1 680 ? 31.404 34.593  -59.305 1.00 48.66  ? 706  SER   A O    1 
ATOM   10305 C CB   . SER   A  1 680 ? 32.550 37.043  -59.664 1.00 51.00  ? 706  SER   A CB   1 
ATOM   10306 O OG   . SER   A  1 680 ? 33.138 38.333  -59.701 1.00 53.46  ? 706  SER   A OG   1 
ATOM   10307 H H    . SER   A  1 680 ? 33.673 35.931  -57.168 0.00 67.03  ? 706  SER   A H    1 
ATOM   10308 H HA   . SER   A  1 680 ? 31.243 37.316  -57.987 0.00 68.59  ? 706  SER   A HA   1 
ATOM   10309 H HB2  . SER   A  1 680 ? 33.292 36.318  -59.995 0.00 70.10  ? 706  SER   A HB2  1 
ATOM   10310 H HB3  . SER   A  1 680 ? 31.698 37.034  -60.342 0.00 71.02  ? 706  SER   A HB3  1 
ATOM   10311 H HG   . SER   A  1 680 ? 34.090 38.281  -59.427 0.00 73.90  ? 706  SER   A HG   1 
ATOM   10312 N N    . LEU   A  1 681 ? 31.232 34.690  -57.051 1.00 47.56  ? 707  LEU   A N    1 
ATOM   10313 C CA   . LEU   A  1 681 ? 30.733 33.325  -56.904 1.00 47.43  ? 707  LEU   A CA   1 
ATOM   10314 C C    . LEU   A  1 681 ? 29.371 33.116  -57.587 1.00 47.14  ? 707  LEU   A C    1 
ATOM   10315 O O    . LEU   A  1 681 ? 29.127 32.023  -58.080 1.00 46.83  ? 707  LEU   A O    1 
ATOM   10316 C CB   . LEU   A  1 681 ? 30.663 32.943  -55.411 1.00 47.67  ? 707  LEU   A CB   1 
ATOM   10317 C CG   . LEU   A  1 681 ? 30.394 31.470  -55.060 1.00 49.32  ? 707  LEU   A CG   1 
ATOM   10318 C CD1  . LEU   A  1 681 ? 31.394 30.533  -55.737 1.00 49.84  ? 707  LEU   A CD1  1 
ATOM   10319 C CD2  . LEU   A  1 681 ? 30.473 31.249  -53.560 1.00 50.12  ? 707  LEU   A CD2  1 
ATOM   10320 H H    . LEU   A  1 681 ? 31.312 35.192  -56.172 0.00 64.75  ? 707  LEU   A H    1 
ATOM   10321 H HA   . LEU   A  1 681 ? 31.449 32.668  -57.397 0.00 63.47  ? 707  LEU   A HA   1 
ATOM   10322 H HB2  . LEU   A  1 681 ? 31.615 33.202  -54.950 0.00 63.41  ? 707  LEU   A HB2  1 
ATOM   10323 H HB3  . LEU   A  1 681 ? 29.868 33.531  -54.952 0.00 64.02  ? 707  LEU   A HB3  1 
ATOM   10324 H HG   . LEU   A  1 681 ? 29.392 31.198  -55.386 0.00 64.98  ? 707  LEU   A HG   1 
ATOM   10325 H HD11 . LEU   A  1 681 ? 31.327 29.551  -55.269 0.00 64.26  ? 707  LEU   A HD11 1 
ATOM   10326 H HD12 . LEU   A  1 681 ? 31.148 30.450  -56.794 0.00 65.13  ? 707  LEU   A HD12 1 
ATOM   10327 H HD13 . LEU   A  1 681 ? 32.399 30.934  -55.618 0.00 64.80  ? 707  LEU   A HD13 1 
ATOM   10328 H HD21 . LEU   A  1 681 ? 29.755 30.482  -53.273 0.00 64.97  ? 707  LEU   A HD21 1 
ATOM   10329 H HD22 . LEU   A  1 681 ? 31.480 30.915  -53.312 0.00 64.80  ? 707  LEU   A HD22 1 
ATOM   10330 H HD23 . LEU   A  1 681 ? 30.256 32.180  -53.040 0.00 65.69  ? 707  LEU   A HD23 1 
ATOM   10331 N N    . SER   A  1 682 ? 28.514 34.156  -57.679 1.00 47.00  ? 708  SER   A N    1 
ATOM   10332 C CA   . SER   A  1 682 ? 27.218 34.045  -58.360 1.00 47.17  ? 708  SER   A CA   1 
ATOM   10333 C C    . SER   A  1 682 ? 27.381 33.790  -59.869 1.00 46.98  ? 708  SER   A C    1 
ATOM   10334 O O    . SER   A  1 682 ? 26.507 33.177  -60.475 1.00 46.86  ? 708  SER   A O    1 
ATOM   10335 C CB   . SER   A  1 682 ? 26.382 35.304  -58.136 1.00 48.56  ? 708  SER   A CB   1 
ATOM   10336 O OG   . SER   A  1 682 ? 26.948 36.433  -58.781 1.00 50.77  ? 708  SER   A OG   1 
ATOM   10337 H H    . SER   A  1 682 ? 28.680 35.078  -57.288 0.00 65.00  ? 708  SER   A H    1 
ATOM   10338 H HA   . SER   A  1 682 ? 26.671 33.203  -57.939 0.00 64.94  ? 708  SER   A HA   1 
ATOM   10339 H HB2  . SER   A  1 682 ? 25.382 35.137  -58.533 0.00 68.32  ? 708  SER   A HB2  1 
ATOM   10340 H HB3  . SER   A  1 682 ? 26.327 35.501  -57.067 0.00 67.80  ? 708  SER   A HB3  1 
ATOM   10341 H HG   . SER   A  1 682 ? 26.387 37.235  -58.615 0.00 71.92  ? 708  SER   A HG   1 
ATOM   10342 N N    . ASP   A  1 683 ? 28.493 34.239  -60.471 1.00 46.91  ? 709  ASP   A N    1 
ATOM   10343 C CA   . ASP   A  1 683 ? 28.759 33.966  -61.884 1.00 47.84  ? 709  ASP   A CA   1 
ATOM   10344 C C    . ASP   A  1 683 ? 29.133 32.493  -62.118 1.00 47.75  ? 709  ASP   A C    1 
ATOM   10345 O O    . ASP   A  1 683 ? 28.996 32.012  -63.242 1.00 48.08  ? 709  ASP   A O    1 
ATOM   10346 C CB   . ASP   A  1 683 ? 29.913 34.842  -62.398 1.00 50.45  ? 709  ASP   A CB   1 
ATOM   10347 C CG   . ASP   A  1 683 ? 29.617 36.327  -62.442 1.00 56.40  ? 709  ASP   A CG   1 
ATOM   10348 O OD1  . ASP   A  1 683 ? 28.421 36.698  -62.376 1.00 57.42  ? 709  ASP   A OD1  1 
ATOM   10349 O OD2  . ASP   A  1 683 ? 30.579 37.119  -62.551 1.00 59.07  ? 709  ASP   A OD2  1 
ATOM   10350 H H    . ASP   A  1 683 ? 29.220 34.785  -60.020 0.00 65.38  ? 709  ASP   A H    1 
ATOM   10351 H HA   . ASP   A  1 683 ? 27.871 34.181  -62.475 0.00 67.35  ? 709  ASP   A HA   1 
ATOM   10352 H HB2  . ASP   A  1 683 ? 30.783 34.694  -61.759 0.00 69.69  ? 709  ASP   A HB2  1 
ATOM   10353 H HB3  . ASP   A  1 683 ? 30.153 34.531  -63.414 0.00 70.34  ? 709  ASP   A HB3  1 
ATOM   10354 N N    . PHE   A  1 684 ? 29.642 31.795  -61.084 1.00 46.92  ? 710  PHE   A N    1 
ATOM   10355 C CA   . PHE   A  1 684 ? 30.088 30.417  -61.207 1.00 46.53  ? 710  PHE   A CA   1 
ATOM   10356 C C    . PHE   A  1 684 ? 29.104 29.397  -60.644 1.00 45.97  ? 710  PHE   A C    1 
ATOM   10357 O O    . PHE   A  1 684 ? 29.215 28.224  -60.994 1.00 46.24  ? 710  PHE   A O    1 
ATOM   10358 C CB   . PHE   A  1 684 ? 31.478 30.248  -60.573 1.00 46.19  ? 710  PHE   A CB   1 
ATOM   10359 C CG   . PHE   A  1 684 ? 32.471 31.322  -60.965 1.00 46.67  ? 710  PHE   A CG   1 
ATOM   10360 C CD1  . PHE   A  1 684 ? 32.576 31.750  -62.280 1.00 47.19  ? 710  PHE   A CD1  1 
ATOM   10361 C CD2  . PHE   A  1 684 ? 33.313 31.886  -60.025 1.00 47.48  ? 710  PHE   A CD2  1 
ATOM   10362 C CE1  . PHE   A  1 684 ? 33.488 32.734  -62.636 1.00 47.86  ? 710  PHE   A CE1  1 
ATOM   10363 C CE2  . PHE   A  1 684 ? 34.215 32.877  -60.384 1.00 48.04  ? 710  PHE   A CE2  1 
ATOM   10364 C CZ   . PHE   A  1 684 ? 34.296 33.297  -61.686 1.00 47.82  ? 710  PHE   A CZ   1 
ATOM   10365 H H    . PHE   A  1 684 ? 29.767 32.158  -60.144 0.00 63.83  ? 710  PHE   A H    1 
ATOM   10366 H HA   . PHE   A  1 684 ? 30.208 30.189  -62.263 0.00 62.94  ? 710  PHE   A HA   1 
ATOM   10367 H HB2  . PHE   A  1 684 ? 31.368 30.267  -59.490 0.00 61.40  ? 710  PHE   A HB2  1 
ATOM   10368 H HB3  . PHE   A  1 684 ? 31.890 29.289  -60.885 0.00 61.22  ? 710  PHE   A HB3  1 
ATOM   10369 H HD1  . PHE   A  1 684 ? 31.948 31.320  -63.040 0.00 64.13  ? 710  PHE   A HD1  1 
ATOM   10370 H HD2  . PHE   A  1 684 ? 33.249 31.576  -58.995 0.00 63.03  ? 710  PHE   A HD2  1 
ATOM   10371 H HE1  . PHE   A  1 684 ? 33.554 33.062  -63.659 0.00 65.66  ? 710  PHE   A HE1  1 
ATOM   10372 H HE2  . PHE   A  1 684 ? 34.852 33.318  -59.638 0.00 64.47  ? 710  PHE   A HE2  1 
ATOM   10373 H HZ   . PHE   A  1 684 ? 35.004 34.057  -61.963 0.00 65.27  ? 710  PHE   A HZ   1 
ATOM   10374 N N    . THR   A  1 685 ? 28.160 29.804  -59.776 1.00 45.28  ? 711  THR   A N    1 
ATOM   10375 C CA   . THR   A  1 685 ? 27.189 28.859  -59.221 1.00 45.54  ? 711  THR   A CA   1 
ATOM   10376 C C    . THR   A  1 685 ? 25.891 29.534  -58.800 1.00 45.99  ? 711  THR   A C    1 
ATOM   10377 O O    . THR   A  1 685 ? 25.906 30.648  -58.284 1.00 46.50  ? 711  THR   A O    1 
ATOM   10378 C CB   . THR   A  1 685 ? 27.794 28.047  -58.047 1.00 46.28  ? 711  THR   A CB   1 
ATOM   10379 O OG1  . THR   A  1 685 ? 26.865 27.038  -57.654 1.00 47.17  ? 711  THR   A OG1  1 
ATOM   10380 C CG2  . THR   A  1 685 ? 28.155 28.906  -56.840 1.00 46.33  ? 711  THR   A CG2  1 
ATOM   10381 H H    . THR   A  1 685 ? 28.043 30.751  -59.430 0.00 61.41  ? 711  THR   A H    1 
ATOM   10382 H HA   . THR   A  1 685 ? 26.930 28.147  -60.003 0.00 60.97  ? 711  THR   A HA   1 
ATOM   10383 H HB   . THR   A  1 685 ? 28.707 27.564  -58.393 0.00 60.58  ? 711  THR   A HB   1 
ATOM   10384 H HG1  . THR   A  1 685 ? 27.332 26.333  -57.133 0.00 61.12  ? 711  THR   A HG1  1 
ATOM   10385 H HG21 . THR   A  1 685 ? 28.734 28.315  -56.132 0.00 60.33  ? 711  THR   A HG21 1 
ATOM   10386 H HG22 . THR   A  1 685 ? 28.746 29.766  -57.150 0.00 61.30  ? 711  THR   A HG22 1 
ATOM   10387 H HG23 . THR   A  1 685 ? 27.253 29.253  -56.336 0.00 61.24  ? 711  THR   A HG23 1 
ATOM   10388 N N    . SER   A  1 686 ? 24.770 28.842  -59.022 1.00 45.53  ? 712  SER   A N    1 
ATOM   10389 C CA   . SER   A  1 686 ? 23.433 29.263  -58.601 1.00 45.39  ? 712  SER   A CA   1 
ATOM   10390 C C    . SER   A  1 686 ? 22.702 28.142  -57.816 1.00 44.32  ? 712  SER   A C    1 
ATOM   10391 O O    . SER   A  1 686 ? 21.545 28.332  -57.452 1.00 44.78  ? 712  SER   A O    1 
ATOM   10392 C CB   . SER   A  1 686 ? 22.602 29.669  -59.813 1.00 47.79  ? 712  SER   A CB   1 
ATOM   10393 O OG   . SER   A  1 686 ? 22.332 28.546  -60.635 1.00 51.26  ? 712  SER   A OG   1 
ATOM   10394 H H    . SER   A  1 686 ? 24.754 27.967  -59.535 0.00 61.41  ? 712  SER   A H    1 
ATOM   10395 H HA   . SER   A  1 686 ? 23.495 30.127  -57.942 0.00 62.24  ? 712  SER   A HA   1 
ATOM   10396 H HB2  . SER   A  1 686 ? 21.659 30.096  -59.473 0.00 66.29  ? 712  SER   A HB2  1 
ATOM   10397 H HB3  . SER   A  1 686 ? 23.158 30.405  -60.391 0.00 66.17  ? 712  SER   A HB3  1 
ATOM   10398 H HG   . SER   A  1 686 ? 21.800 28.824  -61.427 0.00 70.45  ? 712  SER   A HG   1 
ATOM   10399 N N    . SER   A  1 687 ? 23.376 27.001  -57.523 1.00 42.58  ? 713  SER   A N    1 
ATOM   10400 C CA   . SER   A  1 687 ? 22.805 25.875  -56.794 1.00 41.24  ? 713  SER   A CA   1 
ATOM   10401 C C    . SER   A  1 687 ? 23.439 25.679  -55.411 1.00 39.15  ? 713  SER   A C    1 
ATOM   10402 O O    . SER   A  1 687 ? 22.831 25.037  -54.556 1.00 38.63  ? 713  SER   A O    1 
ATOM   10403 C CB   . SER   A  1 687 ? 22.983 24.596  -57.607 1.00 43.01  ? 713  SER   A CB   1 
ATOM   10404 O OG   . SER   A  1 687 ? 24.330 24.424  -58.022 1.00 45.40  ? 713  SER   A OG   1 
ATOM   10405 H H    . SER   A  1 687 ? 24.337 26.820  -57.796 0.00 56.97  ? 713  SER   A H    1 
ATOM   10406 H HA   . SER   A  1 687 ? 21.736 26.017  -56.649 0.00 55.60  ? 713  SER   A HA   1 
ATOM   10407 H HB2  . SER   A  1 687 ? 22.689 23.747  -56.992 0.00 56.55  ? 713  SER   A HB2  1 
ATOM   10408 H HB3  . SER   A  1 687 ? 22.349 24.649  -58.491 0.00 57.50  ? 713  SER   A HB3  1 
ATOM   10409 H HG   . SER   A  1 687 ? 24.849 23.949  -57.321 0.00 58.83  ? 713  SER   A HG   1 
ATOM   10410 N N    . LEU   A  1 688 ? 24.668 26.181  -55.198 1.00 37.66  ? 714  LEU   A N    1 
ATOM   10411 C CA   . LEU   A  1 688 ? 25.373 25.983  -53.933 1.00 36.96  ? 714  LEU   A CA   1 
ATOM   10412 C C    . LEU   A  1 688 ? 24.577 26.528  -52.745 1.00 35.03  ? 714  LEU   A C    1 
ATOM   10413 O O    . LEU   A  1 688 ? 24.225 27.699  -52.741 1.00 35.12  ? 714  LEU   A O    1 
ATOM   10414 C CB   . LEU   A  1 688 ? 26.763 26.646  -54.010 1.00 37.74  ? 714  LEU   A CB   1 
ATOM   10415 C CG   . LEU   A  1 688 ? 27.770 26.238  -52.953 1.00 39.49  ? 714  LEU   A CG   1 
ATOM   10416 C CD1  . LEU   A  1 688 ? 28.107 24.752  -53.058 1.00 39.93  ? 714  LEU   A CD1  1 
ATOM   10417 C CD2  . LEU   A  1 688 ? 29.032 27.057  -53.085 1.00 40.25  ? 714  LEU   A CD2  1 
ATOM   10418 H H    . LEU   A  1 688 ? 25.188 26.724  -55.879 0.00 50.18  ? 714  LEU   A H    1 
ATOM   10419 H HA   . LEU   A  1 688 ? 25.497 24.910  -53.802 0.00 47.92  ? 714  LEU   A HA   1 
ATOM   10420 H HB2  . LEU   A  1 688 ? 27.213 26.410  -54.973 0.00 49.28  ? 714  LEU   A HB2  1 
ATOM   10421 H HB3  . LEU   A  1 688 ? 26.628 27.724  -53.934 0.00 49.78  ? 714  LEU   A HB3  1 
ATOM   10422 H HG   . LEU   A  1 688 ? 27.353 26.418  -51.964 0.00 50.61  ? 714  LEU   A HG   1 
ATOM   10423 H HD11 . LEU   A  1 688 ? 29.034 24.567  -52.517 0.00 50.05  ? 714  LEU   A HD11 1 
ATOM   10424 H HD12 . LEU   A  1 688 ? 27.310 24.167  -52.601 0.00 50.36  ? 714  LEU   A HD12 1 
ATOM   10425 H HD13 . LEU   A  1 688 ? 28.224 24.478  -54.105 0.00 50.60  ? 714  LEU   A HD13 1 
ATOM   10426 H HD21 . LEU   A  1 688 ? 29.688 26.820  -52.249 0.00 51.17  ? 714  LEU   A HD21 1 
ATOM   10427 H HD22 . LEU   A  1 688 ? 29.522 26.806  -54.024 0.00 51.62  ? 714  LEU   A HD22 1 
ATOM   10428 H HD23 . LEU   A  1 688 ? 28.777 28.115  -53.065 0.00 52.17  ? 714  LEU   A HD23 1 
ATOM   10429 N N    . ARG   A  1 689 ? 24.238 25.656  -51.789 1.00 33.41  ? 715  ARG   A N    1 
ATOM   10430 C CA   . ARG   A  1 689 ? 23.471 25.978  -50.586 1.00 32.49  ? 715  ARG   A CA   1 
ATOM   10431 C C    . ARG   A  1 689 ? 24.358 25.977  -49.345 1.00 30.25  ? 715  ARG   A C    1 
ATOM   10432 O O    . ARG   A  1 689 ? 24.084 26.731  -48.426 1.00 30.16  ? 715  ARG   A O    1 
ATOM   10433 C CB   . ARG   A  1 689 ? 22.347 24.958  -50.371 1.00 34.98  ? 715  ARG   A CB   1 
ATOM   10434 C CG   . ARG   A  1 689 ? 21.260 24.967  -51.441 1.00 40.04  ? 715  ARG   A CG   1 
ATOM   10435 C CD   . ARG   A  1 689 ? 20.250 23.876  -51.131 1.00 46.24  ? 715  ARG   A CD   1 
ATOM   10436 N NE   . ARG   A  1 689 ? 19.145 23.831  -52.090 1.00 52.85  ? 715  ARG   A NE   1 
ATOM   10437 C CZ   . ARG   A  1 689 ? 18.133 22.965  -52.035 1.00 56.79  ? 715  ARG   A CZ   1 
ATOM   10438 N NH1  . ARG   A  1 689 ? 18.079 22.052  -51.066 1.00 56.81  ? 715  ARG   A NH1  1 
ATOM   10439 N NH2  . ARG   A  1 689 ? 17.171 22.999  -52.950 1.00 56.99  ? 715  ARG   A NH2  1 
ATOM   10440 H H    . ARG   A  1 689 ? 24.490 24.674  -51.820 0.00 43.40  ? 715  ARG   A H    1 
ATOM   10441 H HA   . ARG   A  1 689 ? 22.998 26.953  -50.682 0.00 43.52  ? 715  ARG   A HA   1 
ATOM   10442 H HB2  . ARG   A  1 689 ? 22.779 23.960  -50.343 0.00 45.21  ? 715  ARG   A HB2  1 
ATOM   10443 H HB3  . ARG   A  1 689 ? 21.868 25.165  -49.415 0.00 45.83  ? 715  ARG   A HB3  1 
ATOM   10444 H HG2  . ARG   A  1 689 ? 20.745 25.926  -51.435 0.00 53.10  ? 715  ARG   A HG2  1 
ATOM   10445 H HG3  . ARG   A  1 689 ? 21.702 24.775  -52.417 0.00 52.47  ? 715  ARG   A HG3  1 
ATOM   10446 H HD2  . ARG   A  1 689 ? 20.756 22.912  -51.152 0.00 59.20  ? 715  ARG   A HD2  1 
ATOM   10447 H HD3  . ARG   A  1 689 ? 19.829 24.047  -50.142 0.00 59.80  ? 715  ARG   A HD3  1 
ATOM   10448 H HE   . ARG   A  1 689 ? 19.154 24.511  -52.844 0.00 68.82  ? 715  ARG   A HE   1 
ATOM   10449 H HH11 . ARG   A  1 689 ? 18.791 21.994  -50.346 0.00 72.10  ? 715  ARG   A HH11 1 
ATOM   10450 H HH12 . ARG   A  1 689 ? 17.302 21.400  -51.036 0.00 72.65  ? 715  ARG   A HH12 1 
ATOM   10451 H HH21 . ARG   A  1 689 ? 17.197 23.688  -53.696 0.00 74.49  ? 715  ARG   A HH21 1 
ATOM   10452 H HH22 . ARG   A  1 689 ? 16.401 22.339  -52.910 0.00 74.09  ? 715  ARG   A HH22 1 
ATOM   10453 N N    . THR   A  1 690 ? 25.360 25.084  -49.275 1.00 28.66  ? 716  THR   A N    1 
ATOM   10454 C CA   . THR   A  1 690 ? 26.254 24.982  -48.123 1.00 27.67  ? 716  THR   A CA   1 
ATOM   10455 C C    . THR   A  1 690 ? 27.717 25.115  -48.605 1.00 26.79  ? 716  THR   A C    1 
ATOM   10456 O O    . THR   A  1 690 ? 28.116 24.434  -49.550 1.00 26.55  ? 716  THR   A O    1 
ATOM   10457 C CB   . THR   A  1 690 ? 26.027 23.643  -47.390 1.00 29.40  ? 716  THR   A CB   1 
ATOM   10458 O OG1  . THR   A  1 690 ? 24.669 23.542  -46.926 1.00 30.79  ? 716  THR   A OG1  1 
ATOM   10459 C CG2  . THR   A  1 690 ? 26.973 23.451  -46.219 1.00 29.59  ? 716  THR   A CG2  1 
ATOM   10460 H H    . THR   A  1 690 ? 25.572 24.402  -49.996 0.00 36.86  ? 716  THR   A H    1 
ATOM   10461 H HA   . THR   A  1 690 ? 26.059 25.784  -47.412 0.00 35.63  ? 716  THR   A HA   1 
ATOM   10462 H HB   . THR   A  1 690 ? 26.201 22.835  -48.098 0.00 36.58  ? 716  THR   A HB   1 
ATOM   10463 H HG1  . THR   A  1 690 ? 24.515 24.130  -46.141 0.00 38.90  ? 716  THR   A HG1  1 
ATOM   10464 H HG21 . THR   A  1 690 ? 26.596 22.668  -45.563 0.00 36.21  ? 716  THR   A HG21 1 
ATOM   10465 H HG22 . THR   A  1 690 ? 27.958 23.155  -46.575 0.00 36.21  ? 716  THR   A HG22 1 
ATOM   10466 H HG23 . THR   A  1 690 ? 27.062 24.378  -45.654 0.00 36.78  ? 716  THR   A HG23 1 
ATOM   10467 N N    . LEU   A  1 691 ? 28.498 26.015  -47.966 1.00 25.41  ? 717  LEU   A N    1 
ATOM   10468 C CA   . LEU   A  1 691 ? 29.898 26.224  -48.300 1.00 24.66  ? 717  LEU   A CA   1 
ATOM   10469 C C    . LEU   A  1 691 ? 30.690 26.173  -46.998 1.00 24.06  ? 717  LEU   A C    1 
ATOM   10470 O O    . LEU   A  1 691 ? 30.558 27.070  -46.173 1.00 23.90  ? 717  LEU   A O    1 
ATOM   10471 C CB   . LEU   A  1 691 ? 30.105 27.568  -49.029 1.00 24.54  ? 717  LEU   A CB   1 
ATOM   10472 C CG   . LEU   A  1 691 ? 31.559 27.942  -49.401 1.00 25.17  ? 717  LEU   A CG   1 
ATOM   10473 C CD1  . LEU   A  1 691 ? 32.245 26.835  -50.205 1.00 24.94  ? 717  LEU   A CD1  1 
ATOM   10474 C CD2  . LEU   A  1 691 ? 31.605 29.267  -50.168 1.00 26.14  ? 717  LEU   A CD2  1 
ATOM   10475 H H    . LEU   A  1 691 ? 28.177 26.622  -47.219 0.00 32.69  ? 717  LEU   A H    1 
ATOM   10476 H HA   . LEU   A  1 691 ? 30.255 25.425  -48.946 0.00 31.08  ? 717  LEU   A HA   1 
ATOM   10477 H HB2  . LEU   A  1 691 ? 29.532 27.546  -49.955 0.00 32.20  ? 717  LEU   A HB2  1 
ATOM   10478 H HB3  . LEU   A  1 691 ? 29.721 28.362  -48.391 0.00 32.27  ? 717  LEU   A HB3  1 
ATOM   10479 H HG   . LEU   A  1 691 ? 32.133 28.084  -48.487 0.00 32.40  ? 717  LEU   A HG   1 
ATOM   10480 H HD11 . LEU   A  1 691 ? 33.187 27.215  -50.597 0.00 31.91  ? 717  LEU   A HD11 1 
ATOM   10481 H HD12 . LEU   A  1 691 ? 32.443 25.991  -49.546 0.00 31.33  ? 717  LEU   A HD12 1 
ATOM   10482 H HD13 . LEU   A  1 691 ? 31.601 26.523  -51.025 0.00 32.01  ? 717  LEU   A HD13 1 
ATOM   10483 H HD21 . LEU   A  1 691 ? 32.645 29.519  -50.375 0.00 34.47  ? 717  LEU   A HD21 1 
ATOM   10484 H HD22 . LEU   A  1 691 ? 31.058 29.156  -51.103 0.00 34.76  ? 717  LEU   A HD22 1 
ATOM   10485 H HD23 . LEU   A  1 691 ? 31.147 30.043  -49.558 0.00 34.89  ? 717  LEU   A HD23 1 
ATOM   10486 N N    . LEU   A  1 692 ? 31.453 25.096  -46.786 1.00 23.41  ? 718  LEU   A N    1 
ATOM   10487 C CA   . LEU   A  1 692 ? 32.223 24.945  -45.559 1.00 23.15  ? 718  LEU   A CA   1 
ATOM   10488 C C    . LEU   A  1 692 ? 33.690 25.301  -45.799 1.00 22.71  ? 718  LEU   A C    1 
ATOM   10489 O O    . LEU   A  1 692 ? 34.364 24.650  -46.598 1.00 22.39  ? 718  LEU   A O    1 
ATOM   10490 C CB   . LEU   A  1 692 ? 32.064 23.550  -44.943 1.00 23.47  ? 718  LEU   A CB   1 
ATOM   10491 C CG   . LEU   A  1 692 ? 30.627 22.984  -44.855 1.00 25.43  ? 718  LEU   A CG   1 
ATOM   10492 C CD1  . LEU   A  1 692 ? 30.644 21.555  -44.346 1.00 26.39  ? 718  LEU   A CD1  1 
ATOM   10493 C CD2  . LEU   A  1 692 ? 29.754 23.829  -43.913 1.00 25.77  ? 718  LEU   A CD2  1 
ATOM   10494 H H    . LEU   A  1 692 ? 31.553 24.320  -47.432 0.00 28.61  ? 718  LEU   A H    1 
ATOM   10495 H HA   . LEU   A  1 692 ? 31.841 25.644  -44.822 0.00 28.43  ? 718  LEU   A HA   1 
ATOM   10496 H HB2  . LEU   A  1 692 ? 32.687 22.839  -45.481 0.00 27.63  ? 718  LEU   A HB2  1 
ATOM   10497 H HB3  . LEU   A  1 692 ? 32.426 23.617  -43.918 0.00 27.78  ? 718  LEU   A HB3  1 
ATOM   10498 H HG   . LEU   A  1 692 ? 30.166 22.982  -45.842 0.00 30.56  ? 718  LEU   A HG   1 
ATOM   10499 H HD11 . LEU   A  1 692 ? 29.664 21.109  -44.509 0.00 30.94  ? 718  LEU   A HD11 1 
ATOM   10500 H HD12 . LEU   A  1 692 ? 31.408 20.987  -44.872 0.00 30.61  ? 718  LEU   A HD12 1 
ATOM   10501 H HD13 . LEU   A  1 692 ? 30.870 21.566  -43.280 0.00 30.71  ? 718  LEU   A HD13 1 
ATOM   10502 H HD21 . LEU   A  1 692 ? 28.780 23.350  -43.819 0.00 31.12  ? 718  LEU   A HD21 1 
ATOM   10503 H HD22 . LEU   A  1 692 ? 30.238 23.892  -42.939 0.00 30.95  ? 718  LEU   A HD22 1 
ATOM   10504 H HD23 . LEU   A  1 692 ? 29.641 24.825  -44.336 0.00 31.60  ? 718  LEU   A HD23 1 
ATOM   10505 N N    . LEU   A  1 693 ? 34.168 26.368  -45.134 1.00 22.15  ? 719  LEU   A N    1 
ATOM   10506 C CA   . LEU   A  1 693 ? 35.529 26.854  -45.297 1.00 22.32  ? 719  LEU   A CA   1 
ATOM   10507 C C    . LEU   A  1 693 ? 36.286 27.005  -43.980 1.00 22.58  ? 719  LEU   A C    1 
ATOM   10508 O O    . LEU   A  1 693 ? 37.340 27.638  -43.984 1.00 22.54  ? 719  LEU   A O    1 
ATOM   10509 C CB   . LEU   A  1 693 ? 35.489 28.209  -46.025 1.00 22.81  ? 719  LEU   A CB   1 
ATOM   10510 C CG   . LEU   A  1 693 ? 35.102 28.181  -47.498 1.00 24.18  ? 719  LEU   A CG   1 
ATOM   10511 C CD1  . LEU   A  1 693 ? 34.624 29.547  -47.930 1.00 25.20  ? 719  LEU   A CD1  1 
ATOM   10512 C CD2  . LEU   A  1 693 ? 36.284 27.776  -48.355 1.00 25.22  ? 719  LEU   A CD2  1 
ATOM   10513 H H    . LEU   A  1 693 ? 33.631 26.916  -44.469 0.00 27.46  ? 719  LEU   A H    1 
ATOM   10514 H HA   . LEU   A  1 693 ? 36.106 26.152  -45.895 0.00 27.16  ? 719  LEU   A HA   1 
ATOM   10515 H HB2  . LEU   A  1 693 ? 34.769 28.847  -45.515 0.00 29.09  ? 719  LEU   A HB2  1 
ATOM   10516 H HB3  . LEU   A  1 693 ? 36.473 28.673  -45.986 0.00 28.85  ? 719  LEU   A HB3  1 
ATOM   10517 H HG   . LEU   A  1 693 ? 34.295 27.469  -47.661 0.00 30.45  ? 719  LEU   A HG   1 
ATOM   10518 H HD11 . LEU   A  1 693 ? 34.680 29.618  -49.016 0.00 32.82  ? 719  LEU   A HD11 1 
ATOM   10519 H HD12 . LEU   A  1 693 ? 33.593 29.679  -47.605 0.00 32.81  ? 719  LEU   A HD12 1 
ATOM   10520 H HD13 . LEU   A  1 693 ? 35.255 30.302  -47.465 0.00 32.85  ? 719  LEU   A HD13 1 
ATOM   10521 H HD21 . LEU   A  1 693 ? 35.926 27.544  -49.356 0.00 31.78  ? 719  LEU   A HD21 1 
ATOM   10522 H HD22 . LEU   A  1 693 ? 36.978 28.613  -48.404 0.00 31.98  ? 719  LEU   A HD22 1 
ATOM   10523 H HD23 . LEU   A  1 693 ? 36.788 26.911  -47.927 0.00 31.17  ? 719  LEU   A HD23 1 
ATOM   10524 N N    . SER   A  1 694 ? 35.796 26.418  -42.867 1.00 22.97  ? 720  SER   A N    1 
ATOM   10525 C CA   . SER   A  1 694 ? 36.483 26.555  -41.593 1.00 23.55  ? 720  SER   A CA   1 
ATOM   10526 C C    . SER   A  1 694 ? 37.887 25.940  -41.621 1.00 23.36  ? 720  SER   A C    1 
ATOM   10527 O O    . SER   A  1 694 ? 38.160 25.028  -42.403 1.00 22.99  ? 720  SER   A O    1 
ATOM   10528 C CB   . SER   A  1 694 ? 35.659 25.976  -40.453 1.00 26.02  ? 720  SER   A CB   1 
ATOM   10529 O OG   . SER   A  1 694 ? 35.483 24.579  -40.575 1.00 30.18  ? 720  SER   A OG   1 
ATOM   10530 H H    . SER   A  1 694 ? 34.944 25.870  -42.812 0.00 27.63  ? 720  SER   A H    1 
ATOM   10531 H HA   . SER   A  1 694 ? 36.600 27.618  -41.390 0.00 28.81  ? 720  SER   A HA   1 
ATOM   10532 H HB2  . SER   A  1 694 ? 36.166 26.183  -39.512 0.00 31.09  ? 720  SER   A HB2  1 
ATOM   10533 H HB3  . SER   A  1 694 ? 34.679 26.452  -40.457 0.00 31.39  ? 720  SER   A HB3  1 
ATOM   10534 H HG   . SER   A  1 694 ? 34.966 24.232  -39.801 0.00 35.39  ? 720  SER   A HG   1 
ATOM   10535 N N    . HIS   A  1 695 ? 38.781 26.475  -40.806 1.00 23.13  ? 721  HIS   A N    1 
ATOM   10536 C CA   . HIS   A  1 695 ? 40.163 26.004  -40.736 1.00 23.43  ? 721  HIS   A CA   1 
ATOM   10537 C C    . HIS   A  1 695 ? 40.876 26.201  -42.065 1.00 23.29  ? 721  HIS   A C    1 
ATOM   10538 O O    . HIS   A  1 695 ? 41.388 25.263  -42.655 1.00 23.44  ? 721  HIS   A O    1 
ATOM   10539 C CB   . HIS   A  1 695 ? 40.266 24.562  -40.198 1.00 24.74  ? 721  HIS   A CB   1 
ATOM   10540 C CG   . HIS   A  1 695 ? 39.991 24.488  -38.733 1.00 27.83  ? 721  HIS   A CG   1 
ATOM   10541 N ND1  . HIS   A  1 695 ? 40.949 24.849  -37.805 1.00 30.06  ? 721  HIS   A ND1  1 
ATOM   10542 C CD2  . HIS   A  1 695 ? 38.856 24.147  -38.079 1.00 28.96  ? 721  HIS   A CD2  1 
ATOM   10543 C CE1  . HIS   A  1 695 ? 40.382 24.688  -36.618 1.00 29.85  ? 721  HIS   A CE1  1 
ATOM   10544 N NE2  . HIS   A  1 695 ? 39.123 24.277  -36.735 1.00 29.77  ? 721  HIS   A NE2  1 
ATOM   10545 H H    . HIS   A  1 695 ? 38.589 27.258  -40.190 0.00 27.93  ? 721  HIS   A H    1 
ATOM   10546 H HA   . HIS   A  1 695 ? 40.684 26.633  -40.015 0.00 27.93  ? 721  HIS   A HA   1 
ATOM   10547 H HB2  . HIS   A  1 695 ? 39.553 23.912  -40.703 0.00 28.45  ? 721  HIS   A HB2  1 
ATOM   10548 H HB3  . HIS   A  1 695 ? 41.279 24.191  -40.346 0.00 28.50  ? 721  HIS   A HB3  1 
ATOM   10549 H HD2  . HIS   A  1 695 ? 37.925 23.837  -38.524 0.00 33.47  ? 721  HIS   A HD2  1 
ATOM   10550 H HE1  . HIS   A  1 695 ? 40.878 24.870  -35.678 0.00 34.84  ? 721  HIS   A HE1  1 
ATOM   10551 H HE2  . HIS   A  1 695 ? 38.476 24.097  -35.974 0.00 34.49  ? 721  HIS   A HE2  1 
ATOM   10552 N N    . ASN   A  1 696 ? 40.901 27.440  -42.521 1.00 22.81  ? 722  ASN   A N    1 
ATOM   10553 C CA   . ASN   A  1 696 ? 41.634 27.853  -43.720 1.00 23.41  ? 722  ASN   A CA   1 
ATOM   10554 C C    . ASN   A  1 696 ? 42.410 29.152  -43.345 1.00 25.49  ? 722  ASN   A C    1 
ATOM   10555 O O    . ASN   A  1 696 ? 42.570 29.427  -42.147 1.00 26.11  ? 722  ASN   A O    1 
ATOM   10556 C CB   . ASN   A  1 696 ? 40.661 27.995  -44.921 1.00 22.51  ? 722  ASN   A CB   1 
ATOM   10557 C CG   . ASN   A  1 696 ? 40.427 26.691  -45.642 1.00 22.80  ? 722  ASN   A CG   1 
ATOM   10558 O OD1  . ASN   A  1 696 ? 41.284 26.228  -46.381 1.00 23.41  ? 722  ASN   A OD1  1 
ATOM   10559 N ND2  . ASN   A  1 696 ? 39.283 26.061  -45.447 1.00 21.93  ? 722  ASN   A ND2  1 
ATOM   10560 H H    . ASN   A  1 696 ? 40.419 28.212  -42.071 0.00 27.99  ? 722  ASN   A H    1 
ATOM   10561 H HA   . ASN   A  1 696 ? 42.396 27.113  -43.963 0.00 28.30  ? 722  ASN   A HA   1 
ATOM   10562 H HB2  . ASN   A  1 696 ? 39.706 28.365  -44.549 0.00 27.92  ? 722  ASN   A HB2  1 
ATOM   10563 H HB3  . ASN   A  1 696 ? 41.057 28.697  -45.652 0.00 28.12  ? 722  ASN   A HB3  1 
ATOM   10564 H HD21 . ASN   A  1 696 ? 39.107 25.181  -45.924 0.00 26.02  ? 722  ASN   A HD21 1 
ATOM   10565 H HD22 . ASN   A  1 696 ? 38.580 26.441  -44.822 0.00 26.46  ? 722  ASN   A HD22 1 
ATOM   10566 N N    . ARG   A  1 697 ? 42.938 29.906  -44.314 1.00 26.30  ? 723  ARG   A N    1 
ATOM   10567 C CA   . ARG   A  1 697 ? 43.697 31.117  -44.020 1.00 27.89  ? 723  ARG   A CA   1 
ATOM   10568 C C    . ARG   A  1 697 ? 43.088 32.320  -44.723 1.00 28.78  ? 723  ARG   A C    1 
ATOM   10569 O O    . ARG   A  1 697 ? 43.817 33.162  -45.236 1.00 28.44  ? 723  ARG   A O    1 
ATOM   10570 C CB   . ARG   A  1 697 ? 45.167 30.907  -44.416 1.00 29.78  ? 723  ARG   A CB   1 
ATOM   10571 C CG   . ARG   A  1 697 ? 45.777 29.693  -43.723 1.00 32.89  ? 723  ARG   A CG   1 
ATOM   10572 C CD   . ARG   A  1 697 ? 47.191 29.435  -44.156 1.00 37.38  ? 723  ARG   A CD   1 
ATOM   10573 N NE   . ARG   A  1 697 ? 47.734 28.272  -43.460 1.00 41.74  ? 723  ARG   A NE   1 
ATOM   10574 C CZ   . ARG   A  1 697 ? 48.956 27.783  -43.640 1.00 45.42  ? 723  ARG   A CZ   1 
ATOM   10575 N NH1  . ARG   A  1 697 ? 49.785 28.346  -44.517 1.00 45.23  ? 723  ARG   A NH1  1 
ATOM   10576 N NH2  . ARG   A  1 697 ? 49.360 26.721  -42.950 1.00 46.30  ? 723  ARG   A NH2  1 
ATOM   10577 H H    . ARG   A  1 697 ? 42.893 29.697  -45.305 0.00 33.06  ? 723  ARG   A H    1 
ATOM   10578 H HA   . ARG   A  1 697 ? 43.681 31.335  -42.953 0.00 35.59  ? 723  ARG   A HA   1 
ATOM   10579 H HB2  . ARG   A  1 697 ? 45.232 30.751  -45.491 0.00 37.78  ? 723  ARG   A HB2  1 
ATOM   10580 H HB3  . ARG   A  1 697 ? 45.751 31.779  -44.125 0.00 38.21  ? 723  ARG   A HB3  1 
ATOM   10581 H HG2  . ARG   A  1 697 ? 45.779 29.862  -42.648 0.00 40.91  ? 723  ARG   A HG2  1 
ATOM   10582 H HG3  . ARG   A  1 697 ? 45.202 28.798  -43.959 0.00 40.47  ? 723  ARG   A HG3  1 
ATOM   10583 H HD2  . ARG   A  1 697 ? 47.212 29.234  -45.226 0.00 46.24  ? 723  ARG   A HD2  1 
ATOM   10584 H HD3  . ARG   A  1 697 ? 47.807 30.300  -43.916 0.00 46.70  ? 723  ARG   A HD3  1 
ATOM   10585 H HE   . ARG   A  1 697 ? 47.133 27.818  -42.780 0.00 50.69  ? 723  ARG   A HE   1 
ATOM   10586 H HH11 . ARG   A  1 697 ? 49.515 29.157  -45.062 0.00 55.78  ? 723  ARG   A HH11 1 
ATOM   10587 H HH12 . ARG   A  1 697 ? 50.715 27.960  -44.647 0.00 55.35  ? 723  ARG   A HH12 1 
ATOM   10588 H HH21 . ARG   A  1 697 ? 48.740 26.280  -42.278 0.00 55.62  ? 723  ARG   A HH21 1 
ATOM   10589 H HH22 . ARG   A  1 697 ? 50.293 26.344  -43.088 0.00 55.84  ? 723  ARG   A HH22 1 
ATOM   10590 N N    . ILE   A  1 698 ? 41.746 32.397  -44.768 1.00 29.81  ? 724  ILE   A N    1 
ATOM   10591 C CA   . ILE   A  1 698 ? 41.077 33.524  -45.404 1.00 31.64  ? 724  ILE   A CA   1 
ATOM   10592 C C    . ILE   A  1 698 ? 41.231 34.714  -44.459 1.00 33.43  ? 724  ILE   A C    1 
ATOM   10593 O O    . ILE   A  1 698 ? 40.727 34.654  -43.342 1.00 32.96  ? 724  ILE   A O    1 
ATOM   10594 C CB   . ILE   A  1 698 ? 39.572 33.238  -45.676 1.00 32.53  ? 724  ILE   A CB   1 
ATOM   10595 C CG1  . ILE   A  1 698 ? 39.342 31.926  -46.488 1.00 33.86  ? 724  ILE   A CG1  1 
ATOM   10596 C CG2  . ILE   A  1 698 ? 38.918 34.438  -46.362 1.00 32.93  ? 724  ILE   A CG2  1 
ATOM   10597 C CD1  . ILE   A  1 698 ? 40.115 31.794  -47.740 1.00 35.22  ? 724  ILE   A CD1  1 
ATOM   10598 H H    . ILE   A  1 698 ? 41.113 31.724  -44.348 0.00 38.23  ? 724  ILE   A H    1 
ATOM   10599 H HA   . ILE   A  1 698 ? 41.558 33.759  -46.352 0.00 41.67  ? 724  ILE   A HA   1 
ATOM   10600 H HB   . ILE   A  1 698 ? 39.080 33.107  -44.714 0.00 42.38  ? 724  ILE   A HB   1 
ATOM   10601 H HG12 . ILE   A  1 698 ? 39.610 31.081  -45.855 0.00 42.99  ? 724  ILE   A HG12 1 
ATOM   10602 H HG13 . ILE   A  1 698 ? 38.287 31.856  -46.748 0.00 43.59  ? 724  ILE   A HG13 1 
ATOM   10603 H HG21 . ILE   A  1 698 ? 37.915 34.156  -46.676 0.00 43.74  ? 724  ILE   A HG21 1 
ATOM   10604 H HG22 . ILE   A  1 698 ? 38.842 35.270  -45.663 0.00 44.18  ? 724  ILE   A HG22 1 
ATOM   10605 H HG23 . ILE   A  1 698 ? 39.518 34.729  -47.224 0.00 43.99  ? 724  ILE   A HG23 1 
ATOM   10606 H HD11 . ILE   A  1 698 ? 39.688 30.988  -48.335 0.00 44.86  ? 724  ILE   A HD11 1 
ATOM   10607 H HD12 . ILE   A  1 698 ? 40.082 32.732  -48.293 0.00 45.73  ? 724  ILE   A HD12 1 
ATOM   10608 H HD13 . ILE   A  1 698 ? 41.147 31.552  -47.490 0.00 44.96  ? 724  ILE   A HD13 1 
ATOM   10609 N N    . SER   A  1 699 ? 41.935 35.775  -44.888 1.00 35.13  ? 725  SER   A N    1 
ATOM   10610 C CA   . SER   A  1 699 ? 42.142 36.975  -44.070 1.00 37.46  ? 725  SER   A CA   1 
ATOM   10611 C C    . SER   A  1 699 ? 41.224 38.141  -44.463 1.00 40.58  ? 725  SER   A C    1 
ATOM   10612 O O    . SER   A  1 699 ? 41.209 39.145  -43.758 1.00 41.05  ? 725  SER   A O    1 
ATOM   10613 C CB   . SER   A  1 699 ? 43.593 37.429  -44.166 1.00 38.36  ? 725  SER   A CB   1 
ATOM   10614 O OG   . SER   A  1 699 ? 43.902 37.846  -45.485 1.00 40.95  ? 725  SER   A OG   1 
ATOM   10615 H H    . SER   A  1 699 ? 42.380 35.833  -45.799 0.00 46.95  ? 725  SER   A H    1 
ATOM   10616 H HA   . SER   A  1 699 ? 41.954 36.752  -43.021 0.00 50.11  ? 725  SER   A HA   1 
ATOM   10617 H HB2  . SER   A  1 699 ? 43.750 38.262  -43.482 0.00 52.11  ? 725  SER   A HB2  1 
ATOM   10618 H HB3  . SER   A  1 699 ? 44.243 36.598  -43.897 0.00 51.12  ? 725  SER   A HB3  1 
ATOM   10619 H HG   . SER   A  1 699 ? 44.848 38.145  -45.535 0.00 55.27  ? 725  SER   A HG   1 
ATOM   10620 N N    . HIS   A  1 700 ? 40.467 38.032  -45.566 1.00 42.69  ? 726  HIS   A N    1 
ATOM   10621 C CA   . HIS   A  1 700 ? 39.607 39.119  -46.013 1.00 45.48  ? 726  HIS   A CA   1 
ATOM   10622 C C    . HIS   A  1 700 ? 38.494 38.589  -46.908 1.00 47.21  ? 726  HIS   A C    1 
ATOM   10623 O O    . HIS   A  1 700 ? 38.737 37.707  -47.734 1.00 47.35  ? 726  HIS   A O    1 
ATOM   10624 C CB   . HIS   A  1 700 ? 40.473 40.137  -46.786 1.00 47.43  ? 726  HIS   A CB   1 
ATOM   10625 C CG   . HIS   A  1 700 ? 39.718 41.268  -47.411 1.00 51.51  ? 726  HIS   A CG   1 
ATOM   10626 N ND1  . HIS   A  1 700 ? 39.408 42.417  -46.696 1.00 54.04  ? 726  HIS   A ND1  1 
ATOM   10627 C CD2  . HIS   A  1 700 ? 39.312 41.429  -48.691 1.00 53.16  ? 726  HIS   A CD2  1 
ATOM   10628 C CE1  . HIS   A  1 700 ? 38.789 43.218  -47.549 1.00 54.61  ? 726  HIS   A CE1  1 
ATOM   10629 N NE2  . HIS   A  1 700 ? 38.708 42.666  -48.764 1.00 54.54  ? 726  HIS   A NE2  1 
ATOM   10630 H H    . HIS   A  1 700 ? 40.435 37.219  -46.173 0.00 56.98  ? 726  HIS   A H    1 
ATOM   10631 H HA   . HIS   A  1 700 ? 39.155 39.620  -45.158 0.00 61.86  ? 726  HIS   A HA   1 
ATOM   10632 H HB2  . HIS   A  1 700 ? 41.197 40.570  -46.098 0.00 64.78  ? 726  HIS   A HB2  1 
ATOM   10633 H HB3  . HIS   A  1 700 ? 41.000 39.611  -47.581 0.00 64.29  ? 726  HIS   A HB3  1 
ATOM   10634 H HD2  . HIS   A  1 700 ? 39.441 40.727  -49.497 0.00 72.24  ? 726  HIS   A HD2  1 
ATOM   10635 H HE1  . HIS   A  1 700 ? 38.398 44.189  -47.296 0.00 76.28  ? 726  HIS   A HE1  1 
ATOM   10636 H HE2  . HIS   A  1 700 ? 38.283 43.080  -49.587 0.00 75.67  ? 726  HIS   A HE2  1 
ATOM   10637 N N    . LEU   A  1 701 ? 37.276 39.115  -46.751 1.00 48.44  ? 727  LEU   A N    1 
ATOM   10638 C CA   . LEU   A  1 701 ? 36.152 38.746  -47.605 1.00 50.03  ? 727  LEU   A CA   1 
ATOM   10639 C C    . LEU   A  1 701 ? 36.053 39.808  -48.694 1.00 52.33  ? 727  LEU   A C    1 
ATOM   10640 O O    . LEU   A  1 701 ? 36.044 40.992  -48.361 1.00 52.59  ? 727  LEU   A O    1 
ATOM   10641 C CB   . LEU   A  1 701 ? 34.833 38.683  -46.815 1.00 49.78  ? 727  LEU   A CB   1 
ATOM   10642 C CG   . LEU   A  1 701 ? 34.720 37.596  -45.745 1.00 50.75  ? 727  LEU   A CG   1 
ATOM   10643 C CD1  . LEU   A  1 701 ? 33.336 37.572  -45.152 1.00 51.06  ? 727  LEU   A CD1  1 
ATOM   10644 C CD2  . LEU   A  1 701 ? 35.042 36.201  -46.305 1.00 51.33  ? 727  LEU   A CD2  1 
ATOM   10645 H H    . LEU   A  1 701 ? 37.039 39.803  -46.044 0.00 65.81  ? 727  LEU   A H    1 
ATOM   10646 H HA   . LEU   A  1 701 ? 36.320 37.764  -48.039 0.00 66.74  ? 727  LEU   A HA   1 
ATOM   10647 H HB2  . LEU   A  1 701 ? 34.683 39.641  -46.319 0.00 67.70  ? 727  LEU   A HB2  1 
ATOM   10648 H HB3  . LEU   A  1 701 ? 34.024 38.517  -47.525 0.00 67.19  ? 727  LEU   A HB3  1 
ATOM   10649 H HG   . LEU   A  1 701 ? 35.427 37.810  -44.945 0.00 67.42  ? 727  LEU   A HG   1 
ATOM   10650 H HD11 . LEU   A  1 701 ? 33.353 36.991  -44.232 0.00 67.56  ? 727  LEU   A HD11 1 
ATOM   10651 H HD12 . LEU   A  1 701 ? 33.015 38.592  -44.949 0.00 68.70  ? 727  LEU   A HD12 1 
ATOM   10652 H HD13 . LEU   A  1 701 ? 32.662 37.106  -45.869 0.00 67.88  ? 727  LEU   A HD13 1 
ATOM   10653 H HD21 . LEU   A  1 701 ? 34.726 35.452  -45.582 0.00 66.83  ? 727  LEU   A HD21 1 
ATOM   10654 H HD22 . LEU   A  1 701 ? 34.515 36.062  -47.248 0.00 67.41  ? 727  LEU   A HD22 1 
ATOM   10655 H HD23 . LEU   A  1 701 ? 36.117 36.111  -46.455 0.00 67.12  ? 727  LEU   A HD23 1 
ATOM   10656 N N    . PRO   A  1 702 ? 36.008 39.445  -49.991 1.00 54.10  ? 728  PRO   A N    1 
ATOM   10657 C CA   . PRO   A  1 702 ? 35.914 40.490  -51.034 1.00 55.38  ? 728  PRO   A CA   1 
ATOM   10658 C C    . PRO   A  1 702 ? 34.605 41.287  -50.997 1.00 56.92  ? 728  PRO   A C    1 
ATOM   10659 O O    . PRO   A  1 702 ? 33.644 40.849  -50.369 1.00 56.92  ? 728  PRO   A O    1 
ATOM   10660 C CB   . PRO   A  1 702 ? 36.030 39.715  -52.354 1.00 56.03  ? 728  PRO   A CB   1 
ATOM   10661 C CG   . PRO   A  1 702 ? 36.210 38.300  -52.014 1.00 56.26  ? 728  PRO   A CG   1 
ATOM   10662 C CD   . PRO   A  1 702 ? 36.011 38.084  -50.564 1.00 54.20  ? 728  PRO   A CD   1 
ATOM   10663 H HA   . PRO   A  1 702 ? 36.756 41.176  -50.954 0.00 75.78  ? 728  PRO   A HA   1 
ATOM   10664 H HB2  . PRO   A  1 702 ? 35.114 39.851  -52.927 0.00 76.27  ? 728  PRO   A HB2  1 
ATOM   10665 H HB3  . PRO   A  1 702 ? 36.888 40.082  -52.915 0.00 76.21  ? 728  PRO   A HB3  1 
ATOM   10666 H HG2  . PRO   A  1 702 ? 35.483 37.713  -52.574 0.00 75.04  ? 728  PRO   A HG2  1 
ATOM   10667 H HG3  . PRO   A  1 702 ? 37.219 37.998  -52.291 0.00 74.98  ? 728  PRO   A HG3  1 
ATOM   10668 H HD2  . PRO   A  1 702 ? 35.059 37.589  -50.374 0.00 72.21  ? 728  PRO   A HD2  1 
ATOM   10669 H HD3  . PRO   A  1 702 ? 36.853 37.499  -50.196 0.00 71.83  ? 728  PRO   A HD3  1 
ATOM   10670 N N    . SER   A  1 703 ? 34.524 42.402  -51.737 1.00 58.04  ? 729  SER   A N    1 
ATOM   10671 C CA   . SER   A  1 703 ? 33.304 43.208  -51.776 1.00 59.65  ? 729  SER   A CA   1 
ATOM   10672 C C    . SER   A  1 703 ? 32.155 42.432  -52.430 1.00 61.19  ? 729  SER   A C    1 
ATOM   10673 O O    . SER   A  1 703 ? 32.357 41.776  -53.453 1.00 61.30  ? 729  SER   A O    1 
ATOM   10674 C CB   . SER   A  1 703 ? 33.547 44.502  -52.542 1.00 60.98  ? 729  SER   A CB   1 
ATOM   10675 O OG   . SER   A  1 703 ? 34.605 45.245  -51.960 1.00 63.43  ? 729  SER   A OG   1 
ATOM   10676 H H    . SER   A  1 703 ? 35.276 42.759  -52.318 0.00 80.56  ? 729  SER   A H    1 
ATOM   10677 H HA   . SER   A  1 703 ? 33.021 43.465  -50.756 0.00 83.13  ? 729  SER   A HA   1 
ATOM   10678 H HB2  . SER   A  1 703 ? 33.804 44.256  -53.571 0.00 85.86  ? 729  SER   A HB2  1 
ATOM   10679 H HB3  . SER   A  1 703 ? 32.638 45.102  -52.519 0.00 86.41  ? 729  SER   A HB3  1 
ATOM   10680 H HG   . SER   A  1 703 ? 34.778 46.065  -52.492 0.00 89.50  ? 729  SER   A HG   1 
ATOM   10681 N N    . GLY   A  1 704 ? 30.970 42.515  -51.835 1.00 62.18  ? 730  GLY   A N    1 
ATOM   10682 C CA   . GLY   A  1 704 ? 29.788 41.833  -52.340 1.00 63.67  ? 730  GLY   A CA   1 
ATOM   10683 C C    . GLY   A  1 704 ? 29.945 40.330  -52.363 1.00 65.28  ? 730  GLY   A C    1 
ATOM   10684 O O    . GLY   A  1 704 ? 29.763 39.706  -53.410 1.00 65.69  ? 730  GLY   A O    1 
ATOM   10685 H H    . GLY   A  1 704 ? 30.780 43.074  -51.009 0.00 86.40  ? 730  GLY   A H    1 
ATOM   10686 H HA2  . GLY   A  1 704 ? 28.929 42.073  -51.716 0.00 88.18  ? 730  GLY   A HA2  1 
ATOM   10687 H HA3  . GLY   A  1 704 ? 29.587 42.175  -53.355 0.00 88.34  ? 730  GLY   A HA3  1 
ATOM   10688 N N    . PHE   A  1 705 ? 30.276 39.734  -51.207 1.00 65.86  ? 731  PHE   A N    1 
ATOM   10689 C CA   . PHE   A  1 705 ? 30.469 38.291  -51.125 1.00 66.92  ? 731  PHE   A CA   1 
ATOM   10690 C C    . PHE   A  1 705 ? 29.209 37.590  -50.573 1.00 67.90  ? 731  PHE   A C    1 
ATOM   10691 O O    . PHE   A  1 705 ? 28.676 36.704  -51.239 1.00 68.30  ? 731  PHE   A O    1 
ATOM   10692 C CB   . PHE   A  1 705 ? 31.713 37.941  -50.280 1.00 66.78  ? 731  PHE   A CB   1 
ATOM   10693 C CG   . PHE   A  1 705 ? 31.919 36.452  -50.157 1.00 67.32  ? 731  PHE   A CG   1 
ATOM   10694 C CD1  . PHE   A  1 705 ? 32.428 35.719  -51.214 1.00 68.00  ? 731  PHE   A CD1  1 
ATOM   10695 C CD2  . PHE   A  1 705 ? 31.515 35.773  -49.020 1.00 68.18  ? 731  PHE   A CD2  1 
ATOM   10696 C CE1  . PHE   A  1 705 ? 32.549 34.341  -51.127 1.00 68.76  ? 731  PHE   A CE1  1 
ATOM   10697 C CE2  . PHE   A  1 705 ? 31.650 34.398  -48.930 1.00 68.87  ? 731  PHE   A CE2  1 
ATOM   10698 C CZ   . PHE   A  1 705 ? 32.150 33.689  -49.988 1.00 68.60  ? 731  PHE   A CZ   1 
ATOM   10699 H H    . PHE   A  1 705 ? 30.334 40.221  -50.318 0.00 88.84  ? 731  PHE   A H    1 
ATOM   10700 H HA   . PHE   A  1 705 ? 30.672 37.891  -52.120 0.00 88.87  ? 731  PHE   A HA   1 
ATOM   10701 H HB2  . PHE   A  1 705 ? 32.592 38.356  -50.770 0.00 88.28  ? 731  PHE   A HB2  1 
ATOM   10702 H HB3  . PHE   A  1 705 ? 31.606 38.364  -49.281 0.00 88.27  ? 731  PHE   A HB3  1 
ATOM   10703 H HD1  . PHE   A  1 705 ? 32.720 36.220  -52.126 0.00 88.65  ? 731  PHE   A HD1  1 
ATOM   10704 H HD2  . PHE   A  1 705 ? 31.100 36.318  -48.189 0.00 88.61  ? 731  PHE   A HD2  1 
ATOM   10705 H HE1  . PHE   A  1 705 ? 32.966 33.786  -51.953 0.00 88.07  ? 731  PHE   A HE1  1 
ATOM   10706 H HE2  . PHE   A  1 705 ? 31.346 33.886  -48.031 0.00 87.93  ? 731  PHE   A HE2  1 
ATOM   10707 H HZ   . PHE   A  1 705 ? 32.274 32.625  -49.904 0.00 87.01  ? 731  PHE   A HZ   1 
ATOM   10708 N N    . LEU   A  1 706 ? 28.747 37.972  -49.367 1.00 68.11  ? 732  LEU   A N    1 
ATOM   10709 C CA   . LEU   A  1 706 ? 27.605 37.331  -48.706 1.00 68.77  ? 732  LEU   A CA   1 
ATOM   10710 C C    . LEU   A  1 706 ? 26.233 37.646  -49.316 1.00 69.22  ? 732  LEU   A C    1 
ATOM   10711 O O    . LEU   A  1 706 ? 25.292 36.889  -49.087 1.00 69.49  ? 732  LEU   A O    1 
ATOM   10712 C CB   . LEU   A  1 706 ? 27.574 37.711  -47.204 1.00 69.08  ? 732  LEU   A CB   1 
ATOM   10713 C CG   . LEU   A  1 706 ? 28.757 37.235  -46.325 1.00 70.88  ? 732  LEU   A CG   1 
ATOM   10714 C CD1  . LEU   A  1 706 ? 29.897 38.245  -46.319 1.00 71.58  ? 732  LEU   A CD1  1 
ATOM   10715 C CD2  . LEU   A  1 706 ? 28.311 36.981  -44.896 1.00 71.58  ? 732  LEU   A CD2  1 
ATOM   10716 H H    . LEU   A  1 706 ? 29.142 38.741  -48.836 0.00 90.64  ? 732  LEU   A H    1 
ATOM   10717 H HA   . LEU   A  1 706 ? 27.741 36.252  -48.759 0.00 90.20  ? 732  LEU   A HA   1 
ATOM   10718 H HB2  . LEU   A  1 706 ? 27.507 38.795  -47.127 0.00 91.98  ? 732  LEU   A HB2  1 
ATOM   10719 H HB3  . LEU   A  1 706 ? 26.670 37.278  -46.778 0.00 91.16  ? 732  LEU   A HB3  1 
ATOM   10720 H HG   . LEU   A  1 706 ? 29.149 36.295  -46.713 0.00 92.09  ? 732  LEU   A HG   1 
ATOM   10721 H HD11 . LEU   A  1 706 ? 30.561 38.031  -45.483 0.00 93.53  ? 732  LEU   A HD11 1 
ATOM   10722 H HD12 . LEU   A  1 706 ? 30.456 38.156  -47.249 0.00 93.96  ? 732  LEU   A HD12 1 
ATOM   10723 H HD13 . LEU   A  1 706 ? 29.500 39.253  -46.220 0.00 94.67  ? 732  LEU   A HD13 1 
ATOM   10724 H HD21 . LEU   A  1 706 ? 29.162 36.649  -44.304 0.00 92.73  ? 732  LEU   A HD21 1 
ATOM   10725 H HD22 . LEU   A  1 706 ? 27.906 37.902  -44.479 0.00 93.83  ? 732  LEU   A HD22 1 
ATOM   10726 H HD23 . LEU   A  1 706 ? 27.544 36.208  -44.894 0.00 92.91  ? 732  LEU   A HD23 1 
ATOM   10727 N N    . SER   A  1 707 ? 26.100 38.759  -50.048 1.00 69.16  ? 733  SER   A N    1 
ATOM   10728 C CA   . SER   A  1 707 ? 24.820 39.216  -50.596 1.00 69.44  ? 733  SER   A CA   1 
ATOM   10729 C C    . SER   A  1 707 ? 24.368 38.591  -51.929 1.00 69.23  ? 733  SER   A C    1 
ATOM   10730 O O    . SER   A  1 707 ? 23.186 38.277  -52.075 1.00 69.61  ? 733  SER   A O    1 
ATOM   10731 C CB   . SER   A  1 707 ? 24.853 40.735  -50.759 1.00 70.85  ? 733  SER   A CB   1 
ATOM   10732 O OG   . SER   A  1 707 ? 25.669 41.130  -51.851 1.00 73.38  ? 733  SER   A OG   1 
ATOM   10733 H H    . SER   A  1 707 ? 26.862 39.392  -50.271 0.00 93.25  ? 733  SER   A H    1 
ATOM   10734 H HA   . SER   A  1 707 ? 24.040 39.012  -49.865 0.00 94.14  ? 733  SER   A HA   1 
ATOM   10735 H HB2  . SER   A  1 707 ? 23.841 41.099  -50.929 0.00 97.55  ? 733  SER   A HB2  1 
ATOM   10736 H HB3  . SER   A  1 707 ? 25.255 41.176  -49.848 0.00 96.93  ? 733  SER   A HB3  1 
ATOM   10737 H HG   . SER   A  1 707 ? 26.537 40.650  -51.835 0.00 99.56  ? 733  SER   A HG   1 
ATOM   10738 N N    . GLU   A  1 708 ? 25.270 38.478  -52.916 1.00 68.36  ? 734  GLU   A N    1 
ATOM   10739 C CA   . GLU   A  1 708 ? 24.898 38.043  -54.265 1.00 67.69  ? 734  GLU   A CA   1 
ATOM   10740 C C    . GLU   A  1 708 ? 24.585 36.543  -54.439 1.00 65.98  ? 734  GLU   A C    1 
ATOM   10741 O O    . GLU   A  1 708 ? 23.768 36.224  -55.307 1.00 66.49  ? 734  GLU   A O    1 
ATOM   10742 C CB   . GLU   A  1 708 ? 25.971 38.466  -55.281 1.00 70.54  ? 734  GLU   A CB   1 
ATOM   10743 C CG   . GLU   A  1 708 ? 26.260 39.962  -55.304 1.00 76.05  ? 734  GLU   A CG   1 
ATOM   10744 C CD   . GLU   A  1 708 ? 25.057 40.860  -55.521 1.00 84.08  ? 734  GLU   A CD   1 
ATOM   10745 O OE1  . GLU   A  1 708 ? 24.811 41.254  -56.685 1.00 86.28  ? 734  GLU   A OE1  1 
ATOM   10746 O OE2  . GLU   A  1 708 ? 24.359 41.170  -54.528 1.00 86.12  ? 734  GLU   A OE2  1 
ATOM   10747 H H    . GLU   A  1 708 ? 26.260 38.669  -52.805 0.00 92.53  ? 734  GLU   A H    1 
ATOM   10748 H HA   . GLU   A  1 708 ? 23.985 38.572  -54.534 0.00 92.80  ? 734  GLU   A HA   1 
ATOM   10749 H HB2  . GLU   A  1 708 ? 26.901 37.949  -55.048 0.00 95.00  ? 734  GLU   A HB2  1 
ATOM   10750 H HB3  . GLU   A  1 708 ? 25.636 38.179  -56.277 0.00 95.84  ? 734  GLU   A HB3  1 
ATOM   10751 H HG2  . GLU   A  1 708 ? 26.710 40.248  -54.355 0.00 103.04 ? 734  GLU   A HG2  1 
ATOM   10752 H HG3  . GLU   A  1 708 ? 26.962 40.162  -56.112 0.00 103.35 ? 734  GLU   A HG3  1 
ATOM   10753 N N    . VAL   A  1 709 ? 25.201 35.629  -53.656 1.00 63.74  ? 735  VAL   A N    1 
ATOM   10754 C CA   . VAL   A  1 709 ? 24.905 34.192  -53.813 1.00 61.77  ? 735  VAL   A CA   1 
ATOM   10755 C C    . VAL   A  1 709 ? 23.539 33.916  -53.166 1.00 58.83  ? 735  VAL   A C    1 
ATOM   10756 O O    . VAL   A  1 709 ? 23.454 33.671  -51.966 1.00 59.00  ? 735  VAL   A O    1 
ATOM   10757 C CB   . VAL   A  1 709 ? 26.018 33.268  -53.250 1.00 62.94  ? 735  VAL   A CB   1 
ATOM   10758 C CG1  . VAL   A  1 709 ? 25.792 31.817  -53.669 1.00 63.54  ? 735  VAL   A CG1  1 
ATOM   10759 C CG2  . VAL   A  1 709 ? 27.395 33.731  -53.714 1.00 63.59  ? 735  VAL   A CG2  1 
ATOM   10760 H H    . VAL   A  1 709 ? 25.858 35.853  -52.915 0.00 85.34  ? 735  VAL   A H    1 
ATOM   10761 H HA   . VAL   A  1 709 ? 24.822 33.983  -54.878 0.00 82.66  ? 735  VAL   A HA   1 
ATOM   10762 H HB   . VAL   A  1 709 ? 26.007 33.307  -52.161 0.00 82.65  ? 735  VAL   A HB   1 
ATOM   10763 H HG11 . VAL   A  1 709 ? 26.562 31.197  -53.213 0.00 82.30  ? 735  VAL   A HG11 1 
ATOM   10764 H HG12 . VAL   A  1 709 ? 24.807 31.481  -53.346 0.00 83.03  ? 735  VAL   A HG12 1 
ATOM   10765 H HG13 . VAL   A  1 709 ? 25.868 31.755  -54.754 0.00 83.20  ? 735  VAL   A HG13 1 
ATOM   10766 H HG21 . VAL   A  1 709 ? 28.122 32.958  -53.472 0.00 82.91  ? 735  VAL   A HG21 1 
ATOM   10767 H HG22 . VAL   A  1 709 ? 27.377 33.909  -54.788 0.00 83.96  ? 735  VAL   A HG22 1 
ATOM   10768 H HG23 . VAL   A  1 709 ? 27.655 34.651  -53.191 0.00 83.94  ? 735  VAL   A HG23 1 
ATOM   10769 N N    . SER   A  1 710 ? 22.469 33.996  -53.966 1.00 56.15  ? 736  SER   A N    1 
ATOM   10770 C CA   . SER   A  1 710 ? 21.099 33.824  -53.480 1.00 53.70  ? 736  SER   A CA   1 
ATOM   10771 C C    . SER   A  1 710 ? 20.803 32.441  -52.900 1.00 50.08  ? 736  SER   A C    1 
ATOM   10772 O O    . SER   A  1 710 ? 20.083 32.354  -51.906 1.00 50.47  ? 736  SER   A O    1 
ATOM   10773 C CB   . SER   A  1 710 ? 20.096 34.155  -54.583 1.00 55.10  ? 736  SER   A CB   1 
ATOM   10774 O OG   . SER   A  1 710 ? 20.404 33.491  -55.797 1.00 57.60  ? 736  SER   A OG   1 
ATOM   10775 H H    . SER   A  1 710 ? 22.516 34.187  -54.962 0.00 76.89  ? 736  SER   A H    1 
ATOM   10776 H HA   . SER   A  1 710 ? 20.940 34.549  -52.682 0.00 74.20  ? 736  SER   A HA   1 
ATOM   10777 H HB2  . SER   A  1 710 ? 19.103 33.847  -54.258 0.00 76.65  ? 736  SER   A HB2  1 
ATOM   10778 H HB3  . SER   A  1 710 ? 20.109 35.230  -54.756 0.00 77.15  ? 736  SER   A HB3  1 
ATOM   10779 H HG   . SER   A  1 710 ? 19.704 33.679  -56.475 0.00 79.87  ? 736  SER   A HG   1 
ATOM   10780 N N    . SER   A  1 711 ? 21.331 31.366  -53.503 1.00 46.35  ? 737  SER   A N    1 
ATOM   10781 C CA   . SER   A  1 711 ? 21.064 30.014  -53.006 1.00 43.40  ? 737  SER   A CA   1 
ATOM   10782 C C    . SER   A  1 711 ? 21.827 29.660  -51.717 1.00 39.78  ? 737  SER   A C    1 
ATOM   10783 O O    . SER   A  1 711 ? 21.448 28.694  -51.058 1.00 38.95  ? 737  SER   A O    1 
ATOM   10784 C CB   . SER   A  1 711 ? 21.376 28.980  -54.085 1.00 44.68  ? 737  SER   A CB   1 
ATOM   10785 O OG   . SER   A  1 711 ? 22.713 29.098  -54.541 1.00 47.01  ? 737  SER   A OG   1 
ATOM   10786 H H    . SER   A  1 711 ? 21.932 31.395  -54.321 0.00 63.63  ? 737  SER   A H    1 
ATOM   10787 H HA   . SER   A  1 711 ? 20.001 29.924  -52.786 0.00 59.66  ? 737  SER   A HA   1 
ATOM   10788 H HB2  . SER   A  1 711 ? 21.227 27.984  -53.673 0.00 59.99  ? 737  SER   A HB2  1 
ATOM   10789 H HB3  . SER   A  1 711 ? 20.706 29.138  -54.929 0.00 61.09  ? 737  SER   A HB3  1 
ATOM   10790 H HG   . SER   A  1 711 ? 23.324 28.553  -53.978 0.00 62.38  ? 737  SER   A HG   1 
ATOM   10791 N N    . LEU   A  1 712 ? 22.891 30.403  -51.363 1.00 37.57  ? 738  LEU   A N    1 
ATOM   10792 C CA   . LEU   A  1 712 ? 23.695 30.062  -50.175 1.00 36.08  ? 738  LEU   A CA   1 
ATOM   10793 C C    . LEU   A  1 712 ? 22.941 30.275  -48.844 1.00 34.52  ? 738  LEU   A C    1 
ATOM   10794 O O    . LEU   A  1 712 ? 22.602 31.398  -48.494 1.00 34.56  ? 738  LEU   A O    1 
ATOM   10795 C CB   . LEU   A  1 712 ? 25.032 30.831  -50.185 1.00 36.14  ? 738  LEU   A CB   1 
ATOM   10796 C CG   . LEU   A  1 712 ? 26.159 30.288  -49.310 1.00 37.70  ? 738  LEU   A CG   1 
ATOM   10797 C CD1  . LEU   A  1 712 ? 26.559 28.869  -49.721 1.00 38.45  ? 738  LEU   A CD1  1 
ATOM   10798 C CD2  . LEU   A  1 712 ? 27.381 31.188  -49.393 1.00 38.43  ? 738  LEU   A CD2  1 
ATOM   10799 H H    . LEU   A  1 712 ? 23.222 31.227  -51.854 0.00 51.91  ? 738  LEU   A H    1 
ATOM   10800 H HA   . LEU   A  1 712 ? 23.930 29.004  -50.254 0.00 48.40  ? 738  LEU   A HA   1 
ATOM   10801 H HB2  . LEU   A  1 712 ? 25.416 30.838  -51.204 0.00 49.13  ? 738  LEU   A HB2  1 
ATOM   10802 H HB3  . LEU   A  1 712 ? 24.844 31.856  -49.868 0.00 49.57  ? 738  LEU   A HB3  1 
ATOM   10803 H HG   . LEU   A  1 712 ? 25.826 30.257  -48.273 0.00 50.00  ? 738  LEU   A HG   1 
ATOM   10804 H HD11 . LEU   A  1 712 ? 27.555 28.653  -49.340 0.00 49.82  ? 738  LEU   A HD11 1 
ATOM   10805 H HD12 . LEU   A  1 712 ? 25.852 28.161  -49.292 0.00 50.05  ? 738  LEU   A HD12 1 
ATOM   10806 H HD13 . LEU   A  1 712 ? 26.551 28.795  -50.808 0.00 50.46  ? 738  LEU   A HD13 1 
ATOM   10807 H HD21 . LEU   A  1 712 ? 28.153 30.811  -48.723 0.00 50.61  ? 738  LEU   A HD21 1 
ATOM   10808 H HD22 . LEU   A  1 712 ? 27.752 31.192  -50.418 0.00 51.25  ? 738  LEU   A HD22 1 
ATOM   10809 H HD23 . LEU   A  1 712 ? 27.096 32.196  -49.096 0.00 51.69  ? 738  LEU   A HD23 1 
ATOM   10810 N N    . LYS   A  1 713 ? 22.675 29.178  -48.123 1.00 33.21  ? 739  LYS   A N    1 
ATOM   10811 C CA   . LYS   A  1 713 ? 21.976 29.170  -46.839 1.00 32.55  ? 739  LYS   A CA   1 
ATOM   10812 C C    . LYS   A  1 713 ? 22.961 29.060  -45.664 1.00 31.30  ? 739  LYS   A C    1 
ATOM   10813 O O    . LYS   A  1 713 ? 22.737 29.678  -44.623 1.00 31.34  ? 739  LYS   A O    1 
ATOM   10814 C CB   . LYS   A  1 713 ? 20.998 27.980  -46.776 1.00 34.60  ? 739  LYS   A CB   1 
ATOM   10815 C CG   . LYS   A  1 713 ? 19.880 27.996  -47.839 1.00 39.70  ? 739  LYS   A CG   1 
ATOM   10816 C CD   . LYS   A  1 713 ? 18.900 29.171  -47.734 1.00 44.22  ? 739  LYS   A CD   1 
ATOM   10817 C CE   . LYS   A  1 713 ? 18.175 29.262  -46.406 1.00 48.02  ? 739  LYS   A CE   1 
ATOM   10818 N NZ   . LYS   A  1 713 ? 17.100 30.291  -46.427 1.00 49.37  ? 739  LYS   A NZ   1 
ATOM   10819 H H    . LYS   A  1 713 ? 22.944 28.244  -48.412 0.00 44.55  ? 739  LYS   A H    1 
ATOM   10820 H HA   . LYS   A  1 713 ? 21.400 30.084  -46.707 0.00 44.91  ? 739  LYS   A HA   1 
ATOM   10821 H HB2  . LYS   A  1 713 ? 21.570 27.065  -46.925 0.00 45.87  ? 739  LYS   A HB2  1 
ATOM   10822 H HB3  . LYS   A  1 713 ? 20.541 27.945  -45.788 0.00 46.46  ? 739  LYS   A HB3  1 
ATOM   10823 H HG2  . LYS   A  1 713 ? 20.336 28.034  -48.827 0.00 53.27  ? 739  LYS   A HG2  1 
ATOM   10824 H HG3  . LYS   A  1 713 ? 19.300 27.079  -47.738 0.00 52.99  ? 739  LYS   A HG3  1 
ATOM   10825 H HD2  . LYS   A  1 713 ? 19.432 30.106  -47.898 0.00 59.90  ? 739  LYS   A HD2  1 
ATOM   10826 H HD3  . LYS   A  1 713 ? 18.141 29.052  -48.506 0.00 60.00  ? 739  LYS   A HD3  1 
ATOM   10827 H HE2  . LYS   A  1 713 ? 17.723 28.299  -46.175 0.00 63.91  ? 739  LYS   A HE2  1 
ATOM   10828 H HE3  . LYS   A  1 713 ? 18.879 29.546  -45.626 0.00 63.98  ? 739  LYS   A HE3  1 
ATOM   10829 H HZ1  . LYS   A  1 713 ? 16.633 30.324  -45.526 0.00 66.93  ? 739  LYS   A HZ1  1 
ATOM   10830 H HZ2  . LYS   A  1 713 ? 17.496 31.204  -46.627 0.00 67.23  ? 739  LYS   A HZ2  1 
ATOM   10831 H HZ3  . LYS   A  1 713 ? 16.417 30.064  -47.143 0.00 67.18  ? 739  LYS   A HZ3  1 
ATOM   10832 N N    . HIS   A  1 714 ? 24.018 28.246  -45.808 1.00 29.69  ? 740  HIS   A N    1 
ATOM   10833 C CA   . HIS   A  1 714 ? 24.986 28.014  -44.736 1.00 28.90  ? 740  HIS   A CA   1 
ATOM   10834 C C    . HIS   A  1 714 ? 26.410 28.311  -45.233 1.00 28.31  ? 740  HIS   A C    1 
ATOM   10835 O O    . HIS   A  1 714 ? 26.887 27.657  -46.162 1.00 28.05  ? 740  HIS   A O    1 
ATOM   10836 C CB   . HIS   A  1 714 ? 24.866 26.550  -44.276 1.00 28.94  ? 740  HIS   A CB   1 
ATOM   10837 C CG   . HIS   A  1 714 ? 25.783 26.134  -43.161 1.00 29.88  ? 740  HIS   A CG   1 
ATOM   10838 N ND1  . HIS   A  1 714 ? 25.829 24.822  -42.735 1.00 31.23  ? 740  HIS   A ND1  1 
ATOM   10839 C CD2  . HIS   A  1 714 ? 26.645 26.863  -42.411 1.00 30.18  ? 740  HIS   A CD2  1 
ATOM   10840 C CE1  . HIS   A  1 714 ? 26.715 24.790  -41.750 1.00 31.29  ? 740  HIS   A CE1  1 
ATOM   10841 N NE2  . HIS   A  1 714 ? 27.238 25.993  -41.527 1.00 30.81  ? 740  HIS   A NE2  1 
ATOM   10842 H H    . HIS   A  1 714 ? 24.229 27.725  -46.653 0.00 39.34  ? 740  HIS   A H    1 
ATOM   10843 H HA   . HIS   A  1 714 ? 24.783 28.647  -43.876 0.00 38.28  ? 740  HIS   A HA   1 
ATOM   10844 H HB2  . HIS   A  1 714 ? 23.844 26.373  -43.943 0.00 37.53  ? 740  HIS   A HB2  1 
ATOM   10845 H HB3  . HIS   A  1 714 ? 25.085 25.910  -45.129 0.00 37.12  ? 740  HIS   A HB3  1 
ATOM   10846 H HD2  . HIS   A  1 714 ? 26.830 27.923  -42.491 0.00 38.75  ? 740  HIS   A HD2  1 
ATOM   10847 H HE1  . HIS   A  1 714 ? 26.979 23.899  -41.202 0.00 38.11  ? 740  HIS   A HE1  1 
ATOM   10848 H HE2  . HIS   A  1 714 ? 27.939 26.226  -40.830 0.00 38.27  ? 740  HIS   A HE2  1 
ATOM   10849 N N    . LEU   A  1 715 ? 27.067 29.309  -44.615 1.00 26.61  ? 741  LEU   A N    1 
ATOM   10850 C CA   . LEU   A  1 715 ? 28.441 29.682  -44.916 1.00 25.56  ? 741  LEU   A CA   1 
ATOM   10851 C C    . LEU   A  1 715 ? 29.225 29.526  -43.618 1.00 25.41  ? 741  LEU   A C    1 
ATOM   10852 O O    . LEU   A  1 715 ? 28.873 30.146  -42.613 1.00 25.56  ? 741  LEU   A O    1 
ATOM   10853 C CB   . LEU   A  1 715 ? 28.514 31.119  -45.432 1.00 25.25  ? 741  LEU   A CB   1 
ATOM   10854 C CG   . LEU   A  1 715 ? 29.901 31.761  -45.563 1.00 25.86  ? 741  LEU   A CG   1 
ATOM   10855 C CD1  . LEU   A  1 715 ? 30.826 30.939  -46.459 1.00 25.96  ? 741  LEU   A CD1  1 
ATOM   10856 C CD2  . LEU   A  1 715 ? 29.766 33.182  -46.110 1.00 25.99  ? 741  LEU   A CD2  1 
ATOM   10857 H H    . LEU   A  1 715 ? 26.662 29.886  -43.885 0.00 35.63  ? 741  LEU   A H    1 
ATOM   10858 H HA   . LEU   A  1 715 ? 28.869 29.026  -45.671 0.00 33.61  ? 741  LEU   A HA   1 
ATOM   10859 H HB2  . LEU   A  1 715 ? 28.053 31.149  -46.417 0.00 34.62  ? 741  LEU   A HB2  1 
ATOM   10860 H HB3  . LEU   A  1 715 ? 27.937 31.740  -44.748 0.00 34.74  ? 741  LEU   A HB3  1 
ATOM   10861 H HG   . LEU   A  1 715 ? 30.364 31.843  -44.581 0.00 34.95  ? 741  LEU   A HG   1 
ATOM   10862 H HD11 . LEU   A  1 715 ? 31.740 31.502  -46.641 0.00 34.85  ? 741  LEU   A HD11 1 
ATOM   10863 H HD12 . LEU   A  1 715 ? 31.068 30.005  -45.956 0.00 34.12  ? 741  LEU   A HD12 1 
ATOM   10864 H HD13 . LEU   A  1 715 ? 30.320 30.734  -47.401 0.00 34.85  ? 741  LEU   A HD13 1 
ATOM   10865 H HD21 . LEU   A  1 715 ? 30.717 33.698  -45.989 0.00 36.23  ? 741  LEU   A HD21 1 
ATOM   10866 H HD22 . LEU   A  1 715 ? 29.505 33.132  -47.166 0.00 36.33  ? 741  LEU   A HD22 1 
ATOM   10867 H HD23 . LEU   A  1 715 ? 28.986 33.704  -45.559 0.00 36.58  ? 741  LEU   A HD23 1 
ATOM   10868 N N    . ASP   A  1 716 ? 30.232 28.645  -43.619 1.00 24.45  ? 742  ASP   A N    1 
ATOM   10869 C CA   . ASP   A  1 716 ? 31.042 28.432  -42.430 1.00 24.60  ? 742  ASP   A CA   1 
ATOM   10870 C C    . ASP   A  1 716 ? 32.442 29.007  -42.668 1.00 24.03  ? 742  ASP   A C    1 
ATOM   10871 O O    . ASP   A  1 716 ? 33.225 28.462  -43.447 1.00 22.87  ? 742  ASP   A O    1 
ATOM   10872 C CB   . ASP   A  1 716 ? 31.035 26.943  -42.014 1.00 26.26  ? 742  ASP   A CB   1 
ATOM   10873 C CG   . ASP   A  1 716 ? 32.123 26.522  -41.043 1.00 31.87  ? 742  ASP   A CG   1 
ATOM   10874 O OD1  . ASP   A  1 716 ? 32.561 27.377  -40.226 1.00 31.29  ? 742  ASP   A OD1  1 
ATOM   10875 O OD2  . ASP   A  1 716 ? 32.527 25.330  -41.083 1.00 34.82  ? 742  ASP   A OD2  1 
ATOM   10876 H H    . ASP   A  1 716 ? 30.508 28.072  -44.411 0.00 31.30  ? 742  ASP   A H    1 
ATOM   10877 H HA   . ASP   A  1 716 ? 30.610 28.972  -41.591 0.00 31.61  ? 742  ASP   A HA   1 
ATOM   10878 H HB2  . ASP   A  1 716 ? 30.086 26.748  -41.516 0.00 32.65  ? 742  ASP   A HB2  1 
ATOM   10879 H HB3  . ASP   A  1 716 ? 31.099 26.310  -42.894 0.00 32.38  ? 742  ASP   A HB3  1 
ATOM   10880 N N    . LEU   A  1 717 ? 32.718 30.154  -42.027 1.00 23.89  ? 743  LEU   A N    1 
ATOM   10881 C CA   . LEU   A  1 717 ? 34.015 30.824  -42.095 1.00 24.23  ? 743  LEU   A CA   1 
ATOM   10882 C C    . LEU   A  1 717 ? 34.770 30.759  -40.748 1.00 24.46  ? 743  LEU   A C    1 
ATOM   10883 O O    . LEU   A  1 717 ? 35.731 31.510  -40.564 1.00 24.76  ? 743  LEU   A O    1 
ATOM   10884 C CB   . LEU   A  1 717 ? 33.819 32.285  -42.534 1.00 24.68  ? 743  LEU   A CB   1 
ATOM   10885 C CG   . LEU   A  1 717 ? 33.469 32.494  -44.009 1.00 26.67  ? 743  LEU   A CG   1 
ATOM   10886 C CD1  . LEU   A  1 717 ? 32.941 33.889  -44.236 1.00 27.42  ? 743  LEU   A CD1  1 
ATOM   10887 C CD2  . LEU   A  1 717 ? 34.675 32.201  -44.907 1.00 28.10  ? 743  LEU   A CD2  1 
ATOM   10888 H H    . LEU   A  1 717 ? 32.054 30.648  -41.439 0.00 31.33  ? 743  LEU   A H    1 
ATOM   10889 H HA   . LEU   A  1 717 ? 34.656 30.325  -42.818 0.00 31.27  ? 743  LEU   A HA   1 
ATOM   10890 H HB2  . LEU   A  1 717 ? 33.009 32.717  -41.948 0.00 33.25  ? 743  LEU   A HB2  1 
ATOM   10891 H HB3  . LEU   A  1 717 ? 34.732 32.849  -42.348 0.00 33.09  ? 743  LEU   A HB3  1 
ATOM   10892 H HG   . LEU   A  1 717 ? 32.680 31.797  -44.286 0.00 35.41  ? 743  LEU   A HG   1 
ATOM   10893 H HD11 . LEU   A  1 717 ? 32.885 34.090  -45.305 0.00 37.66  ? 743  LEU   A HD11 1 
ATOM   10894 H HD12 . LEU   A  1 717 ? 31.947 33.961  -43.798 0.00 37.58  ? 743  LEU   A HD12 1 
ATOM   10895 H HD13 . LEU   A  1 717 ? 33.607 34.599  -43.748 0.00 37.67  ? 743  LEU   A HD13 1 
ATOM   10896 H HD21 . LEU   A  1 717 ? 34.471 32.566  -45.912 0.00 37.43  ? 743  LEU   A HD21 1 
ATOM   10897 H HD22 . LEU   A  1 717 ? 35.557 32.699  -44.507 0.00 37.27  ? 743  LEU   A HD22 1 
ATOM   10898 H HD23 . LEU   A  1 717 ? 34.843 31.126  -44.953 0.00 36.52  ? 743  LEU   A HD23 1 
ATOM   10899 N N    . SER   A  1 718 ? 34.375 29.864  -39.823 1.00 24.22  ? 744  SER   A N    1 
ATOM   10900 C CA   . SER   A  1 718 ? 35.043 29.777  -38.522 1.00 24.79  ? 744  SER   A CA   1 
ATOM   10901 C C    . SER   A  1 718 ? 36.516 29.352  -38.651 1.00 25.32  ? 744  SER   A C    1 
ATOM   10902 O O    . SER   A  1 718 ? 36.911 28.795  -39.664 1.00 24.85  ? 744  SER   A O    1 
ATOM   10903 C CB   . SER   A  1 718 ? 34.292 28.837  -37.584 1.00 25.68  ? 744  SER   A CB   1 
ATOM   10904 O OG   . SER   A  1 718 ? 34.302 27.488  -38.015 1.00 28.00  ? 744  SER   A OG   1 
ATOM   10905 H H    . SER   A  1 718 ? 33.626 29.189  -39.936 0.00 30.64  ? 744  SER   A H    1 
ATOM   10906 H HA   . SER   A  1 718 ? 35.028 30.765  -38.064 0.00 31.87  ? 744  SER   A HA   1 
ATOM   10907 H HB2  . SER   A  1 718 ? 34.760 28.887  -36.602 0.00 32.02  ? 744  SER   A HB2  1 
ATOM   10908 H HB3  . SER   A  1 718 ? 33.258 29.171  -37.512 0.00 32.34  ? 744  SER   A HB3  1 
ATOM   10909 H HG   . SER   A  1 718 ? 33.676 27.373  -38.777 0.00 34.23  ? 744  SER   A HG   1 
ATOM   10910 N N    . SER   A  1 719 ? 37.331 29.705  -37.660 1.00 25.58  ? 745  SER   A N    1 
ATOM   10911 C CA   . SER   A  1 719 ? 38.749 29.358  -37.606 1.00 26.42  ? 745  SER   A CA   1 
ATOM   10912 C C    . SER   A  1 719 ? 39.523 29.735  -38.866 1.00 26.71  ? 745  SER   A C    1 
ATOM   10913 O O    . SER   A  1 719 ? 40.244 28.921  -39.428 1.00 27.87  ? 745  SER   A O    1 
ATOM   10914 C CB   . SER   A  1 719 ? 38.919 27.882  -37.261 1.00 28.19  ? 745  SER   A CB   1 
ATOM   10915 O OG   . SER   A  1 719 ? 38.242 27.586  -36.051 1.00 31.34  ? 745  SER   A OG   1 
ATOM   10916 H H    . SER   A  1 719 ? 37.024 30.245  -36.857 0.00 32.33  ? 745  SER   A H    1 
ATOM   10917 H HA   . SER   A  1 719 ? 39.196 29.919  -36.786 0.00 33.04  ? 745  SER   A HA   1 
ATOM   10918 H HB2  . SER   A  1 719 ? 38.499 27.272  -38.059 0.00 33.96  ? 745  SER   A HB2  1 
ATOM   10919 H HB3  . SER   A  1 719 ? 39.976 27.660  -37.124 0.00 34.06  ? 745  SER   A HB3  1 
ATOM   10920 H HG   . SER   A  1 719 ? 38.336 26.621  -35.836 0.00 37.44  ? 745  SER   A HG   1 
ATOM   10921 N N    . ASN   A  1 720 ? 39.352 30.964  -39.322 1.00 25.95  ? 746  ASN   A N    1 
ATOM   10922 C CA   . ASN   A  1 720 ? 40.102 31.512  -40.448 1.00 26.50  ? 746  ASN   A CA   1 
ATOM   10923 C C    . ASN   A  1 720 ? 40.979 32.673  -39.876 1.00 27.42  ? 746  ASN   A C    1 
ATOM   10924 O O    . ASN   A  1 720 ? 41.291 32.630  -38.679 1.00 27.53  ? 746  ASN   A O    1 
ATOM   10925 C CB   . ASN   A  1 720 ? 39.126 31.907  -41.594 1.00 26.43  ? 746  ASN   A CB   1 
ATOM   10926 C CG   . ASN   A  1 720 ? 38.881 30.772  -42.562 1.00 28.01  ? 746  ASN   A CG   1 
ATOM   10927 O OD1  . ASN   A  1 720 ? 39.634 30.592  -43.522 1.00 27.65  ? 746  ASN   A OD1  1 
ATOM   10928 N ND2  . ASN   A  1 720 ? 37.849 29.968  -42.319 1.00 28.13  ? 746  ASN   A ND2  1 
ATOM   10929 H H    . ASN   A  1 720 ? 38.695 31.626  -38.922 0.00 33.39  ? 746  ASN   A H    1 
ATOM   10930 H HA   . ASN   A  1 720 ? 40.816 30.776  -40.817 0.00 33.57  ? 746  ASN   A HA   1 
ATOM   10931 H HB2  . ASN   A  1 720 ? 38.170 32.193  -41.158 0.00 34.39  ? 746  ASN   A HB2  1 
ATOM   10932 H HB3  . ASN   A  1 720 ? 39.515 32.735  -42.182 0.00 34.64  ? 746  ASN   A HB3  1 
ATOM   10933 H HD21 . ASN   A  1 720 ? 37.654 29.196  -42.948 0.00 35.06  ? 746  ASN   A HD21 1 
ATOM   10934 H HD22 . ASN   A  1 720 ? 37.252 30.124  -41.513 0.00 35.44  ? 746  ASN   A HD22 1 
ATOM   10935 N N    . LEU   A  1 721 ? 41.433 33.645  -40.688 1.00 27.80  ? 747  LEU   A N    1 
ATOM   10936 C CA   . LEU   A  1 721 ? 42.262 34.739  -40.195 1.00 29.05  ? 747  LEU   A CA   1 
ATOM   10937 C C    . LEU   A  1 721 ? 41.572 36.086  -40.449 1.00 29.72  ? 747  LEU   A C    1 
ATOM   10938 O O    . LEU   A  1 721 ? 42.244 37.067  -40.729 1.00 29.61  ? 747  LEU   A O    1 
ATOM   10939 C CB   . LEU   A  1 721 ? 43.642 34.671  -40.881 1.00 29.63  ? 747  LEU   A CB   1 
ATOM   10940 C CG   . LEU   A  1 721 ? 44.415 33.355  -40.655 1.00 31.43  ? 747  LEU   A CG   1 
ATOM   10941 C CD1  . LEU   A  1 721 ? 45.673 33.317  -41.492 1.00 32.12  ? 747  LEU   A CD1  1 
ATOM   10942 C CD2  . LEU   A  1 721 ? 44.771 33.161  -39.186 1.00 32.53  ? 747  LEU   A CD2  1 
ATOM   10943 H H    . LEU   A  1 721 ? 41.294 33.689  -41.691 0.00 36.70  ? 747  LEU   A H    1 
ATOM   10944 H HA   . LEU   A  1 721 ? 42.419 34.665  -39.121 0.00 38.66  ? 747  LEU   A HA   1 
ATOM   10945 H HB2  . LEU   A  1 721 ? 43.505 34.795  -41.954 0.00 39.50  ? 747  LEU   A HB2  1 
ATOM   10946 H HB3  . LEU   A  1 721 ? 44.269 35.474  -40.496 0.00 39.85  ? 747  LEU   A HB3  1 
ATOM   10947 H HG   . LEU   A  1 721 ? 43.793 32.514  -40.956 0.00 40.38  ? 747  LEU   A HG   1 
ATOM   10948 H HD11 . LEU   A  1 721 ? 46.155 32.349  -41.363 0.00 41.21  ? 747  LEU   A HD11 1 
ATOM   10949 H HD12 . LEU   A  1 721 ? 45.406 33.460  -42.538 0.00 41.80  ? 747  LEU   A HD12 1 
ATOM   10950 H HD13 . LEU   A  1 721 ? 46.341 34.111  -41.164 0.00 42.16  ? 747  LEU   A HD13 1 
ATOM   10951 H HD21 . LEU   A  1 721 ? 45.479 32.340  -39.095 0.00 41.61  ? 747  LEU   A HD21 1 
ATOM   10952 H HD22 . LEU   A  1 721 ? 45.214 34.079  -38.802 0.00 42.54  ? 747  LEU   A HD22 1 
ATOM   10953 H HD23 . LEU   A  1 721 ? 43.867 32.920  -38.629 0.00 41.87  ? 747  LEU   A HD23 1 
ATOM   10954 N N    . LEU   A  1 722 ? 40.224 36.129  -40.341 1.00 29.81  ? 748  LEU   A N    1 
ATOM   10955 C CA   . LEU   A  1 722 ? 39.474 37.352  -40.568 1.00 30.78  ? 748  LEU   A CA   1 
ATOM   10956 C C    . LEU   A  1 722 ? 39.685 38.314  -39.401 1.00 32.42  ? 748  LEU   A C    1 
ATOM   10957 O O    . LEU   A  1 722 ? 39.417 37.941  -38.260 1.00 32.44  ? 748  LEU   A O    1 
ATOM   10958 C CB   . LEU   A  1 722 ? 37.970 37.060  -40.701 1.00 30.30  ? 748  LEU   A CB   1 
ATOM   10959 C CG   . LEU   A  1 722 ? 37.538 36.155  -41.853 1.00 31.12  ? 748  LEU   A CG   1 
ATOM   10960 C CD1  . LEU   A  1 722 ? 36.064 35.793  -41.716 1.00 31.08  ? 748  LEU   A CD1  1 
ATOM   10961 C CD2  . LEU   A  1 722 ? 37.819 36.811  -43.208 1.00 31.59  ? 748  LEU   A CD2  1 
ATOM   10962 H H    . LEU   A  1 722 ? 39.639 35.341  -40.082 0.00 40.07  ? 748  LEU   A H    1 
ATOM   10963 H HA   . LEU   A  1 722 ? 39.817 37.827  -41.486 0.00 42.78  ? 748  LEU   A HA   1 
ATOM   10964 H HB2  . LEU   A  1 722 ? 37.635 36.586  -39.780 0.00 41.55  ? 748  LEU   A HB2  1 
ATOM   10965 H HB3  . LEU   A  1 722 ? 37.450 38.009  -40.824 0.00 42.50  ? 748  LEU   A HB3  1 
ATOM   10966 H HG   . LEU   A  1 722 ? 38.110 35.230  -41.807 0.00 41.78  ? 748  LEU   A HG   1 
ATOM   10967 H HD11 . LEU   A  1 722 ? 35.781 35.143  -42.542 0.00 42.03  ? 748  LEU   A HD11 1 
ATOM   10968 H HD12 . LEU   A  1 722 ? 35.915 35.272  -40.771 0.00 41.97  ? 748  LEU   A HD12 1 
ATOM   10969 H HD13 . LEU   A  1 722 ? 35.468 36.704  -41.737 0.00 42.96  ? 748  LEU   A HD13 1 
ATOM   10970 H HD21 . LEU   A  1 722 ? 37.336 36.227  -43.989 0.00 43.19  ? 748  LEU   A HD21 1 
ATOM   10971 H HD22 . LEU   A  1 722 ? 37.425 37.826  -43.201 0.00 44.09  ? 748  LEU   A HD22 1 
ATOM   10972 H HD23 . LEU   A  1 722 ? 38.895 36.828  -43.376 0.00 43.33  ? 748  LEU   A HD23 1 
ATOM   10973 N N    . LYS   A  1 723 ? 40.168 39.539  -39.692 1.00 33.95  ? 749  LYS   A N    1 
ATOM   10974 C CA   . LYS   A  1 723 ? 40.372 40.599  -38.704 1.00 36.69  ? 749  LYS   A CA   1 
ATOM   10975 C C    . LYS   A  1 723 ? 39.081 41.447  -38.595 1.00 39.31  ? 749  LYS   A C    1 
ATOM   10976 O O    . LYS   A  1 723 ? 38.805 42.015  -37.551 1.00 39.05  ? 749  LYS   A O    1 
ATOM   10977 C CB   . LYS   A  1 723 ? 41.554 41.496  -39.111 1.00 39.20  ? 749  LYS   A CB   1 
ATOM   10978 C CG   . LYS   A  1 723 ? 42.898 40.771  -39.197 1.00 44.33  ? 749  LYS   A CG   1 
ATOM   10979 C CD   . LYS   A  1 723 ? 43.984 41.616  -39.874 1.00 50.23  ? 749  LYS   A CD   1 
ATOM   10980 C CE   . LYS   A  1 723 ? 44.238 42.928  -39.173 1.00 54.84  ? 749  LYS   A CE   1 
ATOM   10981 N NZ   . LYS   A  1 723 ? 45.586 43.491  -39.481 1.00 58.03  ? 749  LYS   A NZ   1 
ATOM   10982 H H    . LYS   A  1 723 ? 40.411 39.836  -40.632 0.00 47.81  ? 749  LYS   A H    1 
ATOM   10983 H HA   . LYS   A  1 723 ? 40.591 40.180  -37.723 0.00 51.30  ? 749  LYS   A HA   1 
ATOM   10984 H HB2  . LYS   A  1 723 ? 41.347 41.940  -40.084 0.00 55.49  ? 749  LYS   A HB2  1 
ATOM   10985 H HB3  . LYS   A  1 723 ? 41.649 42.283  -38.364 0.00 55.73  ? 749  LYS   A HB3  1 
ATOM   10986 H HG2  . LYS   A  1 723 ? 43.240 40.530  -38.191 0.00 60.64  ? 749  LYS   A HG2  1 
ATOM   10987 H HG3  . LYS   A  1 723 ? 42.782 39.860  -39.779 0.00 60.20  ? 749  LYS   A HG3  1 
ATOM   10988 H HD2  . LYS   A  1 723 ? 44.916 41.053  -39.882 0.00 68.08  ? 749  LYS   A HD2  1 
ATOM   10989 H HD3  . LYS   A  1 723 ? 43.673 41.837  -40.895 0.00 68.63  ? 749  LYS   A HD3  1 
ATOM   10990 H HE2  . LYS   A  1 723 ? 43.491 43.651  -39.498 0.00 75.43  ? 749  LYS   A HE2  1 
ATOM   10991 H HE3  . LYS   A  1 723 ? 44.166 42.775  -38.098 0.00 74.81  ? 749  LYS   A HE3  1 
ATOM   10992 H HZ1  . LYS   A  1 723 ? 45.705 44.381  -39.007 0.00 79.81  ? 749  LYS   A HZ1  1 
ATOM   10993 H HZ2  . LYS   A  1 723 ? 46.309 42.852  -39.167 0.00 78.72  ? 749  LYS   A HZ2  1 
ATOM   10994 H HZ3  . LYS   A  1 723 ? 45.683 43.635  -40.481 0.00 79.26  ? 749  LYS   A HZ3  1 
ATOM   10995 N N    . THR   A  1 724 ? 38.298 41.555  -39.680 1.00 41.51  ? 750  THR   A N    1 
ATOM   10996 C CA   . THR   A  1 724 ? 37.040 42.300  -39.697 1.00 44.37  ? 750  THR   A CA   1 
ATOM   10997 C C    . THR   A  1 724 ? 36.188 41.871  -40.926 1.00 47.19  ? 750  THR   A C    1 
ATOM   10998 O O    . THR   A  1 724 ? 36.635 41.057  -41.732 1.00 47.22  ? 750  THR   A O    1 
ATOM   10999 C CB   . THR   A  1 724 ? 37.336 43.827  -39.716 1.00 45.85  ? 750  THR   A CB   1 
ATOM   11000 O OG1  . THR   A  1 724 ? 36.095 44.519  -39.558 1.00 47.29  ? 750  THR   A OG1  1 
ATOM   11001 C CG2  . THR   A  1 724 ? 38.027 44.273  -41.007 1.00 45.98  ? 750  THR   A CG2  1 
ATOM   11002 H H    . THR   A  1 724 ? 38.531 41.155  -40.583 0.00 57.93  ? 750  THR   A H    1 
ATOM   11003 H HA   . THR   A  1 724 ? 36.471 42.069  -38.798 0.00 62.17  ? 750  THR   A HA   1 
ATOM   11004 H HB   . THR   A  1 724 ? 37.987 44.083  -38.881 0.00 65.25  ? 750  THR   A HB   1 
ATOM   11005 H HG1  . THR   A  1 724 ? 36.249 45.500  -39.565 0.00 68.26  ? 750  THR   A HG1  1 
ATOM   11006 H HG21 . THR   A  1 724 ? 38.407 45.286  -40.885 0.00 66.32  ? 750  THR   A HG21 1 
ATOM   11007 H HG22 . THR   A  1 724 ? 38.859 43.613  -41.246 0.00 65.04  ? 750  THR   A HG22 1 
ATOM   11008 H HG23 . THR   A  1 724 ? 37.322 44.272  -41.838 0.00 65.71  ? 750  THR   A HG23 1 
ATOM   11009 N N    . ILE   A  1 725 ? 34.961 42.402  -41.044 1.00 49.25  ? 751  ILE   A N    1 
ATOM   11010 C CA   . ILE   A  1 725 ? 34.100 42.188  -42.194 1.00 51.69  ? 751  ILE   A CA   1 
ATOM   11011 C C    . ILE   A  1 725 ? 33.573 43.588  -42.527 1.00 54.38  ? 751  ILE   A C    1 
ATOM   11012 O O    . ILE   A  1 725 ? 32.832 44.161  -41.729 1.00 54.16  ? 751  ILE   A O    1 
ATOM   11013 C CB   . ILE   A  1 725 ? 32.967 41.160  -41.922 1.00 52.22  ? 751  ILE   A CB   1 
ATOM   11014 C CG1  . ILE   A  1 725 ? 33.544 39.807  -41.413 1.00 52.94  ? 751  ILE   A CG1  1 
ATOM   11015 C CG2  . ILE   A  1 725 ? 32.156 40.952  -43.205 1.00 52.74  ? 751  ILE   A CG2  1 
ATOM   11016 C CD1  . ILE   A  1 725 ? 32.509 38.792  -40.914 1.00 53.80  ? 751  ILE   A CD1  1 
ATOM   11017 H H    . ILE   A  1 725 ? 34.539 42.980  -40.324 0.00 69.01  ? 751  ILE   A H    1 
ATOM   11018 H HA   . ILE   A  1 725 ? 34.688 41.834  -43.040 0.00 71.23  ? 751  ILE   A HA   1 
ATOM   11019 H HB   . ILE   A  1 725 ? 32.308 41.564  -41.156 0.00 71.96  ? 751  ILE   A HB   1 
ATOM   11020 H HG12 . ILE   A  1 725 ? 34.090 39.338  -42.230 0.00 71.05  ? 751  ILE   A HG12 1 
ATOM   11021 H HG13 . ILE   A  1 725 ? 34.223 39.993  -40.582 0.00 71.37  ? 751  ILE   A HG13 1 
ATOM   11022 H HG21 . ILE   A  1 725 ? 31.425 40.158  -43.064 0.00 71.91  ? 751  ILE   A HG21 1 
ATOM   11023 H HG22 . ILE   A  1 725 ? 31.632 41.873  -43.455 0.00 73.12  ? 751  ILE   A HG22 1 
ATOM   11024 H HG23 . ILE   A  1 725 ? 32.839 40.696  -44.012 0.00 72.12  ? 751  ILE   A HG23 1 
ATOM   11025 H HD11 . ILE   A  1 725 ? 33.023 38.023  -40.339 0.00 71.29  ? 751  ILE   A HD11 1 
ATOM   11026 H HD12 . ILE   A  1 725 ? 31.781 39.304  -40.288 0.00 72.36  ? 751  ILE   A HD12 1 
ATOM   11027 H HD13 . ILE   A  1 725 ? 32.013 38.334  -41.768 0.00 71.77  ? 751  ILE   A HD13 1 
ATOM   11028 N N    . ASN   A  1 726 ? 34.026 44.169  -43.653 1.00 56.75  ? 752  ASN   A N    1 
ATOM   11029 C CA   . ASN   A  1 726 ? 33.643 45.527  -44.059 1.00 59.71  ? 752  ASN   A CA   1 
ATOM   11030 C C    . ASN   A  1 726 ? 32.192 45.594  -44.535 1.00 62.04  ? 752  ASN   A C    1 
ATOM   11031 O O    . ASN   A  1 726 ? 31.675 44.608  -45.055 1.00 62.09  ? 752  ASN   A O    1 
ATOM   11032 C CB   . ASN   A  1 726 ? 34.565 46.032  -45.181 1.00 61.74  ? 752  ASN   A CB   1 
ATOM   11033 C CG   . ASN   A  1 726 ? 36.017 46.172  -44.783 1.00 66.12  ? 752  ASN   A CG   1 
ATOM   11034 O OD1  . ASN   A  1 726 ? 36.357 46.302  -43.600 1.00 67.68  ? 752  ASN   A OD1  1 
ATOM   11035 N ND2  . ASN   A  1 726 ? 36.913 46.164  -45.769 1.00 67.09  ? 752  ASN   A ND2  1 
ATOM   11036 H H    . ASN   A  1 726 ? 34.651 43.713  -44.310 0.00 78.76  ? 752  ASN   A H    1 
ATOM   11037 H HA   . ASN   A  1 726 ? 33.745 46.198  -43.208 0.00 84.29  ? 752  ASN   A HA   1 
ATOM   11038 H HB2  . ASN   A  1 726 ? 34.509 45.336  -46.017 0.00 86.14  ? 752  ASN   A HB2  1 
ATOM   11039 H HB3  . ASN   A  1 726 ? 34.217 47.013  -45.501 0.00 87.46  ? 752  ASN   A HB3  1 
ATOM   11040 H HD21 . ASN   A  1 726 ? 37.901 46.254  -45.555 0.00 92.70  ? 752  ASN   A HD21 1 
ATOM   11041 H HD22 . ASN   A  1 726 ? 36.611 46.073  -46.734 0.00 92.78  ? 752  ASN   A HD22 1 
ATOM   11042 N N    . LYS   A  1 727 ? 31.560 46.779  -44.409 1.00 63.86  ? 753  LYS   A N    1 
ATOM   11043 C CA   . LYS   A  1 727 ? 30.171 47.014  -44.833 1.00 65.96  ? 753  LYS   A CA   1 
ATOM   11044 C C    . LYS   A  1 727 ? 29.948 46.596  -46.304 1.00 67.51  ? 753  LYS   A C    1 
ATOM   11045 O O    . LYS   A  1 727 ? 28.867 46.108  -46.629 1.00 67.89  ? 753  LYS   A O    1 
ATOM   11046 C CB   . LYS   A  1 727 ? 29.804 48.503  -44.645 1.00 68.47  ? 753  LYS   A CB   1 
ATOM   11047 C CG   . LYS   A  1 727 ? 28.309 48.820  -44.771 1.00 73.29  ? 753  LYS   A CG   1 
ATOM   11048 C CD   . LYS   A  1 727 ? 28.070 50.306  -45.033 1.00 78.07  ? 753  LYS   A CD   1 
ATOM   11049 C CE   . LYS   A  1 727 ? 26.609 50.645  -45.221 1.00 82.20  ? 753  LYS   A CE   1 
ATOM   11050 N NZ   . LYS   A  1 727 ? 25.884 50.770  -43.928 1.00 84.64  ? 753  LYS   A NZ   1 
ATOM   11051 H H    . LYS   A  1 727 ? 32.006 47.605  -44.024 0.00 90.79  ? 753  LYS   A H    1 
ATOM   11052 H HA   . LYS   A  1 727 ? 29.503 46.421  -44.209 0.00 92.95  ? 753  LYS   A HA   1 
ATOM   11053 H HB2  . LYS   A  1 727 ? 30.109 48.820  -43.649 0.00 97.73  ? 753  LYS   A HB2  1 
ATOM   11054 H HB3  . LYS   A  1 727 ? 30.333 49.086  -45.397 0.00 98.06  ? 753  LYS   A HB3  1 
ATOM   11055 H HG2  . LYS   A  1 727 ? 27.873 48.261  -45.597 0.00 103.81 ? 753  LYS   A HG2  1 
ATOM   11056 H HG3  . LYS   A  1 727 ? 27.810 48.558  -43.838 0.00 103.94 ? 753  LYS   A HG3  1 
ATOM   11057 H HD2  . LYS   A  1 727 ? 28.441 50.881  -44.185 0.00 111.52 ? 753  LYS   A HD2  1 
ATOM   11058 H HD3  . LYS   A  1 727 ? 28.599 50.597  -45.940 0.00 111.37 ? 753  LYS   A HD3  1 
ATOM   11059 H HE2  . LYS   A  1 727 ? 26.528 51.594  -45.748 0.00 117.79 ? 753  LYS   A HE2  1 
ATOM   11060 H HE3  . LYS   A  1 727 ? 26.132 49.856  -45.801 0.00 116.39 ? 753  LYS   A HE3  1 
ATOM   11061 H HZ1  . LYS   A  1 727 ? 24.900 50.953  -44.099 0.00 120.62 ? 753  LYS   A HZ1  1 
ATOM   11062 H HZ2  . LYS   A  1 727 ? 25.972 49.913  -43.391 0.00 119.34 ? 753  LYS   A HZ2  1 
ATOM   11063 H HZ3  . LYS   A  1 727 ? 26.271 51.538  -43.389 0.00 120.68 ? 753  LYS   A HZ3  1 
ATOM   11064 N N    . SER   A  1 728 ? 30.953 46.768  -47.185 1.00 68.24  ? 754  SER   A N    1 
ATOM   11065 C CA   . SER   A  1 728 ? 30.823 46.386  -48.594 1.00 69.61  ? 754  SER   A CA   1 
ATOM   11066 C C    . SER   A  1 728 ? 30.689 44.868  -48.810 1.00 70.89  ? 754  SER   A C    1 
ATOM   11067 O O    . SER   A  1 728 ? 30.023 44.453  -49.756 1.00 71.20  ? 754  SER   A O    1 
ATOM   11068 C CB   . SER   A  1 728 ? 32.008 46.910  -49.400 1.00 70.98  ? 754  SER   A CB   1 
ATOM   11069 O OG   . SER   A  1 728 ? 33.224 46.317  -48.975 1.00 73.25  ? 754  SER   A OG   1 
ATOM   11070 H H    . SER   A  1 728 ? 31.855 47.178  -46.962 0.00 96.05  ? 754  SER   A H    1 
ATOM   11071 H HA   . SER   A  1 728 ? 29.925 46.854  -48.996 0.00 98.16  ? 754  SER   A HA   1 
ATOM   11072 H HB2  . SER   A  1 728 ? 31.849 46.674  -50.451 0.00 99.46  ? 754  SER   A HB2  1 
ATOM   11073 H HB3  . SER   A  1 728 ? 32.076 47.989  -49.269 0.00 100.25 ? 754  SER   A HB3  1 
ATOM   11074 H HG   . SER   A  1 728 ? 33.975 46.645  -49.536 0.00 101.56 ? 754  SER   A HG   1 
ATOM   11075 N N    . ALA   A  1 729 ? 31.315 44.043  -47.954 1.00 71.42  ? 755  ALA   A N    1 
ATOM   11076 C CA   . ALA   A  1 729 ? 31.245 42.588  -48.089 1.00 72.56  ? 755  ALA   A CA   1 
ATOM   11077 C C    . ALA   A  1 729 ? 29.864 42.018  -47.744 1.00 73.69  ? 755  ALA   A C    1 
ATOM   11078 O O    . ALA   A  1 729 ? 29.452 41.033  -48.357 1.00 73.79  ? 755  ALA   A O    1 
ATOM   11079 C CB   . ALA   A  1 729 ? 32.301 41.935  -47.208 1.00 72.73  ? 755  ALA   A CB   1 
ATOM   11080 H H    . ALA   A  1 729 ? 31.884 44.346  -47.170 0.00 97.69  ? 755  ALA   A H    1 
ATOM   11081 H HA   . ALA   A  1 729 ? 31.469 42.316  -49.119 0.00 97.87  ? 755  ALA   A HA   1 
ATOM   11082 H HB1  . ALA   A  1 729 ? 32.255 40.855  -47.342 0.00 96.67  ? 755  ALA   A HB1  1 
ATOM   11083 H HB2  . ALA   A  1 729 ? 33.284 42.305  -47.496 0.00 97.50  ? 755  ALA   A HB2  1 
ATOM   11084 H HB3  . ALA   A  1 729 ? 32.101 42.187  -46.167 0.00 97.53  ? 755  ALA   A HB3  1 
ATOM   11085 N N    . LEU   A  1 730 ? 29.156 42.608  -46.763 1.00 74.37  ? 756  LEU   A N    1 
ATOM   11086 C CA   . LEU   A  1 730 ? 27.848 42.091  -46.349 1.00 75.51  ? 756  LEU   A CA   1 
ATOM   11087 C C    . LEU   A  1 730 ? 26.710 42.398  -47.349 1.00 76.37  ? 756  LEU   A C    1 
ATOM   11088 O O    . LEU   A  1 730 ? 26.031 41.468  -47.789 1.00 76.47  ? 756  LEU   A O    1 
ATOM   11089 C CB   . LEU   A  1 730 ? 27.437 42.637  -44.958 1.00 75.81  ? 756  LEU   A CB   1 
ATOM   11090 C CG   . LEU   A  1 730 ? 28.173 42.209  -43.672 1.00 77.19  ? 756  LEU   A CG   1 
ATOM   11091 C CD1  . LEU   A  1 730 ? 28.667 40.784  -43.722 1.00 77.86  ? 756  LEU   A CD1  1 
ATOM   11092 C CD2  . LEU   A  1 730 ? 29.246 43.189  -43.306 1.00 77.77  ? 756  LEU   A CD2  1 
ATOM   11093 H H    . LEU   A  1 730 ? 29.456 43.428  -46.245 0.00 101.01 ? 756  LEU   A H    1 
ATOM   11094 H HA   . LEU   A  1 730 ? 27.927 41.009  -46.260 0.00 101.03 ? 756  LEU   A HA   1 
ATOM   11095 H HB2  . LEU   A  1 730 ? 27.496 43.723  -45.003 0.00 103.34 ? 756  LEU   A HB2  1 
ATOM   11096 H HB3  . LEU   A  1 730 ? 26.394 42.359  -44.808 0.00 102.62 ? 756  LEU   A HB3  1 
ATOM   11097 H HG   . LEU   A  1 730 ? 27.450 42.237  -42.859 0.00 103.67 ? 756  LEU   A HG   1 
ATOM   11098 H HD11 . LEU   A  1 730 ? 28.987 40.479  -42.727 0.00 102.82 ? 756  LEU   A HD11 1 
ATOM   11099 H HD12 . LEU   A  1 730 ? 27.845 40.158  -44.064 0.00 102.99 ? 756  LEU   A HD12 1 
ATOM   11100 H HD13 . LEU   A  1 730 ? 29.505 40.722  -44.415 0.00 103.05 ? 756  LEU   A HD13 1 
ATOM   11101 H HD21 . LEU   A  1 730 ? 29.778 42.822  -42.430 0.00 104.19 ? 756  LEU   A HD21 1 
ATOM   11102 H HD22 . LEU   A  1 730 ? 29.931 43.298  -44.145 0.00 104.65 ? 756  LEU   A HD22 1 
ATOM   11103 H HD23 . LEU   A  1 730 ? 28.784 44.148  -43.078 0.00 105.48 ? 756  LEU   A HD23 1 
ATOM   11104 N N    . GLU   A  1 731 ? 26.465 43.693  -47.663 1.00 76.70  ? 757  GLU   A N    1 
ATOM   11105 C CA   . GLU   A  1 731 ? 25.352 44.095  -48.526 1.00 77.60  ? 757  GLU   A CA   1 
ATOM   11106 C C    . GLU   A  1 731 ? 25.811 44.719  -49.844 1.00 78.12  ? 757  GLU   A C    1 
ATOM   11107 O O    . GLU   A  1 731 ? 26.929 45.227  -49.935 1.00 78.29  ? 757  GLU   A O    1 
ATOM   11108 C CB   . GLU   A  1 731 ? 24.461 45.100  -47.776 1.00 80.05  ? 757  GLU   A CB   1 
ATOM   11109 C CG   . GLU   A  1 731 ? 23.813 44.552  -46.513 1.00 84.69  ? 757  GLU   A CG   1 
ATOM   11110 C CD   . GLU   A  1 731 ? 23.129 45.588  -45.640 1.00 90.90  ? 757  GLU   A CD   1 
ATOM   11111 O OE1  . GLU   A  1 731 ? 22.983 46.750  -46.086 1.00 92.20  ? 757  GLU   A OE1  1 
ATOM   11112 O OE2  . GLU   A  1 731 ? 22.737 45.237  -44.504 1.00 92.96  ? 757  GLU   A OE2  1 
ATOM   11113 H H    . GLU   A  1 731 ? 27.012 44.477  -47.320 0.00 105.41 ? 757  GLU   A H    1 
ATOM   11114 H HA   . GLU   A  1 731 ? 24.732 43.234  -48.769 0.00 106.50 ? 757  GLU   A HA   1 
ATOM   11115 H HB2  . GLU   A  1 731 ? 25.073 45.955  -47.494 0.00 111.22 ? 757  GLU   A HB2  1 
ATOM   11116 H HB3  . GLU   A  1 731 ? 23.664 45.425  -48.443 0.00 111.41 ? 757  GLU   A HB3  1 
ATOM   11117 H HG2  . GLU   A  1 731 ? 23.060 43.821  -46.803 0.00 115.60 ? 757  GLU   A HG2  1 
ATOM   11118 H HG3  . GLU   A  1 731 ? 24.572 44.069  -45.900 0.00 115.24 ? 757  GLU   A HG3  1 
ATOM   11119 N N    . THR   A  1 732 ? 24.941 44.675  -50.872 1.00 78.16  ? 758  THR   A N    1 
ATOM   11120 C CA   . THR   A  1 732 ? 25.209 45.273  -52.183 1.00 78.67  ? 758  THR   A CA   1 
ATOM   11121 C C    . THR   A  1 732 ? 23.863 45.738  -52.824 1.00 78.66  ? 758  THR   A C    1 
ATOM   11122 O O    . THR   A  1 732 ? 23.553 46.929  -52.749 1.00 78.96  ? 758  THR   A O    1 
ATOM   11123 C CB   . THR   A  1 732 ? 26.084 44.336  -53.059 1.00 80.33  ? 758  THR   A CB   1 
ATOM   11124 O OG1  . THR   A  1 732 ? 27.328 44.095  -52.400 1.00 81.49  ? 758  THR   A OG1  1 
ATOM   11125 C CG2  . THR   A  1 732 ? 26.337 44.906  -54.454 1.00 80.80  ? 758  THR   A CG2  1 
ATOM   11126 H H    . THR   A  1 732 ? 24.034 44.222  -50.818 0.00 108.53 ? 758  THR   A H    1 
ATOM   11127 H HA   . THR   A  1 732 ? 25.802 46.173  -52.026 0.00 110.31 ? 758  THR   A HA   1 
ATOM   11128 H HB   . THR   A  1 732 ? 25.566 43.385  -53.180 0.00 110.46 ? 758  THR   A HB   1 
ATOM   11129 H HG1  . THR   A  1 732 ? 27.825 44.946  -52.282 0.00 112.17 ? 758  THR   A HG1  1 
ATOM   11130 H HG21 . THR   A  1 732 ? 27.111 44.326  -54.953 0.00 111.63 ? 758  THR   A HG21 1 
ATOM   11131 H HG22 . THR   A  1 732 ? 25.428 44.858  -55.053 0.00 112.60 ? 758  THR   A HG22 1 
ATOM   11132 H HG23 . THR   A  1 732 ? 26.660 45.944  -54.381 0.00 112.90 ? 758  THR   A HG23 1 
ATOM   11133 N N    . LYS   A  1 733 ? 23.057 44.815  -53.409 1.00 78.17  ? 759  LYS   A N    1 
ATOM   11134 C CA   . LYS   A  1 733 ? 21.769 45.150  -54.039 1.00 78.17  ? 759  LYS   A CA   1 
ATOM   11135 C C    . LYS   A  1 733 ? 20.633 44.273  -53.483 1.00 77.61  ? 759  LYS   A C    1 
ATOM   11136 O O    . LYS   A  1 733 ? 19.577 44.797  -53.119 1.00 77.75  ? 759  LYS   A O    1 
ATOM   11137 C CB   . LYS   A  1 733 ? 21.850 45.060  -55.581 1.00 80.11  ? 759  LYS   A CB   1 
ATOM   11138 C CG   . LYS   A  1 733 ? 22.471 43.775  -56.137 1.00 84.39  ? 759  LYS   A CG   1 
ATOM   11139 C CD   . LYS   A  1 733 ? 22.479 43.753  -57.672 1.00 88.94  ? 759  LYS   A CD   1 
ATOM   11140 C CE   . LYS   A  1 733 ? 21.342 42.965  -58.290 1.00 92.68  ? 759  LYS   A CE   1 
ATOM   11141 N NZ   . LYS   A  1 733 ? 20.019 43.618  -58.091 1.00 94.95  ? 759  LYS   A NZ   1 
ATOM   11142 H H    . LYS   A  1 733 ? 23.294 43.829  -53.458 0.00 109.21 ? 759  LYS   A H    1 
ATOM   11143 H HA   . LYS   A  1 733 ? 21.515 46.184  -53.808 0.00 111.79 ? 759  LYS   A HA   1 
ATOM   11144 H HB2  . LYS   A  1 733 ? 20.841 45.138  -55.983 0.00 114.13 ? 759  LYS   A HB2  1 
ATOM   11145 H HB3  . LYS   A  1 733 ? 22.450 45.895  -55.941 0.00 113.98 ? 759  LYS   A HB3  1 
ATOM   11146 H HG2  . LYS   A  1 733 ? 23.505 43.699  -55.802 0.00 116.97 ? 759  LYS   A HG2  1 
ATOM   11147 H HG3  . LYS   A  1 733 ? 21.902 42.916  -55.788 0.00 117.09 ? 759  LYS   A HG3  1 
ATOM   11148 H HD2  . LYS   A  1 733 ? 22.404 44.776  -58.038 0.00 124.33 ? 759  LYS   A HD2  1 
ATOM   11149 H HD3  . LYS   A  1 733 ? 23.414 43.311  -58.013 0.00 122.82 ? 759  LYS   A HD3  1 
ATOM   11150 H HE2  . LYS   A  1 733 ? 21.513 42.881  -59.362 0.00 128.13 ? 759  LYS   A HE2  1 
ATOM   11151 H HE3  . LYS   A  1 733 ? 21.304 41.972  -57.844 0.00 127.06 ? 759  LYS   A HE3  1 
ATOM   11152 H HZ1  . LYS   A  1 733 ? 19.301 43.099  -58.588 0.00 131.65 ? 759  LYS   A HZ1  1 
ATOM   11153 H HZ2  . LYS   A  1 733 ? 19.782 43.633  -57.105 0.00 131.40 ? 759  LYS   A HZ2  1 
ATOM   11154 H HZ3  . LYS   A  1 733 ? 20.042 44.569  -58.445 0.00 132.43 ? 759  LYS   A HZ3  1 
ATOM   11155 N N    . THR   A  1 734 ? 20.859 42.952  -53.395 1.00 76.70  ? 760  THR   A N    1 
ATOM   11156 C CA   . THR   A  1 734 ? 19.890 42.003  -52.849 1.00 76.34  ? 760  THR   A CA   1 
ATOM   11157 C C    . THR   A  1 734 ? 20.420 41.536  -51.496 1.00 75.46  ? 760  THR   A C    1 
ATOM   11158 O O    . THR   A  1 734 ? 21.553 41.060  -51.432 1.00 75.74  ? 760  THR   A O    1 
ATOM   11159 C CB   . THR   A  1 734 ? 19.722 40.812  -53.800 1.00 77.75  ? 760  THR   A CB   1 
ATOM   11160 O OG1  . THR   A  1 734 ? 20.985 40.162  -53.972 1.00 78.79  ? 760  THR   A OG1  1 
ATOM   11161 C CG2  . THR   A  1 734 ? 19.145 41.219  -55.150 1.00 78.16  ? 760  THR   A CG2  1 
ATOM   11162 H H    . THR   A  1 734 ? 21.722 42.505  -53.688 0.00 107.08 ? 760  THR   A H    1 
ATOM   11163 H HA   . THR   A  1 734 ? 18.914 42.466  -52.710 0.00 107.50 ? 760  THR   A HA   1 
ATOM   11164 H HB   . THR   A  1 734 ? 19.027 40.105  -53.350 0.00 107.53 ? 760  THR   A HB   1 
ATOM   11165 H HG1  . THR   A  1 734 ? 20.889 39.386  -54.584 0.00 107.83 ? 760  THR   A HG1  1 
ATOM   11166 H HG21 . THR   A  1 734 ? 19.001 40.337  -55.772 0.00 108.79 ? 760  THR   A HG21 1 
ATOM   11167 H HG22 . THR   A  1 734 ? 18.185 41.714  -55.009 0.00 109.95 ? 760  THR   A HG22 1 
ATOM   11168 H HG23 . THR   A  1 734 ? 19.820 41.903  -55.662 0.00 109.59 ? 760  THR   A HG23 1 
ATOM   11169 N N    . THR   A  1 735 ? 19.630 41.679  -50.415 1.00 74.16  ? 761  THR   A N    1 
ATOM   11170 C CA   . THR   A  1 735 ? 20.075 41.260  -49.080 1.00 73.27  ? 761  THR   A CA   1 
ATOM   11171 C C    . THR   A  1 735 ? 20.384 39.747  -49.020 1.00 71.28  ? 761  THR   A C    1 
ATOM   11172 O O    . THR   A  1 735 ? 19.994 38.988  -49.907 1.00 71.64  ? 761  THR   A O    1 
ATOM   11173 C CB   . THR   A  1 735 ? 19.068 41.714  -47.987 1.00 75.05  ? 761  THR   A CB   1 
ATOM   11174 O OG1  . THR   A  1 735 ? 19.681 41.584  -46.695 1.00 76.31  ? 761  THR   A OG1  1 
ATOM   11175 C CG2  . THR   A  1 735 ? 17.769 40.913  -48.014 1.00 75.41  ? 761  THR   A CG2  1 
ATOM   11176 H H    . THR   A  1 735 ? 18.705 42.096  -50.428 0.00 103.86 ? 761  THR   A H    1 
ATOM   11177 H HA   . THR   A  1 735 ? 21.018 41.773  -48.893 0.00 101.47 ? 761  THR   A HA   1 
ATOM   11178 H HB   . THR   A  1 735 ? 18.818 42.762  -48.146 0.00 105.14 ? 761  THR   A HB   1 
ATOM   11179 H HG1  . THR   A  1 735 ? 19.258 42.208  -46.048 0.00 105.72 ? 761  THR   A HG1  1 
ATOM   11180 H HG21 . THR   A  1 735 ? 17.025 41.400  -47.385 0.00 105.26 ? 761  THR   A HG21 1 
ATOM   11181 H HG22 . THR   A  1 735 ? 17.390 40.845  -49.032 0.00 105.19 ? 761  THR   A HG22 1 
ATOM   11182 H HG23 . THR   A  1 735 ? 17.936 39.908  -47.628 0.00 103.90 ? 761  THR   A HG23 1 
ATOM   11183 N N    . THR   A  1 736 ? 21.093 39.326  -47.971 1.00 69.03  ? 762  THR   A N    1 
ATOM   11184 C CA   . THR   A  1 736 ? 21.538 37.943  -47.810 1.00 67.23  ? 762  THR   A CA   1 
ATOM   11185 C C    . THR   A  1 736 ? 20.421 36.916  -47.580 1.00 64.52  ? 762  THR   A C    1 
ATOM   11186 O O    . THR   A  1 736 ? 19.606 37.092  -46.674 1.00 64.83  ? 762  THR   A O    1 
ATOM   11187 C CB   . THR   A  1 736 ? 22.501 37.853  -46.611 1.00 68.90  ? 762  THR   A CB   1 
ATOM   11188 O OG1  . THR   A  1 736 ? 21.827 38.331  -45.440 1.00 70.10  ? 762  THR   A OG1  1 
ATOM   11189 C CG2  . THR   A  1 736 ? 23.779 38.655  -46.822 1.00 69.39  ? 762  THR   A CG2  1 
ATOM   11190 H H    . THR   A  1 736 ? 21.342 39.939  -47.201 0.00 94.70  ? 762  THR   A H    1 
ATOM   11191 H HA   . THR   A  1 736 ? 22.093 37.656  -48.702 0.00 90.94  ? 762  THR   A HA   1 
ATOM   11192 H HB   . THR   A  1 736 ? 22.786 36.812  -46.468 0.00 91.84  ? 762  THR   A HB   1 
ATOM   11193 H HG1  . THR   A  1 736 ? 21.369 37.593  -44.959 0.00 94.23  ? 762  THR   A HG1  1 
ATOM   11194 H HG21 . THR   A  1 736 ? 24.430 38.549  -45.956 0.00 92.77  ? 762  THR   A HG21 1 
ATOM   11195 H HG22 . THR   A  1 736 ? 24.311 38.280  -47.695 0.00 92.95  ? 762  THR   A HG22 1 
ATOM   11196 H HG23 . THR   A  1 736 ? 23.551 39.709  -46.966 0.00 94.02  ? 762  THR   A HG23 1 
ATOM   11197 N N    . LYS   A  1 737 ? 20.430 35.808  -48.346 1.00 61.56  ? 763  LYS   A N    1 
ATOM   11198 C CA   . LYS   A  1 737 ? 19.504 34.689  -48.103 1.00 59.07  ? 763  LYS   A CA   1 
ATOM   11199 C C    . LYS   A  1 737 ? 20.161 33.626  -47.155 1.00 55.38  ? 763  LYS   A C    1 
ATOM   11200 O O    . LYS   A  1 737 ? 19.655 32.510  -47.025 1.00 55.39  ? 763  LYS   A O    1 
ATOM   11201 C CB   . LYS   A  1 737 ? 19.026 34.055  -49.427 1.00 61.28  ? 763  LYS   A CB   1 
ATOM   11202 C CG   . LYS   A  1 737 ? 17.925 34.849  -50.137 1.00 66.38  ? 763  LYS   A CG   1 
ATOM   11203 C CD   . LYS   A  1 737 ? 18.408 36.197  -50.656 1.00 71.49  ? 763  LYS   A CD   1 
ATOM   11204 C CE   . LYS   A  1 737 ? 18.259 36.330  -52.147 1.00 75.57  ? 763  LYS   A CE   1 
ATOM   11205 N NZ   . LYS   A  1 737 ? 18.884 37.582  -52.643 1.00 78.32  ? 763  LYS   A NZ   1 
ATOM   11206 H H    . LYS   A  1 737 ? 21.065 35.655  -49.123 0.00 83.49  ? 763  LYS   A H    1 
ATOM   11207 H HA   . LYS   A  1 737 ? 18.623 35.052  -47.575 0.00 80.83  ? 763  LYS   A HA   1 
ATOM   11208 H HB2  . LYS   A  1 737 ? 19.867 33.967  -50.113 0.00 82.82  ? 763  LYS   A HB2  1 
ATOM   11209 H HB3  . LYS   A  1 737 ? 18.613 33.067  -49.229 0.00 82.62  ? 763  LYS   A HB3  1 
ATOM   11210 H HG2  . LYS   A  1 737 ? 17.558 34.271  -50.984 0.00 90.30  ? 763  LYS   A HG2  1 
ATOM   11211 H HG3  . LYS   A  1 737 ? 17.113 35.033  -49.435 0.00 90.60  ? 763  LYS   A HG3  1 
ATOM   11212 H HD2  . LYS   A  1 737 ? 17.822 36.987  -50.189 0.00 97.84  ? 763  LYS   A HD2  1 
ATOM   11213 H HD3  . LYS   A  1 737 ? 19.462 36.323  -50.415 0.00 96.76  ? 763  LYS   A HD3  1 
ATOM   11214 H HE2  . LYS   A  1 737 ? 18.753 35.490  -52.635 0.00 101.91 ? 763  LYS   A HE2  1 
ATOM   11215 H HE3  . LYS   A  1 737 ? 17.201 36.350  -52.404 0.00 103.11 ? 763  LYS   A HE3  1 
ATOM   11216 H HZ1  . LYS   A  1 737 ? 18.771 37.654  -53.650 0.00 106.82 ? 763  LYS   A HZ1  1 
ATOM   11217 H HZ2  . LYS   A  1 737 ? 18.444 38.382  -52.200 0.00 107.10 ? 763  LYS   A HZ2  1 
ATOM   11218 H HZ3  . LYS   A  1 737 ? 19.875 37.587  -52.422 0.00 105.99 ? 763  LYS   A HZ3  1 
ATOM   11219 N N    . LEU   A  1 738 ? 21.262 33.991  -46.464 1.00 52.02  ? 764  LEU   A N    1 
ATOM   11220 C CA   . LEU   A  1 738 ? 21.901 33.119  -45.500 1.00 49.16  ? 764  LEU   A CA   1 
ATOM   11221 C C    . LEU   A  1 738 ? 20.999 32.964  -44.286 1.00 46.07  ? 764  LEU   A C    1 
ATOM   11222 O O    . LEU   A  1 738 ? 20.288 33.894  -43.907 1.00 45.99  ? 764  LEU   A O    1 
ATOM   11223 C CB   . LEU   A  1 738 ? 23.226 33.719  -45.001 1.00 49.22  ? 764  LEU   A CB   1 
ATOM   11224 C CG   . LEU   A  1 738 ? 24.433 33.632  -45.917 1.00 50.45  ? 764  LEU   A CG   1 
ATOM   11225 C CD1  . LEU   A  1 738 ? 25.517 34.588  -45.449 1.00 50.82  ? 764  LEU   A CD1  1 
ATOM   11226 C CD2  . LEU   A  1 738 ? 24.974 32.212  -45.994 1.00 50.69  ? 764  LEU   A CD2  1 
ATOM   11227 H H    . LEU   A  1 738 ? 21.733 34.885  -46.560 0.00 70.86  ? 764  LEU   A H    1 
ATOM   11228 H HA   . LEU   A  1 738 ? 22.089 32.146  -45.947 0.00 65.60  ? 764  LEU   A HA   1 
ATOM   11229 H HB2  . LEU   A  1 738 ? 23.068 34.772  -44.771 0.00 66.64  ? 764  LEU   A HB2  1 
ATOM   11230 H HB3  . LEU   A  1 738 ? 23.492 33.204  -44.079 0.00 65.48  ? 764  LEU   A HB3  1 
ATOM   11231 H HG   . LEU   A  1 738 ? 24.136 33.928  -46.922 0.00 67.64  ? 764  LEU   A HG   1 
ATOM   11232 H HD11 . LEU   A  1 738 ? 26.393 34.475  -46.086 0.00 67.35  ? 764  LEU   A HD11 1 
ATOM   11233 H HD12 . LEU   A  1 738 ? 25.143 35.608  -45.521 0.00 68.49  ? 764  LEU   A HD12 1 
ATOM   11234 H HD13 . LEU   A  1 738 ? 25.770 34.357  -44.415 0.00 67.61  ? 764  LEU   A HD13 1 
ATOM   11235 H HD21 . LEU   A  1 738 ? 25.902 32.220  -46.563 0.00 66.36  ? 764  LEU   A HD21 1 
ATOM   11236 H HD22 . LEU   A  1 738 ? 25.163 31.845  -44.986 0.00 66.10  ? 764  LEU   A HD22 1 
ATOM   11237 H HD23 . LEU   A  1 738 ? 24.251 31.570  -46.495 0.00 66.48  ? 764  LEU   A HD23 1 
ATOM   11238 N N    . SER   A  1 739 ? 21.044 31.796  -43.678 1.00 43.43  ? 765  SER   A N    1 
ATOM   11239 C CA   . SER   A  1 739 ? 20.357 31.491  -42.431 1.00 41.77  ? 765  SER   A CA   1 
ATOM   11240 C C    . SER   A  1 739 ? 21.382 31.104  -41.332 1.00 40.03  ? 765  SER   A C    1 
ATOM   11241 O O    . SER   A  1 739 ? 21.024 31.150  -40.159 1.00 39.70  ? 765  SER   A O    1 
ATOM   11242 C CB   . SER   A  1 739 ? 19.334 30.380  -42.636 1.00 43.23  ? 765  SER   A CB   1 
ATOM   11243 O OG   . SER   A  1 739 ? 19.947 29.159  -43.013 1.00 45.39  ? 765  SER   A OG   1 
ATOM   11244 H H    . SER   A  1 739 ? 21.552 30.999  -44.048 0.00 58.00  ? 765  SER   A H    1 
ATOM   11245 H HA   . SER   A  1 739 ? 19.817 32.365  -42.070 0.00 57.14  ? 765  SER   A HA   1 
ATOM   11246 H HB2  . SER   A  1 739 ? 18.792 30.227  -41.704 0.00 58.02  ? 765  SER   A HB2  1 
ATOM   11247 H HB3  . SER   A  1 739 ? 18.641 30.684  -43.419 0.00 58.55  ? 765  SER   A HB3  1 
ATOM   11248 H HG   . SER   A  1 739 ? 19.256 28.455  -43.132 0.00 59.70  ? 765  SER   A HG   1 
ATOM   11249 N N    . MET   A  1 740 ? 22.647 30.740  -41.696 1.00 38.48  ? 766  MET   A N    1 
ATOM   11250 C CA   . MET   A  1 740 ? 23.694 30.407  -40.736 1.00 37.46  ? 766  MET   A CA   1 
ATOM   11251 C C    . MET   A  1 740 ? 25.061 30.871  -41.247 1.00 35.55  ? 766  MET   A C    1 
ATOM   11252 O O    . MET   A  1 740 ? 25.497 30.482  -42.331 1.00 35.23  ? 766  MET   A O    1 
ATOM   11253 C CB   . MET   A  1 740 ? 23.741 28.904  -40.446 1.00 39.03  ? 766  MET   A CB   1 
ATOM   11254 C CG   . MET   A  1 740 ? 24.774 28.551  -39.378 1.00 43.60  ? 766  MET   A CG   1 
ATOM   11255 S SD   . MET   A  1 740 ? 24.649 26.856  -38.802 1.00 55.28  ? 766  MET   A SD   1 
ATOM   11256 C CE   . MET   A  1 740 ? 23.197 26.978  -37.748 1.00 53.38  ? 766  MET   A CE   1 
ATOM   11257 H H    . MET   A  1 740 ? 22.969 30.659  -42.655 0.00 51.21  ? 766  MET   A H    1 
ATOM   11258 H HA   . MET   A  1 740 ? 23.487 30.905  -39.791 0.00 49.69  ? 766  MET   A HA   1 
ATOM   11259 H HB2  . MET   A  1 740 ? 22.761 28.579  -40.100 0.00 50.61  ? 766  MET   A HB2  1 
ATOM   11260 H HB3  . MET   A  1 740 ? 24.010 28.379  -41.361 0.00 50.24  ? 766  MET   A HB3  1 
ATOM   11261 H HG2  . MET   A  1 740 ? 25.778 28.677  -39.781 0.00 55.23  ? 766  MET   A HG2  1 
ATOM   11262 H HG3  . MET   A  1 740 ? 24.634 29.206  -38.520 0.00 55.72  ? 766  MET   A HG3  1 
ATOM   11263 H HE1  . MET   A  1 740 ? 23.117 26.072  -37.150 0.00 66.28  ? 766  MET   A HE1  1 
ATOM   11264 H HE2  . MET   A  1 740 ? 23.305 27.843  -37.095 0.00 67.06  ? 766  MET   A HE2  1 
ATOM   11265 H HE3  . MET   A  1 740 ? 22.310 27.090  -38.370 0.00 67.10  ? 766  MET   A HE3  1 
ATOM   11266 N N    . LEU   A  1 741 ? 25.743 31.664  -40.424 1.00 34.33  ? 767  LEU   A N    1 
ATOM   11267 C CA   . LEU   A  1 741 ? 27.060 32.196  -40.700 1.00 33.80  ? 767  LEU   A CA   1 
ATOM   11268 C C    . LEU   A  1 741 ? 27.917 31.873  -39.482 1.00 33.03  ? 767  LEU   A C    1 
ATOM   11269 O O    . LEU   A  1 741 ? 27.656 32.399  -38.398 1.00 33.29  ? 767  LEU   A O    1 
ATOM   11270 C CB   . LEU   A  1 741 ? 26.953 33.710  -40.927 1.00 33.81  ? 767  LEU   A CB   1 
ATOM   11271 C CG   . LEU   A  1 741 ? 28.254 34.491  -41.086 1.00 35.37  ? 767  LEU   A CG   1 
ATOM   11272 C CD1  . LEU   A  1 741 ? 29.091 33.961  -42.255 1.00 35.33  ? 767  LEU   A CD1  1 
ATOM   11273 C CD2  . LEU   A  1 741 ? 27.962 35.977  -41.265 1.00 36.21  ? 767  LEU   A CD2  1 
ATOM   11274 H H    . LEU   A  1 741 ? 25.396 31.968  -39.520 0.00 45.91  ? 767  LEU   A H    1 
ATOM   11275 H HA   . LEU   A  1 741 ? 27.499 31.733  -41.583 0.00 44.75  ? 767  LEU   A HA   1 
ATOM   11276 H HB2  . LEU   A  1 741 ? 26.371 33.876  -41.832 0.00 46.29  ? 767  LEU   A HB2  1 
ATOM   11277 H HB3  . LEU   A  1 741 ? 26.425 34.142  -40.078 0.00 46.30  ? 767  LEU   A HB3  1 
ATOM   11278 H HG   . LEU   A  1 741 ? 28.843 34.396  -40.176 0.00 47.72  ? 767  LEU   A HG   1 
ATOM   11279 H HD11 . LEU   A  1 741 ? 29.941 34.624  -42.410 0.00 47.72  ? 767  LEU   A HD11 1 
ATOM   11280 H HD12 . LEU   A  1 741 ? 29.447 32.960  -42.017 0.00 46.84  ? 767  LEU   A HD12 1 
ATOM   11281 H HD13 . LEU   A  1 741 ? 28.472 33.935  -43.150 0.00 47.73  ? 767  LEU   A HD13 1 
ATOM   11282 H HD21 . LEU   A  1 741 ? 28.899 36.511  -41.414 0.00 50.08  ? 767  LEU   A HD21 1 
ATOM   11283 H HD22 . LEU   A  1 741 ? 27.318 36.109  -42.133 0.00 50.28  ? 767  LEU   A HD22 1 
ATOM   11284 H HD23 . LEU   A  1 741 ? 27.462 36.349  -40.372 0.00 50.26  ? 767  LEU   A HD23 1 
ATOM   11285 N N    . GLU   A  1 742 ? 28.895 30.973  -39.637 1.00 31.48  ? 768  GLU   A N    1 
ATOM   11286 C CA   . GLU   A  1 742 ? 29.792 30.601  -38.545 1.00 30.48  ? 768  GLU   A CA   1 
ATOM   11287 C C    . GLU   A  1 742 ? 31.066 31.435  -38.659 1.00 29.42  ? 768  GLU   A C    1 
ATOM   11288 O O    . GLU   A  1 742 ? 31.614 31.575  -39.758 1.00 29.14  ? 768  GLU   A O    1 
ATOM   11289 C CB   . GLU   A  1 742 ? 30.123 29.102  -38.564 1.00 32.17  ? 768  GLU   A CB   1 
ATOM   11290 C CG   . GLU   A  1 742 ? 28.912 28.214  -38.809 1.00 35.14  ? 768  GLU   A CG   1 
ATOM   11291 C CD   . GLU   A  1 742 ? 29.153 26.742  -38.548 1.00 39.16  ? 768  GLU   A CD   1 
ATOM   11292 O OE1  . GLU   A  1 742 ? 29.575 26.406  -37.419 1.00 38.23  ? 768  GLU   A OE1  1 
ATOM   11293 O OE2  . GLU   A  1 742 ? 28.903 25.923  -39.462 1.00 42.11  ? 768  GLU   A OE2  1 
ATOM   11294 H H    . GLU   A  1 742 ? 29.100 30.494  -40.509 0.00 40.84  ? 768  GLU   A H    1 
ATOM   11295 H HA   . GLU   A  1 742 ? 29.322 30.809  -37.585 0.00 39.62  ? 768  GLU   A HA   1 
ATOM   11296 H HB2  . GLU   A  1 742 ? 30.870 28.901  -39.329 0.00 40.44  ? 768  GLU   A HB2  1 
ATOM   11297 H HB3  . GLU   A  1 742 ? 30.532 28.841  -37.589 0.00 40.40  ? 768  GLU   A HB3  1 
ATOM   11298 H HG2  . GLU   A  1 742 ? 28.103 28.539  -38.157 0.00 44.33  ? 768  GLU   A HG2  1 
ATOM   11299 H HG3  . GLU   A  1 742 ? 28.609 28.312  -39.850 0.00 44.19  ? 768  GLU   A HG3  1 
ATOM   11300 N N    . LEU   A  1 743 ? 31.497 32.040  -37.538 1.00 28.59  ? 769  LEU   A N    1 
ATOM   11301 C CA   . LEU   A  1 743 ? 32.671 32.908  -37.503 1.00 28.75  ? 769  LEU   A CA   1 
ATOM   11302 C C    . LEU   A  1 743 ? 33.547 32.741  -36.250 1.00 28.41  ? 769  LEU   A C    1 
ATOM   11303 O O    . LEU   A  1 743 ? 34.491 33.512  -36.092 1.00 28.55  ? 769  LEU   A O    1 
ATOM   11304 C CB   . LEU   A  1 743 ? 32.192 34.362  -37.564 1.00 28.95  ? 769  LEU   A CB   1 
ATOM   11305 C CG   . LEU   A  1 743 ? 31.588 34.822  -38.886 1.00 30.21  ? 769  LEU   A CG   1 
ATOM   11306 C CD1  . LEU   A  1 743 ? 30.764 36.073  -38.669 1.00 31.48  ? 769  LEU   A CD1  1 
ATOM   11307 C CD2  . LEU   A  1 743 ? 32.661 35.100  -39.917 1.00 30.52  ? 769  LEU   A CD2  1 
ATOM   11308 H H    . LEU   A  1 743 ? 31.030 31.960  -36.640 0.00 37.63  ? 769  LEU   A H    1 
ATOM   11309 H HA   . LEU   A  1 743 ? 33.311 32.713  -38.361 0.00 37.89  ? 769  LEU   A HA   1 
ATOM   11310 H HB2  . LEU   A  1 743 ? 31.433 34.497  -36.796 0.00 39.44  ? 769  LEU   A HB2  1 
ATOM   11311 H HB3  . LEU   A  1 743 ? 33.028 35.028  -37.359 0.00 39.49  ? 769  LEU   A HB3  1 
ATOM   11312 H HG   . LEU   A  1 743 ? 30.935 34.046  -39.281 0.00 40.84  ? 769  LEU   A HG   1 
ATOM   11313 H HD11 . LEU   A  1 743 ? 30.399 36.433  -39.630 0.00 43.92  ? 769  LEU   A HD11 1 
ATOM   11314 H HD12 . LEU   A  1 743 ? 29.922 35.836  -38.022 0.00 43.59  ? 769  LEU   A HD12 1 
ATOM   11315 H HD13 . LEU   A  1 743 ? 31.390 36.831  -38.201 0.00 43.93  ? 769  LEU   A HD13 1 
ATOM   11316 H HD21 . LEU   A  1 743 ? 32.189 35.470  -40.826 0.00 41.88  ? 769  LEU   A HD21 1 
ATOM   11317 H HD22 . LEU   A  1 743 ? 33.346 35.851  -39.528 0.00 41.90  ? 769  LEU   A HD22 1 
ATOM   11318 H HD23 . LEU   A  1 743 ? 33.202 34.182  -40.138 0.00 40.93  ? 769  LEU   A HD23 1 
ATOM   11319 N N    . HIS   A  1 744 ? 33.254 31.776  -35.369 1.00 28.10  ? 770  HIS   A N    1 
ATOM   11320 C CA   . HIS   A  1 744 ? 34.065 31.578  -34.164 1.00 28.48  ? 770  HIS   A CA   1 
ATOM   11321 C C    . HIS   A  1 744 ? 35.503 31.200  -34.524 1.00 27.96  ? 770  HIS   A C    1 
ATOM   11322 O O    . HIS   A  1 744 ? 35.719 30.548  -35.529 1.00 27.29  ? 770  HIS   A O    1 
ATOM   11323 C CB   . HIS   A  1 744 ? 33.446 30.509  -33.248 1.00 29.15  ? 770  HIS   A CB   1 
ATOM   11324 C CG   . HIS   A  1 744 ? 33.487 29.111  -33.786 1.00 31.16  ? 770  HIS   A CG   1 
ATOM   11325 N ND1  . HIS   A  1 744 ? 32.435 28.587  -34.514 1.00 33.06  ? 770  HIS   A ND1  1 
ATOM   11326 C CD2  . HIS   A  1 744 ? 34.437 28.157  -33.651 1.00 32.37  ? 770  HIS   A CD2  1 
ATOM   11327 C CE1  . HIS   A  1 744 ? 32.783 27.343  -34.809 1.00 33.13  ? 770  HIS   A CE1  1 
ATOM   11328 N NE2  . HIS   A  1 744 ? 33.984 27.047  -34.320 1.00 33.52  ? 770  HIS   A NE2  1 
ATOM   11329 H H    . HIS   A  1 744 ? 32.472 31.134  -35.444 0.00 36.33  ? 770  HIS   A H    1 
ATOM   11330 H HA   . HIS   A  1 744 ? 34.103 32.511  -33.605 0.00 37.35  ? 770  HIS   A HA   1 
ATOM   11331 H HB2  . HIS   A  1 744 ? 33.998 30.511  -32.310 0.00 37.14  ? 770  HIS   A HB2  1 
ATOM   11332 H HB3  . HIS   A  1 744 ? 32.404 30.766  -33.062 0.00 37.44  ? 770  HIS   A HB3  1 
ATOM   11333 H HD2  . HIS   A  1 744 ? 35.370 28.251  -33.120 0.00 39.70  ? 770  HIS   A HD2  1 
ATOM   11334 H HE1  . HIS   A  1 744 ? 32.173 26.659  -35.374 0.00 40.19  ? 770  HIS   A HE1  1 
ATOM   11335 H HE2  . HIS   A  1 744 ? 34.473 26.163  -34.421 0.00 40.17  ? 770  HIS   A HE2  1 
ATOM   11336 N N    . GLY   A  1 745 ? 36.464 31.641  -33.728 1.00 27.71  ? 771  GLY   A N    1 
ATOM   11337 C CA   . GLY   A  1 745 ? 37.871 31.331  -33.964 1.00 28.09  ? 771  GLY   A CA   1 
ATOM   11338 C C    . GLY   A  1 745 ? 38.621 32.283  -34.877 1.00 28.41  ? 771  GLY   A C    1 
ATOM   11339 O O    . GLY   A  1 745 ? 39.788 32.026  -35.173 1.00 29.37  ? 771  GLY   A O    1 
ATOM   11340 H H    . GLY   A  1 745 ? 36.308 32.213  -32.905 0.00 36.08  ? 771  GLY   A H    1 
ATOM   11341 H HA2  . GLY   A  1 745 ? 38.384 31.338  -33.003 0.00 35.93  ? 771  GLY   A HA2  1 
ATOM   11342 H HA3  . GLY   A  1 745 ? 37.965 30.326  -34.372 0.00 35.36  ? 771  GLY   A HA3  1 
ATOM   11343 N N    . ASN   A  1 746 ? 37.997 33.395  -35.325 1.00 27.87  ? 772  ASN   A N    1 
ATOM   11344 C CA   . ASN   A  1 746 ? 38.692 34.367  -36.179 1.00 27.29  ? 772  ASN   A CA   1 
ATOM   11345 C C    . ASN   A  1 746 ? 39.328 35.441  -35.295 1.00 28.18  ? 772  ASN   A C    1 
ATOM   11346 O O    . ASN   A  1 746 ? 38.722 35.860  -34.309 1.00 28.53  ? 772  ASN   A O    1 
ATOM   11347 C CB   . ASN   A  1 746 ? 37.738 35.013  -37.188 1.00 27.13  ? 772  ASN   A CB   1 
ATOM   11348 C CG   . ASN   A  1 746 ? 37.434 34.119  -38.368 1.00 27.26  ? 772  ASN   A CG   1 
ATOM   11349 O OD1  . ASN   A  1 746 ? 38.243 34.012  -39.291 1.00 26.41  ? 772  ASN   A OD1  1 
ATOM   11350 N ND2  . ASN   A  1 746 ? 36.290 33.438  -38.349 1.00 25.66  ? 772  ASN   A ND2  1 
ATOM   11351 H H    . ASN   A  1 746 ? 37.044 33.664  -35.101 0.00 36.93  ? 772  ASN   A H    1 
ATOM   11352 H HA   . ASN   A  1 746 ? 39.475 33.856  -36.737 0.00 36.17  ? 772  ASN   A HA   1 
ATOM   11353 H HB2  . ASN   A  1 746 ? 36.804 35.282  -36.696 0.00 36.99  ? 772  ASN   A HB2  1 
ATOM   11354 H HB3  . ASN   A  1 746 ? 38.212 35.911  -37.578 0.00 37.25  ? 772  ASN   A HB3  1 
ATOM   11355 H HD21 . ASN   A  1 746 ? 36.057 32.824  -39.123 0.00 33.92  ? 772  ASN   A HD21 1 
ATOM   11356 H HD22 . ASN   A  1 746 ? 35.655 33.517  -37.561 0.00 34.32  ? 772  ASN   A HD22 1 
ATOM   11357 N N    . PRO   A  1 747 ? 40.554 35.895  -35.611 1.00 28.61  ? 773  PRO   A N    1 
ATOM   11358 C CA   . PRO   A  1 747 ? 41.208 36.903  -34.764 1.00 29.06  ? 773  PRO   A CA   1 
ATOM   11359 C C    . PRO   A  1 747 ? 40.690 38.320  -35.038 1.00 29.43  ? 773  PRO   A C    1 
ATOM   11360 O O    . PRO   A  1 747 ? 41.370 39.135  -35.646 1.00 29.50  ? 773  PRO   A O    1 
ATOM   11361 C CB   . PRO   A  1 747 ? 42.679 36.720  -35.135 1.00 29.76  ? 773  PRO   A CB   1 
ATOM   11362 C CG   . PRO   A  1 747 ? 42.636 36.397  -36.592 1.00 29.96  ? 773  PRO   A CG   1 
ATOM   11363 C CD   . PRO   A  1 747 ? 41.426 35.500  -36.738 1.00 28.25  ? 773  PRO   A CD   1 
ATOM   11364 H HA   . PRO   A  1 747 ? 41.085 36.668  -33.708 0.00 40.00  ? 773  PRO   A HA   1 
ATOM   11365 H HB2  . PRO   A  1 747 ? 43.255 37.620  -34.935 0.00 41.37  ? 773  PRO   A HB2  1 
ATOM   11366 H HB3  . PRO   A  1 747 ? 43.090 35.882  -34.574 0.00 40.33  ? 773  PRO   A HB3  1 
ATOM   11367 H HG2  . PRO   A  1 747 ? 42.512 37.308  -37.174 0.00 41.33  ? 773  PRO   A HG2  1 
ATOM   11368 H HG3  . PRO   A  1 747 ? 43.545 35.872  -36.880 0.00 40.47  ? 773  PRO   A HG3  1 
ATOM   11369 H HD2  . PRO   A  1 747 ? 40.920 35.692  -37.682 0.00 38.34  ? 773  PRO   A HD2  1 
ATOM   11370 H HD3  . PRO   A  1 747 ? 41.722 34.457  -36.643 0.00 37.61  ? 773  PRO   A HD3  1 
ATOM   11371 N N    . PHE   A  1 748 ? 39.447 38.586  -34.645 1.00 29.85  ? 774  PHE   A N    1 
ATOM   11372 C CA   . PHE   A  1 748 ? 38.806 39.878  -34.891 1.00 30.85  ? 774  PHE   A CA   1 
ATOM   11373 C C    . PHE   A  1 748 ? 39.512 41.050  -34.189 1.00 31.75  ? 774  PHE   A C    1 
ATOM   11374 O O    . PHE   A  1 748 ? 39.979 40.900  -33.066 1.00 30.78  ? 774  PHE   A O    1 
ATOM   11375 C CB   . PHE   A  1 748 ? 37.328 39.831  -34.450 1.00 30.87  ? 774  PHE   A CB   1 
ATOM   11376 C CG   . PHE   A  1 748 ? 36.424 39.095  -35.412 1.00 31.79  ? 774  PHE   A CG   1 
ATOM   11377 C CD1  . PHE   A  1 748 ? 36.075 39.657  -36.624 1.00 33.27  ? 774  PHE   A CD1  1 
ATOM   11378 C CD2  . PHE   A  1 748 ? 35.911 37.853  -35.095 1.00 32.69  ? 774  PHE   A CD2  1 
ATOM   11379 C CE1  . PHE   A  1 748 ? 35.276 38.965  -37.525 1.00 34.15  ? 774  PHE   A CE1  1 
ATOM   11380 C CE2  . PHE   A  1 748 ? 35.085 37.179  -35.986 1.00 33.73  ? 774  PHE   A CE2  1 
ATOM   11381 C CZ   . PHE   A  1 748 ? 34.794 37.726  -37.204 1.00 33.71  ? 774  PHE   A CZ   1 
ATOM   11382 H H    . PHE   A  1 748 ? 38.859 37.917  -34.160 0.00 41.80  ? 774  PHE   A H    1 
ATOM   11383 H HA   . PHE   A  1 748 ? 38.843 40.069  -35.962 0.00 44.35  ? 774  PHE   A HA   1 
ATOM   11384 H HB2  . PHE   A  1 748 ? 37.253 39.357  -33.472 0.00 44.12  ? 774  PHE   A HB2  1 
ATOM   11385 H HB3  . PHE   A  1 748 ? 36.961 40.854  -34.381 0.00 45.13  ? 774  PHE   A HB3  1 
ATOM   11386 H HD1  . PHE   A  1 748 ? 36.470 40.622  -36.896 0.00 47.83  ? 774  PHE   A HD1  1 
ATOM   11387 H HD2  . PHE   A  1 748 ? 36.164 37.392  -34.156 0.00 45.08  ? 774  PHE   A HD2  1 
ATOM   11388 H HE1  . PHE   A  1 748 ? 35.021 39.413  -38.470 0.00 48.24  ? 774  PHE   A HE1  1 
ATOM   11389 H HE2  . PHE   A  1 748 ? 34.727 36.194  -35.747 0.00 45.69  ? 774  PHE   A HE2  1 
ATOM   11390 H HZ   . PHE   A  1 748 ? 34.148 37.205  -37.889 0.00 46.39  ? 774  PHE   A HZ   1 
ATOM   11391 N N    . GLU   A  1 749 ? 39.583 42.205  -34.884 1.00 32.85  ? 775  GLU   A N    1 
ATOM   11392 C CA   . GLU   A  1 749 ? 40.145 43.459  -34.412 1.00 34.96  ? 775  GLU   A CA   1 
ATOM   11393 C C    . GLU   A  1 749 ? 38.944 44.229  -33.873 1.00 36.55  ? 775  GLU   A C    1 
ATOM   11394 O O    . GLU   A  1 749 ? 38.038 44.563  -34.637 1.00 36.52  ? 775  GLU   A O    1 
ATOM   11395 C CB   . GLU   A  1 749 ? 40.809 44.224  -35.566 1.00 37.79  ? 775  GLU   A CB   1 
ATOM   11396 C CG   . GLU   A  1 749 ? 41.581 45.453  -35.103 1.00 44.22  ? 775  GLU   A CG   1 
ATOM   11397 C CD   . GLU   A  1 749 ? 42.623 45.994  -36.064 1.00 52.01  ? 775  GLU   A CD   1 
ATOM   11398 O OE1  . GLU   A  1 749 ? 43.081 47.140  -35.848 1.00 54.03  ? 775  GLU   A OE1  1 
ATOM   11399 O OE2  . GLU   A  1 749 ? 42.993 45.279  -37.023 1.00 54.21  ? 775  GLU   A OE2  1 
ATOM   11400 H H    . GLU   A  1 749 ? 39.228 42.293  -35.831 0.00 48.28  ? 775  GLU   A H    1 
ATOM   11401 H HA   . GLU   A  1 749 ? 40.874 43.297  -33.620 0.00 51.56  ? 775  GLU   A HA   1 
ATOM   11402 H HB2  . GLU   A  1 749 ? 41.494 43.545  -36.069 0.00 55.00  ? 775  GLU   A HB2  1 
ATOM   11403 H HB3  . GLU   A  1 749 ? 40.045 44.554  -36.268 0.00 55.81  ? 775  GLU   A HB3  1 
ATOM   11404 H HG2  . GLU   A  1 749 ? 40.866 46.254  -34.920 0.00 64.84  ? 775  GLU   A HG2  1 
ATOM   11405 H HG3  . GLU   A  1 749 ? 42.097 45.211  -34.175 0.00 64.03  ? 775  GLU   A HG3  1 
ATOM   11406 N N    . CYS   A  1 750 ? 38.902 44.433  -32.558 1.00 37.39  ? 776  CYS   A N    1 
ATOM   11407 C CA   . CYS   A  1 750 ? 37.788 45.085  -31.894 1.00 38.50  ? 776  CYS   A CA   1 
ATOM   11408 C C    . CYS   A  1 750 ? 38.049 46.534  -31.592 1.00 39.93  ? 776  CYS   A C    1 
ATOM   11409 O O    . CYS   A  1 750 ? 38.223 46.931  -30.445 1.00 40.39  ? 776  CYS   A O    1 
ATOM   11410 C CB   . CYS   A  1 750 ? 37.384 44.303  -30.653 1.00 38.57  ? 776  CYS   A CB   1 
ATOM   11411 S SG   . CYS   A  1 750 ? 36.627 42.705  -31.035 1.00 40.90  ? 776  CYS   A SG   1 
ATOM   11412 H H    . CYS   A  1 750 ? 39.643 44.161  -31.920 0.00 55.30  ? 776  CYS   A H    1 
ATOM   11413 H HA   . CYS   A  1 750 ? 36.918 45.062  -32.547 0.00 57.47  ? 776  CYS   A HA   1 
ATOM   11414 H HB2  . CYS   A  1 750 ? 38.269 44.113  -30.046 0.00 56.95  ? 776  CYS   A HB2  1 
ATOM   11415 H HB3  . CYS   A  1 750 ? 36.664 44.879  -30.075 0.00 57.66  ? 776  CYS   A HB3  1 
ATOM   11416 N N    . THR   A  1 751 ? 38.061 47.317  -32.658 1.00 40.55  ? 777  THR   A N    1 
ATOM   11417 C CA   . THR   A  1 751 ? 38.153 48.772  -32.669 1.00 41.70  ? 777  THR   A CA   1 
ATOM   11418 C C    . THR   A  1 751 ? 36.801 49.242  -33.283 1.00 42.74  ? 777  THR   A C    1 
ATOM   11419 O O    . THR   A  1 751 ? 35.934 48.400  -33.562 1.00 42.32  ? 777  THR   A O    1 
ATOM   11420 C CB   . THR   A  1 751 ? 39.383 49.196  -33.507 1.00 42.91  ? 777  THR   A CB   1 
ATOM   11421 O OG1  . THR   A  1 751 ? 39.198 48.729  -34.846 1.00 43.47  ? 777  THR   A OG1  1 
ATOM   11422 C CG2  . THR   A  1 751 ? 40.692 48.661  -32.937 1.00 43.37  ? 777  THR   A CG2  1 
ATOM   11423 H H    . THR   A  1 751 ? 38.004 46.939  -33.599 0.00 61.24  ? 777  THR   A H    1 
ATOM   11424 H HA   . THR   A  1 751 ? 38.248 49.178  -31.663 0.00 64.59  ? 777  THR   A HA   1 
ATOM   11425 H HB   . THR   A  1 751 ? 39.442 50.283  -33.521 0.00 66.74  ? 777  THR   A HB   1 
ATOM   11426 H HG1  . THR   A  1 751 ? 39.979 48.979  -35.405 0.00 66.16  ? 777  THR   A HG1  1 
ATOM   11427 H HG21 . THR   A  1 751 ? 41.531 49.063  -33.501 0.00 66.14  ? 777  THR   A HG21 1 
ATOM   11428 H HG22 . THR   A  1 751 ? 40.793 48.956  -31.893 0.00 66.25  ? 777  THR   A HG22 1 
ATOM   11429 H HG23 . THR   A  1 751 ? 40.714 47.574  -33.000 0.00 65.01  ? 777  THR   A HG23 1 
ATOM   11430 N N    . CYS   A  1 752 ? 36.609 50.552  -33.507 1.00 43.87  ? 778  CYS   A N    1 
ATOM   11431 C CA   . CYS   A  1 752 ? 35.387 51.034  -34.151 1.00 45.54  ? 778  CYS   A CA   1 
ATOM   11432 C C    . CYS   A  1 752 ? 35.223 50.462  -35.593 1.00 47.10  ? 778  CYS   A C    1 
ATOM   11433 O O    . CYS   A  1 752 ? 34.117 50.477  -36.119 1.00 47.70  ? 778  CYS   A O    1 
ATOM   11434 C CB   . CYS   A  1 752 ? 35.336 52.558  -34.114 1.00 46.34  ? 778  CYS   A CB   1 
ATOM   11435 S SG   . CYS   A  1 752 ? 35.267 53.231  -32.430 1.00 49.34  ? 778  CYS   A SG   1 
ATOM   11436 H H    . CYS   A  1 752 ? 37.266 51.284  -33.256 0.00 68.98  ? 778  CYS   A H    1 
ATOM   11437 H HA   . CYS   A  1 752 ? 34.537 50.680  -33.569 0.00 70.79  ? 778  CYS   A HA   1 
ATOM   11438 H HB2  . CYS   A  1 752 ? 36.227 52.955  -34.597 0.00 73.48  ? 778  CYS   A HB2  1 
ATOM   11439 H HB3  . CYS   A  1 752 ? 34.447 52.891  -34.647 0.00 73.68  ? 778  CYS   A HB3  1 
ATOM   11440 H HG   . CYS   A  1 752 ? 35.230 54.566  -32.500 0.00 78.86  ? 778  CYS   A HG   1 
ATOM   11441 N N    . ASP   A  1 753 ? 36.284 49.852  -36.173 1.00 47.68  ? 779  ASP   A N    1 
ATOM   11442 C CA   . ASP   A  1 753 ? 36.223 49.211  -37.488 1.00 48.77  ? 779  ASP   A CA   1 
ATOM   11443 C C    . ASP   A  1 753 ? 35.292 47.979  -37.499 1.00 48.76  ? 779  ASP   A C    1 
ATOM   11444 O O    . ASP   A  1 753 ? 34.844 47.581  -38.570 1.00 49.31  ? 779  ASP   A O    1 
ATOM   11445 C CB   . ASP   A  1 753 ? 37.630 48.802  -37.959 1.00 51.72  ? 779  ASP   A CB   1 
ATOM   11446 C CG   . ASP   A  1 753 ? 38.598 49.953  -38.160 1.00 58.94  ? 779  ASP   A CG   1 
ATOM   11447 O OD1  . ASP   A  1 753 ? 39.815 49.749  -37.943 1.00 60.61  ? 779  ASP   A OD1  1 
ATOM   11448 O OD2  . ASP   A  1 753 ? 38.140 51.062  -38.528 1.00 61.41  ? 779  ASP   A OD2  1 
ATOM   11449 H H    . ASP   A  1 753 ? 37.201 49.782  -35.745 0.00 72.13  ? 779  ASP   A H    1 
ATOM   11450 H HA   . ASP   A  1 753 ? 35.822 49.926  -38.204 0.00 73.70  ? 779  ASP   A HA   1 
ATOM   11451 H HB2  . ASP   A  1 753 ? 38.068 48.138  -37.215 0.00 75.51  ? 779  ASP   A HB2  1 
ATOM   11452 H HB3  . ASP   A  1 753 ? 37.539 48.280  -38.910 0.00 75.66  ? 779  ASP   A HB3  1 
ATOM   11453 N N    . ILE   A  1 754 ? 35.018 47.356  -36.339 1.00 48.01  ? 780  ILE   A N    1 
ATOM   11454 C CA   . ILE   A  1 754 ? 34.067 46.229  -36.282 1.00 47.51  ? 780  ILE   A CA   1 
ATOM   11455 C C    . ILE   A  1 754 ? 32.589 46.726  -36.191 1.00 46.76  ? 780  ILE   A C    1 
ATOM   11456 O O    . ILE   A  1 754 ? 31.683 45.901  -36.271 1.00 46.72  ? 780  ILE   A O    1 
ATOM   11457 C CB   . ILE   A  1 754 ? 34.409 45.249  -35.110 1.00 47.79  ? 780  ILE   A CB   1 
ATOM   11458 C CG1  . ILE   A  1 754 ? 33.831 43.831  -35.341 1.00 48.92  ? 780  ILE   A CG1  1 
ATOM   11459 C CG2  . ILE   A  1 754 ? 33.906 45.791  -33.784 1.00 48.12  ? 780  ILE   A CG2  1 
ATOM   11460 C CD1  . ILE   A  1 754 ? 34.551 43.015  -36.363 1.00 50.42  ? 780  ILE   A CD1  1 
ATOM   11461 H H    . ILE   A  1 754 ? 35.432 47.582  -35.440 0.00 70.92  ? 780  ILE   A H    1 
ATOM   11462 H HA   . ILE   A  1 754 ? 34.149 45.673  -37.214 0.00 68.95  ? 780  ILE   A HA   1 
ATOM   11463 H HB   . ILE   A  1 754 ? 35.490 45.141  -35.030 0.00 68.73  ? 780  ILE   A HB   1 
ATOM   11464 H HG12 . ILE   A  1 754 ? 33.877 43.285  -34.400 0.00 68.91  ? 780  ILE   A HG12 1 
ATOM   11465 H HG13 . ILE   A  1 754 ? 32.793 43.915  -35.660 0.00 69.51  ? 780  ILE   A HG13 1 
ATOM   11466 H HG21 . ILE   A  1 754 ? 34.449 45.293  -32.981 0.00 69.47  ? 780  ILE   A HG21 1 
ATOM   11467 H HG22 . ILE   A  1 754 ? 34.084 46.864  -33.739 0.00 70.73  ? 780  ILE   A HG22 1 
ATOM   11468 H HG23 . ILE   A  1 754 ? 32.843 45.577  -33.680 0.00 69.90  ? 780  ILE   A HG23 1 
ATOM   11469 H HD11 . ILE   A  1 754 ? 34.233 41.978  -36.265 0.00 69.66  ? 780  ILE   A HD11 1 
ATOM   11470 H HD12 . ILE   A  1 754 ? 34.302 43.376  -37.359 0.00 70.66  ? 780  ILE   A HD12 1 
ATOM   11471 H HD13 . ILE   A  1 754 ? 35.624 43.091  -36.194 0.00 70.25  ? 780  ILE   A HD13 1 
ATOM   11472 N N    . GLY   A  1 755 ? 32.365 48.036  -36.010 1.00 46.21  ? 781  GLY   A N    1 
ATOM   11473 C CA   . GLY   A  1 755 ? 31.034 48.616  -35.858 1.00 45.96  ? 781  GLY   A CA   1 
ATOM   11474 C C    . GLY   A  1 755 ? 30.068 48.293  -36.979 1.00 45.21  ? 781  GLY   A C    1 
ATOM   11475 O O    . GLY   A  1 755 ? 28.907 47.977  -36.718 1.00 45.17  ? 781  GLY   A O    1 
ATOM   11476 H H    . GLY   A  1 755 ? 33.088 48.748  -35.997 0.00 70.07  ? 781  GLY   A H    1 
ATOM   11477 H HA2  . GLY   A  1 755 ? 30.594 48.265  -34.926 0.00 69.87  ? 781  GLY   A HA2  1 
ATOM   11478 H HA3  . GLY   A  1 755 ? 31.128 49.699  -35.795 0.00 70.96  ? 781  GLY   A HA3  1 
ATOM   11479 N N    . ASP   A  1 756 ? 30.535 48.349  -38.228 1.00 44.55  ? 782  ASP   A N    1 
ATOM   11480 C CA   . ASP   A  1 756 ? 29.686 48.049  -39.379 1.00 44.61  ? 782  ASP   A CA   1 
ATOM   11481 C C    . ASP   A  1 756 ? 29.150 46.613  -39.324 1.00 43.58  ? 782  ASP   A C    1 
ATOM   11482 O O    . ASP   A  1 756 ? 27.956 46.415  -39.547 1.00 43.80  ? 782  ASP   A O    1 
ATOM   11483 C CB   . ASP   A  1 756 ? 30.441 48.290  -40.695 1.00 47.59  ? 782  ASP   A CB   1 
ATOM   11484 C CG   . ASP   A  1 756 ? 30.731 49.752  -40.979 1.00 54.25  ? 782  ASP   A CG   1 
ATOM   11485 O OD1  . ASP   A  1 756 ? 29.806 50.581  -40.832 1.00 55.32  ? 782  ASP   A OD1  1 
ATOM   11486 O OD2  . ASP   A  1 756 ? 31.880 50.066  -41.362 1.00 57.79  ? 782  ASP   A OD2  1 
ATOM   11487 H H    . ASP   A  1 756 ? 31.489 48.598  -38.469 0.00 68.26  ? 782  ASP   A H    1 
ATOM   11488 H HA   . ASP   A  1 756 ? 28.833 48.726  -39.352 0.00 69.07  ? 782  ASP   A HA   1 
ATOM   11489 H HB2  . ASP   A  1 756 ? 31.391 47.759  -40.661 0.00 71.31  ? 782  ASP   A HB2  1 
ATOM   11490 H HB3  . ASP   A  1 756 ? 29.840 47.905  -41.516 0.00 71.82  ? 782  ASP   A HB3  1 
ATOM   11491 N N    . PHE   A  1 757 ? 29.997 45.614  -38.989 1.00 42.12  ? 783  PHE   A N    1 
ATOM   11492 C CA   . PHE   A  1 757 ? 29.523 44.232  -38.882 1.00 41.63  ? 783  PHE   A CA   1 
ATOM   11493 C C    . PHE   A  1 757 ? 28.587 44.072  -37.676 1.00 41.39  ? 783  PHE   A C    1 
ATOM   11494 O O    . PHE   A  1 757 ? 27.621 43.320  -37.760 1.00 41.23  ? 783  PHE   A O    1 
ATOM   11495 C CB   . PHE   A  1 757 ? 30.689 43.228  -38.799 1.00 41.23  ? 783  PHE   A CB   1 
ATOM   11496 C CG   . PHE   A  1 757 ? 30.222 41.790  -38.720 1.00 41.22  ? 783  PHE   A CG   1 
ATOM   11497 C CD1  . PHE   A  1 757 ? 29.475 41.229  -39.742 1.00 41.95  ? 783  PHE   A CD1  1 
ATOM   11498 C CD2  . PHE   A  1 757 ? 30.522 41.004  -37.619 1.00 41.55  ? 783  PHE   A CD2  1 
ATOM   11499 C CE1  . PHE   A  1 757 ? 29.030 39.914  -39.659 1.00 42.39  ? 783  PHE   A CE1  1 
ATOM   11500 C CE2  . PHE   A  1 757 ? 30.071 39.694  -37.539 1.00 42.02  ? 783  PHE   A CE2  1 
ATOM   11501 C CZ   . PHE   A  1 757 ? 29.311 39.167  -38.549 1.00 41.92  ? 783  PHE   A CZ   1 
ATOM   11502 H H    . PHE   A  1 757 ? 30.986 45.732  -38.793 0.00 63.13  ? 783  PHE   A H    1 
ATOM   11503 H HA   . PHE   A  1 757 ? 28.950 43.994  -39.777 0.00 61.69  ? 783  PHE   A HA   1 
ATOM   11504 H HB2  . PHE   A  1 757 ? 31.306 43.330  -39.690 0.00 60.18  ? 783  PHE   A HB2  1 
ATOM   11505 H HB3  . PHE   A  1 757 ? 31.281 43.448  -37.912 0.00 60.22  ? 783  PHE   A HB3  1 
ATOM   11506 H HD1  . PHE   A  1 757 ? 29.221 41.822  -40.604 0.00 60.45  ? 783  PHE   A HD1  1 
ATOM   11507 H HD2  . PHE   A  1 757 ? 31.095 41.415  -36.805 0.00 59.14  ? 783  PHE   A HD2  1 
ATOM   11508 H HE1  . PHE   A  1 757 ? 28.441 39.494  -40.456 0.00 59.53  ? 783  PHE   A HE1  1 
ATOM   11509 H HE2  . PHE   A  1 757 ? 30.306 39.096  -36.674 0.00 58.25  ? 783  PHE   A HE2  1 
ATOM   11510 H HZ   . PHE   A  1 757 ? 28.984 38.142  -38.495 0.00 57.83  ? 783  PHE   A HZ   1 
ATOM   11511 N N    . ARG   A  1 758 ? 28.846 44.784  -36.574 1.00 41.29  ? 784  ARG   A N    1 
ATOM   11512 C CA   . ARG   A  1 758 ? 27.962 44.745  -35.405 1.00 41.93  ? 784  ARG   A CA   1 
ATOM   11513 C C    . ARG   A  1 758 ? 26.569 45.280  -35.773 1.00 42.47  ? 784  ARG   A C    1 
ATOM   11514 O O    . ARG   A  1 758 ? 25.557 44.694  -35.380 1.00 42.30  ? 784  ARG   A O    1 
ATOM   11515 C CB   . ARG   A  1 758 ? 28.546 45.579  -34.246 1.00 43.09  ? 784  ARG   A CB   1 
ATOM   11516 C CG   . ARG   A  1 758 ? 29.689 44.896  -33.500 1.00 46.67  ? 784  ARG   A CG   1 
ATOM   11517 C CD   . ARG   A  1 758 ? 29.218 43.797  -32.541 1.00 50.50  ? 784  ARG   A CD   1 
ATOM   11518 N NE   . ARG   A  1 758 ? 28.284 44.284  -31.518 1.00 53.82  ? 784  ARG   A NE   1 
ATOM   11519 C CZ   . ARG   A  1 758 ? 28.633 44.990  -30.443 1.00 56.32  ? 784  ARG   A CZ   1 
ATOM   11520 N NH1  . ARG   A  1 758 ? 29.907 45.313  -30.236 1.00 55.79  ? 784  ARG   A NH1  1 
ATOM   11521 N NH2  . ARG   A  1 758 ? 27.712 45.382  -29.571 1.00 56.69  ? 784  ARG   A NH2  1 
ATOM   11522 H H    . ARG   A  1 758 ? 29.667 45.367  -36.448 0.00 62.10  ? 784  ARG   A H    1 
ATOM   11523 H HA   . ARG   A  1 758 ? 27.841 43.711  -35.089 0.00 62.02  ? 784  ARG   A HA   1 
ATOM   11524 H HB2  . ARG   A  1 758 ? 28.923 46.521  -34.642 0.00 65.36  ? 784  ARG   A HB2  1 
ATOM   11525 H HB3  . ARG   A  1 758 ? 27.745 45.789  -33.539 0.00 65.09  ? 784  ARG   A HB3  1 
ATOM   11526 H HG2  . ARG   A  1 758 ? 30.363 44.446  -34.227 0.00 67.69  ? 784  ARG   A HG2  1 
ATOM   11527 H HG3  . ARG   A  1 758 ? 30.222 45.640  -32.910 0.00 68.72  ? 784  ARG   A HG3  1 
ATOM   11528 H HD2  . ARG   A  1 758 ? 28.705 43.016  -33.099 0.00 71.63  ? 784  ARG   A HD2  1 
ATOM   11529 H HD3  . ARG   A  1 758 ? 30.082 43.357  -32.045 0.00 71.61  ? 784  ARG   A HD3  1 
ATOM   11530 H HE   . ARG   A  1 758 ? 27.303 44.054  -31.644 0.00 76.81  ? 784  ARG   A HE   1 
ATOM   11531 H HH11 . ARG   A  1 758 ? 30.649 45.046  -30.873 0.00 79.22  ? 784  ARG   A HH11 1 
ATOM   11532 H HH12 . ARG   A  1 758 ? 30.153 45.852  -29.412 0.00 80.09  ? 784  ARG   A HH12 1 
ATOM   11533 H HH21 . ARG   A  1 758 ? 26.736 45.145  -29.716 0.00 81.38  ? 784  ARG   A HH21 1 
ATOM   11534 H HH22 . ARG   A  1 758 ? 27.975 45.923  -28.754 0.00 81.77  ? 784  ARG   A HH22 1 
ATOM   11535 N N    . ARG   A  1 759 ? 26.521 46.363  -36.555 1.00 42.88  ? 785  ARG   A N    1 
ATOM   11536 C CA   . ARG   A  1 759 ? 25.246 46.925  -36.991 1.00 44.20  ? 785  ARG   A CA   1 
ATOM   11537 C C    . ARG   A  1 759 ? 24.549 45.967  -37.963 1.00 44.41  ? 785  ARG   A C    1 
ATOM   11538 O O    . ARG   A  1 759 ? 23.337 45.791  -37.869 1.00 45.02  ? 785  ARG   A O    1 
ATOM   11539 C CB   . ARG   A  1 759 ? 25.439 48.320  -37.606 1.00 46.56  ? 785  ARG   A CB   1 
ATOM   11540 C CG   . ARG   A  1 759 ? 25.818 49.371  -36.561 1.00 51.78  ? 785  ARG   A CG   1 
ATOM   11541 C CD   . ARG   A  1 759 ? 26.231 50.705  -37.158 1.00 57.00  ? 785  ARG   A CD   1 
ATOM   11542 N NE   . ARG   A  1 759 ? 27.406 51.229  -36.449 1.00 61.34  ? 785  ARG   A NE   1 
ATOM   11543 C CZ   . ARG   A  1 759 ? 28.603 51.514  -36.971 1.00 64.63  ? 785  ARG   A CZ   1 
ATOM   11544 N NH1  . ARG   A  1 759 ? 28.831 51.362  -38.275 1.00 64.72  ? 785  ARG   A NH1  1 
ATOM   11545 N NH2  . ARG   A  1 759 ? 29.577 51.973  -36.195 1.00 65.07  ? 785  ARG   A NH2  1 
ATOM   11546 H H    . ARG   A  1 759 ? 27.336 46.871  -36.884 0.00 65.80  ? 785  ARG   A H    1 
ATOM   11547 H HA   . ARG   A  1 759 ? 24.595 47.028  -36.123 0.00 68.29  ? 785  ARG   A HA   1 
ATOM   11548 H HB2  . ARG   A  1 759 ? 26.228 48.275  -38.355 0.00 71.72  ? 785  ARG   A HB2  1 
ATOM   11549 H HB3  . ARG   A  1 759 ? 24.505 48.630  -38.071 0.00 72.54  ? 785  ARG   A HB3  1 
ATOM   11550 H HG2  . ARG   A  1 759 ? 24.957 49.551  -35.919 0.00 79.43  ? 785  ARG   A HG2  1 
ATOM   11551 H HG3  . ARG   A  1 759 ? 26.651 48.997  -35.968 0.00 78.46  ? 785  ARG   A HG3  1 
ATOM   11552 H HD2  . ARG   A  1 759 ? 26.368 50.582  -38.230 0.00 86.21  ? 785  ARG   A HD2  1 
ATOM   11553 H HD3  . ARG   A  1 759 ? 25.420 51.412  -36.989 0.00 87.21  ? 785  ARG   A HD3  1 
ATOM   11554 H HE   . ARG   A  1 759 ? 27.297 51.368  -35.449 0.00 91.81  ? 785  ARG   A HE   1 
ATOM   11555 H HH11 . ARG   A  1 759 ? 28.155 51.013  -38.944 0.00 95.37  ? 785  ARG   A HH11 1 
ATOM   11556 H HH12 . ARG   A  1 759 ? 29.751 51.595  -38.633 0.00 95.46  ? 785  ARG   A HH12 1 
ATOM   11557 H HH21 . ARG   A  1 759 ? 29.423 52.108  -35.201 0.00 96.40  ? 785  ARG   A HH21 1 
ATOM   11558 H HH22 . ARG   A  1 759 ? 30.478 52.208  -36.597 0.00 96.23  ? 785  ARG   A HH22 1 
ATOM   11559 N N    . TRP   A  1 760 ? 25.313 45.299  -38.844 1.00 43.57  ? 786  TRP   A N    1 
ATOM   11560 C CA   . TRP   A  1 760 ? 24.758 44.317  -39.771 1.00 43.07  ? 786  TRP   A CA   1 
ATOM   11561 C C    . TRP   A  1 760 ? 24.141 43.147  -38.995 1.00 43.08  ? 786  TRP   A C    1 
ATOM   11562 O O    . TRP   A  1 760 ? 23.076 42.662  -39.376 1.00 43.13  ? 786  TRP   A O    1 
ATOM   11563 C CB   . TRP   A  1 760 ? 25.849 43.797  -40.712 1.00 42.60  ? 786  TRP   A CB   1 
ATOM   11564 C CG   . TRP   A  1 760 ? 25.344 42.816  -41.721 1.00 42.70  ? 786  TRP   A CG   1 
ATOM   11565 C CD1  . TRP   A  1 760 ? 24.862 43.098  -42.963 1.00 43.38  ? 786  TRP   A CD1  1 
ATOM   11566 C CD2  . TRP   A  1 760 ? 25.309 41.389  -41.591 1.00 42.36  ? 786  TRP   A CD2  1 
ATOM   11567 N NE1  . TRP   A  1 760 ? 24.576 41.933  -43.633 1.00 43.52  ? 786  TRP   A NE1  1 
ATOM   11568 C CE2  . TRP   A  1 760 ? 24.803 40.871  -42.798 1.00 43.04  ? 786  TRP   A CE2  1 
ATOM   11569 C CE3  . TRP   A  1 760 ? 25.632 40.498  -40.559 1.00 42.76  ? 786  TRP   A CE3  1 
ATOM   11570 C CZ2  . TRP   A  1 760 ? 24.615 39.507  -43.002 1.00 43.52  ? 786  TRP   A CZ2  1 
ATOM   11571 C CZ3  . TRP   A  1 760 ? 25.449 39.147  -40.764 1.00 43.40  ? 786  TRP   A CZ3  1 
ATOM   11572 C CH2  . TRP   A  1 760 ? 24.942 38.665  -41.972 1.00 43.62  ? 786  TRP   A CH2  1 
ATOM   11573 H H    . TRP   A  1 760 ? 26.313 45.433  -38.954 0.00 65.79  ? 786  TRP   A H    1 
ATOM   11574 H HA   . TRP   A  1 760 ? 23.979 44.784  -40.372 0.00 65.50  ? 786  TRP   A HA   1 
ATOM   11575 H HB2  . TRP   A  1 760 ? 26.280 44.638  -41.253 0.00 64.16  ? 786  TRP   A HB2  1 
ATOM   11576 H HB3  . TRP   A  1 760 ? 26.617 43.302  -40.120 0.00 62.96  ? 786  TRP   A HB3  1 
ATOM   11577 H HD1  . TRP   A  1 760 ? 24.806 44.084  -43.393 0.00 65.33  ? 786  TRP   A HD1  1 
ATOM   11578 H HE1  . TRP   A  1 760 ? 24.169 41.872  -44.590 0.00 64.21  ? 786  TRP   A HE1  1 
ATOM   11579 H HE3  . TRP   A  1 760 ? 26.029 40.860  -39.626 0.00 61.51  ? 786  TRP   A HE3  1 
ATOM   11580 H HZ2  . TRP   A  1 760 ? 24.207 39.131  -43.922 0.00 62.18  ? 786  TRP   A HZ2  1 
ATOM   11581 H HZ3  . TRP   A  1 760 ? 25.707 38.453  -39.982 0.00 60.73  ? 786  TRP   A HZ3  1 
ATOM   11582 H HH2  . TRP   A  1 760 ? 24.817 37.606  -42.102 0.00 60.88  ? 786  TRP   A HH2  1 
ATOM   11583 N N    . MET   A  1 761 ? 24.802 42.684  -37.917 1.00 42.74  ? 787  MET   A N    1 
ATOM   11584 C CA   . MET   A  1 761 ? 24.276 41.597  -37.086 1.00 43.25  ? 787  MET   A CA   1 
ATOM   11585 C C    . MET   A  1 761 ? 22.920 41.984  -36.484 1.00 44.38  ? 787  MET   A C    1 
ATOM   11586 O O    . MET   A  1 761 ? 22.035 41.135  -36.403 1.00 44.66  ? 787  MET   A O    1 
ATOM   11587 C CB   . MET   A  1 761 ? 25.268 41.223  -35.957 1.00 43.31  ? 787  MET   A CB   1 
ATOM   11588 C CG   . MET   A  1 761 ? 26.498 40.473  -36.448 1.00 44.62  ? 787  MET   A CG   1 
ATOM   11589 S SD   . MET   A  1 761 ? 27.832 40.333  -35.218 1.00 44.90  ? 787  MET   A SD   1 
ATOM   11590 C CE   . MET   A  1 761 ? 27.078 39.277  -34.044 1.00 40.98  ? 787  MET   A CE   1 
ATOM   11591 H H    . MET   A  1 761 ? 25.706 43.029  -37.609 0.00 63.09  ? 787  MET   A H    1 
ATOM   11592 H HA   . MET   A  1 761 ? 24.130 40.719  -37.713 0.00 62.48  ? 787  MET   A HA   1 
ATOM   11593 H HB2  . MET   A  1 761 ? 25.605 42.131  -35.459 0.00 63.09  ? 787  MET   A HB2  1 
ATOM   11594 H HB3  . MET   A  1 761 ? 24.756 40.582  -35.241 0.00 62.21  ? 787  MET   A HB3  1 
ATOM   11595 H HG2  . MET   A  1 761 ? 26.200 39.465  -36.733 0.00 62.60  ? 787  MET   A HG2  1 
ATOM   11596 H HG3  . MET   A  1 761 ? 26.901 40.994  -37.315 0.00 63.50  ? 787  MET   A HG3  1 
ATOM   11597 H HE1  . MET   A  1 761 ? 27.853 38.840  -33.416 0.00 57.42  ? 787  MET   A HE1  1 
ATOM   11598 H HE2  . MET   A  1 761 ? 26.394 39.862  -33.431 0.00 58.49  ? 787  MET   A HE2  1 
ATOM   11599 H HE3  . MET   A  1 761 ? 26.533 38.490  -34.560 0.00 57.48  ? 787  MET   A HE3  1 
ATOM   11600 N N    . ASP   A  1 762 ? 22.757 43.255  -36.064 1.00 45.11  ? 788  ASP   A N    1 
ATOM   11601 C CA   . ASP   A  1 762 ? 21.496 43.761  -35.507 1.00 46.55  ? 788  ASP   A CA   1 
ATOM   11602 C C    . ASP   A  1 762 ? 20.394 43.844  -36.581 1.00 47.53  ? 788  ASP   A C    1 
ATOM   11603 O O    . ASP   A  1 762 ? 19.233 43.565  -36.288 1.00 47.60  ? 788  ASP   A O    1 
ATOM   11604 C CB   . ASP   A  1 762 ? 21.701 45.155  -34.870 1.00 48.54  ? 788  ASP   A CB   1 
ATOM   11605 C CG   . ASP   A  1 762 ? 22.605 45.175  -33.654 1.00 53.29  ? 788  ASP   A CG   1 
ATOM   11606 O OD1  . ASP   A  1 762 ? 22.882 44.094  -33.103 1.00 53.63  ? 788  ASP   A OD1  1 
ATOM   11607 O OD2  . ASP   A  1 762 ? 23.047 46.275  -33.264 1.00 56.06  ? 788  ASP   A OD2  1 
ATOM   11608 H H    . ASP   A  1 762 ? 23.491 43.956  -36.091 0.00 67.27  ? 788  ASP   A H    1 
ATOM   11609 H HA   . ASP   A  1 762 ? 21.147 43.077  -34.734 0.00 69.10  ? 788  ASP   A HA   1 
ATOM   11610 H HB2  . ASP   A  1 762 ? 22.134 45.822  -35.614 0.00 73.32  ? 788  ASP   A HB2  1 
ATOM   11611 H HB3  . ASP   A  1 762 ? 20.731 45.539  -34.558 0.00 73.57  ? 788  ASP   A HB3  1 
ATOM   11612 N N    . GLU   A  1 763 ? 20.753 44.232  -37.810 1.00 48.14  ? 789  GLU   A N    1 
ATOM   11613 C CA   . GLU   A  1 763 ? 19.805 44.341  -38.923 1.00 49.50  ? 789  GLU   A CA   1 
ATOM   11614 C C    . GLU   A  1 763 ? 19.468 42.988  -39.574 1.00 50.01  ? 789  GLU   A C    1 
ATOM   11615 O O    . GLU   A  1 763 ? 18.553 42.941  -40.396 1.00 50.68  ? 789  GLU   A O    1 
ATOM   11616 C CB   . GLU   A  1 763 ? 20.372 45.272  -40.010 1.00 52.54  ? 789  GLU   A CB   1 
ATOM   11617 C CG   . GLU   A  1 763 ? 20.555 46.715  -39.567 1.00 58.51  ? 789  GLU   A CG   1 
ATOM   11618 C CD   . GLU   A  1 763 ? 21.354 47.581  -40.523 1.00 66.58  ? 789  GLU   A CD   1 
ATOM   11619 O OE1  . GLU   A  1 763 ? 21.947 47.035  -41.483 1.00 68.25  ? 789  GLU   A OE1  1 
ATOM   11620 O OE2  . GLU   A  1 763 ? 21.394 48.813  -40.305 1.00 70.02  ? 789  GLU   A OE2  1 
ATOM   11621 H H    . GLU   A  1 763 ? 21.700 44.494  -38.066 0.00 72.01  ? 789  GLU   A H    1 
ATOM   11622 H HA   . GLU   A  1 763 ? 18.876 44.783  -38.567 0.00 75.00  ? 789  GLU   A HA   1 
ATOM   11623 H HB2  . GLU   A  1 763 ? 21.339 44.878  -40.321 0.00 77.87  ? 789  GLU   A HB2  1 
ATOM   11624 H HB3  . GLU   A  1 763 ? 19.691 45.280  -40.859 0.00 78.86  ? 789  GLU   A HB3  1 
ATOM   11625 H HG2  . GLU   A  1 763 ? 19.572 47.170  -39.458 0.00 87.52  ? 789  GLU   A HG2  1 
ATOM   11626 H HG3  . GLU   A  1 763 ? 21.073 46.732  -38.610 0.00 86.53  ? 789  GLU   A HG3  1 
ATOM   11627 N N    . HIS   A  1 764 ? 20.220 41.913  -39.266 1.00 49.58  ? 790  HIS   A N    1 
ATOM   11628 C CA   . HIS   A  1 764 ? 20.006 40.593  -39.860 1.00 49.74  ? 790  HIS   A CA   1 
ATOM   11629 C C    . HIS   A  1 764 ? 19.911 39.528  -38.768 1.00 49.83  ? 790  HIS   A C    1 
ATOM   11630 O O    . HIS   A  1 764 ? 20.721 38.602  -38.724 1.00 49.78  ? 790  HIS   A O    1 
ATOM   11631 C CB   . HIS   A  1 764 ? 21.134 40.271  -40.861 1.00 50.30  ? 790  HIS   A CB   1 
ATOM   11632 C CG   . HIS   A  1 764 ? 21.200 41.236  -42.006 1.00 52.56  ? 790  HIS   A CG   1 
ATOM   11633 N ND1  . HIS   A  1 764 ? 21.904 42.422  -41.909 1.00 54.46  ? 790  HIS   A ND1  1 
ATOM   11634 C CD2  . HIS   A  1 764 ? 20.620 41.174  -43.227 1.00 53.76  ? 790  HIS   A CD2  1 
ATOM   11635 C CE1  . HIS   A  1 764 ? 21.736 43.044  -43.066 1.00 54.99  ? 790  HIS   A CE1  1 
ATOM   11636 N NE2  . HIS   A  1 764 ? 20.969 42.330  -43.891 1.00 55.06  ? 790  HIS   A NE2  1 
ATOM   11637 H H    . HIS   A  1 764 ? 20.993 41.915  -38.607 0.00 72.07  ? 790  HIS   A H    1 
ATOM   11638 H HA   . HIS   A  1 764 ? 19.065 40.569  -40.407 0.00 72.16  ? 790  HIS   A HA   1 
ATOM   11639 H HB2  . HIS   A  1 764 ? 22.090 40.302  -40.340 0.00 71.47  ? 790  HIS   A HB2  1 
ATOM   11640 H HB3  . HIS   A  1 764 ? 20.969 39.280  -41.279 0.00 71.26  ? 790  HIS   A HB3  1 
ATOM   11641 H HD1  . HIS   A  1 764 ? 22.440 42.750  -41.112 0.00 78.20  ? 790  HIS   A HD1  1 
ATOM   11642 H HD2  . HIS   A  1 764 ? 20.003 40.378  -43.605 0.00 76.79  ? 790  HIS   A HD2  1 
ATOM   11643 H HE1  . HIS   A  1 764 ? 22.161 44.004  -43.307 0.00 80.09  ? 790  HIS   A HE1  1 
ATOM   11644 N N    . LEU   A  1 765 ? 18.904 39.656  -37.884 1.00 49.63  ? 791  LEU   A N    1 
ATOM   11645 C CA   . LEU   A  1 765 ? 18.682 38.690  -36.808 1.00 49.97  ? 791  LEU   A CA   1 
ATOM   11646 C C    . LEU   A  1 765 ? 18.267 37.307  -37.329 1.00 50.17  ? 791  LEU   A C    1 
ATOM   11647 O O    . LEU   A  1 765 ? 18.374 36.335  -36.582 1.00 50.50  ? 791  LEU   A O    1 
ATOM   11648 C CB   . LEU   A  1 765 ? 17.630 39.211  -35.818 1.00 50.37  ? 791  LEU   A CB   1 
ATOM   11649 C CG   . LEU   A  1 765 ? 17.995 40.479  -35.044 1.00 52.00  ? 791  LEU   A CG   1 
ATOM   11650 C CD1  . LEU   A  1 765 ? 16.814 40.967  -34.226 1.00 52.51  ? 791  LEU   A CD1  1 
ATOM   11651 C CD2  . LEU   A  1 765 ? 19.202 40.249  -34.133 1.00 52.77  ? 791  LEU   A CD2  1 
ATOM   11652 H H    . LEU   A  1 765 ? 18.235 40.418  -37.898 0.00 72.06  ? 791  LEU   A H    1 
ATOM   11653 H HA   . LEU   A  1 765 ? 19.619 38.549  -36.271 0.00 70.53  ? 791  LEU   A HA   1 
ATOM   11654 H HB2  . LEU   A  1 765 ? 16.715 39.421  -36.372 0.00 72.78  ? 791  LEU   A HB2  1 
ATOM   11655 H HB3  . LEU   A  1 765 ? 17.434 38.428  -35.086 0.00 71.73  ? 791  LEU   A HB3  1 
ATOM   11656 H HG   . LEU   A  1 765 ? 18.257 41.261  -35.756 0.00 75.39  ? 791  LEU   A HG   1 
ATOM   11657 H HD11 . LEU   A  1 765 ? 17.086 41.891  -33.718 0.00 76.93  ? 791  LEU   A HD11 1 
ATOM   11658 H HD12 . LEU   A  1 765 ? 15.973 41.149  -34.894 0.00 76.89  ? 791  LEU   A HD12 1 
ATOM   11659 H HD13 . LEU   A  1 765 ? 16.547 40.205  -33.495 0.00 75.93  ? 791  LEU   A HD13 1 
ATOM   11660 H HD21 . LEU   A  1 765 ? 19.277 41.074  -33.426 0.00 75.76  ? 791  LEU   A HD21 1 
ATOM   11661 H HD22 . LEU   A  1 765 ? 19.074 39.309  -33.597 0.00 74.59  ? 791  LEU   A HD22 1 
ATOM   11662 H HD23 . LEU   A  1 765 ? 20.106 40.213  -34.738 0.00 74.79  ? 791  LEU   A HD23 1 
ATOM   11663 N N    . ASN   A  1 766 ? 17.804 37.206  -38.594 1.00 49.79  ? 792  ASN   A N    1 
ATOM   11664 C CA   . ASN   A  1 766 ? 17.450 35.921  -39.201 1.00 49.71  ? 792  ASN   A CA   1 
ATOM   11665 C C    . ASN   A  1 766 ? 18.714 35.103  -39.583 1.00 47.37  ? 792  ASN   A C    1 
ATOM   11666 O O    . ASN   A  1 766 ? 18.614 33.888  -39.755 1.00 47.39  ? 792  ASN   A O    1 
ATOM   11667 C CB   . ASN   A  1 766 ? 16.564 36.147  -40.429 1.00 52.88  ? 792  ASN   A CB   1 
ATOM   11668 C CG   . ASN   A  1 766 ? 15.790 34.920  -40.850 1.00 59.77  ? 792  ASN   A CG   1 
ATOM   11669 O OD1  . ASN   A  1 766 ? 14.831 34.511  -40.179 1.00 62.14  ? 792  ASN   A OD1  1 
ATOM   11670 N ND2  . ASN   A  1 766 ? 16.174 34.299  -41.969 1.00 61.58  ? 792  ASN   A ND2  1 
ATOM   11671 H H    . ASN   A  1 766 ? 17.658 37.990  -39.221 0.00 70.88  ? 792  ASN   A H    1 
ATOM   11672 H HA   . ASN   A  1 766 ? 16.882 35.336  -38.479 0.00 69.30  ? 792  ASN   A HA   1 
ATOM   11673 H HB2  . ASN   A  1 766 ? 15.834 36.919  -40.194 0.00 74.74  ? 792  ASN   A HB2  1 
ATOM   11674 H HB3  . ASN   A  1 766 ? 17.190 36.474  -41.258 0.00 73.96  ? 792  ASN   A HB3  1 
ATOM   11675 H HD21 . ASN   A  1 766 ? 15.675 33.471  -42.280 0.00 83.37  ? 792  ASN   A HD21 1 
ATOM   11676 H HD22 . ASN   A  1 766 ? 16.956 34.646  -42.515 0.00 83.61  ? 792  ASN   A HD22 1 
ATOM   11677 N N    . VAL   A  1 767 ? 19.891 35.753  -39.716 1.00 45.20  ? 793  VAL   A N    1 
ATOM   11678 C CA   . VAL   A  1 767 ? 21.143 35.054  -40.011 1.00 43.61  ? 793  VAL   A CA   1 
ATOM   11679 C C    . VAL   A  1 767 ? 21.724 34.603  -38.670 1.00 41.53  ? 793  VAL   A C    1 
ATOM   11680 O O    . VAL   A  1 767 ? 22.239 35.430  -37.922 1.00 41.32  ? 793  VAL   A O    1 
ATOM   11681 C CB   . VAL   A  1 767 ? 22.153 35.948  -40.772 1.00 44.23  ? 793  VAL   A CB   1 
ATOM   11682 C CG1  . VAL   A  1 767 ? 23.443 35.176  -41.060 1.00 44.53  ? 793  VAL   A CG1  1 
ATOM   11683 C CG2  . VAL   A  1 767 ? 21.549 36.496  -42.067 1.00 44.81  ? 793  VAL   A CG2  1 
ATOM   11684 H H    . VAL   A  1 767 ? 20.013 36.758  -39.644 0.00 63.65  ? 793  VAL   A H    1 
ATOM   11685 H HA   . VAL   A  1 767 ? 20.948 34.179  -40.629 0.00 59.87  ? 793  VAL   A HA   1 
ATOM   11686 H HB   . VAL   A  1 767 ? 22.413 36.803  -40.150 0.00 61.71  ? 793  VAL   A HB   1 
ATOM   11687 H HG11 . VAL   A  1 767 ? 23.959 35.643  -41.897 0.00 60.97  ? 793  VAL   A HG11 1 
ATOM   11688 H HG12 . VAL   A  1 767 ? 24.081 35.205  -40.178 0.00 60.52  ? 793  VAL   A HG12 1 
ATOM   11689 H HG13 . VAL   A  1 767 ? 23.196 34.145  -41.307 0.00 60.24  ? 793  VAL   A HG13 1 
ATOM   11690 H HG21 . VAL   A  1 767 ? 22.271 37.155  -42.546 0.00 62.88  ? 793  VAL   A HG21 1 
ATOM   11691 H HG22 . VAL   A  1 767 ? 21.318 35.663  -42.729 0.00 62.30  ? 793  VAL   A HG22 1 
ATOM   11692 H HG23 . VAL   A  1 767 ? 20.639 37.052  -41.844 0.00 63.34  ? 793  VAL   A HG23 1 
ATOM   11693 N N    . LYS   A  1 768 ? 21.612 33.315  -38.347 1.00 40.01  ? 794  LYS   A N    1 
ATOM   11694 C CA   . LYS   A  1 768 ? 22.111 32.777  -37.084 1.00 39.10  ? 794  LYS   A CA   1 
ATOM   11695 C C    . LYS   A  1 768 ? 23.641 32.716  -37.075 1.00 37.29  ? 794  LYS   A C    1 
ATOM   11696 O O    . LYS   A  1 768 ? 24.232 32.254  -38.044 1.00 36.39  ? 794  LYS   A O    1 
ATOM   11697 C CB   . LYS   A  1 768 ? 21.570 31.355  -36.848 1.00 41.36  ? 794  LYS   A CB   1 
ATOM   11698 C CG   . LYS   A  1 768 ? 20.053 31.261  -36.776 1.00 46.57  ? 794  LYS   A CG   1 
ATOM   11699 C CD   . LYS   A  1 768 ? 19.574 29.884  -36.275 1.00 52.26  ? 794  LYS   A CD   1 
ATOM   11700 C CE   . LYS   A  1 768 ? 19.742 28.753  -37.276 1.00 56.70  ? 794  LYS   A CE   1 
ATOM   11701 N NZ   . LYS   A  1 768 ? 18.886 28.937  -38.487 1.00 59.15  ? 794  LYS   A NZ   1 
ATOM   11702 H H    . LYS   A  1 768 ? 21.188 32.616  -38.949 0.00 54.40  ? 794  LYS   A H    1 
ATOM   11703 H HA   . LYS   A  1 768 ? 21.772 33.407  -36.263 0.00 53.42  ? 794  LYS   A HA   1 
ATOM   11704 H HB2  . LYS   A  1 768 ? 21.905 30.724  -37.670 0.00 54.64  ? 794  LYS   A HB2  1 
ATOM   11705 H HB3  . LYS   A  1 768 ? 21.975 30.982  -35.908 0.00 54.66  ? 794  LYS   A HB3  1 
ATOM   11706 H HG2  . LYS   A  1 768 ? 19.687 32.016  -36.082 0.00 62.30  ? 794  LYS   A HG2  1 
ATOM   11707 H HG3  . LYS   A  1 768 ? 19.636 31.434  -37.767 0.00 62.08  ? 794  LYS   A HG3  1 
ATOM   11708 H HD2  . LYS   A  1 768 ? 20.130 29.616  -35.377 0.00 67.60  ? 794  LYS   A HD2  1 
ATOM   11709 H HD3  . LYS   A  1 768 ? 18.514 29.954  -36.035 0.00 68.41  ? 794  LYS   A HD3  1 
ATOM   11710 H HE2  . LYS   A  1 768 ? 20.780 28.696  -37.597 0.00 72.39  ? 794  LYS   A HE2  1 
ATOM   11711 H HE3  . LYS   A  1 768 ? 19.451 27.817  -36.801 0.00 72.32  ? 794  LYS   A HE3  1 
ATOM   11712 H HZ1  . LYS   A  1 768 ? 18.929 28.105  -39.068 0.00 75.81  ? 794  LYS   A HZ1  1 
ATOM   11713 H HZ2  . LYS   A  1 768 ? 17.923 29.097  -38.211 0.00 76.59  ? 794  LYS   A HZ2  1 
ATOM   11714 H HZ3  . LYS   A  1 768 ? 19.211 29.729  -39.032 0.00 76.58  ? 794  LYS   A HZ3  1 
ATOM   11715 N N    . ILE   A  1 769 ? 24.267 33.142  -35.963 1.00 36.35  ? 795  ILE   A N    1 
ATOM   11716 C CA   . ILE   A  1 769 ? 25.716 33.082  -35.757 1.00 35.91  ? 795  ILE   A CA   1 
ATOM   11717 C C    . ILE   A  1 769 ? 25.893 32.329  -34.437 1.00 36.04  ? 795  ILE   A C    1 
ATOM   11718 O O    . ILE   A  1 769 ? 25.744 32.938  -33.372 1.00 36.29  ? 795  ILE   A O    1 
ATOM   11719 C CB   . ILE   A  1 769 ? 26.388 34.481  -35.716 1.00 35.68  ? 795  ILE   A CB   1 
ATOM   11720 C CG1  . ILE   A  1 769 ? 26.192 35.211  -37.065 1.00 36.15  ? 795  ILE   A CG1  1 
ATOM   11721 C CG2  . ILE   A  1 769 ? 27.896 34.319  -35.405 1.00 35.83  ? 795  ILE   A CG2  1 
ATOM   11722 C CD1  . ILE   A  1 769 ? 26.535 36.683  -37.079 1.00 36.96  ? 795  ILE   A CD1  1 
ATOM   11723 H H    . ILE   A  1 769 ? 23.781 33.542  -35.167 0.00 49.55  ? 795  ILE   A H    1 
ATOM   11724 H HA   . ILE   A  1 769 ? 26.200 32.531  -36.561 0.00 47.80  ? 795  ILE   A HA   1 
ATOM   11725 H HB   . ILE   A  1 769 ? 25.928 35.077  -34.929 0.00 49.08  ? 795  ILE   A HB   1 
ATOM   11726 H HG12 . ILE   A  1 769 ? 26.820 34.725  -37.809 0.00 49.28  ? 795  ILE   A HG12 1 
ATOM   11727 H HG13 . ILE   A  1 769 ? 25.149 35.131  -37.366 0.00 49.95  ? 795  ILE   A HG13 1 
ATOM   11728 H HG21 . ILE   A  1 769 ? 28.374 35.296  -35.368 0.00 48.83  ? 795  ILE   A HG21 1 
ATOM   11729 H HG22 . ILE   A  1 769 ? 28.035 33.831  -34.442 0.00 48.01  ? 795  ILE   A HG22 1 
ATOM   11730 H HG23 . ILE   A  1 769 ? 28.352 33.716  -36.190 0.00 47.88  ? 795  ILE   A HG23 1 
ATOM   11731 H HD11 . ILE   A  1 769 ? 26.319 37.077  -38.071 0.00 51.90  ? 795  ILE   A HD11 1 
ATOM   11732 H HD12 . ILE   A  1 769 ? 25.912 37.185  -36.342 0.00 51.95  ? 795  ILE   A HD12 1 
ATOM   11733 H HD13 . ILE   A  1 769 ? 27.590 36.831  -36.855 0.00 51.33  ? 795  ILE   A HD13 1 
ATOM   11734 N N    . PRO   A  1 770 ? 26.140 31.009  -34.466 1.00 35.54  ? 796  PRO   A N    1 
ATOM   11735 C CA   . PRO   A  1 770 ? 26.269 30.275  -33.198 1.00 35.57  ? 796  PRO   A CA   1 
ATOM   11736 C C    . PRO   A  1 770 ? 27.544 30.582  -32.417 1.00 35.76  ? 796  PRO   A C    1 
ATOM   11737 O O    . PRO   A  1 770 ? 28.532 31.089  -32.963 1.00 35.58  ? 796  PRO   A O    1 
ATOM   11738 C CB   . PRO   A  1 770 ? 26.209 28.795  -33.605 1.00 36.46  ? 796  PRO   A CB   1 
ATOM   11739 C CG   . PRO   A  1 770 ? 26.181 28.753  -35.087 1.00 37.02  ? 796  PRO   A CG   1 
ATOM   11740 C CD   . PRO   A  1 770 ? 26.311 30.133  -35.640 1.00 35.19  ? 796  PRO   A CD   1 
ATOM   11741 H HA   . PRO   A  1 770 ? 25.409 30.482  -32.562 0.00 46.42  ? 796  PRO   A HA   1 
ATOM   11742 H HB2  . PRO   A  1 770 ? 27.095 28.283  -33.230 0.00 45.94  ? 796  PRO   A HB2  1 
ATOM   11743 H HB3  . PRO   A  1 770 ? 25.308 28.342  -33.195 0.00 46.40  ? 796  PRO   A HB3  1 
ATOM   11744 H HG2  . PRO   A  1 770 ? 27.008 28.136  -35.435 0.00 46.57  ? 796  PRO   A HG2  1 
ATOM   11745 H HG3  . PRO   A  1 770 ? 25.236 28.316  -35.407 0.00 47.14  ? 796  PRO   A HG3  1 
ATOM   11746 H HD2  . PRO   A  1 770 ? 27.299 30.273  -36.076 0.00 45.39  ? 796  PRO   A HD2  1 
ATOM   11747 H HD3  . PRO   A  1 770 ? 25.523 30.311  -36.370 0.00 45.89  ? 796  PRO   A HD3  1 
ATOM   11748 N N    . ARG   A  1 771 ? 27.507 30.250  -31.121 1.00 35.50  ? 797  ARG   A N    1 
ATOM   11749 C CA   . ARG   A  1 771 ? 28.626 30.376  -30.201 1.00 35.58  ? 797  ARG   A CA   1 
ATOM   11750 C C    . ARG   A  1 771 ? 29.294 31.752  -30.242 1.00 34.06  ? 797  ARG   A C    1 
ATOM   11751 O O    . ARG   A  1 771 ? 30.501 31.850  -30.484 1.00 33.04  ? 797  ARG   A O    1 
ATOM   11752 C CB   . ARG   A  1 771 ? 29.651 29.260  -30.471 1.00 38.21  ? 797  ARG   A CB   1 
ATOM   11753 C CG   . ARG   A  1 771 ? 29.137 27.837  -30.239 1.00 43.56  ? 797  ARG   A CG   1 
ATOM   11754 C CD   . ARG   A  1 771 ? 29.082 27.433  -28.777 1.00 47.69  ? 797  ARG   A CD   1 
ATOM   11755 N NE   . ARG   A  1 771 ? 30.408 27.378  -28.157 1.00 50.43  ? 797  ARG   A NE   1 
ATOM   11756 C CZ   . ARG   A  1 771 ? 30.679 26.800  -26.991 1.00 52.23  ? 797  ARG   A CZ   1 
ATOM   11757 N NH1  . ARG   A  1 771 ? 29.717 26.200  -26.296 1.00 52.23  ? 797  ARG   A NH1  1 
ATOM   11758 N NH2  . ARG   A  1 771 ? 31.917 26.811  -26.512 1.00 52.05  ? 797  ARG   A NH2  1 
ATOM   11759 H H    . ARG   A  1 771 ? 26.678 29.877  -30.669 0.00 45.75  ? 797  ARG   A H    1 
ATOM   11760 H HA   . ARG   A  1 771 ? 28.250 30.239  -29.188 0.00 45.78  ? 797  ARG   A HA   1 
ATOM   11761 H HB2  . ARG   A  1 771 ? 29.972 29.325  -31.509 0.00 48.01  ? 797  ARG   A HB2  1 
ATOM   11762 H HB3  . ARG   A  1 771 ? 30.511 29.421  -29.822 0.00 48.06  ? 797  ARG   A HB3  1 
ATOM   11763 H HG2  . ARG   A  1 771 ? 28.133 27.741  -30.649 0.00 54.02  ? 797  ARG   A HG2  1 
ATOM   11764 H HG3  . ARG   A  1 771 ? 29.805 27.143  -30.746 0.00 53.42  ? 797  ARG   A HG3  1 
ATOM   11765 H HD2  . ARG   A  1 771 ? 28.471 28.142  -28.221 0.00 59.26  ? 797  ARG   A HD2  1 
ATOM   11766 H HD3  . ARG   A  1 771 ? 28.638 26.440  -28.729 0.00 58.37  ? 797  ARG   A HD3  1 
ATOM   11767 H HE   . ARG   A  1 771 ? 31.188 27.797  -28.655 0.00 61.90  ? 797  ARG   A HE   1 
ATOM   11768 H HH11 . ARG   A  1 771 ? 28.752 26.183  -26.610 0.00 63.86  ? 797  ARG   A HH11 1 
ATOM   11769 H HH12 . ARG   A  1 771 ? 29.940 25.776  -25.401 0.00 63.60  ? 797  ARG   A HH12 1 
ATOM   11770 H HH21 . ARG   A  1 771 ? 32.668 27.248  -27.037 0.00 63.53  ? 797  ARG   A HH21 1 
ATOM   11771 H HH22 . ARG   A  1 771 ? 32.125 26.364  -25.624 0.00 63.34  ? 797  ARG   A HH22 1 
ATOM   11772 N N    . LEU   A  1 772 ? 28.517 32.813  -29.981 1.00 33.79  ? 798  LEU   A N    1 
ATOM   11773 C CA   . LEU   A  1 772 ? 29.052 34.177  -29.938 1.00 34.09  ? 798  LEU   A CA   1 
ATOM   11774 C C    . LEU   A  1 772 ? 30.122 34.326  -28.848 1.00 33.48  ? 798  LEU   A C    1 
ATOM   11775 O O    . LEU   A  1 772 ? 31.016 35.154  -29.003 1.00 33.36  ? 798  LEU   A O    1 
ATOM   11776 C CB   . LEU   A  1 772 ? 27.940 35.199  -29.709 1.00 35.16  ? 798  LEU   A CB   1 
ATOM   11777 C CG   . LEU   A  1 772 ? 26.931 35.361  -30.838 1.00 37.15  ? 798  LEU   A CG   1 
ATOM   11778 C CD1  . LEU   A  1 772 ? 25.767 36.220  -30.385 1.00 37.93  ? 798  LEU   A CD1  1 
ATOM   11779 C CD2  . LEU   A  1 772 ? 27.579 35.967  -32.086 1.00 37.90  ? 798  LEU   A CD2  1 
ATOM   11780 H H    . LEU   A  1 772 ? 27.521 32.752  -29.796 0.00 45.15  ? 798  LEU   A H    1 
ATOM   11781 H HA   . LEU   A  1 772 ? 29.539 34.393  -30.887 0.00 46.00  ? 798  LEU   A HA   1 
ATOM   11782 H HB2  . LEU   A  1 772 ? 27.390 34.896  -28.820 0.00 48.17  ? 798  LEU   A HB2  1 
ATOM   11783 H HB3  . LEU   A  1 772 ? 28.397 36.172  -29.535 0.00 48.70  ? 798  LEU   A HB3  1 
ATOM   11784 H HG   . LEU   A  1 772 ? 26.540 34.380  -31.105 0.00 50.30  ? 798  LEU   A HG   1 
ATOM   11785 H HD11 . LEU   A  1 772 ? 24.997 36.198  -31.154 0.00 52.76  ? 798  LEU   A HD11 1 
ATOM   11786 H HD12 . LEU   A  1 772 ? 25.364 35.825  -29.454 0.00 52.49  ? 798  LEU   A HD12 1 
ATOM   11787 H HD13 . LEU   A  1 772 ? 26.117 37.241  -30.237 0.00 53.18  ? 798  LEU   A HD13 1 
ATOM   11788 H HD21 . LEU   A  1 772 ? 26.791 36.284  -32.768 0.00 52.26  ? 798  LEU   A HD21 1 
ATOM   11789 H HD22 . LEU   A  1 772 ? 28.186 36.823  -31.796 0.00 52.35  ? 798  LEU   A HD22 1 
ATOM   11790 H HD23 . LEU   A  1 772 ? 28.198 35.216  -32.574 0.00 51.29  ? 798  LEU   A HD23 1 
ATOM   11791 N N    . VAL   A  1 773 ? 30.056 33.520  -27.771 1.00 33.04  ? 799  VAL   A N    1 
ATOM   11792 C CA   . VAL   A  1 773 ? 31.100 33.467  -26.739 1.00 33.02  ? 799  VAL   A CA   1 
ATOM   11793 C C    . VAL   A  1 773 ? 32.472 33.151  -27.348 1.00 32.20  ? 799  VAL   A C    1 
ATOM   11794 O O    . VAL   A  1 773 ? 33.474 33.562  -26.775 1.00 32.72  ? 799  VAL   A O    1 
ATOM   11795 C CB   . VAL   A  1 773 ? 30.798 32.409  -25.630 1.00 34.17  ? 799  VAL   A CB   1 
ATOM   11796 C CG1  . VAL   A  1 773 ? 29.737 32.906  -24.660 1.00 34.97  ? 799  VAL   A CG1  1 
ATOM   11797 C CG2  . VAL   A  1 773 ? 30.408 31.054  -26.231 1.00 34.43  ? 799  VAL   A CG2  1 
ATOM   11798 H H    . VAL   A  1 773 ? 29.251 32.939  -27.561 0.00 44.17  ? 799  VAL   A H    1 
ATOM   11799 H HA   . VAL   A  1 773 ? 31.184 34.451  -26.280 0.00 44.87  ? 799  VAL   A HA   1 
ATOM   11800 H HB   . VAL   A  1 773 ? 31.709 32.253  -25.055 0.00 45.02  ? 799  VAL   A HB   1 
ATOM   11801 H HG11 . VAL   A  1 773 ? 29.558 32.140  -23.907 0.00 46.37  ? 799  VAL   A HG11 1 
ATOM   11802 H HG12 . VAL   A  1 773 ? 30.093 33.819  -24.185 0.00 47.24  ? 799  VAL   A HG12 1 
ATOM   11803 H HG13 . VAL   A  1 773 ? 28.819 33.108  -25.212 0.00 46.90  ? 799  VAL   A HG13 1 
ATOM   11804 H HG21 . VAL   A  1 773 ? 30.977 30.272  -25.732 0.00 44.26  ? 799  VAL   A HG21 1 
ATOM   11805 H HG22 . VAL   A  1 773 ? 29.343 30.894  -26.070 0.00 44.81  ? 799  VAL   A HG22 1 
ATOM   11806 H HG23 . VAL   A  1 773 ? 30.624 31.030  -27.298 0.00 44.55  ? 799  VAL   A HG23 1 
ATOM   11807 N N    . ASP   A  1 774 ? 32.517 32.392  -28.470 1.00 31.04  ? 800  ASP   A N    1 
ATOM   11808 C CA   . ASP   A  1 774 ? 33.753 32.002  -29.157 1.00 30.66  ? 800  ASP   A CA   1 
ATOM   11809 C C    . ASP   A  1 774 ? 34.125 32.899  -30.358 1.00 30.38  ? 800  ASP   A C    1 
ATOM   11810 O O    . ASP   A  1 774 ? 35.151 32.647  -30.989 1.00 30.45  ? 800  ASP   A O    1 
ATOM   11811 C CB   . ASP   A  1 774 ? 33.665 30.532  -29.599 1.00 32.28  ? 800  ASP   A CB   1 
ATOM   11812 C CG   . ASP   A  1 774 ? 33.431 29.564  -28.455 1.00 37.07  ? 800  ASP   A CG   1 
ATOM   11813 O OD1  . ASP   A  1 774 ? 33.729 29.928  -27.299 1.00 37.20  ? 800  ASP   A OD1  1 
ATOM   11814 O OD2  . ASP   A  1 774 ? 32.973 28.441  -28.719 1.00 40.11  ? 800  ASP   A OD2  1 
ATOM   11815 H H    . ASP   A  1 774 ? 31.696 32.010  -28.927 0.00 40.73  ? 800  ASP   A H    1 
ATOM   11816 H HA   . ASP   A  1 774 ? 34.588 32.070  -28.462 0.00 40.00  ? 800  ASP   A HA   1 
ATOM   11817 H HB2  . ASP   A  1 774 ? 32.837 30.422  -30.298 0.00 41.11  ? 800  ASP   A HB2  1 
ATOM   11818 H HB3  . ASP   A  1 774 ? 34.600 30.244  -30.076 0.00 40.83  ? 800  ASP   A HB3  1 
ATOM   11819 N N    . VAL   A  1 775 ? 33.300 33.918  -30.684 1.00 29.73  ? 801  VAL   A N    1 
ATOM   11820 C CA   . VAL   A  1 775 ? 33.580 34.897  -31.734 1.00 29.74  ? 801  VAL   A CA   1 
ATOM   11821 C C    . VAL   A  1 775 ? 34.251 36.023  -30.919 1.00 30.19  ? 801  VAL   A C    1 
ATOM   11822 O O    . VAL   A  1 775 ? 33.587 36.933  -30.453 1.00 29.21  ? 801  VAL   A O    1 
ATOM   11823 C CB   . VAL   A  1 775 ? 32.277 35.362  -32.446 1.00 30.35  ? 801  VAL   A CB   1 
ATOM   11824 C CG1  . VAL   A  1 775 ? 32.595 36.348  -33.557 1.00 30.95  ? 801  VAL   A CG1  1 
ATOM   11825 C CG2  . VAL   A  1 775 ? 31.498 34.178  -33.017 1.00 30.77  ? 801  VAL   A CG2  1 
ATOM   11826 H H    . VAL   A  1 775 ? 32.408 34.096  -30.235 0.00 40.16  ? 801  VAL   A H    1 
ATOM   11827 H HA   . VAL   A  1 775 ? 34.279 34.518  -32.477 0.00 40.05  ? 801  VAL   A HA   1 
ATOM   11828 H HB   . VAL   A  1 775 ? 31.626 35.860  -31.729 0.00 42.01  ? 801  VAL   A HB   1 
ATOM   11829 H HG11 . VAL   A  1 775 ? 31.661 36.675  -34.012 0.00 43.13  ? 801  VAL   A HG11 1 
ATOM   11830 H HG12 . VAL   A  1 775 ? 33.129 37.208  -33.155 0.00 43.29  ? 801  VAL   A HG12 1 
ATOM   11831 H HG13 . VAL   A  1 775 ? 33.207 35.840  -34.299 0.00 42.37  ? 801  VAL   A HG13 1 
ATOM   11832 H HG21 . VAL   A  1 775 ? 30.594 34.555  -33.492 0.00 41.83  ? 801  VAL   A HG21 1 
ATOM   11833 H HG22 . VAL   A  1 775 ? 32.113 33.671  -33.760 0.00 41.05  ? 801  VAL   A HG22 1 
ATOM   11834 H HG23 . VAL   A  1 775 ? 31.231 33.489  -32.218 0.00 41.12  ? 801  VAL   A HG23 1 
ATOM   11835 N N    . ILE   A  1 776 ? 35.569 35.891  -30.706 1.00 31.37  ? 802  ILE   A N    1 
ATOM   11836 C CA   . ILE   A  1 776 ? 36.402 36.665  -29.773 1.00 32.67  ? 802  ILE   A CA   1 
ATOM   11837 C C    . ILE   A  1 776 ? 37.352 37.699  -30.404 1.00 33.37  ? 802  ILE   A C    1 
ATOM   11838 O O    . ILE   A  1 776 ? 37.874 37.503  -31.500 1.00 33.38  ? 802  ILE   A O    1 
ATOM   11839 C CB   . ILE   A  1 776 ? 37.209 35.602  -28.922 1.00 34.09  ? 802  ILE   A CB   1 
ATOM   11840 C CG1  . ILE   A  1 776 ? 36.257 34.848  -27.967 1.00 35.45  ? 802  ILE   A CG1  1 
ATOM   11841 C CG2  . ILE   A  1 776 ? 38.349 36.232  -28.117 1.00 35.07  ? 802  ILE   A CG2  1 
ATOM   11842 C CD1  . ILE   A  1 776 ? 36.764 33.407  -27.538 1.00 36.89  ? 802  ILE   A CD1  1 
ATOM   11843 H H    . ILE   A  1 776 ? 36.121 35.208  -31.214 0.00 42.30  ? 802  ILE   A H    1 
ATOM   11844 H HA   . ILE   A  1 776 ? 35.754 37.205  -29.086 0.00 45.32  ? 802  ILE   A HA   1 
ATOM   11845 H HB   . ILE   A  1 776 ? 37.684 34.872  -29.577 0.00 45.39  ? 802  ILE   A HB   1 
ATOM   11846 H HG12 . ILE   A  1 776 ? 36.147 35.438  -27.058 0.00 47.71  ? 802  ILE   A HG12 1 
ATOM   11847 H HG13 . ILE   A  1 776 ? 35.283 34.724  -28.437 0.00 47.18  ? 802  ILE   A HG13 1 
ATOM   11848 H HG21 . ILE   A  1 776 ? 38.678 35.540  -27.343 0.00 47.18  ? 802  ILE   A HG21 1 
ATOM   11849 H HG22 . ILE   A  1 776 ? 39.189 36.441  -28.778 0.00 47.53  ? 802  ILE   A HG22 1 
ATOM   11850 H HG23 . ILE   A  1 776 ? 37.997 37.153  -27.655 0.00 48.17  ? 802  ILE   A HG23 1 
ATOM   11851 H HD11 . ILE   A  1 776 ? 36.030 32.967  -26.865 0.00 48.01  ? 802  ILE   A HD11 1 
ATOM   11852 H HD12 . ILE   A  1 776 ? 36.865 32.790  -28.429 0.00 47.70  ? 802  ILE   A HD12 1 
ATOM   11853 H HD13 . ILE   A  1 776 ? 37.723 33.483  -27.029 0.00 48.22  ? 802  ILE   A HD13 1 
ATOM   11854 N N    . CYS   A  1 777 ? 37.636 38.767  -29.639 1.00 33.84  ? 803  CYS   A N    1 
ATOM   11855 C CA   . CYS   A  1 777 ? 38.567 39.823  -30.016 1.00 34.74  ? 803  CYS   A CA   1 
ATOM   11856 C C    . CYS   A  1 777 ? 39.981 39.322  -29.779 1.00 35.47  ? 803  CYS   A C    1 
ATOM   11857 O O    . CYS   A  1 777 ? 40.285 38.914  -28.659 1.00 35.95  ? 803  CYS   A O    1 
ATOM   11858 C CB   . CYS   A  1 777 ? 38.326 41.082  -29.181 1.00 35.48  ? 803  CYS   A CB   1 
ATOM   11859 S SG   . CYS   A  1 777 ? 36.643 41.741  -29.258 1.00 40.98  ? 803  CYS   A SG   1 
ATOM   11860 H H    . CYS   A  1 777 ? 37.225 38.924  -28.724 0.00 47.78  ? 803  CYS   A H    1 
ATOM   11861 H HA   . CYS   A  1 777 ? 38.438 40.075  -31.068 0.00 49.32  ? 803  CYS   A HA   1 
ATOM   11862 H HB2  . CYS   A  1 777 ? 38.536 40.855  -28.137 0.00 51.07  ? 803  CYS   A HB2  1 
ATOM   11863 H HB3  . CYS   A  1 777 ? 39.000 41.864  -29.527 0.00 51.59  ? 803  CYS   A HB3  1 
ATOM   11864 N N    . ALA   A  1 778 ? 40.860 39.433  -30.775 1.00 35.53  ? 804  ALA   A N    1 
ATOM   11865 C CA   . ALA   A  1 778 ? 42.282 39.127  -30.612 1.00 36.39  ? 804  ALA   A CA   1 
ATOM   11866 C C    . ALA   A  1 778 ? 43.088 40.407  -30.304 1.00 36.98  ? 804  ALA   A C    1 
ATOM   11867 O O    . ALA   A  1 778 ? 44.187 40.306  -29.771 1.00 36.91  ? 804  ALA   A O    1 
ATOM   11868 C CB   . ALA   A  1 778 ? 42.833 38.478  -31.866 1.00 36.70  ? 804  ALA   A CB   1 
ATOM   11869 H H    . ALA   A  1 778 ? 40.621 39.737  -31.714 0.00 49.91  ? 804  ALA   A H    1 
ATOM   11870 H HA   . ALA   A  1 778 ? 42.430 38.427  -29.792 0.00 50.24  ? 804  ALA   A HA   1 
ATOM   11871 H HB1  . ALA   A  1 778 ? 43.911 38.370  -31.758 0.00 50.41  ? 804  ALA   A HB1  1 
ATOM   11872 H HB2  . ALA   A  1 778 ? 42.381 37.494  -31.980 0.00 49.81  ? 804  ALA   A HB2  1 
ATOM   11873 H HB3  . ALA   A  1 778 ? 42.607 39.098  -32.731 0.00 50.79  ? 804  ALA   A HB3  1 
ATOM   11874 N N    . SER   A  1 779 ? 42.556 41.601  -30.661 1.00 37.46  ? 805  SER   A N    1 
ATOM   11875 C CA   . SER   A  1 779 ? 43.210 42.891  -30.462 1.00 38.46  ? 805  SER   A CA   1 
ATOM   11876 C C    . SER   A  1 779 ? 42.158 44.009  -30.358 1.00 39.41  ? 805  SER   A C    1 
ATOM   11877 O O    . SER   A  1 779 ? 41.076 43.850  -30.917 1.00 39.53  ? 805  SER   A O    1 
ATOM   11878 C CB   . SER   A  1 779 ? 44.125 43.183  -31.651 1.00 39.79  ? 805  SER   A CB   1 
ATOM   11879 O OG   . SER   A  1 779 ? 43.405 43.418  -32.849 1.00 42.81  ? 805  SER   A OG   1 
ATOM   11880 H H    . SER   A  1 779 ? 41.656 41.699  -31.120 0.00 53.60  ? 805  SER   A H    1 
ATOM   11881 H HA   . SER   A  1 779 ? 43.803 42.865  -29.549 0.00 55.83  ? 805  SER   A HA   1 
ATOM   11882 H HB2  . SER   A  1 779 ? 44.726 44.068  -31.451 0.00 58.13  ? 805  SER   A HB2  1 
ATOM   11883 H HB3  . SER   A  1 779 ? 44.775 42.323  -31.806 0.00 56.83  ? 805  SER   A HB3  1 
ATOM   11884 H HG   . SER   A  1 779 ? 42.938 42.591  -33.138 0.00 60.48  ? 805  SER   A HG   1 
ATOM   11885 N N    . PRO   A  1 780 ? 42.461 45.177  -29.743 1.00 39.93  ? 806  PRO   A N    1 
ATOM   11886 C CA   . PRO   A  1 780 ? 43.671 45.504  -28.966 1.00 40.18  ? 806  PRO   A CA   1 
ATOM   11887 C C    . PRO   A  1 780 ? 43.704 44.745  -27.627 1.00 40.56  ? 806  PRO   A C    1 
ATOM   11888 O O    . PRO   A  1 780 ? 42.778 43.999  -27.303 1.00 40.31  ? 806  PRO   A O    1 
ATOM   11889 C CB   . PRO   A  1 780 ? 43.567 47.027  -28.806 1.00 40.83  ? 806  PRO   A CB   1 
ATOM   11890 C CG   . PRO   A  1 780 ? 42.100 47.293  -28.756 1.00 41.15  ? 806  PRO   A CG   1 
ATOM   11891 C CD   . PRO   A  1 780 ? 41.460 46.262  -29.659 1.00 39.40  ? 806  PRO   A CD   1 
ATOM   11892 H HA   . PRO   A  1 780 ? 44.577 45.275  -29.524 0.00 59.72  ? 806  PRO   A HA   1 
ATOM   11893 H HB2  . PRO   A  1 780 ? 44.049 47.336  -27.879 0.00 62.33  ? 806  PRO   A HB2  1 
ATOM   11894 H HB3  . PRO   A  1 780 ? 44.020 47.521  -29.665 0.00 62.24  ? 806  PRO   A HB3  1 
ATOM   11895 H HG2  . PRO   A  1 780 ? 41.747 47.180  -27.733 0.00 62.58  ? 806  PRO   A HG2  1 
ATOM   11896 H HG3  . PRO   A  1 780 ? 41.898 48.299  -29.122 0.00 63.31  ? 806  PRO   A HG3  1 
ATOM   11897 H HD2  . PRO   A  1 780 ? 40.536 45.894  -29.216 0.00 59.28  ? 806  PRO   A HD2  1 
ATOM   11898 H HD3  . PRO   A  1 780 ? 41.284 46.685  -30.647 0.00 59.73  ? 806  PRO   A HD3  1 
ATOM   11899 N N    . GLY   A  1 781 ? 44.789 44.906  -26.872 1.00 41.14  ? 807  GLY   A N    1 
ATOM   11900 C CA   . GLY   A  1 781 ? 44.976 44.223  -25.592 1.00 42.39  ? 807  GLY   A CA   1 
ATOM   11901 C C    . GLY   A  1 781 ? 43.816 44.336  -24.621 1.00 43.56  ? 807  GLY   A C    1 
ATOM   11902 O O    . GLY   A  1 781 ? 43.408 43.342  -24.022 1.00 43.51  ? 807  GLY   A O    1 
ATOM   11903 H H    . GLY   A  1 781 ? 45.563 45.512  -27.122 0.00 61.43  ? 807  GLY   A H    1 
ATOM   11904 H HA2  . GLY   A  1 781 ? 45.151 43.165  -25.781 0.00 61.38  ? 807  GLY   A HA2  1 
ATOM   11905 H HA3  . GLY   A  1 781 ? 45.861 44.627  -25.104 0.00 62.64  ? 807  GLY   A HA3  1 
ATOM   11906 N N    . ASP   A  1 782 ? 43.271 45.545  -24.469 1.00 44.70  ? 808  ASP   A N    1 
ATOM   11907 C CA   . ASP   A  1 782 ? 42.133 45.792  -23.569 1.00 46.19  ? 808  ASP   A CA   1 
ATOM   11908 C C    . ASP   A  1 782 ? 40.846 45.022  -23.933 1.00 46.47  ? 808  ASP   A C    1 
ATOM   11909 O O    . ASP   A  1 782 ? 40.007 44.822  -23.054 1.00 46.65  ? 808  ASP   A O    1 
ATOM   11910 C CB   . ASP   A  1 782 ? 41.831 47.297  -23.474 1.00 49.46  ? 808  ASP   A CB   1 
ATOM   11911 C CG   . ASP   A  1 782 ? 41.704 47.999  -24.812 1.00 57.22  ? 808  ASP   A CG   1 
ATOM   11912 O OD1  . ASP   A  1 782 ? 42.739 48.154  -25.500 1.00 59.30  ? 808  ASP   A OD1  1 
ATOM   11913 O OD2  . ASP   A  1 782 ? 40.575 48.404  -25.165 1.00 60.16  ? 808  ASP   A OD2  1 
ATOM   11914 H H    . ASP   A  1 782 ? 43.635 46.371  -24.932 0.00 66.68  ? 808  ASP   A H    1 
ATOM   11915 H HA   . ASP   A  1 782 ? 42.424 45.463  -22.572 0.00 68.19  ? 808  ASP   A HA   1 
ATOM   11916 H HB2  . ASP   A  1 782 ? 40.893 47.430  -22.939 0.00 73.61  ? 808  ASP   A HB2  1 
ATOM   11917 H HB3  . ASP   A  1 782 ? 42.639 47.778  -22.925 0.00 73.90  ? 808  ASP   A HB3  1 
ATOM   11918 N N    . GLN   A  1 783 ? 40.687 44.597  -25.206 1.00 46.22  ? 809  GLN   A N    1 
ATOM   11919 C CA   . GLN   A  1 783 ? 39.504 43.859  -25.674 1.00 46.33  ? 809  GLN   A CA   1 
ATOM   11920 C C    . GLN   A  1 783 ? 39.743 42.360  -25.861 1.00 46.70  ? 809  GLN   A C    1 
ATOM   11921 O O    . GLN   A  1 783 ? 38.772 41.617  -26.032 1.00 46.84  ? 809  GLN   A O    1 
ATOM   11922 C CB   . GLN   A  1 783 ? 39.001 44.454  -27.000 1.00 47.32  ? 809  GLN   A CB   1 
ATOM   11923 C CG   . GLN   A  1 783 ? 38.789 45.968  -26.983 1.00 49.16  ? 809  GLN   A CG   1 
ATOM   11924 C CD   . GLN   A  1 783 ? 37.821 46.424  -25.918 1.00 52.99  ? 809  GLN   A CD   1 
ATOM   11925 O OE1  . GLN   A  1 783 ? 36.971 45.661  -25.449 1.00 54.07  ? 809  GLN   A OE1  1 
ATOM   11926 N NE2  . GLN   A  1 783 ? 37.920 47.690  -25.519 1.00 53.67  ? 809  GLN   A NE2  1 
ATOM   11927 H H    . GLN   A  1 783 ? 41.359 44.758  -25.949 0.00 67.05  ? 809  GLN   A H    1 
ATOM   11928 H HA   . GLN   A  1 783 ? 38.697 43.954  -24.949 0.00 66.80  ? 809  GLN   A HA   1 
ATOM   11929 H HB2  . GLN   A  1 783 ? 39.733 44.235  -27.776 0.00 67.74  ? 809  GLN   A HB2  1 
ATOM   11930 H HB3  . GLN   A  1 783 ? 38.051 43.988  -27.254 0.00 67.69  ? 809  GLN   A HB3  1 
ATOM   11931 H HG2  . GLN   A  1 783 ? 39.743 46.463  -26.810 0.00 71.83  ? 809  GLN   A HG2  1 
ATOM   11932 H HG3  . GLN   A  1 783 ? 38.387 46.274  -27.948 0.00 71.58  ? 809  GLN   A HG3  1 
ATOM   11933 H HE21 . GLN   A  1 783 ? 38.618 48.303  -25.927 0.00 78.92  ? 809  GLN   A HE21 1 
ATOM   11934 H HE22 . GLN   A  1 783 ? 37.292 48.045  -24.805 0.00 78.96  ? 809  GLN   A HE22 1 
ATOM   11935 N N    . ARG   A  1 784 ? 41.011 41.902  -25.839 1.00 46.61  ? 810  ARG   A N    1 
ATOM   11936 C CA   . ARG   A  1 784 ? 41.352 40.486  -26.006 1.00 46.83  ? 810  ARG   A CA   1 
ATOM   11937 C C    . ARG   A  1 784 ? 40.559 39.569  -25.049 1.00 45.71  ? 810  ARG   A C    1 
ATOM   11938 O O    . ARG   A  1 784 ? 40.366 39.915  -23.885 1.00 45.39  ? 810  ARG   A O    1 
ATOM   11939 C CB   . ARG   A  1 784 ? 42.873 40.293  -25.830 1.00 49.36  ? 810  ARG   A CB   1 
ATOM   11940 C CG   . ARG   A  1 784 ? 43.354 38.836  -25.758 1.00 54.67  ? 810  ARG   A CG   1 
ATOM   11941 C CD   . ARG   A  1 784 ? 44.686 38.561  -26.451 1.00 59.38  ? 810  ARG   A CD   1 
ATOM   11942 N NE   . ARG   A  1 784 ? 45.698 39.611  -26.289 1.00 63.49  ? 810  ARG   A NE   1 
ATOM   11943 C CZ   . ARG   A  1 784 ? 46.882 39.615  -26.898 1.00 67.32  ? 810  ARG   A CZ   1 
ATOM   11944 N NH1  . ARG   A  1 784 ? 47.727 40.622  -26.712 1.00 67.80  ? 810  ARG   A NH1  1 
ATOM   11945 N NH2  . ARG   A  1 784 ? 47.223 38.625  -27.713 1.00 68.06  ? 810  ARG   A NH2  1 
ATOM   11946 H H    . ARG   A  1 784 ? 41.825 42.497  -25.723 0.00 65.87  ? 810  ARG   A H    1 
ATOM   11947 H HA   . ARG   A  1 784 ? 41.108 40.198  -27.028 0.00 64.31  ? 810  ARG   A HA   1 
ATOM   11948 H HB2  . ARG   A  1 784 ? 43.370 40.768  -26.675 0.00 67.82  ? 810  ARG   A HB2  1 
ATOM   11949 H HB3  . ARG   A  1 784 ? 43.182 40.779  -24.906 0.00 68.12  ? 810  ARG   A HB3  1 
ATOM   11950 H HG2  . ARG   A  1 784 ? 43.462 38.555  -24.712 0.00 73.02  ? 810  ARG   A HG2  1 
ATOM   11951 H HG3  . ARG   A  1 784 ? 42.620 38.192  -26.240 0.00 72.50  ? 810  ARG   A HG3  1 
ATOM   11952 H HD2  . ARG   A  1 784 ? 45.102 37.637  -26.051 0.00 77.95  ? 810  ARG   A HD2  1 
ATOM   11953 H HD3  . ARG   A  1 784 ? 44.501 38.447  -27.519 0.00 78.21  ? 810  ARG   A HD3  1 
ATOM   11954 H HE   . ARG   A  1 784 ? 45.487 40.390  -25.673 0.00 84.80  ? 810  ARG   A HE   1 
ATOM   11955 H HH11 . ARG   A  1 784 ? 47.489 41.392  -26.096 0.00 90.77  ? 810  ARG   A HH11 1 
ATOM   11956 H HH12 . ARG   A  1 784 ? 48.622 40.619  -27.191 0.00 90.18  ? 810  ARG   A HH12 1 
ATOM   11957 H HH21 . ARG   A  1 784 ? 46.593 37.851  -27.899 0.00 88.36  ? 810  ARG   A HH21 1 
ATOM   11958 H HH22 . ARG   A  1 784 ? 48.121 38.648  -28.185 0.00 88.99  ? 810  ARG   A HH22 1 
ATOM   11959 N N    . GLY   A  1 785 ? 40.096 38.430  -25.569 1.00 44.74  ? 811  GLY   A N    1 
ATOM   11960 C CA   . GLY   A  1 785 ? 39.325 37.456  -24.801 1.00 44.30  ? 811  GLY   A CA   1 
ATOM   11961 C C    . GLY   A  1 785 ? 37.822 37.669  -24.823 1.00 43.70  ? 811  GLY   A C    1 
ATOM   11962 O O    . GLY   A  1 785 ? 37.060 36.710  -24.688 1.00 43.98  ? 811  GLY   A O    1 
ATOM   11963 H H    . GLY   A  1 785 ? 40.246 38.142  -26.530 0.00 60.51  ? 811  GLY   A H    1 
ATOM   11964 H HA2  . GLY   A  1 785 ? 39.522 36.464  -25.205 0.00 59.10  ? 811  GLY   A HA2  1 
ATOM   11965 H HA3  . GLY   A  1 785 ? 39.653 37.459  -23.762 0.00 59.97  ? 811  GLY   A HA3  1 
ATOM   11966 N N    . LYS   A  1 786 ? 37.376 38.912  -25.004 1.00 42.82  ? 812  LYS   A N    1 
ATOM   11967 C CA   . LYS   A  1 786 ? 35.955 39.238  -25.005 1.00 43.12  ? 812  LYS   A CA   1 
ATOM   11968 C C    . LYS   A  1 786 ? 35.275 38.967  -26.346 1.00 42.65  ? 812  LYS   A C    1 
ATOM   11969 O O    . LYS   A  1 786 ? 35.881 39.145  -27.401 1.00 42.69  ? 812  LYS   A O    1 
ATOM   11970 C CB   . LYS   A  1 786 ? 35.762 40.717  -24.626 1.00 45.74  ? 812  LYS   A CB   1 
ATOM   11971 C CG   . LYS   A  1 786 ? 36.248 41.053  -23.218 1.00 51.02  ? 812  LYS   A CG   1 
ATOM   11972 C CD   . LYS   A  1 786 ? 36.188 42.546  -22.950 1.00 57.23  ? 812  LYS   A CD   1 
ATOM   11973 C CE   . LYS   A  1 786 ? 36.666 42.901  -21.561 1.00 62.08  ? 812  LYS   A CE   1 
ATOM   11974 N NZ   . LYS   A  1 786 ? 35.649 42.579  -20.521 1.00 65.34  ? 812  LYS   A NZ   1 
ATOM   11975 H H    . LYS   A  1 786 ? 37.970 39.723  -25.142 0.00 59.54  ? 812  LYS   A H    1 
ATOM   11976 H HA   . LYS   A  1 786 ? 35.452 38.647  -24.242 0.00 59.47  ? 812  LYS   A HA   1 
ATOM   11977 H HB2  . LYS   A  1 786 ? 36.307 41.343  -25.331 0.00 64.25  ? 812  LYS   A HB2  1 
ATOM   11978 H HB3  . LYS   A  1 786 ? 34.699 40.952  -24.674 0.00 64.21  ? 812  LYS   A HB3  1 
ATOM   11979 H HG2  . LYS   A  1 786 ? 35.611 40.551  -22.491 0.00 70.58  ? 812  LYS   A HG2  1 
ATOM   11980 H HG3  . LYS   A  1 786 ? 37.282 40.734  -23.097 0.00 70.46  ? 812  LYS   A HG3  1 
ATOM   11981 H HD2  . LYS   A  1 786 ? 36.824 43.061  -23.667 0.00 79.52  ? 812  LYS   A HD2  1 
ATOM   11982 H HD3  . LYS   A  1 786 ? 35.158 42.886  -23.052 0.00 79.66  ? 812  LYS   A HD3  1 
ATOM   11983 H HE2  . LYS   A  1 786 ? 37.569 42.334  -21.338 0.00 85.22  ? 812  LYS   A HE2  1 
ATOM   11984 H HE3  . LYS   A  1 786 ? 36.873 43.969  -21.515 0.00 86.45  ? 812  LYS   A HE3  1 
ATOM   11985 H HZ1  . LYS   A  1 786 ? 36.004 42.825  -19.603 0.00 90.04  ? 812  LYS   A HZ1  1 
ATOM   11986 H HZ2  . LYS   A  1 786 ? 34.799 43.105  -20.696 0.00 90.15  ? 812  LYS   A HZ2  1 
ATOM   11987 H HZ3  . LYS   A  1 786 ? 35.432 41.588  -20.536 0.00 88.98  ? 812  LYS   A HZ3  1 
ATOM   11988 N N    . SER   A  1 787 ? 33.995 38.582  -26.301 1.00 42.04  ? 813  SER   A N    1 
ATOM   11989 C CA   . SER   A  1 787 ? 33.196 38.366  -27.505 1.00 41.92  ? 813  SER   A CA   1 
ATOM   11990 C C    . SER   A  1 787 ? 33.032 39.697  -28.241 1.00 41.74  ? 813  SER   A C    1 
ATOM   11991 O O    . SER   A  1 787 ? 32.955 40.749  -27.596 1.00 41.77  ? 813  SER   A O    1 
ATOM   11992 C CB   . SER   A  1 787 ? 31.817 37.824  -27.135 1.00 42.79  ? 813  SER   A CB   1 
ATOM   11993 O OG   . SER   A  1 787 ? 30.998 37.669  -28.283 1.00 44.08  ? 813  SER   A OG   1 
ATOM   11994 H H    . SER   A  1 787 ? 33.483 38.410  -25.442 0.00 58.04  ? 813  SER   A H    1 
ATOM   11995 H HA   . SER   A  1 787 ? 33.686 37.649  -28.161 0.00 57.02  ? 813  SER   A HA   1 
ATOM   11996 H HB2  . SER   A  1 787 ? 31.936 36.855  -26.653 0.00 57.96  ? 813  SER   A HB2  1 
ATOM   11997 H HB3  . SER   A  1 787 ? 31.334 38.522  -26.452 0.00 59.18  ? 813  SER   A HB3  1 
ATOM   11998 H HG   . SER   A  1 787 ? 30.130 37.259  -28.029 0.00 59.80  ? 813  SER   A HG   1 
ATOM   11999 N N    . ILE   A  1 788 ? 32.967 39.660  -29.581 1.00 41.43  ? 814  ILE   A N    1 
ATOM   12000 C CA   . ILE   A  1 788 ? 32.800 40.887  -30.361 1.00 42.14  ? 814  ILE   A CA   1 
ATOM   12001 C C    . ILE   A  1 788 ? 31.468 41.584  -30.018 1.00 43.71  ? 814  ILE   A C    1 
ATOM   12002 O O    . ILE   A  1 788 ? 31.395 42.804  -30.084 1.00 43.78  ? 814  ILE   A O    1 
ATOM   12003 C CB   . ILE   A  1 788 ? 32.971 40.652  -31.892 1.00 41.94  ? 814  ILE   A CB   1 
ATOM   12004 C CG1  . ILE   A  1 788 ? 31.791 39.858  -32.497 1.00 42.50  ? 814  ILE   A CG1  1 
ATOM   12005 C CG2  . ILE   A  1 788 ? 34.324 39.975  -32.191 1.00 41.99  ? 814  ILE   A CG2  1 
ATOM   12006 C CD1  . ILE   A  1 788 ? 31.815 39.791  -34.010 1.00 43.60  ? 814  ILE   A CD1  1 
ATOM   12007 H H    . ILE   A  1 788 ? 33.002 38.806  -30.128 0.00 57.11  ? 814  ILE   A H    1 
ATOM   12008 H HA   . ILE   A  1 788 ? 33.594 41.573  -30.068 0.00 59.82  ? 814  ILE   A HA   1 
ATOM   12009 H HB   . ILE   A  1 788 ? 32.984 41.629  -32.372 0.00 59.54  ? 814  ILE   A HB   1 
ATOM   12010 H HG12 . ILE   A  1 788 ? 31.821 38.838  -32.115 0.00 58.46  ? 814  ILE   A HG12 1 
ATOM   12011 H HG13 . ILE   A  1 788 ? 30.844 40.323  -32.227 0.00 59.65  ? 814  ILE   A HG13 1 
ATOM   12012 H HG21 . ILE   A  1 788 ? 34.532 40.036  -33.258 0.00 58.22  ? 814  ILE   A HG21 1 
ATOM   12013 H HG22 . ILE   A  1 788 ? 35.105 40.488  -31.631 0.00 58.56  ? 814  ILE   A HG22 1 
ATOM   12014 H HG23 . ILE   A  1 788 ? 34.272 38.932  -31.884 0.00 57.58  ? 814  ILE   A HG23 1 
ATOM   12015 H HD11 . ILE   A  1 788 ? 30.879 39.355  -34.357 0.00 60.22  ? 814  ILE   A HD11 1 
ATOM   12016 H HD12 . ILE   A  1 788 ? 31.927 40.799  -34.408 0.00 61.04  ? 814  ILE   A HD12 1 
ATOM   12017 H HD13 . ILE   A  1 788 ? 32.648 39.169  -34.332 0.00 59.79  ? 814  ILE   A HD13 1 
ATOM   12018 N N    . VAL   A  1 789 ? 30.434 40.817  -29.631 1.00 44.98  ? 815  VAL   A N    1 
ATOM   12019 C CA   . VAL   A  1 789 ? 29.127 41.367  -29.269 1.00 46.99  ? 815  VAL   A CA   1 
ATOM   12020 C C    . VAL   A  1 789 ? 29.160 42.088  -27.885 1.00 49.11  ? 815  VAL   A C    1 
ATOM   12021 O O    . VAL   A  1 789 ? 28.258 42.873  -27.596 1.00 49.52  ? 815  VAL   A O    1 
ATOM   12022 C CB   . VAL   A  1 789 ? 28.016 40.266  -29.357 1.00 47.72  ? 815  VAL   A CB   1 
ATOM   12023 C CG1  . VAL   A  1 789 ? 28.051 39.351  -28.144 1.00 48.05  ? 815  VAL   A CG1  1 
ATOM   12024 C CG2  . VAL   A  1 789 ? 26.627 40.877  -29.512 1.00 48.80  ? 815  VAL   A CG2  1 
ATOM   12025 H H    . VAL   A  1 789 ? 30.462 39.804  -29.576 0.00 62.51  ? 815  VAL   A H    1 
ATOM   12026 H HA   . VAL   A  1 789 ? 28.901 42.135  -30.008 0.00 66.88  ? 815  VAL   A HA   1 
ATOM   12027 H HB   . VAL   A  1 789 ? 28.174 39.644  -30.237 0.00 66.10  ? 815  VAL   A HB   1 
ATOM   12028 H HG11 . VAL   A  1 789 ? 27.534 38.425  -28.390 0.00 65.96  ? 815  VAL   A HG11 1 
ATOM   12029 H HG12 . VAL   A  1 789 ? 29.089 39.146  -27.886 0.00 66.17  ? 815  VAL   A HG12 1 
ATOM   12030 H HG13 . VAL   A  1 789 ? 27.546 39.835  -27.309 0.00 67.04  ? 815  VAL   A HG13 1 
ATOM   12031 H HG21 . VAL   A  1 789 ? 25.896 40.074  -29.598 0.00 68.30  ? 815  VAL   A HG21 1 
ATOM   12032 H HG22 . VAL   A  1 789 ? 26.406 41.487  -28.638 0.00 69.26  ? 815  VAL   A HG22 1 
ATOM   12033 H HG23 . VAL   A  1 789 ? 26.609 41.494  -30.410 0.00 69.09  ? 815  VAL   A HG23 1 
ATOM   12034 N N    . SER   A  1 790 ? 30.197 41.851  -27.052 1.00 50.42  ? 816  SER   A N    1 
ATOM   12035 C CA   . SER   A  1 790 ? 30.348 42.521  -25.753 1.00 52.26  ? 816  SER   A CA   1 
ATOM   12036 C C    . SER   A  1 790 ? 31.055 43.896  -25.853 1.00 54.09  ? 816  SER   A C    1 
ATOM   12037 O O    . SER   A  1 790 ? 31.063 44.639  -24.871 1.00 54.43  ? 816  SER   A O    1 
ATOM   12038 C CB   . SER   A  1 790 ? 31.139 41.638  -24.792 1.00 53.72  ? 816  SER   A CB   1 
ATOM   12039 O OG   . SER   A  1 790 ? 30.485 40.401  -24.563 1.00 56.68  ? 816  SER   A OG   1 
ATOM   12040 H H    . SER   A  1 790 ? 30.944 41.188  -27.235 0.00 70.14  ? 816  SER   A H    1 
ATOM   12041 H HA   . SER   A  1 790 ? 29.367 42.681  -25.307 0.00 73.98  ? 816  SER   A HA   1 
ATOM   12042 H HB2  . SER   A  1 790 ? 32.124 41.444  -25.215 0.00 74.36  ? 816  SER   A HB2  1 
ATOM   12043 H HB3  . SER   A  1 790 ? 31.243 42.157  -23.841 0.00 75.21  ? 816  SER   A HB3  1 
ATOM   12044 H HG   . SER   A  1 790 ? 31.021 39.845  -23.939 0.00 77.10  ? 816  SER   A HG   1 
ATOM   12045 N N    . LEU   A  1 791 ? 31.676 44.216  -27.004 1.00 55.03  ? 817  LEU   A N    1 
ATOM   12046 C CA   . LEU   A  1 791 ? 32.403 45.474  -27.192 1.00 56.47  ? 817  LEU   A CA   1 
ATOM   12047 C C    . LEU   A  1 791 ? 31.480 46.699  -27.016 1.00 57.91  ? 817  LEU   A C    1 
ATOM   12048 O O    . LEU   A  1 791 ? 30.317 46.657  -27.422 1.00 58.19  ? 817  LEU   A O    1 
ATOM   12049 C CB   . LEU   A  1 791 ? 33.079 45.475  -28.581 1.00 56.98  ? 817  LEU   A CB   1 
ATOM   12050 C CG   . LEU   A  1 791 ? 33.900 46.701  -28.981 1.00 59.14  ? 817  LEU   A CG   1 
ATOM   12051 C CD1  . LEU   A  1 791 ? 35.090 46.905  -28.066 1.00 59.89  ? 817  LEU   A CD1  1 
ATOM   12052 C CD2  . LEU   A  1 791 ? 34.353 46.592  -30.418 1.00 59.92  ? 817  LEU   A CD2  1 
ATOM   12053 H H    . LEU   A  1 791 ? 31.692 43.614  -27.822 0.00 77.31  ? 817  LEU   A H    1 
ATOM   12054 H HA   . LEU   A  1 791 ? 33.182 45.524  -26.434 0.00 80.45  ? 817  LEU   A HA   1 
ATOM   12055 H HB2  . LEU   A  1 791 ? 33.749 44.617  -28.624 0.00 80.01  ? 817  LEU   A HB2  1 
ATOM   12056 H HB3  . LEU   A  1 791 ? 32.301 45.356  -29.334 0.00 80.73  ? 817  LEU   A HB3  1 
ATOM   12057 H HG   . LEU   A  1 791 ? 33.273 47.589  -28.921 0.00 85.03  ? 817  LEU   A HG   1 
ATOM   12058 H HD11 . LEU   A  1 791 ? 35.680 47.749  -28.421 0.00 85.81  ? 817  LEU   A HD11 1 
ATOM   12059 H HD12 . LEU   A  1 791 ? 34.741 47.116  -27.057 0.00 85.53  ? 817  LEU   A HD12 1 
ATOM   12060 H HD13 . LEU   A  1 791 ? 35.696 46.001  -28.068 0.00 84.42  ? 817  LEU   A HD13 1 
ATOM   12061 H HD21 . LEU   A  1 791 ? 35.256 47.181  -30.570 0.00 85.20  ? 817  LEU   A HD21 1 
ATOM   12062 H HD22 . LEU   A  1 791 ? 34.535 45.546  -30.658 0.00 83.97  ? 817  LEU   A HD22 1 
ATOM   12063 H HD23 . LEU   A  1 791 ? 33.559 46.976  -31.058 0.00 85.22  ? 817  LEU   A HD23 1 
ATOM   12064 N N    . GLU   A  1 792 ? 32.006 47.779  -26.388 1.00 58.51  ? 818  GLU   A N    1 
ATOM   12065 C CA   . GLU   A  1 792 ? 31.283 49.023  -26.098 1.00 59.55  ? 818  GLU   A CA   1 
ATOM   12066 C C    . GLU   A  1 792 ? 30.206 48.784  -25.036 1.00 60.30  ? 818  GLU   A C    1 
ATOM   12067 O O    . GLU   A  1 792 ? 30.323 49.278  -23.913 1.00 60.65  ? 818  GLU   A O    1 
ATOM   12068 C CB   . GLU   A  1 792 ? 30.665 49.657  -27.363 1.00 61.73  ? 818  GLU   A CB   1 
ATOM   12069 C CG   . GLU   A  1 792 ? 31.684 50.233  -28.326 1.00 66.54  ? 818  GLU   A CG   1 
ATOM   12070 C CD   . GLU   A  1 792 ? 31.226 50.221  -29.771 1.00 73.64  ? 818  GLU   A CD   1 
ATOM   12071 O OE1  . GLU   A  1 792 ? 30.565 51.200  -30.186 1.00 74.63  ? 818  GLU   A OE1  1 
ATOM   12072 O OE2  . GLU   A  1 792 ? 31.525 49.238  -30.489 1.00 76.27  ? 818  GLU   A OE2  1 
ATOM   12073 H H    . GLU   A  1 792 ? 32.965 47.813  -26.057 0.00 84.87  ? 818  GLU   A H    1 
ATOM   12074 H HA   . GLU   A  1 792 ? 31.993 49.740  -25.689 0.00 87.97  ? 818  GLU   A HA   1 
ATOM   12075 H HB2  . GLU   A  1 792 ? 30.074 48.916  -27.900 0.00 89.92  ? 818  GLU   A HB2  1 
ATOM   12076 H HB3  . GLU   A  1 792 ? 30.017 50.476  -27.052 0.00 91.39  ? 818  GLU   A HB3  1 
ATOM   12077 H HG2  . GLU   A  1 792 ? 31.863 51.271  -28.053 0.00 97.43  ? 818  GLU   A HG2  1 
ATOM   12078 H HG3  . GLU   A  1 792 ? 32.615 49.675  -28.251 0.00 95.86  ? 818  GLU   A HG3  1 
ATOM   12079 N N    . ARG   B  1 6   ? 71.486 40.628  -32.477 1.00 41.32  ? 32   ARG   B N    1 
ATOM   12080 C CA   . ARG   B  1 6   ? 70.722 39.417  -32.785 1.00 41.38  ? 32   ARG   B CA   1 
ATOM   12081 C C    . ARG   B  1 6   ? 70.379 39.402  -34.275 1.00 41.68  ? 32   ARG   B C    1 
ATOM   12082 O O    . ARG   B  1 6   ? 69.825 40.376  -34.778 1.00 42.23  ? 32   ARG   B O    1 
ATOM   12083 C CB   . ARG   B  1 6   ? 69.433 39.383  -31.940 1.00 41.94  ? 32   ARG   B CB   1 
ATOM   12084 C CG   . ARG   B  1 6   ? 69.117 38.043  -31.299 1.00 43.01  ? 32   ARG   B CG   1 
ATOM   12085 C CD   . ARG   B  1 6   ? 67.931 38.159  -30.362 1.00 42.97  ? 32   ARG   B CD   1 
ATOM   12086 N NE   . ARG   B  1 6   ? 68.313 38.160  -28.952 1.00 43.00  ? 32   ARG   B NE   1 
ATOM   12087 C CZ   . ARG   B  1 6   ? 68.629 37.075  -28.246 1.00 41.92  ? 32   ARG   B CZ   1 
ATOM   12088 N NH1  . ARG   B  1 6   ? 68.664 35.879  -28.827 1.00 40.09  ? 32   ARG   B NH1  1 
ATOM   12089 N NH2  . ARG   B  1 6   ? 68.950 37.182  -26.964 1.00 40.06  ? 32   ARG   B NH2  1 
ATOM   12090 H HA   . ARG   B  1 6   ? 71.357 38.559  -32.567 0.00 57.92  ? 32   ARG   B HA   1 
ATOM   12091 H HB2  . ARG   B  1 6   ? 69.517 40.110  -31.132 0.00 59.47  ? 32   ARG   B HB2  1 
ATOM   12092 H HB3  . ARG   B  1 6   ? 68.589 39.648  -32.574 0.00 58.70  ? 32   ARG   B HB3  1 
ATOM   12093 H HG2  . ARG   B  1 6   ? 68.867 37.324  -32.078 0.00 58.73  ? 32   ARG   B HG2  1 
ATOM   12094 H HG3  . ARG   B  1 6   ? 69.982 37.702  -30.732 0.00 59.46  ? 32   ARG   B HG3  1 
ATOM   12095 H HD2  . ARG   B  1 6   ? 67.423 39.101  -30.563 0.00 59.80  ? 32   ARG   B HD2  1 
ATOM   12096 H HD3  . ARG   B  1 6   ? 67.241 37.332  -30.519 0.00 58.78  ? 32   ARG   B HD3  1 
ATOM   12097 H HE   . ARG   B  1 6   ? 68.297 39.053  -28.469 0.00 60.65  ? 32   ARG   B HE   1 
ATOM   12098 H HH11 . ARG   B  1 6   ? 68.437 35.739  -29.806 0.00 54.93  ? 32   ARG   B HH11 1 
ATOM   12099 H HH12 . ARG   B  1 6   ? 68.919 35.067  -28.274 0.00 55.16  ? 32   ARG   B HH12 1 
ATOM   12100 H HH21 . ARG   B  1 6   ? 68.935 38.088  -26.505 0.00 57.37  ? 32   ARG   B HH21 1 
ATOM   12101 H HH22 . ARG   B  1 6   ? 69.208 36.358  -26.431 0.00 56.51  ? 32   ARG   B HH22 1 
ATOM   12102 N N    . SER   B  1 7   ? 70.725 38.313  -34.983 1.00 41.24  ? 33   SER   B N    1 
ATOM   12103 C CA   . SER   B  1 7   ? 70.515 38.204  -36.428 1.00 41.11  ? 33   SER   B CA   1 
ATOM   12104 C C    . SER   B  1 7   ? 69.027 38.155  -36.789 1.00 39.80  ? 33   SER   B C    1 
ATOM   12105 O O    . SER   B  1 7   ? 68.264 37.441  -36.144 1.00 39.60  ? 33   SER   B O    1 
ATOM   12106 C CB   . SER   B  1 7   ? 71.232 36.967  -36.972 1.00 43.48  ? 33   SER   B CB   1 
ATOM   12107 O OG   . SER   B  1 7   ? 70.868 36.665  -38.311 1.00 47.35  ? 33   SER   B OG   1 
ATOM   12108 H H    . SER   B  1 7   ? 71.152 37.489  -34.573 0.00 56.62  ? 33   SER   B H    1 
ATOM   12109 H HA   . SER   B  1 7   ? 70.955 39.080  -36.904 0.00 56.68  ? 33   SER   B HA   1 
ATOM   12110 H HB2  . SER   B  1 7   ? 72.306 37.148  -36.938 0.00 58.78  ? 33   SER   B HB2  1 
ATOM   12111 H HB3  . SER   B  1 7   ? 70.985 36.111  -36.347 0.00 58.03  ? 33   SER   B HB3  1 
ATOM   12112 H HG   . SER   B  1 7   ? 70.991 35.698  -38.501 0.00 62.07  ? 33   SER   B HG   1 
ATOM   12113 N N    . TYR   B  1 8   ? 68.629 38.888  -37.840 1.00 38.56  ? 34   TYR   B N    1 
ATOM   12114 C CA   . TYR   B  1 8   ? 67.240 38.907  -38.301 1.00 38.12  ? 34   TYR   B CA   1 
ATOM   12115 C C    . TYR   B  1 8   ? 67.216 39.196  -39.815 1.00 37.97  ? 34   TYR   B C    1 
ATOM   12116 O O    . TYR   B  1 8   ? 67.926 40.111  -40.245 1.00 38.30  ? 34   TYR   B O    1 
ATOM   12117 C CB   . TYR   B  1 8   ? 66.428 39.977  -37.540 1.00 37.64  ? 34   TYR   B CB   1 
ATOM   12118 C CG   . TYR   B  1 8   ? 64.958 39.915  -37.883 1.00 37.75  ? 34   TYR   B CG   1 
ATOM   12119 C CD1  . TYR   B  1 8   ? 64.112 39.028  -37.233 1.00 38.24  ? 34   TYR   B CD1  1 
ATOM   12120 C CD2  . TYR   B  1 8   ? 64.447 40.622  -38.963 1.00 38.24  ? 34   TYR   B CD2  1 
ATOM   12121 C CE1  . TYR   B  1 8   ? 62.779 38.900  -37.601 1.00 38.88  ? 34   TYR   B CE1  1 
ATOM   12122 C CE2  . TYR   B  1 8   ? 63.121 40.489  -39.351 1.00 38.86  ? 34   TYR   B CE2  1 
ATOM   12123 C CZ   . TYR   B  1 8   ? 62.287 39.629  -38.664 1.00 39.46  ? 34   TYR   B CZ   1 
ATOM   12124 O OH   . TYR   B  1 8   ? 60.974 39.485  -39.035 1.00 40.56  ? 34   TYR   B OH   1 
ATOM   12125 H H    . TYR   B  1 8   ? 69.245 39.475  -38.391 0.00 53.19  ? 34   TYR   B H    1 
ATOM   12126 H HA   . TYR   B  1 8   ? 66.795 37.933  -38.104 0.00 51.41  ? 34   TYR   B HA   1 
ATOM   12127 H HB2  . TYR   B  1 8   ? 66.535 39.814  -36.469 0.00 52.15  ? 34   TYR   B HB2  1 
ATOM   12128 H HB3  . TYR   B  1 8   ? 66.799 40.966  -37.808 0.00 52.62  ? 34   TYR   B HB3  1 
ATOM   12129 H HD1  . TYR   B  1 8   ? 64.491 38.445  -36.410 0.00 51.80  ? 34   TYR   B HD1  1 
ATOM   12130 H HD2  . TYR   B  1 8   ? 65.093 41.283  -39.514 0.00 52.98  ? 34   TYR   B HD2  1 
ATOM   12131 H HE1  . TYR   B  1 8   ? 62.134 38.224  -37.065 0.00 52.04  ? 34   TYR   B HE1  1 
ATOM   12132 H HE2  . TYR   B  1 8   ? 62.748 41.072  -40.177 0.00 53.23  ? 34   TYR   B HE2  1 
ATOM   12133 H HH   . TYR   B  1 8   ? 60.747 40.091  -39.787 0.00 54.58  ? 34   TYR   B HH   1 
ATOM   12134 N N    . PRO   B  1 9   ? 66.454 38.456  -40.657 1.00 37.58  ? 35   PRO   B N    1 
ATOM   12135 C CA   . PRO   B  1 9   ? 65.526 37.353  -40.347 1.00 37.56  ? 35   PRO   B CA   1 
ATOM   12136 C C    . PRO   B  1 9   ? 66.131 35.947  -40.249 1.00 38.17  ? 35   PRO   B C    1 
ATOM   12137 O O    . PRO   B  1 9   ? 65.398 35.022  -39.903 1.00 37.95  ? 35   PRO   B O    1 
ATOM   12138 C CB   . PRO   B  1 9   ? 64.532 37.433  -41.510 1.00 37.92  ? 35   PRO   B CB   1 
ATOM   12139 C CG   . PRO   B  1 9   ? 65.359 37.869  -42.668 1.00 38.25  ? 35   PRO   B CG   1 
ATOM   12140 C CD   . PRO   B  1 9   ? 66.443 38.759  -42.104 1.00 36.57  ? 35   PRO   B CD   1 
ATOM   12141 H HA   . PRO   B  1 9   ? 64.971 37.563  -39.434 0.00 50.04  ? 35   PRO   B HA   1 
ATOM   12142 H HB2  . PRO   B  1 9   ? 64.103 36.452  -41.708 0.00 49.46  ? 35   PRO   B HB2  1 
ATOM   12143 H HB3  . PRO   B  1 9   ? 63.754 38.163  -41.288 0.00 50.39  ? 35   PRO   B HB3  1 
ATOM   12144 H HG2  . PRO   B  1 9   ? 65.794 36.997  -43.153 0.00 50.17  ? 35   PRO   B HG2  1 
ATOM   12145 H HG3  . PRO   B  1 9   ? 64.737 38.424  -43.369 0.00 50.78  ? 35   PRO   B HG3  1 
ATOM   12146 H HD2  . PRO   B  1 9   ? 67.404 38.509  -42.549 0.00 49.27  ? 35   PRO   B HD2  1 
ATOM   12147 H HD3  . PRO   B  1 9   ? 66.189 39.805  -42.269 0.00 49.85  ? 35   PRO   B HD3  1 
ATOM   12148 N N    . CYS   B  1 10  ? 67.431 35.763  -40.574 1.00 38.67  ? 36   CYS   B N    1 
ATOM   12149 C CA   . CYS   B  1 10  ? 68.079 34.441  -40.573 1.00 39.82  ? 36   CYS   B CA   1 
ATOM   12150 C C    . CYS   B  1 10  ? 68.638 34.055  -39.190 1.00 41.27  ? 36   CYS   B C    1 
ATOM   12151 O O    . CYS   B  1 10  ? 68.933 34.926  -38.386 1.00 41.53  ? 36   CYS   B O    1 
ATOM   12152 C CB   . CYS   B  1 10  ? 69.188 34.393  -41.630 1.00 40.30  ? 36   CYS   B CB   1 
ATOM   12153 S SG   . CYS   B  1 10  ? 68.843 35.328  -43.151 1.00 42.19  ? 36   CYS   B SG   1 
ATOM   12154 H H    . CYS   B  1 10  ? 68.070 36.505  -40.840 0.00 51.07  ? 36   CYS   B H    1 
ATOM   12155 H HA   . CYS   B  1 10  ? 67.349 33.683  -40.852 0.00 50.92  ? 36   CYS   B HA   1 
ATOM   12156 H HB2  . CYS   B  1 10  ? 70.100 34.801  -41.194 0.00 52.50  ? 36   CYS   B HB2  1 
ATOM   12157 H HB3  . CYS   B  1 10  ? 69.353 33.355  -41.912 0.00 51.56  ? 36   CYS   B HB3  1 
ATOM   12158 N N    . ASP   B  1 11  ? 68.866 32.750  -38.960 1.00 42.57  ? 37   ASP   B N    1 
ATOM   12159 C CA   . ASP   B  1 11  ? 69.504 32.212  -37.746 1.00 44.41  ? 37   ASP   B CA   1 
ATOM   12160 C C    . ASP   B  1 11  ? 70.934 31.779  -38.129 1.00 46.92  ? 37   ASP   B C    1 
ATOM   12161 O O    . ASP   B  1 11  ? 71.086 31.004  -39.064 1.00 47.11  ? 37   ASP   B O    1 
ATOM   12162 C CB   . ASP   B  1 11  ? 68.718 31.007  -37.192 1.00 45.04  ? 37   ASP   B CB   1 
ATOM   12163 C CG   . ASP   B  1 11  ? 67.459 31.392  -36.443 1.00 48.40  ? 37   ASP   B CG   1 
ATOM   12164 O OD1  . ASP   B  1 11  ? 67.565 32.145  -35.449 1.00 49.20  ? 37   ASP   B OD1  1 
ATOM   12165 O OD2  . ASP   B  1 11  ? 66.369 30.947  -36.849 1.00 50.05  ? 37   ASP   B OD2  1 
ATOM   12166 H H    . ASP   B  1 11  ? 68.614 32.026  -39.626 0.00 53.89  ? 37   ASP   B H    1 
ATOM   12167 H HA   . ASP   B  1 11  ? 69.566 32.972  -36.969 0.00 57.21  ? 37   ASP   B HA   1 
ATOM   12168 H HB2  . ASP   B  1 11  ? 68.433 30.352  -38.013 0.00 56.37  ? 37   ASP   B HB2  1 
ATOM   12169 H HB3  . ASP   B  1 11  ? 69.359 30.465  -36.498 0.00 56.89  ? 37   ASP   B HB3  1 
ATOM   12170 N N    . GLU   B  1 12  ? 71.970 32.244  -37.417 1.00 48.82  ? 38   GLU   B N    1 
ATOM   12171 C CA   . GLU   B  1 12  ? 73.372 31.940  -37.759 1.00 51.42  ? 38   GLU   B CA   1 
ATOM   12172 C C    . GLU   B  1 12  ? 74.048 30.835  -36.923 1.00 54.53  ? 38   GLU   B C    1 
ATOM   12173 O O    . GLU   B  1 12  ? 74.250 31.022  -35.726 1.00 55.12  ? 38   GLU   B O    1 
ATOM   12174 C CB   . GLU   B  1 12  ? 74.205 33.226  -37.650 1.00 53.29  ? 38   GLU   B CB   1 
ATOM   12175 C CG   . GLU   B  1 12  ? 73.831 34.286  -38.673 1.00 57.26  ? 38   GLU   B CG   1 
ATOM   12176 C CD   . GLU   B  1 12  ? 74.550 35.611  -38.509 1.00 63.77  ? 38   GLU   B CD   1 
ATOM   12177 O OE1  . GLU   B  1 12  ? 75.135 35.846  -37.427 1.00 65.64  ? 38   GLU   B OE1  1 
ATOM   12178 O OE2  . GLU   B  1 12  ? 74.511 36.427  -39.458 1.00 65.08  ? 38   GLU   B OE2  1 
ATOM   12179 H H    . GLU   B  1 12  ? 71.872 32.843  -36.603 0.00 63.04  ? 38   GLU   B H    1 
ATOM   12180 H HA   . GLU   B  1 12  ? 73.427 31.629  -38.801 0.00 65.57  ? 38   GLU   B HA   1 
ATOM   12181 H HB2  . GLU   B  1 12  ? 74.063 33.642  -36.654 0.00 69.34  ? 38   GLU   B HB2  1 
ATOM   12182 H HB3  . GLU   B  1 12  ? 75.254 32.975  -37.798 0.00 69.12  ? 38   GLU   B HB3  1 
ATOM   12183 H HG2  . GLU   B  1 12  ? 74.067 33.906  -39.666 0.00 73.62  ? 38   GLU   B HG2  1 
ATOM   12184 H HG3  . GLU   B  1 12  ? 72.763 34.484  -38.603 0.00 73.77  ? 38   GLU   B HG3  1 
ATOM   12185 N N    . LYS   B  1 13  ? 74.458 29.719  -37.571 1.00 56.52  ? 39   LYS   B N    1 
ATOM   12186 C CA   . LYS   B  1 13  ? 75.178 28.601  -36.935 1.00 58.95  ? 39   LYS   B CA   1 
ATOM   12187 C C    . LYS   B  1 13  ? 76.643 28.619  -37.402 1.00 61.04  ? 39   LYS   B C    1 
ATOM   12188 O O    . LYS   B  1 13  ? 76.899 28.838  -38.584 1.00 61.15  ? 39   LYS   B O    1 
ATOM   12189 C CB   . LYS   B  1 13  ? 74.542 27.243  -37.305 1.00 61.46  ? 39   LYS   B CB   1 
ATOM   12190 C CG   . LYS   B  1 13  ? 73.207 26.968  -36.611 1.00 66.83  ? 39   LYS   B CG   1 
ATOM   12191 C CD   . LYS   B  1 13  ? 73.013 25.495  -36.229 1.00 72.12  ? 39   LYS   B CD   1 
ATOM   12192 C CE   . LYS   B  1 13  ? 72.761 24.604  -37.421 1.00 76.44  ? 39   LYS   B CE   1 
ATOM   12193 N NZ   . LYS   B  1 13  ? 72.624 23.176  -37.024 1.00 78.91  ? 39   LYS   B NZ   1 
ATOM   12194 H H    . LYS   B  1 13  ? 74.299 29.559  -38.561 0.00 71.08  ? 39   LYS   B H    1 
ATOM   12195 H HA   . LYS   B  1 13  ? 75.163 28.700  -35.851 0.00 74.48  ? 39   LYS   B HA   1 
ATOM   12196 H HB2  . LYS   B  1 13  ? 74.364 27.216  -38.379 0.00 76.16  ? 39   LYS   B HB2  1 
ATOM   12197 H HB3  . LYS   B  1 13  ? 75.238 26.451  -37.033 0.00 76.41  ? 39   LYS   B HB3  1 
ATOM   12198 H HG2  . LYS   B  1 13  ? 73.148 27.556  -35.698 0.00 82.96  ? 39   LYS   B HG2  1 
ATOM   12199 H HG3  . LYS   B  1 13  ? 72.396 27.249  -37.281 0.00 82.30  ? 39   LYS   B HG3  1 
ATOM   12200 H HD2  . LYS   B  1 13  ? 73.900 25.130  -35.715 0.00 88.67  ? 39   LYS   B HD2  1 
ATOM   12201 H HD3  . LYS   B  1 13  ? 72.150 25.416  -35.569 0.00 88.33  ? 39   LYS   B HD3  1 
ATOM   12202 H HE2  . LYS   B  1 13  ? 71.836 24.911  -37.906 0.00 92.76  ? 39   LYS   B HE2  1 
ATOM   12203 H HE3  . LYS   B  1 13  ? 73.593 24.682  -38.119 0.00 93.09  ? 39   LYS   B HE3  1 
ATOM   12204 H HZ1  . LYS   B  1 13  ? 72.397 22.610  -37.835 0.00 95.17  ? 39   LYS   B HZ1  1 
ATOM   12205 H HZ2  . LYS   B  1 13  ? 73.495 22.843  -36.623 0.00 95.78  ? 39   LYS   B HZ2  1 
ATOM   12206 H HZ3  . LYS   B  1 13  ? 71.885 23.077  -36.335 0.00 95.51  ? 39   LYS   B HZ3  1 
ATOM   12207 N N    . LYS   B  1 14  ? 77.601 28.377  -36.487 1.00 62.35  ? 40   LYS   B N    1 
ATOM   12208 C CA   . LYS   B  1 14  ? 79.033 28.390  -36.817 1.00 63.90  ? 40   LYS   B CA   1 
ATOM   12209 C C    . LYS   B  1 14  ? 79.572 26.963  -36.874 1.00 64.89  ? 40   LYS   B C    1 
ATOM   12210 O O    . LYS   B  1 14  ? 79.962 26.488  -37.942 1.00 65.42  ? 40   LYS   B O    1 
ATOM   12211 C CB   . LYS   B  1 14  ? 79.834 29.209  -35.785 1.00 66.42  ? 40   LYS   B CB   1 
ATOM   12212 C CG   . LYS   B  1 14  ? 79.109 30.423  -35.181 1.00 71.49  ? 40   LYS   B CG   1 
ATOM   12213 C CD   . LYS   B  1 14  ? 78.570 31.415  -36.224 1.00 76.53  ? 40   LYS   B CD   1 
ATOM   12214 C CE   . LYS   B  1 14  ? 77.718 32.502  -35.605 1.00 80.65  ? 40   LYS   B CE   1 
ATOM   12215 N NZ   . LYS   B  1 14  ? 78.526 33.497  -34.853 1.00 83.23  ? 40   LYS   B NZ   1 
ATOM   12216 H H    . LYS   B  1 14  ? 77.413 28.154  -35.515 0.00 79.09  ? 40   LYS   B H    1 
ATOM   12217 H HA   . LYS   B  1 14  ? 79.200 28.847  -37.791 0.00 81.33  ? 40   LYS   B HA   1 
ATOM   12218 H HB2  . LYS   B  1 14  ? 80.103 28.549  -34.962 0.00 85.21  ? 40   LYS   B HB2  1 
ATOM   12219 H HB3  . LYS   B  1 14  ? 80.740 29.574  -36.266 0.00 85.54  ? 40   LYS   B HB3  1 
ATOM   12220 H HG2  . LYS   B  1 14  ? 78.273 30.077  -34.575 0.00 91.36  ? 40   LYS   B HG2  1 
ATOM   12221 H HG3  . LYS   B  1 14  ? 79.813 30.964  -34.550 0.00 92.29  ? 40   LYS   B HG3  1 
ATOM   12222 H HD2  . LYS   B  1 14  ? 79.408 31.888  -36.733 0.00 98.08  ? 40   LYS   B HD2  1 
ATOM   12223 H HD3  . LYS   B  1 14  ? 77.946 30.887  -36.944 0.00 97.09  ? 40   LYS   B HD3  1 
ATOM   12224 H HE2  . LYS   B  1 14  ? 77.184 33.027  -36.396 0.00 102.79 ? 40   LYS   B HE2  1 
ATOM   12225 H HE3  . LYS   B  1 14  ? 77.008 32.051  -34.913 0.00 102.79 ? 40   LYS   B HE3  1 
ATOM   12226 H HZ1  . LYS   B  1 14  ? 77.914 34.181  -34.418 0.00 107.24 ? 40   LYS   B HZ1  1 
ATOM   12227 H HZ2  . LYS   B  1 14  ? 79.070 33.038  -34.129 0.00 107.23 ? 40   LYS   B HZ2  1 
ATOM   12228 H HZ3  . LYS   B  1 14  ? 79.158 33.977  -35.485 0.00 107.21 ? 40   LYS   B HZ3  1 
ATOM   12229 N N    . ASP   B  1 17  ? 84.866 25.453  -40.348 1.00 62.95  ? 43   ASP   B N    1 
ATOM   12230 C CA   . ASP   B  1 17  ? 85.519 26.509  -41.118 1.00 63.26  ? 43   ASP   B CA   1 
ATOM   12231 C C    . ASP   B  1 17  ? 84.486 27.275  -41.970 1.00 62.49  ? 43   ASP   B C    1 
ATOM   12232 O O    . ASP   B  1 17  ? 84.708 27.497  -43.164 1.00 62.96  ? 43   ASP   B O    1 
ATOM   12233 C CB   . ASP   B  1 17  ? 86.627 25.913  -42.012 1.00 65.78  ? 43   ASP   B CB   1 
ATOM   12234 C CG   . ASP   B  1 17  ? 87.664 25.106  -41.259 1.00 71.75  ? 43   ASP   B CG   1 
ATOM   12235 O OD1  . ASP   B  1 17  ? 87.630 23.855  -41.357 1.00 72.90  ? 43   ASP   B OD1  1 
ATOM   12236 O OD2  . ASP   B  1 17  ? 88.519 25.723  -40.581 1.00 74.27  ? 43   ASP   B OD2  1 
ATOM   12237 H HA   . ASP   B  1 17  ? 85.981 27.215  -40.429 0.00 81.99  ? 43   ASP   B HA   1 
ATOM   12238 H HB2  . ASP   B  1 17  ? 86.169 25.257  -42.751 0.00 84.12  ? 43   ASP   B HB2  1 
ATOM   12239 H HB3  . ASP   B  1 17  ? 87.152 26.725  -42.512 0.00 85.08  ? 43   ASP   B HB3  1 
ATOM   12240 N N    . SER   B  1 18  ? 83.358 27.687  -41.354 1.00 60.98  ? 44   SER   B N    1 
ATOM   12241 C CA   . SER   B  1 18  ? 82.299 28.420  -42.055 1.00 59.73  ? 44   SER   B CA   1 
ATOM   12242 C C    . SER   B  1 18  ? 81.209 28.931  -41.081 1.00 58.01  ? 44   SER   B C    1 
ATOM   12243 O O    . SER   B  1 18  ? 81.164 28.516  -39.921 1.00 58.61  ? 44   SER   B O    1 
ATOM   12244 C CB   . SER   B  1 18  ? 81.663 27.532  -43.123 1.00 60.95  ? 44   SER   B CB   1 
ATOM   12245 O OG   . SER   B  1 18  ? 81.242 26.295  -42.574 1.00 63.31  ? 44   SER   B OG   1 
ATOM   12246 H H    . SER   B  1 18  ? 83.155 27.531  -40.372 0.00 78.23  ? 44   SER   B H    1 
ATOM   12247 H HA   . SER   B  1 18  ? 82.737 29.283  -42.552 0.00 76.88  ? 44   SER   B HA   1 
ATOM   12248 H HB2  . SER   B  1 18  ? 80.791 28.038  -43.534 0.00 77.02  ? 44   SER   B HB2  1 
ATOM   12249 H HB3  . SER   B  1 18  ? 82.385 27.343  -43.917 0.00 77.28  ? 44   SER   B HB3  1 
ATOM   12250 H HG   . SER   B  1 18  ? 80.811 25.741  -43.277 0.00 79.08  ? 44   SER   B HG   1 
ATOM   12251 N N    . VAL   B  1 19  ? 80.344 29.843  -41.559 1.00 55.65  ? 45   VAL   B N    1 
ATOM   12252 C CA   . VAL   B  1 19  ? 79.222 30.389  -40.786 1.00 53.75  ? 45   VAL   B CA   1 
ATOM   12253 C C    . VAL   B  1 19  ? 78.001 30.392  -41.729 1.00 50.74  ? 45   VAL   B C    1 
ATOM   12254 O O    . VAL   B  1 19  ? 78.028 31.016  -42.793 1.00 50.63  ? 45   VAL   B O    1 
ATOM   12255 C CB   . VAL   B  1 19  ? 79.510 31.775  -40.111 1.00 54.93  ? 45   VAL   B CB   1 
ATOM   12256 C CG1  . VAL   B  1 19  ? 80.476 32.622  -40.925 1.00 55.82  ? 45   VAL   B CG1  1 
ATOM   12257 C CG2  . VAL   B  1 19  ? 78.221 32.546  -39.814 1.00 55.39  ? 45   VAL   B CG2  1 
ATOM   12258 H H    . VAL   B  1 19  ? 80.397 30.220  -42.500 0.00 71.51  ? 45   VAL   B H    1 
ATOM   12259 H HA   . VAL   B  1 19  ? 78.995 29.684  -39.988 0.00 68.98  ? 45   VAL   B HA   1 
ATOM   12260 H HB   . VAL   B  1 19  ? 80.000 31.614  -39.151 0.00 71.71  ? 45   VAL   B HB   1 
ATOM   12261 H HG11 . VAL   B  1 19  ? 80.532 33.615  -40.483 0.00 73.56  ? 45   VAL   B HG11 1 
ATOM   12262 H HG12 . VAL   B  1 19  ? 81.463 32.161  -40.906 0.00 73.19  ? 45   VAL   B HG12 1 
ATOM   12263 H HG13 . VAL   B  1 19  ? 80.115 32.688  -41.950 0.00 72.71  ? 45   VAL   B HG13 1 
ATOM   12264 H HG21 . VAL   B  1 19  ? 78.459 33.359  -39.130 0.00 72.51  ? 45   VAL   B HG21 1 
ATOM   12265 H HG22 . VAL   B  1 19  ? 77.820 32.964  -40.737 0.00 71.82  ? 45   VAL   B HG22 1 
ATOM   12266 H HG23 . VAL   B  1 19  ? 77.496 31.878  -39.351 0.00 71.49  ? 45   VAL   B HG23 1 
ATOM   12267 N N    . ILE   B  1 20  ? 76.951 29.665  -41.339 1.00 48.02  ? 46   ILE   B N    1 
ATOM   12268 C CA   . ILE   B  1 20  ? 75.752 29.467  -42.133 1.00 46.29  ? 46   ILE   B CA   1 
ATOM   12269 C C    . ILE   B  1 20  ? 74.606 30.363  -41.671 1.00 43.61  ? 46   ILE   B C    1 
ATOM   12270 O O    . ILE   B  1 20  ? 74.296 30.390  -40.481 1.00 43.80  ? 46   ILE   B O    1 
ATOM   12271 C CB   . ILE   B  1 20  ? 75.332 27.969  -42.025 1.00 47.48  ? 46   ILE   B CB   1 
ATOM   12272 C CG1  . ILE   B  1 20  ? 76.489 27.011  -42.447 1.00 49.08  ? 46   ILE   B CG1  1 
ATOM   12273 C CG2  . ILE   B  1 20  ? 74.064 27.710  -42.847 1.00 47.87  ? 46   ILE   B CG2  1 
ATOM   12274 C CD1  . ILE   B  1 20  ? 76.324 25.544  -41.989 1.00 50.57  ? 46   ILE   B CD1  1 
ATOM   12275 H H    . ILE   B  1 20  ? 76.897 29.191  -40.443 0.00 61.14  ? 46   ILE   B H    1 
ATOM   12276 H HA   . ILE   B  1 20  ? 75.959 29.671  -43.183 0.00 58.57  ? 46   ILE   B HA   1 
ATOM   12277 H HB   . ILE   B  1 20  ? 75.094 27.763  -40.983 0.00 59.34  ? 46   ILE   B HB   1 
ATOM   12278 H HG12 . ILE   B  1 20  ? 76.547 26.992  -43.534 0.00 61.03  ? 46   ILE   B HG12 1 
ATOM   12279 H HG13 . ILE   B  1 20  ? 77.436 27.360  -42.038 0.00 61.63  ? 46   ILE   B HG13 1 
ATOM   12280 H HG21 . ILE   B  1 20  ? 73.979 26.648  -43.071 0.00 58.82  ? 46   ILE   B HG21 1 
ATOM   12281 H HG22 . ILE   B  1 20  ? 73.194 28.019  -42.271 0.00 59.22  ? 46   ILE   B HG22 1 
ATOM   12282 H HG23 . ILE   B  1 20  ? 74.119 28.280  -43.773 0.00 59.37  ? 46   ILE   B HG23 1 
ATOM   12283 H HD11 . ILE   B  1 20  ? 77.283 25.037  -42.086 0.00 62.56  ? 46   ILE   B HD11 1 
ATOM   12284 H HD12 . ILE   B  1 20  ? 75.997 25.530  -40.951 0.00 62.51  ? 46   ILE   B HD12 1 
ATOM   12285 H HD13 . ILE   B  1 20  ? 75.588 25.049  -42.620 0.00 62.00  ? 46   ILE   B HD13 1 
ATOM   12286 N N    . ALA   B  1 21  ? 73.940 31.043  -42.613 1.00 40.87  ? 47   ALA   B N    1 
ATOM   12287 C CA   . ALA   B  1 21  ? 72.745 31.834  -42.336 1.00 39.28  ? 47   ALA   B CA   1 
ATOM   12288 C C    . ALA   B  1 21  ? 71.551 30.986  -42.755 1.00 37.57  ? 47   ALA   B C    1 
ATOM   12289 O O    . ALA   B  1 21  ? 71.292 30.830  -43.948 1.00 37.12  ? 47   ALA   B O    1 
ATOM   12290 C CB   . ALA   B  1 21  ? 72.757 33.131  -43.122 1.00 39.39  ? 47   ALA   B CB   1 
ATOM   12291 H H    . ALA   B  1 21  ? 74.207 31.057  -43.592 0.00 52.08  ? 47   ALA   B H    1 
ATOM   12292 H HA   . ALA   B  1 21  ? 72.665 32.082  -41.279 0.00 50.58  ? 47   ALA   B HA   1 
ATOM   12293 H HB1  . ALA   B  1 21  ? 71.783 33.608  -43.023 0.00 50.95  ? 47   ALA   B HB1  1 
ATOM   12294 H HB2  . ALA   B  1 21  ? 73.524 33.780  -42.704 0.00 51.47  ? 47   ALA   B HB2  1 
ATOM   12295 H HB3  . ALA   B  1 21  ? 72.962 32.923  -44.171 0.00 50.75  ? 47   ALA   B HB3  1 
ATOM   12296 N N    . GLU   B  1 22  ? 70.874 30.387  -41.779 1.00 36.28  ? 48   GLU   B N    1 
ATOM   12297 C CA   . GLU   B  1 22  ? 69.700 29.571  -41.999 1.00 36.09  ? 48   GLU   B CA   1 
ATOM   12298 C C    . GLU   B  1 22  ? 68.540 30.533  -42.169 1.00 34.79  ? 48   GLU   B C    1 
ATOM   12299 O O    . GLU   B  1 22  ? 68.087 31.135  -41.198 1.00 34.39  ? 48   GLU   B O    1 
ATOM   12300 C CB   . GLU   B  1 22  ? 69.474 28.620  -40.808 1.00 39.89  ? 48   GLU   B CB   1 
ATOM   12301 C CG   . GLU   B  1 22  ? 70.642 27.664  -40.590 1.00 47.37  ? 48   GLU   B CG   1 
ATOM   12302 C CD   . GLU   B  1 22  ? 70.408 26.593  -39.539 1.00 56.55  ? 48   GLU   B CD   1 
ATOM   12303 O OE1  . GLU   B  1 22  ? 70.444 25.392  -39.898 1.00 58.51  ? 48   GLU   B OE1  1 
ATOM   12304 O OE2  . GLU   B  1 22  ? 70.187 26.951  -38.359 1.00 59.25  ? 48   GLU   B OE2  1 
ATOM   12305 H H    . GLU   B  1 22  ? 71.126 30.460  -40.798 0.00 46.00  ? 48   GLU   B H    1 
ATOM   12306 H HA   . GLU   B  1 22  ? 69.814 28.967  -42.898 0.00 44.61  ? 48   GLU   B HA   1 
ATOM   12307 H HB2  . GLU   B  1 22  ? 69.347 29.202  -39.896 0.00 49.58  ? 48   GLU   B HB2  1 
ATOM   12308 H HB3  . GLU   B  1 22  ? 68.582 28.024  -40.995 0.00 48.81  ? 48   GLU   B HB3  1 
ATOM   12309 H HG2  . GLU   B  1 22  ? 70.856 27.159  -41.531 0.00 57.83  ? 48   GLU   B HG2  1 
ATOM   12310 H HG3  . GLU   B  1 22  ? 71.512 28.239  -40.278 0.00 58.57  ? 48   GLU   B HG3  1 
ATOM   12311 N N    . CYS   B  1 23  ? 68.102 30.733  -43.411 1.00 33.75  ? 49   CYS   B N    1 
ATOM   12312 C CA   . CYS   B  1 23  ? 67.054 31.694  -43.723 1.00 33.46  ? 49   CYS   B CA   1 
ATOM   12313 C C    . CYS   B  1 23  ? 65.913 31.066  -44.524 1.00 31.99  ? 49   CYS   B C    1 
ATOM   12314 O O    . CYS   B  1 23  ? 65.177 31.798  -45.166 1.00 31.71  ? 49   CYS   B O    1 
ATOM   12315 C CB   . CYS   B  1 23  ? 67.683 32.863  -44.482 1.00 35.14  ? 49   CYS   B CB   1 
ATOM   12316 S SG   . CYS   B  1 23  ? 67.150 34.494  -43.922 1.00 41.30  ? 49   CYS   B SG   1 
ATOM   12317 H H    . CYS   B  1 23  ? 68.454 30.246  -44.229 0.00 41.90  ? 49   CYS   B H    1 
ATOM   12318 H HA   . CYS   B  1 23  ? 66.610 32.073  -42.804 0.00 42.18  ? 49   CYS   B HA   1 
ATOM   12319 H HB2  . CYS   B  1 23  ? 68.764 32.825  -44.346 0.00 44.73  ? 49   CYS   B HB2  1 
ATOM   12320 H HB3  . CYS   B  1 23  ? 67.460 32.778  -45.544 0.00 44.38  ? 49   CYS   B HB3  1 
ATOM   12321 N N    . SER   B  1 24  ? 65.744 29.737  -44.484 1.00 31.47  ? 50   SER   B N    1 
ATOM   12322 C CA   . SER   B  1 24  ? 64.719 29.069  -45.277 1.00 32.24  ? 50   SER   B CA   1 
ATOM   12323 C C    . SER   B  1 24  ? 63.343 29.105  -44.637 1.00 33.31  ? 50   SER   B C    1 
ATOM   12324 O O    . SER   B  1 24  ? 63.234 29.191  -43.413 1.00 33.34  ? 50   SER   B O    1 
ATOM   12325 C CB   . SER   B  1 24  ? 65.110 27.612  -45.519 1.00 32.50  ? 50   SER   B CB   1 
ATOM   12326 O OG   . SER   B  1 24  ? 65.032 26.859  -44.322 1.00 34.18  ? 50   SER   B OG   1 
ATOM   12327 H H    . SER   B  1 24  ? 66.281 29.096  -43.908 0.00 38.40  ? 50   SER   B H    1 
ATOM   12328 H HA   . SER   B  1 24  ? 64.652 29.547  -46.253 0.00 39.10  ? 50   SER   B HA   1 
ATOM   12329 H HB2  . SER   B  1 24  ? 64.430 27.181  -46.253 0.00 38.49  ? 50   SER   B HB2  1 
ATOM   12330 H HB3  . SER   B  1 24  ? 66.132 27.577  -45.892 0.00 38.87  ? 50   SER   B HB3  1 
ATOM   12331 H HG   . SER   B  1 24  ? 65.297 25.918  -44.495 0.00 40.29  ? 50   SER   B HG   1 
ATOM   12332 N N    . ASN   B  1 25  ? 62.304 28.962  -45.469 1.00 33.75  ? 51   ASN   B N    1 
ATOM   12333 C CA   . ASN   B  1 25  ? 60.918 28.818  -45.041 1.00 34.69  ? 51   ASN   B CA   1 
ATOM   12334 C C    . ASN   B  1 25  ? 60.454 29.868  -44.029 1.00 35.06  ? 51   ASN   B C    1 
ATOM   12335 O O    . ASN   B  1 25  ? 59.882 29.523  -42.996 1.00 35.79  ? 51   ASN   B O    1 
ATOM   12336 C CB   . ASN   B  1 25  ? 60.724 27.387  -44.496 1.00 36.55  ? 51   ASN   B CB   1 
ATOM   12337 C CG   . ASN   B  1 25  ? 59.279 26.982  -44.334 1.00 41.71  ? 51   ASN   B CG   1 
ATOM   12338 O OD1  . ASN   B  1 25  ? 58.390 27.457  -45.056 1.00 43.56  ? 51   ASN   B OD1  1 
ATOM   12339 N ND2  . ASN   B  1 25  ? 59.008 26.095  -43.379 1.00 42.81  ? 51   ASN   B ND2  1 
ATOM   12340 H H    . ASN   B  1 25  ? 62.401 28.938  -46.479 0.00 40.44  ? 51   ASN   B H    1 
ATOM   12341 H HA   . ASN   B  1 25  ? 60.292 28.928  -45.926 0.00 41.44  ? 51   ASN   B HA   1 
ATOM   12342 H HB2  . ASN   B  1 25  ? 61.185 26.688  -45.192 0.00 42.92  ? 51   ASN   B HB2  1 
ATOM   12343 H HB3  . ASN   B  1 25  ? 61.216 27.313  -43.528 0.00 43.26  ? 51   ASN   B HB3  1 
ATOM   12344 H HD21 . ASN   B  1 25  ? 58.051 25.790  -43.232 0.00 50.09  ? 51   ASN   B HD21 1 
ATOM   12345 H HD22 . ASN   B  1 25  ? 59.750 25.716  -42.800 0.00 50.17  ? 51   ASN   B HD22 1 
ATOM   12346 N N    . ARG   B  1 26  ? 60.675 31.144  -44.340 1.00 34.58  ? 52   ARG   B N    1 
ATOM   12347 C CA   . ARG   B  1 26  ? 60.318 32.274  -43.470 1.00 34.78  ? 52   ARG   B CA   1 
ATOM   12348 C C    . ARG   B  1 26  ? 59.439 33.308  -44.184 1.00 34.61  ? 52   ARG   B C    1 
ATOM   12349 O O    . ARG   B  1 26  ? 59.350 34.437  -43.719 1.00 34.66  ? 52   ARG   B O    1 
ATOM   12350 C CB   . ARG   B  1 26  ? 61.604 32.958  -42.964 1.00 36.31  ? 52   ARG   B CB   1 
ATOM   12351 C CG   . ARG   B  1 26  ? 62.430 32.058  -42.076 1.00 39.68  ? 52   ARG   B CG   1 
ATOM   12352 C CD   . ARG   B  1 26  ? 63.877 32.464  -42.015 1.00 41.39  ? 52   ARG   B CD   1 
ATOM   12353 N NE   . ARG   B  1 26  ? 64.665 31.370  -41.446 1.00 44.13  ? 52   ARG   B NE   1 
ATOM   12354 C CZ   . ARG   B  1 26  ? 65.021 31.232  -40.169 1.00 46.32  ? 52   ARG   B CZ   1 
ATOM   12355 N NH1  . ARG   B  1 26  ? 64.697 32.159  -39.272 1.00 46.31  ? 52   ARG   B NH1  1 
ATOM   12356 N NH2  . ARG   B  1 26  ? 65.732 30.180  -39.784 1.00 46.69  ? 52   ARG   B NH2  1 
ATOM   12357 H H    . ARG   B  1 26  ? 61.111 31.437  -45.208 0.00 42.42  ? 52   ARG   B H    1 
ATOM   12358 H HA   . ARG   B  1 26  ? 59.766 31.928  -42.598 0.00 43.00  ? 52   ARG   B HA   1 
ATOM   12359 H HB2  . ARG   B  1 26  ? 62.213 33.232  -43.823 0.00 45.50  ? 52   ARG   B HB2  1 
ATOM   12360 H HB3  . ARG   B  1 26  ? 61.355 33.842  -42.379 0.00 45.85  ? 52   ARG   B HB3  1 
ATOM   12361 H HG2  . ARG   B  1 26  ? 62.027 32.082  -41.066 0.00 49.29  ? 52   ARG   B HG2  1 
ATOM   12362 H HG3  . ARG   B  1 26  ? 62.399 31.038  -42.453 0.00 48.70  ? 52   ARG   B HG3  1 
ATOM   12363 H HD2  . ARG   B  1 26  ? 64.240 32.598  -43.033 0.00 51.58  ? 52   ARG   B HD2  1 
ATOM   12364 H HD3  . ARG   B  1 26  ? 64.001 33.400  -41.476 0.00 52.10  ? 52   ARG   B HD3  1 
ATOM   12365 H HE   . ARG   B  1 26  ? 64.946 30.637  -42.090 0.00 54.21  ? 52   ARG   B HE   1 
ATOM   12366 H HH11 . ARG   B  1 26  ? 64.134 32.975  -39.486 0.00 58.08  ? 52   ARG   B HH11 1 
ATOM   12367 H HH12 . ARG   B  1 26  ? 64.979 32.023  -38.307 0.00 57.94  ? 52   ARG   B HH12 1 
ATOM   12368 H HH21 . ARG   B  1 26  ? 66.005 29.471  -40.458 0.00 57.15  ? 52   ARG   B HH21 1 
ATOM   12369 H HH22 . ARG   B  1 26  ? 66.015 30.078  -38.815 0.00 57.63  ? 52   ARG   B HH22 1 
ATOM   12370 N N    . ARG   B  1 27  ? 58.789 32.943  -45.303 1.00 34.21  ? 53   ARG   B N    1 
ATOM   12371 C CA   . ARG   B  1 27  ? 57.890 33.856  -46.009 1.00 33.95  ? 53   ARG   B CA   1 
ATOM   12372 C C    . ARG   B  1 27  ? 58.575 35.128  -46.523 1.00 34.21  ? 53   ARG   B C    1 
ATOM   12373 O O    . ARG   B  1 27  ? 57.926 36.171  -46.647 1.00 34.24  ? 53   ARG   B O    1 
ATOM   12374 C CB   . ARG   B  1 27  ? 56.682 34.196  -45.104 1.00 34.66  ? 53   ARG   B CB   1 
ATOM   12375 C CG   . ARG   B  1 27  ? 56.049 32.953  -44.445 1.00 35.89  ? 53   ARG   B CG   1 
ATOM   12376 C CD   . ARG   B  1 27  ? 54.959 33.295  -43.436 1.00 37.95  ? 53   ARG   B CD   1 
ATOM   12377 N NE   . ARG   B  1 27  ? 55.438 34.164  -42.356 1.00 40.13  ? 53   ARG   B NE   1 
ATOM   12378 C CZ   . ARG   B  1 27  ? 56.175 33.770  -41.319 1.00 41.62  ? 53   ARG   B CZ   1 
ATOM   12379 N NH1  . ARG   B  1 27  ? 56.559 32.499  -41.208 1.00 40.18  ? 53   ARG   B NH1  1 
ATOM   12380 N NH2  . ARG   B  1 27  ? 56.550 34.644  -40.392 1.00 41.71  ? 53   ARG   B NH2  1 
ATOM   12381 H H    . ARG   B  1 27  ? 58.833 32.026  -45.736 0.00 42.09  ? 53   ARG   B H    1 
ATOM   12382 H HA   . ARG   B  1 27  ? 57.499 33.331  -46.879 0.00 42.30  ? 53   ARG   B HA   1 
ATOM   12383 H HB2  . ARG   B  1 27  ? 57.014 34.876  -44.320 0.00 44.01  ? 53   ARG   B HB2  1 
ATOM   12384 H HB3  . ARG   B  1 27  ? 55.913 34.677  -45.706 0.00 43.83  ? 53   ARG   B HB3  1 
ATOM   12385 H HG2  . ARG   B  1 27  ? 55.606 32.331  -45.221 0.00 44.24  ? 53   ARG   B HG2  1 
ATOM   12386 H HG3  . ARG   B  1 27  ? 56.808 32.389  -43.906 0.00 44.33  ? 53   ARG   B HG3  1 
ATOM   12387 H HD2  . ARG   B  1 27  ? 54.164 33.828  -43.956 0.00 47.50  ? 53   ARG   B HD2  1 
ATOM   12388 H HD3  . ARG   B  1 27  ? 54.561 32.378  -43.004 0.00 46.87  ? 53   ARG   B HD3  1 
ATOM   12389 H HE   . ARG   B  1 27  ? 55.164 35.141  -42.402 0.00 50.85  ? 53   ARG   B HE   1 
ATOM   12390 H HH11 . ARG   B  1 27  ? 56.295 31.795  -41.890 0.00 49.35  ? 53   ARG   B HH11 1 
ATOM   12391 H HH12 . ARG   B  1 27  ? 57.123 32.215  -40.414 0.00 49.70  ? 53   ARG   B HH12 1 
ATOM   12392 H HH21 . ARG   B  1 27  ? 56.270 35.616  -40.465 0.00 53.18  ? 53   ARG   B HH21 1 
ATOM   12393 H HH22 . ARG   B  1 27  ? 57.118 34.345  -39.606 0.00 52.65  ? 53   ARG   B HH22 1 
ATOM   12394 N N    . LEU   B  1 28  ? 59.868 35.040  -46.857 1.00 34.33  ? 54   LEU   B N    1 
ATOM   12395 C CA   . LEU   B  1 28  ? 60.607 36.199  -47.343 1.00 35.42  ? 54   LEU   B CA   1 
ATOM   12396 C C    . LEU   B  1 28  ? 60.181 36.499  -48.774 1.00 36.44  ? 54   LEU   B C    1 
ATOM   12397 O O    . LEU   B  1 28  ? 60.187 35.599  -49.603 1.00 36.62  ? 54   LEU   B O    1 
ATOM   12398 C CB   . LEU   B  1 28  ? 62.118 35.941  -47.287 1.00 35.56  ? 54   LEU   B CB   1 
ATOM   12399 C CG   . LEU   B  1 28  ? 62.674 35.599  -45.915 1.00 37.10  ? 54   LEU   B CG   1 
ATOM   12400 C CD1  . LEU   B  1 28  ? 64.117 35.162  -46.013 1.00 37.45  ? 54   LEU   B CD1  1 
ATOM   12401 C CD2  . LEU   B  1 28  ? 62.510 36.766  -44.929 1.00 37.76  ? 54   LEU   B CD2  1 
ATOM   12402 H H    . LEU   B  1 28  ? 60.418 34.187  -46.828 0.00 43.24  ? 54   LEU   B H    1 
ATOM   12403 H HA   . LEU   B  1 28  ? 60.382 37.065  -46.722 0.00 46.00  ? 54   LEU   B HA   1 
ATOM   12404 H HB2  . LEU   B  1 28  ? 62.355 35.111  -47.951 0.00 45.23  ? 54   LEU   B HB2  1 
ATOM   12405 H HB3  . LEU   B  1 28  ? 62.631 36.838  -47.629 0.00 46.13  ? 54   LEU   B HB3  1 
ATOM   12406 H HG   . LEU   B  1 28  ? 62.105 34.757  -45.528 0.00 47.02  ? 54   LEU   B HG   1 
ATOM   12407 H HD11 . LEU   B  1 28  ? 64.500 34.956  -45.014 0.00 47.80  ? 54   LEU   B HD11 1 
ATOM   12408 H HD12 . LEU   B  1 28  ? 64.173 34.261  -46.622 0.00 47.32  ? 54   LEU   B HD12 1 
ATOM   12409 H HD13 . LEU   B  1 28  ? 64.695 35.958  -46.477 0.00 48.21  ? 54   LEU   B HD13 1 
ATOM   12410 H HD21 . LEU   B  1 28  ? 63.084 36.555  -44.028 0.00 48.91  ? 54   LEU   B HD21 1 
ATOM   12411 H HD22 . LEU   B  1 28  ? 62.872 37.680  -45.397 0.00 49.37  ? 54   LEU   B HD22 1 
ATOM   12412 H HD23 . LEU   B  1 28  ? 61.458 36.871  -44.672 0.00 48.89  ? 54   LEU   B HD23 1 
ATOM   12413 N N    . GLN   B  1 29  ? 59.754 37.736  -49.041 1.00 36.83  ? 55   GLN   B N    1 
ATOM   12414 C CA   . GLN   B  1 29  ? 59.319 38.184  -50.369 1.00 38.06  ? 55   GLN   B CA   1 
ATOM   12415 C C    . GLN   B  1 29  ? 60.498 38.693  -51.219 1.00 38.63  ? 55   GLN   B C    1 
ATOM   12416 O O    . GLN   B  1 29  ? 60.377 38.777  -52.441 1.00 38.79  ? 55   GLN   B O    1 
ATOM   12417 C CB   . GLN   B  1 29  ? 58.256 39.296  -50.232 1.00 40.59  ? 55   GLN   B CB   1 
ATOM   12418 C CG   . GLN   B  1 29  ? 56.937 38.795  -49.637 1.00 46.01  ? 55   GLN   B CG   1 
ATOM   12419 C CD   . GLN   B  1 29  ? 55.984 39.906  -49.247 1.00 52.80  ? 55   GLN   B CD   1 
ATOM   12420 O OE1  . GLN   B  1 29  ? 56.241 41.101  -49.448 1.00 55.92  ? 55   GLN   B OE1  1 
ATOM   12421 N NE2  . GLN   B  1 29  ? 54.854 39.533  -48.669 1.00 53.70  ? 55   GLN   B NE2  1 
ATOM   12422 H H    . GLN   B  1 29  ? 59.703 38.471  -48.343 0.00 48.34  ? 55   GLN   B H    1 
ATOM   12423 H HA   . GLN   B  1 29  ? 58.854 37.356  -50.903 0.00 49.18  ? 55   GLN   B HA   1 
ATOM   12424 H HB2  . GLN   B  1 29  ? 58.648 40.084  -49.591 0.00 53.71  ? 55   GLN   B HB2  1 
ATOM   12425 H HB3  . GLN   B  1 29  ? 58.042 39.699  -51.221 0.00 53.48  ? 55   GLN   B HB3  1 
ATOM   12426 H HG2  . GLN   B  1 29  ? 56.434 38.171  -50.374 0.00 59.18  ? 55   GLN   B HG2  1 
ATOM   12427 H HG3  . GLN   B  1 29  ? 57.146 38.212  -48.741 0.00 59.18  ? 55   GLN   B HG3  1 
ATOM   12428 H HE21 . GLN   B  1 29  ? 54.669 38.548  -48.504 0.00 68.68  ? 55   GLN   B HE21 1 
ATOM   12429 H HE22 . GLN   B  1 29  ? 54.176 40.232  -48.383 0.00 69.65  ? 55   GLN   B HE22 1 
ATOM   12430 N N    . GLU   B  1 30  ? 61.615 39.075  -50.573 1.00 38.78  ? 56   GLU   B N    1 
ATOM   12431 C CA   . GLU   B  1 30  ? 62.826 39.547  -51.232 1.00 39.60  ? 56   GLU   B CA   1 
ATOM   12432 C C    . GLU   B  1 30  ? 64.046 38.999  -50.474 1.00 38.49  ? 56   GLU   B C    1 
ATOM   12433 O O    . GLU   B  1 30  ? 63.923 38.563  -49.330 1.00 37.73  ? 56   GLU   B O    1 
ATOM   12434 C CB   . GLU   B  1 30  ? 62.871 41.097  -51.231 1.00 43.90  ? 56   GLU   B CB   1 
ATOM   12435 C CG   . GLU   B  1 30  ? 61.702 41.757  -51.940 1.00 52.46  ? 56   GLU   B CG   1 
ATOM   12436 C CD   . GLU   B  1 30  ? 62.095 42.907  -52.843 1.00 62.51  ? 56   GLU   B CD   1 
ATOM   12437 O OE1  . GLU   B  1 30  ? 62.256 42.675  -54.064 1.00 64.98  ? 56   GLU   B OE1  1 
ATOM   12438 O OE2  . GLU   B  1 30  ? 62.245 44.040  -52.330 1.00 65.58  ? 56   GLU   B OE2  1 
ATOM   12439 H H    . GLU   B  1 30  ? 61.712 39.092  -49.563 0.00 51.07  ? 56   GLU   B H    1 
ATOM   12440 H HA   . GLU   B  1 30  ? 62.875 39.192  -52.261 0.00 52.15  ? 56   GLU   B HA   1 
ATOM   12441 H HB2  . GLU   B  1 30  ? 62.870 41.444  -50.199 0.00 58.60  ? 56   GLU   B HB2  1 
ATOM   12442 H HB3  . GLU   B  1 30  ? 63.786 41.421  -51.726 0.00 58.62  ? 56   GLU   B HB3  1 
ATOM   12443 H HG2  . GLU   B  1 30  ? 61.201 41.009  -52.555 0.00 68.52  ? 56   GLU   B HG2  1 
ATOM   12444 H HG3  . GLU   B  1 30  ? 61.011 42.143  -51.193 0.00 69.15  ? 56   GLU   B HG3  1 
ATOM   12445 N N    . VAL   B  1 31  ? 65.240 39.071  -51.087 1.00 38.03  ? 57   VAL   B N    1 
ATOM   12446 C CA   . VAL   B  1 31  ? 66.472 38.654  -50.416 1.00 37.84  ? 57   VAL   B CA   1 
ATOM   12447 C C    . VAL   B  1 31  ? 66.718 39.671  -49.273 1.00 38.05  ? 57   VAL   B C    1 
ATOM   12448 O O    . VAL   B  1 31  ? 66.656 40.876  -49.532 1.00 37.46  ? 57   VAL   B O    1 
ATOM   12449 C CB   . VAL   B  1 31  ? 67.668 38.610  -51.396 1.00 38.06  ? 57   VAL   B CB   1 
ATOM   12450 C CG1  . VAL   B  1 31  ? 68.971 38.341  -50.652 1.00 38.06  ? 57   VAL   B CG1  1 
ATOM   12451 C CG2  . VAL   B  1 31  ? 67.439 37.562  -52.486 1.00 38.37  ? 57   VAL   B CG2  1 
ATOM   12452 H H    . VAL   B  1 31  ? 65.373 39.421  -52.029 0.00 50.59  ? 57   VAL   B H    1 
ATOM   12453 H HA   . VAL   B  1 31  ? 66.335 37.646  -50.028 0.00 49.56  ? 57   VAL   B HA   1 
ATOM   12454 H HB   . VAL   B  1 31  ? 67.758 39.580  -51.882 0.00 50.98  ? 57   VAL   B HB   1 
ATOM   12455 H HG11 . VAL   B  1 31  ? 69.733 38.043  -51.370 0.00 50.43  ? 57   VAL   B HG11 1 
ATOM   12456 H HG12 . VAL   B  1 31  ? 69.300 39.246  -50.143 0.00 51.06  ? 57   VAL   B HG12 1 
ATOM   12457 H HG13 . VAL   B  1 31  ? 68.813 37.540  -49.933 0.00 50.10  ? 57   VAL   B HG13 1 
ATOM   12458 H HG21 . VAL   B  1 31  ? 68.317 37.501  -53.126 0.00 50.31  ? 57   VAL   B HG21 1 
ATOM   12459 H HG22 . VAL   B  1 31  ? 67.262 36.597  -52.013 0.00 49.72  ? 57   VAL   B HG22 1 
ATOM   12460 H HG23 . VAL   B  1 31  ? 66.573 37.848  -53.082 0.00 50.28  ? 57   VAL   B HG23 1 
ATOM   12461 N N    . PRO   B  1 32  ? 66.903 39.232  -48.010 1.00 38.52  ? 58   PRO   B N    1 
ATOM   12462 C CA   . PRO   B  1 32  ? 67.059 40.216  -46.927 1.00 39.30  ? 58   PRO   B CA   1 
ATOM   12463 C C    . PRO   B  1 32  ? 68.328 41.031  -47.053 1.00 40.54  ? 58   PRO   B C    1 
ATOM   12464 O O    . PRO   B  1 32  ? 69.387 40.464  -47.320 1.00 40.52  ? 58   PRO   B O    1 
ATOM   12465 C CB   . PRO   B  1 32  ? 67.075 39.383  -45.644 1.00 39.81  ? 58   PRO   B CB   1 
ATOM   12466 C CG   . PRO   B  1 32  ? 67.094 37.981  -46.046 1.00 40.10  ? 58   PRO   B CG   1 
ATOM   12467 C CD   . PRO   B  1 32  ? 66.948 37.845  -47.514 1.00 38.00  ? 58   PRO   B CD   1 
ATOM   12468 H HA   . PRO   B  1 32  ? 66.195 40.880  -46.901 0.00 53.25  ? 58   PRO   B HA   1 
ATOM   12469 H HB2  . PRO   B  1 32  ? 67.970 39.623  -45.071 0.00 53.54  ? 58   PRO   B HB2  1 
ATOM   12470 H HB3  . PRO   B  1 32  ? 66.182 39.599  -45.059 0.00 53.31  ? 58   PRO   B HB3  1 
ATOM   12471 H HG2  . PRO   B  1 32  ? 68.039 37.542  -45.731 0.00 52.69  ? 58   PRO   B HG2  1 
ATOM   12472 H HG3  . PRO   B  1 32  ? 66.271 37.469  -45.550 0.00 52.46  ? 58   PRO   B HG3  1 
ATOM   12473 H HD2  . PRO   B  1 32  ? 67.811 37.312  -47.909 0.00 49.88  ? 58   PRO   B HD2  1 
ATOM   12474 H HD3  . PRO   B  1 32  ? 66.019 37.333  -47.756 0.00 49.65  ? 58   PRO   B HD3  1 
ATOM   12475 N N    . GLN   B  1 33  ? 68.220 42.354  -46.865 1.00 41.23  ? 59   GLN   B N    1 
ATOM   12476 C CA   . GLN   B  1 33  ? 69.382 43.241  -46.901 1.00 42.70  ? 59   GLN   B CA   1 
ATOM   12477 C C    . GLN   B  1 33  ? 70.022 43.372  -45.501 1.00 43.49  ? 59   GLN   B C    1 
ATOM   12478 O O    . GLN   B  1 33  ? 70.739 44.337  -45.264 1.00 44.09  ? 59   GLN   B O    1 
ATOM   12479 C CB   . GLN   B  1 33  ? 68.985 44.619  -47.467 1.00 44.79  ? 59   GLN   B CB   1 
ATOM   12480 C CG   . GLN   B  1 33  ? 68.385 44.557  -48.879 1.00 49.64  ? 59   GLN   B CG   1 
ATOM   12481 C CD   . GLN   B  1 33  ? 69.341 43.972  -49.896 1.00 55.58  ? 59   GLN   B CD   1 
ATOM   12482 O OE1  . GLN   B  1 33  ? 69.115 42.891  -50.464 1.00 56.61  ? 59   GLN   B OE1  1 
ATOM   12483 N NE2  . GLN   B  1 33  ? 70.439 44.671  -50.141 1.00 57.62  ? 59   GLN   B NE2  1 
ATOM   12484 H H    . GLN   B  1 33  ? 67.350 42.841  -46.677 0.00 56.90  ? 59   GLN   B H    1 
ATOM   12485 H HA   . GLN   B  1 33  ? 70.146 42.822  -47.554 0.00 59.01  ? 59   GLN   B HA   1 
ATOM   12486 H HB2  . GLN   B  1 33  ? 68.243 45.071  -46.810 0.00 62.68  ? 59   GLN   B HB2  1 
ATOM   12487 H HB3  . GLN   B  1 33  ? 69.868 45.254  -47.522 0.00 62.99  ? 59   GLN   B HB3  1 
ATOM   12488 H HG2  . GLN   B  1 33  ? 67.484 43.946  -48.867 0.00 67.53  ? 59   GLN   B HG2  1 
ATOM   12489 H HG3  . GLN   B  1 33  ? 68.139 45.569  -49.198 0.00 68.63  ? 59   GLN   B HG3  1 
ATOM   12490 H HE21 . GLN   B  1 33  ? 70.604 45.548  -49.658 0.00 78.52  ? 59   GLN   B HE21 1 
ATOM   12491 H HE22 . GLN   B  1 33  ? 71.120 44.326  -50.810 0.00 77.77  ? 59   GLN   B HE22 1 
ATOM   12492 N N    . THR   B  1 34  ? 69.806 42.383  -44.596 1.00 43.65  ? 60   THR   B N    1 
ATOM   12493 C CA   . THR   B  1 34  ? 70.370 42.385  -43.244 1.00 44.25  ? 60   THR   B CA   1 
ATOM   12494 C C    . THR   B  1 34  ? 71.143 41.080  -42.950 1.00 44.39  ? 60   THR   B C    1 
ATOM   12495 O O    . THR   B  1 34  ? 71.273 40.705  -41.784 1.00 44.33  ? 60   THR   B O    1 
ATOM   12496 C CB   . THR   B  1 34  ? 69.255 42.643  -42.216 1.00 45.41  ? 60   THR   B CB   1 
ATOM   12497 O OG1  . THR   B  1 34  ? 68.241 41.653  -42.380 1.00 46.26  ? 60   THR   B OG1  1 
ATOM   12498 C CG2  . THR   B  1 34  ? 68.648 44.038  -42.356 1.00 45.74  ? 60   THR   B CG2  1 
ATOM   12499 H H    . THR   B  1 34  ? 69.253 41.550  -44.774 0.00 59.51  ? 60   THR   B H    1 
ATOM   12500 H HA   . THR   B  1 34  ? 71.089 43.196  -43.141 0.00 61.78  ? 60   THR   B HA   1 
ATOM   12501 H HB   . THR   B  1 34  ? 69.663 42.577  -41.209 0.00 62.80  ? 60   THR   B HB   1 
ATOM   12502 H HG1  . THR   B  1 34  ? 68.467 40.834  -41.865 0.00 62.45  ? 60   THR   B HG1  1 
ATOM   12503 H HG21 . THR   B  1 34  ? 67.900 44.196  -41.580 0.00 63.85  ? 60   THR   B HG21 1 
ATOM   12504 H HG22 . THR   B  1 34  ? 69.426 44.793  -42.256 0.00 64.40  ? 60   THR   B HG22 1 
ATOM   12505 H HG23 . THR   B  1 34  ? 68.173 44.145  -43.330 0.00 63.61  ? 60   THR   B HG23 1 
ATOM   12506 N N    . VAL   B  1 35  ? 71.682 40.408  -43.990 1.00 44.32  ? 61   VAL   B N    1 
ATOM   12507 C CA   . VAL   B  1 35  ? 72.486 39.196  -43.796 1.00 44.79  ? 61   VAL   B CA   1 
ATOM   12508 C C    . VAL   B  1 35  ? 73.855 39.648  -43.259 1.00 44.78  ? 61   VAL   B C    1 
ATOM   12509 O O    . VAL   B  1 35  ? 74.342 40.715  -43.630 1.00 44.76  ? 61   VAL   B O    1 
ATOM   12510 C CB   . VAL   B  1 35  ? 72.624 38.365  -45.104 1.00 45.76  ? 61   VAL   B CB   1 
ATOM   12511 C CG1  . VAL   B  1 35  ? 73.505 37.132  -44.887 1.00 46.18  ? 61   VAL   B CG1  1 
ATOM   12512 C CG2  . VAL   B  1 35  ? 71.253 37.955  -45.639 1.00 46.27  ? 61   VAL   B CG2  1 
ATOM   12513 H H    . VAL   B  1 35  ? 71.607 40.686  -44.963 0.00 60.24  ? 61   VAL   B H    1 
ATOM   12514 H HA   . VAL   B  1 35  ? 72.014 38.560  -43.049 0.00 59.96  ? 61   VAL   B HA   1 
ATOM   12515 H HB   . VAL   B  1 35  ? 73.103 38.983  -45.861 0.00 61.23  ? 61   VAL   B HB   1 
ATOM   12516 H HG11 . VAL   B  1 35  ? 73.378 36.451  -45.727 0.00 60.49  ? 61   VAL   B HG11 1 
ATOM   12517 H HG12 . VAL   B  1 35  ? 74.548 37.437  -44.828 0.00 61.38  ? 61   VAL   B HG12 1 
ATOM   12518 H HG13 . VAL   B  1 35  ? 73.205 36.642  -43.962 0.00 60.77  ? 61   VAL   B HG13 1 
ATOM   12519 H HG21 . VAL   B  1 35  ? 71.385 37.343  -46.530 0.00 60.55  ? 61   VAL   B HG21 1 
ATOM   12520 H HG22 . VAL   B  1 35  ? 70.731 37.384  -44.873 0.00 60.61  ? 61   VAL   B HG22 1 
ATOM   12521 H HG23 . VAL   B  1 35  ? 70.682 38.847  -45.893 0.00 61.27  ? 61   VAL   B HG23 1 
ATOM   12522 N N    . GLY   B  1 36  ? 74.444 38.858  -42.370 1.00 44.70  ? 62   GLY   B N    1 
ATOM   12523 C CA   . GLY   B  1 36  ? 75.727 39.200  -41.774 1.00 45.08  ? 62   GLY   B CA   1 
ATOM   12524 C C    . GLY   B  1 36  ? 76.868 39.267  -42.772 1.00 45.13  ? 62   GLY   B C    1 
ATOM   12525 O O    . GLY   B  1 36  ? 76.975 38.411  -43.651 1.00 45.16  ? 62   GLY   B O    1 
ATOM   12526 H H    . GLY   B  1 36  ? 74.064 37.974  -42.046 0.00 60.18  ? 62   GLY   B H    1 
ATOM   12527 H HA2  . GLY   B  1 36  ? 75.633 40.164  -41.275 0.00 62.38  ? 62   GLY   B HA2  1 
ATOM   12528 H HA3  . GLY   B  1 36  ? 75.980 38.454  -41.022 0.00 61.58  ? 62   GLY   B HA3  1 
ATOM   12529 N N    . LYS   B  1 37  ? 77.724 40.290  -42.644 1.00 44.93  ? 63   LYS   B N    1 
ATOM   12530 C CA   . LYS   B  1 37  ? 78.911 40.504  -43.486 1.00 45.28  ? 63   LYS   B CA   1 
ATOM   12531 C C    . LYS   B  1 37  ? 79.852 39.291  -43.506 1.00 45.22  ? 63   LYS   B C    1 
ATOM   12532 O O    . LYS   B  1 37  ? 80.537 39.060  -44.498 1.00 45.49  ? 63   LYS   B O    1 
ATOM   12533 C CB   . LYS   B  1 37  ? 79.705 41.732  -42.976 1.00 47.47  ? 63   LYS   B CB   1 
ATOM   12534 C CG   . LYS   B  1 37  ? 80.231 41.588  -41.536 1.00 52.30  ? 63   LYS   B CG   1 
ATOM   12535 C CD   . LYS   B  1 37  ? 81.012 42.808  -41.050 1.00 57.54  ? 63   LYS   B CD   1 
ATOM   12536 C CE   . LYS   B  1 37  ? 82.505 42.588  -41.100 1.00 62.09  ? 63   LYS   B CE   1 
ATOM   12537 N NZ   . LYS   B  1 37  ? 83.257 43.737  -40.526 1.00 64.91  ? 63   LYS   B NZ   1 
ATOM   12538 H H    . LYS   B  1 37  ? 77.593 41.029  -41.960 0.00 63.15  ? 63   LYS   B H    1 
ATOM   12539 H HA   . LYS   B  1 37  ? 78.593 40.704  -44.508 0.00 63.28  ? 63   LYS   B HA   1 
ATOM   12540 H HB2  . LYS   B  1 37  ? 80.564 41.887  -43.628 0.00 67.34  ? 63   LYS   B HB2  1 
ATOM   12541 H HB3  . LYS   B  1 37  ? 79.057 42.607  -43.007 0.00 67.40  ? 63   LYS   B HB3  1 
ATOM   12542 H HG2  . LYS   B  1 37  ? 79.391 41.450  -40.857 0.00 72.98  ? 63   LYS   B HG2  1 
ATOM   12543 H HG3  . LYS   B  1 37  ? 80.898 40.730  -41.470 0.00 72.96  ? 63   LYS   B HG3  1 
ATOM   12544 H HD2  . LYS   B  1 37  ? 80.772 43.663  -41.680 0.00 80.93  ? 63   LYS   B HD2  1 
ATOM   12545 H HD3  . LYS   B  1 37  ? 80.738 43.015  -40.017 0.00 80.84  ? 63   LYS   B HD3  1 
ATOM   12546 H HE2  . LYS   B  1 37  ? 82.764 41.703  -40.521 0.00 86.15  ? 63   LYS   B HE2  1 
ATOM   12547 H HE3  . LYS   B  1 37  ? 82.815 42.463  -42.137 0.00 86.31  ? 63   LYS   B HE3  1 
ATOM   12548 H HZ1  . LYS   B  1 37  ? 84.255 43.589  -40.639 0.00 91.25  ? 63   LYS   B HZ1  1 
ATOM   12549 H HZ2  . LYS   B  1 37  ? 82.994 44.596  -40.999 0.00 91.31  ? 63   LYS   B HZ2  1 
ATOM   12550 H HZ3  . LYS   B  1 37  ? 83.048 43.827  -39.537 0.00 91.16  ? 63   LYS   B HZ3  1 
ATOM   12551 N N    . TYR   B  1 38  ? 79.924 38.566  -42.382 1.00 44.76  ? 64   TYR   B N    1 
ATOM   12552 C CA   . TYR   B  1 38  ? 80.788 37.396  -42.221 1.00 44.66  ? 64   TYR   B CA   1 
ATOM   12553 C C    . TYR   B  1 38  ? 80.154 36.076  -42.720 1.00 42.13  ? 64   TYR   B C    1 
ATOM   12554 O O    . TYR   B  1 38  ? 80.869 35.083  -42.823 1.00 42.08  ? 64   TYR   B O    1 
ATOM   12555 C CB   . TYR   B  1 38  ? 81.246 37.259  -40.753 1.00 46.17  ? 64   TYR   B CB   1 
ATOM   12556 C CG   . TYR   B  1 38  ? 80.131 37.349  -39.733 1.00 48.86  ? 64   TYR   B CG   1 
ATOM   12557 C CD1  . TYR   B  1 38  ? 79.252 36.294  -39.540 1.00 50.48  ? 64   TYR   B CD1  1 
ATOM   12558 C CD2  . TYR   B  1 38  ? 79.930 38.507  -38.994 1.00 50.62  ? 64   TYR   B CD2  1 
ATOM   12559 C CE1  . TYR   B  1 38  ? 78.207 36.383  -38.631 1.00 51.87  ? 64   TYR   B CE1  1 
ATOM   12560 C CE2  . TYR   B  1 38  ? 78.895 38.604  -38.073 1.00 52.05  ? 64   TYR   B CE2  1 
ATOM   12561 C CZ   . TYR   B  1 38  ? 78.034 37.539  -37.893 1.00 53.14  ? 64   TYR   B CZ   1 
ATOM   12562 O OH   . TYR   B  1 38  ? 77.018 37.639  -36.971 1.00 55.15  ? 64   TYR   B OH   1 
ATOM   12563 H H    . TYR   B  1 38  ? 79.376 38.785  -41.557 0.00 62.33  ? 64   TYR   B H    1 
ATOM   12564 H HA   . TYR   B  1 38  ? 81.694 37.548  -42.807 0.00 62.09  ? 64   TYR   B HA   1 
ATOM   12565 H HB2  . TYR   B  1 38  ? 81.746 36.301  -40.620 0.00 63.70  ? 64   TYR   B HB2  1 
ATOM   12566 H HB3  . TYR   B  1 38  ? 81.940 38.069  -40.538 0.00 64.70  ? 64   TYR   B HB3  1 
ATOM   12567 H HD1  . TYR   B  1 38  ? 79.372 35.394  -40.118 0.00 67.68  ? 64   TYR   B HD1  1 
ATOM   12568 H HD2  . TYR   B  1 38  ? 80.595 39.344  -39.124 0.00 70.57  ? 64   TYR   B HD2  1 
ATOM   12569 H HE1  . TYR   B  1 38  ? 77.545 35.543  -38.497 0.00 69.16  ? 64   TYR   B HE1  1 
ATOM   12570 H HE2  . TYR   B  1 38  ? 78.766 39.506  -37.498 0.00 72.13  ? 64   TYR   B HE2  1 
ATOM   12571 H HH   . TYR   B  1 38  ? 76.574 36.761  -36.836 0.00 73.81  ? 64   TYR   B HH   1 
ATOM   12572 N N    . VAL   B  1 39  ? 78.839 36.057  -43.034 1.00 39.57  ? 65   VAL   B N    1 
ATOM   12573 C CA   . VAL   B  1 39  ? 78.158 34.853  -43.523 1.00 38.03  ? 65   VAL   B CA   1 
ATOM   12574 C C    . VAL   B  1 39  ? 78.838 34.312  -44.789 1.00 36.01  ? 65   VAL   B C    1 
ATOM   12575 O O    . VAL   B  1 39  ? 79.137 35.084  -45.691 1.00 35.71  ? 65   VAL   B O    1 
ATOM   12576 C CB   . VAL   B  1 39  ? 76.642 35.135  -43.766 1.00 38.52  ? 65   VAL   B CB   1 
ATOM   12577 C CG1  . VAL   B  1 39  ? 75.983 34.026  -44.580 1.00 38.74  ? 65   VAL   B CG1  1 
ATOM   12578 C CG2  . VAL   B  1 39  ? 75.898 35.339  -42.443 1.00 38.75  ? 65   VAL   B CG2  1 
ATOM   12579 H H    . VAL   B  1 39  ? 78.221 36.858  -42.954 0.00 54.46  ? 65   VAL   B H    1 
ATOM   12580 H HA   . VAL   B  1 39  ? 78.242 34.085  -42.755 0.00 51.30  ? 65   VAL   B HA   1 
ATOM   12581 H HB   . VAL   B  1 39  ? 76.543 36.053  -44.342 0.00 52.10  ? 65   VAL   B HB   1 
ATOM   12582 H HG11 . VAL   B  1 39  ? 74.904 34.152  -44.517 0.00 50.98  ? 65   VAL   B HG11 1 
ATOM   12583 H HG12 . VAL   B  1 39  ? 76.277 34.106  -45.625 0.00 51.19  ? 65   VAL   B HG12 1 
ATOM   12584 H HG13 . VAL   B  1 39  ? 76.274 33.058  -44.176 0.00 50.90  ? 65   VAL   B HG13 1 
ATOM   12585 H HG21 . VAL   B  1 39  ? 74.883 35.668  -42.657 0.00 51.96  ? 65   VAL   B HG21 1 
ATOM   12586 H HG22 . VAL   B  1 39  ? 75.877 34.395  -41.901 0.00 51.76  ? 65   VAL   B HG22 1 
ATOM   12587 H HG23 . VAL   B  1 39  ? 76.414 36.096  -41.853 0.00 52.74  ? 65   VAL   B HG23 1 
ATOM   12588 N N    . THR   B  1 40  ? 79.077 32.989  -44.839 1.00 34.97  ? 66   THR   B N    1 
ATOM   12589 C CA   . THR   B  1 40  ? 79.708 32.315  -45.979 1.00 34.22  ? 66   THR   B CA   1 
ATOM   12590 C C    . THR   B  1 40  ? 78.737 31.385  -46.717 1.00 33.57  ? 66   THR   B C    1 
ATOM   12591 O O    . THR   B  1 40  ? 79.011 31.040  -47.857 1.00 34.09  ? 66   THR   B O    1 
ATOM   12592 C CB   . THR   B  1 40  ? 80.933 31.517  -45.520 1.00 34.84  ? 66   THR   B CB   1 
ATOM   12593 O OG1  . THR   B  1 40  ? 80.507 30.476  -44.643 1.00 35.34  ? 66   THR   B OG1  1 
ATOM   12594 C CG2  . THR   B  1 40  ? 81.976 32.388  -44.836 1.00 35.23  ? 66   THR   B CG2  1 
ATOM   12595 H H    . THR   B  1 40  ? 78.842 32.347  -44.089 0.00 46.83  ? 66   THR   B H    1 
ATOM   12596 H HA   . THR   B  1 40  ? 80.063 33.049  -46.700 0.00 46.29  ? 66   THR   B HA   1 
ATOM   12597 H HB   . THR   B  1 40  ? 81.401 31.066  -46.394 0.00 46.68  ? 66   THR   B HB   1 
ATOM   12598 H HG1  . THR   B  1 40  ? 81.297 29.990  -44.289 0.00 47.11  ? 66   THR   B HG1  1 
ATOM   12599 H HG21 . THR   B  1 40  ? 82.839 31.783  -44.561 0.00 48.22  ? 66   THR   B HG21 1 
ATOM   12600 H HG22 . THR   B  1 40  ? 82.302 33.173  -45.516 0.00 48.47  ? 66   THR   B HG22 1 
ATOM   12601 H HG23 . THR   B  1 40  ? 81.565 32.842  -43.936 0.00 48.31  ? 66   THR   B HG23 1 
ATOM   12602 N N    . GLU   B  1 41  ? 77.638 30.940  -46.083 1.00 32.64  ? 67   GLU   B N    1 
ATOM   12603 C CA   . GLU   B  1 41  ? 76.662 30.062  -46.734 1.00 32.11  ? 67   GLU   B CA   1 
ATOM   12604 C C    . GLU   B  1 41  ? 75.283 30.609  -46.421 1.00 31.07  ? 67   GLU   B C    1 
ATOM   12605 O O    . GLU   B  1 41  ? 74.951 30.783  -45.253 1.00 31.07  ? 67   GLU   B O    1 
ATOM   12606 C CB   . GLU   B  1 41  ? 76.801 28.610  -46.245 1.00 34.76  ? 67   GLU   B CB   1 
ATOM   12607 C CG   . GLU   B  1 41  ? 78.224 28.075  -46.362 1.00 39.88  ? 67   GLU   B CG   1 
ATOM   12608 C CD   . GLU   B  1 41  ? 78.418 26.587  -46.135 1.00 47.01  ? 67   GLU   B CD   1 
ATOM   12609 O OE1  . GLU   B  1 41  ? 77.420 25.879  -45.862 1.00 47.96  ? 67   GLU   B OE1  1 
ATOM   12610 O OE2  . GLU   B  1 41  ? 79.580 26.130  -46.224 1.00 49.81  ? 67   GLU   B OE2  1 
ATOM   12611 H H    . GLU   B  1 41  ? 77.398 31.151  -45.120 0.00 42.95  ? 67   GLU   B H    1 
ATOM   12612 H HA   . GLU   B  1 41  ? 76.795 30.064  -47.815 0.00 41.42  ? 67   GLU   B HA   1 
ATOM   12613 H HB2  . GLU   B  1 41  ? 76.508 28.573  -45.197 0.00 44.21  ? 67   GLU   B HB2  1 
ATOM   12614 H HB3  . GLU   B  1 41  ? 76.146 27.975  -46.840 0.00 43.72  ? 67   GLU   B HB3  1 
ATOM   12615 H HG2  . GLU   B  1 41  ? 78.605 28.307  -47.355 0.00 50.66  ? 67   GLU   B HG2  1 
ATOM   12616 H HG3  . GLU   B  1 41  ? 78.836 28.583  -45.619 0.00 51.02  ? 67   GLU   B HG3  1 
ATOM   12617 N N    . LEU   B  1 42  ? 74.508 30.935  -47.447 1.00 29.98  ? 68   LEU   B N    1 
ATOM   12618 C CA   . LEU   B  1 42  ? 73.194 31.532  -47.265 1.00 29.87  ? 68   LEU   B CA   1 
ATOM   12619 C C    . LEU   B  1 42  ? 72.128 30.609  -47.826 1.00 29.71  ? 68   LEU   B C    1 
ATOM   12620 O O    . LEU   B  1 42  ? 72.138 30.306  -49.019 1.00 29.31  ? 68   LEU   B O    1 
ATOM   12621 C CB   . LEU   B  1 42  ? 73.182 32.897  -47.969 1.00 30.30  ? 68   LEU   B CB   1 
ATOM   12622 C CG   . LEU   B  1 42  ? 71.894 33.716  -47.981 1.00 31.93  ? 68   LEU   B CG   1 
ATOM   12623 C CD1  . LEU   B  1 42  ? 71.305 33.884  -46.578 1.00 32.52  ? 68   LEU   B CD1  1 
ATOM   12624 C CD2  . LEU   B  1 42  ? 72.167 35.095  -48.579 1.00 32.79  ? 68   LEU   B CD2  1 
ATOM   12625 H H    . LEU   B  1 42  ? 74.751 30.796  -48.423 0.00 38.58  ? 68   LEU   B H    1 
ATOM   12626 H HA   . LEU   B  1 42  ? 72.991 31.702  -46.210 0.00 38.59  ? 68   LEU   B HA   1 
ATOM   12627 H HB2  . LEU   B  1 42  ? 73.935 33.514  -47.482 0.00 40.00  ? 68   LEU   B HB2  1 
ATOM   12628 H HB3  . LEU   B  1 42  ? 73.469 32.741  -49.008 0.00 39.43  ? 68   LEU   B HB3  1 
ATOM   12629 H HG   . LEU   B  1 42  ? 71.156 33.220  -48.608 0.00 41.14  ? 68   LEU   B HG   1 
ATOM   12630 H HD11 . LEU   B  1 42  ? 70.472 34.584  -46.626 0.00 42.48  ? 68   LEU   B HD11 1 
ATOM   12631 H HD12 . LEU   B  1 42  ? 70.952 32.918  -46.221 0.00 41.84  ? 68   LEU   B HD12 1 
ATOM   12632 H HD13 . LEU   B  1 42  ? 72.077 34.269  -45.913 0.00 42.72  ? 68   LEU   B HD13 1 
ATOM   12633 H HD21 . LEU   B  1 42  ? 71.239 35.665  -48.604 0.00 43.33  ? 68   LEU   B HD21 1 
ATOM   12634 H HD22 . LEU   B  1 42  ? 72.899 35.611  -47.960 0.00 43.69  ? 68   LEU   B HD22 1 
ATOM   12635 H HD23 . LEU   B  1 42  ? 72.556 34.972  -49.588 0.00 43.21  ? 68   LEU   B HD23 1 
ATOM   12636 N N    . ASP   B  1 43  ? 71.231 30.130  -46.952 1.00 29.24  ? 69   ASP   B N    1 
ATOM   12637 C CA   . ASP   B  1 43  ? 70.146 29.257  -47.342 1.00 28.98  ? 69   ASP   B CA   1 
ATOM   12638 C C    . ASP   B  1 43  ? 68.873 30.056  -47.345 1.00 28.60  ? 69   ASP   B C    1 
ATOM   12639 O O    . ASP   B  1 43  ? 68.337 30.339  -46.280 1.00 28.89  ? 69   ASP   B O    1 
ATOM   12640 C CB   . ASP   B  1 43  ? 70.043 28.034  -46.407 1.00 30.21  ? 69   ASP   B CB   1 
ATOM   12641 C CG   . ASP   B  1 43  ? 68.997 26.984  -46.795 1.00 35.23  ? 69   ASP   B CG   1 
ATOM   12642 O OD1  . ASP   B  1 43  ? 68.265 27.201  -47.784 1.00 34.37  ? 69   ASP   B OD1  1 
ATOM   12643 O OD2  . ASP   B  1 43  ? 68.916 25.948  -46.108 1.00 39.23  ? 69   ASP   B OD2  1 
ATOM   12644 H H    . ASP   B  1 43  ? 71.236 30.330  -45.957 0.00 36.90  ? 69   ASP   B H    1 
ATOM   12645 H HA   . ASP   B  1 43  ? 70.312 28.898  -48.353 0.00 35.67  ? 69   ASP   B HA   1 
ATOM   12646 H HB2  . ASP   B  1 43  ? 71.011 27.534  -46.402 0.00 36.92  ? 69   ASP   B HB2  1 
ATOM   12647 H HB3  . ASP   B  1 43  ? 69.813 28.374  -45.398 0.00 37.07  ? 69   ASP   B HB3  1 
ATOM   12648 N N    . LEU   B  1 44  ? 68.386 30.409  -48.537 1.00 27.92  ? 70   LEU   B N    1 
ATOM   12649 C CA   . LEU   B  1 44  ? 67.120 31.124  -48.717 1.00 28.13  ? 70   LEU   B CA   1 
ATOM   12650 C C    . LEU   B  1 44  ? 66.044 30.252  -49.373 1.00 27.80  ? 70   LEU   B C    1 
ATOM   12651 O O    . LEU   B  1 44  ? 65.089 30.796  -49.934 1.00 28.00  ? 70   LEU   B O    1 
ATOM   12652 C CB   . LEU   B  1 44  ? 67.359 32.365  -49.591 1.00 28.71  ? 70   LEU   B CB   1 
ATOM   12653 C CG   . LEU   B  1 44  ? 68.049 33.529  -48.917 1.00 30.56  ? 70   LEU   B CG   1 
ATOM   12654 C CD1  . LEU   B  1 44  ? 68.646 34.447  -49.947 1.00 30.80  ? 70   LEU   B CD1  1 
ATOM   12655 C CD2  . LEU   B  1 44  ? 67.071 34.315  -48.059 1.00 31.10  ? 70   LEU   B CD2  1 
ATOM   12656 H H    . LEU   B  1 44  ? 68.854 30.210  -49.416 0.00 34.60  ? 70   LEU   B H    1 
ATOM   12657 H HA   . LEU   B  1 44  ? 66.722 31.430  -47.751 0.00 35.12  ? 70   LEU   B HA   1 
ATOM   12658 H HB2  . LEU   B  1 44  ? 67.958 32.074  -50.453 0.00 36.16  ? 70   LEU   B HB2  1 
ATOM   12659 H HB3  . LEU   B  1 44  ? 66.404 32.758  -49.937 0.00 36.26  ? 70   LEU   B HB3  1 
ATOM   12660 H HG   . LEU   B  1 44  ? 68.855 33.175  -48.275 0.00 39.08  ? 70   LEU   B HG   1 
ATOM   12661 H HD11 . LEU   B  1 44  ? 69.095 35.295  -49.433 0.00 40.33  ? 70   LEU   B HD11 1 
ATOM   12662 H HD12 . LEU   B  1 44  ? 69.410 33.909  -50.507 0.00 39.69  ? 70   LEU   B HD12 1 
ATOM   12663 H HD13 . LEU   B  1 44  ? 67.860 34.788  -50.619 0.00 39.86  ? 70   LEU   B HD13 1 
ATOM   12664 H HD21 . LEU   B  1 44  ? 67.637 34.988  -47.417 0.00 40.45  ? 70   LEU   B HD21 1 
ATOM   12665 H HD22 . LEU   B  1 44  ? 66.428 34.899  -48.716 0.00 40.16  ? 70   LEU   B HD22 1 
ATOM   12666 H HD23 . LEU   B  1 44  ? 66.459 33.652  -47.451 0.00 39.65  ? 70   LEU   B HD23 1 
ATOM   12667 N N    . SER   B  1 45  ? 66.166 28.929  -49.290 1.00 27.44  ? 71   SER   B N    1 
ATOM   12668 C CA   . SER   B  1 45  ? 65.218 28.033  -49.934 1.00 28.32  ? 71   SER   B CA   1 
ATOM   12669 C C    . SER   B  1 45  ? 63.804 28.127  -49.338 1.00 29.35  ? 71   SER   B C    1 
ATOM   12670 O O    . SER   B  1 45  ? 63.644 28.545  -48.194 1.00 29.04  ? 71   SER   B O    1 
ATOM   12671 C CB   . SER   B  1 45  ? 65.721 26.594  -49.861 1.00 29.23  ? 71   SER   B CB   1 
ATOM   12672 O OG   . SER   B  1 45  ? 65.675 26.103  -48.530 1.00 31.92  ? 71   SER   B OG   1 
ATOM   12673 H H    . SER   B  1 45  ? 66.890 28.444  -48.769 0.00 33.08  ? 71   SER   B H    1 
ATOM   12674 H HA   . SER   B  1 45  ? 65.149 28.301  -50.987 0.00 33.84  ? 71   SER   B HA   1 
ATOM   12675 H HB2  . SER   B  1 45  ? 65.091 25.968  -50.491 0.00 34.11  ? 71   SER   B HB2  1 
ATOM   12676 H HB3  . SER   B  1 45  ? 66.749 26.559  -50.216 0.00 34.51  ? 71   SER   B HB3  1 
ATOM   12677 H HG   . SER   B  1 45  ? 66.299 26.612  -47.950 0.00 37.75  ? 71   SER   B HG   1 
ATOM   12678 N N    . ASP   B  1 46  ? 62.783 27.736  -50.120 1.00 29.88  ? 72   ASP   B N    1 
ATOM   12679 C CA   . ASP   B  1 46  ? 61.392 27.683  -49.665 1.00 31.42  ? 72   ASP   B CA   1 
ATOM   12680 C C    . ASP   B  1 46  ? 60.844 29.014  -49.128 1.00 32.11  ? 72   ASP   B C    1 
ATOM   12681 O O    . ASP   B  1 46  ? 60.150 29.043  -48.115 1.00 32.73  ? 72   ASP   B O    1 
ATOM   12682 C CB   . ASP   B  1 46  ? 61.214 26.566  -48.628 1.00 33.91  ? 72   ASP   B CB   1 
ATOM   12683 C CG   . ASP   B  1 46  ? 61.642 25.221  -49.153 1.00 41.40  ? 72   ASP   B CG   1 
ATOM   12684 O OD1  . ASP   B  1 46  ? 60.851 24.595  -49.888 1.00 42.92  ? 72   ASP   B OD1  1 
ATOM   12685 O OD2  . ASP   B  1 46  ? 62.768 24.789  -48.827 1.00 45.82  ? 72   ASP   B OD2  1 
ATOM   12686 H H    . ASP   B  1 46  ? 62.897 27.449  -51.087 0.00 35.19  ? 72   ASP   B H    1 
ATOM   12687 H HA   . ASP   B  1 46  ? 60.775 27.416  -50.521 0.00 36.89  ? 72   ASP   B HA   1 
ATOM   12688 H HB2  . ASP   B  1 46  ? 61.804 26.792  -47.742 0.00 39.75  ? 72   ASP   B HB2  1 
ATOM   12689 H HB3  . ASP   B  1 46  ? 60.161 26.484  -48.363 0.00 39.52  ? 72   ASP   B HB3  1 
ATOM   12690 N N    . ASN   B  1 47  ? 61.133 30.099  -49.825 1.00 31.67  ? 73   ASN   B N    1 
ATOM   12691 C CA   . ASN   B  1 47  ? 60.613 31.415  -49.478 1.00 32.17  ? 73   ASN   B CA   1 
ATOM   12692 C C    . ASN   B  1 47  ? 59.727 31.898  -50.658 1.00 32.75  ? 73   ASN   B C    1 
ATOM   12693 O O    . ASN   B  1 47  ? 59.407 31.097  -51.542 1.00 32.36  ? 73   ASN   B O    1 
ATOM   12694 C CB   . ASN   B  1 47  ? 61.799 32.353  -49.132 1.00 32.80  ? 73   ASN   B CB   1 
ATOM   12695 C CG   . ASN   B  1 47  ? 62.277 32.190  -47.717 1.00 35.13  ? 73   ASN   B CG   1 
ATOM   12696 O OD1  . ASN   B  1 47  ? 61.491 32.284  -46.776 1.00 36.43  ? 73   ASN   B OD1  1 
ATOM   12697 N ND2  . ASN   B  1 47  ? 63.565 31.924  -47.526 1.00 34.98  ? 73   ASN   B ND2  1 
ATOM   12698 H H    . ASN   B  1 47  ? 61.720 30.105  -50.653 0.00 38.26  ? 73   ASN   B H    1 
ATOM   12699 H HA   . ASN   B  1 47  ? 59.948 31.354  -48.617 0.00 39.30  ? 73   ASN   B HA   1 
ATOM   12700 H HB2  . ASN   B  1 47  ? 62.660 32.092  -49.741 0.00 40.51  ? 73   ASN   B HB2  1 
ATOM   12701 H HB3  . ASN   B  1 47  ? 61.522 33.395  -49.286 0.00 41.02  ? 73   ASN   B HB3  1 
ATOM   12702 H HD21 . ASN   B  1 47  ? 63.913 31.810  -46.580 0.00 43.22  ? 73   ASN   B HD21 1 
ATOM   12703 H HD22 . ASN   B  1 47  ? 64.209 31.837  -48.306 0.00 43.18  ? 73   ASN   B HD22 1 
ATOM   12704 N N    . PHE   B  1 48  ? 59.299 33.165  -50.664 1.00 33.63  ? 74   PHE   B N    1 
ATOM   12705 C CA   . PHE   B  1 48  ? 58.470 33.719  -51.734 1.00 34.93  ? 74   PHE   B CA   1 
ATOM   12706 C C    . PHE   B  1 48  ? 59.251 34.728  -52.590 1.00 34.66  ? 74   PHE   B C    1 
ATOM   12707 O O    . PHE   B  1 48  ? 58.643 35.649  -53.131 1.00 35.06  ? 74   PHE   B O    1 
ATOM   12708 C CB   . PHE   B  1 48  ? 57.223 34.397  -51.134 1.00 36.02  ? 74   PHE   B CB   1 
ATOM   12709 C CG   . PHE   B  1 48  ? 56.433 33.559  -50.157 1.00 37.81  ? 74   PHE   B CG   1 
ATOM   12710 C CD1  . PHE   B  1 48  ? 56.183 32.222  -50.410 1.00 39.41  ? 74   PHE   B CD1  1 
ATOM   12711 C CD2  . PHE   B  1 48  ? 55.812 34.141  -49.066 1.00 39.48  ? 74   PHE   B CD2  1 
ATOM   12712 C CE1  . PHE   B  1 48  ? 55.384 31.470  -49.555 1.00 40.39  ? 74   PHE   B CE1  1 
ATOM   12713 C CE2  . PHE   B  1 48  ? 55.001 33.389  -48.222 1.00 40.52  ? 74   PHE   B CE2  1 
ATOM   12714 C CZ   . PHE   B  1 48  ? 54.819 32.052  -48.456 1.00 40.36  ? 74   PHE   B CZ   1 
ATOM   12715 H H    . PHE   B  1 48  ? 59.509 33.840  -49.936 0.00 42.13  ? 74   PHE   B H    1 
ATOM   12716 H HA   . PHE   B  1 48  ? 58.123 32.931  -52.400 0.00 43.31  ? 74   PHE   B HA   1 
ATOM   12717 H HB2  . PHE   B  1 48  ? 57.536 35.304  -50.619 0.00 45.69  ? 74   PHE   B HB2  1 
ATOM   12718 H HB3  . PHE   B  1 48  ? 56.542 34.653  -51.944 0.00 45.43  ? 74   PHE   B HB3  1 
ATOM   12719 H HD1  . PHE   B  1 48  ? 56.630 31.739  -51.257 0.00 48.15  ? 74   PHE   B HD1  1 
ATOM   12720 H HD2  . PHE   B  1 48  ? 55.949 35.191  -48.872 0.00 49.80  ? 74   PHE   B HD2  1 
ATOM   12721 H HE1  . PHE   B  1 48  ? 55.243 30.418  -49.738 0.00 48.76  ? 74   PHE   B HE1  1 
ATOM   12722 H HE2  . PHE   B  1 48  ? 54.560 33.846  -47.352 0.00 50.45  ? 74   PHE   B HE2  1 
ATOM   12723 H HZ   . PHE   B  1 48  ? 54.209 31.467  -47.788 0.00 49.18  ? 74   PHE   B HZ   1 
ATOM   12724 N N    . ILE   B  1 49  ? 60.584 34.589  -52.686 1.00 34.02  ? 75   ILE   B N    1 
ATOM   12725 C CA   . ILE   B  1 49  ? 61.413 35.494  -53.482 1.00 34.14  ? 75   ILE   B CA   1 
ATOM   12726 C C    . ILE   B  1 49  ? 61.086 35.304  -54.971 1.00 34.63  ? 75   ILE   B C    1 
ATOM   12727 O O    . ILE   B  1 49  ? 61.101 34.175  -55.460 1.00 34.28  ? 75   ILE   B O    1 
ATOM   12728 C CB   . ILE   B  1 49  ? 62.924 35.268  -53.213 1.00 34.08  ? 75   ILE   B CB   1 
ATOM   12729 C CG1  . ILE   B  1 49  ? 63.285 35.489  -51.712 1.00 34.79  ? 75   ILE   B CG1  1 
ATOM   12730 C CG2  . ILE   B  1 49  ? 63.751 36.182  -54.108 1.00 34.39  ? 75   ILE   B CG2  1 
ATOM   12731 C CD1  . ILE   B  1 49  ? 64.526 34.783  -51.263 1.00 35.94  ? 75   ILE   B CD1  1 
ATOM   12732 H H    . ILE   B  1 49  ? 61.121 33.886  -52.191 0.00 42.71  ? 75   ILE   B H    1 
ATOM   12733 H HA   . ILE   B  1 49  ? 61.179 36.520  -53.200 0.00 44.15  ? 75   ILE   B HA   1 
ATOM   12734 H HB   . ILE   B  1 49  ? 63.151 34.237  -53.482 0.00 43.08  ? 75   ILE   B HB   1 
ATOM   12735 H HG12 . ILE   B  1 49  ? 63.440 36.555  -51.551 0.00 45.04  ? 75   ILE   B HG12 1 
ATOM   12736 H HG13 . ILE   B  1 49  ? 62.473 35.143  -51.075 0.00 44.28  ? 75   ILE   B HG13 1 
ATOM   12737 H HG21 . ILE   B  1 49  ? 64.736 36.326  -53.668 0.00 44.58  ? 75   ILE   B HG21 1 
ATOM   12738 H HG22 . ILE   B  1 49  ? 63.863 35.720  -55.088 0.00 44.25  ? 75   ILE   B HG22 1 
ATOM   12739 H HG23 . ILE   B  1 49  ? 63.245 37.142  -54.204 0.00 44.88  ? 75   ILE   B HG23 1 
ATOM   12740 H HD11 . ILE   B  1 49  ? 64.612 34.881  -50.182 0.00 45.71  ? 75   ILE   B HD11 1 
ATOM   12741 H HD12 . ILE   B  1 49  ? 64.455 33.731  -51.537 0.00 45.14  ? 75   ILE   B HD12 1 
ATOM   12742 H HD13 . ILE   B  1 49  ? 65.395 35.233  -51.740 0.00 45.92  ? 75   ILE   B HD13 1 
ATOM   12743 N N    . THR   B  1 50  ? 60.784 36.412  -55.676 1.00 34.71  ? 76   THR   B N    1 
ATOM   12744 C CA   . THR   B  1 50  ? 60.427 36.391  -57.096 1.00 35.36  ? 76   THR   B CA   1 
ATOM   12745 C C    . THR   B  1 50  ? 61.505 37.003  -57.993 1.00 35.55  ? 76   THR   B C    1 
ATOM   12746 O O    . THR   B  1 50  ? 61.478 36.759  -59.198 1.00 36.10  ? 76   THR   B O    1 
ATOM   12747 C CB   . THR   B  1 50  ? 59.097 37.140  -57.299 1.00 36.85  ? 76   THR   B CB   1 
ATOM   12748 O OG1  . THR   B  1 50  ? 59.223 38.461  -56.758 1.00 37.83  ? 76   THR   B OG1  1 
ATOM   12749 C CG2  . THR   B  1 50  ? 57.912 36.422  -56.649 1.00 36.95  ? 76   THR   B CG2  1 
ATOM   12750 H H    . THR   B  1 50  ? 60.780 37.349  -55.285 0.00 45.32  ? 76   THR   B H    1 
ATOM   12751 H HA   . THR   B  1 50  ? 60.271 35.368  -57.433 0.00 45.29  ? 76   THR   B HA   1 
ATOM   12752 H HB   . THR   B  1 50  ? 58.892 37.206  -58.367 0.00 48.08  ? 76   THR   B HB   1 
ATOM   12753 H HG1  . THR   B  1 50  ? 59.591 39.088  -57.434 0.00 50.13  ? 76   THR   B HG1  1 
ATOM   12754 H HG21 . THR   B  1 50  ? 57.080 37.117  -56.539 0.00 48.03  ? 76   THR   B HG21 1 
ATOM   12755 H HG22 . THR   B  1 50  ? 57.586 35.599  -57.283 0.00 47.32  ? 76   THR   B HG22 1 
ATOM   12756 H HG23 . THR   B  1 50  ? 58.181 36.034  -55.668 0.00 47.39  ? 76   THR   B HG23 1 
ATOM   12757 N N    . HIS   B  1 51  ? 62.428 37.815  -57.439 1.00 35.18  ? 77   HIS   B N    1 
ATOM   12758 C CA   . HIS   B  1 51  ? 63.453 38.482  -58.231 1.00 35.46  ? 77   HIS   B CA   1 
ATOM   12759 C C    . HIS   B  1 51  ? 64.828 38.418  -57.586 1.00 34.80  ? 77   HIS   B C    1 
ATOM   12760 O O    . HIS   B  1 51  ? 64.954 38.616  -56.374 1.00 34.74  ? 77   HIS   B O    1 
ATOM   12761 C CB   . HIS   B  1 51  ? 63.097 39.972  -58.395 1.00 37.11  ? 77   HIS   B CB   1 
ATOM   12762 C CG   . HIS   B  1 51  ? 61.906 40.230  -59.261 1.00 40.81  ? 77   HIS   B CG   1 
ATOM   12763 N ND1  . HIS   B  1 51  ? 60.617 40.143  -58.760 1.00 43.06  ? 77   HIS   B ND1  1 
ATOM   12764 C CD2  . HIS   B  1 51  ? 61.846 40.586  -60.566 1.00 42.29  ? 77   HIS   B CD2  1 
ATOM   12765 C CE1  . HIS   B  1 51  ? 59.815 40.433  -59.774 1.00 43.76  ? 77   HIS   B CE1  1 
ATOM   12766 N NE2  . HIS   B  1 51  ? 60.512 40.704  -60.883 1.00 43.79  ? 77   HIS   B NE2  1 
ATOM   12767 H H    . HIS   B  1 51  ? 62.489 38.040  -56.451 0.00 46.37  ? 77   HIS   B H    1 
ATOM   12768 H HA   . HIS   B  1 51  ? 63.519 38.040  -59.223 0.00 46.98  ? 77   HIS   B HA   1 
ATOM   12769 H HB2  . HIS   B  1 51  ? 62.888 40.391  -57.412 0.00 50.03  ? 77   HIS   B HB2  1 
ATOM   12770 H HB3  . HIS   B  1 51  ? 63.946 40.487  -58.841 0.00 50.25  ? 77   HIS   B HB3  1 
ATOM   12771 H HD2  . HIS   B  1 51  ? 62.679 40.741  -61.229 0.00 56.82  ? 77   HIS   B HD2  1 
ATOM   12772 H HE1  . HIS   B  1 51  ? 58.740 40.452  -59.713 0.00 58.22  ? 77   HIS   B HE1  1 
ATOM   12773 H HE2  . HIS   B  1 51  ? 60.129 40.948  -61.790 0.00 58.79  ? 77   HIS   B HE2  1 
ATOM   12774 N N    . ILE   B  1 52  ? 65.865 38.244  -58.425 1.00 34.07  ? 78   ILE   B N    1 
ATOM   12775 C CA   . ILE   B  1 52  ? 67.270 38.300  -58.028 1.00 33.77  ? 78   ILE   B CA   1 
ATOM   12776 C C    . ILE   B  1 52  ? 67.929 39.293  -58.985 1.00 34.32  ? 78   ILE   B C    1 
ATOM   12777 O O    . ILE   B  1 52  ? 67.853 39.110  -60.202 1.00 34.06  ? 78   ILE   B O    1 
ATOM   12778 C CB   . ILE   B  1 52  ? 67.997 36.938  -58.095 1.00 33.29  ? 78   ILE   B CB   1 
ATOM   12779 C CG1  . ILE   B  1 52  ? 67.274 35.836  -57.276 1.00 33.78  ? 78   ILE   B CG1  1 
ATOM   12780 C CG2  . ILE   B  1 52  ? 69.466 37.101  -57.664 1.00 33.19  ? 78   ILE   B CG2  1 
ATOM   12781 C CD1  . ILE   B  1 52  ? 67.189 36.074  -55.794 1.00 34.89  ? 78   ILE   B CD1  1 
ATOM   12782 H H    . ILE   B  1 52  ? 65.758 38.062  -59.418 0.00 45.46  ? 78   ILE   B H    1 
ATOM   12783 H HA   . ILE   B  1 52  ? 67.361 38.688  -57.015 0.00 45.40  ? 78   ILE   B HA   1 
ATOM   12784 H HB   . ILE   B  1 52  ? 67.999 36.626  -59.138 0.00 43.99  ? 78   ILE   B HB   1 
ATOM   12785 H HG12 . ILE   B  1 52  ? 66.258 35.737  -57.654 0.00 43.87  ? 78   ILE   B HG12 1 
ATOM   12786 H HG13 . ILE   B  1 52  ? 67.804 34.895  -57.421 0.00 43.61  ? 78   ILE   B HG13 1 
ATOM   12787 H HG21 . ILE   B  1 52  ? 69.803 36.175  -57.201 0.00 43.74  ? 78   ILE   B HG21 1 
ATOM   12788 H HG22 . ILE   B  1 52  ? 70.065 37.298  -58.551 0.00 44.40  ? 78   ILE   B HG22 1 
ATOM   12789 H HG23 . ILE   B  1 52  ? 69.557 37.927  -56.959 0.00 44.56  ? 78   ILE   B HG23 1 
ATOM   12790 H HD11 . ILE   B  1 52  ? 66.681 35.226  -55.337 0.00 44.87  ? 78   ILE   B HD11 1 
ATOM   12791 H HD12 . ILE   B  1 52  ? 68.190 36.167  -55.378 0.00 45.49  ? 78   ILE   B HD12 1 
ATOM   12792 H HD13 . ILE   B  1 52  ? 66.621 36.984  -55.607 0.00 45.73  ? 78   ILE   B HD13 1 
ATOM   12793 N N    . THR   B  1 53  ? 68.561 40.339  -58.446 1.00 34.69  ? 79   THR   B N    1 
ATOM   12794 C CA   . THR   B  1 53  ? 69.251 41.359  -59.240 1.00 36.04  ? 79   THR   B CA   1 
ATOM   12795 C C    . THR   B  1 53  ? 70.728 41.493  -58.778 1.00 36.73  ? 79   THR   B C    1 
ATOM   12796 O O    . THR   B  1 53  ? 71.133 40.824  -57.825 1.00 36.53  ? 79   THR   B O    1 
ATOM   12797 C CB   . THR   B  1 53  ? 68.472 42.704  -59.137 1.00 37.71  ? 79   THR   B CB   1 
ATOM   12798 O OG1  . THR   B  1 53  ? 68.681 43.265  -57.838 1.00 38.63  ? 79   THR   B OG1  1 
ATOM   12799 C CG2  . THR   B  1 53  ? 66.976 42.546  -59.429 1.00 37.83  ? 79   THR   B CG2  1 
ATOM   12800 H H    . THR   B  1 53  ? 68.618 40.515  -57.448 0.00 47.64  ? 79   THR   B H    1 
ATOM   12801 H HA   . THR   B  1 53  ? 69.270 41.077  -60.291 0.00 49.84  ? 79   THR   B HA   1 
ATOM   12802 H HB   . THR   B  1 53  ? 68.875 43.393  -59.878 0.00 53.10  ? 79   THR   B HB   1 
ATOM   12803 H HG1  . THR   B  1 53  ? 68.193 44.126  -57.757 0.00 54.43  ? 79   THR   B HG1  1 
ATOM   12804 H HG21 . THR   B  1 53  ? 66.515 43.526  -59.537 0.00 53.08  ? 79   THR   B HG21 1 
ATOM   12805 H HG22 . THR   B  1 53  ? 66.830 41.982  -60.349 0.00 52.27  ? 79   THR   B HG22 1 
ATOM   12806 H HG23 . THR   B  1 53  ? 66.485 42.021  -58.610 0.00 52.12  ? 79   THR   B HG23 1 
ATOM   12807 N N    . ASN   B  1 54  ? 71.534 42.354  -59.447 1.00 37.48  ? 80   ASN   B N    1 
ATOM   12808 C CA   . ASN   B  1 54  ? 72.917 42.600  -59.022 1.00 38.61  ? 80   ASN   B CA   1 
ATOM   12809 C C    . ASN   B  1 54  ? 73.005 43.345  -57.652 1.00 38.85  ? 80   ASN   B C    1 
ATOM   12810 O O    . ASN   B  1 54  ? 74.098 43.465  -57.102 1.00 39.24  ? 80   ASN   B O    1 
ATOM   12811 C CB   . ASN   B  1 54  ? 73.733 43.322  -60.113 1.00 40.90  ? 80   ASN   B CB   1 
ATOM   12812 C CG   . ASN   B  1 54  ? 73.272 44.709  -60.500 1.00 45.92  ? 80   ASN   B CG   1 
ATOM   12813 O OD1  . ASN   B  1 54  ? 72.318 45.267  -59.945 1.00 47.74  ? 80   ASN   B OD1  1 
ATOM   12814 N ND2  . ASN   B  1 54  ? 73.947 45.298  -61.487 1.00 47.29  ? 80   ASN   B ND2  1 
ATOM   12815 H H    . ASN   B  1 54  ? 71.246 42.865  -60.275 0.00 52.83  ? 80   ASN   B H    1 
ATOM   12816 H HA   . ASN   B  1 54  ? 73.398 41.634  -58.879 0.00 53.74  ? 80   ASN   B HA   1 
ATOM   12817 H HB2  . ASN   B  1 54  ? 74.762 43.409  -59.767 0.00 57.80  ? 80   ASN   B HB2  1 
ATOM   12818 H HB3  . ASN   B  1 54  ? 73.706 42.712  -61.015 0.00 57.29  ? 80   ASN   B HB3  1 
ATOM   12819 H HD21 . ASN   B  1 54  ? 73.687 46.230  -61.794 0.00 67.15  ? 80   ASN   B HD21 1 
ATOM   12820 H HD22 . ASN   B  1 54  ? 74.719 44.813  -61.934 0.00 66.47  ? 80   ASN   B HD22 1 
ATOM   12821 N N    . GLU   B  1 55  ? 71.862 43.804  -57.096 1.00 38.20  ? 81   GLU   B N    1 
ATOM   12822 C CA   . GLU   B  1 55  ? 71.790 44.434  -55.775 1.00 38.11  ? 81   GLU   B CA   1 
ATOM   12823 C C    . GLU   B  1 55  ? 71.306 43.456  -54.675 1.00 37.23  ? 81   GLU   B C    1 
ATOM   12824 O O    . GLU   B  1 55  ? 71.335 43.823  -53.504 1.00 37.09  ? 81   GLU   B O    1 
ATOM   12825 C CB   . GLU   B  1 55  ? 70.834 45.633  -55.824 1.00 40.95  ? 81   GLU   B CB   1 
ATOM   12826 C CG   . GLU   B  1 55  ? 71.302 46.739  -56.752 1.00 47.84  ? 81   GLU   B CG   1 
ATOM   12827 C CD   . GLU   B  1 55  ? 70.461 47.997  -56.672 1.00 57.58  ? 81   GLU   B CD   1 
ATOM   12828 O OE1  . GLU   B  1 55  ? 70.974 49.076  -57.050 1.00 59.84  ? 81   GLU   B OE1  1 
ATOM   12829 O OE2  . GLU   B  1 55  ? 69.295 47.909  -56.218 1.00 60.39  ? 81   GLU   B OE2  1 
ATOM   12830 H H    . GLU   B  1 55  ? 70.953 43.760  -57.545 0.00 54.04  ? 81   GLU   B H    1 
ATOM   12831 H HA   . GLU   B  1 55  ? 72.768 44.811  -55.480 0.00 54.81  ? 81   GLU   B HA   1 
ATOM   12832 H HB2  . GLU   B  1 55  ? 69.856 45.294  -56.164 0.00 58.14  ? 81   GLU   B HB2  1 
ATOM   12833 H HB3  . GLU   B  1 55  ? 70.750 46.059  -54.825 0.00 58.74  ? 81   GLU   B HB3  1 
ATOM   12834 H HG2  . GLU   B  1 55  ? 72.325 47.006  -56.491 0.00 67.80  ? 81   GLU   B HG2  1 
ATOM   12835 H HG3  . GLU   B  1 55  ? 71.265 46.379  -57.779 0.00 67.29  ? 81   GLU   B HG3  1 
ATOM   12836 N N    . SER   B  1 56  ? 70.845 42.239  -55.030 1.00 36.68  ? 82   SER   B N    1 
ATOM   12837 C CA   . SER   B  1 56  ? 70.339 41.273  -54.045 1.00 36.61  ? 82   SER   B CA   1 
ATOM   12838 C C    . SER   B  1 56  ? 71.393 40.820  -53.023 1.00 37.13  ? 82   SER   B C    1 
ATOM   12839 O O    . SER   B  1 56  ? 71.095 40.766  -51.833 1.00 36.91  ? 82   SER   B O    1 
ATOM   12840 C CB   . SER   B  1 56  ? 69.761 40.048  -54.748 1.00 36.90  ? 82   SER   B CB   1 
ATOM   12841 O OG   . SER   B  1 56  ? 68.640 40.382  -55.548 1.00 38.31  ? 82   SER   B OG   1 
ATOM   12842 H H    . SER   B  1 56  ? 70.806 41.885  -55.980 0.00 51.05  ? 82   SER   B H    1 
ATOM   12843 H HA   . SER   B  1 56  ? 69.533 41.751  -53.491 0.00 50.69  ? 82   SER   B HA   1 
ATOM   12844 H HB2  . SER   B  1 56  ? 70.527 39.607  -55.383 0.00 49.99  ? 82   SER   B HB2  1 
ATOM   12845 H HB3  . SER   B  1 56  ? 69.452 39.328  -53.992 0.00 49.68  ? 82   SER   B HB3  1 
ATOM   12846 H HG   . SER   B  1 56  ? 68.027 40.991  -55.057 0.00 52.06  ? 82   SER   B HG   1 
ATOM   12847 N N    . PHE   B  1 57  ? 72.603 40.484  -53.480 1.00 37.69  ? 83   PHE   B N    1 
ATOM   12848 C CA   . PHE   B  1 57  ? 73.685 40.029  -52.598 1.00 38.95  ? 83   PHE   B CA   1 
ATOM   12849 C C    . PHE   B  1 57  ? 74.820 41.065  -52.541 1.00 40.91  ? 83   PHE   B C    1 
ATOM   12850 O O    . PHE   B  1 57  ? 75.984 40.693  -52.390 1.00 41.40  ? 83   PHE   B O    1 
ATOM   12851 C CB   . PHE   B  1 57  ? 74.203 38.667  -53.086 1.00 38.32  ? 83   PHE   B CB   1 
ATOM   12852 C CG   . PHE   B  1 57  ? 73.106 37.628  -53.155 1.00 38.67  ? 83   PHE   B CG   1 
ATOM   12853 C CD1  . PHE   B  1 57  ? 72.599 37.058  -52.002 1.00 38.95  ? 83   PHE   B CD1  1 
ATOM   12854 C CD2  . PHE   B  1 57  ? 72.536 37.274  -54.368 1.00 39.23  ? 83   PHE   B CD2  1 
ATOM   12855 C CE1  . PHE   B  1 57  ? 71.560 36.138  -52.062 1.00 39.62  ? 83   PHE   B CE1  1 
ATOM   12856 C CE2  . PHE   B  1 57  ? 71.496 36.353  -54.424 1.00 39.65  ? 83   PHE   B CE2  1 
ATOM   12857 C CZ   . PHE   B  1 57  ? 71.016 35.791  -53.273 1.00 39.28  ? 83   PHE   B CZ   1 
ATOM   12858 H H    . PHE   B  1 57  ? 72.864 40.509  -54.460 0.00 51.81  ? 83   PHE   B H    1 
ATOM   12859 H HA   . PHE   B  1 57  ? 73.319 39.889  -51.583 0.00 53.14  ? 83   PHE   B HA   1 
ATOM   12860 H HB2  . PHE   B  1 57  ? 74.626 38.790  -54.082 0.00 52.00  ? 83   PHE   B HB2  1 
ATOM   12861 H HB3  . PHE   B  1 57  ? 74.960 38.295  -52.397 0.00 51.86  ? 83   PHE   B HB3  1 
ATOM   12862 H HD1  . PHE   B  1 57  ? 73.014 37.330  -51.046 0.00 51.75  ? 83   PHE   B HD1  1 
ATOM   12863 H HD2  . PHE   B  1 57  ? 72.900 37.718  -55.279 0.00 52.21  ? 83   PHE   B HD2  1 
ATOM   12864 H HE1  . PHE   B  1 57  ? 71.185 35.691  -51.157 0.00 51.38  ? 83   PHE   B HE1  1 
ATOM   12865 H HE2  . PHE   B  1 57  ? 71.072 36.076  -55.374 0.00 51.58  ? 83   PHE   B HE2  1 
ATOM   12866 H HZ   . PHE   B  1 57  ? 70.219 35.070  -53.312 0.00 50.50  ? 83   PHE   B HZ   1 
ATOM   12867 N N    . GLN   B  1 58  ? 74.475 42.363  -52.617 1.00 41.87  ? 84   GLN   B N    1 
ATOM   12868 C CA   . GLN   B  1 58  ? 75.454 43.452  -52.608 1.00 43.24  ? 84   GLN   B CA   1 
ATOM   12869 C C    . GLN   B  1 58  ? 76.171 43.501  -51.251 1.00 43.81  ? 84   GLN   B C    1 
ATOM   12870 O O    . GLN   B  1 58  ? 75.520 43.419  -50.210 1.00 44.16  ? 84   GLN   B O    1 
ATOM   12871 C CB   . GLN   B  1 58  ? 74.755 44.816  -52.869 1.00 45.86  ? 84   GLN   B CB   1 
ATOM   12872 C CG   . GLN   B  1 58  ? 75.403 45.700  -53.947 1.00 50.65  ? 84   GLN   B CG   1 
ATOM   12873 C CD   . GLN   B  1 58  ? 74.844 47.110  -53.976 1.00 56.40  ? 84   GLN   B CD   1 
ATOM   12874 O OE1  . GLN   B  1 58  ? 75.595 48.095  -53.987 1.00 58.05  ? 84   GLN   B OE1  1 
ATOM   12875 N NE2  . GLN   B  1 58  ? 73.519 47.253  -54.002 1.00 57.23  ? 84   GLN   B NE2  1 
ATOM   12876 H H    . GLN   B  1 58  ? 73.511 42.679  -52.640 0.00 58.23  ? 84   GLN   B H    1 
ATOM   12877 H HA   . GLN   B  1 58  ? 76.192 43.245  -53.382 0.00 60.77  ? 84   GLN   B HA   1 
ATOM   12878 H HB2  . GLN   B  1 58  ? 73.727 44.648  -53.186 0.00 64.22  ? 84   GLN   B HB2  1 
ATOM   12879 H HB3  . GLN   B  1 58  ? 74.757 45.384  -51.940 0.00 64.92  ? 84   GLN   B HB3  1 
ATOM   12880 H HG2  . GLN   B  1 58  ? 76.472 45.768  -53.748 0.00 71.31  ? 84   GLN   B HG2  1 
ATOM   12881 H HG3  . GLN   B  1 58  ? 75.234 45.251  -54.924 0.00 70.71  ? 84   GLN   B HG3  1 
ATOM   12882 H HE21 . GLN   B  1 58  ? 72.904 46.446  -54.032 0.00 78.88  ? 84   GLN   B HE21 1 
ATOM   12883 H HE22 . GLN   B  1 58  ? 73.118 48.185  -54.024 0.00 80.08  ? 84   GLN   B HE22 1 
ATOM   12884 N N    . GLY   B  1 59  ? 77.495 43.605  -51.280 1.00 43.61  ? 85   GLY   B N    1 
ATOM   12885 C CA   . GLY   B  1 59  ? 78.308 43.661  -50.070 1.00 43.89  ? 85   GLY   B CA   1 
ATOM   12886 C C    . GLY   B  1 59  ? 78.432 42.358  -49.297 1.00 43.76  ? 85   GLY   B C    1 
ATOM   12887 O O    . GLY   B  1 59  ? 78.832 42.387  -48.128 1.00 44.21  ? 85   GLY   B O    1 
ATOM   12888 H H    . GLY   B  1 59  ? 78.047 43.657  -52.131 0.00 61.99  ? 85   GLY   B H    1 
ATOM   12889 H HA2  . GLY   B  1 59  ? 79.314 43.980  -50.341 0.00 63.02  ? 85   GLY   B HA2  1 
ATOM   12890 H HA3  . GLY   B  1 59  ? 77.891 44.411  -49.400 0.00 62.96  ? 85   GLY   B HA3  1 
ATOM   12891 N N    . LEU   B  1 60  ? 78.095 41.205  -49.923 1.00 42.72  ? 86   LEU   B N    1 
ATOM   12892 C CA   . LEU   B  1 60  ? 78.191 39.895  -49.273 1.00 42.37  ? 86   LEU   B CA   1 
ATOM   12893 C C    . LEU   B  1 60  ? 79.261 39.065  -50.009 1.00 41.95  ? 86   LEU   B C    1 
ATOM   12894 O O    . LEU   B  1 60  ? 78.999 37.949  -50.447 1.00 41.64  ? 86   LEU   B O    1 
ATOM   12895 C CB   . LEU   B  1 60  ? 76.826 39.164  -49.292 1.00 42.52  ? 86   LEU   B CB   1 
ATOM   12896 C CG   . LEU   B  1 60  ? 75.634 39.855  -48.630 1.00 44.06  ? 86   LEU   B CG   1 
ATOM   12897 C CD1  . LEU   B  1 60  ? 74.389 39.006  -48.758 1.00 44.32  ? 86   LEU   B CD1  1 
ATOM   12898 C CD2  . LEU   B  1 60  ? 75.894 40.115  -47.148 1.00 45.10  ? 86   LEU   B CD2  1 
ATOM   12899 H H    . LEU   B  1 60  ? 77.760 41.141  -50.879 0.00 59.48  ? 86   LEU   B H    1 
ATOM   12900 H HA   . LEU   B  1 60  ? 78.508 39.990  -48.236 0.00 58.86  ? 86   LEU   B HA   1 
ATOM   12901 H HB2  . LEU   B  1 60  ? 76.552 38.963  -50.327 0.00 57.77  ? 86   LEU   B HB2  1 
ATOM   12902 H HB3  . LEU   B  1 60  ? 76.947 38.225  -48.755 0.00 57.60  ? 86   LEU   B HB3  1 
ATOM   12903 H HG   . LEU   B  1 60  ? 75.450 40.810  -49.121 0.00 60.45  ? 86   LEU   B HG   1 
ATOM   12904 H HD11 . LEU   B  1 60  ? 73.532 39.581  -48.411 0.00 59.68  ? 86   LEU   B HD11 1 
ATOM   12905 H HD12 . LEU   B  1 60  ? 74.253 38.722  -49.800 0.00 59.27  ? 86   LEU   B HD12 1 
ATOM   12906 H HD13 . LEU   B  1 60  ? 74.508 38.114  -48.144 0.00 59.14  ? 86   LEU   B HD13 1 
ATOM   12907 H HD21 . LEU   B  1 60  ? 74.981 40.494  -46.692 0.00 61.63  ? 86   LEU   B HD21 1 
ATOM   12908 H HD22 . LEU   B  1 60  ? 76.191 39.183  -46.670 0.00 61.22  ? 86   LEU   B HD22 1 
ATOM   12909 H HD23 . LEU   B  1 60  ? 76.687 40.855  -47.048 0.00 62.23  ? 86   LEU   B HD23 1 
ATOM   12910 N N    . GLN   B  1 61  ? 80.477 39.614  -50.117 1.00 41.59  ? 87   GLN   B N    1 
ATOM   12911 C CA   . GLN   B  1 61  ? 81.591 38.965  -50.818 1.00 41.79  ? 87   GLN   B CA   1 
ATOM   12912 C C    . GLN   B  1 61  ? 82.098 37.668  -50.190 1.00 40.94  ? 87   GLN   B C    1 
ATOM   12913 O O    . GLN   B  1 61  ? 82.716 36.876  -50.898 1.00 41.51  ? 87   GLN   B O    1 
ATOM   12914 C CB   . GLN   B  1 61  ? 82.768 39.949  -50.984 1.00 44.46  ? 87   GLN   B CB   1 
ATOM   12915 C CG   . GLN   B  1 61  ? 82.456 41.156  -51.866 1.00 49.43  ? 87   GLN   B CG   1 
ATOM   12916 C CD   . GLN   B  1 61  ? 82.036 40.736  -53.257 1.00 55.15  ? 87   GLN   B CD   1 
ATOM   12917 O OE1  . GLN   B  1 61  ? 82.661 39.864  -53.877 1.00 57.16  ? 87   GLN   B OE1  1 
ATOM   12918 N NE2  . GLN   B  1 61  ? 80.953 41.315  -53.774 1.00 56.28  ? 87   GLN   B NE2  1 
ATOM   12919 H H    . GLN   B  1 61  ? 80.720 40.513  -49.715 0.00 58.73  ? 87   GLN   B H    1 
ATOM   12920 H HA   . GLN   B  1 61  ? 81.236 38.685  -51.808 0.00 57.97  ? 87   GLN   B HA   1 
ATOM   12921 H HB2  . GLN   B  1 61  ? 83.052 40.323  -50.001 0.00 62.80  ? 87   GLN   B HB2  1 
ATOM   12922 H HB3  . GLN   B  1 61  ? 83.610 39.418  -51.425 0.00 62.38  ? 87   GLN   B HB3  1 
ATOM   12923 H HG2  . GLN   B  1 61  ? 81.654 41.730  -51.405 0.00 68.96  ? 87   GLN   B HG2  1 
ATOM   12924 H HG3  . GLN   B  1 61  ? 83.350 41.770  -51.956 0.00 69.50  ? 87   GLN   B HG3  1 
ATOM   12925 H HE21 . GLN   B  1 61  ? 80.437 42.014  -53.250 0.00 76.86  ? 87   GLN   B HE21 1 
ATOM   12926 H HE22 . GLN   B  1 61  ? 80.643 41.058  -54.705 0.00 76.31  ? 87   GLN   B HE22 1 
ATOM   12927 N N    . ASN   B  1 62  ? 81.864 37.442  -48.894 1.00 39.78  ? 88   ASN   B N    1 
ATOM   12928 C CA   . ASN   B  1 62  ? 82.293 36.197  -48.247 1.00 39.32  ? 88   ASN   B CA   1 
ATOM   12929 C C    . ASN   B  1 62  ? 81.425 34.980  -48.645 1.00 36.20  ? 88   ASN   B C    1 
ATOM   12930 O O    . ASN   B  1 62  ? 81.796 33.858  -48.303 1.00 35.72  ? 88   ASN   B O    1 
ATOM   12931 C CB   . ASN   B  1 62  ? 82.312 36.355  -46.708 1.00 42.93  ? 88   ASN   B CB   1 
ATOM   12932 C CG   . ASN   B  1 62  ? 83.496 37.060  -46.203 1.00 50.46  ? 88   ASN   B CG   1 
ATOM   12933 O OD1  . ASN   B  1 62  ? 84.579 36.465  -46.227 1.00 52.16  ? 88   ASN   B OD1  1 
ATOM   12934 N ND2  . ASN   B  1 62  ? 83.410 38.222  -45.567 1.00 54.32  ? 88   ASN   B ND2  1 
ATOM   12935 H H    . ASN   B  1 62  ? 81.396 38.092  -48.271 0.00 55.64  ? 88   ASN   B H    1 
ATOM   12936 H HA   . ASN   B  1 62  ? 83.306 35.965  -48.575 0.00 54.65  ? 88   ASN   B HA   1 
ATOM   12937 H HB2  . ASN   B  1 62  ? 81.426 36.897  -46.382 0.00 59.05  ? 88   ASN   B HB2  1 
ATOM   12938 H HB3  . ASN   B  1 62  ? 82.315 35.367  -46.250 0.00 58.61  ? 88   ASN   B HB3  1 
ATOM   12939 H HD21 . ASN   B  1 62  ? 84.150 38.644  -46.094 0.00 74.62  ? 88   ASN   B HD21 1 
ATOM   12940 H HD22 . ASN   B  1 62  ? 82.541 38.658  -45.279 0.00 74.17  ? 88   ASN   B HD22 1 
ATOM   12941 N N    . LEU   B  1 63  ? 80.296 35.178  -49.361 1.00 33.82  ? 89   LEU   B N    1 
ATOM   12942 C CA   . LEU   B  1 63  ? 79.443 34.052  -49.734 1.00 32.34  ? 89   LEU   B CA   1 
ATOM   12943 C C    . LEU   B  1 63  ? 80.123 33.083  -50.689 1.00 30.84  ? 89   LEU   B C    1 
ATOM   12944 O O    . LEU   B  1 63  ? 80.511 33.470  -51.792 1.00 30.67  ? 89   LEU   B O    1 
ATOM   12945 C CB   . LEU   B  1 63  ? 78.124 34.511  -50.380 1.00 32.37  ? 89   LEU   B CB   1 
ATOM   12946 C CG   . LEU   B  1 63  ? 77.122 35.234  -49.492 1.00 33.65  ? 89   LEU   B CG   1 
ATOM   12947 C CD1  . LEU   B  1 63  ? 75.931 35.721  -50.313 1.00 33.94  ? 89   LEU   B CD1  1 
ATOM   12948 C CD2  . LEU   B  1 63  ? 76.620 34.350  -48.361 1.00 33.63  ? 89   LEU   B CD2  1 
ATOM   12949 H H    . LEU   B  1 63  ? 79.949 36.076  -49.684 0.00 46.87  ? 89   LEU   B H    1 
ATOM   12950 H HA   . LEU   B  1 63  ? 79.204 33.508  -48.823 0.00 43.75  ? 89   LEU   B HA   1 
ATOM   12951 H HB2  . LEU   B  1 63  ? 78.365 35.180  -51.204 0.00 44.14  ? 89   LEU   B HB2  1 
ATOM   12952 H HB3  . LEU   B  1 63  ? 77.620 33.629  -50.773 0.00 43.25  ? 89   LEU   B HB3  1 
ATOM   12953 H HG   . LEU   B  1 63  ? 77.624 36.090  -49.044 0.00 46.05  ? 89   LEU   B HG   1 
ATOM   12954 H HD11 . LEU   B  1 63  ? 75.279 36.317  -49.677 0.00 45.85  ? 89   LEU   B HD11 1 
ATOM   12955 H HD12 . LEU   B  1 63  ? 76.292 36.324  -51.144 0.00 46.01  ? 89   LEU   B HD12 1 
ATOM   12956 H HD13 . LEU   B  1 63  ? 75.388 34.854  -50.689 0.00 45.11  ? 89   LEU   B HD13 1 
ATOM   12957 H HD21 . LEU   B  1 63  ? 75.776 34.849  -47.887 0.00 45.03  ? 89   LEU   B HD21 1 
ATOM   12958 H HD22 . LEU   B  1 63  ? 76.316 33.385  -48.763 0.00 44.43  ? 89   LEU   B HD22 1 
ATOM   12959 H HD23 . LEU   B  1 63  ? 77.414 34.223  -47.627 0.00 45.21  ? 89   LEU   B HD23 1 
ATOM   12960 N N    . THR   B  1 64  ? 80.244 31.820  -50.263 1.00 29.63  ? 90   THR   B N    1 
ATOM   12961 C CA   . THR   B  1 64  ? 80.758 30.706  -51.056 1.00 29.58  ? 90   THR   B CA   1 
ATOM   12962 C C    . THR   B  1 64  ? 79.611 29.783  -51.510 1.00 28.80  ? 90   THR   B C    1 
ATOM   12963 O O    . THR   B  1 64  ? 79.832 28.963  -52.402 1.00 28.57  ? 90   THR   B O    1 
ATOM   12964 C CB   . THR   B  1 64  ? 81.808 29.911  -50.270 1.00 31.48  ? 90   THR   B CB   1 
ATOM   12965 O OG1  . THR   B  1 64  ? 81.176 29.203  -49.207 1.00 33.00  ? 90   THR   B OG1  1 
ATOM   12966 C CG2  . THR   B  1 64  ? 82.917 30.793  -49.720 1.00 32.15  ? 90   THR   B CG2  1 
ATOM   12967 H H    . THR   B  1 64  ? 79.987 31.521  -49.327 0.00 39.86  ? 90   THR   B H    1 
ATOM   12968 H HA   . THR   B  1 64  ? 81.275 31.081  -51.937 0.00 39.86  ? 90   THR   B HA   1 
ATOM   12969 H HB   . THR   B  1 64  ? 82.269 29.189  -50.944 0.00 41.80  ? 90   THR   B HB   1 
ATOM   12970 H HG1  . THR   B  1 64  ? 80.834 29.835  -48.522 0.00 43.58  ? 90   THR   B HG1  1 
ATOM   12971 H HG21 . THR   B  1 64  ? 83.706 30.172  -49.297 0.00 43.61  ? 90   THR   B HG21 1 
ATOM   12972 H HG22 . THR   B  1 64  ? 83.337 31.404  -50.517 0.00 43.86  ? 90   THR   B HG22 1 
ATOM   12973 H HG23 . THR   B  1 64  ? 82.532 31.446  -48.938 0.00 43.73  ? 90   THR   B HG23 1 
ATOM   12974 N N    . LYS   B  1 65  ? 78.413 29.864  -50.884 1.00 27.61  ? 91   LYS   B N    1 
ATOM   12975 C CA   . LYS   B  1 65  ? 77.296 28.997  -51.226 1.00 27.36  ? 91   LYS   B CA   1 
ATOM   12976 C C    . LYS   B  1 65  ? 75.989 29.746  -51.059 1.00 26.09  ? 91   LYS   B C    1 
ATOM   12977 O O    . LYS   B  1 65  ? 75.789 30.418  -50.050 1.00 26.03  ? 91   LYS   B O    1 
ATOM   12978 C CB   . LYS   B  1 65  ? 77.305 27.750  -50.318 1.00 29.06  ? 91   LYS   B CB   1 
ATOM   12979 C CG   . LYS   B  1 65  ? 76.083 26.833  -50.454 1.00 33.91  ? 91   LYS   B CG   1 
ATOM   12980 C CD   . LYS   B  1 65  ? 76.273 25.539  -49.685 1.00 38.97  ? 91   LYS   B CD   1 
ATOM   12981 C CE   . LYS   B  1 65  ? 75.047 24.662  -49.733 1.00 43.30  ? 91   LYS   B CE   1 
ATOM   12982 N NZ   . LYS   B  1 65  ? 75.122 23.563  -48.733 1.00 46.34  ? 91   LYS   B NZ   1 
ATOM   12983 H H    . LYS   B  1 65  ? 78.188 30.509  -50.134 0.00 36.42  ? 91   LYS   B H    1 
ATOM   12984 H HA   . LYS   B  1 65  ? 77.375 28.667  -52.261 0.00 35.11  ? 91   LYS   B HA   1 
ATOM   12985 H HB2  . LYS   B  1 65  ? 78.189 27.157  -50.548 0.00 36.92  ? 91   LYS   B HB2  1 
ATOM   12986 H HB3  . LYS   B  1 65  ? 77.343 28.083  -49.282 0.00 37.07  ? 91   LYS   B HB3  1 
ATOM   12987 H HG2  . LYS   B  1 65  ? 75.208 27.327  -50.032 0.00 42.02  ? 91   LYS   B HG2  1 
ATOM   12988 H HG3  . LYS   B  1 65  ? 75.908 26.596  -51.502 0.00 41.90  ? 91   LYS   B HG3  1 
ATOM   12989 H HD2  . LYS   B  1 65  ? 77.104 24.985  -50.119 0.00 47.83  ? 91   LYS   B HD2  1 
ATOM   12990 H HD3  . LYS   B  1 65  ? 76.482 25.772  -48.642 0.00 47.99  ? 91   LYS   B HD3  1 
ATOM   12991 H HE2  . LYS   B  1 65  ? 74.165 25.261  -49.516 0.00 52.37  ? 91   LYS   B HE2  1 
ATOM   12992 H HE3  . LYS   B  1 65  ? 74.966 24.214  -50.722 0.00 52.20  ? 91   LYS   B HE3  1 
ATOM   12993 H HZ1  . LYS   B  1 65  ? 74.289 22.985  -48.790 0.00 55.41  ? 91   LYS   B HZ1  1 
ATOM   12994 H HZ2  . LYS   B  1 65  ? 75.937 22.985  -48.909 0.00 55.84  ? 91   LYS   B HZ2  1 
ATOM   12995 H HZ3  . LYS   B  1 65  ? 75.187 23.950  -47.797 0.00 55.98  ? 91   LYS   B HZ3  1 
ATOM   12996 N N    . ILE   B  1 66  ? 75.091 29.612  -52.038 1.00 24.61  ? 92   ILE   B N    1 
ATOM   12997 C CA   . ILE   B  1 66  ? 73.756 30.187  -51.968 1.00 24.23  ? 92   ILE   B CA   1 
ATOM   12998 C C    . ILE   B  1 66  ? 72.794 29.088  -52.353 1.00 23.97  ? 92   ILE   B C    1 
ATOM   12999 O O    . ILE   B  1 66  ? 72.962 28.459  -53.401 1.00 24.03  ? 92   ILE   B O    1 
ATOM   13000 C CB   . ILE   B  1 66  ? 73.548 31.435  -52.878 1.00 24.23  ? 92   ILE   B CB   1 
ATOM   13001 C CG1  . ILE   B  1 66  ? 74.354 32.633  -52.361 1.00 24.70  ? 92   ILE   B CG1  1 
ATOM   13002 C CG2  . ILE   B  1 66  ? 72.040 31.787  -52.968 1.00 24.86  ? 92   ILE   B CG2  1 
ATOM   13003 C CD1  . ILE   B  1 66  ? 74.594 33.724  -53.386 1.00 26.01  ? 92   ILE   B CD1  1 
ATOM   13004 H H    . ILE   B  1 66  ? 75.257 29.105  -52.902 0.00 31.41  ? 92   ILE   B H    1 
ATOM   13005 H HA   . ILE   B  1 66  ? 73.529 30.490  -50.947 0.00 31.13  ? 92   ILE   B HA   1 
ATOM   13006 H HB   . ILE   B  1 66  ? 73.901 31.185  -53.878 0.00 31.44  ? 92   ILE   B HB   1 
ATOM   13007 H HG12 . ILE   B  1 66  ? 73.814 33.080  -51.527 0.00 32.81  ? 92   ILE   B HG12 1 
ATOM   13008 H HG13 . ILE   B  1 66  ? 75.328 32.286  -52.020 0.00 32.81  ? 92   ILE   B HG13 1 
ATOM   13009 H HG21 . ILE   B  1 66  ? 71.916 32.810  -53.318 0.00 32.48  ? 92   ILE   B HG21 1 
ATOM   13010 H HG22 . ILE   B  1 66  ? 71.549 31.120  -53.676 0.00 31.71  ? 92   ILE   B HG22 1 
ATOM   13011 H HG23 . ILE   B  1 66  ? 71.588 31.682  -51.983 0.00 31.95  ? 92   ILE   B HG23 1 
ATOM   13012 H HD11 . ILE   B  1 66  ? 75.326 34.419  -52.978 0.00 35.28  ? 92   ILE   B HD11 1 
ATOM   13013 H HD12 . ILE   B  1 66  ? 74.976 33.275  -54.302 0.00 34.68  ? 92   ILE   B HD12 1 
ATOM   13014 H HD13 . ILE   B  1 66  ? 73.668 34.259  -53.590 0.00 34.85  ? 92   ILE   B HD13 1 
ATOM   13015 N N    . ASN   B  1 67  ? 71.750 28.904  -51.544 1.00 23.47  ? 93   ASN   B N    1 
ATOM   13016 C CA   . ASN   B  1 67  ? 70.707 27.948  -51.856 1.00 23.67  ? 93   ASN   B CA   1 
ATOM   13017 C C    . ASN   B  1 67  ? 69.405 28.745  -52.028 1.00 24.67  ? 93   ASN   B C    1 
ATOM   13018 O O    . ASN   B  1 67  ? 68.882 29.309  -51.076 1.00 25.35  ? 93   ASN   B O    1 
ATOM   13019 C CB   . ASN   B  1 67  ? 70.624 26.856  -50.774 1.00 23.98  ? 93   ASN   B CB   1 
ATOM   13020 C CG   . ASN   B  1 67  ? 69.475 25.903  -50.944 1.00 25.66  ? 93   ASN   B CG   1 
ATOM   13021 O OD1  . ASN   B  1 67  ? 68.597 26.096  -51.779 1.00 25.86  ? 93   ASN   B OD1  1 
ATOM   13022 N ND2  . ASN   B  1 67  ? 69.459 24.844  -50.149 1.00 26.41  ? 93   ASN   B ND2  1 
ATOM   13023 H H    . ASN   B  1 67  ? 71.595 29.401  -50.672 0.00 29.41  ? 93   ASN   B H    1 
ATOM   13024 H HA   . ASN   B  1 67  ? 70.922 27.449  -52.798 0.00 28.78  ? 93   ASN   B HA   1 
ATOM   13025 H HB2  . ASN   B  1 67  ? 71.539 26.267  -50.817 0.00 28.90  ? 93   ASN   B HB2  1 
ATOM   13026 H HB3  . ASN   B  1 67  ? 70.531 27.300  -49.788 0.00 29.07  ? 93   ASN   B HB3  1 
ATOM   13027 H HD21 . ASN   B  1 67  ? 68.706 24.167  -50.220 0.00 30.65  ? 93   ASN   B HD21 1 
ATOM   13028 H HD22 . ASN   B  1 67  ? 70.198 24.712  -49.465 0.00 31.09  ? 93   ASN   B HD22 1 
ATOM   13029 N N    . LEU   B  1 68  ? 68.917 28.831  -53.261 1.00 24.87  ? 94   LEU   B N    1 
ATOM   13030 C CA   . LEU   B  1 68  ? 67.673 29.532  -53.586 1.00 25.03  ? 94   LEU   B CA   1 
ATOM   13031 C C    . LEU   B  1 68  ? 66.602 28.552  -54.098 1.00 24.87  ? 94   LEU   B C    1 
ATOM   13032 O O    . LEU   B  1 68  ? 65.654 28.978  -54.739 1.00 24.92  ? 94   LEU   B O    1 
ATOM   13033 C CB   . LEU   B  1 68  ? 67.974 30.641  -54.625 1.00 25.84  ? 94   LEU   B CB   1 
ATOM   13034 C CG   . LEU   B  1 68  ? 68.432 31.999  -54.077 1.00 27.24  ? 94   LEU   B CG   1 
ATOM   13035 C CD1  . LEU   B  1 68  ? 69.186 32.773  -55.139 1.00 27.98  ? 94   LEU   B CD1  1 
ATOM   13036 C CD2  . LEU   B  1 68  ? 67.242 32.808  -53.541 1.00 27.90  ? 94   LEU   B CD2  1 
ATOM   13037 H H    . LEU   B  1 68  ? 69.356 28.411  -54.074 0.00 30.32  ? 94   LEU   B H    1 
ATOM   13038 H HA   . LEU   B  1 68  ? 67.254 29.990  -52.690 0.00 30.79  ? 94   LEU   B HA   1 
ATOM   13039 H HB2  . LEU   B  1 68  ? 68.784 30.290  -55.261 0.00 32.16  ? 94   LEU   B HB2  1 
ATOM   13040 H HB3  . LEU   B  1 68  ? 67.095 30.835  -55.237 0.00 32.15  ? 94   LEU   B HB3  1 
ATOM   13041 H HG   . LEU   B  1 68  ? 69.119 31.836  -53.249 0.00 34.45  ? 94   LEU   B HG   1 
ATOM   13042 H HD11 . LEU   B  1 68  ? 69.342 33.796  -54.799 0.00 36.24  ? 94   LEU   B HD11 1 
ATOM   13043 H HD12 . LEU   B  1 68  ? 70.146 32.290  -55.312 0.00 35.73  ? 94   LEU   B HD12 1 
ATOM   13044 H HD13 . LEU   B  1 68  ? 68.601 32.775  -56.058 0.00 35.73  ? 94   LEU   B HD13 1 
ATOM   13045 H HD21 . LEU   B  1 68  ? 67.604 33.767  -53.172 0.00 35.87  ? 94   LEU   B HD21 1 
ATOM   13046 H HD22 . LEU   B  1 68  ? 66.527 32.969  -54.346 0.00 35.42  ? 94   LEU   B HD22 1 
ATOM   13047 H HD23 . LEU   B  1 68  ? 66.769 32.260  -52.728 0.00 35.10  ? 94   LEU   B HD23 1 
ATOM   13048 N N    . ASN   B  1 69  ? 66.685 27.260  -53.726 1.00 24.61  ? 95   ASN   B N    1 
ATOM   13049 C CA   . ASN   B  1 69  ? 65.712 26.252  -54.142 1.00 25.16  ? 95   ASN   B CA   1 
ATOM   13050 C C    . ASN   B  1 69  ? 64.294 26.576  -53.735 1.00 26.46  ? 95   ASN   B C    1 
ATOM   13051 O O    . ASN   B  1 69  ? 64.069 27.127  -52.660 1.00 25.65  ? 95   ASN   B O    1 
ATOM   13052 C CB   . ASN   B  1 69  ? 66.072 24.877  -53.533 1.00 25.10  ? 95   ASN   B CB   1 
ATOM   13053 C CG   . ASN   B  1 69  ? 67.356 24.235  -54.011 1.00 26.61  ? 95   ASN   B CG   1 
ATOM   13054 O OD1  . ASN   B  1 69  ? 67.841 23.259  -53.418 1.00 28.45  ? 95   ASN   B OD1  1 
ATOM   13055 N ND2  . ASN   B  1 69  ? 68.015 24.825  -54.976 1.00 24.36  ? 95   ASN   B ND2  1 
ATOM   13056 H H    . ASN   B  1 69  ? 67.400 26.890  -53.107 0.00 29.18  ? 95   ASN   B H    1 
ATOM   13057 H HA   . ASN   B  1 69  ? 65.719 26.171  -55.228 0.00 29.50  ? 95   ASN   B HA   1 
ATOM   13058 H HB2  . ASN   B  1 69  ? 66.149 24.992  -52.453 0.00 28.98  ? 95   ASN   B HB2  1 
ATOM   13059 H HB3  . ASN   B  1 69  ? 65.264 24.184  -53.761 0.00 28.68  ? 95   ASN   B HB3  1 
ATOM   13060 H HD21 . ASN   B  1 69  ? 68.868 24.403  -55.321 0.00 28.39  ? 95   ASN   B HD21 1 
ATOM   13061 H HD22 . ASN   B  1 69  ? 67.787 25.768  -55.274 0.00 28.65  ? 95   ASN   B HD22 1 
ATOM   13062 N N    . HIS   B  1 70  ? 63.330 26.154  -54.561 1.00 28.03  ? 96   HIS   B N    1 
ATOM   13063 C CA   . HIS   B  1 70  ? 61.906 26.271  -54.247 1.00 30.33  ? 96   HIS   B CA   1 
ATOM   13064 C C    . HIS   B  1 70  ? 61.503 27.734  -53.942 1.00 31.62  ? 96   HIS   B C    1 
ATOM   13065 O O    . HIS   B  1 70  ? 61.014 28.048  -52.860 1.00 31.32  ? 96   HIS   B O    1 
ATOM   13066 C CB   . HIS   B  1 70  ? 61.537 25.329  -53.075 1.00 32.39  ? 96   HIS   B CB   1 
ATOM   13067 C CG   . HIS   B  1 70  ? 62.290 24.024  -53.022 1.00 36.86  ? 96   HIS   B CG   1 
ATOM   13068 N ND1  . HIS   B  1 70  ? 62.062 23.009  -53.939 1.00 39.26  ? 96   HIS   B ND1  1 
ATOM   13069 C CD2  . HIS   B  1 70  ? 63.182 23.580  -52.105 1.00 38.95  ? 96   HIS   B CD2  1 
ATOM   13070 C CE1  . HIS   B  1 70  ? 62.880 22.020  -53.608 1.00 39.88  ? 96   HIS   B CE1  1 
ATOM   13071 N NE2  . HIS   B  1 70  ? 63.562 22.308  -52.501 1.00 40.19  ? 96   HIS   B NE2  1 
ATOM   13072 H H    . HIS   B  1 70  ? 63.500 25.720  -55.463 0.00 32.63  ? 96   HIS   B H    1 
ATOM   13073 H HA   . HIS   B  1 70  ? 61.334 25.948  -55.115 0.00 35.31  ? 96   HIS   B HA   1 
ATOM   13074 H HB2  . HIS   B  1 70  ? 61.742 25.830  -52.131 0.00 37.61  ? 96   HIS   B HB2  1 
ATOM   13075 H HB3  . HIS   B  1 70  ? 60.475 25.096  -53.141 0.00 37.36  ? 96   HIS   B HB3  1 
ATOM   13076 H HD1  . HIS   B  1 70  ? 61.385 23.010  -54.695 0.00 45.12  ? 96   HIS   B HD1  1 
ATOM   13077 H HD2  . HIS   B  1 70  ? 63.529 24.113  -51.236 0.00 45.03  ? 96   HIS   B HD2  1 
ATOM   13078 H HE1  . HIS   B  1 70  ? 62.981 21.101  -54.162 0.00 45.41  ? 96   HIS   B HE1  1 
ATOM   13079 N N    . ASN   B  1 71  ? 61.742 28.614  -54.904 1.00 32.81  ? 97   ASN   B N    1 
ATOM   13080 C CA   . ASN   B  1 71  ? 61.428 30.042  -54.836 1.00 34.78  ? 97   ASN   B CA   1 
ATOM   13081 C C    . ASN   B  1 71  ? 60.814 30.512  -56.170 1.00 38.05  ? 97   ASN   B C    1 
ATOM   13082 O O    . ASN   B  1 71  ? 61.487 30.373  -57.189 1.00 38.65  ? 97   ASN   B O    1 
ATOM   13083 C CB   . ASN   B  1 71  ? 62.721 30.838  -54.596 1.00 34.60  ? 97   ASN   B CB   1 
ATOM   13084 C CG   . ASN   B  1 71  ? 63.014 31.128  -53.153 1.00 35.44  ? 97   ASN   B CG   1 
ATOM   13085 O OD1  . ASN   B  1 71  ? 63.952 30.599  -52.539 1.00 35.97  ? 97   ASN   B OD1  1 
ATOM   13086 N ND2  . ASN   B  1 71  ? 62.162 31.941  -52.604 1.00 34.40  ? 97   ASN   B ND2  1 
ATOM   13087 H H    . ASN   B  1 71  ? 62.171 28.329  -55.776 0.00 39.19  ? 97   ASN   B H    1 
ATOM   13088 H HA   . ASN   B  1 71  ? 60.720 30.218  -54.029 0.00 42.10  ? 97   ASN   B HA   1 
ATOM   13089 H HB2  . ASN   B  1 71  ? 63.565 30.275  -54.991 0.00 42.09  ? 97   ASN   B HB2  1 
ATOM   13090 H HB3  . ASN   B  1 71  ? 62.645 31.794  -55.114 0.00 42.66  ? 97   ASN   B HB3  1 
ATOM   13091 H HD21 . ASN   B  1 71  ? 62.247 32.232  -51.640 0.00 42.49  ? 97   ASN   B HD21 1 
ATOM   13092 H HD22 . ASN   B  1 71  ? 61.386 32.273  -53.165 0.00 42.49  ? 97   ASN   B HD22 1 
ATOM   13093 N N    . PRO   B  1 72  ? 59.600 31.113  -56.222 1.00 40.25  ? 98   PRO   B N    1 
ATOM   13094 C CA   . PRO   B  1 72  ? 58.657 31.379  -55.119 1.00 42.38  ? 98   PRO   B CA   1 
ATOM   13095 C C    . PRO   B  1 72  ? 57.976 30.117  -54.583 1.00 45.09  ? 98   PRO   B C    1 
ATOM   13096 O O    . PRO   B  1 72  ? 58.121 29.038  -55.151 1.00 45.79  ? 98   PRO   B O    1 
ATOM   13097 C CB   . PRO   B  1 72  ? 57.645 32.368  -55.742 1.00 42.74  ? 98   PRO   B CB   1 
ATOM   13098 C CG   . PRO   B  1 72  ? 58.176 32.719  -57.118 1.00 42.52  ? 98   PRO   B CG   1 
ATOM   13099 C CD   . PRO   B  1 72  ? 59.037 31.566  -57.508 1.00 40.27  ? 98   PRO   B CD   1 
ATOM   13100 H HA   . PRO   B  1 72  ? 59.163 31.888  -54.300 0.00 51.89  ? 98   PRO   B HA   1 
ATOM   13101 H HB2  . PRO   B  1 72  ? 56.670 31.887  -55.820 0.00 52.47  ? 98   PRO   B HB2  1 
ATOM   13102 H HB3  . PRO   B  1 72  ? 57.581 33.259  -55.121 0.00 52.98  ? 98   PRO   B HB3  1 
ATOM   13103 H HG2  . PRO   B  1 72  ? 57.349 32.843  -57.815 0.00 52.81  ? 98   PRO   B HG2  1 
ATOM   13104 H HG3  . PRO   B  1 72  ? 58.774 33.626  -57.057 0.00 53.04  ? 98   PRO   B HG3  1 
ATOM   13105 H HD2  . PRO   B  1 72  ? 58.432 30.778  -57.955 0.00 49.23  ? 98   PRO   B HD2  1 
ATOM   13106 H HD3  . PRO   B  1 72  ? 59.812 31.910  -58.189 0.00 49.71  ? 98   PRO   B HD3  1 
ATOM   13107 N N    . ASN   B  1 73  ? 57.213 30.269  -53.489 1.00 46.78  ? 99   ASN   B N    1 
ATOM   13108 C CA   . ASN   B  1 73  ? 56.489 29.189  -52.810 1.00 48.80  ? 99   ASN   B CA   1 
ATOM   13109 C C    . ASN   B  1 73  ? 57.455 28.226  -52.111 1.00 49.78  ? 99   ASN   B C    1 
ATOM   13110 O O    . ASN   B  1 73  ? 57.758 28.409  -50.927 1.00 50.17  ? 99   ASN   B O    1 
ATOM   13111 C CB   . ASN   B  1 73  ? 55.563 28.436  -53.776 1.00 50.94  ? 99   ASN   B CB   1 
ATOM   13112 C CG   . ASN   B  1 73  ? 54.599 29.336  -54.517 1.00 56.06  ? 99   ASN   B CG   1 
ATOM   13113 O OD1  . ASN   B  1 73  ? 54.339 30.480  -54.119 1.00 58.00  ? 99   ASN   B OD1  1 
ATOM   13114 N ND2  . ASN   B  1 73  ? 54.039 28.841  -55.613 1.00 56.89  ? 99   ASN   B ND2  1 
ATOM   13115 H H    . ASN   B  1 73  ? 57.059 31.176  -53.061 0.00 56.81  ? 99   ASN   B H    1 
ATOM   13116 H HA   . ASN   B  1 73  ? 55.860 29.633  -52.040 0.00 58.57  ? 99   ASN   B HA   1 
ATOM   13117 H HB2  . ASN   B  1 73  ? 56.165 27.905  -54.512 0.00 60.65  ? 99   ASN   B HB2  1 
ATOM   13118 H HB3  . ASN   B  1 73  ? 54.972 27.724  -53.204 0.00 60.53  ? 99   ASN   B HB3  1 
ATOM   13119 H HD21 . ASN   B  1 73  ? 53.385 29.405  -56.146 0.00 68.69  ? 99   ASN   B HD21 1 
ATOM   13120 H HD22 . ASN   B  1 73  ? 54.262 27.899  -55.918 0.00 68.03  ? 99   ASN   B HD22 1 
ATOM   13121 N N    . GLY   B  1 87  ? 57.524 32.111  -61.512 1.00 42.45  ? 113  GLY   B N    1 
ATOM   13122 C CA   . GLY   B  1 87  ? 58.881 31.607  -61.343 1.00 42.43  ? 113  GLY   B CA   1 
ATOM   13123 C C    . GLY   B  1 87  ? 59.873 32.674  -60.926 1.00 41.92  ? 113  GLY   B C    1 
ATOM   13124 O O    . GLY   B  1 87  ? 59.572 33.868  -60.985 1.00 42.30  ? 113  GLY   B O    1 
ATOM   13125 H HA2  . GLY   B  1 87  ? 58.887 30.816  -60.595 0.00 52.17  ? 113  GLY   B HA2  1 
ATOM   13126 H HA3  . GLY   B  1 87  ? 59.218 31.186  -62.288 0.00 52.57  ? 113  GLY   B HA3  1 
ATOM   13127 N N    . LEU   B  1 88  ? 61.077 32.249  -60.523 1.00 40.92  ? 114  LEU   B N    1 
ATOM   13128 C CA   . LEU   B  1 88  ? 62.131 33.164  -60.097 1.00 40.56  ? 114  LEU   B CA   1 
ATOM   13129 C C    . LEU   B  1 88  ? 62.713 33.877  -61.319 1.00 40.65  ? 114  LEU   B C    1 
ATOM   13130 O O    . LEU   B  1 88  ? 63.121 33.220  -62.277 1.00 40.65  ? 114  LEU   B O    1 
ATOM   13131 C CB   . LEU   B  1 88  ? 63.242 32.378  -59.382 1.00 40.19  ? 114  LEU   B CB   1 
ATOM   13132 C CG   . LEU   B  1 88  ? 64.385 33.193  -58.759 1.00 40.93  ? 114  LEU   B CG   1 
ATOM   13133 C CD1  . LEU   B  1 88  ? 63.871 34.135  -57.672 1.00 41.17  ? 114  LEU   B CD1  1 
ATOM   13134 C CD2  . LEU   B  1 88  ? 65.449 32.266  -58.180 1.00 41.56  ? 114  LEU   B CD2  1 
ATOM   13135 H H    . LEU   B  1 88  ? 61.344 31.270  -60.480 0.00 50.52  ? 114  LEU   B H    1 
ATOM   13136 H HA   . LEU   B  1 88  ? 61.718 33.899  -59.409 0.00 51.07  ? 114  LEU   B HA   1 
ATOM   13137 H HB2  . LEU   B  1 88  ? 62.789 31.783  -58.590 0.00 49.66  ? 114  LEU   B HB2  1 
ATOM   13138 H HB3  . LEU   B  1 88  ? 63.692 31.711  -60.116 0.00 49.85  ? 114  LEU   B HB3  1 
ATOM   13139 H HG   . LEU   B  1 88  ? 64.866 33.801  -59.524 0.00 51.62  ? 114  LEU   B HG   1 
ATOM   13140 H HD11 . LEU   B  1 88  ? 64.641 34.257  -56.912 0.00 51.86  ? 114  LEU   B HD11 1 
ATOM   13141 H HD12 . LEU   B  1 88  ? 63.639 35.100  -58.121 0.00 52.27  ? 114  LEU   B HD12 1 
ATOM   13142 H HD13 . LEU   B  1 88  ? 62.975 33.708  -57.225 0.00 51.53  ? 114  LEU   B HD13 1 
ATOM   13143 H HD21 . LEU   B  1 88  ? 66.326 32.855  -57.917 0.00 51.91  ? 114  LEU   B HD21 1 
ATOM   13144 H HD22 . LEU   B  1 88  ? 65.049 31.783  -57.290 0.00 51.31  ? 114  LEU   B HD22 1 
ATOM   13145 H HD23 . LEU   B  1 88  ? 65.710 31.510  -58.919 0.00 51.39  ? 114  LEU   B HD23 1 
ATOM   13146 N N    . ASN   B  1 89  ? 62.763 35.208  -61.283 1.00 40.17  ? 115  ASN   B N    1 
ATOM   13147 C CA   . ASN   B  1 89  ? 63.306 35.983  -62.389 1.00 40.42  ? 115  ASN   B CA   1 
ATOM   13148 C C    . ASN   B  1 89  ? 64.687 36.506  -61.946 1.00 38.56  ? 115  ASN   B C    1 
ATOM   13149 O O    . ASN   B  1 89  ? 64.791 37.311  -61.023 1.00 38.16  ? 115  ASN   B O    1 
ATOM   13150 C CB   . ASN   B  1 89  ? 62.296 37.060  -62.855 1.00 44.16  ? 115  ASN   B CB   1 
ATOM   13151 C CG   . ASN   B  1 89  ? 62.845 38.297  -63.435 1.00 52.40  ? 115  ASN   B CG   1 
ATOM   13152 O OD1  . ASN   B  1 89  ? 64.007 38.322  -63.878 1.00 52.96  ? 115  ASN   B OD1  1 
ATOM   13153 N ND2  . ASN   B  1 89  ? 62.046 39.335  -63.645 1.00 58.63  ? 115  ASN   B ND2  1 
ATOM   13154 H H    . ASN   B  1 89  ? 62.450 35.773  -60.500 0.00 51.62  ? 115  ASN   B H    1 
ATOM   13155 H HA   . ASN   B  1 89  ? 63.459 35.340  -63.254 0.00 52.13  ? 115  ASN   B HA   1 
ATOM   13156 H HB2  . ASN   B  1 89  ? 61.649 36.611  -63.607 0.00 57.24  ? 115  ASN   B HB2  1 
ATOM   13157 H HB3  . ASN   B  1 89  ? 61.690 37.358  -62.001 0.00 57.37  ? 115  ASN   B HB3  1 
ATOM   13158 H HD21 . ASN   B  1 89  ? 62.745 39.869  -63.176 0.00 76.21  ? 115  ASN   B HD21 1 
ATOM   13159 H HD22 . ASN   B  1 89  ? 61.045 39.326  -63.485 0.00 75.96  ? 115  ASN   B HD22 1 
ATOM   13160 N N    . ILE   B  1 90  ? 65.743 35.982  -62.586 1.00 37.09  ? 116  ILE   B N    1 
ATOM   13161 C CA   . ILE   B  1 90  ? 67.126 36.331  -62.304 1.00 36.40  ? 116  ILE   B CA   1 
ATOM   13162 C C    . ILE   B  1 90  ? 67.640 37.156  -63.479 1.00 36.47  ? 116  ILE   B C    1 
ATOM   13163 O O    . ILE   B  1 90  ? 67.637 36.677  -64.611 1.00 36.70  ? 116  ILE   B O    1 
ATOM   13164 C CB   . ILE   B  1 90  ? 67.975 35.045  -62.123 1.00 35.91  ? 116  ILE   B CB   1 
ATOM   13165 C CG1  . ILE   B  1 90  ? 67.349 34.106  -61.051 1.00 36.15  ? 116  ILE   B CG1  1 
ATOM   13166 C CG2  . ILE   B  1 90  ? 69.433 35.413  -61.785 1.00 36.33  ? 116  ILE   B CG2  1 
ATOM   13167 C CD1  . ILE   B  1 90  ? 68.060 32.801  -60.850 1.00 36.73  ? 116  ILE   B CD1  1 
ATOM   13168 H H    . ILE   B  1 90  ? 65.667 35.289  -63.323 0.00 48.21  ? 116  ILE   B H    1 
ATOM   13169 H HA   . ILE   B  1 90  ? 67.207 36.915  -61.388 0.00 48.01  ? 116  ILE   B HA   1 
ATOM   13170 H HB   . ILE   B  1 90  ? 67.977 34.508  -63.070 0.00 46.58  ? 116  ILE   B HB   1 
ATOM   13171 H HG12 . ILE   B  1 90  ? 67.339 34.622  -60.093 0.00 46.50  ? 116  ILE   B HG12 1 
ATOM   13172 H HG13 . ILE   B  1 90  ? 66.331 33.853  -61.343 0.00 46.22  ? 116  ILE   B HG13 1 
ATOM   13173 H HG21 . ILE   B  1 90  ? 70.013 34.501  -61.655 0.00 47.11  ? 116  ILE   B HG21 1 
ATOM   13174 H HG22 . ILE   B  1 90  ? 69.874 35.995  -62.593 0.00 47.88  ? 116  ILE   B HG22 1 
ATOM   13175 H HG23 . ILE   B  1 90  ? 69.445 35.993  -60.864 0.00 47.65  ? 116  ILE   B HG23 1 
ATOM   13176 H HD11 . ILE   B  1 90  ? 67.344 32.074  -60.470 0.00 46.15  ? 116  ILE   B HD11 1 
ATOM   13177 H HD12 . ILE   B  1 90  ? 68.459 32.465  -61.805 0.00 46.56  ? 116  ILE   B HD12 1 
ATOM   13178 H HD13 . ILE   B  1 90  ? 68.867 32.943  -60.133 0.00 46.64  ? 116  ILE   B HD13 1 
ATOM   13179 N N    . THR   B  1 91  ? 68.117 38.370  -63.213 1.00 35.90  ? 117  THR   B N    1 
ATOM   13180 C CA   . THR   B  1 91  ? 68.649 39.229  -64.263 1.00 35.72  ? 117  THR   B CA   1 
ATOM   13181 C C    . THR   B  1 91  ? 70.046 38.767  -64.684 1.00 35.31  ? 117  THR   B C    1 
ATOM   13182 O O    . THR   B  1 91  ? 70.733 38.075  -63.926 1.00 35.04  ? 117  THR   B O    1 
ATOM   13183 C CB   . THR   B  1 91  ? 68.709 40.669  -63.763 1.00 37.40  ? 117  THR   B CB   1 
ATOM   13184 O OG1  . THR   B  1 91  ? 69.539 40.694  -62.601 1.00 39.28  ? 117  THR   B OG1  1 
ATOM   13185 C CG2  . THR   B  1 91  ? 67.331 41.237  -63.447 1.00 37.51  ? 117  THR   B CG2  1 
ATOM   13186 H H    . THR   B  1 91  ? 68.162 38.776  -62.284 0.00 48.52  ? 117  THR   B H    1 
ATOM   13187 H HA   . THR   B  1 91  ? 67.997 39.202  -65.135 0.00 48.90  ? 117  THR   B HA   1 
ATOM   13188 H HB   . THR   B  1 91  ? 69.160 41.296  -64.531 0.00 52.05  ? 117  THR   B HB   1 
ATOM   13189 H HG1  . THR   B  1 91  ? 69.724 41.632  -62.335 0.00 54.28  ? 117  THR   B HG1  1 
ATOM   13190 H HG21 . THR   B  1 91  ? 67.416 42.289  -63.179 0.00 52.41  ? 117  THR   B HG21 1 
ATOM   13191 H HG22 . THR   B  1 91  ? 66.683 41.144  -64.317 0.00 51.87  ? 117  THR   B HG22 1 
ATOM   13192 H HG23 . THR   B  1 91  ? 66.885 40.697  -62.613 0.00 51.41  ? 117  THR   B HG23 1 
ATOM   13193 N N    . ASP   B  1 92  ? 70.472 39.176  -65.895 1.00 34.87  ? 118  ASP   B N    1 
ATOM   13194 C CA   . ASP   B  1 92  ? 71.792 38.863  -66.443 1.00 34.94  ? 118  ASP   B CA   1 
ATOM   13195 C C    . ASP   B  1 92  ? 72.874 39.427  -65.507 1.00 34.66  ? 118  ASP   B C    1 
ATOM   13196 O O    . ASP   B  1 92  ? 72.833 40.605  -65.158 1.00 35.18  ? 118  ASP   B O    1 
ATOM   13197 C CB   . ASP   B  1 92  ? 71.926 39.486  -67.855 1.00 37.11  ? 118  ASP   B CB   1 
ATOM   13198 C CG   . ASP   B  1 92  ? 73.219 39.205  -68.606 1.00 44.64  ? 118  ASP   B CG   1 
ATOM   13199 O OD1  . ASP   B  1 92  ? 74.131 38.575  -68.019 1.00 45.80  ? 118  ASP   B OD1  1 
ATOM   13200 O OD2  . ASP   B  1 92  ? 73.329 39.632  -69.783 1.00 48.13  ? 118  ASP   B OD2  1 
ATOM   13201 H H    . ASP   B  1 92  ? 69.898 39.738  -66.516 0.00 48.55  ? 118  ASP   B H    1 
ATOM   13202 H HA   . ASP   B  1 92  ? 71.904 37.782  -66.522 0.00 47.89  ? 118  ASP   B HA   1 
ATOM   13203 H HB2  . ASP   B  1 92  ? 71.110 39.112  -68.471 0.00 51.40  ? 118  ASP   B HB2  1 
ATOM   13204 H HB3  . ASP   B  1 92  ? 71.838 40.567  -67.758 0.00 52.11  ? 118  ASP   B HB3  1 
ATOM   13205 N N    . GLY   B  1 93  ? 73.813 38.580  -65.104 1.00 33.67  ? 119  GLY   B N    1 
ATOM   13206 C CA   . GLY   B  1 93  ? 74.903 38.978  -64.226 1.00 33.21  ? 119  GLY   B CA   1 
ATOM   13207 C C    . GLY   B  1 93  ? 74.509 39.308  -62.798 1.00 32.49  ? 119  GLY   B C    1 
ATOM   13208 O O    . GLY   B  1 93  ? 75.244 40.022  -62.127 1.00 32.11  ? 119  GLY   B O    1 
ATOM   13209 H H    . GLY   B  1 93  ? 73.852 37.600  -65.367 0.00 46.40  ? 119  GLY   B H    1 
ATOM   13210 H HA2  . GLY   B  1 93  ? 75.637 38.175  -64.190 0.00 46.29  ? 119  GLY   B HA2  1 
ATOM   13211 H HA3  . GLY   B  1 93  ? 75.389 39.857  -64.649 0.00 47.15  ? 119  GLY   B HA3  1 
ATOM   13212 N N    . ALA   B  1 94  ? 73.383 38.771  -62.293 1.00 32.43  ? 120  ALA   B N    1 
ATOM   13213 C CA   . ALA   B  1 94  ? 72.953 39.071  -60.923 1.00 32.69  ? 120  ALA   B CA   1 
ATOM   13214 C C    . ALA   B  1 94  ? 73.975 38.616  -59.862 1.00 32.95  ? 120  ALA   B C    1 
ATOM   13215 O O    . ALA   B  1 94  ? 74.191 39.332  -58.885 1.00 33.35  ? 120  ALA   B O    1 
ATOM   13216 C CB   . ALA   B  1 94  ? 71.604 38.441  -60.638 1.00 32.70  ? 120  ALA   B CB   1 
ATOM   13217 H H    . ALA   B  1 94  ? 72.771 38.129  -62.786 0.00 44.67  ? 120  ALA   B H    1 
ATOM   13218 H HA   . ALA   B  1 94  ? 72.841 40.150  -60.825 0.00 45.86  ? 120  ALA   B HA   1 
ATOM   13219 H HB1  . ALA   B  1 94  ? 71.215 38.892  -59.727 0.00 44.87  ? 120  ALA   B HB1  1 
ATOM   13220 H HB2  . ALA   B  1 94  ? 70.927 38.641  -61.467 0.00 44.85  ? 120  ALA   B HB2  1 
ATOM   13221 H HB3  . ALA   B  1 94  ? 71.729 37.367  -60.503 0.00 44.24  ? 120  ALA   B HB3  1 
ATOM   13222 N N    . PHE   B  1 95  ? 74.583 37.435  -60.049 1.00 32.16  ? 121  PHE   B N    1 
ATOM   13223 C CA   . PHE   B  1 95  ? 75.562 36.868  -59.114 1.00 32.13  ? 121  PHE   B CA   1 
ATOM   13224 C C    . PHE   B  1 95  ? 77.021 37.121  -59.546 1.00 33.24  ? 121  PHE   B C    1 
ATOM   13225 O O    . PHE   B  1 95  ? 77.923 36.587  -58.911 1.00 33.20  ? 121  PHE   B O    1 
ATOM   13226 C CB   . PHE   B  1 95  ? 75.362 35.335  -59.034 1.00 31.17  ? 121  PHE   B CB   1 
ATOM   13227 C CG   . PHE   B  1 95  ? 73.999 34.835  -58.644 1.00 30.71  ? 121  PHE   B CG   1 
ATOM   13228 C CD1  . PHE   B  1 95  ? 73.697 34.573  -57.323 1.00 30.62  ? 121  PHE   B CD1  1 
ATOM   13229 C CD2  . PHE   B  1 95  ? 73.089 34.442  -59.611 1.00 31.20  ? 121  PHE   B CD2  1 
ATOM   13230 C CE1  . PHE   B  1 95  ? 72.463 34.042  -56.970 1.00 31.37  ? 121  PHE   B CE1  1 
ATOM   13231 C CE2  . PHE   B  1 95  ? 71.846 33.933  -59.252 1.00 31.61  ? 121  PHE   B CE2  1 
ATOM   13232 C CZ   . PHE   B  1 95  ? 71.540 33.741  -57.933 1.00 31.25  ? 121  PHE   B CZ   1 
ATOM   13233 H H    . PHE   B  1 95  ? 74.410 36.836  -60.850 0.00 43.81  ? 121  PHE   B H    1 
ATOM   13234 H HA   . PHE   B  1 95  ? 75.424 37.276  -58.115 0.00 44.04  ? 121  PHE   B HA   1 
ATOM   13235 H HB2  . PHE   B  1 95  ? 75.523 34.922  -60.027 0.00 41.91  ? 121  PHE   B HB2  1 
ATOM   13236 H HB3  . PHE   B  1 95  ? 76.074 34.908  -58.330 0.00 41.93  ? 121  PHE   B HB3  1 
ATOM   13237 H HD1  . PHE   B  1 95  ? 74.408 34.827  -56.555 0.00 40.81  ? 121  PHE   B HD1  1 
ATOM   13238 H HD2  . PHE   B  1 95  ? 73.306 34.611  -60.652 0.00 41.42  ? 121  PHE   B HD2  1 
ATOM   13239 H HE1  . PHE   B  1 95  ? 72.220 33.899  -55.931 0.00 40.86  ? 121  PHE   B HE1  1 
ATOM   13240 H HE2  . PHE   B  1 95  ? 71.128 33.678  -60.012 0.00 41.10  ? 121  PHE   B HE2  1 
ATOM   13241 H HZ   . PHE   B  1 95  ? 70.585 33.329  -57.657 0.00 40.27  ? 121  PHE   B HZ   1 
ATOM   13242 N N    . LEU   B  1 96  ? 77.258 37.887  -60.625 1.00 34.35  ? 122  LEU   B N    1 
ATOM   13243 C CA   . LEU   B  1 96  ? 78.600 38.108  -61.174 1.00 36.02  ? 122  LEU   B CA   1 
ATOM   13244 C C    . LEU   B  1 96  ? 79.589 38.729  -60.188 1.00 37.43  ? 122  LEU   B C    1 
ATOM   13245 O O    . LEU   B  1 96  ? 80.763 38.352  -60.201 1.00 38.51  ? 122  LEU   B O    1 
ATOM   13246 C CB   . LEU   B  1 96  ? 78.508 38.968  -62.452 1.00 36.57  ? 122  LEU   B CB   1 
ATOM   13247 C CG   . LEU   B  1 96  ? 79.753 39.032  -63.343 1.00 38.65  ? 122  LEU   B CG   1 
ATOM   13248 C CD1  . LEU   B  1 96  ? 80.089 37.664  -63.931 1.00 39.23  ? 122  LEU   B CD1  1 
ATOM   13249 C CD2  . LEU   B  1 96  ? 79.551 40.032  -64.473 1.00 39.43  ? 122  LEU   B CD2  1 
ATOM   13250 H H    . LEU   B  1 96  ? 76.536 38.393  -61.127 0.00 47.65  ? 122  LEU   B H    1 
ATOM   13251 H HA   . LEU   B  1 96  ? 78.991 37.130  -61.447 0.00 49.64  ? 122  LEU   B HA   1 
ATOM   13252 H HB2  . LEU   B  1 96  ? 77.702 38.580  -63.074 0.00 50.83  ? 122  LEU   B HB2  1 
ATOM   13253 H HB3  . LEU   B  1 96  ? 78.273 39.988  -62.154 0.00 51.61  ? 122  LEU   B HB3  1 
ATOM   13254 H HG   . LEU   B  1 96  ? 80.608 39.366  -62.757 0.00 54.41  ? 122  LEU   B HG   1 
ATOM   13255 H HD11 . LEU   B  1 96  ? 80.799 37.795  -64.746 0.00 54.56  ? 122  LEU   B HD11 1 
ATOM   13256 H HD12 . LEU   B  1 96  ? 80.538 37.041  -63.159 0.00 53.98  ? 122  LEU   B HD12 1 
ATOM   13257 H HD13 . LEU   B  1 96  ? 79.179 37.197  -64.305 0.00 53.82  ? 122  LEU   B HD13 1 
ATOM   13258 H HD21 . LEU   B  1 96  ? 80.469 40.104  -65.054 0.00 55.91  ? 122  LEU   B HD21 1 
ATOM   13259 H HD22 . LEU   B  1 96  ? 78.735 39.688  -65.106 0.00 55.28  ? 122  LEU   B HD22 1 
ATOM   13260 H HD23 . LEU   B  1 96  ? 79.308 41.004  -64.045 0.00 55.99  ? 122  LEU   B HD23 1 
ATOM   13261 N N    . ASN   B  1 97  ? 79.137 39.657  -59.335 1.00 37.78  ? 123  ASN   B N    1 
ATOM   13262 C CA   . ASN   B  1 97  ? 80.014 40.335  -58.370 1.00 38.88  ? 123  ASN   B CA   1 
ATOM   13263 C C    . ASN   B  1 97  ? 80.497 39.444  -57.205 1.00 38.02  ? 123  ASN   B C    1 
ATOM   13264 O O    . ASN   B  1 97  ? 81.417 39.839  -56.494 1.00 38.34  ? 123  ASN   B O    1 
ATOM   13265 C CB   . ASN   B  1 97  ? 79.341 41.624  -57.826 1.00 41.91  ? 123  ASN   B CB   1 
ATOM   13266 C CG   . ASN   B  1 97  ? 78.480 41.453  -56.587 1.00 48.56  ? 123  ASN   B CG   1 
ATOM   13267 O OD1  . ASN   B  1 97  ? 78.764 42.029  -55.529 1.00 50.93  ? 123  ASN   B OD1  1 
ATOM   13268 N ND2  . ASN   B  1 97  ? 77.419 40.648  -56.678 1.00 50.50  ? 123  ASN   B ND2  1 
ATOM   13269 H H    . ASN   B  1 97  ? 78.168 39.955  -59.285 0.00 52.87  ? 123  ASN   B H    1 
ATOM   13270 H HA   . ASN   B  1 97  ? 80.907 40.659  -58.904 0.00 55.27  ? 123  ASN   B HA   1 
ATOM   13271 H HB2  . ASN   B  1 97  ? 80.129 42.330  -57.569 0.00 59.59  ? 123  ASN   B HB2  1 
ATOM   13272 H HB3  . ASN   B  1 97  ? 78.717 42.058  -58.606 0.00 59.08  ? 123  ASN   B HB3  1 
ATOM   13273 H HD21 . ASN   B  1 97  ? 76.819 40.507  -55.872 0.00 68.01  ? 123  ASN   B HD21 1 
ATOM   13274 H HD22 . ASN   B  1 97  ? 77.211 40.176  -57.552 0.00 67.95  ? 123  ASN   B HD22 1 
ATOM   13275 N N    . LEU   B  1 98  ? 79.864 38.286  -56.978 1.00 36.72  ? 124  LEU   B N    1 
ATOM   13276 C CA   . LEU   B  1 98  ? 80.243 37.388  -55.886 1.00 35.77  ? 124  LEU   B CA   1 
ATOM   13277 C C    . LEU   B  1 98  ? 81.447 36.543  -56.328 1.00 35.01  ? 124  LEU   B C    1 
ATOM   13278 O O    . LEU   B  1 98  ? 81.288 35.473  -56.918 1.00 35.06  ? 124  LEU   B O    1 
ATOM   13279 C CB   . LEU   B  1 98  ? 79.044 36.508  -55.503 1.00 35.48  ? 124  LEU   B CB   1 
ATOM   13280 C CG   . LEU   B  1 98  ? 77.777 37.258  -55.091 1.00 36.11  ? 124  LEU   B CG   1 
ATOM   13281 C CD1  . LEU   B  1 98  ? 76.637 36.284  -54.884 1.00 36.77  ? 124  LEU   B CD1  1 
ATOM   13282 C CD2  . LEU   B  1 98  ? 78.010 38.102  -53.834 1.00 36.06  ? 124  LEU   B CD2  1 
ATOM   13283 H H    . LEU   B  1 98  ? 79.088 37.934  -57.528 0.00 50.74  ? 124  LEU   B H    1 
ATOM   13284 H HA   . LEU   B  1 98  ? 80.535 37.960  -55.007 0.00 50.02  ? 124  LEU   B HA   1 
ATOM   13285 H HB2  . LEU   B  1 98  ? 78.777 35.885  -56.355 0.00 48.16  ? 124  LEU   B HB2  1 
ATOM   13286 H HB3  . LEU   B  1 98  ? 79.335 35.873  -54.667 0.00 48.32  ? 124  LEU   B HB3  1 
ATOM   13287 H HG   . LEU   B  1 98  ? 77.484 37.934  -55.892 0.00 49.58  ? 124  LEU   B HG   1 
ATOM   13288 H HD11 . LEU   B  1 98  ? 75.767 36.811  -54.498 0.00 49.39  ? 124  LEU   B HD11 1 
ATOM   13289 H HD12 . LEU   B  1 98  ? 76.393 35.820  -55.839 0.00 49.07  ? 124  LEU   B HD12 1 
ATOM   13290 H HD13 . LEU   B  1 98  ? 76.962 35.523  -54.177 0.00 49.07  ? 124  LEU   B HD13 1 
ATOM   13291 H HD21 . LEU   B  1 98  ? 77.053 38.467  -53.467 0.00 49.71  ? 124  LEU   B HD21 1 
ATOM   13292 H HD22 . LEU   B  1 98  ? 78.490 37.485  -53.076 0.00 49.60  ? 124  LEU   B HD22 1 
ATOM   13293 H HD23 . LEU   B  1 98  ? 78.647 38.949  -54.084 0.00 50.36  ? 124  LEU   B HD23 1 
ATOM   13294 N N    . LYS   B  1 99  ? 82.651 37.035  -56.021 1.00 34.32  ? 125  LYS   B N    1 
ATOM   13295 C CA   . LYS   B  1 99  ? 83.912 36.444  -56.464 1.00 34.55  ? 125  LYS   B CA   1 
ATOM   13296 C C    . LYS   B  1 99  ? 84.324 35.115  -55.814 1.00 33.73  ? 125  LYS   B C    1 
ATOM   13297 O O    . LYS   B  1 99  ? 85.144 34.427  -56.411 1.00 33.11  ? 125  LYS   B O    1 
ATOM   13298 C CB   . LYS   B  1 99  ? 85.053 37.460  -56.313 1.00 37.16  ? 125  LYS   B CB   1 
ATOM   13299 C CG   . LYS   B  1 99  ? 84.889 38.693  -57.202 1.00 43.09  ? 125  LYS   B CG   1 
ATOM   13300 C CD   . LYS   B  1 99  ? 85.354 38.457  -58.644 1.00 50.31  ? 125  LYS   B CD   1 
ATOM   13301 C CE   . LYS   B  1 99  ? 86.851 38.638  -58.798 1.00 56.13  ? 125  LYS   B CE   1 
ATOM   13302 N NZ   . LYS   B  1 99  ? 87.289 38.436  -60.206 1.00 60.33  ? 125  LYS   B NZ   1 
ATOM   13303 H H    . LYS   B  1 99  ? 82.784 37.863  -55.450 0.00 48.93  ? 125  LYS   B H    1 
ATOM   13304 H HA   . LYS   B  1 99  ? 83.805 36.229  -57.526 0.00 48.74  ? 125  LYS   B HA   1 
ATOM   13305 H HB2  . LYS   B  1 99  ? 85.100 37.796  -55.278 0.00 53.09  ? 125  LYS   B HB2  1 
ATOM   13306 H HB3  . LYS   B  1 99  ? 85.990 36.974  -56.578 0.00 52.99  ? 125  LYS   B HB3  1 
ATOM   13307 H HG2  . LYS   B  1 99  ? 83.843 38.991  -57.235 0.00 60.36  ? 125  LYS   B HG2  1 
ATOM   13308 H HG3  . LYS   B  1 99  ? 85.488 39.503  -56.787 0.00 61.19  ? 125  LYS   B HG3  1 
ATOM   13309 H HD2  . LYS   B  1 99  ? 85.108 37.445  -58.961 0.00 68.70  ? 125  LYS   B HD2  1 
ATOM   13310 H HD3  . LYS   B  1 99  ? 84.861 39.177  -59.296 0.00 69.48  ? 125  LYS   B HD3  1 
ATOM   13311 H HE2  . LYS   B  1 99  ? 87.122 39.650  -58.502 0.00 77.50  ? 125  LYS   B HE2  1 
ATOM   13312 H HE3  . LYS   B  1 99  ? 87.374 37.911  -58.180 0.00 76.73  ? 125  LYS   B HE3  1 
ATOM   13313 H HZ1  . LYS   B  1 99  ? 88.294 38.563  -60.277 0.00 82.48  ? 125  LYS   B HZ1  1 
ATOM   13314 H HZ2  . LYS   B  1 99  ? 87.050 37.499  -60.514 0.00 81.50  ? 125  LYS   B HZ2  1 
ATOM   13315 H HZ3  . LYS   B  1 99  ? 86.829 39.109  -60.810 0.00 82.21  ? 125  LYS   B HZ3  1 
ATOM   13316 N N    . ASN   B  1 100 ? 83.798 34.750  -54.628 1.00 33.65  ? 126  ASN   B N    1 
ATOM   13317 C CA   . ASN   B  1 100 ? 84.117 33.454  -53.999 1.00 33.93  ? 126  ASN   B CA   1 
ATOM   13318 C C    . ASN   B  1 100 ? 82.913 32.488  -54.044 1.00 32.12  ? 126  ASN   B C    1 
ATOM   13319 O O    . ASN   B  1 100 ? 82.950 31.471  -53.354 1.00 31.95  ? 126  ASN   B O    1 
ATOM   13320 C CB   . ASN   B  1 100 ? 84.600 33.646  -52.538 1.00 37.72  ? 126  ASN   B CB   1 
ATOM   13321 C CG   . ASN   B  1 100 ? 85.333 32.435  -51.931 1.00 43.74  ? 126  ASN   B CG   1 
ATOM   13322 O OD1  . ASN   B  1 100 ? 85.129 31.264  -52.335 1.00 45.27  ? 126  ASN   B OD1  1 
ATOM   13323 N ND2  . ASN   B  1 100 ? 86.197 32.679  -50.936 1.00 44.66  ? 126  ASN   B ND2  1 
ATOM   13324 H H    . ASN   B  1 100 ? 83.162 35.319  -54.079 0.00 47.07  ? 126  ASN   B H    1 
ATOM   13325 H HA   . ASN   B  1 100 ? 84.934 32.969  -54.531 0.00 46.98  ? 126  ASN   B HA   1 
ATOM   13326 H HB2  . ASN   B  1 100 ? 85.281 34.495  -52.511 0.00 52.42  ? 126  ASN   B HB2  1 
ATOM   13327 H HB3  . ASN   B  1 100 ? 83.733 33.852  -51.912 0.00 51.60  ? 126  ASN   B HB3  1 
ATOM   13328 H HD21 . ASN   B  1 100 ? 86.703 31.911  -50.506 0.00 60.38  ? 126  ASN   B HD21 1 
ATOM   13329 H HD22 . ASN   B  1 100 ? 86.346 33.627  -50.608 0.00 60.94  ? 126  ASN   B HD22 1 
ATOM   13330 N N    . LEU   B  1 101 ? 81.862 32.769  -54.853 1.00 30.46  ? 127  LEU   B N    1 
ATOM   13331 C CA   . LEU   B  1 101 ? 80.703 31.885  -54.924 1.00 28.82  ? 127  LEU   B CA   1 
ATOM   13332 C C    . LEU   B  1 101 ? 81.123 30.598  -55.627 1.00 27.68  ? 127  LEU   B C    1 
ATOM   13333 O O    . LEU   B  1 101 ? 81.569 30.647  -56.772 1.00 27.00  ? 127  LEU   B O    1 
ATOM   13334 C CB   . LEU   B  1 101 ? 79.537 32.553  -55.662 1.00 29.13  ? 127  LEU   B CB   1 
ATOM   13335 C CG   . LEU   B  1 101 ? 78.209 31.774  -55.653 1.00 30.66  ? 127  LEU   B CG   1 
ATOM   13336 C CD1  . LEU   B  1 101 ? 77.628 31.689  -54.240 1.00 31.27  ? 127  LEU   B CD1  1 
ATOM   13337 C CD2  . LEU   B  1 101 ? 77.207 32.403  -56.607 1.00 31.05  ? 127  LEU   B CD2  1 
ATOM   13338 H H    . LEU   B  1 101 ? 81.785 33.576  -55.464 0.00 41.98  ? 127  LEU   B H    1 
ATOM   13339 H HA   . LEU   B  1 101 ? 80.367 31.658  -53.916 0.00 38.81  ? 127  LEU   B HA   1 
ATOM   13340 H HB2  . LEU   B  1 101 ? 79.352 33.524  -55.206 0.00 39.64  ? 127  LEU   B HB2  1 
ATOM   13341 H HB3  . LEU   B  1 101 ? 79.823 32.693  -56.703 0.00 39.43  ? 127  LEU   B HB3  1 
ATOM   13342 H HG   . LEU   B  1 101 ? 78.380 30.755  -55.997 0.00 40.09  ? 127  LEU   B HG   1 
ATOM   13343 H HD11 . LEU   B  1 101 ? 76.584 31.386  -54.306 0.00 40.59  ? 127  LEU   B HD11 1 
ATOM   13344 H HD12 . LEU   B  1 101 ? 78.183 30.947  -53.669 0.00 40.84  ? 127  LEU   B HD12 1 
ATOM   13345 H HD13 . LEU   B  1 101 ? 77.703 32.665  -53.762 0.00 41.40  ? 127  LEU   B HD13 1 
ATOM   13346 H HD21 . LEU   B  1 101 ? 76.297 31.805  -56.614 0.00 40.45  ? 127  LEU   B HD21 1 
ATOM   13347 H HD22 . LEU   B  1 101 ? 76.985 33.415  -56.268 0.00 41.27  ? 127  LEU   B HD22 1 
ATOM   13348 H HD23 . LEU   B  1 101 ? 77.639 32.433  -57.606 0.00 41.07  ? 127  LEU   B HD23 1 
ATOM   13349 N N    . ARG   B  1 102 ? 81.018 29.466  -54.926 1.00 26.74  ? 128  ARG   B N    1 
ATOM   13350 C CA   . ARG   B  1 102 ? 81.393 28.145  -55.418 1.00 26.83  ? 128  ARG   B CA   1 
ATOM   13351 C C    . ARG   B  1 102 ? 80.174 27.272  -55.686 1.00 25.95  ? 128  ARG   B C    1 
ATOM   13352 O O    . ARG   B  1 102 ? 80.160 26.529  -56.666 1.00 25.31  ? 128  ARG   B O    1 
ATOM   13353 C CB   . ARG   B  1 102 ? 82.295 27.433  -54.389 1.00 28.74  ? 128  ARG   B CB   1 
ATOM   13354 C CG   . ARG   B  1 102 ? 83.592 28.169  -54.038 1.00 34.74  ? 128  ARG   B CG   1 
ATOM   13355 C CD   . ARG   B  1 102 ? 84.565 28.179  -55.196 1.00 41.02  ? 128  ARG   B CD   1 
ATOM   13356 N NE   . ARG   B  1 102 ? 85.776 28.951  -54.913 1.00 46.35  ? 128  ARG   B NE   1 
ATOM   13357 C CZ   . ARG   B  1 102 ? 86.699 29.255  -55.824 1.00 49.23  ? 128  ARG   B CZ   1 
ATOM   13358 N NH1  . ARG   B  1 102 ? 86.558 28.853  -57.092 1.00 47.40  ? 128  ARG   B NH1  1 
ATOM   13359 N NH2  . ARG   B  1 102 ? 87.768 29.964  -55.482 1.00 50.37  ? 128  ARG   B NH2  1 
ATOM   13360 H H    . ARG   B  1 102 ? 80.669 29.430  -53.973 0.00 35.55  ? 128  ARG   B H    1 
ATOM   13361 H HA   . ARG   B  1 102 ? 81.933 28.236  -56.358 0.00 35.63  ? 128  ARG   B HA   1 
ATOM   13362 H HB2  . ARG   B  1 102 ? 81.732 27.308  -53.465 0.00 37.57  ? 128  ARG   B HB2  1 
ATOM   13363 H HB3  . ARG   B  1 102 ? 82.571 26.458  -54.787 0.00 37.55  ? 128  ARG   B HB3  1 
ATOM   13364 H HG2  . ARG   B  1 102 ? 83.372 29.201  -53.767 0.00 45.98  ? 128  ARG   B HG2  1 
ATOM   13365 H HG3  . ARG   B  1 102 ? 84.070 27.661  -53.202 0.00 45.71  ? 128  ARG   B HG3  1 
ATOM   13366 H HD2  . ARG   B  1 102 ? 84.859 27.156  -55.428 0.00 53.31  ? 128  ARG   B HD2  1 
ATOM   13367 H HD3  . ARG   B  1 102 ? 84.106 28.646  -56.065 0.00 53.50  ? 128  ARG   B HD3  1 
ATOM   13368 H HE   . ARG   B  1 102 ? 85.909 29.281  -53.962 0.00 60.85  ? 128  ARG   B HE   1 
ATOM   13369 H HH11 . ARG   B  1 102 ? 85.764 28.303  -57.399 0.00 61.65  ? 128  ARG   B HH11 1 
ATOM   13370 H HH12 . ARG   B  1 102 ? 87.272 29.090  -57.774 0.00 62.49  ? 128  ARG   B HH12 1 
ATOM   13371 H HH21 . ARG   B  1 102 ? 87.885 30.283  -54.526 0.00 66.80  ? 128  ARG   B HH21 1 
ATOM   13372 H HH22 . ARG   B  1 102 ? 88.473 30.196  -56.174 0.00 66.95  ? 128  ARG   B HH22 1 
ATOM   13373 N N    . GLU   B  1 103 ? 79.168 27.320  -54.807 1.00 25.59  ? 129  GLU   B N    1 
ATOM   13374 C CA   . GLU   B  1 103 ? 77.989 26.468  -54.948 1.00 25.84  ? 129  GLU   B CA   1 
ATOM   13375 C C    . GLU   B  1 103 ? 76.726 27.301  -55.104 1.00 25.62  ? 129  GLU   B C    1 
ATOM   13376 O O    . GLU   B  1 103 ? 76.459 28.166  -54.273 1.00 25.49  ? 129  GLU   B O    1 
ATOM   13377 C CB   . GLU   B  1 103 ? 77.904 25.544  -53.722 1.00 28.21  ? 129  GLU   B CB   1 
ATOM   13378 C CG   . GLU   B  1 103 ? 76.803 24.494  -53.792 1.00 34.45  ? 129  GLU   B CG   1 
ATOM   13379 C CD   . GLU   B  1 103 ? 76.848 23.456  -52.683 1.00 42.31  ? 129  GLU   B CD   1 
ATOM   13380 O OE1  . GLU   B  1 103 ? 77.823 23.448  -51.897 1.00 44.10  ? 129  GLU   B OE1  1 
ATOM   13381 O OE2  . GLU   B  1 103 ? 75.900 22.644  -52.602 1.00 45.00  ? 129  GLU   B OE2  1 
ATOM   13382 H H    . GLU   B  1 103 ? 79.136 27.922  -53.991 0.00 33.18  ? 129  GLU   B H    1 
ATOM   13383 H HA   . GLU   B  1 103 ? 78.080 25.825  -55.822 0.00 32.51  ? 129  GLU   B HA   1 
ATOM   13384 H HB2  . GLU   B  1 103 ? 78.857 25.022  -53.642 0.00 35.32  ? 129  GLU   B HB2  1 
ATOM   13385 H HB3  . GLU   B  1 103 ? 77.743 26.153  -52.834 0.00 35.36  ? 129  GLU   B HB3  1 
ATOM   13386 H HG2  . GLU   B  1 103 ? 75.835 24.989  -53.725 0.00 41.99  ? 129  GLU   B HG2  1 
ATOM   13387 H HG3  . GLU   B  1 103 ? 76.883 23.968  -54.742 0.00 41.97  ? 129  GLU   B HG3  1 
ATOM   13388 N N    . LEU   B  1 104 ? 75.944 27.037  -56.160 1.00 25.04  ? 130  LEU   B N    1 
ATOM   13389 C CA   . LEU   B  1 104 ? 74.695 27.741  -56.414 1.00 24.92  ? 130  LEU   B CA   1 
ATOM   13390 C C    . LEU   B  1 104 ? 73.599 26.716  -56.702 1.00 24.23  ? 130  LEU   B C    1 
ATOM   13391 O O    . LEU   B  1 104 ? 73.672 25.980  -57.690 1.00 23.14  ? 130  LEU   B O    1 
ATOM   13392 C CB   . LEU   B  1 104 ? 74.864 28.710  -57.599 1.00 25.20  ? 130  LEU   B CB   1 
ATOM   13393 C CG   . LEU   B  1 104 ? 73.659 29.578  -57.987 1.00 26.55  ? 130  LEU   B CG   1 
ATOM   13394 C CD1  . LEU   B  1 104 ? 73.070 30.342  -56.778 1.00 27.30  ? 130  LEU   B CD1  1 
ATOM   13395 C CD2  . LEU   B  1 104 ? 74.057 30.566  -59.079 1.00 27.03  ? 130  LEU   B CD2  1 
ATOM   13396 H H    . LEU   B  1 104 ? 76.151 26.337  -56.865 0.00 31.26  ? 130  LEU   B H    1 
ATOM   13397 H HA   . LEU   B  1 104 ? 74.406 28.316  -55.536 0.00 31.33  ? 130  LEU   B HA   1 
ATOM   13398 H HB2  . LEU   B  1 104 ? 75.680 29.390  -57.359 0.00 32.39  ? 130  LEU   B HB2  1 
ATOM   13399 H HB3  . LEU   B  1 104 ? 75.134 28.125  -58.478 0.00 31.88  ? 130  LEU   B HB3  1 
ATOM   13400 H HG   . LEU   B  1 104 ? 72.875 28.940  -58.393 0.00 33.33  ? 130  LEU   B HG   1 
ATOM   13401 H HD11 . LEU   B  1 104 ? 72.347 31.072  -57.139 0.00 34.86  ? 130  LEU   B HD11 1 
ATOM   13402 H HD12 . LEU   B  1 104 ? 72.573 29.635  -56.116 0.00 34.30  ? 130  LEU   B HD12 1 
ATOM   13403 H HD13 . LEU   B  1 104 ? 73.877 30.847  -56.250 0.00 35.03  ? 130  LEU   B HD13 1 
ATOM   13404 H HD21 . LEU   B  1 104 ? 73.198 31.181  -59.341 0.00 34.86  ? 130  LEU   B HD21 1 
ATOM   13405 H HD22 . LEU   B  1 104 ? 74.864 31.196  -58.708 0.00 35.15  ? 130  LEU   B HD22 1 
ATOM   13406 H HD23 . LEU   B  1 104 ? 74.394 30.009  -59.952 0.00 34.69  ? 130  LEU   B HD23 1 
ATOM   13407 N N    . LEU   B  1 105 ? 72.600 26.647  -55.805 1.00 23.28  ? 131  LEU   B N    1 
ATOM   13408 C CA   . LEU   B  1 105 ? 71.507 25.707  -55.948 1.00 23.42  ? 131  LEU   B CA   1 
ATOM   13409 C C    . LEU   B  1 105 ? 70.267 26.495  -56.339 1.00 22.82  ? 131  LEU   B C    1 
ATOM   13410 O O    . LEU   B  1 105 ? 69.834 27.378  -55.605 1.00 22.33  ? 131  LEU   B O    1 
ATOM   13411 C CB   . LEU   B  1 105 ? 71.304 24.893  -54.647 1.00 23.66  ? 131  LEU   B CB   1 
ATOM   13412 C CG   . LEU   B  1 105 ? 72.557 24.360  -53.967 1.00 25.38  ? 131  LEU   B CG   1 
ATOM   13413 C CD1  . LEU   B  1 105 ? 72.200 23.605  -52.704 1.00 25.79  ? 131  LEU   B CD1  1 
ATOM   13414 C CD2  . LEU   B  1 105 ? 73.352 23.447  -54.920 1.00 26.37  ? 131  LEU   B CD2  1 
ATOM   13415 H H    . LEU   B  1 105 ? 72.525 27.224  -54.973 0.00 28.58  ? 131  LEU   B H    1 
ATOM   13416 H HA   . LEU   B  1 105 ? 71.724 24.990  -56.738 0.00 27.97  ? 131  LEU   B HA   1 
ATOM   13417 H HB2  . LEU   B  1 105 ? 70.720 25.464  -53.927 0.00 28.10  ? 131  LEU   B HB2  1 
ATOM   13418 H HB3  . LEU   B  1 105 ? 70.779 23.978  -54.912 0.00 27.71  ? 131  LEU   B HB3  1 
ATOM   13419 H HG   . LEU   B  1 105 ? 73.199 25.193  -53.683 0.00 30.56  ? 131  LEU   B HG   1 
ATOM   13420 H HD11 . LEU   B  1 105 ? 73.116 23.254  -52.230 0.00 30.48  ? 131  LEU   B HD11 1 
ATOM   13421 H HD12 . LEU   B  1 105 ? 71.664 24.272  -52.030 0.00 30.47  ? 131  LEU   B HD12 1 
ATOM   13422 H HD13 . LEU   B  1 105 ? 71.571 22.756  -52.963 0.00 30.03  ? 131  LEU   B HD13 1 
ATOM   13423 H HD21 . LEU   B  1 105 ? 74.167 22.985  -54.366 0.00 31.35  ? 131  LEU   B HD21 1 
ATOM   13424 H HD22 . LEU   B  1 105 ? 72.693 22.676  -55.315 0.00 30.98  ? 131  LEU   B HD22 1 
ATOM   13425 H HD23 . LEU   B  1 105 ? 73.760 24.043  -55.735 0.00 31.59  ? 131  LEU   B HD23 1 
ATOM   13426 N N    . LEU   B  1 106 ? 69.722 26.203  -57.519 1.00 22.88  ? 132  LEU   B N    1 
ATOM   13427 C CA   . LEU   B  1 106 ? 68.557 26.895  -58.054 1.00 23.29  ? 132  LEU   B CA   1 
ATOM   13428 C C    . LEU   B  1 106 ? 67.533 25.879  -58.559 1.00 24.15  ? 132  LEU   B C    1 
ATOM   13429 O O    . LEU   B  1 106 ? 67.016 25.999  -59.666 1.00 24.68  ? 132  LEU   B O    1 
ATOM   13430 C CB   . LEU   B  1 106 ? 68.984 27.849  -59.191 1.00 23.30  ? 132  LEU   B CB   1 
ATOM   13431 C CG   . LEU   B  1 106 ? 69.803 29.079  -58.814 1.00 25.17  ? 132  LEU   B CG   1 
ATOM   13432 C CD1  . LEU   B  1 106 ? 70.499 29.648  -60.046 1.00 26.03  ? 132  LEU   B CD1  1 
ATOM   13433 C CD2  . LEU   B  1 106 ? 68.919 30.168  -58.208 1.00 25.82  ? 132  LEU   B CD2  1 
ATOM   13434 H H    . LEU   B  1 106 ? 70.062 25.479  -58.143 0.00 27.29  ? 132  LEU   B H    1 
ATOM   13435 H HA   . LEU   B  1 106 ? 68.064 27.473  -57.274 0.00 28.08  ? 132  LEU   B HA   1 
ATOM   13436 H HB2  . LEU   B  1 106 ? 69.575 27.278  -59.905 0.00 28.46  ? 132  LEU   B HB2  1 
ATOM   13437 H HB3  . LEU   B  1 106 ? 68.089 28.231  -59.678 0.00 28.57  ? 132  LEU   B HB3  1 
ATOM   13438 H HG   . LEU   B  1 106 ? 70.561 28.801  -58.083 0.00 31.20  ? 132  LEU   B HG   1 
ATOM   13439 H HD11 . LEU   B  1 106 ? 70.990 30.582  -59.775 0.00 33.10  ? 132  LEU   B HD11 1 
ATOM   13440 H HD12 . LEU   B  1 106 ? 71.237 28.930  -60.400 0.00 32.59  ? 132  LEU   B HD12 1 
ATOM   13441 H HD13 . LEU   B  1 106 ? 69.756 29.830  -60.820 0.00 32.75  ? 132  LEU   B HD13 1 
ATOM   13442 H HD21 . LEU   B  1 106 ? 69.553 30.947  -57.788 0.00 32.63  ? 132  LEU   B HD21 1 
ATOM   13443 H HD22 . LEU   B  1 106 ? 68.299 30.586  -58.999 0.00 32.43  ? 132  LEU   B HD22 1 
ATOM   13444 H HD23 . LEU   B  1 106 ? 68.281 29.743  -57.436 0.00 31.98  ? 132  LEU   B HD23 1 
ATOM   13445 N N    . GLU   B  1 107 ? 67.214 24.899  -57.731 1.00 24.08  ? 133  GLU   B N    1 
ATOM   13446 C CA   . GLU   B  1 107 ? 66.264 23.856  -58.081 1.00 24.41  ? 133  GLU   B CA   1 
ATOM   13447 C C    . GLU   B  1 107 ? 64.824 24.287  -57.873 1.00 24.55  ? 133  GLU   B C    1 
ATOM   13448 O O    . GLU   B  1 107 ? 64.543 25.066  -56.974 1.00 24.51  ? 133  GLU   B O    1 
ATOM   13449 C CB   . GLU   B  1 107 ? 66.520 22.595  -57.241 1.00 25.70  ? 133  GLU   B CB   1 
ATOM   13450 C CG   . GLU   B  1 107 ? 67.968 22.120  -57.266 1.00 27.64  ? 133  GLU   B CG   1 
ATOM   13451 C CD   . GLU   B  1 107 ? 68.223 20.837  -56.501 1.00 30.02  ? 133  GLU   B CD   1 
ATOM   13452 O OE1  . GLU   B  1 107 ? 67.258 20.247  -55.963 1.00 28.71  ? 133  GLU   B OE1  1 
ATOM   13453 O OE2  . GLU   B  1 107 ? 69.404 20.433  -56.417 1.00 31.36  ? 133  GLU   B OE2  1 
ATOM   13454 H H    . GLU   B  1 107 ? 67.608 24.777  -56.807 0.00 28.08  ? 133  GLU   B H    1 
ATOM   13455 H HA   . GLU   B  1 107 ? 66.396 23.580  -59.126 0.00 28.22  ? 133  GLU   B HA   1 
ATOM   13456 H HB2  . GLU   B  1 107 ? 66.255 22.804  -56.206 0.00 29.27  ? 133  GLU   B HB2  1 
ATOM   13457 H HB3  . GLU   B  1 107 ? 65.899 21.790  -57.631 0.00 29.10  ? 133  GLU   B HB3  1 
ATOM   13458 H HG2  . GLU   B  1 107 ? 68.285 21.988  -58.299 0.00 31.80  ? 133  GLU   B HG2  1 
ATOM   13459 H HG3  . GLU   B  1 107 ? 68.599 22.877  -56.804 0.00 31.94  ? 133  GLU   B HG3  1 
ATOM   13460 N N    . ASP   B  1 108 ? 63.912 23.749  -58.683 1.00 24.76  ? 134  ASP   B N    1 
ATOM   13461 C CA   . ASP   B  1 108 ? 62.479 23.980  -58.527 1.00 26.10  ? 134  ASP   B CA   1 
ATOM   13462 C C    . ASP   B  1 108 ? 62.118 25.468  -58.534 1.00 26.31  ? 134  ASP   B C    1 
ATOM   13463 O O    . ASP   B  1 108 ? 61.379 25.942  -57.669 1.00 26.47  ? 134  ASP   B O    1 
ATOM   13464 C CB   . ASP   B  1 108 ? 62.013 23.289  -57.236 1.00 28.99  ? 134  ASP   B CB   1 
ATOM   13465 C CG   . ASP   B  1 108 ? 60.517 23.147  -57.093 1.00 36.54  ? 134  ASP   B CG   1 
ATOM   13466 O OD1  . ASP   B  1 108 ? 59.811 23.239  -58.126 1.00 38.53  ? 134  ASP   B OD1  1 
ATOM   13467 O OD2  . ASP   B  1 108 ? 60.050 22.938  -55.952 1.00 38.73  ? 134  ASP   B OD2  1 
ATOM   13468 H H    . ASP   B  1 108 ? 64.134 23.138  -59.463 0.00 28.38  ? 134  ASP   B H    1 
ATOM   13469 H HA   . ASP   B  1 108 ? 61.977 23.509  -59.371 0.00 29.97  ? 134  ASP   B HA   1 
ATOM   13470 H HB2  . ASP   B  1 108 ? 62.438 22.286  -57.208 0.00 32.87  ? 134  ASP   B HB2  1 
ATOM   13471 H HB3  . ASP   B  1 108 ? 62.377 23.866  -56.387 0.00 33.22  ? 134  ASP   B HB3  1 
ATOM   13472 N N    . ASN   B  1 109 ? 62.638 26.194  -59.521 1.00 26.03  ? 135  ASN   B N    1 
ATOM   13473 C CA   . ASN   B  1 109 ? 62.406 27.634  -59.654 1.00 26.27  ? 135  ASN   B CA   1 
ATOM   13474 C C    . ASN   B  1 109 ? 61.684 28.016  -60.952 1.00 26.48  ? 135  ASN   B C    1 
ATOM   13475 O O    . ASN   B  1 109 ? 61.596 29.209  -61.243 1.00 26.36  ? 135  ASN   B O    1 
ATOM   13476 C CB   . ASN   B  1 109 ? 63.759 28.364  -59.585 1.00 27.31  ? 135  ASN   B CB   1 
ATOM   13477 C CG   . ASN   B  1 109 ? 64.426 28.358  -58.239 1.00 31.13  ? 135  ASN   B CG   1 
ATOM   13478 O OD1  . ASN   B  1 109 ? 65.634 28.177  -58.129 1.00 33.55  ? 135  ASN   B OD1  1 
ATOM   13479 N ND2  . ASN   B  1 109 ? 63.712 28.682  -57.214 1.00 30.46  ? 135  ASN   B ND2  1 
ATOM   13480 H H    . ASN   B  1 109 ? 63.216 25.808  -60.261 0.00 30.72  ? 135  ASN   B H    1 
ATOM   13481 H HA   . ASN   B  1 109 ? 61.767 27.993  -58.850 0.00 31.51  ? 135  ASN   B HA   1 
ATOM   13482 H HB2  . ASN   B  1 109 ? 64.446 27.823  -60.232 0.00 32.99  ? 135  ASN   B HB2  1 
ATOM   13483 H HB3  . ASN   B  1 109 ? 63.663 29.401  -59.905 0.00 33.47  ? 135  ASN   B HB3  1 
ATOM   13484 H HD21 . ASN   B  1 109 ? 64.136 28.688  -56.292 0.00 36.66  ? 135  ASN   B HD21 1 
ATOM   13485 H HD22 . ASN   B  1 109 ? 62.785 29.066  -57.355 0.00 36.81  ? 135  ASN   B HD22 1 
ATOM   13486 N N    . GLN   B  1 110 ? 61.187 27.032  -61.738 1.00 26.80  ? 136  GLN   B N    1 
ATOM   13487 C CA   . GLN   B  1 110 ? 60.541 27.294  -63.032 1.00 27.50  ? 136  GLN   B CA   1 
ATOM   13488 C C    . GLN   B  1 110 ? 61.395 28.181  -63.955 1.00 26.73  ? 136  GLN   B C    1 
ATOM   13489 O O    . GLN   B  1 110 ? 60.837 28.972  -64.707 1.00 27.44  ? 136  GLN   B O    1 
ATOM   13490 C CB   . GLN   B  1 110 ? 59.139 27.907  -62.834 1.00 30.54  ? 136  GLN   B CB   1 
ATOM   13491 C CG   . GLN   B  1 110 ? 58.200 27.012  -62.015 1.00 36.23  ? 136  GLN   B CG   1 
ATOM   13492 C CD   . GLN   B  1 110 ? 56.735 27.270  -62.290 1.00 44.69  ? 136  GLN   B CD   1 
ATOM   13493 O OE1  . GLN   B  1 110 ? 56.350 28.206  -63.003 1.00 47.58  ? 136  GLN   B OE1  1 
ATOM   13494 N NE2  . GLN   B  1 110 ? 55.873 26.429  -61.733 1.00 46.70  ? 136  GLN   B NE2  1 
ATOM   13495 H H    . GLN   B  1 110 ? 61.206 26.043  -61.514 0.00 31.85  ? 136  GLN   B H    1 
ATOM   13496 H HA   . GLN   B  1 110 ? 60.407 26.340  -63.540 0.00 33.12  ? 136  GLN   B HA   1 
ATOM   13497 H HB2  . GLN   B  1 110 ? 59.232 28.862  -62.320 0.00 37.42  ? 136  GLN   B HB2  1 
ATOM   13498 H HB3  . GLN   B  1 110 ? 58.687 28.048  -63.815 0.00 37.42  ? 136  GLN   B HB3  1 
ATOM   13499 H HG2  . GLN   B  1 110 ? 58.408 25.970  -62.256 0.00 43.28  ? 136  GLN   B HG2  1 
ATOM   13500 H HG3  . GLN   B  1 110 ? 58.378 27.192  -60.955 0.00 43.45  ? 136  GLN   B HG3  1 
ATOM   13501 H HE21 . GLN   B  1 110 ? 56.210 25.661  -61.161 0.00 55.64  ? 136  GLN   B HE21 1 
ATOM   13502 H HE22 . GLN   B  1 110 ? 54.876 26.550  -61.883 0.00 56.14  ? 136  GLN   B HE22 1 
ATOM   13503 N N    . LEU   B  1 111 ? 62.736 28.062  -63.897 1.00 25.36  ? 137  LEU   B N    1 
ATOM   13504 C CA   . LEU   B  1 111 ? 63.602 28.887  -64.733 1.00 25.35  ? 137  LEU   B CA   1 
ATOM   13505 C C    . LEU   B  1 111 ? 63.420 28.516  -66.206 1.00 25.67  ? 137  LEU   B C    1 
ATOM   13506 O O    . LEU   B  1 111 ? 63.456 27.336  -66.534 1.00 24.62  ? 137  LEU   B O    1 
ATOM   13507 C CB   . LEU   B  1 111 ? 65.077 28.712  -64.339 1.00 25.23  ? 137  LEU   B CB   1 
ATOM   13508 C CG   . LEU   B  1 111 ? 65.456 29.190  -62.937 1.00 26.83  ? 137  LEU   B CG   1 
ATOM   13509 C CD1  . LEU   B  1 111 ? 66.857 28.754  -62.574 1.00 26.98  ? 137  LEU   B CD1  1 
ATOM   13510 C CD2  . LEU   B  1 111 ? 65.330 30.687  -62.797 1.00 27.80  ? 137  LEU   B CD2  1 
ATOM   13511 H H    . LEU   B  1 111 ? 63.236 27.407  -63.304 0.00 30.90  ? 137  LEU   B H    1 
ATOM   13512 H HA   . LEU   B  1 111 ? 63.325 29.928  -64.585 0.00 32.00  ? 137  LEU   B HA   1 
ATOM   13513 H HB2  . LEU   B  1 111 ? 65.331 27.656  -64.404 0.00 31.12  ? 137  LEU   B HB2  1 
ATOM   13514 H HB3  . LEU   B  1 111 ? 65.686 29.271  -65.048 0.00 31.81  ? 137  LEU   B HB3  1 
ATOM   13515 H HG   . LEU   B  1 111 ? 64.760 28.736  -62.237 0.00 33.02  ? 137  LEU   B HG   1 
ATOM   13516 H HD11 . LEU   B  1 111 ? 67.094 29.109  -61.573 0.00 33.41  ? 137  LEU   B HD11 1 
ATOM   13517 H HD12 . LEU   B  1 111 ? 66.909 27.666  -62.605 0.00 33.04  ? 137  LEU   B HD12 1 
ATOM   13518 H HD13 . LEU   B  1 111 ? 67.556 29.181  -63.292 0.00 33.73  ? 137  LEU   B HD13 1 
ATOM   13519 H HD21 . LEU   B  1 111 ? 65.816 31.005  -61.876 0.00 35.04  ? 137  LEU   B HD21 1 
ATOM   13520 H HD22 . LEU   B  1 111 ? 65.803 31.172  -63.650 0.00 35.37  ? 137  LEU   B HD22 1 
ATOM   13521 H HD23 . LEU   B  1 111 ? 64.276 30.955  -62.754 0.00 35.06  ? 137  LEU   B HD23 1 
ATOM   13522 N N    . PRO   B  1 112 ? 63.213 29.495  -67.108 1.00 26.97  ? 138  PRO   B N    1 
ATOM   13523 C CA   . PRO   B  1 112 ? 63.075 29.159  -68.535 1.00 27.67  ? 138  PRO   B CA   1 
ATOM   13524 C C    . PRO   B  1 112 ? 64.406 28.947  -69.259 1.00 28.14  ? 138  PRO   B C    1 
ATOM   13525 O O    . PRO   B  1 112 ? 64.416 28.403  -70.354 1.00 28.51  ? 138  PRO   B O    1 
ATOM   13526 C CB   . PRO   B  1 112 ? 62.369 30.389  -69.098 1.00 28.69  ? 138  PRO   B CB   1 
ATOM   13527 C CG   . PRO   B  1 112 ? 62.920 31.524  -68.273 1.00 28.95  ? 138  PRO   B CG   1 
ATOM   13528 C CD   . PRO   B  1 112 ? 63.152 30.956  -66.892 1.00 27.15  ? 138  PRO   B CD   1 
ATOM   13529 H HA   . PRO   B  1 112 ? 62.434 28.291  -68.680 0.00 35.06  ? 138  PRO   B HA   1 
ATOM   13530 H HB2  . PRO   B  1 112 ? 62.621 30.514  -70.150 0.00 37.43  ? 138  PRO   B HB2  1 
ATOM   13531 H HB3  . PRO   B  1 112 ? 61.293 30.294  -68.960 0.00 37.07  ? 138  PRO   B HB3  1 
ATOM   13532 H HG2  . PRO   B  1 112 ? 63.857 31.868  -68.707 0.00 37.92  ? 138  PRO   B HG2  1 
ATOM   13533 H HG3  . PRO   B  1 112 ? 62.193 32.333  -68.239 0.00 38.00  ? 138  PRO   B HG3  1 
ATOM   13534 H HD2  . PRO   B  1 112 ? 64.094 31.321  -66.486 0.00 35.08  ? 138  PRO   B HD2  1 
ATOM   13535 H HD3  . PRO   B  1 112 ? 62.316 31.211  -66.243 0.00 34.96  ? 138  PRO   B HD3  1 
ATOM   13536 N N    . GLN   B  1 113 ? 65.518 29.423  -68.679 1.00 28.54  ? 139  GLN   B N    1 
ATOM   13537 C CA   . GLN   B  1 113 ? 66.850 29.332  -69.270 1.00 29.69  ? 139  GLN   B CA   1 
ATOM   13538 C C    . GLN   B  1 113 ? 67.894 29.209  -68.169 1.00 29.98  ? 139  GLN   B C    1 
ATOM   13539 O O    . GLN   B  1 113 ? 67.639 29.588  -67.019 1.00 30.19  ? 139  GLN   B O    1 
ATOM   13540 C CB   . GLN   B  1 113 ? 67.170 30.647  -70.039 1.00 32.26  ? 139  GLN   B CB   1 
ATOM   13541 C CG   . GLN   B  1 113 ? 66.296 30.955  -71.250 1.00 37.46  ? 139  GLN   B CG   1 
ATOM   13542 C CD   . GLN   B  1 113 ? 66.499 30.012  -72.414 1.00 43.26  ? 139  GLN   B CD   1 
ATOM   13543 O OE1  . GLN   B  1 113 ? 67.477 29.263  -72.484 1.00 45.84  ? 139  GLN   B OE1  1 
ATOM   13544 N NE2  . GLN   B  1 113 ? 65.560 30.021  -73.354 1.00 43.09  ? 139  GLN   B NE2  1 
ATOM   13545 H H    . GLN   B  1 113 ? 65.535 29.907  -67.788 0.00 36.54  ? 139  GLN   B H    1 
ATOM   13546 H HA   . GLN   B  1 113 ? 66.936 28.479  -69.941 0.00 37.99  ? 139  GLN   B HA   1 
ATOM   13547 H HB2  . GLN   B  1 113 ? 67.053 31.478  -69.345 0.00 42.01  ? 139  GLN   B HB2  1 
ATOM   13548 H HB3  . GLN   B  1 113 ? 68.206 30.610  -70.373 0.00 42.00  ? 139  GLN   B HB3  1 
ATOM   13549 H HG2  . GLN   B  1 113 ? 65.250 30.896  -70.953 0.00 48.34  ? 139  GLN   B HG2  1 
ATOM   13550 H HG3  . GLN   B  1 113 ? 66.524 31.962  -71.596 0.00 48.96  ? 139  GLN   B HG3  1 
ATOM   13551 H HE21 . GLN   B  1 113 ? 64.759 30.639  -73.269 0.00 55.62  ? 139  GLN   B HE21 1 
ATOM   13552 H HE22 . GLN   B  1 113 ? 65.641 29.407  -74.159 0.00 55.46  ? 139  GLN   B HE22 1 
ATOM   13553 N N    . ILE   B  1 114 ? 69.125 28.809  -68.535 1.00 29.56  ? 140  ILE   B N    1 
ATOM   13554 C CA   . ILE   B  1 114 ? 70.243 28.850  -67.591 1.00 30.11  ? 140  ILE   B CA   1 
ATOM   13555 C C    . ILE   B  1 114 ? 70.532 30.361  -67.376 1.00 30.00  ? 140  ILE   B C    1 
ATOM   13556 O O    . ILE   B  1 114 ? 70.602 31.087  -68.378 1.00 30.22  ? 140  ILE   B O    1 
ATOM   13557 C CB   . ILE   B  1 114 ? 71.505 28.150  -68.152 1.00 30.91  ? 140  ILE   B CB   1 
ATOM   13558 C CG1  . ILE   B  1 114 ? 71.222 26.643  -68.377 1.00 32.21  ? 140  ILE   B CG1  1 
ATOM   13559 C CG2  . ILE   B  1 114 ? 72.714 28.393  -67.214 1.00 31.15  ? 140  ILE   B CG2  1 
ATOM   13560 C CD1  . ILE   B  1 114 ? 72.370 25.832  -68.942 1.00 33.51  ? 140  ILE   B CD1  1 
ATOM   13561 H H    . ILE   B  1 114 ? 69.365 28.471  -69.460 0.00 37.90  ? 140  ILE   B H    1 
ATOM   13562 H HA   . ILE   B  1 114 ? 69.962 28.343  -66.670 0.00 38.00  ? 140  ILE   B HA   1 
ATOM   13563 H HB   . ILE   B  1 114 ? 71.733 28.598  -69.118 0.00 39.76  ? 140  ILE   B HB   1 
ATOM   13564 H HG12 . ILE   B  1 114 ? 70.914 26.191  -67.437 0.00 40.11  ? 140  ILE   B HG12 1 
ATOM   13565 H HG13 . ILE   B  1 114 ? 70.413 26.567  -69.102 0.00 40.52  ? 140  ILE   B HG13 1 
ATOM   13566 H HG21 . ILE   B  1 114 ? 73.529 27.716  -67.464 0.00 39.69  ? 140  ILE   B HG21 1 
ATOM   13567 H HG22 . ILE   B  1 114 ? 73.072 29.415  -67.335 0.00 40.15  ? 140  ILE   B HG22 1 
ATOM   13568 H HG23 . ILE   B  1 114 ? 72.403 28.229  -66.184 0.00 39.44  ? 140  ILE   B HG23 1 
ATOM   13569 H HD11 . ILE   B  1 114 ? 71.969 24.939  -69.418 0.00 41.87  ? 140  ILE   B HD11 1 
ATOM   13570 H HD12 . ILE   B  1 114 ? 72.909 26.435  -69.671 0.00 42.47  ? 140  ILE   B HD12 1 
ATOM   13571 H HD13 . ILE   B  1 114 ? 73.036 25.544  -68.130 0.00 41.91  ? 140  ILE   B HD13 1 
ATOM   13572 N N    . PRO   B  1 115 ? 70.624 30.881  -66.132 1.00 29.69  ? 141  PRO   B N    1 
ATOM   13573 C CA   . PRO   B  1 115 ? 70.887 32.322  -65.971 1.00 29.69  ? 141  PRO   B CA   1 
ATOM   13574 C C    . PRO   B  1 115 ? 72.160 32.781  -66.680 1.00 30.11  ? 141  PRO   B C    1 
ATOM   13575 O O    . PRO   B  1 115 ? 73.161 32.069  -66.672 1.00 30.00  ? 141  PRO   B O    1 
ATOM   13576 C CB   . PRO   B  1 115 ? 71.009 32.499  -64.458 1.00 30.23  ? 141  PRO   B CB   1 
ATOM   13577 C CG   . PRO   B  1 115 ? 70.289 31.346  -63.871 1.00 30.78  ? 141  PRO   B CG   1 
ATOM   13578 C CD   . PRO   B  1 115 ? 70.503 30.205  -64.823 1.00 29.08  ? 141  PRO   B CD   1 
ATOM   13579 H HA   . PRO   B  1 115 ? 70.037 32.897  -66.335 0.00 39.15  ? 141  PRO   B HA   1 
ATOM   13580 H HB2  . PRO   B  1 115 ? 72.059 32.487  -64.169 0.00 39.55  ? 141  PRO   B HB2  1 
ATOM   13581 H HB3  . PRO   B  1 115 ? 70.543 33.439  -64.164 0.00 39.73  ? 141  PRO   B HB3  1 
ATOM   13582 H HG2  . PRO   B  1 115 ? 70.702 31.115  -62.890 0.00 39.30  ? 141  PRO   B HG2  1 
ATOM   13583 H HG3  . PRO   B  1 115 ? 69.228 31.580  -63.802 0.00 39.42  ? 141  PRO   B HG3  1 
ATOM   13584 H HD2  . PRO   B  1 115 ? 71.420 29.669  -64.579 0.00 37.06  ? 141  PRO   B HD2  1 
ATOM   13585 H HD3  . PRO   B  1 115 ? 69.630 29.555  -64.789 0.00 36.83  ? 141  PRO   B HD3  1 
ATOM   13586 N N    . SER   B  1 116 ? 72.100 33.957  -67.318 1.00 30.20  ? 142  SER   B N    1 
ATOM   13587 C CA   . SER   B  1 116 ? 73.230 34.544  -68.032 1.00 30.54  ? 142  SER   B CA   1 
ATOM   13588 C C    . SER   B  1 116 ? 74.185 35.239  -67.073 1.00 30.51  ? 142  SER   B C    1 
ATOM   13589 O O    . SER   B  1 116 ? 73.755 35.804  -66.063 1.00 30.86  ? 142  SER   B O    1 
ATOM   13590 C CB   . SER   B  1 116 ? 72.730 35.568  -69.044 1.00 32.36  ? 142  SER   B CB   1 
ATOM   13591 O OG   . SER   B  1 116 ? 71.911 34.957  -70.025 1.00 35.84  ? 142  SER   B OG   1 
ATOM   13592 H H    . SER   B  1 116 ? 71.266 34.533  -67.359 0.00 40.79  ? 142  SER   B H    1 
ATOM   13593 H HA   . SER   B  1 116 ? 73.768 33.766  -68.571 0.00 41.35  ? 142  SER   B HA   1 
ATOM   13594 H HB2  . SER   B  1 116 ? 72.145 36.323  -68.523 0.00 44.74  ? 142  SER   B HB2  1 
ATOM   13595 H HB3  . SER   B  1 116 ? 73.583 36.041  -69.527 0.00 44.41  ? 142  SER   B HB3  1 
ATOM   13596 H HG   . SER   B  1 116 ? 71.296 35.623  -70.429 0.00 48.78  ? 142  SER   B HG   1 
ATOM   13597 N N    . GLY   B  1 117 ? 75.467 35.231  -67.422 1.00 29.68  ? 143  GLY   B N    1 
ATOM   13598 C CA   . GLY   B  1 117 ? 76.503 35.899  -66.650 1.00 29.56  ? 143  GLY   B CA   1 
ATOM   13599 C C    . GLY   B  1 117 ? 76.707 35.353  -65.254 1.00 29.29  ? 143  GLY   B C    1 
ATOM   13600 O O    . GLY   B  1 117 ? 76.833 36.132  -64.308 1.00 29.92  ? 143  GLY   B O    1 
ATOM   13601 H H    . GLY   B  1 117 ? 75.826 34.770  -68.251 0.00 41.08  ? 143  GLY   B H    1 
ATOM   13602 H HA2  . GLY   B  1 117 ? 77.450 35.821  -67.180 0.00 41.60  ? 143  GLY   B HA2  1 
ATOM   13603 H HA3  . GLY   B  1 117 ? 76.257 36.956  -66.562 0.00 41.74  ? 143  GLY   B HA3  1 
ATOM   13604 N N    . LEU   B  1 118 ? 76.735 34.023  -65.106 1.00 28.47  ? 144  LEU   B N    1 
ATOM   13605 C CA   . LEU   B  1 118 ? 76.987 33.408  -63.799 1.00 28.56  ? 144  LEU   B CA   1 
ATOM   13606 C C    . LEU   B  1 118 ? 78.483 33.556  -63.462 1.00 28.90  ? 144  LEU   B C    1 
ATOM   13607 O O    . LEU   B  1 118 ? 79.321 33.614  -64.375 1.00 28.77  ? 144  LEU   B O    1 
ATOM   13608 C CB   . LEU   B  1 118 ? 76.595 31.922  -63.793 1.00 28.60  ? 144  LEU   B CB   1 
ATOM   13609 C CG   . LEU   B  1 118 ? 75.103 31.610  -63.716 1.00 30.09  ? 144  LEU   B CG   1 
ATOM   13610 C CD1  . LEU   B  1 118 ? 74.841 30.142  -64.025 1.00 30.76  ? 144  LEU   B CD1  1 
ATOM   13611 C CD2  . LEU   B  1 118 ? 74.525 31.989  -62.353 1.00 30.38  ? 144  LEU   B CD2  1 
ATOM   13612 H H    . LEU   B  1 118 ? 76.596 33.363  -65.863 0.00 38.84  ? 144  LEU   B H    1 
ATOM   13613 H HA   . LEU   B  1 118 ? 76.404 33.936  -63.047 0.00 38.80  ? 144  LEU   B HA   1 
ATOM   13614 H HB2  . LEU   B  1 118 ? 76.956 31.465  -64.712 0.00 38.16  ? 144  LEU   B HB2  1 
ATOM   13615 H HB3  . LEU   B  1 118 ? 77.078 31.444  -62.942 0.00 37.98  ? 144  LEU   B HB3  1 
ATOM   13616 H HG   . LEU   B  1 118 ? 74.586 32.201  -64.470 0.00 39.74  ? 144  LEU   B HG   1 
ATOM   13617 H HD11 . LEU   B  1 118 ? 73.771 29.948  -63.974 0.00 39.47  ? 144  LEU   B HD11 1 
ATOM   13618 H HD12 . LEU   B  1 118 ? 75.205 29.919  -65.027 0.00 39.87  ? 144  LEU   B HD12 1 
ATOM   13619 H HD13 . LEU   B  1 118 ? 75.365 29.527  -63.294 0.00 39.54  ? 144  LEU   B HD13 1 
ATOM   13620 H HD21 . LEU   B  1 118 ? 73.553 31.511  -62.237 0.00 39.36  ? 144  LEU   B HD21 1 
ATOM   13621 H HD22 . LEU   B  1 118 ? 75.199 31.653  -61.566 0.00 39.65  ? 144  LEU   B HD22 1 
ATOM   13622 H HD23 . LEU   B  1 118 ? 74.401 33.069  -62.304 0.00 40.15  ? 144  LEU   B HD23 1 
ATOM   13623 N N    . PRO   B  1 119 ? 78.845 33.631  -62.165 1.00 28.86  ? 145  PRO   B N    1 
ATOM   13624 C CA   . PRO   B  1 119 ? 80.253 33.829  -61.817 1.00 29.07  ? 145  PRO   B CA   1 
ATOM   13625 C C    . PRO   B  1 119 ? 81.122 32.648  -62.188 1.00 29.54  ? 145  PRO   B C    1 
ATOM   13626 O O    . PRO   B  1 119 ? 80.767 31.502  -61.934 1.00 29.89  ? 145  PRO   B O    1 
ATOM   13627 C CB   . PRO   B  1 119 ? 80.235 34.056  -60.296 1.00 29.24  ? 145  PRO   B CB   1 
ATOM   13628 C CG   . PRO   B  1 119 ? 78.959 33.542  -59.828 1.00 29.49  ? 145  PRO   B CG   1 
ATOM   13629 C CD   . PRO   B  1 119 ? 77.992 33.634  -60.970 1.00 28.29  ? 145  PRO   B CD   1 
ATOM   13630 H HA   . PRO   B  1 119 ? 80.619 34.733  -62.299 0.00 40.70  ? 145  PRO   B HA   1 
ATOM   13631 H HB2  . PRO   B  1 119 ? 81.059 33.511  -59.837 0.00 40.35  ? 145  PRO   B HB2  1 
ATOM   13632 H HB3  . PRO   B  1 119 ? 80.322 35.121  -60.087 0.00 40.85  ? 145  PRO   B HB3  1 
ATOM   13633 H HG2  . PRO   B  1 119 ? 79.073 32.512  -59.495 0.00 39.68  ? 145  PRO   B HG2  1 
ATOM   13634 H HG3  . PRO   B  1 119 ? 78.615 34.159  -59.000 0.00 40.22  ? 145  PRO   B HG3  1 
ATOM   13635 H HD2  . PRO   B  1 119 ? 77.296 32.796  -60.974 0.00 38.02  ? 145  PRO   B HD2  1 
ATOM   13636 H HD3  . PRO   B  1 119 ? 77.491 34.599  -60.939 0.00 38.83  ? 145  PRO   B HD3  1 
ATOM   13637 N N    . GLU   B  1 120 ? 82.289 32.962  -62.736 1.00 29.68  ? 146  GLU   B N    1 
ATOM   13638 C CA   . GLU   B  1 120 ? 83.303 32.007  -63.183 1.00 30.42  ? 146  GLU   B CA   1 
ATOM   13639 C C    . GLU   B  1 120 ? 83.909 31.182  -62.017 1.00 29.77  ? 146  GLU   B C    1 
ATOM   13640 O O    . GLU   B  1 120 ? 84.505 30.133  -62.266 1.00 30.03  ? 146  GLU   B O    1 
ATOM   13641 C CB   . GLU   B  1 120 ? 84.421 32.778  -63.918 1.00 33.69  ? 146  GLU   B CB   1 
ATOM   13642 C CG   . GLU   B  1 120 ? 85.309 31.948  -64.797 1.00 40.67  ? 146  GLU   B CG   1 
ATOM   13643 C CD   . GLU   B  1 120 ? 86.223 32.805  -65.650 1.00 49.34  ? 146  GLU   B CD   1 
ATOM   13644 O OE1  . GLU   B  1 120 ? 85.825 33.143  -66.789 1.00 52.93  ? 146  GLU   B OE1  1 
ATOM   13645 O OE2  . GLU   B  1 120 ? 87.330 33.146  -65.175 1.00 50.40  ? 146  GLU   B OE2  1 
ATOM   13646 H H    . GLU   B  1 120 ? 82.568 33.933  -62.841 0.00 41.69  ? 146  GLU   B H    1 
ATOM   13647 H HA   . GLU   B  1 120 ? 82.845 31.313  -63.886 0.00 41.73  ? 146  GLU   B HA   1 
ATOM   13648 H HB2  . GLU   B  1 120 ? 83.967 33.531  -64.560 0.00 46.94  ? 146  GLU   B HB2  1 
ATOM   13649 H HB3  . GLU   B  1 120 ? 85.052 33.266  -63.176 0.00 47.05  ? 146  GLU   B HB3  1 
ATOM   13650 H HG2  . GLU   B  1 120 ? 85.929 31.305  -64.174 0.00 55.03  ? 146  GLU   B HG2  1 
ATOM   13651 H HG3  . GLU   B  1 120 ? 84.691 31.346  -65.463 0.00 54.81  ? 146  GLU   B HG3  1 
ATOM   13652 N N    . SER   B  1 121 ? 83.728 31.616  -60.765 1.00 28.96  ? 147  SER   B N    1 
ATOM   13653 C CA   . SER   B  1 121 ? 84.228 30.879  -59.610 1.00 28.97  ? 147  SER   B CA   1 
ATOM   13654 C C    . SER   B  1 121 ? 83.378 29.651  -59.261 1.00 28.46  ? 147  SER   B C    1 
ATOM   13655 O O    . SER   B  1 121 ? 83.768 28.913  -58.367 1.00 28.87  ? 147  SER   B O    1 
ATOM   13656 C CB   . SER   B  1 121 ? 84.299 31.804  -58.398 1.00 30.13  ? 147  SER   B CB   1 
ATOM   13657 O OG   . SER   B  1 121 ? 83.018 32.360  -58.129 1.00 31.74  ? 147  SER   B OG   1 
ATOM   13658 H H    . SER   B  1 121 ? 83.255 32.476  -60.507 0.00 40.30  ? 147  SER   B H    1 
ATOM   13659 H HA   . SER   B  1 121 ? 85.241 30.536  -59.813 0.00 40.19  ? 147  SER   B HA   1 
ATOM   13660 H HB2  . SER   B  1 121 ? 84.649 31.248  -57.530 0.00 41.60  ? 147  SER   B HB2  1 
ATOM   13661 H HB3  . SER   B  1 121 ? 84.993 32.615  -58.619 0.00 42.27  ? 147  SER   B HB3  1 
ATOM   13662 H HG   . SER   B  1 121 ? 82.530 31.810  -57.462 0.00 43.03  ? 147  SER   B HG   1 
ATOM   13663 N N    . LEU   B  1 122 ? 82.216 29.435  -59.913 1.00 27.52  ? 148  LEU   B N    1 
ATOM   13664 C CA   . LEU   B  1 122 ? 81.355 28.301  -59.588 1.00 27.38  ? 148  LEU   B CA   1 
ATOM   13665 C C    . LEU   B  1 122 ? 82.007 26.945  -59.822 1.00 26.49  ? 148  LEU   B C    1 
ATOM   13666 O O    . LEU   B  1 122 ? 82.541 26.706  -60.896 1.00 26.75  ? 148  LEU   B O    1 
ATOM   13667 C CB   . LEU   B  1 122 ? 80.046 28.336  -60.410 1.00 27.32  ? 148  LEU   B CB   1 
ATOM   13668 C CG   . LEU   B  1 122 ? 79.029 29.427  -60.075 1.00 28.67  ? 148  LEU   B CG   1 
ATOM   13669 C CD1  . LEU   B  1 122 ? 77.840 29.385  -61.061 1.00 29.03  ? 148  LEU   B CD1  1 
ATOM   13670 C CD2  . LEU   B  1 122 ? 78.527 29.315  -58.630 1.00 28.76  ? 148  LEU   B CD2  1 
ATOM   13671 H H    . LEU   B  1 122 ? 81.841 30.025  -60.648 0.00 37.20  ? 148  LEU   B H    1 
ATOM   13672 H HA   . LEU   B  1 122 ? 81.100 28.365  -58.532 0.00 36.13  ? 148  LEU   B HA   1 
ATOM   13673 H HB2  . LEU   B  1 122 ? 80.304 28.449  -61.462 0.00 36.04  ? 148  LEU   B HB2  1 
ATOM   13674 H HB3  . LEU   B  1 122 ? 79.540 27.382  -60.271 0.00 35.39  ? 148  LEU   B HB3  1 
ATOM   13675 H HG   . LEU   B  1 122 ? 79.525 30.389  -60.192 0.00 38.03  ? 148  LEU   B HG   1 
ATOM   13676 H HD11 . LEU   B  1 122 ? 77.158 30.203  -60.833 0.00 37.84  ? 148  LEU   B HD11 1 
ATOM   13677 H HD12 . LEU   B  1 122 ? 78.220 29.491  -62.076 0.00 37.95  ? 148  LEU   B HD12 1 
ATOM   13678 H HD13 . LEU   B  1 122 ? 77.326 28.431  -60.955 0.00 37.27  ? 148  LEU   B HD13 1 
ATOM   13679 H HD21 . LEU   B  1 122 ? 77.629 29.921  -58.524 0.00 37.37  ? 148  LEU   B HD21 1 
ATOM   13680 H HD22 . LEU   B  1 122 ? 78.306 28.272  -58.409 0.00 36.96  ? 148  LEU   B HD22 1 
ATOM   13681 H HD23 . LEU   B  1 122 ? 79.295 29.688  -57.954 0.00 37.70  ? 148  LEU   B HD23 1 
ATOM   13682 N N    . THR   B  1 123 ? 81.919 26.054  -58.824 1.00 25.27  ? 149  THR   B N    1 
ATOM   13683 C CA   . THR   B  1 123 ? 82.355 24.656  -58.918 1.00 25.17  ? 149  THR   B CA   1 
ATOM   13684 C C    . THR   B  1 123 ? 81.117 23.713  -58.896 1.00 24.38  ? 149  THR   B C    1 
ATOM   13685 O O    . THR   B  1 123 ? 81.223 22.581  -59.348 1.00 23.71  ? 149  THR   B O    1 
ATOM   13686 C CB   . THR   B  1 123 ? 83.321 24.297  -57.798 1.00 26.86  ? 149  THR   B CB   1 
ATOM   13687 O OG1  . THR   B  1 123 ? 82.638 24.426  -56.552 1.00 28.60  ? 149  THR   B OG1  1 
ATOM   13688 C CG2  . THR   B  1 123 ? 84.588 25.160  -57.814 1.00 27.49  ? 149  THR   B CG2  1 
ATOM   13689 H H    . THR   B  1 123 ? 81.550 26.277  -57.905 0.00 33.04  ? 149  THR   B H    1 
ATOM   13690 H HA   . THR   B  1 123 ? 82.909 24.494  -59.840 0.00 32.92  ? 149  THR   B HA   1 
ATOM   13691 H HB   . THR   B  1 123 ? 83.639 23.265  -57.938 0.00 34.79  ? 149  THR   B HB   1 
ATOM   13692 H HG1  . THR   B  1 123 ? 82.225 23.569  -56.262 0.00 36.44  ? 149  THR   B HG1  1 
ATOM   13693 H HG21 . THR   B  1 123 ? 85.279 24.813  -57.047 0.00 36.52  ? 149  THR   B HG21 1 
ATOM   13694 H HG22 . THR   B  1 123 ? 85.072 25.093  -58.787 0.00 36.56  ? 149  THR   B HG22 1 
ATOM   13695 H HG23 . THR   B  1 123 ? 84.335 26.200  -57.613 0.00 36.59  ? 149  THR   B HG23 1 
ATOM   13696 N N    . GLU   B  1 124 ? 79.963 24.157  -58.349 1.00 24.34  ? 150  GLU   B N    1 
ATOM   13697 C CA   . GLU   B  1 124 ? 78.760 23.335  -58.279 1.00 24.60  ? 150  GLU   B CA   1 
ATOM   13698 C C    . GLU   B  1 124 ? 77.551 24.178  -58.638 1.00 24.11  ? 150  GLU   B C    1 
ATOM   13699 O O    . GLU   B  1 124 ? 77.321 25.216  -58.016 1.00 24.34  ? 150  GLU   B O    1 
ATOM   13700 C CB   . GLU   B  1 124 ? 78.617 22.752  -56.860 1.00 27.86  ? 150  GLU   B CB   1 
ATOM   13701 C CG   . GLU   B  1 124 ? 79.675 21.694  -56.562 1.00 36.10  ? 150  GLU   B CG   1 
ATOM   13702 C CD   . GLU   B  1 124 ? 80.321 21.736  -55.194 1.00 46.39  ? 150  GLU   B CD   1 
ATOM   13703 O OE1  . GLU   B  1 124 ? 81.496 22.164  -55.103 1.00 49.24  ? 150  GLU   B OE1  1 
ATOM   13704 O OE2  . GLU   B  1 124 ? 79.661 21.314  -54.216 1.00 47.99  ? 150  GLU   B OE2  1 
ATOM   13705 H H    . GLU   B  1 124 ? 79.830 25.072  -57.930 0.00 31.06  ? 150  GLU   B H    1 
ATOM   13706 H HA   . GLU   B  1 124 ? 78.821 22.509  -58.987 0.00 30.45  ? 150  GLU   B HA   1 
ATOM   13707 H HB2  . GLU   B  1 124 ? 78.726 23.554  -56.132 0.00 34.48  ? 150  GLU   B HB2  1 
ATOM   13708 H HB3  . GLU   B  1 124 ? 77.637 22.288  -56.762 0.00 33.88  ? 150  GLU   B HB3  1 
ATOM   13709 H HG2  . GLU   B  1 124 ? 79.194 20.721  -56.637 0.00 43.83  ? 150  GLU   B HG2  1 
ATOM   13710 H HG3  . GLU   B  1 124 ? 80.469 21.759  -57.305 0.00 44.47  ? 150  GLU   B HG3  1 
ATOM   13711 N N    . LEU   B  1 125 ? 76.783 23.741  -59.649 1.00 23.36  ? 151  LEU   B N    1 
ATOM   13712 C CA   . LEU   B  1 125 ? 75.593 24.453  -60.108 1.00 23.09  ? 151  LEU   B CA   1 
ATOM   13713 C C    . LEU   B  1 125 ? 74.479 23.445  -60.242 1.00 22.81  ? 151  LEU   B C    1 
ATOM   13714 O O    . LEU   B  1 125 ? 74.615 22.497  -61.022 1.00 22.35  ? 151  LEU   B O    1 
ATOM   13715 C CB   . LEU   B  1 125 ? 75.879 25.102  -61.485 1.00 23.52  ? 151  LEU   B CB   1 
ATOM   13716 C CG   . LEU   B  1 125 ? 74.695 25.772  -62.210 1.00 24.52  ? 151  LEU   B CG   1 
ATOM   13717 C CD1  . LEU   B  1 125 ? 74.080 26.886  -61.367 1.00 24.72  ? 151  LEU   B CD1  1 
ATOM   13718 C CD2  . LEU   B  1 125 ? 75.138 26.329  -63.567 1.00 25.33  ? 151  LEU   B CD2  1 
ATOM   13719 H H    . LEU   B  1 125 ? 76.961 22.892  -60.176 0.00 28.67  ? 151  LEU   B H    1 
ATOM   13720 H HA   . LEU   B  1 125 ? 75.293 25.227  -59.404 0.00 28.53  ? 151  LEU   B HA   1 
ATOM   13721 H HB2  . LEU   B  1 125 ? 76.642 25.867  -61.346 0.00 29.71  ? 151  LEU   B HB2  1 
ATOM   13722 H HB3  . LEU   B  1 125 ? 76.265 24.331  -62.149 0.00 29.27  ? 151  LEU   B HB3  1 
ATOM   13723 H HG   . LEU   B  1 125 ? 73.918 25.035  -62.409 0.00 30.22  ? 151  LEU   B HG   1 
ATOM   13724 H HD11 . LEU   B  1 125 ? 73.330 27.405  -61.962 0.00 31.02  ? 151  LEU   B HD11 1 
ATOM   13725 H HD12 . LEU   B  1 125 ? 73.612 26.452  -60.485 0.00 30.61  ? 151  LEU   B HD12 1 
ATOM   13726 H HD13 . LEU   B  1 125 ? 74.866 27.579  -61.069 0.00 31.28  ? 151  LEU   B HD13 1 
ATOM   13727 H HD21 . LEU   B  1 125 ? 74.282 26.789  -64.060 0.00 32.00  ? 151  LEU   B HD21 1 
ATOM   13728 H HD22 . LEU   B  1 125 ? 75.917 27.073  -63.408 0.00 32.33  ? 151  LEU   B HD22 1 
ATOM   13729 H HD23 . LEU   B  1 125 ? 75.523 25.513  -64.177 0.00 31.89  ? 151  LEU   B HD23 1 
ATOM   13730 N N    . SER   B  1 126 ? 73.369 23.622  -59.489 1.00 22.57  ? 152  SER   B N    1 
ATOM   13731 C CA   . SER   B  1 126 ? 72.238 22.716  -59.600 1.00 22.73  ? 152  SER   B CA   1 
ATOM   13732 C C    . SER   B  1 126 ? 71.041 23.450  -60.163 1.00 22.80  ? 152  SER   B C    1 
ATOM   13733 O O    . SER   B  1 126 ? 70.596 24.438  -59.583 1.00 23.41  ? 152  SER   B O    1 
ATOM   13734 C CB   . SER   B  1 126 ? 71.901 22.077  -58.257 1.00 24.33  ? 152  SER   B CB   1 
ATOM   13735 O OG   . SER   B  1 126 ? 70.915 21.075  -58.444 1.00 26.64  ? 152  SER   B OG   1 
ATOM   13736 H H    . SER   B  1 126 ? 73.235 24.368  -58.814 0.00 27.20  ? 152  SER   B H    1 
ATOM   13737 H HA   . SER   B  1 126 ? 72.495 21.914  -60.289 0.00 26.75  ? 152  SER   B HA   1 
ATOM   13738 H HB2  . SER   B  1 126 ? 72.799 21.626  -57.839 0.00 28.43  ? 152  SER   B HB2  1 
ATOM   13739 H HB3  . SER   B  1 126 ? 71.510 22.837  -57.582 0.00 28.48  ? 152  SER   B HB3  1 
ATOM   13740 H HG   . SER   B  1 126 ? 70.685 20.657  -57.573 0.00 30.59  ? 152  SER   B HG   1 
ATOM   13741 N N    . LEU   B  1 127 ? 70.533 22.980  -61.296 1.00 22.37  ? 153  LEU   B N    1 
ATOM   13742 C CA   . LEU   B  1 127 ? 69.362 23.529  -61.966 1.00 22.94  ? 153  LEU   B CA   1 
ATOM   13743 C C    . LEU   B  1 127 ? 68.286 22.439  -62.157 1.00 23.16  ? 153  LEU   B C    1 
ATOM   13744 O O    . LEU   B  1 127 ? 67.488 22.507  -63.098 1.00 24.33  ? 153  LEU   B O    1 
ATOM   13745 C CB   . LEU   B  1 127 ? 69.821 24.132  -63.299 1.00 23.44  ? 153  LEU   B CB   1 
ATOM   13746 C CG   . LEU   B  1 127 ? 70.714 25.381  -63.184 1.00 25.24  ? 153  LEU   B CG   1 
ATOM   13747 C CD1  . LEU   B  1 127 ? 71.554 25.542  -64.425 1.00 25.99  ? 153  LEU   B CD1  1 
ATOM   13748 C CD2  . LEU   B  1 127 ? 69.875 26.634  -62.947 1.00 25.66  ? 153  LEU   B CD2  1 
ATOM   13749 H H    . LEU   B  1 127 ? 70.915 22.184  -61.798 0.00 26.30  ? 153  LEU   B H    1 
ATOM   13750 H HA   . LEU   B  1 127 ? 68.912 24.320  -61.368 0.00 27.21  ? 153  LEU   B HA   1 
ATOM   13751 H HB2  . LEU   B  1 127 ? 70.399 23.374  -63.824 0.00 28.10  ? 153  LEU   B HB2  1 
ATOM   13752 H HB3  . LEU   B  1 127 ? 68.953 24.418  -63.890 0.00 28.21  ? 153  LEU   B HB3  1 
ATOM   13753 H HG   . LEU   B  1 127 ? 71.405 25.282  -62.347 0.00 30.71  ? 153  LEU   B HG   1 
ATOM   13754 H HD11 . LEU   B  1 127 ? 71.988 26.541  -64.441 0.00 32.38  ? 153  LEU   B HD11 1 
ATOM   13755 H HD12 . LEU   B  1 127 ? 72.345 24.794  -64.416 0.00 31.91  ? 153  LEU   B HD12 1 
ATOM   13756 H HD13 . LEU   B  1 127 ? 70.911 25.391  -65.290 0.00 32.02  ? 153  LEU   B HD13 1 
ATOM   13757 H HD21 . LEU   B  1 127 ? 70.541 27.483  -62.800 0.00 31.84  ? 153  LEU   B HD21 1 
ATOM   13758 H HD22 . LEU   B  1 127 ? 69.246 26.805  -63.820 0.00 31.61  ? 153  LEU   B HD22 1 
ATOM   13759 H HD23 . LEU   B  1 127 ? 69.251 26.495  -62.066 0.00 31.25  ? 153  LEU   B HD23 1 
ATOM   13760 N N    . ILE   B  1 128 ? 68.205 21.489  -61.207 1.00 22.35  ? 154  ILE   B N    1 
ATOM   13761 C CA   . ILE   B  1 128 ? 67.227 20.398  -61.231 1.00 22.52  ? 154  ILE   B CA   1 
ATOM   13762 C C    . ILE   B  1 128 ? 65.809 20.962  -61.149 1.00 22.90  ? 154  ILE   B C    1 
ATOM   13763 O O    . ILE   B  1 128 ? 65.580 21.946  -60.460 1.00 23.59  ? 154  ILE   B O    1 
ATOM   13764 C CB   . ILE   B  1 128 ? 67.509 19.405  -60.047 1.00 22.83  ? 154  ILE   B CB   1 
ATOM   13765 C CG1  . ILE   B  1 128 ? 68.823 18.620  -60.281 1.00 23.34  ? 154  ILE   B CG1  1 
ATOM   13766 C CG2  . ILE   B  1 128 ? 66.333 18.439  -59.801 1.00 22.54  ? 154  ILE   B CG2  1 
ATOM   13767 C CD1  . ILE   B  1 128 ? 69.359 17.897  -58.993 1.00 24.39  ? 154  ILE   B CD1  1 
ATOM   13768 H H    . ILE   B  1 128 ? 68.802 21.471  -60.387 0.00 25.63  ? 154  ILE   B H    1 
ATOM   13769 H HA   . ILE   B  1 128 ? 67.330 19.850  -62.166 0.00 25.55  ? 154  ILE   B HA   1 
ATOM   13770 H HB   . ILE   B  1 128 ? 67.622 19.974  -59.126 0.00 25.57  ? 154  ILE   B HB   1 
ATOM   13771 H HG12 . ILE   B  1 128 ? 68.648 17.861  -61.042 0.00 26.14  ? 154  ILE   B HG12 1 
ATOM   13772 H HG13 . ILE   B  1 128 ? 69.599 19.306  -60.617 0.00 26.48  ? 154  ILE   B HG13 1 
ATOM   13773 H HG21 . ILE   B  1 128 ? 66.570 17.818  -58.939 0.00 24.66  ? 154  ILE   B HG21 1 
ATOM   13774 H HG22 . ILE   B  1 128 ? 65.422 18.991  -59.576 0.00 24.85  ? 154  ILE   B HG22 1 
ATOM   13775 H HG23 . ILE   B  1 128 ? 66.191 17.816  -60.683 0.00 24.86  ? 154  ILE   B HG23 1 
ATOM   13776 H HD11 . ILE   B  1 128 ? 70.383 17.562  -59.147 0.00 27.37  ? 154  ILE   B HD11 1 
ATOM   13777 H HD12 . ILE   B  1 128 ? 69.319 18.593  -58.157 0.00 27.28  ? 154  ILE   B HD12 1 
ATOM   13778 H HD13 . ILE   B  1 128 ? 68.732 17.030  -58.787 0.00 26.99  ? 154  ILE   B HD13 1 
ATOM   13779 N N    . GLN   B  1 129 ? 64.856 20.327  -61.831 1.00 22.41  ? 155  GLN   B N    1 
ATOM   13780 C CA   . GLN   B  1 129 ? 63.447 20.692  -61.746 1.00 22.17  ? 155  GLN   B CA   1 
ATOM   13781 C C    . GLN   B  1 129 ? 63.142 22.147  -62.141 1.00 22.78  ? 155  GLN   B C    1 
ATOM   13782 O O    . GLN   B  1 129 ? 62.469 22.876  -61.413 1.00 23.19  ? 155  GLN   B O    1 
ATOM   13783 C CB   . GLN   B  1 129 ? 62.882 20.356  -60.330 1.00 22.68  ? 155  GLN   B CB   1 
ATOM   13784 C CG   . GLN   B  1 129 ? 62.464 18.883  -60.157 1.00 24.28  ? 155  GLN   B CG   1 
ATOM   13785 C CD   . GLN   B  1 129 ? 61.207 18.545  -60.954 1.00 27.08  ? 155  GLN   B CD   1 
ATOM   13786 O OE1  . GLN   B  1 129 ? 60.575 19.408  -61.590 1.00 26.47  ? 155  GLN   B OE1  1 
ATOM   13787 N NE2  . GLN   B  1 129 ? 60.807 17.270  -60.948 1.00 27.53  ? 155  GLN   B NE2  1 
ATOM   13788 H H    . GLN   B  1 129 ? 65.028 19.542  -62.451 0.00 25.20  ? 155  GLN   B H    1 
ATOM   13789 H HA   . GLN   B  1 129 ? 62.925 20.088  -62.486 0.00 24.92  ? 155  GLN   B HA   1 
ATOM   13790 H HB2  . GLN   B  1 129 ? 63.635 20.566  -59.573 0.00 25.23  ? 155  GLN   B HB2  1 
ATOM   13791 H HB3  . GLN   B  1 129 ? 61.999 20.958  -60.122 0.00 25.31  ? 155  GLN   B HB3  1 
ATOM   13792 H HG2  . GLN   B  1 129 ? 63.267 18.236  -60.509 0.00 26.77  ? 155  GLN   B HG2  1 
ATOM   13793 H HG3  . GLN   B  1 129 ? 62.260 18.692  -59.105 0.00 26.61  ? 155  GLN   B HG3  1 
ATOM   13794 H HE21 . GLN   B  1 129 ? 61.332 16.575  -60.429 0.00 30.29  ? 155  GLN   B HE21 1 
ATOM   13795 H HE22 . GLN   B  1 129 ? 59.975 16.998  -61.462 0.00 30.50  ? 155  GLN   B HE22 1 
ATOM   13796 N N    . ASN   B  1 130 ? 63.575 22.531  -63.334 1.00 22.93  ? 156  ASN   B N    1 
ATOM   13797 C CA   . ASN   B  1 130 ? 63.259 23.833  -63.917 1.00 22.97  ? 156  ASN   B CA   1 
ATOM   13798 C C    . ASN   B  1 130 ? 62.607 23.591  -65.313 1.00 23.67  ? 156  ASN   B C    1 
ATOM   13799 O O    . ASN   B  1 130 ? 62.159 22.470  -65.574 1.00 23.39  ? 156  ASN   B O    1 
ATOM   13800 C CB   . ASN   B  1 130 ? 64.533 24.692  -63.961 1.00 23.25  ? 156  ASN   B CB   1 
ATOM   13801 C CG   . ASN   B  1 130 ? 64.875 25.248  -62.611 1.00 25.03  ? 156  ASN   B CG   1 
ATOM   13802 O OD1  . ASN   B  1 130 ? 64.149 26.067  -62.069 1.00 25.63  ? 156  ASN   B OD1  1 
ATOM   13803 N ND2  . ASN   B  1 130 ? 65.977 24.833  -62.048 1.00 25.33  ? 156  ASN   B ND2  1 
ATOM   13804 H H    . ASN   B  1 130 ? 64.158 21.952  -63.931 0.00 26.57  ? 156  ASN   B H    1 
ATOM   13805 H HA   . ASN   B  1 130 ? 62.509 24.351  -63.321 0.00 27.07  ? 156  ASN   B HA   1 
ATOM   13806 H HB2  . ASN   B  1 130 ? 65.356 24.078  -64.322 0.00 27.64  ? 156  ASN   B HB2  1 
ATOM   13807 H HB3  . ASN   B  1 130 ? 64.394 25.542  -64.627 0.00 28.06  ? 156  ASN   B HB3  1 
ATOM   13808 H HD21 . ASN   B  1 130 ? 66.239 25.190  -61.135 0.00 30.02  ? 156  ASN   B HD21 1 
ATOM   13809 H HD22 . ASN   B  1 130 ? 66.578 24.165  -62.517 0.00 29.95  ? 156  ASN   B HD22 1 
ATOM   13810 N N    . ASN   B  1 131 ? 62.478 24.633  -66.163 1.00 23.75  ? 157  ASN   B N    1 
ATOM   13811 C CA   . ASN   B  1 131 ? 61.917 24.520  -67.511 1.00 24.33  ? 157  ASN   B CA   1 
ATOM   13812 C C    . ASN   B  1 131 ? 63.006 24.845  -68.541 1.00 24.81  ? 157  ASN   B C    1 
ATOM   13813 O O    . ASN   B  1 131 ? 62.730 25.511  -69.537 1.00 25.77  ? 157  ASN   B O    1 
ATOM   13814 C CB   . ASN   B  1 131 ? 60.738 25.489  -67.647 1.00 25.67  ? 157  ASN   B CB   1 
ATOM   13815 C CG   . ASN   B  1 131 ? 59.652 25.247  -66.617 1.00 28.62  ? 157  ASN   B CG   1 
ATOM   13816 O OD1  . ASN   B  1 131 ? 59.427 24.117  -66.168 1.00 28.77  ? 157  ASN   B OD1  1 
ATOM   13817 N ND2  . ASN   B  1 131 ? 58.949 26.299  -66.221 1.00 29.25  ? 157  ASN   B ND2  1 
ATOM   13818 H H    . ASN   B  1 131 ? 62.724 25.591  -65.932 0.00 28.88  ? 157  ASN   B H    1 
ATOM   13819 H HA   . ASN   B  1 131 ? 61.555 23.512  -67.706 0.00 29.38  ? 157  ASN   B HA   1 
ATOM   13820 H HB2  . ASN   B  1 131 ? 61.107 26.507  -67.529 0.00 31.81  ? 157  ASN   B HB2  1 
ATOM   13821 H HB3  . ASN   B  1 131 ? 60.285 25.367  -68.630 0.00 31.75  ? 157  ASN   B HB3  1 
ATOM   13822 H HD21 . ASN   B  1 131 ? 58.211 26.183  -65.535 0.00 35.63  ? 157  ASN   B HD21 1 
ATOM   13823 H HD22 . ASN   B  1 131 ? 59.140 27.218  -66.609 0.00 36.17  ? 157  ASN   B HD22 1 
ATOM   13824 N N    . ILE   B  1 132 ? 64.237 24.374  -68.306 1.00 24.19  ? 158  ILE   B N    1 
ATOM   13825 C CA   . ILE   B  1 132 ? 65.378 24.645  -69.172 1.00 24.96  ? 158  ILE   B CA   1 
ATOM   13826 C C    . ILE   B  1 132 ? 65.457 23.565  -70.236 1.00 26.54  ? 158  ILE   B C    1 
ATOM   13827 O O    . ILE   B  1 132 ? 65.690 22.400  -69.910 1.00 26.75  ? 158  ILE   B O    1 
ATOM   13828 C CB   . ILE   B  1 132 ? 66.687 24.713  -68.347 1.00 25.10  ? 158  ILE   B CB   1 
ATOM   13829 C CG1  . ILE   B  1 132 ? 66.626 25.877  -67.333 1.00 25.41  ? 158  ILE   B CG1  1 
ATOM   13830 C CG2  . ILE   B  1 132 ? 67.900 24.874  -69.284 1.00 25.56  ? 158  ILE   B CG2  1 
ATOM   13831 C CD1  . ILE   B  1 132 ? 67.711 25.817  -66.242 1.00 26.27  ? 158  ILE   B CD1  1 
ATOM   13832 H H    . ILE   B  1 132 ? 64.474 23.776  -67.521 0.00 29.29  ? 158  ILE   B H    1 
ATOM   13833 H HA   . ILE   B  1 132 ? 65.257 25.616  -69.651 0.00 31.26  ? 158  ILE   B HA   1 
ATOM   13834 H HB   . ILE   B  1 132 ? 66.801 23.779  -67.798 0.00 30.57  ? 158  ILE   B HB   1 
ATOM   13835 H HG12 . ILE   B  1 132 ? 66.754 26.816  -67.871 0.00 31.83  ? 158  ILE   B HG12 1 
ATOM   13836 H HG13 . ILE   B  1 132 ? 65.664 25.874  -66.824 0.00 31.26  ? 158  ILE   B HG13 1 
ATOM   13837 H HG21 . ILE   B  1 132 ? 68.798 24.988  -68.678 0.00 31.82  ? 158  ILE   B HG21 1 
ATOM   13838 H HG22 . ILE   B  1 132 ? 68.020 23.989  -69.905 0.00 31.75  ? 158  ILE   B HG22 1 
ATOM   13839 H HG23 . ILE   B  1 132 ? 67.756 25.754  -69.909 0.00 32.22  ? 158  ILE   B HG23 1 
ATOM   13840 H HD11 . ILE   B  1 132 ? 67.437 26.498  -65.439 0.00 32.33  ? 158  ILE   B HD11 1 
ATOM   13841 H HD12 . ILE   B  1 132 ? 67.775 24.798  -65.864 0.00 31.93  ? 158  ILE   B HD12 1 
ATOM   13842 H HD13 . ILE   B  1 132 ? 68.667 26.123  -66.666 0.00 32.55  ? 158  ILE   B HD13 1 
ATOM   13843 N N    . TYR   B  1 133 ? 65.249 23.938  -71.499 1.00 27.06  ? 159  TYR   B N    1 
ATOM   13844 C CA   . TYR   B  1 133 ? 65.290 23.003  -72.632 1.00 28.04  ? 159  TYR   B CA   1 
ATOM   13845 C C    . TYR   B  1 133 ? 66.433 23.328  -73.610 1.00 29.41  ? 159  TYR   B C    1 
ATOM   13846 O O    . TYR   B  1 133 ? 66.490 22.719  -74.663 1.00 30.66  ? 159  TYR   B O    1 
ATOM   13847 C CB   . TYR   B  1 133 ? 63.933 23.014  -73.384 1.00 28.03  ? 159  TYR   B CB   1 
ATOM   13848 C CG   . TYR   B  1 133 ? 62.734 22.979  -72.457 1.00 28.63  ? 159  TYR   B CG   1 
ATOM   13849 C CD1  . TYR   B  1 133 ? 62.666 22.070  -71.414 1.00 29.46  ? 159  TYR   B CD1  1 
ATOM   13850 C CD2  . TYR   B  1 133 ? 61.707 23.906  -72.578 1.00 29.78  ? 159  TYR   B CD2  1 
ATOM   13851 C CE1  . TYR   B  1 133 ? 61.649 22.126  -70.472 1.00 30.60  ? 159  TYR   B CE1  1 
ATOM   13852 C CE2  . TYR   B  1 133 ? 60.631 23.913  -71.692 1.00 30.43  ? 159  TYR   B CE2  1 
ATOM   13853 C CZ   . TYR   B  1 133 ? 60.618 23.033  -70.624 1.00 31.69  ? 159  TYR   B CZ   1 
ATOM   13854 O OH   . TYR   B  1 133 ? 59.583 23.004  -69.713 1.00 33.27  ? 159  TYR   B OH   1 
ATOM   13855 H H    . TYR   B  1 133 ? 65.044 24.890  -71.785 0.00 34.12  ? 159  TYR   B H    1 
ATOM   13856 H HA   . TYR   B  1 133 ? 65.450 21.985  -72.281 0.00 34.74  ? 159  TYR   B HA   1 
ATOM   13857 H HB2  . TYR   B  1 133 ? 63.875 23.921  -73.984 0.00 35.66  ? 159  TYR   B HB2  1 
ATOM   13858 H HB3  . TYR   B  1 133 ? 63.881 22.140  -74.031 0.00 35.24  ? 159  TYR   B HB3  1 
ATOM   13859 H HD1  . TYR   B  1 133 ? 63.478 21.381  -71.258 0.00 35.96  ? 159  TYR   B HD1  1 
ATOM   13860 H HD2  . TYR   B  1 133 ? 61.726 24.619  -73.386 0.00 37.77  ? 159  TYR   B HD2  1 
ATOM   13861 H HE1  . TYR   B  1 133 ? 61.614 21.401  -69.676 0.00 36.89  ? 159  TYR   B HE1  1 
ATOM   13862 H HE2  . TYR   B  1 133 ? 59.849 24.645  -71.807 0.00 38.15  ? 159  TYR   B HE2  1 
ATOM   13863 H HH   . TYR   B  1 133 ? 58.908 23.700  -69.926 0.00 40.81  ? 159  TYR   B HH   1 
ATOM   13864 N N    . ASN   B  1 134 ? 67.325 24.271  -73.287 1.00 29.46  ? 160  ASN   B N    1 
ATOM   13865 C CA   . ASN   B  1 134 ? 68.422 24.663  -74.147 1.00 30.60  ? 160  ASN   B CA   1 
ATOM   13866 C C    . ASN   B  1 134 ? 69.665 24.826  -73.274 1.00 30.58  ? 160  ASN   B C    1 
ATOM   13867 O O    . ASN   B  1 134 ? 69.640 25.610  -72.326 1.00 30.78  ? 160  ASN   B O    1 
ATOM   13868 C CB   . ASN   B  1 134 ? 68.054 25.990  -74.836 1.00 32.80  ? 160  ASN   B CB   1 
ATOM   13869 C CG   . ASN   B  1 134 ? 68.820 26.297  -76.095 1.00 37.93  ? 160  ASN   B CG   1 
ATOM   13870 O OD1  . ASN   B  1 134 ? 69.561 25.465  -76.641 1.00 38.67  ? 160  ASN   B OD1  1 
ATOM   13871 N ND2  . ASN   B  1 134 ? 68.661 27.517  -76.583 1.00 39.97  ? 160  ASN   B ND2  1 
ATOM   13872 H H    . ASN   B  1 134 ? 67.322 24.797  -72.420 0.00 37.25  ? 160  ASN   B H    1 
ATOM   13873 H HA   . ASN   B  1 134 ? 68.611 23.899  -74.899 0.00 39.20  ? 160  ASN   B HA   1 
ATOM   13874 H HB2  . ASN   B  1 134 ? 66.999 25.954  -75.103 0.00 42.35  ? 160  ASN   B HB2  1 
ATOM   13875 H HB3  . ASN   B  1 134 ? 68.223 26.814  -74.146 0.00 42.38  ? 160  ASN   B HB3  1 
ATOM   13876 H HD21 . ASN   B  1 134 ? 69.147 27.792  -77.431 0.00 52.37  ? 160  ASN   B HD21 1 
ATOM   13877 H HD22 . ASN   B  1 134 ? 68.051 28.178  -76.112 0.00 51.99  ? 160  ASN   B HD22 1 
ATOM   13878 N N    . ILE   B  1 135 ? 70.726 24.049  -73.556 1.00 30.31  ? 161  ILE   B N    1 
ATOM   13879 C CA   . ILE   B  1 135 ? 72.001 24.107  -72.835 1.00 30.41  ? 161  ILE   B CA   1 
ATOM   13880 C C    . ILE   B  1 135 ? 72.984 24.737  -73.826 1.00 30.68  ? 161  ILE   B C    1 
ATOM   13881 O O    . ILE   B  1 135 ? 73.386 24.079  -74.782 1.00 30.06  ? 161  ILE   B O    1 
ATOM   13882 C CB   . ILE   B  1 135 ? 72.460 22.689  -72.381 1.00 30.69  ? 161  ILE   B CB   1 
ATOM   13883 C CG1  . ILE   B  1 135 ? 71.306 21.882  -71.713 1.00 31.59  ? 161  ILE   B CG1  1 
ATOM   13884 C CG2  . ILE   B  1 135 ? 73.702 22.771  -71.483 1.00 30.93  ? 161  ILE   B CG2  1 
ATOM   13885 C CD1  . ILE   B  1 135 ? 70.635 22.514  -70.590 1.00 33.34  ? 161  ILE   B CD1  1 
ATOM   13886 H H    . ILE   B  1 135 ? 70.733 23.354  -74.295 0.00 38.72  ? 161  ILE   B H    1 
ATOM   13887 H HA   . ILE   B  1 135 ? 71.927 24.740  -71.953 0.00 38.68  ? 161  ILE   B HA   1 
ATOM   13888 H HB   . ILE   B  1 135 ? 72.753 22.129  -73.267 0.00 38.85  ? 161  ILE   B HB   1 
ATOM   13889 H HG12 . ILE   B  1 135 ? 70.548 21.664  -72.464 0.00 39.35  ? 161  ILE   B HG12 1 
ATOM   13890 H HG13 . ILE   B  1 135 ? 71.717 20.942  -71.345 0.00 39.04  ? 161  ILE   B HG13 1 
ATOM   13891 H HG21 . ILE   B  1 135 ? 73.895 21.788  -71.055 0.00 38.67  ? 161  ILE   B HG21 1 
ATOM   13892 H HG22 . ILE   B  1 135 ? 74.559 23.080  -72.078 0.00 39.31  ? 161  ILE   B HG22 1 
ATOM   13893 H HG23 . ILE   B  1 135 ? 73.520 23.492  -70.688 0.00 38.90  ? 161  ILE   B HG23 1 
ATOM   13894 H HD11 . ILE   B  1 135 ? 69.906 21.817  -70.179 0.00 40.82  ? 161  ILE   B HD11 1 
ATOM   13895 H HD12 . ILE   B  1 135 ? 71.382 22.753  -69.836 0.00 41.12  ? 161  ILE   B HD12 1 
ATOM   13896 H HD13 . ILE   B  1 135 ? 70.131 23.420  -70.922 0.00 41.40  ? 161  ILE   B HD13 1 
ATOM   13897 N N    . THR   B  1 136 ? 73.330 26.023  -73.624 1.00 31.12  ? 162  THR   B N    1 
ATOM   13898 C CA   . THR   B  1 136 ? 74.160 26.771  -74.563 1.00 32.46  ? 162  THR   B CA   1 
ATOM   13899 C C    . THR   B  1 136 ? 75.515 27.175  -74.008 1.00 32.40  ? 162  THR   B C    1 
ATOM   13900 O O    . THR   B  1 136 ? 75.695 27.260  -72.789 1.00 32.09  ? 162  THR   B O    1 
ATOM   13901 C CB   . THR   B  1 136 ? 73.394 28.030  -75.023 1.00 35.11  ? 162  THR   B CB   1 
ATOM   13902 O OG1  . THR   B  1 136 ? 73.278 28.934  -73.922 1.00 37.05  ? 162  THR   B OG1  1 
ATOM   13903 C CG2  . THR   B  1 136 ? 72.013 27.707  -75.571 1.00 35.40  ? 162  THR   B CG2  1 
ATOM   13904 H H    . THR   B  1 136 ? 73.045 26.570  -72.818 0.00 40.42  ? 162  THR   B H    1 
ATOM   13905 H HA   . THR   B  1 136 ? 74.344 26.175  -75.455 0.00 42.81  ? 162  THR   B HA   1 
ATOM   13906 H HB   . THR   B  1 136 ? 73.961 28.514  -75.817 0.00 46.74  ? 162  THR   B HB   1 
ATOM   13907 H HG1  . THR   B  1 136 ? 72.779 29.745  -74.202 0.00 48.87  ? 162  THR   B HG1  1 
ATOM   13908 H HG21 . THR   B  1 136 ? 71.593 28.589  -76.053 0.00 46.90  ? 162  THR   B HG21 1 
ATOM   13909 H HG22 . THR   B  1 136 ? 72.079 26.902  -76.301 0.00 46.51  ? 162  THR   B HG22 1 
ATOM   13910 H HG23 . THR   B  1 136 ? 71.348 27.402  -74.765 0.00 46.12  ? 162  THR   B HG23 1 
ATOM   13911 N N    . LYS   B  1 137 ? 76.461 27.458  -74.921 1.00 32.63  ? 163  LYS   B N    1 
ATOM   13912 C CA   . LYS   B  1 137 ? 77.801 27.936  -74.594 1.00 33.26  ? 163  LYS   B CA   1 
ATOM   13913 C C    . LYS   B  1 137 ? 77.732 29.259  -73.845 1.00 33.86  ? 163  LYS   B C    1 
ATOM   13914 O O    . LYS   B  1 137 ? 78.519 29.481  -72.925 1.00 33.72  ? 163  LYS   B O    1 
ATOM   13915 C CB   . LYS   B  1 137 ? 78.648 28.092  -75.872 1.00 35.07  ? 163  LYS   B CB   1 
ATOM   13916 C CG   . LYS   B  1 137 ? 79.003 26.762  -76.513 1.00 38.51  ? 163  LYS   B CG   1 
ATOM   13917 C CD   . LYS   B  1 137 ? 79.993 26.895  -77.660 1.00 42.49  ? 163  LYS   B CD   1 
ATOM   13918 C CE   . LYS   B  1 137 ? 80.485 25.538  -78.098 1.00 46.20  ? 163  LYS   B CE   1 
ATOM   13919 N NZ   . LYS   B  1 137 ? 81.350 25.609  -79.306 1.00 49.13  ? 163  LYS   B NZ   1 
ATOM   13920 H H    . LYS   B  1 137 ? 76.303 27.363  -75.919 0.00 43.79  ? 163  LYS   B H    1 
ATOM   13921 H HA   . LYS   B  1 137 ? 78.308 27.228  -73.941 0.00 44.36  ? 163  LYS   B HA   1 
ATOM   13922 H HB2  . LYS   B  1 137 ? 78.096 28.684  -76.601 0.00 47.64  ? 163  LYS   B HB2  1 
ATOM   13923 H HB3  . LYS   B  1 137 ? 79.578 28.596  -75.615 0.00 47.64  ? 163  LYS   B HB3  1 
ATOM   13924 H HG2  . LYS   B  1 137 ? 79.460 26.129  -75.755 0.00 51.05  ? 163  LYS   B HG2  1 
ATOM   13925 H HG3  . LYS   B  1 137 ? 78.097 26.296  -76.897 0.00 51.14  ? 163  LYS   B HG3  1 
ATOM   13926 H HD2  . LYS   B  1 137 ? 79.505 27.373  -78.508 0.00 56.98  ? 163  LYS   B HD2  1 
ATOM   13927 H HD3  . LYS   B  1 137 ? 80.850 27.483  -77.334 0.00 56.96  ? 163  LYS   B HD3  1 
ATOM   13928 H HE2  . LYS   B  1 137 ? 81.068 25.095  -77.293 0.00 60.82  ? 163  LYS   B HE2  1 
ATOM   13929 H HE3  . LYS   B  1 137 ? 79.629 24.907  -78.330 0.00 60.75  ? 163  LYS   B HE3  1 
ATOM   13930 H HZ1  . LYS   B  1 137 ? 81.673 24.680  -79.555 0.00 65.05  ? 163  LYS   B HZ1  1 
ATOM   13931 H HZ2  . LYS   B  1 137 ? 80.825 25.994  -80.084 0.00 65.34  ? 163  LYS   B HZ2  1 
ATOM   13932 H HZ3  . LYS   B  1 137 ? 82.154 26.201  -79.125 0.00 65.41  ? 163  LYS   B HZ3  1 
ATOM   13933 N N    . GLU   B  1 138 ? 76.779 30.132  -74.220 1.00 34.20  ? 164  GLU   B N    1 
ATOM   13934 C CA   . GLU   B  1 138 ? 76.576 31.420  -73.562 1.00 35.19  ? 164  GLU   B CA   1 
ATOM   13935 C C    . GLU   B  1 138 ? 76.300 31.226  -72.063 1.00 34.91  ? 164  GLU   B C    1 
ATOM   13936 O O    . GLU   B  1 138 ? 76.812 31.982  -71.251 1.00 35.39  ? 164  GLU   B O    1 
ATOM   13937 C CB   . GLU   B  1 138 ? 75.390 32.166  -74.218 1.00 38.81  ? 164  GLU   B CB   1 
ATOM   13938 C CG   . GLU   B  1 138 ? 75.329 33.647  -73.890 1.00 45.92  ? 164  GLU   B CG   1 
ATOM   13939 C CD   . GLU   B  1 138 ? 73.972 34.128  -73.417 1.00 54.62  ? 164  GLU   B CD   1 
ATOM   13940 O OE1  . GLU   B  1 138 ? 72.959 33.821  -74.088 1.00 55.81  ? 164  GLU   B OE1  1 
ATOM   13941 O OE2  . GLU   B  1 138 ? 73.923 34.823  -72.376 1.00 57.85  ? 164  GLU   B OE2  1 
ATOM   13942 H H    . GLU   B  1 138 ? 76.139 29.970  -74.991 0.00 46.23  ? 164  GLU   B H    1 
ATOM   13943 H HA   . GLU   B  1 138 ? 77.475 32.024  -73.673 0.00 48.04  ? 164  GLU   B HA   1 
ATOM   13944 H HB2  . GLU   B  1 138 ? 75.467 32.087  -75.302 0.00 52.49  ? 164  GLU   B HB2  1 
ATOM   13945 H HB3  . GLU   B  1 138 ? 74.465 31.701  -73.877 0.00 51.82  ? 164  GLU   B HB3  1 
ATOM   13946 H HG2  . GLU   B  1 138 ? 76.052 33.872  -73.108 0.00 61.23  ? 164  GLU   B HG2  1 
ATOM   13947 H HG3  . GLU   B  1 138 ? 75.581 34.209  -74.788 0.00 61.74  ? 164  GLU   B HG3  1 
ATOM   13948 N N    . GLY   B  1 139 ? 75.538 30.194  -71.720 1.00 34.30  ? 165  GLY   B N    1 
ATOM   13949 C CA   . GLY   B  1 139 ? 75.182 29.889  -70.345 1.00 34.11  ? 165  GLY   B CA   1 
ATOM   13950 C C    . GLY   B  1 139 ? 76.251 29.246  -69.479 1.00 33.39  ? 165  GLY   B C    1 
ATOM   13951 O O    . GLY   B  1 139 ? 76.414 29.666  -68.330 1.00 32.78  ? 165  GLY   B O    1 
ATOM   13952 H H    . GLY   B  1 139 ? 75.125 29.542  -72.380 0.00 45.37  ? 165  GLY   B H    1 
ATOM   13953 H HA2  . GLY   B  1 139 ? 74.870 30.809  -69.853 0.00 44.98  ? 165  GLY   B HA2  1 
ATOM   13954 H HA3  . GLY   B  1 139 ? 74.325 29.216  -70.354 0.00 44.44  ? 165  GLY   B HA3  1 
ATOM   13955 N N    . ILE   B  1 140 ? 76.959 28.200  -69.976 1.00 32.90  ? 166  ILE   B N    1 
ATOM   13956 C CA   . ILE   B  1 140 ? 77.908 27.472  -69.120 1.00 33.01  ? 166  ILE   B CA   1 
ATOM   13957 C C    . ILE   B  1 140 ? 79.357 27.326  -69.622 1.00 32.97  ? 166  ILE   B C    1 
ATOM   13958 O O    . ILE   B  1 140 ? 80.164 26.849  -68.828 1.00 32.36  ? 166  ILE   B O    1 
ATOM   13959 C CB   . ILE   B  1 140 ? 77.351 26.064  -68.784 1.00 33.99  ? 166  ILE   B CB   1 
ATOM   13960 C CG1  . ILE   B  1 140 ? 77.304 25.141  -70.018 1.00 34.89  ? 166  ILE   B CG1  1 
ATOM   13961 C CG2  . ILE   B  1 140 ? 75.969 26.165  -68.127 1.00 34.60  ? 166  ILE   B CG2  1 
ATOM   13962 C CD1  . ILE   B  1 140 ? 77.064 23.701  -69.666 1.00 36.52  ? 166  ILE   B CD1  1 
ATOM   13963 H H    . ILE   B  1 140 ? 76.896 27.856  -70.929 0.00 43.13  ? 166  ILE   B H    1 
ATOM   13964 H HA   . ILE   B  1 140 ? 77.995 27.987  -68.165 0.00 42.99  ? 166  ILE   B HA   1 
ATOM   13965 H HB   . ILE   B  1 140 ? 78.016 25.610  -68.051 0.00 43.45  ? 166  ILE   B HB   1 
ATOM   13966 H HG12 . ILE   B  1 140 ? 76.490 25.462  -70.667 0.00 44.66  ? 166  ILE   B HG12 1 
ATOM   13967 H HG13 . ILE   B  1 140 ? 78.245 25.176  -70.565 0.00 44.95  ? 166  ILE   B HG13 1 
ATOM   13968 H HG21 . ILE   B  1 140 ? 75.716 25.209  -67.671 0.00 43.51  ? 166  ILE   B HG21 1 
ATOM   13969 H HG22 . ILE   B  1 140 ? 75.996 26.943  -67.365 0.00 44.01  ? 166  ILE   B HG22 1 
ATOM   13970 H HG23 . ILE   B  1 140 ? 75.230 26.416  -68.887 0.00 44.00  ? 166  ILE   B HG23 1 
ATOM   13971 H HD11 . ILE   B  1 140 ? 77.215 23.081  -70.548 0.00 46.15  ? 166  ILE   B HD11 1 
ATOM   13972 H HD12 . ILE   B  1 140 ? 77.761 23.406  -68.883 0.00 46.04  ? 166  ILE   B HD12 1 
ATOM   13973 H HD13 . ILE   B  1 140 ? 76.040 23.585  -69.315 0.00 45.76  ? 166  ILE   B HD13 1 
ATOM   13974 N N    . SER   B  1 141 ? 79.712 27.676  -70.882 1.00 33.41  ? 167  SER   B N    1 
ATOM   13975 C CA   . SER   B  1 141 ? 81.105 27.481  -71.326 1.00 34.33  ? 167  SER   B CA   1 
ATOM   13976 C C    . SER   B  1 141 ? 82.107 28.369  -70.587 1.00 34.46  ? 167  SER   B C    1 
ATOM   13977 O O    . SER   B  1 141 ? 83.248 27.938  -70.365 1.00 34.71  ? 167  SER   B O    1 
ATOM   13978 C CB   . SER   B  1 141 ? 81.234 27.627  -72.837 1.00 36.37  ? 167  SER   B CB   1 
ATOM   13979 O OG   . SER   B  1 141 ? 80.532 26.556  -73.459 1.00 39.02  ? 167  SER   B OG   1 
ATOM   13980 H H    . SER   B  1 141 ? 79.093 28.073  -71.582 0.00 44.40  ? 167  SER   B H    1 
ATOM   13981 H HA   . SER   B  1 141 ? 81.385 26.460  -71.068 0.00 45.48  ? 167  SER   B HA   1 
ATOM   13982 H HB2  . SER   B  1 141 ? 80.797 28.574  -73.149 0.00 48.86  ? 167  SER   B HB2  1 
ATOM   13983 H HB3  . SER   B  1 141 ? 82.289 27.594  -73.106 0.00 48.93  ? 167  SER   B HB3  1 
ATOM   13984 H HG   . SER   B  1 141 ? 81.008 26.253  -74.277 0.00 51.69  ? 167  SER   B HG   1 
ATOM   13985 N N    . ARG   B  1 142 ? 81.689 29.556  -70.126 1.00 34.27  ? 168  ARG   B N    1 
ATOM   13986 C CA   . ARG   B  1 142 ? 82.598 30.410  -69.343 1.00 34.84  ? 168  ARG   B CA   1 
ATOM   13987 C C    . ARG   B  1 142 ? 82.828 29.863  -67.909 1.00 32.82  ? 168  ARG   B C    1 
ATOM   13988 O O    . ARG   B  1 142 ? 83.748 30.311  -67.238 1.00 32.63  ? 168  ARG   B O    1 
ATOM   13989 C CB   . ARG   B  1 142 ? 82.087 31.867  -69.280 1.00 38.70  ? 168  ARG   B CB   1 
ATOM   13990 C CG   . ARG   B  1 142 ? 82.481 32.702  -70.502 1.00 45.95  ? 168  ARG   B CG   1 
ATOM   13991 C CD   . ARG   B  1 142 ? 81.706 34.000  -70.625 1.00 51.59  ? 168  ARG   B CD   1 
ATOM   13992 N NE   . ARG   B  1 142 ? 80.353 33.769  -71.131 1.00 55.88  ? 168  ARG   B NE   1 
ATOM   13993 C CZ   . ARG   B  1 142 ? 79.558 34.706  -71.646 1.00 59.34  ? 168  ARG   B CZ   1 
ATOM   13994 N NH1  . ARG   B  1 142 ? 79.969 35.969  -71.732 1.00 60.04  ? 168  ARG   B NH1  1 
ATOM   13995 N NH2  . ARG   B  1 142 ? 78.342 34.385  -72.069 1.00 59.77  ? 168  ARG   B NH2  1 
ATOM   13996 H H    . ARG   B  1 142 ? 80.759 29.939  -70.256 0.00 46.17  ? 168  ARG   B H    1 
ATOM   13997 H HA   . ARG   B  1 142 ? 83.576 30.403  -69.826 0.00 47.69  ? 168  ARG   B HA   1 
ATOM   13998 H HB2  . ARG   B  1 142 ? 81.002 31.876  -69.196 0.00 52.06  ? 168  ARG   B HB2  1 
ATOM   13999 H HB3  . ARG   B  1 142 ? 82.523 32.351  -68.407 0.00 52.53  ? 168  ARG   B HB3  1 
ATOM   14000 H HG2  . ARG   B  1 142 ? 83.538 32.955  -70.436 0.00 62.06  ? 168  ARG   B HG2  1 
ATOM   14001 H HG3  . ARG   B  1 142 ? 82.295 32.118  -71.402 0.00 61.57  ? 168  ARG   B HG3  1 
ATOM   14002 H HD2  . ARG   B  1 142 ? 81.637 34.477  -69.648 0.00 68.80  ? 168  ARG   B HD2  1 
ATOM   14003 H HD3  . ARG   B  1 142 ? 82.240 34.637  -71.327 0.00 69.32  ? 168  ARG   B HD3  1 
ATOM   14004 H HE   . ARG   B  1 142 ? 79.993 32.822  -71.077 0.00 73.15  ? 168  ARG   B HE   1 
ATOM   14005 H HH11 . ARG   B  1 142 ? 80.884 36.263  -71.406 0.00 79.84  ? 168  ARG   B HH11 1 
ATOM   14006 H HH12 . ARG   B  1 142 ? 79.349 36.675  -72.117 0.00 79.81  ? 168  ARG   B HH12 1 
ATOM   14007 H HH21 . ARG   B  1 142 ? 78.015 33.426  -72.007 0.00 77.81  ? 168  ARG   B HH21 1 
ATOM   14008 H HH22 . ARG   B  1 142 ? 77.730 35.097  -72.457 0.00 78.55  ? 168  ARG   B HH22 1 
ATOM   14009 N N    . LEU   B  1 143 ? 82.039 28.869  -67.458 1.00 31.26  ? 169  LEU   B N    1 
ATOM   14010 C CA   . LEU   B  1 143 ? 82.192 28.305  -66.124 1.00 30.54  ? 169  LEU   B CA   1 
ATOM   14011 C C    . LEU   B  1 143 ? 83.233 27.179  -66.126 1.00 30.62  ? 169  LEU   B C    1 
ATOM   14012 O O    . LEU   B  1 143 ? 82.925 26.030  -65.831 1.00 30.39  ? 169  LEU   B O    1 
ATOM   14013 C CB   . LEU   B  1 143 ? 80.829 27.824  -65.594 1.00 29.95  ? 169  LEU   B CB   1 
ATOM   14014 C CG   . LEU   B  1 143 ? 79.668 28.813  -65.694 1.00 30.62  ? 169  LEU   B CG   1 
ATOM   14015 C CD1  . LEU   B  1 143 ? 78.396 28.199  -65.132 1.00 31.61  ? 169  LEU   B CD1  1 
ATOM   14016 C CD2  . LEU   B  1 143 ? 79.989 30.115  -64.965 1.00 30.78  ? 169  LEU   B CD2  1 
ATOM   14017 H H    . LEU   B  1 143 ? 81.292 28.430  -67.988 0.00 41.80  ? 169  LEU   B H    1 
ATOM   14018 H HA   . LEU   B  1 143 ? 82.552 29.070  -65.437 0.00 41.14  ? 169  LEU   B HA   1 
ATOM   14019 H HB2  . LEU   B  1 143 ? 80.530 26.908  -66.100 0.00 39.27  ? 169  LEU   B HB2  1 
ATOM   14020 H HB3  . LEU   B  1 143 ? 80.962 27.653  -64.528 0.00 39.42  ? 169  LEU   B HB3  1 
ATOM   14021 H HG   . LEU   B  1 143 ? 79.488 29.052  -66.741 0.00 40.58  ? 169  LEU   B HG   1 
ATOM   14022 H HD11 . LEU   B  1 143 ? 77.585 28.920  -65.223 0.00 41.06  ? 169  LEU   B HD11 1 
ATOM   14023 H HD12 . LEU   B  1 143 ? 78.156 27.298  -65.695 0.00 40.73  ? 169  LEU   B HD12 1 
ATOM   14024 H HD13 . LEU   B  1 143 ? 78.556 27.951  -64.083 0.00 40.83  ? 169  LEU   B HD13 1 
ATOM   14025 H HD21 . LEU   B  1 143 ? 79.110 30.756  -64.984 0.00 41.05  ? 169  LEU   B HD21 1 
ATOM   14026 H HD22 . LEU   B  1 143 ? 80.266 29.889  -63.937 0.00 40.91  ? 169  LEU   B HD22 1 
ATOM   14027 H HD23 . LEU   B  1 143 ? 80.811 30.622  -65.469 0.00 41.50  ? 169  LEU   B HD23 1 
ATOM   14028 N N    . ILE   B  1 144 ? 84.485 27.549  -66.384 1.00 31.31  ? 170  ILE   B N    1 
ATOM   14029 C CA   . ILE   B  1 144 ? 85.596 26.606  -66.523 1.00 32.34  ? 170  ILE   B CA   1 
ATOM   14030 C C    . ILE   B  1 144 ? 85.998 25.875  -65.225 1.00 31.72  ? 170  ILE   B C    1 
ATOM   14031 O O    . ILE   B  1 144 ? 86.643 24.833  -65.343 1.00 32.40  ? 170  ILE   B O    1 
ATOM   14032 C CB   . ILE   B  1 144 ? 86.839 27.262  -67.191 1.00 34.04  ? 170  ILE   B CB   1 
ATOM   14033 C CG1  . ILE   B  1 144 ? 87.644 28.179  -66.234 1.00 35.82  ? 170  ILE   B CG1  1 
ATOM   14034 C CG2  . ILE   B  1 144 ? 86.458 27.989  -68.491 1.00 34.82  ? 170  ILE   B CG2  1 
ATOM   14035 C CD1  . ILE   B  1 144 ? 86.932 29.184  -65.486 1.00 37.43  ? 170  ILE   B CD1  1 
ATOM   14036 H H    . ILE   B  1 144 ? 84.756 28.522  -66.479 0.00 42.68  ? 170  ILE   B H    1 
ATOM   14037 H HA   . ILE   B  1 144 ? 85.257 25.829  -67.209 0.00 43.39  ? 170  ILE   B HA   1 
ATOM   14038 H HB   . ILE   B  1 144 ? 87.503 26.446  -67.476 0.00 46.41  ? 170  ILE   B HB   1 
ATOM   14039 H HG12 . ILE   B  1 144 ? 88.195 27.565  -65.523 0.00 48.88  ? 170  ILE   B HG12 1 
ATOM   14040 H HG13 . ILE   B  1 144 ? 88.357 28.739  -66.836 0.00 49.46  ? 170  ILE   B HG13 1 
ATOM   14041 H HG21 . ILE   B  1 144 ? 87.366 28.202  -69.051 0.00 48.06  ? 170  ILE   B HG21 1 
ATOM   14042 H HG22 . ILE   B  1 144 ? 85.805 27.342  -69.076 0.00 47.28  ? 170  ILE   B HG22 1 
ATOM   14043 H HG23 . ILE   B  1 144 ? 85.943 28.917  -68.246 0.00 47.66  ? 170  ILE   B HG23 1 
ATOM   14044 H HD11 . ILE   B  1 144 ? 87.651 29.745  -64.891 0.00 51.25  ? 170  ILE   B HD11 1 
ATOM   14045 H HD12 . ILE   B  1 144 ? 86.428 29.857  -66.177 0.00 51.00  ? 170  ILE   B HD12 1 
ATOM   14046 H HD13 . ILE   B  1 144 ? 86.206 28.713  -64.826 0.00 50.38  ? 170  ILE   B HD13 1 
ATOM   14047 N N    . ASN   B  1 145 ? 85.604 26.358  -64.022 1.00 29.91  ? 171  ASN   B N    1 
ATOM   14048 C CA   . ASN   B  1 145 ? 85.909 25.670  -62.765 1.00 28.91  ? 171  ASN   B CA   1 
ATOM   14049 C C    . ASN   B  1 145 ? 84.775 24.686  -62.348 1.00 28.21  ? 171  ASN   B C    1 
ATOM   14050 O O    . ASN   B  1 145 ? 84.873 24.100  -61.269 1.00 28.06  ? 171  ASN   B O    1 
ATOM   14051 C CB   . ASN   B  1 145 ? 86.153 26.694  -61.645 1.00 29.13  ? 171  ASN   B CB   1 
ATOM   14052 C CG   . ASN   B  1 145 ? 87.362 27.568  -61.901 1.00 31.67  ? 171  ASN   B CG   1 
ATOM   14053 O OD1  . ASN   B  1 145 ? 88.471 27.071  -62.110 1.00 32.85  ? 171  ASN   B OD1  1 
ATOM   14054 N ND2  . ASN   B  1 145 ? 87.189 28.885  -61.899 1.00 30.74  ? 171  ASN   B ND2  1 
ATOM   14055 H H    . ASN   B  1 145 ? 85.045 27.194  -63.889 0.00 40.40  ? 171  ASN   B H    1 
ATOM   14056 H HA   . ASN   B  1 145 ? 86.824 25.090  -62.872 0.00 39.12  ? 171  ASN   B HA   1 
ATOM   14057 H HB2  . ASN   B  1 145 ? 85.268 27.320  -61.544 0.00 39.39  ? 171  ASN   B HB2  1 
ATOM   14058 H HB3  . ASN   B  1 145 ? 86.332 26.164  -60.710 0.00 39.37  ? 171  ASN   B HB3  1 
ATOM   14059 H HD21 . ASN   B  1 145 ? 87.982 29.495  -62.069 0.00 43.06  ? 171  ASN   B HD21 1 
ATOM   14060 H HD22 . ASN   B  1 145 ? 86.273 29.289  -61.734 0.00 42.34  ? 171  ASN   B HD22 1 
ATOM   14061 N N    . LEU   B  1 146 ? 83.710 24.511  -63.164 1.00 27.64  ? 172  LEU   B N    1 
ATOM   14062 C CA   . LEU   B  1 146 ? 82.617 23.596  -62.813 1.00 27.48  ? 172  LEU   B CA   1 
ATOM   14063 C C    . LEU   B  1 146 ? 83.113 22.169  -62.615 1.00 27.37  ? 172  LEU   B C    1 
ATOM   14064 O O    . LEU   B  1 146 ? 83.829 21.642  -63.464 1.00 27.64  ? 172  LEU   B O    1 
ATOM   14065 C CB   . LEU   B  1 146 ? 81.496 23.562  -63.880 1.00 27.63  ? 172  LEU   B CB   1 
ATOM   14066 C CG   . LEU   B  1 146 ? 80.318 24.529  -63.743 1.00 28.64  ? 172  LEU   B CG   1 
ATOM   14067 C CD1  . LEU   B  1 146 ? 79.261 24.246  -64.822 1.00 28.74  ? 172  LEU   B CD1  1 
ATOM   14068 C CD2  . LEU   B  1 146 ? 79.680 24.480  -62.357 1.00 28.67  ? 172  LEU   B CD2  1 
ATOM   14069 H H    . LEU   B  1 146 ? 83.573 24.983  -64.052 0.00 36.58  ? 172  LEU   B H    1 
ATOM   14070 H HA   . LEU   B  1 146 ? 82.195 23.931  -61.869 0.00 35.46  ? 172  LEU   B HA   1 
ATOM   14071 H HB2  . LEU   B  1 146 ? 81.936 23.727  -64.863 0.00 35.83  ? 172  LEU   B HB2  1 
ATOM   14072 H HB3  . LEU   B  1 146 ? 81.065 22.561  -63.862 0.00 35.18  ? 172  LEU   B HB3  1 
ATOM   14073 H HG   . LEU   B  1 146 ? 80.695 25.538  -63.891 0.00 37.06  ? 172  LEU   B HG   1 
ATOM   14074 H HD11 . LEU   B  1 146 ? 78.491 25.014  -64.775 0.00 36.58  ? 172  LEU   B HD11 1 
ATOM   14075 H HD12 . LEU   B  1 146 ? 79.742 24.262  -65.799 0.00 36.83  ? 172  LEU   B HD12 1 
ATOM   14076 H HD13 . LEU   B  1 146 ? 78.823 23.269  -64.637 0.00 36.18  ? 172  LEU   B HD13 1 
ATOM   14077 H HD21 . LEU   B  1 146 ? 78.649 24.824  -62.428 0.00 36.19  ? 172  LEU   B HD21 1 
ATOM   14078 H HD22 . LEU   B  1 146 ? 79.710 23.458  -61.986 0.00 36.06  ? 172  LEU   B HD22 1 
ATOM   14079 H HD23 . LEU   B  1 146 ? 80.232 25.139  -61.688 0.00 36.62  ? 172  LEU   B HD23 1 
ATOM   14080 N N    . LYS   B  1 147 ? 82.728 21.568  -61.486 1.00 26.90  ? 173  LYS   B N    1 
ATOM   14081 C CA   . LYS   B  1 147 ? 83.047 20.201  -61.099 1.00 27.36  ? 173  LYS   B CA   1 
ATOM   14082 C C    . LYS   B  1 147 ? 81.755 19.372  -61.158 1.00 26.02  ? 173  LYS   B C    1 
ATOM   14083 O O    . LYS   B  1 147 ? 81.782 18.253  -61.667 1.00 25.85  ? 173  LYS   B O    1 
ATOM   14084 C CB   . LYS   B  1 147 ? 83.629 20.174  -59.673 1.00 31.58  ? 173  LYS   B CB   1 
ATOM   14085 C CG   . LYS   B  1 147 ? 84.263 18.834  -59.288 1.00 39.05  ? 173  LYS   B CG   1 
ATOM   14086 C CD   . LYS   B  1 147 ? 84.645 18.767  -57.802 1.00 45.20  ? 173  LYS   B CD   1 
ATOM   14087 C CE   . LYS   B  1 147 ? 83.516 18.245  -56.936 1.00 50.59  ? 173  LYS   B CE   1 
ATOM   14088 N NZ   . LYS   B  1 147 ? 83.928 18.070  -55.513 1.00 54.12  ? 173  LYS   B NZ   1 
ATOM   14089 H H    . LYS   B  1 147 ? 82.177 22.036  -60.773 0.00 34.20  ? 173  LYS   B H    1 
ATOM   14090 H HA   . LYS   B  1 147 ? 83.775 19.762  -61.779 0.00 34.88  ? 173  LYS   B HA   1 
ATOM   14091 H HB2  . LYS   B  1 147 ? 84.399 20.940  -59.595 0.00 40.24  ? 173  LYS   B HB2  1 
ATOM   14092 H HB3  . LYS   B  1 147 ? 82.828 20.379  -58.964 0.00 39.55  ? 173  LYS   B HB3  1 
ATOM   14093 H HG2  . LYS   B  1 147 ? 83.558 18.028  -59.487 0.00 48.37  ? 173  LYS   B HG2  1 
ATOM   14094 H HG3  . LYS   B  1 147 ? 85.168 18.689  -59.876 0.00 49.07  ? 173  LYS   B HG3  1 
ATOM   14095 H HD2  . LYS   B  1 147 ? 85.497 18.099  -57.683 0.00 56.35  ? 173  LYS   B HD2  1 
ATOM   14096 H HD3  . LYS   B  1 147 ? 84.900 19.767  -57.453 0.00 56.44  ? 173  LYS   B HD3  1 
ATOM   14097 H HE2  . LYS   B  1 147 ? 82.687 18.951  -56.963 0.00 61.97  ? 173  LYS   B HE2  1 
ATOM   14098 H HE3  . LYS   B  1 147 ? 83.196 17.274  -57.311 0.00 61.85  ? 173  LYS   B HE3  1 
ATOM   14099 H HZ1  . LYS   B  1 147 ? 83.142 17.738  -54.963 0.00 66.10  ? 173  LYS   B HZ1  1 
ATOM   14100 H HZ2  . LYS   B  1 147 ? 84.684 17.395  -55.452 0.00 66.59  ? 173  LYS   B HZ2  1 
ATOM   14101 H HZ3  . LYS   B  1 147 ? 84.244 18.957  -55.132 0.00 66.73  ? 173  LYS   B HZ3  1 
ATOM   14102 N N    . ASN   B  1 148 ? 80.637 19.894  -60.617 1.00 24.78  ? 174  ASN   B N    1 
ATOM   14103 C CA   . ASN   B  1 148 ? 79.367 19.167  -60.621 1.00 24.06  ? 174  ASN   B CA   1 
ATOM   14104 C C    . ASN   B  1 148 ? 78.268 20.014  -61.258 1.00 23.10  ? 174  ASN   B C    1 
ATOM   14105 O O    . ASN   B  1 148 ? 78.019 21.138  -60.818 1.00 23.32  ? 174  ASN   B O    1 
ATOM   14106 C CB   . ASN   B  1 148 ? 78.955 18.785  -59.197 1.00 26.06  ? 174  ASN   B CB   1 
ATOM   14107 C CG   . ASN   B  1 148 ? 79.991 18.005  -58.415 1.00 30.49  ? 174  ASN   B CG   1 
ATOM   14108 O OD1  . ASN   B  1 148 ? 80.840 17.305  -58.963 1.00 31.82  ? 174  ASN   B OD1  1 
ATOM   14109 N ND2  . ASN   B  1 148 ? 79.909 18.057  -57.096 1.00 32.97  ? 174  ASN   B ND2  1 
ATOM   14110 H H    . ASN   B  1 148 ? 80.582 20.801  -60.164 0.00 30.86  ? 174  ASN   B H    1 
ATOM   14111 H HA   . ASN   B  1 148 ? 79.457 18.251  -61.201 0.00 29.29  ? 174  ASN   B HA   1 
ATOM   14112 H HB2  . ASN   B  1 148 ? 78.734 19.702  -58.653 0.00 31.54  ? 174  ASN   B HB2  1 
ATOM   14113 H HB3  . ASN   B  1 148 ? 78.057 18.172  -59.252 0.00 31.12  ? 174  ASN   B HB3  1 
ATOM   14114 H HD21 . ASN   B  1 148 ? 80.577 17.544  -56.528 0.00 39.87  ? 174  ASN   B HD21 1 
ATOM   14115 H HD22 . ASN   B  1 148 ? 79.161 18.576  -56.648 0.00 39.64  ? 174  ASN   B HD22 1 
ATOM   14116 N N    . LEU   B  1 149 ? 77.614 19.480  -62.297 1.00 21.99  ? 175  LEU   B N    1 
ATOM   14117 C CA   . LEU   B  1 149 ? 76.549 20.192  -62.995 1.00 21.85  ? 175  LEU   B CA   1 
ATOM   14118 C C    . LEU   B  1 149 ? 75.306 19.318  -63.025 1.00 21.54  ? 175  LEU   B C    1 
ATOM   14119 O O    . LEU   B  1 149 ? 75.324 18.248  -63.641 1.00 20.91  ? 175  LEU   B O    1 
ATOM   14120 C CB   . LEU   B  1 149 ? 76.996 20.550  -64.430 1.00 22.36  ? 175  LEU   B CB   1 
ATOM   14121 C CG   . LEU   B  1 149 ? 75.955 21.265  -65.303 1.00 24.16  ? 175  LEU   B CG   1 
ATOM   14122 C CD1  . LEU   B  1 149 ? 75.411 22.539  -64.625 1.00 24.40  ? 175  LEU   B CD1  1 
ATOM   14123 C CD2  . LEU   B  1 149 ? 76.544 21.592  -66.679 1.00 25.01  ? 175  LEU   B CD2  1 
ATOM   14124 H H    . LEU   B  1 149 ? 77.792 18.556  -62.677 0.00 26.57  ? 175  LEU   B H    1 
ATOM   14125 H HA   . LEU   B  1 149 ? 76.306 21.115  -62.471 0.00 26.54  ? 175  LEU   B HA   1 
ATOM   14126 H HB2  . LEU   B  1 149 ? 77.874 21.190  -64.364 0.00 27.77  ? 175  LEU   B HB2  1 
ATOM   14127 H HB3  . LEU   B  1 149 ? 77.264 19.627  -64.940 0.00 27.40  ? 175  LEU   B HB3  1 
ATOM   14128 H HG   . LEU   B  1 149 ? 75.111 20.600  -65.477 0.00 29.37  ? 175  LEU   B HG   1 
ATOM   14129 H HD11 . LEU   B  1 149 ? 74.843 23.115  -65.353 0.00 30.15  ? 175  LEU   B HD11 1 
ATOM   14130 H HD12 . LEU   B  1 149 ? 74.761 22.255  -63.798 0.00 29.70  ? 175  LEU   B HD12 1 
ATOM   14131 H HD13 . LEU   B  1 149 ? 76.248 23.129  -64.254 0.00 30.29  ? 175  LEU   B HD13 1 
ATOM   14132 H HD21 . LEU   B  1 149 ? 75.796 22.109  -67.278 0.00 31.17  ? 175  LEU   B HD21 1 
ATOM   14133 H HD22 . LEU   B  1 149 ? 77.417 22.229  -66.546 0.00 31.41  ? 175  LEU   B HD22 1 
ATOM   14134 H HD23 . LEU   B  1 149 ? 76.835 20.664  -67.168 0.00 31.06  ? 175  LEU   B HD23 1 
ATOM   14135 N N    . TYR   B  1 150 ? 74.228 19.768  -62.353 1.00 21.94  ? 176  TYR   B N    1 
ATOM   14136 C CA   . TYR   B  1 150 ? 72.974 19.026  -62.304 1.00 23.11  ? 176  TYR   B CA   1 
ATOM   14137 C C    . TYR   B  1 150 ? 71.908 19.738  -63.111 1.00 24.27  ? 176  TYR   B C    1 
ATOM   14138 O O    . TYR   B  1 150 ? 71.530 20.856  -62.777 1.00 24.80  ? 176  TYR   B O    1 
ATOM   14139 C CB   . TYR   B  1 150 ? 72.471 18.831  -60.863 1.00 23.55  ? 176  TYR   B CB   1 
ATOM   14140 C CG   . TYR   B  1 150 ? 73.504 18.306  -59.891 1.00 25.00  ? 176  TYR   B CG   1 
ATOM   14141 C CD1  . TYR   B  1 150 ? 74.421 19.157  -59.296 1.00 26.50  ? 176  TYR   B CD1  1 
ATOM   14142 C CD2  . TYR   B  1 150 ? 73.521 16.969  -59.520 1.00 26.19  ? 176  TYR   B CD2  1 
ATOM   14143 C CE1  . TYR   B  1 150 ? 75.365 18.684  -58.394 1.00 27.94  ? 176  TYR   B CE1  1 
ATOM   14144 C CE2  . TYR   B  1 150 ? 74.459 16.482  -58.619 1.00 27.75  ? 176  TYR   B CE2  1 
ATOM   14145 C CZ   . TYR   B  1 150 ? 75.392 17.341  -58.069 1.00 29.29  ? 176  TYR   B CZ   1 
ATOM   14146 O OH   . TYR   B  1 150 ? 76.321 16.889  -57.163 1.00 31.85  ? 176  TYR   B OH   1 
ATOM   14147 H H    . TYR   B  1 150 ? 74.193 20.638  -61.832 0.00 26.01  ? 176  TYR   B H    1 
ATOM   14148 H HA   . TYR   B  1 150 ? 73.118 18.036  -62.730 0.00 26.83  ? 176  TYR   B HA   1 
ATOM   14149 H HB2  . TYR   B  1 150 ? 72.049 19.750  -60.464 0.00 27.20  ? 176  TYR   B HB2  1 
ATOM   14150 H HB3  . TYR   B  1 150 ? 71.683 18.083  -60.928 0.00 26.88  ? 176  TYR   B HB3  1 
ATOM   14151 H HD1  . TYR   B  1 150 ? 74.419 20.202  -59.558 0.00 31.20  ? 176  TYR   B HD1  1 
ATOM   14152 H HD2  . TYR   B  1 150 ? 72.818 16.286  -59.963 0.00 29.84  ? 176  TYR   B HD2  1 
ATOM   14153 H HE1  . TYR   B  1 150 ? 76.080 19.360  -57.957 0.00 33.00  ? 176  TYR   B HE1  1 
ATOM   14154 H HE2  . TYR   B  1 150 ? 74.466 15.433  -58.374 0.00 31.78  ? 176  TYR   B HE2  1 
ATOM   14155 H HH   . TYR   B  1 150 ? 76.252 15.905  -57.045 0.00 37.08  ? 176  TYR   B HH   1 
ATOM   14156 N N    . LEU   B  1 151 ? 71.428 19.091  -64.169 1.00 24.08  ? 177  LEU   B N    1 
ATOM   14157 C CA   . LEU   B  1 151 ? 70.371 19.611  -65.034 1.00 24.46  ? 177  LEU   B CA   1 
ATOM   14158 C C    . LEU   B  1 151 ? 69.195 18.609  -65.160 1.00 23.54  ? 177  LEU   B C    1 
ATOM   14159 O O    . LEU   B  1 151 ? 68.374 18.734  -66.069 1.00 23.88  ? 177  LEU   B O    1 
ATOM   14160 C CB   . LEU   B  1 151 ? 70.989 19.885  -66.416 1.00 25.47  ? 177  LEU   B CB   1 
ATOM   14161 C CG   . LEU   B  1 151 ? 71.992 21.038  -66.487 1.00 28.25  ? 177  LEU   B CG   1 
ATOM   14162 C CD1  . LEU   B  1 151 ? 72.922 20.877  -67.685 1.00 28.89  ? 177  LEU   B CD1  1 
ATOM   14163 C CD2  . LEU   B  1 151 ? 71.276 22.352  -66.606 1.00 29.58  ? 177  LEU   B CD2  1 
ATOM   14164 H H    . LEU   B  1 151 ? 71.756 18.179  -64.471 0.00 28.06  ? 177  LEU   B H    1 
ATOM   14165 H HA   . LEU   B  1 151 ? 69.965 20.538  -64.635 0.00 28.73  ? 177  LEU   B HA   1 
ATOM   14166 H HB2  . LEU   B  1 151 ? 71.516 18.985  -66.731 0.00 30.25  ? 177  LEU   B HB2  1 
ATOM   14167 H HB3  . LEU   B  1 151 ? 70.200 20.115  -67.130 0.00 30.37  ? 177  LEU   B HB3  1 
ATOM   14168 H HG   . LEU   B  1 151 ? 72.609 21.065  -65.590 0.00 33.96  ? 177  LEU   B HG   1 
ATOM   14169 H HD11 . LEU   B  1 151 ? 73.546 21.765  -67.770 0.00 35.43  ? 177  LEU   B HD11 1 
ATOM   14170 H HD12 . LEU   B  1 151 ? 73.545 19.997  -67.534 0.00 35.02  ? 177  LEU   B HD12 1 
ATOM   14171 H HD13 . LEU   B  1 151 ? 72.323 20.757  -68.587 0.00 35.19  ? 177  LEU   B HD13 1 
ATOM   14172 H HD21 . LEU   B  1 151 ? 71.981 23.161  -66.419 0.00 36.09  ? 177  LEU   B HD21 1 
ATOM   14173 H HD22 . LEU   B  1 151 ? 70.873 22.439  -67.613 0.00 35.99  ? 177  LEU   B HD22 1 
ATOM   14174 H HD23 . LEU   B  1 151 ? 70.456 22.392  -65.892 0.00 35.59  ? 177  LEU   B HD23 1 
ATOM   14175 N N    . ALA   B  1 152 ? 69.081 17.656  -64.231 1.00 22.80  ? 178  ALA   B N    1 
ATOM   14176 C CA   . ALA   B  1 152 ? 68.059 16.627  -64.294 1.00 22.85  ? 178  ALA   B CA   1 
ATOM   14177 C C    . ALA   B  1 152 ? 66.633 17.143  -64.065 1.00 22.30  ? 178  ALA   B C    1 
ATOM   14178 O O    . ALA   B  1 152 ? 66.431 18.216  -63.490 1.00 22.43  ? 178  ALA   B O    1 
ATOM   14179 C CB   . ALA   B  1 152 ? 68.388 15.514  -63.289 1.00 23.16  ? 178  ALA   B CB   1 
ATOM   14180 H H    . ALA   B  1 152 ? 69.669 17.581  -63.406 0.00 25.95  ? 178  ALA   B H    1 
ATOM   14181 H HA   . ALA   B  1 152 ? 68.091 16.182  -65.288 0.00 25.93  ? 178  ALA   B HA   1 
ATOM   14182 H HB1  . ALA   B  1 152 ? 67.655 14.716  -63.397 0.00 25.72  ? 178  ALA   B HB1  1 
ATOM   14183 H HB2  . ALA   B  1 152 ? 69.386 15.132  -63.499 0.00 26.00  ? 178  ALA   B HB2  1 
ATOM   14184 H HB3  . ALA   B  1 152 ? 68.348 15.920  -62.279 0.00 25.77  ? 178  ALA   B HB3  1 
ATOM   14185 N N    . TRP   B  1 153 ? 65.649 16.393  -64.573 1.00 22.01  ? 179  TRP   B N    1 
ATOM   14186 C CA   . TRP   B  1 153 ? 64.232 16.649  -64.339 1.00 22.05  ? 179  TRP   B CA   1 
ATOM   14187 C C    . TRP   B  1 153 ? 63.722 18.002  -64.868 1.00 22.43  ? 179  TRP   B C    1 
ATOM   14188 O O    . TRP   B  1 153 ? 62.986 18.695  -64.166 1.00 22.35  ? 179  TRP   B O    1 
ATOM   14189 C CB   . TRP   B  1 153 ? 63.919 16.496  -62.831 1.00 21.46  ? 179  TRP   B CB   1 
ATOM   14190 C CG   . TRP   B  1 153 ? 64.114 15.111  -62.309 1.00 21.05  ? 179  TRP   B CG   1 
ATOM   14191 C CD1  . TRP   B  1 153 ? 65.228 14.607  -61.714 1.00 21.81  ? 179  TRP   B CD1  1 
ATOM   14192 C CD2  . TRP   B  1 153 ? 63.109 14.089  -62.214 1.00 20.67  ? 179  TRP   B CD2  1 
ATOM   14193 N NE1  . TRP   B  1 153 ? 64.992 13.318  -61.289 1.00 21.91  ? 179  TRP   B NE1  1 
ATOM   14194 C CE2  . TRP   B  1 153 ? 63.681 13.000  -61.527 1.00 21.20  ? 179  TRP   B CE2  1 
ATOM   14195 C CE3  . TRP   B  1 153 ? 61.780 13.993  -62.645 1.00 21.07  ? 179  TRP   B CE3  1 
ATOM   14196 C CZ2  . TRP   B  1 153 ? 62.986 11.805  -61.309 1.00 21.56  ? 179  TRP   B CZ2  1 
ATOM   14197 C CZ3  . TRP   B  1 153 ? 61.072 12.832  -62.381 1.00 21.74  ? 179  TRP   B CZ3  1 
ATOM   14198 C CH2  . TRP   B  1 153 ? 61.672 11.756  -61.714 1.00 21.89  ? 179  TRP   B CH2  1 
ATOM   14199 H H    . TRP   B  1 153 ? 65.814 15.602  -65.186 0.00 24.63  ? 179  TRP   B H    1 
ATOM   14200 H HA   . TRP   B  1 153 ? 63.667 15.877  -64.860 0.00 24.51  ? 179  TRP   B HA   1 
ATOM   14201 H HB2  . TRP   B  1 153 ? 64.540 17.174  -62.247 0.00 23.55  ? 179  TRP   B HB2  1 
ATOM   14202 H HB3  . TRP   B  1 153 ? 62.870 16.730  -62.662 0.00 23.47  ? 179  TRP   B HB3  1 
ATOM   14203 H HD1  . TRP   B  1 153 ? 66.161 15.136  -61.603 0.00 23.69  ? 179  TRP   B HD1  1 
ATOM   14204 H HE1  . TRP   B  1 153 ? 65.676 12.711  -60.791 0.00 23.37  ? 179  TRP   B HE1  1 
ATOM   14205 H HE3  . TRP   B  1 153 ? 61.293 14.839  -63.103 0.00 22.76  ? 179  TRP   B HE3  1 
ATOM   14206 H HZ2  . TRP   B  1 153 ? 63.456 10.961  -60.825 0.00 22.64  ? 179  TRP   B HZ2  1 
ATOM   14207 H HZ3  . TRP   B  1 153 ? 60.040 12.760  -62.684 0.00 23.22  ? 179  TRP   B HZ3  1 
ATOM   14208 H HH2  . TRP   B  1 153 ? 61.109 10.850  -61.561 0.00 23.05  ? 179  TRP   B HH2  1 
ATOM   14209 N N    . ASN   B  1 154 ? 64.099 18.371  -66.103 1.00 22.45  ? 180  ASN   B N    1 
ATOM   14210 C CA   . ASN   B  1 154 ? 63.559 19.583  -66.725 1.00 22.97  ? 180  ASN   B CA   1 
ATOM   14211 C C    . ASN   B  1 154 ? 62.472 19.214  -67.751 1.00 23.86  ? 180  ASN   B C    1 
ATOM   14212 O O    . ASN   B  1 154 ? 61.592 20.030  -67.981 1.00 24.36  ? 180  ASN   B O    1 
ATOM   14213 C CB   . ASN   B  1 154 ? 64.664 20.484  -67.332 1.00 23.74  ? 180  ASN   B CB   1 
ATOM   14214 C CG   . ASN   B  1 154 ? 65.370 21.336  -66.300 1.00 25.31  ? 180  ASN   B CG   1 
ATOM   14215 O OD1  . ASN   B  1 154 ? 65.227 22.553  -66.273 1.00 25.90  ? 180  ASN   B OD1  1 
ATOM   14216 N ND2  . ASN   B  1 154 ? 66.090 20.719  -65.385 1.00 26.05  ? 180  ASN   B ND2  1 
ATOM   14217 H H    . ASN   B  1 154 ? 64.759 17.862  -66.683 0.00 25.75  ? 180  ASN   B H    1 
ATOM   14218 H HA   . ASN   B  1 154 ? 63.043 20.179  -65.974 0.00 26.59  ? 180  ASN   B HA   1 
ATOM   14219 H HB2  . ASN   B  1 154 ? 65.407 19.854  -67.820 0.00 27.96  ? 180  ASN   B HB2  1 
ATOM   14220 H HB3  . ASN   B  1 154 ? 64.210 21.152  -68.063 0.00 28.24  ? 180  ASN   B HB3  1 
ATOM   14221 H HD21 . ASN   B  1 154 ? 66.578 21.257  -64.676 0.00 30.45  ? 180  ASN   B HD21 1 
ATOM   14222 H HD22 . ASN   B  1 154 ? 66.154 19.706  -65.387 0.00 30.22  ? 180  ASN   B HD22 1 
ATOM   14223 N N    . CYS   B  1 155 ? 62.495 17.998  -68.337 1.00 24.10  ? 181  CYS   B N    1 
ATOM   14224 C CA   . CYS   B  1 155 ? 61.469 17.594  -69.298 1.00 24.85  ? 181  CYS   B CA   1 
ATOM   14225 C C    . CYS   B  1 155 ? 61.250 16.081  -69.205 1.00 24.88  ? 181  CYS   B C    1 
ATOM   14226 O O    . CYS   B  1 155 ? 62.107 15.309  -69.615 1.00 24.90  ? 181  CYS   B O    1 
ATOM   14227 C CB   . CYS   B  1 155 ? 61.857 18.016  -70.711 1.00 26.67  ? 181  CYS   B CB   1 
ATOM   14228 S SG   . CYS   B  1 155 ? 60.616 17.608  -71.960 1.00 33.31  ? 181  CYS   B SG   1 
ATOM   14229 H H    . CYS   B  1 155 ? 63.200 17.285  -68.181 0.00 27.93  ? 181  CYS   B H    1 
ATOM   14230 H HA   . CYS   B  1 155 ? 60.535 18.079  -69.025 0.00 29.17  ? 181  CYS   B HA   1 
ATOM   14231 H HB2  . CYS   B  1 155 ? 61.998 19.096  -70.727 0.00 32.00  ? 181  CYS   B HB2  1 
ATOM   14232 H HB3  . CYS   B  1 155 ? 62.786 17.519  -70.987 0.00 31.81  ? 181  CYS   B HB3  1 
ATOM   14233 N N    . TYR   B  1 156 ? 60.112 15.653  -68.661 1.00 24.42  ? 182  TYR   B N    1 
ATOM   14234 C CA   . TYR   B  1 156 ? 59.881 14.235  -68.392 1.00 24.13  ? 182  TYR   B CA   1 
ATOM   14235 C C    . TYR   B  1 156 ? 58.408 13.913  -68.211 1.00 24.05  ? 182  TYR   B C    1 
ATOM   14236 O O    . TYR   B  1 156 ? 57.604 14.824  -68.019 1.00 24.05  ? 182  TYR   B O    1 
ATOM   14237 C CB   . TYR   B  1 156 ? 60.645 13.861  -67.094 1.00 23.57  ? 182  TYR   B CB   1 
ATOM   14238 C CG   . TYR   B  1 156 ? 60.184 14.690  -65.918 1.00 24.22  ? 182  TYR   B CG   1 
ATOM   14239 C CD1  . TYR   B  1 156 ? 60.679 15.971  -65.709 1.00 25.26  ? 182  TYR   B CD1  1 
ATOM   14240 C CD2  . TYR   B  1 156 ? 59.136 14.264  -65.116 1.00 24.75  ? 182  TYR   B CD2  1 
ATOM   14241 C CE1  . TYR   B  1 156 ? 60.173 16.785  -64.704 1.00 25.89  ? 182  TYR   B CE1  1 
ATOM   14242 C CE2  . TYR   B  1 156 ? 58.643 15.054  -64.090 1.00 25.82  ? 182  TYR   B CE2  1 
ATOM   14243 C CZ   . TYR   B  1 156 ? 59.164 16.319  -63.885 1.00 26.78  ? 182  TYR   B CZ   1 
ATOM   14244 O OH   . TYR   B  1 156 ? 58.695 17.107  -62.860 1.00 27.98  ? 182  TYR   B OH   1 
ATOM   14245 H H    . TYR   B  1 156 ? 59.337 16.250  -68.388 0.00 28.22  ? 182  TYR   B H    1 
ATOM   14246 H HA   . TYR   B  1 156 ? 60.258 13.626  -69.212 0.00 27.76  ? 182  TYR   B HA   1 
ATOM   14247 H HB2  . TYR   B  1 156 ? 60.461 12.812  -66.863 0.00 26.38  ? 182  TYR   B HB2  1 
ATOM   14248 H HB3  . TYR   B  1 156 ? 61.710 14.031  -67.238 0.00 26.60  ? 182  TYR   B HB3  1 
ATOM   14249 H HD1  . TYR   B  1 156 ? 61.456 16.347  -66.353 0.00 28.70  ? 182  TYR   B HD1  1 
ATOM   14250 H HD2  . TYR   B  1 156 ? 58.717 13.285  -65.275 0.00 27.48  ? 182  TYR   B HD2  1 
ATOM   14251 H HE1  . TYR   B  1 156 ? 60.600 17.760  -64.534 0.00 29.28  ? 182  TYR   B HE1  1 
ATOM   14252 H HE2  . TYR   B  1 156 ? 57.854 14.674  -63.462 0.00 28.53  ? 182  TYR   B HE2  1 
ATOM   14253 H HH   . TYR   B  1 156 ? 57.961 16.651  -62.372 0.00 31.18  ? 182  TYR   B HH   1 
ATOM   14254 N N    . PHE   B  1 157 ? 58.056 12.607  -68.280 1.00 24.12  ? 183  PHE   B N    1 
ATOM   14255 C CA   . PHE   B  1 157 ? 56.694 12.097  -68.073 1.00 24.41  ? 183  PHE   B CA   1 
ATOM   14256 C C    . PHE   B  1 157 ? 55.699 12.844  -69.008 1.00 25.17  ? 183  PHE   B C    1 
ATOM   14257 O O    . PHE   B  1 157 ? 56.020 12.962  -70.193 1.00 24.88  ? 183  PHE   B O    1 
ATOM   14258 C CB   . PHE   B  1 157 ? 56.342 12.175  -66.561 1.00 24.25  ? 183  PHE   B CB   1 
ATOM   14259 C CG   . PHE   B  1 157 ? 57.161 11.366  -65.584 1.00 24.76  ? 183  PHE   B CG   1 
ATOM   14260 C CD1  . PHE   B  1 157 ? 58.100 10.449  -66.024 1.00 25.87  ? 183  PHE   B CD1  1 
ATOM   14261 C CD2  . PHE   B  1 157 ? 57.033 11.566  -64.223 1.00 25.40  ? 183  PHE   B CD2  1 
ATOM   14262 C CE1  . PHE   B  1 157 ? 58.880 9.739   -65.115 1.00 26.03  ? 183  PHE   B CE1  1 
ATOM   14263 C CE2  . PHE   B  1 157 ? 57.809 10.847  -63.323 1.00 25.99  ? 183  PHE   B CE2  1 
ATOM   14264 C CZ   . PHE   B  1 157 ? 58.711 9.926   -63.778 1.00 25.55  ? 183  PHE   B CZ   1 
ATOM   14265 H H    . PHE   B  1 157 ? 58.719 11.866  -68.483 0.00 27.43  ? 183  PHE   B H    1 
ATOM   14266 H HA   . PHE   B  1 157 ? 56.671 11.048  -68.365 0.00 27.78  ? 183  PHE   B HA   1 
ATOM   14267 H HB2  . PHE   B  1 157 ? 56.432 13.216  -66.254 0.00 27.19  ? 183  PHE   B HB2  1 
ATOM   14268 H HB3  . PHE   B  1 157 ? 55.313 11.856  -66.425 0.00 27.19  ? 183  PHE   B HB3  1 
ATOM   14269 H HD1  . PHE   B  1 157 ? 58.245 10.268  -67.075 0.00 29.05  ? 183  PHE   B HD1  1 
ATOM   14270 H HD2  . PHE   B  1 157 ? 56.316 12.282  -63.856 0.00 27.91  ? 183  PHE   B HD2  1 
ATOM   14271 H HE1  . PHE   B  1 157 ? 59.588 9.011   -65.470 0.00 28.76  ? 183  PHE   B HE1  1 
ATOM   14272 H HE2  . PHE   B  1 157 ? 57.683 11.001  -62.265 0.00 28.12  ? 183  PHE   B HE2  1 
ATOM   14273 H HZ   . PHE   B  1 157 ? 59.313 9.371   -63.077 0.00 27.64  ? 183  PHE   B HZ   1 
ATOM   14274 N N    . ASN   B  1 158 ? 54.556 13.377  -68.519 1.00 25.18  ? 184  ASN   B N    1 
ATOM   14275 C CA   . ASN   B  1 158 ? 53.623 14.120  -69.360 1.00 26.18  ? 184  ASN   B CA   1 
ATOM   14276 C C    . ASN   B  1 158 ? 53.746 15.633  -69.168 1.00 27.68  ? 184  ASN   B C    1 
ATOM   14277 O O    . ASN   B  1 158 ? 52.840 16.361  -69.571 1.00 28.31  ? 184  ASN   B O    1 
ATOM   14278 C CB   . ASN   B  1 158 ? 52.185 13.664  -69.105 1.00 26.15  ? 184  ASN   B CB   1 
ATOM   14279 C CG   . ASN   B  1 158 ? 51.945 12.201  -69.393 1.00 28.88  ? 184  ASN   B CG   1 
ATOM   14280 O OD1  . ASN   B  1 158 ? 51.339 11.489  -68.594 1.00 28.70  ? 184  ASN   B OD1  1 
ATOM   14281 N ND2  . ASN   B  1 158 ? 52.341 11.719  -70.570 1.00 29.65  ? 184  ASN   B ND2  1 
ATOM   14282 H H    . ASN   B  1 158 ? 54.236 13.311  -67.558 0.00 28.85  ? 184  ASN   B H    1 
ATOM   14283 H HA   . ASN   B  1 158 ? 53.838 13.936  -70.411 0.00 31.02  ? 184  ASN   B HA   1 
ATOM   14284 H HB2  . ASN   B  1 158 ? 51.939 13.844  -68.060 0.00 30.46  ? 184  ASN   B HB2  1 
ATOM   14285 H HB3  . ASN   B  1 158 ? 51.506 14.226  -69.745 0.00 31.09  ? 184  ASN   B HB3  1 
ATOM   14286 H HD21 . ASN   B  1 158 ? 52.184 10.739  -70.784 0.00 35.23  ? 184  ASN   B HD21 1 
ATOM   14287 H HD22 . ASN   B  1 158 ? 52.761 12.318  -71.273 0.00 35.44  ? 184  ASN   B HD22 1 
ATOM   14288 N N    . LYS   B  1 159 ? 54.891 16.137  -68.657 1.00 28.09  ? 185  LYS   B N    1 
ATOM   14289 C CA   . LYS   B  1 159 ? 55.109 17.578  -68.557 1.00 28.59  ? 185  LYS   B CA   1 
ATOM   14290 C C    . LYS   B  1 159 ? 55.096 18.187  -69.967 1.00 29.47  ? 185  LYS   B C    1 
ATOM   14291 O O    . LYS   B  1 159 ? 55.596 17.574  -70.914 1.00 29.09  ? 185  LYS   B O    1 
ATOM   14292 C CB   . LYS   B  1 159 ? 56.470 17.878  -67.902 1.00 29.38  ? 185  LYS   B CB   1 
ATOM   14293 C CG   . LYS   B  1 159 ? 56.749 19.363  -67.721 1.00 30.80  ? 185  LYS   B CG   1 
ATOM   14294 C CD   . LYS   B  1 159 ? 58.113 19.601  -67.076 1.00 32.77  ? 185  LYS   B CD   1 
ATOM   14295 C CE   . LYS   B  1 159 ? 58.439 21.071  -67.065 1.00 35.10  ? 185  LYS   B CE   1 
ATOM   14296 N NZ   . LYS   B  1 159 ? 59.751 21.350  -66.423 1.00 36.09  ? 185  LYS   B NZ   1 
ATOM   14297 H H    . LYS   B  1 159 ? 55.675 15.590  -68.316 0.00 32.70  ? 185  LYS   B H    1 
ATOM   14298 H HA   . LYS   B  1 159 ? 54.320 18.030  -67.957 0.00 33.71  ? 185  LYS   B HA   1 
ATOM   14299 H HB2  . LYS   B  1 159 ? 56.497 17.412  -66.918 0.00 34.09  ? 185  LYS   B HB2  1 
ATOM   14300 H HB3  . LYS   B  1 159 ? 57.259 17.465  -68.529 0.00 34.48  ? 185  LYS   B HB3  1 
ATOM   14301 H HG2  . LYS   B  1 159 ? 56.759 19.871  -68.684 0.00 36.71  ? 185  LYS   B HG2  1 
ATOM   14302 H HG3  . LYS   B  1 159 ? 55.987 19.796  -67.075 0.00 36.32  ? 185  LYS   B HG3  1 
ATOM   14303 H HD2  . LYS   B  1 159 ? 58.096 19.245  -66.047 0.00 38.20  ? 185  LYS   B HD2  1 
ATOM   14304 H HD3  . LYS   B  1 159 ? 58.882 19.081  -67.646 0.00 38.53  ? 185  LYS   B HD3  1 
ATOM   14305 H HE2  . LYS   B  1 159 ? 58.481 21.435  -68.091 0.00 41.96  ? 185  LYS   B HE2  1 
ATOM   14306 H HE3  . LYS   B  1 159 ? 57.670 21.605  -66.509 0.00 41.64  ? 185  LYS   B HE3  1 
ATOM   14307 H HZ1  . LYS   B  1 159 ? 59.941 22.347  -66.439 0.00 42.91  ? 185  LYS   B HZ1  1 
ATOM   14308 H HZ2  . LYS   B  1 159 ? 59.739 21.032  -65.459 0.00 42.38  ? 185  LYS   B HZ2  1 
ATOM   14309 H HZ3  . LYS   B  1 159 ? 60.490 20.865  -66.921 0.00 42.67  ? 185  LYS   B HZ3  1 
ATOM   14310 N N    . VAL   B  1 160 ? 54.486 19.363  -70.109 1.00 30.61  ? 186  VAL   B N    1 
ATOM   14311 C CA   . VAL   B  1 160 ? 54.458 20.059  -71.388 1.00 32.04  ? 186  VAL   B CA   1 
ATOM   14312 C C    . VAL   B  1 160 ? 55.832 20.695  -71.473 1.00 33.23  ? 186  VAL   B C    1 
ATOM   14313 O O    . VAL   B  1 160 ? 56.143 21.567  -70.664 1.00 33.77  ? 186  VAL   B O    1 
ATOM   14314 C CB   . VAL   B  1 160 ? 53.332 21.109  -71.482 1.00 33.44  ? 186  VAL   B CB   1 
ATOM   14315 C CG1  . VAL   B  1 160 ? 53.368 21.814  -72.842 1.00 34.40  ? 186  VAL   B CG1  1 
ATOM   14316 C CG2  . VAL   B  1 160 ? 51.963 20.463  -71.236 1.00 34.17  ? 186  VAL   B CG2  1 
ATOM   14317 H H    . VAL   B  1 160 ? 54.022 19.862  -69.356 0.00 36.92  ? 186  VAL   B H    1 
ATOM   14318 H HA   . VAL   B  1 160 ? 54.328 19.352  -72.206 0.00 39.40  ? 186  VAL   B HA   1 
ATOM   14319 H HB   . VAL   B  1 160 ? 53.482 21.863  -70.711 0.00 41.24  ? 186  VAL   B HB   1 
ATOM   14320 H HG11 . VAL   B  1 160 ? 52.436 22.359  -72.985 0.00 43.40  ? 186  VAL   B HG11 1 
ATOM   14321 H HG12 . VAL   B  1 160 ? 54.201 22.515  -72.867 0.00 43.16  ? 186  VAL   B HG12 1 
ATOM   14322 H HG13 . VAL   B  1 160 ? 53.488 21.069  -73.628 0.00 43.18  ? 186  VAL   B HG13 1 
ATOM   14323 H HG21 . VAL   B  1 160 ? 51.186 21.214  -71.369 0.00 42.50  ? 186  VAL   B HG21 1 
ATOM   14324 H HG22 . VAL   B  1 160 ? 51.822 19.655  -71.952 0.00 42.27  ? 186  VAL   B HG22 1 
ATOM   14325 H HG23 . VAL   B  1 160 ? 51.924 20.072  -70.221 0.00 41.77  ? 186  VAL   B HG23 1 
ATOM   14326 N N    . CYS   B  1 161 ? 56.691 20.171  -72.343 1.00 33.34  ? 187  CYS   B N    1 
ATOM   14327 C CA   . CYS   B  1 161 ? 58.065 20.647  -72.434 1.00 33.92  ? 187  CYS   B CA   1 
ATOM   14328 C C    . CYS   B  1 161 ? 58.670 20.314  -73.788 1.00 35.21  ? 187  CYS   B C    1 
ATOM   14329 O O    . CYS   B  1 161 ? 58.212 19.408  -74.482 1.00 35.79  ? 187  CYS   B O    1 
ATOM   14330 C CB   . CYS   B  1 161 ? 58.901 20.072  -71.290 1.00 33.76  ? 187  CYS   B CB   1 
ATOM   14331 S SG   . CYS   B  1 161 ? 58.858 18.266  -71.156 1.00 34.83  ? 187  CYS   B SG   1 
ATOM   14332 H H    . CYS   B  1 161 ? 56.475 19.421  -72.992 0.00 41.02  ? 187  CYS   B H    1 
ATOM   14333 H HA   . CYS   B  1 161 ? 58.073 21.732  -72.341 0.00 41.85  ? 187  CYS   B HA   1 
ATOM   14334 H HB2  . CYS   B  1 161 ? 59.939 20.366  -71.437 0.00 41.00  ? 187  CYS   B HB2  1 
ATOM   14335 H HB3  . CYS   B  1 161 ? 58.534 20.482  -70.350 0.00 40.76  ? 187  CYS   B HB3  1 
ATOM   14336 N N    . GLU   B  1 162 ? 59.716 21.050  -74.153 1.00 35.68  ? 188  GLU   B N    1 
ATOM   14337 C CA   . GLU   B  1 162 ? 60.415 20.865  -75.417 1.00 36.29  ? 188  GLU   B CA   1 
ATOM   14338 C C    . GLU   B  1 162 ? 61.533 19.847  -75.266 1.00 35.73  ? 188  GLU   B C    1 
ATOM   14339 O O    . GLU   B  1 162 ? 62.081 19.674  -74.175 1.00 35.71  ? 188  GLU   B O    1 
ATOM   14340 C CB   . GLU   B  1 162 ? 61.050 22.202  -75.888 1.00 39.85  ? 188  GLU   B CB   1 
ATOM   14341 C CG   . GLU   B  1 162 ? 60.237 22.998  -76.892 1.00 48.38  ? 188  GLU   B CG   1 
ATOM   14342 C CD   . GLU   B  1 162 ? 58.942 23.567  -76.354 1.00 59.17  ? 188  GLU   B CD   1 
ATOM   14343 O OE1  . GLU   B  1 162 ? 58.855 23.796  -75.125 1.00 62.04  ? 188  GLU   B OE1  1 
ATOM   14344 O OE2  . GLU   B  1 162 ? 58.012 23.787  -77.165 1.00 61.69  ? 188  GLU   B OE2  1 
ATOM   14345 H H    . GLU   B  1 162 ? 60.107 21.779  -73.565 0.00 44.28  ? 188  GLU   B H    1 
ATOM   14346 H HA   . GLU   B  1 162 ? 59.729 20.495  -76.178 0.00 45.65  ? 188  GLU   B HA   1 
ATOM   14347 H HB2  . GLU   B  1 162 ? 61.264 22.845  -75.035 0.00 49.97  ? 188  GLU   B HB2  1 
ATOM   14348 H HB3  . GLU   B  1 162 ? 61.991 21.961  -76.380 0.00 50.23  ? 188  GLU   B HB3  1 
ATOM   14349 H HG2  . GLU   B  1 162 ? 60.841 23.832  -77.247 0.00 61.23  ? 188  GLU   B HG2  1 
ATOM   14350 H HG3  . GLU   B  1 162 ? 59.987 22.346  -77.728 0.00 61.10  ? 188  GLU   B HG3  1 
ATOM   14351 N N    . LYS   B  1 163 ? 61.946 19.241  -76.390 1.00 35.17  ? 189  LYS   B N    1 
ATOM   14352 C CA   . LYS   B  1 163 ? 63.113 18.360  -76.430 1.00 35.08  ? 189  LYS   B CA   1 
ATOM   14353 C C    . LYS   B  1 163 ? 64.351 19.206  -76.091 1.00 34.05  ? 189  LYS   B C    1 
ATOM   14354 O O    . LYS   B  1 163 ? 64.408 20.381  -76.461 1.00 33.81  ? 189  LYS   B O    1 
ATOM   14355 C CB   . LYS   B  1 163 ? 63.289 17.733  -77.825 1.00 37.96  ? 189  LYS   B CB   1 
ATOM   14356 C CG   . LYS   B  1 163 ? 62.206 16.723  -78.175 1.00 43.77  ? 189  LYS   B CG   1 
ATOM   14357 C CD   . LYS   B  1 163 ? 62.417 16.126  -79.561 1.00 49.54  ? 189  LYS   B CD   1 
ATOM   14358 C CE   . LYS   B  1 163 ? 61.428 15.024  -79.872 1.00 54.77  ? 189  LYS   B CE   1 
ATOM   14359 N NZ   . LYS   B  1 163 ? 61.681 13.788  -79.073 1.00 57.58  ? 189  LYS   B NZ   1 
ATOM   14360 H H    . LYS   B  1 163 ? 61.490 19.356  -77.290 0.00 44.41  ? 189  LYS   B H    1 
ATOM   14361 H HA   . LYS   B  1 163 ? 62.998 17.573  -75.689 0.00 43.40  ? 189  LYS   B HA   1 
ATOM   14362 H HB2  . LYS   B  1 163 ? 63.270 18.519  -78.578 0.00 48.06  ? 189  LYS   B HB2  1 
ATOM   14363 H HB3  . LYS   B  1 163 ? 64.248 17.217  -77.858 0.00 47.58  ? 189  LYS   B HB3  1 
ATOM   14364 H HG2  . LYS   B  1 163 ? 62.227 15.914  -77.446 0.00 54.25  ? 189  LYS   B HG2  1 
ATOM   14365 H HG3  . LYS   B  1 163 ? 61.235 17.217  -78.160 0.00 54.72  ? 189  LYS   B HG3  1 
ATOM   14366 H HD2  . LYS   B  1 163 ? 62.296 16.909  -80.308 0.00 62.42  ? 189  LYS   B HD2  1 
ATOM   14367 H HD3  . LYS   B  1 163 ? 63.420 15.706  -79.619 0.00 61.98  ? 189  LYS   B HD3  1 
ATOM   14368 H HE2  . LYS   B  1 163 ? 60.423 15.373  -79.643 0.00 68.31  ? 189  LYS   B HE2  1 
ATOM   14369 H HE3  . LYS   B  1 163 ? 61.503 14.765  -80.927 0.00 68.74  ? 189  LYS   B HE3  1 
ATOM   14370 H HZ1  . LYS   B  1 163 ? 61.055 13.048  -79.376 0.00 71.35  ? 189  LYS   B HZ1  1 
ATOM   14371 H HZ2  . LYS   B  1 163 ? 62.640 13.481  -79.202 0.00 71.28  ? 189  LYS   B HZ2  1 
ATOM   14372 H HZ3  . LYS   B  1 163 ? 61.522 13.967  -78.087 0.00 70.89  ? 189  LYS   B HZ3  1 
ATOM   14373 N N    . THR   B  1 164 ? 65.299 18.639  -75.361 1.00 33.61  ? 190  THR   B N    1 
ATOM   14374 C CA   . THR   B  1 164 ? 66.477 19.388  -74.935 1.00 33.63  ? 190  THR   B CA   1 
ATOM   14375 C C    . THR   B  1 164 ? 67.444 19.593  -76.085 1.00 33.40  ? 190  THR   B C    1 
ATOM   14376 O O    . THR   B  1 164 ? 67.826 18.631  -76.749 1.00 33.98  ? 190  THR   B O    1 
ATOM   14377 C CB   . THR   B  1 164 ? 67.181 18.659  -73.780 1.00 34.79  ? 190  THR   B CB   1 
ATOM   14378 O OG1  . THR   B  1 164 ? 66.225 18.309  -72.791 1.00 35.98  ? 190  THR   B OG1  1 
ATOM   14379 C CG2  . THR   B  1 164 ? 68.290 19.491  -73.152 1.00 34.87  ? 190  THR   B CG2  1 
ATOM   14380 H H    . THR   B  1 164 ? 65.286 17.672  -75.051 0.00 41.46  ? 190  THR   B H    1 
ATOM   14381 H HA   . THR   B  1 164 ? 66.162 20.360  -74.559 0.00 41.82  ? 190  THR   B HA   1 
ATOM   14382 H HB   . THR   B  1 164 ? 67.633 17.748  -74.171 0.00 42.72  ? 190  THR   B HB   1 
ATOM   14383 H HG1  . THR   B  1 164 ? 65.782 19.127  -72.444 0.00 43.74  ? 190  THR   B HG1  1 
ATOM   14384 H HG21 . THR   B  1 164 ? 68.602 19.038  -72.212 0.00 42.51  ? 190  THR   B HG21 1 
ATOM   14385 H HG22 . THR   B  1 164 ? 69.153 19.538  -73.815 0.00 43.10  ? 190  THR   B HG22 1 
ATOM   14386 H HG23 . THR   B  1 164 ? 67.935 20.502  -72.959 0.00 42.94  ? 190  THR   B HG23 1 
ATOM   14387 N N    . ASN   B  1 165 ? 67.851 20.840  -76.313 1.00 32.48  ? 191  ASN   B N    1 
ATOM   14388 C CA   . ASN   B  1 165 ? 68.838 21.162  -77.322 1.00 32.51  ? 191  ASN   B CA   1 
ATOM   14389 C C    . ASN   B  1 165 ? 70.170 21.373  -76.611 1.00 32.29  ? 191  ASN   B C    1 
ATOM   14390 O O    . ASN   B  1 165 ? 70.327 22.362  -75.896 1.00 32.66  ? 191  ASN   B O    1 
ATOM   14391 C CB   . ASN   B  1 165 ? 68.440 22.417  -78.101 1.00 33.60  ? 191  ASN   B CB   1 
ATOM   14392 C CG   . ASN   B  1 165 ? 69.483 22.814  -79.119 1.00 37.92  ? 191  ASN   B CG   1 
ATOM   14393 O OD1  . ASN   B  1 165 ? 69.934 21.996  -79.919 1.00 39.06  ? 191  ASN   B OD1  1 
ATOM   14394 N ND2  . ASN   B  1 165 ? 69.930 24.057  -79.095 1.00 39.31  ? 191  ASN   B ND2  1 
ATOM   14395 H H    . ASN   B  1 165 ? 67.492 21.657  -75.831 0.00 41.17  ? 191  ASN   B H    1 
ATOM   14396 H HA   . ASN   B  1 165 ? 68.940 20.351  -78.041 0.00 41.78  ? 191  ASN   B HA   1 
ATOM   14397 H HB2  . ASN   B  1 165 ? 67.514 22.218  -78.637 0.00 43.60  ? 191  ASN   B HB2  1 
ATOM   14398 H HB3  . ASN   B  1 165 ? 68.291 23.237  -77.401 0.00 43.43  ? 191  ASN   B HB3  1 
ATOM   14399 H HD21 . ASN   B  1 165 ? 70.631 24.349  -79.769 0.00 51.53  ? 191  ASN   B HD21 1 
ATOM   14400 H HD22 . ASN   B  1 165 ? 69.582 24.725  -78.415 0.00 51.06  ? 191  ASN   B HD22 1 
ATOM   14401 N N    . ILE   B  1 166 ? 71.121 20.451  -76.801 1.00 31.64  ? 192  ILE   B N    1 
ATOM   14402 C CA   . ILE   B  1 166 ? 72.457 20.562  -76.227 1.00 31.40  ? 192  ILE   B CA   1 
ATOM   14403 C C    . ILE   B  1 166 ? 73.319 21.174  -77.334 1.00 30.74  ? 192  ILE   B C    1 
ATOM   14404 O O    . ILE   B  1 166 ? 73.484 20.537  -78.374 1.00 30.47  ? 192  ILE   B O    1 
ATOM   14405 C CB   . ILE   B  1 166 ? 73.011 19.170  -75.798 1.00 32.30  ? 192  ILE   B CB   1 
ATOM   14406 C CG1  . ILE   B  1 166 ? 72.032 18.382  -74.871 1.00 33.75  ? 192  ILE   B CG1  1 
ATOM   14407 C CG2  . ILE   B  1 166 ? 74.396 19.315  -75.160 1.00 33.00  ? 192  ILE   B CG2  1 
ATOM   14408 C CD1  . ILE   B  1 166 ? 71.885 18.857  -73.502 1.00 35.20  ? 192  ILE   B CD1  1 
ATOM   14409 H H    . ILE   B  1 166 ? 70.995 19.607  -77.351 0.00 40.53  ? 192  ILE   B H    1 
ATOM   14410 H HA   . ILE   B  1 166 ? 72.464 21.218  -75.359 0.00 40.07  ? 192  ILE   B HA   1 
ATOM   14411 H HB   . ILE   B  1 166 ? 73.134 18.571  -76.699 0.00 41.19  ? 192  ILE   B HB   1 
ATOM   14412 H HG12 . ILE   B  1 166 ? 71.039 18.372  -75.319 0.00 42.22  ? 192  ILE   B HG12 1 
ATOM   14413 H HG13 . ILE   B  1 166 ? 72.394 17.357  -74.807 0.00 42.07  ? 192  ILE   B HG13 1 
ATOM   14414 H HG21 . ILE   B  1 166 ? 74.673 18.365  -74.704 0.00 41.61  ? 192  ILE   B HG21 1 
ATOM   14415 H HG22 . ILE   B  1 166 ? 75.129 19.584  -75.918 0.00 42.24  ? 192  ILE   B HG22 1 
ATOM   14416 H HG23 . ILE   B  1 166 ? 74.346 20.086  -74.393 0.00 41.76  ? 192  ILE   B HG23 1 
ATOM   14417 H HD11 . ILE   B  1 166 ? 71.042 18.343  -73.043 0.00 43.27  ? 192  ILE   B HD11 1 
ATOM   14418 H HD12 . ILE   B  1 166 ? 72.793 18.634  -72.944 0.00 43.51  ? 192  ILE   B HD12 1 
ATOM   14419 H HD13 . ILE   B  1 166 ? 71.707 19.931  -73.516 0.00 43.76  ? 192  ILE   B HD13 1 
ATOM   14420 N N    . GLU   B  1 167 ? 73.834 22.406  -77.149 1.00 30.20  ? 193  GLU   B N    1 
ATOM   14421 C CA   . GLU   B  1 167 ? 74.665 23.032  -78.177 1.00 30.36  ? 193  GLU   B CA   1 
ATOM   14422 C C    . GLU   B  1 167 ? 75.960 22.229  -78.364 1.00 30.04  ? 193  GLU   B C    1 
ATOM   14423 O O    . GLU   B  1 167 ? 76.595 21.862  -77.381 1.00 29.42  ? 193  GLU   B O    1 
ATOM   14424 C CB   . GLU   B  1 167 ? 74.970 24.503  -77.843 1.00 31.74  ? 193  GLU   B CB   1 
ATOM   14425 C CG   . GLU   B  1 167 ? 75.517 25.273  -79.035 1.00 37.62  ? 193  GLU   B CG   1 
ATOM   14426 C CD   . GLU   B  1 167 ? 76.010 26.666  -78.715 1.00 43.57  ? 193  GLU   B CD   1 
ATOM   14427 O OE1  . GLU   B  1 167 ? 75.526 27.255  -77.723 1.00 43.03  ? 193  GLU   B OE1  1 
ATOM   14428 O OE2  . GLU   B  1 167 ? 76.882 27.171  -79.460 1.00 46.34  ? 193  GLU   B OE2  1 
ATOM   14429 H H    . GLU   B  1 167 ? 73.698 22.974  -76.318 0.00 39.45  ? 193  GLU   B H    1 
ATOM   14430 H HA   . GLU   B  1 167 ? 74.110 23.002  -79.115 0.00 40.62  ? 193  GLU   B HA   1 
ATOM   14431 H HB2  . GLU   B  1 167 ? 74.052 24.992  -77.522 0.00 42.21  ? 193  GLU   B HB2  1 
ATOM   14432 H HB3  . GLU   B  1 167 ? 75.712 24.544  -77.048 0.00 42.20  ? 193  GLU   B HB3  1 
ATOM   14433 H HG2  . GLU   B  1 167 ? 76.357 24.731  -79.466 0.00 50.18  ? 193  GLU   B HG2  1 
ATOM   14434 H HG3  . GLU   B  1 167 ? 74.725 25.367  -79.776 0.00 50.19  ? 193  GLU   B HG3  1 
ATOM   14435 N N    . ASP   B  1 168 ? 76.336 21.933  -79.623 1.00 29.59  ? 194  ASP   B N    1 
ATOM   14436 C CA   . ASP   B  1 168 ? 77.518 21.115  -79.917 1.00 29.89  ? 194  ASP   B CA   1 
ATOM   14437 C C    . ASP   B  1 168 ? 78.786 21.604  -79.205 1.00 29.44  ? 194  ASP   B C    1 
ATOM   14438 O O    . ASP   B  1 168 ? 79.141 22.769  -79.326 1.00 29.76  ? 194  ASP   B O    1 
ATOM   14439 C CB   . ASP   B  1 168 ? 77.765 21.048  -81.432 1.00 31.87  ? 194  ASP   B CB   1 
ATOM   14440 C CG   . ASP   B  1 168 ? 78.822 20.030  -81.795 1.00 35.81  ? 194  ASP   B CG   1 
ATOM   14441 O OD1  . ASP   B  1 168 ? 78.570 18.820  -81.606 1.00 37.60  ? 194  ASP   B OD1  1 
ATOM   14442 O OD2  . ASP   B  1 168 ? 79.902 20.439  -82.250 1.00 37.43  ? 194  ASP   B OD2  1 
ATOM   14443 H H    . ASP   B  1 168 ? 75.851 22.259  -80.453 0.00 40.24  ? 194  ASP   B H    1 
ATOM   14444 H HA   . ASP   B  1 168 ? 77.311 20.101  -79.581 0.00 40.14  ? 194  ASP   B HA   1 
ATOM   14445 H HB2  . ASP   B  1 168 ? 76.842 20.765  -81.935 0.00 43.38  ? 194  ASP   B HB2  1 
ATOM   14446 H HB3  . ASP   B  1 168 ? 78.100 22.023  -81.782 0.00 43.77  ? 194  ASP   B HB3  1 
ATOM   14447 N N    . GLY   B  1 169 ? 79.420 20.728  -78.428 1.00 28.57  ? 195  GLY   B N    1 
ATOM   14448 C CA   . GLY   B  1 169 ? 80.634 21.067  -77.698 1.00 27.84  ? 195  GLY   B CA   1 
ATOM   14449 C C    . GLY   B  1 169 ? 80.427 21.941  -76.475 1.00 27.81  ? 195  GLY   B C    1 
ATOM   14450 O O    . GLY   B  1 169 ? 81.407 22.451  -75.928 1.00 27.78  ? 195  GLY   B O    1 
ATOM   14451 H H    . GLY   B  1 169 ? 79.124 19.768  -78.284 0.00 38.42  ? 195  GLY   B H    1 
ATOM   14452 H HA2  . GLY   B  1 169 ? 81.119 20.151  -77.366 0.00 37.76  ? 195  GLY   B HA2  1 
ATOM   14453 H HA3  . GLY   B  1 169 ? 81.322 21.583  -78.367 0.00 38.37  ? 195  GLY   B HA3  1 
ATOM   14454 N N    . VAL   B  1 170 ? 79.174 22.101  -75.994 1.00 27.52  ? 196  VAL   B N    1 
ATOM   14455 C CA   . VAL   B  1 170 ? 78.918 22.958  -74.831 1.00 27.84  ? 196  VAL   B CA   1 
ATOM   14456 C C    . VAL   B  1 170 ? 79.719 22.535  -73.582 1.00 27.57  ? 196  VAL   B C    1 
ATOM   14457 O O    . VAL   B  1 170 ? 80.246 23.398  -72.875 1.00 27.70  ? 196  VAL   B O    1 
ATOM   14458 C CB   . VAL   B  1 170 ? 77.404 23.082  -74.524 1.00 28.73  ? 196  VAL   B CB   1 
ATOM   14459 C CG1  . VAL   B  1 170 ? 76.813 21.774  -74.009 1.00 29.61  ? 196  VAL   B CG1  1 
ATOM   14460 C CG2  . VAL   B  1 170 ? 77.136 24.205  -73.539 1.00 29.57  ? 196  VAL   B CG2  1 
ATOM   14461 H H    . VAL   B  1 170 ? 78.340 21.666  -76.373 0.00 36.76  ? 196  VAL   B H    1 
ATOM   14462 H HA   . VAL   B  1 170 ? 79.285 23.948  -75.099 0.00 37.49  ? 196  VAL   B HA   1 
ATOM   14463 H HB   . VAL   B  1 170 ? 76.886 23.328  -75.450 0.00 38.01  ? 196  VAL   B HB   1 
ATOM   14464 H HG11 . VAL   B  1 170 ? 75.731 21.886  -73.970 0.00 38.15  ? 196  VAL   B HG11 1 
ATOM   14465 H HG12 . VAL   B  1 170 ? 77.081 20.964  -74.686 0.00 38.40  ? 196  VAL   B HG12 1 
ATOM   14466 H HG13 . VAL   B  1 170 ? 77.187 21.566  -73.007 0.00 38.10  ? 196  VAL   B HG13 1 
ATOM   14467 H HG21 . VAL   B  1 170 ? 76.064 24.271  -73.363 0.00 38.55  ? 196  VAL   B HG21 1 
ATOM   14468 H HG22 . VAL   B  1 170 ? 77.659 24.029  -72.601 0.00 38.61  ? 196  VAL   B HG22 1 
ATOM   14469 H HG23 . VAL   B  1 170 ? 77.485 25.130  -73.992 0.00 39.20  ? 196  VAL   B HG23 1 
ATOM   14470 N N    . PHE   B  1 171 ? 79.820 21.228  -73.319 1.00 26.78  ? 197  PHE   B N    1 
ATOM   14471 C CA   . PHE   B  1 171 ? 80.559 20.740  -72.149 1.00 26.70  ? 197  PHE   B CA   1 
ATOM   14472 C C    . PHE   B  1 171 ? 82.059 20.531  -72.403 1.00 27.79  ? 197  PHE   B C    1 
ATOM   14473 O O    . PHE   B  1 171 ? 82.804 20.337  -71.444 1.00 27.71  ? 197  PHE   B O    1 
ATOM   14474 C CB   . PHE   B  1 171 ? 79.967 19.401  -71.671 1.00 25.98  ? 197  PHE   B CB   1 
ATOM   14475 C CG   . PHE   B  1 171 ? 78.472 19.400  -71.482 1.00 25.84  ? 197  PHE   B CG   1 
ATOM   14476 C CD1  . PHE   B  1 171 ? 77.882 20.175  -70.495 1.00 25.99  ? 197  PHE   B CD1  1 
ATOM   14477 C CD2  . PHE   B  1 171 ? 77.658 18.608  -72.273 1.00 26.02  ? 197  PHE   B CD2  1 
ATOM   14478 C CE1  . PHE   B  1 171 ? 76.508 20.155  -70.309 1.00 26.18  ? 197  PHE   B CE1  1 
ATOM   14479 C CE2  . PHE   B  1 171 ? 76.285 18.575  -72.066 1.00 26.83  ? 197  PHE   B CE2  1 
ATOM   14480 C CZ   . PHE   B  1 171 ? 75.720 19.350  -71.087 1.00 26.25  ? 197  PHE   B CZ   1 
ATOM   14481 H H    . PHE   B  1 171 ? 79.425 20.494  -73.897 0.00 35.19  ? 197  PHE   B H    1 
ATOM   14482 H HA   . PHE   B  1 171 ? 80.455 21.451  -71.331 0.00 34.92  ? 197  PHE   B HA   1 
ATOM   14483 H HB2  . PHE   B  1 171 ? 80.218 18.633  -72.402 0.00 33.74  ? 197  PHE   B HB2  1 
ATOM   14484 H HB3  . PHE   B  1 171 ? 80.417 19.150  -70.712 0.00 33.49  ? 197  PHE   B HB3  1 
ATOM   14485 H HD1  . PHE   B  1 171 ? 78.498 20.799  -69.869 0.00 33.16  ? 197  PHE   B HD1  1 
ATOM   14486 H HD2  . PHE   B  1 171 ? 78.090 17.983  -73.035 0.00 33.36  ? 197  PHE   B HD2  1 
ATOM   14487 H HE1  . PHE   B  1 171 ? 76.063 20.761  -69.539 0.00 32.79  ? 197  PHE   B HE1  1 
ATOM   14488 H HE2  . PHE   B  1 171 ? 75.662 17.957  -72.690 0.00 33.76  ? 197  PHE   B HE2  1 
ATOM   14489 H HZ   . PHE   B  1 171 ? 74.653 19.343  -70.947 0.00 32.67  ? 197  PHE   B HZ   1 
ATOM   14490 N N    . GLU   B  1 172 ? 82.487 20.506  -73.679 1.00 28.58  ? 198  GLU   B N    1 
ATOM   14491 C CA   . GLU   B  1 172 ? 83.864 20.222  -74.095 1.00 29.83  ? 198  GLU   B CA   1 
ATOM   14492 C C    . GLU   B  1 172 ? 84.935 21.027  -73.369 1.00 30.50  ? 198  GLU   B C    1 
ATOM   14493 O O    . GLU   B  1 172 ? 85.984 20.474  -73.050 1.00 30.86  ? 198  GLU   B O    1 
ATOM   14494 C CB   . GLU   B  1 172 ? 84.009 20.442  -75.611 1.00 33.18  ? 198  GLU   B CB   1 
ATOM   14495 C CG   . GLU   B  1 172 ? 85.255 19.854  -76.232 1.00 38.97  ? 198  GLU   B CG   1 
ATOM   14496 C CD   . GLU   B  1 172 ? 85.247 19.965  -77.745 1.00 45.53  ? 198  GLU   B CD   1 
ATOM   14497 O OE1  . GLU   B  1 172 ? 84.682 20.954  -78.268 1.00 44.91  ? 198  GLU   B OE1  1 
ATOM   14498 O OE2  . GLU   B  1 172 ? 85.803 19.060  -78.407 1.00 49.50  ? 198  GLU   B OE2  1 
ATOM   14499 H H    . GLU   B  1 172 ? 81.870 20.694  -74.462 0.00 38.13  ? 198  GLU   B H    1 
ATOM   14500 H HA   . GLU   B  1 172 ? 84.056 19.167  -73.904 0.00 39.84  ? 198  GLU   B HA   1 
ATOM   14501 H HB2  . GLU   B  1 172 ? 83.160 19.995  -76.125 0.00 44.31  ? 198  GLU   B HB2  1 
ATOM   14502 H HB3  . GLU   B  1 172 ? 84.026 21.516  -75.791 0.00 44.74  ? 198  GLU   B HB3  1 
ATOM   14503 H HG2  . GLU   B  1 172 ? 86.134 20.385  -75.869 0.00 52.13  ? 198  GLU   B HG2  1 
ATOM   14504 H HG3  . GLU   B  1 172 ? 85.322 18.800  -75.972 0.00 51.65  ? 198  GLU   B HG3  1 
ATOM   14505 N N    . THR   B  1 173 ? 84.707 22.331  -73.162 1.00 30.41  ? 199  THR   B N    1 
ATOM   14506 C CA   . THR   B  1 173 ? 85.679 23.201  -72.498 1.00 31.24  ? 199  THR   B CA   1 
ATOM   14507 C C    . THR   B  1 173 ? 85.590 23.175  -70.966 1.00 30.85  ? 199  THR   B C    1 
ATOM   14508 O O    . THR   B  1 173 ? 86.398 23.836  -70.306 1.00 31.44  ? 199  THR   B O    1 
ATOM   14509 C CB   . THR   B  1 173 ? 85.541 24.624  -73.034 1.00 33.69  ? 199  THR   B CB   1 
ATOM   14510 O OG1  . THR   B  1 173 ? 84.223 25.093  -72.742 1.00 35.28  ? 199  THR   B OG1  1 
ATOM   14511 C CG2  . THR   B  1 173 ? 85.797 24.694  -74.531 1.00 34.58  ? 199  THR   B CG2  1 
ATOM   14512 H H    . THR   B  1 173 ? 83.861 22.815  -73.447 0.00 41.04  ? 199  THR   B H    1 
ATOM   14513 H HA   . THR   B  1 173 ? 86.684 22.873  -72.760 0.00 42.79  ? 199  THR   B HA   1 
ATOM   14514 H HB   . THR   B  1 173 ? 86.265 25.271  -72.538 0.00 46.09  ? 199  THR   B HB   1 
ATOM   14515 H HG1  . THR   B  1 173 ? 84.115 26.027  -73.060 0.00 47.64  ? 199  THR   B HG1  1 
ATOM   14516 H HG21 . THR   B  1 173 ? 85.814 25.734  -74.853 0.00 47.66  ? 199  THR   B HG21 1 
ATOM   14517 H HG22 . THR   B  1 173 ? 86.756 24.236  -74.768 0.00 47.58  ? 199  THR   B HG22 1 
ATOM   14518 H HG23 . THR   B  1 173 ? 85.008 24.176  -75.073 0.00 47.09  ? 199  THR   B HG23 1 
ATOM   14519 N N    . LEU   B  1 174 ? 84.655 22.402  -70.390 1.00 29.93  ? 200  LEU   B N    1 
ATOM   14520 C CA   . LEU   B  1 174 ? 84.548 22.274  -68.940 1.00 29.92  ? 200  LEU   B CA   1 
ATOM   14521 C C    . LEU   B  1 174 ? 85.501 21.134  -68.548 1.00 28.80  ? 200  LEU   B C    1 
ATOM   14522 O O    . LEU   B  1 174 ? 85.066 20.033  -68.185 1.00 28.04  ? 200  LEU   B O    1 
ATOM   14523 C CB   . LEU   B  1 174 ? 83.099 21.965  -68.518 1.00 30.69  ? 200  LEU   B CB   1 
ATOM   14524 C CG   . LEU   B  1 174 ? 82.078 23.114  -68.511 1.00 33.67  ? 200  LEU   B CG   1 
ATOM   14525 C CD1  . LEU   B  1 174 ? 82.117 23.945  -69.755 1.00 35.46  ? 200  LEU   B CD1  1 
ATOM   14526 C CD2  . LEU   B  1 174 ? 80.669 22.587  -68.267 1.00 33.86  ? 200  LEU   B CD2  1 
ATOM   14527 H H    . LEU   B  1 174 ? 83.957 21.862  -70.891 0.00 39.74  ? 200  LEU   B H    1 
ATOM   14528 H HA   . LEU   B  1 174 ? 84.858 23.189  -68.437 0.00 39.87  ? 200  LEU   B HA   1 
ATOM   14529 H HB2  . LEU   B  1 174 ? 82.699 21.143  -69.111 0.00 39.81  ? 200  LEU   B HB2  1 
ATOM   14530 H HB3  . LEU   B  1 174 ? 83.152 21.679  -67.471 0.00 39.77  ? 200  LEU   B HB3  1 
ATOM   14531 H HG   . LEU   B  1 174 ? 82.320 23.772  -67.677 0.00 43.59  ? 200  LEU   B HG   1 
ATOM   14532 H HD11 . LEU   B  1 174 ? 81.236 24.584  -69.763 0.00 46.05  ? 200  LEU   B HD11 1 
ATOM   14533 H HD12 . LEU   B  1 174 ? 83.017 24.559  -69.745 0.00 46.52  ? 200  LEU   B HD12 1 
ATOM   14534 H HD13 . LEU   B  1 174 ? 82.114 23.291  -70.626 0.00 46.14  ? 200  LEU   B HD13 1 
ATOM   14535 H HD21 . LEU   B  1 174 ? 79.984 23.427  -68.170 0.00 43.21  ? 200  LEU   B HD21 1 
ATOM   14536 H HD22 . LEU   B  1 174 ? 80.368 21.955  -69.100 0.00 43.18  ? 200  LEU   B HD22 1 
ATOM   14537 H HD23 . LEU   B  1 174 ? 80.668 22.004  -67.348 0.00 42.92  ? 200  LEU   B HD23 1 
ATOM   14538 N N    . THR   B  1 175 ? 86.807 21.426  -68.609 1.00 27.93  ? 201  THR   B N    1 
ATOM   14539 C CA   . THR   B  1 175 ? 87.873 20.449  -68.404 1.00 28.38  ? 201  THR   B CA   1 
ATOM   14540 C C    . THR   B  1 175 ? 88.113 20.041  -66.932 1.00 28.76  ? 201  THR   B C    1 
ATOM   14541 O O    . THR   B  1 175 ? 88.972 19.203  -66.683 1.00 29.41  ? 201  THR   B O    1 
ATOM   14542 C CB   . THR   B  1 175 ? 89.159 20.944  -69.081 1.00 29.26  ? 201  THR   B CB   1 
ATOM   14543 O OG1  . THR   B  1 175 ? 89.626 22.126  -68.421 1.00 29.71  ? 201  THR   B OG1  1 
ATOM   14544 C CG2  . THR   B  1 175 ? 88.948 21.221  -70.570 1.00 29.87  ? 201  THR   B CG2  1 
ATOM   14545 H H    . THR   B  1 175 ? 87.153 22.364  -68.783 0.00 38.11  ? 201  THR   B H    1 
ATOM   14546 H HA   . THR   B  1 175 ? 87.589 19.537  -68.927 0.00 38.29  ? 201  THR   B HA   1 
ATOM   14547 H HB   . THR   B  1 175 ? 89.921 20.170  -68.995 0.00 40.34  ? 201  THR   B HB   1 
ATOM   14548 H HG1  . THR   B  1 175 ? 90.457 22.451  -68.856 0.00 41.52  ? 201  THR   B HG1  1 
ATOM   14549 H HG21 . THR   B  1 175 ? 89.909 21.391  -71.053 0.00 41.63  ? 201  THR   B HG21 1 
ATOM   14550 H HG22 . THR   B  1 175 ? 88.459 20.370  -71.043 0.00 40.90  ? 201  THR   B HG22 1 
ATOM   14551 H HG23 . THR   B  1 175 ? 88.330 22.107  -70.704 0.00 41.13  ? 201  THR   B HG23 1 
ATOM   14552 N N    . ASN   B  1 176 ? 87.346 20.573  -65.976 1.00 28.43  ? 202  ASN   B N    1 
ATOM   14553 C CA   . ASN   B  1 176 ? 87.392 20.122  -64.575 1.00 28.28  ? 202  ASN   B CA   1 
ATOM   14554 C C    . ASN   B  1 176 ? 86.058 19.421  -64.173 1.00 27.20  ? 202  ASN   B C    1 
ATOM   14555 O O    . ASN   B  1 176 ? 85.881 19.092  -62.999 1.00 27.93  ? 202  ASN   B O    1 
ATOM   14556 C CB   . ASN   B  1 176 ? 87.670 21.305  -63.645 1.00 30.47  ? 202  ASN   B CB   1 
ATOM   14557 C CG   . ASN   B  1 176 ? 88.949 22.052  -63.961 1.00 35.89  ? 202  ASN   B CG   1 
ATOM   14558 O OD1  . ASN   B  1 176 ? 88.954 23.283  -64.091 1.00 38.34  ? 202  ASN   B OD1  1 
ATOM   14559 N ND2  . ASN   B  1 176 ? 90.070 21.341  -64.087 1.00 35.79  ? 202  ASN   B ND2  1 
ATOM   14560 H H    . ASN   B  1 176 ? 86.679 21.325  -66.119 0.00 37.94  ? 202  ASN   B H    1 
ATOM   14561 H HA   . ASN   B  1 176 ? 88.188 19.394  -64.428 0.00 37.75  ? 202  ASN   B HA   1 
ATOM   14562 H HB2  . ASN   B  1 176 ? 86.845 22.011  -63.719 0.00 40.32  ? 202  ASN   B HB2  1 
ATOM   14563 H HB3  . ASN   B  1 176 ? 87.751 20.939  -62.622 0.00 40.34  ? 202  ASN   B HB3  1 
ATOM   14564 H HD21 . ASN   B  1 176 ? 90.942 21.816  -64.297 0.00 48.34  ? 202  ASN   B HD21 1 
ATOM   14565 H HD22 . ASN   B  1 176 ? 90.066 20.335  -63.952 0.00 47.65  ? 202  ASN   B HD22 1 
ATOM   14566 N N    . LEU   B  1 177 ? 85.122 19.197  -65.131 1.00 25.56  ? 203  LEU   B N    1 
ATOM   14567 C CA   . LEU   B  1 177 ? 83.822 18.604  -64.844 1.00 25.27  ? 203  LEU   B CA   1 
ATOM   14568 C C    . LEU   B  1 177 ? 83.970 17.138  -64.509 1.00 24.98  ? 203  LEU   B C    1 
ATOM   14569 O O    . LEU   B  1 177 ? 84.484 16.374  -65.324 1.00 23.89  ? 203  LEU   B O    1 
ATOM   14570 C CB   . LEU   B  1 177 ? 82.890 18.766  -66.051 1.00 25.04  ? 203  LEU   B CB   1 
ATOM   14571 C CG   . LEU   B  1 177 ? 81.396 18.514  -65.815 1.00 26.06  ? 203  LEU   B CG   1 
ATOM   14572 C CD1  . LEU   B  1 177 ? 80.814 19.538  -64.823 1.00 26.54  ? 203  LEU   B CD1  1 
ATOM   14573 C CD2  . LEU   B  1 177 ? 80.637 18.550  -67.141 1.00 26.59  ? 203  LEU   B CD2  1 
ATOM   14574 H H    . LEU   B  1 177 ? 85.252 19.393  -66.118 0.00 33.64  ? 203  LEU   B H    1 
ATOM   14575 H HA   . LEU   B  1 177 ? 83.395 19.130  -63.991 0.00 32.36  ? 203  LEU   B HA   1 
ATOM   14576 H HB2  . LEU   B  1 177 ? 82.977 19.794  -66.390 0.00 32.39  ? 203  LEU   B HB2  1 
ATOM   14577 H HB3  . LEU   B  1 177 ? 83.215 18.096  -66.844 0.00 32.26  ? 203  LEU   B HB3  1 
ATOM   14578 H HG   . LEU   B  1 177 ? 81.261 17.522  -65.387 0.00 32.59  ? 203  LEU   B HG   1 
ATOM   14579 H HD11 . LEU   B  1 177 ? 79.728 19.533  -64.904 0.00 32.99  ? 203  LEU   B HD11 1 
ATOM   14580 H HD12 . LEU   B  1 177 ? 81.095 19.254  -63.810 0.00 33.19  ? 203  LEU   B HD12 1 
ATOM   14581 H HD13 . LEU   B  1 177 ? 81.201 20.530  -65.054 0.00 33.61  ? 203  LEU   B HD13 1 
ATOM   14582 H HD21 . LEU   B  1 177 ? 79.574 18.411  -66.951 0.00 33.16  ? 203  LEU   B HD21 1 
ATOM   14583 H HD22 . LEU   B  1 177 ? 80.807 19.515  -67.616 0.00 33.79  ? 203  LEU   B HD22 1 
ATOM   14584 H HD23 . LEU   B  1 177 ? 81.009 17.750  -67.779 0.00 33.58  ? 203  LEU   B HD23 1 
ATOM   14585 N N    . GLU   B  1 178 ? 83.527 16.759  -63.305 1.00 25.48  ? 204  GLU   B N    1 
ATOM   14586 C CA   . GLU   B  1 178 ? 83.582 15.397  -62.784 1.00 25.98  ? 204  GLU   B CA   1 
ATOM   14587 C C    . GLU   B  1 178 ? 82.191 14.756  -62.734 1.00 25.75  ? 204  GLU   B C    1 
ATOM   14588 O O    . GLU   B  1 178 ? 82.105 13.543  -62.866 1.00 26.36  ? 204  GLU   B O    1 
ATOM   14589 C CB   . GLU   B  1 178 ? 84.211 15.398  -61.384 1.00 28.16  ? 204  GLU   B CB   1 
ATOM   14590 C CG   . GLU   B  1 178 ? 85.665 15.838  -61.395 1.00 33.30  ? 204  GLU   B CG   1 
ATOM   14591 C CD   . GLU   B  1 178 ? 86.348 15.788  -60.042 1.00 40.66  ? 204  GLU   B CD   1 
ATOM   14592 O OE1  . GLU   B  1 178 ? 85.638 15.718  -59.010 1.00 41.83  ? 204  GLU   B OE1  1 
ATOM   14593 O OE2  . GLU   B  1 178 ? 87.599 15.832  -60.016 1.00 44.63  ? 204  GLU   B OE2  1 
ATOM   14594 H H    . GLU   B  1 178 ? 83.104 17.399  -62.640 0.00 32.09  ? 204  GLU   B H    1 
ATOM   14595 H HA   . GLU   B  1 178 ? 84.208 14.775  -63.421 0.00 32.81  ? 204  GLU   B HA   1 
ATOM   14596 H HB2  . GLU   B  1 178 ? 83.649 16.079  -60.746 0.00 35.12  ? 204  GLU   B HB2  1 
ATOM   14597 H HB3  . GLU   B  1 178 ? 84.170 14.388  -60.978 0.00 35.12  ? 204  GLU   B HB3  1 
ATOM   14598 H HG2  . GLU   B  1 178 ? 86.221 15.187  -62.068 0.00 42.21  ? 204  GLU   B HG2  1 
ATOM   14599 H HG3  . GLU   B  1 178 ? 85.719 16.867  -61.748 0.00 42.21  ? 204  GLU   B HG3  1 
ATOM   14600 N N    . LEU   B  1 179 ? 81.113 15.538  -62.527 1.00 24.69  ? 205  LEU   B N    1 
ATOM   14601 C CA   . LEU   B  1 179 ? 79.766 14.987  -62.473 1.00 23.98  ? 205  LEU   B CA   1 
ATOM   14602 C C    . LEU   B  1 179 ? 78.845 15.778  -63.402 1.00 23.55  ? 205  LEU   B C    1 
ATOM   14603 O O    . LEU   B  1 179 ? 78.778 17.009  -63.316 1.00 23.43  ? 205  LEU   B O    1 
ATOM   14604 C CB   . LEU   B  1 179 ? 79.226 15.002  -61.032 1.00 23.75  ? 205  LEU   B CB   1 
ATOM   14605 C CG   . LEU   B  1 179 ? 77.840 14.376  -60.785 1.00 25.18  ? 205  LEU   B CG   1 
ATOM   14606 C CD1  . LEU   B  1 179 ? 77.693 13.953  -59.316 1.00 25.60  ? 205  LEU   B CD1  1 
ATOM   14607 C CD2  . LEU   B  1 179 ? 76.703 15.334  -61.133 1.00 25.71  ? 205  LEU   B CD2  1 
ATOM   14608 H H    . LEU   B  1 179 ? 81.141 16.542  -62.379 0.00 30.38  ? 205  LEU   B H    1 
ATOM   14609 H HA   . LEU   B  1 179 ? 79.764 13.949  -62.804 0.00 28.88  ? 205  LEU   B HA   1 
ATOM   14610 H HB2  . LEU   B  1 179 ? 79.936 14.457  -60.411 0.00 28.44  ? 205  LEU   B HB2  1 
ATOM   14611 H HB3  . LEU   B  1 179 ? 79.180 16.034  -60.689 0.00 28.45  ? 205  LEU   B HB3  1 
ATOM   14612 H HG   . LEU   B  1 179 ? 77.732 13.486  -61.403 0.00 29.55  ? 205  LEU   B HG   1 
ATOM   14613 H HD11 . LEU   B  1 179 ? 76.698 13.536  -59.163 0.00 29.57  ? 205  LEU   B HD11 1 
ATOM   14614 H HD12 . LEU   B  1 179 ? 78.447 13.201  -59.083 0.00 30.00  ? 205  LEU   B HD12 1 
ATOM   14615 H HD13 . LEU   B  1 179 ? 77.830 14.828  -58.683 0.00 29.97  ? 205  LEU   B HD13 1 
ATOM   14616 H HD21 . LEU   B  1 179 ? 75.756 14.879  -60.846 0.00 29.79  ? 205  LEU   B HD21 1 
ATOM   14617 H HD22 . LEU   B  1 179 ? 76.842 16.269  -60.592 0.00 30.20  ? 205  LEU   B HD22 1 
ATOM   14618 H HD23 . LEU   B  1 179 ? 76.703 15.521  -62.205 0.00 30.26  ? 205  LEU   B HD23 1 
ATOM   14619 N N    . LEU   B  1 180 ? 78.163 15.067  -64.306 1.00 22.61  ? 206  LEU   B N    1 
ATOM   14620 C CA   . LEU   B  1 180 ? 77.205 15.680  -65.216 1.00 22.26  ? 206  LEU   B CA   1 
ATOM   14621 C C    . LEU   B  1 180 ? 75.937 14.864  -65.113 1.00 22.65  ? 206  LEU   B C    1 
ATOM   14622 O O    . LEU   B  1 180 ? 75.958 13.668  -65.398 1.00 23.74  ? 206  LEU   B O    1 
ATOM   14623 C CB   . LEU   B  1 180 ? 77.726 15.676  -66.660 1.00 21.88  ? 206  LEU   B CB   1 
ATOM   14624 C CG   . LEU   B  1 180 ? 76.764 16.181  -67.742 1.00 23.00  ? 206  LEU   B CG   1 
ATOM   14625 C CD1  . LEU   B  1 180 ? 76.347 17.627  -67.477 1.00 23.53  ? 206  LEU   B CD1  1 
ATOM   14626 C CD2  . LEU   B  1 180 ? 77.407 16.063  -69.126 1.00 23.68  ? 206  LEU   B CD2  1 
ATOM   14627 H H    . LEU   B  1 180 ? 78.243 14.063  -64.431 0.00 27.06  ? 206  LEU   B H    1 
ATOM   14628 H HA   . LEU   B  1 180 ? 76.992 16.706  -64.921 0.00 26.74  ? 206  LEU   B HA   1 
ATOM   14629 H HB2  . LEU   B  1 180 ? 78.612 16.309  -66.698 0.00 26.91  ? 206  LEU   B HB2  1 
ATOM   14630 H HB3  . LEU   B  1 180 ? 78.002 14.655  -66.920 0.00 26.61  ? 206  LEU   B HB3  1 
ATOM   14631 H HG   . LEU   B  1 180 ? 75.865 15.569  -67.758 0.00 27.74  ? 206  LEU   B HG   1 
ATOM   14632 H HD11 . LEU   B  1 180 ? 75.816 18.007  -68.349 0.00 28.83  ? 206  LEU   B HD11 1 
ATOM   14633 H HD12 . LEU   B  1 180 ? 75.689 17.655  -66.610 0.00 28.41  ? 206  LEU   B HD12 1 
ATOM   14634 H HD13 . LEU   B  1 180 ? 77.236 18.227  -67.291 0.00 28.96  ? 206  LEU   B HD13 1 
ATOM   14635 H HD21 . LEU   B  1 180 ? 76.697 16.404  -69.878 0.00 29.28  ? 206  LEU   B HD21 1 
ATOM   14636 H HD22 . LEU   B  1 180 ? 78.304 16.680  -69.154 0.00 29.51  ? 206  LEU   B HD22 1 
ATOM   14637 H HD23 . LEU   B  1 180 ? 77.667 15.021  -69.307 0.00 29.21  ? 206  LEU   B HD23 1 
ATOM   14638 N N    . SER   B  1 181 ? 74.839 15.492  -64.712 1.00 22.06  ? 207  SER   B N    1 
ATOM   14639 C CA   . SER   B  1 181 ? 73.560 14.799  -64.613 1.00 21.85  ? 207  SER   B CA   1 
ATOM   14640 C C    . SER   B  1 181 ? 72.549 15.446  -65.542 1.00 21.92  ? 207  SER   B C    1 
ATOM   14641 O O    . SER   B  1 181 ? 72.194 16.601  -65.345 1.00 22.31  ? 207  SER   B O    1 
ATOM   14642 C CB   . SER   B  1 181 ? 73.050 14.778  -63.172 1.00 22.32  ? 207  SER   B CB   1 
ATOM   14643 O OG   . SER   B  1 181 ? 71.776 14.156  -63.106 1.00 23.53  ? 207  SER   B OG   1 
ATOM   14644 H H    . SER   B  1 181 ? 74.791 16.471  -64.449 0.00 25.91  ? 207  SER   B H    1 
ATOM   14645 H HA   . SER   B  1 181 ? 73.683 13.772  -64.944 0.00 25.22  ? 207  SER   B HA   1 
ATOM   14646 H HB2  . SER   B  1 181 ? 73.750 14.214  -62.557 0.00 25.44  ? 207  SER   B HB2  1 
ATOM   14647 H HB3  . SER   B  1 181 ? 72.963 15.794  -62.796 0.00 25.52  ? 207  SER   B HB3  1 
ATOM   14648 H HG   . SER   B  1 181 ? 71.451 14.147  -62.168 0.00 26.41  ? 207  SER   B HG   1 
ATOM   14649 N N    . LEU   B  1 182 ? 72.117 14.711  -66.578 1.00 21.22  ? 208  LEU   B N    1 
ATOM   14650 C CA   . LEU   B  1 182 ? 71.093 15.170  -67.525 1.00 21.05  ? 208  LEU   B CA   1 
ATOM   14651 C C    . LEU   B  1 182 ? 69.861 14.246  -67.522 1.00 20.77  ? 208  LEU   B C    1 
ATOM   14652 O O    . LEU   B  1 182 ? 69.034 14.342  -68.417 1.00 19.48  ? 208  LEU   B O    1 
ATOM   14653 C CB   . LEU   B  1 182 ? 71.682 15.219  -68.940 1.00 21.64  ? 208  LEU   B CB   1 
ATOM   14654 C CG   . LEU   B  1 182 ? 72.808 16.208  -69.175 1.00 24.51  ? 208  LEU   B CG   1 
ATOM   14655 C CD1  . LEU   B  1 182 ? 73.643 15.793  -70.397 1.00 25.15  ? 208  LEU   B CD1  1 
ATOM   14656 C CD2  . LEU   B  1 182 ? 72.242 17.612  -69.393 1.00 26.41  ? 208  LEU   B CD2  1 
ATOM   14657 H H    . LEU   B  1 182 ? 72.460 13.782  -66.803 0.00 24.59  ? 208  LEU   B H    1 
ATOM   14658 H HA   . LEU   B  1 182 ? 70.743 16.165  -67.254 0.00 24.50  ? 208  LEU   B HA   1 
ATOM   14659 H HB2  . LEU   B  1 182 ? 72.056 14.229  -69.190 0.00 25.61  ? 208  LEU   B HB2  1 
ATOM   14660 H HB3  . LEU   B  1 182 ? 70.894 15.495  -69.640 0.00 25.70  ? 208  LEU   B HB3  1 
ATOM   14661 H HG   . LEU   B  1 182 ? 73.475 16.241  -68.315 0.00 29.30  ? 208  LEU   B HG   1 
ATOM   14662 H HD11 . LEU   B  1 182 ? 74.399 16.554  -70.582 0.00 30.79  ? 208  LEU   B HD11 1 
ATOM   14663 H HD12 . LEU   B  1 182 ? 74.118 14.836  -70.192 0.00 30.44  ? 208  LEU   B HD12 1 
ATOM   14664 H HD13 . LEU   B  1 182 ? 72.984 15.706  -71.260 0.00 30.62  ? 208  LEU   B HD13 1 
ATOM   14665 H HD21 . LEU   B  1 182 ? 73.033 18.341  -69.224 0.00 32.03  ? 208  LEU   B HD21 1 
ATOM   14666 H HD22 . LEU   B  1 182 ? 71.892 17.689  -70.421 0.00 32.04  ? 208  LEU   B HD22 1 
ATOM   14667 H HD23 . LEU   B  1 182 ? 71.413 17.795  -68.713 0.00 31.58  ? 208  LEU   B HD23 1 
ATOM   14668 N N    . SER   B  1 183 ? 69.697 13.408  -66.482 1.00 20.88  ? 209  SER   B N    1 
ATOM   14669 C CA   . SER   B  1 183 ? 68.582 12.473  -66.391 1.00 20.94  ? 209  SER   B CA   1 
ATOM   14670 C C    . SER   B  1 183 ? 67.222 13.142  -66.445 1.00 20.90  ? 209  SER   B C    1 
ATOM   14671 O O    . SER   B  1 183 ? 67.088 14.289  -66.054 1.00 20.85  ? 209  SER   B O    1 
ATOM   14672 C CB   . SER   B  1 183 ? 68.686 11.675  -65.089 1.00 21.46  ? 209  SER   B CB   1 
ATOM   14673 O OG   . SER   B  1 183 ? 69.908 10.955  -65.031 1.00 21.74  ? 209  SER   B OG   1 
ATOM   14674 H H    . SER   B  1 183 ? 70.324 13.381  -65.684 0.00 23.60  ? 209  SER   B H    1 
ATOM   14675 H HA   . SER   B  1 183 ? 68.645 11.770  -67.221 0.00 23.66  ? 209  SER   B HA   1 
ATOM   14676 H HB2  . SER   B  1 183 ? 68.647 12.367  -64.250 0.00 23.71  ? 209  SER   B HB2  1 
ATOM   14677 H HB3  . SER   B  1 183 ? 67.848 10.983  -65.037 0.00 23.68  ? 209  SER   B HB3  1 
ATOM   14678 H HG   . SER   B  1 183 ? 69.961 10.446  -64.180 0.00 24.09  ? 209  SER   B HG   1 
ATOM   14679 N N    . PHE   B  1 184 ? 66.195 12.418  -66.913 1.00 21.16  ? 210  PHE   B N    1 
ATOM   14680 C CA   . PHE   B  1 184 ? 64.826 12.929  -66.955 1.00 21.22  ? 210  PHE   B CA   1 
ATOM   14681 C C    . PHE   B  1 184 ? 64.719 14.215  -67.767 1.00 22.11  ? 210  PHE   B C    1 
ATOM   14682 O O    . PHE   B  1 184 ? 64.193 15.243  -67.324 1.00 22.00  ? 210  PHE   B O    1 
ATOM   14683 C CB   . PHE   B  1 184 ? 64.252 13.077  -65.523 1.00 20.92  ? 210  PHE   B CB   1 
ATOM   14684 C CG   . PHE   B  1 184 ? 64.114 11.741  -64.833 1.00 21.14  ? 210  PHE   B CG   1 
ATOM   14685 C CD1  . PHE   B  1 184 ? 65.172 11.194  -64.131 1.00 21.71  ? 210  PHE   B CD1  1 
ATOM   14686 C CD2  . PHE   B  1 184 ? 62.952 10.996  -64.958 1.00 21.98  ? 210  PHE   B CD2  1 
ATOM   14687 C CE1  . PHE   B  1 184 ? 65.054 9.942   -63.528 1.00 22.19  ? 210  PHE   B CE1  1 
ATOM   14688 C CE2  . PHE   B  1 184 ? 62.824 9.762   -64.322 1.00 22.47  ? 210  PHE   B CE2  1 
ATOM   14689 C CZ   . PHE   B  1 184 ? 63.886 9.226   -63.647 1.00 21.82  ? 210  PHE   B CZ   1 
ATOM   14690 H H    . PHE   B  1 184 ? 66.284 11.466  -67.255 0.00 23.69  ? 210  PHE   B H    1 
ATOM   14691 H HA   . PHE   B  1 184 ? 64.217 12.189  -67.473 0.00 23.75  ? 210  PHE   B HA   1 
ATOM   14692 H HB2  . PHE   B  1 184 ? 64.906 13.697  -64.914 0.00 22.97  ? 210  PHE   B HB2  1 
ATOM   14693 H HB3  . PHE   B  1 184 ? 63.259 13.523  -65.575 0.00 23.01  ? 210  PHE   B HB3  1 
ATOM   14694 H HD1  . PHE   B  1 184 ? 66.092 11.747  -64.042 0.00 23.66  ? 210  PHE   B HD1  1 
ATOM   14695 H HD2  . PHE   B  1 184 ? 62.118 11.403  -65.505 0.00 24.05  ? 210  PHE   B HD2  1 
ATOM   14696 H HE1  . PHE   B  1 184 ? 65.877 9.533   -62.966 0.00 23.89  ? 210  PHE   B HE1  1 
ATOM   14697 H HE2  . PHE   B  1 184 ? 61.914 9.196   -64.425 0.00 24.28  ? 210  PHE   B HE2  1 
ATOM   14698 H HZ   . PHE   B  1 184 ? 63.787 8.268   -63.162 0.00 23.28  ? 210  PHE   B HZ   1 
ATOM   14699 N N    . ASN   B  1 185 ? 65.269 14.125  -68.975 1.00 22.37  ? 211  ASN   B N    1 
ATOM   14700 C CA   . ASN   B  1 185 ? 65.234 15.132  -70.040 1.00 22.70  ? 211  ASN   B CA   1 
ATOM   14701 C C    . ASN   B  1 185 ? 65.086 14.342  -71.352 1.00 23.87  ? 211  ASN   B C    1 
ATOM   14702 O O    . ASN   B  1 185 ? 65.476 13.179  -71.377 1.00 24.28  ? 211  ASN   B O    1 
ATOM   14703 C CB   . ASN   B  1 185 ? 66.522 15.940  -70.061 1.00 22.88  ? 211  ASN   B CB   1 
ATOM   14704 C CG   . ASN   B  1 185 ? 66.617 16.940  -68.922 1.00 24.02  ? 211  ASN   B CG   1 
ATOM   14705 O OD1  . ASN   B  1 185 ? 65.727 17.774  -68.737 1.00 25.63  ? 211  ASN   B OD1  1 
ATOM   14706 N ND2  . ASN   B  1 185 ? 67.679 16.891  -68.142 1.00 21.69  ? 211  ASN   B ND2  1 
ATOM   14707 H H    . ASN   B  1 185 ? 65.801 13.305  -69.249 0.00 25.75  ? 211  ASN   B H    1 
ATOM   14708 H HA   . ASN   B  1 185 ? 64.379 15.796  -69.921 0.00 26.54  ? 211  ASN   B HA   1 
ATOM   14709 H HB2  . ASN   B  1 185 ? 67.364 15.252  -70.002 0.00 26.87  ? 211  ASN   B HB2  1 
ATOM   14710 H HB3  . ASN   B  1 185 ? 66.568 16.498  -70.995 0.00 27.25  ? 211  ASN   B HB3  1 
ATOM   14711 H HD21 . ASN   B  1 185 ? 67.765 17.549  -67.372 0.00 25.16  ? 211  ASN   B HD21 1 
ATOM   14712 H HD22 . ASN   B  1 185 ? 68.412 16.206  -68.297 0.00 25.24  ? 211  ASN   B HD22 1 
ATOM   14713 N N    . SER   B  1 186 ? 64.522 14.928  -72.412 1.00 24.35  ? 212  SER   B N    1 
ATOM   14714 C CA   . SER   B  1 186 ? 64.409 14.213  -73.686 1.00 25.93  ? 212  SER   B CA   1 
ATOM   14715 C C    . SER   B  1 186 ? 65.650 14.537  -74.512 1.00 27.03  ? 212  SER   B C    1 
ATOM   14716 O O    . SER   B  1 186 ? 65.699 15.583  -75.169 1.00 28.62  ? 212  SER   B O    1 
ATOM   14717 C CB   . SER   B  1 186 ? 63.128 14.590  -74.415 1.00 27.71  ? 212  SER   B CB   1 
ATOM   14718 O OG   . SER   B  1 186 ? 63.097 14.011  -75.711 1.00 31.73  ? 212  SER   B OG   1 
ATOM   14719 H H    . SER   B  1 186 ? 64.146 15.871  -72.418 0.00 29.23  ? 212  SER   B H    1 
ATOM   14720 H HA   . SER   B  1 186 ? 64.373 13.137  -73.519 0.00 31.20  ? 212  SER   B HA   1 
ATOM   14721 H HB2  . SER   B  1 186 ? 62.280 14.214  -73.845 0.00 33.52  ? 212  SER   B HB2  1 
ATOM   14722 H HB3  . SER   B  1 186 ? 63.067 15.673  -74.490 0.00 33.90  ? 212  SER   B HB3  1 
ATOM   14723 H HG   . SER   B  1 186 ? 63.476 13.094  -75.697 0.00 38.85  ? 212  SER   B HG   1 
ATOM   14724 N N    . LEU   B  1 187 ? 66.667 13.658  -74.464 1.00 26.05  ? 213  LEU   B N    1 
ATOM   14725 C CA   . LEU   B  1 187 ? 67.925 13.875  -75.181 1.00 26.12  ? 213  LEU   B CA   1 
ATOM   14726 C C    . LEU   B  1 187 ? 68.003 13.140  -76.525 1.00 27.89  ? 213  LEU   B C    1 
ATOM   14727 O O    . LEU   B  1 187 ? 68.632 13.667  -77.447 1.00 28.08  ? 213  LEU   B O    1 
ATOM   14728 C CB   . LEU   B  1 187 ? 69.129 13.432  -74.333 1.00 24.80  ? 213  LEU   B CB   1 
ATOM   14729 C CG   . LEU   B  1 187 ? 69.267 13.992  -72.907 1.00 25.27  ? 213  LEU   B CG   1 
ATOM   14730 C CD1  . LEU   B  1 187 ? 70.568 13.550  -72.304 1.00 24.70  ? 213  LEU   B CD1  1 
ATOM   14731 C CD2  . LEU   B  1 187 ? 69.170 15.506  -72.880 1.00 26.01  ? 213  LEU   B CD2  1 
ATOM   14732 H H    . LEU   B  1 187 ? 66.648 12.793  -73.934 0.00 31.55  ? 213  LEU   B H    1 
ATOM   14733 H HA   . LEU   B  1 187 ? 68.056 14.936  -75.391 0.00 32.38  ? 213  LEU   B HA   1 
ATOM   14734 H HB2  . LEU   B  1 187 ? 69.104 12.346  -74.258 0.00 30.31  ? 213  LEU   B HB2  1 
ATOM   14735 H HB3  . LEU   B  1 187 ? 70.031 13.725  -74.867 0.00 30.69  ? 213  LEU   B HB3  1 
ATOM   14736 H HG   . LEU   B  1 187 ? 68.455 13.614  -72.288 0.00 30.30  ? 213  LEU   B HG   1 
ATOM   14737 H HD11 . LEU   B  1 187 ? 70.595 13.846  -71.256 0.00 29.57  ? 213  LEU   B HD11 1 
ATOM   14738 H HD12 . LEU   B  1 187 ? 70.647 12.468  -72.386 0.00 29.79  ? 213  LEU   B HD12 1 
ATOM   14739 H HD13 . LEU   B  1 187 ? 71.386 14.026  -72.843 0.00 30.13  ? 213  LEU   B HD13 1 
ATOM   14740 H HD21 . LEU   B  1 187 ? 69.514 15.867  -71.912 0.00 31.41  ? 213  LEU   B HD21 1 
ATOM   14741 H HD22 . LEU   B  1 187 ? 69.783 15.921  -73.678 0.00 31.96  ? 213  LEU   B HD22 1 
ATOM   14742 H HD23 . LEU   B  1 187 ? 68.127 15.783  -73.026 0.00 31.60  ? 213  LEU   B HD23 1 
ATOM   14743 N N    . SER   B  1 188 ? 67.474 11.895  -76.616 1.00 28.34  ? 214  SER   B N    1 
ATOM   14744 C CA   . SER   B  1 188 ? 67.520 11.062  -77.839 1.00 29.20  ? 214  SER   B CA   1 
ATOM   14745 C C    . SER   B  1 188 ? 68.897 10.438  -78.139 1.00 29.69  ? 214  SER   B C    1 
ATOM   14746 O O    . SER   B  1 188 ? 68.949 9.334   -78.676 1.00 29.65  ? 214  SER   B O    1 
ATOM   14747 C CB   . SER   B  1 188 ? 67.011 11.818  -79.068 1.00 30.25  ? 214  SER   B CB   1 
ATOM   14748 O OG   . SER   B  1 188 ? 65.629 12.114  -78.966 1.00 33.21  ? 214  SER   B OG   1 
ATOM   14749 H H    . SER   B  1 188 ? 67.005 11.429  -75.847 0.00 34.87  ? 214  SER   B H    1 
ATOM   14750 H HA   . SER   B  1 188 ? 66.846 10.221  -77.679 0.00 36.52  ? 214  SER   B HA   1 
ATOM   14751 H HB2  . SER   B  1 188 ? 67.565 12.747  -79.197 0.00 38.49  ? 214  SER   B HB2  1 
ATOM   14752 H HB3  . SER   B  1 188 ? 67.163 11.187  -79.943 0.00 38.69  ? 214  SER   B HB3  1 
ATOM   14753 H HG   . SER   B  1 188 ? 65.325 12.606  -79.774 0.00 42.20  ? 214  SER   B HG   1 
ATOM   14754 N N    . HIS   B  1 189 ? 69.994 11.140  -77.855 1.00 29.90  ? 215  HIS   B N    1 
ATOM   14755 C CA   . HIS   B  1 189 ? 71.344 10.624  -78.094 1.00 30.54  ? 215  HIS   B CA   1 
ATOM   14756 C C    . HIS   B  1 189 ? 72.277 11.079  -76.986 1.00 30.18  ? 215  HIS   B C    1 
ATOM   14757 O O    . HIS   B  1 189 ? 72.075 12.147  -76.402 1.00 30.05  ? 215  HIS   B O    1 
ATOM   14758 C CB   . HIS   B  1 189 ? 71.891 11.159  -79.435 1.00 32.83  ? 215  HIS   B CB   1 
ATOM   14759 C CG   . HIS   B  1 189 ? 71.005 10.879  -80.603 1.00 37.62  ? 215  HIS   B CG   1 
ATOM   14760 N ND1  . HIS   B  1 189 ? 71.156 9.735   -81.364 1.00 40.48  ? 215  HIS   B ND1  1 
ATOM   14761 C CD2  . HIS   B  1 189 ? 69.951 11.584  -81.077 1.00 39.50  ? 215  HIS   B CD2  1 
ATOM   14762 C CE1  . HIS   B  1 189 ? 70.203 9.787   -82.285 1.00 41.12  ? 215  HIS   B CE1  1 
ATOM   14763 N NE2  . HIS   B  1 189 ? 69.453 10.882  -82.146 1.00 41.06  ? 215  HIS   B NE2  1 
ATOM   14764 H H    . HIS   B  1 189 ? 69.997 12.078  -77.469 0.00 37.57  ? 215  HIS   B H    1 
ATOM   14765 H HA   . HIS   B  1 189 ? 71.352 9.536   -78.116 0.00 38.64  ? 215  HIS   B HA   1 
ATOM   14766 H HB2  . HIS   B  1 189 ? 72.011 12.239  -79.362 0.00 41.98  ? 215  HIS   B HB2  1 
ATOM   14767 H HB3  . HIS   B  1 189 ? 72.855 10.691  -79.631 0.00 42.13  ? 215  HIS   B HB3  1 
ATOM   14768 H HD2  . HIS   B  1 189 ? 69.575 12.516  -80.690 0.00 50.28  ? 215  HIS   B HD2  1 
ATOM   14769 H HE1  . HIS   B  1 189 ? 70.048 9.035   -83.043 0.00 53.18  ? 215  HIS   B HE1  1 
ATOM   14770 H HE2  . HIS   B  1 189 ? 68.656 11.141  -82.719 0.00 52.89  ? 215  HIS   B HE2  1 
ATOM   14771 N N    . VAL   B  1 190 ? 73.355 10.323  -76.742 1.00 29.86  ? 216  VAL   B N    1 
ATOM   14772 C CA   . VAL   B  1 190 ? 74.380 10.724  -75.771 1.00 30.20  ? 216  VAL   B CA   1 
ATOM   14773 C C    . VAL   B  1 190 ? 75.056 11.982  -76.340 1.00 30.93  ? 216  VAL   B C    1 
ATOM   14774 O O    . VAL   B  1 190 ? 75.398 11.964  -77.521 1.00 31.32  ? 216  VAL   B O    1 
ATOM   14775 C CB   . VAL   B  1 190 ? 75.433 9.607   -75.555 1.00 30.42  ? 216  VAL   B CB   1 
ATOM   14776 C CG1  . VAL   B  1 190 ? 76.610 10.107  -74.709 1.00 30.29  ? 216  VAL   B CG1  1 
ATOM   14777 C CG2  . VAL   B  1 190 ? 74.789 8.370   -74.932 1.00 31.03  ? 216  VAL   B CG2  1 
ATOM   14778 H H    . VAL   B  1 190 ? 73.548 9.443   -77.212 0.00 37.77  ? 216  VAL   B H    1 
ATOM   14779 H HA   . VAL   B  1 190 ? 73.899 10.916  -74.815 0.00 37.48  ? 216  VAL   B HA   1 
ATOM   14780 H HB   . VAL   B  1 190 ? 75.830 9.315   -76.526 0.00 38.58  ? 216  VAL   B HB   1 
ATOM   14781 H HG11 . VAL   B  1 190 ? 77.218 9.252   -74.418 0.00 38.03  ? 216  VAL   B HG11 1 
ATOM   14782 H HG12 . VAL   B  1 190 ? 77.226 10.793  -75.290 0.00 38.33  ? 216  VAL   B HG12 1 
ATOM   14783 H HG13 . VAL   B  1 190 ? 76.226 10.602  -73.819 0.00 37.69  ? 216  VAL   B HG13 1 
ATOM   14784 H HG21 . VAL   B  1 190 ? 75.562 7.642   -74.693 0.00 38.71  ? 216  VAL   B HG21 1 
ATOM   14785 H HG22 . VAL   B  1 190 ? 74.257 8.663   -74.029 0.00 38.27  ? 216  VAL   B HG22 1 
ATOM   14786 H HG23 . VAL   B  1 190 ? 74.090 7.939   -75.647 0.00 38.75  ? 216  VAL   B HG23 1 
ATOM   14787 N N    . PRO   B  1 191 ? 75.180 13.090  -75.581 1.00 31.09  ? 217  PRO   B N    1 
ATOM   14788 C CA   . PRO   B  1 191 ? 75.792 14.287  -76.168 1.00 30.99  ? 217  PRO   B CA   1 
ATOM   14789 C C    . PRO   B  1 191 ? 77.238 14.048  -76.583 1.00 31.87  ? 217  PRO   B C    1 
ATOM   14790 O O    . PRO   B  1 191 ? 78.004 13.478  -75.802 1.00 32.51  ? 217  PRO   B O    1 
ATOM   14791 C CB   . PRO   B  1 191 ? 75.739 15.334  -75.048 1.00 31.82  ? 217  PRO   B CB   1 
ATOM   14792 C CG   . PRO   B  1 191 ? 74.938 14.752  -73.955 1.00 32.20  ? 217  PRO   B CG   1 
ATOM   14793 C CD   . PRO   B  1 191 ? 74.779 13.299  -74.171 1.00 30.37  ? 217  PRO   B CD   1 
ATOM   14794 H HA   . PRO   B  1 191 ? 75.184 14.631  -77.002 0.00 39.54  ? 217  PRO   B HA   1 
ATOM   14795 H HB2  . PRO   B  1 191 ? 76.746 15.559  -74.704 0.00 40.20  ? 217  PRO   B HB2  1 
ATOM   14796 H HB3  . PRO   B  1 191 ? 75.259 16.234  -75.430 0.00 40.22  ? 217  PRO   B HB3  1 
ATOM   14797 H HG2  . PRO   B  1 191 ? 75.451 14.931  -73.011 0.00 39.88  ? 217  PRO   B HG2  1 
ATOM   14798 H HG3  . PRO   B  1 191 ? 73.962 15.234  -73.943 0.00 39.92  ? 217  PRO   B HG3  1 
ATOM   14799 H HD2  . PRO   B  1 191 ? 75.430 12.748  -73.495 0.00 37.64  ? 217  PRO   B HD2  1 
ATOM   14800 H HD3  . PRO   B  1 191 ? 73.732 13.040  -74.021 0.00 37.52  ? 217  PRO   B HD3  1 
ATOM   14801 N N    . PRO   B  1 192 ? 77.645 14.486  -77.787 1.00 31.40  ? 218  PRO   B N    1 
ATOM   14802 C CA   . PRO   B  1 192 ? 79.055 14.335  -78.163 1.00 30.79  ? 218  PRO   B CA   1 
ATOM   14803 C C    . PRO   B  1 192 ? 79.941 15.359  -77.455 1.00 29.88  ? 218  PRO   B C    1 
ATOM   14804 O O    . PRO   B  1 192 ? 79.450 16.301  -76.818 1.00 29.83  ? 218  PRO   B O    1 
ATOM   14805 C CB   . PRO   B  1 192 ? 79.041 14.532  -79.683 1.00 32.17  ? 218  PRO   B CB   1 
ATOM   14806 C CG   . PRO   B  1 192 ? 77.854 15.360  -79.961 1.00 32.74  ? 218  PRO   B CG   1 
ATOM   14807 C CD   . PRO   B  1 192 ? 76.870 15.182  -78.835 1.00 31.02  ? 218  PRO   B CD   1 
ATOM   14808 H HA   . PRO   B  1 192 ? 79.420 13.332  -77.946 0.00 40.32  ? 218  PRO   B HA   1 
ATOM   14809 H HB2  . PRO   B  1 192 ? 79.950 15.045  -79.994 0.00 42.89  ? 218  PRO   B HB2  1 
ATOM   14810 H HB3  . PRO   B  1 192 ? 78.960 13.566  -80.179 0.00 42.64  ? 218  PRO   B HB3  1 
ATOM   14811 H HG2  . PRO   B  1 192 ? 78.156 16.404  -80.032 0.00 43.35  ? 218  PRO   B HG2  1 
ATOM   14812 H HG3  . PRO   B  1 192 ? 77.407 15.038  -80.900 0.00 43.40  ? 218  PRO   B HG3  1 
ATOM   14813 H HD2  . PRO   B  1 192 ? 76.530 16.151  -78.474 0.00 40.43  ? 218  PRO   B HD2  1 
ATOM   14814 H HD3  . PRO   B  1 192 ? 76.036 14.565  -79.165 0.00 40.44  ? 218  PRO   B HD3  1 
ATOM   14815 N N    . LYS   B  1 193 ? 81.250 15.161  -77.558 1.00 29.04  ? 219  LYS   B N    1 
ATOM   14816 C CA   . LYS   B  1 193 ? 82.260 16.079  -77.041 1.00 29.02  ? 219  LYS   B CA   1 
ATOM   14817 C C    . LYS   B  1 193 ? 82.123 16.317  -75.544 1.00 29.28  ? 219  LYS   B C    1 
ATOM   14818 O O    . LYS   B  1 193 ? 81.967 17.449  -75.091 1.00 29.37  ? 219  LYS   B O    1 
ATOM   14819 C CB   . LYS   B  1 193 ? 82.230 17.405  -77.826 1.00 30.01  ? 219  LYS   B CB   1 
ATOM   14820 C CG   . LYS   B  1 193 ? 82.445 17.222  -79.329 1.00 33.88  ? 219  LYS   B CG   1 
ATOM   14821 C CD   . LYS   B  1 193 ? 82.409 18.558  -80.068 1.00 37.55  ? 219  LYS   B CD   1 
ATOM   14822 C CE   . LYS   B  1 193 ? 82.683 18.409  -81.548 1.00 40.39  ? 219  LYS   B CE   1 
ATOM   14823 N NZ   . LYS   B  1 193 ? 82.649 19.725  -82.234 1.00 42.72  ? 219  LYS   B NZ   1 
ATOM   14824 H H    . LYS   B  1 193 ? 81.653 14.348  -78.012 0.00 38.83  ? 219  LYS   B H    1 
ATOM   14825 H HA   . LYS   B  1 193 ? 83.239 15.632  -77.205 0.00 39.09  ? 219  LYS   B HA   1 
ATOM   14826 H HB2  . LYS   B  1 193 ? 81.259 17.875  -77.684 0.00 40.16  ? 219  LYS   B HB2  1 
ATOM   14827 H HB3  . LYS   B  1 193 ? 83.019 18.058  -77.457 0.00 40.56  ? 219  LYS   B HB3  1 
ATOM   14828 H HG2  . LYS   B  1 193 ? 83.420 16.766  -79.499 0.00 45.79  ? 219  LYS   B HG2  1 
ATOM   14829 H HG3  . LYS   B  1 193 ? 81.658 16.594  -79.743 0.00 45.40  ? 219  LYS   B HG3  1 
ATOM   14830 H HD2  . LYS   B  1 193 ? 81.421 19.003  -79.951 0.00 50.13  ? 219  LYS   B HD2  1 
ATOM   14831 H HD3  . LYS   B  1 193 ? 83.168 19.217  -79.649 0.00 50.48  ? 219  LYS   B HD3  1 
ATOM   14832 H HE2  . LYS   B  1 193 ? 83.672 17.975  -81.689 0.00 54.54  ? 219  LYS   B HE2  1 
ATOM   14833 H HE3  . LYS   B  1 193 ? 81.922 17.770  -81.994 0.00 54.20  ? 219  LYS   B HE3  1 
ATOM   14834 H HZ1  . LYS   B  1 193 ? 82.853 19.606  -83.221 0.00 57.91  ? 219  LYS   B HZ1  1 
ATOM   14835 H HZ2  . LYS   B  1 193 ? 81.730 20.144  -82.135 0.00 57.34  ? 219  LYS   B HZ2  1 
ATOM   14836 H HZ3  . LYS   B  1 193 ? 83.341 20.346  -81.827 0.00 57.64  ? 219  LYS   B HZ3  1 
ATOM   14837 N N    . LEU   B  1 194 ? 82.172 15.241  -74.781 1.00 29.60  ? 220  LEU   B N    1 
ATOM   14838 C CA   . LEU   B  1 194 ? 82.143 15.331  -73.324 1.00 29.66  ? 220  LEU   B CA   1 
ATOM   14839 C C    . LEU   B  1 194 ? 83.580 15.408  -72.828 1.00 29.47  ? 220  LEU   B C    1 
ATOM   14840 O O    . LEU   B  1 194 ? 84.478 14.819  -73.449 1.00 30.08  ? 220  LEU   B O    1 
ATOM   14841 C CB   . LEU   B  1 194 ? 81.419 14.127  -72.721 1.00 29.84  ? 220  LEU   B CB   1 
ATOM   14842 C CG   . LEU   B  1 194 ? 79.943 14.001  -73.064 1.00 31.07  ? 220  LEU   B CG   1 
ATOM   14843 C CD1  . LEU   B  1 194 ? 79.369 12.729  -72.479 1.00 31.57  ? 220  LEU   B CD1  1 
ATOM   14844 C CD2  . LEU   B  1 194 ? 79.150 15.214  -72.582 1.00 31.18  ? 220  LEU   B CD2  1 
ATOM   14845 H H    . LEU   B  1 194 ? 82.215 14.293  -75.140 0.00 38.80  ? 220  LEU   B H    1 
ATOM   14846 H HA   . LEU   B  1 194 ? 81.621 16.236  -73.021 0.00 38.34  ? 220  LEU   B HA   1 
ATOM   14847 H HB2  . LEU   B  1 194 ? 81.912 13.221  -73.067 0.00 38.38  ? 220  LEU   B HB2  1 
ATOM   14848 H HB3  . LEU   B  1 194 ? 81.496 14.190  -71.636 0.00 37.99  ? 220  LEU   B HB3  1 
ATOM   14849 H HG   . LEU   B  1 194 ? 79.841 13.947  -74.147 0.00 39.66  ? 220  LEU   B HG   1 
ATOM   14850 H HD11 . LEU   B  1 194 ? 78.328 12.632  -72.786 0.00 39.46  ? 220  LEU   B HD11 1 
ATOM   14851 H HD12 . LEU   B  1 194 ? 79.944 11.880  -72.844 0.00 39.82  ? 220  LEU   B HD12 1 
ATOM   14852 H HD13 . LEU   B  1 194 ? 79.431 12.779  -71.392 0.00 39.38  ? 220  LEU   B HD13 1 
ATOM   14853 H HD21 . LEU   B  1 194 ? 78.089 14.969  -72.582 0.00 39.07  ? 220  LEU   B HD21 1 
ATOM   14854 H HD22 . LEU   B  1 194 ? 79.474 15.476  -71.576 0.00 39.19  ? 220  LEU   B HD22 1 
ATOM   14855 H HD23 . LEU   B  1 194 ? 79.326 16.048  -73.261 0.00 39.63  ? 220  LEU   B HD23 1 
ATOM   14856 N N    . PRO   B  1 195 ? 83.848 16.165  -71.745 1.00 28.75  ? 221  PRO   B N    1 
ATOM   14857 C CA   . PRO   B  1 195 ? 85.231 16.279  -71.269 1.00 28.31  ? 221  PRO   B CA   1 
ATOM   14858 C C    . PRO   B  1 195 ? 85.714 14.987  -70.627 1.00 27.97  ? 221  PRO   B C    1 
ATOM   14859 O O    . PRO   B  1 195 ? 84.961 14.338  -69.890 1.00 27.55  ? 221  PRO   B O    1 
ATOM   14860 C CB   . PRO   B  1 195 ? 85.177 17.426  -70.265 1.00 29.08  ? 221  PRO   B CB   1 
ATOM   14861 C CG   . PRO   B  1 195 ? 83.771 17.410  -69.763 1.00 29.84  ? 221  PRO   B CG   1 
ATOM   14862 C CD   . PRO   B  1 195 ? 82.913 16.927  -70.896 1.00 28.49  ? 221  PRO   B CD   1 
ATOM   14863 H HA   . PRO   B  1 195 ? 85.893 16.560  -72.087 0.00 37.81  ? 221  PRO   B HA   1 
ATOM   14864 H HB2  . PRO   B  1 195 ? 85.879 17.241  -69.452 0.00 38.29  ? 221  PRO   B HB2  1 
ATOM   14865 H HB3  . PRO   B  1 195 ? 85.402 18.367  -70.763 0.00 38.54  ? 221  PRO   B HB3  1 
ATOM   14866 H HG2  . PRO   B  1 195 ? 83.700 16.741  -68.907 0.00 38.33  ? 221  PRO   B HG2  1 
ATOM   14867 H HG3  . PRO   B  1 195 ? 83.483 18.420  -69.476 0.00 38.61  ? 221  PRO   B HG3  1 
ATOM   14868 H HD2  . PRO   B  1 195 ? 82.123 16.278  -70.522 0.00 36.51  ? 221  PRO   B HD2  1 
ATOM   14869 H HD3  . PRO   B  1 195 ? 82.505 17.772  -71.447 0.00 37.01  ? 221  PRO   B HD3  1 
ATOM   14870 N N    . SER   B  1 196 ? 86.968 14.621  -70.907 1.00 27.62  ? 222  SER   B N    1 
ATOM   14871 C CA   . SER   B  1 196 ? 87.589 13.402  -70.382 1.00 27.82  ? 222  SER   B CA   1 
ATOM   14872 C C    . SER   B  1 196 ? 87.806 13.417  -68.858 1.00 26.83  ? 222  SER   B C    1 
ATOM   14873 O O    . SER   B  1 196 ? 88.173 12.392  -68.290 1.00 26.88  ? 222  SER   B O    1 
ATOM   14874 C CB   . SER   B  1 196 ? 88.907 13.141  -71.101 1.00 30.29  ? 222  SER   B CB   1 
ATOM   14875 O OG   . SER   B  1 196 ? 89.721 14.298  -71.053 1.00 34.81  ? 222  SER   B OG   1 
ATOM   14876 H H    . SER   B  1 196 ? 87.591 15.161  -71.500 0.00 37.28  ? 222  SER   B H    1 
ATOM   14877 H HA   . SER   B  1 196 ? 86.928 12.565  -70.604 0.00 36.92  ? 222  SER   B HA   1 
ATOM   14878 H HB2  . SER   B  1 196 ? 89.428 12.314  -70.622 0.00 40.81  ? 222  SER   B HB2  1 
ATOM   14879 H HB3  . SER   B  1 196 ? 88.701 12.900  -72.142 0.00 40.87  ? 222  SER   B HB3  1 
ATOM   14880 H HG   . SER   B  1 196 ? 90.577 14.131  -71.527 0.00 46.96  ? 222  SER   B HG   1 
ATOM   14881 N N    . SER   B  1 197 ? 87.583 14.560  -68.196 1.00 25.75  ? 223  SER   B N    1 
ATOM   14882 C CA   . SER   B  1 197 ? 87.665 14.648  -66.740 1.00 25.30  ? 223  SER   B CA   1 
ATOM   14883 C C    . SER   B  1 197 ? 86.447 13.954  -66.072 1.00 24.89  ? 223  SER   B C    1 
ATOM   14884 O O    . SER   B  1 197 ? 86.485 13.723  -64.862 1.00 24.91  ? 223  SER   B O    1 
ATOM   14885 C CB   . SER   B  1 197 ? 87.694 16.113  -66.309 1.00 25.76  ? 223  SER   B CB   1 
ATOM   14886 O OG   . SER   B  1 197 ? 86.614 16.827  -66.897 1.00 27.59  ? 223  SER   B OG   1 
ATOM   14887 H H    . SER   B  1 197 ? 87.352 15.445  -68.635 0.00 34.44  ? 223  SER   B H    1 
ATOM   14888 H HA   . SER   B  1 197 ? 88.577 14.170  -66.386 0.00 33.90  ? 223  SER   B HA   1 
ATOM   14889 H HB2  . SER   B  1 197 ? 87.617 16.166  -65.224 0.00 34.14  ? 223  SER   B HB2  1 
ATOM   14890 H HB3  . SER   B  1 197 ? 88.633 16.558  -66.636 0.00 34.76  ? 223  SER   B HB3  1 
ATOM   14891 H HG   . SER   B  1 197 ? 85.817 16.805  -66.304 0.00 35.91  ? 223  SER   B HG   1 
ATOM   14892 N N    . LEU   B  1 198 ? 85.357 13.672  -66.820 1.00 24.48  ? 224  LEU   B N    1 
ATOM   14893 C CA   . LEU   B  1 198 ? 84.158 13.084  -66.225 1.00 24.77  ? 224  LEU   B CA   1 
ATOM   14894 C C    . LEU   B  1 198 ? 84.411 11.807  -65.436 1.00 24.60  ? 224  LEU   B C    1 
ATOM   14895 O O    . LEU   B  1 198 ? 85.144 10.925  -65.888 1.00 24.26  ? 224  LEU   B O    1 
ATOM   14896 C CB   . LEU   B  1 198 ? 83.080 12.788  -67.278 1.00 25.11  ? 224  LEU   B CB   1 
ATOM   14897 C CG   . LEU   B  1 198 ? 82.216 13.958  -67.748 1.00 27.28  ? 224  LEU   B CG   1 
ATOM   14898 C CD1  . LEU   B  1 198 ? 81.260 13.513  -68.850 1.00 28.44  ? 224  LEU   B CD1  1 
ATOM   14899 C CD2  . LEU   B  1 198 ? 81.429 14.569  -66.587 1.00 27.08  ? 224  LEU   B CD2  1 
ATOM   14900 H H    . LEU   B  1 198 ? 85.266 13.851  -67.814 0.00 31.91  ? 224  LEU   B H    1 
ATOM   14901 H HA   . LEU   B  1 198 ? 83.783 13.828  -65.524 0.00 31.39  ? 224  LEU   B HA   1 
ATOM   14902 H HB2  . LEU   B  1 198 ? 83.565 12.369  -68.158 0.00 32.06  ? 224  LEU   B HB2  1 
ATOM   14903 H HB3  . LEU   B  1 198 ? 82.404 12.043  -66.861 0.00 31.46  ? 224  LEU   B HB3  1 
ATOM   14904 H HG   . LEU   B  1 198 ? 82.866 14.729  -68.158 0.00 34.64  ? 224  LEU   B HG   1 
ATOM   14905 H HD11 . LEU   B  1 198 ? 80.740 14.384  -69.247 0.00 35.61  ? 224  LEU   B HD11 1 
ATOM   14906 H HD12 . LEU   B  1 198 ? 81.830 13.028  -69.641 0.00 35.88  ? 224  LEU   B HD12 1 
ATOM   14907 H HD13 . LEU   B  1 198 ? 80.539 12.811  -68.432 0.00 35.26  ? 224  LEU   B HD13 1 
ATOM   14908 H HD21 . LEU   B  1 198 ? 80.564 15.092  -66.991 0.00 33.57  ? 224  LEU   B HD21 1 
ATOM   14909 H HD22 . LEU   B  1 198 ? 81.105 13.778  -65.911 0.00 33.40  ? 224  LEU   B HD22 1 
ATOM   14910 H HD23 . LEU   B  1 198 ? 82.064 15.278  -66.058 0.00 33.86  ? 224  LEU   B HD23 1 
ATOM   14911 N N    . ARG   B  1 199 ? 83.770 11.729  -64.259 1.00 24.31  ? 225  ARG   B N    1 
ATOM   14912 C CA   . ARG   B  1 199 ? 83.799 10.604  -63.340 1.00 25.05  ? 225  ARG   B CA   1 
ATOM   14913 C C    . ARG   B  1 199 ? 82.395 9.994   -63.232 1.00 23.61  ? 225  ARG   B C    1 
ATOM   14914 O O    . ARG   B  1 199 ? 82.275 8.780   -63.175 1.00 24.10  ? 225  ARG   B O    1 
ATOM   14915 C CB   . ARG   B  1 199 ? 84.332 11.046  -61.959 1.00 28.73  ? 225  ARG   B CB   1 
ATOM   14916 C CG   . ARG   B  1 199 ? 85.836 11.324  -61.998 1.00 35.79  ? 225  ARG   B CG   1 
ATOM   14917 C CD   . ARG   B  1 199 ? 86.396 11.845  -60.702 1.00 44.24  ? 225  ARG   B CD   1 
ATOM   14918 N NE   . ARG   B  1 199 ? 87.863 11.873  -60.747 1.00 50.99  ? 225  ARG   B NE   1 
ATOM   14919 C CZ   . ARG   B  1 199 ? 88.641 12.383  -59.796 1.00 55.26  ? 225  ARG   B CZ   1 
ATOM   14920 N NH1  . ARG   B  1 199 ? 88.106 12.923  -58.706 1.00 55.16  ? 225  ARG   B NH1  1 
ATOM   14921 N NH2  . ARG   B  1 199 ? 89.961 12.357  -59.927 1.00 56.88  ? 225  ARG   B NH2  1 
ATOM   14922 H H    . ARG   B  1 199 ? 83.210 12.492  -63.893 0.00 30.33  ? 225  ARG   B H    1 
ATOM   14923 H HA   . ARG   B  1 199 ? 84.473 9.831   -63.703 0.00 31.50  ? 225  ARG   B HA   1 
ATOM   14924 H HB2  . ARG   B  1 199 ? 83.822 11.958  -61.651 0.00 35.54  ? 225  ARG   B HB2  1 
ATOM   14925 H HB3  . ARG   B  1 199 ? 84.151 10.252  -61.236 0.00 35.54  ? 225  ARG   B HB3  1 
ATOM   14926 H HG2  . ARG   B  1 199 ? 86.350 10.394  -62.236 0.00 44.92  ? 225  ARG   B HG2  1 
ATOM   14927 H HG3  . ARG   B  1 199 ? 86.039 12.067  -62.768 0.00 44.93  ? 225  ARG   B HG3  1 
ATOM   14928 H HD2  . ARG   B  1 199 ? 86.038 12.860  -60.531 0.00 54.92  ? 225  ARG   B HD2  1 
ATOM   14929 H HD3  . ARG   B  1 199 ? 86.088 11.191  -59.888 0.00 54.79  ? 225  ARG   B HD3  1 
ATOM   14930 H HE   . ARG   B  1 199 ? 88.311 11.470  -61.563 0.00 63.90  ? 225  ARG   B HE   1 
ATOM   14931 H HH11 . ARG   B  1 199 ? 87.102 12.960  -58.568 0.00 68.33  ? 225  ARG   B HH11 1 
ATOM   14932 H HH12 . ARG   B  1 199 ? 88.712 13.309  -57.989 0.00 69.00  ? 225  ARG   B HH12 1 
ATOM   14933 H HH21 . ARG   B  1 199 ? 90.379 11.945  -60.755 0.00 71.81  ? 225  ARG   B HH21 1 
ATOM   14934 H HH22 . ARG   B  1 199 ? 90.561 12.744  -59.206 0.00 71.86  ? 225  ARG   B HH22 1 
ATOM   14935 N N    . LYS   B  1 200 ? 81.340 10.814  -63.236 1.00 22.22  ? 226  LYS   B N    1 
ATOM   14936 C CA   . LYS   B  1 200 ? 79.968 10.336  -63.101 1.00 21.89  ? 226  LYS   B CA   1 
ATOM   14937 C C    . LYS   B  1 200 ? 79.096 10.968  -64.165 1.00 22.05  ? 226  LYS   B C    1 
ATOM   14938 O O    . LYS   B  1 200 ? 78.960 12.192  -64.201 1.00 22.41  ? 226  LYS   B O    1 
ATOM   14939 C CB   . LYS   B  1 200 ? 79.419 10.657  -61.699 1.00 22.67  ? 226  LYS   B CB   1 
ATOM   14940 C CG   . LYS   B  1 200 ? 80.337 10.161  -60.592 1.00 24.45  ? 226  LYS   B CG   1 
ATOM   14941 C CD   . LYS   B  1 200 ? 79.630 10.000  -59.246 1.00 27.88  ? 226  LYS   B CD   1 
ATOM   14942 C CE   . LYS   B  1 200 ? 80.596 9.413   -58.236 1.00 30.94  ? 226  LYS   B CE   1 
ATOM   14943 N NZ   . LYS   B  1 200 ? 79.925 9.008   -56.970 1.00 32.12  ? 226  LYS   B NZ   1 
ATOM   14944 H H    . LYS   B  1 200 ? 81.399 11.824  -63.311 0.00 27.14  ? 226  LYS   B H    1 
ATOM   14945 H HA   . LYS   B  1 200 ? 79.926 9.256   -63.232 0.00 26.19  ? 226  LYS   B HA   1 
ATOM   14946 H HB2  . LYS   B  1 200 ? 79.318 11.737  -61.592 0.00 26.86  ? 226  LYS   B HB2  1 
ATOM   14947 H HB3  . LYS   B  1 200 ? 78.449 10.177  -61.577 0.00 26.54  ? 226  LYS   B HB3  1 
ATOM   14948 H HG2  . LYS   B  1 200 ? 80.738 9.190   -60.880 0.00 29.22  ? 226  LYS   B HG2  1 
ATOM   14949 H HG3  . LYS   B  1 200 ? 81.150 10.874  -60.461 0.00 29.37  ? 226  LYS   B HG3  1 
ATOM   14950 H HD2  . LYS   B  1 200 ? 79.299 10.974  -58.887 0.00 32.79  ? 226  LYS   B HD2  1 
ATOM   14951 H HD3  . LYS   B  1 200 ? 78.785 9.321   -59.351 0.00 32.61  ? 226  LYS   B HD3  1 
ATOM   14952 H HE2  . LYS   B  1 200 ? 81.067 8.525   -58.657 0.00 36.89  ? 226  LYS   B HE2  1 
ATOM   14953 H HE3  . LYS   B  1 200 ? 81.351 10.159  -57.995 0.00 36.98  ? 226  LYS   B HE3  1 
ATOM   14954 H HZ1  . LYS   B  1 200 ? 80.606 8.616   -56.328 0.00 38.00  ? 226  LYS   B HZ1  1 
ATOM   14955 H HZ2  . LYS   B  1 200 ? 79.489 9.816   -56.537 0.00 37.72  ? 226  LYS   B HZ2  1 
ATOM   14956 H HZ3  . LYS   B  1 200 ? 79.214 8.310   -57.160 0.00 37.61  ? 226  LYS   B HZ3  1 
ATOM   14957 N N    . LEU   B  1 201 ? 78.486 10.134  -65.013 1.00 21.40  ? 227  LEU   B N    1 
ATOM   14958 C CA   . LEU   B  1 201 ? 77.610 10.599  -66.085 1.00 21.42  ? 227  LEU   B CA   1 
ATOM   14959 C C    . LEU   B  1 201 ? 76.224 10.003  -65.893 1.00 20.81  ? 227  LEU   B C    1 
ATOM   14960 O O    . LEU   B  1 201 ? 76.068 8.780   -65.979 1.00 21.02  ? 227  LEU   B O    1 
ATOM   14961 C CB   . LEU   B  1 201 ? 78.199 10.193  -67.449 1.00 21.73  ? 227  LEU   B CB   1 
ATOM   14962 C CG   . LEU   B  1 201 ? 77.423 10.578  -68.700 1.00 24.02  ? 227  LEU   B CG   1 
ATOM   14963 C CD1  . LEU   B  1 201 ? 77.138 12.084  -68.748 1.00 24.82  ? 227  LEU   B CD1  1 
ATOM   14964 C CD2  . LEU   B  1 201 ? 78.191 10.133  -69.962 1.00 24.43  ? 227  LEU   B CD2  1 
ATOM   14965 H H    . LEU   B  1 201 ? 78.579 9.123   -64.993 0.00 25.51  ? 227  LEU   B H    1 
ATOM   14966 H HA   . LEU   B  1 201 ? 77.526 11.684  -66.061 0.00 25.55  ? 227  LEU   B HA   1 
ATOM   14967 H HB2  . LEU   B  1 201 ? 79.179 10.659  -67.537 0.00 26.56  ? 227  LEU   B HB2  1 
ATOM   14968 H HB3  . LEU   B  1 201 ? 78.314 9.110   -67.462 0.00 26.29  ? 227  LEU   B HB3  1 
ATOM   14969 H HG   . LEU   B  1 201 ? 76.470 10.052  -68.705 0.00 28.89  ? 227  LEU   B HG   1 
ATOM   14970 H HD11 . LEU   B  1 201 ? 76.756 12.340  -69.735 0.00 30.24  ? 227  LEU   B HD11 1 
ATOM   14971 H HD12 . LEU   B  1 201 ? 76.392 12.331  -67.994 0.00 29.78  ? 227  LEU   B HD12 1 
ATOM   14972 H HD13 . LEU   B  1 201 ? 78.062 12.627  -68.554 0.00 30.30  ? 227  LEU   B HD13 1 
ATOM   14973 H HD21 . LEU   B  1 201 ? 77.634 10.435  -70.848 0.00 30.15  ? 227  LEU   B HD21 1 
ATOM   14974 H HD22 . LEU   B  1 201 ? 79.173 10.604  -69.965 0.00 30.31  ? 227  LEU   B HD22 1 
ATOM   14975 H HD23 . LEU   B  1 201 ? 78.299 9.050   -69.946 0.00 30.07  ? 227  LEU   B HD23 1 
ATOM   14976 N N    . PHE   B  1 202 ? 75.221 10.858  -65.592 1.00 20.00  ? 228  PHE   B N    1 
ATOM   14977 C CA   . PHE   B  1 202 ? 73.849 10.380  -65.402 1.00 20.17  ? 228  PHE   B CA   1 
ATOM   14978 C C    . PHE   B  1 202 ? 72.960 10.725  -66.593 1.00 20.28  ? 228  PHE   B C    1 
ATOM   14979 O O    . PHE   B  1 202 ? 72.712 11.897  -66.856 1.00 21.19  ? 228  PHE   B O    1 
ATOM   14980 C CB   . PHE   B  1 202 ? 73.217 10.863  -64.073 1.00 19.85  ? 228  PHE   B CB   1 
ATOM   14981 C CG   . PHE   B  1 202 ? 74.003 10.555  -62.821 1.00 21.36  ? 228  PHE   B CG   1 
ATOM   14982 C CD1  . PHE   B  1 202 ? 75.114 11.317  -62.472 1.00 22.51  ? 228  PHE   B CD1  1 
ATOM   14983 C CD2  . PHE   B  1 202 ? 73.576 9.572   -61.939 1.00 21.71  ? 228  PHE   B CD2  1 
ATOM   14984 C CE1  . PHE   B  1 202 ? 75.784 11.089  -61.267 1.00 23.14  ? 228  PHE   B CE1  1 
ATOM   14985 C CE2  . PHE   B  1 202 ? 74.257 9.340   -60.743 1.00 22.65  ? 228  PHE   B CE2  1 
ATOM   14986 C CZ   . PHE   B  1 202 ? 75.360 10.087  -60.423 1.00 22.83  ? 228  PHE   B CZ   1 
ATOM   14987 H H    . PHE   B  1 202 ? 75.327 11.860  -65.474 0.00 23.25  ? 228  PHE   B H    1 
ATOM   14988 H HA   . PHE   B  1 202 ? 73.877 9.298   -65.332 0.00 23.03  ? 228  PHE   B HA   1 
ATOM   14989 H HB2  . PHE   B  1 202 ? 73.018 11.931  -64.088 0.00 22.39  ? 228  PHE   B HB2  1 
ATOM   14990 H HB3  . PHE   B  1 202 ? 72.263 10.347  -63.975 0.00 22.15  ? 228  PHE   B HB3  1 
ATOM   14991 H HD1  . PHE   B  1 202 ? 75.447 12.107  -63.124 0.00 25.93  ? 228  PHE   B HD1  1 
ATOM   14992 H HD2  . PHE   B  1 202 ? 72.705 8.980   -62.172 0.00 24.10  ? 228  PHE   B HD2  1 
ATOM   14993 H HE1  . PHE   B  1 202 ? 76.661 11.662  -61.021 0.00 26.66  ? 228  PHE   B HE1  1 
ATOM   14994 H HE2  . PHE   B  1 202 ? 73.926 8.552   -60.085 0.00 25.18  ? 228  PHE   B HE2  1 
ATOM   14995 H HZ   . PHE   B  1 202 ? 75.896 9.891   -59.510 0.00 25.82  ? 228  PHE   B HZ   1 
ATOM   14996 N N    . LEU   B  1 203 ? 72.449 9.691   -67.283 1.00 20.09  ? 229  LEU   B N    1 
ATOM   14997 C CA   . LEU   B  1 203 ? 71.594 9.819   -68.461 1.00 20.58  ? 229  LEU   B CA   1 
ATOM   14998 C C    . LEU   B  1 203 ? 70.372 8.903   -68.333 1.00 20.33  ? 229  LEU   B C    1 
ATOM   14999 O O    . LEU   B  1 203 ? 69.940 8.288   -69.317 1.00 20.27  ? 229  LEU   B O    1 
ATOM   15000 C CB   . LEU   B  1 203 ? 72.405 9.427   -69.705 1.00 20.88  ? 229  LEU   B CB   1 
ATOM   15001 C CG   . LEU   B  1 203 ? 73.646 10.265  -69.984 1.00 23.87  ? 229  LEU   B CG   1 
ATOM   15002 C CD1  . LEU   B  1 203 ? 74.553 9.556   -70.972 1.00 23.84  ? 229  LEU   B CD1  1 
ATOM   15003 C CD2  . LEU   B  1 203 ? 73.258 11.640  -70.485 1.00 25.03  ? 229  LEU   B CD2  1 
ATOM   15004 H H    . LEU   B  1 203 ? 72.613 8.718   -67.043 0.00 23.05  ? 229  LEU   B H    1 
ATOM   15005 H HA   . LEU   B  1 203 ? 71.227 10.838  -68.574 0.00 23.82  ? 229  LEU   B HA   1 
ATOM   15006 H HB2  . LEU   B  1 203 ? 72.746 8.404   -69.561 0.00 24.60  ? 229  LEU   B HB2  1 
ATOM   15007 H HB3  . LEU   B  1 203 ? 71.772 9.488   -70.589 0.00 24.73  ? 229  LEU   B HB3  1 
ATOM   15008 H HG   . LEU   B  1 203 ? 74.208 10.402  -69.062 0.00 28.35  ? 229  LEU   B HG   1 
ATOM   15009 H HD11 . LEU   B  1 203 ? 75.352 10.230  -71.278 0.00 29.07  ? 229  LEU   B HD11 1 
ATOM   15010 H HD12 . LEU   B  1 203 ? 74.974 8.673   -70.492 0.00 28.78  ? 229  LEU   B HD12 1 
ATOM   15011 H HD13 . LEU   B  1 203 ? 73.956 9.261   -71.833 0.00 28.96  ? 229  LEU   B HD13 1 
ATOM   15012 H HD21 . LEU   B  1 203 ? 74.157 12.192  -70.753 0.00 30.23  ? 229  LEU   B HD21 1 
ATOM   15013 H HD22 . LEU   B  1 203 ? 72.607 11.543  -71.353 0.00 30.12  ? 229  LEU   B HD22 1 
ATOM   15014 H HD23 . LEU   B  1 203 ? 72.739 12.157  -69.681 0.00 29.73  ? 229  LEU   B HD23 1 
ATOM   15015 N N    . SER   B  1 204 ? 69.786 8.835   -67.131 1.00 19.92  ? 230  SER   B N    1 
ATOM   15016 C CA   . SER   B  1 204 ? 68.622 7.997   -66.906 1.00 19.68  ? 230  SER   B CA   1 
ATOM   15017 C C    . SER   B  1 204 ? 67.381 8.635   -67.514 1.00 20.55  ? 230  SER   B C    1 
ATOM   15018 O O    . SER   B  1 204 ? 67.243 9.843   -67.424 1.00 21.50  ? 230  SER   B O    1 
ATOM   15019 C CB   . SER   B  1 204 ? 68.395 7.781   -65.405 1.00 20.40  ? 230  SER   B CB   1 
ATOM   15020 O OG   . SER   B  1 204 ? 67.203 7.036   -65.195 1.00 21.76  ? 230  SER   B OG   1 
ATOM   15021 H H    . SER   B  1 204 ? 70.085 9.350   -66.309 0.00 22.31  ? 230  SER   B H    1 
ATOM   15022 H HA   . SER   B  1 204 ? 68.773 7.021   -67.364 0.00 22.08  ? 230  SER   B HA   1 
ATOM   15023 H HB2  . SER   B  1 204 ? 69.237 7.223   -64.997 0.00 22.47  ? 230  SER   B HB2  1 
ATOM   15024 H HB3  . SER   B  1 204 ? 68.306 8.741   -64.899 0.00 22.34  ? 230  SER   B HB3  1 
ATOM   15025 H HG   . SER   B  1 204 ? 67.237 6.196   -65.725 0.00 24.05  ? 230  SER   B HG   1 
ATOM   15026 N N    . ASN   B  1 205 ? 66.459 7.842   -68.113 1.00 19.62  ? 231  ASN   B N    1 
ATOM   15027 C CA   . ASN   B  1 205 ? 65.188 8.355   -68.633 1.00 20.41  ? 231  ASN   B CA   1 
ATOM   15028 C C    . ASN   B  1 205 ? 65.384 9.545   -69.582 1.00 21.40  ? 231  ASN   B C    1 
ATOM   15029 O O    . ASN   B  1 205 ? 64.801 10.620  -69.386 1.00 21.22  ? 231  ASN   B O    1 
ATOM   15030 C CB   . ASN   B  1 205 ? 64.274 8.738   -67.453 1.00 21.24  ? 231  ASN   B CB   1 
ATOM   15031 C CG   . ASN   B  1 205 ? 63.698 7.548   -66.737 1.00 22.94  ? 231  ASN   B CG   1 
ATOM   15032 O OD1  . ASN   B  1 205 ? 62.515 7.272   -66.866 1.00 23.16  ? 231  ASN   B OD1  1 
ATOM   15033 N ND2  . ASN   B  1 205 ? 64.511 6.840   -65.952 1.00 22.71  ? 231  ASN   B ND2  1 
ATOM   15034 H H    . ASN   B  1 205 ? 66.575 6.842   -68.242 0.00 22.01  ? 231  ASN   B H    1 
ATOM   15035 H HA   . ASN   B  1 205 ? 64.696 7.561   -69.194 0.00 23.08  ? 231  ASN   B HA   1 
ATOM   15036 H HB2  . ASN   B  1 205 ? 64.817 9.343   -66.728 0.00 23.47  ? 231  ASN   B HB2  1 
ATOM   15037 H HB3  . ASN   B  1 205 ? 63.421 9.302   -67.827 0.00 23.67  ? 231  ASN   B HB3  1 
ATOM   15038 H HD21 . ASN   B  1 205 ? 64.158 6.029   -65.453 0.00 24.87  ? 231  ASN   B HD21 1 
ATOM   15039 H HD22 . ASN   B  1 205 ? 65.483 7.114   -65.855 0.00 25.04  ? 231  ASN   B HD22 1 
ATOM   15040 N N    . THR   B  1 206 ? 66.257 9.348   -70.581 1.00 21.54  ? 232  THR   B N    1 
ATOM   15041 C CA   . THR   B  1 206 ? 66.607 10.371  -71.564 1.00 22.28  ? 232  THR   B CA   1 
ATOM   15042 C C    . THR   B  1 206 ? 66.218 10.018  -72.998 1.00 23.80  ? 232  THR   B C    1 
ATOM   15043 O O    . THR   B  1 206 ? 66.624 10.742  -73.912 1.00 23.83  ? 232  THR   B O    1 
ATOM   15044 C CB   . THR   B  1 206 ? 68.114 10.672  -71.491 1.00 22.31  ? 232  THR   B CB   1 
ATOM   15045 O OG1  . THR   B  1 206 ? 68.844 9.456   -71.663 1.00 22.42  ? 232  THR   B OG1  1 
ATOM   15046 C CG2  . THR   B  1 206 ? 68.508 11.375  -70.194 1.00 22.16  ? 232  THR   B CG2  1 
ATOM   15047 H H    . THR   B  1 206 ? 66.743 8.469   -70.733 0.00 25.00  ? 232  THR   B H    1 
ATOM   15048 H HA   . THR   B  1 206 ? 66.083 11.297  -71.334 0.00 26.11  ? 232  THR   B HA   1 
ATOM   15049 H HB   . THR   B  1 206 ? 68.391 11.335  -72.307 0.00 26.59  ? 232  THR   B HB   1 
ATOM   15050 H HG1  . THR   B  1 206 ? 68.870 8.929   -70.821 0.00 26.27  ? 232  THR   B HG1  1 
ATOM   15051 H HG21 . THR   B  1 206 ? 69.578 11.578  -70.190 0.00 25.95  ? 232  THR   B HG21 1 
ATOM   15052 H HG22 . THR   B  1 206 ? 67.970 12.318  -70.102 0.00 25.81  ? 232  THR   B HG22 1 
ATOM   15053 H HG23 . THR   B  1 206 ? 68.266 10.744  -69.340 0.00 25.55  ? 232  THR   B HG23 1 
ATOM   15054 N N    . GLN   B  1 207 ? 65.425 8.945   -73.207 1.00 24.39  ? 233  GLN   B N    1 
ATOM   15055 C CA   . GLN   B  1 207 ? 65.006 8.488   -74.539 1.00 26.16  ? 233  GLN   B CA   1 
ATOM   15056 C C    . GLN   B  1 207 ? 66.174 8.154   -75.468 1.00 27.50  ? 233  GLN   B C    1 
ATOM   15057 O O    . GLN   B  1 207 ? 66.054 8.333   -76.687 1.00 27.90  ? 233  GLN   B O    1 
ATOM   15058 C CB   . GLN   B  1 207 ? 64.040 9.487   -75.191 1.00 28.44  ? 233  GLN   B CB   1 
ATOM   15059 C CG   . GLN   B  1 207 ? 62.802 9.752   -74.348 1.00 33.41  ? 233  GLN   B CG   1 
ATOM   15060 C CD   . GLN   B  1 207 ? 61.865 10.753  -74.979 1.00 40.93  ? 233  GLN   B CD   1 
ATOM   15061 O OE1  . GLN   B  1 207 ? 62.235 11.532  -75.858 1.00 43.23  ? 233  GLN   B OE1  1 
ATOM   15062 N NE2  . GLN   B  1 207 ? 60.620 10.769  -74.525 1.00 42.88  ? 233  GLN   B NE2  1 
ATOM   15063 H H    . GLN   B  1 207 ? 65.040 8.363   -72.469 0.00 28.84  ? 233  GLN   B H    1 
ATOM   15064 H HA   . GLN   B  1 207 ? 64.447 7.563   -74.403 0.00 31.60  ? 233  GLN   B HA   1 
ATOM   15065 H HB2  . GLN   B  1 207 ? 64.561 10.432  -75.345 0.00 34.67  ? 233  GLN   B HB2  1 
ATOM   15066 H HB3  . GLN   B  1 207 ? 63.694 9.088   -76.144 0.00 34.93  ? 233  GLN   B HB3  1 
ATOM   15067 H HG2  . GLN   B  1 207 ? 62.260 8.816   -74.221 0.00 40.21  ? 233  GLN   B HG2  1 
ATOM   15068 H HG3  . GLN   B  1 207 ? 63.097 10.149  -73.377 0.00 39.93  ? 233  GLN   B HG3  1 
ATOM   15069 H HE21 . GLN   B  1 207 ? 60.340 10.133  -73.786 0.00 51.41  ? 233  GLN   B HE21 1 
ATOM   15070 H HE22 . GLN   B  1 207 ? 59.948 11.425  -74.909 0.00 51.89  ? 233  GLN   B HE22 1 
ATOM   15071 N N    . ILE   B  1 208 ? 67.279 7.630   -74.920 1.00 28.13  ? 234  ILE   B N    1 
ATOM   15072 C CA   . ILE   B  1 208 ? 68.427 7.218   -75.735 1.00 29.83  ? 234  ILE   B CA   1 
ATOM   15073 C C    . ILE   B  1 208 ? 68.185 5.731   -76.062 1.00 31.93  ? 234  ILE   B C    1 
ATOM   15074 O O    . ILE   B  1 208 ? 68.202 4.893   -75.163 1.00 33.39  ? 234  ILE   B O    1 
ATOM   15075 C CB   . ILE   B  1 208 ? 69.771 7.453   -75.004 1.00 30.23  ? 234  ILE   B CB   1 
ATOM   15076 C CG1  . ILE   B  1 208 ? 69.928 8.948   -74.616 1.00 30.85  ? 234  ILE   B CG1  1 
ATOM   15077 C CG2  . ILE   B  1 208 ? 70.941 7.009   -75.902 1.00 30.83  ? 234  ILE   B CG2  1 
ATOM   15078 C CD1  . ILE   B  1 208 ? 71.232 9.313   -73.837 1.00 32.11  ? 234  ILE   B CD1  1 
ATOM   15079 H H    . ILE   B  1 208 ? 67.416 7.471   -73.926 0.00 33.94  ? 234  ILE   B H    1 
ATOM   15080 H HA   . ILE   B  1 208 ? 68.462 7.786   -76.663 0.00 37.00  ? 234  ILE   B HA   1 
ATOM   15081 H HB   . ILE   B  1 208 ? 69.783 6.856   -74.093 0.00 36.75  ? 234  ILE   B HB   1 
ATOM   15082 H HG12 . ILE   B  1 208 ? 69.916 9.543   -75.529 0.00 37.95  ? 234  ILE   B HG12 1 
ATOM   15083 H HG13 . ILE   B  1 208 ? 69.093 9.243   -73.982 0.00 37.36  ? 234  ILE   B HG13 1 
ATOM   15084 H HG21 . ILE   B  1 208 ? 71.884 7.161   -75.380 0.00 38.11  ? 234  ILE   B HG21 1 
ATOM   15085 H HG22 . ILE   B  1 208 ? 70.847 5.952   -76.146 0.00 38.29  ? 234  ILE   B HG22 1 
ATOM   15086 H HG23 . ILE   B  1 208 ? 70.927 7.601   -76.816 0.00 38.48  ? 234  ILE   B HG23 1 
ATOM   15087 H HD11 . ILE   B  1 208 ? 71.118 10.307  -73.405 0.00 38.94  ? 234  ILE   B HD11 1 
ATOM   15088 H HD12 . ILE   B  1 208 ? 71.394 8.579   -73.049 0.00 38.85  ? 234  ILE   B HD12 1 
ATOM   15089 H HD13 . ILE   B  1 208 ? 72.072 9.313   -74.529 0.00 39.40  ? 234  ILE   B HD13 1 
ATOM   15090 N N    . LYS   B  1 209 ? 67.954 5.407   -77.323 1.00 31.59  ? 235  LYS   B N    1 
ATOM   15091 C CA   . LYS   B  1 209 ? 67.630 4.041   -77.739 1.00 31.89  ? 235  LYS   B CA   1 
ATOM   15092 C C    . LYS   B  1 209 ? 68.848 3.216   -78.170 1.00 31.08  ? 235  LYS   B C    1 
ATOM   15093 O O    . LYS   B  1 209 ? 68.780 1.981   -78.164 1.00 29.86  ? 235  LYS   B O    1 
ATOM   15094 C CB   . LYS   B  1 209 ? 66.615 4.098   -78.890 1.00 33.91  ? 235  LYS   B CB   1 
ATOM   15095 C CG   . LYS   B  1 209 ? 65.346 4.877   -78.543 1.00 39.42  ? 235  LYS   B CG   1 
ATOM   15096 C CD   . LYS   B  1 209 ? 64.439 5.058   -79.752 1.00 45.17  ? 235  LYS   B CD   1 
ATOM   15097 C CE   . LYS   B  1 209 ? 63.307 6.025   -79.490 1.00 49.91  ? 235  LYS   B CE   1 
ATOM   15098 N NZ   . LYS   B  1 209 ? 62.285 5.459   -78.568 1.00 52.06  ? 235  LYS   B NZ   1 
ATOM   15099 H H    . LYS   B  1 209 ? 67.982 6.062   -78.098 0.00 39.66  ? 235  LYS   B H    1 
ATOM   15100 H HA   . LYS   B  1 209 ? 67.147 3.509   -76.921 0.00 39.69  ? 235  LYS   B HA   1 
ATOM   15101 H HB2  . LYS   B  1 209 ? 67.080 4.583   -79.747 0.00 43.14  ? 235  LYS   B HB2  1 
ATOM   15102 H HB3  . LYS   B  1 209 ? 66.323 3.083   -79.155 0.00 42.99  ? 235  LYS   B HB3  1 
ATOM   15103 H HG2  . LYS   B  1 209 ? 64.790 4.330   -77.783 0.00 48.89  ? 235  LYS   B HG2  1 
ATOM   15104 H HG3  . LYS   B  1 209 ? 65.603 5.869   -78.175 0.00 48.97  ? 235  LYS   B HG3  1 
ATOM   15105 H HD2  . LYS   B  1 209 ? 65.026 5.446   -80.583 0.00 56.87  ? 235  LYS   B HD2  1 
ATOM   15106 H HD3  . LYS   B  1 209 ? 64.008 4.095   -80.019 0.00 56.73  ? 235  LYS   B HD3  1 
ATOM   15107 H HE2  . LYS   B  1 209 ? 63.702 6.935   -79.040 0.00 61.83  ? 235  LYS   B HE2  1 
ATOM   15108 H HE3  . LYS   B  1 209 ? 62.816 6.260   -80.433 0.00 62.45  ? 235  LYS   B HE3  1 
ATOM   15109 H HZ1  . LYS   B  1 209 ? 61.509 6.108   -78.479 0.00 64.24  ? 235  LYS   B HZ1  1 
ATOM   15110 H HZ2  . LYS   B  1 209 ? 61.940 4.577   -78.933 0.00 64.50  ? 235  LYS   B HZ2  1 
ATOM   15111 H HZ3  . LYS   B  1 209 ? 62.686 5.307   -77.648 0.00 63.92  ? 235  LYS   B HZ3  1 
ATOM   15112 N N    . TYR   B  1 210 ? 69.937 3.888   -78.577 1.00 31.16  ? 236  TYR   B N    1 
ATOM   15113 C CA   . TYR   B  1 210 ? 71.126 3.223   -79.081 1.00 32.03  ? 236  TYR   B CA   1 
ATOM   15114 C C    . TYR   B  1 210 ? 72.382 3.819   -78.463 1.00 31.41  ? 236  TYR   B C    1 
ATOM   15115 O O    . TYR   B  1 210 ? 72.493 5.039   -78.333 1.00 32.01  ? 236  TYR   B O    1 
ATOM   15116 C CB   . TYR   B  1 210 ? 71.159 3.366   -80.619 1.00 33.50  ? 236  TYR   B CB   1 
ATOM   15117 C CG   . TYR   B  1 210 ? 72.435 2.870   -81.259 1.00 36.54  ? 236  TYR   B CG   1 
ATOM   15118 C CD1  . TYR   B  1 210 ? 72.791 1.532   -81.198 1.00 38.24  ? 236  TYR   B CD1  1 
ATOM   15119 C CD2  . TYR   B  1 210 ? 73.239 3.721   -82.007 1.00 38.41  ? 236  TYR   B CD2  1 
ATOM   15120 C CE1  . TYR   B  1 210 ? 73.968 1.071   -81.769 1.00 39.64  ? 236  TYR   B CE1  1 
ATOM   15121 C CE2  . TYR   B  1 210 ? 74.386 3.257   -82.641 1.00 39.93  ? 236  TYR   B CE2  1 
ATOM   15122 C CZ   . TYR   B  1 210 ? 74.744 1.928   -82.523 1.00 41.22  ? 236  TYR   B CZ   1 
ATOM   15123 O OH   . TYR   B  1 210 ? 75.866 1.437   -83.146 1.00 43.75  ? 236  TYR   B OH   1 
ATOM   15124 H H    . TYR   B  1 210 ? 70.025 4.899   -78.587 0.00 39.56  ? 236  TYR   B H    1 
ATOM   15125 H HA   . TYR   B  1 210 ? 71.101 2.161   -78.846 0.00 41.07  ? 236  TYR   B HA   1 
ATOM   15126 H HB2  . TYR   B  1 210 ? 70.336 2.790   -81.040 0.00 43.56  ? 236  TYR   B HB2  1 
ATOM   15127 H HB3  . TYR   B  1 210 ? 71.036 4.418   -80.874 0.00 43.41  ? 236  TYR   B HB3  1 
ATOM   15128 H HD1  . TYR   B  1 210 ? 72.192 0.857   -80.611 0.00 49.53  ? 236  TYR   B HD1  1 
ATOM   15129 H HD2  . TYR   B  1 210 ? 72.966 4.757   -82.113 0.00 49.99  ? 236  TYR   B HD2  1 
ATOM   15130 H HE1  . TYR   B  1 210 ? 74.225 0.028   -81.704 0.00 52.06  ? 236  TYR   B HE1  1 
ATOM   15131 H HE2  . TYR   B  1 210 ? 74.994 3.941   -83.208 0.00 52.62  ? 236  TYR   B HE2  1 
ATOM   15132 H HH   . TYR   B  1 210 ? 76.310 2.141   -83.686 0.00 57.82  ? 236  TYR   B HH   1 
ATOM   15133 N N    . ILE   B  1 211 ? 73.331 2.956   -78.085 1.00 30.14  ? 237  ILE   B N    1 
ATOM   15134 C CA   . ILE   B  1 211 ? 74.621 3.371   -77.559 1.00 29.90  ? 237  ILE   B CA   1 
ATOM   15135 C C    . ILE   B  1 211 ? 75.652 2.884   -78.563 1.00 30.60  ? 237  ILE   B C    1 
ATOM   15136 O O    . ILE   B  1 211 ? 75.823 1.681   -78.742 1.00 30.03  ? 237  ILE   B O    1 
ATOM   15137 C CB   . ILE   B  1 211 ? 74.910 2.819   -76.145 1.00 29.65  ? 237  ILE   B CB   1 
ATOM   15138 C CG1  . ILE   B  1 211 ? 73.764 3.154   -75.149 1.00 30.64  ? 237  ILE   B CG1  1 
ATOM   15139 C CG2  . ILE   B  1 211 ? 76.251 3.324   -75.641 1.00 29.60  ? 237  ILE   B CG2  1 
ATOM   15140 C CD1  . ILE   B  1 211 ? 73.548 4.659   -74.865 1.00 31.56  ? 237  ILE   B CD1  1 
ATOM   15141 H H    . ILE   B  1 211 ? 73.234 1.947   -78.133 0.00 38.83  ? 237  ILE   B H    1 
ATOM   15142 H HA   . ILE   B  1 211 ? 74.685 4.457   -77.511 0.00 38.29  ? 237  ILE   B HA   1 
ATOM   15143 H HB   . ILE   B  1 211 ? 74.992 1.737   -76.200 0.00 37.87  ? 237  ILE   B HB   1 
ATOM   15144 H HG12 . ILE   B  1 211 ? 72.826 2.748   -75.526 0.00 38.36  ? 237  ILE   B HG12 1 
ATOM   15145 H HG13 . ILE   B  1 211 ? 74.001 2.682   -74.198 0.00 38.12  ? 237  ILE   B HG13 1 
ATOM   15146 H HG21 . ILE   B  1 211 ? 76.376 2.970   -74.620 0.00 37.41  ? 237  ILE   B HG21 1 
ATOM   15147 H HG22 . ILE   B  1 211 ? 77.052 2.930   -76.265 0.00 38.08  ? 237  ILE   B HG22 1 
ATOM   15148 H HG23 . ILE   B  1 211 ? 76.269 4.413   -75.671 0.00 37.59  ? 237  ILE   B HG23 1 
ATOM   15149 H HD11 . ILE   B  1 211 ? 72.710 4.759   -74.177 0.00 38.84  ? 237  ILE   B HD11 1 
ATOM   15150 H HD12 . ILE   B  1 211 ? 74.441 5.083   -74.410 0.00 39.17  ? 237  ILE   B HD12 1 
ATOM   15151 H HD13 . ILE   B  1 211 ? 73.315 5.180   -75.793 0.00 39.42  ? 237  ILE   B HD13 1 
ATOM   15152 N N    . SER   B  1 212 ? 76.301 3.820   -79.245 1.00 31.74  ? 238  SER   B N    1 
ATOM   15153 C CA   . SER   B  1 212 ? 77.300 3.517   -80.262 1.00 33.41  ? 238  SER   B CA   1 
ATOM   15154 C C    . SER   B  1 212 ? 78.683 3.280   -79.632 1.00 34.65  ? 238  SER   B C    1 
ATOM   15155 O O    . SER   B  1 212 ? 78.905 3.533   -78.439 1.00 34.53  ? 238  SER   B O    1 
ATOM   15156 C CB   . SER   B  1 212 ? 77.365 4.668   -81.269 1.00 34.97  ? 238  SER   B CB   1 
ATOM   15157 O OG   . SER   B  1 212 ? 78.007 5.804   -80.720 1.00 37.78  ? 238  SER   B OG   1 
ATOM   15158 H H    . SER   B  1 212 ? 76.159 4.817   -79.122 0.00 41.30  ? 238  SER   B H    1 
ATOM   15159 H HA   . SER   B  1 212 ? 77.016 2.621   -80.810 0.00 44.31  ? 238  SER   B HA   1 
ATOM   15160 H HB2  . SER   B  1 212 ? 77.922 4.338   -82.145 0.00 46.71  ? 238  SER   B HB2  1 
ATOM   15161 H HB3  . SER   B  1 212 ? 76.351 4.942   -81.558 0.00 46.14  ? 238  SER   B HB3  1 
ATOM   15162 H HG   . SER   B  1 212 ? 78.038 6.535   -81.392 0.00 49.64  ? 238  SER   B HG   1 
ATOM   15163 N N    . GLU   B  1 213 ? 79.618 2.822   -80.452 1.00 35.23  ? 239  GLU   B N    1 
ATOM   15164 C CA   . GLU   B  1 213 ? 80.994 2.593   -80.029 1.00 36.08  ? 239  GLU   B CA   1 
ATOM   15165 C C    . GLU   B  1 213 ? 81.675 3.898   -79.563 1.00 35.49  ? 239  GLU   B C    1 
ATOM   15166 O O    . GLU   B  1 213 ? 82.446 3.853   -78.612 1.00 36.30  ? 239  GLU   B O    1 
ATOM   15167 C CB   . GLU   B  1 213 ? 81.780 1.971   -81.192 1.00 39.55  ? 239  GLU   B CB   1 
ATOM   15168 C CG   . GLU   B  1 213 ? 83.174 1.487   -80.831 1.00 46.14  ? 239  GLU   B CG   1 
ATOM   15169 C CD   . GLU   B  1 213 ? 83.857 0.671   -81.910 1.00 52.79  ? 239  GLU   B CD   1 
ATOM   15170 O OE1  . GLU   B  1 213 ? 83.191 0.311   -82.907 1.00 54.35  ? 239  GLU   B OE1  1 
ATOM   15171 O OE2  . GLU   B  1 213 ? 85.070 0.401   -81.762 1.00 55.76  ? 239  GLU   B OE2  1 
ATOM   15172 H H    . GLU   B  1 213 ? 79.435 2.609   -81.428 0.00 47.23  ? 239  GLU   B H    1 
ATOM   15173 H HA   . GLU   B  1 213 ? 81.006 1.878   -79.210 0.00 47.87  ? 239  GLU   B HA   1 
ATOM   15174 H HB2  . GLU   B  1 213 ? 81.214 1.115   -81.555 0.00 53.06  ? 239  GLU   B HB2  1 
ATOM   15175 H HB3  . GLU   B  1 213 ? 81.879 2.710   -81.987 0.00 53.18  ? 239  GLU   B HB3  1 
ATOM   15176 H HG2  . GLU   B  1 213 ? 83.825 2.337   -80.648 0.00 61.14  ? 239  GLU   B HG2  1 
ATOM   15177 H HG3  . GLU   B  1 213 ? 83.117 0.891   -79.923 0.00 60.90  ? 239  GLU   B HG3  1 
ATOM   15178 N N    . GLU   B  1 214 ? 81.363 5.051   -80.189 1.00 34.23  ? 240  GLU   B N    1 
ATOM   15179 C CA   . GLU   B  1 214 ? 81.979 6.349   -79.880 1.00 34.30  ? 240  GLU   B CA   1 
ATOM   15180 C C    . GLU   B  1 214 ? 81.301 7.193   -78.799 1.00 33.01  ? 240  GLU   B C    1 
ATOM   15181 O O    . GLU   B  1 214 ? 81.861 8.231   -78.448 1.00 33.03  ? 240  GLU   B O    1 
ATOM   15182 C CB   . GLU   B  1 214 ? 82.040 7.220   -81.157 1.00 38.94  ? 240  GLU   B CB   1 
ATOM   15183 C CG   . GLU   B  1 214 ? 82.735 6.591   -82.353 1.00 47.53  ? 240  GLU   B CG   1 
ATOM   15184 C CD   . GLU   B  1 214 ? 83.749 7.468   -83.064 1.00 59.15  ? 240  GLU   B CD   1 
ATOM   15185 O OE1  . GLU   B  1 214 ? 84.595 8.091   -82.380 1.00 61.84  ? 240  GLU   B OE1  1 
ATOM   15186 O OE2  . GLU   B  1 214 ? 83.711 7.513   -84.316 1.00 63.24  ? 240  GLU   B OE2  1 
ATOM   15187 H H    . GLU   B  1 214 ? 80.682 5.119   -80.939 0.00 45.85  ? 240  GLU   B H    1 
ATOM   15188 H HA   . GLU   B  1 214 ? 83.006 6.197   -79.552 0.00 45.98  ? 240  GLU   B HA   1 
ATOM   15189 H HB2  . GLU   B  1 214 ? 81.019 7.443   -81.462 0.00 51.62  ? 240  GLU   B HB2  1 
ATOM   15190 H HB3  . GLU   B  1 214 ? 82.551 8.152   -80.921 0.00 51.79  ? 240  GLU   B HB3  1 
ATOM   15191 H HG2  . GLU   B  1 214 ? 83.251 5.685   -82.040 0.00 62.80  ? 240  GLU   B HG2  1 
ATOM   15192 H HG3  . GLU   B  1 214 ? 81.972 6.333   -83.085 0.00 62.86  ? 240  GLU   B HG3  1 
ATOM   15193 N N    . ASP   B  1 215 ? 80.104 6.825   -78.309 1.00 31.85  ? 241  ASP   B N    1 
ATOM   15194 C CA   . ASP   B  1 215 ? 79.398 7.662   -77.326 1.00 31.97  ? 241  ASP   B CA   1 
ATOM   15195 C C    . ASP   B  1 215 ? 80.210 7.999   -76.058 1.00 32.39  ? 241  ASP   B C    1 
ATOM   15196 O O    . ASP   B  1 215 ? 80.042 9.096   -75.522 1.00 32.39  ? 241  ASP   B O    1 
ATOM   15197 C CB   . ASP   B  1 215 ? 78.031 7.054   -76.948 1.00 32.75  ? 241  ASP   B CB   1 
ATOM   15198 C CG   . ASP   B  1 215 ? 76.958 7.242   -78.015 1.00 36.79  ? 241  ASP   B CG   1 
ATOM   15199 O OD1  . ASP   B  1 215 ? 77.140 8.101   -78.897 1.00 38.01  ? 241  ASP   B OD1  1 
ATOM   15200 O OD2  . ASP   B  1 215 ? 75.937 6.532   -77.965 1.00 38.20  ? 241  ASP   B OD2  1 
ATOM   15201 H H    . ASP   B  1 215 ? 79.605 5.979   -78.564 0.00 41.85  ? 241  ASP   B H    1 
ATOM   15202 H HA   . ASP   B  1 215 ? 79.216 8.618   -77.813 0.00 41.54  ? 241  ASP   B HA   1 
ATOM   15203 H HB2  . ASP   B  1 215 ? 78.146 5.987   -76.768 0.00 42.00  ? 241  ASP   B HB2  1 
ATOM   15204 H HB3  . ASP   B  1 215 ? 77.679 7.541   -76.040 0.00 41.60  ? 241  ASP   B HB3  1 
ATOM   15205 N N    . PHE   B  1 216 ? 81.100 7.109   -75.595 1.00 32.60  ? 242  PHE   B N    1 
ATOM   15206 C CA   . PHE   B  1 216 ? 81.903 7.362   -74.382 1.00 32.82  ? 242  PHE   B CA   1 
ATOM   15207 C C    . PHE   B  1 216 ? 83.410 7.134   -74.604 1.00 35.22  ? 242  PHE   B C    1 
ATOM   15208 O O    . PHE   B  1 216 ? 84.128 6.910   -73.632 1.00 36.02  ? 242  PHE   B O    1 
ATOM   15209 C CB   . PHE   B  1 216 ? 81.452 6.403   -73.265 1.00 31.65  ? 242  PHE   B CB   1 
ATOM   15210 C CG   . PHE   B  1 216 ? 79.963 6.293   -73.060 1.00 30.97  ? 242  PHE   B CG   1 
ATOM   15211 C CD1  . PHE   B  1 216 ? 79.220 7.387   -72.661 1.00 31.11  ? 242  PHE   B CD1  1 
ATOM   15212 C CD2  . PHE   B  1 216 ? 79.314 5.085   -73.221 1.00 31.28  ? 242  PHE   B CD2  1 
ATOM   15213 C CE1  . PHE   B  1 216 ? 77.852 7.285   -72.473 1.00 31.42  ? 242  PHE   B CE1  1 
ATOM   15214 C CE2  . PHE   B  1 216 ? 77.950 4.985   -73.023 1.00 31.52  ? 242  PHE   B CE2  1 
ATOM   15215 C CZ   . PHE   B  1 216 ? 77.225 6.086   -72.657 1.00 31.06  ? 242  PHE   B CZ   1 
ATOM   15216 H H    . PHE   B  1 216 ? 81.285 6.207   -76.020 0.00 42.32  ? 242  PHE   B H    1 
ATOM   15217 H HA   . PHE   B  1 216 ? 81.770 8.380   -74.022 0.00 42.07  ? 242  PHE   B HA   1 
ATOM   15218 H HB2  . PHE   B  1 216 ? 81.839 5.411   -73.492 0.00 40.64  ? 242  PHE   B HB2  1 
ATOM   15219 H HB3  . PHE   B  1 216 ? 81.874 6.746   -72.323 0.00 40.28  ? 242  PHE   B HB3  1 
ATOM   15220 H HD1  . PHE   B  1 216 ? 79.705 8.339   -72.533 0.00 39.07  ? 242  PHE   B HD1  1 
ATOM   15221 H HD2  . PHE   B  1 216 ? 79.868 4.210   -73.514 0.00 39.78  ? 242  PHE   B HD2  1 
ATOM   15222 H HE1  . PHE   B  1 216 ? 77.283 8.151   -72.179 0.00 38.78  ? 242  PHE   B HE1  1 
ATOM   15223 H HE2  . PHE   B  1 216 ? 77.461 4.037   -73.146 0.00 39.40  ? 242  PHE   B HE2  1 
ATOM   15224 H HZ   . PHE   B  1 216 ? 76.164 6.001   -72.492 0.00 38.27  ? 242  PHE   B HZ   1 
ATOM   15225 N N    . LYS   B  1 217 ? 83.895 7.152   -75.856 1.00 36.28  ? 243  LYS   B N    1 
ATOM   15226 C CA   . LYS   B  1 217 ? 85.289 6.781   -76.166 1.00 37.39  ? 243  LYS   B CA   1 
ATOM   15227 C C    . LYS   B  1 217 ? 86.424 7.468   -75.365 1.00 36.91  ? 243  LYS   B C    1 
ATOM   15228 O O    . LYS   B  1 217 ? 87.429 6.803   -75.073 1.00 37.72  ? 243  LYS   B O    1 
ATOM   15229 C CB   . LYS   B  1 217 ? 85.609 6.958   -77.677 1.00 40.60  ? 243  LYS   B CB   1 
ATOM   15230 C CG   . LYS   B  1 217 ? 85.628 5.647   -78.448 1.00 46.63  ? 243  LYS   B CG   1 
ATOM   15231 C CD   . LYS   B  1 217 ? 85.800 5.809   -79.937 1.00 51.88  ? 243  LYS   B CD   1 
ATOM   15232 C CE   . LYS   B  1 217 ? 85.328 4.533   -80.571 1.00 56.42  ? 243  LYS   B CE   1 
ATOM   15233 N NZ   . LYS   B  1 217 ? 85.576 4.462   -82.031 1.00 58.30  ? 243  LYS   B NZ   1 
ATOM   15234 H H    . LYS   B  1 217 ? 83.352 7.418   -76.672 0.00 47.45  ? 243  LYS   B H    1 
ATOM   15235 H HA   . LYS   B  1 217 ? 85.350 5.727   -75.893 0.00 49.23  ? 243  LYS   B HA   1 
ATOM   15236 H HB2  . LYS   B  1 217 ? 84.883 7.619   -78.148 0.00 53.54  ? 243  LYS   B HB2  1 
ATOM   15237 H HB3  . LYS   B  1 217 ? 86.602 7.397   -77.772 0.00 53.98  ? 243  LYS   B HB3  1 
ATOM   15238 H HG2  . LYS   B  1 217 ? 86.453 5.037   -78.084 0.00 61.33  ? 243  LYS   B HG2  1 
ATOM   15239 H HG3  . LYS   B  1 217 ? 84.684 5.134   -78.268 0.00 60.83  ? 243  LYS   B HG3  1 
ATOM   15240 H HD2  . LYS   B  1 217 ? 85.184 6.632   -80.297 0.00 67.89  ? 243  LYS   B HD2  1 
ATOM   15241 H HD3  . LYS   B  1 217 ? 86.850 5.970   -80.176 0.00 68.39  ? 243  LYS   B HD3  1 
ATOM   15242 H HE2  . LYS   B  1 217 ? 85.829 3.690   -80.098 0.00 73.70  ? 243  LYS   B HE2  1 
ATOM   15243 H HE3  . LYS   B  1 217 ? 84.255 4.474   -80.406 0.00 73.30  ? 243  LYS   B HE3  1 
ATOM   15244 H HZ1  . LYS   B  1 217 ? 86.533 4.168   -82.199 0.00 76.89  ? 243  LYS   B HZ1  1 
ATOM   15245 H HZ2  . LYS   B  1 217 ? 84.945 3.790   -82.455 0.00 76.60  ? 243  LYS   B HZ2  1 
ATOM   15246 H HZ3  . LYS   B  1 217 ? 85.424 5.371   -82.455 0.00 76.55  ? 243  LYS   B HZ3  1 
ATOM   15247 N N    . GLY   B  1 218 ? 86.319 8.769   -75.107 1.00 34.96  ? 244  GLY   B N    1 
ATOM   15248 C CA   . GLY   B  1 218 ? 87.370 9.493   -74.390 1.00 33.45  ? 244  GLY   B CA   1 
ATOM   15249 C C    . GLY   B  1 218 ? 87.204 9.545   -72.876 1.00 31.77  ? 244  GLY   B C    1 
ATOM   15250 O O    . GLY   B  1 218 ? 88.053 10.108  -72.181 1.00 32.12  ? 244  GLY   B O    1 
ATOM   15251 H H    . GLY   B  1 218 ? 85.531 9.346   -75.382 0.00 46.08  ? 244  GLY   B H    1 
ATOM   15252 H HA2  . GLY   B  1 218 ? 88.347 9.065   -74.611 0.00 45.03  ? 244  GLY   B HA2  1 
ATOM   15253 H HA3  . GLY   B  1 218 ? 87.379 10.520  -74.750 0.00 44.70  ? 244  GLY   B HA3  1 
ATOM   15254 N N    . LEU   B  1 219 ? 86.141 8.940   -72.343 1.00 30.21  ? 245  LEU   B N    1 
ATOM   15255 C CA   . LEU   B  1 219 ? 85.844 8.981   -70.914 1.00 29.00  ? 245  LEU   B CA   1 
ATOM   15256 C C    . LEU   B  1 219 ? 86.602 7.908   -70.110 1.00 28.10  ? 245  LEU   B C    1 
ATOM   15257 O O    . LEU   B  1 219 ? 85.997 7.081   -69.433 1.00 27.50  ? 245  LEU   B O    1 
ATOM   15258 C CB   . LEU   B  1 219 ? 84.319 8.889   -70.705 1.00 28.63  ? 245  LEU   B CB   1 
ATOM   15259 C CG   . LEU   B  1 219 ? 83.467 9.911   -71.507 1.00 29.67  ? 245  LEU   B CG   1 
ATOM   15260 C CD1  . LEU   B  1 219 ? 81.996 9.776   -71.192 1.00 29.47  ? 245  LEU   B CD1  1 
ATOM   15261 C CD2  . LEU   B  1 219 ? 83.913 11.342  -71.225 1.00 30.19  ? 245  LEU   B CD2  1 
ATOM   15262 H H    . LEU   B  1 219 ? 85.462 8.394   -72.862 0.00 39.72  ? 245  LEU   B H    1 
ATOM   15263 H HA   . LEU   B  1 219 ? 86.161 9.942   -70.512 0.00 37.97  ? 245  LEU   B HA   1 
ATOM   15264 H HB2  . LEU   B  1 219 ? 83.986 7.892   -70.989 0.00 36.92  ? 245  LEU   B HB2  1 
ATOM   15265 H HB3  . LEU   B  1 219 ? 84.106 9.062   -69.652 0.00 36.66  ? 245  LEU   B HB3  1 
ATOM   15266 H HG   . LEU   B  1 219 ? 83.594 9.724   -72.572 0.00 38.41  ? 245  LEU   B HG   1 
ATOM   15267 H HD11 . LEU   B  1 219 ? 81.421 10.294  -71.958 0.00 37.39  ? 245  LEU   B HD11 1 
ATOM   15268 H HD12 . LEU   B  1 219 ? 81.724 8.723   -71.164 0.00 37.28  ? 245  LEU   B HD12 1 
ATOM   15269 H HD13 . LEU   B  1 219 ? 81.804 10.229  -70.221 0.00 37.10  ? 245  LEU   B HD13 1 
ATOM   15270 H HD21 . LEU   B  1 219 ? 83.096 12.022  -71.462 0.00 38.68  ? 245  LEU   B HD21 1 
ATOM   15271 H HD22 . LEU   B  1 219 ? 84.186 11.427  -70.176 0.00 38.72  ? 245  LEU   B HD22 1 
ATOM   15272 H HD23 . LEU   B  1 219 ? 84.775 11.572  -71.850 0.00 39.27  ? 245  LEU   B HD23 1 
ATOM   15273 N N    . ILE   B  1 220 ? 87.931 8.013   -70.110 1.00 28.09  ? 246  ILE   B N    1 
ATOM   15274 C CA   . ILE   B  1 220 ? 88.831 7.065   -69.457 1.00 28.76  ? 246  ILE   B CA   1 
ATOM   15275 C C    . ILE   B  1 220 ? 88.848 7.132   -67.919 1.00 27.97  ? 246  ILE   B C    1 
ATOM   15276 O O    . ILE   B  1 220 ? 89.383 6.211   -67.314 1.00 28.28  ? 246  ILE   B O    1 
ATOM   15277 C CB   . ILE   B  1 220 ? 90.284 7.164   -70.026 1.00 30.15  ? 246  ILE   B CB   1 
ATOM   15278 C CG1  . ILE   B  1 220 ? 90.978 8.487   -69.652 1.00 31.38  ? 246  ILE   B CG1  1 
ATOM   15279 C CG2  . ILE   B  1 220 ? 90.282 6.924   -71.556 1.00 31.28  ? 246  ILE   B CG2  1 
ATOM   15280 C CD1  . ILE   B  1 220 ? 92.476 8.546   -70.092 1.00 33.73  ? 246  ILE   B CD1  1 
ATOM   15281 H H    . ILE   B  1 220 ? 88.412 8.778   -70.572 0.00 37.70  ? 246  ILE   B H    1 
ATOM   15282 H HA   . ILE   B  1 220 ? 88.479 6.066   -69.705 0.00 38.44  ? 246  ILE   B HA   1 
ATOM   15283 H HB   . ILE   B  1 220 ? 90.862 6.358   -69.575 0.00 41.01  ? 246  ILE   B HB   1 
ATOM   15284 H HG12 . ILE   B  1 220 ? 90.458 9.312   -70.137 0.00 42.36  ? 246  ILE   B HG12 1 
ATOM   15285 H HG13 . ILE   B  1 220 ? 90.966 8.625   -68.572 0.00 42.30  ? 246  ILE   B HG13 1 
ATOM   15286 H HG21 . ILE   B  1 220 ? 91.301 6.762   -71.904 0.00 43.00  ? 246  ILE   B HG21 1 
ATOM   15287 H HG22 . ILE   B  1 220 ? 89.675 6.046   -71.773 0.00 42.36  ? 246  ILE   B HG22 1 
ATOM   15288 H HG23 . ILE   B  1 220 ? 89.857 7.798   -72.049 0.00 42.42  ? 246  ILE   B HG23 1 
ATOM   15289 H HD11 . ILE   B  1 220 ? 92.935 9.432   -69.655 0.00 46.13  ? 246  ILE   B HD11 1 
ATOM   15290 H HD12 . ILE   B  1 220 ? 92.985 7.651   -69.739 0.00 46.21  ? 246  ILE   B HD12 1 
ATOM   15291 H HD13 . ILE   B  1 220 ? 92.530 8.608   -71.178 0.00 46.24  ? 246  ILE   B HD13 1 
ATOM   15292 N N    . ASN   B  1 221 ? 88.321 8.195   -67.288 1.00 27.76  ? 247  ASN   B N    1 
ATOM   15293 C CA   . ASN   B  1 221 ? 88.243 8.289   -65.816 1.00 28.02  ? 247  ASN   B CA   1 
ATOM   15294 C C    . ASN   B  1 221 ? 86.824 8.003   -65.277 1.00 25.99  ? 247  ASN   B C    1 
ATOM   15295 O O    . ASN   B  1 221 ? 86.595 8.165   -64.077 1.00 25.51  ? 247  ASN   B O    1 
ATOM   15296 C CB   . ASN   B  1 221 ? 88.664 9.691   -65.343 1.00 31.69  ? 247  ASN   B CB   1 
ATOM   15297 C CG   . ASN   B  1 221 ? 90.107 9.960   -65.384 1.00 40.31  ? 247  ASN   B CG   1 
ATOM   15298 O OD1  . ASN   B  1 221 ? 90.920 9.038   -65.534 1.00 41.34  ? 247  ASN   B OD1  1 
ATOM   15299 N ND2  . ASN   B  1 221 ? 90.525 11.167  -65.060 1.00 46.06  ? 247  ASN   B ND2  1 
ATOM   15300 H H    . ASN   B  1 221 ? 87.942 9.009   -67.760 0.00 36.60  ? 247  ASN   B H    1 
ATOM   15301 H HA   . ASN   B  1 221 ? 88.903 7.561   -65.346 0.00 36.94  ? 247  ASN   B HA   1 
ATOM   15302 H HB2  . ASN   B  1 221 ? 88.174 10.440  -65.965 0.00 41.14  ? 247  ASN   B HB2  1 
ATOM   15303 H HB3  . ASN   B  1 221 ? 88.359 9.835   -64.308 0.00 40.99  ? 247  ASN   B HB3  1 
ATOM   15304 H HD21 . ASN   B  1 221 ? 91.157 11.192  -65.835 0.00 59.62  ? 247  ASN   B HD21 1 
ATOM   15305 H HD22 . ASN   B  1 221 ? 89.919 11.920  -64.753 0.00 58.99  ? 247  ASN   B HD22 1 
ATOM   15306 N N    . LEU   B  1 222 ? 85.871 7.617   -66.146 1.00 24.56  ? 248  LEU   B N    1 
ATOM   15307 C CA   . LEU   B  1 222 ? 84.493 7.393   -65.725 1.00 23.97  ? 248  LEU   B CA   1 
ATOM   15308 C C    . LEU   B  1 222 ? 84.389 6.239   -64.741 1.00 23.76  ? 248  LEU   B C    1 
ATOM   15309 O O    . LEU   B  1 222 ? 84.841 5.137   -65.049 1.00 23.52  ? 248  LEU   B O    1 
ATOM   15310 C CB   . LEU   B  1 222 ? 83.582 7.127   -66.945 1.00 23.83  ? 248  LEU   B CB   1 
ATOM   15311 C CG   . LEU   B  1 222 ? 82.094 7.441   -66.757 1.00 25.24  ? 248  LEU   B CG   1 
ATOM   15312 C CD1  . LEU   B  1 222 ? 81.861 8.961   -66.632 1.00 25.39  ? 248  LEU   B CD1  1 
ATOM   15313 C CD2  . LEU   B  1 222 ? 81.263 6.859   -67.912 1.00 25.55  ? 248  LEU   B CD2  1 
ATOM   15314 H H    . LEU   B  1 222 ? 86.028 7.421   -67.129 0.00 31.97  ? 248  LEU   B H    1 
ATOM   15315 H HA   . LEU   B  1 222 ? 84.156 8.301   -65.232 0.00 30.30  ? 248  LEU   B HA   1 
ATOM   15316 H HB2  . LEU   B  1 222 ? 83.929 7.731   -67.781 0.00 30.49  ? 248  LEU   B HB2  1 
ATOM   15317 H HB3  . LEU   B  1 222 ? 83.659 6.074   -67.212 0.00 30.35  ? 248  LEU   B HB3  1 
ATOM   15318 H HG   . LEU   B  1 222 ? 81.751 6.975   -65.835 0.00 31.17  ? 248  LEU   B HG   1 
ATOM   15319 H HD11 . LEU   B  1 222 ? 80.806 9.165   -66.812 0.00 31.22  ? 248  LEU   B HD11 1 
ATOM   15320 H HD12 . LEU   B  1 222 ? 82.118 9.286   -65.625 0.00 31.40  ? 248  LEU   B HD12 1 
ATOM   15321 H HD13 . LEU   B  1 222 ? 82.471 9.489   -67.364 0.00 31.81  ? 248  LEU   B HD13 1 
ATOM   15322 H HD21 . LEU   B  1 222 ? 80.209 7.072   -67.736 0.00 31.44  ? 248  LEU   B HD21 1 
ATOM   15323 H HD22 . LEU   B  1 222 ? 81.584 7.320   -68.845 0.00 32.05  ? 248  LEU   B HD22 1 
ATOM   15324 H HD23 . LEU   B  1 222 ? 81.419 5.783   -67.955 0.00 31.88  ? 248  LEU   B HD23 1 
ATOM   15325 N N    . THR   B  1 223 ? 83.829 6.508   -63.547 1.00 23.91  ? 249  THR   B N    1 
ATOM   15326 C CA   . THR   B  1 223 ? 83.600 5.508   -62.508 1.00 23.92  ? 249  THR   B CA   1 
ATOM   15327 C C    . THR   B  1 223 ? 82.093 5.141   -62.420 1.00 23.60  ? 249  THR   B C    1 
ATOM   15328 O O    . THR   B  1 223 ? 81.773 4.078   -61.894 1.00 23.82  ? 249  THR   B O    1 
ATOM   15329 C CB   . THR   B  1 223 ? 84.137 5.973   -61.155 1.00 25.71  ? 249  THR   B CB   1 
ATOM   15330 O OG1  . THR   B  1 223 ? 83.359 7.082   -60.710 1.00 27.82  ? 249  THR   B OG1  1 
ATOM   15331 C CG2  . THR   B  1 223 ? 85.624 6.324   -61.207 1.00 25.22  ? 249  THR   B CG2  1 
ATOM   15332 H H    . THR   B  1 223 ? 83.519 7.432   -63.265 0.00 29.73  ? 249  THR   B H    1 
ATOM   15333 H HA   . THR   B  1 223 ? 84.177 4.612   -62.722 0.00 30.01  ? 249  THR   B HA   1 
ATOM   15334 H HB   . THR   B  1 223 ? 84.017 5.157   -60.442 0.00 31.82  ? 249  THR   B HB   1 
ATOM   15335 H HG1  . THR   B  1 223 ? 83.584 7.897   -61.230 0.00 34.21  ? 249  THR   B HG1  1 
ATOM   15336 H HG21 . THR   B  1 223 ? 85.984 6.545   -60.203 0.00 31.88  ? 249  THR   B HG21 1 
ATOM   15337 H HG22 . THR   B  1 223 ? 86.188 5.485   -61.610 0.00 32.13  ? 249  THR   B HG22 1 
ATOM   15338 H HG23 . THR   B  1 223 ? 85.787 7.200   -61.835 0.00 31.94  ? 249  THR   B HG23 1 
ATOM   15339 N N    . LEU   B  1 224 ? 81.174 6.010   -62.906 1.00 22.90  ? 250  LEU   B N    1 
ATOM   15340 C CA   . LEU   B  1 224 ? 79.748 5.717   -62.866 1.00 22.34  ? 250  LEU   B CA   1 
ATOM   15341 C C    . LEU   B  1 224 ? 79.096 6.084   -64.176 1.00 22.52  ? 250  LEU   B C    1 
ATOM   15342 O O    . LEU   B  1 224 ? 79.359 7.168   -64.712 1.00 23.07  ? 250  LEU   B O    1 
ATOM   15343 C CB   . LEU   B  1 224 ? 79.050 6.472   -61.711 1.00 21.70  ? 250  LEU   B CB   1 
ATOM   15344 C CG   . LEU   B  1 224 ? 77.521 6.261   -61.581 1.00 22.10  ? 250  LEU   B CG   1 
ATOM   15345 C CD1  . LEU   B  1 224 ? 77.098 6.322   -60.139 1.00 22.54  ? 250  LEU   B CD1  1 
ATOM   15346 C CD2  . LEU   B  1 224 ? 76.736 7.304   -62.388 1.00 22.10  ? 250  LEU   B CD2  1 
ATOM   15347 H H    . LEU   B  1 224 ? 81.381 6.916   -63.314 0.00 27.85  ? 250  LEU   B H    1 
ATOM   15348 H HA   . LEU   B  1 224 ? 79.589 4.652   -62.704 0.00 26.65  ? 250  LEU   B HA   1 
ATOM   15349 H HB2  . LEU   B  1 224 ? 79.503 6.146   -60.776 0.00 25.54  ? 250  LEU   B HB2  1 
ATOM   15350 H HB3  . LEU   B  1 224 ? 79.222 7.539   -61.842 0.00 25.57  ? 250  LEU   B HB3  1 
ATOM   15351 H HG   . LEU   B  1 224 ? 77.237 5.275   -61.949 0.00 25.59  ? 250  LEU   B HG   1 
ATOM   15352 H HD11 . LEU   B  1 224 ? 76.013 6.241   -60.085 0.00 25.53  ? 250  LEU   B HD11 1 
ATOM   15353 H HD12 . LEU   B  1 224 ? 77.556 5.496   -59.597 0.00 25.89  ? 250  LEU   B HD12 1 
ATOM   15354 H HD13 . LEU   B  1 224 ? 77.422 7.273   -59.717 0.00 25.84  ? 250  LEU   B HD13 1 
ATOM   15355 H HD21 . LEU   B  1 224 ? 75.670 7.103   -62.282 0.00 25.20  ? 250  LEU   B HD21 1 
ATOM   15356 H HD22 . LEU   B  1 224 ? 76.966 8.298   -62.008 0.00 25.47  ? 250  LEU   B HD22 1 
ATOM   15357 H HD23 . LEU   B  1 224 ? 77.020 7.234   -63.437 0.00 25.70  ? 250  LEU   B HD23 1 
ATOM   15358 N N    . LEU   B  1 225 ? 78.219 5.189   -64.673 1.00 21.55  ? 251  LEU   B N    1 
ATOM   15359 C CA   . LEU   B  1 225 ? 77.432 5.410   -65.865 1.00 21.35  ? 251  LEU   B CA   1 
ATOM   15360 C C    . LEU   B  1 225 ? 76.018 4.940   -65.549 1.00 22.18  ? 251  LEU   B C    1 
ATOM   15361 O O    . LEU   B  1 225 ? 75.816 3.783   -65.162 1.00 22.72  ? 251  LEU   B O    1 
ATOM   15362 C CB   . LEU   B  1 225 ? 77.993 4.636   -67.079 1.00 21.25  ? 251  LEU   B CB   1 
ATOM   15363 C CG   . LEU   B  1 225 ? 77.220 4.796   -68.395 1.00 23.47  ? 251  LEU   B CG   1 
ATOM   15364 C CD1  . LEU   B  1 225 ? 77.131 6.268   -68.816 1.00 24.05  ? 251  LEU   B CD1  1 
ATOM   15365 C CD2  . LEU   B  1 225 ? 77.871 3.972   -69.510 1.00 23.88  ? 251  LEU   B CD2  1 
ATOM   15366 H H    . LEU   B  1 225 ? 78.043 4.280   -64.255 0.00 25.54  ? 251  LEU   B H    1 
ATOM   15367 H HA   . LEU   B  1 225 ? 77.410 6.473   -66.098 0.00 25.37  ? 251  LEU   B HA   1 
ATOM   15368 H HB2  . LEU   B  1 225 ? 79.003 4.994   -67.268 0.00 25.95  ? 251  LEU   B HB2  1 
ATOM   15369 H HB3  . LEU   B  1 225 ? 78.017 3.574   -66.835 0.00 25.71  ? 251  LEU   B HB3  1 
ATOM   15370 H HG   . LEU   B  1 225 ? 76.207 4.419   -68.269 0.00 28.19  ? 251  LEU   B HG   1 
ATOM   15371 H HD11 . LEU   B  1 225 ? 76.793 6.319   -69.850 0.00 29.29  ? 251  LEU   B HD11 1 
ATOM   15372 H HD12 . LEU   B  1 225 ? 76.414 6.779   -68.176 0.00 28.80  ? 251  LEU   B HD12 1 
ATOM   15373 H HD13 . LEU   B  1 225 ? 78.114 6.726   -68.720 0.00 29.32  ? 251  LEU   B HD13 1 
ATOM   15374 H HD21 . LEU   B  1 225 ? 77.276 4.063   -70.417 0.00 29.45  ? 251  LEU   B HD21 1 
ATOM   15375 H HD22 . LEU   B  1 225 ? 78.877 4.351   -69.688 0.00 29.64  ? 251  LEU   B HD22 1 
ATOM   15376 H HD23 . LEU   B  1 225 ? 77.917 2.930   -69.199 0.00 29.40  ? 251  LEU   B HD23 1 
ATOM   15377 N N    . ASP   B  1 226 ? 75.045 5.828   -65.722 1.00 21.34  ? 252  ASP   B N    1 
ATOM   15378 C CA   . ASP   B  1 226 ? 73.655 5.493   -65.474 1.00 21.32  ? 252  ASP   B CA   1 
ATOM   15379 C C    . ASP   B  1 226 ? 72.875 5.672   -66.763 1.00 21.82  ? 252  ASP   B C    1 
ATOM   15380 O O    . ASP   B  1 226 ? 72.614 6.803   -67.164 1.00 22.54  ? 252  ASP   B O    1 
ATOM   15381 C CB   . ASP   B  1 226 ? 73.095 6.358   -64.328 1.00 20.54  ? 252  ASP   B CB   1 
ATOM   15382 C CG   . ASP   B  1 226 ? 71.604 6.222   -64.066 1.00 23.65  ? 252  ASP   B CG   1 
ATOM   15383 O OD1  . ASP   B  1 226 ? 70.991 5.263   -64.588 1.00 22.67  ? 252  ASP   B OD1  1 
ATOM   15384 O OD2  . ASP   B  1 226 ? 71.059 7.051   -63.292 1.00 23.54  ? 252  ASP   B OD2  1 
ATOM   15385 H H    . ASP   B  1 226 ? 75.182 6.787   -66.029 0.00 24.84  ? 252  ASP   B H    1 
ATOM   15386 H HA   . ASP   B  1 226 ? 73.578 4.448   -65.183 0.00 24.42  ? 252  ASP   B HA   1 
ATOM   15387 H HB2  . ASP   B  1 226 ? 73.609 6.077   -63.410 0.00 23.08  ? 252  ASP   B HB2  1 
ATOM   15388 H HB3  . ASP   B  1 226 ? 73.285 7.406   -64.536 0.00 23.20  ? 252  ASP   B HB3  1 
ATOM   15389 N N    . LEU   B  1 227 ? 72.525 4.550   -67.416 1.00 21.24  ? 253  LEU   B N    1 
ATOM   15390 C CA   . LEU   B  1 227 ? 71.701 4.538   -68.633 1.00 21.68  ? 253  LEU   B CA   1 
ATOM   15391 C C    . LEU   B  1 227 ? 70.304 3.934   -68.353 1.00 21.28  ? 253  LEU   B C    1 
ATOM   15392 O O    . LEU   B  1 227 ? 69.630 3.500   -69.289 1.00 21.71  ? 253  LEU   B O    1 
ATOM   15393 C CB   . LEU   B  1 227 ? 72.411 3.712   -69.723 1.00 22.35  ? 253  LEU   B CB   1 
ATOM   15394 C CG   . LEU   B  1 227 ? 73.641 4.342   -70.366 1.00 25.23  ? 253  LEU   B CG   1 
ATOM   15395 C CD1  . LEU   B  1 227 ? 74.383 3.308   -71.215 1.00 25.85  ? 253  LEU   B CD1  1 
ATOM   15396 C CD2  . LEU   B  1 227 ? 73.254 5.557   -71.225 1.00 26.34  ? 253  LEU   B CD2  1 
ATOM   15397 H H    . LEU   B  1 227 ? 72.790 3.617   -67.115 0.00 24.63  ? 253  LEU   B H    1 
ATOM   15398 H HA   . LEU   B  1 227 ? 71.539 5.551   -68.997 0.00 25.29  ? 253  LEU   B HA   1 
ATOM   15399 H HB2  . LEU   B  1 227 ? 72.747 2.779   -69.277 0.00 26.55  ? 253  LEU   B HB2  1 
ATOM   15400 H HB3  . LEU   B  1 227 ? 71.717 3.496   -70.534 0.00 26.66  ? 253  LEU   B HB3  1 
ATOM   15401 H HG   . LEU   B  1 227 ? 74.314 4.689   -69.584 0.00 30.21  ? 253  LEU   B HG   1 
ATOM   15402 H HD11 . LEU   B  1 227 ? 75.194 3.793   -71.756 0.00 31.76  ? 253  LEU   B HD11 1 
ATOM   15403 H HD12 . LEU   B  1 227 ? 74.788 2.540   -70.557 0.00 31.47  ? 253  LEU   B HD12 1 
ATOM   15404 H HD13 . LEU   B  1 227 ? 73.678 2.858   -71.912 0.00 31.61  ? 253  LEU   B HD13 1 
ATOM   15405 H HD21 . LEU   B  1 227 ? 74.114 5.860   -71.822 0.00 32.04  ? 253  LEU   B HD21 1 
ATOM   15406 H HD22 . LEU   B  1 227 ? 72.427 5.287   -71.879 0.00 31.81  ? 253  LEU   B HD22 1 
ATOM   15407 H HD23 . LEU   B  1 227 ? 72.965 6.381   -70.577 0.00 31.49  ? 253  LEU   B HD23 1 
ATOM   15408 N N    . SER   B  1 228 ? 69.839 3.950   -67.090 1.00 20.42  ? 254  SER   B N    1 
ATOM   15409 C CA   . SER   B  1 228 ? 68.549 3.377   -66.747 1.00 19.73  ? 254  SER   B CA   1 
ATOM   15410 C C    . SER   B  1 228 ? 67.370 4.111   -67.384 1.00 19.96  ? 254  SER   B C    1 
ATOM   15411 O O    . SER   B  1 228 ? 67.491 5.270   -67.740 1.00 20.21  ? 254  SER   B O    1 
ATOM   15412 C CB   . SER   B  1 228 ? 68.388 3.317   -65.223 1.00 19.29  ? 254  SER   B CB   1 
ATOM   15413 O OG   . SER   B  1 228 ? 68.471 4.598   -64.626 1.00 18.43  ? 254  SER   B OG   1 
ATOM   15414 H H    . SER   B  1 228 ? 70.318 4.365   -66.298 0.00 23.01  ? 254  SER   B H    1 
ATOM   15415 H HA   . SER   B  1 228 ? 68.525 2.351   -67.111 0.00 22.29  ? 254  SER   B HA   1 
ATOM   15416 H HB2  . SER   B  1 228 ? 67.415 2.886   -64.991 0.00 21.10  ? 254  SER   B HB2  1 
ATOM   15417 H HB3  . SER   B  1 228 ? 69.176 2.688   -64.812 0.00 21.30  ? 254  SER   B HB3  1 
ATOM   15418 H HG   . SER   B  1 228 ? 69.419 4.889   -64.571 0.00 20.11  ? 254  SER   B HG   1 
ATOM   15419 N N    . GLY   B  1 229 ? 66.239 3.429   -67.532 1.00 20.07  ? 255  GLY   B N    1 
ATOM   15420 C CA   . GLY   B  1 229 ? 65.015 4.020   -68.061 1.00 19.95  ? 255  GLY   B CA   1 
ATOM   15421 C C    . GLY   B  1 229 ? 65.004 4.363   -69.537 1.00 20.03  ? 255  GLY   B C    1 
ATOM   15422 O O    . GLY   B  1 229 ? 64.095 5.070   -69.980 1.00 20.32  ? 255  GLY   B O    1 
ATOM   15423 H H    . GLY   B  1 229 ? 66.141 2.446   -67.297 0.00 22.50  ? 255  GLY   B H    1 
ATOM   15424 H HA2  . GLY   B  1 229 ? 64.192 3.329   -67.883 0.00 22.30  ? 255  GLY   B HA2  1 
ATOM   15425 H HA3  . GLY   B  1 229 ? 64.805 4.937   -67.511 0.00 22.15  ? 255  GLY   B HA3  1 
ATOM   15426 N N    . ASN   B  1 230 ? 65.995 3.869   -70.313 1.00 19.79  ? 256  ASN   B N    1 
ATOM   15427 C CA   . ASN   B  1 230 ? 66.069 4.104   -71.763 1.00 20.14  ? 256  ASN   B CA   1 
ATOM   15428 C C    . ASN   B  1 230 ? 65.586 2.814   -72.392 1.00 20.96  ? 256  ASN   B C    1 
ATOM   15429 O O    . ASN   B  1 230 ? 66.187 1.778   -72.153 1.00 21.27  ? 256  ASN   B O    1 
ATOM   15430 C CB   . ASN   B  1 230 ? 67.494 4.472   -72.145 1.00 20.47  ? 256  ASN   B CB   1 
ATOM   15431 C CG   . ASN   B  1 230 ? 67.868 5.817   -71.559 1.00 21.99  ? 256  ASN   B CG   1 
ATOM   15432 O OD1  . ASN   B  1 230 ? 67.195 6.809   -71.805 1.00 23.48  ? 256  ASN   B OD1  1 
ATOM   15433 N ND2  . ASN   B  1 230 ? 68.920 5.888   -70.749 1.00 21.44  ? 256  ASN   B ND2  1 
ATOM   15434 H H    . ASN   B  1 230 ? 66.753 3.285   -69.974 0.00 22.87  ? 256  ASN   B H    1 
ATOM   15435 H HA   . ASN   B  1 230 ? 65.411 4.917   -72.067 0.00 23.72  ? 256  ASN   B HA   1 
ATOM   15436 H HB2  . ASN   B  1 230 ? 68.176 3.712   -71.768 0.00 24.30  ? 256  ASN   B HB2  1 
ATOM   15437 H HB3  . ASN   B  1 230 ? 67.568 4.538   -73.230 0.00 24.65  ? 256  ASN   B HB3  1 
ATOM   15438 H HD21 . ASN   B  1 230 ? 69.182 6.783   -70.349 0.00 25.02  ? 256  ASN   B HD21 1 
ATOM   15439 H HD22 . ASN   B  1 230 ? 69.461 5.060   -70.524 0.00 25.16  ? 256  ASN   B HD22 1 
ATOM   15440 N N    . CYS   B  1 231 ? 64.447 2.860   -73.118 1.00 21.69  ? 257  CYS   B N    1 
ATOM   15441 C CA   . CYS   B  1 231 ? 63.671 1.690   -73.559 1.00 22.81  ? 257  CYS   B CA   1 
ATOM   15442 C C    . CYS   B  1 231 ? 63.121 1.016   -72.307 1.00 23.44  ? 257  CYS   B C    1 
ATOM   15443 O O    . CYS   B  1 231 ? 63.461 -0.118  -72.000 1.00 23.48  ? 257  CYS   B O    1 
ATOM   15444 C CB   . CYS   B  1 231 ? 64.482 0.723   -74.408 1.00 24.29  ? 257  CYS   B CB   1 
ATOM   15445 S SG   . CYS   B  1 231 ? 64.975 1.411   -75.998 1.00 29.64  ? 257  CYS   B SG   1 
ATOM   15446 H H    . CYS   B  1 231 ? 64.025 3.729   -73.428 0.00 26.05  ? 257  CYS   B H    1 
ATOM   15447 H HA   . CYS   B  1 231 ? 62.810 2.015   -74.138 0.00 27.76  ? 257  CYS   B HA   1 
ATOM   15448 H HB2  . CYS   B  1 231 ? 65.382 0.426   -73.873 0.00 29.70  ? 257  CYS   B HB2  1 
ATOM   15449 H HB3  . CYS   B  1 231 ? 63.872 -0.157  -74.615 0.00 29.98  ? 257  CYS   B HB3  1 
ATOM   15450 N N    . PRO   B  1 232 ? 62.251 1.712   -71.569 1.00 23.50  ? 258  PRO   B N    1 
ATOM   15451 C CA   . PRO   B  1 232 ? 61.772 1.159   -70.292 1.00 23.30  ? 258  PRO   B CA   1 
ATOM   15452 C C    . PRO   B  1 232 ? 60.823 -0.028  -70.362 1.00 22.96  ? 258  PRO   B C    1 
ATOM   15453 O O    . PRO   B  1 232 ? 60.191 -0.280  -71.394 1.00 22.39  ? 258  PRO   B O    1 
ATOM   15454 C CB   . PRO   B  1 232 ? 61.084 2.359   -69.640 1.00 24.02  ? 258  PRO   B CB   1 
ATOM   15455 C CG   . PRO   B  1 232 ? 60.610 3.181   -70.813 1.00 24.45  ? 258  PRO   B CG   1 
ATOM   15456 C CD   . PRO   B  1 232 ? 61.741 3.081   -71.796 1.00 22.74  ? 258  PRO   B CD   1 
ATOM   15457 H HA   . PRO   B  1 232 ? 62.626 0.887   -69.674 0.00 26.99  ? 258  PRO   B HA   1 
ATOM   15458 H HB2  . PRO   B  1 232 ? 60.244 2.020   -69.037 0.00 27.51  ? 258  PRO   B HB2  1 
ATOM   15459 H HB3  . PRO   B  1 232 ? 61.799 2.917   -69.035 0.00 27.45  ? 258  PRO   B HB3  1 
ATOM   15460 H HG2  . PRO   B  1 232 ? 59.699 2.751   -71.229 0.00 28.66  ? 258  PRO   B HG2  1 
ATOM   15461 H HG3  . PRO   B  1 232 ? 60.455 4.214   -70.504 0.00 28.32  ? 258  PRO   B HG3  1 
ATOM   15462 H HD2  . PRO   B  1 232 ? 61.357 3.198   -72.808 0.00 27.09  ? 258  PRO   B HD2  1 
ATOM   15463 H HD3  . PRO   B  1 232 ? 62.507 3.820   -71.564 0.00 26.64  ? 258  PRO   B HD3  1 
ATOM   15464 N N    . ARG   B  1 233 ? 60.753 -0.781  -69.238 1.00 22.31  ? 259  ARG   B N    1 
ATOM   15465 C CA   . ARG   B  1 233 ? 59.814 -1.886  -69.059 1.00 22.46  ? 259  ARG   B CA   1 
ATOM   15466 C C    . ARG   B  1 233 ? 58.617 -1.171  -68.414 1.00 21.68  ? 259  ARG   B C    1 
ATOM   15467 O O    . ARG   B  1 233 ? 58.741 -0.698  -67.289 1.00 20.41  ? 259  ARG   B O    1 
ATOM   15468 C CB   . ARG   B  1 233 ? 60.410 -2.988  -68.162 1.00 24.39  ? 259  ARG   B CB   1 
ATOM   15469 C CG   . ARG   B  1 233 ? 59.361 -3.841  -67.457 1.00 27.87  ? 259  ARG   B CG   1 
ATOM   15470 C CD   . ARG   B  1 233 ? 59.945 -5.069  -66.797 1.00 29.33  ? 259  ARG   B CD   1 
ATOM   15471 N NE   . ARG   B  1 233 ? 58.896 -5.771  -66.052 1.00 30.05  ? 259  ARG   B NE   1 
ATOM   15472 C CZ   . ARG   B  1 233 ? 58.926 -7.054  -65.698 1.00 28.77  ? 259  ARG   B CZ   1 
ATOM   15473 N NH1  . ARG   B  1 233 ? 59.976 -7.812  -66.001 1.00 23.82  ? 259  ARG   B NH1  1 
ATOM   15474 N NH2  . ARG   B  1 233 ? 57.903 -7.590  -65.033 1.00 28.58  ? 259  ARG   B NH2  1 
ATOM   15475 H H    . ARG   B  1 233 ? 61.347 -0.619  -68.431 0.00 25.58  ? 259  ARG   B H    1 
ATOM   15476 H HA   . ARG   B  1 233 ? 59.524 -2.322  -70.014 0.00 26.50  ? 259  ARG   B HA   1 
ATOM   15477 H HB2  . ARG   B  1 233 ? 61.018 -3.650  -68.777 0.00 28.65  ? 259  ARG   B HB2  1 
ATOM   15478 H HB3  . ARG   B  1 233 ? 61.029 -2.539  -67.386 0.00 28.05  ? 259  ARG   B HB3  1 
ATOM   15479 H HG2  . ARG   B  1 233 ? 58.892 -3.252  -66.670 0.00 32.13  ? 259  ARG   B HG2  1 
ATOM   15480 H HG3  . ARG   B  1 233 ? 58.615 -4.164  -68.181 0.00 32.74  ? 259  ARG   B HG3  1 
ATOM   15481 H HD2  . ARG   B  1 233 ? 60.332 -5.712  -67.585 0.00 34.63  ? 259  ARG   B HD2  1 
ATOM   15482 H HD3  . ARG   B  1 233 ? 60.737 -4.779  -66.107 0.00 34.03  ? 259  ARG   B HD3  1 
ATOM   15483 H HE   . ARG   B  1 233 ? 58.066 -5.238  -65.809 0.00 34.87  ? 259  ARG   B HE   1 
ATOM   15484 H HH11 . ARG   B  1 233 ? 60.787 -7.452  -66.493 0.00 28.11  ? 259  ARG   B HH11 1 
ATOM   15485 H HH12 . ARG   B  1 233 ? 59.983 -8.785  -65.711 0.00 28.20  ? 259  ARG   B HH12 1 
ATOM   15486 H HH21 . ARG   B  1 233 ? 57.094 -7.025  -64.795 0.00 33.21  ? 259  ARG   B HH21 1 
ATOM   15487 H HH22 . ARG   B  1 233 ? 57.928 -8.566  -64.754 0.00 33.56  ? 259  ARG   B HH22 1 
ATOM   15488 N N    . CYS   B  1 234 ? 57.496 -1.063  -69.126 1.00 21.75  ? 260  CYS   B N    1 
ATOM   15489 C CA   . CYS   B  1 234 ? 56.378 -0.228  -68.701 1.00 22.85  ? 260  CYS   B CA   1 
ATOM   15490 C C    . CYS   B  1 234 ? 55.196 -0.919  -68.054 1.00 22.40  ? 260  CYS   B C    1 
ATOM   15491 O O    . CYS   B  1 234 ? 54.341 -0.188  -67.544 1.00 22.31  ? 260  CYS   B O    1 
ATOM   15492 C CB   . CYS   B  1 234 ? 55.909 0.609   -69.885 1.00 24.44  ? 260  CYS   B CB   1 
ATOM   15493 S SG   . CYS   B  1 234 ? 57.131 1.834   -70.430 1.00 30.54  ? 260  CYS   B SG   1 
ATOM   15494 H H    . CYS   B  1 234 ? 57.329 -1.552  -69.999 0.00 25.59  ? 260  CYS   B H    1 
ATOM   15495 H HA   . CYS   B  1 234 ? 56.732 0.470   -67.944 0.00 26.02  ? 260  CYS   B HA   1 
ATOM   15496 H HB2  . CYS   B  1 234 ? 55.702 -0.050  -70.727 0.00 28.96  ? 260  CYS   B HB2  1 
ATOM   15497 H HB3  . CYS   B  1 234 ? 55.003 1.150   -69.616 0.00 28.50  ? 260  CYS   B HB3  1 
ATOM   15498 N N    . PHE   B  1 235 ? 55.110 -2.265  -68.033 1.00 21.34  ? 261  PHE   B N    1 
ATOM   15499 C CA   . PHE   B  1 235 ? 53.955 -2.912  -67.409 1.00 20.57  ? 261  PHE   B CA   1 
ATOM   15500 C C    . PHE   B  1 235 ? 53.875 -2.555  -65.920 1.00 20.18  ? 261  PHE   B C    1 
ATOM   15501 O O    . PHE   B  1 235 ? 54.882 -2.606  -65.223 1.00 20.33  ? 261  PHE   B O    1 
ATOM   15502 C CB   . PHE   B  1 235 ? 53.981 -4.433  -67.602 1.00 20.42  ? 261  PHE   B CB   1 
ATOM   15503 C CG   . PHE   B  1 235 ? 52.831 -5.118  -66.894 1.00 20.62  ? 261  PHE   B CG   1 
ATOM   15504 C CD1  . PHE   B  1 235 ? 51.526 -4.898  -67.292 1.00 21.03  ? 261  PHE   B CD1  1 
ATOM   15505 C CD2  . PHE   B  1 235 ? 53.050 -5.873  -65.757 1.00 21.20  ? 261  PHE   B CD2  1 
ATOM   15506 C CE1  . PHE   B  1 235 ? 50.463 -5.448  -66.584 1.00 21.58  ? 261  PHE   B CE1  1 
ATOM   15507 C CE2  . PHE   B  1 235 ? 51.988 -6.460  -65.074 1.00 21.44  ? 261  PHE   B CE2  1 
ATOM   15508 C CZ   . PHE   B  1 235 ? 50.702 -6.245  -65.496 1.00 21.40  ? 261  PHE   B CZ   1 
ATOM   15509 H H    . PHE   B  1 235 ? 55.795 -2.910  -68.416 0.00 24.87  ? 261  PHE   B H    1 
ATOM   15510 H HA   . PHE   B  1 235 ? 53.059 -2.539  -67.901 0.00 23.93  ? 261  PHE   B HA   1 
ATOM   15511 H HB2  . PHE   B  1 235 ? 53.902 -4.656  -68.665 0.00 24.30  ? 261  PHE   B HB2  1 
ATOM   15512 H HB3  . PHE   B  1 235 ? 54.916 -4.828  -67.205 0.00 23.78  ? 261  PHE   B HB3  1 
ATOM   15513 H HD1  . PHE   B  1 235 ? 51.329 -4.270  -68.145 0.00 25.04  ? 261  PHE   B HD1  1 
ATOM   15514 H HD2  . PHE   B  1 235 ? 54.057 -6.054  -65.419 0.00 24.48  ? 261  PHE   B HD2  1 
ATOM   15515 H HE1  . PHE   B  1 235 ? 49.454 -5.296  -66.927 0.00 25.73  ? 261  PHE   B HE1  1 
ATOM   15516 H HE2  . PHE   B  1 235 ? 52.175 -7.074  -64.210 0.00 24.78  ? 261  PHE   B HE2  1 
ATOM   15517 H HZ   . PHE   B  1 235 ? 49.879 -6.693  -64.965 0.00 25.12  ? 261  PHE   B HZ   1 
ATOM   15518 N N    . ASN   B  1 236 ? 52.707 -2.102  -65.475 1.00 19.86  ? 262  ASN   B N    1 
ATOM   15519 C CA   . ASN   B  1 236 ? 52.474 -1.728  -64.083 1.00 19.26  ? 262  ASN   B CA   1 
ATOM   15520 C C    . ASN   B  1 236 ? 53.402 -0.614  -63.567 1.00 19.81  ? 262  ASN   B C    1 
ATOM   15521 O O    . ASN   B  1 236 ? 53.711 -0.582  -62.373 1.00 19.96  ? 262  ASN   B O    1 
ATOM   15522 C CB   . ASN   B  1 236 ? 52.603 -2.963  -63.189 1.00 19.64  ? 262  ASN   B CB   1 
ATOM   15523 C CG   . ASN   B  1 236 ? 51.962 -2.757  -61.839 1.00 21.24  ? 262  ASN   B CG   1 
ATOM   15524 O OD1  . ASN   B  1 236 ? 50.847 -2.237  -61.757 1.00 21.04  ? 262  ASN   B OD1  1 
ATOM   15525 N ND2  . ASN   B  1 236 ? 52.662 -3.114  -60.773 1.00 22.33  ? 262  ASN   B ND2  1 
ATOM   15526 H H    . ASN   B  1 236 ? 51.886 -1.977  -66.057 0.00 22.54  ? 262  ASN   B H    1 
ATOM   15527 H HA   . ASN   B  1 236 ? 51.455 -1.350  -64.024 0.00 21.19  ? 262  ASN   B HA   1 
ATOM   15528 H HB2  . ASN   B  1 236 ? 52.105 -3.803  -63.672 0.00 21.85  ? 262  ASN   B HB2  1 
ATOM   15529 H HB3  . ASN   B  1 236 ? 53.660 -3.189  -63.055 0.00 21.46  ? 262  ASN   B HB3  1 
ATOM   15530 H HD21 . ASN   B  1 236 ? 52.264 -2.990  -59.848 0.00 23.98  ? 262  ASN   B HD21 1 
ATOM   15531 H HD22 . ASN   B  1 236 ? 53.587 -3.521  -60.870 0.00 24.20  ? 262  ASN   B HD22 1 
ATOM   15532 N N    . ALA   B  1 237 ? 53.848 0.301   -64.451 1.00 20.31  ? 263  ALA   B N    1 
ATOM   15533 C CA   . ALA   B  1 237 ? 54.746 1.367   -64.020 1.00 21.18  ? 263  ALA   B CA   1 
ATOM   15534 C C    . ALA   B  1 237 ? 54.000 2.344   -63.122 1.00 21.13  ? 263  ALA   B C    1 
ATOM   15535 O O    . ALA   B  1 237 ? 52.886 2.743   -63.472 1.00 20.48  ? 263  ALA   B O    1 
ATOM   15536 C CB   . ALA   B  1 237 ? 55.301 2.115   -65.226 1.00 21.62  ? 263  ALA   B CB   1 
ATOM   15537 H H    . ALA   B  1 237 ? 53.610 0.335   -65.436 0.00 22.45  ? 263  ALA   B H    1 
ATOM   15538 H HA   . ALA   B  1 237 ? 55.588 0.916   -63.496 0.00 22.80  ? 263  ALA   B HA   1 
ATOM   15539 H HB1  . ALA   B  1 237 ? 55.970 2.902   -64.878 0.00 23.51  ? 263  ALA   B HB1  1 
ATOM   15540 H HB2  . ALA   B  1 237 ? 55.846 1.414   -65.856 0.00 23.90  ? 263  ALA   B HB2  1 
ATOM   15541 H HB3  . ALA   B  1 237 ? 54.474 2.550   -65.784 0.00 23.87  ? 263  ALA   B HB3  1 
ATOM   15542 N N    . PRO   B  1 238 ? 54.617 2.806   -62.013 1.00 21.90  ? 264  PRO   B N    1 
ATOM   15543 C CA   . PRO   B  1 238 ? 53.949 3.807   -61.161 1.00 22.63  ? 264  PRO   B CA   1 
ATOM   15544 C C    . PRO   B  1 238 ? 54.165 5.259   -61.648 1.00 23.72  ? 264  PRO   B C    1 
ATOM   15545 O O    . PRO   B  1 238 ? 54.086 6.194   -60.851 1.00 24.15  ? 264  PRO   B O    1 
ATOM   15546 C CB   . PRO   B  1 238 ? 54.596 3.554   -59.791 1.00 23.19  ? 264  PRO   B CB   1 
ATOM   15547 C CG   . PRO   B  1 238 ? 55.995 3.148   -60.129 1.00 23.26  ? 264  PRO   B CG   1 
ATOM   15548 C CD   . PRO   B  1 238 ? 55.921 2.407   -61.444 1.00 21.61  ? 264  PRO   B CD   1 
ATOM   15549 H HA   . PRO   B  1 238 ? 52.881 3.617   -61.070 0.00 23.95  ? 264  PRO   B HA   1 
ATOM   15550 H HB2  . PRO   B  1 238 ? 54.589 4.451   -59.174 0.00 24.10  ? 264  PRO   B HB2  1 
ATOM   15551 H HB3  . PRO   B  1 238 ? 54.075 2.740   -59.290 0.00 24.21  ? 264  PRO   B HB3  1 
ATOM   15552 H HG2  . PRO   B  1 238 ? 56.617 4.037   -60.224 0.00 24.32  ? 264  PRO   B HG2  1 
ATOM   15553 H HG3  . PRO   B  1 238 ? 56.381 2.496   -59.347 0.00 24.23  ? 264  PRO   B HG3  1 
ATOM   15554 H HD2  . PRO   B  1 238 ? 56.731 2.719   -62.103 0.00 22.80  ? 264  PRO   B HD2  1 
ATOM   15555 H HD3  . PRO   B  1 238 ? 55.949 1.335   -61.258 0.00 22.73  ? 264  PRO   B HD3  1 
ATOM   15556 N N    . PHE   B  1 239 ? 54.470 5.447   -62.953 1.00 23.75  ? 265  PHE   B N    1 
ATOM   15557 C CA   . PHE   B  1 239 ? 54.685 6.763   -63.564 1.00 24.04  ? 265  PHE   B CA   1 
ATOM   15558 C C    . PHE   B  1 239 ? 54.356 6.670   -65.069 1.00 25.09  ? 265  PHE   B C    1 
ATOM   15559 O O    . PHE   B  1 239 ? 54.298 5.549   -65.599 1.00 24.78  ? 265  PHE   B O    1 
ATOM   15560 C CB   . PHE   B  1 239 ? 56.146 7.237   -63.360 1.00 24.06  ? 265  PHE   B CB   1 
ATOM   15561 C CG   . PHE   B  1 239 ? 57.160 6.222   -63.840 1.00 25.40  ? 265  PHE   B CG   1 
ATOM   15562 C CD1  . PHE   B  1 239 ? 57.564 5.184   -63.021 1.00 27.07  ? 265  PHE   B CD1  1 
ATOM   15563 C CD2  . PHE   B  1 239 ? 57.648 6.264   -65.130 1.00 25.96  ? 265  PHE   B CD2  1 
ATOM   15564 C CE1  . PHE   B  1 239 ? 58.439 4.211   -63.489 1.00 27.58  ? 265  PHE   B CE1  1 
ATOM   15565 C CE2  . PHE   B  1 239 ? 58.535 5.301   -65.583 1.00 27.16  ? 265  PHE   B CE2  1 
ATOM   15566 C CZ   . PHE   B  1 239 ? 58.937 4.293   -64.753 1.00 27.16  ? 265  PHE   B CZ   1 
ATOM   15567 H H    . PHE   B  1 239 ? 54.579 4.691   -63.620 0.00 25.73  ? 265  PHE   B H    1 
ATOM   15568 H HA   . PHE   B  1 239 ? 54.015 7.481   -63.093 0.00 25.98  ? 265  PHE   B HA   1 
ATOM   15569 H HB2  . PHE   B  1 239 ? 56.301 8.158   -63.919 0.00 26.08  ? 265  PHE   B HB2  1 
ATOM   15570 H HB3  . PHE   B  1 239 ? 56.318 7.412   -62.298 0.00 25.69  ? 265  PHE   B HB3  1 
ATOM   15571 H HD1  . PHE   B  1 239 ? 57.174 5.115   -62.019 0.00 29.23  ? 265  PHE   B HD1  1 
ATOM   15572 H HD2  . PHE   B  1 239 ? 57.338 7.054   -65.792 0.00 28.77  ? 265  PHE   B HD2  1 
ATOM   15573 H HE1  . PHE   B  1 239 ? 58.765 3.422   -62.833 0.00 30.07  ? 265  PHE   B HE1  1 
ATOM   15574 H HE2  . PHE   B  1 239 ? 58.923 5.358   -66.588 0.00 30.40  ? 265  PHE   B HE2  1 
ATOM   15575 H HZ   . PHE   B  1 239 ? 59.630 3.549   -65.106 0.00 30.09  ? 265  PHE   B HZ   1 
ATOM   15576 N N    . PRO   B  1 240 ? 54.120 7.795   -65.787 1.00 26.00  ? 266  PRO   B N    1 
ATOM   15577 C CA   . PRO   B  1 240 ? 53.857 7.695   -67.238 1.00 26.90  ? 266  PRO   B CA   1 
ATOM   15578 C C    . PRO   B  1 240 ? 55.088 7.132   -67.944 1.00 28.18  ? 266  PRO   B C    1 
ATOM   15579 O O    . PRO   B  1 240 ? 56.178 7.677   -67.812 1.00 28.71  ? 266  PRO   B O    1 
ATOM   15580 C CB   . PRO   B  1 240 ? 53.564 9.144   -67.648 1.00 27.35  ? 266  PRO   B CB   1 
ATOM   15581 C CG   . PRO   B  1 240 ? 53.207 9.827   -66.390 1.00 27.45  ? 266  PRO   B CG   1 
ATOM   15582 C CD   . PRO   B  1 240 ? 54.108 9.204   -65.355 1.00 25.78  ? 266  PRO   B CD   1 
ATOM   15583 H HA   . PRO   B  1 240 ? 52.981 7.075   -67.427 0.00 30.66  ? 266  PRO   B HA   1 
ATOM   15584 H HB2  . PRO   B  1 240 ? 54.444 9.601   -68.097 0.00 31.31  ? 266  PRO   B HB2  1 
ATOM   15585 H HB3  . PRO   B  1 240 ? 52.724 9.164   -68.341 0.00 31.54  ? 266  PRO   B HB3  1 
ATOM   15586 H HG2  . PRO   B  1 240 ? 53.337 10.903  -66.484 0.00 31.15  ? 266  PRO   B HG2  1 
ATOM   15587 H HG3  . PRO   B  1 240 ? 52.168 9.604   -66.152 0.00 31.10  ? 266  PRO   B HG3  1 
ATOM   15588 H HD2  . PRO   B  1 240 ? 55.108 9.632   -65.411 0.00 28.63  ? 266  PRO   B HD2  1 
ATOM   15589 H HD3  . PRO   B  1 240 ? 53.668 9.330   -64.368 0.00 28.46  ? 266  PRO   B HD3  1 
ATOM   15590 N N    . CYS   B  1 241 ? 54.922 5.995   -68.610 1.00 28.82  ? 267  CYS   B N    1 
ATOM   15591 C CA   . CYS   B  1 241 ? 56.010 5.227   -69.184 1.00 29.47  ? 267  CYS   B CA   1 
ATOM   15592 C C    . CYS   B  1 241 ? 55.785 5.005   -70.680 1.00 30.07  ? 267  CYS   B C    1 
ATOM   15593 O O    . CYS   B  1 241 ? 54.743 4.486   -71.063 1.00 29.37  ? 267  CYS   B O    1 
ATOM   15594 C CB   . CYS   B  1 241 ? 56.101 3.898   -68.432 1.00 30.00  ? 267  CYS   B CB   1 
ATOM   15595 S SG   . CYS   B  1 241 ? 57.600 2.945   -68.780 1.00 31.56  ? 267  CYS   B SG   1 
ATOM   15596 H H    . CYS   B  1 241 ? 54.018 5.565   -68.776 0.00 33.29  ? 267  CYS   B H    1 
ATOM   15597 H HA   . CYS   B  1 241 ? 56.959 5.745   -69.050 0.00 33.94  ? 267  CYS   B HA   1 
ATOM   15598 H HB2  . CYS   B  1 241 ? 56.083 4.101   -67.362 0.00 34.18  ? 267  CYS   B HB2  1 
ATOM   15599 H HB3  . CYS   B  1 241 ? 55.245 3.282   -68.702 0.00 34.69  ? 267  CYS   B HB3  1 
ATOM   15600 N N    . VAL   B  1 242 ? 56.768 5.371   -71.518 1.00 31.08  ? 268  VAL   B N    1 
ATOM   15601 C CA   . VAL   B  1 242 ? 56.687 5.187   -72.970 1.00 32.43  ? 268  VAL   B CA   1 
ATOM   15602 C C    . VAL   B  1 242 ? 57.749 4.160   -73.359 1.00 31.76  ? 268  VAL   B C    1 
ATOM   15603 O O    . VAL   B  1 242 ? 58.934 4.472   -73.280 1.00 31.80  ? 268  VAL   B O    1 
ATOM   15604 C CB   . VAL   B  1 242 ? 56.918 6.516   -73.742 1.00 34.67  ? 268  VAL   B CB   1 
ATOM   15605 C CG1  . VAL   B  1 242 ? 56.858 6.278   -75.256 1.00 35.53  ? 268  VAL   B CG1  1 
ATOM   15606 C CG2  . VAL   B  1 242 ? 55.903 7.581   -73.321 1.00 35.74  ? 268  VAL   B CG2  1 
ATOM   15607 H H    . VAL   B  1 242 ? 57.637 5.803   -71.222 0.00 36.53  ? 268  VAL   B H    1 
ATOM   15608 H HA   . VAL   B  1 242 ? 55.699 4.829   -73.256 0.00 39.02  ? 268  VAL   B HA   1 
ATOM   15609 H HB   . VAL   B  1 242 ? 57.909 6.899   -73.504 0.00 41.58  ? 268  VAL   B HB   1 
ATOM   15610 H HG11 . VAL   B  1 242 ? 56.683 7.228   -75.760 0.00 43.54  ? 268  VAL   B HG11 1 
ATOM   15611 H HG12 . VAL   B  1 242 ? 57.808 5.868   -75.591 0.00 43.42  ? 268  VAL   B HG12 1 
ATOM   15612 H HG13 . VAL   B  1 242 ? 56.051 5.582   -75.479 0.00 43.53  ? 268  VAL   B HG13 1 
ATOM   15613 H HG21 . VAL   B  1 242 ? 56.071 8.485   -73.904 0.00 43.15  ? 268  VAL   B HG21 1 
ATOM   15614 H HG22 . VAL   B  1 242 ? 54.898 7.204   -73.507 0.00 43.12  ? 268  VAL   B HG22 1 
ATOM   15615 H HG23 . VAL   B  1 242 ? 56.026 7.801   -72.261 0.00 42.56  ? 268  VAL   B HG23 1 
ATOM   15616 N N    . PRO   B  1 243 ? 57.373 2.942   -73.771 1.00 31.29  ? 269  PRO   B N    1 
ATOM   15617 C CA   . PRO   B  1 243 ? 58.403 1.967   -74.160 1.00 31.01  ? 269  PRO   B CA   1 
ATOM   15618 C C    . PRO   B  1 243 ? 58.981 2.254   -75.537 1.00 31.01  ? 269  PRO   B C    1 
ATOM   15619 O O    . PRO   B  1 243 ? 58.363 2.952   -76.354 1.00 30.69  ? 269  PRO   B O    1 
ATOM   15620 C CB   . PRO   B  1 243 ? 57.647 0.639   -74.194 1.00 31.74  ? 269  PRO   B CB   1 
ATOM   15621 C CG   . PRO   B  1 243 ? 56.230 0.998   -74.448 1.00 32.59  ? 269  PRO   B CG   1 
ATOM   15622 C CD   . PRO   B  1 243 ? 56.010 2.404   -73.954 1.00 31.05  ? 269  PRO   B CD   1 
ATOM   15623 H HA   . PRO   B  1 243 ? 59.198 1.907   -73.418 0.00 37.39  ? 269  PRO   B HA   1 
ATOM   15624 H HB2  . PRO   B  1 243 ? 58.030 0.039   -75.018 0.00 39.12  ? 269  PRO   B HB2  1 
ATOM   15625 H HB3  . PRO   B  1 243 ? 57.756 0.121   -73.242 0.00 38.45  ? 269  PRO   B HB3  1 
ATOM   15626 H HG2  . PRO   B  1 243 ? 56.036 0.938   -75.519 0.00 40.38  ? 269  PRO   B HG2  1 
ATOM   15627 H HG3  . PRO   B  1 243 ? 55.587 0.307   -73.905 0.00 39.86  ? 269  PRO   B HG3  1 
ATOM   15628 H HD2  . PRO   B  1 243 ? 55.475 2.986   -74.703 0.00 38.06  ? 269  PRO   B HD2  1 
ATOM   15629 H HD3  . PRO   B  1 243 ? 55.478 2.395   -73.003 0.00 37.47  ? 269  PRO   B HD3  1 
ATOM   15630 N N    . CYS   B  1 244 ? 60.132 1.648   -75.830 1.00 30.88  ? 270  CYS   B N    1 
ATOM   15631 C CA   . CYS   B  1 244 ? 60.697 1.714   -77.177 1.00 31.44  ? 270  CYS   B CA   1 
ATOM   15632 C C    . CYS   B  1 244 ? 59.772 0.897   -78.108 1.00 32.86  ? 270  CYS   B C    1 
ATOM   15633 O O    . CYS   B  1 244 ? 59.009 0.059   -77.623 1.00 32.80  ? 270  CYS   B O    1 
ATOM   15634 C CB   . CYS   B  1 244 ? 62.136 1.206   -77.193 1.00 30.40  ? 270  CYS   B CB   1 
ATOM   15635 S SG   . CYS   B  1 244 ? 63.333 2.433   -76.611 1.00 31.01  ? 270  CYS   B SG   1 
ATOM   15636 H H    . CYS   B  1 244 ? 60.684 1.122   -75.159 0.00 37.93  ? 270  CYS   B H    1 
ATOM   15637 H HA   . CYS   B  1 244 ? 60.704 2.746   -77.522 0.00 39.36  ? 270  CYS   B HA   1 
ATOM   15638 H HB2  . CYS   B  1 244 ? 62.222 0.316   -76.572 0.00 37.98  ? 270  CYS   B HB2  1 
ATOM   15639 H HB3  . CYS   B  1 244 ? 62.399 0.957   -78.220 0.00 38.56  ? 270  CYS   B HB3  1 
ATOM   15640 N N    . ASP   B  1 245 ? 59.758 1.185   -79.418 1.00 34.16  ? 271  ASP   B N    1 
ATOM   15641 C CA   . ASP   B  1 245 ? 58.828 0.516   -80.344 1.00 36.05  ? 271  ASP   B CA   1 
ATOM   15642 C C    . ASP   B  1 245 ? 58.837 -1.020  -80.217 1.00 36.48  ? 271  ASP   B C    1 
ATOM   15643 O O    . ASP   B  1 245 ? 59.902 -1.620  -80.193 1.00 36.28  ? 271  ASP   B O    1 
ATOM   15644 C CB   . ASP   B  1 245 ? 59.082 0.972   -81.795 1.00 39.60  ? 271  ASP   B CB   1 
ATOM   15645 C CG   . ASP   B  1 245 ? 58.710 2.428   -82.070 1.00 46.97  ? 271  ASP   B CG   1 
ATOM   15646 O OD1  . ASP   B  1 245 ? 58.156 3.090   -81.154 1.00 48.65  ? 271  ASP   B OD1  1 
ATOM   15647 O OD2  . ASP   B  1 245 ? 58.978 2.906   -83.195 1.00 50.07  ? 271  ASP   B OD2  1 
ATOM   15648 H H    . ASP   B  1 245 ? 60.373 1.863   -79.855 0.00 43.71  ? 271  ASP   B H    1 
ATOM   15649 H HA   . ASP   B  1 245 ? 57.824 0.841   -80.075 0.00 46.36  ? 271  ASP   B HA   1 
ATOM   15650 H HB2  . ASP   B  1 245 ? 60.142 0.866   -82.018 0.00 51.36  ? 271  ASP   B HB2  1 
ATOM   15651 H HB3  . ASP   B  1 245 ? 58.495 0.348   -82.467 0.00 51.75  ? 271  ASP   B HB3  1 
ATOM   15652 N N    . GLY   B  1 246 ? 57.659 -1.605  -80.001 1.00 37.04  ? 272  GLY   B N    1 
ATOM   15653 C CA   . GLY   B  1 246 ? 57.509 -3.040  -79.776 1.00 37.75  ? 272  GLY   B CA   1 
ATOM   15654 C C    . GLY   B  1 246 ? 58.046 -3.523  -78.433 1.00 37.75  ? 272  GLY   B C    1 
ATOM   15655 O O    . GLY   B  1 246 ? 58.341 -4.710  -78.272 1.00 38.44  ? 272  GLY   B O    1 
ATOM   15656 H H    . GLY   B  1 246 ? 56.773 -1.110  -79.974 0.00 47.85  ? 272  GLY   B H    1 
ATOM   15657 H HA2  . GLY   B  1 246 ? 56.454 -3.302  -79.833 0.00 49.03  ? 272  GLY   B HA2  1 
ATOM   15658 H HA3  . GLY   B  1 246 ? 58.037 -3.580  -80.561 0.00 49.32  ? 272  GLY   B HA3  1 
ATOM   15659 N N    . GLY   B  1 247 ? 58.169 -2.621  -77.460 1.00 36.55  ? 273  GLY   B N    1 
ATOM   15660 C CA   . GLY   B  1 247 ? 58.765 -2.945  -76.165 1.00 35.74  ? 273  GLY   B CA   1 
ATOM   15661 C C    . GLY   B  1 247 ? 60.218 -3.388  -76.287 1.00 34.56  ? 273  GLY   B C    1 
ATOM   15662 O O    . GLY   B  1 247 ? 60.704 -4.147  -75.445 1.00 34.22  ? 273  GLY   B O    1 
ATOM   15663 H H    . GLY   B  1 247 ? 57.855 -1.657  -77.518 0.00 46.17  ? 273  GLY   B H    1 
ATOM   15664 H HA2  . GLY   B  1 247 ? 58.727 -2.079  -75.508 0.00 44.40  ? 273  GLY   B HA2  1 
ATOM   15665 H HA3  . GLY   B  1 247 ? 58.199 -3.752  -75.702 0.00 44.80  ? 273  GLY   B HA3  1 
ATOM   15666 N N    . ALA   B  1 248 ? 60.918 -2.933  -77.353 1.00 33.61  ? 274  ALA   B N    1 
ATOM   15667 C CA   . ALA   B  1 248 ? 62.292 -3.328  -77.662 1.00 32.60  ? 274  ALA   B CA   1 
ATOM   15668 C C    . ALA   B  1 248 ? 63.295 -2.943  -76.573 1.00 31.04  ? 274  ALA   B C    1 
ATOM   15669 O O    . ALA   B  1 248 ? 63.095 -1.990  -75.837 1.00 29.92  ? 274  ALA   B O    1 
ATOM   15670 C CB   . ALA   B  1 248 ? 62.730 -2.723  -78.999 1.00 32.65  ? 274  ALA   B CB   1 
ATOM   15671 H H    . ALA   B  1 248 ? 60.551 -2.260  -78.019 0.00 42.85  ? 274  ALA   B H    1 
ATOM   15672 H HA   . ALA   B  1 248 ? 62.312 -4.411  -77.774 0.00 41.93  ? 274  ALA   B HA   1 
ATOM   15673 H HB1  . ALA   B  1 248 ? 63.754 -3.027  -79.211 0.00 42.32  ? 274  ALA   B HB1  1 
ATOM   15674 H HB2  . ALA   B  1 248 ? 62.068 -3.083  -79.785 0.00 42.58  ? 274  ALA   B HB2  1 
ATOM   15675 H HB3  . ALA   B  1 248 ? 62.677 -1.637  -78.929 0.00 41.94  ? 274  ALA   B HB3  1 
ATOM   15676 N N    . SER   B  1 249 ? 64.392 -3.695  -76.525 1.00 30.35  ? 275  SER   B N    1 
ATOM   15677 C CA   . SER   B  1 249 ? 65.514 -3.471  -75.627 1.00 30.67  ? 275  SER   B CA   1 
ATOM   15678 C C    . SER   B  1 249 ? 66.312 -2.249  -76.054 1.00 30.10  ? 275  SER   B C    1 
ATOM   15679 O O    . SER   B  1 249 ? 66.296 -1.870  -77.233 1.00 29.97  ? 275  SER   B O    1 
ATOM   15680 C CB   . SER   B  1 249 ? 66.443 -4.681  -75.691 1.00 32.48  ? 275  SER   B CB   1 
ATOM   15681 O OG   . SER   B  1 249 ? 67.569 -4.556  -74.846 1.00 35.22  ? 275  SER   B OG   1 
ATOM   15682 H H    . SER   B  1 249 ? 64.510 -4.481  -77.157 0.00 39.02  ? 275  SER   B H    1 
ATOM   15683 H HA   . SER   B  1 249 ? 65.181 -3.349  -74.600 0.00 38.21  ? 275  SER   B HA   1 
ATOM   15684 H HB2  . SER   B  1 249 ? 65.880 -5.562  -75.386 0.00 41.18  ? 275  SER   B HB2  1 
ATOM   15685 H HB3  . SER   B  1 249 ? 66.779 -4.810  -76.719 0.00 41.58  ? 275  SER   B HB3  1 
ATOM   15686 H HG   . SER   B  1 249 ? 68.346 -4.167  -75.327 0.00 44.34  ? 275  SER   B HG   1 
ATOM   15687 N N    . ILE   B  1 250 ? 67.118 -1.685  -75.126 1.00 29.36  ? 276  ILE   B N    1 
ATOM   15688 C CA   . ILE   B  1 250 ? 68.113 -0.665  -75.479 1.00 29.05  ? 276  ILE   B CA   1 
ATOM   15689 C C    . ILE   B  1 250 ? 69.153 -1.409  -76.351 1.00 29.11  ? 276  ILE   B C    1 
ATOM   15690 O O    . ILE   B  1 250 ? 69.421 -2.596  -76.107 1.00 28.98  ? 276  ILE   B O    1 
ATOM   15691 C CB   . ILE   B  1 250 ? 68.804 -0.056  -74.229 1.00 29.00  ? 276  ILE   B CB   1 
ATOM   15692 C CG1  . ILE   B  1 250 ? 69.624 1.198   -74.605 1.00 29.72  ? 276  ILE   B CG1  1 
ATOM   15693 C CG2  . ILE   B  1 250 ? 69.694 -1.099  -73.510 1.00 29.38  ? 276  ILE   B CG2  1 
ATOM   15694 C CD1  . ILE   B  1 250 ? 70.228 1.948   -73.391 1.00 30.29  ? 276  ILE   B CD1  1 
ATOM   15695 H H    . ILE   B  1 250 ? 67.088 -1.913  -74.138 0.00 36.35  ? 276  ILE   B H    1 
ATOM   15696 H HA   . ILE   B  1 250 ? 67.653 0.132   -76.061 0.00 36.39  ? 276  ILE   B HA   1 
ATOM   15697 H HB   . ILE   B  1 250 ? 68.017 0.263   -73.547 0.00 35.46  ? 276  ILE   B HB   1 
ATOM   15698 H HG12 . ILE   B  1 250 ? 70.452 0.903   -75.248 0.00 37.06  ? 276  ILE   B HG12 1 
ATOM   15699 H HG13 . ILE   B  1 250 ? 68.978 1.896   -75.134 0.00 36.75  ? 276  ILE   B HG13 1 
ATOM   15700 H HG21 . ILE   B  1 250 ? 70.106 -0.665  -72.600 0.00 35.96  ? 276  ILE   B HG21 1 
ATOM   15701 H HG22 . ILE   B  1 250 ? 69.083 -1.964  -73.257 0.00 36.27  ? 276  ILE   B HG22 1 
ATOM   15702 H HG23 . ILE   B  1 250 ? 70.519 -1.407  -74.150 0.00 36.63  ? 276  ILE   B HG23 1 
ATOM   15703 H HD11 . ILE   B  1 250 ? 70.518 2.951   -73.698 0.00 37.01  ? 276  ILE   B HD11 1 
ATOM   15704 H HD12 . ILE   B  1 250 ? 69.483 1.992   -72.597 0.00 36.64  ? 276  ILE   B HD12 1 
ATOM   15705 H HD13 . ILE   B  1 250 ? 71.104 1.403   -73.045 0.00 37.04  ? 276  ILE   B HD13 1 
ATOM   15706 N N    . ASN   B  1 251 ? 69.674 -0.753  -77.374 1.00 28.93  ? 277  ASN   B N    1 
ATOM   15707 C CA   . ASN   B  1 251 ? 70.625 -1.385  -78.289 1.00 28.97  ? 277  ASN   B CA   1 
ATOM   15708 C C    . ASN   B  1 251 ? 72.011 -0.874  -77.950 1.00 28.39  ? 277  ASN   B C    1 
ATOM   15709 O O    . ASN   B  1 251 ? 72.326 0.244   -78.296 1.00 28.51  ? 277  ASN   B O    1 
ATOM   15710 C CB   . ASN   B  1 251 ? 70.241 -1.051  -79.731 1.00 30.18  ? 277  ASN   B CB   1 
ATOM   15711 C CG   . ASN   B  1 251 ? 71.109 -1.716  -80.765 1.00 34.48  ? 277  ASN   B CG   1 
ATOM   15712 O OD1  . ASN   B  1 251 ? 72.154 -2.303  -80.461 1.00 35.75  ? 277  ASN   B OD1  1 
ATOM   15713 N ND2  . ASN   B  1 251 ? 70.685 -1.639  -82.021 1.00 35.52  ? 277  ASN   B ND2  1 
ATOM   15714 H H    . ASN   B  1 251 ? 69.460 0.212   -77.605 0.00 36.97  ? 277  ASN   B H    1 
ATOM   15715 H HA   . ASN   B  1 251 ? 70.617 -2.469  -78.193 0.00 37.80  ? 277  ASN   B HA   1 
ATOM   15716 H HB2  . ASN   B  1 251 ? 69.219 -1.386  -79.901 0.00 39.61  ? 277  ASN   B HB2  1 
ATOM   15717 H HB3  . ASN   B  1 251 ? 70.296 0.026   -79.886 0.00 39.47  ? 277  ASN   B HB3  1 
ATOM   15718 H HD21 . ASN   B  1 251 ? 71.223 -2.069  -82.766 0.00 47.56  ? 277  ASN   B HD21 1 
ATOM   15719 H HD22 . ASN   B  1 251 ? 69.819 -1.154  -82.232 0.00 47.04  ? 277  ASN   B HD22 1 
ATOM   15720 N N    . ILE   B  1 252 ? 72.819 -1.664  -77.237 1.00 28.32  ? 278  ILE   B N    1 
ATOM   15721 C CA   . ILE   B  1 252 ? 74.166 -1.246  -76.853 1.00 28.84  ? 278  ILE   B CA   1 
ATOM   15722 C C    . ILE   B  1 252 ? 75.178 -1.969  -77.729 1.00 29.64  ? 278  ILE   B C    1 
ATOM   15723 O O    . ILE   B  1 252 ? 75.250 -3.194  -77.691 1.00 30.32  ? 278  ILE   B O    1 
ATOM   15724 C CB   . ILE   B  1 252 ? 74.457 -1.479  -75.340 1.00 28.99  ? 278  ILE   B CB   1 
ATOM   15725 C CG1  . ILE   B  1 252 ? 73.525 -0.645  -74.456 1.00 29.89  ? 278  ILE   B CG1  1 
ATOM   15726 C CG2  . ILE   B  1 252 ? 75.926 -1.150  -75.025 1.00 29.13  ? 278  ILE   B CG2  1 
ATOM   15727 C CD1  . ILE   B  1 252 ? 73.377 -1.182  -72.986 1.00 30.74  ? 278  ILE   B CD1  1 
ATOM   15728 H H    . ILE   B  1 252 ? 72.570 -2.590  -76.905 0.00 36.81  ? 278  ILE   B H    1 
ATOM   15729 H HA   . ILE   B  1 252 ? 74.275 -0.183  -77.045 0.00 37.32  ? 278  ILE   B HA   1 
ATOM   15730 H HB   . ILE   B  1 252 ? 74.288 -2.532  -75.121 0.00 37.25  ? 278  ILE   B HB   1 
ATOM   15731 H HG12 . ILE   B  1 252 ? 73.933 0.362   -74.391 0.00 37.56  ? 278  ILE   B HG12 1 
ATOM   15732 H HG13 . ILE   B  1 252 ? 72.534 -0.603  -74.903 0.00 37.64  ? 278  ILE   B HG13 1 
ATOM   15733 H HG21 . ILE   B  1 252 ? 76.033 -0.933  -73.964 0.00 37.10  ? 278  ILE   B HG21 1 
ATOM   15734 H HG22 . ILE   B  1 252 ? 76.550 -2.006  -75.279 0.00 37.81  ? 278  ILE   B HG22 1 
ATOM   15735 H HG23 . ILE   B  1 252 ? 76.232 -0.283  -75.610 0.00 37.54  ? 278  ILE   B HG23 1 
ATOM   15736 H HD11 . ILE   B  1 252 ? 72.554 -0.656  -72.505 0.00 37.91  ? 278  ILE   B HD11 1 
ATOM   15737 H HD12 . ILE   B  1 252 ? 73.169 -2.250  -73.021 0.00 38.42  ? 278  ILE   B HD12 1 
ATOM   15738 H HD13 . ILE   B  1 252 ? 74.299 -0.999  -72.438 0.00 38.24  ? 278  ILE   B HD13 1 
ATOM   15739 N N    . ASP   B  1 253 ? 75.989 -1.220  -78.489 1.00 29.40  ? 279  ASP   B N    1 
ATOM   15740 C CA   . ASP   B  1 253 ? 77.003 -1.813  -79.353 1.00 30.13  ? 279  ASP   B CA   1 
ATOM   15741 C C    . ASP   B  1 253 ? 77.995 -2.653  -78.532 1.00 30.41  ? 279  ASP   B C    1 
ATOM   15742 O O    . ASP   B  1 253 ? 78.316 -2.303  -77.394 1.00 29.61  ? 279  ASP   B O    1 
ATOM   15743 C CB   . ASP   B  1 253 ? 77.761 -0.719  -80.122 1.00 32.33  ? 279  ASP   B CB   1 
ATOM   15744 C CG   . ASP   B  1 253 ? 78.736 -1.282  -81.137 1.00 38.17  ? 279  ASP   B CG   1 
ATOM   15745 O OD1  . ASP   B  1 253 ? 78.289 -1.661  -82.229 1.00 39.57  ? 279  ASP   B OD1  1 
ATOM   15746 O OD2  . ASP   B  1 253 ? 79.948 -1.374  -80.817 1.00 39.87  ? 279  ASP   B OD2  1 
ATOM   15747 H H    . ASP   B  1 253 ? 75.966 -0.206  -78.532 0.00 38.84  ? 279  ASP   B H    1 
ATOM   15748 H HA   . ASP   B  1 253 ? 76.512 -2.458  -80.080 0.00 40.80  ? 279  ASP   B HA   1 
ATOM   15749 H HB2  . ASP   B  1 253 ? 77.040 -0.102  -80.656 0.00 43.35  ? 279  ASP   B HB2  1 
ATOM   15750 H HB3  . ASP   B  1 253 ? 78.321 -0.110  -79.414 0.00 43.13  ? 279  ASP   B HB3  1 
ATOM   15751 N N    . ARG   B  1 254 ? 78.426 -3.783  -79.096 1.00 31.22  ? 280  ARG   B N    1 
ATOM   15752 C CA   . ARG   B  1 254 ? 79.388 -4.714  -78.495 1.00 32.81  ? 280  ARG   B CA   1 
ATOM   15753 C C    . ARG   B  1 254 ? 80.623 -3.995  -77.887 1.00 33.05  ? 280  ARG   B C    1 
ATOM   15754 O O    . ARG   B  1 254 ? 81.086 -4.393  -76.813 1.00 33.06  ? 280  ARG   B O    1 
ATOM   15755 C CB   . ARG   B  1 254 ? 79.777 -5.796  -79.550 1.00 35.97  ? 280  ARG   B CB   1 
ATOM   15756 C CG   . ARG   B  1 254 ? 81.208 -6.353  -79.556 1.00 42.64  ? 280  ARG   B CG   1 
ATOM   15757 C CD   . ARG   B  1 254 ? 81.408 -7.323  -78.425 1.00 48.64  ? 280  ARG   B CD   1 
ATOM   15758 N NE   . ARG   B  1 254 ? 82.786 -7.826  -78.347 1.00 54.06  ? 280  ARG   B NE   1 
ATOM   15759 C CZ   . ARG   B  1 254 ? 83.804 -7.207  -77.744 1.00 56.65  ? 280  ARG   B CZ   1 
ATOM   15760 N NH1  . ARG   B  1 254 ? 83.627 -6.019  -77.165 1.00 57.02  ? 280  ARG   B NH1  1 
ATOM   15761 N NH2  . ARG   B  1 254 ? 85.008 -7.765  -77.722 1.00 55.90  ? 280  ARG   B NH2  1 
ATOM   15762 H H    . ARG   B  1 254 ? 78.089 -4.085  -80.005 0.00 42.74  ? 280  ARG   B H    1 
ATOM   15763 H HA   . ARG   B  1 254 ? 78.884 -5.227  -77.679 0.00 44.24  ? 280  ARG   B HA   1 
ATOM   15764 H HB2  . ARG   B  1 254 ? 79.110 -6.646  -79.407 0.00 49.08  ? 280  ARG   B HB2  1 
ATOM   15765 H HB3  . ARG   B  1 254 ? 79.607 -5.391  -80.546 0.00 49.30  ? 280  ARG   B HB3  1 
ATOM   15766 H HG2  . ARG   B  1 254 ? 81.359 -6.905  -80.482 0.00 58.11  ? 280  ARG   B HG2  1 
ATOM   15767 H HG3  . ARG   B  1 254 ? 81.950 -5.559  -79.488 0.00 57.54  ? 280  ARG   B HG3  1 
ATOM   15768 H HD2  . ARG   B  1 254 ? 81.122 -6.863  -77.481 0.00 64.12  ? 280  ARG   B HD2  1 
ATOM   15769 H HD3  . ARG   B  1 254 ? 80.767 -8.184  -78.605 0.00 64.79  ? 280  ARG   B HD3  1 
ATOM   15770 H HE   . ARG   B  1 254 ? 82.966 -8.733  -78.764 0.00 72.12  ? 280  ARG   B HE   1 
ATOM   15771 H HH11 . ARG   B  1 254 ? 82.732 -5.540  -77.164 0.00 74.18  ? 280  ARG   B HH11 1 
ATOM   15772 H HH12 . ARG   B  1 254 ? 84.416 -5.557  -76.725 0.00 74.55  ? 280  ARG   B HH12 1 
ATOM   15773 H HH21 . ARG   B  1 254 ? 85.161 -8.671  -78.156 0.00 74.78  ? 280  ARG   B HH21 1 
ATOM   15774 H HH22 . ARG   B  1 254 ? 85.785 -7.291  -77.273 0.00 74.28  ? 280  ARG   B HH22 1 
ATOM   15775 N N    . PHE   B  1 255 ? 81.098 -2.908  -78.534 1.00 32.67  ? 281  PHE   B N    1 
ATOM   15776 C CA   . PHE   B  1 255 ? 82.277 -2.151  -78.098 1.00 33.05  ? 281  PHE   B CA   1 
ATOM   15777 C C    . PHE   B  1 255 ? 81.989 -0.832  -77.358 1.00 31.45  ? 281  PHE   B C    1 
ATOM   15778 O O    . PHE   B  1 255 ? 82.929 -0.094  -77.093 1.00 30.94  ? 281  PHE   B O    1 
ATOM   15779 C CB   . PHE   B  1 255 ? 83.145 -1.839  -79.331 1.00 34.27  ? 281  PHE   B CB   1 
ATOM   15780 C CG   . PHE   B  1 255 ? 83.683 -3.051  -80.035 1.00 36.77  ? 281  PHE   B CG   1 
ATOM   15781 C CD1  . PHE   B  1 255 ? 84.486 -3.956  -79.370 1.00 38.47  ? 281  PHE   B CD1  1 
ATOM   15782 C CD2  . PHE   B  1 255 ? 83.457 -3.245  -81.382 1.00 38.05  ? 281  PHE   B CD2  1 
ATOM   15783 C CE1  . PHE   B  1 255 ? 85.041 -5.034  -80.041 1.00 39.21  ? 281  PHE   B CE1  1 
ATOM   15784 C CE2  . PHE   B  1 255 ? 84.023 -4.318  -82.042 1.00 39.19  ? 281  PHE   B CE2  1 
ATOM   15785 C CZ   . PHE   B  1 255 ? 84.764 -5.228  -81.354 1.00 39.04  ? 281  PHE   B CZ   1 
ATOM   15786 H H    . PHE   B  1 255 ? 80.681 -2.530  -79.379 0.00 44.51  ? 281  PHE   B H    1 
ATOM   15787 H HA   . PHE   B  1 255 ? 82.878 -2.763  -77.428 0.00 44.91  ? 281  PHE   B HA   1 
ATOM   15788 H HB2  . PHE   B  1 255 ? 82.528 -1.302  -80.049 0.00 46.92  ? 281  PHE   B HB2  1 
ATOM   15789 H HB3  . PHE   B  1 255 ? 84.001 -1.230  -79.045 0.00 46.95  ? 281  PHE   B HB3  1 
ATOM   15790 H HD1  . PHE   B  1 255 ? 84.695 -3.814  -78.327 0.00 52.45  ? 281  PHE   B HD1  1 
ATOM   15791 H HD2  . PHE   B  1 255 ? 82.847 -2.550  -81.936 0.00 52.52  ? 281  PHE   B HD2  1 
ATOM   15792 H HE1  . PHE   B  1 255 ? 85.637 -5.752  -79.507 0.00 54.50  ? 281  PHE   B HE1  1 
ATOM   15793 H HE2  . PHE   B  1 255 ? 83.808 -4.487  -83.084 0.00 55.05  ? 281  PHE   B HE2  1 
ATOM   15794 H HZ   . PHE   B  1 255 ? 85.197 -6.056  -81.872 0.00 55.16  ? 281  PHE   B HZ   1 
ATOM   15795 N N    . ALA   B  1 256 ? 80.727 -0.531  -77.010 1.00 30.71  ? 282  ALA   B N    1 
ATOM   15796 C CA   . ALA   B  1 256 ? 80.374 0.722   -76.326 1.00 30.73  ? 282  ALA   B CA   1 
ATOM   15797 C C    . ALA   B  1 256 ? 81.129 1.013   -75.026 1.00 29.73  ? 282  ALA   B C    1 
ATOM   15798 O O    . ALA   B  1 256 ? 81.311 2.183   -74.691 1.00 29.55  ? 282  ALA   B O    1 
ATOM   15799 C CB   . ALA   B  1 256 ? 78.880 0.761   -76.048 1.00 31.30  ? 282  ALA   B CB   1 
ATOM   15800 H H    . ALA   B  1 256 ? 79.924 -1.125  -77.190 0.00 40.93  ? 282  ALA   B H    1 
ATOM   15801 H HA   . ALA   B  1 256 ? 80.592 1.554   -76.993 0.00 40.63  ? 282  ALA   B HA   1 
ATOM   15802 H HB1  . ALA   B  1 256 ? 78.687 1.589   -75.367 0.00 40.33  ? 282  ALA   B HB1  1 
ATOM   15803 H HB2  . ALA   B  1 256 ? 78.348 0.913   -76.986 0.00 40.87  ? 282  ALA   B HB2  1 
ATOM   15804 H HB3  . ALA   B  1 256 ? 78.570 -0.173  -75.584 0.00 40.63  ? 282  ALA   B HB3  1 
ATOM   15805 N N    . PHE   B  1 257 ? 81.493 -0.014  -74.258 1.00 29.50  ? 283  PHE   B N    1 
ATOM   15806 C CA   . PHE   B  1 257 ? 82.184 0.198   -72.980 1.00 29.72  ? 283  PHE   B CA   1 
ATOM   15807 C C    . PHE   B  1 257 ? 83.624 -0.347  -73.004 1.00 30.48  ? 283  PHE   B C    1 
ATOM   15808 O O    . PHE   B  1 257 ? 84.205 -0.556  -71.937 1.00 30.18  ? 283  PHE   B O    1 
ATOM   15809 C CB   . PHE   B  1 257 ? 81.390 -0.483  -71.854 1.00 29.73  ? 283  PHE   B CB   1 
ATOM   15810 C CG   . PHE   B  1 257 ? 79.894 -0.232  -71.824 1.00 30.13  ? 283  PHE   B CG   1 
ATOM   15811 C CD1  . PHE   B  1 257 ? 79.379 1.032   -72.055 1.00 31.09  ? 283  PHE   B CD1  1 
ATOM   15812 C CD2  . PHE   B  1 257 ? 79.019 -1.232  -71.448 1.00 30.62  ? 283  PHE   B CD2  1 
ATOM   15813 C CE1  . PHE   B  1 257 ? 78.010 1.270   -71.968 1.00 31.89  ? 283  PHE   B CE1  1 
ATOM   15814 C CE2  . PHE   B  1 257 ? 77.658 -0.989  -71.346 1.00 31.39  ? 283  PHE   B CE2  1 
ATOM   15815 C CZ   . PHE   B  1 257 ? 77.159 0.259   -71.614 1.00 31.48  ? 283  PHE   B CZ   1 
ATOM   15816 H H    . PHE   B  1 257 ? 81.327 -0.991  -74.476 0.00 38.94  ? 283  PHE   B H    1 
ATOM   15817 H HA   . PHE   B  1 257 ? 82.244 1.257   -72.737 0.00 38.64  ? 283  PHE   B HA   1 
ATOM   15818 H HB2  . PHE   B  1 257 ? 81.542 -1.558  -71.937 0.00 38.66  ? 283  PHE   B HB2  1 
ATOM   15819 H HB3  . PHE   B  1 257 ? 81.787 -0.135  -70.903 0.00 38.24  ? 283  PHE   B HB3  1 
ATOM   15820 H HD1  . PHE   B  1 257 ? 80.035 1.841   -72.327 0.00 39.50  ? 283  PHE   B HD1  1 
ATOM   15821 H HD2  . PHE   B  1 257 ? 79.407 -2.205  -71.220 0.00 39.08  ? 283  PHE   B HD2  1 
ATOM   15822 H HE1  . PHE   B  1 257 ? 77.621 2.251   -72.180 0.00 39.78  ? 283  PHE   B HE1  1 
ATOM   15823 H HE2  . PHE   B  1 257 ? 76.987 -1.789  -71.081 0.00 39.30  ? 283  PHE   B HE2  1 
ATOM   15824 H HZ   . PHE   B  1 257 ? 76.099 0.441   -71.557 0.00 39.01  ? 283  PHE   B HZ   1 
ATOM   15825 N N    . GLN   B  1 258 ? 84.223 -0.541  -74.205 1.00 30.96  ? 284  GLN   B N    1 
ATOM   15826 C CA   . GLN   B  1 258 ? 85.559 -1.125  -74.318 1.00 32.32  ? 284  GLN   B CA   1 
ATOM   15827 C C    . GLN   B  1 258 ? 86.666 -0.303  -73.656 1.00 32.89  ? 284  GLN   B C    1 
ATOM   15828 O O    . GLN   B  1 258 ? 87.678 -0.880  -73.255 1.00 33.65  ? 284  GLN   B O    1 
ATOM   15829 C CB   . GLN   B  1 258 ? 85.917 -1.421  -75.789 1.00 34.59  ? 284  GLN   B CB   1 
ATOM   15830 C CG   . GLN   B  1 258 ? 86.259 -0.188  -76.616 1.00 39.37  ? 284  GLN   B CG   1 
ATOM   15831 C CD   . GLN   B  1 258 ? 86.501 -0.520  -78.071 1.00 44.40  ? 284  GLN   B CD   1 
ATOM   15832 O OE1  . GLN   B  1 258 ? 86.870 -1.649  -78.426 1.00 45.49  ? 284  GLN   B OE1  1 
ATOM   15833 N NE2  . GLN   B  1 258 ? 86.307 0.465   -78.942 1.00 45.45  ? 284  GLN   B NE2  1 
ATOM   15834 H H    . GLN   B  1 258 ? 83.822 -0.288  -75.103 0.00 41.49  ? 284  GLN   B H    1 
ATOM   15835 H HA   . GLN   B  1 258 ? 85.528 -2.084  -73.804 0.00 43.60  ? 284  GLN   B HA   1 
ATOM   15836 H HB2  . GLN   B  1 258 ? 86.784 -2.080  -75.806 0.00 47.33  ? 284  GLN   B HB2  1 
ATOM   15837 H HB3  . GLN   B  1 258 ? 85.072 -1.917  -76.264 0.00 46.87  ? 284  GLN   B HB3  1 
ATOM   15838 H HG2  . GLN   B  1 258 ? 85.431 0.517   -76.552 0.00 52.39  ? 284  GLN   B HG2  1 
ATOM   15839 H HG3  . GLN   B  1 258 ? 87.176 0.268   -76.247 0.00 52.92  ? 284  GLN   B HG3  1 
ATOM   15840 H HE21 . GLN   B  1 258 ? 86.022 1.385   -78.622 0.00 60.40  ? 284  GLN   B HE21 1 
ATOM   15841 H HE22 . GLN   B  1 258 ? 86.453 0.301   -79.933 0.00 61.15  ? 284  GLN   B HE22 1 
ATOM   15842 N N    . ASN   B  1 259 ? 86.509 1.028   -73.580 1.00 32.56  ? 285  ASN   B N    1 
ATOM   15843 C CA   . ASN   B  1 259 ? 87.509 1.907   -72.959 1.00 33.39  ? 285  ASN   B CA   1 
ATOM   15844 C C    . ASN   B  1 259 ? 87.091 2.395   -71.565 1.00 32.15  ? 285  ASN   B C    1 
ATOM   15845 O O    . ASN   B  1 259 ? 87.784 3.243   -71.018 1.00 32.12  ? 285  ASN   B O    1 
ATOM   15846 C CB   . ASN   B  1 259 ? 87.768 3.122   -73.845 1.00 36.45  ? 285  ASN   B CB   1 
ATOM   15847 C CG   . ASN   B  1 259 ? 88.351 2.776   -75.187 1.00 43.15  ? 285  ASN   B CG   1 
ATOM   15848 O OD1  . ASN   B  1 259 ? 89.320 2.006   -75.291 1.00 45.45  ? 285  ASN   B OD1  1 
ATOM   15849 N ND2  . ASN   B  1 259 ? 87.811 3.360   -76.253 1.00 45.45  ? 285  ASN   B ND2  1 
ATOM   15850 H H    . ASN   B  1 259 ? 85.712 1.535   -73.949 0.00 43.42  ? 285  ASN   B H    1 
ATOM   15851 H HA   . ASN   B  1 259 ? 88.458 1.385   -72.844 0.00 45.12  ? 285  ASN   B HA   1 
ATOM   15852 H HB2  . ASN   B  1 259 ? 86.826 3.648   -73.989 0.00 48.21  ? 285  ASN   B HB2  1 
ATOM   15853 H HB3  . ASN   B  1 259 ? 88.489 3.777   -73.360 0.00 48.66  ? 285  ASN   B HB3  1 
ATOM   15854 H HD21 . ASN   B  1 259 ? 88.178 3.155   -77.177 0.00 60.42  ? 285  ASN   B HD21 1 
ATOM   15855 H HD22 . ASN   B  1 259 ? 87.043 4.017   -76.159 0.00 59.64  ? 285  ASN   B HD22 1 
ATOM   15856 N N    . LEU   B  1 260 ? 85.987 1.880   -70.984 1.00 30.49  ? 286  LEU   B N    1 
ATOM   15857 C CA   . LEU   B  1 260 ? 85.536 2.308   -69.655 1.00 29.50  ? 286  LEU   B CA   1 
ATOM   15858 C C    . LEU   B  1 260 ? 86.168 1.418   -68.581 1.00 27.87  ? 286  LEU   B C    1 
ATOM   15859 O O    . LEU   B  1 260 ? 85.471 0.766   -67.803 1.00 28.20  ? 286  LEU   B O    1 
ATOM   15860 C CB   . LEU   B  1 260 ? 83.995 2.292   -69.568 1.00 29.82  ? 286  LEU   B CB   1 
ATOM   15861 C CG   . LEU   B  1 260 ? 83.259 3.222   -70.544 1.00 31.92  ? 286  LEU   B CG   1 
ATOM   15862 C CD1  . LEU   B  1 260 ? 81.753 3.158   -70.338 1.00 32.67  ? 286  LEU   B CD1  1 
ATOM   15863 C CD2  . LEU   B  1 260 ? 83.713 4.667   -70.397 1.00 32.97  ? 286  LEU   B CD2  1 
ATOM   15864 H H    . LEU   B  1 260 ? 85.390 1.167   -71.389 0.00 40.22  ? 286  LEU   B H    1 
ATOM   15865 H HA   . LEU   B  1 260 ? 85.870 3.324   -69.457 0.00 38.52  ? 286  LEU   B HA   1 
ATOM   15866 H HB2  . LEU   B  1 260 ? 83.649 1.277   -69.758 0.00 38.46  ? 286  LEU   B HB2  1 
ATOM   15867 H HB3  . LEU   B  1 260 ? 83.704 2.592   -68.563 0.00 38.06  ? 286  LEU   B HB3  1 
ATOM   15868 H HG   . LEU   B  1 260 ? 83.474 2.907   -71.564 0.00 41.16  ? 286  LEU   B HG   1 
ATOM   15869 H HD11 . LEU   B  1 260 ? 81.261 3.746   -71.111 0.00 41.21  ? 286  LEU   B HD11 1 
ATOM   15870 H HD12 . LEU   B  1 260 ? 81.432 2.119   -70.403 0.00 41.25  ? 286  LEU   B HD12 1 
ATOM   15871 H HD13 . LEU   B  1 260 ? 81.514 3.559   -69.355 0.00 40.89  ? 286  LEU   B HD13 1 
ATOM   15872 H HD21 . LEU   B  1 260 ? 83.005 5.318   -70.908 0.00 41.91  ? 286  LEU   B HD21 1 
ATOM   15873 H HD22 . LEU   B  1 260 ? 83.755 4.920   -69.339 0.00 41.82  ? 286  LEU   B HD22 1 
ATOM   15874 H HD23 . LEU   B  1 260 ? 84.699 4.780   -70.847 0.00 42.47  ? 286  LEU   B HD23 1 
ATOM   15875 N N    . THR   B  1 261 ? 87.501 1.433   -68.540 1.00 26.22  ? 287  THR   B N    1 
ATOM   15876 C CA   . THR   B  1 261 ? 88.312 0.614   -67.642 1.00 26.64  ? 287  THR   B CA   1 
ATOM   15877 C C    . THR   B  1 261 ? 88.128 0.956   -66.160 1.00 25.11  ? 287  THR   B C    1 
ATOM   15878 O O    . THR   B  1 261 ? 88.352 0.097   -65.302 1.00 24.89  ? 287  THR   B O    1 
ATOM   15879 C CB   . THR   B  1 261 ? 89.805 0.744   -68.026 1.00 29.81  ? 287  THR   B CB   1 
ATOM   15880 O OG1  . THR   B  1 261 ? 89.973 0.374   -69.408 1.00 32.73  ? 287  THR   B OG1  1 
ATOM   15881 C CG2  . THR   B  1 261 ? 90.700 -0.100  -67.153 1.00 31.89  ? 287  THR   B CG2  1 
ATOM   15882 H H    . THR   B  1 261 ? 88.045 2.039   -69.147 0.00 35.45  ? 287  THR   B H    1 
ATOM   15883 H HA   . THR   B  1 261 ? 88.029 -0.430  -67.771 0.00 36.02  ? 287  THR   B HA   1 
ATOM   15884 H HB   . THR   B  1 261 ? 90.108 1.782   -67.903 0.00 40.39  ? 287  THR   B HB   1 
ATOM   15885 H HG1  . THR   B  1 261 ? 90.879 0.633   -69.719 0.00 44.71  ? 287  THR   B HG1  1 
ATOM   15886 H HG21 . THR   B  1 261 ? 91.657 -0.263  -67.647 0.00 43.79  ? 287  THR   B HG21 1 
ATOM   15887 H HG22 . THR   B  1 261 ? 90.889 0.399   -66.203 0.00 43.12  ? 287  THR   B HG22 1 
ATOM   15888 H HG23 . THR   B  1 261 ? 90.233 -1.064  -66.957 0.00 43.19  ? 287  THR   B HG23 1 
ATOM   15889 N N    . GLN   B  1 262 ? 87.747 2.195   -65.855 1.00 24.35  ? 288  GLN   B N    1 
ATOM   15890 C CA   . GLN   B  1 262 ? 87.590 2.628   -64.472 1.00 24.58  ? 288  GLN   B CA   1 
ATOM   15891 C C    . GLN   B  1 262 ? 86.158 2.552   -63.932 1.00 24.66  ? 288  GLN   B C    1 
ATOM   15892 O O    . GLN   B  1 262 ? 85.930 2.971   -62.795 1.00 25.00  ? 288  GLN   B O    1 
ATOM   15893 C CB   . GLN   B  1 262 ? 88.160 4.060   -64.336 1.00 25.74  ? 288  GLN   B CB   1 
ATOM   15894 C CG   . GLN   B  1 262 ? 89.622 4.171   -64.792 1.00 26.32  ? 288  GLN   B CG   1 
ATOM   15895 C CD   . GLN   B  1 262 ? 90.505 3.171   -64.079 1.00 30.06  ? 288  GLN   B CD   1 
ATOM   15896 O OE1  . GLN   B  1 262 ? 91.104 2.274   -64.686 1.00 32.94  ? 288  GLN   B OE1  1 
ATOM   15897 N NE2  . GLN   B  1 262 ? 90.570 3.286   -62.780 1.00 29.89  ? 288  GLN   B NE2  1 
ATOM   15898 H H    . GLN   B  1 262 ? 87.555 2.931   -66.526 0.00 32.46  ? 288  GLN   B H    1 
ATOM   15899 H HA   . GLN   B  1 262 ? 88.173 1.984   -63.816 0.00 32.67  ? 288  GLN   B HA   1 
ATOM   15900 H HB2  . GLN   B  1 262 ? 87.566 4.736   -64.951 0.00 33.73  ? 288  GLN   B HB2  1 
ATOM   15901 H HB3  . GLN   B  1 262 ? 88.112 4.371   -63.294 0.00 33.77  ? 288  GLN   B HB3  1 
ATOM   15902 H HG2  . GLN   B  1 262 ? 89.695 3.992   -65.863 0.00 35.47  ? 288  GLN   B HG2  1 
ATOM   15903 H HG3  . GLN   B  1 262 ? 89.990 5.170   -64.562 0.00 35.34  ? 288  GLN   B HG3  1 
ATOM   15904 H HE21 . GLN   B  1 262 ? 90.103 4.062   -62.320 0.00 39.51  ? 288  GLN   B HE21 1 
ATOM   15905 H HE22 . GLN   B  1 262 ? 91.151 2.654   -62.238 0.00 40.10  ? 288  GLN   B HE22 1 
ATOM   15906 N N    . LEU   B  1 263 ? 85.213 1.982   -64.693 1.00 24.58  ? 289  LEU   B N    1 
ATOM   15907 C CA   . LEU   B  1 263 ? 83.828 1.905   -64.232 1.00 24.95  ? 289  LEU   B CA   1 
ATOM   15908 C C    . LEU   B  1 263 ? 83.681 1.011   -62.984 1.00 23.85  ? 289  LEU   B C    1 
ATOM   15909 O O    . LEU   B  1 263 ? 84.209 -0.100  -62.947 1.00 23.42  ? 289  LEU   B O    1 
ATOM   15910 C CB   . LEU   B  1 263 ? 82.880 1.435   -65.360 1.00 25.93  ? 289  LEU   B CB   1 
ATOM   15911 C CG   . LEU   B  1 263 ? 81.460 2.028   -65.340 1.00 28.47  ? 289  LEU   B CG   1 
ATOM   15912 C CD1  . LEU   B  1 263 ? 81.472 3.511   -65.766 1.00 29.23  ? 289  LEU   B CD1  1 
ATOM   15913 C CD2  . LEU   B  1 263 ? 80.531 1.244   -66.255 1.00 29.33  ? 289  LEU   B CD2  1 
ATOM   15914 H H    . LEU   B  1 263 ? 85.374 1.550   -65.597 0.00 31.91  ? 289  LEU   B H    1 
ATOM   15915 H HA   . LEU   B  1 263 ? 83.552 2.915   -63.941 0.00 31.32  ? 289  LEU   B HA   1 
ATOM   15916 H HB2  . LEU   B  1 263 ? 83.312 1.695   -66.325 0.00 32.93  ? 289  LEU   B HB2  1 
ATOM   15917 H HB3  . LEU   B  1 263 ? 82.781 0.353   -65.290 0.00 32.74  ? 289  LEU   B HB3  1 
ATOM   15918 H HG   . LEU   B  1 263 ? 81.062 1.970   -64.328 0.00 34.89  ? 289  LEU   B HG   1 
ATOM   15919 H HD11 . LEU   B  1 263 ? 80.441 3.839   -65.886 0.00 35.73  ? 289  LEU   B HD11 1 
ATOM   15920 H HD12 . LEU   B  1 263 ? 81.949 4.122   -65.002 0.00 36.01  ? 289  LEU   B HD12 1 
ATOM   15921 H HD13 . LEU   B  1 263 ? 82.005 3.611   -66.711 0.00 36.37  ? 289  LEU   B HD13 1 
ATOM   15922 H HD21 . LEU   B  1 263 ? 79.538 1.683   -66.179 0.00 35.85  ? 289  LEU   B HD21 1 
ATOM   15923 H HD22 . LEU   B  1 263 ? 80.896 1.315   -67.278 0.00 36.49  ? 289  LEU   B HD22 1 
ATOM   15924 H HD23 . LEU   B  1 263 ? 80.504 0.202   -65.938 0.00 36.26  ? 289  LEU   B HD23 1 
ATOM   15925 N N    . ARG   B  1 264 ? 83.058 1.567   -61.930 1.00 24.20  ? 290  ARG   B N    1 
ATOM   15926 C CA   . ARG   B  1 264 ? 82.729 0.879   -60.673 1.00 23.80  ? 290  ARG   B CA   1 
ATOM   15927 C C    . ARG   B  1 264 ? 81.205 0.693   -60.574 1.00 23.21  ? 290  ARG   B C    1 
ATOM   15928 O O    . ARG   B  1 264 ? 80.768 -0.264  -59.944 1.00 23.73  ? 290  ARG   B O    1 
ATOM   15929 C CB   . ARG   B  1 264 ? 83.213 1.672   -59.431 1.00 25.85  ? 290  ARG   B CB   1 
ATOM   15930 C CG   . ARG   B  1 264 ? 84.588 1.283   -58.880 1.00 28.78  ? 290  ARG   B CG   1 
ATOM   15931 C CD   . ARG   B  1 264 ? 85.694 1.802   -59.767 1.00 30.39  ? 290  ARG   B CD   1 
ATOM   15932 N NE   . ARG   B  1 264 ? 87.025 1.445   -59.275 1.00 32.39  ? 290  ARG   B NE   1 
ATOM   15933 C CZ   . ARG   B  1 264 ? 88.165 1.792   -59.873 1.00 33.66  ? 290  ARG   B CZ   1 
ATOM   15934 N NH1  . ARG   B  1 264 ? 88.145 2.509   -60.990 1.00 31.73  ? 290  ARG   B NH1  1 
ATOM   15935 N NH2  . ARG   B  1 264 ? 89.337 1.425   -59.353 1.00 32.13  ? 290  ARG   B NH2  1 
ATOM   15936 H H    . ARG   B  1 264 ? 82.760 2.537   -61.920 0.00 29.91  ? 290  ARG   B H    1 
ATOM   15937 H HA   . ARG   B  1 264 ? 83.184 -0.109  -60.649 0.00 29.72  ? 290  ARG   B HA   1 
ATOM   15938 H HB2  . ARG   B  1 264 ? 83.251 2.733   -59.677 0.00 31.80  ? 290  ARG   B HB2  1 
ATOM   15939 H HB3  . ARG   B  1 264 ? 82.493 1.514   -58.629 0.00 31.55  ? 290  ARG   B HB3  1 
ATOM   15940 H HG2  . ARG   B  1 264 ? 84.714 1.719   -57.890 0.00 35.79  ? 290  ARG   B HG2  1 
ATOM   15941 H HG3  . ARG   B  1 264 ? 84.667 0.198   -58.827 0.00 36.02  ? 290  ARG   B HG3  1 
ATOM   15942 H HD2  . ARG   B  1 264 ? 85.581 1.374   -60.762 0.00 38.33  ? 290  ARG   B HD2  1 
ATOM   15943 H HD3  . ARG   B  1 264 ? 85.633 2.888   -59.818 0.00 38.12  ? 290  ARG   B HD3  1 
ATOM   15944 H HE   . ARG   B  1 264 ? 87.079 0.915   -58.411 0.00 41.18  ? 290  ARG   B HE   1 
ATOM   15945 H HH11 . ARG   B  1 264 ? 87.273 2.785   -61.430 0.00 40.53  ? 290  ARG   B HH11 1 
ATOM   15946 H HH12 . ARG   B  1 264 ? 89.012 2.716   -61.470 0.00 41.26  ? 290  ARG   B HH12 1 
ATOM   15947 H HH21 . ARG   B  1 264 ? 89.363 0.882   -58.496 0.00 41.86  ? 290  ARG   B HH21 1 
ATOM   15948 H HH22 . ARG   B  1 264 ? 90.211 1.651   -59.815 0.00 42.24  ? 290  ARG   B HH22 1 
ATOM   15949 N N    . TYR   B  1 265 ? 80.390 1.631   -61.124 1.00 22.41  ? 291  TYR   B N    1 
ATOM   15950 C CA   . TYR   B  1 265 ? 78.931 1.578   -61.032 1.00 22.31  ? 291  TYR   B CA   1 
ATOM   15951 C C    . TYR   B  1 265 ? 78.323 1.630   -62.414 1.00 21.54  ? 291  TYR   B C    1 
ATOM   15952 O O    . TYR   B  1 265 ? 78.637 2.543   -63.175 1.00 21.95  ? 291  TYR   B O    1 
ATOM   15953 C CB   . TYR   B  1 265 ? 78.397 2.787   -60.250 1.00 23.01  ? 291  TYR   B CB   1 
ATOM   15954 C CG   . TYR   B  1 265 ? 78.867 2.829   -58.813 1.00 25.44  ? 291  TYR   B CG   1 
ATOM   15955 C CD1  . TYR   B  1 265 ? 80.120 3.316   -58.485 1.00 26.74  ? 291  TYR   B CD1  1 
ATOM   15956 C CD2  . TYR   B  1 265 ? 78.037 2.422   -57.778 1.00 27.21  ? 291  TYR   B CD2  1 
ATOM   15957 C CE1  . TYR   B  1 265 ? 80.561 3.347   -57.165 1.00 28.41  ? 291  TYR   B CE1  1 
ATOM   15958 C CE2  . TYR   B  1 265 ? 78.470 2.435   -56.458 1.00 28.69  ? 291  TYR   B CE2  1 
ATOM   15959 C CZ   . TYR   B  1 265 ? 79.743 2.873   -56.157 1.00 29.95  ? 291  TYR   B CZ   1 
ATOM   15960 O OH   . TYR   B  1 265 ? 80.172 2.924   -54.848 1.00 33.37  ? 291  TYR   B OH   1 
ATOM   15961 H H    . TYR   B  1 265 ? 80.717 2.450   -61.627 0.00 27.08  ? 291  TYR   B H    1 
ATOM   15962 H HA   . TYR   B  1 265 ? 78.596 0.670   -60.530 0.00 26.37  ? 291  TYR   B HA   1 
ATOM   15963 H HB2  . TYR   B  1 265 ? 78.740 3.700   -60.736 0.00 27.01  ? 291  TYR   B HB2  1 
ATOM   15964 H HB3  . TYR   B  1 265 ? 77.309 2.755   -60.248 0.00 26.62  ? 291  TYR   B HB3  1 
ATOM   15965 H HD1  . TYR   B  1 265 ? 80.781 3.646   -59.271 0.00 31.93  ? 291  TYR   B HD1  1 
ATOM   15966 H HD2  . TYR   B  1 265 ? 77.058 2.036   -58.004 0.00 31.41  ? 291  TYR   B HD2  1 
ATOM   15967 H HE1  . TYR   B  1 265 ? 81.552 3.701   -56.935 0.00 34.01  ? 291  TYR   B HE1  1 
ATOM   15968 H HE2  . TYR   B  1 265 ? 77.812 2.088   -55.680 0.00 33.21  ? 291  TYR   B HE2  1 
ATOM   15969 H HH   . TYR   B  1 265 ? 79.525 2.471   -54.247 0.00 39.23  ? 291  TYR   B HH   1 
ATOM   15970 N N    . LEU   B  1 266 ? 77.407 0.699   -62.716 1.00 20.36  ? 292  LEU   B N    1 
ATOM   15971 C CA   . LEU   B  1 266 ? 76.711 0.690   -63.990 1.00 20.56  ? 292  LEU   B CA   1 
ATOM   15972 C C    . LEU   B  1 266 ? 75.245 0.453   -63.706 1.00 20.93  ? 292  LEU   B C    1 
ATOM   15973 O O    . LEU   B  1 266 ? 74.894 -0.543  -63.066 1.00 21.39  ? 292  LEU   B O    1 
ATOM   15974 C CB   . LEU   B  1 266 ? 77.257 -0.414  -64.914 1.00 20.92  ? 292  LEU   B CB   1 
ATOM   15975 C CG   . LEU   B  1 266 ? 76.552 -0.586  -66.271 1.00 21.64  ? 292  LEU   B CG   1 
ATOM   15976 C CD1  . LEU   B  1 266 ? 76.574 0.715   -67.099 1.00 22.55  ? 292  LEU   B CD1  1 
ATOM   15977 C CD2  . LEU   B  1 266 ? 77.179 -1.712  -67.046 1.00 21.62  ? 292  LEU   B CD2  1 
ATOM   15978 H H    . LEU   B  1 266 ? 77.125 -0.057  -62.100 0.00 23.93  ? 292  LEU   B H    1 
ATOM   15979 H HA   . LEU   B  1 266 ? 76.825 1.655   -64.480 0.00 24.30  ? 292  LEU   B HA   1 
ATOM   15980 H HB2  . LEU   B  1 266 ? 78.305 -0.201  -65.120 0.00 25.45  ? 292  LEU   B HB2  1 
ATOM   15981 H HB3  . LEU   B  1 266 ? 77.180 -1.367  -64.392 0.00 25.20  ? 292  LEU   B HB3  1 
ATOM   15982 H HG   . LEU   B  1 266 ? 75.509 -0.857  -66.112 0.00 25.92  ? 292  LEU   B HG   1 
ATOM   15983 H HD11 . LEU   B  1 266 ? 76.151 0.507   -68.081 0.00 27.40  ? 292  LEU   B HD11 1 
ATOM   15984 H HD12 . LEU   B  1 266 ? 75.971 1.477   -66.609 0.00 26.92  ? 292  LEU   B HD12 1 
ATOM   15985 H HD13 . LEU   B  1 266 ? 77.601 1.057   -67.212 0.00 27.48  ? 292  LEU   B HD13 1 
ATOM   15986 H HD21 . LEU   B  1 266 ? 76.746 -1.755  -68.044 0.00 26.76  ? 292  LEU   B HD21 1 
ATOM   15987 H HD22 . LEU   B  1 266 ? 78.254 -1.547  -67.112 0.00 26.88  ? 292  LEU   B HD22 1 
ATOM   15988 H HD23 . LEU   B  1 266 ? 76.975 -2.643  -66.521 0.00 26.62  ? 292  LEU   B HD23 1 
ATOM   15989 N N    . ASN   B  1 267 ? 74.391 1.370   -64.152 1.00 20.81  ? 293  ASN   B N    1 
ATOM   15990 C CA   . ASN   B  1 267 ? 72.957 1.234   -63.952 1.00 20.63  ? 293  ASN   B CA   1 
ATOM   15991 C C    . ASN   B  1 267 ? 72.244 1.051   -65.283 1.00 20.71  ? 293  ASN   B C    1 
ATOM   15992 O O    . ASN   B  1 267 ? 72.156 1.983   -66.079 1.00 21.32  ? 293  ASN   B O    1 
ATOM   15993 C CB   . ASN   B  1 267 ? 72.404 2.439   -63.185 1.00 20.53  ? 293  ASN   B CB   1 
ATOM   15994 C CG   . ASN   B  1 267 ? 71.060 2.189   -62.534 1.00 21.36  ? 293  ASN   B CG   1 
ATOM   15995 O OD1  . ASN   B  1 267 ? 70.338 1.279   -62.922 1.00 21.65  ? 293  ASN   B OD1  1 
ATOM   15996 N ND2  . ASN   B  1 267 ? 70.618 3.066   -61.639 1.00 22.13  ? 293  ASN   B ND2  1 
ATOM   15997 H H    . ASN   B  1 267 ? 74.652 2.215   -64.653 0.00 24.08  ? 293  ASN   B H    1 
ATOM   15998 H HA   . ASN   B  1 267 ? 72.758 0.346   -63.354 0.00 23.43  ? 293  ASN   B HA   1 
ATOM   15999 H HB2  . ASN   B  1 267 ? 73.146 2.687   -62.427 0.00 23.00  ? 293  ASN   B HB2  1 
ATOM   16000 H HB3  . ASN   B  1 267 ? 72.254 3.275   -63.864 0.00 23.04  ? 293  ASN   B HB3  1 
ATOM   16001 H HD21 . ASN   B  1 267 ? 69.700 2.976   -61.214 0.00 24.08  ? 293  ASN   B HD21 1 
ATOM   16002 N N    . LEU   B  1 268 ? 71.748 -0.164  -65.529 1.00 20.12  ? 294  LEU   B N    1 
ATOM   16003 C CA   . LEU   B  1 268 ? 70.960 -0.493  -66.724 1.00 20.24  ? 294  LEU   B CA   1 
ATOM   16004 C C    . LEU   B  1 268 ? 69.542 -0.949  -66.312 1.00 19.66  ? 294  LEU   B C    1 
ATOM   16005 O O    . LEU   B  1 268 ? 68.926 -1.770  -67.002 1.00 19.71  ? 294  LEU   B O    1 
ATOM   16006 C CB   . LEU   B  1 268 ? 71.687 -1.565  -67.553 1.00 20.65  ? 294  LEU   B CB   1 
ATOM   16007 C CG   . LEU   B  1 268 ? 73.018 -1.120  -68.208 1.00 23.30  ? 294  LEU   B CG   1 
ATOM   16008 C CD1  . LEU   B  1 268 ? 73.826 -2.340  -68.678 1.00 24.23  ? 294  LEU   B CD1  1 
ATOM   16009 C CD2  . LEU   B  1 268 ? 72.771 -0.229  -69.411 1.00 23.96  ? 294  LEU   B CD2  1 
ATOM   16010 H H    . LEU   B  1 268 ? 71.877 -0.966  -64.920 0.00 23.14  ? 294  LEU   B H    1 
ATOM   16011 H HA   . LEU   B  1 268 ? 70.816 0.396   -67.334 0.00 23.48  ? 294  LEU   B HA   1 
ATOM   16012 H HB2  . LEU   B  1 268 ? 71.922 -2.403  -66.900 0.00 24.45  ? 294  LEU   B HB2  1 
ATOM   16013 H HB3  . LEU   B  1 268 ? 71.040 -1.898  -68.362 0.00 24.59  ? 294  LEU   B HB3  1 
ATOM   16014 H HG   . LEU   B  1 268 ? 73.614 -0.566  -67.485 0.00 27.78  ? 294  LEU   B HG   1 
ATOM   16015 H HD11 . LEU   B  1 268 ? 74.724 -1.995  -69.188 0.00 29.76  ? 294  LEU   B HD11 1 
ATOM   16016 H HD12 . LEU   B  1 268 ? 74.100 -2.938  -67.810 0.00 29.45  ? 294  LEU   B HD12 1 
ATOM   16017 H HD13 . LEU   B  1 268 ? 73.216 -2.933  -69.357 0.00 29.69  ? 294  LEU   B HD13 1 
ATOM   16018 H HD21 . LEU   B  1 268 ? 73.726 0.158   -69.762 0.00 29.08  ? 294  LEU   B HD21 1 
ATOM   16019 H HD22 . LEU   B  1 268 ? 72.310 -0.832  -70.192 0.00 29.09  ? 294  LEU   B HD22 1 
ATOM   16020 H HD23 . LEU   B  1 268 ? 72.107 0.593   -69.151 0.00 28.58  ? 294  LEU   B HD23 1 
ATOM   16021 N N    . SER   B  1 269 ? 68.999 -0.375  -65.200 1.00 18.54  ? 295  SER   B N    1 
ATOM   16022 C CA   . SER   B  1 269 ? 67.657 -0.711  -64.769 1.00 18.82  ? 295  SER   B CA   1 
ATOM   16023 C C    . SER   B  1 269 ? 66.660 -0.190  -65.791 1.00 19.98  ? 295  SER   B C    1 
ATOM   16024 O O    . SER   B  1 269 ? 66.838 0.892   -66.344 1.00 20.42  ? 295  SER   B O    1 
ATOM   16025 C CB   . SER   B  1 269 ? 67.333 -0.084  -63.416 1.00 20.28  ? 295  SER   B CB   1 
ATOM   16026 O OG   . SER   B  1 269 ? 68.197 -0.581  -62.410 1.00 22.59  ? 295  SER   B OG   1 
ATOM   16027 H H    . SER   B  1 269 ? 69.455 0.316   -64.613 0.00 20.62  ? 295  SER   B H    1 
ATOM   16028 H HA   . SER   B  1 269 ? 67.561 -1.793  -64.687 0.00 21.01  ? 295  SER   B HA   1 
ATOM   16029 H HB2  . SER   B  1 269 ? 67.459 0.996   -63.486 0.00 22.14  ? 295  SER   B HB2  1 
ATOM   16030 H HB3  . SER   B  1 269 ? 66.304 -0.324  -63.155 0.00 22.09  ? 295  SER   B HB3  1 
ATOM   16031 H HG   . SER   B  1 269 ? 69.097 -0.169  -62.494 0.00 25.07  ? 295  SER   B HG   1 
ATOM   16032 N N    . SER   B  1 270 ? 65.619 -0.966  -66.045 1.00 19.57  ? 296  SER   B N    1 
ATOM   16033 C CA   . SER   B  1 270 ? 64.553 -0.578  -66.952 1.00 19.48  ? 296  SER   B CA   1 
ATOM   16034 C C    . SER   B  1 270 ? 65.025 -0.129  -68.340 1.00 19.54  ? 296  SER   B C    1 
ATOM   16035 O O    . SER   B  1 270 ? 64.672 0.937   -68.816 1.00 19.86  ? 296  SER   B O    1 
ATOM   16036 C CB   . SER   B  1 270 ? 63.670 0.486   -66.302 1.00 19.28  ? 296  SER   B CB   1 
ATOM   16037 O OG   . SER   B  1 270 ? 62.406 0.563   -66.951 1.00 20.17  ? 296  SER   B OG   1 
ATOM   16038 H H    . SER   B  1 270 ? 65.477 -1.882  -65.633 0.00 21.93  ? 296  SER   B H    1 
ATOM   16039 H HA   . SER   B  1 270 ? 63.955 -1.475  -67.110 0.00 22.04  ? 296  SER   B HA   1 
ATOM   16040 H HB2  . SER   B  1 270 ? 63.507 0.214   -65.261 0.00 21.07  ? 296  SER   B HB2  1 
ATOM   16041 H HB3  . SER   B  1 270 ? 64.163 1.456   -66.350 0.00 21.25  ? 296  SER   B HB3  1 
ATOM   16042 H HG   . SER   B  1 270 ? 61.845 1.259   -66.520 0.00 22.28  ? 296  SER   B HG   1 
ATOM   16043 N N    . THR   B  1 271 ? 65.892 -0.910  -68.928 1.00 19.30  ? 297  THR   B N    1 
ATOM   16044 C CA   . THR   B  1 271 ? 66.323 -0.802  -70.321 1.00 19.95  ? 297  THR   B CA   1 
ATOM   16045 C C    . THR   B  1 271 ? 65.756 -1.951  -71.215 1.00 21.00  ? 297  THR   B C    1 
ATOM   16046 O O    . THR   B  1 271 ? 66.167 -2.086  -72.379 1.00 21.84  ? 297  THR   B O    1 
ATOM   16047 C CB   . THR   B  1 271 ? 67.838 -0.696  -70.381 1.00 20.21  ? 297  THR   B CB   1 
ATOM   16048 O OG1  . THR   B  1 271 ? 68.423 -1.882  -69.857 1.00 20.37  ? 297  THR   B OG1  1 
ATOM   16049 C CG2  . THR   B  1 271 ? 68.361 0.533   -69.643 1.00 20.68  ? 297  THR   B CG2  1 
ATOM   16050 H H    . THR   B  1 271 ? 66.485 -1.516  -68.381 0.00 22.35  ? 297  THR   B H    1 
ATOM   16051 H HA   . THR   B  1 271 ? 65.938 0.124   -70.745 0.00 23.55  ? 297  THR   B HA   1 
ATOM   16052 H HB   . THR   B  1 271 ? 68.134 -0.597  -71.423 0.00 24.35  ? 297  THR   B HB   1 
ATOM   16053 H HG1  . THR   B  1 271 ? 68.385 -1.897  -68.866 0.00 24.03  ? 297  THR   B HG1  1 
ATOM   16054 H HG21 . THR   B  1 271 ? 69.436 0.625   -69.793 0.00 24.43  ? 297  THR   B HG21 1 
ATOM   16055 H HG22 . THR   B  1 271 ? 67.875 1.430   -70.024 0.00 24.22  ? 297  THR   B HG22 1 
ATOM   16056 H HG23 . THR   B  1 271 ? 68.164 0.450   -68.575 0.00 23.96  ? 297  THR   B HG23 1 
ATOM   16057 N N    . SER   B  1 272 ? 64.796 -2.748  -70.672 1.00 21.28  ? 298  SER   B N    1 
ATOM   16058 C CA   . SER   B  1 272 ? 64.112 -3.854  -71.334 1.00 21.99  ? 298  SER   B CA   1 
ATOM   16059 C C    . SER   B  1 272 ? 65.072 -4.916  -71.871 1.00 22.57  ? 298  SER   B C    1 
ATOM   16060 O O    . SER   B  1 272 ? 64.815 -5.512  -72.907 1.00 23.39  ? 298  SER   B O    1 
ATOM   16061 C CB   . SER   B  1 272 ? 63.181 -3.310  -72.416 1.00 23.35  ? 298  SER   B CB   1 
ATOM   16062 O OG   . SER   B  1 272 ? 62.173 -2.507  -71.827 1.00 25.46  ? 298  SER   B OG   1 
ATOM   16063 H H    . SER   B  1 272 ? 64.437 -2.627  -69.731 0.00 25.15  ? 298  SER   B H    1 
ATOM   16064 H HA   . SER   B  1 272 ? 63.495 -4.357  -70.590 0.00 26.55  ? 298  SER   B HA   1 
ATOM   16065 H HB2  . SER   B  1 272 ? 63.737 -2.658  -73.086 0.00 28.70  ? 298  SER   B HB2  1 
ATOM   16066 H HB3  . SER   B  1 272 ? 62.715 -4.120  -72.975 0.00 28.91  ? 298  SER   B HB3  1 
ATOM   16067 H HG   . SER   B  1 272 ? 62.531 -1.614  -71.580 0.00 30.51  ? 298  SER   B HG   1 
ATOM   16068 N N    . LEU   B  1 273 ? 66.192 -5.139  -71.174 1.00 22.57  ? 299  LEU   B N    1 
ATOM   16069 C CA   . LEU   B  1 273 ? 67.156 -6.140  -71.596 1.00 23.18  ? 299  LEU   B CA   1 
ATOM   16070 C C    . LEU   B  1 273 ? 66.664 -7.570  -71.405 1.00 23.82  ? 299  LEU   B C    1 
ATOM   16071 O O    . LEU   B  1 273 ? 66.144 -7.905  -70.335 1.00 23.37  ? 299  LEU   B O    1 
ATOM   16072 C CB   . LEU   B  1 273 ? 68.462 -5.994  -70.811 1.00 23.08  ? 299  LEU   B CB   1 
ATOM   16073 C CG   . LEU   B  1 273 ? 69.342 -4.804  -71.151 1.00 24.15  ? 299  LEU   B CG   1 
ATOM   16074 C CD1  . LEU   B  1 273 ? 70.370 -4.566  -70.042 1.00 24.50  ? 299  LEU   B CD1  1 
ATOM   16075 C CD2  . LEU   B  1 273 ? 70.031 -4.987  -72.520 1.00 24.05  ? 299  LEU   B CD2  1 
ATOM   16076 H H    . LEU   B  1 273 ? 66.489 -4.623  -70.356 0.00 27.41  ? 299  LEU   B H    1 
ATOM   16077 H HA   . LEU   B  1 273 ? 67.372 -5.982  -72.651 0.00 29.26  ? 299  LEU   B HA   1 
ATOM   16078 H HB2  . LEU   B  1 273 ? 68.225 -5.936  -69.750 0.00 28.30  ? 299  LEU   B HB2  1 
ATOM   16079 H HB3  . LEU   B  1 273 ? 69.053 -6.891  -70.989 0.00 29.00  ? 299  LEU   B HB3  1 
ATOM   16080 H HG   . LEU   B  1 273 ? 68.718 -3.913  -71.211 0.00 29.66  ? 299  LEU   B HG   1 
ATOM   16081 H HD11 . LEU   B  1 273 ? 71.016 -3.736  -70.321 0.00 30.06  ? 299  LEU   B HD11 1 
ATOM   16082 H HD12 . LEU   B  1 273 ? 69.846 -4.328  -69.117 0.00 29.68  ? 299  LEU   B HD12 1 
ATOM   16083 H HD13 . LEU   B  1 273 ? 70.965 -5.469  -69.912 0.00 30.31  ? 299  LEU   B HD13 1 
ATOM   16084 H HD21 . LEU   B  1 273 ? 70.786 -4.210  -72.633 0.00 30.30  ? 299  LEU   B HD21 1 
ATOM   16085 H HD22 . LEU   B  1 273 ? 70.502 -5.968  -72.563 0.00 30.63  ? 299  LEU   B HD22 1 
ATOM   16086 H HD23 . LEU   B  1 273 ? 69.292 -4.892  -73.312 0.00 30.49  ? 299  LEU   B HD23 1 
ATOM   16087 N N    A ARG   B  1 274 ? 66.820 -8.407  -72.447 0.50 23.99  ? 300  ARG   B N    1 
ATOM   16088 N N    B ARG   B  1 274 ? 66.812 -8.393  -72.463 0.50 24.27  ? 300  ARG   B N    1 
ATOM   16089 C CA   A ARG   B  1 274 ? 66.552 -9.851  -72.394 0.50 24.94  ? 300  ARG   B CA   1 
ATOM   16090 C CA   B ARG   B  1 274 ? 66.517 -9.828  -72.464 0.50 25.51  ? 300  ARG   B CA   1 
ATOM   16091 C C    A ARG   B  1 274 ? 67.890 -10.616 -72.433 0.50 26.66  ? 300  ARG   B C    1 
ATOM   16092 C C    B ARG   B  1 274 ? 67.849 -10.631 -72.508 0.50 26.88  ? 300  ARG   B C    1 
ATOM   16093 O O    A ARG   B  1 274 ? 67.963 -11.725 -71.908 0.50 27.05  ? 300  ARG   B O    1 
ATOM   16094 O O    B ARG   B  1 274 ? 67.880 -11.770 -72.049 0.50 27.21  ? 300  ARG   B O    1 
ATOM   16095 C CB   A ARG   B  1 274 ? 65.682 -10.342 -73.569 0.50 25.32  ? 300  ARG   B CB   1 
ATOM   16096 C CB   B ARG   B  1 274 ? 65.620 -10.220 -73.662 0.50 26.72  ? 300  ARG   B CB   1 
ATOM   16097 C CG   A ARG   B  1 274 ? 64.192 -10.063 -73.425 0.50 25.44  ? 300  ARG   B CG   1 
ATOM   16098 C CG   B ARG   B  1 274 ? 64.350 -9.372  -73.781 0.50 28.45  ? 300  ARG   B CG   1 
ATOM   16099 C CD   A ARG   B  1 274 ? 63.896 -8.590  -73.598 0.50 25.16  ? 300  ARG   B CD   1 
ATOM   16100 C CD   B ARG   B  1 274 ? 63.235 -9.992  -74.611 0.50 28.85  ? 300  ARG   B CD   1 
ATOM   16101 N NE   A ARG   B  1 274 ? 62.473 -8.340  -73.815 0.50 24.78  ? 300  ARG   B NE   1 
ATOM   16102 N NE   B ARG   B  1 274 ? 61.956 -9.302  -74.376 0.50 28.67  ? 300  ARG   B NE   1 
ATOM   16103 C CZ   A ARG   B  1 274 ? 61.961 -7.262  -74.413 0.50 25.01  ? 300  ARG   B CZ   1 
ATOM   16104 C CZ   B ARG   B  1 274 ? 60.964 -9.699  -73.569 0.50 28.51  ? 300  ARG   B CZ   1 
ATOM   16105 N NH1  A ARG   B  1 274 ? 60.648 -7.139  -74.559 0.50 26.10  ? 300  ARG   B NH1  1 
ATOM   16106 N NH1  B ARG   B  1 274 ? 59.866 -8.961  -73.445 0.50 28.15  ? 300  ARG   B NH1  1 
ATOM   16107 N NH2  A ARG   B  1 274 ? 62.760 -6.300  -74.876 0.50 22.24  ? 300  ARG   B NH2  1 
ATOM   16108 N NH2  B ARG   B  1 274 ? 61.062 -10.837 -72.882 0.50 26.10  ? 300  ARG   B NH2  1 
ATOM   16109 H H    A ARG   B  1 274 ? 67.124 -8.103  -73.366 0.00 31.00  ? 300  ARG   B H    1 
ATOM   16110 H H    B ARG   B  1 274 ? 67.135 -8.075  -73.372 0.00 31.33  ? 300  ARG   B H    1 
ATOM   16111 H HA   A ARG   B  1 274 ? 66.048 -10.115 -71.466 0.00 31.96  ? 300  ARG   B HA   1 
ATOM   16112 H HA   B ARG   B  1 274 ? 65.989 -10.106 -71.553 0.00 32.67  ? 300  ARG   B HA   1 
ATOM   16113 H HB2  A ARG   B  1 274 ? 66.035 -9.879  -74.489 0.00 33.42  ? 300  ARG   B HB2  1 
ATOM   16114 H HB2  B ARG   B  1 274 ? 66.190 -10.097 -74.582 0.00 35.21  ? 300  ARG   B HB2  1 
ATOM   16115 H HB3  A ARG   B  1 274 ? 65.798 -11.422 -73.645 0.00 33.58  ? 300  ARG   B HB3  1 
ATOM   16116 H HB3  B ARG   B  1 274 ? 65.324 -11.262 -73.548 0.00 35.12  ? 300  ARG   B HB3  1 
ATOM   16117 H HG2  A ARG   B  1 274 ? 63.656 -10.603 -74.204 0.00 33.55  ? 300  ARG   B HG2  1 
ATOM   16118 H HG2  B ARG   B  1 274 ? 63.944 -9.189  -72.792 0.00 36.24  ? 300  ARG   B HG2  1 
ATOM   16119 H HG3  A ARG   B  1 274 ? 63.852 -10.396 -72.446 0.00 32.85  ? 300  ARG   B HG3  1 
ATOM   16120 H HG3  B ARG   B  1 274 ? 64.613 -8.423  -74.246 0.00 36.60  ? 300  ARG   B HG3  1 
ATOM   16121 H HD2  A ARG   B  1 274 ? 64.219 -8.041  -72.715 0.00 31.96  ? 300  ARG   B HD2  1 
ATOM   16122 H HD2  B ARG   B  1 274 ? 63.482 -9.831  -75.660 0.00 37.97  ? 300  ARG   B HD2  1 
ATOM   16123 H HD3  A ARG   B  1 274 ? 64.451 -8.261  -74.475 0.00 32.67  ? 300  ARG   B HD3  1 
ATOM   16124 H HD3  B ARG   B  1 274 ? 63.168 -11.064 -74.437 0.00 37.86  ? 300  ARG   B HD3  1 
ATOM   16125 H HE   A ARG   B  1 274 ? 61.827 -9.050  -73.485 0.00 32.00  ? 300  ARG   B HE   1 
ATOM   16126 H HE   B ARG   B  1 274 ? 61.823 -8.427  -74.873 0.00 37.03  ? 300  ARG   B HE   1 
ATOM   16127 H HH11 A ARG   B  1 274 ? 60.025 -7.866  -74.222 0.00 33.55  ? 300  ARG   B HH11 1 
ATOM   16128 H HH11 B ARG   B  1 274 ? 59.768 -8.097  -73.968 0.00 35.97  ? 300  ARG   B HH11 1 
ATOM   16129 H HH12 A ARG   B  1 274 ? 60.257 -6.322  -75.016 0.00 33.46  ? 300  ARG   B HH12 1 
ATOM   16130 H HH12 B ARG   B  1 274 ? 59.109 -9.264  -72.840 0.00 35.85  ? 300  ARG   B HH12 1 
ATOM   16131 H HH21 A ARG   B  1 274 ? 63.770 -6.323  -74.778 0.00 28.74  ? 300  ARG   B HH21 1 
ATOM   16132 H HH21 B ARG   B  1 274 ? 61.878 -11.438 -72.906 0.00 34.04  ? 300  ARG   B HH21 1 
ATOM   16133 H HH22 A ARG   B  1 274 ? 62.344 -5.488  -75.320 0.00 28.72  ? 300  ARG   B HH22 1 
ATOM   16134 H HH22 B ARG   B  1 274 ? 60.295 -11.107 -72.275 0.00 33.69  ? 300  ARG   B HH22 1 
ATOM   16135 N N    . LYS   B  1 275 ? 68.930 -10.049 -73.075 1.00 27.62  ? 301  LYS   B N    1 
ATOM   16136 C CA   . LYS   B  1 275 ? 70.242 -10.660 -73.189 1.00 29.28  ? 301  LYS   B CA   1 
ATOM   16137 C C    . LYS   B  1 275 ? 71.287 -9.642  -72.749 1.00 29.56  ? 301  LYS   B C    1 
ATOM   16138 O O    . LYS   B  1 275 ? 71.174 -8.454  -73.036 1.00 30.22  ? 301  LYS   B O    1 
ATOM   16139 C CB   . LYS   B  1 275 ? 70.494 -11.077 -74.651 1.00 32.31  ? 301  LYS   B CB   1 
ATOM   16140 C CG   . LYS   B  1 275 ? 69.446 -12.042 -75.205 1.00 40.22  ? 301  LYS   B CG   1 
ATOM   16141 C CD   . LYS   B  1 275 ? 69.495 -13.429 -74.548 1.00 47.74  ? 301  LYS   B CD   1 
ATOM   16142 C CE   . LYS   B  1 275 ? 68.525 -14.391 -75.196 1.00 54.24  ? 301  LYS   B CE   1 
ATOM   16143 N NZ   . LYS   B  1 275 ? 68.792 -15.810 -74.815 1.00 57.79  ? 301  LYS   B NZ   1 
ATOM   16144 H H    . LYS   B  1 275 ? 68.915 -9.141  -73.529 0.00 35.88  ? 301  LYS   B H    1 
ATOM   16145 H HA   . LYS   B  1 275 ? 70.343 -11.539 -72.555 0.00 38.45  ? 301  LYS   B HA   1 
ATOM   16146 H HB2  . LYS   B  1 275 ? 70.491 -10.186 -75.277 0.00 42.64  ? 301  LYS   B HB2  1 
ATOM   16147 H HB3  . LYS   B  1 275 ? 71.465 -11.568 -74.713 0.00 43.00  ? 301  LYS   B HB3  1 
ATOM   16148 H HG2  . LYS   B  1 275 ? 68.448 -11.633 -75.059 0.00 52.27  ? 301  LYS   B HG2  1 
ATOM   16149 H HG3  . LYS   B  1 275 ? 69.632 -12.174 -76.270 0.00 53.05  ? 301  LYS   B HG3  1 
ATOM   16150 H HD2  . LYS   B  1 275 ? 70.499 -13.839 -74.648 0.00 62.17  ? 301  LYS   B HD2  1 
ATOM   16151 H HD3  . LYS   B  1 275 ? 69.226 -13.343 -73.497 0.00 61.40  ? 301  LYS   B HD3  1 
ATOM   16152 H HE2  . LYS   B  1 275 ? 67.513 -14.142 -74.880 0.00 69.78  ? 301  LYS   B HE2  1 
ATOM   16153 H HE3  . LYS   B  1 275 ? 68.608 -14.312 -76.279 0.00 70.49  ? 301  LYS   B HE3  1 
ATOM   16154 H HZ1  . LYS   B  1 275 ? 68.097 -16.418 -75.235 0.00 75.14  ? 301  LYS   B HZ1  1 
ATOM   16155 H HZ2  . LYS   B  1 275 ? 69.712 -16.088 -75.140 0.00 75.18  ? 301  LYS   B HZ2  1 
ATOM   16156 H HZ3  . LYS   B  1 275 ? 68.753 -15.912 -73.806 0.00 74.50  ? 301  LYS   B HZ3  1 
ATOM   16157 N N    . ILE   B  1 276 ? 72.304 -10.107 -72.045 1.00 29.35  ? 302  ILE   B N    1 
ATOM   16158 C CA   . ILE   B  1 276 ? 73.403 -9.273  -71.603 1.00 29.29  ? 302  ILE   B CA   1 
ATOM   16159 C C    . ILE   B  1 276 ? 74.608 -9.790  -72.363 1.00 29.58  ? 302  ILE   B C    1 
ATOM   16160 O O    . ILE   B  1 276 ? 74.928 -10.974 -72.267 1.00 30.35  ? 302  ILE   B O    1 
ATOM   16161 C CB   . ILE   B  1 276 ? 73.601 -9.351  -70.074 1.00 29.91  ? 302  ILE   B CB   1 
ATOM   16162 C CG1  . ILE   B  1 276 ? 72.336 -8.815  -69.346 1.00 30.53  ? 302  ILE   B CG1  1 
ATOM   16163 C CG2  . ILE   B  1 276 ? 74.848 -8.553  -69.672 1.00 30.56  ? 302  ILE   B CG2  1 
ATOM   16164 C CD1  . ILE   B  1 276 ? 72.327 -9.009  -67.917 1.00 32.01  ? 302  ILE   B CD1  1 
ATOM   16165 H H    . ILE   B  1 276 ? 72.413 -11.079 -71.774 0.00 38.45  ? 302  ILE   B H    1 
ATOM   16166 H HA   . ILE   B  1 276 ? 73.242 -8.228  -71.860 0.00 37.69  ? 302  ILE   B HA   1 
ATOM   16167 H HB   . ILE   B  1 276 ? 73.747 -10.394 -69.801 0.00 38.56  ? 302  ILE   B HB   1 
ATOM   16168 H HG12 . ILE   B  1 276 ? 72.261 -7.744  -69.528 0.00 38.20  ? 302  ILE   B HG12 1 
ATOM   16169 H HG13 . ILE   B  1 276 ? 71.453 -9.316  -69.739 0.00 38.55  ? 302  ILE   B HG13 1 
ATOM   16170 H HG21 . ILE   B  1 276 ? 74.914 -8.481  -68.589 0.00 38.69  ? 302  ILE   B HG21 1 
ATOM   16171 H HG22 . ILE   B  1 276 ? 75.742 -9.056  -70.038 0.00 39.41  ? 302  ILE   B HG22 1 
ATOM   16172 H HG23 . ILE   B  1 276 ? 74.782 -7.555  -70.103 0.00 38.80  ? 302  ILE   B HG23 1 
ATOM   16173 H HD11 . ILE   B  1 276 ? 71.299 -8.943  -67.564 0.00 39.60  ? 302  ILE   B HD11 1 
ATOM   16174 H HD12 . ILE   B  1 276 ? 72.739 -9.990  -67.685 0.00 40.19  ? 302  ILE   B HD12 1 
ATOM   16175 H HD13 . ILE   B  1 276 ? 72.922 -8.230  -67.442 0.00 39.67  ? 302  ILE   B HD13 1 
ATOM   16176 N N    . ASN   B  1 277 ? 75.258 -8.926  -73.138 1.00 28.90  ? 303  ASN   B N    1 
ATOM   16177 C CA   . ASN   B  1 277 ? 76.450 -9.319  -73.876 1.00 28.91  ? 303  ASN   B CA   1 
ATOM   16178 C C    . ASN   B  1 277 ? 77.622 -9.355  -72.894 1.00 28.80  ? 303  ASN   B C    1 
ATOM   16179 O O    . ASN   B  1 277 ? 78.024 -8.311  -72.396 1.00 29.27  ? 303  ASN   B O    1 
ATOM   16180 C CB   . ASN   B  1 277 ? 76.715 -8.335  -75.010 1.00 29.97  ? 303  ASN   B CB   1 
ATOM   16181 C CG   . ASN   B  1 277 ? 77.796 -8.783  -75.955 1.00 33.21  ? 303  ASN   B CG   1 
ATOM   16182 O OD1  . ASN   B  1 277 ? 78.564 -9.706  -75.675 1.00 34.01  ? 303  ASN   B OD1  1 
ATOM   16183 N ND2  . ASN   B  1 277 ? 77.874 -8.140  -77.109 1.00 34.01  ? 303  ASN   B ND2  1 
ATOM   16184 H H    . ASN   B  1 277 ? 74.994 -7.956  -73.278 0.00 37.92  ? 303  ASN   B H    1 
ATOM   16185 H HA   . ASN   B  1 277 ? 76.312 -10.306 -74.316 0.00 39.23  ? 303  ASN   B HA   1 
ATOM   16186 H HB2  . ASN   B  1 277 ? 75.798 -8.224  -75.588 0.00 40.21  ? 303  ASN   B HB2  1 
ATOM   16187 H HB3  . ASN   B  1 277 ? 77.003 -7.370  -74.595 0.00 39.89  ? 303  ASN   B HB3  1 
ATOM   16188 H HD21 . ASN   B  1 277 ? 78.586 -8.398  -77.785 0.00 46.48  ? 303  ASN   B HD21 1 
ATOM   16189 H HD22 . ASN   B  1 277 ? 77.220 -7.392  -77.317 0.00 45.72  ? 303  ASN   B HD22 1 
ATOM   16190 N N    . ALA   B  1 278 ? 78.167 -10.545 -72.614 1.00 28.84  ? 304  ALA   B N    1 
ATOM   16191 C CA   . ALA   B  1 278 ? 79.297 -10.707 -71.695 1.00 29.36  ? 304  ALA   B CA   1 
ATOM   16192 C C    . ALA   B  1 278 ? 80.498 -9.823  -72.085 1.00 29.60  ? 304  ALA   B C    1 
ATOM   16193 O O    . ALA   B  1 278 ? 81.240 -9.378  -71.209 1.00 30.38  ? 304  ALA   B O    1 
ATOM   16194 C CB   . ALA   B  1 278 ? 79.729 -12.173 -71.661 1.00 29.41  ? 304  ALA   B CB   1 
ATOM   16195 H H    . ALA   B  1 278 ? 77.841 -11.424 -73.004 0.00 39.44  ? 304  ALA   B H    1 
ATOM   16196 H HA   . ALA   B  1 278 ? 78.980 -10.424 -70.692 0.00 39.34  ? 304  ALA   B HA   1 
ATOM   16197 H HB1  . ALA   B  1 278 ? 80.567 -12.276 -70.974 0.00 40.52  ? 304  ALA   B HB1  1 
ATOM   16198 H HB2  . ALA   B  1 278 ? 78.891 -12.780 -71.320 0.00 40.34  ? 304  ALA   B HB2  1 
ATOM   16199 H HB3  . ALA   B  1 278 ? 80.027 -12.478 -72.662 0.00 40.93  ? 304  ALA   B HB3  1 
ATOM   16200 N N    . ALA   B  1 279 ? 80.679 -9.568  -73.387 1.00 29.30  ? 305  ALA   B N    1 
ATOM   16201 C CA   . ALA   B  1 279 ? 81.768 -8.733  -73.896 1.00 29.52  ? 305  ALA   B CA   1 
ATOM   16202 C C    . ALA   B  1 279 ? 81.710 -7.273  -73.405 1.00 29.72  ? 305  ALA   B C    1 
ATOM   16203 O O    . ALA   B  1 279 ? 82.752 -6.615  -73.366 1.00 30.39  ? 305  ALA   B O    1 
ATOM   16204 C CB   . ALA   B  1 279 ? 81.784 -8.775  -75.409 1.00 29.54  ? 305  ALA   B CB   1 
ATOM   16205 H H    . ALA   B  1 279 ? 80.086 -9.946  -74.119 0.00 40.43  ? 305  ALA   B H    1 
ATOM   16206 H HA   . ALA   B  1 279 ? 82.711 -9.153  -73.551 0.00 41.02  ? 305  ALA   B HA   1 
ATOM   16207 H HB1  . ALA   B  1 279 ? 82.580 -8.125  -75.769 0.00 41.40  ? 305  ALA   B HB1  1 
ATOM   16208 H HB2  . ALA   B  1 279 ? 81.963 -9.798  -75.735 0.00 41.70  ? 305  ALA   B HB2  1 
ATOM   16209 H HB3  . ALA   B  1 279 ? 80.820 -8.428  -75.781 0.00 40.98  ? 305  ALA   B HB3  1 
ATOM   16210 N N    . TRP   B  1 280 ? 80.533 -6.784  -72.977 1.00 29.01  ? 306  TRP   B N    1 
ATOM   16211 C CA   . TRP   B  1 280 ? 80.411 -5.435  -72.409 1.00 29.73  ? 306  TRP   B CA   1 
ATOM   16212 C C    . TRP   B  1 280 ? 81.322 -5.252  -71.183 1.00 29.89  ? 306  TRP   B C    1 
ATOM   16213 O O    . TRP   B  1 280 ? 81.769 -4.140  -70.921 1.00 29.85  ? 306  TRP   B O    1 
ATOM   16214 C CB   . TRP   B  1 280 ? 78.961 -5.155  -71.952 1.00 29.64  ? 306  TRP   B CB   1 
ATOM   16215 C CG   . TRP   B  1 280 ? 77.947 -5.021  -73.046 1.00 30.26  ? 306  TRP   B CG   1 
ATOM   16216 C CD1  . TRP   B  1 280 ? 78.173 -4.710  -74.353 1.00 31.13  ? 306  TRP   B CD1  1 
ATOM   16217 C CD2  . TRP   B  1 280 ? 76.527 -5.161  -72.903 1.00 30.34  ? 306  TRP   B CD2  1 
ATOM   16218 N NE1  . TRP   B  1 280 ? 76.986 -4.716  -75.049 1.00 31.41  ? 306  TRP   B NE1  1 
ATOM   16219 C CE2  . TRP   B  1 280 ? 75.956 -4.956  -74.172 1.00 31.05  ? 306  TRP   B CE2  1 
ATOM   16220 C CE3  . TRP   B  1 280 ? 75.685 -5.460  -71.825 1.00 30.50  ? 306  TRP   B CE3  1 
ATOM   16221 C CZ2  . TRP   B  1 280 ? 74.582 -5.055  -74.395 1.00 31.50  ? 306  TRP   B CZ2  1 
ATOM   16222 C CZ3  . TRP   B  1 280 ? 74.323 -5.529  -72.042 1.00 31.37  ? 306  TRP   B CZ3  1 
ATOM   16223 C CH2  . TRP   B  1 280 ? 73.784 -5.334  -73.315 1.00 31.52  ? 306  TRP   B CH2  1 
ATOM   16224 H H    . TRP   B  1 280 ? 79.652 -7.286  -73.020 0.00 38.86  ? 306  TRP   B H    1 
ATOM   16225 H HA   . TRP   B  1 280 ? 80.699 -4.695  -73.153 0.00 39.40  ? 306  TRP   B HA   1 
ATOM   16226 H HB2  . TRP   B  1 280 ? 78.640 -5.986  -71.326 0.00 38.53  ? 306  TRP   B HB2  1 
ATOM   16227 H HB3  . TRP   B  1 280 ? 78.940 -4.241  -71.362 0.00 38.22  ? 306  TRP   B HB3  1 
ATOM   16228 H HD1  . TRP   B  1 280 ? 79.144 -4.558  -74.795 0.00 41.14  ? 306  TRP   B HD1  1 
ATOM   16229 H HE1  . TRP   B  1 280 ? 76.881 -4.507  -76.063 0.00 41.38  ? 306  TRP   B HE1  1 
ATOM   16230 H HE3  . TRP   B  1 280 ? 76.091 -5.619  -70.844 0.00 38.76  ? 306  TRP   B HE3  1 
ATOM   16231 H HZ2  . TRP   B  1 280 ? 74.160 -4.888  -75.369 0.00 40.81  ? 306  TRP   B HZ2  1 
ATOM   16232 H HZ3  . TRP   B  1 280 ? 73.666 -5.759  -71.222 0.00 39.44  ? 306  TRP   B HZ3  1 
ATOM   16233 H HH2  . TRP   B  1 280 ? 72.718 -5.398  -73.449 0.00 40.07  ? 306  TRP   B HH2  1 
ATOM   16234 N N    . PHE   B  1 281 ? 81.587 -6.337  -70.439 1.00 30.21  ? 307  PHE   B N    1 
ATOM   16235 C CA   . PHE   B  1 281 ? 82.381 -6.306  -69.204 1.00 30.91  ? 307  PHE   B CA   1 
ATOM   16236 C C    . PHE   B  1 281 ? 83.824 -6.800  -69.379 1.00 32.16  ? 307  PHE   B C    1 
ATOM   16237 O O    . PHE   B  1 281 ? 84.536 -6.921  -68.389 1.00 32.72  ? 307  PHE   B O    1 
ATOM   16238 C CB   . PHE   B  1 281 ? 81.669 -7.158  -68.136 1.00 30.50  ? 307  PHE   B CB   1 
ATOM   16239 C CG   . PHE   B  1 281 ? 80.211 -6.799  -67.965 1.00 30.97  ? 307  PHE   B CG   1 
ATOM   16240 C CD1  . PHE   B  1 281 ? 79.840 -5.619  -67.339 1.00 31.34  ? 307  PHE   B CD1  1 
ATOM   16241 C CD2  . PHE   B  1 281 ? 79.218 -7.573  -68.543 1.00 31.83  ? 307  PHE   B CD2  1 
ATOM   16242 C CE1  . PHE   B  1 281 ? 78.501 -5.268  -67.219 1.00 32.01  ? 307  PHE   B CE1  1 
ATOM   16243 C CE2  . PHE   B  1 281 ? 77.879 -7.211  -68.430 1.00 32.49  ? 307  PHE   B CE2  1 
ATOM   16244 C CZ   . PHE   B  1 281 ? 77.528 -6.061  -67.770 1.00 31.85  ? 307  PHE   B CZ   1 
ATOM   16245 H H    . PHE   B  1 281 ? 81.251 -7.271  -70.651 0.00 40.07  ? 307  PHE   B H    1 
ATOM   16246 H HA   . PHE   B  1 281 ? 82.427 -5.289  -68.817 0.00 40.33  ? 307  PHE   B HA   1 
ATOM   16247 H HB2  . PHE   B  1 281 ? 81.725 -8.207  -68.422 0.00 40.26  ? 307  PHE   B HB2  1 
ATOM   16248 H HB3  . PHE   B  1 281 ? 82.159 -7.006  -67.176 0.00 39.80  ? 307  PHE   B HB3  1 
ATOM   16249 H HD1  . PHE   B  1 281 ? 80.595 -4.992  -66.896 0.00 39.80  ? 307  PHE   B HD1  1 
ATOM   16250 H HD2  . PHE   B  1 281 ? 79.479 -8.478  -69.068 0.00 41.45  ? 307  PHE   B HD2  1 
ATOM   16251 H HE1  . PHE   B  1 281 ? 78.231 -4.370  -66.693 0.00 39.77  ? 307  PHE   B HE1  1 
ATOM   16252 H HE2  . PHE   B  1 281 ? 77.115 -7.840  -68.856 0.00 41.41  ? 307  PHE   B HE2  1 
ATOM   16253 H HZ   . PHE   B  1 281 ? 76.490 -5.788  -67.672 0.00 39.68  ? 307  PHE   B HZ   1 
ATOM   16254 N N    . LYS   B  1 282 ? 84.270 -7.059  -70.622 1.00 32.20  ? 308  LYS   B N    1 
ATOM   16255 C CA   . LYS   B  1 282 ? 85.615 -7.567  -70.898 1.00 33.06  ? 308  LYS   B CA   1 
ATOM   16256 C C    . LYS   B  1 282 ? 86.719 -6.646  -70.369 1.00 32.95  ? 308  LYS   B C    1 
ATOM   16257 O O    . LYS   B  1 282 ? 87.743 -7.148  -69.900 1.00 33.70  ? 308  LYS   B O    1 
ATOM   16258 C CB   . LYS   B  1 282 ? 85.792 -7.793  -72.416 1.00 35.65  ? 308  LYS   B CB   1 
ATOM   16259 C CG   . LYS   B  1 282 ? 86.991 -8.642  -72.811 1.00 41.48  ? 308  LYS   B CG   1 
ATOM   16260 C CD   . LYS   B  1 282 ? 87.195 -8.600  -74.324 1.00 47.46  ? 308  LYS   B CD   1 
ATOM   16261 C CE   . LYS   B  1 282 ? 88.108 -9.690  -74.845 1.00 52.91  ? 308  LYS   B CE   1 
ATOM   16262 N NZ   . LYS   B  1 282 ? 87.353 -10.921 -75.224 1.00 56.11  ? 308  LYS   B NZ   1 
ATOM   16263 H H    . LYS   B  1 282 ? 83.725 -6.900  -71.462 0.00 43.34  ? 308  LYS   B H    1 
ATOM   16264 H HA   . LYS   B  1 282 ? 85.727 -8.533  -70.407 0.00 45.24  ? 308  LYS   B HA   1 
ATOM   16265 H HB2  . LYS   B  1 282 ? 84.908 -8.298  -72.802 0.00 48.62  ? 308  LYS   B HB2  1 
ATOM   16266 H HB3  . LYS   B  1 282 ? 85.901 -6.824  -72.900 0.00 48.58  ? 308  LYS   B HB3  1 
ATOM   16267 H HG2  . LYS   B  1 282 ? 87.896 -8.263  -72.340 0.00 56.54  ? 308  LYS   B HG2  1 
ATOM   16268 H HG3  . LYS   B  1 282 ? 86.814 -9.676  -72.517 0.00 56.61  ? 308  LYS   B HG3  1 
ATOM   16269 H HD2  . LYS   B  1 282 ? 86.226 -8.709  -74.809 0.00 63.93  ? 308  LYS   B HD2  1 
ATOM   16270 H HD3  . LYS   B  1 282 ? 87.637 -7.641  -74.591 0.00 64.08  ? 308  LYS   B HD3  1 
ATOM   16271 H HE2  . LYS   B  1 282 ? 88.630 -9.327  -75.728 0.00 71.82  ? 308  LYS   B HE2  1 
ATOM   16272 H HE3  . LYS   B  1 282 ? 88.823 -9.959  -74.069 0.00 71.62  ? 308  LYS   B HE3  1 
ATOM   16273 H HZ1  . LYS   B  1 282 ? 87.998 -11.640 -75.538 0.00 76.11  ? 308  LYS   B HZ1  1 
ATOM   16274 H HZ2  . LYS   B  1 282 ? 86.835 -11.271 -74.424 0.00 75.21  ? 308  LYS   B HZ2  1 
ATOM   16275 H HZ3  . LYS   B  1 282 ? 86.701 -10.715 -75.974 0.00 75.45  ? 308  LYS   B HZ3  1 
ATOM   16276 N N    . ASN   B  1 283 ? 86.531 -5.314  -70.453 1.00 31.64  ? 309  ASN   B N    1 
ATOM   16277 C CA   . ASN   B  1 283 ? 87.542 -4.360  -69.995 1.00 31.60  ? 309  ASN   B CA   1 
ATOM   16278 C C    . ASN   B  1 283 ? 87.071 -3.529  -68.799 1.00 30.37  ? 309  ASN   B C    1 
ATOM   16279 O O    . ASN   B  1 283 ? 87.531 -2.400  -68.653 1.00 29.92  ? 309  ASN   B O    1 
ATOM   16280 C CB   . ASN   B  1 283 ? 87.953 -3.447  -71.153 1.00 33.60  ? 309  ASN   B CB   1 
ATOM   16281 C CG   . ASN   B  1 283 ? 88.491 -4.204  -72.347 1.00 38.32  ? 309  ASN   B CG   1 
ATOM   16282 O OD1  . ASN   B  1 283 ? 89.298 -5.124  -72.217 1.00 40.19  ? 309  ASN   B OD1  1 
ATOM   16283 N ND2  . ASN   B  1 283 ? 88.083 -3.822  -73.541 1.00 39.57  ? 309  ASN   B ND2  1 
ATOM   16284 H H    . ASN   B  1 283 ? 85.703 -4.872  -70.839 0.00 42.67  ? 309  ASN   B H    1 
ATOM   16285 H HA   . ASN   B  1 283 ? 88.441 -4.882  -69.673 0.00 43.39  ? 309  ASN   B HA   1 
ATOM   16286 H HB2  . ASN   B  1 283 ? 87.083 -2.870  -71.460 0.00 45.25  ? 309  ASN   B HB2  1 
ATOM   16287 H HB3  . ASN   B  1 283 ? 88.746 -2.778  -70.824 0.00 45.74  ? 309  ASN   B HB3  1 
ATOM   16288 H HD21 . ASN   B  1 283 ? 88.426 -4.312  -74.361 0.00 53.91  ? 309  ASN   B HD21 1 
ATOM   16289 H HD22 . ASN   B  1 283 ? 87.440 -3.046  -73.650 0.00 53.05  ? 309  ASN   B HD22 1 
ATOM   16290 N N    . MET   B  1 284 ? 86.200 -4.103  -67.919 1.00 29.51  ? 310  MET   B N    1 
ATOM   16291 C CA   . MET   B  1 284 ? 85.722 -3.464  -66.686 1.00 29.78  ? 310  MET   B CA   1 
ATOM   16292 C C    . MET   B  1 284 ? 86.211 -4.325  -65.492 1.00 29.18  ? 310  MET   B C    1 
ATOM   16293 O O    . MET   B  1 284 ? 85.401 -4.974  -64.804 1.00 29.52  ? 310  MET   B O    1 
ATOM   16294 C CB   . MET   B  1 284 ? 84.179 -3.396  -66.645 1.00 31.14  ? 310  MET   B CB   1 
ATOM   16295 C CG   . MET   B  1 284 ? 83.558 -2.260  -67.354 1.00 34.15  ? 310  MET   B CG   1 
ATOM   16296 S SD   . MET   B  1 284 ? 81.772 -2.294  -67.025 1.00 33.75  ? 310  MET   B SD   1 
ATOM   16297 C CE   . MET   B  1 284 ? 81.217 -1.621  -68.525 1.00 33.62  ? 310  MET   B CE   1 
ATOM   16298 H H    . MET   B  1 284 ? 85.817 -5.036  -68.033 0.00 39.58  ? 310  MET   B H    1 
ATOM   16299 H HA   . MET   B  1 284 ? 86.122 -2.457  -66.584 0.00 39.20  ? 310  MET   B HA   1 
ATOM   16300 H HB2  . MET   B  1 284 ? 83.768 -4.319  -67.049 0.00 40.45  ? 310  MET   B HB2  1 
ATOM   16301 H HB3  . MET   B  1 284 ? 83.887 -3.282  -65.603 0.00 40.01  ? 310  MET   B HB3  1 
ATOM   16302 H HG2  . MET   B  1 284 ? 83.960 -1.320  -66.979 0.00 43.56  ? 310  MET   B HG2  1 
ATOM   16303 H HG3  . MET   B  1 284 ? 83.731 -2.355  -68.425 0.00 43.95  ? 310  MET   B HG3  1 
ATOM   16304 H HE1  . MET   B  1 284 ? 80.130 -1.563  -68.507 0.00 42.10  ? 310  MET   B HE1  1 
ATOM   16305 H HE2  . MET   B  1 284 ? 81.641 -0.623  -68.631 0.00 42.41  ? 310  MET   B HE2  1 
ATOM   16306 H HE3  . MET   B  1 284 ? 81.542 -2.257  -69.346 0.00 42.82  ? 310  MET   B HE3  1 
ATOM   16307 N N    . PRO   B  1 285 ? 87.525 -4.335  -65.209 1.00 28.33  ? 311  PRO   B N    1 
ATOM   16308 C CA   . PRO   B  1 285 ? 88.027 -5.187  -64.121 1.00 27.80  ? 311  PRO   B CA   1 
ATOM   16309 C C    . PRO   B  1 285 ? 87.631 -4.752  -62.721 1.00 27.49  ? 311  PRO   B C    1 
ATOM   16310 O O    . PRO   B  1 285 ? 87.719 -5.568  -61.812 1.00 27.93  ? 311  PRO   B O    1 
ATOM   16311 C CB   . PRO   B  1 285 ? 89.551 -5.140  -64.320 1.00 28.81  ? 311  PRO   B CB   1 
ATOM   16312 C CG   . PRO   B  1 285 ? 89.802 -3.837  -64.958 1.00 29.29  ? 311  PRO   B CG   1 
ATOM   16313 C CD   . PRO   B  1 285 ? 88.634 -3.635  -65.886 1.00 27.95  ? 311  PRO   B CD   1 
ATOM   16314 H HA   . PRO   B  1 285 ? 87.697 -6.214  -64.273 0.00 37.85  ? 311  PRO   B HA   1 
ATOM   16315 H HB2  . PRO   B  1 285 ? 90.054 -5.199  -63.356 0.00 39.69  ? 311  PRO   B HB2  1 
ATOM   16316 H HB3  . PRO   B  1 285 ? 89.866 -5.954  -64.971 0.00 40.01  ? 311  PRO   B HB3  1 
ATOM   16317 H HG2  . PRO   B  1 285 ? 89.833 -3.055  -64.201 0.00 39.84  ? 311  PRO   B HG2  1 
ATOM   16318 H HG3  . PRO   B  1 285 ? 90.738 -3.874  -65.515 0.00 40.59  ? 311  PRO   B HG3  1 
ATOM   16319 H HD2  . PRO   B  1 285 ? 88.408 -2.575  -65.986 0.00 37.80  ? 311  PRO   B HD2  1 
ATOM   16320 H HD3  . PRO   B  1 285 ? 88.838 -4.091  -66.855 0.00 38.43  ? 311  PRO   B HD3  1 
ATOM   16321 N N    . HIS   B  1 286 ? 87.198 -3.494  -62.536 1.00 26.53  ? 312  HIS   B N    1 
ATOM   16322 C CA   . HIS   B  1 286 ? 86.842 -2.966  -61.218 1.00 26.32  ? 312  HIS   B CA   1 
ATOM   16323 C C    . HIS   B  1 286 ? 85.325 -2.831  -60.987 1.00 25.68  ? 312  HIS   B C    1 
ATOM   16324 O O    . HIS   B  1 286 ? 84.955 -2.225  -59.983 1.00 26.80  ? 312  HIS   B O    1 
ATOM   16325 C CB   . HIS   B  1 286 ? 87.465 -1.570  -61.042 1.00 27.13  ? 312  HIS   B CB   1 
ATOM   16326 C CG   . HIS   B  1 286 ? 88.933 -1.497  -61.322 1.00 29.77  ? 312  HIS   B CG   1 
ATOM   16327 N ND1  . HIS   B  1 286 ? 89.868 -1.893  -60.382 1.00 31.90  ? 312  HIS   B ND1  1 
ATOM   16328 C CD2  . HIS   B  1 286 ? 89.585 -1.024  -62.414 1.00 31.01  ? 312  HIS   B CD2  1 
ATOM   16329 C CE1  . HIS   B  1 286 ? 91.052 -1.665  -60.932 1.00 32.80  ? 312  HIS   B CE1  1 
ATOM   16330 N NE2  . HIS   B  1 286 ? 90.929 -1.143  -62.155 1.00 32.60  ? 312  HIS   B NE2  1 
ATOM   16331 H H    . HIS   B  1 286 ? 87.092 -2.801  -63.270 0.00 35.21  ? 312  HIS   B H    1 
ATOM   16332 H HA   . HIS   B  1 286 ? 87.244 -3.602  -60.430 0.00 34.83  ? 312  HIS   B HA   1 
ATOM   16333 H HB2  . HIS   B  1 286 ? 86.964 -0.875  -61.715 0.00 35.36  ? 312  HIS   B HB2  1 
ATOM   16334 H HB3  . HIS   B  1 286 ? 87.328 -1.247  -60.011 0.00 35.39  ? 312  HIS   B HB3  1 
ATOM   16335 H HD1  . HIS   B  1 286 ? 89.686 -2.281  -59.461 0.00 42.25  ? 312  HIS   B HD1  1 
ATOM   16336 H HD2  . HIS   B  1 286 ? 89.135 -0.629  -63.311 0.00 41.06  ? 312  HIS   B HD2  1 
ATOM   16337 H HE1  . HIS   B  1 286 ? 91.995 -1.875  -60.454 0.00 44.40  ? 312  HIS   B HE1  1 
ATOM   16338 N N    . LEU   B  1 287 ? 84.432 -3.336  -61.890 1.00 24.38  ? 313  LEU   B N    1 
ATOM   16339 C CA   . LEU   B  1 287 ? 82.981 -3.141  -61.698 1.00 23.30  ? 313  LEU   B CA   1 
ATOM   16340 C C    . LEU   B  1 287 ? 82.525 -3.691  -60.351 1.00 22.81  ? 313  LEU   B C    1 
ATOM   16341 O O    . LEU   B  1 287 ? 82.774 -4.859  -60.054 1.00 22.42  ? 313  LEU   B O    1 
ATOM   16342 C CB   . LEU   B  1 287 ? 82.137 -3.756  -62.836 1.00 22.51  ? 313  LEU   B CB   1 
ATOM   16343 C CG   . LEU   B  1 287 ? 80.653 -3.328  -62.848 1.00 23.39  ? 313  LEU   B CG   1 
ATOM   16344 C CD1  . LEU   B  1 287 ? 80.488 -1.831  -63.172 1.00 24.16  ? 313  LEU   B CD1  1 
ATOM   16345 C CD2  . LEU   B  1 287 ? 79.853 -4.162  -63.824 1.00 23.82  ? 313  LEU   B CD2  1 
ATOM   16346 H H    . LEU   B  1 287 ? 84.669 -3.868  -62.721 0.00 31.83  ? 313  LEU   B H    1 
ATOM   16347 H HA   . LEU   B  1 287 ? 82.812 -2.067  -61.712 0.00 29.42  ? 313  LEU   B HA   1 
ATOM   16348 H HB2  . LEU   B  1 287 ? 82.565 -3.447  -63.786 0.00 28.93  ? 313  LEU   B HB2  1 
ATOM   16349 H HB3  . LEU   B  1 287 ? 82.170 -4.842  -62.753 0.00 28.92  ? 313  LEU   B HB3  1 
ATOM   16350 H HG   . LEU   B  1 287 ? 80.218 -3.495  -61.864 0.00 28.95  ? 313  LEU   B HG   1 
ATOM   16351 H HD11 . LEU   B  1 287 ? 79.453 -1.635  -63.445 0.00 29.57  ? 313  LEU   B HD11 1 
ATOM   16352 H HD12 . LEU   B  1 287 ? 80.741 -1.240  -62.294 0.00 29.72  ? 313  LEU   B HD12 1 
ATOM   16353 H HD13 . LEU   B  1 287 ? 81.147 -1.566  -63.999 0.00 30.16  ? 313  LEU   B HD13 1 
ATOM   16354 H HD21 . LEU   B  1 287 ? 78.816 -3.832  -63.814 0.00 29.43  ? 313  LEU   B HD21 1 
ATOM   16355 H HD22 . LEU   B  1 287 ? 80.274 -4.043  -64.821 0.00 30.08  ? 313  LEU   B HD22 1 
ATOM   16356 H HD23 . LEU   B  1 287 ? 79.904 -5.207  -63.522 0.00 29.98  ? 313  LEU   B HD23 1 
ATOM   16357 N N    . LYS   B  1 288 ? 81.920 -2.822  -59.530 1.00 22.81  ? 314  LYS   B N    1 
ATOM   16358 C CA   . LYS   B  1 288 ? 81.516 -3.122  -58.160 1.00 23.16  ? 314  LYS   B CA   1 
ATOM   16359 C C    . LYS   B  1 288 ? 79.998 -3.225  -57.962 1.00 22.70  ? 314  LYS   B C    1 
ATOM   16360 O O    . LYS   B  1 288 ? 79.562 -4.024  -57.122 1.00 22.71  ? 314  LYS   B O    1 
ATOM   16361 C CB   . LYS   B  1 288 ? 82.056 -2.003  -57.252 1.00 26.47  ? 314  LYS   B CB   1 
ATOM   16362 C CG   . LYS   B  1 288 ? 82.037 -2.335  -55.770 1.00 32.99  ? 314  LYS   B CG   1 
ATOM   16363 C CD   . LYS   B  1 288 ? 82.688 -1.235  -54.943 1.00 40.06  ? 314  LYS   B CD   1 
ATOM   16364 C CE   . LYS   B  1 288 ? 81.714 -0.124  -54.627 1.00 45.65  ? 314  LYS   B CE   1 
ATOM   16365 N NZ   . LYS   B  1 288 ? 82.362 0.983   -53.869 1.00 49.83  ? 314  LYS   B NZ   1 
ATOM   16366 H H    . LYS   B  1 288 ? 81.677 -1.874  -59.800 0.00 28.19  ? 314  LYS   B H    1 
ATOM   16367 H HA   . LYS   B  1 288 ? 81.965 -4.057  -57.831 0.00 28.88  ? 314  LYS   B HA   1 
ATOM   16368 H HB2  . LYS   B  1 288 ? 83.088 -1.805  -57.537 0.00 32.84  ? 314  LYS   B HB2  1 
ATOM   16369 H HB3  . LYS   B  1 288 ? 81.453 -1.109  -57.407 0.00 32.16  ? 314  LYS   B HB3  1 
ATOM   16370 H HG2  . LYS   B  1 288 ? 81.008 -2.441  -55.430 0.00 39.90  ? 314  LYS   B HG2  1 
ATOM   16371 H HG3  . LYS   B  1 288 ? 82.585 -3.261  -55.601 0.00 40.60  ? 314  LYS   B HG3  1 
ATOM   16372 H HD2  . LYS   B  1 288 ? 83.035 -1.659  -54.001 0.00 48.93  ? 314  LYS   B HD2  1 
ATOM   16373 H HD3  . LYS   B  1 288 ? 83.525 -0.805  -55.491 0.00 49.06  ? 314  LYS   B HD3  1 
ATOM   16374 H HE2  . LYS   B  1 288 ? 81.318 0.289   -55.554 0.00 54.83  ? 314  LYS   B HE2  1 
ATOM   16375 H HE3  . LYS   B  1 288 ? 80.906 -0.523  -54.017 0.00 54.72  ? 314  LYS   B HE3  1 
ATOM   16376 H HZ1  . LYS   B  1 288 ? 81.684 1.714   -53.676 0.00 59.76  ? 314  LYS   B HZ1  1 
ATOM   16377 H HZ2  . LYS   B  1 288 ? 82.728 0.632   -52.990 0.00 60.23  ? 314  LYS   B HZ2  1 
ATOM   16378 H HZ3  . LYS   B  1 288 ? 83.122 1.377   -54.413 0.00 60.33  ? 314  LYS   B HZ3  1 
ATOM   16379 N N    . VAL   B  1 289 ? 79.211 -2.357  -58.629 1.00 21.51  ? 315  VAL   B N    1 
ATOM   16380 C CA   . VAL   B  1 289 ? 77.752 -2.334  -58.483 1.00 22.13  ? 315  VAL   B CA   1 
ATOM   16381 C C    . VAL   B  1 289 ? 77.123 -2.392  -59.866 1.00 21.83  ? 315  VAL   B C    1 
ATOM   16382 O O    . VAL   B  1 289 ? 77.442 -1.566  -60.722 1.00 22.72  ? 315  VAL   B O    1 
ATOM   16383 C CB   . VAL   B  1 289 ? 77.263 -1.085  -57.693 1.00 23.25  ? 315  VAL   B CB   1 
ATOM   16384 C CG1  . VAL   B  1 289 ? 75.735 -1.093  -57.522 1.00 23.98  ? 315  VAL   B CG1  1 
ATOM   16385 C CG2  . VAL   B  1 289 ? 77.969 -0.983  -56.337 1.00 23.70  ? 315  VAL   B CG2  1 
ATOM   16386 H H    . VAL   B  1 289 ? 79.557 -1.652  -59.272 0.00 25.85  ? 315  VAL   B H    1 
ATOM   16387 H HA   . VAL   B  1 289 ? 77.421 -3.213  -57.932 0.00 26.08  ? 315  VAL   B HA   1 
ATOM   16388 H HB   . VAL   B  1 289 ? 77.522 -0.193  -58.262 0.00 27.04  ? 315  VAL   B HB   1 
ATOM   16389 H HG11 . VAL   B  1 289 ? 75.457 -0.379  -56.749 0.00 27.24  ? 315  VAL   B HG11 1 
ATOM   16390 H HG12 . VAL   B  1 289 ? 75.269 -0.797  -58.461 0.00 27.42  ? 315  VAL   B HG12 1 
ATOM   16391 H HG13 . VAL   B  1 289 ? 75.412 -2.095  -57.244 0.00 27.51  ? 315  VAL   B HG13 1 
ATOM   16392 H HG21 . VAL   B  1 289 ? 77.514 -0.185  -55.752 0.00 27.36  ? 315  VAL   B HG21 1 
ATOM   16393 H HG22 . VAL   B  1 289 ? 77.881 -1.933  -55.812 0.00 27.70  ? 315  VAL   B HG22 1 
ATOM   16394 H HG23 . VAL   B  1 289 ? 79.020 -0.751  -56.503 0.00 27.93  ? 315  VAL   B HG23 1 
ATOM   16395 N N    . LEU   B  1 290 ? 76.260 -3.392  -60.090 1.00 20.68  ? 316  LEU   B N    1 
ATOM   16396 C CA   . LEU   B  1 290 ? 75.576 -3.586  -61.364 1.00 20.72  ? 316  LEU   B CA   1 
ATOM   16397 C C    . LEU   B  1 290 ? 74.074 -3.646  -61.081 1.00 21.62  ? 316  LEU   B C    1 
ATOM   16398 O O    . LEU   B  1 290 ? 73.600 -4.546  -60.381 1.00 22.21  ? 316  LEU   B O    1 
ATOM   16399 C CB   . LEU   B  1 290 ? 76.063 -4.879  -62.050 1.00 20.61  ? 316  LEU   B CB   1 
ATOM   16400 C CG   . LEU   B  1 290 ? 75.411 -5.244  -63.393 1.00 22.15  ? 316  LEU   B CG   1 
ATOM   16401 C CD1  . LEU   B  1 290 ? 75.437 -4.070  -64.387 1.00 22.36  ? 316  LEU   B CD1  1 
ATOM   16402 C CD2  . LEU   B  1 290 ? 76.074 -6.467  -64.000 1.00 22.41  ? 316  LEU   B CD2  1 
ATOM   16403 H H    . LEU   B  1 290 ? 76.010 -4.097  -59.404 0.00 24.28  ? 316  LEU   B H    1 
ATOM   16404 H HA   . LEU   B  1 290 ? 75.776 -2.745  -62.025 0.00 24.42  ? 316  LEU   B HA   1 
ATOM   16405 H HB2  . LEU   B  1 290 ? 77.133 -4.785  -62.228 0.00 25.05  ? 316  LEU   B HB2  1 
ATOM   16406 H HB3  . LEU   B  1 290 ? 75.884 -5.712  -61.371 0.00 24.78  ? 316  LEU   B HB3  1 
ATOM   16407 H HG   . LEU   B  1 290 ? 74.371 -5.508  -63.211 0.00 26.55  ? 316  LEU   B HG   1 
ATOM   16408 H HD11 . LEU   B  1 290 ? 75.122 -4.427  -65.366 0.00 27.17  ? 316  LEU   B HD11 1 
ATOM   16409 H HD12 . LEU   B  1 290 ? 74.749 -3.296  -64.045 0.00 26.60  ? 316  LEU   B HD12 1 
ATOM   16410 H HD13 . LEU   B  1 290 ? 76.448 -3.670  -64.442 0.00 27.15  ? 316  LEU   B HD13 1 
ATOM   16411 H HD21 . LEU   B  1 290 ? 75.624 -6.684  -64.967 0.00 27.76  ? 316  LEU   B HD21 1 
ATOM   16412 H HD22 . LEU   B  1 290 ? 77.138 -6.267  -64.122 0.00 27.86  ? 316  LEU   B HD22 1 
ATOM   16413 H HD23 . LEU   B  1 290 ? 75.933 -7.314  -63.329 0.00 27.66  ? 316  LEU   B HD23 1 
ATOM   16414 N N    . ASP   B  1 291 ? 73.348 -2.640  -61.551 1.00 21.60  ? 317  ASP   B N    1 
ATOM   16415 C CA   . ASP   B  1 291 ? 71.914 -2.543  -61.344 1.00 22.49  ? 317  ASP   B CA   1 
ATOM   16416 C C    . ASP   B  1 291 ? 71.219 -2.945  -62.647 1.00 22.33  ? 317  ASP   B C    1 
ATOM   16417 O O    . ASP   B  1 291 ? 71.429 -2.311  -63.693 1.00 22.77  ? 317  ASP   B O    1 
ATOM   16418 C CB   . ASP   B  1 291 ? 71.558 -1.102  -60.923 1.00 25.14  ? 317  ASP   B CB   1 
ATOM   16419 C CG   . ASP   B  1 291 ? 70.340 -1.006  -60.055 1.00 32.80  ? 317  ASP   B CG   1 
ATOM   16420 O OD1  . ASP   B  1 291 ? 69.459 -1.886  -60.176 1.00 33.21  ? 317  ASP   B OD1  1 
ATOM   16421 O OD2  . ASP   B  1 291 ? 70.238 -0.029  -59.276 1.00 35.38  ? 317  ASP   B OD2  1 
ATOM   16422 H H    . ASP   B  1 291 ? 73.723 -1.860  -62.081 0.00 24.87  ? 317  ASP   B H    1 
ATOM   16423 H HA   . ASP   B  1 291 ? 71.618 -3.235  -60.558 0.00 25.48  ? 317  ASP   B HA   1 
ATOM   16424 H HB2  . ASP   B  1 291 ? 72.397 -0.668  -60.380 0.00 28.40  ? 317  ASP   B HB2  1 
ATOM   16425 H HB3  . ASP   B  1 291 ? 71.341 -0.509  -61.809 0.00 28.41  ? 317  ASP   B HB3  1 
ATOM   16426 N N    . LEU   B  1 292 ? 70.446 -4.045  -62.600 1.00 21.13  ? 318  LEU   B N    1 
ATOM   16427 C CA   . LEU   B  1 292 ? 69.704 -4.579  -63.748 1.00 20.38  ? 318  LEU   B CA   1 
ATOM   16428 C C    . LEU   B  1 292 ? 68.236 -4.834  -63.382 1.00 19.74  ? 318  LEU   B C    1 
ATOM   16429 O O    . LEU   B  1 292 ? 67.617 -5.788  -63.876 1.00 19.55  ? 318  LEU   B O    1 
ATOM   16430 C CB   . LEU   B  1 292 ? 70.351 -5.892  -64.200 1.00 20.72  ? 318  LEU   B CB   1 
ATOM   16431 C CG   . LEU   B  1 292 ? 71.748 -5.789  -64.815 1.00 23.05  ? 318  LEU   B CG   1 
ATOM   16432 C CD1  . LEU   B  1 292 ? 72.434 -7.156  -64.779 1.00 23.56  ? 318  LEU   B CD1  1 
ATOM   16433 C CD2  . LEU   B  1 292 ? 71.675 -5.298  -66.247 1.00 23.02  ? 318  LEU   B CD2  1 
ATOM   16434 H H    . LEU   B  1 292 ? 70.306 -4.602  -61.763 0.00 24.07  ? 318  LEU   B H    1 
ATOM   16435 H HA   . LEU   B  1 292 ? 69.706 -3.863  -64.566 0.00 23.50  ? 318  LEU   B HA   1 
ATOM   16436 H HB2  . LEU   B  1 292 ? 70.422 -6.555  -63.340 0.00 24.31  ? 318  LEU   B HB2  1 
ATOM   16437 H HB3  . LEU   B  1 292 ? 69.728 -6.355  -64.963 0.00 24.51  ? 318  LEU   B HB3  1 
ATOM   16438 H HG   . LEU   B  1 292 ? 72.351 -5.082  -64.247 0.00 27.32  ? 318  LEU   B HG   1 
ATOM   16439 H HD11 . LEU   B  1 292 ? 73.366 -7.098  -65.339 0.00 28.83  ? 318  LEU   B HD11 1 
ATOM   16440 H HD12 . LEU   B  1 292 ? 72.640 -7.418  -63.743 0.00 28.42  ? 318  LEU   B HD12 1 
ATOM   16441 H HD13 . LEU   B  1 292 ? 71.773 -7.896  -65.227 0.00 28.69  ? 318  LEU   B HD13 1 
ATOM   16442 H HD21 . LEU   B  1 292 ? 72.676 -5.026  -66.579 0.00 27.85  ? 318  LEU   B HD21 1 
ATOM   16443 H HD22 . LEU   B  1 292 ? 71.296 -6.108  -66.869 0.00 27.92  ? 318  LEU   B HD22 1 
ATOM   16444 H HD23 . LEU   B  1 292 ? 71.010 -4.440  -66.323 0.00 27.38  ? 318  LEU   B HD23 1 
ATOM   16445 N N    . GLU   B  1 293 ? 67.661 -3.951  -62.578 1.00 19.79  ? 319  GLU   B N    1 
ATOM   16446 C CA   . GLU   B  1 293 ? 66.268 -4.092  -62.155 1.00 20.19  ? 319  GLU   B CA   1 
ATOM   16447 C C    . GLU   B  1 293 ? 65.320 -3.776  -63.291 1.00 20.19  ? 319  GLU   B C    1 
ATOM   16448 O O    . GLU   B  1 293 ? 65.679 -3.026  -64.178 1.00 20.73  ? 319  GLU   B O    1 
ATOM   16449 C CB   . GLU   B  1 293 ? 65.944 -3.107  -61.020 1.00 22.33  ? 319  GLU   B CB   1 
ATOM   16450 C CG   . GLU   B  1 293 ? 66.852 -3.205  -59.826 1.00 26.94  ? 319  GLU   B CG   1 
ATOM   16451 C CD   . GLU   B  1 293 ? 66.659 -2.032  -58.889 1.00 31.20  ? 319  GLU   B CD   1 
ATOM   16452 O OE1  . GLU   B  1 293 ? 67.445 -1.063  -58.996 1.00 30.92  ? 319  GLU   B OE1  1 
ATOM   16453 O OE2  . GLU   B  1 293 ? 65.715 -2.067  -58.068 1.00 34.85  ? 319  GLU   B OE2  1 
ATOM   16454 H H    . GLU   B  1 293 ? 68.104 -3.094  -62.263 0.00 21.95  ? 319  GLU   B H    1 
ATOM   16455 H HA   . GLU   B  1 293 ? 66.080 -5.107  -61.809 0.00 22.46  ? 319  GLU   B HA   1 
ATOM   16456 H HB2  . GLU   B  1 293 ? 66.021 -2.092  -61.407 0.00 24.41  ? 319  GLU   B HB2  1 
ATOM   16457 H HB3  . GLU   B  1 293 ? 64.927 -3.293  -60.680 0.00 24.35  ? 319  GLU   B HB3  1 
ATOM   16458 H HG2  . GLU   B  1 293 ? 66.663 -4.133  -59.291 0.00 29.99  ? 319  GLU   B HG2  1 
ATOM   16459 H HG3  . GLU   B  1 293 ? 67.894 -3.182  -60.140 0.00 30.13  ? 319  GLU   B HG3  1 
ATOM   16460 N N    . PHE   B  1 294 ? 64.079 -4.264  -63.214 1.00 19.09  ? 320  PHE   B N    1 
ATOM   16461 C CA   . PHE   B  1 294 ? 63.039 -3.916  -64.173 1.00 19.52  ? 320  PHE   B CA   1 
ATOM   16462 C C    . PHE   B  1 294 ? 63.425 -4.210  -65.610 1.00 20.35  ? 320  PHE   B C    1 
ATOM   16463 O O    . PHE   B  1 294 ? 63.206 -3.394  -66.497 1.00 20.97  ? 320  PHE   B O    1 
ATOM   16464 C CB   . PHE   B  1 294 ? 62.604 -2.443  -63.982 1.00 18.75  ? 320  PHE   B CB   1 
ATOM   16465 C CG   . PHE   B  1 294 ? 61.950 -2.207  -62.632 1.00 18.95  ? 320  PHE   B CG   1 
ATOM   16466 C CD1  . PHE   B  1 294 ? 60.621 -2.548  -62.418 1.00 19.56  ? 320  PHE   B CD1  1 
ATOM   16467 C CD2  . PHE   B  1 294 ? 62.662 -1.643  -61.586 1.00 18.88  ? 320  PHE   B CD2  1 
ATOM   16468 C CE1  . PHE   B  1 294 ? 60.017 -2.318  -61.180 1.00 20.21  ? 320  PHE   B CE1  1 
ATOM   16469 C CE2  . PHE   B  1 294 ? 62.056 -1.411  -60.352 1.00 19.42  ? 320  PHE   B CE2  1 
ATOM   16470 C CZ   . PHE   B  1 294 ? 60.743 -1.756  -60.154 1.00 19.25  ? 320  PHE   B CZ   1 
ATOM   16471 H H    . PHE   B  1 294 ? 63.768 -4.905  -62.492 0.00 21.02  ? 320  PHE   B H    1 
ATOM   16472 H HA   . PHE   B  1 294 ? 62.171 -4.537  -63.958 0.00 21.69  ? 320  PHE   B HA   1 
ATOM   16473 H HB2  . PHE   B  1 294 ? 63.468 -1.786  -64.065 0.00 20.41  ? 320  PHE   B HB2  1 
ATOM   16474 H HB3  . PHE   B  1 294 ? 61.863 -2.185  -64.737 0.00 20.55  ? 320  PHE   B HB3  1 
ATOM   16475 H HD1  . PHE   B  1 294 ? 60.047 -2.986  -63.219 0.00 21.22  ? 320  PHE   B HD1  1 
ATOM   16476 H HD2  . PHE   B  1 294 ? 63.694 -1.367  -61.728 0.00 20.02  ? 320  PHE   B HD2  1 
ATOM   16477 H HE1  . PHE   B  1 294 ? 58.987 -2.585  -61.026 0.00 21.43  ? 320  PHE   B HE1  1 
ATOM   16478 H HE2  . PHE   B  1 294 ? 62.624 -0.973  -59.548 0.00 20.13  ? 320  PHE   B HE2  1 
ATOM   16479 H HZ   . PHE   B  1 294 ? 60.280 -1.584  -59.198 0.00 19.82  ? 320  PHE   B HZ   1 
ATOM   16480 N N    . ASN   B  1 295 ? 64.000 -5.392  -65.830 1.00 19.91  ? 321  ASN   B N    1 
ATOM   16481 C CA   . ASN   B  1 295 ? 64.350 -5.884  -67.154 1.00 19.74  ? 321  ASN   B CA   1 
ATOM   16482 C C    . ASN   B  1 295 ? 63.592 -7.206  -67.382 1.00 20.52  ? 321  ASN   B C    1 
ATOM   16483 O O    . ASN   B  1 295 ? 62.621 -7.467  -66.670 1.00 20.76  ? 321  ASN   B O    1 
ATOM   16484 C CB   . ASN   B  1 295 ? 65.900 -6.028  -67.254 1.00 20.19  ? 321  ASN   B CB   1 
ATOM   16485 C CG   . ASN   B  1 295 ? 66.665 -4.754  -67.389 1.00 20.85  ? 321  ASN   B CG   1 
ATOM   16486 O OD1  . ASN   B  1 295 ? 67.594 -4.457  -66.620 1.00 22.55  ? 321  ASN   B OD1  1 
ATOM   16487 N ND2  . ASN   B  1 295 ? 66.282 -3.940  -68.322 1.00 18.36  ? 321  ASN   B ND2  1 
ATOM   16488 H H    . ASN   B  1 295 ? 64.230 -6.053  -65.096 0.00 22.88  ? 321  ASN   B H    1 
ATOM   16489 H HA   . ASN   B  1 295 ? 63.992 -5.200  -67.921 0.00 23.24  ? 321  ASN   B HA   1 
ATOM   16490 H HB2  . ASN   B  1 295 ? 66.263 -6.550  -66.370 0.00 23.82  ? 321  ASN   B HB2  1 
ATOM   16491 H HB3  . ASN   B  1 295 ? 66.150 -6.588  -68.152 0.00 24.31  ? 321  ASN   B HB3  1 
ATOM   16492 H HD21 . ASN   B  1 295 ? 66.863 -3.128  -68.478 0.00 21.56  ? 321  ASN   B HD21 1 
ATOM   16493 H HD22 . ASN   B  1 295 ? 65.464 -4.106  -68.898 0.00 21.74  ? 321  ASN   B HD22 1 
ATOM   16494 N N    . TYR   B  1 296 ? 63.971 -8.018  -68.380 1.00 21.45  ? 322  TYR   B N    1 
ATOM   16495 C CA   . TYR   B  1 296 ? 63.324 -9.298  -68.662 1.00 22.61  ? 322  TYR   B CA   1 
ATOM   16496 C C    . TYR   B  1 296 ? 64.422 -10.377 -68.618 1.00 22.34  ? 322  TYR   B C    1 
ATOM   16497 O O    . TYR   B  1 296 ? 64.592 -11.151 -69.560 1.00 22.26  ? 322  TYR   B O    1 
ATOM   16498 C CB   . TYR   B  1 296 ? 62.703 -9.232  -70.055 1.00 23.17  ? 322  TYR   B CB   1 
ATOM   16499 C CG   . TYR   B  1 296 ? 61.676 -8.136  -70.239 1.00 24.74  ? 322  TYR   B CG   1 
ATOM   16500 C CD1  . TYR   B  1 296 ? 60.393 -8.262  -69.720 1.00 26.14  ? 322  TYR   B CD1  1 
ATOM   16501 C CD2  . TYR   B  1 296 ? 61.977 -6.990  -70.959 1.00 25.21  ? 322  TYR   B CD2  1 
ATOM   16502 C CE1  . TYR   B  1 296 ? 59.437 -7.269  -69.911 1.00 27.26  ? 322  TYR   B CE1  1 
ATOM   16503 C CE2  . TYR   B  1 296 ? 61.025 -6.007  -71.179 1.00 26.33  ? 322  TYR   B CE2  1 
ATOM   16504 C CZ   . TYR   B  1 296 ? 59.754 -6.144  -70.652 1.00 27.73  ? 322  TYR   B CZ   1 
ATOM   16505 O OH   . TYR   B  1 296 ? 58.795 -5.183  -70.897 1.00 28.89  ? 322  TYR   B OH   1 
ATOM   16506 H H    . TYR   B  1 296 ? 64.705 -7.808  -69.048 0.00 26.27  ? 322  TYR   B H    1 
ATOM   16507 H HA   . TYR   B  1 296 ? 62.553 -9.547  -67.934 0.00 27.67  ? 322  TYR   B HA   1 
ATOM   16508 H HB2  . TYR   B  1 296 ? 63.542 -8.981  -70.697 0.00 29.10  ? 322  TYR   B HB2  1 
ATOM   16509 H HB3  . TYR   B  1 296 ? 62.259 -10.188 -70.328 0.00 29.26  ? 322  TYR   B HB3  1 
ATOM   16510 H HD1  . TYR   B  1 296 ? 60.136 -9.141  -69.155 0.00 32.12  ? 322  TYR   B HD1  1 
ATOM   16511 H HD2  . TYR   B  1 296 ? 62.956 -6.873  -71.393 0.00 31.20  ? 322  TYR   B HD2  1 
ATOM   16512 H HE1  . TYR   B  1 296 ? 58.443 -7.393  -69.516 0.00 33.15  ? 322  TYR   B HE1  1 
ATOM   16513 H HE2  . TYR   B  1 296 ? 61.283 -5.137  -71.756 0.00 32.25  ? 322  TYR   B HE2  1 
ATOM   16514 H HH   . TYR   B  1 296 ? 59.181 -4.407  -71.382 0.00 35.05  ? 322  TYR   B HH   1 
ATOM   16515 N N    . LEU   B  1 297 ? 65.158 -10.429 -67.503 1.00 22.21  ? 323  LEU   B N    1 
ATOM   16516 C CA   . LEU   B  1 297 ? 66.333 -11.292 -67.396 1.00 22.54  ? 323  LEU   B CA   1 
ATOM   16517 C C    . LEU   B  1 297 ? 66.148 -12.634 -66.677 1.00 23.22  ? 323  LEU   B C    1 
ATOM   16518 O O    . LEU   B  1 297 ? 67.162 -13.188 -66.280 1.00 23.47  ? 323  LEU   B O    1 
ATOM   16519 C CB   . LEU   B  1 297 ? 67.463 -10.491 -66.723 1.00 22.00  ? 323  LEU   B CB   1 
ATOM   16520 C CG   . LEU   B  1 297 ? 67.891 -9.225  -67.470 1.00 22.18  ? 323  LEU   B CG   1 
ATOM   16521 C CD1  . LEU   B  1 297 ? 68.750 -8.345  -66.576 1.00 22.40  ? 323  LEU   B CD1  1 
ATOM   16522 C CD2  . LEU   B  1 297 ? 68.622 -9.577  -68.803 1.00 22.53  ? 323  LEU   B CD2  1 
ATOM   16523 H H    . LEU   B  1 297 ? 64.963 -9.892  -66.663 0.00 27.08  ? 323  LEU   B H    1 
ATOM   16524 H HA   . LEU   B  1 297 ? 66.677 -11.554 -68.394 0.00 28.62  ? 323  LEU   B HA   1 
ATOM   16525 H HB2  . LEU   B  1 297 ? 67.131 -10.190 -65.730 0.00 26.88  ? 323  LEU   B HB2  1 
ATOM   16526 H HB3  . LEU   B  1 297 ? 68.355 -11.109 -66.635 0.00 27.54  ? 323  LEU   B HB3  1 
ATOM   16527 H HG   . LEU   B  1 297 ? 67.004 -8.651  -67.730 0.00 27.19  ? 323  LEU   B HG   1 
ATOM   16528 H HD11 . LEU   B  1 297 ? 69.220 -7.567  -67.175 0.00 27.29  ? 323  LEU   B HD11 1 
ATOM   16529 H HD12 . LEU   B  1 297 ? 68.112 -7.890  -65.820 0.00 26.88  ? 323  LEU   B HD12 1 
ATOM   16530 H HD13 . LEU   B  1 297 ? 69.507 -8.962  -66.094 0.00 27.42  ? 323  LEU   B HD13 1 
ATOM   16531 H HD21 . LEU   B  1 297 ? 69.044 -8.666  -69.225 0.00 28.27  ? 323  LEU   B HD21 1 
ATOM   16532 H HD22 . LEU   B  1 297 ? 69.421 -10.283 -68.583 0.00 28.60  ? 323  LEU   B HD22 1 
ATOM   16533 H HD23 . LEU   B  1 297 ? 67.918 -10.004 -69.515 0.00 28.60  ? 323  LEU   B HD23 1 
ATOM   16534 N N    . VAL   B  1 298 ? 64.928 -13.218 -66.592 1.00 23.00  ? 324  VAL   B N    1 
ATOM   16535 C CA   . VAL   B  1 298 ? 64.772 -14.558 -65.980 1.00 23.69  ? 324  VAL   B CA   1 
ATOM   16536 C C    . VAL   B  1 298 ? 65.659 -15.603 -66.723 1.00 24.51  ? 324  VAL   B C    1 
ATOM   16537 O O    . VAL   B  1 298 ? 66.339 -16.395 -66.066 1.00 24.80  ? 324  VAL   B O    1 
ATOM   16538 C CB   . VAL   B  1 298 ? 63.274 -15.005 -65.905 1.00 24.35  ? 324  VAL   B CB   1 
ATOM   16539 C CG1  . VAL   B  1 298 ? 63.123 -16.526 -65.730 1.00 25.11  ? 324  VAL   B CG1  1 
ATOM   16540 C CG2  . VAL   B  1 298 ? 62.535 -14.260 -64.791 1.00 23.96  ? 324  VAL   B CG2  1 
ATOM   16541 H H    . VAL   B  1 298 ? 64.060 -12.803 -66.918 0.00 28.92  ? 324  VAL   B H    1 
ATOM   16542 H HA   . VAL   B  1 298 ? 65.170 -14.501 -64.967 0.00 29.89  ? 324  VAL   B HA   1 
ATOM   16543 H HB   . VAL   B  1 298 ? 62.786 -14.747 -66.844 0.00 31.11  ? 324  VAL   B HB   1 
ATOM   16544 H HG11 . VAL   B  1 298 ? 62.102 -16.740 -65.418 0.00 32.32  ? 324  VAL   B HG11 1 
ATOM   16545 H HG12 . VAL   B  1 298 ? 63.315 -17.027 -66.677 0.00 32.87  ? 324  VAL   B HG12 1 
ATOM   16546 H HG13 . VAL   B  1 298 ? 63.819 -16.874 -64.968 0.00 32.36  ? 324  VAL   B HG13 1 
ATOM   16547 H HG21 . VAL   B  1 298 ? 61.482 -14.537 -64.815 0.00 29.92  ? 324  VAL   B HG21 1 
ATOM   16548 H HG22 . VAL   B  1 298 ? 62.970 -14.538 -63.833 0.00 29.74  ? 324  VAL   B HG22 1 
ATOM   16549 H HG23 . VAL   B  1 298 ? 62.640 -13.188 -64.952 0.00 29.55  ? 324  VAL   B HG23 1 
ATOM   16550 N N    . GLY   B  1 299 ? 65.644 -15.578 -68.057 1.00 24.31  ? 325  GLY   B N    1 
ATOM   16551 C CA   . GLY   B  1 299 ? 66.476 -16.468 -68.867 1.00 25.61  ? 325  GLY   B CA   1 
ATOM   16552 C C    . GLY   B  1 299 ? 67.959 -16.258 -68.604 1.00 26.19  ? 325  GLY   B C    1 
ATOM   16553 O O    . GLY   B  1 299 ? 68.693 -17.234 -68.392 1.00 27.28  ? 325  GLY   B O    1 
ATOM   16554 H H    . GLY   B  1 299 ? 65.065 -14.955 -68.610 0.00 31.83  ? 325  GLY   B H    1 
ATOM   16555 H HA2  . GLY   B  1 299 ? 66.228 -17.504 -68.641 0.00 34.50  ? 325  GLY   B HA2  1 
ATOM   16556 H HA3  . GLY   B  1 299 ? 66.282 -16.288 -69.923 0.00 34.42  ? 325  GLY   B HA3  1 
ATOM   16557 N N    . GLU   B  1 300 ? 68.407 -14.991 -68.559 1.00 25.09  ? 326  GLU   B N    1 
ATOM   16558 C CA   . GLU   B  1 300 ? 69.809 -14.664 -68.257 1.00 25.39  ? 326  GLU   B CA   1 
ATOM   16559 C C    . GLU   B  1 300 ? 70.207 -15.038 -66.824 1.00 25.34  ? 326  GLU   B C    1 
ATOM   16560 O O    . GLU   B  1 300 ? 71.379 -15.311 -66.580 1.00 26.02  ? 326  GLU   B O    1 
ATOM   16561 C CB   . GLU   B  1 300 ? 70.121 -13.169 -68.505 1.00 27.65  ? 326  GLU   B CB   1 
ATOM   16562 C CG   . GLU   B  1 300 ? 70.441 -12.818 -69.951 1.00 33.63  ? 326  GLU   B CG   1 
ATOM   16563 C CD   . GLU   B  1 300 ? 71.792 -13.281 -70.463 1.00 41.17  ? 326  GLU   B CD   1 
ATOM   16564 O OE1  . GLU   B  1 300 ? 72.575 -13.869 -69.681 1.00 43.61  ? 326  GLU   B OE1  1 
ATOM   16565 O OE2  . GLU   B  1 300 ? 72.076 -13.028 -71.654 1.00 42.21  ? 326  GLU   B OE2  1 
ATOM   16566 H H    . GLU   B  1 300 ? 67.822 -14.181 -68.742 0.00 32.80  ? 326  GLU   B H    1 
ATOM   16567 H HA   . GLU   B  1 300 ? 70.439 -15.268 -68.908 0.00 33.97  ? 326  GLU   B HA   1 
ATOM   16568 H HB2  . GLU   B  1 300 ? 69.261 -12.573 -68.206 0.00 35.35  ? 326  GLU   B HB2  1 
ATOM   16569 H HB3  . GLU   B  1 300 ? 70.976 -12.886 -67.892 0.00 35.62  ? 326  GLU   B HB3  1 
ATOM   16570 H HG2  . GLU   B  1 300 ? 69.682 -13.270 -70.588 0.00 43.52  ? 326  GLU   B HG2  1 
ATOM   16571 H HG3  . GLU   B  1 300 ? 70.412 -11.736 -70.069 0.00 42.95  ? 326  GLU   B HG3  1 
ATOM   16572 N N    . ILE   B  1 301 ? 69.279 -14.986 -65.870 1.00 24.90  ? 327  ILE   B N    1 
ATOM   16573 C CA   . ILE   B  1 301 ? 69.578 -15.398 -64.499 1.00 24.84  ? 327  ILE   B CA   1 
ATOM   16574 C C    . ILE   B  1 301 ? 69.828 -16.915 -64.472 1.00 25.59  ? 327  ILE   B C    1 
ATOM   16575 O O    . ILE   B  1 301 ? 70.657 -17.370 -63.692 1.00 26.37  ? 327  ILE   B O    1 
ATOM   16576 C CB   . ILE   B  1 301 ? 68.469 -14.955 -63.498 1.00 24.00  ? 327  ILE   B CB   1 
ATOM   16577 C CG1  . ILE   B  1 301 ? 68.463 -13.410 -63.351 1.00 24.06  ? 327  ILE   B CG1  1 
ATOM   16578 C CG2  . ILE   B  1 301 ? 68.690 -15.616 -62.126 1.00 24.34  ? 327  ILE   B CG2  1 
ATOM   16579 C CD1  . ILE   B  1 301 ? 67.191 -12.797 -62.722 1.00 23.83  ? 327  ILE   B CD1  1 
ATOM   16580 H H    . ILE   B  1 301 ? 68.332 -14.641 -65.994 0.00 32.03  ? 327  ILE   B H    1 
ATOM   16581 H HA   . ILE   B  1 301 ? 70.502 -14.913 -64.184 0.00 31.95  ? 327  ILE   B HA   1 
ATOM   16582 H HB   . ILE   B  1 301 ? 67.500 -15.274 -63.880 0.00 30.54  ? 327  ILE   B HB   1 
ATOM   16583 H HG12 . ILE   B  1 301 ? 69.313 -13.126 -62.734 0.00 29.87  ? 327  ILE   B HG12 1 
ATOM   16584 H HG13 . ILE   B  1 301 ? 68.573 -12.963 -64.338 0.00 30.06  ? 327  ILE   B HG13 1 
ATOM   16585 H HG21 . ILE   B  1 301 ? 68.119 -15.086 -61.366 0.00 30.41  ? 327  ILE   B HG21 1 
ATOM   16586 H HG22 . ILE   B  1 301 ? 68.346 -16.649 -62.161 0.00 31.20  ? 327  ILE   B HG22 1 
ATOM   16587 H HG23 . ILE   B  1 301 ? 69.751 -15.583 -61.881 0.00 30.97  ? 327  ILE   B HG23 1 
ATOM   16588 H HD11 . ILE   B  1 301 ? 67.199 -11.721 -62.894 0.00 28.87  ? 327  ILE   B HD11 1 
ATOM   16589 H HD12 . ILE   B  1 301 ? 66.311 -13.244 -63.185 0.00 29.31  ? 327  ILE   B HD12 1 
ATOM   16590 H HD13 . ILE   B  1 301 ? 67.185 -12.990 -61.651 0.00 29.00  ? 327  ILE   B HD13 1 
ATOM   16591 N N    . ALA   B  1 302 ? 69.126 -17.695 -65.303 1.00 26.34  ? 328  ALA   B N    1 
ATOM   16592 C CA   . ALA   B  1 302 ? 69.322 -19.143 -65.378 1.00 27.87  ? 328  ALA   B CA   1 
ATOM   16593 C C    . ALA   B  1 302 ? 70.590 -19.556 -66.167 1.00 29.76  ? 328  ALA   B C    1 
ATOM   16594 O O    . ALA   B  1 302 ? 71.078 -20.660 -65.949 1.00 29.71  ? 328  ALA   B O    1 
ATOM   16595 C CB   . ALA   B  1 302 ? 68.098 -19.787 -66.027 1.00 27.95  ? 328  ALA   B CB   1 
ATOM   16596 H H    . ALA   B  1 302 ? 68.402 -17.362 -65.932 0.00 34.81  ? 328  ALA   B H    1 
ATOM   16597 H HA   . ALA   B  1 302 ? 69.403 -19.548 -64.370 0.00 37.32  ? 328  ALA   B HA   1 
ATOM   16598 H HB1  . ALA   B  1 302 ? 68.226 -20.868 -66.028 0.00 38.26  ? 328  ALA   B HB1  1 
ATOM   16599 H HB2  . ALA   B  1 302 ? 67.210 -19.516 -65.458 0.00 37.36  ? 328  ALA   B HB2  1 
ATOM   16600 H HB3  . ALA   B  1 302 ? 68.008 -19.424 -67.050 0.00 37.86  ? 328  ALA   B HB3  1 
ATOM   16601 N N    . SER   B  1 303 ? 71.104 -18.720 -67.092 1.00 31.81  ? 329  SER   B N    1 
ATOM   16602 C CA   . SER   B  1 303 ? 72.237 -19.130 -67.945 1.00 34.74  ? 329  SER   B CA   1 
ATOM   16603 C C    . SER   B  1 303 ? 73.187 -17.986 -68.326 1.00 36.75  ? 329  SER   B C    1 
ATOM   16604 O O    . SER   B  1 303 ? 73.723 -17.959 -69.449 1.00 37.91  ? 329  SER   B O    1 
ATOM   16605 C CB   . SER   B  1 303 ? 71.677 -19.749 -69.221 1.00 37.44  ? 329  SER   B CB   1 
ATOM   16606 O OG   . SER   B  1 303 ? 71.132 -18.735 -70.055 1.00 41.07  ? 329  SER   B OG   1 
ATOM   16607 H H    . SER   B  1 303 ? 70.772 -17.781 -67.285 0.00 42.28  ? 329  SER   B H    1 
ATOM   16608 H HA   . SER   B  1 303 ? 72.841 -19.883 -67.441 0.00 47.12  ? 329  SER   B HA   1 
ATOM   16609 H HB2  . SER   B  1 303 ? 72.471 -20.269 -69.754 0.00 51.16  ? 329  SER   B HB2  1 
ATOM   16610 H HB3  . SER   B  1 303 ? 70.888 -20.451 -68.956 0.00 50.73  ? 329  SER   B HB3  1 
ATOM   16611 H HG   . SER   B  1 303 ? 70.332 -18.329 -69.630 0.00 54.22  ? 329  SER   B HG   1 
ATOM   16612 N N    . GLY   B  1 304 ? 73.421 -17.093 -67.388 1.00 36.75  ? 330  GLY   B N    1 
ATOM   16613 C CA   . GLY   B  1 304 ? 74.218 -15.899 -67.609 1.00 37.70  ? 330  GLY   B CA   1 
ATOM   16614 C C    . GLY   B  1 304 ? 75.705 -16.064 -67.820 1.00 37.68  ? 330  GLY   B C    1 
ATOM   16615 O O    . GLY   B  1 304 ? 76.453 -16.222 -66.855 1.00 38.37  ? 330  GLY   B O    1 
ATOM   16616 H H    . GLY   B  1 304 ? 73.081 -17.167 -66.435 0.00 48.17  ? 330  GLY   B H    1 
ATOM   16617 H HA2  . GLY   B  1 304 ? 73.813 -15.371 -68.472 0.00 49.27  ? 330  GLY   B HA2  1 
ATOM   16618 H HA3  . GLY   B  1 304 ? 74.090 -15.246 -66.747 0.00 48.83  ? 330  GLY   B HA3  1 
ATOM   16619 N N    . ALA   B  1 305 ? 76.150 -15.945 -69.071 1.00 37.12  ? 331  ALA   B N    1 
ATOM   16620 C CA   . ALA   B  1 305 ? 77.574 -15.957 -69.393 1.00 36.66  ? 331  ALA   B CA   1 
ATOM   16621 C C    . ALA   B  1 305 ? 78.256 -14.691 -68.826 1.00 36.03  ? 331  ALA   B C    1 
ATOM   16622 O O    . ALA   B  1 305 ? 79.427 -14.753 -68.453 1.00 36.73  ? 331  ALA   B O    1 
ATOM   16623 C CB   . ALA   B  1 305 ? 77.768 -16.012 -70.902 1.00 36.79  ? 331  ALA   B CB   1 
ATOM   16624 H H    . ALA   B  1 305 ? 75.553 -15.849 -69.885 0.00 49.52  ? 331  ALA   B H    1 
ATOM   16625 H HA   . ALA   B  1 305 ? 78.043 -16.835 -68.951 0.00 49.73  ? 331  ALA   B HA   1 
ATOM   16626 H HB1  . ALA   B  1 305 ? 78.835 -16.033 -71.121 0.00 50.36  ? 331  ALA   B HB1  1 
ATOM   16627 H HB2  . ALA   B  1 305 ? 77.288 -16.909 -71.288 0.00 50.38  ? 331  ALA   B HB2  1 
ATOM   16628 H HB3  . ALA   B  1 305 ? 77.316 -15.127 -71.348 0.00 49.68  ? 331  ALA   B HB3  1 
ATOM   16629 N N    . PHE   B  1 306 ? 77.533 -13.546 -68.756 1.00 35.01  ? 332  PHE   B N    1 
ATOM   16630 C CA   . PHE   B  1 306 ? 78.092 -12.303 -68.216 1.00 34.69  ? 332  PHE   B CA   1 
ATOM   16631 C C    . PHE   B  1 306 ? 78.532 -12.438 -66.749 1.00 34.56  ? 332  PHE   B C    1 
ATOM   16632 O O    . PHE   B  1 306 ? 79.387 -11.671 -66.305 1.00 34.52  ? 332  PHE   B O    1 
ATOM   16633 C CB   . PHE   B  1 306 ? 77.096 -11.134 -68.351 1.00 34.30  ? 332  PHE   B CB   1 
ATOM   16634 C CG   . PHE   B  1 306 ? 75.978 -11.135 -67.333 1.00 34.27  ? 332  PHE   B CG   1 
ATOM   16635 C CD1  . PHE   B  1 306 ? 74.890 -11.981 -67.472 1.00 34.57  ? 332  PHE   B CD1  1 
ATOM   16636 C CD2  . PHE   B  1 306 ? 76.033 -10.314 -66.218 1.00 34.63  ? 332  PHE   B CD2  1 
ATOM   16637 C CE1  . PHE   B  1 306 ? 73.874 -11.995 -66.524 1.00 35.03  ? 332  PHE   B CE1  1 
ATOM   16638 C CE2  . PHE   B  1 306 ? 75.009 -10.324 -65.279 1.00 35.11  ? 332  PHE   B CE2  1 
ATOM   16639 C CZ   . PHE   B  1 306 ? 73.939 -11.164 -65.437 1.00 34.74  ? 332  PHE   B CZ   1 
ATOM   16640 H H    . PHE   B  1 306 ? 76.572 -13.453 -69.070 0.00 46.10  ? 332  PHE   B H    1 
ATOM   16641 H HA   . PHE   B  1 306 ? 78.978 -12.045 -68.795 0.00 45.77  ? 332  PHE   B HA   1 
ATOM   16642 H HB2  . PHE   B  1 306 ? 77.644 -10.200 -68.238 0.00 44.21  ? 332  PHE   B HB2  1 
ATOM   16643 H HB3  . PHE   B  1 306 ? 76.643 -11.166 -69.341 0.00 44.56  ? 332  PHE   B HB3  1 
ATOM   16644 H HD1  . PHE   B  1 306 ? 74.831 -12.636 -68.325 0.00 44.70  ? 332  PHE   B HD1  1 
ATOM   16645 H HD2  . PHE   B  1 306 ? 76.869 -9.647  -66.083 0.00 43.75  ? 332  PHE   B HD2  1 
ATOM   16646 H HE1  . PHE   B  1 306 ? 73.026 -12.651 -66.650 0.00 44.44  ? 332  PHE   B HE1  1 
ATOM   16647 H HE2  . PHE   B  1 306 ? 75.061 -9.673  -64.422 0.00 43.53  ? 332  PHE   B HE2  1 
ATOM   16648 H HZ   . PHE   B  1 306 ? 73.147 -11.172 -64.706 0.00 43.19  ? 332  PHE   B HZ   1 
ATOM   16649 N N    . LEU   B  1 307 ? 77.947 -13.395 -66.001 1.00 34.08  ? 333  LEU   B N    1 
ATOM   16650 C CA   . LEU   B  1 307 ? 78.295 -13.621 -64.598 1.00 34.36  ? 333  LEU   B CA   1 
ATOM   16651 C C    . LEU   B  1 307 ? 79.750 -14.093 -64.424 1.00 34.39  ? 333  LEU   B C    1 
ATOM   16652 O O    . LEU   B  1 307 ? 80.304 -13.933 -63.342 1.00 35.03  ? 333  LEU   B O    1 
ATOM   16653 C CB   . LEU   B  1 307 ? 77.331 -14.645 -63.977 1.00 34.88  ? 333  LEU   B CB   1 
ATOM   16654 C CG   . LEU   B  1 307 ? 75.842 -14.267 -63.960 1.00 36.99  ? 333  LEU   B CG   1 
ATOM   16655 C CD1  . LEU   B  1 307 ? 74.978 -15.495 -63.816 1.00 37.85  ? 333  LEU   B CD1  1 
ATOM   16656 C CD2  . LEU   B  1 307 ? 75.534 -13.303 -62.861 1.00 37.92  ? 333  LEU   B CD2  1 
ATOM   16657 H H    . LEU   B  1 307 ? 77.231 -14.029 -66.342 0.00 44.67  ? 333  LEU   B H    1 
ATOM   16658 H HA   . LEU   B  1 307 ? 78.197 -12.680 -64.059 0.00 44.31  ? 333  LEU   B HA   1 
ATOM   16659 H HB2  . LEU   B  1 307 ? 77.410 -15.566 -64.552 0.00 45.86  ? 333  LEU   B HB2  1 
ATOM   16660 H HB3  . LEU   B  1 307 ? 77.635 -14.828 -62.949 0.00 45.32  ? 333  LEU   B HB3  1 
ATOM   16661 H HG   . LEU   B  1 307 ? 75.572 -13.791 -64.901 0.00 47.35  ? 333  LEU   B HG   1 
ATOM   16662 H HD11 . LEU   B  1 307 ? 73.936 -15.189 -63.737 0.00 48.25  ? 333  LEU   B HD11 1 
ATOM   16663 H HD12 . LEU   B  1 307 ? 75.110 -16.129 -64.692 0.00 49.09  ? 333  LEU   B HD12 1 
ATOM   16664 H HD13 . LEU   B  1 307 ? 75.276 -16.035 -62.918 0.00 48.71  ? 333  LEU   B HD13 1 
ATOM   16665 H HD21 . LEU   B  1 307 ? 74.505 -12.964 -62.971 0.00 47.51  ? 333  LEU   B HD21 1 
ATOM   16666 H HD22 . LEU   B  1 307 ? 75.645 -13.826 -61.913 0.00 47.88  ? 333  LEU   B HD22 1 
ATOM   16667 H HD23 . LEU   B  1 307 ? 76.213 -12.453 -62.907 0.00 47.75  ? 333  LEU   B HD23 1 
ATOM   16668 N N    . THR   B  1 308 ? 80.375 -14.662 -65.473 1.00 33.27  ? 334  THR   B N    1 
ATOM   16669 C CA   . THR   B  1 308 ? 81.771 -15.112 -65.413 1.00 32.62  ? 334  THR   B CA   1 
ATOM   16670 C C    . THR   B  1 308 ? 82.768 -13.929 -65.586 1.00 31.85  ? 334  THR   B C    1 
ATOM   16671 O O    . THR   B  1 308 ? 83.945 -14.085 -65.302 1.00 32.03  ? 334  THR   B O    1 
ATOM   16672 C CB   . THR   B  1 308 ? 82.012 -16.180 -66.499 1.00 33.89  ? 334  THR   B CB   1 
ATOM   16673 O OG1  . THR   B  1 308 ? 81.978 -15.560 -67.784 1.00 35.03  ? 334  THR   B OG1  1 
ATOM   16674 C CG2  . THR   B  1 308 ? 80.988 -17.317 -66.458 1.00 34.14  ? 334  THR   B CG2  1 
ATOM   16675 H H    . THR   B  1 308 ? 79.948 -14.811 -66.382 0.00 44.75  ? 334  THR   B H    1 
ATOM   16676 H HA   . THR   B  1 308 ? 81.966 -15.578 -64.449 0.00 44.51  ? 334  THR   B HA   1 
ATOM   16677 H HB   . THR   B  1 308 ? 82.998 -16.617 -66.347 0.00 47.18  ? 334  THR   B HB   1 
ATOM   16678 H HG1  . THR   B  1 308 ? 81.061 -15.246 -68.002 0.00 47.74  ? 334  THR   B HG1  1 
ATOM   16679 H HG21 . THR   B  1 308 ? 81.316 -18.133 -67.101 0.00 47.74  ? 334  THR   B HG21 1 
ATOM   16680 H HG22 . THR   B  1 308 ? 80.877 -17.688 -65.441 0.00 47.05  ? 334  THR   B HG22 1 
ATOM   16681 H HG23 . THR   B  1 308 ? 80.018 -16.969 -66.810 0.00 46.78  ? 334  THR   B HG23 1 
ATOM   16682 N N    . MET   B  1 309 ? 82.292 -12.758 -66.040 1.00 31.27  ? 335  MET   B N    1 
ATOM   16683 C CA   . MET   B  1 309 ? 83.109 -11.573 -66.303 1.00 31.07  ? 335  MET   B CA   1 
ATOM   16684 C C    . MET   B  1 309 ? 83.185 -10.590 -65.134 1.00 29.79  ? 335  MET   B C    1 
ATOM   16685 O O    . MET   B  1 309 ? 83.788 -9.525  -65.298 1.00 30.05  ? 335  MET   B O    1 
ATOM   16686 C CB   . MET   B  1 309 ? 82.460 -10.804 -67.470 1.00 32.37  ? 335  MET   B CB   1 
ATOM   16687 C CG   . MET   B  1 309 ? 82.232 -11.633 -68.722 1.00 35.79  ? 335  MET   B CG   1 
ATOM   16688 S SD   . MET   B  1 309 ? 83.746 -12.382 -69.366 1.00 42.20  ? 335  MET   B SD   1 
ATOM   16689 C CE   . MET   B  1 309 ? 84.707 -10.967 -69.677 1.00 40.82  ? 335  MET   B CE   1 
ATOM   16690 H H    . MET   B  1 309 ? 81.311 -12.588 -66.237 0.00 41.94  ? 335  MET   B H    1 
ATOM   16691 H HA   . MET   B  1 309 ? 84.121 -11.861 -66.585 0.00 42.46  ? 335  MET   B HA   1 
ATOM   16692 H HB2  . MET   B  1 309 ? 81.490 -10.433 -67.142 0.00 42.81  ? 335  MET   B HB2  1 
ATOM   16693 H HB3  . MET   B  1 309 ? 83.092 -9.958  -67.738 0.00 43.32  ? 335  MET   B HB3  1 
ATOM   16694 H HG2  . MET   B  1 309 ? 81.516 -12.428 -68.515 0.00 47.89  ? 335  MET   B HG2  1 
ATOM   16695 H HG3  . MET   B  1 309 ? 81.836 -10.979 -69.497 0.00 47.75  ? 335  MET   B HG3  1 
ATOM   16696 H HE1  . MET   B  1 309 ? 85.528 -11.235 -70.341 0.00 55.32  ? 335  MET   B HE1  1 
ATOM   16697 H HE2  . MET   B  1 309 ? 84.080 -10.212 -70.148 0.00 54.44  ? 335  MET   B HE2  1 
ATOM   16698 H HE3  . MET   B  1 309 ? 85.103 -10.590 -68.736 0.00 54.58  ? 335  MET   B HE3  1 
ATOM   16699 N N    . LEU   B  1 310 ? 82.596 -10.921 -63.973 1.00 28.28  ? 336  LEU   B N    1 
ATOM   16700 C CA   . LEU   B  1 310 ? 82.462 -9.988  -62.867 1.00 28.17  ? 336  LEU   B CA   1 
ATOM   16701 C C    . LEU   B  1 310 ? 83.021 -10.526 -61.534 1.00 28.21  ? 336  LEU   B C    1 
ATOM   16702 O O    . LEU   B  1 310 ? 82.291 -10.598 -60.540 1.00 27.76  ? 336  LEU   B O    1 
ATOM   16703 C CB   . LEU   B  1 310 ? 80.946 -9.706  -62.755 1.00 28.54  ? 336  LEU   B CB   1 
ATOM   16704 C CG   . LEU   B  1 310 ? 80.288 -9.075  -63.988 1.00 29.94  ? 336  LEU   B CG   1 
ATOM   16705 C CD1  . LEU   B  1 310 ? 78.792 -8.945  -63.811 1.00 29.89  ? 336  LEU   B CD1  1 
ATOM   16706 C CD2  . LEU   B  1 310 ? 80.907 -7.714  -64.294 1.00 31.04  ? 336  LEU   B CD2  1 
ATOM   16707 H H    . LEU   B  1 310 ? 82.214 -11.836 -63.757 0.00 37.91  ? 336  LEU   B H    1 
ATOM   16708 H HA   . LEU   B  1 310 ? 82.976 -9.050  -63.074 0.00 37.07  ? 336  LEU   B HA   1 
ATOM   16709 H HB2  . LEU   B  1 310 ? 80.439 -10.652 -62.566 0.00 37.06  ? 336  LEU   B HB2  1 
ATOM   16710 H HB3  . LEU   B  1 310 ? 80.761 -9.029  -61.926 0.00 36.59  ? 336  LEU   B HB3  1 
ATOM   16711 H HG   . LEU   B  1 310 ? 80.453 -9.717  -64.851 0.00 38.88  ? 336  LEU   B HG   1 
ATOM   16712 H HD11 . LEU   B  1 310 ? 78.348 -8.680  -64.769 0.00 37.90  ? 336  LEU   B HD11 1 
ATOM   16713 H HD12 . LEU   B  1 310 ? 78.385 -9.894  -63.462 0.00 38.00  ? 336  LEU   B HD12 1 
ATOM   16714 H HD13 . LEU   B  1 310 ? 78.590 -8.157  -63.088 0.00 37.51  ? 336  LEU   B HD13 1 
ATOM   16715 H HD21 . LEU   B  1 310 ? 80.224 -7.145  -64.923 0.00 39.44  ? 336  LEU   B HD21 1 
ATOM   16716 H HD22 . LEU   B  1 310 ? 81.091 -7.185  -63.361 0.00 39.45  ? 336  LEU   B HD22 1 
ATOM   16717 H HD23 . LEU   B  1 310 ? 81.849 -7.868  -64.819 0.00 40.12  ? 336  LEU   B HD23 1 
ATOM   16718 N N    . PRO   B  1 311 ? 84.328 -10.852 -61.470 1.00 28.47  ? 337  PRO   B N    1 
ATOM   16719 C CA   . PRO   B  1 311 ? 84.884 -11.400 -60.223 1.00 28.79  ? 337  PRO   B CA   1 
ATOM   16720 C C    . PRO   B  1 311 ? 85.055 -10.416 -59.059 1.00 28.43  ? 337  PRO   B C    1 
ATOM   16721 O O    . PRO   B  1 311 ? 85.195 -10.875 -57.931 1.00 29.11  ? 337  PRO   B O    1 
ATOM   16722 C CB   . PRO   B  1 311 ? 86.231 -11.976 -60.670 1.00 29.57  ? 337  PRO   B CB   1 
ATOM   16723 C CG   . PRO   B  1 311 ? 86.642 -11.119 -61.803 1.00 30.21  ? 337  PRO   B CG   1 
ATOM   16724 C CD   . PRO   B  1 311 ? 85.350 -10.811 -62.536 1.00 28.72  ? 337  PRO   B CD   1 
ATOM   16725 H HA   . PRO   B  1 311 ? 84.262 -12.227 -59.883 0.00 38.81  ? 337  PRO   B HA   1 
ATOM   16726 H HB2  . PRO   B  1 311 ? 86.949 -11.907 -59.853 0.00 40.71  ? 337  PRO   B HB2  1 
ATOM   16727 H HB3  . PRO   B  1 311 ? 86.102 -13.010 -60.988 0.00 40.88  ? 337  PRO   B HB3  1 
ATOM   16728 H HG2  . PRO   B  1 311 ? 87.103 -10.204 -61.432 0.00 41.19  ? 337  PRO   B HG2  1 
ATOM   16729 H HG3  . PRO   B  1 311 ? 87.331 -11.664 -62.448 0.00 41.88  ? 337  PRO   B HG3  1 
ATOM   16730 H HD2  . PRO   B  1 311 ? 85.395 -9.818  -62.981 0.00 38.82  ? 337  PRO   B HD2  1 
ATOM   16731 H HD3  . PRO   B  1 311 ? 85.147 -11.578 -63.281 0.00 39.32  ? 337  PRO   B HD3  1 
ATOM   16732 N N    . ARG   B  1 312 ? 85.029 -9.092  -59.316 1.00 27.98  ? 338  ARG   B N    1 
ATOM   16733 C CA   . ARG   B  1 312 ? 85.138 -8.052  -58.278 1.00 28.26  ? 338  ARG   B CA   1 
ATOM   16734 C C    . ARG   B  1 312 ? 83.780 -7.404  -57.939 1.00 26.41  ? 338  ARG   B C    1 
ATOM   16735 O O    . ARG   B  1 312 ? 83.745 -6.480  -57.125 1.00 26.47  ? 338  ARG   B O    1 
ATOM   16736 C CB   . ARG   B  1 312 ? 86.126 -6.944  -58.737 1.00 32.22  ? 338  ARG   B CB   1 
ATOM   16737 C CG   . ARG   B  1 312 ? 87.417 -6.837  -57.912 1.00 39.47  ? 338  ARG   B CG   1 
ATOM   16738 C CD   . ARG   B  1 312 ? 88.649 -6.874  -58.775 1.00 45.22  ? 338  ARG   B CD   1 
ATOM   16739 N NE   . ARG   B  1 312 ? 88.836 -8.180  -59.405 1.00 50.96  ? 338  ARG   B NE   1 
ATOM   16740 C CZ   . ARG   B  1 312 ? 89.878 -8.509  -60.166 1.00 54.31  ? 338  ARG   B CZ   1 
ATOM   16741 N NH1  . ARG   B  1 312 ? 90.845 -7.625  -60.403 1.00 55.11  ? 338  ARG   B NH1  1 
ATOM   16742 N NH2  . ARG   B  1 312 ? 89.959 -9.725  -60.701 1.00 53.70  ? 338  ARG   B NH2  1 
ATOM   16743 H H    . ARG   B  1 312 ? 84.913 -8.700  -60.245 0.00 37.08  ? 338  ARG   B H    1 
ATOM   16744 H HA   . ARG   B  1 312 ? 85.477 -8.515  -57.352 0.00 37.30  ? 338  ARG   B HA   1 
ATOM   16745 H HB2  . ARG   B  1 312 ? 86.418 -7.136  -59.768 0.00 42.30  ? 338  ARG   B HB2  1 
ATOM   16746 H HB3  . ARG   B  1 312 ? 85.636 -5.973  -58.690 0.00 41.62  ? 338  ARG   B HB3  1 
ATOM   16747 H HG2  . ARG   B  1 312 ? 87.414 -5.891  -57.372 0.00 50.96  ? 338  ARG   B HG2  1 
ATOM   16748 H HG3  . ARG   B  1 312 ? 87.488 -7.667  -57.211 0.00 51.41  ? 338  ARG   B HG3  1 
ATOM   16749 H HD2  . ARG   B  1 312 ? 88.559 -6.123  -59.559 0.00 58.53  ? 338  ARG   B HD2  1 
ATOM   16750 H HD3  . ARG   B  1 312 ? 89.522 -6.665  -58.159 0.00 59.00  ? 338  ARG   B HD3  1 
ATOM   16751 H HE   . ARG   B  1 312 ? 88.123 -8.885  -59.247 0.00 65.94  ? 338  ARG   B HE   1 
ATOM   16752 H HH11 . ARG   B  1 312 ? 90.817 -6.684  -60.022 0.00 71.58  ? 338  ARG   B HH11 1 
ATOM   16753 H HH12 . ARG   B  1 312 ? 91.629 -7.886  -60.993 0.00 72.35  ? 338  ARG   B HH12 1 
ATOM   16754 H HH21 . ARG   B  1 312 ? 89.232 -10.412 -60.531 0.00 70.27  ? 338  ARG   B HH21 1 
ATOM   16755 H HH22 . ARG   B  1 312 ? 90.751 -9.973  -61.286 0.00 70.88  ? 338  ARG   B HH22 1 
ATOM   16756 N N    . LEU   B  1 313 ? 82.668 -7.866  -58.545 1.00 24.21  ? 339  LEU   B N    1 
ATOM   16757 C CA   . LEU   B  1 313 ? 81.365 -7.282  -58.279 1.00 23.21  ? 339  LEU   B CA   1 
ATOM   16758 C C    . LEU   B  1 313 ? 80.935 -7.564  -56.843 1.00 22.26  ? 339  LEU   B C    1 
ATOM   16759 O O    . LEU   B  1 313 ? 81.049 -8.696  -56.378 1.00 21.76  ? 339  LEU   B O    1 
ATOM   16760 C CB   . LEU   B  1 313 ? 80.331 -7.836  -59.258 1.00 23.51  ? 339  LEU   B CB   1 
ATOM   16761 C CG   . LEU   B  1 313 ? 78.986 -7.123  -59.305 1.00 23.87  ? 339  LEU   B CG   1 
ATOM   16762 C CD1  . LEU   B  1 313 ? 79.081 -5.855  -60.178 1.00 23.70  ? 339  LEU   B CD1  1 
ATOM   16763 C CD2  . LEU   B  1 313 ? 77.908 -8.063  -59.842 1.00 24.43  ? 339  LEU   B CD2  1 
ATOM   16764 H H    . LEU   B  1 313 ? 82.641 -8.640  -59.201 0.00 31.57  ? 339  LEU   B H    1 
ATOM   16765 H HA   . LEU   B  1 313 ? 81.429 -6.206  -58.429 0.00 29.27  ? 339  LEU   B HA   1 
ATOM   16766 H HB2  . LEU   B  1 313 ? 80.776 -7.679  -60.237 0.00 29.96  ? 339  LEU   B HB2  1 
ATOM   16767 H HB3  . LEU   B  1 313 ? 80.169 -8.898  -59.073 0.00 29.94  ? 339  LEU   B HB3  1 
ATOM   16768 H HG   . LEU   B  1 313 ? 78.676 -6.813  -58.309 0.00 29.30  ? 339  LEU   B HG   1 
ATOM   16769 H HD11 . LEU   B  1 313 ? 78.122 -5.341  -60.153 0.00 28.83  ? 339  LEU   B HD11 1 
ATOM   16770 H HD12 . LEU   B  1 313 ? 79.858 -5.197  -59.790 0.00 29.28  ? 339  LEU   B HD12 1 
ATOM   16771 H HD13 . LEU   B  1 313 ? 79.316 -6.142  -61.202 0.00 29.50  ? 339  LEU   B HD13 1 
ATOM   16772 H HD21 . LEU   B  1 313 ? 76.974 -7.510  -59.928 0.00 29.85  ? 339  LEU   B HD21 1 
ATOM   16773 H HD22 . LEU   B  1 313 ? 78.215 -8.438  -60.817 0.00 30.56  ? 339  LEU   B HD22 1 
ATOM   16774 H HD23 . LEU   B  1 313 ? 77.788 -8.897  -59.151 0.00 30.33  ? 339  LEU   B HD23 1 
ATOM   16775 N N    . GLU   B  1 314 ? 80.473 -6.525  -56.147 1.00 22.07  ? 340  GLU   B N    1 
ATOM   16776 C CA   . GLU   B  1 314 ? 80.032 -6.631  -54.760 1.00 22.34  ? 340  GLU   B CA   1 
ATOM   16777 C C    . GLU   B  1 314 ? 78.508 -6.551  -54.626 1.00 22.22  ? 340  GLU   B C    1 
ATOM   16778 O O    . GLU   B  1 314 ? 77.967 -7.202  -53.738 1.00 22.95  ? 340  GLU   B O    1 
ATOM   16779 C CB   . GLU   B  1 314 ? 80.700 -5.540  -53.918 1.00 24.30  ? 340  GLU   B CB   1 
ATOM   16780 C CG   . GLU   B  1 314 ? 82.205 -5.720  -53.817 1.00 29.05  ? 340  GLU   B CG   1 
ATOM   16781 C CD   . GLU   B  1 314 ? 82.926 -4.607  -53.084 1.00 35.06  ? 340  GLU   B CD   1 
ATOM   16782 O OE1  . GLU   B  1 314 ? 82.252 -3.818  -52.385 1.00 37.52  ? 340  GLU   B OE1  1 
ATOM   16783 O OE2  . GLU   B  1 314 ? 84.166 -4.513  -53.226 1.00 35.91  ? 340  GLU   B OE2  1 
ATOM   16784 H H    . GLU   B  1 314 ? 80.380 -5.585  -56.520 0.00 27.24  ? 340  GLU   B H    1 
ATOM   16785 H HA   . GLU   B  1 314 ? 80.344 -7.585  -54.338 0.00 27.86  ? 340  GLU   B HA   1 
ATOM   16786 H HB2  . GLU   B  1 314 ? 80.504 -4.567  -54.368 0.00 29.62  ? 340  GLU   B HB2  1 
ATOM   16787 H HB3  . GLU   B  1 314 ? 80.287 -5.572  -52.911 0.00 29.68  ? 340  GLU   B HB3  1 
ATOM   16788 H HG2  . GLU   B  1 314 ? 82.409 -6.651  -53.289 0.00 36.37  ? 340  GLU   B HG2  1 
ATOM   16789 H HG3  . GLU   B  1 314 ? 82.627 -5.770  -54.819 0.00 36.33  ? 340  GLU   B HG3  1 
ATOM   16790 N N    . ILE   B  1 315 ? 77.813 -5.752  -55.454 1.00 21.24  ? 341  ILE   B N    1 
ATOM   16791 C CA   . ILE   B  1 315 ? 76.357 -5.639  -55.364 1.00 21.00  ? 341  ILE   B CA   1 
ATOM   16792 C C    . ILE   B  1 315 ? 75.729 -5.915  -56.717 1.00 21.29  ? 341  ILE   B C    1 
ATOM   16793 O O    . ILE   B  1 315 ? 76.087 -5.273  -57.701 1.00 22.05  ? 341  ILE   B O    1 
ATOM   16794 C CB   . ILE   B  1 315 ? 75.909 -4.254  -54.822 1.00 21.31  ? 341  ILE   B CB   1 
ATOM   16795 C CG1  . ILE   B  1 315 ? 76.639 -3.932  -53.480 1.00 22.36  ? 341  ILE   B CG1  1 
ATOM   16796 C CG2  . ILE   B  1 315 ? 74.373 -4.218  -54.667 1.00 21.64  ? 341  ILE   B CG2  1 
ATOM   16797 C CD1  . ILE   B  1 315 ? 76.337 -2.552  -52.888 1.00 24.50  ? 341  ILE   B CD1  1 
ATOM   16798 H H    . ILE   B  1 315 ? 78.222 -5.171  -56.180 0.00 25.45  ? 341  ILE   B H    1 
ATOM   16799 H HA   . ILE   B  1 315 ? 75.973 -6.385  -54.670 0.00 24.65  ? 341  ILE   B HA   1 
ATOM   16800 H HB   . ILE   B  1 315 ? 76.188 -3.497  -55.553 0.00 24.59  ? 341  ILE   B HB   1 
ATOM   16801 H HG12 . ILE   B  1 315 ? 76.351 -4.676  -52.738 0.00 25.93  ? 341  ILE   B HG12 1 
ATOM   16802 H HG13 . ILE   B  1 315 ? 77.716 -3.971  -53.634 0.00 26.24  ? 341  ILE   B HG13 1 
ATOM   16803 H HG21 . ILE   B  1 315 ? 74.066 -3.283  -54.201 0.00 24.29  ? 341  ILE   B HG21 1 
ATOM   16804 H HG22 . ILE   B  1 315 ? 73.896 -4.288  -55.643 0.00 24.54  ? 341  ILE   B HG22 1 
ATOM   16805 H HG23 . ILE   B  1 315 ? 74.063 -5.058  -54.046 0.00 24.60  ? 341  ILE   B HG23 1 
ATOM   16806 H HD11 . ILE   B  1 315 ? 77.100 -2.319  -52.146 0.00 28.30  ? 341  ILE   B HD11 1 
ATOM   16807 H HD12 . ILE   B  1 315 ? 76.349 -1.813  -53.687 0.00 28.07  ? 341  ILE   B HD12 1 
ATOM   16808 H HD13 . ILE   B  1 315 ? 75.358 -2.575  -52.411 0.00 27.85  ? 341  ILE   B HD13 1 
ATOM   16809 N N    . LEU   B  1 316 ? 74.796 -6.866  -56.767 1.00 20.32  ? 342  LEU   B N    1 
ATOM   16810 C CA   . LEU   B  1 316 ? 74.115 -7.235  -57.995 1.00 20.65  ? 342  LEU   B CA   1 
ATOM   16811 C C    . LEU   B  1 316 ? 72.623 -7.090  -57.741 1.00 20.63  ? 342  LEU   B C    1 
ATOM   16812 O O    . LEU   B  1 316 ? 72.099 -7.764  -56.851 1.00 21.53  ? 342  LEU   B O    1 
ATOM   16813 C CB   . LEU   B  1 316 ? 74.469 -8.692  -58.371 1.00 21.17  ? 342  LEU   B CB   1 
ATOM   16814 C CG   . LEU   B  1 316 ? 73.757 -9.278  -59.607 1.00 22.99  ? 342  LEU   B CG   1 
ATOM   16815 C CD1  . LEU   B  1 316 ? 73.947 -8.380  -60.858 1.00 23.52  ? 342  LEU   B CD1  1 
ATOM   16816 C CD2  . LEU   B  1 316 ? 74.265 -10.706 -59.901 1.00 23.50  ? 342  LEU   B CD2  1 
ATOM   16817 H H    . LEU   B  1 316 ? 74.482 -7.405  -55.967 0.00 23.76  ? 342  LEU   B H    1 
ATOM   16818 H HA   . LEU   B  1 316 ? 74.399 -6.576  -58.813 0.00 24.28  ? 342  LEU   B HA   1 
ATOM   16819 H HB2  . LEU   B  1 316 ? 75.540 -8.744  -58.558 0.00 25.69  ? 342  LEU   B HB2  1 
ATOM   16820 H HB3  . LEU   B  1 316 ? 74.223 -9.331  -57.525 0.00 25.38  ? 342  LEU   B HB3  1 
ATOM   16821 H HG   . LEU   B  1 316 ? 72.688 -9.348  -59.408 0.00 27.47  ? 342  LEU   B HG   1 
ATOM   16822 H HD11 . LEU   B  1 316 ? 73.567 -8.909  -61.731 0.00 28.57  ? 342  LEU   B HD11 1 
ATOM   16823 H HD12 . LEU   B  1 316 ? 73.391 -7.452  -60.724 0.00 27.99  ? 342  LEU   B HD12 1 
ATOM   16824 H HD13 . LEU   B  1 316 ? 75.007 -8.164  -60.987 0.00 28.58  ? 342  LEU   B HD13 1 
ATOM   16825 H HD21 . LEU   B  1 316 ? 73.739 -11.098 -60.770 0.00 29.03  ? 342  LEU   B HD21 1 
ATOM   16826 H HD22 . LEU   B  1 316 ? 75.335 -10.667 -60.097 0.00 29.18  ? 342  LEU   B HD22 1 
ATOM   16827 H HD23 . LEU   B  1 316 ? 74.067 -11.335 -59.034 0.00 28.91  ? 342  LEU   B HD23 1 
ATOM   16828 N N    . ASP   B  1 317 ? 71.948 -6.178  -58.450 1.00 20.05  ? 343  ASP   B N    1 
ATOM   16829 C CA   . ASP   B  1 317 ? 70.511 -5.987  -58.259 1.00 20.14  ? 343  ASP   B CA   1 
ATOM   16830 C C    . ASP   B  1 317 ? 69.736 -6.478  -59.481 1.00 20.69  ? 343  ASP   B C    1 
ATOM   16831 O O    . ASP   B  1 317 ? 69.800 -5.869  -60.548 1.00 21.11  ? 343  ASP   B O    1 
ATOM   16832 C CB   . ASP   B  1 317 ? 70.162 -4.517  -57.916 1.00 21.45  ? 343  ASP   B CB   1 
ATOM   16833 C CG   . ASP   B  1 317 ? 68.779 -4.357  -57.288 1.00 24.54  ? 343  ASP   B CG   1 
ATOM   16834 O OD1  . ASP   B  1 317 ? 67.899 -5.196  -57.565 1.00 23.12  ? 343  ASP   B OD1  1 
ATOM   16835 O OD2  . ASP   B  1 317 ? 68.590 -3.406  -56.489 1.00 27.95  ? 343  ASP   B OD2  1 
ATOM   16836 H H    . ASP   B  1 317 ? 72.356 -5.567  -59.150 0.00 22.93  ? 343  ASP   B H    1 
ATOM   16837 H HA   . ASP   B  1 317 ? 70.185 -6.593  -57.419 0.00 22.59  ? 343  ASP   B HA   1 
ATOM   16838 H HB2  . ASP   B  1 317 ? 70.892 -4.141  -57.201 0.00 23.79  ? 343  ASP   B HB2  1 
ATOM   16839 H HB3  . ASP   B  1 317 ? 70.192 -3.913  -58.821 0.00 23.83  ? 343  ASP   B HB3  1 
ATOM   16840 N N    . LEU   B  1 318 ? 69.029 -7.599  -59.331 1.00 19.85  ? 344  LEU   B N    1 
ATOM   16841 C CA   . LEU   B  1 318 ? 68.224 -8.187  -60.397 1.00 20.30  ? 344  LEU   B CA   1 
ATOM   16842 C C    . LEU   B  1 318 ? 66.726 -8.157  -60.044 1.00 19.60  ? 344  LEU   B C    1 
ATOM   16843 O O    . LEU   B  1 318 ? 65.964 -8.980  -60.553 1.00 19.27  ? 344  LEU   B O    1 
ATOM   16844 C CB   . LEU   B  1 318 ? 68.705 -9.638  -60.633 1.00 20.83  ? 344  LEU   B CB   1 
ATOM   16845 C CG   . LEU   B  1 318 ? 70.037 -9.791  -61.381 1.00 22.19  ? 344  LEU   B CG   1 
ATOM   16846 C CD1  . LEU   B  1 318 ? 70.676 -11.130 -61.047 1.00 22.52  ? 344  LEU   B CD1  1 
ATOM   16847 C CD2  . LEU   B  1 318 ? 69.829 -9.649  -62.897 1.00 23.15  ? 344  LEU   B CD2  1 
ATOM   16848 H H    . LEU   B  1 318 ? 68.984 -8.131  -58.468 0.00 22.54  ? 344  LEU   B H    1 
ATOM   16849 H HA   . LEU   B  1 318 ? 68.345 -7.630  -61.325 0.00 23.34  ? 344  LEU   B HA   1 
ATOM   16850 H HB2  . LEU   B  1 318 ? 68.819 -10.128 -59.668 0.00 24.40  ? 344  LEU   B HB2  1 
ATOM   16851 H HB3  . LEU   B  1 318 ? 67.966 -10.176 -61.223 0.00 24.57  ? 344  LEU   B HB3  1 
ATOM   16852 H HG   . LEU   B  1 318 ? 70.732 -9.014  -61.066 0.00 26.31  ? 344  LEU   B HG   1 
ATOM   16853 H HD11 . LEU   B  1 318 ? 71.334 -11.431 -61.860 0.00 27.66  ? 344  LEU   B HD11 1 
ATOM   16854 H HD12 . LEU   B  1 318 ? 71.251 -11.023 -60.129 0.00 27.20  ? 344  LEU   B HD12 1 
ATOM   16855 H HD13 . LEU   B  1 318 ? 69.890 -11.869 -60.896 0.00 27.35  ? 344  LEU   B HD13 1 
ATOM   16856 H HD21 . LEU   B  1 318 ? 70.796 -9.717  -63.393 0.00 28.11  ? 344  LEU   B HD21 1 
ATOM   16857 H HD22 . LEU   B  1 318 ? 69.178 -10.451 -63.243 0.00 28.03  ? 344  LEU   B HD22 1 
ATOM   16858 H HD23 . LEU   B  1 318 ? 69.374 -8.683  -63.112 0.00 27.54  ? 344  LEU   B HD23 1 
ATOM   16859 N N    . SER   B  1 319 ? 66.293 -7.191  -59.211 1.00 18.65  ? 345  SER   B N    1 
ATOM   16860 C CA   . SER   B  1 319 ? 64.906 -7.118  -58.783 1.00 18.40  ? 345  SER   B CA   1 
ATOM   16861 C C    . SER   B  1 319 ? 63.938 -6.786  -59.913 1.00 18.26  ? 345  SER   B C    1 
ATOM   16862 O O    . SER   B  1 319 ? 64.307 -6.146  -60.891 1.00 18.08  ? 345  SER   B O    1 
ATOM   16863 C CB   . SER   B  1 319 ? 64.737 -6.082  -57.676 1.00 18.70  ? 345  SER   B CB   1 
ATOM   16864 O OG   . SER   B  1 319 ? 65.505 -6.429  -56.534 1.00 18.95  ? 345  SER   B OG   1 
ATOM   16865 H H    . SER   B  1 319 ? 66.867 -6.442  -58.836 0.00 20.44  ? 345  SER   B H    1 
ATOM   16866 H HA   . SER   B  1 319 ? 64.626 -8.088  -58.373 0.00 20.17  ? 345  SER   B HA   1 
ATOM   16867 H HB2  . SER   B  1 319 ? 65.076 -5.112  -58.035 0.00 19.89  ? 345  SER   B HB2  1 
ATOM   16868 H HB3  . SER   B  1 319 ? 63.676 -6.002  -57.451 0.00 19.83  ? 345  SER   B HB3  1 
ATOM   16869 H HG   . SER   B  1 319 ? 66.457 -6.188  -56.679 0.00 20.38  ? 345  SER   B HG   1 
ATOM   16870 N N    . PHE   B  1 320 ? 62.699 -7.245  -59.764 1.00 17.68  ? 346  PHE   B N    1 
ATOM   16871 C CA   . PHE   B  1 320 ? 61.596 -7.013  -60.667 1.00 18.20  ? 346  PHE   B CA   1 
ATOM   16872 C C    . PHE   B  1 320 ? 61.895 -7.379  -62.112 1.00 18.99  ? 346  PHE   B C    1 
ATOM   16873 O O    . PHE   B  1 320 ? 61.646 -6.610  -63.043 1.00 19.33  ? 346  PHE   B O    1 
ATOM   16874 C CB   . PHE   B  1 320 ? 61.104 -5.561  -60.509 1.00 18.36  ? 346  PHE   B CB   1 
ATOM   16875 C CG   . PHE   B  1 320 ? 60.381 -5.368  -59.192 1.00 18.94  ? 346  PHE   B CG   1 
ATOM   16876 C CD1  . PHE   B  1 320 ? 59.101 -5.867  -59.011 1.00 19.84  ? 346  PHE   B CD1  1 
ATOM   16877 C CD2  . PHE   B  1 320 ? 61.014 -4.766  -58.119 1.00 19.56  ? 346  PHE   B CD2  1 
ATOM   16878 C CE1  . PHE   B  1 320 ? 58.462 -5.760  -57.781 1.00 20.35  ? 346  PHE   B CE1  1 
ATOM   16879 C CE2  . PHE   B  1 320 ? 60.365 -4.635  -56.895 1.00 20.40  ? 346  PHE   B CE2  1 
ATOM   16880 C CZ   . PHE   B  1 320 ? 59.094 -5.135  -56.734 1.00 20.32  ? 346  PHE   B CZ   1 
ATOM   16881 H H    . PHE   B  1 320 ? 62.418 -7.814  -58.972 0.00 19.14  ? 346  PHE   B H    1 
ATOM   16882 H HA   . PHE   B  1 320 ? 60.794 -7.690  -60.376 0.00 19.92  ? 346  PHE   B HA   1 
ATOM   16883 H HB2  . PHE   B  1 320 ? 61.944 -4.869  -60.552 0.00 19.61  ? 346  PHE   B HB2  1 
ATOM   16884 H HB3  . PHE   B  1 320 ? 60.388 -5.329  -61.297 0.00 19.78  ? 346  PHE   B HB3  1 
ATOM   16885 H HD1  . PHE   B  1 320 ? 58.604 -6.368  -59.826 0.00 21.41  ? 346  PHE   B HD1  1 
ATOM   16886 H HD2  . PHE   B  1 320 ? 62.012 -4.382  -58.234 0.00 20.54  ? 346  PHE   B HD2  1 
ATOM   16887 H HE1  . PHE   B  1 320 ? 57.458 -6.131  -57.661 0.00 21.54  ? 346  PHE   B HE1  1 
ATOM   16888 H HE2  . PHE   B  1 320 ? 60.862 -4.150  -56.072 0.00 21.10  ? 346  PHE   B HE2  1 
ATOM   16889 H HZ   . PHE   B  1 320 ? 58.592 -5.023  -55.789 0.00 21.00  ? 346  PHE   B HZ   1 
ATOM   16890 N N    . ASN   B  1 321 ? 62.365 -8.611  -62.301 1.00 18.78  ? 347  ASN   B N    1 
ATOM   16891 C CA   . ASN   B  1 321 ? 62.554 -9.172  -63.636 1.00 18.98  ? 347  ASN   B CA   1 
ATOM   16892 C C    . ASN   B  1 321 ? 61.473 -10.264 -63.907 1.00 19.74  ? 347  ASN   B C    1 
ATOM   16893 O O    . ASN   B  1 321 ? 61.588 -11.004 -64.882 1.00 21.31  ? 347  ASN   B O    1 
ATOM   16894 C CB   . ASN   B  1 321 ? 63.985 -9.729  -63.764 1.00 19.33  ? 347  ASN   B CB   1 
ATOM   16895 C CG   . ASN   B  1 321 ? 64.997 -8.673  -64.158 1.00 19.77  ? 347  ASN   B CG   1 
ATOM   16896 O OD1  . ASN   B  1 321 ? 65.285 -8.499  -65.335 1.00 19.24  ? 347  ASN   B OD1  1 
ATOM   16897 N ND2  . ASN   B  1 321 ? 65.532 -7.931  -63.211 1.00 19.95  ? 347  ASN   B ND2  1 
ATOM   16898 H H    . ASN   B  1 321 ? 62.604 -9.248  -61.549 0.00 21.35  ? 347  ASN   B H    1 
ATOM   16899 H HA   . ASN   B  1 321 ? 62.406 -8.407  -64.397 0.00 22.03  ? 347  ASN   B HA   1 
ATOM   16900 H HB2  . ASN   B  1 321 ? 64.297 -10.155 -62.812 0.00 22.66  ? 347  ASN   B HB2  1 
ATOM   16901 H HB3  . ASN   B  1 321 ? 64.012 -10.499 -64.533 0.00 23.15  ? 347  ASN   B HB3  1 
ATOM   16902 H HD21 . ASN   B  1 321 ? 66.212 -7.215  -63.448 0.00 22.98  ? 347  ASN   B HD21 1 
ATOM   16903 H HD22 . ASN   B  1 321 ? 65.265 -8.070  -62.242 0.00 22.82  ? 347  ASN   B HD22 1 
ATOM   16904 N N    . TYR   B  1 322 ? 60.390 -10.323 -63.093 1.00 18.60  ? 348  TYR   B N    1 
ATOM   16905 C CA   . TYR   B  1 322 ? 59.349 -11.324 -63.263 1.00 18.65  ? 348  TYR   B CA   1 
ATOM   16906 C C    . TYR   B  1 322 ? 58.743 -11.354 -64.659 1.00 19.55  ? 348  TYR   B C    1 
ATOM   16907 O O    . TYR   B  1 322 ? 58.708 -10.340 -65.361 1.00 19.53  ? 348  TYR   B O    1 
ATOM   16908 C CB   . TYR   B  1 322 ? 58.227 -11.121 -62.230 1.00 17.99  ? 348  TYR   B CB   1 
ATOM   16909 C CG   . TYR   B  1 322 ? 57.358 -9.898  -62.448 1.00 19.01  ? 348  TYR   B CG   1 
ATOM   16910 C CD1  . TYR   B  1 322 ? 57.595 -8.720  -61.754 1.00 19.66  ? 348  TYR   B CD1  1 
ATOM   16911 C CD2  . TYR   B  1 322 ? 56.208 -9.968  -63.224 1.00 19.90  ? 348  TYR   B CD2  1 
ATOM   16912 C CE1  . TYR   B  1 322 ? 56.770 -7.613  -61.912 1.00 20.56  ? 348  TYR   B CE1  1 
ATOM   16913 C CE2  . TYR   B  1 322 ? 55.405 -8.856  -63.426 1.00 20.54  ? 348  TYR   B CE2  1 
ATOM   16914 C CZ   . TYR   B  1 322 ? 55.661 -7.693  -62.734 1.00 21.51  ? 348  TYR   B CZ   1 
ATOM   16915 O OH   . TYR   B  1 322 ? 54.830 -6.607  -62.898 1.00 24.07  ? 348  TYR   B OH   1 
ATOM   16916 H H    . TYR   B  1 322 ? 60.208 -9.685  -62.325 0.00 21.30  ? 348  TYR   B H    1 
ATOM   16917 H HA   . TYR   B  1 322 ? 59.792 -12.301 -63.076 0.00 22.28  ? 348  TYR   B HA   1 
ATOM   16918 H HB2  . TYR   B  1 322 ? 57.574 -11.992 -62.258 0.00 21.16  ? 348  TYR   B HB2  1 
ATOM   16919 H HB3  . TYR   B  1 322 ? 58.674 -11.035 -61.241 0.00 20.65  ? 348  TYR   B HB3  1 
ATOM   16920 H HD1  . TYR   B  1 322 ? 58.452 -8.651  -61.107 0.00 21.98  ? 348  TYR   B HD1  1 
ATOM   16921 H HD2  . TYR   B  1 322 ? 55.998 -10.875 -63.766 0.00 23.54  ? 348  TYR   B HD2  1 
ATOM   16922 H HE1  . TYR   B  1 322 ? 56.987 -6.697  -61.389 0.00 22.68  ? 348  TYR   B HE1  1 
ATOM   16923 H HE2  . TYR   B  1 322 ? 54.532 -8.928  -64.050 0.00 23.93  ? 348  TYR   B HE2  1 
ATOM   16924 H HH   . TYR   B  1 322 ? 55.086 -6.098  -63.712 0.00 27.39  ? 348  TYR   B HH   1 
ATOM   16925 N N    . ILE   B  1 323 ? 58.236 -12.521 -65.043 1.00 20.34  ? 349  ILE   B N    1 
ATOM   16926 C CA   . ILE   B  1 323 ? 57.546 -12.696 -66.314 1.00 21.77  ? 349  ILE   B CA   1 
ATOM   16927 C C    . ILE   B  1 323 ? 56.064 -12.523 -65.983 1.00 22.29  ? 349  ILE   B C    1 
ATOM   16928 O O    . ILE   B  1 323 ? 55.524 -13.302 -65.204 1.00 22.10  ? 349  ILE   B O    1 
ATOM   16929 C CB   . ILE   B  1 323 ? 57.840 -14.080 -66.946 1.00 22.68  ? 349  ILE   B CB   1 
ATOM   16930 C CG1  . ILE   B  1 323 ? 59.301 -14.184 -67.413 1.00 24.65  ? 349  ILE   B CG1  1 
ATOM   16931 C CG2  . ILE   B  1 323 ? 56.868 -14.355 -68.120 1.00 23.10  ? 349  ILE   B CG2  1 
ATOM   16932 C CD1  . ILE   B  1 323 ? 59.834 -15.683 -67.587 1.00 26.40  ? 349  ILE   B CD1  1 
ATOM   16933 H H    . ILE   B  1 323 ? 58.285 -13.369 -64.489 0.00 25.01  ? 349  ILE   B H    1 
ATOM   16934 H HA   . ILE   B  1 323 ? 57.846 -11.934 -67.032 0.00 27.02  ? 349  ILE   B HA   1 
ATOM   16935 H HB   . ILE   B  1 323 ? 57.725 -14.845 -66.184 0.00 28.83  ? 349  ILE   B HB   1 
ATOM   16936 H HG12 . ILE   B  1 323 ? 59.392 -13.691 -68.381 0.00 31.48  ? 349  ILE   B HG12 1 
ATOM   16937 H HG13 . ILE   B  1 323 ? 59.949 -13.690 -66.692 0.00 30.95  ? 349  ILE   B HG13 1 
ATOM   16938 H HG21 . ILE   B  1 323 ? 57.295 -15.101 -68.788 0.00 30.27  ? 349  ILE   B HG21 1 
ATOM   16939 H HG22 . ILE   B  1 323 ? 55.923 -14.729 -67.727 0.00 29.81  ? 349  ILE   B HG22 1 
ATOM   16940 H HG23 . ILE   B  1 323 ? 56.699 -13.429 -68.668 0.00 29.67  ? 349  ILE   B HG23 1 
ATOM   16941 H HD11 . ILE   B  1 323 ? 60.890 -15.652 -67.849 0.00 34.13  ? 349  ILE   B HD11 1 
ATOM   16942 H HD12 . ILE   B  1 323 ? 59.701 -16.214 -66.645 0.00 33.94  ? 349  ILE   B HD12 1 
ATOM   16943 H HD13 . ILE   B  1 323 ? 59.280 -16.186 -68.377 0.00 34.48  ? 349  ILE   B HD13 1 
ATOM   16944 N N    . LYS   B  1 324 ? 55.400 -11.504 -66.560 1.00 22.83  ? 350  LYS   B N    1 
ATOM   16945 C CA   . LYS   B  1 324 ? 53.972 -11.254 -66.336 1.00 23.70  ? 350  LYS   B CA   1 
ATOM   16946 C C    . LYS   B  1 324 ? 53.151 -12.530 -66.640 1.00 25.09  ? 350  LYS   B C    1 
ATOM   16947 O O    . LYS   B  1 324 ? 53.359 -13.148 -67.678 1.00 24.68  ? 350  LYS   B O    1 
ATOM   16948 C CB   . LYS   B  1 324 ? 53.494 -10.098 -67.246 1.00 24.91  ? 350  LYS   B CB   1 
ATOM   16949 C CG   . LYS   B  1 324 ? 52.011 -9.742  -67.084 1.00 27.01  ? 350  LYS   B CG   1 
ATOM   16950 C CD   . LYS   B  1 324 ? 51.521 -8.714  -68.111 1.00 30.65  ? 350  LYS   B CD   1 
ATOM   16951 C CE   . LYS   B  1 324 ? 50.009 -8.675  -68.119 1.00 34.68  ? 350  LYS   B CE   1 
ATOM   16952 N NZ   . LYS   B  1 324 ? 49.468 -7.696  -69.094 1.00 36.85  ? 350  LYS   B NZ   1 
ATOM   16953 H H    . LYS   B  1 324 ? 55.827 -10.833 -67.192 0.00 28.08  ? 350  LYS   B H    1 
ATOM   16954 H HA   . LYS   B  1 324 ? 53.813 -10.963 -65.299 0.00 28.68  ? 350  LYS   B HA   1 
ATOM   16955 H HB2  . LYS   B  1 324 ? 54.075 -9.208  -67.015 0.00 30.16  ? 350  LYS   B HB2  1 
ATOM   16956 H HB3  . LYS   B  1 324 ? 53.654 -10.374 -68.287 0.00 30.93  ? 350  LYS   B HB3  1 
ATOM   16957 H HG2  . LYS   B  1 324 ? 51.394 -10.630 -67.206 0.00 33.39  ? 350  LYS   B HG2  1 
ATOM   16958 H HG3  . LYS   B  1 324 ? 51.859 -9.319  -66.093 0.00 32.62  ? 350  LYS   B HG3  1 
ATOM   16959 H HD2  . LYS   B  1 324 ? 51.894 -7.726  -67.847 0.00 37.14  ? 350  LYS   B HD2  1 
ATOM   16960 H HD3  . LYS   B  1 324 ? 51.865 -8.998  -69.105 0.00 37.90  ? 350  LYS   B HD3  1 
ATOM   16961 H HE2  . LYS   B  1 324 ? 49.624 -9.658  -68.389 0.00 42.94  ? 350  LYS   B HE2  1 
ATOM   16962 H HE3  . LYS   B  1 324 ? 49.657 -8.394  -67.128 0.00 42.17  ? 350  LYS   B HE3  1 
ATOM   16963 H HZ1  . LYS   B  1 324 ? 48.454 -7.705  -69.069 0.00 45.46  ? 350  LYS   B HZ1  1 
ATOM   16964 H HZ2  . LYS   B  1 324 ? 49.797 -6.763  -68.865 0.00 44.97  ? 350  LYS   B HZ2  1 
ATOM   16965 H HZ3  . LYS   B  1 324 ? 49.779 -7.933  -70.031 0.00 45.67  ? 350  LYS   B HZ3  1 
ATOM   16966 N N    . GLY   B  1 325 ? 52.300 -12.939 -65.710 1.00 25.92  ? 351  GLY   B N    1 
ATOM   16967 C CA   . GLY   B  1 325 ? 51.482 -14.130 -65.903 1.00 27.33  ? 351  GLY   B CA   1 
ATOM   16968 C C    . GLY   B  1 325 ? 52.156 -15.447 -65.568 1.00 27.99  ? 351  GLY   B C    1 
ATOM   16969 O O    . GLY   B  1 325 ? 51.490 -16.485 -65.613 1.00 28.28  ? 351  GLY   B O    1 
ATOM   16970 H H    . GLY   B  1 325 ? 52.148 -12.477 -64.819 0.00 31.77  ? 351  GLY   B H    1 
ATOM   16971 H HA2  . GLY   B  1 325 ? 50.599 -14.046 -65.270 0.00 34.25  ? 351  GLY   B HA2  1 
ATOM   16972 H HA3  . GLY   B  1 325 ? 51.139 -14.180 -66.936 0.00 34.79  ? 351  GLY   B HA3  1 
ATOM   16973 N N    . SER   B  1 326 ? 53.463 -15.435 -65.205 1.00 27.23  ? 352  SER   B N    1 
ATOM   16974 C CA   . SER   B  1 326 ? 54.185 -16.664 -64.860 1.00 26.97  ? 352  SER   B CA   1 
ATOM   16975 C C    . SER   B  1 326 ? 54.533 -16.670 -63.371 1.00 26.29  ? 352  SER   B C    1 
ATOM   16976 O O    . SER   B  1 326 ? 55.232 -15.772 -62.906 1.00 25.92  ? 352  SER   B O    1 
ATOM   16977 C CB   . SER   B  1 326 ? 55.474 -16.747 -65.659 1.00 28.67  ? 352  SER   B CB   1 
ATOM   16978 O OG   . SER   B  1 326 ? 56.214 -17.914 -65.354 1.00 30.89  ? 352  SER   B OG   1 
ATOM   16979 H H    . SER   B  1 326 ? 54.047 -14.606 -65.153 0.00 34.01  ? 352  SER   B H    1 
ATOM   16980 H HA   . SER   B  1 326 ? 53.595 -17.548 -65.095 0.00 34.79  ? 352  SER   B HA   1 
ATOM   16981 H HB2  . SER   B  1 326 ? 55.250 -16.725 -66.725 0.00 36.95  ? 352  SER   B HB2  1 
ATOM   16982 H HB3  . SER   B  1 326 ? 56.052 -15.876 -65.365 0.00 36.17  ? 352  SER   B HB3  1 
ATOM   16983 H HG   . SER   B  1 326 ? 57.051 -17.937 -65.887 0.00 39.77  ? 352  SER   B HG   1 
ATOM   16984 N N    . TYR   B  1 327 ? 54.082 -17.710 -62.642 1.00 25.74  ? 353  TYR   B N    1 
ATOM   16985 C CA   . TYR   B  1 327 ? 54.313 -17.875 -61.205 1.00 25.32  ? 353  TYR   B CA   1 
ATOM   16986 C C    . TYR   B  1 327 ? 54.953 -19.259 -61.019 1.00 26.01  ? 353  TYR   B C    1 
ATOM   16987 O O    . TYR   B  1 327 ? 54.269 -20.211 -60.641 1.00 26.81  ? 353  TYR   B O    1 
ATOM   16988 C CB   . TYR   B  1 327 ? 52.950 -17.760 -60.494 1.00 24.22  ? 353  TYR   B CB   1 
ATOM   16989 C CG   . TYR   B  1 327 ? 52.938 -17.777 -58.979 1.00 23.68  ? 353  TYR   B CG   1 
ATOM   16990 C CD1  . TYR   B  1 327 ? 54.061 -17.408 -58.244 1.00 23.81  ? 353  TYR   B CD1  1 
ATOM   16991 C CD2  . TYR   B  1 327 ? 51.772 -18.064 -58.281 1.00 24.13  ? 353  TYR   B CD2  1 
ATOM   16992 C CE1  . TYR   B  1 327 ? 54.016 -17.318 -56.856 1.00 23.92  ? 353  TYR   B CE1  1 
ATOM   16993 C CE2  . TYR   B  1 327 ? 51.731 -18.030 -56.894 1.00 24.72  ? 353  TYR   B CE2  1 
ATOM   16994 C CZ   . TYR   B  1 327 ? 52.853 -17.646 -56.182 1.00 24.99  ? 353  TYR   B CZ   1 
ATOM   16995 O OH   . TYR   B  1 327 ? 52.788 -17.608 -54.806 1.00 25.33  ? 353  TYR   B OH   1 
ATOM   16996 H H    . TYR   B  1 327 ? 53.537 -18.473 -63.031 0.00 33.08  ? 353  TYR   B H    1 
ATOM   16997 H HA   . TYR   B  1 327 ? 54.974 -17.093 -60.836 0.00 31.38  ? 353  TYR   B HA   1 
ATOM   16998 H HB2  . TYR   B  1 327 ? 52.506 -16.812 -60.794 0.00 30.06  ? 353  TYR   B HB2  1 
ATOM   16999 H HB3  . TYR   B  1 327 ? 52.304 -18.568 -60.835 0.00 30.76  ? 353  TYR   B HB3  1 
ATOM   17000 H HD1  . TYR   B  1 327 ? 54.981 -17.144 -58.728 0.00 29.09  ? 353  TYR   B HD1  1 
ATOM   17001 H HD2  . TYR   B  1 327 ? 50.886 -18.342 -58.827 0.00 30.16  ? 353  TYR   B HD2  1 
ATOM   17002 H HE1  . TYR   B  1 327 ? 54.909 -17.057 -56.312 0.00 28.69  ? 353  TYR   B HE1  1 
ATOM   17003 H HE2  . TYR   B  1 327 ? 50.816 -18.262 -56.375 0.00 30.28  ? 353  TYR   B HE2  1 
ATOM   17004 H HH   . TYR   B  1 327 ? 53.652 -17.308 -54.419 0.00 30.15  ? 353  TYR   B HH   1 
ATOM   17005 N N    . PRO   B  1 328 ? 56.243 -19.414 -61.366 1.00 25.64  ? 354  PRO   B N    1 
ATOM   17006 C CA   . PRO   B  1 328 ? 56.851 -20.760 -61.339 1.00 25.98  ? 354  PRO   B CA   1 
ATOM   17007 C C    . PRO   B  1 328 ? 57.040 -21.333 -59.956 1.00 26.58  ? 354  PRO   B C    1 
ATOM   17008 O O    . PRO   B  1 328 ? 57.118 -20.586 -58.991 1.00 25.67  ? 354  PRO   B O    1 
ATOM   17009 C CB   . PRO   B  1 328 ? 58.209 -20.549 -62.013 1.00 26.31  ? 354  PRO   B CB   1 
ATOM   17010 C CG   . PRO   B  1 328 ? 58.529 -19.101 -61.739 1.00 26.46  ? 354  PRO   B CG   1 
ATOM   17011 C CD   . PRO   B  1 328 ? 57.197 -18.409 -61.875 1.00 24.87  ? 354  PRO   B CD   1 
ATOM   17012 H HA   . PRO   B  1 328 ? 56.261 -21.453 -61.938 0.00 34.26  ? 354  PRO   B HA   1 
ATOM   17013 H HB2  . PRO   B  1 328 ? 58.953 -21.205 -61.563 0.00 34.48  ? 354  PRO   B HB2  1 
ATOM   17014 H HB3  . PRO   B  1 328 ? 58.123 -20.732 -63.083 0.00 34.65  ? 354  PRO   B HB3  1 
ATOM   17015 H HG2  . PRO   B  1 328 ? 58.924 -18.993 -60.730 0.00 33.49  ? 354  PRO   B HG2  1 
ATOM   17016 H HG3  . PRO   B  1 328 ? 59.238 -18.732 -62.478 0.00 33.83  ? 354  PRO   B HG3  1 
ATOM   17017 H HD2  . PRO   B  1 328 ? 57.191 -17.511 -61.260 0.00 31.09  ? 354  PRO   B HD2  1 
ATOM   17018 H HD3  . PRO   B  1 328 ? 56.991 -18.182 -62.920 0.00 31.79  ? 354  PRO   B HD3  1 
ATOM   17019 N N    . GLN   B  1 329 ? 57.149 -22.657 -59.869 1.00 26.98  ? 355  GLN   B N    1 
ATOM   17020 C CA   . GLN   B  1 329 ? 57.363 -23.311 -58.586 1.00 28.15  ? 355  GLN   B CA   1 
ATOM   17021 C C    . GLN   B  1 329 ? 58.675 -22.894 -57.918 1.00 27.74  ? 355  GLN   B C    1 
ATOM   17022 O O    . GLN   B  1 329 ? 58.697 -22.677 -56.704 1.00 27.26  ? 355  GLN   B O    1 
ATOM   17023 C CB   . GLN   B  1 329 ? 57.343 -24.835 -58.766 1.00 31.33  ? 355  GLN   B CB   1 
ATOM   17024 C CG   . GLN   B  1 329 ? 55.952 -25.399 -59.078 1.00 38.14  ? 355  GLN   B CG   1 
ATOM   17025 C CD   . GLN   B  1 329 ? 54.985 -25.275 -57.917 1.00 46.13  ? 355  GLN   B CD   1 
ATOM   17026 O OE1  . GLN   B  1 329 ? 55.370 -25.046 -56.763 1.00 49.02  ? 355  GLN   B OE1  1 
ATOM   17027 N NE2  . GLN   B  1 329 ? 53.700 -25.417 -58.197 1.00 47.73  ? 355  GLN   B NE2  1 
ATOM   17028 H H    . GLN   B  1 329 ? 57.090 -23.288 -60.661 0.00 36.00  ? 355  GLN   B H    1 
ATOM   17029 H HA   . GLN   B  1 329 ? 56.553 -23.023 -57.918 0.00 36.63  ? 355  GLN   B HA   1 
ATOM   17030 H HB2  . GLN   B  1 329 ? 58.003 -25.105 -59.589 0.00 41.87  ? 355  GLN   B HB2  1 
ATOM   17031 H HB3  . GLN   B  1 329 ? 57.705 -25.304 -57.852 0.00 41.57  ? 355  GLN   B HB3  1 
ATOM   17032 H HG2  . GLN   B  1 329 ? 55.532 -24.859 -59.925 0.00 49.98  ? 355  GLN   B HG2  1 
ATOM   17033 H HG3  . GLN   B  1 329 ? 56.046 -26.456 -59.323 0.00 50.67  ? 355  GLN   B HG3  1 
ATOM   17034 H HE21 . GLN   B  1 329 ? 53.404 -25.601 -59.150 0.00 61.72  ? 355  GLN   B HE21 1 
ATOM   17035 H HE22 . GLN   B  1 329 ? 53.009 -25.343 -57.457 0.00 61.20  ? 355  GLN   B HE22 1 
ATOM   17036 N N    . HIS   B  1 330 ? 59.758 -22.778 -58.702 1.00 27.69  ? 356  HIS   B N    1 
ATOM   17037 C CA   . HIS   B  1 330 ? 61.088 -22.507 -58.166 1.00 28.20  ? 356  HIS   B CA   1 
ATOM   17038 C C    . HIS   B  1 330 ? 61.841 -21.406 -58.909 1.00 27.46  ? 356  HIS   B C    1 
ATOM   17039 O O    . HIS   B  1 330 ? 61.541 -21.109 -60.065 1.00 27.61  ? 356  HIS   B O    1 
ATOM   17040 C CB   . HIS   B  1 330 ? 61.942 -23.805 -58.257 1.00 30.16  ? 356  HIS   B CB   1 
ATOM   17041 C CG   . HIS   B  1 330 ? 61.279 -25.006 -57.658 1.00 33.39  ? 356  HIS   B CG   1 
ATOM   17042 N ND1  . HIS   B  1 330 ? 60.956 -26.106 -58.424 1.00 35.25  ? 356  HIS   B ND1  1 
ATOM   17043 C CD2  . HIS   B  1 330 ? 60.835 -25.205 -56.396 1.00 34.69  ? 356  HIS   B CD2  1 
ATOM   17044 C CE1  . HIS   B  1 330 ? 60.362 -26.956 -57.603 1.00 35.81  ? 356  HIS   B CE1  1 
ATOM   17045 N NE2  . HIS   B  1 330 ? 60.258 -26.452 -56.374 1.00 35.99  ? 356  HIS   B NE2  1 
ATOM   17046 H H    . HIS   B  1 330 ? 59.748 -22.873 -59.712 0.00 36.50  ? 356  HIS   B H    1 
ATOM   17047 H HA   . HIS   B  1 330 ? 61.030 -22.219 -57.118 0.00 36.34  ? 356  HIS   B HA   1 
ATOM   17048 H HB2  . HIS   B  1 330 ? 62.140 -24.022 -59.306 0.00 40.09  ? 356  HIS   B HB2  1 
ATOM   17049 H HB3  . HIS   B  1 330 ? 62.881 -23.645 -57.730 0.00 39.65  ? 356  HIS   B HB3  1 
ATOM   17050 H HD1  . HIS   B  1 330 ? 61.137 -26.237 -59.414 0.00 47.27  ? 356  HIS   B HD1  1 
ATOM   17051 H HD2  . HIS   B  1 330 ? 60.916 -24.520 -55.570 0.00 44.94  ? 356  HIS   B HD2  1 
ATOM   17052 H HE1  . HIS   B  1 330 ? 60.008 -27.931 -57.892 0.00 48.47  ? 356  HIS   B HE1  1 
ATOM   17053 N N    . ILE   B  1 331 ? 62.863 -20.852 -58.241 1.00 26.44  ? 357  ILE   B N    1 
ATOM   17054 C CA   . ILE   B  1 331 ? 63.786 -19.877 -58.814 1.00 26.38  ? 357  ILE   B CA   1 
ATOM   17055 C C    . ILE   B  1 331 ? 64.906 -20.674 -59.516 1.00 26.78  ? 357  ILE   B C    1 
ATOM   17056 O O    . ILE   B  1 331 ? 65.342 -21.706 -59.006 1.00 26.81  ? 357  ILE   B O    1 
ATOM   17057 C CB   . ILE   B  1 331 ? 64.330 -18.844 -57.770 1.00 26.17  ? 357  ILE   B CB   1 
ATOM   17058 C CG1  . ILE   B  1 331 ? 65.099 -17.719 -58.485 1.00 27.22  ? 357  ILE   B CG1  1 
ATOM   17059 C CG2  . ILE   B  1 331 ? 65.213 -19.481 -56.670 1.00 26.08  ? 357  ILE   B CG2  1 
ATOM   17060 C CD1  . ILE   B  1 331 ? 65.351 -16.458 -57.601 1.00 28.36  ? 357  ILE   B CD1  1 
ATOM   17061 H H    . ILE   B  1 331 ? 63.055 -21.089 -57.275 0.00 33.93  ? 357  ILE   B H    1 
ATOM   17062 H HA   . ILE   B  1 331 ? 63.257 -19.307 -59.576 0.00 33.55  ? 357  ILE   B HA   1 
ATOM   17063 H HB   . ILE   B  1 331 ? 63.470 -18.393 -57.278 0.00 32.50  ? 357  ILE   B HB   1 
ATOM   17064 H HG12 . ILE   B  1 331 ? 66.070 -18.097 -58.800 0.00 34.22  ? 357  ILE   B HG12 1 
ATOM   17065 H HG13 . ILE   B  1 331 ? 64.531 -17.393 -59.356 0.00 33.85  ? 357  ILE   B HG13 1 
ATOM   17066 H HG21 . ILE   B  1 331 ? 65.385 -18.743 -55.889 0.00 32.54  ? 357  ILE   B HG21 1 
ATOM   17067 H HG22 . ILE   B  1 331 ? 64.720 -20.351 -56.239 0.00 33.20  ? 357  ILE   B HG22 1 
ATOM   17068 H HG23 . ILE   B  1 331 ? 66.167 -19.776 -57.104 0.00 33.27  ? 357  ILE   B HG23 1 
ATOM   17069 H HD11 . ILE   B  1 331 ? 65.771 -15.669 -58.223 0.00 34.52  ? 357  ILE   B HD11 1 
ATOM   17070 H HD12 . ILE   B  1 331 ? 64.406 -16.132 -57.170 0.00 34.34  ? 357  ILE   B HD12 1 
ATOM   17071 H HD13 . ILE   B  1 331 ? 66.054 -16.713 -56.809 0.00 34.72  ? 357  ILE   B HD13 1 
ATOM   17072 N N    . ASN   B  1 332 ? 65.325 -20.223 -60.706 1.00 27.04  ? 358  ASN   B N    1 
ATOM   17073 C CA   . ASN   B  1 332 ? 66.363 -20.897 -61.474 1.00 28.08  ? 358  ASN   B CA   1 
ATOM   17074 C C    . ASN   B  1 332 ? 67.622 -19.996 -61.557 1.00 27.80  ? 358  ASN   B C    1 
ATOM   17075 O O    . ASN   B  1 332 ? 67.704 -19.092 -62.390 1.00 27.69  ? 358  ASN   B O    1 
ATOM   17076 C CB   . ASN   B  1 332 ? 65.826 -21.280 -62.854 1.00 30.03  ? 358  ASN   B CB   1 
ATOM   17077 C CG   . ASN   B  1 332 ? 66.752 -22.178 -63.641 1.00 34.82  ? 358  ASN   B CG   1 
ATOM   17078 O OD1  . ASN   B  1 332 ? 67.873 -22.484 -63.224 1.00 36.32  ? 358  ASN   B OD1  1 
ATOM   17079 N ND2  . ASN   B  1 332 ? 66.301 -22.624 -64.807 1.00 36.40  ? 358  ASN   B ND2  1 
ATOM   17080 H H    . ASN   B  1 332 ? 64.967 -19.388 -61.159 0.00 34.89  ? 358  ASN   B H    1 
ATOM   17081 H HA   . ASN   B  1 332 ? 66.647 -21.827 -60.985 0.00 37.41  ? 358  ASN   B HA   1 
ATOM   17082 H HB2  . ASN   B  1 332 ? 64.887 -21.815 -62.724 0.00 39.92  ? 358  ASN   B HB2  1 
ATOM   17083 H HB3  . ASN   B  1 332 ? 65.656 -20.378 -63.439 0.00 39.53  ? 358  ASN   B HB3  1 
ATOM   17084 H HD21 . ASN   B  1 332 ? 66.883 -23.230 -65.377 0.00 49.19  ? 358  ASN   B HD21 1 
ATOM   17085 H HD22 . ASN   B  1 332 ? 65.376 -22.361 -65.129 0.00 48.52  ? 358  ASN   B HD22 1 
ATOM   17086 N N    . ILE   B  1 333 ? 68.592 -20.278 -60.678 1.00 27.59  ? 359  ILE   B N    1 
ATOM   17087 C CA   . ILE   B  1 333 ? 69.865 -19.549 -60.542 1.00 27.80  ? 359  ILE   B CA   1 
ATOM   17088 C C    . ILE   B  1 333 ? 70.987 -20.316 -61.244 1.00 27.81  ? 359  ILE   B C    1 
ATOM   17089 O O    . ILE   B  1 333 ? 71.256 -21.458 -60.881 1.00 27.77  ? 359  ILE   B O    1 
ATOM   17090 C CB   . ILE   B  1 333 ? 70.181 -19.398 -59.025 1.00 28.38  ? 359  ILE   B CB   1 
ATOM   17091 C CG1  . ILE   B  1 333 ? 69.084 -18.594 -58.288 1.00 29.20  ? 359  ILE   B CG1  1 
ATOM   17092 C CG2  . ILE   B  1 333 ? 71.544 -18.794 -58.797 1.00 29.29  ? 359  ILE   B CG2  1 
ATOM   17093 C CD1  . ILE   B  1 333 ? 68.832 -17.193 -58.810 1.00 30.00  ? 359  ILE   B CD1  1 
ATOM   17094 H H    . ILE   B  1 333 ? 68.525 -21.045 -60.016 0.00 36.55  ? 359  ILE   B H    1 
ATOM   17095 H HA   . ILE   B  1 333 ? 69.792 -18.559 -60.990 0.00 36.13  ? 359  ILE   B HA   1 
ATOM   17096 H HB   . ILE   B  1 333 ? 70.201 -20.396 -58.587 0.00 37.25  ? 359  ILE   B HB   1 
ATOM   17097 H HG12 . ILE   B  1 333 ? 68.143 -19.139 -58.353 0.00 37.27  ? 359  ILE   B HG12 1 
ATOM   17098 H HG13 . ILE   B  1 333 ? 69.363 -18.504 -57.239 0.00 37.04  ? 359  ILE   B HG13 1 
ATOM   17099 H HG21 . ILE   B  1 333 ? 71.595 -18.394 -57.786 0.00 37.64  ? 359  ILE   B HG21 1 
ATOM   17100 H HG22 . ILE   B  1 333 ? 72.307 -19.562 -58.912 0.00 38.47  ? 359  ILE   B HG22 1 
ATOM   17101 H HG23 . ILE   B  1 333 ? 71.702 -17.997 -59.522 0.00 37.78  ? 359  ILE   B HG23 1 
ATOM   17102 H HD11 . ILE   B  1 333 ? 68.204 -16.666 -58.092 0.00 37.20  ? 359  ILE   B HD11 1 
ATOM   17103 H HD12 . ILE   B  1 333 ? 69.777 -16.665 -58.931 0.00 37.61  ? 359  ILE   B HD12 1 
ATOM   17104 H HD13 . ILE   B  1 333 ? 68.313 -17.255 -59.765 0.00 37.75  ? 359  ILE   B HD13 1 
ATOM   17105 N N    . SER   B  1 334 ? 71.657 -19.687 -62.219 1.00 27.46  ? 360  SER   B N    1 
ATOM   17106 C CA   . SER   B  1 334 ? 72.757 -20.320 -62.948 1.00 28.19  ? 360  SER   B CA   1 
ATOM   17107 C C    . SER   B  1 334 ? 73.882 -20.758 -62.032 1.00 29.60  ? 360  SER   B C    1 
ATOM   17108 O O    . SER   B  1 334 ? 74.203 -20.058 -61.071 1.00 30.19  ? 360  SER   B O    1 
ATOM   17109 C CB   . SER   B  1 334 ? 73.355 -19.336 -63.952 1.00 28.59  ? 360  SER   B CB   1 
ATOM   17110 O OG   . SER   B  1 334 ? 74.445 -19.908 -64.659 1.00 29.23  ? 360  SER   B OG   1 
ATOM   17111 H H    . SER   B  1 334 ? 71.459 -18.740 -62.527 0.00 36.42  ? 360  SER   B H    1 
ATOM   17112 H HA   . SER   B  1 334 ? 72.380 -21.186 -63.490 0.00 38.80  ? 360  SER   B HA   1 
ATOM   17113 H HB2  . SER   B  1 334 ? 72.585 -19.047 -64.665 0.00 38.64  ? 360  SER   B HB2  1 
ATOM   17114 H HB3  . SER   B  1 334 ? 73.710 -18.458 -63.415 0.00 38.33  ? 360  SER   B HB3  1 
ATOM   17115 H HG   . SER   B  1 334 ? 74.800 -19.259 -65.321 0.00 40.13  ? 360  SER   B HG   1 
ATOM   17116 N N    . ARG   B  1 335 ? 74.550 -21.867 -62.380 1.00 30.36  ? 361  ARG   B N    1 
ATOM   17117 C CA   . ARG   B  1 335 ? 75.761 -22.292 -61.674 1.00 31.23  ? 361  ARG   B CA   1 
ATOM   17118 C C    . ARG   B  1 335 ? 76.856 -21.193 -61.765 1.00 30.31  ? 361  ARG   B C    1 
ATOM   17119 O O    . ARG   B  1 335 ? 77.708 -21.125 -60.879 1.00 30.27  ? 361  ARG   B O    1 
ATOM   17120 C CB   . ARG   B  1 335 ? 76.321 -23.599 -62.266 1.00 34.58  ? 361  ARG   B CB   1 
ATOM   17121 C CG   . ARG   B  1 335 ? 75.573 -24.862 -61.852 1.00 41.40  ? 361  ARG   B CG   1 
ATOM   17122 C CD   . ARG   B  1 335 ? 76.384 -26.100 -62.208 1.00 49.03  ? 361  ARG   B CD   1 
ATOM   17123 N NE   . ARG   B  1 335 ? 75.740 -27.353 -61.802 1.00 55.43  ? 361  ARG   B NE   1 
ATOM   17124 C CZ   . ARG   B  1 335 ? 74.746 -27.950 -62.459 1.00 60.40  ? 361  ARG   B CZ   1 
ATOM   17125 N NH1  . ARG   B  1 335 ? 74.242 -29.095 -62.014 1.00 61.51  ? 361  ARG   B NH1  1 
ATOM   17126 N NH2  . ARG   B  1 335 ? 74.237 -27.400 -63.560 1.00 60.93  ? 361  ARG   B NH2  1 
ATOM   17127 H H    . ARG   B  1 335 ? 74.277 -22.483 -63.140 0.00 42.37  ? 361  ARG   B H    1 
ATOM   17128 H HA   . ARG   B  1 335 ? 75.527 -22.459 -60.625 0.00 43.22  ? 361  ARG   B HA   1 
ATOM   17129 H HB2  . ARG   B  1 335 ? 76.303 -23.538 -63.353 0.00 48.52  ? 361  ARG   B HB2  1 
ATOM   17130 H HB3  . ARG   B  1 335 ? 77.352 -23.704 -61.931 0.00 48.61  ? 361  ARG   B HB3  1 
ATOM   17131 H HG2  . ARG   B  1 335 ? 75.409 -24.852 -60.775 0.00 56.62  ? 361  ARG   B HG2  1 
ATOM   17132 H HG3  . ARG   B  1 335 ? 74.621 -24.909 -62.379 0.00 56.79  ? 361  ARG   B HG3  1 
ATOM   17133 H HD2  . ARG   B  1 335 ? 76.573 -26.124 -63.280 0.00 67.30  ? 361  ARG   B HD2  1 
ATOM   17134 H HD3  . ARG   B  1 335 ? 77.335 -26.048 -61.680 0.00 67.13  ? 361  ARG   B HD3  1 
ATOM   17135 H HE   . ARG   B  1 335 ? 76.102 -27.808 -60.970 0.00 75.30  ? 361  ARG   B HE   1 
ATOM   17136 H HH11 . ARG   B  1 335 ? 74.612 -29.525 -61.172 0.00 83.25  ? 361  ARG   B HH11 1 
ATOM   17137 H HH12 . ARG   B  1 335 ? 73.474 -29.542 -62.504 0.00 83.28  ? 361  ARG   B HH12 1 
ATOM   17138 H HH21 . ARG   B  1 335 ? 74.582 -26.523 -63.935 0.00 81.44  ? 361  ARG   B HH21 1 
ATOM   17139 H HH22 . ARG   B  1 335 ? 73.471 -27.863 -64.040 0.00 81.96  ? 361  ARG   B HH22 1 
ATOM   17140 N N    . ASN   B  1 336 ? 76.818 -20.331 -62.821 1.00 28.99  ? 362  ASN   B N    1 
ATOM   17141 C CA   . ASN   B  1 336 ? 77.773 -19.234 -63.003 1.00 28.77  ? 362  ASN   B CA   1 
ATOM   17142 C C    . ASN   B  1 336 ? 77.723 -18.169 -61.892 1.00 28.09  ? 362  ASN   B C    1 
ATOM   17143 O O    . ASN   B  1 336 ? 78.645 -17.358 -61.811 1.00 28.26  ? 362  ASN   B O    1 
ATOM   17144 C CB   . ASN   B  1 336 ? 77.599 -18.567 -64.371 1.00 29.71  ? 362  ASN   B CB   1 
ATOM   17145 C CG   . ASN   B  1 336 ? 78.024 -19.424 -65.533 1.00 33.92  ? 362  ASN   B CG   1 
ATOM   17146 O OD1  . ASN   B  1 336 ? 78.902 -20.292 -65.416 1.00 35.05  ? 362  ASN   B OD1  1 
ATOM   17147 N ND2  . ASN   B  1 336 ? 77.427 -19.181 -66.695 1.00 34.68  ? 362  ASN   B ND2  1 
ATOM   17148 H H    . ASN   B  1 336 ? 76.137 -20.381 -63.571 0.00 40.29  ? 362  ASN   B H    1 
ATOM   17149 H HA   . ASN   B  1 336 ? 78.776 -19.657 -62.965 0.00 40.30  ? 362  ASN   B HA   1 
ATOM   17150 H HB2  . ASN   B  1 336 ? 76.557 -18.281 -64.500 0.00 40.52  ? 362  ASN   B HB2  1 
ATOM   17151 H HB3  . ASN   B  1 336 ? 78.236 -17.684 -64.396 0.00 40.70  ? 362  ASN   B HB3  1 
ATOM   17152 H HD21 . ASN   B  1 336 ? 77.675 -19.728 -67.513 0.00 48.14  ? 362  ASN   B HD21 1 
ATOM   17153 H HD22 . ASN   B  1 336 ? 76.729 -18.448 -66.773 0.00 47.13  ? 362  ASN   B HD22 1 
ATOM   17154 N N    . PHE   B  1 337 ? 76.667 -18.147 -61.046 1.00 26.99  ? 363  PHE   B N    1 
ATOM   17155 C CA   . PHE   B  1 337 ? 76.651 -17.238 -59.891 1.00 26.20  ? 363  PHE   B CA   1 
ATOM   17156 C C    . PHE   B  1 337 ? 77.832 -17.572 -58.928 1.00 26.38  ? 363  PHE   B C    1 
ATOM   17157 O O    . PHE   B  1 337 ? 78.286 -16.691 -58.206 1.00 26.44  ? 363  PHE   B O    1 
ATOM   17158 C CB   . PHE   B  1 337 ? 75.305 -17.296 -59.122 1.00 25.28  ? 363  PHE   B CB   1 
ATOM   17159 C CG   . PHE   B  1 337 ? 74.234 -16.355 -59.641 1.00 24.35  ? 363  PHE   B CG   1 
ATOM   17160 C CD1  . PHE   B  1 337 ? 73.454 -16.701 -60.735 1.00 24.60  ? 363  PHE   B CD1  1 
ATOM   17161 C CD2  . PHE   B  1 337 ? 74.064 -15.099 -59.085 1.00 24.34  ? 363  PHE   B CD2  1 
ATOM   17162 C CE1  . PHE   B  1 337 ? 72.465 -15.846 -61.201 1.00 24.66  ? 363  PHE   B CE1  1 
ATOM   17163 C CE2  . PHE   B  1 337 ? 73.086 -14.236 -59.566 1.00 24.71  ? 363  PHE   B CE2  1 
ATOM   17164 C CZ   . PHE   B  1 337 ? 72.301 -14.612 -60.626 1.00 24.68  ? 363  PHE   B CZ   1 
ATOM   17165 H H    . PHE   B  1 337 ? 75.830 -18.712 -61.146 0.00 36.59  ? 363  PHE   B H    1 
ATOM   17166 H HA   . PHE   B  1 337 ? 76.814 -16.221 -60.246 0.00 34.73  ? 363  PHE   B HA   1 
ATOM   17167 H HB2  . PHE   B  1 337 ? 74.908 -18.310 -59.147 0.00 33.78  ? 363  PHE   B HB2  1 
ATOM   17168 H HB3  . PHE   B  1 337 ? 75.508 -17.015 -58.091 0.00 33.26  ? 363  PHE   B HB3  1 
ATOM   17169 H HD1  . PHE   B  1 337 ? 73.568 -17.674 -61.181 0.00 32.73  ? 363  PHE   B HD1  1 
ATOM   17170 H HD2  . PHE   B  1 337 ? 74.674 -14.798 -58.250 0.00 31.11  ? 363  PHE   B HD2  1 
ATOM   17171 H HE1  . PHE   B  1 337 ? 71.851 -16.137 -62.036 0.00 31.98  ? 363  PHE   B HE1  1 
ATOM   17172 H HE2  . PHE   B  1 337 ? 72.952 -13.267 -59.114 0.00 30.73  ? 363  PHE   B HE2  1 
ATOM   17173 H HZ   . PHE   B  1 337 ? 71.548 -13.941 -61.001 0.00 30.94  ? 363  PHE   B HZ   1 
ATOM   17174 N N    . SER   B  1 338 ? 78.330 -18.823 -58.936 1.00 26.23  ? 364  SER   B N    1 
ATOM   17175 C CA   . SER   B  1 338 ? 79.484 -19.244 -58.137 1.00 26.81  ? 364  SER   B CA   1 
ATOM   17176 C C    . SER   B  1 338 ? 80.800 -18.521 -58.537 1.00 27.88  ? 364  SER   B C    1 
ATOM   17177 O O    . SER   B  1 338 ? 81.788 -18.603 -57.795 1.00 28.74  ? 364  SER   B O    1 
ATOM   17178 C CB   . SER   B  1 338 ? 79.689 -20.753 -58.253 1.00 27.40  ? 364  SER   B CB   1 
ATOM   17179 O OG   . SER   B  1 338 ? 80.193 -21.115 -59.530 1.00 30.62  ? 364  SER   B OG   1 
ATOM   17180 H H    . SER   B  1 338 ? 77.937 -19.580 -59.487 0.00 36.38  ? 364  SER   B H    1 
ATOM   17181 H HA   . SER   B  1 338 ? 79.283 -19.016 -57.091 0.00 36.92  ? 364  SER   B HA   1 
ATOM   17182 H HB2  . SER   B  1 338 ? 80.408 -21.065 -57.497 0.00 38.97  ? 364  SER   B HB2  1 
ATOM   17183 H HB3  . SER   B  1 338 ? 78.740 -21.260 -58.086 0.00 38.59  ? 364  SER   B HB3  1 
ATOM   17184 H HG   . SER   B  1 338 ? 79.713 -20.631 -60.252 0.00 42.80  ? 364  SER   B HG   1 
ATOM   17185 N N    . LYS   B  1 339 ? 80.820 -17.848 -59.701 1.00 27.37  ? 365  LYS   B N    1 
ATOM   17186 C CA   . LYS   B  1 339 ? 81.973 -17.093 -60.185 1.00 27.78  ? 365  LYS   B CA   1 
ATOM   17187 C C    . LYS   B  1 339 ? 82.003 -15.656 -59.657 1.00 27.38  ? 365  LYS   B C    1 
ATOM   17188 O O    . LYS   B  1 339 ? 83.009 -14.970 -59.872 1.00 27.78  ? 365  LYS   B O    1 
ATOM   17189 C CB   . LYS   B  1 339 ? 81.984 -17.067 -61.724 1.00 30.28  ? 365  LYS   B CB   1 
ATOM   17190 C CG   . LYS   B  1 339 ? 81.928 -18.445 -62.388 1.00 34.94  ? 365  LYS   B CG   1 
ATOM   17191 C CD   . LYS   B  1 339 ? 83.138 -19.302 -62.061 1.00 41.24  ? 365  LYS   B CD   1 
ATOM   17192 C CE   . LYS   B  1 339 ? 83.162 -20.585 -62.853 1.00 46.44  ? 365  LYS   B CE   1 
ATOM   17193 N NZ   . LYS   B  1 339 ? 84.032 -21.606 -62.208 1.00 48.97  ? 365  LYS   B NZ   1 
ATOM   17194 H H    . LYS   B  1 339 ? 80.041 -17.806 -60.349 0.00 37.77  ? 365  LYS   B H    1 
ATOM   17195 H HA   . LYS   B  1 339 ? 82.892 -17.574 -59.854 0.00 39.07  ? 365  LYS   B HA   1 
ATOM   17196 H HB2  . LYS   B  1 339 ? 81.121 -16.498 -62.065 0.00 41.36  ? 365  LYS   B HB2  1 
ATOM   17197 H HB3  . LYS   B  1 339 ? 82.899 -16.577 -62.057 0.00 42.00  ? 365  LYS   B HB3  1 
ATOM   17198 H HG2  . LYS   B  1 339 ? 81.032 -18.976 -62.069 0.00 47.95  ? 365  LYS   B HG2  1 
ATOM   17199 H HG3  . LYS   B  1 339 ? 81.910 -18.309 -63.468 0.00 48.22  ? 365  LYS   B HG3  1 
ATOM   17200 H HD2  . LYS   B  1 339 ? 84.045 -18.744 -62.289 0.00 56.53  ? 365  LYS   B HD2  1 
ATOM   17201 H HD3  . LYS   B  1 339 ? 83.117 -19.572 -61.006 0.00 56.34  ? 365  LYS   B HD3  1 
ATOM   17202 H HE2  . LYS   B  1 339 ? 82.152 -20.987 -62.916 0.00 63.21  ? 365  LYS   B HE2  1 
ATOM   17203 H HE3  . LYS   B  1 339 ? 83.551 -20.385 -63.850 0.00 63.60  ? 365  LYS   B HE3  1 
ATOM   17204 H HZ1  . LYS   B  1 339 ? 84.073 -22.439 -62.786 0.00 67.63  ? 365  LYS   B HZ1  1 
ATOM   17205 H HZ2  . LYS   B  1 339 ? 84.971 -21.239 -62.092 0.00 67.28  ? 365  LYS   B HZ2  1 
ATOM   17206 H HZ3  . LYS   B  1 339 ? 83.659 -21.857 -61.298 0.00 66.94  ? 365  LYS   B HZ3  1 
ATOM   17207 N N    . LEU   B  1 340 ? 80.923 -15.185 -58.981 1.00 26.44  ? 366  LEU   B N    1 
ATOM   17208 C CA   . LEU   B  1 340 ? 80.884 -13.853 -58.398 1.00 26.15  ? 366  LEU   B CA   1 
ATOM   17209 C C    . LEU   B  1 340 ? 81.586 -13.908 -57.035 1.00 26.03  ? 366  LEU   B C    1 
ATOM   17210 O O    . LEU   B  1 340 ? 80.969 -13.673 -55.990 1.00 25.57  ? 366  LEU   B O    1 
ATOM   17211 C CB   . LEU   B  1 340 ? 79.436 -13.382 -58.248 1.00 25.88  ? 366  LEU   B CB   1 
ATOM   17212 C CG   . LEU   B  1 340 ? 78.609 -13.294 -59.533 1.00 26.43  ? 366  LEU   B CG   1 
ATOM   17213 C CD1  . LEU   B  1 340 ? 77.140 -12.988 -59.196 1.00 26.70  ? 366  LEU   B CD1  1 
ATOM   17214 C CD2  . LEU   B  1 340 ? 79.180 -12.231 -60.474 1.00 26.40  ? 366  LEU   B CD2  1 
ATOM   17215 H H    . LEU   B  1 340 ? 80.060 -15.698 -58.831 0.00 35.60  ? 366  LEU   B H    1 
ATOM   17216 H HA   . LEU   B  1 340 ? 81.422 -13.141 -59.023 0.00 34.82  ? 366  LEU   B HA   1 
ATOM   17217 H HB2  . LEU   B  1 340 ? 78.907 -14.039 -57.560 0.00 33.80  ? 366  LEU   B HB2  1 
ATOM   17218 H HB3  . LEU   B  1 340 ? 79.471 -12.368 -57.853 0.00 33.45  ? 366  LEU   B HB3  1 
ATOM   17219 H HG   . LEU   B  1 340 ? 78.638 -14.254 -60.046 0.00 34.78  ? 366  LEU   B HG   1 
ATOM   17220 H HD11 . LEU   B  1 340 ? 76.597 -12.760 -60.110 0.00 34.02  ? 366  LEU   B HD11 1 
ATOM   17221 H HD12 . LEU   B  1 340 ? 76.701 -13.858 -58.710 0.00 34.21  ? 366  LEU   B HD12 1 
ATOM   17222 H HD13 . LEU   B  1 340 ? 77.106 -12.130 -58.526 0.00 33.73  ? 366  LEU   B HD13 1 
ATOM   17223 H HD21 . LEU   B  1 340 ? 78.490 -12.086 -61.304 0.00 34.15  ? 366  LEU   B HD21 1 
ATOM   17224 H HD22 . LEU   B  1 340 ? 79.307 -11.295 -59.932 0.00 33.95  ? 366  LEU   B HD22 1 
ATOM   17225 H HD23 . LEU   B  1 340 ? 80.139 -12.572 -60.861 0.00 34.75  ? 366  LEU   B HD23 1 
ATOM   17226 N N    . LEU   B  1 341 ? 82.910 -14.138 -57.086 1.00 26.13  ? 367  LEU   B N    1 
ATOM   17227 C CA   . LEU   B  1 341 ? 83.761 -14.331 -55.910 1.00 26.53  ? 367  LEU   B CA   1 
ATOM   17228 C C    . LEU   B  1 341 ? 83.628 -13.231 -54.845 1.00 25.74  ? 367  LEU   B C    1 
ATOM   17229 O O    . LEU   B  1 341 ? 83.604 -13.550 -53.657 1.00 25.83  ? 367  LEU   B O    1 
ATOM   17230 C CB   . LEU   B  1 341 ? 85.241 -14.470 -56.313 1.00 27.58  ? 367  LEU   B CB   1 
ATOM   17231 C CG   . LEU   B  1 341 ? 85.632 -15.528 -57.370 1.00 30.69  ? 367  LEU   B CG   1 
ATOM   17232 C CD1  . LEU   B  1 341 ? 87.140 -15.552 -57.564 1.00 31.56  ? 367  LEU   B CD1  1 
ATOM   17233 C CD2  . LEU   B  1 341 ? 85.125 -16.923 -56.990 1.00 31.74  ? 367  LEU   B CD2  1 
ATOM   17234 H H    . LEU   B  1 341 ? 83.416 -14.149 -57.964 0.00 35.75  ? 367  LEU   B H    1 
ATOM   17235 H HA   . LEU   B  1 341 ? 83.463 -15.268 -55.441 0.00 36.43  ? 367  LEU   B HA   1 
ATOM   17236 H HB2  . LEU   B  1 341 ? 85.572 -13.505 -56.697 0.00 38.00  ? 367  LEU   B HB2  1 
ATOM   17237 H HB3  . LEU   B  1 341 ? 85.807 -14.705 -55.413 0.00 38.43  ? 367  LEU   B HB3  1 
ATOM   17238 H HG   . LEU   B  1 341 ? 85.192 -15.262 -58.330 0.00 42.35  ? 367  LEU   B HG   1 
ATOM   17239 H HD11 . LEU   B  1 341 ? 87.389 -16.295 -58.320 0.00 44.71  ? 367  LEU   B HD11 1 
ATOM   17240 H HD12 . LEU   B  1 341 ? 87.471 -14.566 -57.886 0.00 44.05  ? 367  LEU   B HD12 1 
ATOM   17241 H HD13 . LEU   B  1 341 ? 87.612 -15.809 -56.617 0.00 44.48  ? 367  LEU   B HD13 1 
ATOM   17242 H HD21 . LEU   B  1 341 ? 85.524 -17.649 -57.697 0.00 44.64  ? 367  LEU   B HD21 1 
ATOM   17243 H HD22 . LEU   B  1 341 ? 85.462 -17.164 -55.983 0.00 44.27  ? 367  LEU   B HD22 1 
ATOM   17244 H HD23 . LEU   B  1 341 ? 84.037 -16.933 -57.027 0.00 43.69  ? 367  LEU   B HD23 1 
ATOM   17245 N N    . SER   B  1 342 ? 83.531 -11.954 -55.250 1.00 25.01  ? 368  SER   B N    1 
ATOM   17246 C CA   . SER   B  1 342 ? 83.455 -10.830 -54.301 1.00 24.69  ? 368  SER   B CA   1 
ATOM   17247 C C    . SER   B  1 342 ? 82.034 -10.393 -53.927 1.00 23.40  ? 368  SER   B C    1 
ATOM   17248 O O    . SER   B  1 342 ? 81.892 -9.388  -53.227 1.00 23.25  ? 368  SER   B O    1 
ATOM   17249 C CB   . SER   B  1 342 ? 84.188 -9.614  -54.864 1.00 26.36  ? 368  SER   B CB   1 
ATOM   17250 O OG   . SER   B  1 342 ? 85.523 -9.940  -55.206 1.00 29.88  ? 368  SER   B OG   1 
ATOM   17251 H H    . SER   B  1 342 ? 83.509 -11.662 -56.221 0.00 33.46  ? 368  SER   B H    1 
ATOM   17252 H HA   . SER   B  1 342 ? 83.966 -11.099 -53.378 0.00 32.92  ? 368  SER   B HA   1 
ATOM   17253 H HB2  . SER   B  1 342 ? 83.667 -9.268  -55.756 0.00 34.40  ? 368  SER   B HB2  1 
ATOM   17254 H HB3  . SER   B  1 342 ? 84.214 -8.821  -54.118 0.00 34.42  ? 368  SER   B HB3  1 
ATOM   17255 H HG   . SER   B  1 342 ? 85.558 -10.331 -56.117 0.00 39.70  ? 368  SER   B HG   1 
ATOM   17256 N N    . LEU   B  1 343 ? 80.988 -11.107 -54.386 1.00 22.27  ? 369  LEU   B N    1 
ATOM   17257 C CA   . LEU   B  1 343 ? 79.610 -10.691 -54.103 1.00 21.62  ? 369  LEU   B CA   1 
ATOM   17258 C C    . LEU   B  1 343 ? 79.317 -10.560 -52.609 1.00 21.40  ? 369  LEU   B C    1 
ATOM   17259 O O    . LEU   B  1 343 ? 79.619 -11.464 -51.832 1.00 21.41  ? 369  LEU   B O    1 
ATOM   17260 C CB   . LEU   B  1 343 ? 78.580 -11.644 -54.735 1.00 21.71  ? 369  LEU   B CB   1 
ATOM   17261 C CG   . LEU   B  1 343 ? 77.166 -11.067 -54.936 1.00 23.73  ? 369  LEU   B CG   1 
ATOM   17262 C CD1  . LEU   B  1 343 ? 77.191 -9.834  -55.880 1.00 25.09  ? 369  LEU   B CD1  1 
ATOM   17263 C CD2  . LEU   B  1 343 ? 76.227 -12.148 -55.459 1.00 24.71  ? 369  LEU   B CD2  1 
ATOM   17264 H H    . LEU   B  1 343 ? 81.056 -11.966 -54.921 0.00 29.26  ? 369  LEU   B H    1 
ATOM   17265 H HA   . LEU   B  1 343 ? 79.503 -9.708  -54.556 0.00 27.27  ? 369  LEU   B HA   1 
ATOM   17266 H HB2  . LEU   B  1 343 ? 78.940 -11.954 -55.713 0.00 27.94  ? 369  LEU   B HB2  1 
ATOM   17267 H HB3  . LEU   B  1 343 ? 78.486 -12.521 -54.096 0.00 27.85  ? 369  LEU   B HB3  1 
ATOM   17268 H HG   . LEU   B  1 343 ? 76.778 -10.736 -53.974 0.00 29.19  ? 369  LEU   B HG   1 
ATOM   17269 H HD11 . LEU   B  1 343 ? 76.203 -9.686  -56.315 0.00 30.56  ? 369  LEU   B HD11 1 
ATOM   17270 H HD12 . LEU   B  1 343 ? 77.459 -8.948  -55.307 0.00 30.64  ? 369  LEU   B HD12 1 
ATOM   17271 H HD13 . LEU   B  1 343 ? 77.924 -10.002 -56.668 0.00 31.18  ? 369  LEU   B HD13 1 
ATOM   17272 H HD21 . LEU   B  1 343 ? 75.294 -11.696 -55.793 0.00 30.39  ? 369  LEU   B HD21 1 
ATOM   17273 H HD22 . LEU   B  1 343 ? 76.707 -12.661 -56.291 0.00 31.14  ? 369  LEU   B HD22 1 
ATOM   17274 H HD23 . LEU   B  1 343 ? 76.026 -12.858 -54.658 0.00 30.86  ? 369  LEU   B HD23 1 
ATOM   17275 N N    . ARG   B  1 344 ? 78.756 -9.416  -52.228 1.00 21.16  ? 370  ARG   B N    1 
ATOM   17276 C CA   . ARG   B  1 344 ? 78.382 -9.082  -50.862 1.00 21.94  ? 370  ARG   B CA   1 
ATOM   17277 C C    . ARG   B  1 344 ? 76.864 -9.016  -50.711 1.00 21.30  ? 370  ARG   B C    1 
ATOM   17278 O O    . ARG   B  1 344 ? 76.355 -9.346  -49.642 1.00 20.83  ? 370  ARG   B O    1 
ATOM   17279 C CB   . ARG   B  1 344 ? 78.975 -7.722  -50.458 1.00 24.02  ? 370  ARG   B CB   1 
ATOM   17280 C CG   . ARG   B  1 344 ? 80.493 -7.688  -50.385 1.00 28.41  ? 370  ARG   B CG   1 
ATOM   17281 C CD   . ARG   B  1 344 ? 80.948 -6.358  -49.811 1.00 34.48  ? 370  ARG   B CD   1 
ATOM   17282 N NE   . ARG   B  1 344 ? 82.407 -6.198  -49.816 1.00 41.03  ? 370  ARG   B NE   1 
ATOM   17283 C CZ   . ARG   B  1 344 ? 83.249 -6.701  -48.911 1.00 45.75  ? 370  ARG   B CZ   1 
ATOM   17284 N NH1  . ARG   B  1 344 ? 82.795 -7.450  -47.908 1.00 46.68  ? 370  ARG   B NH1  1 
ATOM   17285 N NH2  . ARG   B  1 344 ? 84.554 -6.479  -49.014 1.00 46.20  ? 370  ARG   B NH2  1 
ATOM   17286 H H    . ARG   B  1 344 ? 78.541 -8.660  -52.871 0.00 26.04  ? 370  ARG   B H    1 
ATOM   17287 H HA   . ARG   B  1 344 ? 78.759 -9.830  -50.165 0.00 27.27  ? 370  ARG   B HA   1 
ATOM   17288 H HB2  . ARG   B  1 344 ? 78.660 -6.974  -51.184 0.00 29.06  ? 370  ARG   B HB2  1 
ATOM   17289 H HB3  . ARG   B  1 344 ? 78.594 -7.458  -49.473 0.00 29.13  ? 370  ARG   B HB3  1 
ATOM   17290 H HG2  . ARG   B  1 344 ? 80.847 -8.486  -49.733 0.00 35.43  ? 370  ARG   B HG2  1 
ATOM   17291 H HG3  . ARG   B  1 344 ? 80.909 -7.798  -51.385 0.00 35.28  ? 370  ARG   B HG3  1 
ATOM   17292 H HD2  . ARG   B  1 344 ? 80.534 -5.564  -50.432 0.00 41.93  ? 370  ARG   B HD2  1 
ATOM   17293 H HD3  . ARG   B  1 344 ? 80.575 -6.246  -48.795 0.00 42.11  ? 370  ARG   B HD3  1 
ATOM   17294 H HE   . ARG   B  1 344 ? 82.799 -5.627  -50.558 0.00 50.64  ? 370  ARG   B HE   1 
ATOM   17295 H HH11 . ARG   B  1 344 ? 81.809 -7.658  -47.789 0.00 57.57  ? 370  ARG   B HH11 1 
ATOM   17296 H HH12 . ARG   B  1 344 ? 83.454 -7.832  -47.238 0.00 58.29  ? 370  ARG   B HH12 1 
ATOM   17297 H HH21 . ARG   B  1 344 ? 84.923 -5.915  -49.773 0.00 57.77  ? 370  ARG   B HH21 1 
ATOM   17298 H HH22 . ARG   B  1 344 ? 85.197 -6.872  -48.334 0.00 58.15  ? 370  ARG   B HH22 1 
ATOM   17299 N N    . ALA   B  1 345 ? 76.137 -8.517  -51.734 1.00 21.07  ? 371  ALA   B N    1 
ATOM   17300 C CA   . ALA   B  1 345 ? 74.684 -8.384  -51.632 1.00 21.23  ? 371  ALA   B CA   1 
ATOM   17301 C C    . ALA   B  1 345 ? 74.027 -8.750  -52.938 1.00 21.44  ? 371  ALA   B C    1 
ATOM   17302 O O    . ALA   B  1 345 ? 74.454 -8.280  -53.994 1.00 21.29  ? 371  ALA   B O    1 
ATOM   17303 C CB   . ALA   B  1 345 ? 74.319 -6.954  -51.257 1.00 21.40  ? 371  ALA   B CB   1 
ATOM   17304 H H    . ALA   B  1 345 ? 76.513 -8.197  -52.620 0.00 25.17  ? 371  ALA   B H    1 
ATOM   17305 H HA   . ALA   B  1 345 ? 74.293 -9.046  -50.861 0.00 24.88  ? 371  ALA   B HA   1 
ATOM   17306 H HB1  . ALA   B  1 345 ? 73.236 -6.872  -51.186 0.00 24.31  ? 371  ALA   B HB1  1 
ATOM   17307 H HB2  . ALA   B  1 345 ? 74.777 -6.713  -50.299 0.00 24.66  ? 371  ALA   B HB2  1 
ATOM   17308 H HB3  . ALA   B  1 345 ? 74.693 -6.281  -52.026 0.00 24.60  ? 371  ALA   B HB3  1 
ATOM   17309 N N    . LEU   B  1 346 ? 72.983 -9.581  -52.871 1.00 20.70  ? 372  LEU   B N    1 
ATOM   17310 C CA   . LEU   B  1 346 ? 72.243 -10.001 -54.047 1.00 20.47  ? 372  LEU   B CA   1 
ATOM   17311 C C    . LEU   B  1 346 ? 70.785 -9.642  -53.839 1.00 19.76  ? 372  LEU   B C    1 
ATOM   17312 O O    . LEU   B  1 346 ? 70.160 -10.114 -52.877 1.00 19.77  ? 372  LEU   B O    1 
ATOM   17313 C CB   . LEU   B  1 346 ? 72.394 -11.512 -54.261 1.00 20.66  ? 372  LEU   B CB   1 
ATOM   17314 C CG   . LEU   B  1 346 ? 71.623 -12.121 -55.441 1.00 21.92  ? 372  LEU   B CG   1 
ATOM   17315 C CD1  . LEU   B  1 346 ? 72.005 -11.443 -56.780 1.00 22.11  ? 372  LEU   B CD1  1 
ATOM   17316 C CD2  . LEU   B  1 346 ? 71.886 -13.630 -55.521 1.00 22.69  ? 372  LEU   B CD2  1 
ATOM   17317 H H    . LEU   B  1 346 ? 72.622 -9.986  -52.013 0.00 24.10  ? 372  LEU   B H    1 
ATOM   17318 H HA   . LEU   B  1 346 ? 72.613 -9.485  -54.931 0.00 23.91  ? 372  LEU   B HA   1 
ATOM   17319 H HB2  . LEU   B  1 346 ? 73.450 -11.736 -54.405 0.00 24.93  ? 372  LEU   B HB2  1 
ATOM   17320 H HB3  . LEU   B  1 346 ? 72.046 -12.016 -53.360 0.00 24.59  ? 372  LEU   B HB3  1 
ATOM   17321 H HG   . LEU   B  1 346 ? 70.552 -11.991 -55.291 0.00 25.96  ? 372  LEU   B HG   1 
ATOM   17322 H HD11 . LEU   B  1 346 ? 71.583 -12.019 -57.603 0.00 26.70  ? 372  LEU   B HD11 1 
ATOM   17323 H HD12 . LEU   B  1 346 ? 71.597 -10.433 -56.799 0.00 26.12  ? 372  LEU   B HD12 1 
ATOM   17324 H HD13 . LEU   B  1 346 ? 73.090 -11.408 -56.866 0.00 26.74  ? 372  LEU   B HD13 1 
ATOM   17325 H HD21 . LEU   B  1 346 ? 71.356 -14.040 -56.379 0.00 27.83  ? 372  LEU   B HD21 1 
ATOM   17326 H HD22 . LEU   B  1 346 ? 72.956 -13.796 -55.628 0.00 28.03  ? 372  LEU   B HD22 1 
ATOM   17327 H HD23 . LEU   B  1 346 ? 71.526 -14.099 -54.606 0.00 27.69  ? 372  LEU   B HD23 1 
ATOM   17328 N N    . HIS   B  1 347 ? 70.247 -8.785  -54.715 1.00 18.96  ? 373  HIS   B N    1 
ATOM   17329 C CA   . HIS   B  1 347 ? 68.856 -8.378  -54.621 1.00 18.70  ? 373  HIS   B CA   1 
ATOM   17330 C C    . HIS   B  1 347 ? 68.039 -9.071  -55.692 1.00 18.63  ? 373  HIS   B C    1 
ATOM   17331 O O    . HIS   B  1 347 ? 68.295 -8.894  -56.888 1.00 17.81  ? 373  HIS   B O    1 
ATOM   17332 C CB   . HIS   B  1 347 ? 68.701 -6.853  -54.673 1.00 19.84  ? 373  HIS   B CB   1 
ATOM   17333 C CG   . HIS   B  1 347 ? 69.562 -6.150  -53.675 1.00 23.28  ? 373  HIS   B CG   1 
ATOM   17334 N ND1  . HIS   B  1 347 ? 69.088 -5.849  -52.418 1.00 24.72  ? 373  HIS   B ND1  1 
ATOM   17335 C CD2  . HIS   B  1 347 ? 70.853 -5.750  -53.763 1.00 24.38  ? 373  HIS   B CD2  1 
ATOM   17336 C CE1  . HIS   B  1 347 ? 70.097 -5.274  -51.776 1.00 25.34  ? 373  HIS   B CE1  1 
ATOM   17337 N NE2  . HIS   B  1 347 ? 71.176 -5.190  -52.545 1.00 25.44  ? 373  HIS   B NE2  1 
ATOM   17338 H H    . HIS   B  1 347 ? 70.741 -8.359  -55.493 0.00 21.47  ? 373  HIS   B H    1 
ATOM   17339 H HA   . HIS   B  1 347 ? 68.464 -8.682  -53.655 0.00 20.62  ? 373  HIS   B HA   1 
ATOM   17340 H HB2  . HIS   B  1 347 ? 68.914 -6.464  -55.664 0.00 21.76  ? 373  HIS   B HB2  1 
ATOM   17341 H HB3  . HIS   B  1 347 ? 67.669 -6.616  -54.419 0.00 21.45  ? 373  HIS   B HB3  1 
ATOM   17342 H HD2  . HIS   B  1 347 ? 71.500 -5.851  -54.617 0.00 27.48  ? 373  HIS   B HD2  1 
ATOM   17343 H HE1  . HIS   B  1 347 ? 70.051 -4.922  -50.761 0.00 27.90  ? 373  HIS   B HE1  1 
ATOM   17344 H HE2  . HIS   B  1 347 ? 72.071 -4.790  -52.285 0.00 28.51  ? 373  HIS   B HE2  1 
ATOM   17345 N N    . LEU   B  1 348 ? 67.076 -9.894  -55.267 1.00 18.47  ? 374  LEU   B N    1 
ATOM   17346 C CA   . LEU   B  1 348 ? 66.213 -10.642 -56.165 1.00 20.05  ? 374  LEU   B CA   1 
ATOM   17347 C C    . LEU   B  1 348 ? 64.756 -10.446 -55.756 1.00 21.11  ? 374  LEU   B C    1 
ATOM   17348 O O    . LEU   B  1 348 ? 64.007 -11.415 -55.654 1.00 21.81  ? 374  LEU   B O    1 
ATOM   17349 C CB   . LEU   B  1 348 ? 66.602 -12.141 -56.158 1.00 20.52  ? 374  LEU   B CB   1 
ATOM   17350 C CG   . LEU   B  1 348 ? 67.846 -12.538 -56.960 1.00 22.31  ? 374  LEU   B CG   1 
ATOM   17351 C CD1  . LEU   B  1 348 ? 68.339 -13.901 -56.518 1.00 23.06  ? 374  LEU   B CD1  1 
ATOM   17352 C CD2  . LEU   B  1 348 ? 67.548 -12.591 -58.466 1.00 22.71  ? 374  LEU   B CD2  1 
ATOM   17353 H H    . LEU   B  1 348 ? 66.868 -10.073 -54.290 0.00 20.49  ? 374  LEU   B H    1 
ATOM   17354 H HA   . LEU   B  1 348 ? 66.306 -10.266 -57.182 0.00 22.73  ? 374  LEU   B HA   1 
ATOM   17355 H HB2  . LEU   B  1 348 ? 66.770 -12.445 -55.126 0.00 23.71  ? 374  LEU   B HB2  1 
ATOM   17356 H HB3  . LEU   B  1 348 ? 65.785 -12.727 -56.577 0.00 23.85  ? 374  LEU   B HB3  1 
ATOM   17357 H HG   . LEU   B  1 348 ? 68.639 -11.811 -56.789 0.00 26.19  ? 374  LEU   B HG   1 
ATOM   17358 H HD11 . LEU   B  1 348 ? 69.164 -14.206 -57.160 0.00 28.00  ? 374  LEU   B HD11 1 
ATOM   17359 H HD12 . LEU   B  1 348 ? 68.680 -13.837 -55.486 0.00 27.57  ? 374  LEU   B HD12 1 
ATOM   17360 H HD13 . LEU   B  1 348 ? 67.522 -14.617 -56.597 0.00 27.78  ? 374  LEU   B HD13 1 
ATOM   17361 H HD21 . LEU   B  1 348 ? 68.454 -12.884 -58.993 0.00 27.31  ? 374  LEU   B HD21 1 
ATOM   17362 H HD22 . LEU   B  1 348 ? 66.762 -13.322 -58.648 0.00 27.15  ? 374  LEU   B HD22 1 
ATOM   17363 H HD23 . LEU   B  1 348 ? 67.229 -11.609 -58.811 0.00 26.70  ? 374  LEU   B HD23 1 
ATOM   17364 N N    . ARG   B  1 349 ? 64.345 -9.191  -55.521 1.00 21.25  ? 375  ARG   B N    1 
ATOM   17365 C CA   . ARG   B  1 349 ? 62.932 -8.922  -55.242 1.00 21.32  ? 375  ARG   B CA   1 
ATOM   17366 C C    . ARG   B  1 349 ? 62.165 -9.101  -56.554 1.00 20.27  ? 375  ARG   B C    1 
ATOM   17367 O O    . ARG   B  1 349 ? 62.760 -8.976  -57.603 1.00 20.62  ? 375  ARG   B O    1 
ATOM   17368 C CB   . ARG   B  1 349 ? 62.709 -7.486  -54.760 1.00 23.96  ? 375  ARG   B CB   1 
ATOM   17369 C CG   . ARG   B  1 349 ? 63.449 -7.132  -53.495 1.00 30.56  ? 375  ARG   B CG   1 
ATOM   17370 C CD   . ARG   B  1 349 ? 62.804 -5.957  -52.791 1.00 37.87  ? 375  ARG   B CD   1 
ATOM   17371 N NE   . ARG   B  1 349 ? 62.776 -4.764  -53.630 1.00 44.02  ? 375  ARG   B NE   1 
ATOM   17372 C CZ   . ARG   B  1 349 ? 62.091 -3.659  -53.356 1.00 50.04  ? 375  ARG   B CZ   1 
ATOM   17373 N NH1  . ARG   B  1 349 ? 61.371 -3.569  -52.240 1.00 51.45  ? 375  ARG   B NH1  1 
ATOM   17374 N NH2  . ARG   B  1 349 ? 62.122 -2.630  -54.192 1.00 51.57  ? 375  ARG   B NH2  1 
ATOM   17375 H H    . ARG   B  1 349 ? 64.938 -8.367  -55.539 0.00 23.27  ? 375  ARG   B H    1 
ATOM   17376 H HA   . ARG   B  1 349 ? 62.541 -9.610  -54.494 0.00 23.27  ? 375  ARG   B HA   1 
ATOM   17377 H HB2  . ARG   B  1 349 ? 63.032 -6.784  -55.522 0.00 25.96  ? 375  ARG   B HB2  1 
ATOM   17378 H HB3  . ARG   B  1 349 ? 61.645 -7.349  -54.572 0.00 25.83  ? 375  ARG   B HB3  1 
ATOM   17379 H HG2  . ARG   B  1 349 ? 63.437 -7.986  -52.820 0.00 33.87  ? 375  ARG   B HG2  1 
ATOM   17380 H HG3  . ARG   B  1 349 ? 64.474 -6.859  -53.742 0.00 33.84  ? 375  ARG   B HG3  1 
ATOM   17381 H HD2  . ARG   B  1 349 ? 61.779 -6.220  -52.535 0.00 42.08  ? 375  ARG   B HD2  1 
ATOM   17382 H HD3  . ARG   B  1 349 ? 63.360 -5.723  -51.885 0.00 42.09  ? 375  ARG   B HD3  1 
ATOM   17383 H HE   . ARG   B  1 349 ? 63.316 -4.784  -54.489 0.00 49.54  ? 375  ARG   B HE   1 
ATOM   17384 H HH11 . ARG   B  1 349 ? 61.315 -4.335  -51.577 0.00 57.92  ? 375  ARG   B HH11 1 
ATOM   17385 H HH12 . ARG   B  1 349 ? 60.852 -2.719  -52.047 0.00 57.68  ? 375  ARG   B HH12 1 
ATOM   17386 H HH21 . ARG   B  1 349 ? 62.670 -2.674  -55.045 0.00 58.28  ? 375  ARG   B HH21 1 
ATOM   17387 H HH22 . ARG   B  1 349 ? 61.604 -1.782  -53.982 0.00 57.95  ? 375  ARG   B HH22 1 
ATOM   17388 N N    . GLY   B  1 350 ? 60.874 -9.387  -56.497 1.00 18.63  ? 376  GLY   B N    1 
ATOM   17389 C CA   . GLY   B  1 350 ? 60.040 -9.438  -57.693 1.00 18.29  ? 376  GLY   B CA   1 
ATOM   17390 C C    . GLY   B  1 350 ? 60.470 -10.325 -58.848 1.00 17.81  ? 376  GLY   B C    1 
ATOM   17391 O O    . GLY   B  1 350 ? 60.222 -9.971  -59.995 1.00 18.17  ? 376  GLY   B O    1 
ATOM   17392 H H    . GLY   B  1 350 ? 60.372 -9.588  -55.638 0.00 20.02  ? 376  GLY   B H    1 
ATOM   17393 H HA2  . GLY   B  1 350 ? 59.044 -9.761  -57.396 0.00 19.89  ? 376  GLY   B HA2  1 
ATOM   17394 H HA3  . GLY   B  1 350 ? 59.951 -8.425  -58.083 0.00 19.72  ? 376  GLY   B HA3  1 
ATOM   17395 N N    . TYR   B  1 351 ? 61.107 -11.476 -58.568 1.00 17.47  ? 377  TYR   B N    1 
ATOM   17396 C CA   . TYR   B  1 351 ? 61.381 -12.546 -59.536 1.00 18.27  ? 377  TYR   B CA   1 
ATOM   17397 C C    . TYR   B  1 351 ? 60.054 -13.319 -59.689 1.00 18.40  ? 377  TYR   B C    1 
ATOM   17398 O O    . TYR   B  1 351 ? 59.615 -13.587 -60.813 1.00 17.69  ? 377  TYR   B O    1 
ATOM   17399 C CB   . TYR   B  1 351 ? 62.496 -13.490 -59.027 1.00 18.53  ? 377  TYR   B CB   1 
ATOM   17400 C CG   . TYR   B  1 351 ? 62.808 -14.639 -59.964 1.00 19.54  ? 377  TYR   B CG   1 
ATOM   17401 C CD1  . TYR   B  1 351 ? 62.030 -15.791 -59.964 1.00 20.36  ? 377  TYR   B CD1  1 
ATOM   17402 C CD2  . TYR   B  1 351 ? 63.948 -14.623 -60.763 1.00 20.56  ? 377  TYR   B CD2  1 
ATOM   17403 C CE1  . TYR   B  1 351 ? 62.324 -16.861 -60.802 1.00 21.12  ? 377  TYR   B CE1  1 
ATOM   17404 C CE2  . TYR   B  1 351 ? 64.281 -15.707 -61.569 1.00 21.45  ? 377  TYR   B CE2  1 
ATOM   17405 C CZ   . TYR   B  1 351 ? 63.448 -16.813 -61.606 1.00 22.42  ? 377  TYR   B CZ   1 
ATOM   17406 O OH   . TYR   B  1 351 ? 63.763 -17.920 -62.345 1.00 24.08  ? 377  TYR   B OH   1 
ATOM   17407 H H    . TYR   B  1 351 ? 61.464 -11.698 -57.644 0.00 19.60  ? 377  TYR   B H    1 
ATOM   17408 H HA   . TYR   B  1 351 ? 61.677 -12.131 -60.498 0.00 21.26  ? 377  TYR   B HA   1 
ATOM   17409 H HB2  . TYR   B  1 351 ? 63.409 -12.912 -58.888 0.00 21.64  ? 377  TYR   B HB2  1 
ATOM   17410 H HB3  . TYR   B  1 351 ? 62.182 -13.919 -58.077 0.00 21.71  ? 377  TYR   B HB3  1 
ATOM   17411 H HD1  . TYR   B  1 351 ? 61.141 -15.829 -59.356 0.00 24.74  ? 377  TYR   B HD1  1 
ATOM   17412 H HD2  . TYR   B  1 351 ? 64.595 -13.760 -60.749 0.00 24.83  ? 377  TYR   B HD2  1 
ATOM   17413 H HE1  . TYR   B  1 351 ? 61.698 -17.738 -60.798 0.00 26.73  ? 377  TYR   B HE1  1 
ATOM   17414 H HE2  . TYR   B  1 351 ? 65.160 -15.660 -62.190 0.00 26.94  ? 377  TYR   B HE2  1 
ATOM   17415 H HH   . TYR   B  1 351 ? 64.547 -17.741 -62.927 0.00 31.01  ? 377  TYR   B HH   1 
ATOM   17416 N N    . VAL   B  1 352 ? 59.404 -13.645 -58.530 1.00 18.44  ? 378  VAL   B N    1 
ATOM   17417 C CA   . VAL   B  1 352 ? 58.083 -14.264 -58.384 1.00 19.35  ? 378  VAL   B CA   1 
ATOM   17418 C C    . VAL   B  1 352 ? 58.150 -15.781 -58.559 1.00 19.89  ? 378  VAL   B C    1 
ATOM   17419 O O    . VAL   B  1 352 ? 58.244 -16.285 -59.667 1.00 20.12  ? 378  VAL   B O    1 
ATOM   17420 C CB   . VAL   B  1 352 ? 56.986 -13.613 -59.263 1.00 20.30  ? 378  VAL   B CB   1 
ATOM   17421 C CG1  . VAL   B  1 352 ? 55.621 -14.246 -58.993 1.00 20.91  ? 378  VAL   B CG1  1 
ATOM   17422 C CG2  . VAL   B  1 352 ? 56.931 -12.105 -59.011 1.00 19.93  ? 378  VAL   B CG2  1 
ATOM   17423 H H    . VAL   B  1 352 ? 59.829 -13.494 -57.621 0.00 21.21  ? 378  VAL   B H    1 
ATOM   17424 H HA   . VAL   B  1 352 ? 57.770 -14.074 -57.359 0.00 22.38  ? 378  VAL   B HA   1 
ATOM   17425 H HB   . VAL   B  1 352 ? 57.231 -13.771 -60.313 0.00 24.04  ? 378  VAL   B HB   1 
ATOM   17426 H HG11 . VAL   B  1 352 ? 54.865 -13.612 -59.452 0.00 24.55  ? 378  VAL   B HG11 1 
ATOM   17427 H HG12 . VAL   B  1 352 ? 55.581 -15.230 -59.458 0.00 25.07  ? 378  VAL   B HG12 1 
ATOM   17428 H HG13 . VAL   B  1 352 ? 55.459 -14.320 -57.919 0.00 24.43  ? 378  VAL   B HG13 1 
ATOM   17429 H HG21 . VAL   B  1 352 ? 56.245 -11.660 -59.729 0.00 22.81  ? 378  VAL   B HG21 1 
ATOM   17430 H HG22 . VAL   B  1 352 ? 56.573 -11.930 -57.998 0.00 22.52  ? 378  VAL   B HG22 1 
ATOM   17431 H HG23 . VAL   B  1 352 ? 57.920 -11.667 -59.135 0.00 22.68  ? 378  VAL   B HG23 1 
ATOM   17432 N N    . PHE   B  1 353 ? 58.117 -16.500 -57.436 1.00 20.24  ? 379  PHE   B N    1 
ATOM   17433 C CA   . PHE   B  1 353 ? 58.175 -17.963 -57.417 1.00 20.61  ? 379  PHE   B CA   1 
ATOM   17434 C C    . PHE   B  1 353 ? 57.547 -18.471 -56.121 1.00 21.36  ? 379  PHE   B C    1 
ATOM   17435 O O    . PHE   B  1 353 ? 57.446 -17.733 -55.137 1.00 20.81  ? 379  PHE   B O    1 
ATOM   17436 C CB   . PHE   B  1 353 ? 59.611 -18.494 -57.609 1.00 19.92  ? 379  PHE   B CB   1 
ATOM   17437 C CG   . PHE   B  1 353 ? 60.591 -18.087 -56.534 1.00 20.14  ? 379  PHE   B CG   1 
ATOM   17438 C CD1  . PHE   B  1 353 ? 61.145 -16.819 -56.524 1.00 20.47  ? 379  PHE   B CD1  1 
ATOM   17439 C CD2  . PHE   B  1 353 ? 61.015 -18.995 -55.580 1.00 20.72  ? 379  PHE   B CD2  1 
ATOM   17440 C CE1  . PHE   B  1 353 ? 62.076 -16.454 -55.554 1.00 21.57  ? 379  PHE   B CE1  1 
ATOM   17441 C CE2  . PHE   B  1 353 ? 61.952 -18.630 -54.614 1.00 21.14  ? 379  PHE   B CE2  1 
ATOM   17442 C CZ   . PHE   B  1 353 ? 62.468 -17.361 -54.601 1.00 21.08  ? 379  PHE   B CZ   1 
ATOM   17443 H H    . PHE   B  1 353 ? 58.074 -16.088 -56.510 0.00 23.99  ? 379  PHE   B H    1 
ATOM   17444 H HA   . PHE   B  1 353 ? 57.571 -18.352 -58.235 0.00 25.62  ? 379  PHE   B HA   1 
ATOM   17445 H HB2  . PHE   B  1 353 ? 59.576 -19.582 -57.636 0.00 25.25  ? 379  PHE   B HB2  1 
ATOM   17446 H HB3  . PHE   B  1 353 ? 59.994 -18.120 -58.558 0.00 24.85  ? 379  PHE   B HB3  1 
ATOM   17447 H HD1  . PHE   B  1 353 ? 60.841 -16.100 -57.264 0.00 24.54  ? 379  PHE   B HD1  1 
ATOM   17448 H HD2  . PHE   B  1 353 ? 60.614 -19.994 -55.577 0.00 26.07  ? 379  PHE   B HD2  1 
ATOM   17449 H HE1  . PHE   B  1 353 ? 62.483 -15.457 -55.546 0.00 25.49  ? 379  PHE   B HE1  1 
ATOM   17450 H HE2  . PHE   B  1 353 ? 62.256 -19.341 -53.866 0.00 26.19  ? 379  PHE   B HE2  1 
ATOM   17451 H HZ   . PHE   B  1 353 ? 63.186 -17.077 -53.852 0.00 25.32  ? 379  PHE   B HZ   1 
ATOM   17452 N N    . GLN   B  1 354 ? 57.103 -19.724 -56.136 1.00 21.71  ? 380  GLN   B N    1 
ATOM   17453 C CA   . GLN   B  1 354 ? 56.324 -20.275 -55.033 1.00 22.49  ? 380  GLN   B CA   1 
ATOM   17454 C C    . GLN   B  1 354 ? 57.111 -20.899 -53.887 1.00 23.08  ? 380  GLN   B C    1 
ATOM   17455 O O    . GLN   B  1 354 ? 56.635 -20.854 -52.762 1.00 22.56  ? 380  GLN   B O    1 
ATOM   17456 C CB   . GLN   B  1 354 ? 55.322 -21.313 -55.578 1.00 23.86  ? 380  GLN   B CB   1 
ATOM   17457 C CG   . GLN   B  1 354 ? 54.513 -20.811 -56.782 1.00 26.75  ? 380  GLN   B CG   1 
ATOM   17458 C CD   . GLN   B  1 354 ? 53.485 -21.800 -57.254 1.00 32.94  ? 380  GLN   B CD   1 
ATOM   17459 O OE1  . GLN   B  1 354 ? 52.721 -22.358 -56.456 1.00 34.72  ? 380  GLN   B OE1  1 
ATOM   17460 N NE2  . GLN   B  1 354 ? 53.431 -22.036 -58.561 1.00 34.58  ? 380  GLN   B NE2  1 
ATOM   17461 H H    . GLN   B  1 354 ? 57.283 -20.381 -56.888 0.00 27.50  ? 380  GLN   B H    1 
ATOM   17462 H HA   . GLN   B  1 354 ? 55.718 -19.475 -54.610 0.00 27.61  ? 380  GLN   B HA   1 
ATOM   17463 H HB2  . GLN   B  1 354 ? 55.864 -22.209 -55.873 0.00 30.67  ? 380  GLN   B HB2  1 
ATOM   17464 H HB3  . GLN   B  1 354 ? 54.618 -21.556 -54.783 0.00 30.18  ? 380  GLN   B HB3  1 
ATOM   17465 H HG2  . GLN   B  1 354 ? 53.992 -19.898 -56.499 0.00 33.27  ? 380  GLN   B HG2  1 
ATOM   17466 H HG3  . GLN   B  1 354 ? 55.195 -20.606 -57.606 0.00 33.77  ? 380  GLN   B HG3  1 
ATOM   17467 H HE21 . GLN   B  1 354 ? 54.054 -21.561 -59.206 0.00 43.99  ? 380  GLN   B HE21 1 
ATOM   17468 H HE22 . GLN   B  1 354 ? 52.750 -22.697 -58.920 0.00 44.49  ? 380  GLN   B HE22 1 
ATOM   17469 N N    . GLU   B  1 355 ? 58.253 -21.533 -54.159 1.00 24.22  ? 381  GLU   B N    1 
ATOM   17470 C CA   . GLU   B  1 355 ? 58.988 -22.247 -53.117 1.00 26.08  ? 381  GLU   B CA   1 
ATOM   17471 C C    . GLU   B  1 355 ? 60.493 -22.103 -53.301 1.00 26.51  ? 381  GLU   B C    1 
ATOM   17472 O O    . GLU   B  1 355 ? 60.989 -22.213 -54.417 1.00 25.55  ? 381  GLU   B O    1 
ATOM   17473 C CB   . GLU   B  1 355 ? 58.607 -23.742 -53.172 1.00 29.45  ? 381  GLU   B CB   1 
ATOM   17474 C CG   . GLU   B  1 355 ? 59.252 -24.603 -52.094 1.00 38.31  ? 381  GLU   B CG   1 
ATOM   17475 C CD   . GLU   B  1 355 ? 58.937 -26.086 -52.186 1.00 48.69  ? 381  GLU   B CD   1 
ATOM   17476 O OE1  . GLU   B  1 355 ? 58.558 -26.556 -53.285 1.00 50.66  ? 381  GLU   B OE1  1 
ATOM   17477 O OE2  . GLU   B  1 355 ? 59.096 -26.784 -51.158 1.00 51.73  ? 381  GLU   B OE2  1 
ATOM   17478 H H    . GLU   B  1 355 ? 58.689 -21.577 -55.075 0.00 30.76  ? 381  GLU   B H    1 
ATOM   17479 H HA   . GLU   B  1 355 ? 58.730 -21.865 -52.131 0.00 32.68  ? 381  GLU   B HA   1 
ATOM   17480 H HB2  . GLU   B  1 355 ? 57.527 -23.830 -53.063 0.00 37.70  ? 381  GLU   B HB2  1 
ATOM   17481 H HB3  . GLU   B  1 355 ? 58.911 -24.131 -54.143 0.00 38.08  ? 381  GLU   B HB3  1 
ATOM   17482 H HG2  . GLU   B  1 355 ? 60.336 -24.516 -52.149 0.00 48.72  ? 381  GLU   B HG2  1 
ATOM   17483 H HG3  . GLU   B  1 355 ? 58.907 -24.254 -51.122 0.00 48.34  ? 381  GLU   B HG3  1 
ATOM   17484 N N    . LEU   B  1 356 ? 61.212 -21.907 -52.193 1.00 27.35  ? 382  LEU   B N    1 
ATOM   17485 C CA   . LEU   B  1 356 ? 62.667 -21.848 -52.216 1.00 28.64  ? 382  LEU   B CA   1 
ATOM   17486 C C    . LEU   B  1 356 ? 63.186 -23.161 -51.631 1.00 30.25  ? 382  LEU   B C    1 
ATOM   17487 O O    . LEU   B  1 356 ? 62.928 -23.455 -50.466 1.00 30.05  ? 382  LEU   B O    1 
ATOM   17488 C CB   . LEU   B  1 356 ? 63.203 -20.639 -51.422 1.00 28.24  ? 382  LEU   B CB   1 
ATOM   17489 C CG   . LEU   B  1 356 ? 64.733 -20.411 -51.500 1.00 28.76  ? 382  LEU   B CG   1 
ATOM   17490 C CD1  . LEU   B  1 356 ? 65.206 -20.126 -52.937 1.00 28.63  ? 382  LEU   B CD1  1 
ATOM   17491 C CD2  . LEU   B  1 356 ? 65.157 -19.290 -50.573 1.00 28.86  ? 382  LEU   B CD2  1 
ATOM   17492 H H    . LEU   B  1 356 ? 60.817 -21.780 -51.267 0.00 34.23  ? 382  LEU   B H    1 
ATOM   17493 H HA   . LEU   B  1 356 ? 63.020 -21.758 -53.242 0.00 36.24  ? 382  LEU   B HA   1 
ATOM   17494 H HB2  . LEU   B  1 356 ? 62.719 -19.736 -51.792 0.00 34.67  ? 382  LEU   B HB2  1 
ATOM   17495 H HB3  . LEU   B  1 356 ? 62.954 -20.779 -50.371 0.00 35.00  ? 382  LEU   B HB3  1 
ATOM   17496 H HG   . LEU   B  1 356 ? 65.241 -21.317 -51.175 0.00 36.25  ? 382  LEU   B HG   1 
ATOM   17497 H HD11 . LEU   B  1 356 ? 66.218 -19.723 -52.905 0.00 35.72  ? 382  LEU   B HD11 1 
ATOM   17498 H HD12 . LEU   B  1 356 ? 65.209 -21.055 -53.505 0.00 36.23  ? 382  LEU   B HD12 1 
ATOM   17499 H HD13 . LEU   B  1 356 ? 64.533 -19.406 -53.399 0.00 35.42  ? 382  LEU   B HD13 1 
ATOM   17500 H HD21 . LEU   B  1 356 ? 66.240 -19.183 -50.611 0.00 35.57  ? 382  LEU   B HD21 1 
ATOM   17501 H HD22 . LEU   B  1 356 ? 64.680 -18.366 -50.895 0.00 35.03  ? 382  LEU   B HD22 1 
ATOM   17502 H HD23 . LEU   B  1 356 ? 64.846 -19.532 -49.558 0.00 35.41  ? 382  LEU   B HD23 1 
ATOM   17503 N N    . ARG   B  1 357 ? 63.853 -23.982 -52.444 1.00 31.65  ? 383  ARG   B N    1 
ATOM   17504 C CA   . ARG   B  1 357 ? 64.435 -25.241 -51.968 1.00 33.87  ? 383  ARG   B CA   1 
ATOM   17505 C C    . ARG   B  1 357 ? 65.945 -25.054 -51.762 1.00 35.14  ? 383  ARG   B C    1 
ATOM   17506 O O    . ARG   B  1 357 ? 66.539 -24.152 -52.343 1.00 35.02  ? 383  ARG   B O    1 
ATOM   17507 C CB   . ARG   B  1 357 ? 64.220 -26.380 -52.976 1.00 35.61  ? 383  ARG   B CB   1 
ATOM   17508 C CG   . ARG   B  1 357 ? 62.780 -26.634 -53.393 1.00 39.03  ? 383  ARG   B CG   1 
ATOM   17509 C CD   . ARG   B  1 357 ? 62.746 -27.685 -54.495 1.00 41.64  ? 383  ARG   B CD   1 
ATOM   17510 N NE   . ARG   B  1 357 ? 63.372 -27.200 -55.727 1.00 43.86  ? 383  ARG   B NE   1 
ATOM   17511 C CZ   . ARG   B  1 357 ? 63.544 -27.926 -56.830 1.00 45.93  ? 383  ARG   B CZ   1 
ATOM   17512 N NH1  . ARG   B  1 357 ? 63.143 -29.194 -56.871 1.00 45.43  ? 383  ARG   B NH1  1 
ATOM   17513 N NH2  . ARG   B  1 357 ? 64.125 -27.393 -57.899 1.00 45.37  ? 383  ARG   B NH2  1 
ATOM   17514 H H    . ARG   B  1 357 ? 64.008 -23.813 -53.433 0.00 40.96  ? 383  ARG   B H    1 
ATOM   17515 H HA   . ARG   B  1 357 ? 63.994 -25.552 -51.022 0.00 44.21  ? 383  ARG   B HA   1 
ATOM   17516 H HB2  . ARG   B  1 357 ? 64.798 -26.143 -53.868 0.00 47.05  ? 383  ARG   B HB2  1 
ATOM   17517 H HB3  . ARG   B  1 357 ? 64.595 -27.302 -52.535 0.00 47.47  ? 383  ARG   B HB3  1 
ATOM   17518 H HG2  . ARG   B  1 357 ? 62.212 -27.006 -52.541 0.00 51.10  ? 383  ARG   B HG2  1 
ATOM   17519 H HG3  . ARG   B  1 357 ? 62.334 -25.719 -53.780 0.00 50.61  ? 383  ARG   B HG3  1 
ATOM   17520 H HD2  . ARG   B  1 357 ? 63.290 -28.568 -54.163 0.00 55.45  ? 383  ARG   B HD2  1 
ATOM   17521 H HD3  . ARG   B  1 357 ? 61.711 -27.942 -54.716 0.00 55.01  ? 383  ARG   B HD3  1 
ATOM   17522 H HE   . ARG   B  1 357 ? 63.686 -26.235 -55.742 0.00 57.14  ? 383  ARG   B HE   1 
ATOM   17523 H HH11 . ARG   B  1 357 ? 62.697 -29.638 -56.075 0.00 60.89  ? 383  ARG   B HH11 1 
ATOM   17524 H HH12 . ARG   B  1 357 ? 63.283 -29.738 -57.717 0.00 61.33  ? 383  ARG   B HH12 1 
ATOM   17525 H HH21 . ARG   B  1 357 ? 64.435 -26.426 -57.887 0.00 59.55  ? 383  ARG   B HH21 1 
ATOM   17526 H HH22 . ARG   B  1 357 ? 64.257 -27.946 -58.740 0.00 60.54  ? 383  ARG   B HH22 1 
ATOM   17527 N N    . GLU   B  1 358 ? 66.566 -25.929 -50.970 1.00 36.72  ? 384  GLU   B N    1 
ATOM   17528 C CA   . GLU   B  1 358 ? 68.007 -25.868 -50.710 1.00 38.66  ? 384  GLU   B CA   1 
ATOM   17529 C C    . GLU   B  1 358 ? 68.846 -26.019 -51.987 1.00 39.65  ? 384  GLU   B C    1 
ATOM   17530 O O    . GLU   B  1 358 ? 69.807 -25.271 -52.173 1.00 40.47  ? 384  GLU   B O    1 
ATOM   17531 C CB   . GLU   B  1 358 ? 68.398 -26.929 -49.674 1.00 42.21  ? 384  GLU   B CB   1 
ATOM   17532 C CG   . GLU   B  1 358 ? 69.882 -26.935 -49.348 1.00 48.82  ? 384  GLU   B CG   1 
ATOM   17533 C CD   . GLU   B  1 358 ? 70.214 -27.449 -47.961 1.00 56.79  ? 384  GLU   B CD   1 
ATOM   17534 O OE1  . GLU   B  1 358 ? 69.534 -28.392 -47.493 1.00 58.20  ? 384  GLU   B OE1  1 
ATOM   17535 O OE2  . GLU   B  1 358 ? 71.165 -26.911 -47.347 1.00 59.14  ? 384  GLU   B OE2  1 
ATOM   17536 H H    . GLU   B  1 358 ? 66.092 -26.683 -50.485 0.00 48.49  ? 384  GLU   B H    1 
ATOM   17537 H HA   . GLU   B  1 358 ? 68.233 -24.887 -50.296 0.00 50.29  ? 384  GLU   B HA   1 
ATOM   17538 H HB2  . GLU   B  1 358 ? 67.852 -26.733 -48.753 0.00 55.31  ? 384  GLU   B HB2  1 
ATOM   17539 H HB3  . GLU   B  1 358 ? 68.134 -27.913 -50.059 0.00 56.10  ? 384  GLU   B HB3  1 
ATOM   17540 H HG2  . GLU   B  1 358 ? 70.399 -27.569 -50.067 0.00 64.35  ? 384  GLU   B HG2  1 
ATOM   17541 H HG3  . GLU   B  1 358 ? 70.258 -25.916 -49.417 0.00 63.39  ? 384  GLU   B HG3  1 
ATOM   17542 N N    . ASP   B  1 359 ? 68.469 -26.943 -52.883 1.00 39.47  ? 385  ASP   B N    1 
ATOM   17543 C CA   . ASP   B  1 359 ? 69.198 -27.133 -54.141 1.00 39.80  ? 385  ASP   B CA   1 
ATOM   17544 C C    . ASP   B  1 359 ? 69.204 -25.868 -55.018 1.00 38.50  ? 385  ASP   B C    1 
ATOM   17545 O O    . ASP   B  1 359 ? 70.118 -25.692 -55.824 1.00 38.46  ? 385  ASP   B O    1 
ATOM   17546 C CB   . ASP   B  1 359 ? 68.598 -28.288 -54.966 1.00 43.32  ? 385  ASP   B CB   1 
ATOM   17547 C CG   . ASP   B  1 359 ? 68.978 -29.687 -54.501 1.00 51.54  ? 385  ASP   B CG   1 
ATOM   17548 O OD1  . ASP   B  1 359 ? 69.716 -29.803 -53.494 1.00 53.12  ? 385  ASP   B OD1  1 
ATOM   17549 O OD2  . ASP   B  1 359 ? 68.528 -30.668 -55.140 1.00 55.00  ? 385  ASP   B OD2  1 
ATOM   17550 H H    . ASP   B  1 359 ? 67.680 -27.569 -52.759 0.00 52.79  ? 385  ASP   B H    1 
ATOM   17551 H HA   . ASP   B  1 359 ? 70.225 -27.404 -53.907 0.00 53.78  ? 385  ASP   B HA   1 
ATOM   17552 H HB2  . ASP   B  1 359 ? 67.512 -28.217 -54.946 0.00 58.03  ? 385  ASP   B HB2  1 
ATOM   17553 H HB3  . ASP   B  1 359 ? 68.945 -28.185 -55.993 0.00 58.45  ? 385  ASP   B HB3  1 
ATOM   17554 N N    . ASP   B  1 360 ? 68.191 -25.000 -54.872 1.00 37.05  ? 386  ASP   B N    1 
ATOM   17555 C CA   . ASP   B  1 360 ? 68.062 -23.814 -55.715 1.00 36.31  ? 386  ASP   B CA   1 
ATOM   17556 C C    . ASP   B  1 360 ? 69.135 -22.730 -55.489 1.00 34.10  ? 386  ASP   B C    1 
ATOM   17557 O O    . ASP   B  1 360 ? 69.449 -22.015 -56.437 1.00 33.99  ? 386  ASP   B O    1 
ATOM   17558 C CB   . ASP   B  1 360 ? 66.652 -23.216 -55.583 1.00 38.64  ? 386  ASP   B CB   1 
ATOM   17559 C CG   . ASP   B  1 360 ? 65.570 -24.179 -56.038 1.00 44.51  ? 386  ASP   B CG   1 
ATOM   17560 O OD1  . ASP   B  1 360 ? 65.789 -24.888 -57.036 1.00 45.53  ? 386  ASP   B OD1  1 
ATOM   17561 O OD2  . ASP   B  1 360 ? 64.503 -24.207 -55.406 1.00 48.04  ? 386  ASP   B OD2  1 
ATOM   17562 H H    . ASP   B  1 360 ? 67.455 -25.083 -54.178 0.00 48.71  ? 386  ASP   B H    1 
ATOM   17563 H HA   . ASP   B  1 360 ? 68.181 -24.128 -56.751 0.00 47.86  ? 386  ASP   B HA   1 
ATOM   17564 H HB2  . ASP   B  1 360 ? 66.466 -22.965 -54.540 0.00 49.45  ? 386  ASP   B HB2  1 
ATOM   17565 H HB3  . ASP   B  1 360 ? 66.586 -22.320 -56.199 0.00 49.43  ? 386  ASP   B HB3  1 
ATOM   17566 N N    . PHE   B  1 361 ? 69.710 -22.625 -54.290 1.00 32.20  ? 387  PHE   B N    1 
ATOM   17567 C CA   . PHE   B  1 361 ? 70.742 -21.623 -54.007 1.00 31.68  ? 387  PHE   B CA   1 
ATOM   17568 C C    . PHE   B  1 361 ? 72.150 -22.220 -53.823 1.00 31.96  ? 387  PHE   B C    1 
ATOM   17569 O O    . PHE   B  1 361 ? 73.041 -21.526 -53.330 1.00 31.89  ? 387  PHE   B O    1 
ATOM   17570 C CB   . PHE   B  1 361 ? 70.316 -20.779 -52.787 1.00 31.01  ? 387  PHE   B CB   1 
ATOM   17571 C CG   . PHE   B  1 361 ? 69.408 -19.591 -53.027 1.00 30.98  ? 387  PHE   B CG   1 
ATOM   17572 C CD1  . PHE   B  1 361 ? 68.908 -19.310 -54.291 1.00 31.35  ? 387  PHE   B CD1  1 
ATOM   17573 C CD2  . PHE   B  1 361 ? 69.087 -18.729 -51.994 1.00 31.20  ? 387  PHE   B CD2  1 
ATOM   17574 C CE1  . PHE   B  1 361 ? 68.108 -18.197 -54.503 1.00 31.92  ? 387  PHE   B CE1  1 
ATOM   17575 C CE2  . PHE   B  1 361 ? 68.308 -17.607 -52.222 1.00 31.63  ? 387  PHE   B CE2  1 
ATOM   17576 C CZ   . PHE   B  1 361 ? 67.819 -17.353 -53.472 1.00 31.25  ? 387  PHE   B CZ   1 
ATOM   17577 H H    . PHE   B  1 361 ? 69.482 -23.213 -53.495 0.00 42.27  ? 387  PHE   B H    1 
ATOM   17578 H HA   . PHE   B  1 361 ? 70.879 -20.954 -54.854 0.00 41.06  ? 387  PHE   B HA   1 
ATOM   17579 H HB2  . PHE   B  1 361 ? 69.799 -21.431 -52.085 0.00 39.93  ? 387  PHE   B HB2  1 
ATOM   17580 H HB3  . PHE   B  1 361 ? 71.202 -20.377 -52.297 0.00 39.80  ? 387  PHE   B HB3  1 
ATOM   17581 H HD1  . PHE   B  1 361 ? 69.087 -19.951 -55.133 0.00 39.89  ? 387  PHE   B HD1  1 
ATOM   17582 H HD2  . PHE   B  1 361 ? 69.494 -18.903 -51.013 0.00 38.93  ? 387  PHE   B HD2  1 
ATOM   17583 H HE1  . PHE   B  1 361 ? 67.710 -18.002 -55.485 0.00 39.56  ? 387  PHE   B HE1  1 
ATOM   17584 H HE2  . PHE   B  1 361 ? 68.079 -16.943 -51.408 0.00 38.42  ? 387  PHE   B HE2  1 
ATOM   17585 H HZ   . PHE   B  1 361 ? 67.188 -16.499 -53.638 0.00 37.85  ? 387  PHE   B HZ   1 
ATOM   17586 N N    . GLN   B  1 362 ? 72.389 -23.451 -54.327 1.00 31.99  ? 388  GLN   B N    1 
ATOM   17587 C CA   . GLN   B  1 362 ? 73.714 -24.070 -54.236 1.00 32.82  ? 388  GLN   B CA   1 
ATOM   17588 C C    . GLN   B  1 362 ? 74.811 -23.210 -54.896 1.00 32.25  ? 388  GLN   B C    1 
ATOM   17589 O O    . GLN   B  1 362 ? 75.891 -23.112 -54.322 1.00 32.37  ? 388  GLN   B O    1 
ATOM   17590 C CB   . GLN   B  1 362 ? 73.741 -25.481 -54.853 1.00 35.69  ? 388  GLN   B CB   1 
ATOM   17591 C CG   . GLN   B  1 362 ? 72.845 -26.468 -54.143 1.00 42.42  ? 388  GLN   B CG   1 
ATOM   17592 C CD   . GLN   B  1 362 ? 73.383 -26.928 -52.814 1.00 49.96  ? 388  GLN   B CD   1 
ATOM   17593 O OE1  . GLN   B  1 362 ? 74.524 -27.392 -52.705 1.00 53.46  ? 388  GLN   B OE1  1 
ATOM   17594 N NE2  . GLN   B  1 362 ? 72.567 -26.824 -51.773 1.00 50.48  ? 388  GLN   B NE2  1 
ATOM   17595 H H    . GLN   B  1 362 ? 71.709 -24.009 -54.833 0.00 43.06  ? 388  GLN   B H    1 
ATOM   17596 H HA   . GLN   B  1 362 ? 73.960 -24.169 -53.180 0.00 44.53  ? 388  GLN   B HA   1 
ATOM   17597 H HB2  . GLN   B  1 362 ? 73.419 -25.446 -55.892 0.00 48.80  ? 388  GLN   B HB2  1 
ATOM   17598 H HB3  . GLN   B  1 362 ? 74.762 -25.858 -54.808 0.00 49.24  ? 388  GLN   B HB3  1 
ATOM   17599 H HG2  . GLN   B  1 362 ? 71.900 -25.958 -53.969 0.00 56.52  ? 388  GLN   B HG2  1 
ATOM   17600 H HG3  . GLN   B  1 362 ? 72.694 -27.342 -54.775 0.00 57.56  ? 388  GLN   B HG3  1 
ATOM   17601 H HE21 . GLN   B  1 362 ? 71.627 -26.455 -51.875 0.00 66.17  ? 388  GLN   B HE21 1 
ATOM   17602 H HE22 . GLN   B  1 362 ? 72.888 -27.121 -50.856 0.00 66.79  ? 388  GLN   B HE22 1 
ATOM   17603 N N    . PRO   B  1 363 ? 74.583 -22.569 -56.068 1.00 31.70  ? 389  PRO   B N    1 
ATOM   17604 C CA   . PRO   B  1 363 ? 75.642 -21.731 -56.660 1.00 31.15  ? 389  PRO   B CA   1 
ATOM   17605 C C    . PRO   B  1 363 ? 76.137 -20.568 -55.789 1.00 30.23  ? 389  PRO   B C    1 
ATOM   17606 O O    . PRO   B  1 363 ? 77.264 -20.138 -55.963 1.00 30.14  ? 389  PRO   B O    1 
ATOM   17607 C CB   . PRO   B  1 363 ? 74.990 -21.205 -57.940 1.00 32.11  ? 389  PRO   B CB   1 
ATOM   17608 C CG   . PRO   B  1 363 ? 73.909 -22.199 -58.256 1.00 32.71  ? 389  PRO   B CG   1 
ATOM   17609 C CD   . PRO   B  1 363 ? 73.371 -22.552 -56.913 1.00 31.27  ? 389  PRO   B CD   1 
ATOM   17610 H HA   . PRO   B  1 363 ? 76.494 -22.353 -56.932 0.00 42.76  ? 389  PRO   B HA   1 
ATOM   17611 H HB2  . PRO   B  1 363 ? 74.561 -20.221 -57.753 0.00 42.51  ? 389  PRO   B HB2  1 
ATOM   17612 H HB3  . PRO   B  1 363 ? 75.731 -21.153 -58.736 0.00 43.39  ? 389  PRO   B HB3  1 
ATOM   17613 H HG2  . PRO   B  1 363 ? 73.144 -21.739 -58.880 0.00 43.75  ? 389  PRO   B HG2  1 
ATOM   17614 H HG3  . PRO   B  1 363 ? 74.334 -23.078 -58.739 0.00 44.67  ? 389  PRO   B HG3  1 
ATOM   17615 H HD2  . PRO   B  1 363 ? 72.687 -21.777 -56.568 0.00 41.57  ? 389  PRO   B HD2  1 
ATOM   17616 H HD3  . PRO   B  1 363 ? 72.880 -23.522 -56.950 0.00 42.51  ? 389  PRO   B HD3  1 
ATOM   17617 N N    . LEU   B  1 364 ? 75.330 -20.082 -54.841 1.00 29.85  ? 390  LEU   B N    1 
ATOM   17618 C CA   . LEU   B  1 364 ? 75.714 -18.963 -53.971 1.00 29.90  ? 390  LEU   B CA   1 
ATOM   17619 C C    . LEU   B  1 364 ? 76.388 -19.372 -52.647 1.00 30.47  ? 390  LEU   B C    1 
ATOM   17620 O O    . LEU   B  1 364 ? 76.905 -18.502 -51.945 1.00 30.41  ? 390  LEU   B O    1 
ATOM   17621 C CB   . LEU   B  1 364 ? 74.432 -18.196 -53.590 1.00 29.84  ? 390  LEU   B CB   1 
ATOM   17622 C CG   . LEU   B  1 364 ? 73.517 -17.727 -54.723 1.00 30.78  ? 390  LEU   B CG   1 
ATOM   17623 C CD1  . LEU   B  1 364 ? 72.160 -17.302 -54.178 1.00 30.59  ? 390  LEU   B CD1  1 
ATOM   17624 C CD2  . LEU   B  1 364 ? 74.150 -16.597 -55.497 1.00 31.45  ? 390  LEU   B CD2  1 
ATOM   17625 H H    . LEU   B  1 364 ? 74.397 -20.431 -54.647 0.00 39.47  ? 390  LEU   B H    1 
ATOM   17626 H HA   . LEU   B  1 364 ? 76.385 -18.281 -54.489 0.00 39.15  ? 390  LEU   B HA   1 
ATOM   17627 H HB2  . LEU   B  1 364 ? 73.836 -18.842 -52.947 0.00 38.46  ? 390  LEU   B HB2  1 
ATOM   17628 H HB3  . LEU   B  1 364 ? 74.725 -17.309 -53.032 0.00 38.10  ? 390  LEU   B HB3  1 
ATOM   17629 H HG   . LEU   B  1 364 ? 73.340 -18.547 -55.417 0.00 39.58  ? 390  LEU   B HG   1 
ATOM   17630 H HD11 . LEU   B  1 364 ? 71.544 -16.944 -55.001 0.00 38.25  ? 390  LEU   B HD11 1 
ATOM   17631 H HD12 . LEU   B  1 364 ? 71.683 -18.158 -53.703 0.00 38.62  ? 390  LEU   B HD12 1 
ATOM   17632 H HD13 . LEU   B  1 364 ? 72.305 -16.505 -53.450 0.00 38.10  ? 390  LEU   B HD13 1 
ATOM   17633 H HD21 . LEU   B  1 364 ? 73.524 -16.365 -56.357 0.00 39.70  ? 390  LEU   B HD21 1 
ATOM   17634 H HD22 . LEU   B  1 364 ? 74.222 -15.725 -54.850 0.00 39.45  ? 390  LEU   B HD22 1 
ATOM   17635 H HD23 . LEU   B  1 364 ? 75.145 -16.889 -55.830 0.00 40.25  ? 390  LEU   B HD23 1 
ATOM   17636 N N    . MET   B  1 365 ? 76.306 -20.659 -52.261 1.00 30.75  ? 391  MET   B N    1 
ATOM   17637 C CA   . MET   B  1 365 ? 76.698 -21.112 -50.928 1.00 31.55  ? 391  MET   B CA   1 
ATOM   17638 C C    . MET   B  1 365 ? 78.183 -21.103 -50.601 1.00 32.33  ? 391  MET   B C    1 
ATOM   17639 O O    . MET   B  1 365 ? 78.516 -21.150 -49.415 1.00 32.52  ? 391  MET   B O    1 
ATOM   17640 C CB   . MET   B  1 365 ? 76.119 -22.512 -50.659 1.00 32.45  ? 391  MET   B CB   1 
ATOM   17641 C CG   . MET   B  1 365 ? 74.613 -22.479 -50.440 1.00 35.39  ? 391  MET   B CG   1 
ATOM   17642 S SD   . MET   B  1 365 ? 73.827 -24.091 -50.415 1.00 42.71  ? 391  MET   B SD   1 
ATOM   17643 C CE   . MET   B  1 365 ? 72.123 -23.591 -50.313 1.00 41.12  ? 391  MET   B CE   1 
ATOM   17644 H H    . MET   B  1 365 ? 75.977 -21.414 -52.854 0.00 41.27  ? 391  MET   B H    1 
ATOM   17645 H HA   . MET   B  1 365 ? 76.246 -20.418 -50.221 0.00 41.72  ? 391  MET   B HA   1 
ATOM   17646 H HB2  . MET   B  1 365 ? 76.332 -23.173 -51.498 0.00 44.15  ? 391  MET   B HB2  1 
ATOM   17647 H HB3  . MET   B  1 365 ? 76.571 -22.914 -49.754 0.00 44.01  ? 391  MET   B HB3  1 
ATOM   17648 H HG2  . MET   B  1 365 ? 74.413 -22.000 -49.482 0.00 46.44  ? 391  MET   B HG2  1 
ATOM   17649 H HG3  . MET   B  1 365 ? 74.156 -21.900 -51.241 0.00 46.42  ? 391  MET   B HG3  1 
ATOM   17650 H HE1  . MET   B  1 365 ? 71.495 -24.402 -50.679 0.00 53.76  ? 391  MET   B HE1  1 
ATOM   17651 H HE2  . MET   B  1 365 ? 71.879 -23.370 -49.275 0.00 53.27  ? 391  MET   B HE2  1 
ATOM   17652 H HE3  . MET   B  1 365 ? 71.973 -22.705 -50.928 0.00 53.07  ? 391  MET   B HE3  1 
ATOM   17653 N N    . GLN   B  1 366 ? 79.054 -21.022 -51.590 1.00 32.91  ? 392  GLN   B N    1 
ATOM   17654 C CA   . GLN   B  1 366 ? 80.493 -20.969 -51.340 1.00 34.60  ? 392  GLN   B CA   1 
ATOM   17655 C C    . GLN   B  1 366 ? 81.048 -19.536 -51.534 1.00 33.78  ? 392  GLN   B C    1 
ATOM   17656 O O    . GLN   B  1 366 ? 82.261 -19.372 -51.448 1.00 34.46  ? 392  GLN   B O    1 
ATOM   17657 C CB   . GLN   B  1 366 ? 81.211 -21.982 -52.268 1.00 38.31  ? 392  GLN   B CB   1 
ATOM   17658 C CG   . GLN   B  1 366 ? 82.456 -22.647 -51.680 1.00 46.35  ? 392  GLN   B CG   1 
ATOM   17659 C CD   . GLN   B  1 366 ? 83.087 -23.661 -52.618 1.00 55.39  ? 392  GLN   B CD   1 
ATOM   17660 O OE1  . GLN   B  1 366 ? 82.482 -24.112 -53.604 1.00 58.57  ? 392  GLN   B OE1  1 
ATOM   17661 N NE2  . GLN   B  1 366 ? 84.327 -24.051 -52.328 1.00 56.92  ? 392  GLN   B NE2  1 
ATOM   17662 H H    . GLN   B  1 366 ? 78.818 -21.005 -52.578 0.00 44.58  ? 392  GLN   B H    1 
ATOM   17663 H HA   . GLN   B  1 366 ? 80.692 -21.244 -50.306 0.00 47.28  ? 392  GLN   B HA   1 
ATOM   17664 H HB2  . GLN   B  1 366 ? 80.500 -22.769 -52.517 0.00 52.46  ? 392  GLN   B HB2  1 
ATOM   17665 H HB3  . GLN   B  1 366 ? 81.515 -21.463 -53.176 0.00 52.27  ? 392  GLN   B HB3  1 
ATOM   17666 H HG2  . GLN   B  1 366 ? 83.197 -21.880 -51.463 0.00 62.70  ? 392  GLN   B HG2  1 
ATOM   17667 H HG3  . GLN   B  1 366 ? 82.178 -23.165 -50.763 0.00 62.87  ? 392  GLN   B HG3  1 
ATOM   17668 H HE21 . GLN   B  1 366 ? 84.800 -23.675 -51.513 0.00 76.92  ? 392  GLN   B HE21 1 
ATOM   17669 H HE22 . GLN   B  1 366 ? 84.797 -24.729 -52.921 0.00 77.51  ? 392  GLN   B HE22 1 
ATOM   17670 N N    . LEU   B  1 367 ? 80.188 -18.503 -51.774 1.00 31.82  ? 393  LEU   B N    1 
ATOM   17671 C CA   . LEU   B  1 367 ? 80.652 -17.127 -51.946 1.00 30.66  ? 393  LEU   B CA   1 
ATOM   17672 C C    . LEU   B  1 367 ? 80.992 -16.625 -50.549 1.00 30.23  ? 393  LEU   B C    1 
ATOM   17673 O O    . LEU   B  1 367 ? 80.122 -16.623 -49.680 1.00 29.91  ? 393  LEU   B O    1 
ATOM   17674 C CB   . LEU   B  1 367 ? 79.589 -16.269 -52.654 1.00 30.37  ? 393  LEU   B CB   1 
ATOM   17675 C CG   . LEU   B  1 367 ? 79.211 -16.742 -54.077 1.00 31.52  ? 393  LEU   B CG   1 
ATOM   17676 C CD1  . LEU   B  1 367 ? 78.148 -15.863 -54.681 1.00 31.79  ? 393  LEU   B CD1  1 
ATOM   17677 C CD2  . LEU   B  1 367 ? 80.422 -16.783 -55.004 1.00 32.44  ? 393  LEU   B CD2  1 
ATOM   17678 H H    . LEU   B  1 367 ? 79.179 -18.589 -51.848 0.00 42.31  ? 393  LEU   B H    1 
ATOM   17679 H HA   . LEU   B  1 367 ? 81.545 -17.132 -52.568 0.00 41.21  ? 393  LEU   B HA   1 
ATOM   17680 H HB2  . LEU   B  1 367 ? 78.681 -16.273 -52.054 0.00 39.48  ? 393  LEU   B HB2  1 
ATOM   17681 H HB3  . LEU   B  1 367 ? 79.965 -15.250 -52.739 0.00 39.59  ? 393  LEU   B HB3  1 
ATOM   17682 H HG   . LEU   B  1 367 ? 78.806 -17.752 -54.012 0.00 41.59  ? 393  LEU   B HG   1 
ATOM   17683 H HD11 . LEU   B  1 367 ? 77.867 -16.257 -55.656 0.00 41.17  ? 393  LEU   B HD11 1 
ATOM   17684 H HD12 . LEU   B  1 367 ? 77.280 -15.863 -54.024 0.00 40.70  ? 393  LEU   B HD12 1 
ATOM   17685 H HD13 . LEU   B  1 367 ? 78.539 -14.852 -54.786 0.00 40.79  ? 393  LEU   B HD13 1 
ATOM   17686 H HD21 . LEU   B  1 367 ? 80.084 -16.853 -56.037 0.00 42.96  ? 393  LEU   B HD21 1 
ATOM   17687 H HD22 . LEU   B  1 367 ? 81.012 -15.878 -54.866 0.00 42.80  ? 393  LEU   B HD22 1 
ATOM   17688 H HD23 . LEU   B  1 367 ? 81.024 -17.659 -54.765 0.00 43.49  ? 393  LEU   B HD23 1 
ATOM   17689 N N    . PRO   B  1 368 ? 82.281 -16.344 -50.267 1.00 29.89  ? 394  PRO   B N    1 
ATOM   17690 C CA   . PRO   B  1 368 ? 82.673 -16.060 -48.879 1.00 29.68  ? 394  PRO   B CA   1 
ATOM   17691 C C    . PRO   B  1 368 ? 82.164 -14.766 -48.263 1.00 29.18  ? 394  PRO   B C    1 
ATOM   17692 O O    . PRO   B  1 368 ? 82.016 -14.730 -47.043 1.00 30.25  ? 394  PRO   B O    1 
ATOM   17693 C CB   . PRO   B  1 368 ? 84.210 -16.087 -48.931 1.00 30.39  ? 394  PRO   B CB   1 
ATOM   17694 C CG   . PRO   B  1 368 ? 84.553 -15.792 -50.325 1.00 30.95  ? 394  PRO   B CG   1 
ATOM   17695 C CD   . PRO   B  1 368 ? 83.450 -16.351 -51.169 1.00 29.36  ? 394  PRO   B CD   1 
ATOM   17696 H HA   . PRO   B  1 368 ? 82.351 -16.884 -48.246 0.00 40.18  ? 394  PRO   B HA   1 
ATOM   17697 H HB2  . PRO   B  1 368 ? 84.612 -15.326 -48.263 0.00 41.38  ? 394  PRO   B HB2  1 
ATOM   17698 H HB3  . PRO   B  1 368 ? 84.568 -17.075 -48.646 0.00 42.02  ? 394  PRO   B HB3  1 
ATOM   17699 H HG2  . PRO   B  1 368 ? 84.619 -14.714 -50.459 0.00 41.82  ? 394  PRO   B HG2  1 
ATOM   17700 H HG3  . PRO   B  1 368 ? 85.501 -16.266 -50.577 0.00 42.76  ? 394  PRO   B HG3  1 
ATOM   17701 H HD2  . PRO   B  1 368 ? 83.277 -15.699 -52.024 0.00 39.74  ? 394  PRO   B HD2  1 
ATOM   17702 H HD3  . PRO   B  1 368 ? 83.687 -17.367 -51.482 0.00 40.53  ? 394  PRO   B HD3  1 
ATOM   17703 N N    . ASN   B  1 369 ? 81.891 -13.723 -49.054 1.00 27.81  ? 395  ASN   B N    1 
ATOM   17704 C CA   . ASN   B  1 369 ? 81.429 -12.452 -48.487 1.00 27.51  ? 395  ASN   B CA   1 
ATOM   17705 C C    . ASN   B  1 369 ? 79.974 -12.128 -48.752 1.00 25.56  ? 395  ASN   B C    1 
ATOM   17706 O O    . ASN   B  1 369 ? 79.573 -11.012 -48.462 1.00 24.93  ? 395  ASN   B O    1 
ATOM   17707 C CB   . ASN   B  1 369 ? 82.336 -11.323 -48.977 1.00 29.71  ? 395  ASN   B CB   1 
ATOM   17708 C CG   . ASN   B  1 369 ? 83.735 -11.534 -48.577 1.00 34.80  ? 395  ASN   B CG   1 
ATOM   17709 O OD1  . ASN   B  1 369 ? 83.996 -12.090 -47.487 1.00 36.05  ? 395  ASN   B OD1  1 
ATOM   17710 N ND2  . ASN   B  1 369 ? 84.719 -10.994 -49.231 1.00 36.92  ? 395  ASN   B ND2  1 
ATOM   17711 H H    . ASN   B  1 369 ? 81.980 -13.715 -50.065 0.00 36.65  ? 395  ASN   B H    1 
ATOM   17712 H HA   . ASN   B  1 369 ? 81.519 -12.474 -47.403 0.00 35.75  ? 395  ASN   B HA   1 
ATOM   17713 H HB2  . ASN   B  1 369 ? 82.297 -11.276 -50.064 0.00 38.27  ? 395  ASN   B HB2  1 
ATOM   17714 H HB3  . ASN   B  1 369 ? 82.019 -10.373 -48.548 0.00 37.94  ? 395  ASN   B HB3  1 
ATOM   17715 H HD21 . ASN   B  1 369 ? 85.234 -11.851 -49.275 0.00 48.32  ? 395  ASN   B HD21 1 
ATOM   17716 H HD22 . ASN   B  1 369 ? 84.608 -10.308 -49.970 0.00 47.60  ? 395  ASN   B HD22 1 
ATOM   17717 N N    . LEU   B  1 370 ? 79.180 -13.086 -49.274 1.00 24.48  ? 396  LEU   B N    1 
ATOM   17718 C CA   . LEU   B  1 370 ? 77.769 -12.842 -49.530 1.00 24.38  ? 396  LEU   B CA   1 
ATOM   17719 C C    . LEU   B  1 370 ? 77.051 -12.737 -48.182 1.00 24.94  ? 396  LEU   B C    1 
ATOM   17720 O O    . LEU   B  1 370 ? 76.793 -13.753 -47.536 1.00 25.97  ? 396  LEU   B O    1 
ATOM   17721 C CB   . LEU   B  1 370 ? 77.178 -13.968 -50.398 1.00 24.07  ? 396  LEU   B CB   1 
ATOM   17722 C CG   . LEU   B  1 370 ? 75.688 -13.841 -50.784 1.00 25.19  ? 396  LEU   B CG   1 
ATOM   17723 C CD1  . LEU   B  1 370 ? 75.379 -12.490 -51.427 1.00 25.03  ? 396  LEU   B CD1  1 
ATOM   17724 C CD2  . LEU   B  1 370 ? 75.288 -14.946 -51.759 1.00 25.98  ? 396  LEU   B CD2  1 
ATOM   17725 H H    . LEU   B  1 370 ? 79.475 -14.025 -49.522 0.00 31.83  ? 396  LEU   B H    1 
ATOM   17726 H HA   . LEU   B  1 370 ? 77.666 -11.899 -50.065 0.00 30.43  ? 396  LEU   B HA   1 
ATOM   17727 H HB2  . LEU   B  1 370 ? 77.745 -14.008 -51.326 0.00 30.78  ? 396  LEU   B HB2  1 
ATOM   17728 H HB3  . LEU   B  1 370 ? 77.295 -14.914 -49.869 0.00 30.90  ? 396  LEU   B HB3  1 
ATOM   17729 H HG   . LEU   B  1 370 ? 75.071 -13.944 -49.893 0.00 31.24  ? 396  LEU   B HG   1 
ATOM   17730 H HD11 . LEU   B  1 370 ? 74.382 -12.527 -51.862 0.00 30.47  ? 396  LEU   B HD11 1 
ATOM   17731 H HD12 . LEU   B  1 370 ? 75.417 -11.712 -50.665 0.00 30.47  ? 396  LEU   B HD12 1 
ATOM   17732 H HD13 . LEU   B  1 370 ? 76.118 -12.287 -52.201 0.00 30.91  ? 396  LEU   B HD13 1 
ATOM   17733 H HD21 . LEU   B  1 370 ? 74.203 -14.967 -51.846 0.00 32.37  ? 396  LEU   B HD21 1 
ATOM   17734 H HD22 . LEU   B  1 370 ? 75.729 -14.729 -52.730 0.00 32.76  ? 396  LEU   B HD22 1 
ATOM   17735 H HD23 . LEU   B  1 370 ? 75.652 -15.902 -51.384 0.00 33.09  ? 396  LEU   B HD23 1 
ATOM   17736 N N    . SER   B  1 371 ? 76.819 -11.510 -47.725 1.00 24.36  ? 397  SER   B N    1 
ATOM   17737 C CA   . SER   B  1 371 ? 76.216 -11.266 -46.422 1.00 25.12  ? 397  SER   B CA   1 
ATOM   17738 C C    . SER   B  1 371 ? 74.746 -10.854 -46.499 1.00 23.99  ? 397  SER   B C    1 
ATOM   17739 O O    . SER   B  1 371 ? 74.054 -10.984 -45.493 1.00 23.46  ? 397  SER   B O    1 
ATOM   17740 C CB   . SER   B  1 371 ? 77.028 -10.234 -45.643 1.00 27.98  ? 397  SER   B CB   1 
ATOM   17741 O OG   . SER   B  1 371 ? 76.936 -8.940  -46.214 1.00 32.58  ? 397  SER   B OG   1 
ATOM   17742 H H    . SER   B  1 371 ? 77.033 -10.659 -48.235 0.00 29.83  ? 397  SER   B H    1 
ATOM   17743 H HA   . SER   B  1 371 ? 76.270 -12.174 -45.825 0.00 30.97  ? 397  SER   B HA   1 
ATOM   17744 H HB2  . SER   B  1 371 ? 76.655 -10.193 -44.621 0.00 34.02  ? 397  SER   B HB2  1 
ATOM   17745 H HB3  . SER   B  1 371 ? 78.072 -10.545 -45.633 0.00 34.54  ? 397  SER   B HB3  1 
ATOM   17746 H HG   . SER   B  1 371 ? 76.825 -8.978  -47.200 0.00 39.20  ? 397  SER   B HG   1 
ATOM   17747 N N    . THR   B  1 372 ? 74.259 -10.358 -47.658 1.00 22.95  ? 398  THR   B N    1 
ATOM   17748 C CA   . THR   B  1 372 ? 72.865 -9.941  -47.801 1.00 22.97  ? 398  THR   B CA   1 
ATOM   17749 C C    . THR   B  1 372 ? 72.168 -10.678 -48.931 1.00 22.10  ? 398  THR   B C    1 
ATOM   17750 O O    . THR   B  1 372 ? 72.684 -10.703 -50.049 1.00 21.53  ? 398  THR   B O    1 
ATOM   17751 C CB   . THR   B  1 372 ? 72.780 -8.418  -48.047 1.00 24.87  ? 398  THR   B CB   1 
ATOM   17752 O OG1  . THR   B  1 372 ? 73.250 -7.739  -46.885 1.00 26.55  ? 398  THR   B OG1  1 
ATOM   17753 C CG2  . THR   B  1 372 ? 71.355 -7.941  -48.351 1.00 24.58  ? 398  THR   B CG2  1 
ATOM   17754 H H    . THR   B  1 372 ? 74.799 -10.220 -48.505 0.00 27.33  ? 398  THR   B H    1 
ATOM   17755 H HA   . THR   B  1 372 ? 72.316 -10.154 -46.886 0.00 26.67  ? 398  THR   B HA   1 
ATOM   17756 H HB   . THR   B  1 372 ? 73.414 -8.154  -48.892 0.00 28.74  ? 398  THR   B HB   1 
ATOM   17757 H HG1  . THR   B  1 372 ? 73.389 -6.776  -47.087 0.00 30.46  ? 398  THR   B HG1  1 
ATOM   17758 H HG21 . THR   B  1 372 ? 71.268 -6.872  -48.165 0.00 27.57  ? 398  THR   B HG21 1 
ATOM   17759 H HG22 . THR   B  1 372 ? 71.107 -8.122  -49.396 0.00 27.82  ? 398  THR   B HG22 1 
ATOM   17760 H HG23 . THR   B  1 372 ? 70.641 -8.472  -47.724 0.00 27.77  ? 398  THR   B HG23 1 
ATOM   17761 N N    . ILE   B  1 373 ? 70.982 -11.247 -48.643 1.00 21.65  ? 399  ILE   B N    1 
ATOM   17762 C CA   . ILE   B  1 373 ? 70.127 -11.904 -49.636 1.00 22.70  ? 399  ILE   B CA   1 
ATOM   17763 C C    . ILE   B  1 373 ? 68.767 -11.253 -49.488 1.00 21.20  ? 399  ILE   B C    1 
ATOM   17764 O O    . ILE   B  1 373 ? 68.185 -11.276 -48.393 1.00 20.11  ? 399  ILE   B O    1 
ATOM   17765 C CB   . ILE   B  1 373 ? 70.052 -13.462 -49.524 1.00 24.86  ? 399  ILE   B CB   1 
ATOM   17766 C CG1  . ILE   B  1 373 ? 69.047 -14.053 -50.546 1.00 26.57  ? 399  ILE   B CG1  1 
ATOM   17767 C CG2  . ILE   B  1 373 ? 69.680 -13.935 -48.122 1.00 25.98  ? 399  ILE   B CG2  1 
ATOM   17768 C CD1  . ILE   B  1 373 ? 69.393 -13.780 -51.981 1.00 28.62  ? 399  ILE   B CD1  1 
ATOM   17769 H H    . ILE   B  1 373 ? 70.575 -11.264 -47.714 0.00 24.95  ? 399  ILE   B H    1 
ATOM   17770 H HA   . ILE   B  1 373 ? 70.503 -11.665 -50.630 0.00 26.40  ? 399  ILE   B HA   1 
ATOM   17771 H HB   . ILE   B  1 373 ? 71.038 -13.860 -49.757 0.00 29.74  ? 399  ILE   B HB   1 
ATOM   17772 H HG12 . ILE   B  1 373 ? 69.042 -15.134 -50.423 0.00 31.82  ? 399  ILE   B HG12 1 
ATOM   17773 H HG13 . ILE   B  1 373 ? 68.044 -13.673 -50.359 0.00 31.13  ? 399  ILE   B HG13 1 
ATOM   17774 H HG21 . ILE   B  1 373 ? 69.737 -15.022 -48.093 0.00 31.13  ? 399  ILE   B HG21 1 
ATOM   17775 H HG22 . ILE   B  1 373 ? 70.373 -13.512 -47.396 0.00 30.74  ? 399  ILE   B HG22 1 
ATOM   17776 H HG23 . ILE   B  1 373 ? 68.661 -13.621 -47.900 0.00 30.44  ? 399  ILE   B HG23 1 
ATOM   17777 H HD11 . ILE   B  1 373 ? 68.797 -14.434 -52.615 0.00 34.13  ? 399  ILE   B HD11 1 
ATOM   17778 H HD12 . ILE   B  1 373 ? 69.167 -12.740 -52.212 0.00 33.64  ? 399  ILE   B HD12 1 
ATOM   17779 H HD13 . ILE   B  1 373 ? 70.454 -13.975 -52.131 0.00 34.31  ? 399  ILE   B HD13 1 
ATOM   17780 N N    . ASN   B  1 374 ? 68.279 -10.632 -50.564 1.00 20.44  ? 400  ASN   B N    1 
ATOM   17781 C CA   . ASN   B  1 374 ? 67.011 -9.936  -50.519 1.00 20.55  ? 400  ASN   B CA   1 
ATOM   17782 C C    . ASN   B  1 374 ? 66.011 -10.598 -51.467 1.00 19.76  ? 400  ASN   B C    1 
ATOM   17783 O O    . ASN   B  1 374 ? 66.170 -10.550 -52.684 1.00 18.89  ? 400  ASN   B O    1 
ATOM   17784 C CB   . ASN   B  1 374 ? 67.254 -8.437  -50.775 1.00 21.62  ? 400  ASN   B CB   1 
ATOM   17785 C CG   . ASN   B  1 374 ? 66.048 -7.599  -51.066 1.00 23.61  ? 400  ASN   B CG   1 
ATOM   17786 O OD1  . ASN   B  1 374 ? 64.915 -7.987  -50.787 1.00 25.78  ? 400  ASN   B OD1  1 
ATOM   17787 N ND2  . ASN   B  1 374 ? 66.275 -6.394  -51.600 1.00 22.21  ? 400  ASN   B ND2  1 
ATOM   17788 H H    . ASN   B  1 374 ? 68.729 -10.595 -51.473 0.00 23.07  ? 400  ASN   B H    1 
ATOM   17789 H HA   . ASN   B  1 374 ? 66.587 -10.000 -49.521 0.00 22.55  ? 400  ASN   B HA   1 
ATOM   17790 H HB2  . ASN   B  1 374 ? 67.687 -8.027  -49.863 0.00 23.56  ? 400  ASN   B HB2  1 
ATOM   17791 H HB3  . ASN   B  1 374 ? 67.979 -8.308  -51.573 0.00 23.77  ? 400  ASN   B HB3  1 
ATOM   17792 H HD21 . ASN   B  1 374 ? 65.499 -5.777  -51.819 0.00 23.57  ? 400  ASN   B HD21 1 
ATOM   17793 H HD22 . ASN   B  1 374 ? 67.225 -6.092  -51.787 0.00 23.89  ? 400  ASN   B HD22 1 
ATOM   17794 N N    . LEU   B  1 375 ? 65.001 -11.280 -50.879 1.00 19.28  ? 401  LEU   B N    1 
ATOM   17795 C CA   . LEU   B  1 375 ? 63.939 -11.931 -51.628 1.00 19.33  ? 401  LEU   B CA   1 
ATOM   17796 C C    . LEU   B  1 375 ? 62.576 -11.335 -51.281 1.00 18.25  ? 401  LEU   B C    1 
ATOM   17797 O O    . LEU   B  1 375 ? 61.582 -12.050 -51.303 1.00 17.96  ? 401  LEU   B O    1 
ATOM   17798 C CB   . LEU   B  1 375 ? 63.947 -13.450 -51.371 1.00 19.75  ? 401  LEU   B CB   1 
ATOM   17799 C CG   . LEU   B  1 375 ? 65.185 -14.214 -51.843 1.00 21.53  ? 401  LEU   B CG   1 
ATOM   17800 C CD1  . LEU   B  1 375 ? 65.295 -15.565 -51.106 1.00 22.29  ? 401  LEU   B CD1  1 
ATOM   17801 C CD2  . LEU   B  1 375 ? 65.133 -14.448 -53.346 1.00 22.19  ? 401  LEU   B CD2  1 
ATOM   17802 H H    . LEU   B  1 375 ? 64.903 -11.402 -49.877 0.00 21.15  ? 401  LEU   B H    1 
ATOM   17803 H HA   . LEU   B  1 375 ? 64.076 -11.758 -52.694 0.00 21.43  ? 401  LEU   B HA   1 
ATOM   17804 H HB2  . LEU   B  1 375 ? 63.836 -13.621 -50.303 0.00 22.26  ? 401  LEU   B HB2  1 
ATOM   17805 H HB3  . LEU   B  1 375 ? 63.107 -13.901 -51.896 0.00 22.39  ? 401  LEU   B HB3  1 
ATOM   17806 H HG   . LEU   B  1 375 ? 66.084 -13.639 -51.622 0.00 24.82  ? 401  LEU   B HG   1 
ATOM   17807 H HD11 . LEU   B  1 375 ? 66.078 -16.160 -51.573 0.00 26.59  ? 401  LEU   B HD11 1 
ATOM   17808 H HD12 . LEU   B  1 375 ? 65.542 -15.380 -50.062 0.00 26.11  ? 401  LEU   B HD12 1 
ATOM   17809 H HD13 . LEU   B  1 375 ? 64.339 -16.080 -51.177 0.00 26.26  ? 401  LEU   B HD13 1 
ATOM   17810 H HD21 . LEU   B  1 375 ? 66.145 -14.627 -53.706 0.00 26.15  ? 401  LEU   B HD21 1 
ATOM   17811 H HD22 . LEU   B  1 375 ? 64.517 -15.325 -53.539 0.00 26.14  ? 401  LEU   B HD22 1 
ATOM   17812 H HD23 . LEU   B  1 375 ? 64.712 -13.587 -53.861 0.00 25.62  ? 401  LEU   B HD23 1 
ATOM   17813 N N    . GLY   B  1 376 ? 62.516 -10.023 -51.061 1.00 18.21  ? 402  GLY   B N    1 
ATOM   17814 C CA   . GLY   B  1 376 ? 61.247 -9.362  -50.796 1.00 18.57  ? 402  GLY   B CA   1 
ATOM   17815 C C    . GLY   B  1 376 ? 60.336 -9.407  -52.013 1.00 18.42  ? 402  GLY   B C    1 
ATOM   17816 O O    . GLY   B  1 376 ? 60.814 -9.425  -53.146 1.00 17.59  ? 402  GLY   B O    1 
ATOM   17817 H H    . GLY   B  1 376 ? 63.307 -9.388  -51.077 0.00 19.21  ? 402  GLY   B H    1 
ATOM   17818 H HA2  . GLY   B  1 376 ? 60.747 -9.852  -49.962 0.00 19.41  ? 402  GLY   B HA2  1 
ATOM   17819 H HA3  . GLY   B  1 376 ? 61.424 -8.320  -50.534 0.00 19.15  ? 402  GLY   B HA3  1 
ATOM   17820 N N    . ILE   B  1 377 ? 59.011 -9.448  -51.791 1.00 18.24  ? 403  ILE   B N    1 
ATOM   17821 C CA   . ILE   B  1 377 ? 57.999 -9.333  -52.857 1.00 18.33  ? 403  ILE   B CA   1 
ATOM   17822 C C    . ILE   B  1 377 ? 58.165 -10.377 -53.976 1.00 18.36  ? 403  ILE   B C    1 
ATOM   17823 O O    . ILE   B  1 377 ? 58.275 -10.031 -55.159 1.00 17.69  ? 403  ILE   B O    1 
ATOM   17824 C CB   . ILE   B  1 377 ? 57.937 -7.863  -53.437 1.00 19.00  ? 403  ILE   B CB   1 
ATOM   17825 C CG1  . ILE   B  1 377 ? 58.099 -6.773  -52.323 1.00 20.16  ? 403  ILE   B CG1  1 
ATOM   17826 C CG2  . ILE   B  1 377 ? 56.621 -7.632  -54.218 1.00 18.91  ? 403  ILE   B CG2  1 
ATOM   17827 C CD1  . ILE   B  1 377 ? 58.325 -5.335  -52.867 1.00 21.66  ? 403  ILE   B CD1  1 
ATOM   17828 H H    . ILE   B  1 377 ? 58.602 -9.558  -50.869 0.00 18.86  ? 403  ILE   B H    1 
ATOM   17829 H HA   . ILE   B  1 377 ? 57.037 -9.537  -52.389 0.00 19.07  ? 403  ILE   B HA   1 
ATOM   17830 H HB   . ILE   B  1 377 ? 58.767 -7.733  -54.129 0.00 19.74  ? 403  ILE   B HB   1 
ATOM   17831 H HG12 . ILE   B  1 377 ? 57.194 -6.759  -51.718 0.00 20.58  ? 403  ILE   B HG12 1 
ATOM   17832 H HG13 . ILE   B  1 377 ? 58.960 -7.001  -51.696 0.00 20.69  ? 403  ILE   B HG13 1 
ATOM   17833 H HG21 . ILE   B  1 377 ? 56.648 -6.654  -54.696 0.00 19.43  ? 403  ILE   B HG21 1 
ATOM   17834 H HG22 . ILE   B  1 377 ? 56.502 -8.401  -54.980 0.00 19.85  ? 403  ILE   B HG22 1 
ATOM   17835 H HG23 . ILE   B  1 377 ? 55.788 -7.674  -53.519 0.00 19.47  ? 403  ILE   B HG23 1 
ATOM   17836 H HD11 . ILE   B  1 377 ? 58.632 -4.692  -52.044 0.00 22.09  ? 403  ILE   B HD11 1 
ATOM   17837 H HD12 . ILE   B  1 377 ? 59.101 -5.362  -53.630 0.00 22.40  ? 403  ILE   B HD12 1 
ATOM   17838 H HD13 . ILE   B  1 377 ? 57.395 -4.961  -53.293 0.00 22.23  ? 403  ILE   B HD13 1 
ATOM   17839 N N    . ASN   B  1 378 ? 58.186 -11.648 -53.599 1.00 18.03  ? 404  ASN   B N    1 
ATOM   17840 C CA   . ASN   B  1 378 ? 58.277 -12.746 -54.562 1.00 17.78  ? 404  ASN   B CA   1 
ATOM   17841 C C    . ASN   B  1 378 ? 57.071 -13.696 -54.491 1.00 17.58  ? 404  ASN   B C    1 
ATOM   17842 O O    . ASN   B  1 378 ? 57.045 -14.686 -55.225 1.00 18.26  ? 404  ASN   B O    1 
ATOM   17843 C CB   . ASN   B  1 378 ? 59.570 -13.541 -54.323 1.00 18.30  ? 404  ASN   B CB   1 
ATOM   17844 C CG   . ASN   B  1 378 ? 60.772 -12.926 -54.979 1.00 18.75  ? 404  ASN   B CG   1 
ATOM   17845 O OD1  . ASN   B  1 378 ? 60.819 -12.849 -56.184 1.00 20.13  ? 404  ASN   B OD1  1 
ATOM   17846 N ND2  . ASN   B  1 378 ? 61.768 -12.511 -54.222 1.00 16.41  ? 404  ASN   B ND2  1 
ATOM   17847 H H    . ASN   B  1 378 ? 58.149 -11.953 -52.632 0.00 19.42  ? 404  ASN   B H    1 
ATOM   17848 H HA   . ASN   B  1 378 ? 58.282 -12.360 -55.580 0.00 19.67  ? 404  ASN   B HA   1 
ATOM   17849 H HB2  . ASN   B  1 378 ? 59.745 -13.633 -53.252 0.00 20.41  ? 404  ASN   B HB2  1 
ATOM   17850 H HB3  . ASN   B  1 378 ? 59.476 -14.523 -54.782 0.00 20.89  ? 404  ASN   B HB3  1 
ATOM   17851 H HD21 . ASN   B  1 378 ? 62.588 -12.093 -54.649 0.00 18.08  ? 404  ASN   B HD21 1 
ATOM   17852 H HD22 . ASN   B  1 378 ? 61.723 -12.615 -53.213 0.00 17.97  ? 404  ASN   B HD22 1 
ATOM   17853 N N    . PHE   B  1 379 ? 56.070 -13.403 -53.629 1.00 17.12  ? 405  PHE   B N    1 
ATOM   17854 C CA   . PHE   B  1 379 ? 54.910 -14.267 -53.410 1.00 17.74  ? 405  PHE   B CA   1 
ATOM   17855 C C    . PHE   B  1 379 ? 55.350 -15.701 -53.051 1.00 18.06  ? 405  PHE   B C    1 
ATOM   17856 O O    . PHE   B  1 379 ? 54.715 -16.659 -53.457 1.00 18.75  ? 405  PHE   B O    1 
ATOM   17857 C CB   . PHE   B  1 379 ? 53.930 -14.193 -54.612 1.00 18.00  ? 405  PHE   B CB   1 
ATOM   17858 C CG   . PHE   B  1 379 ? 53.302 -12.817 -54.728 1.00 19.64  ? 405  PHE   B CG   1 
ATOM   17859 C CD1  . PHE   B  1 379 ? 52.226 -12.458 -53.930 1.00 21.09  ? 405  PHE   B CD1  1 
ATOM   17860 C CD2  . PHE   B  1 379 ? 53.843 -11.858 -55.567 1.00 20.78  ? 405  PHE   B CD2  1 
ATOM   17861 C CE1  . PHE   B  1 379 ? 51.711 -11.171 -53.959 1.00 21.88  ? 405  PHE   B CE1  1 
ATOM   17862 C CE2  . PHE   B  1 379 ? 53.319 -10.573 -55.603 1.00 21.60  ? 405  PHE   B CE2  1 
ATOM   17863 C CZ   . PHE   B  1 379 ? 52.254 -10.240 -54.803 1.00 21.71  ? 405  PHE   B CZ   1 
ATOM   17864 H H    . PHE   B  1 379 ? 56.021 -12.562 -53.064 0.00 18.51  ? 405  PHE   B H    1 
ATOM   17865 H HA   . PHE   B  1 379 ? 54.394 -13.873 -52.538 0.00 19.57  ? 405  PHE   B HA   1 
ATOM   17866 H HB2  . PHE   B  1 379 ? 54.466 -14.407 -55.536 0.00 20.52  ? 405  PHE   B HB2  1 
ATOM   17867 H HB3  . PHE   B  1 379 ? 53.122 -14.910 -54.473 0.00 20.53  ? 405  PHE   B HB3  1 
ATOM   17868 H HD1  . PHE   B  1 379 ? 51.795 -13.170 -53.271 0.00 23.54  ? 405  PHE   B HD1  1 
ATOM   17869 H HD2  . PHE   B  1 379 ? 54.699 -12.101 -56.172 0.00 23.26  ? 405  PHE   B HD2  1 
ATOM   17870 H HE1  . PHE   B  1 379 ? 50.857 -10.919 -53.353 0.00 23.93  ? 405  PHE   B HE1  1 
ATOM   17871 H HE2  . PHE   B  1 379 ? 53.740 -9.837  -56.263 0.00 23.68  ? 405  PHE   B HE2  1 
ATOM   17872 H HZ   . PHE   B  1 379 ? 51.825 -9.253  -54.861 0.00 23.49  ? 405  PHE   B HZ   1 
ATOM   17873 N N    . ILE   B  1 380 ? 56.469 -15.834 -52.302 1.00 18.05  ? 406  ILE   B N    1 
ATOM   17874 C CA   . ILE   B  1 380 ? 56.996 -17.134 -51.902 1.00 18.83  ? 406  ILE   B CA   1 
ATOM   17875 C C    . ILE   B  1 380 ? 56.060 -17.680 -50.841 1.00 19.58  ? 406  ILE   B C    1 
ATOM   17876 O O    . ILE   B  1 380 ? 55.806 -16.997 -49.856 1.00 19.63  ? 406  ILE   B O    1 
ATOM   17877 C CB   . ILE   B  1 380 ? 58.446 -17.037 -51.323 1.00 18.82  ? 406  ILE   B CB   1 
ATOM   17878 C CG1  . ILE   B  1 380 ? 59.453 -16.563 -52.392 1.00 19.91  ? 406  ILE   B CG1  1 
ATOM   17879 C CG2  . ILE   B  1 380 ? 58.879 -18.399 -50.772 1.00 18.77  ? 406  ILE   B CG2  1 
ATOM   17880 C CD1  . ILE   B  1 380 ? 60.741 -15.943 -51.808 1.00 21.22  ? 406  ILE   B CD1  1 
ATOM   17881 H H    . ILE   B  1 380 ? 57.022 -15.058 -51.949 0.00 20.28  ? 406  ILE   B H    1 
ATOM   17882 H HA   . ILE   B  1 380 ? 57.014 -17.805 -52.758 0.00 22.30  ? 406  ILE   B HA   1 
ATOM   17883 H HB   . ILE   B  1 380 ? 58.438 -16.321 -50.502 0.00 21.53  ? 406  ILE   B HB   1 
ATOM   17884 H HG12 . ILE   B  1 380 ? 59.739 -17.413 -53.009 0.00 23.63  ? 406  ILE   B HG12 1 
ATOM   17885 H HG13 . ILE   B  1 380 ? 58.964 -15.809 -53.004 0.00 22.99  ? 406  ILE   B HG13 1 
ATOM   17886 H HG21 . ILE   B  1 380 ? 59.966 -18.456 -50.741 0.00 22.40  ? 406  ILE   B HG21 1 
ATOM   17887 H HG22 . ILE   B  1 380 ? 58.492 -18.515 -49.761 0.00 22.21  ? 406  ILE   B HG22 1 
ATOM   17888 H HG23 . ILE   B  1 380 ? 58.486 -19.186 -51.414 0.00 22.65  ? 406  ILE   B HG23 1 
ATOM   17889 H HD11 . ILE   B  1 380 ? 61.299 -15.470 -52.615 0.00 24.57  ? 406  ILE   B HD11 1 
ATOM   17890 H HD12 . ILE   B  1 380 ? 60.471 -15.199 -51.060 0.00 24.23  ? 406  ILE   B HD12 1 
ATOM   17891 H HD13 . ILE   B  1 380 ? 61.352 -16.722 -51.355 0.00 24.88  ? 406  ILE   B HD13 1 
ATOM   17892 N N    . LYS   B  1 381 ? 55.592 -18.896 -51.008 1.00 20.46  ? 407  LYS   B N    1 
ATOM   17893 C CA   . LYS   B  1 381 ? 54.685 -19.526 -50.050 1.00 22.47  ? 407  LYS   B CA   1 
ATOM   17894 C C    . LYS   B  1 381 ? 55.419 -20.391 -49.037 1.00 24.52  ? 407  LYS   B C    1 
ATOM   17895 O O    . LYS   B  1 381 ? 54.927 -20.543 -47.920 1.00 25.15  ? 407  LYS   B O    1 
ATOM   17896 C CB   . LYS   B  1 381 ? 53.656 -20.392 -50.790 1.00 24.11  ? 407  LYS   B CB   1 
ATOM   17897 C CG   . LYS   B  1 381 ? 52.741 -19.566 -51.683 1.00 28.57  ? 407  LYS   B CG   1 
ATOM   17898 C CD   . LYS   B  1 381 ? 51.589 -20.390 -52.255 1.00 32.95  ? 407  LYS   B CD   1 
ATOM   17899 C CE   . LYS   B  1 381 ? 51.691 -20.671 -53.723 1.00 36.69  ? 407  LYS   B CE   1 
ATOM   17900 N NZ   . LYS   B  1 381 ? 50.354 -21.021 -54.293 1.00 38.51  ? 407  LYS   B NZ   1 
ATOM   17901 H H    . LYS   B  1 381 ? 55.819 -19.492 -51.798 0.00 24.75  ? 407  LYS   B H    1 
ATOM   17902 H HA   . LYS   B  1 381 ? 54.129 -18.769 -49.499 0.00 26.57  ? 407  LYS   B HA   1 
ATOM   17903 H HB2  . LYS   B  1 381 ? 54.172 -21.122 -51.412 0.00 29.73  ? 407  LYS   B HB2  1 
ATOM   17904 H HB3  . LYS   B  1 381 ? 53.041 -20.901 -50.050 0.00 29.48  ? 407  LYS   B HB3  1 
ATOM   17905 H HG2  . LYS   B  1 381 ? 52.313 -18.757 -51.093 0.00 34.10  ? 407  LYS   B HG2  1 
ATOM   17906 H HG3  . LYS   B  1 381 ? 53.326 -19.156 -52.505 0.00 34.40  ? 407  LYS   B HG3  1 
ATOM   17907 H HD2  . LYS   B  1 381 ? 51.543 -21.349 -51.741 0.00 40.49  ? 407  LYS   B HD2  1 
ATOM   17908 H HD3  . LYS   B  1 381 ? 50.661 -19.844 -52.090 0.00 39.98  ? 407  LYS   B HD3  1 
ATOM   17909 H HE2  . LYS   B  1 381 ? 52.054 -19.790 -54.250 0.00 44.81  ? 407  LYS   B HE2  1 
ATOM   17910 H HE3  . LYS   B  1 381 ? 52.363 -21.513 -53.883 0.00 45.43  ? 407  LYS   B HE3  1 
ATOM   17911 H HZ1  . LYS   B  1 381 ? 50.458 -21.326 -55.255 0.00 47.92  ? 407  LYS   B HZ1  1 
ATOM   17912 H HZ2  . LYS   B  1 381 ? 49.931 -21.769 -53.752 0.00 47.83  ? 407  LYS   B HZ2  1 
ATOM   17913 H HZ3  . LYS   B  1 381 ? 49.745 -20.210 -54.269 0.00 47.30  ? 407  LYS   B HZ3  1 
ATOM   17914 N N    . GLN   B  1 382 ? 56.562 -20.996 -49.425 1.00 25.43  ? 408  GLN   B N    1 
ATOM   17915 C CA   . GLN   B  1 382 ? 57.299 -21.882 -48.530 1.00 26.66  ? 408  GLN   B CA   1 
ATOM   17916 C C    . GLN   B  1 382 ? 58.795 -21.826 -48.798 1.00 26.74  ? 408  GLN   B C    1 
ATOM   17917 O O    . GLN   B  1 382 ? 59.214 -21.713 -49.951 1.00 26.14  ? 408  GLN   B O    1 
ATOM   17918 C CB   . GLN   B  1 382 ? 56.817 -23.346 -48.710 1.00 29.40  ? 408  GLN   B CB   1 
ATOM   17919 C CG   . GLN   B  1 382 ? 55.480 -23.677 -48.033 1.00 34.94  ? 408  GLN   B CG   1 
ATOM   17920 C CD   . GLN   B  1 382 ? 55.554 -23.643 -46.511 1.00 41.85  ? 408  GLN   B CD   1 
ATOM   17921 O OE1  . GLN   B  1 382 ? 56.116 -24.554 -45.874 1.00 44.04  ? 408  GLN   B OE1  1 
ATOM   17922 N NE2  . GLN   B  1 382 ? 55.017 -22.578 -45.881 1.00 41.67  ? 408  GLN   B NE2  1 
ATOM   17923 H H    . GLN   B  1 382 ? 56.988 -20.908 -50.342 0.00 31.16  ? 408  GLN   B H    1 
ATOM   17924 H HA   . GLN   B  1 382 ? 57.142 -21.577 -47.497 0.00 32.66  ? 408  GLN   B HA   1 
ATOM   17925 H HB2  . GLN   B  1 382 ? 56.702 -23.544 -49.775 0.00 37.03  ? 408  GLN   B HB2  1 
ATOM   17926 H HB3  . GLN   B  1 382 ? 57.570 -24.014 -48.294 0.00 37.14  ? 408  GLN   B HB3  1 
ATOM   17927 H HG2  . GLN   B  1 382 ? 54.728 -22.963 -48.366 0.00 43.18  ? 408  GLN   B HG2  1 
ATOM   17928 H HG3  . GLN   B  1 382 ? 55.182 -24.683 -48.325 0.00 44.00  ? 408  GLN   B HG3  1 
ATOM   17929 H HE21 . GLN   B  1 382 ? 54.582 -21.828 -46.409 0.00 50.59  ? 408  GLN   B HE21 1 
ATOM   17930 H HE22 . GLN   B  1 382 ? 55.050 -22.524 -44.868 0.00 50.82  ? 408  GLN   B HE22 1 
ATOM   17931 N N    . ILE   B  1 383 ? 59.593 -21.986 -47.734 1.00 27.04  ? 409  ILE   B N    1 
ATOM   17932 C CA   . ILE   B  1 383 ? 61.054 -21.966 -47.789 1.00 28.04  ? 409  ILE   B CA   1 
ATOM   17933 C C    . ILE   B  1 383 ? 61.603 -23.114 -46.958 1.00 29.28  ? 409  ILE   B C    1 
ATOM   17934 O O    . ILE   B  1 383 ? 61.133 -23.337 -45.842 1.00 29.23  ? 409  ILE   B O    1 
ATOM   17935 C CB   . ILE   B  1 383 ? 61.589 -20.607 -47.241 1.00 28.60  ? 409  ILE   B CB   1 
ATOM   17936 C CG1  . ILE   B  1 383 ? 61.071 -19.451 -48.127 1.00 29.86  ? 409  ILE   B CG1  1 
ATOM   17937 C CG2  . ILE   B  1 383 ? 63.153 -20.616 -47.131 1.00 29.07  ? 409  ILE   B CG2  1 
ATOM   17938 C CD1  . ILE   B  1 383 ? 61.607 -18.066 -47.847 1.00 30.73  ? 409  ILE   B CD1  1 
ATOM   17939 H H    . ILE   B  1 383 ? 59.239 -22.143 -46.796 0.00 33.46  ? 409  ILE   B H    1 
ATOM   17940 H HA   . ILE   B  1 383 ? 61.408 -22.082 -48.812 0.00 35.00  ? 409  ILE   B HA   1 
ATOM   17941 H HB   . ILE   B  1 383 ? 61.185 -20.467 -46.239 0.00 34.79  ? 409  ILE   B HB   1 
ATOM   17942 H HG12 . ILE   B  1 383 ? 61.302 -19.683 -49.165 0.00 36.18  ? 409  ILE   B HG12 1 
ATOM   17943 H HG13 . ILE   B  1 383 ? 59.991 -19.390 -48.008 0.00 35.85  ? 409  ILE   B HG13 1 
ATOM   17944 H HG21 . ILE   B  1 383 ? 63.507 -19.642 -46.798 0.00 35.35  ? 409  ILE   B HG21 1 
ATOM   17945 H HG22 . ILE   B  1 383 ? 63.473 -21.358 -46.402 0.00 36.04  ? 409  ILE   B HG22 1 
ATOM   17946 H HG23 . ILE   B  1 383 ? 63.573 -20.850 -48.107 0.00 35.93  ? 409  ILE   B HG23 1 
ATOM   17947 H HD11 . ILE   B  1 383 ? 61.002 -17.339 -48.387 0.00 36.22  ? 409  ILE   B HD11 1 
ATOM   17948 H HD12 . ILE   B  1 383 ? 61.541 -17.888 -46.775 0.00 36.40  ? 409  ILE   B HD12 1 
ATOM   17949 H HD13 . ILE   B  1 383 ? 62.641 -17.999 -48.181 0.00 36.64  ? 409  ILE   B HD13 1 
ATOM   17950 N N    . ASP   B  1 384 ? 62.620 -23.809 -47.477 1.00 30.33  ? 410  ASP   B N    1 
ATOM   17951 C CA   . ASP   B  1 384 ? 63.335 -24.836 -46.718 1.00 31.51  ? 410  ASP   B CA   1 
ATOM   17952 C C    . ASP   B  1 384 ? 64.376 -24.002 -45.971 1.00 30.86  ? 410  ASP   B C    1 
ATOM   17953 O O    . ASP   B  1 384 ? 65.439 -23.745 -46.513 1.00 30.80  ? 410  ASP   B O    1 
ATOM   17954 C CB   . ASP   B  1 384 ? 64.030 -25.863 -47.646 1.00 35.72  ? 410  ASP   B CB   1 
ATOM   17955 C CG   . ASP   B  1 384 ? 63.182 -27.055 -48.071 1.00 46.53  ? 410  ASP   B CG   1 
ATOM   17956 O OD1  . ASP   B  1 384 ? 62.046 -27.200 -47.548 1.00 49.00  ? 410  ASP   B OD1  1 
ATOM   17957 O OD2  . ASP   B  1 384 ? 63.665 -27.861 -48.914 1.00 50.33  ? 410  ASP   B OD2  1 
ATOM   17958 H H    . ASP   B  1 384 ? 62.967 -23.681 -48.421 0.00 38.64  ? 410  ASP   B H    1 
ATOM   17959 H HA   . ASP   B  1 384 ? 62.693 -25.341 -45.998 0.00 40.69  ? 410  ASP   B HA   1 
ATOM   17960 H HB2  . ASP   B  1 384 ? 64.380 -25.367 -48.550 0.00 46.15  ? 410  ASP   B HB2  1 
ATOM   17961 H HB3  . ASP   B  1 384 ? 64.887 -26.272 -47.112 0.00 46.62  ? 410  ASP   B HB3  1 
ATOM   17962 N N    . PHE   B  1 385 ? 64.047 -23.512 -44.770 1.00 30.76  ? 411  PHE   B N    1 
ATOM   17963 C CA   . PHE   B  1 385 ? 64.941 -22.621 -44.027 1.00 31.41  ? 411  PHE   B CA   1 
ATOM   17964 C C    . PHE   B  1 385 ? 66.334 -23.189 -43.710 1.00 32.79  ? 411  PHE   B C    1 
ATOM   17965 O O    . PHE   B  1 385 ? 67.263 -22.403 -43.527 1.00 33.18  ? 411  PHE   B O    1 
ATOM   17966 C CB   . PHE   B  1 385 ? 64.270 -22.131 -42.736 1.00 31.01  ? 411  PHE   B CB   1 
ATOM   17967 C CG   . PHE   B  1 385 ? 63.148 -21.150 -42.962 1.00 31.34  ? 411  PHE   B CG   1 
ATOM   17968 C CD1  . PHE   B  1 385 ? 63.407 -19.799 -43.117 1.00 31.58  ? 411  PHE   B CD1  1 
ATOM   17969 C CD2  . PHE   B  1 385 ? 61.835 -21.583 -43.059 1.00 31.92  ? 411  PHE   B CD2  1 
ATOM   17970 C CE1  . PHE   B  1 385 ? 62.382 -18.904 -43.373 1.00 31.92  ? 411  PHE   B CE1  1 
ATOM   17971 C CE2  . PHE   B  1 385 ? 60.809 -20.681 -43.318 1.00 32.31  ? 411  PHE   B CE2  1 
ATOM   17972 C CZ   . PHE   B  1 385 ? 61.092 -19.349 -43.482 1.00 31.82  ? 411  PHE   B CZ   1 
ATOM   17973 H H    . PHE   B  1 385 ? 63.175 -23.720 -44.294 0.00 39.01  ? 411  PHE   B H    1 
ATOM   17974 H HA   . PHE   B  1 385 ? 65.120 -21.749 -44.655 0.00 39.25  ? 411  PHE   B HA   1 
ATOM   17975 H HB2  . PHE   B  1 385 ? 63.879 -22.983 -42.182 0.00 39.09  ? 411  PHE   B HB2  1 
ATOM   17976 H HB3  . PHE   B  1 385 ? 65.029 -21.616 -42.152 0.00 38.69  ? 411  PHE   B HB3  1 
ATOM   17977 H HD1  . PHE   B  1 385 ? 64.423 -19.443 -43.063 0.00 38.35  ? 411  PHE   B HD1  1 
ATOM   17978 H HD2  . PHE   B  1 385 ? 61.610 -22.631 -42.955 0.00 39.66  ? 411  PHE   B HD2  1 
ATOM   17979 H HE1  . PHE   B  1 385 ? 62.600 -17.855 -43.492 0.00 37.86  ? 411  PHE   B HE1  1 
ATOM   17980 H HE2  . PHE   B  1 385 ? 59.792 -21.025 -43.387 0.00 39.22  ? 411  PHE   B HE2  1 
ATOM   17981 H HZ   . PHE   B  1 385 ? 60.293 -18.648 -43.653 0.00 37.75  ? 411  PHE   B HZ   1 
ATOM   17982 N N    . LYS   B  1 386 ? 66.501 -24.528 -43.675 1.00 33.31  ? 412  LYS   B N    1 
ATOM   17983 C CA   . LYS   B  1 386 ? 67.812 -25.128 -43.411 1.00 34.11  ? 412  LYS   B CA   1 
ATOM   17984 C C    . LYS   B  1 386 ? 68.879 -24.700 -44.421 1.00 33.59  ? 412  LYS   B C    1 
ATOM   17985 O O    . LYS   B  1 386 ? 70.061 -24.805 -44.120 1.00 34.01  ? 412  LYS   B O    1 
ATOM   17986 C CB   . LYS   B  1 386 ? 67.721 -26.667 -43.392 1.00 37.42  ? 412  LYS   B CB   1 
ATOM   17987 C CG   . LYS   B  1 386 ? 67.409 -27.313 -44.739 1.00 43.54  ? 412  LYS   B CG   1 
ATOM   17988 C CD   . LYS   B  1 386 ? 67.124 -28.811 -44.582 1.00 50.28  ? 412  LYS   B CD   1 
ATOM   17989 C CE   . LYS   B  1 386 ? 66.740 -29.461 -45.894 1.00 55.22  ? 412  LYS   B CE   1 
ATOM   17990 N NZ   . LYS   B  1 386 ? 66.500 -30.923 -45.749 1.00 58.56  ? 412  LYS   B NZ   1 
ATOM   17991 H H    . LYS   B  1 386 ? 65.758 -25.206 -43.803 0.00 43.24  ? 412  LYS   B H    1 
ATOM   17992 H HA   . LYS   B  1 386 ? 68.145 -24.807 -42.425 0.00 44.53  ? 412  LYS   B HA   1 
ATOM   17993 H HB2  . LYS   B  1 386 ? 68.676 -27.065 -43.052 0.00 49.75  ? 412  LYS   B HB2  1 
ATOM   17994 H HB3  . LYS   B  1 386 ? 66.936 -26.961 -42.696 0.00 49.30  ? 412  LYS   B HB3  1 
ATOM   17995 H HG2  . LYS   B  1 386 ? 66.529 -26.840 -45.171 0.00 56.52  ? 412  LYS   B HG2  1 
ATOM   17996 H HG3  . LYS   B  1 386 ? 68.262 -27.212 -45.409 0.00 57.08  ? 412  LYS   B HG3  1 
ATOM   17997 H HD2  . LYS   B  1 386 ? 68.019 -29.306 -44.208 0.00 66.25  ? 412  LYS   B HD2  1 
ATOM   17998 H HD3  . LYS   B  1 386 ? 66.302 -28.947 -43.882 0.00 65.68  ? 412  LYS   B HD3  1 
ATOM   17999 H HE2  . LYS   B  1 386 ? 65.823 -29.002 -46.261 0.00 71.62  ? 412  LYS   B HE2  1 
ATOM   18000 H HE3  . LYS   B  1 386 ? 67.546 -29.317 -46.612 0.00 72.14  ? 412  LYS   B HE3  1 
ATOM   18001 H HZ1  . LYS   B  1 386 ? 66.226 -31.318 -46.642 0.00 77.08  ? 412  LYS   B HZ1  1 
ATOM   18002 H HZ2  . LYS   B  1 386 ? 67.348 -31.383 -45.432 0.00 77.28  ? 412  LYS   B HZ2  1 
ATOM   18003 H HZ3  . LYS   B  1 386 ? 65.761 -31.089 -45.074 0.00 76.79  ? 412  LYS   B HZ3  1 
ATOM   18004 N N    . LEU   B  1 387 ? 68.480 -24.230 -45.613 1.00 32.44  ? 413  LEU   B N    1 
ATOM   18005 C CA   . LEU   B  1 387 ? 69.441 -23.829 -46.634 1.00 32.22  ? 413  LEU   B CA   1 
ATOM   18006 C C    . LEU   B  1 387 ? 70.317 -22.634 -46.234 1.00 31.91  ? 413  LEU   B C    1 
ATOM   18007 O O    . LEU   B  1 387 ? 71.466 -22.571 -46.670 1.00 31.94  ? 413  LEU   B O    1 
ATOM   18008 C CB   . LEU   B  1 387 ? 68.715 -23.564 -47.968 1.00 32.17  ? 413  LEU   B CB   1 
ATOM   18009 C CG   . LEU   B  1 387 ? 67.939 -22.249 -48.117 1.00 33.21  ? 413  LEU   B CG   1 
ATOM   18010 C CD1  . LEU   B  1 387 ? 68.815 -21.137 -48.656 1.00 33.58  ? 413  LEU   B CD1  1 
ATOM   18011 C CD2  . LEU   B  1 387 ? 66.787 -22.408 -49.079 1.00 33.89  ? 413  LEU   B CD2  1 
ATOM   18012 H H    . LEU   B  1 387 ? 67.513 -24.113 -45.898 0.00 42.06  ? 413  LEU   B H    1 
ATOM   18013 H HA   . LEU   B  1 387 ? 70.115 -24.668 -46.806 0.00 42.68  ? 413  LEU   B HA   1 
ATOM   18014 H HB2  . LEU   B  1 387 ? 69.451 -23.604 -48.770 0.00 42.03  ? 413  LEU   B HB2  1 
ATOM   18015 H HB3  . LEU   B  1 387 ? 67.997 -24.372 -48.098 0.00 42.06  ? 413  LEU   B HB3  1 
ATOM   18016 H HG   . LEU   B  1 387 ? 67.537 -21.936 -47.154 0.00 42.02  ? 413  LEU   B HG   1 
ATOM   18017 H HD11 . LEU   B  1 387 ? 68.222 -20.228 -48.747 0.00 41.93  ? 413  LEU   B HD11 1 
ATOM   18018 H HD12 . LEU   B  1 387 ? 69.637 -20.973 -47.962 0.00 42.53  ? 413  LEU   B HD12 1 
ATOM   18019 H HD13 . LEU   B  1 387 ? 69.202 -21.426 -49.632 0.00 42.70  ? 413  LEU   B HD13 1 
ATOM   18020 H HD21 . LEU   B  1 387 ? 66.245 -21.465 -49.112 0.00 42.48  ? 413  LEU   B HD21 1 
ATOM   18021 H HD22 . LEU   B  1 387 ? 67.176 -22.652 -50.066 0.00 43.26  ? 413  LEU   B HD22 1 
ATOM   18022 H HD23 . LEU   B  1 387 ? 66.124 -23.197 -48.728 0.00 43.23  ? 413  LEU   B HD23 1 
ATOM   18023 N N    . PHE   B  1 388 ? 69.806 -21.709 -45.397 1.00 31.69  ? 414  PHE   B N    1 
ATOM   18024 C CA   . PHE   B  1 388 ? 70.556 -20.508 -45.023 1.00 31.97  ? 414  PHE   B CA   1 
ATOM   18025 C C    . PHE   B  1 388 ? 71.810 -20.783 -44.187 1.00 33.61  ? 414  PHE   B C    1 
ATOM   18026 O O    . PHE   B  1 388 ? 72.791 -20.054 -44.338 1.00 33.67  ? 414  PHE   B O    1 
ATOM   18027 C CB   . PHE   B  1 388 ? 69.646 -19.492 -44.326 1.00 31.20  ? 414  PHE   B CB   1 
ATOM   18028 C CG   . PHE   B  1 388 ? 68.534 -18.990 -45.221 1.00 30.83  ? 414  PHE   B CG   1 
ATOM   18029 C CD1  . PHE   B  1 388 ? 68.816 -18.246 -46.352 1.00 31.41  ? 414  PHE   B CD1  1 
ATOM   18030 C CD2  . PHE   B  1 388 ? 67.208 -19.251 -44.920 1.00 31.08  ? 414  PHE   B CD2  1 
ATOM   18031 C CE1  . PHE   B  1 388 ? 67.796 -17.804 -47.186 1.00 31.94  ? 414  PHE   B CE1  1 
ATOM   18032 C CE2  . PHE   B  1 388 ? 66.188 -18.775 -45.736 1.00 31.41  ? 414  PHE   B CE2  1 
ATOM   18033 C CZ   . PHE   B  1 388 ? 66.488 -18.053 -46.859 1.00 31.53  ? 414  PHE   B CZ   1 
ATOM   18034 H H    . PHE   B  1 388 ? 68.892 -21.773 -44.958 0.00 40.36  ? 414  PHE   B H    1 
ATOM   18035 H HA   . PHE   B  1 388 ? 70.902 -20.045 -45.946 0.00 40.45  ? 414  PHE   B HA   1 
ATOM   18036 H HB2  . PHE   B  1 388 ? 69.203 -19.957 -43.447 0.00 39.09  ? 414  PHE   B HB2  1 
ATOM   18037 H HB3  . PHE   B  1 388 ? 70.246 -18.633 -44.026 0.00 38.80  ? 414  PHE   B HB3  1 
ATOM   18038 H HD1  . PHE   B  1 388 ? 69.842 -18.045 -46.613 0.00 38.71  ? 414  PHE   B HD1  1 
ATOM   18039 H HD2  . PHE   B  1 388 ? 66.957 -19.811 -44.036 0.00 38.39  ? 414  PHE   B HD2  1 
ATOM   18040 H HE1  . PHE   B  1 388 ? 68.031 -17.225 -48.063 0.00 38.68  ? 414  PHE   B HE1  1 
ATOM   18041 H HE2  . PHE   B  1 388 ? 65.160 -18.986 -45.491 0.00 38.12  ? 414  PHE   B HE2  1 
ATOM   18042 H HZ   . PHE   B  1 388 ? 65.696 -17.699 -47.497 0.00 37.91  ? 414  PHE   B HZ   1 
ATOM   18043 N N    . GLN   B  1 389 ? 71.809 -21.832 -43.346 1.00 34.50  ? 415  GLN   B N    1 
ATOM   18044 C CA   . GLN   B  1 389 ? 73.002 -22.169 -42.566 1.00 36.56  ? 415  GLN   B CA   1 
ATOM   18045 C C    . GLN   B  1 389 ? 74.122 -22.734 -43.462 1.00 38.10  ? 415  GLN   B C    1 
ATOM   18046 O O    . GLN   B  1 389 ? 75.289 -22.677 -43.064 1.00 38.11  ? 415  GLN   B O    1 
ATOM   18047 C CB   . GLN   B  1 389 ? 72.668 -23.118 -41.395 1.00 38.86  ? 415  GLN   B CB   1 
ATOM   18048 C CG   . GLN   B  1 389 ? 72.538 -24.595 -41.758 1.00 43.84  ? 415  GLN   B CG   1 
ATOM   18049 C CD   . GLN   B  1 389 ? 71.811 -25.420 -40.707 1.00 50.80  ? 415  GLN   B CD   1 
ATOM   18050 O OE1  . GLN   B  1 389 ? 71.044 -26.332 -41.040 1.00 53.29  ? 415  GLN   B OE1  1 
ATOM   18051 N NE2  . GLN   B  1 389 ? 72.028 -25.153 -39.415 1.00 51.45  ? 415  GLN   B NE2  1 
ATOM   18052 H H    . GLN   B  1 389 ? 71.021 -22.451 -43.185 0.00 44.60  ? 415  GLN   B H    1 
ATOM   18053 H HA   . GLN   B  1 389 ? 73.388 -21.255 -42.117 0.00 47.25  ? 415  GLN   B HA   1 
ATOM   18054 H HB2  . GLN   B  1 389 ? 73.461 -23.037 -40.653 0.00 50.91  ? 415  GLN   B HB2  1 
ATOM   18055 H HB3  . GLN   B  1 389 ? 71.724 -22.805 -40.952 0.00 50.27  ? 415  GLN   B HB3  1 
ATOM   18056 H HG2  . GLN   B  1 389 ? 71.987 -24.683 -42.693 0.00 57.13  ? 415  GLN   B HG2  1 
ATOM   18057 H HG3  . GLN   B  1 389 ? 73.533 -25.024 -41.872 0.00 57.79  ? 415  GLN   B HG3  1 
ATOM   18058 H HE21 . GLN   B  1 389 ? 72.685 -24.435 -39.127 0.00 66.60  ? 415  GLN   B HE21 1 
ATOM   18059 H HE22 . GLN   B  1 389 ? 71.547 -25.699 -38.707 0.00 66.89  ? 415  GLN   B HE22 1 
ATOM   18060 N N    . ASN   B  1 390 ? 73.792 -23.263 -44.667 1.00 39.29  ? 416  ASN   B N    1 
ATOM   18061 C CA   . ASN   B  1 390 ? 74.830 -23.764 -45.568 1.00 41.08  ? 416  ASN   B CA   1 
ATOM   18062 C C    . ASN   B  1 390 ? 75.516 -22.644 -46.385 1.00 40.39  ? 416  ASN   B C    1 
ATOM   18063 O O    . ASN   B  1 390 ? 76.442 -22.939 -47.139 1.00 40.38  ? 416  ASN   B O    1 
ATOM   18064 C CB   . ASN   B  1 390 ? 74.297 -24.885 -46.485 1.00 45.41  ? 416  ASN   B CB   1 
ATOM   18065 C CG   . ASN   B  1 390 ? 75.319 -25.872 -46.898 1.00 54.47  ? 416  ASN   B CG   1 
ATOM   18066 O OD1  . ASN   B  1 390 ? 76.314 -26.059 -46.173 1.00 56.36  ? 416  ASN   B OD1  1 
ATOM   18067 N ND2  . ASN   B  1 390 ? 75.294 -26.430 -48.097 1.00 59.23  ? 416  ASN   B ND2  1 
ATOM   18068 H H    . ASN   B  1 390 ? 72.851 -23.363 -45.033 0.00 51.25  ? 416  ASN   B H    1 
ATOM   18069 H HA   . ASN   B  1 390 ? 75.607 -24.179 -44.927 0.00 54.65  ? 416  ASN   B HA   1 
ATOM   18070 H HB2  . ASN   B  1 390 ? 73.514 -25.428 -45.957 0.00 59.80  ? 416  ASN   B HB2  1 
ATOM   18071 H HB3  . ASN   B  1 390 ? 73.888 -24.432 -47.387 0.00 59.42  ? 416  ASN   B HB3  1 
ATOM   18072 H HD21 . ASN   B  1 390 ? 75.452 -27.350 -47.735 0.00 78.01  ? 416  ASN   B HD21 1 
ATOM   18073 H HD22 . ASN   B  1 390 ? 74.649 -26.170 -48.835 0.00 77.16  ? 416  ASN   B HD22 1 
ATOM   18074 N N    . PHE   B  1 391 ? 75.085 -21.369 -46.244 1.00 39.28  ? 417  PHE   B N    1 
ATOM   18075 C CA   . PHE   B  1 391 ? 75.785 -20.248 -46.885 1.00 38.56  ? 417  PHE   B CA   1 
ATOM   18076 C C    . PHE   B  1 391 ? 77.039 -19.971 -46.057 1.00 38.78  ? 417  PHE   B C    1 
ATOM   18077 O O    . PHE   B  1 391 ? 77.056 -20.250 -44.855 1.00 39.00  ? 417  PHE   B O    1 
ATOM   18078 C CB   . PHE   B  1 391 ? 74.922 -18.971 -46.919 1.00 37.36  ? 417  PHE   B CB   1 
ATOM   18079 C CG   . PHE   B  1 391 ? 73.997 -18.858 -48.105 1.00 36.95  ? 417  PHE   B CG   1 
ATOM   18080 C CD1  . PHE   B  1 391 ? 72.842 -19.618 -48.176 1.00 37.30  ? 417  PHE   B CD1  1 
ATOM   18081 C CD2  . PHE   B  1 391 ? 74.264 -17.969 -49.131 1.00 36.83  ? 417  PHE   B CD2  1 
ATOM   18082 C CE1  . PHE   B  1 391 ? 71.977 -19.489 -49.248 1.00 37.76  ? 417  PHE   B CE1  1 
ATOM   18083 C CE2  . PHE   B  1 391 ? 73.387 -17.829 -50.190 1.00 37.56  ? 417  PHE   B CE2  1 
ATOM   18084 C CZ   . PHE   B  1 391 ? 72.254 -18.598 -50.249 1.00 37.51  ? 417  PHE   B CZ   1 
ATOM   18085 H H    . PHE   B  1 391 ? 74.262 -21.091 -45.719 0.00 50.64  ? 417  PHE   B H    1 
ATOM   18086 H HA   . PHE   B  1 391 ? 76.086 -20.509 -47.898 0.00 50.07  ? 417  PHE   B HA   1 
ATOM   18087 H HB2  . PHE   B  1 391 ? 74.318 -18.917 -46.015 0.00 47.41  ? 417  PHE   B HB2  1 
ATOM   18088 H HB3  . PHE   B  1 391 ? 75.593 -18.113 -46.948 0.00 47.47  ? 417  PHE   B HB3  1 
ATOM   18089 H HD1  . PHE   B  1 391 ? 72.611 -20.314 -47.386 0.00 47.44  ? 417  PHE   B HD1  1 
ATOM   18090 H HD2  . PHE   B  1 391 ? 75.146 -17.351 -49.093 0.00 46.43  ? 417  PHE   B HD2  1 
ATOM   18091 H HE1  . PHE   B  1 391 ? 71.085 -20.090 -49.298 0.00 47.58  ? 417  PHE   B HE1  1 
ATOM   18092 H HE2  . PHE   B  1 391 ? 73.611 -17.140 -50.988 0.00 46.87  ? 417  PHE   B HE2  1 
ATOM   18093 H HZ   . PHE   B  1 391 ? 71.585 -18.508 -51.089 0.00 46.85  ? 417  PHE   B HZ   1 
ATOM   18094 N N    . SER   B  1 392 ? 78.077 -19.406 -46.683 1.00 38.49  ? 418  SER   B N    1 
ATOM   18095 C CA   . SER   B  1 392 ? 79.327 -19.110 -45.993 1.00 38.99  ? 418  SER   B CA   1 
ATOM   18096 C C    . SER   B  1 392 ? 79.151 -18.190 -44.757 1.00 38.58  ? 418  SER   B C    1 
ATOM   18097 O O    . SER   B  1 392 ? 79.564 -18.574 -43.659 1.00 38.81  ? 418  SER   B O    1 
ATOM   18098 C CB   . SER   B  1 392 ? 80.338 -18.514 -46.970 1.00 41.41  ? 418  SER   B CB   1 
ATOM   18099 O OG   . SER   B  1 392 ? 81.598 -18.344 -46.338 1.00 44.96  ? 418  SER   B OG   1 
ATOM   18100 H H    . SER   B  1 392 ? 78.075 -19.145 -47.664 0.00 50.06  ? 418  SER   B H    1 
ATOM   18101 H HA   . SER   B  1 392 ? 79.744 -20.053 -45.643 0.00 51.68  ? 418  SER   B HA   1 
ATOM   18102 H HB2  . SER   B  1 392 ? 80.459 -19.200 -47.807 0.00 54.51  ? 418  SER   B HB2  1 
ATOM   18103 H HB3  . SER   B  1 392 ? 79.953 -17.562 -47.335 0.00 53.64  ? 418  SER   B HB3  1 
ATOM   18104 H HG   . SER   B  1 392 ? 81.821 -17.386 -46.201 0.00 58.58  ? 418  SER   B HG   1 
ATOM   18105 N N    . ASN   B  1 393 ? 78.553 -16.987 -44.925 1.00 37.39  ? 419  ASN   B N    1 
ATOM   18106 C CA   . ASN   B  1 393 ? 78.349 -16.054 -43.815 1.00 36.47  ? 419  ASN   B CA   1 
ATOM   18107 C C    . ASN   B  1 393 ? 77.219 -15.035 -44.083 1.00 33.56  ? 419  ASN   B C    1 
ATOM   18108 O O    . ASN   B  1 393 ? 77.480 -13.840 -44.243 1.00 33.13  ? 419  ASN   B O    1 
ATOM   18109 C CB   . ASN   B  1 393 ? 79.659 -15.330 -43.481 1.00 39.36  ? 419  ASN   B CB   1 
ATOM   18110 C CG   . ASN   B  1 393 ? 79.564 -14.423 -42.268 1.00 45.29  ? 419  ASN   B CG   1 
ATOM   18111 O OD1  . ASN   B  1 393 ? 78.782 -14.670 -41.336 1.00 47.21  ? 419  ASN   B OD1  1 
ATOM   18112 N ND2  . ASN   B  1 393 ? 80.352 -13.348 -42.252 1.00 46.63  ? 419  ASN   B ND2  1 
ATOM   18113 H H    . ASN   B  1 393 ? 78.211 -16.645 -45.818 0.00 47.84  ? 419  ASN   B H    1 
ATOM   18114 H HA   . ASN   B  1 393 ? 78.051 -16.623 -42.935 0.00 46.81  ? 419  ASN   B HA   1 
ATOM   18115 H HB2  . ASN   B  1 393 ? 80.428 -16.072 -43.269 0.00 50.93  ? 419  ASN   B HB2  1 
ATOM   18116 H HB3  . ASN   B  1 393 ? 79.955 -14.731 -44.341 0.00 50.20  ? 419  ASN   B HB3  1 
ATOM   18117 H HD21 . ASN   B  1 393 ? 80.321 -12.712 -41.463 0.00 58.72  ? 419  ASN   B HD21 1 
ATOM   18118 H HD22 . ASN   B  1 393 ? 80.986 -13.164 -43.023 0.00 58.98  ? 419  ASN   B HD22 1 
ATOM   18119 N N    . LEU   B  1 394 ? 75.961 -15.506 -44.087 1.00 31.60  ? 420  LEU   B N    1 
ATOM   18120 C CA   . LEU   B  1 394 ? 74.829 -14.601 -44.250 1.00 30.26  ? 420  LEU   B CA   1 
ATOM   18121 C C    . LEU   B  1 394 ? 74.653 -13.784 -42.962 1.00 28.20  ? 420  LEU   B C    1 
ATOM   18122 O O    . LEU   B  1 394 ? 74.752 -14.341 -41.871 1.00 27.73  ? 420  LEU   B O    1 
ATOM   18123 C CB   . LEU   B  1 394 ? 73.519 -15.353 -44.565 1.00 31.11  ? 420  LEU   B CB   1 
ATOM   18124 C CG   . LEU   B  1 394 ? 73.282 -15.753 -46.020 1.00 33.42  ? 420  LEU   B CG   1 
ATOM   18125 C CD1  . LEU   B  1 394 ? 72.058 -16.649 -46.121 1.00 34.46  ? 420  LEU   B CD1  1 
ATOM   18126 C CD2  . LEU   B  1 394 ? 73.157 -14.510 -46.938 1.00 33.68  ? 420  LEU   B CD2  1 
ATOM   18127 H H    . LEU   B  1 394 ? 75.719 -16.487 -43.989 0.00 40.07  ? 420  LEU   B H    1 
ATOM   18128 H HA   . LEU   B  1 394 ? 75.043 -13.905 -45.057 0.00 37.32  ? 420  LEU   B HA   1 
ATOM   18129 H HB2  . LEU   B  1 394 ? 73.483 -16.262 -43.967 0.00 38.72  ? 420  LEU   B HB2  1 
ATOM   18130 H HB3  . LEU   B  1 394 ? 72.689 -14.711 -44.276 0.00 37.95  ? 420  LEU   B HB3  1 
ATOM   18131 H HG   . LEU   B  1 394 ? 74.141 -16.328 -46.362 0.00 41.63  ? 420  LEU   B HG   1 
ATOM   18132 H HD11 . LEU   B  1 394 ? 71.428 -16.336 -46.952 0.00 42.12  ? 420  LEU   B HD11 1 
ATOM   18133 H HD12 . LEU   B  1 394 ? 72.385 -17.675 -46.284 0.00 42.89  ? 420  LEU   B HD12 1 
ATOM   18134 H HD13 . LEU   B  1 394 ? 71.500 -16.593 -45.189 0.00 42.29  ? 420  LEU   B HD13 1 
ATOM   18135 H HD21 . LEU   B  1 394 ? 72.690 -14.795 -47.879 0.00 41.01  ? 420  LEU   B HD21 1 
ATOM   18136 H HD22 . LEU   B  1 394 ? 72.557 -13.751 -46.439 0.00 40.62  ? 420  LEU   B HD22 1 
ATOM   18137 H HD23 . LEU   B  1 394 ? 74.150 -14.119 -47.151 0.00 41.15  ? 420  LEU   B HD23 1 
ATOM   18138 N N    . GLU   B  1 395 ? 74.442 -12.464 -43.096 1.00 26.38  ? 421  GLU   B N    1 
ATOM   18139 C CA   . GLU   B  1 395 ? 74.185 -11.547 -41.980 1.00 25.90  ? 421  GLU   B CA   1 
ATOM   18140 C C    . GLU   B  1 395 ? 72.776 -10.933 -42.084 1.00 23.92  ? 421  GLU   B C    1 
ATOM   18141 O O    . GLU   B  1 395 ? 72.235 -10.516 -41.066 1.00 23.43  ? 421  GLU   B O    1 
ATOM   18142 C CB   . GLU   B  1 395 ? 75.239 -10.424 -41.923 1.00 30.37  ? 421  GLU   B CB   1 
ATOM   18143 C CG   . GLU   B  1 395 ? 76.667 -10.919 -41.740 1.00 39.58  ? 421  GLU   B CG   1 
ATOM   18144 C CD   . GLU   B  1 395 ? 77.722 -9.841  -41.917 1.00 52.02  ? 421  GLU   B CD   1 
ATOM   18145 O OE1  . GLU   B  1 395 ? 77.525 -8.723  -41.385 1.00 55.68  ? 421  GLU   B OE1  1 
ATOM   18146 O OE2  . GLU   B  1 395 ? 78.746 -10.112 -42.586 1.00 55.29  ? 421  GLU   B OE2  1 
ATOM   18147 H H    . GLU   B  1 395 ? 74.469 -11.985 -43.990 0.00 31.95  ? 421  GLU   B H    1 
ATOM   18148 H HA   . GLU   B  1 395 ? 74.240 -12.080 -41.033 0.00 31.53  ? 421  GLU   B HA   1 
ATOM   18149 H HB2  . GLU   B  1 395 ? 75.192 -9.856  -42.850 0.00 36.45  ? 421  GLU   B HB2  1 
ATOM   18150 H HB3  . GLU   B  1 395 ? 75.010 -9.766  -41.087 0.00 36.52  ? 421  GLU   B HB3  1 
ATOM   18151 H HG2  . GLU   B  1 395 ? 76.770 -11.321 -40.733 0.00 48.59  ? 421  GLU   B HG2  1 
ATOM   18152 H HG3  . GLU   B  1 395 ? 76.875 -11.697 -42.472 0.00 48.56  ? 421  GLU   B HG3  1 
ATOM   18153 N N    . ILE   B  1 396 ? 72.202 -10.836 -43.306 1.00 22.46  ? 422  ILE   B N    1 
ATOM   18154 C CA   . ILE   B  1 396 ? 70.880 -10.262 -43.538 1.00 21.98  ? 422  ILE   B CA   1 
ATOM   18155 C C    . ILE   B  1 396 ? 70.098 -11.183 -44.459 1.00 21.17  ? 422  ILE   B C    1 
ATOM   18156 O O    . ILE   B  1 396 ? 70.440 -11.299 -45.634 1.00 20.99  ? 422  ILE   B O    1 
ATOM   18157 C CB   . ILE   B  1 396 ? 70.990 -8.833  -44.137 1.00 22.28  ? 422  ILE   B CB   1 
ATOM   18158 C CG1  . ILE   B  1 396 ? 71.617 -7.860  -43.124 1.00 23.45  ? 422  ILE   B CG1  1 
ATOM   18159 C CG2  . ILE   B  1 396 ? 69.598 -8.321  -44.611 1.00 22.44  ? 422  ILE   B CG2  1 
ATOM   18160 C CD1  . ILE   B  1 396 ? 72.024 -6.485  -43.725 1.00 25.19  ? 422  ILE   B CD1  1 
ATOM   18161 H H    . ILE   B  1 396 ? 72.645 -11.130 -44.169 0.00 26.47  ? 422  ILE   B H    1 
ATOM   18162 H HA   . ILE   B  1 396 ? 70.333 -10.178 -42.600 0.00 25.12  ? 422  ILE   B HA   1 
ATOM   18163 H HB   . ILE   B  1 396 ? 71.643 -8.882  -45.006 0.00 25.38  ? 422  ILE   B HB   1 
ATOM   18164 H HG12 . ILE   B  1 396 ? 70.894 -7.669  -42.333 0.00 26.44  ? 422  ILE   B HG12 1 
ATOM   18165 H HG13 . ILE   B  1 396 ? 72.517 -8.303  -42.699 0.00 26.99  ? 422  ILE   B HG13 1 
ATOM   18166 H HG21 . ILE   B  1 396 ? 69.613 -7.240  -44.743 0.00 24.74  ? 422  ILE   B HG21 1 
ATOM   18167 H HG22 . ILE   B  1 396 ? 69.350 -8.780  -45.567 0.00 25.00  ? 422  ILE   B HG22 1 
ATOM   18168 H HG23 . ILE   B  1 396 ? 68.850 -8.591  -43.868 0.00 24.89  ? 422  ILE   B HG23 1 
ATOM   18169 H HD11 . ILE   B  1 396 ? 72.790 -6.040  -43.092 0.00 28.68  ? 422  ILE   B HD11 1 
ATOM   18170 H HD12 . ILE   B  1 396 ? 72.413 -6.636  -44.729 0.00 28.62  ? 422  ILE   B HD12 1 
ATOM   18171 H HD13 . ILE   B  1 396 ? 71.153 -5.831  -43.756 0.00 28.17  ? 422  ILE   B HD13 1 
ATOM   18172 N N    . ILE   B  1 397 ? 69.050 -11.837 -43.932 1.00 20.71  ? 423  ILE   B N    1 
ATOM   18173 C CA   . ILE   B  1 397 ? 68.180 -12.708 -44.715 1.00 20.71  ? 423  ILE   B CA   1 
ATOM   18174 C C    . ILE   B  1 397 ? 66.871 -11.935 -44.782 1.00 19.95  ? 423  ILE   B C    1 
ATOM   18175 O O    . ILE   B  1 397 ? 66.122 -11.914 -43.803 1.00 19.32  ? 423  ILE   B O    1 
ATOM   18176 C CB   . ILE   B  1 397 ? 68.000 -14.107 -44.065 1.00 21.97  ? 423  ILE   B CB   1 
ATOM   18177 C CG1  . ILE   B  1 397 ? 69.366 -14.807 -43.835 1.00 23.55  ? 423  ILE   B CG1  1 
ATOM   18178 C CG2  . ILE   B  1 397 ? 67.065 -14.975 -44.937 1.00 22.73  ? 423  ILE   B CG2  1 
ATOM   18179 C CD1  . ILE   B  1 397 ? 69.304 -15.964 -42.827 1.00 25.38  ? 423  ILE   B CD1  1 
ATOM   18180 H H    . ILE   B  1 397 ? 68.774 -11.782 -42.957 0.00 23.63  ? 423  ILE   B H    1 
ATOM   18181 H HA   . ILE   B  1 397 ? 68.565 -12.846 -45.722 0.00 23.82  ? 423  ILE   B HA   1 
ATOM   18182 H HB   . ILE   B  1 397 ? 67.529 -13.976 -43.093 0.00 25.51  ? 423  ILE   B HB   1 
ATOM   18183 H HG12 . ILE   B  1 397 ? 69.698 -15.211 -44.790 0.00 28.25  ? 423  ILE   B HG12 1 
ATOM   18184 H HG13 . ILE   B  1 397 ? 70.097 -14.092 -43.463 0.00 28.01  ? 423  ILE   B HG13 1 
ATOM   18185 H HG21 . ILE   B  1 397 ? 67.198 -16.029 -44.700 0.00 26.99  ? 423  ILE   B HG21 1 
ATOM   18186 H HG22 . ILE   B  1 397 ? 66.035 -14.693 -44.725 0.00 26.32  ? 423  ILE   B HG22 1 
ATOM   18187 H HG23 . ILE   B  1 397 ? 67.289 -14.801 -45.988 0.00 26.59  ? 423  ILE   B HG23 1 
ATOM   18188 H HD11 . ILE   B  1 397 ? 70.320 -16.225 -42.535 0.00 31.01  ? 423  ILE   B HD11 1 
ATOM   18189 H HD12 . ILE   B  1 397 ? 68.738 -15.649 -41.952 0.00 30.45  ? 423  ILE   B HD12 1 
ATOM   18190 H HD13 . ILE   B  1 397 ? 68.830 -16.829 -43.288 0.00 30.82  ? 423  ILE   B HD13 1 
ATOM   18191 N N    . TYR   B  1 398 ? 66.641 -11.216 -45.887 1.00 18.84  ? 424  TYR   B N    1 
ATOM   18192 C CA   . TYR   B  1 398 ? 65.461 -10.378 -46.014 1.00 19.07  ? 424  TYR   B CA   1 
ATOM   18193 C C    . TYR   B  1 398 ? 64.375 -11.074 -46.836 1.00 18.60  ? 424  TYR   B C    1 
ATOM   18194 O O    . TYR   B  1 398 ? 64.540 -11.284 -48.041 1.00 18.33  ? 424  TYR   B O    1 
ATOM   18195 C CB   . TYR   B  1 398 ? 65.863 -9.007  -46.552 1.00 19.77  ? 424  TYR   B CB   1 
ATOM   18196 C CG   . TYR   B  1 398 ? 64.751 -7.986  -46.570 1.00 21.54  ? 424  TYR   B CG   1 
ATOM   18197 C CD1  . TYR   B  1 398 ? 64.519 -7.161  -45.478 1.00 22.94  ? 424  TYR   B CD1  1 
ATOM   18198 C CD2  . TYR   B  1 398 ? 63.996 -7.777  -47.710 1.00 22.89  ? 424  TYR   B CD2  1 
ATOM   18199 C CE1  . TYR   B  1 398 ? 63.524 -6.189  -45.509 1.00 24.21  ? 424  TYR   B CE1  1 
ATOM   18200 C CE2  . TYR   B  1 398 ? 63.011 -6.802  -47.756 1.00 24.24  ? 424  TYR   B CE2  1 
ATOM   18201 C CZ   . TYR   B  1 398 ? 62.808 -5.978  -46.671 1.00 25.93  ? 424  TYR   B CZ   1 
ATOM   18202 O OH   . TYR   B  1 398 ? 61.798 -5.039  -46.696 1.00 29.60  ? 424  TYR   B OH   1 
ATOM   18203 H H    . TYR   B  1 398 ? 67.251 -11.190 -46.696 0.00 20.84  ? 424  TYR   B H    1 
ATOM   18204 H HA   . TYR   B  1 398 ? 65.056 -10.190 -45.024 0.00 20.46  ? 424  TYR   B HA   1 
ATOM   18205 H HB2  . TYR   B  1 398 ? 66.650 -8.611  -45.911 0.00 21.20  ? 424  TYR   B HB2  1 
ATOM   18206 H HB3  . TYR   B  1 398 ? 66.246 -9.098  -47.564 0.00 21.26  ? 424  TYR   B HB3  1 
ATOM   18207 H HD1  . TYR   B  1 398 ? 65.106 -7.290  -44.584 0.00 24.46  ? 424  TYR   B HD1  1 
ATOM   18208 H HD2  . TYR   B  1 398 ? 64.180 -8.382  -48.581 0.00 24.56  ? 424  TYR   B HD2  1 
ATOM   18209 H HE1  . TYR   B  1 398 ? 63.355 -5.562  -44.649 0.00 25.39  ? 424  TYR   B HE1  1 
ATOM   18210 H HE2  . TYR   B  1 398 ? 62.436 -6.671  -48.656 0.00 25.60  ? 424  TYR   B HE2  1 
ATOM   18211 H HH   . TYR   B  1 398 ? 61.480 -4.885  -47.623 0.00 31.57  ? 424  TYR   B HH   1 
ATOM   18212 N N    . LEU   B  1 399 ? 63.283 -11.484 -46.158 1.00 18.28  ? 425  LEU   B N    1 
ATOM   18213 C CA   . LEU   B  1 399 ? 62.159 -12.202 -46.784 1.00 18.78  ? 425  LEU   B CA   1 
ATOM   18214 C C    . LEU   B  1 399 ? 60.822 -11.463 -46.565 1.00 18.88  ? 425  LEU   B C    1 
ATOM   18215 O O    . LEU   B  1 399 ? 59.763 -12.089 -46.644 1.00 19.74  ? 425  LEU   B O    1 
ATOM   18216 C CB   . LEU   B  1 399 ? 62.075 -13.617 -46.179 1.00 19.05  ? 425  LEU   B CB   1 
ATOM   18217 C CG   . LEU   B  1 399 ? 63.362 -14.447 -46.228 1.00 22.82  ? 425  LEU   B CG   1 
ATOM   18218 C CD1  . LEU   B  1 399 ? 63.236 -15.706 -45.384 1.00 23.63  ? 425  LEU   B CD1  1 
ATOM   18219 C CD2  . LEU   B  1 399 ? 63.750 -14.748 -47.661 1.00 24.81  ? 425  LEU   B CD2  1 
ATOM   18220 H H    . LEU   B  1 399 ? 63.141 -11.334 -45.165 0.00 19.51  ? 425  LEU   B H    1 
ATOM   18221 H HA   . LEU   B  1 399 ? 62.307 -12.299 -47.858 0.00 20.35  ? 425  LEU   B HA   1 
ATOM   18222 H HB2  . LEU   B  1 399 ? 61.808 -13.509 -45.129 0.00 20.87  ? 425  LEU   B HB2  1 
ATOM   18223 H HB3  . LEU   B  1 399 ? 61.304 -14.185 -46.696 0.00 21.07  ? 425  LEU   B HB3  1 
ATOM   18224 H HG   . LEU   B  1 399 ? 64.169 -13.858 -45.796 0.00 25.85  ? 425  LEU   B HG   1 
ATOM   18225 H HD11 . LEU   B  1 399 ? 63.987 -16.437 -45.680 0.00 27.64  ? 425  LEU   B HD11 1 
ATOM   18226 H HD12 . LEU   B  1 399 ? 63.387 -15.433 -44.341 0.00 27.18  ? 425  LEU   B HD12 1 
ATOM   18227 H HD13 . LEU   B  1 399 ? 62.233 -16.112 -45.507 0.00 27.30  ? 425  LEU   B HD13 1 
ATOM   18228 H HD21 . LEU   B  1 399 ? 64.490 -15.547 -47.686 0.00 28.90  ? 425  LEU   B HD21 1 
ATOM   18229 H HD22 . LEU   B  1 399 ? 62.867 -15.033 -48.232 0.00 28.51  ? 425  LEU   B HD22 1 
ATOM   18230 H HD23 . LEU   B  1 399 ? 64.191 -13.840 -48.069 0.00 28.32  ? 425  LEU   B HD23 1 
ATOM   18231 N N    . SER   B  1 400 ? 60.869 -10.148 -46.304 1.00 17.52  ? 426  SER   B N    1 
ATOM   18232 C CA   . SER   B  1 400 ? 59.671 -9.366  -46.040 1.00 17.37  ? 426  SER   B CA   1 
ATOM   18233 C C    . SER   B  1 400 ? 58.738 -9.375  -47.242 1.00 17.56  ? 426  SER   B C    1 
ATOM   18234 O O    . SER   B  1 400 ? 59.191 -9.393  -48.376 1.00 16.79  ? 426  SER   B O    1 
ATOM   18235 C CB   . SER   B  1 400 ? 60.036 -7.916  -45.705 1.00 17.74  ? 426  SER   B CB   1 
ATOM   18236 O OG   . SER   B  1 400 ? 58.887 -7.107  -45.464 1.00 19.49  ? 426  SER   B OG   1 
ATOM   18237 H H    . SER   B  1 400 ? 61.718 -9.592  -46.289 0.00 18.00  ? 426  SER   B H    1 
ATOM   18238 H HA   . SER   B  1 400 ? 59.151 -9.796  -45.185 0.00 17.60  ? 426  SER   B HA   1 
ATOM   18239 H HB2  . SER   B  1 400 ? 60.659 -7.912  -44.812 0.00 17.75  ? 426  SER   B HB2  1 
ATOM   18240 H HB3  . SER   B  1 400 ? 60.590 -7.494  -46.542 0.00 17.69  ? 426  SER   B HB3  1 
ATOM   18241 H HG   . SER   B  1 400 ? 58.161 -7.642  -45.048 0.00 19.59  ? 426  SER   B HG   1 
ATOM   18242 N N    . GLU   B  1 401 ? 57.432 -9.364  -46.979 1.00 17.84  ? 427  GLU   B N    1 
ATOM   18243 C CA   . GLU   B  1 401 ? 56.415 -9.242  -48.018 1.00 17.55  ? 427  GLU   B CA   1 
ATOM   18244 C C    . GLU   B  1 401 ? 56.382 -10.419 -48.973 1.00 18.14  ? 427  GLU   B C    1 
ATOM   18245 O O    . GLU   B  1 401 ? 56.646 -10.287 -50.169 1.00 19.09  ? 427  GLU   B O    1 
ATOM   18246 C CB   . GLU   B  1 401 ? 56.590 -7.907  -48.765 1.00 18.31  ? 427  GLU   B CB   1 
ATOM   18247 C CG   . GLU   B  1 401 ? 55.361 -7.469  -49.540 1.00 19.74  ? 427  GLU   B CG   1 
ATOM   18248 C CD   . GLU   B  1 401 ? 54.174 -7.206  -48.638 1.00 23.97  ? 427  GLU   B CD   1 
ATOM   18249 O OE1  . GLU   B  1 401 ? 53.281 -8.081  -48.545 1.00 25.06  ? 427  GLU   B OE1  1 
ATOM   18250 O OE2  . GLU   B  1 401 ? 54.146 -6.119  -48.020 1.00 24.69  ? 427  GLU   B OE2  1 
ATOM   18251 H H    . GLU   B  1 401 ? 57.041 -9.456  -46.048 0.00 17.97  ? 427  GLU   B H    1 
ATOM   18252 H HA   . GLU   B  1 401 ? 55.455 -9.237  -47.506 0.00 17.58  ? 427  GLU   B HA   1 
ATOM   18253 H HB2  . GLU   B  1 401 ? 56.801 -7.132  -48.029 0.00 18.11  ? 427  GLU   B HB2  1 
ATOM   18254 H HB3  . GLU   B  1 401 ? 57.427 -7.975  -49.458 0.00 18.41  ? 427  GLU   B HB3  1 
ATOM   18255 H HG2  . GLU   B  1 401 ? 55.592 -6.537  -50.052 0.00 19.84  ? 427  GLU   B HG2  1 
ATOM   18256 H HG3  . GLU   B  1 401 ? 55.082 -8.236  -50.261 0.00 20.20  ? 427  GLU   B HG3  1 
ATOM   18257 N N    . ASN   B  1 402 ? 56.048 -11.568 -48.444 1.00 17.22  ? 428  ASN   B N    1 
ATOM   18258 C CA   . ASN   B  1 402 ? 55.892 -12.793 -49.223 1.00 18.06  ? 428  ASN   B CA   1 
ATOM   18259 C C    . ASN   B  1 402 ? 54.561 -13.449 -48.731 1.00 20.06  ? 428  ASN   B C    1 
ATOM   18260 O O    . ASN   B  1 402 ? 53.713 -12.729 -48.196 1.00 20.89  ? 428  ASN   B O    1 
ATOM   18261 C CB   . ASN   B  1 402 ? 57.195 -13.662 -49.073 1.00 17.35  ? 428  ASN   B CB   1 
ATOM   18262 C CG   . ASN   B  1 402 ? 58.257 -13.232 -50.058 1.00 18.11  ? 428  ASN   B CG   1 
ATOM   18263 O OD1  . ASN   B  1 402 ? 58.060 -13.344 -51.276 1.00 17.42  ? 428  ASN   B OD1  1 
ATOM   18264 N ND2  . ASN   B  1 402 ? 59.368 -12.703 -49.561 1.00 17.59  ? 428  ASN   B ND2  1 
ATOM   18265 H H    . ASN   B  1 402 ? 55.880 -11.701 -47.452 0.00 17.81  ? 428  ASN   B H    1 
ATOM   18266 H HA   . ASN   B  1 402 ? 55.731 -12.557 -50.273 0.00 19.28  ? 428  ASN   B HA   1 
ATOM   18267 H HB2  . ASN   B  1 402 ? 57.574 -13.546 -48.059 0.00 18.61  ? 428  ASN   B HB2  1 
ATOM   18268 H HB3  . ASN   B  1 402 ? 57.002 -14.715 -49.270 0.00 19.04  ? 428  ASN   B HB3  1 
ATOM   18269 H HD21 . ASN   B  1 402 ? 60.102 -12.402 -50.195 0.00 18.88  ? 428  ASN   B HD21 1 
ATOM   18270 H HD22 . ASN   B  1 402 ? 59.494 -12.591 -48.561 0.00 18.76  ? 428  ASN   B HD22 1 
ATOM   18271 N N    A ARG   B  1 403 ? 54.358 -14.748 -48.952 0.50 20.42  ? 429  ARG   B N    1 
ATOM   18272 N N    B ARG   B  1 403 ? 54.355 -14.757 -48.958 0.50 20.75  ? 429  ARG   B N    1 
ATOM   18273 C CA   A ARG   B  1 403 ? 53.167 -15.460 -48.496 0.50 21.44  ? 429  ARG   B CA   1 
ATOM   18274 C CA   B ARG   B  1 403 ? 53.173 -15.505 -48.511 0.50 22.10  ? 429  ARG   B CA   1 
ATOM   18275 C C    A ARG   B  1 403 ? 53.588 -16.664 -47.642 0.50 22.45  ? 429  ARG   B C    1 
ATOM   18276 C C    B ARG   B  1 403 ? 53.594 -16.684 -47.627 0.50 22.73  ? 429  ARG   B C    1 
ATOM   18277 O O    A ARG   B  1 403 ? 52.986 -17.731 -47.737 0.50 22.87  ? 429  ARG   B O    1 
ATOM   18278 O O    B ARG   B  1 403 ? 52.982 -17.750 -47.672 0.50 23.10  ? 429  ARG   B O    1 
ATOM   18279 C CB   A ARG   B  1 403 ? 52.325 -15.898 -49.711 0.50 22.33  ? 429  ARG   B CB   1 
ATOM   18280 C CB   B ARG   B  1 403 ? 52.390 -16.012 -49.749 0.50 23.94  ? 429  ARG   B CB   1 
ATOM   18281 C CG   A ARG   B  1 403 ? 51.966 -14.754 -50.663 0.50 24.00  ? 429  ARG   B CG   1 
ATOM   18282 C CG   B ARG   B  1 403 ? 51.244 -15.099 -50.162 0.50 27.81  ? 429  ARG   B CG   1 
ATOM   18283 C CD   A ARG   B  1 403 ? 50.997 -13.711 -50.123 0.50 27.23  ? 429  ARG   B CD   1 
ATOM   18284 C CD   B ARG   B  1 403 ? 51.176 -14.892 -51.644 0.50 31.57  ? 429  ARG   B CD   1 
ATOM   18285 N NE   A ARG   B  1 403 ? 49.586 -14.114 -50.217 0.50 29.45  ? 429  ARG   B NE   1 
ATOM   18286 N NE   B ARG   B  1 403 ? 50.734 -16.083 -52.381 0.50 33.94  ? 429  ARG   B NE   1 
ATOM   18287 C CZ   A ARG   B  1 403 ? 48.843 -14.638 -49.240 0.50 30.54  ? 429  ARG   B CZ   1 
ATOM   18288 C CZ   B ARG   B  1 403 ? 49.759 -16.147 -53.295 0.50 35.82  ? 429  ARG   B CZ   1 
ATOM   18289 N NH1  A ARG   B  1 403 ? 47.571 -14.950 -49.461 0.50 30.43  ? 429  ARG   B NH1  1 
ATOM   18290 N NH1  B ARG   B  1 403 ? 49.477 -17.299 -53.890 0.50 35.04  ? 429  ARG   B NH1  1 
ATOM   18291 N NH2  A ARG   B  1 403 ? 49.368 -14.867 -48.036 0.50 29.23  ? 429  ARG   B NH2  1 
ATOM   18292 N NH2  B ARG   B  1 403 ? 49.049 -15.066 -53.610 0.50 35.98  ? 429  ARG   B NH2  1 
ATOM   18293 H H    A ARG   B  1 403 ? 54.986 -15.347 -49.478 0.00 22.89  ? 429  ARG   B H    1 
ATOM   18294 H H    B ARG   B  1 403 ? 54.994 -15.344 -49.484 0.00 23.29  ? 429  ARG   B H    1 
ATOM   18295 H HA   A ARG   B  1 403 ? 52.551 -14.829 -47.858 0.00 23.80  ? 429  ARG   B HA   1 
ATOM   18296 H HA   B ARG   B  1 403 ? 52.543 -14.878 -47.882 0.00 24.60  ? 429  ARG   B HA   1 
ATOM   18297 H HB2  A ARG   B  1 403 ? 52.886 -16.640 -50.278 0.00 25.71  ? 429  ARG   B HB2  1 
ATOM   18298 H HB2  B ARG   B  1 403 ? 53.083 -16.109 -50.583 0.00 27.50  ? 429  ARG   B HB2  1 
ATOM   18299 H HB3  A ARG   B  1 403 ? 51.392 -16.332 -49.356 0.00 25.54  ? 429  ARG   B HB3  1 
ATOM   18300 H HB3  B ARG   B  1 403 ? 51.939 -16.983 -49.551 0.00 27.70  ? 429  ARG   B HB3  1 
ATOM   18301 H HG2  A ARG   B  1 403 ? 52.874 -14.215 -50.925 0.00 27.00  ? 429  ARG   B HG2  1 
ATOM   18302 H HG2  B ARG   B  1 403 ? 50.303 -15.543 -49.842 0.00 31.96  ? 429  ARG   B HG2  1 
ATOM   18303 H HG3  A ARG   B  1 403 ? 51.522 -15.178 -51.563 0.00 27.44  ? 429  ARG   B HG3  1 
ATOM   18304 H HG3  B ARG   B  1 403 ? 51.371 -14.121 -49.700 0.00 31.43  ? 429  ARG   B HG3  1 
ATOM   18305 H HD2  A ARG   B  1 403 ? 51.264 -13.401 -49.115 0.00 30.46  ? 429  ARG   B HD2  1 
ATOM   18306 H HD2  B ARG   B  1 403 ? 50.541 -14.022 -51.792 0.00 36.22  ? 429  ARG   B HD2  1 
ATOM   18307 H HD3  A ARG   B  1 403 ? 51.092 -12.838 -50.767 0.00 30.50  ? 429  ARG   B HD3  1 
ATOM   18308 H HD3  B ARG   B  1 403 ? 52.192 -14.684 -51.973 0.00 36.37  ? 429  ARG   B HD3  1 
ATOM   18309 H HE   A ARG   B  1 403 ? 49.132 -13.952 -51.111 0.00 33.65  ? 429  ARG   B HE   1 
ATOM   18310 H HE   B ARG   B  1 403 ? 51.242 -16.940 -52.190 0.00 40.06  ? 429  ARG   B HE   1 
ATOM   18311 H HH11 A ARG   B  1 403 ? 47.152 -14.779 -50.369 0.00 35.15  ? 429  ARG   B HH11 1 
ATOM   18312 H HH11 B ARG   B  1 403 ? 50.006 -18.134 -53.660 0.00 42.13  ? 429  ARG   B HH11 1 
ATOM   18313 H HH12 A ARG   B  1 403 ? 47.005 -15.355 -48.722 0.00 35.14  ? 429  ARG   B HH12 1 
ATOM   18314 H HH12 B ARG   B  1 403 ? 48.732 -17.354 -54.577 0.00 42.12  ? 429  ARG   B HH12 1 
ATOM   18315 H HH21 A ARG   B  1 403 ? 50.336 -14.675 -47.802 0.00 33.17  ? 429  ARG   B HH21 1 
ATOM   18316 H HH21 B ARG   B  1 403 ? 49.190 -14.143 -53.217 0.00 41.88  ? 429  ARG   B HH21 1 
ATOM   18317 H HH22 A ARG   B  1 403 ? 48.781 -15.282 -47.319 0.00 33.40  ? 429  ARG   B HH22 1 
ATOM   18318 H HH22 B ARG   B  1 403 ? 48.314 -15.167 -54.302 0.00 42.48  ? 429  ARG   B HH22 1 
ATOM   18319 N N    . ILE   B  1 404 ? 54.626 -16.486 -46.805 1.00 22.90  ? 430  ILE   B N    1 
ATOM   18320 C CA   . ILE   B  1 404 ? 55.154 -17.540 -45.967 1.00 24.30  ? 430  ILE   B CA   1 
ATOM   18321 C C    . ILE   B  1 404 ? 54.156 -17.783 -44.860 1.00 24.75  ? 430  ILE   B C    1 
ATOM   18322 O O    . ILE   B  1 404 ? 53.722 -16.839 -44.218 1.00 23.96  ? 430  ILE   B O    1 
ATOM   18323 C CB   . ILE   B  1 404 ? 56.563 -17.156 -45.447 1.00 25.51  ? 430  ILE   B CB   1 
ATOM   18324 C CG1  . ILE   B  1 404 ? 57.534 -16.950 -46.648 1.00 27.01  ? 430  ILE   B CG1  1 
ATOM   18325 C CG2  . ILE   B  1 404 ? 57.080 -18.249 -44.518 1.00 25.95  ? 430  ILE   B CG2  1 
ATOM   18326 C CD1  . ILE   B  1 404 ? 58.834 -16.144 -46.319 1.00 28.83  ? 430  ILE   B CD1  1 
ATOM   18327 H H    . ILE   B  1 404 ? 55.099 -15.598 -46.670 0.00 25.72  ? 430  ILE   B H    1 
ATOM   18328 H HA   . ILE   B  1 404 ? 55.265 -18.449 -46.557 0.00 28.41  ? 430  ILE   B HA   1 
ATOM   18329 H HB   . ILE   B  1 404 ? 56.494 -16.226 -44.884 0.00 29.03  ? 430  ILE   B HB   1 
ATOM   18330 H HG12 . ILE   B  1 404 ? 57.842 -17.930 -47.011 0.00 31.63  ? 430  ILE   B HG12 1 
ATOM   18331 H HG13 . ILE   B  1 404 ? 57.028 -16.413 -47.448 0.00 31.08  ? 430  ILE   B HG13 1 
ATOM   18332 H HG21 . ILE   B  1 404 ? 58.160 -18.162 -44.415 0.00 30.34  ? 430  ILE   B HG21 1 
ATOM   18333 H HG22 . ILE   B  1 404 ? 56.619 -18.136 -43.538 0.00 30.18  ? 430  ILE   B HG22 1 
ATOM   18334 H HG23 . ILE   B  1 404 ? 56.825 -19.221 -44.937 0.00 30.66  ? 430  ILE   B HG23 1 
ATOM   18335 H HD11 . ILE   B  1 404 ? 59.361 -15.935 -47.249 0.00 33.23  ? 430  ILE   B HD11 1 
ATOM   18336 H HD12 . ILE   B  1 404 ? 58.557 -15.211 -45.831 0.00 32.84  ? 430  ILE   B HD12 1 
ATOM   18337 H HD13 . ILE   B  1 404 ? 59.474 -16.732 -45.663 0.00 33.42  ? 430  ILE   B HD13 1 
ATOM   18338 N N    . SER   B  1 405 ? 53.735 -19.018 -44.697 1.00 25.63  ? 431  SER   B N    1 
ATOM   18339 C CA   . SER   B  1 405 ? 52.732 -19.373 -43.696 1.00 27.63  ? 431  SER   B CA   1 
ATOM   18340 C C    . SER   B  1 405 ? 53.363 -20.361 -42.669 1.00 29.54  ? 431  SER   B C    1 
ATOM   18341 O O    . SER   B  1 405 ? 54.553 -20.680 -42.790 1.00 29.76  ? 431  SER   B O    1 
ATOM   18342 C CB   . SER   B  1 405 ? 51.514 -19.947 -44.421 1.00 28.93  ? 431  SER   B CB   1 
ATOM   18343 O OG   . SER   B  1 405 ? 51.830 -21.222 -44.947 1.00 31.89  ? 431  SER   B OG   1 
ATOM   18344 H H    . SER   B  1 405 ? 54.061 -19.815 -45.234 0.00 30.42  ? 431  SER   B H    1 
ATOM   18345 H HA   . SER   B  1 405 ? 52.399 -18.497 -43.142 0.00 32.20  ? 431  SER   B HA   1 
ATOM   18346 H HB2  . SER   B  1 405 ? 50.669 -20.020 -43.739 0.00 34.38  ? 431  SER   B HB2  1 
ATOM   18347 H HB3  . SER   B  1 405 ? 51.258 -19.285 -45.247 0.00 34.17  ? 431  SER   B HB3  1 
ATOM   18348 H HG   . SER   B  1 405 ? 52.389 -21.128 -45.761 0.00 38.49  ? 431  SER   B HG   1 
ATOM   18349 N N    . PRO   B  1 406 ? 52.640 -20.801 -41.615 1.00 30.81  ? 432  PRO   B N    1 
ATOM   18350 C CA   . PRO   B  1 406 ? 53.254 -21.722 -40.641 1.00 32.43  ? 432  PRO   B CA   1 
ATOM   18351 C C    . PRO   B  1 406 ? 53.877 -22.969 -41.277 1.00 34.84  ? 432  PRO   B C    1 
ATOM   18352 O O    . PRO   B  1 406 ? 53.314 -23.554 -42.204 1.00 34.81  ? 432  PRO   B O    1 
ATOM   18353 C CB   . PRO   B  1 406 ? 52.101 -22.055 -39.698 1.00 32.66  ? 432  PRO   B CB   1 
ATOM   18354 C CG   . PRO   B  1 406 ? 51.198 -20.842 -39.790 1.00 32.44  ? 432  PRO   B CG   1 
ATOM   18355 C CD   . PRO   B  1 406 ? 51.238 -20.516 -41.261 1.00 30.01  ? 432  PRO   B CD   1 
ATOM   18356 H HA   . PRO   B  1 406 ? 54.016 -21.186 -40.077 0.00 38.99  ? 432  PRO   B HA   1 
ATOM   18357 H HB2  . PRO   B  1 406 ? 51.586 -22.951 -40.043 0.00 39.94  ? 432  PRO   B HB2  1 
ATOM   18358 H HB3  . PRO   B  1 406 ? 52.476 -22.186 -38.684 0.00 39.63  ? 432  PRO   B HB3  1 
ATOM   18359 H HG2  . PRO   B  1 406 ? 50.190 -21.089 -39.461 0.00 38.91  ? 432  PRO   B HG2  1 
ATOM   18360 H HG3  . PRO   B  1 406 ? 51.623 -20.027 -39.208 0.00 38.48  ? 432  PRO   B HG3  1 
ATOM   18361 H HD2  . PRO   B  1 406 ? 50.564 -21.191 -41.787 0.00 36.07  ? 432  PRO   B HD2  1 
ATOM   18362 H HD3  . PRO   B  1 406 ? 50.990 -19.470 -41.433 0.00 35.37  ? 432  PRO   B HD3  1 
ATOM   18363 N N    . LEU   B  1 407 ? 55.089 -23.315 -40.828 1.00 36.44  ? 433  LEU   B N    1 
ATOM   18364 C CA   . LEU   B  1 407 ? 55.833 -24.455 -41.361 1.00 38.61  ? 433  LEU   B CA   1 
ATOM   18365 C C    . LEU   B  1 407 ? 55.091 -25.767 -41.087 1.00 39.98  ? 433  LEU   B C    1 
ATOM   18366 O O    . LEU   B  1 407 ? 54.457 -25.915 -40.038 1.00 40.84  ? 433  LEU   B O    1 
ATOM   18367 C CB   . LEU   B  1 407 ? 57.240 -24.487 -40.734 1.00 39.40  ? 433  LEU   B CB   1 
ATOM   18368 C CG   . LEU   B  1 407 ? 58.283 -25.373 -41.422 1.00 42.01  ? 433  LEU   B CG   1 
ATOM   18369 C CD1  . LEU   B  1 407 ? 59.674 -24.930 -41.046 1.00 42.87  ? 433  LEU   B CD1  1 
ATOM   18370 C CD2  . LEU   B  1 407 ? 58.100 -26.840 -41.061 1.00 42.90  ? 433  LEU   B CD2  1 
ATOM   18371 H H    . LEU   B  1 407 ? 55.575 -22.817 -40.089 0.00 44.59  ? 433  LEU   B H    1 
ATOM   18372 H HA   . LEU   B  1 407 ? 55.941 -24.343 -42.439 0.00 47.91  ? 433  LEU   B HA   1 
ATOM   18373 H HB2  . LEU   B  1 407 ? 57.641 -23.474 -40.740 0.00 48.57  ? 433  LEU   B HB2  1 
ATOM   18374 H HB3  . LEU   B  1 407 ? 57.148 -24.831 -39.705 0.00 49.17  ? 433  LEU   B HB3  1 
ATOM   18375 H HG   . LEU   B  1 407 ? 58.184 -25.278 -42.503 0.00 52.62  ? 433  LEU   B HG   1 
ATOM   18376 H HD11 . LEU   B  1 407 ? 60.399 -25.616 -41.483 0.00 54.04  ? 433  LEU   B HD11 1 
ATOM   18377 H HD12 . LEU   B  1 407 ? 59.844 -23.924 -41.427 0.00 53.17  ? 433  LEU   B HD12 1 
ATOM   18378 H HD13 . LEU   B  1 407 ? 59.766 -24.934 -39.960 0.00 53.64  ? 433  LEU   B HD13 1 
ATOM   18379 H HD21 . LEU   B  1 407 ? 58.873 -27.427 -41.553 0.00 54.81  ? 433  LEU   B HD21 1 
ATOM   18380 H HD22 . LEU   B  1 407 ? 58.180 -26.954 -39.981 0.00 54.51  ? 433  LEU   B HD22 1 
ATOM   18381 H HD23 . LEU   B  1 407 ? 57.119 -27.173 -41.397 0.00 54.51  ? 433  LEU   B HD23 1 
ATOM   18382 N N    . PHE   B  1 433 ? 56.336 17.862  -57.078 1.00 39.92  ? 459  PHE   B N    1 
ATOM   18383 C CA   . PHE   B  1 433 ? 56.783 16.625  -57.729 1.00 39.99  ? 459  PHE   B CA   1 
ATOM   18384 C C    . PHE   B  1 433 ? 56.706 15.394  -56.792 1.00 39.01  ? 459  PHE   B C    1 
ATOM   18385 O O    . PHE   B  1 433 ? 56.878 15.531  -55.586 1.00 39.96  ? 459  PHE   B O    1 
ATOM   18386 C CB   . PHE   B  1 433 ? 58.190 16.785  -58.335 1.00 40.33  ? 459  PHE   B CB   1 
ATOM   18387 C CG   . PHE   B  1 433 ? 59.202 17.560  -57.525 1.00 41.31  ? 459  PHE   B CG   1 
ATOM   18388 C CD1  . PHE   B  1 433 ? 59.997 16.922  -56.591 1.00 42.50  ? 459  PHE   B CD1  1 
ATOM   18389 C CD2  . PHE   B  1 433 ? 59.437 18.905  -57.782 1.00 42.37  ? 459  PHE   B CD2  1 
ATOM   18390 C CE1  . PHE   B  1 433 ? 60.971 17.628  -55.885 1.00 43.56  ? 459  PHE   B CE1  1 
ATOM   18391 C CE2  . PHE   B  1 433 ? 60.426 19.603  -57.096 1.00 43.43  ? 459  PHE   B CE2  1 
ATOM   18392 C CZ   . PHE   B  1 433 ? 61.193 18.962  -56.156 1.00 43.27  ? 459  PHE   B CZ   1 
ATOM   18393 H HA   . PHE   B  1 433 ? 56.120 16.443  -58.572 0.00 44.94  ? 459  PHE   B HA   1 
ATOM   18394 H HB2  . PHE   B  1 433 ? 58.604 15.790  -58.496 0.00 45.19  ? 459  PHE   B HB2  1 
ATOM   18395 H HB3  . PHE   B  1 433 ? 58.090 17.291  -59.294 0.00 45.56  ? 459  PHE   B HB3  1 
ATOM   18396 H HD1  . PHE   B  1 433 ? 59.841 15.871  -56.389 0.00 47.55  ? 459  PHE   B HD1  1 
ATOM   18397 H HD2  . PHE   B  1 433 ? 58.858 19.413  -58.535 0.00 48.31  ? 459  PHE   B HD2  1 
ATOM   18398 H HE1  . PHE   B  1 433 ? 61.568 17.118  -55.144 0.00 48.97  ? 459  PHE   B HE1  1 
ATOM   18399 H HE2  . PHE   B  1 433 ? 60.580 20.654  -57.295 0.00 49.72  ? 459  PHE   B HE2  1 
ATOM   18400 H HZ   . PHE   B  1 433 ? 61.932 19.515  -55.600 0.00 49.15  ? 459  PHE   B HZ   1 
ATOM   18401 N N    . GLU   B  1 434 ? 56.468 14.196  -57.362 1.00 36.85  ? 460  GLU   B N    1 
ATOM   18402 C CA   . GLU   B  1 434 ? 56.317 12.932  -56.621 1.00 34.76  ? 460  GLU   B CA   1 
ATOM   18403 C C    . GLU   B  1 434 ? 57.632 12.223  -56.260 1.00 32.17  ? 460  GLU   B C    1 
ATOM   18404 O O    . GLU   B  1 434 ? 57.680 11.518  -55.248 1.00 31.35  ? 460  GLU   B O    1 
ATOM   18405 C CB   . GLU   B  1 434 ? 55.460 11.965  -57.467 1.00 35.76  ? 460  GLU   B CB   1 
ATOM   18406 C CG   . GLU   B  1 434 ? 55.266 10.567  -56.893 1.00 38.14  ? 460  GLU   B CG   1 
ATOM   18407 C CD   . GLU   B  1 434 ? 54.556 9.586   -57.809 1.00 42.51  ? 460  GLU   B CD   1 
ATOM   18408 O OE1  . GLU   B  1 434 ? 54.478 8.385   -57.450 1.00 43.98  ? 460  GLU   B OE1  1 
ATOM   18409 O OE2  . GLU   B  1 434 ? 54.083 10.012  -58.887 1.00 43.10  ? 460  GLU   B OE2  1 
ATOM   18410 H H    . GLU   B  1 434 ? 56.377 14.078  -58.366 0.00 40.79  ? 460  GLU   B H    1 
ATOM   18411 H HA   . GLU   B  1 434 ? 55.777 13.123  -55.695 0.00 37.79  ? 460  GLU   B HA   1 
ATOM   18412 H HB2  . GLU   B  1 434 ? 54.473 12.406  -57.601 0.00 39.24  ? 460  GLU   B HB2  1 
ATOM   18413 H HB3  . GLU   B  1 434 ? 55.939 11.844  -58.438 0.00 39.25  ? 460  GLU   B HB3  1 
ATOM   18414 H HG2  . GLU   B  1 434 ? 56.232 10.115  -56.676 0.00 41.69  ? 460  GLU   B HG2  1 
ATOM   18415 H HG3  . GLU   B  1 434 ? 54.691 10.645  -55.972 0.00 41.68  ? 460  GLU   B HG3  1 
ATOM   18416 N N    . PHE   B  1 435 ? 58.638 12.282  -57.147 1.00 29.75  ? 461  PHE   B N    1 
ATOM   18417 C CA   . PHE   B  1 435 ? 59.895 11.563  -56.969 1.00 27.89  ? 461  PHE   B CA   1 
ATOM   18418 C C    . PHE   B  1 435 ? 61.014 12.499  -56.543 1.00 26.85  ? 461  PHE   B C    1 
ATOM   18419 O O    . PHE   B  1 435 ? 61.224 13.535  -57.162 1.00 26.89  ? 461  PHE   B O    1 
ATOM   18420 C CB   . PHE   B  1 435 ? 60.260 10.844  -58.284 1.00 27.00  ? 461  PHE   B CB   1 
ATOM   18421 C CG   . PHE   B  1 435 ? 59.212 9.835   -58.701 1.00 26.98  ? 461  PHE   B CG   1 
ATOM   18422 C CD1  . PHE   B  1 435 ? 59.180 8.571   -58.138 1.00 27.70  ? 461  PHE   B CD1  1 
ATOM   18423 C CD2  . PHE   B  1 435 ? 58.229 10.169  -59.617 1.00 27.53  ? 461  PHE   B CD2  1 
ATOM   18424 C CE1  . PHE   B  1 435 ? 58.197 7.653   -58.500 1.00 28.05  ? 461  PHE   B CE1  1 
ATOM   18425 C CE2  . PHE   B  1 435 ? 57.250 9.250   -59.980 1.00 28.02  ? 461  PHE   B CE2  1 
ATOM   18426 C CZ   . PHE   B  1 435 ? 57.240 7.998   -59.419 1.00 27.83  ? 461  PHE   B CZ   1 
ATOM   18427 H H    . PHE   B  1 435 ? 58.606 12.818  -58.008 0.00 32.03  ? 461  PHE   B H    1 
ATOM   18428 H HA   . PHE   B  1 435 ? 59.783 10.788  -56.213 0.00 29.39  ? 461  PHE   B HA   1 
ATOM   18429 H HB2  . PHE   B  1 435 ? 60.355 11.583  -59.078 0.00 28.80  ? 461  PHE   B HB2  1 
ATOM   18430 H HB3  . PHE   B  1 435 ? 61.203 10.314  -58.152 0.00 28.60  ? 461  PHE   B HB3  1 
ATOM   18431 H HD1  . PHE   B  1 435 ? 59.930 8.293   -57.416 0.00 29.18  ? 461  PHE   B HD1  1 
ATOM   18432 H HD2  . PHE   B  1 435 ? 58.225 11.151  -60.059 0.00 29.54  ? 461  PHE   B HD2  1 
ATOM   18433 H HE1  . PHE   B  1 435 ? 58.195 6.667   -58.067 0.00 29.64  ? 461  PHE   B HE1  1 
ATOM   18434 H HE2  . PHE   B  1 435 ? 56.498 9.520   -60.702 0.00 30.18  ? 461  PHE   B HE2  1 
ATOM   18435 H HZ   . PHE   B  1 435 ? 56.485 7.282   -59.707 0.00 29.68  ? 461  PHE   B HZ   1 
ATOM   18436 N N    . ASP   B  1 436 ? 61.735 12.130  -55.486 1.00 25.84  ? 462  ASP   B N    1 
ATOM   18437 C CA   . ASP   B  1 436 ? 62.839 12.924  -54.982 1.00 25.44  ? 462  ASP   B CA   1 
ATOM   18438 C C    . ASP   B  1 436 ? 63.973 12.845  -56.015 1.00 25.31  ? 462  ASP   B C    1 
ATOM   18439 O O    . ASP   B  1 436 ? 64.510 11.757  -56.239 1.00 25.27  ? 462  ASP   B O    1 
ATOM   18440 C CB   . ASP   B  1 436 ? 63.307 12.372  -53.629 1.00 26.72  ? 462  ASP   B CB   1 
ATOM   18441 C CG   . ASP   B  1 436 ? 64.492 13.085  -53.004 1.00 29.83  ? 462  ASP   B CG   1 
ATOM   18442 O OD1  . ASP   B  1 436 ? 64.997 14.052  -53.611 1.00 28.52  ? 462  ASP   B OD1  1 
ATOM   18443 O OD2  . ASP   B  1 436 ? 64.914 12.672  -51.907 1.00 33.16  ? 462  ASP   B OD2  1 
ATOM   18444 H H    . ASP   B  1 436 ? 61.572 11.278  -54.959 0.00 26.91  ? 462  ASP   B H    1 
ATOM   18445 H HA   . ASP   B  1 436 ? 62.507 13.950  -54.832 0.00 26.77  ? 462  ASP   B HA   1 
ATOM   18446 H HB2  . ASP   B  1 436 ? 62.477 12.449  -52.927 0.00 27.98  ? 462  ASP   B HB2  1 
ATOM   18447 H HB3  . ASP   B  1 436 ? 63.579 11.325  -53.748 0.00 28.02  ? 462  ASP   B HB3  1 
ATOM   18448 N N    . PRO   B  1 437 ? 64.354 13.969  -56.649 1.00 25.51  ? 463  PRO   B N    1 
ATOM   18449 C CA   . PRO   B  1 437 ? 65.424 13.894  -57.663 1.00 26.08  ? 463  PRO   B CA   1 
ATOM   18450 C C    . PRO   B  1 437 ? 66.811 13.539  -57.139 1.00 26.07  ? 463  PRO   B C    1 
ATOM   18451 O O    . PRO   B  1 437 ? 67.672 13.204  -57.944 1.00 26.28  ? 463  PRO   B O    1 
ATOM   18452 C CB   . PRO   B  1 437 ? 65.411 15.276  -58.324 1.00 27.41  ? 463  PRO   B CB   1 
ATOM   18453 C CG   . PRO   B  1 437 ? 64.690 16.171  -57.408 1.00 28.04  ? 463  PRO   B CG   1 
ATOM   18454 C CD   . PRO   B  1 437 ? 63.818 15.340  -56.509 1.00 25.55  ? 463  PRO   B CD   1 
ATOM   18455 H HA   . PRO   B  1 437 ? 65.153 13.159  -58.418 0.00 28.04  ? 463  PRO   B HA   1 
ATOM   18456 H HB2  . PRO   B  1 437 ? 66.443 15.597  -58.455 0.00 30.08  ? 463  PRO   B HB2  1 
ATOM   18457 H HB3  . PRO   B  1 437 ? 64.900 15.217  -59.284 0.00 29.98  ? 463  PRO   B HB3  1 
ATOM   18458 H HG2  . PRO   B  1 437 ? 65.413 16.727  -56.814 0.00 30.73  ? 463  PRO   B HG2  1 
ATOM   18459 H HG3  . PRO   B  1 437 ? 64.078 16.858  -57.991 0.00 30.76  ? 463  PRO   B HG3  1 
ATOM   18460 H HD2  . PRO   B  1 437 ? 63.914 15.684  -55.480 0.00 27.31  ? 463  PRO   B HD2  1 
ATOM   18461 H HD3  . PRO   B  1 437 ? 62.784 15.377  -56.847 0.00 27.32  ? 463  PRO   B HD3  1 
ATOM   18462 N N    . HIS   B  1 438 ? 67.034 13.604  -55.810 1.00 25.42  ? 464  HIS   B N    1 
ATOM   18463 C CA   . HIS   B  1 438 ? 68.311 13.253  -55.198 1.00 25.84  ? 464  HIS   B CA   1 
ATOM   18464 C C    . HIS   B  1 438 ? 68.342 11.804  -54.652 1.00 26.40  ? 464  HIS   B C    1 
ATOM   18465 O O    . HIS   B  1 438 ? 69.311 11.446  -53.990 1.00 27.07  ? 464  HIS   B O    1 
ATOM   18466 C CB   . HIS   B  1 438 ? 68.638 14.267  -54.086 1.00 26.66  ? 464  HIS   B CB   1 
ATOM   18467 C CG   . HIS   B  1 438 ? 68.704 15.677  -54.595 1.00 28.61  ? 464  HIS   B CG   1 
ATOM   18468 N ND1  . HIS   B  1 438 ? 69.804 16.139  -55.294 1.00 30.33  ? 464  HIS   B ND1  1 
ATOM   18469 C CD2  . HIS   B  1 438 ? 67.768 16.654  -54.557 1.00 29.88  ? 464  HIS   B CD2  1 
ATOM   18470 C CE1  . HIS   B  1 438 ? 69.525 17.394  -55.616 1.00 30.98  ? 464  HIS   B CE1  1 
ATOM   18471 N NE2  . HIS   B  1 438 ? 68.311 17.749  -55.191 1.00 30.89  ? 464  HIS   B NE2  1 
ATOM   18472 H H    . HIS   B  1 438 ? 66.352 13.913  -55.126 0.00 27.13  ? 464  HIS   B H    1 
ATOM   18473 H HA   . HIS   B  1 438 ? 69.109 13.337  -55.934 0.00 28.01  ? 464  HIS   B HA   1 
ATOM   18474 H HB2  . HIS   B  1 438 ? 67.866 14.219  -53.319 0.00 28.75  ? 464  HIS   B HB2  1 
ATOM   18475 H HB3  . HIS   B  1 438 ? 69.608 14.028  -53.653 0.00 29.02  ? 464  HIS   B HB3  1 
ATOM   18476 H HD2  . HIS   B  1 438 ? 66.788 16.587  -54.119 0.00 32.85  ? 464  HIS   B HD2  1 
ATOM   18477 H HE1  . HIS   B  1 438 ? 70.191 18.048  -56.151 0.00 35.07  ? 464  HIS   B HE1  1 
ATOM   18478 H HE2  . HIS   B  1 438 ? 67.870 18.656  -55.317 0.00 34.67  ? 464  HIS   B HE2  1 
ATOM   18479 N N    . SER   B  1 439 ? 67.303 10.980  -54.927 1.00 26.57  ? 465  SER   B N    1 
ATOM   18480 C CA   . SER   B  1 439 ? 67.212 9.583   -54.480 1.00 27.57  ? 465  SER   B CA   1 
ATOM   18481 C C    . SER   B  1 439 ? 67.287 8.619   -55.683 1.00 26.82  ? 465  SER   B C    1 
ATOM   18482 O O    . SER   B  1 439 ? 67.172 9.035   -56.841 1.00 26.91  ? 465  SER   B O    1 
ATOM   18483 C CB   . SER   B  1 439 ? 65.880 9.341   -53.754 1.00 30.83  ? 465  SER   B CB   1 
ATOM   18484 O OG   . SER   B  1 439 ? 65.804 10.027  -52.519 1.00 36.09  ? 465  SER   B OG   1 
ATOM   18485 H H    . SER   B  1 439 ? 66.494 11.251  -55.476 0.00 28.28  ? 465  SER   B H    1 
ATOM   18486 H HA   . SER   B  1 439 ? 68.020 9.334   -53.794 0.00 29.45  ? 465  SER   B HA   1 
ATOM   18487 H HB2  . SER   B  1 439 ? 65.069 9.675   -54.400 0.00 33.02  ? 465  SER   B HB2  1 
ATOM   18488 H HB3  . SER   B  1 439 ? 65.776 8.274   -53.555 0.00 32.98  ? 465  SER   B HB3  1 
ATOM   18489 H HG   . SER   B  1 439 ? 64.919 9.868   -52.097 0.00 39.19  ? 465  SER   B HG   1 
ATOM   18490 N N    . ASN   B  1 440 ? 67.436 7.317   -55.389 1.00 25.84  ? 466  ASN   B N    1 
ATOM   18491 C CA   . ASN   B  1 440 ? 67.428 6.266   -56.388 1.00 24.90  ? 466  ASN   B CA   1 
ATOM   18492 C C    . ASN   B  1 440 ? 65.972 6.098   -56.817 1.00 24.76  ? 466  ASN   B C    1 
ATOM   18493 O O    . ASN   B  1 440 ? 65.085 5.942   -55.968 1.00 25.11  ? 466  ASN   B O    1 
ATOM   18494 C CB   . ASN   B  1 440 ? 67.959 4.968   -55.787 1.00 25.07  ? 466  ASN   B CB   1 
ATOM   18495 C CG   . ASN   B  1 440 ? 68.341 3.930   -56.816 1.00 25.27  ? 466  ASN   B CG   1 
ATOM   18496 O OD1  . ASN   B  1 440 ? 67.481 3.375   -57.521 1.00 24.32  ? 466  ASN   B OD1  1 
ATOM   18497 N ND2  . ASN   B  1 440 ? 69.634 3.640   -56.925 1.00 25.48  ? 466  ASN   B ND2  1 
ATOM   18498 H H    . ASN   B  1 440 ? 67.549 6.973   -54.440 0.00 27.27  ? 466  ASN   B H    1 
ATOM   18499 H HA   . ASN   B  1 440 ? 68.047 6.546   -57.240 0.00 26.48  ? 466  ASN   B HA   1 
ATOM   18500 H HB2  . ASN   B  1 440 ? 68.836 5.196   -55.185 0.00 26.62  ? 466  ASN   B HB2  1 
ATOM   18501 H HB3  . ASN   B  1 440 ? 67.187 4.529   -55.157 0.00 26.39  ? 466  ASN   B HB3  1 
ATOM   18502 H HD21 . ASN   B  1 440 ? 69.935 2.948   -57.605 0.00 27.63  ? 466  ASN   B HD21 1 
ATOM   18503 H HD22 . ASN   B  1 440 ? 70.325 4.101   -56.343 0.00 27.51  ? 466  ASN   B HD22 1 
ATOM   18504 N N    . PHE   B  1 441 ? 65.716 6.153   -58.122 1.00 23.16  ? 467  PHE   B N    1 
ATOM   18505 C CA   . PHE   B  1 441 ? 64.368 6.046   -58.671 1.00 22.83  ? 467  PHE   B CA   1 
ATOM   18506 C C    . PHE   B  1 441 ? 63.823 4.617   -58.664 1.00 23.15  ? 467  PHE   B C    1 
ATOM   18507 O O    . PHE   B  1 441 ? 62.606 4.459   -58.591 1.00 24.02  ? 467  PHE   B O    1 
ATOM   18508 C CB   . PHE   B  1 441 ? 64.380 6.577   -60.127 1.00 22.25  ? 467  PHE   B CB   1 
ATOM   18509 C CG   . PHE   B  1 441 ? 63.046 6.649   -60.827 1.00 22.92  ? 467  PHE   B CG   1 
ATOM   18510 C CD1  . PHE   B  1 441 ? 62.124 7.629   -60.498 1.00 23.57  ? 467  PHE   B CD1  1 
ATOM   18511 C CD2  . PHE   B  1 441 ? 62.759 5.809   -61.895 1.00 23.84  ? 467  PHE   B CD2  1 
ATOM   18512 C CE1  . PHE   B  1 441 ? 60.918 7.733   -61.190 1.00 24.80  ? 467  PHE   B CE1  1 
ATOM   18513 C CE2  . PHE   B  1 441 ? 61.561 5.922   -62.589 1.00 24.81  ? 467  PHE   B CE2  1 
ATOM   18514 C CZ   . PHE   B  1 441 ? 60.634 6.865   -62.215 1.00 24.46  ? 467  PHE   B CZ   1 
ATOM   18515 H H    . PHE   B  1 441 ? 66.432 6.269   -58.833 0.00 24.38  ? 467  PHE   B H    1 
ATOM   18516 H HA   . PHE   B  1 441 ? 63.689 6.674   -58.096 0.00 23.61  ? 467  PHE   B HA   1 
ATOM   18517 H HB2  . PHE   B  1 441 ? 64.786 7.588   -60.116 0.00 23.32  ? 467  PHE   B HB2  1 
ATOM   18518 H HB3  . PHE   B  1 441 ? 65.028 5.931   -60.718 0.00 23.44  ? 467  PHE   B HB3  1 
ATOM   18519 H HD1  . PHE   B  1 441 ? 62.333 8.310   -59.689 0.00 24.67  ? 467  PHE   B HD1  1 
ATOM   18520 H HD2  . PHE   B  1 441 ? 63.470 5.055   -62.193 0.00 25.51  ? 467  PHE   B HD2  1 
ATOM   18521 H HE1  . PHE   B  1 441 ? 60.194 8.477   -60.900 0.00 26.28  ? 467  PHE   B HE1  1 
ATOM   18522 H HE2  . PHE   B  1 441 ? 61.337 5.236   -63.389 0.00 26.83  ? 467  PHE   B HE2  1 
ATOM   18523 H HZ   . PHE   B  1 441 ? 59.700 6.943   -62.747 0.00 26.21  ? 467  PHE   B HZ   1 
ATOM   18524 N N    . TYR   B  1 442 ? 64.686 3.585   -58.811 1.00 22.49  ? 468  TYR   B N    1 
ATOM   18525 C CA   . TYR   B  1 442 ? 64.216 2.195   -58.939 1.00 22.83  ? 468  TYR   B CA   1 
ATOM   18526 C C    . TYR   B  1 442 ? 64.100 1.390   -57.637 1.00 23.61  ? 468  TYR   B C    1 
ATOM   18527 O O    . TYR   B  1 442 ? 63.363 0.402   -57.633 1.00 24.26  ? 468  TYR   B O    1 
ATOM   18528 C CB   . TYR   B  1 442 ? 65.084 1.450   -59.961 1.00 22.17  ? 468  TYR   B CB   1 
ATOM   18529 C CG   . TYR   B  1 442 ? 64.869 2.025   -61.343 1.00 21.51  ? 468  TYR   B CG   1 
ATOM   18530 C CD1  . TYR   B  1 442 ? 63.681 1.803   -62.029 1.00 21.90  ? 468  TYR   B CD1  1 
ATOM   18531 C CD2  . TYR   B  1 442 ? 65.769 2.928   -61.887 1.00 21.87  ? 468  TYR   B CD2  1 
ATOM   18532 C CE1  . TYR   B  1 442 ? 63.419 2.419   -63.241 1.00 22.66  ? 468  TYR   B CE1  1 
ATOM   18533 C CE2  . TYR   B  1 442 ? 65.529 3.534   -63.114 1.00 22.49  ? 468  TYR   B CE2  1 
ATOM   18534 C CZ   . TYR   B  1 442 ? 64.378 3.231   -63.816 1.00 23.74  ? 468  TYR   B CZ   1 
ATOM   18535 O OH   . TYR   B  1 442 ? 64.119 3.859   -65.010 1.00 24.80  ? 468  TYR   B OH   1 
ATOM   18536 H H    . TYR   B  1 442 ? 65.696 3.676   -58.848 0.00 23.57  ? 468  TYR   B H    1 
ATOM   18537 H HA   . TYR   B  1 442 ? 63.196 2.215   -59.320 0.00 23.91  ? 468  TYR   B HA   1 
ATOM   18538 H HB2  . TYR   B  1 442 ? 66.136 1.549   -59.698 0.00 23.51  ? 468  TYR   B HB2  1 
ATOM   18539 H HB3  . TYR   B  1 442 ? 64.799 0.398   -59.980 0.00 23.53  ? 468  TYR   B HB3  1 
ATOM   18540 H HD1  . TYR   B  1 442 ? 62.940 1.146   -61.601 0.00 23.28  ? 468  TYR   B HD1  1 
ATOM   18541 H HD2  . TYR   B  1 442 ? 66.687 3.142   -61.366 0.00 23.37  ? 468  TYR   B HD2  1 
ATOM   18542 H HE1  . TYR   B  1 442 ? 62.511 2.181   -63.769 0.00 24.54  ? 468  TYR   B HE1  1 
ATOM   18543 H HE2  . TYR   B  1 442 ? 66.268 4.190   -63.546 0.00 24.42  ? 468  TYR   B HE2  1 
ATOM   18544 H HH   . TYR   B  1 442 ? 63.173 3.735   -65.283 0.00 27.38  ? 468  TYR   B HH   1 
ATOM   18545 N N    . HIS   B  1 443 ? 64.729 1.818   -56.529 1.00 23.56  ? 469  HIS   B N    1 
ATOM   18546 C CA   . HIS   B  1 443 ? 64.544 1.133   -55.244 1.00 24.20  ? 469  HIS   B CA   1 
ATOM   18547 C C    . HIS   B  1 443 ? 64.803 2.094   -54.093 1.00 24.51  ? 469  HIS   B C    1 
ATOM   18548 O O    . HIS   B  1 443 ? 65.495 3.102   -54.264 1.00 23.58  ? 469  HIS   B O    1 
ATOM   18549 C CB   . HIS   B  1 443 ? 65.455 -0.105  -55.131 1.00 25.25  ? 469  HIS   B CB   1 
ATOM   18550 C CG   . HIS   B  1 443 ? 66.909 0.205   -55.271 1.00 27.26  ? 469  HIS   B CG   1 
ATOM   18551 N ND1  . HIS   B  1 443 ? 67.582 -0.029  -56.454 1.00 29.31  ? 469  HIS   B ND1  1 
ATOM   18552 C CD2  . HIS   B  1 443 ? 67.775 0.731   -54.373 1.00 27.93  ? 469  HIS   B CD2  1 
ATOM   18553 C CE1  . HIS   B  1 443 ? 68.830 0.351   -56.240 1.00 29.10  ? 469  HIS   B CE1  1 
ATOM   18554 N NE2  . HIS   B  1 443 ? 68.988 0.820   -55.002 1.00 28.88  ? 469  HIS   B NE2  1 
ATOM   18555 H H    . HIS   B  1 443 ? 65.363 2.609   -56.487 0.00 24.57  ? 469  HIS   B H    1 
ATOM   18556 H HA   . HIS   B  1 443 ? 63.513 0.796   -55.150 0.00 25.11  ? 469  HIS   B HA   1 
ATOM   18557 H HB2  . HIS   B  1 443 ? 65.305 -0.564  -54.154 0.00 26.61  ? 469  HIS   B HB2  1 
ATOM   18558 H HB3  . HIS   B  1 443 ? 65.187 -0.813  -55.914 0.00 26.81  ? 469  HIS   B HB3  1 
ATOM   18559 H HD2  . HIS   B  1 443 ? 67.553 1.026   -53.361 0.00 29.92  ? 469  HIS   B HD2  1 
ATOM   18560 H HE1  . HIS   B  1 443 ? 69.615 0.292   -56.973 0.00 32.08  ? 469  HIS   B HE1  1 
ATOM   18561 H HE2  . HIS   B  1 443 ? 69.850 1.173   -54.599 0.00 31.54  ? 469  HIS   B HE2  1 
ATOM   18562 N N    . PHE   B  1 444 ? 64.256 1.775   -52.917 1.00 25.51  ? 470  PHE   B N    1 
ATOM   18563 C CA   . PHE   B  1 444 ? 64.496 2.587   -51.737 1.00 27.43  ? 470  PHE   B CA   1 
ATOM   18564 C C    . PHE   B  1 444 ? 65.939 2.387   -51.259 1.00 26.80  ? 470  PHE   B C    1 
ATOM   18565 O O    . PHE   B  1 444 ? 66.498 1.309   -51.423 1.00 26.36  ? 470  PHE   B O    1 
ATOM   18566 C CB   . PHE   B  1 444 ? 63.438 2.331   -50.641 1.00 29.45  ? 470  PHE   B CB   1 
ATOM   18567 C CG   . PHE   B  1 444 ? 63.327 0.970   -49.988 1.00 32.99  ? 470  PHE   B CG   1 
ATOM   18568 C CD1  . PHE   B  1 444 ? 64.300 0.527   -49.107 1.00 35.08  ? 470  PHE   B CD1  1 
ATOM   18569 C CD2  . PHE   B  1 444 ? 62.142 0.252   -50.052 1.00 35.03  ? 470  PHE   B CD2  1 
ATOM   18570 C CE1  . PHE   B  1 444 ? 64.144 -0.663  -48.401 1.00 36.61  ? 470  PHE   B CE1  1 
ATOM   18571 C CE2  . PHE   B  1 444 ? 61.982 -0.930  -49.336 1.00 36.49  ? 470  PHE   B CE2  1 
ATOM   18572 C CZ   . PHE   B  1 444 ? 62.969 -1.361  -48.488 1.00 36.59  ? 470  PHE   B CZ   1 
ATOM   18573 H H    . PHE   B  1 444 ? 63.652 0.973   -52.768 0.00 26.46  ? 470  PHE   B H    1 
ATOM   18574 H HA   . PHE   B  1 444 ? 64.392 3.635   -52.014 0.00 28.64  ? 470  PHE   B HA   1 
ATOM   18575 H HB2  . PHE   B  1 444 ? 63.630 3.039   -49.836 0.00 30.89  ? 470  PHE   B HB2  1 
ATOM   18576 H HB3  . PHE   B  1 444 ? 62.465 2.557   -51.073 0.00 30.85  ? 470  PHE   B HB3  1 
ATOM   18577 H HD1  . PHE   B  1 444 ? 65.208 1.095   -48.993 0.00 37.92  ? 470  PHE   B HD1  1 
ATOM   18578 H HD2  . PHE   B  1 444 ? 61.337 0.597   -50.679 0.00 37.53  ? 470  PHE   B HD2  1 
ATOM   18579 H HE1  . PHE   B  1 444 ? 64.931 -1.012  -47.754 0.00 39.89  ? 470  PHE   B HE1  1 
ATOM   18580 H HE2  . PHE   B  1 444 ? 61.074 -1.500  -49.436 0.00 39.40  ? 470  PHE   B HE2  1 
ATOM   18581 H HZ   . PHE   B  1 444 ? 62.865 -2.304  -47.978 0.00 39.73  ? 470  PHE   B HZ   1 
ATOM   18582 N N    . THR   B  1 445 ? 66.550 3.436   -50.697 1.00 27.28  ? 471  THR   B N    1 
ATOM   18583 C CA   . THR   B  1 445 ? 67.944 3.378   -50.251 1.00 28.17  ? 471  THR   B CA   1 
ATOM   18584 C C    . THR   B  1 445 ? 68.112 3.206   -48.731 1.00 28.34  ? 471  THR   B C    1 
ATOM   18585 O O    . THR   B  1 445 ? 69.246 3.054   -48.271 1.00 28.53  ? 471  THR   B O    1 
ATOM   18586 C CB   . THR   B  1 445 ? 68.692 4.613   -50.768 1.00 30.88  ? 471  THR   B CB   1 
ATOM   18587 O OG1  . THR   B  1 445 ? 68.029 5.791   -50.297 1.00 32.62  ? 471  THR   B OG1  1 
ATOM   18588 C CG2  . THR   B  1 445 ? 68.760 4.642   -52.278 1.00 31.38  ? 471  THR   B CG2  1 
ATOM   18589 H H    . THR   B  1 445 ? 66.104 4.332   -50.527 0.00 28.58  ? 471  THR   B H    1 
ATOM   18590 H HA   . THR   B  1 445 ? 68.433 2.512   -50.695 0.00 30.11  ? 471  THR   B HA   1 
ATOM   18591 H HB   . THR   B  1 445 ? 69.713 4.604   -50.389 0.00 33.51  ? 471  THR   B HB   1 
ATOM   18592 H HG1  . THR   B  1 445 ? 68.492 6.604   -50.628 0.00 35.36  ? 471  THR   B HG1  1 
ATOM   18593 H HG21 . THR   B  1 445 ? 69.378 5.478   -52.602 0.00 34.11  ? 471  THR   B HG21 1 
ATOM   18594 H HG22 . THR   B  1 445 ? 69.194 3.715   -52.651 0.00 34.12  ? 471  THR   B HG22 1 
ATOM   18595 H HG23 . THR   B  1 445 ? 67.763 4.765   -52.699 0.00 33.85  ? 471  THR   B HG23 1 
ATOM   18596 N N    . ARG   B  1 446 ? 67.015 3.164   -47.969 1.00 28.15  ? 472  ARG   B N    1 
ATOM   18597 C CA   . ARG   B  1 446 ? 67.105 2.951   -46.517 1.00 28.99  ? 472  ARG   B CA   1 
ATOM   18598 C C    . ARG   B  1 446 ? 67.607 1.522   -46.222 1.00 28.52  ? 472  ARG   B C    1 
ATOM   18599 O O    . ARG   B  1 446 ? 67.407 0.624   -47.050 1.00 28.21  ? 472  ARG   B O    1 
ATOM   18600 C CB   . ARG   B  1 446 ? 65.746 3.178   -45.835 1.00 31.56  ? 472  ARG   B CB   1 
ATOM   18601 C CG   . ARG   B  1 446 ? 64.662 2.163   -46.206 1.00 36.84  ? 472  ARG   B CG   1 
ATOM   18602 C CD   . ARG   B  1 446 ? 63.497 2.232   -45.247 1.00 41.74  ? 472  ARG   B CD   1 
ATOM   18603 N NE   . ARG   B  1 446 ? 62.395 1.339   -45.619 1.00 46.07  ? 472  ARG   B NE   1 
ATOM   18604 C CZ   . ARG   B  1 446 ? 62.353 0.026   -45.388 1.00 49.68  ? 472  ARG   B CZ   1 
ATOM   18605 N NH1  . ARG   B  1 446 ? 63.384 -0.592  -44.813 1.00 49.73  ? 472  ARG   B NH1  1 
ATOM   18606 N NH2  . ARG   B  1 446 ? 61.291 -0.684  -45.751 1.00 50.62  ? 472  ARG   B NH2  1 
ATOM   18607 H H    . ARG   B  1 446 ? 66.065 3.287   -48.304 0.00 29.60  ? 472  ARG   B H    1 
ATOM   18608 H HA   . ARG   B  1 446 ? 67.804 3.689   -46.127 0.00 30.91  ? 472  ARG   B HA   1 
ATOM   18609 H HB2  . ARG   B  1 446 ? 65.887 3.128   -44.757 0.00 33.71  ? 472  ARG   B HB2  1 
ATOM   18610 H HB3  . ARG   B  1 446 ? 65.382 4.167   -46.109 0.00 33.57  ? 472  ARG   B HB3  1 
ATOM   18611 H HG2  . ARG   B  1 446 ? 64.287 2.391   -47.203 0.00 39.80  ? 472  ARG   B HG2  1 
ATOM   18612 H HG3  . ARG   B  1 446 ? 65.044 1.144   -46.179 0.00 39.98  ? 472  ARG   B HG3  1 
ATOM   18613 H HD2  . ARG   B  1 446 ? 63.835 1.989   -44.241 0.00 45.68  ? 472  ARG   B HD2  1 
ATOM   18614 H HD3  . ARG   B  1 446 ? 63.107 3.248   -45.261 0.00 45.51  ? 472  ARG   B HD3  1 
ATOM   18615 H HE   . ARG   B  1 446 ? 61.584 1.768   -46.054 0.00 50.59  ? 472  ARG   B HE   1 
ATOM   18616 H HH11 . ARG   B  1 446 ? 64.220 -0.096  -44.523 0.00 55.45  ? 472  ARG   B HH11 1 
ATOM   18617 H HH12 . ARG   B  1 446 ? 63.340 -1.594  -44.657 0.00 55.47  ? 472  ARG   B HH12 1 
ATOM   18618 H HH21 . ARG   B  1 446 ? 60.499 -0.231  -46.196 0.00 56.08  ? 472  ARG   B HH21 1 
ATOM   18619 H HH22 . ARG   B  1 446 ? 61.264 -1.686  -45.588 0.00 56.29  ? 472  ARG   B HH22 1 
ATOM   18620 N N    . PRO   B  1 447 ? 68.228 1.263   -45.053 1.00 27.93  ? 473  PRO   B N    1 
ATOM   18621 C CA   . PRO   B  1 447 ? 68.684 -0.119  -44.771 1.00 27.03  ? 473  PRO   B CA   1 
ATOM   18622 C C    . PRO   B  1 447 ? 67.520 -1.115  -44.797 1.00 25.56  ? 473  PRO   B C    1 
ATOM   18623 O O    . PRO   B  1 447 ? 66.383 -0.740  -44.481 1.00 24.82  ? 473  PRO   B O    1 
ATOM   18624 C CB   . PRO   B  1 447 ? 69.316 -0.023  -43.371 1.00 27.96  ? 473  PRO   B CB   1 
ATOM   18625 C CG   . PRO   B  1 447 ? 69.566 1.430   -43.135 1.00 28.77  ? 473  PRO   B CG   1 
ATOM   18626 C CD   . PRO   B  1 447 ? 68.543 2.185   -43.939 1.00 27.56  ? 473  PRO   B CD   1 
ATOM   18627 H HA   . PRO   B  1 447 ? 69.443 -0.425  -45.490 0.00 29.16  ? 473  PRO   B HA   1 
ATOM   18628 H HB2  . PRO   B  1 447 ? 68.620 -0.418  -42.633 0.00 30.23  ? 473  PRO   B HB2  1 
ATOM   18629 H HB3  . PRO   B  1 447 ? 70.251 -0.582  -43.354 0.00 30.57  ? 473  PRO   B HB3  1 
ATOM   18630 H HG2  . PRO   B  1 447 ? 69.447 1.650   -42.076 0.00 31.28  ? 473  PRO   B HG2  1 
ATOM   18631 H HG3  . PRO   B  1 447 ? 70.573 1.685   -43.463 0.00 31.44  ? 473  PRO   B HG3  1 
ATOM   18632 H HD2  . PRO   B  1 447 ? 67.652 2.381   -43.343 0.00 29.33  ? 473  PRO   B HD2  1 
ATOM   18633 H HD3  . PRO   B  1 447 ? 68.998 3.108   -44.294 0.00 29.52  ? 473  PRO   B HD3  1 
ATOM   18634 N N    . LEU   B  1 448 ? 67.781 -2.357  -45.228 1.00 24.81  ? 474  LEU   B N    1 
ATOM   18635 C CA   . LEU   B  1 448 ? 66.723 -3.380  -45.278 1.00 24.55  ? 474  LEU   B CA   1 
ATOM   18636 C C    . LEU   B  1 448 ? 66.195 -3.674  -43.871 1.00 24.37  ? 474  LEU   B C    1 
ATOM   18637 O O    . LEU   B  1 448 ? 64.997 -3.820  -43.666 1.00 23.77  ? 474  LEU   B O    1 
ATOM   18638 C CB   . LEU   B  1 448 ? 67.275 -4.680  -45.883 1.00 24.27  ? 474  LEU   B CB   1 
ATOM   18639 C CG   . LEU   B  1 448 ? 67.690 -4.609  -47.348 1.00 25.79  ? 474  LEU   B CG   1 
ATOM   18640 C CD1  . LEU   B  1 448 ? 68.333 -5.900  -47.770 1.00 26.79  ? 474  LEU   B CD1  1 
ATOM   18641 C CD2  . LEU   B  1 448 ? 66.494 -4.292  -48.243 1.00 26.27  ? 474  LEU   B CD2  1 
ATOM   18642 H H    . LEU   B  1 448 ? 68.694 -2.679  -45.533 0.00 26.58  ? 474  LEU   B H    1 
ATOM   18643 H HA   . LEU   B  1 448 ? 65.887 -3.017  -45.873 0.00 25.78  ? 474  LEU   B HA   1 
ATOM   18644 H HB2  . LEU   B  1 448 ? 68.152 -4.981  -45.311 0.00 26.17  ? 474  LEU   B HB2  1 
ATOM   18645 H HB3  . LEU   B  1 448 ? 66.511 -5.452  -45.797 0.00 25.93  ? 474  LEU   B HB3  1 
ATOM   18646 H HG   . LEU   B  1 448 ? 68.422 -3.812  -47.470 0.00 27.85  ? 474  LEU   B HG   1 
ATOM   18647 H HD11 . LEU   B  1 448 ? 68.662 -5.811  -48.803 0.00 29.46  ? 474  LEU   B HD11 1 
ATOM   18648 H HD12 . LEU   B  1 448 ? 69.189 -6.098  -47.127 0.00 29.60  ? 474  LEU   B HD12 1 
ATOM   18649 H HD13 . LEU   B  1 448 ? 67.605 -6.705  -47.680 0.00 29.41  ? 474  LEU   B HD13 1 
ATOM   18650 H HD21 . LEU   B  1 448 ? 66.758 -4.507  -49.277 0.00 28.27  ? 474  LEU   B HD21 1 
ATOM   18651 H HD22 . LEU   B  1 448 ? 65.646 -4.905  -47.941 0.00 28.12  ? 474  LEU   B HD22 1 
ATOM   18652 H HD23 . LEU   B  1 448 ? 66.245 -3.235  -48.149 0.00 27.95  ? 474  LEU   B HD23 1 
ATOM   18653 N N    . ILE   B  1 449 ? 67.113 -3.746  -42.914 1.00 24.81  ? 475  ILE   B N    1 
ATOM   18654 C CA   . ILE   B  1 449 ? 66.824 -4.032  -41.516 1.00 25.04  ? 475  ILE   B CA   1 
ATOM   18655 C C    . ILE   B  1 449 ? 67.273 -2.835  -40.689 1.00 24.01  ? 475  ILE   B C    1 
ATOM   18656 O O    . ILE   B  1 449 ? 68.286 -2.220  -41.018 1.00 23.64  ? 475  ILE   B O    1 
ATOM   18657 C CB   . ILE   B  1 449 ? 67.542 -5.379  -41.177 1.00 26.72  ? 475  ILE   B CB   1 
ATOM   18658 C CG1  . ILE   B  1 449 ? 66.829 -6.505  -42.032 1.00 28.32  ? 475  ILE   B CG1  1 
ATOM   18659 C CG2  . ILE   B  1 449 ? 67.538 -5.655  -39.653 1.00 27.23  ? 475  ILE   B CG2  1 
ATOM   18660 C CD1  . ILE   B  1 449 ? 67.120 -7.868  -41.761 1.00 30.09  ? 475  ILE   B CD1  1 
ATOM   18661 H H    . ILE   B  1 449 ? 68.108 -3.628  -43.076 0.00 26.69  ? 475  ILE   B H    1 
ATOM   18662 H HA   . ILE   B  1 449 ? 65.755 -4.163  -41.356 0.00 26.68  ? 475  ILE   B HA   1 
ATOM   18663 H HB   . ILE   B  1 449 ? 68.590 -5.338  -41.475 0.00 29.45  ? 475  ILE   B HB   1 
ATOM   18664 H HG12 . ILE   B  1 449 ? 65.752 -6.395  -41.911 0.00 30.95  ? 475  ILE   B HG12 1 
ATOM   18665 H HG13 . ILE   B  1 449 ? 67.084 -6.351  -43.079 0.00 31.13  ? 475  ILE   B HG13 1 
ATOM   18666 H HG21 . ILE   B  1 449 ? 67.923 -6.655  -39.460 0.00 30.31  ? 475  ILE   B HG21 1 
ATOM   18667 H HG22 . ILE   B  1 449 ? 68.178 -4.931  -39.150 0.00 30.11  ? 475  ILE   B HG22 1 
ATOM   18668 H HG23 . ILE   B  1 449 ? 66.517 -5.574  -39.284 0.00 29.84  ? 475  ILE   B HG23 1 
ATOM   18669 H HD11 . ILE   B  1 449 ? 66.722 -8.481  -42.568 0.00 33.65  ? 475  ILE   B HD11 1 
ATOM   18670 H HD12 . ILE   B  1 449 ? 68.199 -7.989  -41.694 0.00 33.89  ? 475  ILE   B HD12 1 
ATOM   18671 H HD13 . ILE   B  1 449 ? 66.643 -8.145  -40.822 0.00 33.67  ? 475  ILE   B HD13 1 
ATOM   18672 N N    . LYS   B  1 450 ? 66.503 -2.443  -39.636 1.00 23.42  ? 476  LYS   B N    1 
ATOM   18673 C CA   . LYS   B  1 450 ? 66.857 -1.294  -38.788 1.00 24.21  ? 476  LYS   B CA   1 
ATOM   18674 C C    . LYS   B  1 450 ? 68.286 -1.455  -38.254 1.00 24.46  ? 476  LYS   B C    1 
ATOM   18675 O O    . LYS   B  1 450 ? 68.607 -2.560  -37.812 1.00 24.27  ? 476  LYS   B O    1 
ATOM   18676 C CB   . LYS   B  1 450 ? 65.914 -1.169  -37.575 1.00 26.79  ? 476  LYS   B CB   1 
ATOM   18677 C CG   . LYS   B  1 450 ? 64.532 -0.589  -37.890 1.00 32.92  ? 476  LYS   B CG   1 
ATOM   18678 C CD   . LYS   B  1 450 ? 63.652 -0.608  -36.644 1.00 38.59  ? 476  LYS   B CD   1 
ATOM   18679 C CE   . LYS   B  1 450 ? 62.355 0.159   -36.781 1.00 42.85  ? 476  LYS   B CE   1 
ATOM   18680 N NZ   . LYS   B  1 450 ? 61.560 0.138   -35.514 1.00 44.12  ? 476  LYS   B NZ   1 
ATOM   18681 H H    . LYS   B  1 450 ? 65.640 -2.902  -39.362 0.00 24.71  ? 476  LYS   B H    1 
ATOM   18682 H HA   . LYS   B  1 450 ? 66.755 -0.391  -39.386 0.00 25.62  ? 476  LYS   B HA   1 
ATOM   18683 H HB2  . LYS   B  1 450 ? 65.774 -2.157  -37.141 0.00 28.93  ? 476  LYS   B HB2  1 
ATOM   18684 H HB3  . LYS   B  1 450 ? 66.383 -0.515  -36.842 0.00 28.94  ? 476  LYS   B HB3  1 
ATOM   18685 H HG2  . LYS   B  1 450 ? 64.637 0.443   -38.223 0.00 35.73  ? 476  LYS   B HG2  1 
ATOM   18686 H HG3  . LYS   B  1 450 ? 64.052 -1.191  -38.661 0.00 35.72  ? 476  LYS   B HG3  1 
ATOM   18687 H HD2  . LYS   B  1 450 ? 63.388 -1.639  -36.414 0.00 42.73  ? 476  LYS   B HD2  1 
ATOM   18688 H HD3  . LYS   B  1 450 ? 64.209 -0.176  -35.814 0.00 42.80  ? 476  LYS   B HD3  1 
ATOM   18689 H HE2  . LYS   B  1 450 ? 62.577 1.197   -37.028 0.00 47.40  ? 476  LYS   B HE2  1 
ATOM   18690 H HE3  . LYS   B  1 450 ? 61.753 -0.294  -37.567 0.00 47.33  ? 476  LYS   B HE3  1 
ATOM   18691 H HZ1  . LYS   B  1 450 ? 60.680 0.625   -35.649 0.00 48.88  ? 476  LYS   B HZ1  1 
ATOM   18692 H HZ2  . LYS   B  1 450 ? 61.369 -0.820  -35.239 0.00 49.13  ? 476  LYS   B HZ2  1 
ATOM   18693 H HZ3  . LYS   B  1 450 ? 62.079 0.597   -34.771 0.00 49.19  ? 476  LYS   B HZ3  1 
ATOM   18694 N N    . PRO   B  1 451 ? 69.190 -0.458  -38.410 1.00 25.07  ? 477  PRO   B N    1 
ATOM   18695 C CA   . PRO   B  1 451 ? 70.576 -0.648  -37.932 1.00 24.73  ? 477  PRO   B CA   1 
ATOM   18696 C C    . PRO   B  1 451 ? 70.682 -1.084  -36.474 1.00 24.04  ? 477  PRO   B C    1 
ATOM   18697 O O    . PRO   B  1 451 ? 71.585 -1.838  -36.142 1.00 23.41  ? 477  PRO   B O    1 
ATOM   18698 C CB   . PRO   B  1 451 ? 71.231 0.724   -38.137 1.00 25.93  ? 477  PRO   B CB   1 
ATOM   18699 C CG   . PRO   B  1 451 ? 70.383 1.430   -39.113 1.00 26.83  ? 477  PRO   B CG   1 
ATOM   18700 C CD   . PRO   B  1 451 ? 68.992 0.890   -38.979 1.00 25.07  ? 477  PRO   B CD   1 
ATOM   18701 H HA   . PRO   B  1 451 ? 71.089 -1.377  -38.558 0.00 27.43  ? 477  PRO   B HA   1 
ATOM   18702 H HB2  . PRO   B  1 451 ? 71.248 1.262   -37.190 0.00 28.89  ? 477  PRO   B HB2  1 
ATOM   18703 H HB3  . PRO   B  1 451 ? 72.240 0.596   -38.524 0.00 29.02  ? 477  PRO   B HB3  1 
ATOM   18704 H HG2  . PRO   B  1 451 ? 70.397 2.497   -38.896 0.00 29.46  ? 477  PRO   B HG2  1 
ATOM   18705 H HG3  . PRO   B  1 451 ? 70.762 1.247   -40.117 0.00 29.47  ? 477  PRO   B HG3  1 
ATOM   18706 H HD2  . PRO   B  1 451 ? 68.399 1.511   -38.309 0.00 27.00  ? 477  PRO   B HD2  1 
ATOM   18707 H HD3  . PRO   B  1 451 ? 68.548 0.839   -39.971 0.00 26.88  ? 477  PRO   B HD3  1 
ATOM   18708 N N    . GLN   B  1 452 ? 69.757 -0.636  -35.614 1.00 23.92  ? 478  GLN   B N    1 
ATOM   18709 C CA   . GLN   B  1 452 ? 69.769 -0.997  -34.200 1.00 24.30  ? 478  GLN   B CA   1 
ATOM   18710 C C    . GLN   B  1 452 ? 69.551 -2.498  -33.987 1.00 24.15  ? 478  GLN   B C    1 
ATOM   18711 O O    . GLN   B  1 452 ? 70.077 -3.055  -33.025 1.00 24.46  ? 478  GLN   B O    1 
ATOM   18712 C CB   . GLN   B  1 452 ? 68.722 -0.184  -33.418 1.00 26.31  ? 478  GLN   B CB   1 
ATOM   18713 C CG   . GLN   B  1 452 ? 69.016 1.324   -33.373 1.00 29.46  ? 478  GLN   B CG   1 
ATOM   18714 C CD   . GLN   B  1 452 ? 68.297 2.106   -34.464 1.00 32.06  ? 478  GLN   B CD   1 
ATOM   18715 O OE1  . GLN   B  1 452 ? 68.044 1.614   -35.563 1.00 32.48  ? 478  GLN   B OE1  1 
ATOM   18716 N NE2  . GLN   B  1 452 ? 67.965 3.360   -34.192 1.00 32.24  ? 478  GLN   B NE2  1 
ATOM   18717 H H    . GLN   B  1 452 ? 68.990 -0.020  -35.865 0.00 26.19  ? 478  GLN   B H    1 
ATOM   18718 H HA   . GLN   B  1 452 ? 70.749 -0.753  -33.793 0.00 27.51  ? 478  GLN   B HA   1 
ATOM   18719 H HB2  . GLN   B  1 452 ? 67.741 -0.338  -33.866 0.00 29.11  ? 478  GLN   B HB2  1 
ATOM   18720 H HB3  . GLN   B  1 452 ? 68.706 -0.542  -32.390 0.00 29.64  ? 478  GLN   B HB3  1 
ATOM   18721 H HG2  . GLN   B  1 452 ? 68.692 1.712   -32.409 0.00 33.29  ? 478  GLN   B HG2  1 
ATOM   18722 H HG3  . GLN   B  1 452 ? 70.086 1.488   -33.497 0.00 33.44  ? 478  GLN   B HG3  1 
ATOM   18723 H HE21 . GLN   B  1 452 ? 68.192 3.769   -33.292 0.00 36.29  ? 478  GLN   B HE21 1 
ATOM   18724 H HE22 . GLN   B  1 452 ? 67.485 3.914   -34.894 0.00 35.83  ? 478  GLN   B HE22 1 
ATOM   18725 N N    . CYS   B  1 453 ? 68.784 -3.148  -34.875 1.00 23.62  ? 479  CYS   B N    1 
ATOM   18726 C CA   . CYS   B  1 453 ? 68.520 -4.579  -34.820 1.00 23.63  ? 479  CYS   B CA   1 
ATOM   18727 C C    . CYS   B  1 453 ? 69.692 -5.331  -35.465 1.00 24.16  ? 479  CYS   B C    1 
ATOM   18728 O O    . CYS   B  1 453 ? 70.246 -6.239  -34.840 1.00 25.24  ? 479  CYS   B O    1 
ATOM   18729 C CB   . CYS   B  1 453 ? 67.191 -4.874  -35.513 1.00 22.76  ? 479  CYS   B CB   1 
ATOM   18730 S SG   . CYS   B  1 453 ? 66.514 -6.529  -35.196 1.00 24.65  ? 479  CYS   B SG   1 
ATOM   18731 H H    . CYS   B  1 453 ? 68.309 -2.698  -35.651 0.00 25.94  ? 479  CYS   B H    1 
ATOM   18732 H HA   . CYS   B  1 453 ? 68.431 -4.905  -33.784 0.00 26.57  ? 479  CYS   B HA   1 
ATOM   18733 H HB2  . CYS   B  1 453 ? 66.485 -4.149  -35.113 0.00 24.76  ? 479  CYS   B HB2  1 
ATOM   18734 H HB3  . CYS   B  1 453 ? 67.302 -4.742  -36.587 0.00 24.81  ? 479  CYS   B HB3  1 
ATOM   18735 N N    . ALA   B  1 454 ? 70.110 -4.929  -36.680 1.00 23.77  ? 480  ALA   B N    1 
ATOM   18736 C CA   . ALA   B  1 454 ? 71.223 -5.580  -37.370 1.00 24.09  ? 480  ALA   B CA   1 
ATOM   18737 C C    . ALA   B  1 454 ? 72.547 -5.515  -36.594 1.00 24.16  ? 480  ALA   B C    1 
ATOM   18738 O O    . ALA   B  1 454 ? 73.339 -6.442  -36.718 1.00 23.97  ? 480  ALA   B O    1 
ATOM   18739 C CB   . ALA   B  1 454 ? 71.405 -4.989  -38.766 1.00 24.15  ? 480  ALA   B CB   1 
ATOM   18740 H H    . ALA   B  1 454 ? 69.700 -4.162  -37.202 0.00 26.43  ? 480  ALA   B H    1 
ATOM   18741 H HA   . ALA   B  1 454 ? 70.975 -6.633  -37.493 0.00 27.51  ? 480  ALA   B HA   1 
ATOM   18742 H HB1  . ALA   B  1 454 ? 72.251 -5.478  -39.245 0.00 27.52  ? 480  ALA   B HB1  1 
ATOM   18743 H HB2  . ALA   B  1 454 ? 70.498 -5.159  -39.344 0.00 26.98  ? 480  ALA   B HB2  1 
ATOM   18744 H HB3  . ALA   B  1 454 ? 71.597 -3.921  -38.678 0.00 27.17  ? 480  ALA   B HB3  1 
ATOM   18745 N N    . ALA   B  1 455 ? 72.782 -4.448  -35.792 1.00 24.24  ? 481  ALA   B N    1 
ATOM   18746 C CA   . ALA   B  1 455 ? 74.006 -4.299  -34.982 1.00 24.83  ? 481  ALA   B CA   1 
ATOM   18747 C C    . ALA   B  1 455 ? 74.233 -5.465  -34.032 1.00 24.74  ? 481  ALA   B C    1 
ATOM   18748 O O    . ALA   B  1 455 ? 75.371 -5.707  -33.637 1.00 24.43  ? 481  ALA   B O    1 
ATOM   18749 C CB   . ALA   B  1 455 ? 73.948 -3.014  -34.168 1.00 25.16  ? 481  ALA   B CB   1 
ATOM   18750 H H    . ALA   B  1 455 ? 72.147 -3.664  -35.688 0.00 27.81  ? 481  ALA   B H    1 
ATOM   18751 H HA   . ALA   B  1 455 ? 74.865 -4.239  -35.649 0.00 29.46  ? 481  ALA   B HA   1 
ATOM   18752 H HB1  . ALA   B  1 455 ? 74.860 -2.926  -33.579 0.00 30.06  ? 481  ALA   B HB1  1 
ATOM   18753 H HB2  . ALA   B  1 455 ? 73.864 -2.169  -34.851 0.00 29.41  ? 481  ALA   B HB2  1 
ATOM   18754 H HB3  . ALA   B  1 455 ? 73.081 -3.049  -33.511 0.00 29.51  ? 481  ALA   B HB3  1 
ATOM   18755 N N    . TYR   B  1 456 ? 73.156 -6.163  -33.630 1.00 24.21  ? 482  TYR   B N    1 
ATOM   18756 C CA   . TYR   B  1 456 ? 73.268 -7.297  -32.728 1.00 24.25  ? 482  TYR   B CA   1 
ATOM   18757 C C    . TYR   B  1 456 ? 73.803 -8.565  -33.370 1.00 24.19  ? 482  TYR   B C    1 
ATOM   18758 O O    . TYR   B  1 456 ? 74.268 -9.435  -32.635 1.00 24.18  ? 482  TYR   B O    1 
ATOM   18759 C CB   . TYR   B  1 456 ? 71.918 -7.598  -32.053 1.00 24.37  ? 482  TYR   B CB   1 
ATOM   18760 C CG   . TYR   B  1 456 ? 71.626 -6.686  -30.889 1.00 25.80  ? 482  TYR   B CG   1 
ATOM   18761 C CD1  . TYR   B  1 456 ? 72.328 -6.805  -29.695 1.00 26.62  ? 482  TYR   B CD1  1 
ATOM   18762 C CD2  . TYR   B  1 456 ? 70.655 -5.702  -30.979 1.00 26.84  ? 482  TYR   B CD2  1 
ATOM   18763 C CE1  . TYR   B  1 456 ? 72.053 -5.982  -28.612 1.00 28.04  ? 482  TYR   B CE1  1 
ATOM   18764 C CE2  . TYR   B  1 456 ? 70.364 -4.875  -29.900 1.00 28.06  ? 482  TYR   B CE2  1 
ATOM   18765 C CZ   . TYR   B  1 456 ? 71.057 -5.026  -28.714 1.00 28.94  ? 482  TYR   B CZ   1 
ATOM   18766 O OH   . TYR   B  1 456 ? 70.775 -4.186  -27.674 1.00 30.39  ? 482  TYR   B OH   1 
ATOM   18767 H H    . TYR   B  1 456 ? 72.200 -5.946  -33.893 0.00 28.44  ? 482  TYR   B H    1 
ATOM   18768 H HA   . TYR   B  1 456 ? 73.999 -7.046  -31.960 0.00 29.64  ? 482  TYR   B HA   1 
ATOM   18769 H HB2  . TYR   B  1 456 ? 71.107 -7.517  -32.774 0.00 28.79  ? 482  TYR   B HB2  1 
ATOM   18770 H HB3  . TYR   B  1 456 ? 71.947 -8.612  -31.658 0.00 29.48  ? 482  TYR   B HB3  1 
ATOM   18771 H HD1  . TYR   B  1 456 ? 73.087 -7.564  -29.602 0.00 32.80  ? 482  TYR   B HD1  1 
ATOM   18772 H HD2  . TYR   B  1 456 ? 70.092 -5.593  -31.890 0.00 31.32  ? 482  TYR   B HD2  1 
ATOM   18773 H HE1  . TYR   B  1 456 ? 72.606 -6.104  -27.695 0.00 34.57  ? 482  TYR   B HE1  1 
ATOM   18774 H HE2  . TYR   B  1 456 ? 69.600 -4.120  -29.987 0.00 32.83  ? 482  TYR   B HE2  1 
ATOM   18775 H HH   . TYR   B  1 456 ? 71.380 -4.352  -26.904 0.00 36.96  ? 482  TYR   B HH   1 
ATOM   18776 N N    . GLY   B  1 457 ? 73.747 -8.685  -34.691 1.00 23.81  ? 483  GLY   B N    1 
ATOM   18777 C CA   . GLY   B  1 457 ? 74.253 -9.874  -35.361 1.00 23.78  ? 483  GLY   B CA   1 
ATOM   18778 C C    . GLY   B  1 457 ? 73.359 -10.309 -36.491 1.00 24.04  ? 483  GLY   B C    1 
ATOM   18779 O O    . GLY   B  1 457 ? 72.686 -9.476  -37.096 1.00 24.73  ? 483  GLY   B O    1 
ATOM   18780 H H    . GLY   B  1 457 ? 73.357 -7.999  -35.331 0.00 28.44  ? 483  GLY   B H    1 
ATOM   18781 H HA2  . GLY   B  1 457 ? 75.245 -9.671  -35.762 0.00 29.32  ? 483  GLY   B HA2  1 
ATOM   18782 H HA3  . GLY   B  1 457 ? 74.335 -10.707 -34.664 0.00 29.46  ? 483  GLY   B HA3  1 
ATOM   18783 N N    . LYS   B  1 458 ? 73.372 -11.613 -36.797 1.00 23.22  ? 484  LYS   B N    1 
ATOM   18784 C CA   . LYS   B  1 458 ? 72.611 -12.224 -37.893 1.00 23.51  ? 484  LYS   B CA   1 
ATOM   18785 C C    . LYS   B  1 458 ? 71.119 -11.830 -37.817 1.00 22.82  ? 484  LYS   B C    1 
ATOM   18786 O O    . LYS   B  1 458 ? 70.498 -11.992 -36.770 1.00 22.49  ? 484  LYS   B O    1 
ATOM   18787 C CB   . LYS   B  1 458 ? 72.725 -13.761 -37.798 1.00 27.08  ? 484  LYS   B CB   1 
ATOM   18788 C CG   . LYS   B  1 458 ? 73.139 -14.502 -39.037 1.00 34.17  ? 484  LYS   B CG   1 
ATOM   18789 C CD   . LYS   B  1 458 ? 74.034 -15.699 -38.721 1.00 37.61  ? 484  LYS   B CD   1 
ATOM   18790 C CE   . LYS   B  1 458 ? 75.503 -15.358 -38.700 1.00 40.26  ? 484  LYS   B CE   1 
ATOM   18791 N NZ   . LYS   B  1 458 ? 76.359 -16.566 -38.744 1.00 39.34  ? 484  LYS   B NZ   1 
ATOM   18792 H H    . LYS   B  1 458 ? 73.947 -12.274 -36.285 0.00 28.81  ? 484  LYS   B H    1 
ATOM   18793 H HA   . LYS   B  1 458 ? 73.017 -11.859 -38.836 0.00 28.43  ? 484  LYS   B HA   1 
ATOM   18794 H HB2  . LYS   B  1 458 ? 73.423 -14.041 -37.010 0.00 33.74  ? 484  LYS   B HB2  1 
ATOM   18795 H HB3  . LYS   B  1 458 ? 71.740 -14.152 -37.559 0.00 33.28  ? 484  LYS   B HB3  1 
ATOM   18796 H HG2  . LYS   B  1 458 ? 72.243 -14.887 -39.522 0.00 41.73  ? 484  LYS   B HG2  1 
ATOM   18797 H HG3  . LYS   B  1 458 ? 73.673 -13.844 -39.718 0.00 41.81  ? 484  LYS   B HG3  1 
ATOM   18798 H HD2  . LYS   B  1 458 ? 73.755 -16.135 -37.763 0.00 46.98  ? 484  LYS   B HD2  1 
ATOM   18799 H HD3  . LYS   B  1 458 ? 73.882 -16.427 -39.516 0.00 46.85  ? 484  LYS   B HD3  1 
ATOM   18800 H HE2  . LYS   B  1 458 ? 75.753 -14.744 -39.564 0.00 50.28  ? 484  LYS   B HE2  1 
ATOM   18801 H HE3  . LYS   B  1 458 ? 75.725 -14.820 -37.780 0.00 50.14  ? 484  LYS   B HE3  1 
ATOM   18802 H HZ1  . LYS   B  1 458 ? 77.293 -16.310 -39.049 0.00 50.21  ? 484  LYS   B HZ1  1 
ATOM   18803 H HZ2  . LYS   B  1 458 ? 76.425 -16.974 -37.817 0.00 50.04  ? 484  LYS   B HZ2  1 
ATOM   18804 H HZ3  . LYS   B  1 458 ? 75.983 -17.258 -39.384 0.00 50.13  ? 484  LYS   B HZ3  1 
ATOM   18805 N N    . ALA   B  1 459 ? 70.563 -11.321 -38.928 1.00 22.07  ? 485  ALA   B N    1 
ATOM   18806 C CA   . ALA   B  1 459 ? 69.188 -10.867 -38.972 1.00 21.10  ? 485  ALA   B CA   1 
ATOM   18807 C C    . ALA   B  1 459 ? 68.342 -11.658 -39.947 1.00 20.30  ? 485  ALA   B C    1 
ATOM   18808 O O    . ALA   B  1 459 ? 68.778 -11.963 -41.062 1.00 20.29  ? 485  ALA   B O    1 
ATOM   18809 C CB   . ALA   B  1 459 ? 69.148 -9.400  -39.331 1.00 20.84  ? 485  ALA   B CB   1 
ATOM   18810 H H    . ALA   B  1 459 ? 71.044 -11.210 -39.814 0.00 25.88  ? 485  ALA   B H    1 
ATOM   18811 H HA   . ALA   B  1 459 ? 68.740 -10.961 -37.985 0.00 24.23  ? 485  ALA   B HA   1 
ATOM   18812 H HB1  . ALA   B  1 459 ? 68.116 -9.055  -39.294 0.00 23.20  ? 485  ALA   B HB1  1 
ATOM   18813 H HB2  . ALA   B  1 459 ? 69.755 -8.843  -38.620 0.00 23.62  ? 485  ALA   B HB2  1 
ATOM   18814 H HB3  . ALA   B  1 459 ? 69.552 -9.275  -40.334 0.00 23.49  ? 485  ALA   B HB3  1 
ATOM   18815 N N    . LEU   B  1 460 ? 67.107 -11.953 -39.528 1.00 18.89  ? 486  LEU   B N    1 
ATOM   18816 C CA   . LEU   B  1 460 ? 66.127 -12.657 -40.337 1.00 18.55  ? 486  LEU   B CA   1 
ATOM   18817 C C    . LEU   B  1 460 ? 64.871 -11.806 -40.332 1.00 17.62  ? 486  LEU   B C    1 
ATOM   18818 O O    . LEU   B  1 460 ? 64.284 -11.592 -39.273 1.00 17.73  ? 486  LEU   B O    1 
ATOM   18819 C CB   . LEU   B  1 460 ? 65.844 -14.028 -39.723 1.00 19.35  ? 486  LEU   B CB   1 
ATOM   18820 C CG   . LEU   B  1 460 ? 64.701 -14.847 -40.358 1.00 21.46  ? 486  LEU   B CG   1 
ATOM   18821 C CD1  . LEU   B  1 460 ? 64.958 -15.088 -41.869 1.00 21.78  ? 486  LEU   B CD1  1 
ATOM   18822 C CD2  . LEU   B  1 460 ? 64.577 -16.163 -39.659 1.00 22.87  ? 486  LEU   B CD2  1 
ATOM   18823 H H    . LEU   B  1 460 ? 66.743 -11.703 -38.615 0.00 21.25  ? 486  LEU   B H    1 
ATOM   18824 H HA   . LEU   B  1 460 ? 66.474 -12.786 -41.361 0.00 20.89  ? 486  LEU   B HA   1 
ATOM   18825 H HB2  . LEU   B  1 460 ? 66.750 -14.627 -39.797 0.00 22.56  ? 486  LEU   B HB2  1 
ATOM   18826 H HB3  . LEU   B  1 460 ? 65.595 -13.882 -38.673 0.00 22.18  ? 486  LEU   B HB3  1 
ATOM   18827 H HG   . LEU   B  1 460 ? 63.751 -14.325 -40.246 0.00 24.39  ? 486  LEU   B HG   1 
ATOM   18828 H HD11 . LEU   B  1 460 ? 64.259 -15.843 -42.226 0.00 25.26  ? 486  LEU   B HD11 1 
ATOM   18829 H HD12 . LEU   B  1 460 ? 64.804 -14.155 -42.410 0.00 24.82  ? 486  LEU   B HD12 1 
ATOM   18830 H HD13 . LEU   B  1 460 ? 65.982 -15.433 -42.005 0.00 25.47  ? 486  LEU   B HD13 1 
ATOM   18831 H HD21 . LEU   B  1 460 ? 63.680 -16.673 -40.006 0.00 26.84  ? 486  LEU   B HD21 1 
ATOM   18832 H HD22 . LEU   B  1 460 ? 65.461 -16.748 -39.908 0.00 27.21  ? 486  LEU   B HD22 1 
ATOM   18833 H HD23 . LEU   B  1 460 ? 64.525 -16.000 -38.582 0.00 26.87  ? 486  LEU   B HD23 1 
ATOM   18834 N N    . ASP   B  1 461 ? 64.485 -11.280 -41.493 1.00 17.29  ? 487  ASP   B N    1 
ATOM   18835 C CA   . ASP   B  1 461 ? 63.298 -10.443 -41.594 1.00 17.49  ? 487  ASP   B CA   1 
ATOM   18836 C C    . ASP   B  1 461 ? 62.176 -11.206 -42.291 1.00 17.35  ? 487  ASP   B C    1 
ATOM   18837 O O    . ASP   B  1 461 ? 62.240 -11.439 -43.491 1.00 17.52  ? 487  ASP   B O    1 
ATOM   18838 C CB   . ASP   B  1 461 ? 63.629 -9.122  -42.314 1.00 20.03  ? 487  ASP   B CB   1 
ATOM   18839 C CG   . ASP   B  1 461 ? 62.516 -8.090  -42.282 1.00 23.30  ? 487  ASP   B CG   1 
ATOM   18840 O OD1  . ASP   B  1 461 ? 61.344 -8.482  -42.156 1.00 22.39  ? 487  ASP   B OD1  1 
ATOM   18841 O OD2  . ASP   B  1 461 ? 62.822 -6.893  -42.385 1.00 27.68  ? 487  ASP   B OD2  1 
ATOM   18842 H H    . ASP   B  1 461 ? 64.965 -11.411 -42.377 0.00 18.68  ? 487  ASP   B H    1 
ATOM   18843 H HA   . ASP   B  1 461 ? 62.958 -10.188 -40.594 0.00 18.35  ? 487  ASP   B HA   1 
ATOM   18844 H HB2  . ASP   B  1 461 ? 64.509 -8.679  -41.851 0.00 21.24  ? 487  ASP   B HB2  1 
ATOM   18845 H HB3  . ASP   B  1 461 ? 63.826 -9.330  -43.363 0.00 21.23  ? 487  ASP   B HB3  1 
ATOM   18846 N N    . LEU   B  1 462 ? 61.166 -11.614 -41.527 1.00 17.20  ? 488  LEU   B N    1 
ATOM   18847 C CA   . LEU   B  1 462 ? 59.984 -12.319 -42.030 1.00 17.73  ? 488  LEU   B CA   1 
ATOM   18848 C C    . LEU   B  1 462 ? 58.728 -11.450 -41.872 1.00 17.64  ? 488  LEU   B C    1 
ATOM   18849 O O    . LEU   B  1 462 ? 57.604 -11.986 -41.775 1.00 18.22  ? 488  LEU   B O    1 
ATOM   18850 C CB   . LEU   B  1 462 ? 59.820 -13.646 -41.261 1.00 18.68  ? 488  LEU   B CB   1 
ATOM   18851 C CG   . LEU   B  1 462 ? 60.784 -14.768 -41.649 1.00 20.59  ? 488  LEU   B CG   1 
ATOM   18852 C CD1  . LEU   B  1 462 ? 60.878 -15.800 -40.532 1.00 21.19  ? 488  LEU   B CD1  1 
ATOM   18853 C CD2  . LEU   B  1 462 ? 60.363 -15.433 -42.966 1.00 21.15  ? 488  LEU   B CD2  1 
ATOM   18854 H H    . LEU   B  1 462 ? 61.128 -11.466 -40.523 0.00 18.07  ? 488  LEU   B H    1 
ATOM   18855 H HA   . LEU   B  1 462 ? 60.090 -12.536 -43.091 0.00 18.81  ? 488  LEU   B HA   1 
ATOM   18856 H HB2  . LEU   B  1 462 ? 59.966 -13.452 -40.199 0.00 20.26  ? 488  LEU   B HB2  1 
ATOM   18857 H HB3  . LEU   B  1 462 ? 58.819 -14.044 -41.419 0.00 20.27  ? 488  LEU   B HB3  1 
ATOM   18858 H HG   . LEU   B  1 462 ? 61.782 -14.358 -41.790 0.00 23.00  ? 488  LEU   B HG   1 
ATOM   18859 H HD11 . LEU   B  1 462 ? 61.507 -16.624 -40.867 0.00 24.45  ? 488  LEU   B HD11 1 
ATOM   18860 H HD12 . LEU   B  1 462 ? 61.320 -15.332 -39.653 0.00 24.05  ? 488  LEU   B HD12 1 
ATOM   18861 H HD13 . LEU   B  1 462 ? 59.879 -16.165 -40.299 0.00 24.10  ? 488  LEU   B HD13 1 
ATOM   18862 H HD21 . LEU   B  1 462 ? 61.065 -16.233 -43.192 0.00 24.17  ? 488  LEU   B HD21 1 
ATOM   18863 H HD22 . LEU   B  1 462 ? 59.361 -15.846 -42.856 0.00 23.85  ? 488  LEU   B HD22 1 
ATOM   18864 H HD23 . LEU   B  1 462 ? 60.368 -14.704 -43.773 0.00 23.59  ? 488  LEU   B HD23 1 
ATOM   18865 N N    . SER   B  1 463 ? 58.894 -10.096 -41.879 1.00 16.70  ? 489  SER   B N    1 
ATOM   18866 C CA   . SER   B  1 463 ? 57.770 -9.209  -41.714 1.00 16.92  ? 489  SER   B CA   1 
ATOM   18867 C C    . SER   B  1 463 ? 56.849 -9.278  -42.900 1.00 17.07  ? 489  SER   B C    1 
ATOM   18868 O O    . SER   B  1 463 ? 57.278 -9.635  -43.996 1.00 15.86  ? 489  SER   B O    1 
ATOM   18869 C CB   . SER   B  1 463 ? 58.229 -7.768  -41.516 1.00 18.28  ? 489  SER   B CB   1 
ATOM   18870 O OG   . SER   B  1 463 ? 58.995 -7.271  -42.605 1.00 20.38  ? 489  SER   B OG   1 
ATOM   18871 H H    . SER   B  1 463 ? 59.775 -9.609  -42.012 0.00 16.81  ? 489  SER   B H    1 
ATOM   18872 H HA   . SER   B  1 463 ? 57.208 -9.505  -40.829 0.00 16.86  ? 489  SER   B HA   1 
ATOM   18873 H HB2  . SER   B  1 463 ? 57.353 -7.134  -41.388 0.00 18.00  ? 489  SER   B HB2  1 
ATOM   18874 H HB3  . SER   B  1 463 ? 58.830 -7.753  -40.610 0.00 18.27  ? 489  SER   B HB3  1 
ATOM   18875 H HG   . SER   B  1 463 ? 59.897 -7.685  -42.608 0.00 20.81  ? 489  SER   B HG   1 
ATOM   18876 N N    . LEU   B  1 464 ? 55.567 -8.937  -42.685 1.00 17.03  ? 490  LEU   B N    1 
ATOM   18877 C CA   . LEU   B  1 464 ? 54.600 -8.896  -43.776 1.00 17.59  ? 490  LEU   B CA   1 
ATOM   18878 C C    . LEU   B  1 464 ? 54.471 -10.225 -44.505 1.00 17.62  ? 490  LEU   B C    1 
ATOM   18879 O O    . LEU   B  1 464 ? 54.503 -10.287 -45.728 1.00 19.02  ? 490  LEU   B O    1 
ATOM   18880 C CB   . LEU   B  1 464 ? 54.915 -7.727  -44.732 1.00 18.19  ? 490  LEU   B CB   1 
ATOM   18881 C CG   . LEU   B  1 464 ? 54.861 -6.316  -44.070 1.00 20.32  ? 490  LEU   B CG   1 
ATOM   18882 C CD1  . LEU   B  1 464 ? 55.744 -5.333  -44.808 1.00 20.53  ? 490  LEU   B CD1  1 
ATOM   18883 C CD2  . LEU   B  1 464 ? 53.432 -5.806  -44.006 1.00 21.28  ? 490  LEU   B CD2  1 
ATOM   18884 H H    . LEU   B  1 464 ? 55.183 -8.685  -41.781 0.00 16.68  ? 490  LEU   B H    1 
ATOM   18885 H HA   . LEU   B  1 464 ? 53.627 -8.688  -43.335 0.00 17.32  ? 490  LEU   B HA   1 
ATOM   18886 H HB2  . LEU   B  1 464 ? 55.911 -7.858  -45.152 0.00 17.96  ? 490  LEU   B HB2  1 
ATOM   18887 H HB3  . LEU   B  1 464 ? 54.177 -7.726  -45.533 0.00 17.91  ? 490  LEU   B HB3  1 
ATOM   18888 H HG   . LEU   B  1 464 ? 55.236 -6.356  -43.049 0.00 20.18  ? 490  LEU   B HG   1 
ATOM   18889 H HD11 . LEU   B  1 464 ? 55.664 -4.357  -44.332 0.00 20.14  ? 490  LEU   B HD11 1 
ATOM   18890 H HD12 . LEU   B  1 464 ? 56.774 -5.682  -44.766 0.00 20.40  ? 490  LEU   B HD12 1 
ATOM   18891 H HD13 . LEU   B  1 464 ? 55.415 -5.271  -45.845 0.00 20.31  ? 490  LEU   B HD13 1 
ATOM   18892 H HD21 . LEU   B  1 464 ? 53.430 -4.828  -43.528 0.00 21.06  ? 490  LEU   B HD21 1 
ATOM   18893 H HD22 . LEU   B  1 464 ? 53.034 -5.727  -45.016 0.00 21.23  ? 490  LEU   B HD22 1 
ATOM   18894 H HD23 . LEU   B  1 464 ? 52.830 -6.502  -43.424 0.00 21.32  ? 490  LEU   B HD23 1 
ATOM   18895 N N    . ASN   B  1 465 ? 54.325 -11.295 -43.735 1.00 17.01  ? 491  ASN   B N    1 
ATOM   18896 C CA   . ASN   B  1 465 ? 54.066 -12.625 -44.274 1.00 16.94  ? 491  ASN   B CA   1 
ATOM   18897 C C    . ASN   B  1 465 ? 52.749 -13.105 -43.594 1.00 17.66  ? 491  ASN   B C    1 
ATOM   18898 O O    . ASN   B  1 465 ? 51.968 -12.258 -43.138 1.00 17.41  ? 491  ASN   B O    1 
ATOM   18899 C CB   . ASN   B  1 465 ? 55.305 -13.531 -44.047 1.00 16.65  ? 491  ASN   B CB   1 
ATOM   18900 C CG   . ASN   B  1 465 ? 56.356 -13.346 -45.114 1.00 19.21  ? 491  ASN   B CG   1 
ATOM   18901 O OD1  . ASN   B  1 465 ? 56.200 -13.857 -46.213 1.00 20.70  ? 491  ASN   B OD1  1 
ATOM   18902 N ND2  . ASN   B  1 465 ? 57.422 -12.612 -44.844 1.00 18.00  ? 491  ASN   B ND2  1 
ATOM   18903 H H    . ASN   B  1 465 ? 54.371 -11.281 -42.721 0.00 17.22  ? 491  ASN   B H    1 
ATOM   18904 H HA   . ASN   B  1 465 ? 53.854 -12.579 -45.341 0.00 17.56  ? 491  ASN   B HA   1 
ATOM   18905 H HB2  . ASN   B  1 465 ? 55.747 -13.285 -43.082 0.00 17.39  ? 491  ASN   B HB2  1 
ATOM   18906 H HB3  . ASN   B  1 465 ? 55.037 -14.586 -44.061 0.00 17.77  ? 491  ASN   B HB3  1 
ATOM   18907 H HD21 . ASN   B  1 465 ? 58.135 -12.480 -45.556 0.00 18.98  ? 491  ASN   B HD21 1 
ATOM   18908 H HD22 . ASN   B  1 465 ? 57.530 -12.166 -43.940 0.00 18.81  ? 491  ASN   B HD22 1 
ATOM   18909 N N    . SER   B  1 466 ? 52.460 -14.416 -43.595 1.00 18.29  ? 492  SER   B N    1 
ATOM   18910 C CA   . SER   B  1 466 ? 51.256 -14.969 -42.993 1.00 20.46  ? 492  SER   B CA   1 
ATOM   18911 C C    . SER   B  1 466 ? 51.630 -16.058 -41.974 1.00 21.24  ? 492  SER   B C    1 
ATOM   18912 O O    . SER   B  1 466 ? 51.001 -17.112 -41.943 1.00 21.40  ? 492  SER   B O    1 
ATOM   18913 C CB   . SER   B  1 466 ? 50.354 -15.524 -44.089 1.00 22.50  ? 492  SER   B CB   1 
ATOM   18914 O OG   . SER   B  1 466 ? 49.909 -14.463 -44.917 1.00 26.67  ? 492  SER   B OG   1 
ATOM   18915 H H    . SER   B  1 466 ? 53.016 -15.133 -44.049 0.00 19.87  ? 492  SER   B H    1 
ATOM   18916 H HA   . SER   B  1 466 ? 50.702 -14.202 -42.454 0.00 22.15  ? 492  SER   B HA   1 
ATOM   18917 H HB2  . SER   B  1 466 ? 50.912 -16.242 -44.689 0.00 25.33  ? 492  SER   B HB2  1 
ATOM   18918 H HB3  . SER   B  1 466 ? 49.481 -15.999 -43.645 0.00 25.24  ? 492  SER   B HB3  1 
ATOM   18919 H HG   . SER   B  1 466 ? 49.106 -14.746 -45.429 0.00 29.96  ? 492  SER   B HG   1 
ATOM   18920 N N    . ILE   B  1 467 ? 52.645 -15.803 -41.125 1.00 21.65  ? 493  ILE   B N    1 
ATOM   18921 C CA   . ILE   B  1 467 ? 53.036 -16.774 -40.092 1.00 22.36  ? 493  ILE   B CA   1 
ATOM   18922 C C    . ILE   B  1 467 ? 52.114 -16.453 -38.920 1.00 23.19  ? 493  ILE   B C    1 
ATOM   18923 O O    . ILE   B  1 467 ? 52.535 -15.848 -37.937 1.00 23.25  ? 493  ILE   B O    1 
ATOM   18924 C CB   . ILE   B  1 467 ? 54.558 -16.685 -39.756 1.00 22.82  ? 493  ILE   B CB   1 
ATOM   18925 C CG1  . ILE   B  1 467 ? 55.406 -16.800 -41.054 1.00 23.94  ? 493  ILE   B CG1  1 
ATOM   18926 C CG2  . ILE   B  1 467 ? 54.968 -17.780 -38.739 1.00 22.99  ? 493  ILE   B CG2  1 
ATOM   18927 C CD1  . ILE   B  1 467 ? 56.946 -16.632 -40.823 1.00 25.51  ? 493  ILE   B CD1  1 
ATOM   18928 H H    . ILE   B  1 467 ? 53.194 -14.949 -41.117 0.00 23.79  ? 493  ILE   B H    1 
ATOM   18929 H HA   . ILE   B  1 467 ? 52.835 -17.791 -40.423 0.00 25.57  ? 493  ILE   B HA   1 
ATOM   18930 H HB   . ILE   B  1 467 ? 54.761 -15.712 -39.312 0.00 25.51  ? 493  ILE   B HB   1 
ATOM   18931 H HG12 . ILE   B  1 467 ? 55.240 -17.781 -41.497 0.00 27.55  ? 493  ILE   B HG12 1 
ATOM   18932 H HG13 . ILE   B  1 467 ? 55.106 -16.023 -41.756 0.00 26.95  ? 493  ILE   B HG13 1 
ATOM   18933 H HG21 . ILE   B  1 467 ? 55.988 -17.600 -38.403 0.00 26.46  ? 493  ILE   B HG21 1 
ATOM   18934 H HG22 . ILE   B  1 467 ? 54.301 -17.758 -37.879 0.00 26.42  ? 493  ILE   B HG22 1 
ATOM   18935 H HG23 . ILE   B  1 467 ? 54.907 -18.751 -39.227 0.00 26.77  ? 493  ILE   B HG23 1 
ATOM   18936 H HD11 . ILE   B  1 467 ? 57.430 -16.540 -41.794 0.00 29.14  ? 493  ILE   B HD11 1 
ATOM   18937 H HD12 . ILE   B  1 467 ? 57.123 -15.736 -40.229 0.00 28.88  ? 493  ILE   B HD12 1 
ATOM   18938 H HD13 . ILE   B  1 467 ? 57.332 -17.508 -40.305 0.00 29.49  ? 493  ILE   B HD13 1 
ATOM   18939 N N    A PHE   B  1 468 ? 50.828 -16.814 -39.056 0.50 23.52  ? 494  PHE   B N    1 
ATOM   18940 N N    B PHE   B  1 468 ? 50.836 -16.842 -39.047 0.50 23.76  ? 494  PHE   B N    1 
ATOM   18941 C CA   A PHE   B  1 468 ? 49.823 -16.523 -38.032 0.50 24.20  ? 494  PHE   B CA   1 
ATOM   18942 C CA   B PHE   B  1 468 ? 49.821 -16.555 -38.022 0.50 24.69  ? 494  PHE   B CA   1 
ATOM   18943 C C    A PHE   B  1 468 ? 50.002 -17.325 -36.729 0.50 25.47  ? 494  PHE   B C    1 
ATOM   18944 C C    B PHE   B  1 468 ? 50.063 -17.291 -36.708 0.50 25.69  ? 494  PHE   B C    1 
ATOM   18945 O O    A PHE   B  1 468 ? 49.378 -16.985 -35.727 0.50 25.25  ? 494  PHE   B O    1 
ATOM   18946 O O    B PHE   B  1 468 ? 49.486 -16.913 -35.691 0.50 25.48  ? 494  PHE   B O    1 
ATOM   18947 C CB   A PHE   B  1 468 ? 48.386 -16.685 -38.582 0.50 23.76  ? 494  PHE   B CB   1 
ATOM   18948 C CB   B PHE   B  1 468 ? 48.395 -16.935 -38.468 0.50 24.65  ? 494  PHE   B CB   1 
ATOM   18949 C CG   A PHE   B  1 468 ? 47.998 -18.061 -39.076 0.50 24.01  ? 494  PHE   B CG   1 
ATOM   18950 C CG   B PHE   B  1 468 ? 48.060 -16.885 -39.935 0.50 25.35  ? 494  PHE   B CG   1 
ATOM   18951 C CD1  A PHE   B  1 468 ? 47.463 -19.002 -38.214 0.50 24.48  ? 494  PHE   B CD1  1 
ATOM   18952 C CD1  B PHE   B  1 468 ? 47.959 -18.046 -40.677 0.50 26.34  ? 494  PHE   B CD1  1 
ATOM   18953 C CD2  A PHE   B  1 468 ? 48.134 -18.400 -40.411 0.50 24.64  ? 494  PHE   B CD2  1 
ATOM   18954 C CD2  B PHE   B  1 468 ? 47.828 -15.682 -40.564 0.50 26.27  ? 494  PHE   B CD2  1 
ATOM   18955 C CE1  A PHE   B  1 468 ? 47.087 -20.259 -38.677 0.50 24.93  ? 494  PHE   B CE1  1 
ATOM   18956 C CE1  B PHE   B  1 468 ? 47.625 -17.999 -42.021 0.50 27.29  ? 494  PHE   B CE1  1 
ATOM   18957 C CE2  A PHE   B  1 468 ? 47.761 -19.659 -40.869 0.50 25.21  ? 494  PHE   B CE2  1 
ATOM   18958 C CE2  B PHE   B  1 468 ? 47.474 -15.636 -41.907 0.50 26.96  ? 494  PHE   B CE2  1 
ATOM   18959 C CZ   A PHE   B  1 468 ? 47.243 -20.580 -39.998 0.50 24.79  ? 494  PHE   B CZ   1 
ATOM   18960 C CZ   B PHE   B  1 468 ? 47.377 -16.794 -42.626 0.50 26.92  ? 494  PHE   B CZ   1 
ATOM   18961 H H    A PHE   B  1 468 ? 50.471 -17.295 -39.875 0.00 26.78  ? 494  PHE   B H    1 
ATOM   18962 H H    B PHE   B  1 468 ? 50.511 -17.394 -39.834 0.00 27.11  ? 494  PHE   B H    1 
ATOM   18963 H HA   A PHE   B  1 468 ? 49.932 -15.467 -37.795 0.00 27.05  ? 494  PHE   B HA   1 
ATOM   18964 H HA   B PHE   B  1 468 ? 49.835 -15.483 -37.837 0.00 27.64  ? 494  PHE   B HA   1 
ATOM   18965 H HB2  A PHE   B  1 468 ? 47.688 -16.420 -37.789 0.00 26.87  ? 494  PHE   B HB2  1 
ATOM   18966 H HB2  B PHE   B  1 468 ? 48.197 -17.949 -38.124 0.00 28.42  ? 494  PHE   B HB2  1 
ATOM   18967 H HB3  A PHE   B  1 468 ? 48.261 -15.996 -39.416 0.00 26.70  ? 494  PHE   B HB3  1 
ATOM   18968 H HB3  B PHE   B  1 468 ? 47.705 -16.255 -37.970 0.00 27.87  ? 494  PHE   B HB3  1 
ATOM   18969 H HD1  A PHE   B  1 468 ? 47.336 -18.757 -37.173 0.00 28.55  ? 494  PHE   B HD1  1 
ATOM   18970 H HD1  B PHE   B  1 468 ? 48.148 -18.999 -40.212 0.00 30.84  ? 494  PHE   B HD1  1 
ATOM   18971 H HD2  A PHE   B  1 468 ? 48.544 -17.683 -41.103 0.00 28.33  ? 494  PHE   B HD2  1 
ATOM   18972 H HD2  B PHE   B  1 468 ? 47.854 -14.796 -39.974 0.00 29.38  ? 494  PHE   B HD2  1 
ATOM   18973 H HE1  A PHE   B  1 468 ? 46.680 -20.984 -37.992 0.00 29.96  ? 494  PHE   B HE1  1 
ATOM   18974 H HE1  B PHE   B  1 468 ? 47.564 -18.910 -42.592 0.00 32.09  ? 494  PHE   B HE1  1 
ATOM   18975 H HE2  A PHE   B  1 468 ? 47.884 -19.913 -41.908 0.00 29.89  ? 494  PHE   B HE2  1 
ATOM   18976 H HE2  B PHE   B  1 468 ? 47.279 -14.689 -42.382 0.00 30.29  ? 494  PHE   B HE2  1 
ATOM   18977 H HZ   A PHE   B  1 468 ? 46.956 -21.555 -40.352 0.00 30.03  ? 494  PHE   B HZ   1 
ATOM   18978 H HZ   B PHE   B  1 468 ? 47.130 -16.759 -43.674 0.00 30.99  ? 494  PHE   B HZ   1 
ATOM   18979 N N    . PHE   B  1 469 ? 50.827 -18.387 -36.747 1.00 26.69  ? 495  PHE   B N    1 
ATOM   18980 C CA   . PHE   B  1 469 ? 51.080 -19.226 -35.588 1.00 29.43  ? 495  PHE   B CA   1 
ATOM   18981 C C    . PHE   B  1 469 ? 52.484 -19.792 -35.719 1.00 30.76  ? 495  PHE   B C    1 
ATOM   18982 O O    . PHE   B  1 469 ? 52.834 -20.328 -36.778 1.00 30.88  ? 495  PHE   B O    1 
ATOM   18983 C CB   . PHE   B  1 469 ? 50.067 -20.382 -35.574 1.00 30.39  ? 495  PHE   B CB   1 
ATOM   18984 C CG   . PHE   B  1 469 ? 50.242 -21.339 -34.420 1.00 32.54  ? 495  PHE   B CG   1 
ATOM   18985 C CD1  . PHE   B  1 469 ? 49.762 -21.023 -33.159 1.00 33.60  ? 495  PHE   B CD1  1 
ATOM   18986 C CD2  . PHE   B  1 469 ? 50.851 -22.569 -34.603 1.00 33.78  ? 495  PHE   B CD2  1 
ATOM   18987 C CE1  . PHE   B  1 469 ? 49.897 -21.916 -32.104 1.00 34.49  ? 495  PHE   B CE1  1 
ATOM   18988 C CE2  . PHE   B  1 469 ? 51.004 -23.451 -33.538 1.00 34.53  ? 495  PHE   B CE2  1 
ATOM   18989 C CZ   . PHE   B  1 469 ? 50.548 -23.110 -32.293 1.00 34.33  ? 495  PHE   B CZ   1 
ATOM   18990 H H    . PHE   B  1 469 ? 51.305 -18.722 -37.576 0.00 31.13  ? 495  PHE   B H    1 
ATOM   18991 H HA   . PHE   B  1 469 ? 51.005 -18.668 -34.656 0.00 34.54  ? 495  PHE   B HA   1 
ATOM   18992 H HB2  . PHE   B  1 469 ? 49.063 -19.965 -35.508 0.00 36.11  ? 495  PHE   B HB2  1 
ATOM   18993 H HB3  . PHE   B  1 469 ? 50.168 -20.947 -36.500 0.00 36.44  ? 495  PHE   B HB3  1 
ATOM   18994 H HD1  . PHE   B  1 469 ? 49.269 -20.080 -32.999 0.00 40.18  ? 495  PHE   B HD1  1 
ATOM   18995 H HD2  . PHE   B  1 469 ? 51.234 -22.838 -35.573 0.00 41.32  ? 495  PHE   B HD2  1 
ATOM   18996 H HE1  . PHE   B  1 469 ? 49.539 -21.648 -31.125 0.00 42.03  ? 495  PHE   B HE1  1 
ATOM   18997 H HE2  . PHE   B  1 469 ? 51.497 -24.397 -33.690 0.00 43.03  ? 495  PHE   B HE2  1 
ATOM   18998 H HZ   . PHE   B  1 469 ? 50.651 -23.801 -31.474 0.00 42.72  ? 495  PHE   B HZ   1 
ATOM   18999 N N    . ILE   B  1 470 ? 53.285 -19.675 -34.651 1.00 30.90  ? 496  ILE   B N    1 
ATOM   19000 C CA   . ILE   B  1 470 ? 54.641 -20.196 -34.623 1.00 31.36  ? 496  ILE   B CA   1 
ATOM   19001 C C    . ILE   B  1 470 ? 54.549 -21.583 -34.003 1.00 32.54  ? 496  ILE   B C    1 
ATOM   19002 O O    . ILE   B  1 470 ? 54.273 -21.704 -32.807 1.00 32.03  ? 496  ILE   B O    1 
ATOM   19003 C CB   . ILE   B  1 470 ? 55.582 -19.265 -33.816 1.00 31.53  ? 496  ILE   B CB   1 
ATOM   19004 C CG1  . ILE   B  1 470 ? 55.644 -17.853 -34.460 1.00 32.63  ? 496  ILE   B CG1  1 
ATOM   19005 C CG2  . ILE   B  1 470 ? 56.973 -19.886 -33.706 1.00 31.61  ? 496  ILE   B CG2  1 
ATOM   19006 C CD1  . ILE   B  1 470 ? 56.176 -16.772 -33.551 1.00 34.03  ? 496  ILE   B CD1  1 
ATOM   19007 H H    . ILE   B  1 470 ? 53.022 -19.224 -33.780 0.00 36.64  ? 496  ILE   B H    1 
ATOM   19008 H HA   . ILE   B  1 470 ? 55.043 -20.271 -35.632 0.00 37.57  ? 496  ILE   B HA   1 
ATOM   19009 H HB   . ILE   B  1 470 ? 55.181 -19.164 -32.809 0.00 37.61  ? 496  ILE   B HB   1 
ATOM   19010 H HG12 . ILE   B  1 470 ? 56.299 -17.899 -35.329 0.00 38.33  ? 496  ILE   B HG12 1 
ATOM   19011 H HG13 . ILE   B  1 470 ? 54.649 -17.543 -34.775 0.00 38.13  ? 496  ILE   B HG13 1 
ATOM   19012 H HG21 . ILE   B  1 470 ? 57.642 -19.165 -33.241 0.00 37.90  ? 496  ILE   B HG21 1 
ATOM   19013 H HG22 . ILE   B  1 470 ? 56.938 -20.781 -33.086 0.00 38.46  ? 496  ILE   B HG22 1 
ATOM   19014 H HG23 . ILE   B  1 470 ? 57.325 -20.134 -34.706 0.00 38.09  ? 496  ILE   B HG23 1 
ATOM   19015 H HD11 . ILE   B  1 470 ? 55.923 -15.802 -33.977 0.00 39.41  ? 496  ILE   B HD11 1 
ATOM   19016 H HD12 . ILE   B  1 470 ? 55.721 -16.876 -32.568 0.00 39.89  ? 496  ILE   B HD12 1 
ATOM   19017 H HD13 . ILE   B  1 470 ? 57.257 -16.872 -33.474 0.00 39.93  ? 496  ILE   B HD13 1 
ATOM   19018 N N    . GLY   B  1 471 ? 54.729 -22.603 -34.836 1.00 33.79  ? 497  GLY   B N    1 
ATOM   19019 C CA   . GLY   B  1 471 ? 54.710 -23.999 -34.421 1.00 35.48  ? 497  GLY   B CA   1 
ATOM   19020 C C    . GLY   B  1 471 ? 56.064 -24.446 -33.902 1.00 37.03  ? 497  GLY   B C    1 
ATOM   19021 O O    . GLY   B  1 471 ? 57.067 -23.743 -34.074 1.00 37.13  ? 497  GLY   B O    1 
ATOM   19022 H H    . GLY   B  1 471 ? 54.889 -22.500 -35.833 0.00 41.36  ? 497  GLY   B H    1 
ATOM   19023 H HA2  . GLY   B  1 471 ? 53.961 -24.139 -33.643 0.00 44.19  ? 497  GLY   B HA2  1 
ATOM   19024 H HA3  . GLY   B  1 471 ? 54.445 -24.626 -35.271 0.00 44.32  ? 497  GLY   B HA3  1 
ATOM   19025 N N    . PRO   B  1 472 ? 56.137 -25.647 -33.304 1.00 38.20  ? 498  PRO   B N    1 
ATOM   19026 C CA   . PRO   B  1 472 ? 57.415 -26.102 -32.730 1.00 38.79  ? 498  PRO   B CA   1 
ATOM   19027 C C    . PRO   B  1 472 ? 58.600 -26.254 -33.688 1.00 38.98  ? 498  PRO   B C    1 
ATOM   19028 O O    . PRO   B  1 472 ? 59.723 -26.223 -33.199 1.00 40.02  ? 498  PRO   B O    1 
ATOM   19029 C CB   . PRO   B  1 472 ? 57.063 -27.449 -32.078 1.00 39.85  ? 498  PRO   B CB   1 
ATOM   19030 C CG   . PRO   B  1 472 ? 55.760 -27.860 -32.667 1.00 40.21  ? 498  PRO   B CG   1 
ATOM   19031 C CD   . PRO   B  1 472 ? 55.042 -26.592 -33.007 1.00 38.28  ? 498  PRO   B CD   1 
ATOM   19032 H HA   . PRO   B  1 472 ? 57.710 -25.413 -31.938 0.00 49.27  ? 498  PRO   B HA   1 
ATOM   19033 H HB2  . PRO   B  1 472 ? 57.835 -28.181 -32.310 0.00 51.88  ? 498  PRO   B HB2  1 
ATOM   19034 H HB3  . PRO   B  1 472 ? 56.971 -27.314 -31.000 0.00 51.48  ? 498  PRO   B HB3  1 
ATOM   19035 H HG2  . PRO   B  1 472 ? 55.935 -28.451 -33.564 0.00 52.12  ? 498  PRO   B HG2  1 
ATOM   19036 H HG3  . PRO   B  1 472 ? 55.194 -28.432 -31.934 0.00 52.18  ? 498  PRO   B HG3  1 
ATOM   19037 H HD2  . PRO   B  1 472 ? 54.415 -26.746 -33.884 0.00 48.78  ? 498  PRO   B HD2  1 
ATOM   19038 H HD3  . PRO   B  1 472 ? 54.460 -26.244 -32.154 0.00 48.69  ? 498  PRO   B HD3  1 
ATOM   19039 N N    . ASN   B  1 473 ? 58.393 -26.377 -35.015 1.00 38.20  ? 499  ASN   B N    1 
ATOM   19040 C CA   . ASN   B  1 473 ? 59.504 -26.525 -35.972 1.00 37.73  ? 499  ASN   B CA   1 
ATOM   19041 C C    . ASN   B  1 473 ? 59.753 -25.285 -36.838 1.00 36.55  ? 499  ASN   B C    1 
ATOM   19042 O O    . ASN   B  1 473 ? 60.599 -25.353 -37.728 1.00 36.53  ? 499  ASN   B O    1 
ATOM   19043 C CB   . ASN   B  1 473 ? 59.236 -27.710 -36.909 1.00 39.55  ? 499  ASN   B CB   1 
ATOM   19044 C CG   . ASN   B  1 473 ? 58.889 -28.983 -36.183 1.00 44.25  ? 499  ASN   B CG   1 
ATOM   19045 O OD1  . ASN   B  1 473 ? 59.481 -29.308 -35.147 1.00 46.13  ? 499  ASN   B OD1  1 
ATOM   19046 N ND2  . ASN   B  1 473 ? 57.915 -29.730 -36.694 1.00 45.23  ? 499  ASN   B ND2  1 
ATOM   19047 H H    . ASN   B  1 473 ? 57.481 -26.382 -35.460 0.00 48.68  ? 499  ASN   B H    1 
ATOM   19048 H HA   . ASN   B  1 473 ? 60.431 -26.745 -35.444 0.00 48.69  ? 499  ASN   B HA   1 
ATOM   19049 H HB2  . ASN   B  1 473 ? 58.410 -27.445 -37.567 0.00 50.81  ? 499  ASN   B HB2  1 
ATOM   19050 H HB3  . ASN   B  1 473 ? 60.130 -27.911 -37.497 0.00 51.28  ? 499  ASN   B HB3  1 
ATOM   19051 H HD21 . ASN   B  1 473 ? 57.652 -30.595 -36.232 0.00 59.29  ? 499  ASN   B HD21 1 
ATOM   19052 H HD22 . ASN   B  1 473 ? 57.433 -29.449 -37.542 0.00 58.58  ? 499  ASN   B HD22 1 
ATOM   19053 N N    . GLN   B  1 474 ? 59.054 -24.161 -36.595 1.00 35.16  ? 500  GLN   B N    1 
ATOM   19054 C CA   . GLN   B  1 474 ? 59.187 -22.961 -37.429 1.00 34.30  ? 500  GLN   B CA   1 
ATOM   19055 C C    . GLN   B  1 474 ? 60.624 -22.471 -37.611 1.00 33.63  ? 500  GLN   B C    1 
ATOM   19056 O O    . GLN   B  1 474 ? 61.001 -22.117 -38.726 1.00 33.30  ? 500  GLN   B O    1 
ATOM   19057 C CB   . GLN   B  1 474 ? 58.330 -21.810 -36.856 1.00 35.20  ? 500  GLN   B CB   1 
ATOM   19058 C CG   . GLN   B  1 474 ? 58.282 -20.541 -37.714 1.00 37.22  ? 500  GLN   B CG   1 
ATOM   19059 C CD   . GLN   B  1 474 ? 57.676 -20.799 -39.079 1.00 39.29  ? 500  GLN   B CD   1 
ATOM   19060 O OE1  . GLN   B  1 474 ? 56.544 -21.273 -39.186 1.00 39.65  ? 500  GLN   B OE1  1 
ATOM   19061 N NE2  . GLN   B  1 474 ? 58.409 -20.512 -40.156 1.00 39.70  ? 500  GLN   B NE2  1 
ATOM   19062 H H    . GLN   B  1 474 ? 58.400 -24.036 -35.828 0.00 44.01  ? 500  GLN   B H    1 
ATOM   19063 H HA   . GLN   B  1 474 ? 58.800 -23.217 -38.414 0.00 42.52  ? 500  GLN   B HA   1 
ATOM   19064 H HB2  . GLN   B  1 474 ? 57.307 -22.161 -36.735 0.00 43.05  ? 500  GLN   B HB2  1 
ATOM   19065 H HB3  . GLN   B  1 474 ? 58.742 -21.536 -35.886 0.00 43.01  ? 500  GLN   B HB3  1 
ATOM   19066 H HG2  . GLN   B  1 474 ? 57.646 -19.814 -37.212 0.00 44.54  ? 500  GLN   B HG2  1 
ATOM   19067 H HG3  . GLN   B  1 474 ? 59.280 -20.120 -37.830 0.00 44.81  ? 500  GLN   B HG3  1 
ATOM   19068 H HE21 . GLN   B  1 474 ? 59.345 -20.132 -40.064 0.00 47.70  ? 500  GLN   B HE21 1 
ATOM   19069 H HE22 . GLN   B  1 474 ? 58.026 -20.679 -41.082 0.00 47.76  ? 500  GLN   B HE22 1 
ATOM   19070 N N    . PHE   B  1 475 ? 61.404 -22.406 -36.524 1.00 33.28  ? 501  PHE   B N    1 
ATOM   19071 C CA   . PHE   B  1 475 ? 62.761 -21.859 -36.576 1.00 33.75  ? 501  PHE   B CA   1 
ATOM   19072 C C    . PHE   B  1 475 ? 63.868 -22.912 -36.493 1.00 34.59  ? 501  PHE   B C    1 
ATOM   19073 O O    . PHE   B  1 475 ? 65.005 -22.589 -36.143 1.00 35.04  ? 501  PHE   B O    1 
ATOM   19074 C CB   . PHE   B  1 475 ? 62.904 -20.796 -35.469 1.00 33.47  ? 501  PHE   B CB   1 
ATOM   19075 C CG   . PHE   B  1 475 ? 61.903 -19.677 -35.638 1.00 33.93  ? 501  PHE   B CG   1 
ATOM   19076 C CD1  . PHE   B  1 475 ? 61.886 -18.911 -36.791 1.00 34.63  ? 501  PHE   B CD1  1 
ATOM   19077 C CD2  . PHE   B  1 475 ? 60.973 -19.400 -34.653 1.00 34.64  ? 501  PHE   B CD2  1 
ATOM   19078 C CE1  . PHE   B  1 475 ? 60.958 -17.892 -36.956 1.00 34.97  ? 501  PHE   B CE1  1 
ATOM   19079 C CE2  . PHE   B  1 475 ? 60.056 -18.367 -34.818 1.00 35.15  ? 501  PHE   B CE2  1 
ATOM   19080 C CZ   . PHE   B  1 475 ? 60.050 -17.630 -35.970 1.00 34.65  ? 501  PHE   B CZ   1 
ATOM   19081 H H    . PHE   B  1 475 ? 61.127 -22.722 -35.600 0.00 41.57  ? 501  PHE   B H    1 
ATOM   19082 H HA   . PHE   B  1 475 ? 62.901 -21.352 -37.528 0.00 41.71  ? 501  PHE   B HA   1 
ATOM   19083 H HB2  . PHE   B  1 475 ? 62.737 -21.267 -34.501 0.00 41.58  ? 501  PHE   B HB2  1 
ATOM   19084 H HB3  . PHE   B  1 475 ? 63.899 -20.354 -35.501 0.00 41.32  ? 501  PHE   B HB3  1 
ATOM   19085 H HD1  . PHE   B  1 475 ? 62.591 -19.119 -37.579 0.00 41.81  ? 501  PHE   B HD1  1 
ATOM   19086 H HD2  . PHE   B  1 475 ? 60.969 -19.970 -33.739 0.00 42.26  ? 501  PHE   B HD2  1 
ATOM   19087 H HE1  . PHE   B  1 475 ? 60.954 -17.312 -37.864 0.00 41.29  ? 501  PHE   B HE1  1 
ATOM   19088 H HE2  . PHE   B  1 475 ? 59.346 -18.151 -34.040 0.00 41.92  ? 501  PHE   B HE2  1 
ATOM   19089 H HZ   . PHE   B  1 475 ? 59.329 -16.845 -36.104 0.00 40.66  ? 501  PHE   B HZ   1 
ATOM   19090 N N    . GLU   B  1 476 ? 63.563 -24.144 -36.889 1.00 34.79  ? 502  GLU   B N    1 
ATOM   19091 C CA   . GLU   B  1 476 ? 64.533 -25.230 -36.863 1.00 35.96  ? 502  GLU   B CA   1 
ATOM   19092 C C    . GLU   B  1 476 ? 65.567 -25.047 -37.981 1.00 35.85  ? 502  GLU   B C    1 
ATOM   19093 O O    . GLU   B  1 476 ? 65.239 -24.505 -39.039 1.00 35.44  ? 502  GLU   B O    1 
ATOM   19094 C CB   . GLU   B  1 476 ? 63.808 -26.569 -37.057 1.00 39.62  ? 502  GLU   B CB   1 
ATOM   19095 C CG   . GLU   B  1 476 ? 64.680 -27.792 -36.827 1.00 47.77  ? 502  GLU   B CG   1 
ATOM   19096 C CD   . GLU   B  1 476 ? 63.979 -29.121 -37.029 1.00 58.04  ? 502  GLU   B CD   1 
ATOM   19097 O OE1  . GLU   B  1 476 ? 62.851 -29.131 -37.575 1.00 60.89  ? 502  GLU   B OE1  1 
ATOM   19098 O OE2  . GLU   B  1 476 ? 64.569 -30.158 -36.647 1.00 60.92  ? 502  GLU   B OE2  1 
ATOM   19099 H H    . GLU   B  1 476 ? 62.657 -24.422 -37.253 0.00 44.27  ? 502  GLU   B H    1 
ATOM   19100 H HA   . GLU   B  1 476 ? 65.044 -25.247 -35.901 0.00 46.65  ? 502  GLU   B HA   1 
ATOM   19101 H HB2  . GLU   B  1 476 ? 62.976 -26.622 -36.356 0.00 51.24  ? 502  GLU   B HB2  1 
ATOM   19102 H HB3  . GLU   B  1 476 ? 63.434 -26.610 -38.079 0.00 51.22  ? 502  GLU   B HB3  1 
ATOM   19103 H HG2  . GLU   B  1 476 ? 65.521 -27.774 -37.518 0.00 62.05  ? 502  GLU   B HG2  1 
ATOM   19104 H HG3  . GLU   B  1 476 ? 65.049 -27.768 -35.803 0.00 62.08  ? 502  GLU   B HG3  1 
ATOM   19105 N N    . ASN   B  1 477 ? 66.808 -25.516 -37.741 1.00 35.69  ? 503  ASN   B N    1 
ATOM   19106 C CA   . ASN   B  1 477 ? 67.904 -25.497 -38.716 1.00 35.85  ? 503  ASN   B CA   1 
ATOM   19107 C C    . ASN   B  1 477 ? 68.305 -24.088 -39.187 1.00 35.20  ? 503  ASN   B C    1 
ATOM   19108 O O    . ASN   B  1 477 ? 68.855 -23.924 -40.274 1.00 35.27  ? 503  ASN   B O    1 
ATOM   19109 C CB   . ASN   B  1 477 ? 67.534 -26.369 -39.921 1.00 37.87  ? 503  ASN   B CB   1 
ATOM   19110 C CG   . ASN   B  1 477 ? 67.041 -27.743 -39.541 1.00 42.32  ? 503  ASN   B CG   1 
ATOM   19111 O OD1  . ASN   B  1 477 ? 67.645 -28.422 -38.705 1.00 43.73  ? 503  ASN   B OD1  1 
ATOM   19112 N ND2  . ASN   B  1 477 ? 65.925 -28.182 -40.126 1.00 43.62  ? 503  ASN   B ND2  1 
ATOM   19113 H H    . ASN   B  1 477 ? 67.086 -25.925 -36.854 0.00 47.05  ? 503  ASN   B H    1 
ATOM   19114 H HA   . ASN   B  1 477 ? 68.782 -25.944 -38.251 0.00 47.56  ? 503  ASN   B HA   1 
ATOM   19115 H HB2  . ASN   B  1 477 ? 66.762 -25.859 -40.496 0.00 49.32  ? 503  ASN   B HB2  1 
ATOM   19116 H HB3  . ASN   B  1 477 ? 68.419 -26.509 -40.540 0.00 50.04  ? 503  ASN   B HB3  1 
ATOM   19117 H HD21 . ASN   B  1 477 ? 65.566 -29.103 -39.891 0.00 57.66  ? 503  ASN   B HD21 1 
ATOM   19118 H HD22 . ASN   B  1 477 ? 65.430 -27.612 -40.804 0.00 56.81  ? 503  ASN   B HD22 1 
ATOM   19119 N N    . LEU   B  1 478 ? 68.078 -23.088 -38.346 1.00 33.96  ? 504  LEU   B N    1 
ATOM   19120 C CA   . LEU   B  1 478 ? 68.385 -21.699 -38.657 1.00 33.20  ? 504  LEU   B CA   1 
ATOM   19121 C C    . LEU   B  1 478 ? 69.748 -21.352 -38.058 1.00 31.98  ? 504  LEU   B C    1 
ATOM   19122 O O    . LEU   B  1 478 ? 70.118 -21.940 -37.041 1.00 32.04  ? 504  LEU   B O    1 
ATOM   19123 C CB   . LEU   B  1 478 ? 67.291 -20.818 -38.006 1.00 33.63  ? 504  LEU   B CB   1 
ATOM   19124 C CG   . LEU   B  1 478 ? 66.577 -19.715 -38.792 1.00 35.34  ? 504  LEU   B CG   1 
ATOM   19125 C CD1  . LEU   B  1 478 ? 66.302 -20.104 -40.219 1.00 36.05  ? 504  LEU   B CD1  1 
ATOM   19126 C CD2  . LEU   B  1 478 ? 65.276 -19.388 -38.130 1.00 35.61  ? 504  LEU   B CD2  1 
ATOM   19127 H H    . LEU   B  1 478 ? 67.733 -23.215 -37.401 0.00 43.81  ? 504  LEU   B H    1 
ATOM   19128 H HA   . LEU   B  1 478 ? 68.410 -21.547 -39.734 0.00 42.14  ? 504  LEU   B HA   1 
ATOM   19129 H HB2  . LEU   B  1 478 ? 66.490 -21.463 -37.649 0.00 42.32  ? 504  LEU   B HB2  1 
ATOM   19130 H HB3  . LEU   B  1 478 ? 67.746 -20.328 -37.146 0.00 42.21  ? 504  LEU   B HB3  1 
ATOM   19131 H HG   . LEU   B  1 478 ? 67.184 -18.812 -38.789 0.00 43.41  ? 504  LEU   B HG   1 
ATOM   19132 H HD11 . LEU   B  1 478 ? 65.453 -19.534 -40.594 0.00 44.01  ? 504  LEU   B HD11 1 
ATOM   19133 H HD12 . LEU   B  1 478 ? 67.184 -19.895 -40.822 0.00 44.53  ? 504  LEU   B HD12 1 
ATOM   19134 H HD13 . LEU   B  1 478 ? 66.087 -21.171 -40.224 0.00 44.82  ? 504  LEU   B HD13 1 
ATOM   19135 H HD21 . LEU   B  1 478 ? 64.977 -18.372 -38.383 0.00 43.10  ? 504  LEU   B HD21 1 
ATOM   19136 H HD22 . LEU   B  1 478 ? 64.525 -20.086 -38.493 0.00 43.62  ? 504  LEU   B HD22 1 
ATOM   19137 H HD23 . LEU   B  1 478 ? 65.391 -19.479 -37.051 0.00 43.72  ? 504  LEU   B HD23 1 
ATOM   19138 N N    . PRO   B  1 479 ? 70.513 -20.396 -38.630 1.00 30.93  ? 505  PRO   B N    1 
ATOM   19139 C CA   . PRO   B  1 479 ? 71.762 -19.986 -37.956 1.00 29.93  ? 505  PRO   B CA   1 
ATOM   19140 C C    . PRO   B  1 479 ? 71.457 -19.245 -36.630 1.00 28.70  ? 505  PRO   B C    1 
ATOM   19141 O O    . PRO   B  1 479 ? 70.283 -19.107 -36.250 1.00 28.61  ? 505  PRO   B O    1 
ATOM   19142 C CB   . PRO   B  1 479 ? 72.467 -19.113 -38.999 1.00 30.89  ? 505  PRO   B CB   1 
ATOM   19143 C CG   . PRO   B  1 479 ? 71.409 -18.646 -39.927 1.00 31.67  ? 505  PRO   B CG   1 
ATOM   19144 C CD   . PRO   B  1 479 ? 70.217 -19.554 -39.810 1.00 30.14  ? 505  PRO   B CD   1 
ATOM   19145 H HA   . PRO   B  1 479 ? 72.389 -20.852 -37.748 0.00 39.19  ? 505  PRO   B HA   1 
ATOM   19146 H HB2  . PRO   B  1 479 ? 72.944 -18.269 -38.505 0.00 39.44  ? 505  PRO   B HB2  1 
ATOM   19147 H HB3  . PRO   B  1 479 ? 73.207 -19.707 -39.531 0.00 39.93  ? 505  PRO   B HB3  1 
ATOM   19148 H HG2  . PRO   B  1 479 ? 71.127 -17.631 -39.652 0.00 39.46  ? 505  PRO   B HG2  1 
ATOM   19149 H HG3  . PRO   B  1 479 ? 71.794 -18.657 -40.946 0.00 39.82  ? 505  PRO   B HG3  1 
ATOM   19150 H HD2  . PRO   B  1 479 ? 69.318 -18.965 -39.644 0.00 37.70  ? 505  PRO   B HD2  1 
ATOM   19151 H HD3  . PRO   B  1 479 ? 70.127 -20.171 -40.703 0.00 38.36  ? 505  PRO   B HD3  1 
ATOM   19152 N N    . ASP   B  1 480 ? 72.497 -18.814 -35.893 1.00 27.50  ? 506  ASP   B N    1 
ATOM   19153 C CA   . ASP   B  1 480 ? 72.317 -18.118 -34.618 1.00 27.38  ? 506  ASP   B CA   1 
ATOM   19154 C C    . ASP   B  1 480 ? 71.751 -16.728 -34.876 1.00 25.60  ? 506  ASP   B C    1 
ATOM   19155 O O    . ASP   B  1 480 ? 72.504 -15.760 -35.000 1.00 26.57  ? 506  ASP   B O    1 
ATOM   19156 C CB   . ASP   B  1 480 ? 73.654 -18.045 -33.839 1.00 30.33  ? 506  ASP   B CB   1 
ATOM   19157 C CG   . ASP   B  1 480 ? 73.553 -17.389 -32.466 1.00 36.87  ? 506  ASP   B CG   1 
ATOM   19158 O OD1  . ASP   B  1 480 ? 72.473 -16.858 -32.135 1.00 38.21  ? 506  ASP   B OD1  1 
ATOM   19159 O OD2  . ASP   B  1 480 ? 74.556 -17.399 -31.731 1.00 39.18  ? 506  ASP   B OD2  1 
ATOM   19160 H H    . ASP   B  1 480 ? 73.470 -18.932 -36.158 0.00 36.02  ? 506  ASP   B H    1 
ATOM   19161 H HA   . ASP   B  1 480 ? 71.607 -18.669 -34.005 0.00 35.49  ? 506  ASP   B HA   1 
ATOM   19162 H HB2  . ASP   B  1 480 ? 74.014 -19.061 -33.684 0.00 40.02  ? 506  ASP   B HB2  1 
ATOM   19163 H HB3  . ASP   B  1 480 ? 74.386 -17.491 -34.425 0.00 39.43  ? 506  ASP   B HB3  1 
ATOM   19164 N N    . ILE   B  1 481 ? 70.420 -16.633 -34.967 1.00 22.90  ? 507  ILE   B N    1 
ATOM   19165 C CA   . ILE   B  1 481 ? 69.754 -15.372 -35.244 1.00 21.79  ? 507  ILE   B CA   1 
ATOM   19166 C C    . ILE   B  1 481 ? 69.768 -14.486 -34.012 1.00 21.30  ? 507  ILE   B C    1 
ATOM   19167 O O    . ILE   B  1 481 ? 69.336 -14.924 -32.951 1.00 22.41  ? 507  ILE   B O    1 
ATOM   19168 C CB   . ILE   B  1 481 ? 68.311 -15.610 -35.761 1.00 21.75  ? 507  ILE   B CB   1 
ATOM   19169 C CG1  . ILE   B  1 481 ? 68.295 -16.460 -37.076 1.00 22.87  ? 507  ILE   B CG1  1 
ATOM   19170 C CG2  . ILE   B  1 481 ? 67.587 -14.286 -35.959 1.00 21.61  ? 507  ILE   B CG2  1 
ATOM   19171 C CD1  . ILE   B  1 481 ? 69.049 -15.866 -38.287 1.00 23.96  ? 507  ILE   B CD1  1 
ATOM   19172 H H    . ILE   B  1 481 ? 69.785 -17.414 -34.843 0.00 29.00  ? 507  ILE   B H    1 
ATOM   19173 H HA   . ILE   B  1 481 ? 70.295 -14.848 -36.028 0.00 26.81  ? 507  ILE   B HA   1 
ATOM   19174 H HB   . ILE   B  1 481 ? 67.772 -16.170 -34.998 0.00 26.66  ? 507  ILE   B HB   1 
ATOM   19175 H HG12 . ILE   B  1 481 ? 68.735 -17.433 -36.867 0.00 28.45  ? 507  ILE   B HG12 1 
ATOM   19176 H HG13 . ILE   B  1 481 ? 67.259 -16.601 -37.382 0.00 27.75  ? 507  ILE   B HG13 1 
ATOM   19177 H HG21 . ILE   B  1 481 ? 66.761 -14.433 -36.654 0.00 25.49  ? 507  ILE   B HG21 1 
ATOM   19178 H HG22 . ILE   B  1 481 ? 67.190 -13.944 -35.004 0.00 25.65  ? 507  ILE   B HG22 1 
ATOM   19179 H HG23 . ILE   B  1 481 ? 68.284 -13.551 -36.359 0.00 25.62  ? 507  ILE   B HG23 1 
ATOM   19180 H HD11 . ILE   B  1 481 ? 68.831 -16.475 -39.163 0.00 29.22  ? 507  ILE   B HD11 1 
ATOM   19181 H HD12 . ILE   B  1 481 ? 68.722 -14.842 -38.457 0.00 28.71  ? 507  ILE   B HD12 1 
ATOM   19182 H HD13 . ILE   B  1 481 ? 70.120 -15.889 -38.089 0.00 29.45  ? 507  ILE   B HD13 1 
ATOM   19183 N N    . ALA   B  1 482 ? 70.244 -13.239 -34.163 1.00 20.38  ? 508  ALA   B N    1 
ATOM   19184 C CA   . ALA   B  1 482 ? 70.278 -12.208 -33.126 1.00 20.31  ? 508  ALA   B CA   1 
ATOM   19185 C C    . ALA   B  1 482 ? 69.162 -11.160 -33.320 1.00 20.42  ? 508  ALA   B C    1 
ATOM   19186 O O    . ALA   B  1 482 ? 68.745 -10.519 -32.353 1.00 19.88  ? 508  ALA   B O    1 
ATOM   19187 C CB   . ALA   B  1 482 ? 71.613 -11.494 -33.176 1.00 20.21  ? 508  ALA   B CB   1 
ATOM   19188 H H    . ALA   B  1 482 ? 70.628 -12.897 -35.038 0.00 24.76  ? 508  ALA   B H    1 
ATOM   19189 H HA   . ALA   B  1 482 ? 70.182 -12.651 -32.137 0.00 24.97  ? 508  ALA   B HA   1 
ATOM   19190 H HB1  . ALA   B  1 482 ? 71.688 -10.825 -32.320 0.00 24.78  ? 508  ALA   B HB1  1 
ATOM   19191 H HB2  . ALA   B  1 482 ? 72.411 -12.235 -33.142 0.00 25.23  ? 508  ALA   B HB2  1 
ATOM   19192 H HB3  . ALA   B  1 482 ? 71.676 -10.923 -34.102 0.00 24.50  ? 508  ALA   B HB3  1 
ATOM   19193 N N    . CYS   B  1 483 ? 68.739 -10.929 -34.566 1.00 20.27  ? 509  CYS   B N    1 
ATOM   19194 C CA   . CYS   B  1 483 ? 67.757 -9.903  -34.900 1.00 20.74  ? 509  CYS   B CA   1 
ATOM   19195 C C    . CYS   B  1 483 ? 66.644 -10.583 -35.682 1.00 21.20  ? 509  CYS   B C    1 
ATOM   19196 O O    . CYS   B  1 483 ? 66.902 -11.146 -36.746 1.00 21.24  ? 509  CYS   B O    1 
ATOM   19197 C CB   . CYS   B  1 483 ? 68.453 -8.802  -35.701 1.00 21.63  ? 509  CYS   B CB   1 
ATOM   19198 S SG   . CYS   B  1 483 ? 67.353 -7.699  -36.627 1.00 25.10  ? 509  CYS   B SG   1 
ATOM   19199 H H    . CYS   B  1 483 ? 69.066 -11.427 -35.388 0.00 23.77  ? 509  CYS   B H    1 
ATOM   19200 H HA   . CYS   B  1 483 ? 67.333 -9.452  -34.005 0.00 23.62  ? 509  CYS   B HA   1 
ATOM   19201 H HB2  . CYS   B  1 483 ? 69.030 -8.184  -35.014 0.00 24.69  ? 509  CYS   B HB2  1 
ATOM   19202 H HB3  . CYS   B  1 483 ? 69.126 -9.268  -36.418 0.00 24.74  ? 509  CYS   B HB3  1 
ATOM   19203 N N    . LEU   B  1 484 ? 65.409 -10.578 -35.147 1.00 20.22  ? 510  LEU   B N    1 
ATOM   19204 C CA   . LEU   B  1 484 ? 64.299 -11.269 -35.789 1.00 19.78  ? 510  LEU   B CA   1 
ATOM   19205 C C    . LEU   B  1 484 ? 63.124 -10.336 -35.937 1.00 19.66  ? 510  LEU   B C    1 
ATOM   19206 O O    . LEU   B  1 484 ? 62.675 -9.746  -34.953 1.00 19.90  ? 510  LEU   B O    1 
ATOM   19207 C CB   . LEU   B  1 484 ? 63.887 -12.483 -34.940 1.00 20.18  ? 510  LEU   B CB   1 
ATOM   19208 C CG   . LEU   B  1 484 ? 62.677 -13.299 -35.436 1.00 22.09  ? 510  LEU   B CG   1 
ATOM   19209 C CD1  . LEU   B  1 484 ? 62.939 -13.883 -36.852 1.00 22.43  ? 510  LEU   B CD1  1 
ATOM   19210 C CD2  . LEU   B  1 484 ? 62.355 -14.424 -34.454 1.00 22.43  ? 510  LEU   B CD2  1 
ATOM   19211 H H    . LEU   B  1 484 ? 65.156 -10.112 -34.283 0.00 22.63  ? 510  LEU   B H    1 
ATOM   19212 H HA   . LEU   B  1 484 ? 64.588 -11.621 -36.777 0.00 22.04  ? 510  LEU   B HA   1 
ATOM   19213 H HB2  . LEU   B  1 484 ? 64.735 -13.164 -34.889 0.00 23.18  ? 510  LEU   B HB2  1 
ATOM   19214 H HB3  . LEU   B  1 484 ? 63.648 -12.130 -33.938 0.00 22.82  ? 510  LEU   B HB3  1 
ATOM   19215 H HG   . LEU   B  1 484 ? 61.794 -12.664 -35.492 0.00 24.73  ? 510  LEU   B HG   1 
ATOM   19216 H HD11 . LEU   B  1 484 ? 62.138 -14.575 -37.107 0.00 25.60  ? 510  LEU   B HD11 1 
ATOM   19217 H HD12 . LEU   B  1 484 ? 62.959 -13.070 -37.577 0.00 25.25  ? 510  LEU   B HD12 1 
ATOM   19218 H HD13 . LEU   B  1 484 ? 63.895 -14.404 -36.850 0.00 25.87  ? 510  LEU   B HD13 1 
ATOM   19219 H HD21 . LEU   B  1 484 ? 61.597 -15.074 -34.888 0.00 25.87  ? 510  LEU   B HD21 1 
ATOM   19220 H HD22 . LEU   B  1 484 ? 63.264 -14.991 -34.261 0.00 26.22  ? 510  LEU   B HD22 1 
ATOM   19221 H HD23 . LEU   B  1 484 ? 61.981 -13.996 -33.526 0.00 25.79  ? 510  LEU   B HD23 1 
ATOM   19222 N N    . ASN   B  1 485 ? 62.595 -10.229 -37.146 1.00 18.27  ? 511  ASN   B N    1 
ATOM   19223 C CA   . ASN   B  1 485 ? 61.439 -9.395  -37.388 1.00 17.99  ? 511  ASN   B CA   1 
ATOM   19224 C C    . ASN   B  1 485 ? 60.257 -10.249 -37.855 1.00 17.79  ? 511  ASN   B C    1 
ATOM   19225 O O    . ASN   B  1 485 ? 60.313 -10.861 -38.908 1.00 17.67  ? 511  ASN   B O    1 
ATOM   19226 C CB   . ASN   B  1 485 ? 61.781 -8.254  -38.355 1.00 19.03  ? 511  ASN   B CB   1 
ATOM   19227 C CG   . ASN   B  1 485 ? 60.726 -7.253  -38.546 1.00 20.83  ? 511  ASN   B CG   1 
ATOM   19228 O OD1  . ASN   B  1 485 ? 59.670 -7.303  -37.889 1.00 20.50  ? 511  ASN   B OD1  1 
ATOM   19229 N ND2  . ASN   B  1 485 ? 60.982 -6.202  -39.293 1.00 22.73  ? 511  ASN   B ND2  1 
ATOM   19230 H H    . ASN   B  1 485 ? 62.933 -10.703 -37.977 0.00 19.59  ? 511  ASN   B H    1 
ATOM   19231 H HA   . ASN   B  1 485 ? 61.130 -8.910  -36.465 0.00 18.71  ? 511  ASN   B HA   1 
ATOM   19232 H HB2  . ASN   B  1 485 ? 62.669 -7.738  -37.991 0.00 19.81  ? 511  ASN   B HB2  1 
ATOM   19233 H HB3  . ASN   B  1 485 ? 61.975 -8.668  -39.341 0.00 19.79  ? 511  ASN   B HB3  1 
ATOM   19234 H HD21 . ASN   B  1 485 ? 60.130 -6.385  -39.770 0.00 23.53  ? 511  ASN   B HD21 1 
ATOM   19235 H HD22 . ASN   B  1 485 ? 61.892 -6.027  -39.706 0.00 23.69  ? 511  ASN   B HD22 1 
ATOM   19236 N N    . LEU   B  1 486 ? 59.218 -10.336 -37.015 1.00 17.05  ? 512  LEU   B N    1 
ATOM   19237 C CA   . LEU   B  1 486 ? 57.969 -11.034 -37.316 1.00 18.13  ? 512  LEU   B CA   1 
ATOM   19238 C C    . LEU   B  1 486 ? 56.792 -10.022 -37.336 1.00 18.00  ? 512  LEU   B C    1 
ATOM   19239 O O    . LEU   B  1 486 ? 55.637 -10.400 -37.124 1.00 18.26  ? 512  LEU   B O    1 
ATOM   19240 C CB   . LEU   B  1 486 ? 57.720 -12.122 -36.263 1.00 19.51  ? 512  LEU   B CB   1 
ATOM   19241 C CG   . LEU   B  1 486 ? 58.661 -13.331 -36.327 1.00 22.62  ? 512  LEU   B CG   1 
ATOM   19242 C CD1  . LEU   B  1 486 ? 58.601 -14.114 -35.038 1.00 23.01  ? 512  LEU   B CD1  1 
ATOM   19243 C CD2  . LEU   B  1 486 ? 58.293 -14.259 -37.508 1.00 23.74  ? 512  LEU   B CD2  1 
ATOM   19244 H H    . LEU   B  1 486 ? 59.206 -9.918  -36.091 0.00 17.59  ? 512  LEU   B H    1 
ATOM   19245 H HA   . LEU   B  1 486 ? 58.009 -11.497 -38.300 0.00 18.97  ? 512  LEU   B HA   1 
ATOM   19246 H HB2  . LEU   B  1 486 ? 57.836 -11.672 -35.280 0.00 20.88  ? 512  LEU   B HB2  1 
ATOM   19247 H HB3  . LEU   B  1 486 ? 56.709 -12.511 -36.372 0.00 20.90  ? 512  LEU   B HB3  1 
ATOM   19248 H HG   . LEU   B  1 486 ? 59.686 -12.991 -36.468 0.00 25.06  ? 512  LEU   B HG   1 
ATOM   19249 H HD11 . LEU   B  1 486 ? 59.276 -14.965 -35.107 0.00 26.18  ? 512  LEU   B HD11 1 
ATOM   19250 H HD12 . LEU   B  1 486 ? 58.914 -13.470 -34.218 0.00 25.79  ? 512  LEU   B HD12 1 
ATOM   19251 H HD13 . LEU   B  1 486 ? 57.579 -14.454 -34.879 0.00 25.85  ? 512  LEU   B HD13 1 
ATOM   19252 H HD21 . LEU   B  1 486 ? 58.919 -15.148 -37.462 0.00 26.87  ? 512  LEU   B HD21 1 
ATOM   19253 H HD22 . LEU   B  1 486 ? 57.244 -14.544 -37.426 0.00 26.52  ? 512  LEU   B HD22 1 
ATOM   19254 H HD23 . LEU   B  1 486 ? 58.464 -13.743 -38.451 0.00 26.34  ? 512  LEU   B HD23 1 
ATOM   19255 N N    . SER   B  1 487 ? 57.077 -8.742  -37.624 1.00 17.03  ? 513  SER   B N    1 
ATOM   19256 C CA   . SER   B  1 487 ? 56.055 -7.716  -37.682 1.00 16.72  ? 513  SER   B CA   1 
ATOM   19257 C C    . SER   B  1 487 ? 55.016 -8.044  -38.745 1.00 17.03  ? 513  SER   B C    1 
ATOM   19258 O O    . SER   B  1 487 ? 55.371 -8.596  -39.784 1.00 17.00  ? 513  SER   B O    1 
ATOM   19259 C CB   . SER   B  1 487 ? 56.676 -6.369  -38.029 1.00 17.82  ? 513  SER   B CB   1 
ATOM   19260 O OG   . SER   B  1 487 ? 55.714 -5.337  -38.148 1.00 19.87  ? 513  SER   B OG   1 
ATOM   19261 H H    . SER   B  1 487 ? 58.008 -8.405  -37.847 0.00 16.98  ? 513  SER   B H    1 
ATOM   19262 H HA   . SER   B  1 487 ? 55.562 -7.641  -36.714 0.00 16.36  ? 513  SER   B HA   1 
ATOM   19263 H HB2  . SER   B  1 487 ? 57.380 -6.098  -37.244 0.00 17.50  ? 513  SER   B HB2  1 
ATOM   19264 H HB3  . SER   B  1 487 ? 57.202 -6.460  -38.978 0.00 17.43  ? 513  SER   B HB3  1 
ATOM   19265 H HG   . SER   B  1 487 ? 55.006 -5.447  -37.460 0.00 19.69  ? 513  SER   B HG   1 
ATOM   19266 N N    . ALA   B  1 488 ? 53.741 -7.699  -38.495 1.00 17.10  ? 514  ALA   B N    1 
ATOM   19267 C CA   . ALA   B  1 488 ? 52.659 -7.840  -39.486 1.00 17.25  ? 514  ALA   B CA   1 
ATOM   19268 C C    . ALA   B  1 488 ? 52.543 -9.228  -40.110 1.00 17.31  ? 514  ALA   B C    1 
ATOM   19269 O O    . ALA   B  1 488 ? 52.591 -9.386  -41.325 1.00 18.05  ? 514  ALA   B O    1 
ATOM   19270 C CB   . ALA   B  1 488 ? 52.793 -6.766  -40.573 1.00 17.93  ? 514  ALA   B CB   1 
ATOM   19271 H H    . ALA   B  1 488 ? 53.422 -7.317  -37.611 0.00 16.59  ? 514  ALA   B H    1 
ATOM   19272 H HA   . ALA   B  1 488 ? 51.717 -7.651  -38.975 0.00 16.74  ? 514  ALA   B HA   1 
ATOM   19273 H HB1  . ALA   B  1 488 ? 51.927 -6.808  -41.231 0.00 17.36  ? 514  ALA   B HB1  1 
ATOM   19274 H HB2  . ALA   B  1 488 ? 52.847 -5.789  -40.096 0.00 17.22  ? 514  ALA   B HB2  1 
ATOM   19275 H HB3  . ALA   B  1 488 ? 53.705 -6.946  -41.141 0.00 17.40  ? 514  ALA   B HB3  1 
ATOM   19276 N N    . ASN   B  1 489 ? 52.406 -10.236 -39.264 1.00 16.56  ? 515  ASN   B N    1 
ATOM   19277 C CA   . ASN   B  1 489 ? 52.169 -11.616 -39.679 1.00 16.66  ? 515  ASN   B CA   1 
ATOM   19278 C C    . ASN   B  1 489 ? 50.788 -12.114 -39.237 1.00 17.44  ? 515  ASN   B C    1 
ATOM   19279 O O    . ASN   B  1 489 ? 50.549 -13.321 -39.299 1.00 17.40  ? 515  ASN   B O    1 
ATOM   19280 C CB   . ASN   B  1 489 ? 53.275 -12.535 -39.119 1.00 16.72  ? 515  ASN   B CB   1 
ATOM   19281 C CG   . ASN   B  1 489 ? 54.456 -12.615 -40.056 1.00 18.57  ? 515  ASN   B CG   1 
ATOM   19282 O OD1  . ASN   B  1 489 ? 54.449 -13.407 -41.002 1.00 19.12  ? 515  ASN   B OD1  1 
ATOM   19283 N ND2  . ASN   B  1 489 ? 55.441 -11.762 -39.868 1.00 19.01  ? 515  ASN   B ND2  1 
ATOM   19284 H H    . ASN   B  1 489 ? 52.451 -10.122 -38.257 0.00 16.45  ? 515  ASN   B H    1 
ATOM   19285 H HA   . ASN   B  1 489 ? 52.148 -11.678 -40.766 0.00 16.87  ? 515  ASN   B HA   1 
ATOM   19286 H HB2  . ASN   B  1 489 ? 53.618 -12.146 -38.160 0.00 17.17  ? 515  ASN   B HB2  1 
ATOM   19287 H HB3  . ASN   B  1 489 ? 52.905 -13.550 -38.988 0.00 17.49  ? 515  ASN   B HB3  1 
ATOM   19288 H HD21 . ASN   B  1 489 ? 56.251 -11.788 -40.480 0.00 19.86  ? 515  ASN   B HD21 1 
ATOM   19289 H HD22 . ASN   B  1 489 ? 55.396 -11.073 -39.125 0.00 19.68  ? 515  ASN   B HD22 1 
ATOM   19290 N N    . SER   B  1 490 ? 49.873 -11.200 -38.831 1.00 18.07  ? 516  SER   B N    1 
ATOM   19291 C CA   . SER   B  1 490 ? 48.527 -11.523 -38.364 1.00 19.74  ? 516  SER   B CA   1 
ATOM   19292 C C    . SER   B  1 490 ? 48.546 -12.598 -37.275 1.00 20.64  ? 516  SER   B C    1 
ATOM   19293 O O    . SER   B  1 490 ? 47.642 -13.422 -37.193 1.00 20.92  ? 516  SER   B O    1 
ATOM   19294 C CB   A SER   B  1 490 ? 47.631 -11.934 -39.530 0.50 21.85  ? 516  SER   B CB   1 
ATOM   19295 C CB   B SER   B  1 490 ? 47.675 -11.939 -39.559 0.50 20.84  ? 516  SER   B CB   1 
ATOM   19296 O OG   A SER   B  1 490 ? 47.896 -13.232 -40.036 0.50 24.99  ? 516  SER   B OG   1 
ATOM   19297 O OG   B SER   B  1 490 ? 47.695 -10.942 -40.568 0.50 22.26  ? 516  SER   B OG   1 
ATOM   19298 H H    . SER   B  1 490 ? 50.034 -10.198 -38.824 0.00 18.26  ? 516  SER   B H    1 
ATOM   19299 H HA   . SER   B  1 490 ? 48.094 -10.626 -37.925 0.00 20.45  ? 516  SER   B HA   1 
ATOM   19300 H HB2  A SER   B  1 490 ? 46.598 -11.908 -39.185 0.00 23.35  ? 516  SER   B HB2  1 
ATOM   19301 H HB2  B SER   B  1 490 ? 48.118 -12.827 -40.003 0.00 22.28  ? 516  SER   B HB2  1 
ATOM   19302 H HB3  A SER   B  1 490 ? 47.765 -11.216 -40.339 0.00 23.11  ? 516  SER   B HB3  1 
ATOM   19303 H HB3  B SER   B  1 490 ? 46.649 -12.125 -39.248 0.00 22.18  ? 516  SER   B HB3  1 
ATOM   19304 H HG   A SER   B  1 490 ? 48.871 -13.420 -40.053 0.00 27.39  ? 516  SER   B HG   1 
ATOM   19305 H HG   B SER   B  1 490 ? 47.407 -11.327 -41.438 0.00 23.66  ? 516  SER   B HG   1 
ATOM   19306 N N    . ASN   B  1 491 ? 49.599 -12.578 -36.424 1.00 20.27  ? 517  ASN   B N    1 
ATOM   19307 C CA   . ASN   B  1 491 ? 49.785 -13.590 -35.405 1.00 20.78  ? 517  ASN   B CA   1 
ATOM   19308 C C    . ASN   B  1 491 ? 48.901 -13.309 -34.200 1.00 20.35  ? 517  ASN   B C    1 
ATOM   19309 O O    . ASN   B  1 491 ? 49.047 -12.277 -33.569 1.00 19.96  ? 517  ASN   B O    1 
ATOM   19310 C CB   . ASN   B  1 491 ? 51.262 -13.681 -35.016 1.00 22.49  ? 517  ASN   B CB   1 
ATOM   19311 C CG   . ASN   B  1 491 ? 51.560 -14.911 -34.194 1.00 24.48  ? 517  ASN   B CG   1 
ATOM   19312 O OD1  . ASN   B  1 491 ? 50.791 -15.288 -33.306 1.00 24.49  ? 517  ASN   B OD1  1 
ATOM   19313 N ND2  . ASN   B  1 491 ? 52.631 -15.613 -34.513 1.00 24.46  ? 517  ASN   B ND2  1 
ATOM   19314 H H    . ASN   B  1 491 ? 50.321 -11.865 -36.411 0.00 21.39  ? 517  ASN   B H    1 
ATOM   19315 H HA   . ASN   B  1 491 ? 49.492 -14.562 -35.794 0.00 22.77  ? 517  ASN   B HA   1 
ATOM   19316 H HB2  . ASN   B  1 491 ? 51.858 -13.708 -35.927 0.00 24.58  ? 517  ASN   B HB2  1 
ATOM   19317 H HB3  . ASN   B  1 491 ? 51.531 -12.807 -34.425 0.00 24.44  ? 517  ASN   B HB3  1 
ATOM   19318 H HD21 . ASN   B  1 491 ? 52.859 -16.447 -33.981 0.00 27.94  ? 517  ASN   B HD21 1 
ATOM   19319 H HD22 . ASN   B  1 491 ? 53.231 -15.331 -35.281 0.00 27.50  ? 517  ASN   B HD22 1 
ATOM   19320 N N    . ALA   B  1 492 ? 47.977 -14.238 -33.896 1.00 20.78  ? 518  ALA   B N    1 
ATOM   19321 C CA   . ALA   B  1 492 ? 47.035 -14.110 -32.785 1.00 22.17  ? 518  ALA   B CA   1 
ATOM   19322 C C    . ALA   B  1 492 ? 47.256 -15.187 -31.709 1.00 23.12  ? 518  ALA   B C    1 
ATOM   19323 O O    . ALA   B  1 492 ? 46.345 -15.434 -30.910 1.00 24.43  ? 518  ALA   B O    1 
ATOM   19324 C CB   . ALA   B  1 492 ? 45.614 -14.218 -33.327 1.00 22.48  ? 518  ALA   B CB   1 
ATOM   19325 H H    . ALA   B  1 492 ? 47.856 -15.108 -34.406 0.00 23.05  ? 518  ALA   B H    1 
ATOM   19326 H HA   . ALA   B  1 492 ? 47.128 -13.137 -32.307 0.00 24.36  ? 518  ALA   B HA   1 
ATOM   19327 H HB1  . ALA   B  1 492 ? 44.914 -13.875 -32.566 0.00 25.01  ? 518  ALA   B HB1  1 
ATOM   19328 H HB2  . ALA   B  1 492 ? 45.522 -13.601 -34.220 0.00 24.78  ? 518  ALA   B HB2  1 
ATOM   19329 H HB3  . ALA   B  1 492 ? 45.408 -15.258 -33.575 0.00 25.30  ? 518  ALA   B HB3  1 
ATOM   19330 N N    . GLN   B  1 493 ? 48.445 -15.798 -31.645 1.00 22.52  ? 519  GLN   B N    1 
ATOM   19331 C CA   . GLN   B  1 493 ? 48.688 -16.882 -30.698 1.00 22.98  ? 519  GLN   B CA   1 
ATOM   19332 C C    . GLN   B  1 493 ? 48.998 -16.390 -29.271 1.00 23.33  ? 519  GLN   B C    1 
ATOM   19333 O O    . GLN   B  1 493 ? 49.318 -15.219 -29.065 1.00 22.62  ? 519  GLN   B O    1 
ATOM   19334 C CB   . GLN   B  1 493 ? 49.812 -17.814 -31.215 1.00 23.81  ? 519  GLN   B CB   1 
ATOM   19335 C CG   . GLN   B  1 493 ? 51.230 -17.425 -30.794 1.00 27.23  ? 519  GLN   B CG   1 
ATOM   19336 C CD   . GLN   B  1 493 ? 52.233 -18.298 -31.490 1.00 31.88  ? 519  GLN   B CD   1 
ATOM   19337 O OE1  . GLN   B  1 493 ? 52.808 -17.907 -32.498 1.00 31.91  ? 519  GLN   B OE1  1 
ATOM   19338 N NE2  . GLN   B  1 493 ? 52.444 -19.512 -30.987 1.00 32.35  ? 519  GLN   B NE2  1 
ATOM   19339 H H    . GLN   B  1 493 ? 49.259 -15.555 -32.200 0.00 25.43  ? 519  GLN   B H    1 
ATOM   19340 H HA   . GLN   B  1 493 ? 47.792 -17.497 -30.634 0.00 26.76  ? 519  GLN   B HA   1 
ATOM   19341 H HB2  . GLN   B  1 493 ? 49.624 -18.817 -30.834 0.00 28.17  ? 519  GLN   B HB2  1 
ATOM   19342 H HB3  . GLN   B  1 493 ? 49.782 -17.832 -32.303 0.00 27.68  ? 519  GLN   B HB3  1 
ATOM   19343 H HG2  . GLN   B  1 493 ? 51.422 -16.388 -31.064 0.00 31.49  ? 519  GLN   B HG2  1 
ATOM   19344 H HG3  . GLN   B  1 493 ? 51.365 -17.573 -29.723 0.00 32.04  ? 519  GLN   B HG3  1 
ATOM   19345 H HE21 . GLN   B  1 493 ? 51.935 -19.820 -30.165 0.00 38.93  ? 519  GLN   B HE21 1 
ATOM   19346 H HE22 . GLN   B  1 493 ? 53.113 -20.135 -31.429 0.00 38.95  ? 519  GLN   B HE22 1 
ATOM   19347 N N    . VAL   B  1 494 ? 48.938 -17.322 -28.317 1.00 24.01  ? 520  VAL   B N    1 
ATOM   19348 C CA   . VAL   B  1 494 ? 49.328 -17.105 -26.939 1.00 24.49  ? 520  VAL   B CA   1 
ATOM   19349 C C    . VAL   B  1 494 ? 50.741 -17.653 -26.872 1.00 24.99  ? 520  VAL   B C    1 
ATOM   19350 O O    . VAL   B  1 494 ? 50.916 -18.873 -26.836 1.00 25.61  ? 520  VAL   B O    1 
ATOM   19351 C CB   . VAL   B  1 494 ? 48.400 -17.840 -25.935 1.00 25.33  ? 520  VAL   B CB   1 
ATOM   19352 C CG1  . VAL   B  1 494 ? 48.930 -17.721 -24.503 1.00 25.35  ? 520  VAL   B CG1  1 
ATOM   19353 C CG2  . VAL   B  1 494 ? 46.977 -17.306 -26.025 1.00 25.73  ? 520  VAL   B CG2  1 
ATOM   19354 H H    . VAL   B  1 494 ? 48.607 -18.267 -28.487 0.00 28.51  ? 520  VAL   B H    1 
ATOM   19355 H HA   . VAL   B  1 494 ? 49.338 -16.045 -26.689 0.00 28.69  ? 520  VAL   B HA   1 
ATOM   19356 H HB   . VAL   B  1 494 ? 48.365 -18.898 -26.191 0.00 30.66  ? 520  VAL   B HB   1 
ATOM   19357 H HG11 . VAL   B  1 494 ? 48.149 -18.027 -23.808 0.00 30.84  ? 520  VAL   B HG11 1 
ATOM   19358 H HG12 . VAL   B  1 494 ? 49.791 -18.375 -24.373 0.00 30.89  ? 520  VAL   B HG12 1 
ATOM   19359 H HG13 . VAL   B  1 494 ? 49.214 -16.688 -24.311 0.00 30.35  ? 520  VAL   B HG13 1 
ATOM   19360 H HG21 . VAL   B  1 494 ? 46.353 -17.826 -25.299 0.00 30.95  ? 520  VAL   B HG21 1 
ATOM   19361 H HG22 . VAL   B  1 494 ? 46.985 -16.238 -25.810 0.00 30.36  ? 520  VAL   B HG22 1 
ATOM   19362 H HG23 . VAL   B  1 494 ? 46.591 -17.479 -27.029 0.00 30.55  ? 520  VAL   B HG23 1 
ATOM   19363 N N    . LEU   B  1 495 ? 51.761 -16.775 -26.888 1.00 24.78  ? 521  LEU   B N    1 
ATOM   19364 C CA   . LEU   B  1 495 ? 53.159 -17.196 -26.743 1.00 24.77  ? 521  LEU   B CA   1 
ATOM   19365 C C    . LEU   B  1 495 ? 53.307 -17.756 -25.319 1.00 25.91  ? 521  LEU   B C    1 
ATOM   19366 O O    . LEU   B  1 495 ? 52.717 -17.217 -24.376 1.00 24.68  ? 521  LEU   B O    1 
ATOM   19367 C CB   . LEU   B  1 495 ? 54.112 -16.022 -26.981 1.00 25.28  ? 521  LEU   B CB   1 
ATOM   19368 C CG   . LEU   B  1 495 ? 54.102 -15.463 -28.423 1.00 27.27  ? 521  LEU   B CG   1 
ATOM   19369 C CD1  . LEU   B  1 495 ? 54.791 -14.117 -28.482 1.00 28.25  ? 521  LEU   B CD1  1 
ATOM   19370 C CD2  . LEU   B  1 495 ? 54.739 -16.437 -29.400 1.00 28.39  ? 521  LEU   B CD2  1 
ATOM   19371 H H    . LEU   B  1 495 ? 51.646 -15.773 -27.004 0.00 28.98  ? 521  LEU   B H    1 
ATOM   19372 H HA   . LEU   B  1 495 ? 53.379 -17.991 -27.454 0.00 29.70  ? 521  LEU   B HA   1 
ATOM   19373 H HB2  . LEU   B  1 495 ? 53.840 -15.210 -26.309 0.00 29.70  ? 521  LEU   B HB2  1 
ATOM   19374 H HB3  . LEU   B  1 495 ? 55.126 -16.351 -26.759 0.00 30.07  ? 521  LEU   B HB3  1 
ATOM   19375 H HG   . LEU   B  1 495 ? 53.071 -15.311 -28.739 0.00 31.63  ? 521  LEU   B HG   1 
ATOM   19376 H HD11 . LEU   B  1 495 ? 54.774 -13.747 -29.506 0.00 32.37  ? 521  LEU   B HD11 1 
ATOM   19377 H HD12 . LEU   B  1 495 ? 54.266 -13.421 -27.829 0.00 32.52  ? 521  LEU   B HD12 1 
ATOM   19378 H HD13 . LEU   B  1 495 ? 55.818 -14.240 -28.145 0.00 32.83  ? 521  LEU   B HD13 1 
ATOM   19379 H HD21 . LEU   B  1 495 ? 54.882 -15.935 -30.356 0.00 33.05  ? 521  LEU   B HD21 1 
ATOM   19380 H HD22 . LEU   B  1 495 ? 55.700 -16.766 -29.008 0.00 33.60  ? 521  LEU   B HD22 1 
ATOM   19381 H HD23 . LEU   B  1 495 ? 54.081 -17.293 -29.540 0.00 33.54  ? 521  LEU   B HD23 1 
ATOM   19382 N N    . SER   B  1 496 ? 53.988 -18.893 -25.184 1.00 27.53  ? 522  SER   B N    1 
ATOM   19383 C CA   . SER   B  1 496 ? 54.032 -19.604 -23.919 1.00 29.40  ? 522  SER   B CA   1 
ATOM   19384 C C    . SER   B  1 496 ? 55.409 -20.083 -23.461 1.00 30.06  ? 522  SER   B C    1 
ATOM   19385 O O    . SER   B  1 496 ? 55.477 -20.926 -22.567 1.00 30.94  ? 522  SER   B O    1 
ATOM   19386 C CB   . SER   B  1 496 ? 53.075 -20.781 -24.017 1.00 31.36  ? 522  SER   B CB   1 
ATOM   19387 O OG   . SER   B  1 496 ? 53.528 -21.666 -25.028 1.00 34.93  ? 522  SER   B OG   1 
ATOM   19388 H H    . SER   B  1 496 ? 54.519 -19.339 -25.925 0.00 33.85  ? 522  SER   B H    1 
ATOM   19389 H HA   . SER   B  1 496 ? 53.661 -18.964 -23.120 0.00 36.48  ? 522  SER   B HA   1 
ATOM   19390 H HB2  . SER   B  1 496 ? 53.010 -21.292 -23.058 0.00 39.61  ? 522  SER   B HB2  1 
ATOM   19391 H HB3  . SER   B  1 496 ? 52.090 -20.406 -24.293 0.00 38.94  ? 522  SER   B HB3  1 
ATOM   19392 H HG   . SER   B  1 496 ? 53.192 -21.383 -25.919 0.00 43.38  ? 522  SER   B HG   1 
ATOM   19393 N N    . GLY   B  1 497 ? 56.478 -19.515 -24.001 1.00 29.38  ? 523  GLY   B N    1 
ATOM   19394 C CA   . GLY   B  1 497 ? 57.828 -19.856 -23.574 1.00 29.59  ? 523  GLY   B CA   1 
ATOM   19395 C C    . GLY   B  1 497 ? 58.551 -20.989 -24.278 1.00 29.73  ? 523  GLY   B C    1 
ATOM   19396 O O    . GLY   B  1 497 ? 59.594 -21.412 -23.785 1.00 29.96  ? 523  GLY   B O    1 
ATOM   19397 H H    . GLY   B  1 497 ? 56.459 -18.809 -24.730 0.00 36.36  ? 523  GLY   B H    1 
ATOM   19398 H HA2  . GLY   B  1 497 ? 58.442 -18.966 -23.708 0.00 37.19  ? 523  GLY   B HA2  1 
ATOM   19399 H HA3  . GLY   B  1 497 ? 57.829 -20.076 -22.507 0.00 37.77  ? 523  GLY   B HA3  1 
ATOM   19400 N N    . THR   B  1 498 ? 58.048 -21.491 -25.414 1.00 29.55  ? 524  THR   B N    1 
ATOM   19401 C CA   . THR   B  1 498 ? 58.728 -22.573 -26.168 1.00 30.63  ? 524  THR   B CA   1 
ATOM   19402 C C    . THR   B  1 498 ? 58.890 -22.284 -27.665 1.00 29.83  ? 524  THR   B C    1 
ATOM   19403 O O    . THR   B  1 498 ? 59.656 -22.985 -28.331 1.00 30.80  ? 524  THR   B O    1 
ATOM   19404 C CB   . THR   B  1 498 ? 57.914 -23.869 -26.066 1.00 33.47  ? 524  THR   B CB   1 
ATOM   19405 O OG1  . THR   B  1 498 ? 56.592 -23.612 -26.566 1.00 35.48  ? 524  THR   B OG1  1 
ATOM   19406 C CG2  . THR   B  1 498 ? 57.845 -24.407 -24.641 1.00 34.37  ? 524  THR   B CG2  1 
ATOM   19407 H H    . THR   B  1 498 ? 57.159 -21.210 -25.816 0.00 37.31  ? 524  THR   B H    1 
ATOM   19408 H HA   . THR   B  1 498 ? 59.720 -22.769 -25.766 0.00 39.63  ? 524  THR   B HA   1 
ATOM   19409 H HB   . THR   B  1 498 ? 58.376 -24.635 -26.687 0.00 43.45  ? 524  THR   B HB   1 
ATOM   19410 H HG1  . THR   B  1 498 ? 56.038 -24.434 -26.503 0.00 45.48  ? 524  THR   B HG1  1 
ATOM   19411 H HG21 . THR   B  1 498 ? 57.314 -25.357 -24.629 0.00 45.09  ? 524  THR   B HG21 1 
ATOM   19412 H HG22 . THR   B  1 498 ? 58.851 -24.557 -24.252 0.00 45.05  ? 524  THR   B HG22 1 
ATOM   19413 H HG23 . THR   B  1 498 ? 57.318 -23.702 -23.999 0.00 44.49  ? 524  THR   B HG23 1 
ATOM   19414 N N    . GLU   B  1 499 ? 58.177 -21.289 -28.196 1.00 28.00  ? 525  GLU   B N    1 
ATOM   19415 C CA   . GLU   B  1 499 ? 58.166 -20.978 -29.622 1.00 27.24  ? 525  GLU   B CA   1 
ATOM   19416 C C    . GLU   B  1 499 ? 59.520 -20.627 -30.218 1.00 27.25  ? 525  GLU   B C    1 
ATOM   19417 O O    . GLU   B  1 499 ? 59.744 -20.894 -31.402 1.00 27.40  ? 525  GLU   B O    1 
ATOM   19418 C CB   . GLU   B  1 499 ? 57.167 -19.835 -29.918 1.00 28.11  ? 525  GLU   B CB   1 
ATOM   19419 C CG   . GLU   B  1 499 ? 55.710 -20.209 -29.682 1.00 30.31  ? 525  GLU   B CG   1 
ATOM   19420 C CD   . GLU   B  1 499 ? 55.246 -20.277 -28.238 1.00 33.87  ? 525  GLU   B CD   1 
ATOM   19421 O OE1  . GLU   B  1 499 ? 55.906 -19.677 -27.359 1.00 34.04  ? 525  GLU   B OE1  1 
ATOM   19422 O OE2  . GLU   B  1 499 ? 54.203 -20.918 -27.982 1.00 35.33  ? 525  GLU   B OE2  1 
ATOM   19423 H H    . GLU   B  1 499 ? 57.615 -20.642 -27.653 0.00 34.94  ? 525  GLU   B H    1 
ATOM   19424 H HA   . GLU   B  1 499 ? 57.810 -21.860 -30.152 0.00 34.12  ? 525  GLU   B HA   1 
ATOM   19425 H HB2  . GLU   B  1 499 ? 57.415 -18.969 -29.305 0.00 34.15  ? 525  GLU   B HB2  1 
ATOM   19426 H HB3  . GLU   B  1 499 ? 57.262 -19.568 -30.970 0.00 34.09  ? 525  GLU   B HB3  1 
ATOM   19427 H HG2  . GLU   B  1 499 ? 55.088 -19.470 -30.185 0.00 36.58  ? 525  GLU   B HG2  1 
ATOM   19428 H HG3  . GLU   B  1 499 ? 55.532 -21.188 -30.127 0.00 37.28  ? 525  GLU   B HG3  1 
ATOM   19429 N N    . PHE   B  1 500 ? 60.404 -19.998 -29.439 1.00 26.85  ? 526  PHE   B N    1 
ATOM   19430 C CA   . PHE   B  1 500 ? 61.705 -19.551 -29.931 1.00 27.54  ? 526  PHE   B CA   1 
ATOM   19431 C C    . PHE   B  1 500 ? 62.882 -20.386 -29.421 1.00 29.11  ? 526  PHE   B C    1 
ATOM   19432 O O    . PHE   B  1 500 ? 64.021 -19.955 -29.563 1.00 29.06  ? 526  PHE   B O    1 
ATOM   19433 C CB   . PHE   B  1 500 ? 61.896 -18.071 -29.563 1.00 26.87  ? 526  PHE   B CB   1 
ATOM   19434 C CG   . PHE   B  1 500 ? 60.855 -17.179 -30.195 1.00 26.28  ? 526  PHE   B CG   1 
ATOM   19435 C CD1  . PHE   B  1 500 ? 60.975 -16.774 -31.513 1.00 26.48  ? 526  PHE   B CD1  1 
ATOM   19436 C CD2  . PHE   B  1 500 ? 59.724 -16.797 -29.489 1.00 26.33  ? 526  PHE   B CD2  1 
ATOM   19437 C CE1  . PHE   B  1 500 ? 59.997 -15.977 -32.104 1.00 26.22  ? 526  PHE   B CE1  1 
ATOM   19438 C CE2  . PHE   B  1 500 ? 58.755 -15.996 -30.083 1.00 26.06  ? 526  PHE   B CE2  1 
ATOM   19439 C CZ   . PHE   B  1 500 ? 58.906 -15.583 -31.381 1.00 25.74  ? 526  PHE   B CZ   1 
ATOM   19440 H H    . PHE   B  1 500 ? 60.252 -19.768 -28.462 0.00 33.49  ? 526  PHE   B H    1 
ATOM   19441 H HA   . PHE   B  1 500 ? 61.733 -19.601 -31.019 0.00 34.09  ? 526  PHE   B HA   1 
ATOM   19442 H HB2  . PHE   B  1 500 ? 61.834 -17.958 -28.482 0.00 33.16  ? 526  PHE   B HB2  1 
ATOM   19443 H HB3  . PHE   B  1 500 ? 62.866 -17.728 -29.920 0.00 33.01  ? 526  PHE   B HB3  1 
ATOM   19444 H HD1  . PHE   B  1 500 ? 61.835 -17.070 -32.086 0.00 31.77  ? 526  PHE   B HD1  1 
ATOM   19445 H HD2  . PHE   B  1 500 ? 59.603 -17.108 -28.465 0.00 31.83  ? 526  PHE   B HD2  1 
ATOM   19446 H HE1  . PHE   B  1 500 ? 60.113 -15.651 -33.125 0.00 30.58  ? 526  PHE   B HE1  1 
ATOM   19447 H HE2  . PHE   B  1 500 ? 57.892 -15.690 -29.517 0.00 30.63  ? 526  PHE   B HE2  1 
ATOM   19448 H HZ   . PHE   B  1 500 ? 58.151 -14.967 -31.841 0.00 29.71  ? 526  PHE   B HZ   1 
ATOM   19449 N N    . SER   B  1 501 ? 62.630 -21.603 -28.906 1.00 30.24  ? 527  SER   B N    1 
ATOM   19450 C CA   . SER   B  1 501 ? 63.686 -22.465 -28.368 1.00 31.52  ? 527  SER   B CA   1 
ATOM   19451 C C    . SER   B  1 501 ? 64.778 -22.875 -29.381 1.00 31.66  ? 527  SER   B C    1 
ATOM   19452 O O    . SER   B  1 501 ? 65.895 -23.159 -28.956 1.00 32.66  ? 527  SER   B O    1 
ATOM   19453 C CB   . SER   B  1 501 ? 63.078 -23.700 -27.714 1.00 34.82  ? 527  SER   B CB   1 
ATOM   19454 O OG   . SER   B  1 501 ? 62.158 -24.340 -28.586 1.00 39.75  ? 527  SER   B OG   1 
ATOM   19455 H H    . SER   B  1 501 ? 61.710 -22.027 -28.856 0.00 38.63  ? 527  SER   B H    1 
ATOM   19456 H HA   . SER   B  1 501 ? 64.186 -21.910 -27.574 0.00 40.90  ? 527  SER   B HA   1 
ATOM   19457 H HB2  . SER   B  1 501 ? 63.875 -24.400 -27.470 0.00 45.86  ? 527  SER   B HB2  1 
ATOM   19458 H HB3  . SER   B  1 501 ? 62.556 -23.399 -26.806 0.00 45.26  ? 527  SER   B HB3  1 
ATOM   19459 H HG   . SER   B  1 501 ? 61.255 -23.939 -28.490 0.00 50.83  ? 527  SER   B HG   1 
ATOM   19460 N N    . ALA   B  1 502 ? 64.495 -22.891 -30.697 1.00 30.64  ? 528  ALA   B N    1 
ATOM   19461 C CA   . ALA   B  1 502 ? 65.510 -23.231 -31.704 1.00 29.91  ? 528  ALA   B CA   1 
ATOM   19462 C C    . ALA   B  1 502 ? 66.455 -22.049 -32.026 1.00 29.48  ? 528  ALA   B C    1 
ATOM   19463 O O    . ALA   B  1 502 ? 67.542 -22.258 -32.560 1.00 29.99  ? 528  ALA   B O    1 
ATOM   19464 C CB   . ALA   B  1 502 ? 64.843 -23.721 -32.971 1.00 29.70  ? 528  ALA   B CB   1 
ATOM   19465 H H    . ALA   B  1 502 ? 63.584 -22.685 -31.094 0.00 39.39  ? 528  ALA   B H    1 
ATOM   19466 H HA   . ALA   B  1 502 ? 66.124 -24.052 -31.336 0.00 39.66  ? 528  ALA   B HA   1 
ATOM   19467 H HB1  . ALA   B  1 502 ? 65.612 -24.005 -33.687 0.00 38.92  ? 528  ALA   B HB1  1 
ATOM   19468 H HB2  . ALA   B  1 502 ? 64.219 -24.581 -32.734 0.00 39.00  ? 528  ALA   B HB2  1 
ATOM   19469 H HB3  . ALA   B  1 502 ? 64.231 -22.920 -33.381 0.00 38.18  ? 528  ALA   B HB3  1 
ATOM   19470 N N    . ILE   B  1 503 ? 66.047 -20.813 -31.709 1.00 28.14  ? 529  ILE   B N    1 
ATOM   19471 C CA   . ILE   B  1 503 ? 66.868 -19.613 -31.888 1.00 27.35  ? 529  ILE   B CA   1 
ATOM   19472 C C    . ILE   B  1 503 ? 66.812 -18.872 -30.540 1.00 26.64  ? 529  ILE   B C    1 
ATOM   19473 O O    . ILE   B  1 503 ? 66.203 -17.818 -30.440 1.00 25.60  ? 529  ILE   B O    1 
ATOM   19474 C CB   . ILE   B  1 503 ? 66.366 -18.740 -33.090 1.00 27.65  ? 529  ILE   B CB   1 
ATOM   19475 C CG1  . ILE   B  1 503 ? 64.838 -18.531 -33.055 1.00 28.64  ? 529  ILE   B CG1  1 
ATOM   19476 C CG2  . ILE   B  1 503 ? 66.790 -19.381 -34.433 1.00 27.66  ? 529  ILE   B CG2  1 
ATOM   19477 C CD1  . ILE   B  1 503 ? 64.355 -17.491 -34.044 1.00 30.52  ? 529  ILE   B CD1  1 
ATOM   19478 H H    . ILE   B  1 503 ? 65.142 -20.602 -31.303 0.00 35.85  ? 529  ILE   B H    1 
ATOM   19479 H HA   . ILE   B  1 503 ? 67.912 -19.876 -32.057 0.00 35.18  ? 529  ILE   B HA   1 
ATOM   19480 H HB   . ILE   B  1 503 ? 66.844 -17.764 -33.022 0.00 34.34  ? 529  ILE   B HB   1 
ATOM   19481 H HG12 . ILE   B  1 503 ? 64.345 -19.470 -33.301 0.00 35.53  ? 529  ILE   B HG12 1 
ATOM   19482 H HG13 . ILE   B  1 503 ? 64.537 -18.202 -32.061 0.00 35.29  ? 529  ILE   B HG13 1 
ATOM   19483 H HG21 . ILE   B  1 503 ? 66.633 -18.668 -35.240 0.00 34.32  ? 529  ILE   B HG21 1 
ATOM   19484 H HG22 . ILE   B  1 503 ? 67.843 -19.651 -34.383 0.00 35.11  ? 529  ILE   B HG22 1 
ATOM   19485 H HG23 . ILE   B  1 503 ? 66.187 -20.272 -34.605 0.00 34.89  ? 529  ILE   B HG23 1 
ATOM   19486 H HD11 . ILE   B  1 503 ? 63.306 -17.283 -33.841 0.00 36.73  ? 529  ILE   B HD11 1 
ATOM   19487 H HD12 . ILE   B  1 503 ? 64.947 -16.584 -33.926 0.00 36.81  ? 529  ILE   B HD12 1 
ATOM   19488 H HD13 . ILE   B  1 503 ? 64.458 -17.877 -35.057 0.00 37.02  ? 529  ILE   B HD13 1 
ATOM   19489 N N    . PRO   B  1 504 ? 67.396 -19.455 -29.474 1.00 26.70  ? 530  PRO   B N    1 
ATOM   19490 C CA   . PRO   B  1 504 ? 67.253 -18.854 -28.140 1.00 26.45  ? 530  PRO   B CA   1 
ATOM   19491 C C    . PRO   B  1 504 ? 68.128 -17.641 -27.854 1.00 26.64  ? 530  PRO   B C    1 
ATOM   19492 O O    . PRO   B  1 504 ? 67.995 -17.056 -26.774 1.00 27.22  ? 530  PRO   B O    1 
ATOM   19493 C CB   . PRO   B  1 504 ? 67.578 -20.025 -27.199 1.00 27.39  ? 530  PRO   B CB   1 
ATOM   19494 C CG   . PRO   B  1 504 ? 68.547 -20.858 -27.963 1.00 27.95  ? 530  PRO   B CG   1 
ATOM   19495 C CD   . PRO   B  1 504 ? 68.152 -20.726 -29.421 1.00 26.48  ? 530  PRO   B CD   1 
ATOM   19496 H HA   . PRO   B  1 504 ? 66.217 -18.576 -27.958 0.00 33.95  ? 530  PRO   B HA   1 
ATOM   19497 H HB2  . PRO   B  1 504 ? 68.028 -19.657 -26.278 0.00 36.34  ? 530  PRO   B HB2  1 
ATOM   19498 H HB3  . PRO   B  1 504 ? 66.672 -20.589 -26.989 0.00 36.16  ? 530  PRO   B HB3  1 
ATOM   19499 H HG2  . PRO   B  1 504 ? 69.555 -20.480 -27.805 0.00 37.41  ? 530  PRO   B HG2  1 
ATOM   19500 H HG3  . PRO   B  1 504 ? 68.471 -21.896 -27.641 0.00 37.70  ? 530  PRO   B HG3  1 
ATOM   19501 H HD2  . PRO   B  1 504 ? 69.040 -20.666 -30.048 0.00 35.12  ? 530  PRO   B HD2  1 
ATOM   19502 H HD3  . PRO   B  1 504 ? 67.514 -21.558 -29.715 0.00 35.12  ? 530  PRO   B HD3  1 
ATOM   19503 N N    . HIS   B  1 505 ? 69.025 -17.258 -28.786 1.00 25.33  ? 531  HIS   B N    1 
ATOM   19504 C CA   . HIS   B  1 505 ? 69.921 -16.122 -28.576 1.00 25.08  ? 531  HIS   B CA   1 
ATOM   19505 C C    . HIS   B  1 505 ? 69.477 -14.867 -29.326 1.00 24.12  ? 531  HIS   B C    1 
ATOM   19506 O O    . HIS   B  1 505 ? 70.295 -13.986 -29.589 1.00 24.95  ? 531  HIS   B O    1 
ATOM   19507 C CB   . HIS   B  1 505 ? 71.365 -16.528 -28.913 1.00 26.31  ? 531  HIS   B CB   1 
ATOM   19508 C CG   . HIS   B  1 505 ? 71.779 -17.765 -28.181 1.00 30.72  ? 531  HIS   B CG   1 
ATOM   19509 N ND1  . HIS   B  1 505 ? 71.900 -17.776 -26.800 1.00 33.58  ? 531  HIS   B ND1  1 
ATOM   19510 C CD2  . HIS   B  1 505 ? 72.010 -19.014 -28.646 1.00 32.48  ? 531  HIS   B CD2  1 
ATOM   19511 C CE1  . HIS   B  1 505 ? 72.220 -19.016 -26.466 1.00 33.77  ? 531  HIS   B CE1  1 
ATOM   19512 N NE2  . HIS   B  1 505 ? 72.305 -19.799 -27.544 1.00 34.10  ? 531  HIS   B NE2  1 
ATOM   19513 H H    . HIS   B  1 505 ? 69.164 -17.705 -29.686 0.00 32.73  ? 531  HIS   B H    1 
ATOM   19514 H HA   . HIS   B  1 505 ? 69.935 -15.855 -27.521 0.00 32.53  ? 531  HIS   B HA   1 
ATOM   19515 H HB2  . HIS   B  1 505 ? 71.442 -16.721 -29.982 0.00 34.20  ? 531  HIS   B HB2  1 
ATOM   19516 H HB3  . HIS   B  1 505 ? 72.045 -15.727 -28.629 0.00 34.37  ? 531  HIS   B HB3  1 
ATOM   19517 H HD1  . HIS   B  1 505 ? 71.770 -16.990 -26.172 0.00 44.03  ? 531  HIS   B HD1  1 
ATOM   19518 H HD2  . HIS   B  1 505 ? 71.971 -19.336 -29.672 0.00 42.77  ? 531  HIS   B HD2  1 
ATOM   19519 H HE1  . HIS   B  1 505 ? 72.390 -19.350 -25.457 0.00 45.48  ? 531  HIS   B HE1  1 
ATOM   19520 N N    . VAL   B  1 506 ? 68.170 -14.736 -29.615 1.00 22.49  ? 532  VAL   B N    1 
ATOM   19521 C CA   . VAL   B  1 506 ? 67.644 -13.527 -30.246 1.00 22.16  ? 532  VAL   B CA   1 
ATOM   19522 C C    . VAL   B  1 506 ? 67.832 -12.369 -29.226 1.00 22.29  ? 532  VAL   B C    1 
ATOM   19523 O O    . VAL   B  1 506 ? 67.534 -12.541 -28.055 1.00 22.87  ? 532  VAL   B O    1 
ATOM   19524 C CB   . VAL   B  1 506 ? 66.155 -13.687 -30.650 1.00 22.13  ? 532  VAL   B CB   1 
ATOM   19525 C CG1  . VAL   B  1 506 ? 65.560 -12.345 -31.096 1.00 22.13  ? 532  VAL   B CG1  1 
ATOM   19526 C CG2  . VAL   B  1 506 ? 65.994 -14.743 -31.749 1.00 21.65  ? 532  VAL   B CG2  1 
ATOM   19527 H H    . VAL   B  1 506 ? 67.457 -15.429 -29.413 0.00 28.16  ? 532  VAL   B H    1 
ATOM   19528 H HA   . VAL   B  1 506 ? 68.212 -13.312 -31.148 0.00 27.01  ? 532  VAL   B HA   1 
ATOM   19529 H HB   . VAL   B  1 506 ? 65.590 -14.024 -29.783 0.00 26.78  ? 532  VAL   B HB   1 
ATOM   19530 H HG11 . VAL   B  1 506 ? 64.677 -12.533 -31.703 0.00 25.81  ? 532  VAL   B HG11 1 
ATOM   19531 H HG12 . VAL   B  1 506 ? 65.275 -11.766 -30.219 0.00 26.01  ? 532  VAL   B HG12 1 
ATOM   19532 H HG13 . VAL   B  1 506 ? 66.303 -11.799 -31.676 0.00 25.99  ? 532  VAL   B HG13 1 
ATOM   19533 H HG21 . VAL   B  1 506 ? 64.938 -14.848 -31.990 0.00 25.90  ? 532  VAL   B HG21 1 
ATOM   19534 H HG22 . VAL   B  1 506 ? 66.547 -14.423 -32.630 0.00 26.03  ? 532  VAL   B HG22 1 
ATOM   19535 H HG23 . VAL   B  1 506 ? 66.383 -15.696 -31.391 0.00 26.59  ? 532  VAL   B HG23 1 
ATOM   19536 N N    . LYS   B  1 507 ? 68.440 -11.271 -29.655 1.00 22.17  ? 533  LYS   B N    1 
ATOM   19537 C CA   . LYS   B  1 507 ? 68.711 -10.101 -28.812 1.00 22.50  ? 533  LYS   B CA   1 
ATOM   19538 C C    . LYS   B  1 507 ? 67.712 -8.963  -29.108 1.00 21.23  ? 533  LYS   B C    1 
ATOM   19539 O O    . LYS   B  1 507 ? 67.432 -8.161  -28.225 1.00 21.51  ? 533  LYS   B O    1 
ATOM   19540 C CB   . LYS   B  1 507 ? 70.132 -9.553  -29.081 1.00 25.09  ? 533  LYS   B CB   1 
ATOM   19541 C CG   . LYS   B  1 507 ? 71.273 -10.576 -29.121 1.00 30.66  ? 533  LYS   B CG   1 
ATOM   19542 C CD   . LYS   B  1 507 ? 71.609 -11.169 -27.783 1.00 34.49  ? 533  LYS   B CD   1 
ATOM   19543 C CE   . LYS   B  1 507 ? 72.783 -12.133 -27.872 1.00 38.50  ? 533  LYS   B CE   1 
ATOM   19544 N NZ   . LYS   B  1 507 ? 74.104 -11.433 -27.903 1.00 40.75  ? 533  LYS   B NZ   1 
ATOM   19545 H H    . LYS   B  1 507 ? 68.769 -11.147 -30.608 0.00 26.71  ? 533  LYS   B H    1 
ATOM   19546 H HA   . LYS   B  1 507 ? 68.644 -10.354 -27.755 0.00 27.52  ? 533  LYS   B HA   1 
ATOM   19547 H HB2  . LYS   B  1 507 ? 70.122 -9.045  -30.044 0.00 30.24  ? 533  LYS   B HB2  1 
ATOM   19548 H HB3  . LYS   B  1 507 ? 70.372 -8.835  -28.299 0.00 30.66  ? 533  LYS   B HB3  1 
ATOM   19549 H HG2  . LYS   B  1 507 ? 71.013 -11.391 -29.796 0.00 37.81  ? 533  LYS   B HG2  1 
ATOM   19550 H HG3  . LYS   B  1 507 ? 72.167 -10.076 -29.489 0.00 37.89  ? 533  LYS   B HG3  1 
ATOM   19551 H HD2  . LYS   B  1 507 ? 71.875 -10.369 -27.093 0.00 43.05  ? 533  LYS   B HD2  1 
ATOM   19552 H HD3  . LYS   B  1 507 ? 70.747 -11.718 -27.408 0.00 42.95  ? 533  LYS   B HD3  1 
ATOM   19553 H HE2  . LYS   B  1 507 ? 72.773 -12.792 -27.006 0.00 48.81  ? 533  LYS   B HE2  1 
ATOM   19554 H HE3  . LYS   B  1 507 ? 72.694 -12.720 -28.785 0.00 48.33  ? 533  LYS   B HE3  1 
ATOM   19555 H HZ1  . LYS   B  1 507 ? 74.856 -12.114 -27.936 0.00 51.81  ? 533  LYS   B HZ1  1 
ATOM   19556 H HZ2  . LYS   B  1 507 ? 74.162 -10.838 -28.724 0.00 51.03  ? 533  LYS   B HZ2  1 
ATOM   19557 H HZ3  . LYS   B  1 507 ? 74.213 -10.860 -27.073 0.00 51.44  ? 533  LYS   B HZ3  1 
ATOM   19558 N N    . TYR   B  1 508 ? 67.211 -8.863  -30.347 1.00 20.23  ? 534  TYR   B N    1 
ATOM   19559 C CA   . TYR   B  1 508 ? 66.280 -7.807  -30.751 1.00 20.49  ? 534  TYR   B CA   1 
ATOM   19560 C C    . TYR   B  1 508 ? 65.121 -8.487  -31.483 1.00 19.82  ? 534  TYR   B C    1 
ATOM   19561 O O    . TYR   B  1 508 ? 65.312 -9.049  -32.569 1.00 19.48  ? 534  TYR   B O    1 
ATOM   19562 C CB   . TYR   B  1 508 ? 67.010 -6.781  -31.638 1.00 21.08  ? 534  TYR   B CB   1 
ATOM   19563 C CG   . TYR   B  1 508 ? 66.263 -5.484  -31.899 1.00 22.49  ? 534  TYR   B CG   1 
ATOM   19564 C CD1  . TYR   B  1 508 ? 65.008 -5.490  -32.496 1.00 23.44  ? 534  TYR   B CD1  1 
ATOM   19565 C CD2  . TYR   B  1 508 ? 66.875 -4.255  -31.696 1.00 23.89  ? 534  TYR   B CD2  1 
ATOM   19566 C CE1  . TYR   B  1 508 ? 64.349 -4.310  -32.805 1.00 24.87  ? 534  TYR   B CE1  1 
ATOM   19567 C CE2  . TYR   B  1 508 ? 66.243 -3.066  -32.047 1.00 25.16  ? 534  TYR   B CE2  1 
ATOM   19568 C CZ   . TYR   B  1 508 ? 64.969 -3.097  -32.574 1.00 26.37  ? 534  TYR   B CZ   1 
ATOM   19569 O OH   . TYR   B  1 508 ? 64.302 -1.941  -32.875 1.00 29.06  ? 534  TYR   B OH   1 
ATOM   19570 H H    . TYR   B  1 508 ? 67.446 -9.480  -31.118 0.00 23.55  ? 534  TYR   B H    1 
ATOM   19571 H HA   . TYR   B  1 508 ? 65.887 -7.280  -29.883 0.00 23.31  ? 534  TYR   B HA   1 
ATOM   19572 H HB2  . TYR   B  1 508 ? 67.952 -6.527  -31.153 0.00 24.13  ? 534  TYR   B HB2  1 
ATOM   19573 H HB3  . TYR   B  1 508 ? 67.220 -7.235  -32.604 0.00 23.80  ? 534  TYR   B HB3  1 
ATOM   19574 H HD1  . TYR   B  1 508 ? 64.514 -6.426  -32.689 0.00 25.88  ? 534  TYR   B HD1  1 
ATOM   19575 H HD2  . TYR   B  1 508 ? 67.872 -4.215  -31.286 0.00 27.12  ? 534  TYR   B HD2  1 
ATOM   19576 H HE1  . TYR   B  1 508 ? 63.358 -4.341  -33.229 0.00 26.98  ? 534  TYR   B HE1  1 
ATOM   19577 H HE2  . TYR   B  1 508 ? 66.723 -2.125  -31.828 0.00 28.02  ? 534  TYR   B HE2  1 
ATOM   19578 H HH   . TYR   B  1 508 ? 64.865 -1.144  -32.692 0.00 32.06  ? 534  TYR   B HH   1 
ATOM   19579 N N    . LEU   B  1 509 ? 63.941 -8.472  -30.862 1.00 19.62  ? 535  LEU   B N    1 
ATOM   19580 C CA   . LEU   B  1 509 ? 62.750 -9.114  -31.403 1.00 20.12  ? 535  LEU   B CA   1 
ATOM   19581 C C    . LEU   B  1 509 ? 61.656 -8.096  -31.715 1.00 19.08  ? 535  LEU   B C    1 
ATOM   19582 O O    . LEU   B  1 509 ? 61.173 -7.414  -30.814 1.00 18.65  ? 535  LEU   B O    1 
ATOM   19583 C CB   . LEU   B  1 509 ? 62.237 -10.145 -30.388 1.00 20.39  ? 535  LEU   B CB   1 
ATOM   19584 C CG   . LEU   B  1 509 ? 60.926 -10.865 -30.741 1.00 22.07  ? 535  LEU   B CG   1 
ATOM   19585 C CD1  . LEU   B  1 509 ? 61.028 -11.614 -32.076 1.00 23.31  ? 535  LEU   B CD1  1 
ATOM   19586 C CD2  . LEU   B  1 509 ? 60.529 -11.829 -29.636 1.00 22.51  ? 535  LEU   B CD2  1 
ATOM   19587 H H    . LEU   B  1 509 ? 63.770 -8.019  -29.970 0.00 21.92  ? 535  LEU   B H    1 
ATOM   19588 H HA   . LEU   B  1 509 ? 62.995 -9.650  -32.319 0.00 22.28  ? 535  LEU   B HA   1 
ATOM   19589 H HB2  . LEU   B  1 509 ? 63.003 -10.906 -30.245 0.00 23.24  ? 535  LEU   B HB2  1 
ATOM   19590 H HB3  . LEU   B  1 509 ? 62.059 -9.624  -29.449 0.00 22.94  ? 535  LEU   B HB3  1 
ATOM   19591 H HG   . LEU   B  1 509 ? 60.142 -10.113 -30.807 0.00 24.49  ? 535  LEU   B HG   1 
ATOM   19592 H HD11 . LEU   B  1 509 ? 60.159 -12.259 -32.198 0.00 26.26  ? 535  LEU   B HD11 1 
ATOM   19593 H HD12 . LEU   B  1 509 ? 61.067 -10.891 -32.889 0.00 25.96  ? 535  LEU   B HD12 1 
ATOM   19594 H HD13 . LEU   B  1 509 ? 61.940 -12.209 -32.064 0.00 26.55  ? 535  LEU   B HD13 1 
ATOM   19595 H HD21 . LEU   B  1 509 ? 59.608 -12.336 -29.915 0.00 25.62  ? 535  LEU   B HD21 1 
ATOM   19596 H HD22 . LEU   B  1 509 ? 61.326 -12.558 -29.501 0.00 26.02  ? 535  LEU   B HD22 1 
ATOM   19597 H HD23 . LEU   B  1 509 ? 60.381 -11.266 -28.715 0.00 25.70  ? 535  LEU   B HD23 1 
ATOM   19598 N N    . ASP   B  1 510 ? 61.241 -8.030  -32.993 1.00 17.75  ? 536  ASP   B N    1 
ATOM   19599 C CA   . ASP   B  1 510 ? 60.179 -7.132  -33.415 1.00 17.10  ? 536  ASP   B CA   1 
ATOM   19600 C C    . ASP   B  1 510 ? 58.904 -7.967  -33.686 1.00 16.99  ? 536  ASP   B C    1 
ATOM   19601 O O    . ASP   B  1 510 ? 58.886 -8.793  -34.594 1.00 17.17  ? 536  ASP   B O    1 
ATOM   19602 C CB   . ASP   B  1 510 ? 60.647 -6.291  -34.628 1.00 17.56  ? 536  ASP   B CB   1 
ATOM   19603 C CG   . ASP   B  1 510 ? 59.630 -5.289  -35.156 1.00 19.35  ? 536  ASP   B CG   1 
ATOM   19604 O OD1  . ASP   B  1 510 ? 58.427 -5.530  -34.996 1.00 21.51  ? 536  ASP   B OD1  1 
ATOM   19605 O OD2  . ASP   B  1 510 ? 60.048 -4.274  -35.749 1.00 19.96  ? 536  ASP   B OD2  1 
ATOM   19606 H H    . ASP   B  1 510 ? 61.624 -8.583  -33.753 0.00 18.77  ? 536  ASP   B H    1 
ATOM   19607 H HA   . ASP   B  1 510 ? 59.953 -6.424  -32.621 0.00 17.51  ? 536  ASP   B HA   1 
ATOM   19608 H HB2  . ASP   B  1 510 ? 61.528 -5.726  -34.326 0.00 17.94  ? 536  ASP   B HB2  1 
ATOM   19609 H HB3  . ASP   B  1 510 ? 60.910 -6.947  -35.453 0.00 17.91  ? 536  ASP   B HB3  1 
ATOM   19610 N N    . LEU   B  1 511 ? 57.876 -7.816  -32.827 1.00 17.09  ? 537  LEU   B N    1 
ATOM   19611 C CA   . LEU   B  1 511 ? 56.590 -8.505  -32.992 1.00 18.01  ? 537  LEU   B CA   1 
ATOM   19612 C C    . LEU   B  1 511 ? 55.457 -7.499  -33.216 1.00 17.91  ? 537  LEU   B C    1 
ATOM   19613 O O    . LEU   B  1 511 ? 54.296 -7.812  -32.943 1.00 18.24  ? 537  LEU   B O    1 
ATOM   19614 C CB   . LEU   B  1 511 ? 56.264 -9.359  -31.747 1.00 18.85  ? 537  LEU   B CB   1 
ATOM   19615 C CG   . LEU   B  1 511 ? 57.081 -10.628 -31.533 1.00 20.99  ? 537  LEU   B CG   1 
ATOM   19616 C CD1  . LEU   B  1 511 ? 56.874 -11.156 -30.110 1.00 21.28  ? 537  LEU   B CD1  1 
ATOM   19617 C CD2  . LEU   B  1 511 ? 56.718 -11.721 -32.534 1.00 21.66  ? 537  LEU   B CD2  1 
ATOM   19618 H H    . LEU   B  1 511 ? 57.905 -7.223  -32.004 0.00 17.46  ? 537  LEU   B H    1 
ATOM   19619 H HA   . LEU   B  1 511 ? 56.614 -9.134  -33.879 0.00 18.56  ? 537  LEU   B HA   1 
ATOM   19620 H HB2  . LEU   B  1 511 ? 56.404 -8.739  -30.864 0.00 19.88  ? 537  LEU   B HB2  1 
ATOM   19621 H HB3  . LEU   B  1 511 ? 55.226 -9.679  -31.802 0.00 19.83  ? 537  LEU   B HB3  1 
ATOM   19622 H HG   . LEU   B  1 511 ? 58.131 -10.392 -31.687 0.00 22.84  ? 537  LEU   B HG   1 
ATOM   19623 H HD11 . LEU   B  1 511 ? 57.296 -12.157 -30.034 0.00 23.77  ? 537  LEU   B HD11 1 
ATOM   19624 H HD12 . LEU   B  1 511 ? 57.373 -10.488 -29.409 0.00 23.50  ? 537  LEU   B HD12 1 
ATOM   19625 H HD13 . LEU   B  1 511 ? 55.807 -11.188 -29.898 0.00 23.41  ? 537  LEU   B HD13 1 
ATOM   19626 H HD21 . LEU   B  1 511 ? 57.584 -12.366 -32.668 0.00 23.92  ? 537  LEU   B HD21 1 
ATOM   19627 H HD22 . LEU   B  1 511 ? 55.902 -12.305 -32.112 0.00 23.80  ? 537  LEU   B HD22 1 
ATOM   19628 H HD23 . LEU   B  1 511 ? 56.403 -11.311 -33.492 0.00 23.44  ? 537  LEU   B HD23 1 
ATOM   19629 N N    . THR   B  1 512 ? 55.769 -6.322  -33.769 1.00 17.34  ? 538  THR   B N    1 
ATOM   19630 C CA   . THR   B  1 512 ? 54.781 -5.275  -33.934 1.00 17.19  ? 538  THR   B CA   1 
ATOM   19631 C C    . THR   B  1 512 ? 53.713 -5.614  -34.954 1.00 17.87  ? 538  THR   B C    1 
ATOM   19632 O O    . THR   B  1 512 ? 53.923 -6.455  -35.820 1.00 17.32  ? 538  THR   B O    1 
ATOM   19633 C CB   . THR   B  1 512 ? 55.449 -3.947  -34.323 1.00 18.28  ? 538  THR   B CB   1 
ATOM   19634 O OG1  . THR   B  1 512 ? 55.981 -4.042  -35.651 1.00 20.30  ? 538  THR   B OG1  1 
ATOM   19635 C CG2  . THR   B  1 512 ? 56.516 -3.533  -33.356 1.00 18.36  ? 538  THR   B CG2  1 
ATOM   19636 H H    . THR   B  1 512 ? 56.675 -6.094  -34.166 0.00 17.18  ? 538  THR   B H    1 
ATOM   19637 H HA   . THR   B  1 512 ? 54.285 -5.122  -32.976 0.00 16.83  ? 538  THR   B HA   1 
ATOM   19638 H HB   . THR   B  1 512 ? 54.686 -3.170  -34.317 0.00 17.76  ? 538  THR   B HB   1 
ATOM   19639 H HG1  . THR   B  1 512 ? 56.743 -4.679  -35.674 0.00 20.36  ? 538  THR   B HG1  1 
ATOM   19640 H HG21 . THR   B  1 512 ? 56.817 -2.506  -33.553 0.00 18.05  ? 538  THR   B HG21 1 
ATOM   19641 H HG22 . THR   B  1 512 ? 56.141 -3.607  -32.337 0.00 18.27  ? 538  THR   B HG22 1 
ATOM   19642 H HG23 . THR   B  1 512 ? 57.389 -4.177  -33.455 0.00 18.29  ? 538  THR   B HG23 1 
ATOM   19643 N N    . ASN   B  1 513 ? 52.563 -4.942  -34.845 1.00 18.55  ? 539  ASN   B N    1 
ATOM   19644 C CA   . ASN   B  1 513 ? 51.507 -5.035  -35.839 1.00 18.86  ? 539  ASN   B CA   1 
ATOM   19645 C C    . ASN   B  1 513 ? 50.997 -6.443  -36.052 1.00 19.02  ? 539  ASN   B C    1 
ATOM   19646 O O    . ASN   B  1 513 ? 50.775 -6.857  -37.180 1.00 19.76  ? 539  ASN   B O    1 
ATOM   19647 C CB   . ASN   B  1 513 ? 51.985 -4.394  -37.154 1.00 20.46  ? 539  ASN   B CB   1 
ATOM   19648 C CG   . ASN   B  1 513 ? 52.228 -2.911  -37.005 1.00 24.84  ? 539  ASN   B CG   1 
ATOM   19649 O OD1  . ASN   B  1 513 ? 53.347 -2.459  -36.804 1.00 27.76  ? 539  ASN   B OD1  1 
ATOM   19650 N ND2  . ASN   B  1 513 ? 51.177 -2.122  -37.083 1.00 24.46  ? 539  ASN   B ND2  1 
ATOM   19651 H H    . ASN   B  1 513 ? 52.330 -4.355  -34.052 0.00 18.16  ? 539  ASN   B H    1 
ATOM   19652 H HA   . ASN   B  1 513 ? 50.662 -4.445  -35.487 0.00 18.39  ? 539  ASN   B HA   1 
ATOM   19653 H HB2  . ASN   B  1 513 ? 52.909 -4.860  -37.491 0.00 20.24  ? 539  ASN   B HB2  1 
ATOM   19654 H HB3  . ASN   B  1 513 ? 51.215 -4.508  -37.915 0.00 20.15  ? 539  ASN   B HB3  1 
ATOM   19655 H HD21 . ASN   B  1 513 ? 51.298 -1.119  -36.991 0.00 24.66  ? 539  ASN   B HD21 1 
ATOM   19656 H HD22 . ASN   B  1 513 ? 50.250 -2.509  -37.229 0.00 24.77  ? 539  ASN   B HD22 1 
ATOM   19657 N N    . ASN   B  1 514 ? 50.762 -7.164  -34.968 1.00 18.33  ? 540  ASN   B N    1 
ATOM   19658 C CA   . ASN   B  1 514 ? 50.169 -8.498  -35.010 1.00 17.78  ? 540  ASN   B CA   1 
ATOM   19659 C C    . ASN   B  1 514 ? 48.832 -8.407  -34.208 1.00 18.06  ? 540  ASN   B C    1 
ATOM   19660 O O    . ASN   B  1 514 ? 48.293 -7.313  -34.055 1.00 18.62  ? 540  ASN   B O    1 
ATOM   19661 C CB   . ASN   B  1 514 ? 51.192 -9.519  -34.452 1.00 17.65  ? 540  ASN   B CB   1 
ATOM   19662 C CG   . ASN   B  1 514 ? 52.221 -9.902  -35.486 1.00 18.69  ? 540  ASN   B CG   1 
ATOM   19663 O OD1  . ASN   B  1 514 ? 51.881 -10.496 -36.515 1.00 18.97  ? 540  ASN   B OD1  1 
ATOM   19664 N ND2  . ASN   B  1 514 ? 53.479 -9.567  -35.266 1.00 18.76  ? 540  ASN   B ND2  1 
ATOM   19665 H H    . ASN   B  1 514 ? 50.967 -6.855  -34.024 0.00 18.23  ? 540  ASN   B H    1 
ATOM   19666 H HA   . ASN   B  1 514 ? 49.903 -8.780  -36.028 0.00 17.75  ? 540  ASN   B HA   1 
ATOM   19667 H HB2  . ASN   B  1 514 ? 51.694 -9.080  -33.592 0.00 17.87  ? 540  ASN   B HB2  1 
ATOM   19668 H HB3  . ASN   B  1 514 ? 50.697 -10.441 -34.151 0.00 18.09  ? 540  ASN   B HB3  1 
ATOM   19669 H HD21 . ASN   B  1 514 ? 54.189 -9.814  -35.948 0.00 19.23  ? 540  ASN   B HD21 1 
ATOM   19670 H HD22 . ASN   B  1 514 ? 53.748 -9.063  -34.427 0.00 19.19  ? 540  ASN   B HD22 1 
ATOM   19671 N N    . ARG   B  1 515 ? 48.280 -9.514  -33.763 1.00 18.65  ? 541  ARG   B N    1 
ATOM   19672 C CA   . ARG   B  1 515 ? 47.092 -9.528  -32.893 1.00 20.03  ? 541  ARG   B CA   1 
ATOM   19673 C C    . ARG   B  1 515 ? 47.407 -10.486 -31.713 1.00 19.39  ? 541  ARG   B C    1 
ATOM   19674 O O    . ARG   B  1 515 ? 46.582 -11.290 -31.291 1.00 19.88  ? 541  ARG   B O    1 
ATOM   19675 C CB   . ARG   B  1 515 ? 45.806 -9.894  -33.687 1.00 24.17  ? 541  ARG   B CB   1 
ATOM   19676 C CG   . ARG   B  1 515 ? 45.996 -10.733 -34.939 1.00 31.69  ? 541  ARG   B CG   1 
ATOM   19677 C CD   . ARG   B  1 515 ? 44.672 -11.232 -35.502 1.00 37.68  ? 541  ARG   B CD   1 
ATOM   19678 N NE   . ARG   B  1 515 ? 43.901 -10.172 -36.147 1.00 43.56  ? 541  ARG   B NE   1 
ATOM   19679 C CZ   . ARG   B  1 515 ? 42.637 -10.297 -36.561 1.00 47.37  ? 541  ARG   B CZ   1 
ATOM   19680 N NH1  . ARG   B  1 515 ? 41.977 -11.439 -36.381 1.00 47.90  ? 541  ARG   B NH1  1 
ATOM   19681 N NH2  . ARG   B  1 515 ? 42.023 -9.280  -37.154 1.00 46.63  ? 541  ARG   B NH2  1 
ATOM   19682 H H    . ARG   B  1 515 ? 48.599 -10.449 -33.993 0.00 19.31  ? 541  ARG   B H    1 
ATOM   19683 H HA   . ARG   B  1 515 ? 46.933 -8.543  -32.456 0.00 20.79  ? 541  ARG   B HA   1 
ATOM   19684 H HB2  . ARG   B  1 515 ? 45.108 -10.416 -33.036 0.00 26.16  ? 541  ARG   B HB2  1 
ATOM   19685 H HB3  . ARG   B  1 515 ? 45.346 -8.960  -34.008 0.00 25.77  ? 541  ARG   B HB3  1 
ATOM   19686 H HG2  . ARG   B  1 515 ? 46.484 -10.131 -35.705 0.00 34.86  ? 541  ARG   B HG2  1 
ATOM   19687 H HG3  . ARG   B  1 515 ? 46.612 -11.598 -34.698 0.00 35.24  ? 541  ARG   B HG3  1 
ATOM   19688 H HD2  . ARG   B  1 515 ? 44.872 -12.000 -36.247 0.00 42.56  ? 541  ARG   B HD2  1 
ATOM   19689 H HD3  . ARG   B  1 515 ? 44.073 -11.648 -34.693 0.00 42.61  ? 541  ARG   B HD3  1 
ATOM   19690 H HE   . ARG   B  1 515 ? 44.369 -9.285  -36.307 0.00 49.05  ? 541  ARG   B HE   1 
ATOM   19691 H HH11 . ARG   B  1 515 ? 42.410 -12.243 -35.939 0.00 55.13  ? 541  ARG   B HH11 1 
ATOM   19692 H HH12 . ARG   B  1 515 ? 41.017 -11.518 -36.699 0.00 55.11  ? 541  ARG   B HH12 1 
ATOM   19693 H HH21 . ARG   B  1 515 ? 42.508 -8.399  -37.293 0.00 52.74  ? 541  ARG   B HH21 1 
ATOM   19694 H HH22 . ARG   B  1 515 ? 41.060 -9.372  -37.461 0.00 53.11  ? 541  ARG   B HH22 1 
ATOM   19695 N N    . LEU   B  1 516 ? 48.626 -10.372 -31.171 1.00 18.59  ? 542  LEU   B N    1 
ATOM   19696 C CA   . LEU   B  1 516 ? 49.094 -11.264 -30.123 1.00 18.64  ? 542  LEU   B CA   1 
ATOM   19697 C C    . LEU   B  1 516 ? 48.218 -11.264 -28.866 1.00 18.35  ? 542  LEU   B C    1 
ATOM   19698 O O    . LEU   B  1 516 ? 47.688 -10.235 -28.457 1.00 18.24  ? 542  LEU   B O    1 
ATOM   19699 C CB   . LEU   B  1 516 ? 50.562 -10.962 -29.780 1.00 19.45  ? 542  LEU   B CB   1 
ATOM   19700 C CG   . LEU   B  1 516 ? 51.566 -11.384 -30.879 1.00 21.93  ? 542  LEU   B CG   1 
ATOM   19701 C CD1  . LEU   B  1 516 ? 52.916 -10.772 -30.647 1.00 22.24  ? 542  LEU   B CD1  1 
ATOM   19702 C CD2  . LEU   B  1 516 ? 51.662 -12.927 -30.974 1.00 23.16  ? 542  LEU   B CD2  1 
ATOM   19703 H H    . LEU   B  1 516 ? 49.297 -9.655  -31.428 0.00 19.33  ? 542  LEU   B H    1 
ATOM   19704 H HA   . LEU   B  1 516 ? 49.025 -12.264 -30.548 0.00 20.08  ? 542  LEU   B HA   1 
ATOM   19705 H HB2  . LEU   B  1 516 ? 50.680 -9.892  -29.614 0.00 20.66  ? 542  LEU   B HB2  1 
ATOM   19706 H HB3  . LEU   B  1 516 ? 50.821 -11.497 -28.868 0.00 21.12  ? 542  LEU   B HB3  1 
ATOM   19707 H HG   . LEU   B  1 516 ? 51.211 -11.019 -31.842 0.00 23.60  ? 542  LEU   B HG   1 
ATOM   19708 H HD11 . LEU   B  1 516 ? 53.623 -11.225 -31.339 0.00 24.18  ? 542  LEU   B HD11 1 
ATOM   19709 H HD12 . LEU   B  1 516 ? 52.856 -9.698  -30.822 0.00 23.88  ? 542  LEU   B HD12 1 
ATOM   19710 H HD13 . LEU   B  1 516 ? 53.223 -10.965 -29.619 0.00 24.35  ? 542  LEU   B HD13 1 
ATOM   19711 H HD21 . LEU   B  1 516 ? 52.574 -13.201 -31.502 0.00 25.69  ? 542  LEU   B HD21 1 
ATOM   19712 H HD22 . LEU   B  1 516 ? 51.673 -13.355 -29.972 0.00 25.90  ? 542  LEU   B HD22 1 
ATOM   19713 H HD23 . LEU   B  1 516 ? 50.810 -13.308 -31.534 0.00 25.67  ? 542  LEU   B HD23 1 
ATOM   19714 N N    . ASP   B  1 517 ? 47.984 -12.452 -28.342 1.00 17.83  ? 543  ASP   B N    1 
ATOM   19715 C CA   . ASP   B  1 517 ? 47.135 -12.648 -27.172 1.00 18.35  ? 543  ASP   B CA   1 
ATOM   19716 C C    . ASP   B  1 517 ? 48.077 -12.911 -26.013 1.00 19.96  ? 543  ASP   B C    1 
ATOM   19717 O O    . ASP   B  1 517 ? 48.553 -14.031 -25.840 1.00 20.61  ? 543  ASP   B O    1 
ATOM   19718 C CB   . ASP   B  1 517 ? 46.194 -13.827 -27.435 1.00 18.46  ? 543  ASP   B CB   1 
ATOM   19719 C CG   . ASP   B  1 517 ? 45.202 -14.133 -26.334 1.00 23.49  ? 543  ASP   B CG   1 
ATOM   19720 O OD1  . ASP   B  1 517 ? 45.164 -13.373 -25.328 1.00 24.78  ? 543  ASP   B OD1  1 
ATOM   19721 O OD2  . ASP   B  1 517 ? 44.454 -15.123 -26.474 1.00 24.69  ? 543  ASP   B OD2  1 
ATOM   19722 H H    . ASP   B  1 517 ? 48.377 -13.320 -28.691 0.00 19.61  ? 543  ASP   B H    1 
ATOM   19723 H HA   . ASP   B  1 517 ? 46.533 -11.766 -26.958 0.00 20.16  ? 543  ASP   B HA   1 
ATOM   19724 H HB2  . ASP   B  1 517 ? 45.617 -13.603 -28.331 0.00 20.55  ? 543  ASP   B HB2  1 
ATOM   19725 H HB3  . ASP   B  1 517 ? 46.784 -14.726 -27.608 0.00 20.92  ? 543  ASP   B HB3  1 
ATOM   19726 N N    . PHE   B  1 518 ? 48.400 -11.859 -25.252 1.00 20.45  ? 544  PHE   B N    1 
ATOM   19727 C CA   . PHE   B  1 518 ? 49.306 -11.999 -24.116 1.00 21.45  ? 544  PHE   B CA   1 
ATOM   19728 C C    . PHE   B  1 518 ? 48.534 -12.637 -22.964 1.00 22.27  ? 544  PHE   B C    1 
ATOM   19729 O O    . PHE   B  1 518 ? 47.934 -11.933 -22.163 1.00 22.82  ? 544  PHE   B O    1 
ATOM   19730 C CB   . PHE   B  1 518 ? 49.912 -10.638 -23.750 1.00 21.45  ? 544  PHE   B CB   1 
ATOM   19731 C CG   . PHE   B  1 518 ? 50.777 -10.113 -24.875 1.00 22.26  ? 544  PHE   B CG   1 
ATOM   19732 C CD1  . PHE   B  1 518 ? 52.062 -10.594 -25.064 1.00 22.96  ? 544  PHE   B CD1  1 
ATOM   19733 C CD2  . PHE   B  1 518 ? 50.269 -9.216  -25.800 1.00 22.92  ? 544  PHE   B CD2  1 
ATOM   19734 C CE1  . PHE   B  1 518 ? 52.845 -10.137 -26.114 1.00 23.61  ? 544  PHE   B CE1  1 
ATOM   19735 C CE2  . PHE   B  1 518 ? 51.076 -8.724  -26.829 1.00 23.74  ? 544  PHE   B CE2  1 
ATOM   19736 C CZ   . PHE   B  1 518 ? 52.351 -9.198  -26.981 1.00 23.52  ? 544  PHE   B CZ   1 
ATOM   19737 H H    . PHE   B  1 518 ? 48.051 -10.917 -25.398 0.00 22.76  ? 544  PHE   B H    1 
ATOM   19738 H HA   . PHE   B  1 518 ? 50.128 -12.663 -24.376 0.00 24.59  ? 544  PHE   B HA   1 
ATOM   19739 H HB2  . PHE   B  1 518 ? 49.116 -9.919  -23.559 0.00 24.16  ? 544  PHE   B HB2  1 
ATOM   19740 H HB3  . PHE   B  1 518 ? 50.536 -10.748 -22.865 0.00 24.53  ? 544  PHE   B HB3  1 
ATOM   19741 H HD1  . PHE   B  1 518 ? 52.464 -11.320 -24.376 0.00 26.22  ? 544  PHE   B HD1  1 
ATOM   19742 H HD2  . PHE   B  1 518 ? 49.277 -8.821  -25.670 0.00 25.28  ? 544  PHE   B HD2  1 
ATOM   19743 H HE1  . PHE   B  1 518 ? 53.853 -10.498 -26.229 0.00 26.54  ? 544  PHE   B HE1  1 
ATOM   19744 H HE2  . PHE   B  1 518 ? 50.681 -8.004  -27.525 0.00 25.81  ? 544  PHE   B HE2  1 
ATOM   19745 H HZ   . PHE   B  1 518 ? 52.960 -8.845  -27.795 0.00 25.74  ? 544  PHE   B HZ   1 
ATOM   19746 N N    . ASP   B  1 519 ? 48.510 -13.986 -22.923 1.00 21.78  ? 545  ASP   B N    1 
ATOM   19747 C CA   . ASP   B  1 519 ? 47.732 -14.724 -21.933 1.00 22.15  ? 545  ASP   B CA   1 
ATOM   19748 C C    . ASP   B  1 519 ? 48.537 -15.830 -21.234 1.00 22.76  ? 545  ASP   B C    1 
ATOM   19749 O O    . ASP   B  1 519 ? 47.958 -16.835 -20.825 1.00 22.20  ? 545  ASP   B O    1 
ATOM   19750 C CB   . ASP   B  1 519 ? 46.503 -15.341 -22.631 1.00 22.51  ? 545  ASP   B CB   1 
ATOM   19751 C CG   . ASP   B  1 519 ? 45.431 -15.784 -21.671 1.00 26.20  ? 545  ASP   B CG   1 
ATOM   19752 O OD1  . ASP   B  1 519 ? 45.269 -15.125 -20.633 1.00 28.08  ? 545  ASP   B OD1  1 
ATOM   19753 O OD2  . ASP   B  1 519 ? 44.752 -16.796 -21.959 1.00 26.04  ? 545  ASP   B OD2  1 
ATOM   19754 H H    . ASP   B  1 519 ? 49.022 -14.583 -23.563 0.00 25.62  ? 545  ASP   B H    1 
ATOM   19755 H HA   . ASP   B  1 519 ? 47.393 -14.038 -21.160 0.00 26.42  ? 545  ASP   B HA   1 
ATOM   19756 H HB2  . ASP   B  1 519 ? 46.069 -14.597 -23.297 0.00 26.52  ? 545  ASP   B HB2  1 
ATOM   19757 H HB3  . ASP   B  1 519 ? 46.820 -16.211 -23.205 0.00 26.98  ? 545  ASP   B HB3  1 
ATOM   19758 N N    . ASN   B  1 520 ? 49.851 -15.667 -21.110 1.00 23.76  ? 546  ASN   B N    1 
ATOM   19759 C CA   . ASN   B  1 520 ? 50.680 -16.676 -20.441 1.00 25.55  ? 546  ASN   B CA   1 
ATOM   19760 C C    . ASN   B  1 520 ? 51.896 -15.998 -19.821 1.00 25.92  ? 546  ASN   B C    1 
ATOM   19761 O O    . ASN   B  1 520 ? 52.658 -15.361 -20.542 1.00 26.08  ? 546  ASN   B O    1 
ATOM   19762 C CB   . ASN   B  1 520 ? 51.104 -17.794 -21.427 1.00 28.96  ? 546  ASN   B CB   1 
ATOM   19763 C CG   . ASN   B  1 520 ? 51.724 -18.911 -20.710 1.00 35.55  ? 546  ASN   B CG   1 
ATOM   19764 O OD1  . ASN   B  1 520 ? 52.915 -18.825 -20.407 1.00 36.06  ? 546  ASN   B OD1  1 
ATOM   19765 N ND2  . ASN   B  1 520 ? 51.092 -20.047 -20.502 1.00 41.52  ? 546  ASN   B ND2  1 
ATOM   19766 H H    . ASN   B  1 520 ? 50.377 -14.865 -21.442 0.00 28.61  ? 546  ASN   B H    1 
ATOM   19767 H HA   . ASN   B  1 520 ? 50.108 -17.128 -19.632 0.00 31.83  ? 546  ASN   B HA   1 
ATOM   19768 H HB2  . ASN   B  1 520 ? 50.225 -18.164 -21.954 0.00 35.70  ? 546  ASN   B HB2  1 
ATOM   19769 H HB3  . ASN   B  1 520 ? 51.830 -17.396 -22.135 0.00 35.51  ? 546  ASN   B HB3  1 
ATOM   19770 H HD21 . ASN   B  1 520 ? 51.355 -19.984 -19.540 0.00 52.04  ? 546  ASN   B HD21 1 
ATOM   19771 H HD22 . ASN   B  1 520 ? 50.199 -20.307 -20.904 0.00 51.73  ? 546  ASN   B HD22 1 
ATOM   19772 N N    . ALA   B  1 521 ? 52.080 -16.126 -18.492 1.00 26.36  ? 547  ALA   B N    1 
ATOM   19773 C CA   . ALA   B  1 521 ? 53.198 -15.496 -17.775 1.00 26.78  ? 547  ALA   B CA   1 
ATOM   19774 C C    . ALA   B  1 521 ? 54.597 -15.939 -18.233 1.00 27.01  ? 547  ALA   B C    1 
ATOM   19775 O O    . ALA   B  1 521 ? 55.565 -15.269 -17.887 1.00 27.10  ? 547  ALA   B O    1 
ATOM   19776 C CB   . ALA   B  1 521 ? 53.051 -15.728 -16.278 1.00 26.89  ? 547  ALA   B CB   1 
ATOM   19777 H H    . ALA   B  1 521 ? 51.472 -16.662 -17.882 0.00 33.25  ? 547  ALA   B H    1 
ATOM   19778 H HA   . ALA   B  1 521 ? 53.137 -14.421 -17.938 0.00 33.28  ? 547  ALA   B HA   1 
ATOM   19779 H HB1  . ALA   B  1 521 ? 53.913 -15.304 -15.763 0.00 34.42  ? 547  ALA   B HB1  1 
ATOM   19780 H HB2  . ALA   B  1 521 ? 52.139 -15.246 -15.931 0.00 34.15  ? 547  ALA   B HB2  1 
ATOM   19781 H HB3  . ALA   B  1 521 ? 53.005 -16.799 -16.087 0.00 34.63  ? 547  ALA   B HB3  1 
ATOM   19782 N N    . SER   B  1 522 ? 54.717 -17.065 -18.959 1.00 26.87  ? 548  SER   B N    1 
ATOM   19783 C CA   . SER   B  1 522 ? 56.011 -17.561 -19.433 1.00 27.25  ? 548  SER   B CA   1 
ATOM   19784 C C    . SER   B  1 522 ? 56.335 -17.136 -20.878 1.00 26.43  ? 548  SER   B C    1 
ATOM   19785 O O    . SER   B  1 522 ? 57.338 -17.587 -21.420 1.00 26.18  ? 548  SER   B O    1 
ATOM   19786 C CB   . SER   B  1 522 ? 56.057 -19.085 -19.350 1.00 29.87  ? 548  SER   B CB   1 
ATOM   19787 O OG   . SER   B  1 522 ? 55.664 -19.537 -18.067 1.00 33.38  ? 548  SER   B OG   1 
ATOM   19788 H H    . SER   B  1 522 ? 53.943 -17.660 -19.236 0.00 34.02  ? 548  SER   B H    1 
ATOM   19789 H HA   . SER   B  1 522 ? 56.811 -17.189 -18.795 0.00 34.85  ? 548  SER   B HA   1 
ATOM   19790 H HB2  . SER   B  1 522 ? 55.380 -19.501 -20.096 0.00 38.18  ? 548  SER   B HB2  1 
ATOM   19791 H HB3  . SER   B  1 522 ? 57.074 -19.425 -19.541 0.00 38.56  ? 548  SER   B HB3  1 
ATOM   19792 H HG   . SER   B  1 522 ? 55.708 -20.528 -18.030 0.00 43.39  ? 548  SER   B HG   1 
ATOM   19793 N N    . ALA   B  1 523 ? 55.510 -16.284 -21.507 1.00 25.22  ? 549  ALA   B N    1 
ATOM   19794 C CA   . ALA   B  1 523 ? 55.750 -15.851 -22.883 1.00 24.34  ? 549  ALA   B CA   1 
ATOM   19795 C C    . ALA   B  1 523 ? 57.159 -15.289 -23.099 1.00 22.95  ? 549  ALA   B C    1 
ATOM   19796 O O    . ALA   B  1 523 ? 57.619 -14.486 -22.292 1.00 22.37  ? 549  ALA   B O    1 
ATOM   19797 C CB   . ALA   B  1 523 ? 54.732 -14.781 -23.268 1.00 24.38  ? 549  ALA   B CB   1 
ATOM   19798 H H    . ALA   B  1 523 ? 54.678 -15.875 -21.096 0.00 31.09  ? 549  ALA   B H    1 
ATOM   19799 H HA   . ALA   B  1 523 ? 55.609 -16.702 -23.548 0.00 29.78  ? 549  ALA   B HA   1 
ATOM   19800 H HB1  . ALA   B  1 523 ? 54.926 -14.462 -24.291 0.00 28.94  ? 549  ALA   B HB1  1 
ATOM   19801 H HB2  . ALA   B  1 523 ? 53.731 -15.201 -23.193 0.00 29.27  ? 549  ALA   B HB2  1 
ATOM   19802 H HB3  . ALA   B  1 523 ? 54.835 -13.934 -22.590 0.00 29.19  ? 549  ALA   B HB3  1 
ATOM   19803 N N    . LEU   B  1 524 ? 57.849 -15.729 -24.169 1.00 22.04  ? 550  LEU   B N    1 
ATOM   19804 C CA   . LEU   B  1 524 ? 59.158 -15.200 -24.554 1.00 22.77  ? 550  LEU   B CA   1 
ATOM   19805 C C    . LEU   B  1 524 ? 60.310 -15.436 -23.573 1.00 23.98  ? 550  LEU   B C    1 
ATOM   19806 O O    . LEU   B  1 524 ? 61.445 -15.099 -23.922 1.00 24.33  ? 550  LEU   B O    1 
ATOM   19807 C CB   . LEU   B  1 524 ? 59.047 -13.687 -24.847 1.00 22.71  ? 550  LEU   B CB   1 
ATOM   19808 C CG   . LEU   B  1 524 ? 58.022 -13.287 -25.903 1.00 24.21  ? 550  LEU   B CG   1 
ATOM   19809 C CD1  . LEU   B  1 524 ? 57.946 -11.798 -26.036 1.00 24.19  ? 550  LEU   B CD1  1 
ATOM   19810 C CD2  . LEU   B  1 524 ? 58.376 -13.900 -27.254 1.00 24.88  ? 550  LEU   B CD2  1 
ATOM   19811 H H    . LEU   B  1 524 ? 57.517 -16.455 -24.796 0.00 26.91  ? 550  LEU   B H    1 
ATOM   19812 H HA   . LEU   B  1 524 ? 59.448 -15.695 -25.480 0.00 27.71  ? 550  LEU   B HA   1 
ATOM   19813 H HB2  . LEU   B  1 524 ? 58.792 -13.163 -23.927 0.00 27.19  ? 550  LEU   B HB2  1 
ATOM   19814 H HB3  . LEU   B  1 524 ? 60.014 -13.328 -25.195 0.00 27.13  ? 550  LEU   B HB3  1 
ATOM   19815 H HG   . LEU   B  1 524 ? 57.036 -13.648 -25.615 0.00 28.47  ? 550  LEU   B HG   1 
ATOM   19816 H HD11 . LEU   B  1 524 ? 57.159 -11.537 -26.742 0.00 27.71  ? 550  LEU   B HD11 1 
ATOM   19817 H HD12 . LEU   B  1 524 ? 57.724 -11.366 -25.062 0.00 28.11  ? 550  LEU   B HD12 1 
ATOM   19818 H HD13 . LEU   B  1 524 ? 58.906 -11.428 -26.394 0.00 28.00  ? 550  LEU   B HD13 1 
ATOM   19819 H HD21 . LEU   B  1 524 ? 57.928 -13.306 -28.049 0.00 28.81  ? 550  LEU   B HD21 1 
ATOM   19820 H HD22 . LEU   B  1 524 ? 59.458 -13.913 -27.372 0.00 29.32  ? 550  LEU   B HD22 1 
ATOM   19821 H HD23 . LEU   B  1 524 ? 57.988 -14.918 -27.291 0.00 29.41  ? 550  LEU   B HD23 1 
ATOM   19822 N N    . THR   B  1 525 ? 60.061 -16.079 -22.416 1.00 24.68  ? 551  THR   B N    1 
ATOM   19823 C CA   . THR   B  1 525 ? 61.085 -16.328 -21.388 1.00 25.88  ? 551  THR   B CA   1 
ATOM   19824 C C    . THR   B  1 525 ? 62.223 -17.254 -21.852 1.00 26.59  ? 551  THR   B C    1 
ATOM   19825 O O    . THR   B  1 525 ? 63.295 -17.237 -21.236 1.00 27.35  ? 551  THR   B O    1 
ATOM   19826 C CB   . THR   B  1 525 ? 60.429 -16.833 -20.088 1.00 27.31  ? 551  THR   B CB   1 
ATOM   19827 O OG1  . THR   B  1 525 ? 59.729 -18.054 -20.349 1.00 28.48  ? 551  THR   B OG1  1 
ATOM   19828 C CG2  . THR   B  1 525 ? 59.462 -15.795 -19.474 1.00 27.79  ? 551  THR   B CG2  1 
ATOM   19829 H H    . THR   B  1 525 ? 59.155 -16.460 -22.165 0.00 30.99  ? 551  THR   B H    1 
ATOM   19830 H HA   . THR   B  1 525 ? 61.547 -15.371 -21.151 0.00 32.85  ? 551  THR   B HA   1 
ATOM   19831 H HB   . THR   B  1 525 ? 61.211 -17.030 -19.357 0.00 35.52  ? 551  THR   B HB   1 
ATOM   19832 H HG1  . THR   B  1 525 ? 58.866 -17.887 -20.810 0.00 36.31  ? 551  THR   B HG1  1 
ATOM   19833 H HG21 . THR   B  1 525 ? 59.227 -16.066 -18.446 0.00 35.68  ? 551  THR   B HG21 1 
ATOM   19834 H HG22 . THR   B  1 525 ? 59.919 -14.808 -19.494 0.00 35.13  ? 551  THR   B HG22 1 
ATOM   19835 H HG23 . THR   B  1 525 ? 58.536 -15.755 -20.046 0.00 34.99  ? 551  THR   B HG23 1 
ATOM   19836 N N    . GLU   B  1 526 ? 62.020 -18.043 -22.933 1.00 26.25  ? 552  GLU   B N    1 
ATOM   19837 C CA   . GLU   B  1 526 ? 63.086 -18.868 -23.513 1.00 26.22  ? 552  GLU   B CA   1 
ATOM   19838 C C    . GLU   B  1 526 ? 64.205 -17.984 -24.123 1.00 26.20  ? 552  GLU   B C    1 
ATOM   19839 O O    . GLU   B  1 526 ? 65.301 -18.479 -24.332 1.00 26.87  ? 552  GLU   B O    1 
ATOM   19840 C CB   . GLU   B  1 526 ? 62.540 -19.871 -24.566 1.00 27.09  ? 552  GLU   B CB   1 
ATOM   19841 C CG   . GLU   B  1 526 ? 62.060 -19.283 -25.895 1.00 27.46  ? 552  GLU   B CG   1 
ATOM   19842 C CD   . GLU   B  1 526 ? 60.627 -18.796 -25.892 1.00 30.44  ? 552  GLU   B CD   1 
ATOM   19843 O OE1  . GLU   B  1 526 ? 60.190 -18.249 -24.859 1.00 31.88  ? 552  GLU   B OE1  1 
ATOM   19844 O OE2  . GLU   B  1 526 ? 59.929 -18.966 -26.916 1.00 30.44  ? 552  GLU   B OE2  1 
ATOM   19845 H H    . GLU   B  1 526 ? 61.138 -18.135 -23.426 0.00 33.45  ? 552  GLU   B H    1 
ATOM   19846 H HA   . GLU   B  1 526 ? 63.536 -19.457 -22.716 0.00 34.59  ? 552  GLU   B HA   1 
ATOM   19847 H HB2  . GLU   B  1 526 ? 63.328 -20.585 -24.798 0.00 35.47  ? 552  GLU   B HB2  1 
ATOM   19848 H HB3  . GLU   B  1 526 ? 61.695 -20.399 -24.127 0.00 35.21  ? 552  GLU   B HB3  1 
ATOM   19849 H HG2  . GLU   B  1 526 ? 62.685 -18.444 -26.197 0.00 34.67  ? 552  GLU   B HG2  1 
ATOM   19850 H HG3  . GLU   B  1 526 ? 62.127 -20.066 -26.650 0.00 35.05  ? 552  GLU   B HG3  1 
ATOM   19851 N N    . LEU   B  1 527 ? 63.921 -16.696 -24.428 1.00 25.24  ? 553  LEU   B N    1 
ATOM   19852 C CA   . LEU   B  1 527 ? 64.889 -15.763 -24.977 1.00 25.25  ? 553  LEU   B CA   1 
ATOM   19853 C C    . LEU   B  1 527 ? 65.662 -15.081 -23.853 1.00 26.53  ? 553  LEU   B C    1 
ATOM   19854 O O    . LEU   B  1 527 ? 65.500 -13.886 -23.613 1.00 26.52  ? 553  LEU   B O    1 
ATOM   19855 C CB   . LEU   B  1 527 ? 64.183 -14.721 -25.880 1.00 24.74  ? 553  LEU   B CB   1 
ATOM   19856 C CG   . LEU   B  1 527 ? 63.475 -15.302 -27.115 1.00 25.00  ? 553  LEU   B CG   1 
ATOM   19857 C CD1  . LEU   B  1 527 ? 62.804 -14.196 -27.933 1.00 24.87  ? 553  LEU   B CD1  1 
ATOM   19858 C CD2  . LEU   B  1 527 ? 64.456 -16.062 -28.010 1.00 25.35  ? 553  LEU   B CD2  1 
ATOM   19859 H H    . LEU   B  1 527 ? 63.006 -16.272 -24.314 0.00 31.80  ? 553  LEU   B H    1 
ATOM   19860 H HA   . LEU   B  1 527 ? 65.615 -16.301 -25.584 0.00 32.13  ? 553  LEU   B HA   1 
ATOM   19861 H HB2  . LEU   B  1 527 ? 63.434 -14.192 -25.293 0.00 30.46  ? 553  LEU   B HB2  1 
ATOM   19862 H HB3  . LEU   B  1 527 ? 64.927 -14.011 -26.237 0.00 30.52  ? 553  LEU   B HB3  1 
ATOM   19863 H HG   . LEU   B  1 527 ? 62.704 -15.999 -26.791 0.00 30.79  ? 553  LEU   B HG   1 
ATOM   19864 H HD11 . LEU   B  1 527 ? 62.219 -14.650 -28.732 0.00 29.73  ? 553  LEU   B HD11 1 
ATOM   19865 H HD12 . LEU   B  1 527 ? 62.157 -13.616 -27.278 0.00 29.73  ? 553  LEU   B HD12 1 
ATOM   19866 H HD13 . LEU   B  1 527 ? 63.574 -13.553 -28.356 0.00 29.77  ? 553  LEU   B HD13 1 
ATOM   19867 H HD21 . LEU   B  1 527 ? 64.135 -15.982 -29.047 0.00 31.04  ? 553  LEU   B HD21 1 
ATOM   19868 H HD22 . LEU   B  1 527 ? 65.452 -15.638 -27.891 0.00 31.46  ? 553  LEU   B HD22 1 
ATOM   19869 H HD23 . LEU   B  1 527 ? 64.455 -17.107 -27.706 0.00 31.75  ? 553  LEU   B HD23 1 
ATOM   19870 N N    . SER   B  1 528 ? 66.570 -15.836 -23.218 1.00 27.45  ? 554  SER   B N    1 
ATOM   19871 C CA   . SER   B  1 528 ? 67.337 -15.360 -22.063 1.00 27.97  ? 554  SER   B CA   1 
ATOM   19872 C C    . SER   B  1 528 ? 68.249 -14.141 -22.343 1.00 26.87  ? 554  SER   B C    1 
ATOM   19873 O O    . SER   B  1 528 ? 68.465 -13.330 -21.444 1.00 27.26  ? 554  SER   B O    1 
ATOM   19874 C CB   . SER   B  1 528 ? 68.135 -16.504 -21.437 1.00 30.52  ? 554  SER   B CB   1 
ATOM   19875 O OG   . SER   B  1 528 ? 69.372 -16.752 -22.082 1.00 34.51  ? 554  SER   B OG   1 
ATOM   19876 H H    . SER   B  1 528 ? 66.801 -16.782 -23.504 0.00 35.78  ? 554  SER   B H    1 
ATOM   19877 H HA   . SER   B  1 528 ? 66.618 -15.036 -21.311 0.00 36.47  ? 554  SER   B HA   1 
ATOM   19878 H HB2  . SER   B  1 528 ? 68.342 -16.240 -20.401 0.00 40.68  ? 554  SER   B HB2  1 
ATOM   19879 H HB3  . SER   B  1 528 ? 67.538 -17.414 -21.459 0.00 40.48  ? 554  SER   B HB3  1 
ATOM   19880 H HG   . SER   B  1 528 ? 69.258 -16.729 -23.068 0.00 45.19  ? 554  SER   B HG   1 
ATOM   19881 N N    . ASP   B  1 529 ? 68.759 -13.997 -23.569 1.00 25.57  ? 555  ASP   B N    1 
ATOM   19882 C CA   . ASP   B  1 529 ? 69.621 -12.871 -23.923 1.00 25.20  ? 555  ASP   B CA   1 
ATOM   19883 C C    . ASP   B  1 529 ? 68.847 -11.677 -24.528 1.00 23.26  ? 555  ASP   B C    1 
ATOM   19884 O O    . ASP   B  1 529 ? 69.477 -10.761 -25.050 1.00 23.00  ? 555  ASP   B O    1 
ATOM   19885 C CB   . ASP   B  1 529 ? 70.678 -13.343 -24.940 1.00 28.10  ? 555  ASP   B CB   1 
ATOM   19886 C CG   . ASP   B  1 529 ? 71.663 -14.362 -24.403 1.00 35.93  ? 555  ASP   B CG   1 
ATOM   19887 O OD1  . ASP   B  1 529 ? 71.761 -14.497 -23.167 1.00 36.73  ? 555  ASP   B OD1  1 
ATOM   19888 O OD2  . ASP   B  1 529 ? 72.360 -14.999 -25.223 1.00 40.59  ? 555  ASP   B OD2  1 
ATOM   19889 H H    . ASP   B  1 529 ? 68.599 -14.644 -24.334 0.00 33.17  ? 555  ASP   B H    1 
ATOM   19890 H HA   . ASP   B  1 529 ? 70.147 -12.501 -23.044 0.00 33.00  ? 555  ASP   B HA   1 
ATOM   19891 H HB2  . ASP   B  1 529 ? 70.178 -13.780 -25.803 0.00 36.04  ? 555  ASP   B HB2  1 
ATOM   19892 H HB3  . ASP   B  1 529 ? 71.272 -12.486 -25.250 0.00 36.22  ? 555  ASP   B HB3  1 
ATOM   19893 N N    . LEU   B  1 530 ? 67.509 -11.672 -24.464 1.00 22.47  ? 556  LEU   B N    1 
ATOM   19894 C CA   . LEU   B  1 530 ? 66.723 -10.594 -25.073 1.00 21.90  ? 556  LEU   B CA   1 
ATOM   19895 C C    . LEU   B  1 530 ? 67.076 -9.224  -24.474 1.00 21.95  ? 556  LEU   B C    1 
ATOM   19896 O O    . LEU   B  1 530 ? 67.071 -9.065  -23.248 1.00 21.48  ? 556  LEU   B O    1 
ATOM   19897 C CB   . LEU   B  1 530 ? 65.227 -10.874 -24.902 1.00 21.66  ? 556  LEU   B CB   1 
ATOM   19898 C CG   . LEU   B  1 530 ? 64.258 -10.055 -25.792 1.00 22.78  ? 556  LEU   B CG   1 
ATOM   19899 C CD1  . LEU   B  1 530 ? 64.548 -10.268 -27.266 1.00 22.82  ? 556  LEU   B CD1  1 
ATOM   19900 C CD2  . LEU   B  1 530 ? 62.834 -10.446 -25.477 1.00 23.06  ? 556  LEU   B CD2  1 
ATOM   19901 H H    . LEU   B  1 530 ? 66.943 -12.367 -23.989 0.00 28.47  ? 556  LEU   B H    1 
ATOM   19902 H HA   . LEU   B  1 530 ? 66.969 -10.582 -26.134 0.00 26.79  ? 556  LEU   B HA   1 
ATOM   19903 H HB2  . LEU   B  1 530 ? 65.040 -11.922 -25.129 0.00 26.59  ? 556  LEU   B HB2  1 
ATOM   19904 H HB3  . LEU   B  1 530 ? 64.961 -10.672 -23.866 0.00 26.62  ? 556  LEU   B HB3  1 
ATOM   19905 H HG   . LEU   B  1 530 ? 64.375 -8.994  -25.572 0.00 27.03  ? 556  LEU   B HG   1 
ATOM   19906 H HD11 . LEU   B  1 530 ? 63.685 -9.959  -27.852 0.00 26.57  ? 556  LEU   B HD11 1 
ATOM   19907 H HD12 . LEU   B  1 530 ? 65.406 -9.662  -27.553 0.00 26.96  ? 556  LEU   B HD12 1 
ATOM   19908 H HD13 . LEU   B  1 530 ? 64.759 -11.323 -27.439 0.00 27.21  ? 556  LEU   B HD13 1 
ATOM   19909 H HD21 . LEU   B  1 530 ? 62.156 -9.946  -26.165 0.00 26.93  ? 556  LEU   B HD21 1 
ATOM   19910 H HD22 . LEU   B  1 530 ? 62.733 -11.526 -25.581 0.00 27.53  ? 556  LEU   B HD22 1 
ATOM   19911 H HD23 . LEU   B  1 530 ? 62.606 -10.150 -24.454 0.00 27.49  ? 556  LEU   B HD23 1 
ATOM   19912 N N    . GLU   B  1 531 ? 67.408 -8.256  -25.352 1.00 21.60  ? 557  GLU   B N    1 
ATOM   19913 C CA   . GLU   B  1 531 ? 67.747 -6.885  -24.965 1.00 22.20  ? 557  GLU   B CA   1 
ATOM   19914 C C    . GLU   B  1 531 ? 66.700 -5.863  -25.414 1.00 21.89  ? 557  GLU   B C    1 
ATOM   19915 O O    . GLU   B  1 531 ? 66.503 -4.860  -24.726 1.00 21.92  ? 557  GLU   B O    1 
ATOM   19916 C CB   . GLU   B  1 531 ? 69.121 -6.490  -25.515 1.00 24.22  ? 557  GLU   B CB   1 
ATOM   19917 C CG   . GLU   B  1 531 ? 70.251 -7.260  -24.847 1.00 26.97  ? 557  GLU   B CG   1 
ATOM   19918 C CD   . GLU   B  1 531 ? 71.633 -6.685  -25.053 1.00 33.37  ? 557  GLU   B CD   1 
ATOM   19919 O OE1  . GLU   B  1 531 ? 71.744 -5.464  -25.304 1.00 35.01  ? 557  GLU   B OE1  1 
ATOM   19920 O OE2  . GLU   B  1 531 ? 72.612 -7.453  -24.932 1.00 36.82  ? 557  GLU   B OE2  1 
ATOM   19921 H H    . GLU   B  1 531 ? 67.457 -8.399  -26.356 0.00 26.05  ? 557  GLU   B H    1 
ATOM   19922 H HA   . GLU   B  1 531 ? 67.817 -6.805  -23.883 0.00 27.27  ? 557  GLU   B HA   1 
ATOM   19923 H HB2  . GLU   B  1 531 ? 69.152 -6.699  -26.583 0.00 29.32  ? 557  GLU   B HB2  1 
ATOM   19924 H HB3  . GLU   B  1 531 ? 69.259 -5.424  -25.337 0.00 29.49  ? 557  GLU   B HB3  1 
ATOM   19925 H HG2  . GLU   B  1 531 ? 70.071 -7.291  -23.773 0.00 33.78  ? 557  GLU   B HG2  1 
ATOM   19926 H HG3  . GLU   B  1 531 ? 70.258 -8.274  -25.244 0.00 33.59  ? 557  GLU   B HG3  1 
ATOM   19927 N N    . VAL   B  1 532 ? 66.102 -6.061  -26.584 1.00 20.99  ? 558  VAL   B N    1 
ATOM   19928 C CA   . VAL   B  1 532 ? 65.112 -5.130  -27.133 1.00 20.62  ? 558  VAL   B CA   1 
ATOM   19929 C C    . VAL   B  1 532 ? 63.909 -5.942  -27.559 1.00 20.27  ? 558  VAL   B C    1 
ATOM   19930 O O    . VAL   B  1 532 ? 64.060 -6.918  -28.299 1.00 20.41  ? 558  VAL   B O    1 
ATOM   19931 C CB   . VAL   B  1 532 ? 65.682 -4.333  -28.327 1.00 20.82  ? 558  VAL   B CB   1 
ATOM   19932 C CG1  . VAL   B  1 532 ? 64.618 -3.390  -28.916 1.00 20.75  ? 558  VAL   B CG1  1 
ATOM   19933 C CG2  . VAL   B  1 532 ? 66.953 -3.566  -27.939 1.00 20.30  ? 558  VAL   B CG2  1 
ATOM   19934 H H    . VAL   B  1 532 ? 66.279 -6.853  -27.193 0.00 24.54  ? 558  VAL   B H    1 
ATOM   19935 H HA   . VAL   B  1 532 ? 64.794 -4.413  -26.379 0.00 23.60  ? 558  VAL   B HA   1 
ATOM   19936 H HB   . VAL   B  1 532 ? 65.956 -5.039  -29.109 0.00 23.53  ? 558  VAL   B HB   1 
ATOM   19937 H HG11 . VAL   B  1 532 ? 65.112 -2.625  -29.514 0.00 22.89  ? 558  VAL   B HG11 1 
ATOM   19938 H HG12 . VAL   B  1 532 ? 63.940 -3.959  -29.551 0.00 22.79  ? 558  VAL   B HG12 1 
ATOM   19939 H HG13 . VAL   B  1 532 ? 64.064 -2.926  -28.102 0.00 23.02  ? 558  VAL   B HG13 1 
ATOM   19940 H HG21 . VAL   B  1 532 ? 67.303 -2.994  -28.796 0.00 23.07  ? 558  VAL   B HG21 1 
ATOM   19941 H HG22 . VAL   B  1 532 ? 66.733 -2.897  -27.109 0.00 23.33  ? 558  VAL   B HG22 1 
ATOM   19942 H HG23 . VAL   B  1 532 ? 67.723 -4.277  -27.644 0.00 23.60  ? 558  VAL   B HG23 1 
ATOM   19943 N N    . LEU   B  1 533 ? 62.718 -5.545  -27.090 1.00 19.58  ? 559  LEU   B N    1 
ATOM   19944 C CA   . LEU   B  1 533 ? 61.477 -6.213  -27.431 1.00 19.75  ? 559  LEU   B CA   1 
ATOM   19945 C C    . LEU   B  1 533 ? 60.465 -5.160  -27.880 1.00 19.67  ? 559  LEU   B C    1 
ATOM   19946 O O    . LEU   B  1 533 ? 60.149 -4.248  -27.108 1.00 19.97  ? 559  LEU   B O    1 
ATOM   19947 C CB   . LEU   B  1 533 ? 60.948 -6.971  -26.212 1.00 20.11  ? 559  LEU   B CB   1 
ATOM   19948 C CG   . LEU   B  1 533 ? 59.615 -7.716  -26.386 1.00 21.85  ? 559  LEU   B CG   1 
ATOM   19949 C CD1  . LEU   B  1 533 ? 59.636 -8.664  -27.597 1.00 22.19  ? 559  LEU   B CD1  1 
ATOM   19950 C CD2  . LEU   B  1 533 ? 59.236 -8.470  -25.101 1.00 22.94  ? 559  LEU   B CD2  1 
ATOM   19951 H H    . LEU   B  1 533 ? 62.582 -4.757  -26.465 0.00 21.91  ? 559  LEU   B H    1 
ATOM   19952 H HA   . LEU   B  1 533 ? 61.634 -6.918  -28.246 0.00 21.83  ? 559  LEU   B HA   1 
ATOM   19953 H HB2  . LEU   B  1 533 ? 61.698 -7.700  -25.909 0.00 22.94  ? 559  LEU   B HB2  1 
ATOM   19954 H HB3  . LEU   B  1 533 ? 60.806 -6.253  -25.406 0.00 22.67  ? 559  LEU   B HB3  1 
ATOM   19955 H HG   . LEU   B  1 533 ? 58.842 -6.974  -26.563 0.00 24.29  ? 559  LEU   B HG   1 
ATOM   19956 H HD11 . LEU   B  1 533 ? 58.819 -9.378  -27.507 0.00 24.91  ? 559  LEU   B HD11 1 
ATOM   19957 H HD12 . LEU   B  1 533 ? 59.502 -8.071  -28.501 0.00 24.56  ? 559  LEU   B HD12 1 
ATOM   19958 H HD13 . LEU   B  1 533 ? 60.589 -9.187  -27.644 0.00 25.12  ? 559  LEU   B HD13 1 
ATOM   19959 H HD21 . LEU   B  1 533 ? 58.265 -8.944  -25.242 0.00 26.15  ? 559  LEU   B HD21 1 
ATOM   19960 H HD22 . LEU   B  1 533 ? 59.991 -9.227  -24.898 0.00 26.56  ? 559  LEU   B HD22 1 
ATOM   19961 H HD23 . LEU   B  1 533 ? 59.186 -7.763  -24.274 0.00 26.32  ? 559  LEU   B HD23 1 
ATOM   19962 N N    . ASP   B  1 534 ? 59.948 -5.290  -29.110 1.00 18.14  ? 560  ASP   B N    1 
ATOM   19963 C CA   . ASP   B  1 534 ? 58.967 -4.349  -29.644 1.00 17.37  ? 560  ASP   B CA   1 
ATOM   19964 C C    . ASP   B  1 534 ? 57.604 -5.054  -29.812 1.00 17.82  ? 560  ASP   B C    1 
ATOM   19965 O O    . ASP   B  1 534 ? 57.446 -5.904  -30.688 1.00 18.19  ? 560  ASP   B O    1 
ATOM   19966 C CB   . ASP   B  1 534 ? 59.464 -3.723  -30.971 1.00 18.41  ? 560  ASP   B CB   1 
ATOM   19967 C CG   . ASP   B  1 534 ? 58.794 -2.390  -31.327 1.00 20.32  ? 560  ASP   B CG   1 
ATOM   19968 O OD1  . ASP   B  1 534 ? 57.734 -2.068  -30.723 1.00 20.25  ? 560  ASP   B OD1  1 
ATOM   19969 O OD2  . ASP   B  1 534 ? 59.313 -1.685  -32.226 1.00 20.34  ? 560  ASP   B OD2  1 
ATOM   19970 H H    . ASP   B  1 534 ? 60.189 -6.032  -29.761 0.00 19.23  ? 560  ASP   B H    1 
ATOM   19971 H HA   . ASP   B  1 534 ? 58.833 -3.535  -28.936 0.00 17.95  ? 560  ASP   B HA   1 
ATOM   19972 H HB2  . ASP   B  1 534 ? 60.536 -3.546  -30.898 0.00 19.07  ? 560  ASP   B HB2  1 
ATOM   19973 H HB3  . ASP   B  1 534 ? 59.258 -4.404  -31.794 0.00 18.84  ? 560  ASP   B HB3  1 
ATOM   19974 N N    . LEU   B  1 535 ? 56.639 -4.729  -28.932 1.00 17.67  ? 561  LEU   B N    1 
ATOM   19975 C CA   . LEU   B  1 535 ? 55.272 -5.283  -28.977 1.00 17.81  ? 561  LEU   B CA   1 
ATOM   19976 C C    . LEU   B  1 535 ? 54.242 -4.236  -29.423 1.00 17.69  ? 561  LEU   B C    1 
ATOM   19977 O O    . LEU   B  1 535 ? 53.042 -4.411  -29.160 1.00 18.29  ? 561  LEU   B O    1 
ATOM   19978 C CB   . LEU   B  1 535 ? 54.874 -5.811  -27.585 1.00 18.14  ? 561  LEU   B CB   1 
ATOM   19979 C CG   . LEU   B  1 535 ? 55.832 -6.792  -26.924 1.00 20.11  ? 561  LEU   B CG   1 
ATOM   19980 C CD1  . LEU   B  1 535 ? 55.320 -7.227  -25.558 1.00 20.31  ? 561  LEU   B CD1  1 
ATOM   19981 C CD2  . LEU   B  1 535 ? 56.066 -8.030  -27.820 1.00 21.17  ? 561  LEU   B CD2  1 
ATOM   19982 H H    . LEU   B  1 535 ? 56.772 -4.081  -28.162 0.00 18.28  ? 561  LEU   B H    1 
ATOM   19983 H HA   . LEU   B  1 535 ? 55.215 -6.114  -29.677 0.00 18.28  ? 561  LEU   B HA   1 
ATOM   19984 H HB2  . LEU   B  1 535 ? 54.768 -4.960  -26.914 0.00 19.01  ? 561  LEU   B HB2  1 
ATOM   19985 H HB3  . LEU   B  1 535 ? 53.918 -6.326  -27.668 0.00 18.97  ? 561  LEU   B HB3  1 
ATOM   19986 H HG   . LEU   B  1 535 ? 56.771 -6.265  -26.768 0.00 21.77  ? 561  LEU   B HG   1 
ATOM   19987 H HD11 . LEU   B  1 535 ? 56.049 -7.892  -25.098 0.00 22.55  ? 561  LEU   B HD11 1 
ATOM   19988 H HD12 . LEU   B  1 535 ? 55.177 -6.346  -24.935 0.00 22.26  ? 561  LEU   B HD12 1 
ATOM   19989 H HD13 . LEU   B  1 535 ? 54.372 -7.750  -25.686 0.00 22.23  ? 561  LEU   B HD13 1 
ATOM   19990 H HD21 . LEU   B  1 535 ? 56.574 -8.798  -27.237 0.00 23.34  ? 561  LEU   B HD21 1 
ATOM   19991 H HD22 . LEU   B  1 535 ? 55.105 -8.403  -28.170 0.00 22.95  ? 561  LEU   B HD22 1 
ATOM   19992 H HD23 . LEU   B  1 535 ? 56.686 -7.745  -28.668 0.00 22.89  ? 561  LEU   B HD23 1 
ATOM   19993 N N    . SER   B  1 536 ? 54.682 -3.158  -30.086 1.00 17.51  ? 562  SER   B N    1 
ATOM   19994 C CA   . SER   B  1 536 ? 53.788 -2.085  -30.519 1.00 17.94  ? 562  SER   B CA   1 
ATOM   19995 C C    . SER   B  1 536 ? 52.679 -2.588  -31.428 1.00 17.89  ? 562  SER   B C    1 
ATOM   19996 O O    . SER   B  1 536 ? 52.896 -3.527  -32.180 1.00 17.99  ? 562  SER   B O    1 
ATOM   19997 C CB   . SER   B  1 536 ? 54.557 -1.019  -31.293 1.00 20.07  ? 562  SER   B CB   1 
ATOM   19998 O OG   . SER   B  1 536 ? 55.621 -0.464  -30.541 1.00 24.01  ? 562  SER   B OG   1 
ATOM   19999 H H    . SER   B  1 536 ? 55.650 -2.988  -30.339 0.00 17.46  ? 562  SER   B H    1 
ATOM   20000 H HA   . SER   B  1 536 ? 53.339 -1.618  -29.644 0.00 17.83  ? 562  SER   B HA   1 
ATOM   20001 H HB2  . SER   B  1 536 ? 54.968 -1.472  -32.194 0.00 20.06  ? 562  SER   B HB2  1 
ATOM   20002 H HB3  . SER   B  1 536 ? 53.869 -0.220  -31.564 0.00 20.01  ? 562  SER   B HB3  1 
ATOM   20003 H HG   . SER   B  1 536 ? 56.388 -1.094  -30.519 0.00 25.13  ? 562  SER   B HG   1 
ATOM   20004 N N    . TYR   B  1 537 ? 51.510 -1.950  -31.380 1.00 17.83  ? 563  TYR   B N    1 
ATOM   20005 C CA   . TYR   B  1 537 ? 50.388 -2.291  -32.248 1.00 18.69  ? 563  TYR   B CA   1 
ATOM   20006 C C    . TYR   B  1 537 ? 49.943 -3.765  -32.181 1.00 18.16  ? 563  TYR   B C    1 
ATOM   20007 O O    . TYR   B  1 537 ? 49.829 -4.431  -33.209 1.00 18.07  ? 563  TYR   B O    1 
ATOM   20008 C CB   . TYR   B  1 537 ? 50.714 -1.878  -33.693 1.00 20.07  ? 563  TYR   B CB   1 
ATOM   20009 C CG   . TYR   B  1 537 ? 50.928 -0.393  -33.840 1.00 22.04  ? 563  TYR   B CG   1 
ATOM   20010 C CD1  . TYR   B  1 537 ? 49.854 0.472   -33.991 1.00 23.53  ? 563  TYR   B CD1  1 
ATOM   20011 C CD2  . TYR   B  1 537 ? 52.208 0.144   -33.876 1.00 23.57  ? 563  TYR   B CD2  1 
ATOM   20012 C CE1  . TYR   B  1 537 ? 50.049 1.836   -34.179 1.00 25.24  ? 563  TYR   B CE1  1 
ATOM   20013 C CE2  . TYR   B  1 537 ? 52.414 1.505   -34.050 1.00 25.13  ? 563  TYR   B CE2  1 
ATOM   20014 C CZ   . TYR   B  1 537 ? 51.331 2.348   -34.200 1.00 26.96  ? 563  TYR   B CZ   1 
ATOM   20015 O OH   . TYR   B  1 537 ? 51.522 3.696   -34.369 1.00 31.30  ? 563  TYR   B OH   1 
ATOM   20016 H H    . TYR   B  1 537 ? 51.308 -1.187  -30.743 0.00 17.42  ? 563  TYR   B H    1 
ATOM   20017 H HA   . TYR   B  1 537 ? 49.531 -1.694  -31.938 0.00 18.31  ? 563  TYR   B HA   1 
ATOM   20018 H HB2  . TYR   B  1 537 ? 51.620 -2.373  -34.037 0.00 19.76  ? 563  TYR   B HB2  1 
ATOM   20019 H HB3  . TYR   B  1 537 ? 49.878 -2.141  -34.340 0.00 19.71  ? 563  TYR   B HB3  1 
ATOM   20020 H HD1  . TYR   B  1 537 ? 48.851 0.077   -33.986 0.00 23.78  ? 563  TYR   B HD1  1 
ATOM   20021 H HD2  . TYR   B  1 537 ? 53.060 -0.506  -33.769 0.00 23.89  ? 563  TYR   B HD2  1 
ATOM   20022 H HE1  . TYR   B  1 537 ? 49.202 2.492   -34.286 0.00 25.73  ? 563  TYR   B HE1  1 
ATOM   20023 H HE2  . TYR   B  1 537 ? 53.421 1.892   -34.066 0.00 25.65  ? 563  TYR   B HE2  1 
ATOM   20024 H HH   . TYR   B  1 537 ? 52.488 3.924   -34.370 0.00 32.98  ? 563  TYR   B HH   1 
ATOM   20025 N N    . ASN   B  1 538 ? 49.691 -4.259  -30.965 1.00 17.11  ? 564  ASN   B N    1 
ATOM   20026 C CA   . ASN   B  1 538 ? 49.107 -5.582  -30.716 1.00 17.27  ? 564  ASN   B CA   1 
ATOM   20027 C C    . ASN   B  1 538 ? 47.886 -5.361  -29.797 1.00 17.60  ? 564  ASN   B C    1 
ATOM   20028 O O    . ASN   B  1 538 ? 47.725 -6.052  -28.798 1.00 18.71  ? 564  ASN   B O    1 
ATOM   20029 C CB   . ASN   B  1 538 ? 50.130 -6.513  -30.053 1.00 17.10  ? 564  ASN   B CB   1 
ATOM   20030 C CG   . ASN   B  1 538 ? 51.062 -7.134  -31.054 1.00 16.97  ? 564  ASN   B CG   1 
ATOM   20031 O OD1  . ASN   B  1 538 ? 50.661 -8.023  -31.790 1.00 16.72  ? 564  ASN   B OD1  1 
ATOM   20032 N ND2  . ASN   B  1 538 ? 52.303 -6.689  -31.118 1.00 17.52  ? 564  ASN   B ND2  1 
ATOM   20033 H H    . ASN   B  1 538 ? 49.890 -3.754  -30.107 0.00 16.84  ? 564  ASN   B H    1 
ATOM   20034 H HA   . ASN   B  1 538 ? 48.743 -6.031  -31.638 0.00 17.11  ? 564  ASN   B HA   1 
ATOM   20035 H HB2  . ASN   B  1 538 ? 50.710 -5.951  -29.322 0.00 17.22  ? 564  ASN   B HB2  1 
ATOM   20036 H HB3  . ASN   B  1 538 ? 49.618 -7.340  -29.564 0.00 17.38  ? 564  ASN   B HB3  1 
ATOM   20037 H HD21 . ASN   B  1 538 ? 52.948 -7.096  -31.788 0.00 17.61  ? 564  ASN   B HD21 1 
ATOM   20038 H HD22 . ASN   B  1 538 ? 52.620 -5.943  -30.508 0.00 17.60  ? 564  ASN   B HD22 1 
ATOM   20039 N N    . SER   B  1 539 ? 47.054 -4.360  -30.122 1.00 17.14  ? 565  SER   B N    1 
ATOM   20040 C CA   . SER   B  1 539 ? 45.922 -3.982  -29.283 1.00 18.15  ? 565  SER   B CA   1 
ATOM   20041 C C    . SER   B  1 539 ? 44.750 -4.940  -29.314 1.00 18.51  ? 565  SER   B C    1 
ATOM   20042 O O    . SER   B  1 539 ? 43.869 -4.815  -28.457 1.00 18.69  ? 565  SER   B O    1 
ATOM   20043 C CB   . SER   B  1 539 ? 45.398 -2.611  -29.706 1.00 19.96  ? 565  SER   B CB   1 
ATOM   20044 O OG   . SER   B  1 539 ? 44.848 -2.670  -31.011 1.00 23.75  ? 565  SER   B OG   1 
ATOM   20045 H H    . SER   B  1 539 ? 47.126 -3.805  -30.969 0.00 16.81  ? 565  SER   B H    1 
ATOM   20046 H HA   . SER   B  1 539 ? 46.257 -3.900  -28.250 0.00 18.46  ? 565  SER   B HA   1 
ATOM   20047 H HB2  . SER   B  1 539 ? 44.594 -2.337  -29.027 0.00 20.47  ? 565  SER   B HB2  1 
ATOM   20048 H HB3  . SER   B  1 539 ? 46.199 -1.873  -29.677 0.00 20.25  ? 565  SER   B HB3  1 
ATOM   20049 H HG   . SER   B  1 539 ? 45.574 -2.699  -31.688 0.00 24.62  ? 565  SER   B HG   1 
ATOM   20050 N N    . HIS   B  1 540 ? 44.690 -5.854  -30.307 1.00 18.45  ? 566  HIS   B N    1 
ATOM   20051 C CA   . HIS   B  1 540 ? 43.529 -6.727  -30.524 1.00 18.89  ? 566  HIS   B CA   1 
ATOM   20052 C C    . HIS   B  1 540 ? 42.865 -7.278  -29.251 1.00 18.84  ? 566  HIS   B C    1 
ATOM   20053 O O    . HIS   B  1 540 ? 41.658 -7.102  -29.076 1.00 18.64  ? 566  HIS   B O    1 
ATOM   20054 C CB   . HIS   B  1 540 ? 43.863 -7.892  -31.482 1.00 19.90  ? 566  HIS   B CB   1 
ATOM   20055 C CG   . HIS   B  1 540 ? 42.657 -8.695  -31.882 1.00 22.75  ? 566  HIS   B CG   1 
ATOM   20056 N ND1  . HIS   B  1 540 ? 42.158 -8.647  -33.169 1.00 24.60  ? 566  HIS   B ND1  1 
ATOM   20057 C CD2  . HIS   B  1 540 ? 41.885 -9.535  -31.146 1.00 23.87  ? 566  HIS   B CD2  1 
ATOM   20058 C CE1  . HIS   B  1 540 ? 41.105 -9.451  -33.184 1.00 25.16  ? 566  HIS   B CE1  1 
ATOM   20059 N NE2  . HIS   B  1 540 ? 40.888 -9.994  -31.983 1.00 25.16  ? 566  HIS   B NE2  1 
ATOM   20060 H H    . HIS   B  1 540 ? 45.429 -6.017  -30.983 0.00 18.73  ? 566  HIS   B H    1 
ATOM   20061 H HA   . HIS   B  1 540 ? 42.792 -6.122  -31.051 0.00 19.46  ? 566  HIS   B HA   1 
ATOM   20062 H HB2  . HIS   B  1 540 ? 44.304 -7.490  -32.393 0.00 20.61  ? 566  HIS   B HB2  1 
ATOM   20063 H HB3  . HIS   B  1 540 ? 44.567 -8.564  -30.992 0.00 20.91  ? 566  HIS   B HB3  1 
ATOM   20064 H HD2  . HIS   B  1 540 ? 42.023 -9.794  -30.110 0.00 26.22  ? 566  HIS   B HD2  1 
ATOM   20065 H HE1  . HIS   B  1 540 ? 40.500 -9.643  -34.055 0.00 27.59  ? 566  HIS   B HE1  1 
ATOM   20066 H HE2  . HIS   B  1 540 ? 40.133 -10.624 -31.732 0.00 27.99  ? 566  HIS   B HE2  1 
ATOM   20067 N N    . TYR   B  1 541 ? 43.629 -7.979  -28.404 1.00 18.95  ? 567  TYR   B N    1 
ATOM   20068 C CA   . TYR   B  1 541 ? 43.065 -8.597  -27.210 1.00 19.21  ? 567  TYR   B CA   1 
ATOM   20069 C C    . TYR   B  1 541 ? 43.101 -7.682  -25.996 1.00 19.76  ? 567  TYR   B C    1 
ATOM   20070 O O    . TYR   B  1 541 ? 42.206 -7.781  -25.149 1.00 19.60  ? 567  TYR   B O    1 
ATOM   20071 C CB   . TYR   B  1 541 ? 43.747 -9.948  -26.924 1.00 19.21  ? 567  TYR   B CB   1 
ATOM   20072 C CG   . TYR   B  1 541 ? 43.292 -11.014 -27.897 1.00 19.67  ? 567  TYR   B CG   1 
ATOM   20073 C CD1  . TYR   B  1 541 ? 42.029 -11.583 -27.787 1.00 20.04  ? 567  TYR   B CD1  1 
ATOM   20074 C CD2  . TYR   B  1 541 ? 44.042 -11.317 -29.024 1.00 19.80  ? 567  TYR   B CD2  1 
ATOM   20075 C CE1  . TYR   B  1 541 ? 41.560 -12.486 -28.732 1.00 20.82  ? 567  TYR   B CE1  1 
ATOM   20076 C CE2  . TYR   B  1 541 ? 43.608 -12.258 -29.948 1.00 20.69  ? 567  TYR   B CE2  1 
ATOM   20077 C CZ   . TYR   B  1 541 ? 42.363 -12.841 -29.801 1.00 21.78  ? 567  TYR   B CZ   1 
ATOM   20078 O OH   . TYR   B  1 541 ? 41.900 -13.695 -30.779 1.00 22.82  ? 567  TYR   B OH   1 
ATOM   20079 H H    . TYR   B  1 541 ? 44.628 -8.111  -28.519 0.00 20.01  ? 567  TYR   B H    1 
ATOM   20080 H HA   . TYR   B  1 541 ? 42.011 -8.786  -27.407 0.00 20.80  ? 567  TYR   B HA   1 
ATOM   20081 H HB2  . TYR   B  1 541 ? 44.827 -9.843  -27.005 0.00 20.86  ? 567  TYR   B HB2  1 
ATOM   20082 H HB3  . TYR   B  1 541 ? 43.477 -10.273 -25.920 0.00 21.19  ? 567  TYR   B HB3  1 
ATOM   20083 H HD1  . TYR   B  1 541 ? 41.403 -11.322 -26.950 0.00 22.40  ? 567  TYR   B HD1  1 
ATOM   20084 H HD2  . TYR   B  1 541 ? 45.018 -10.875 -29.140 0.00 21.44  ? 567  TYR   B HD2  1 
ATOM   20085 H HE1  . TYR   B  1 541 ? 40.593 -12.939 -28.598 0.00 23.55  ? 567  TYR   B HE1  1 
ATOM   20086 H HE2  . TYR   B  1 541 ? 44.217 -12.495 -30.803 0.00 22.72  ? 567  TYR   B HE2  1 
ATOM   20087 H HH   . TYR   B  1 541 ? 40.961 -13.965 -30.601 0.00 25.97  ? 567  TYR   B HH   1 
ATOM   20088 N N    . PHE   B  1 542 ? 44.084 -6.757  -25.914 1.00 19.43  ? 568  PHE   B N    1 
ATOM   20089 C CA   . PHE   B  1 542 ? 44.112 -5.799  -24.797 1.00 19.47  ? 568  PHE   B CA   1 
ATOM   20090 C C    . PHE   B  1 542 ? 42.835 -4.943  -24.762 1.00 19.39  ? 568  PHE   B C    1 
ATOM   20091 O O    . PHE   B  1 542 ? 42.415 -4.536  -23.678 1.00 18.92  ? 568  PHE   B O    1 
ATOM   20092 C CB   . PHE   B  1 542 ? 45.313 -4.848  -24.900 1.00 18.77  ? 568  PHE   B CB   1 
ATOM   20093 C CG   . PHE   B  1 542 ? 46.649 -5.434  -24.511 1.00 19.18  ? 568  PHE   B CG   1 
ATOM   20094 C CD1  . PHE   B  1 542 ? 46.860 -5.933  -23.235 1.00 19.56  ? 568  PHE   B CD1  1 
ATOM   20095 C CD2  . PHE   B  1 542 ? 47.700 -5.461  -25.410 1.00 19.84  ? 568  PHE   B CD2  1 
ATOM   20096 C CE1  . PHE   B  1 542 ? 48.094 -6.448  -22.870 1.00 20.60  ? 568  PHE   B CE1  1 
ATOM   20097 C CE2  . PHE   B  1 542 ? 48.942 -5.961  -25.033 1.00 20.96  ? 568  PHE   B CE2  1 
ATOM   20098 C CZ   . PHE   B  1 542 ? 49.127 -6.464  -23.774 1.00 20.67  ? 568  PHE   B CZ   1 
ATOM   20099 H H    . PHE   B  1 542 ? 44.859 -6.664  -26.562 0.00 20.67  ? 568  PHE   B H    1 
ATOM   20100 H HA   . PHE   B  1 542 ? 44.175 -6.344  -23.857 0.00 21.21  ? 568  PHE   B HA   1 
ATOM   20101 H HB2  . PHE   B  1 542 ? 45.386 -4.488  -25.925 0.00 19.70  ? 568  PHE   B HB2  1 
ATOM   20102 H HB3  . PHE   B  1 542 ? 45.132 -4.003  -24.238 0.00 20.00  ? 568  PHE   B HB3  1 
ATOM   20103 H HD1  . PHE   B  1 542 ? 46.056 -5.917  -22.519 0.00 21.49  ? 568  PHE   B HD1  1 
ATOM   20104 H HD2  . PHE   B  1 542 ? 47.570 -5.065  -26.403 0.00 20.90  ? 568  PHE   B HD2  1 
ATOM   20105 H HE1  . PHE   B  1 542 ? 48.243 -6.839  -21.877 0.00 23.01  ? 568  PHE   B HE1  1 
ATOM   20106 H HE2  . PHE   B  1 542 ? 49.748 -5.989  -25.747 0.00 22.49  ? 568  PHE   B HE2  1 
ATOM   20107 H HZ   . PHE   B  1 542 ? 50.079 -6.876  -23.496 0.00 22.76  ? 568  PHE   B HZ   1 
ATOM   20108 N N    . ARG   B  1 543 ? 42.248 -4.640  -25.932 1.00 20.14  ? 569  ARG   B N    1 
ATOM   20109 C CA   . ARG   B  1 543 ? 41.067 -3.781  -25.964 1.00 21.63  ? 569  ARG   B CA   1 
ATOM   20110 C C    . ARG   B  1 543 ? 39.772 -4.497  -25.487 1.00 21.39  ? 569  ARG   B C    1 
ATOM   20111 O O    . ARG   B  1 543 ? 38.807 -3.808  -25.188 1.00 22.53  ? 569  ARG   B O    1 
ATOM   20112 C CB   . ARG   B  1 543 ? 40.892 -3.108  -27.330 1.00 24.35  ? 569  ARG   B CB   1 
ATOM   20113 C CG   . ARG   B  1 543 ? 40.438 -3.999  -28.441 1.00 29.83  ? 569  ARG   B CG   1 
ATOM   20114 C CD   . ARG   B  1 543 ? 40.782 -3.351  -29.772 1.00 34.70  ? 569  ARG   B CD   1 
ATOM   20115 N NE   . ARG   B  1 543 ? 40.352 -4.191  -30.891 1.00 39.56  ? 569  ARG   B NE   1 
ATOM   20116 C CZ   . ARG   B  1 543 ? 40.940 -4.253  -32.088 1.00 42.21  ? 569  ARG   B CZ   1 
ATOM   20117 N NH1  . ARG   B  1 543 ? 42.017 -3.510  -32.355 1.00 42.66  ? 569  ARG   B NH1  1 
ATOM   20118 N NH2  . ARG   B  1 543 ? 40.467 -5.068  -33.022 1.00 40.98  ? 569  ARG   B NH2  1 
ATOM   20119 H H    . ARG   B  1 543 ? 42.563 -4.948  -26.846 0.00 21.41  ? 569  ARG   B H    1 
ATOM   20120 H HA   . ARG   B  1 543 ? 41.268 -2.942  -25.302 0.00 23.40  ? 569  ARG   B HA   1 
ATOM   20121 H HB2  . ARG   B  1 543 ? 40.153 -2.315  -27.228 0.00 26.43  ? 569  ARG   B HB2  1 
ATOM   20122 H HB3  . ARG   B  1 543 ? 41.850 -2.673  -27.611 0.00 26.20  ? 569  ARG   B HB3  1 
ATOM   20123 H HG2  . ARG   B  1 543 ? 40.950 -4.958  -28.376 0.00 32.98  ? 569  ARG   B HG2  1 
ATOM   20124 H HG3  . ARG   B  1 543 ? 39.359 -4.134  -28.387 0.00 33.08  ? 569  ARG   B HG3  1 
ATOM   20125 H HD2  . ARG   B  1 543 ? 40.292 -2.381  -29.850 0.00 38.46  ? 569  ARG   B HD2  1 
ATOM   20126 H HD3  . ARG   B  1 543 ? 41.865 -3.240  -29.784 0.00 38.36  ? 569  ARG   B HD3  1 
ATOM   20127 H HE   . ARG   B  1 543 ? 39.549 -4.789  -30.729 0.00 44.53  ? 569  ARG   B HE   1 
ATOM   20128 H HH11 . ARG   B  1 543 ? 42.419 -2.845  -31.704 0.00 47.60  ? 569  ARG   B HH11 1 
ATOM   20129 H HH12 . ARG   B  1 543 ? 42.430 -3.569  -33.281 0.00 47.51  ? 569  ARG   B HH12 1 
ATOM   20130 H HH21 . ARG   B  1 543 ? 39.658 -5.650  -32.832 0.00 46.13  ? 569  ARG   B HH21 1 
ATOM   20131 H HH22 . ARG   B  1 543 ? 40.910 -5.116  -33.934 0.00 45.81  ? 569  ARG   B HH22 1 
ATOM   20132 N N    . ILE   B  1 544 ? 39.781 -5.837  -25.319 1.00 19.68  ? 570  ILE   B N    1 
ATOM   20133 C CA   . ILE   B  1 544 ? 38.625 -6.606  -24.850 1.00 19.79  ? 570  ILE   B CA   1 
ATOM   20134 C C    . ILE   B  1 544 ? 38.724 -6.764  -23.322 1.00 19.28  ? 570  ILE   B C    1 
ATOM   20135 O O    . ILE   B  1 544 ? 39.617 -7.463  -22.846 1.00 18.38  ? 570  ILE   B O    1 
ATOM   20136 C CB   . ILE   B  1 544 ? 38.583 -8.015  -25.533 1.00 20.38  ? 570  ILE   B CB   1 
ATOM   20137 C CG1  . ILE   B  1 544 ? 38.790 -7.911  -27.076 1.00 20.85  ? 570  ILE   B CG1  1 
ATOM   20138 C CG2  . ILE   B  1 544 ? 37.246 -8.733  -25.174 1.00 20.90  ? 570  ILE   B CG2  1 
ATOM   20139 C CD1  . ILE   B  1 544 ? 39.134 -9.222  -27.730 1.00 21.85  ? 570  ILE   B CD1  1 
ATOM   20140 H H    . ILE   B  1 544 ? 40.584 -6.431  -25.499 0.00 21.45  ? 570  ILE   B H    1 
ATOM   20141 H HA   . ILE   B  1 544 ? 37.701 -6.084  -25.091 0.00 21.97  ? 570  ILE   B HA   1 
ATOM   20142 H HB   . ILE   B  1 544 ? 39.399 -8.617  -25.134 0.00 22.80  ? 570  ILE   B HB   1 
ATOM   20143 H HG12 . ILE   B  1 544 ? 37.871 -7.543  -27.529 0.00 23.04  ? 570  ILE   B HG12 1 
ATOM   20144 H HG13 . ILE   B  1 544 ? 39.610 -7.231  -27.302 0.00 22.78  ? 570  ILE   B HG13 1 
ATOM   20145 H HG21 . ILE   B  1 544 ? 37.147 -9.644  -25.762 0.00 23.80  ? 570  ILE   B HG21 1 
ATOM   20146 H HG22 . ILE   B  1 544 ? 37.244 -8.990  -24.116 0.00 23.93  ? 570  ILE   B HG22 1 
ATOM   20147 H HG23 . ILE   B  1 544 ? 36.417 -8.062  -25.394 0.00 23.71  ? 570  ILE   B HG23 1 
ATOM   20148 H HD11 . ILE   B  1 544 ? 39.500 -9.025  -28.737 0.00 24.10  ? 570  ILE   B HD11 1 
ATOM   20149 H HD12 . ILE   B  1 544 ? 39.901 -9.728  -27.146 0.00 24.39  ? 570  ILE   B HD12 1 
ATOM   20150 H HD13 . ILE   B  1 544 ? 38.241 -9.842  -27.784 0.00 24.54  ? 570  ILE   B HD13 1 
ATOM   20151 N N    . ALA   B  1 545 ? 37.807 -6.150  -22.562 1.00 19.53  ? 571  ALA   B N    1 
ATOM   20152 C CA   . ALA   B  1 545 ? 37.864 -6.248  -21.099 1.00 20.03  ? 571  ALA   B CA   1 
ATOM   20153 C C    . ALA   B  1 545 ? 37.703 -7.672  -20.570 1.00 20.93  ? 571  ALA   B C    1 
ATOM   20154 O O    . ALA   B  1 545 ? 38.377 -8.048  -19.610 1.00 20.49  ? 571  ALA   B O    1 
ATOM   20155 C CB   . ALA   B  1 545 ? 36.809 -5.342  -20.461 1.00 19.99  ? 571  ALA   B CB   1 
ATOM   20156 H H    . ALA   B  1 545 ? 37.037 -5.589  -22.913 0.00 22.09  ? 571  ALA   B H    1 
ATOM   20157 H HA   . ALA   B  1 545 ? 38.842 -5.893  -20.778 0.00 22.92  ? 571  ALA   B HA   1 
ATOM   20158 H HB1  . ALA   B  1 545 ? 36.871 -5.433  -19.378 0.00 23.40  ? 571  ALA   B HB1  1 
ATOM   20159 H HB2  . ALA   B  1 545 ? 36.998 -4.313  -20.762 0.00 22.96  ? 571  ALA   B HB2  1 
ATOM   20160 H HB3  . ALA   B  1 545 ? 35.824 -5.653  -20.806 0.00 23.25  ? 571  ALA   B HB3  1 
ATOM   20161 N N    . GLY   B  1 546 ? 36.790 -8.428  -21.177 1.00 21.33  ? 572  GLY   B N    1 
ATOM   20162 C CA   . GLY   B  1 546 ? 36.401 -9.756  -20.723 1.00 21.31  ? 572  GLY   B CA   1 
ATOM   20163 C C    . GLY   B  1 546 ? 37.398 -10.877 -20.897 1.00 21.04  ? 572  GLY   B C    1 
ATOM   20164 O O    . GLY   B  1 546 ? 37.182 -11.953 -20.336 1.00 21.11  ? 572  GLY   B O    1 
ATOM   20165 H H    . GLY   B  1 546 ? 36.275 -8.139  -22.003 0.00 24.85  ? 572  GLY   B H    1 
ATOM   20166 H HA2  . GLY   B  1 546 ? 36.164 -9.697  -19.661 0.00 25.58  ? 572  GLY   B HA2  1 
ATOM   20167 H HA3  . GLY   B  1 546 ? 35.491 -10.047 -21.245 0.00 25.40  ? 572  GLY   B HA3  1 
ATOM   20168 N N    . VAL   B  1 547 ? 38.446 -10.674 -21.712 1.00 20.17  ? 573  VAL   B N    1 
ATOM   20169 C CA   . VAL   B  1 547 ? 39.483 -11.682 -21.866 1.00 19.82  ? 573  VAL   B CA   1 
ATOM   20170 C C    . VAL   B  1 547 ? 40.620 -11.371 -20.892 1.00 20.02  ? 573  VAL   B C    1 
ATOM   20171 O O    . VAL   B  1 547 ? 40.732 -10.242 -20.411 1.00 19.99  ? 573  VAL   B O    1 
ATOM   20172 C CB   . VAL   B  1 547 ? 39.979 -11.849 -23.317 1.00 19.85  ? 573  VAL   B CB   1 
ATOM   20173 C CG1  . VAL   B  1 547 ? 38.805 -12.018 -24.269 1.00 20.45  ? 573  VAL   B CG1  1 
ATOM   20174 C CG2  . VAL   B  1 547 ? 40.873 -10.684 -23.745 1.00 20.22  ? 573  VAL   B CG2  1 
ATOM   20175 H H    . VAL   B  1 547 ? 38.596 -9.843  -22.274 0.00 23.36  ? 573  VAL   B H    1 
ATOM   20176 H HA   . VAL   B  1 547 ? 39.072 -12.642 -21.570 0.00 23.58  ? 573  VAL   B HA   1 
ATOM   20177 H HB   . VAL   B  1 547 ? 40.577 -12.757 -23.372 0.00 23.14  ? 573  VAL   B HB   1 
ATOM   20178 H HG11 . VAL   B  1 547 ? 39.186 -12.266 -25.258 0.00 23.58  ? 573  VAL   B HG11 1 
ATOM   20179 H HG12 . VAL   B  1 547 ? 38.165 -12.819 -23.904 0.00 24.05  ? 573  VAL   B HG12 1 
ATOM   20180 H HG13 . VAL   B  1 547 ? 38.244 -11.086 -24.316 0.00 23.59  ? 573  VAL   B HG13 1 
ATOM   20181 H HG21 . VAL   B  1 547 ? 40.895 -10.642 -24.833 0.00 22.86  ? 573  VAL   B HG21 1 
ATOM   20182 H HG22 . VAL   B  1 547 ? 40.472 -9.755  -23.343 0.00 23.01  ? 573  VAL   B HG22 1 
ATOM   20183 H HG23 . VAL   B  1 547 ? 41.882 -10.849 -23.371 0.00 23.08  ? 573  VAL   B HG23 1 
ATOM   20184 N N    . THR   B  1 548 ? 41.391 -12.392 -20.514 1.00 19.57  ? 574  THR   B N    1 
ATOM   20185 C CA   . THR   B  1 548 ? 42.505 -12.201 -19.574 1.00 19.69  ? 574  THR   B CA   1 
ATOM   20186 C C    . THR   B  1 548 ? 43.741 -11.628 -20.303 1.00 19.71  ? 574  THR   B C    1 
ATOM   20187 O O    . THR   B  1 548 ? 43.897 -11.838 -21.507 1.00 20.04  ? 574  THR   B O    1 
ATOM   20188 C CB   . THR   B  1 548 ? 42.789 -13.500 -18.830 1.00 20.54  ? 574  THR   B CB   1 
ATOM   20189 O OG1  . THR   B  1 548 ? 42.954 -14.524 -19.795 1.00 21.15  ? 574  THR   B OG1  1 
ATOM   20190 C CG2  . THR   B  1 548 ? 41.643 -13.884 -17.882 1.00 21.38  ? 574  THR   B CG2  1 
ATOM   20191 H H    . THR   B  1 548 ? 41.271 -13.349 -20.831 0.00 23.41  ? 574  THR   B H    1 
ATOM   20192 H HA   . THR   B  1 548 ? 42.222 -11.457 -18.830 0.00 23.57  ? 574  THR   B HA   1 
ATOM   20193 H HB   . THR   B  1 548 ? 43.698 -13.395 -18.239 0.00 25.09  ? 574  THR   B HB   1 
ATOM   20194 H HG1  . THR   B  1 548 ? 43.888 -14.526 -20.133 0.00 25.61  ? 574  THR   B HG1  1 
ATOM   20195 H HG21 . THR   B  1 548 ? 41.892 -14.798 -17.345 0.00 26.74  ? 574  THR   B HG21 1 
ATOM   20196 H HG22 . THR   B  1 548 ? 41.470 -13.084 -17.163 0.00 26.41  ? 574  THR   B HG22 1 
ATOM   20197 H HG23 . THR   B  1 548 ? 40.729 -14.049 -18.451 0.00 26.35  ? 574  THR   B HG23 1 
ATOM   20198 N N    . HIS   B  1 549 ? 44.563 -10.837 -19.584 1.00 18.76  ? 575  HIS   B N    1 
ATOM   20199 C CA   . HIS   B  1 549 ? 45.768 -10.207 -20.148 1.00 18.93  ? 575  HIS   B CA   1 
ATOM   20200 C C    . HIS   B  1 549 ? 46.888 -10.373 -19.129 1.00 19.75  ? 575  HIS   B C    1 
ATOM   20201 O O    . HIS   B  1 549 ? 46.713 -10.028 -17.970 1.00 19.36  ? 575  HIS   B O    1 
ATOM   20202 C CB   . HIS   B  1 549 ? 45.552 -8.707  -20.439 1.00 18.99  ? 575  HIS   B CB   1 
ATOM   20203 C CG   . HIS   B  1 549 ? 44.231 -8.369  -21.063 1.00 19.57  ? 575  HIS   B CG   1 
ATOM   20204 N ND1  . HIS   B  1 549 ? 43.131 -8.055  -20.292 1.00 20.64  ? 575  HIS   B ND1  1 
ATOM   20205 C CD2  . HIS   B  1 549 ? 43.876 -8.331  -22.364 1.00 19.23  ? 575  HIS   B CD2  1 
ATOM   20206 C CE1  . HIS   B  1 549 ? 42.153 -7.820  -21.143 1.00 21.06  ? 575  HIS   B CE1  1 
ATOM   20207 N NE2  . HIS   B  1 549 ? 42.550 -8.007  -22.399 1.00 20.76  ? 575  HIS   B NE2  1 
ATOM   20208 H H    . HIS   B  1 549 ? 44.418 -10.615 -18.604 0.00 22.26  ? 575  HIS   B H    1 
ATOM   20209 H HA   . HIS   B  1 549 ? 46.061 -10.700 -21.073 0.00 21.83  ? 575  HIS   B HA   1 
ATOM   20210 H HB2  . HIS   B  1 549 ? 45.627 -8.149  -19.509 0.00 21.87  ? 575  HIS   B HB2  1 
ATOM   20211 H HB3  . HIS   B  1 549 ? 46.329 -8.373  -21.124 0.00 21.49  ? 575  HIS   B HB3  1 
ATOM   20212 H HD2  . HIS   B  1 549 ? 44.514 -8.522  -23.211 0.00 21.36  ? 575  HIS   B HD2  1 
ATOM   20213 H HE1  . HIS   B  1 549 ? 41.160 -7.517  -20.859 0.00 24.13  ? 575  HIS   B HE1  1 
ATOM   20214 H HE2  . HIS   B  1 549 ? 41.970 -7.923  -23.228 0.00 23.25  ? 575  HIS   B HE2  1 
ATOM   20215 N N    . HIS   B  1 550 ? 48.053 -10.835 -19.581 1.00 20.07  ? 576  HIS   B N    1 
ATOM   20216 C CA   . HIS   B  1 550 ? 49.172 -11.117 -18.700 1.00 21.00  ? 576  HIS   B CA   1 
ATOM   20217 C C    . HIS   B  1 550 ? 50.480 -10.537 -19.239 1.00 22.07  ? 576  HIS   B C    1 
ATOM   20218 O O    . HIS   B  1 550 ? 50.937 -10.931 -20.323 1.00 22.03  ? 576  HIS   B O    1 
ATOM   20219 C CB   . HIS   B  1 550 ? 49.296 -12.650 -18.543 1.00 21.03  ? 576  HIS   B CB   1 
ATOM   20220 C CG   . HIS   B  1 550 ? 48.201 -13.265 -17.714 1.00 22.43  ? 576  HIS   B CG   1 
ATOM   20221 N ND1  . HIS   B  1 550 ? 48.215 -13.193 -16.332 1.00 24.18  ? 576  HIS   B ND1  1 
ATOM   20222 C CD2  . HIS   B  1 550 ? 47.098 -13.950 -18.101 1.00 23.78  ? 576  HIS   B CD2  1 
ATOM   20223 C CE1  . HIS   B  1 550 ? 47.124 -13.825 -15.919 1.00 24.54  ? 576  HIS   B CE1  1 
ATOM   20224 N NE2  . HIS   B  1 550 ? 46.414 -14.288 -16.949 1.00 24.68  ? 576  HIS   B NE2  1 
ATOM   20225 H H    . HIS   B  1 550 ? 48.257 -11.021 -20.557 0.00 23.41  ? 576  HIS   B H    1 
ATOM   20226 H HA   . HIS   B  1 550 ? 49.001 -10.702 -17.709 0.00 25.27  ? 576  HIS   B HA   1 
ATOM   20227 H HB2  . HIS   B  1 550 ? 49.262 -13.108 -19.531 0.00 25.32  ? 576  HIS   B HB2  1 
ATOM   20228 H HB3  . HIS   B  1 550 ? 50.246 -12.876 -18.062 0.00 25.73  ? 576  HIS   B HB3  1 
ATOM   20229 H HD2  . HIS   B  1 550 ? 46.804 -14.185 -19.109 0.00 28.91  ? 576  HIS   B HD2  1 
ATOM   20230 H HE1  . HIS   B  1 550 ? 46.845 -13.947 -14.886 0.00 30.99  ? 576  HIS   B HE1  1 
ATOM   20231 H HE2  . HIS   B  1 550 ? 45.535 -14.793 -16.899 0.00 30.75  ? 576  HIS   B HE2  1 
ATOM   20232 N N    . LEU   B  1 551 ? 51.115 -9.643  -18.454 1.00 22.34  ? 577  LEU   B N    1 
ATOM   20233 C CA   . LEU   B  1 551 ? 52.416 -9.068  -18.811 1.00 23.32  ? 577  LEU   B CA   1 
ATOM   20234 C C    . LEU   B  1 551 ? 53.528 -9.441  -17.798 1.00 24.26  ? 577  LEU   B C    1 
ATOM   20235 O O    . LEU   B  1 551 ? 54.587 -8.822  -17.820 1.00 25.13  ? 577  LEU   B O    1 
ATOM   20236 C CB   . LEU   B  1 551 ? 52.279 -7.532  -18.949 1.00 23.58  ? 577  LEU   B CB   1 
ATOM   20237 C CG   . LEU   B  1 551 ? 51.449 -7.059  -20.154 1.00 25.09  ? 577  LEU   B CG   1 
ATOM   20238 C CD1  . LEU   B  1 551 ? 51.310 -5.533  -20.161 1.00 26.12  ? 577  LEU   B CD1  1 
ATOM   20239 C CD2  . LEU   B  1 551 ? 52.064 -7.530  -21.474 1.00 25.41  ? 577  LEU   B CD2  1 
ATOM   20240 H H    . LEU   B  1 551 ? 50.755 -9.292  -17.572 0.00 26.76  ? 577  LEU   B H    1 
ATOM   20241 H HA   . LEU   B  1 551 ? 52.747 -9.460  -19.771 0.00 27.47  ? 577  LEU   B HA   1 
ATOM   20242 H HB2  . LEU   B  1 551 ? 51.797 -7.150  -18.050 0.00 27.85  ? 577  LEU   B HB2  1 
ATOM   20243 H HB3  . LEU   B  1 551 ? 53.264 -7.081  -19.051 0.00 27.67  ? 577  LEU   B HB3  1 
ATOM   20244 H HG   . LEU   B  1 551 ? 50.449 -7.486  -20.082 0.00 29.03  ? 577  LEU   B HG   1 
ATOM   20245 H HD11 . LEU   B  1 551 ? 50.624 -5.244  -20.956 0.00 29.76  ? 577  LEU   B HD11 1 
ATOM   20246 H HD12 . LEU   B  1 551 ? 50.921 -5.208  -19.197 0.00 30.27  ? 577  LEU   B HD12 1 
ATOM   20247 H HD13 . LEU   B  1 551 ? 52.289 -5.088  -20.335 0.00 30.02  ? 577  LEU   B HD13 1 
ATOM   20248 H HD21 . LEU   B  1 551 ? 51.821 -6.816  -22.258 0.00 28.82  ? 577  LEU   B HD21 1 
ATOM   20249 H HD22 . LEU   B  1 551 ? 53.145 -7.598  -21.358 0.00 29.27  ? 577  LEU   B HD22 1 
ATOM   20250 H HD23 . LEU   B  1 551 ? 51.656 -8.509  -21.725 0.00 29.20  ? 577  LEU   B HD23 1 
ATOM   20251 N N    . GLU   B  1 552 ? 53.341 -10.507 -17.001 1.00 24.02  ? 578  GLU   B N    1 
ATOM   20252 C CA   . GLU   B  1 552 ? 54.310 -10.937 -15.982 1.00 24.76  ? 578  GLU   B CA   1 
ATOM   20253 C C    . GLU   B  1 552 ? 55.657 -11.383 -16.512 1.00 25.27  ? 578  GLU   B C    1 
ATOM   20254 O O    . GLU   B  1 552 ? 56.636 -11.373 -15.755 1.00 25.03  ? 578  GLU   B O    1 
ATOM   20255 C CB   . GLU   B  1 552 ? 53.771 -12.115 -15.146 1.00 26.70  ? 578  GLU   B CB   1 
ATOM   20256 C CG   . GLU   B  1 552 ? 52.452 -11.852 -14.458 1.00 30.53  ? 578  GLU   B CG   1 
ATOM   20257 C CD   . GLU   B  1 552 ? 51.237 -12.293 -15.242 1.00 35.39  ? 578  GLU   B CD   1 
ATOM   20258 O OE1  . GLU   B  1 552 ? 51.348 -12.410 -16.481 1.00 37.03  ? 578  GLU   B OE1  1 
ATOM   20259 O OE2  . GLU   B  1 552 ? 50.179 -12.530 -14.620 1.00 37.22  ? 578  GLU   B OE2  1 
ATOM   20260 H H    . GLU   B  1 552 ? 52.538 -11.125 -17.065 0.00 29.43  ? 578  GLU   B H    1 
ATOM   20261 H HA   . GLU   B  1 552 ? 54.486 -10.105 -15.301 0.00 30.92  ? 578  GLU   B HA   1 
ATOM   20262 H HB2  . GLU   B  1 552 ? 53.666 -12.987 -15.790 0.00 33.60  ? 578  GLU   B HB2  1 
ATOM   20263 H HB3  . GLU   B  1 552 ? 54.498 -12.337 -14.367 0.00 34.03  ? 578  GLU   B HB3  1 
ATOM   20264 H HG2  . GLU   B  1 552 ? 52.441 -12.367 -13.499 0.00 38.69  ? 578  GLU   B HG2  1 
ATOM   20265 H HG3  . GLU   B  1 552 ? 52.357 -10.778 -14.308 0.00 38.07  ? 578  GLU   B HG3  1 
ATOM   20266 N N    . PHE   B  1 553 ? 55.705 -11.843 -17.778 1.00 24.94  ? 579  PHE   B N    1 
ATOM   20267 C CA   . PHE   B  1 553 ? 56.948 -12.323 -18.367 1.00 25.17  ? 579  PHE   B CA   1 
ATOM   20268 C C    . PHE   B  1 553 ? 58.065 -11.281 -18.391 1.00 26.02  ? 579  PHE   B C    1 
ATOM   20269 O O    . PHE   B  1 553 ? 59.225 -11.674 -18.429 1.00 26.16  ? 579  PHE   B O    1 
ATOM   20270 C CB   . PHE   B  1 553 ? 56.701 -12.848 -19.792 1.00 23.98  ? 579  PHE   B CB   1 
ATOM   20271 C CG   . PHE   B  1 553 ? 56.125 -11.827 -20.741 1.00 23.66  ? 579  PHE   B CG   1 
ATOM   20272 C CD1  . PHE   B  1 553 ? 56.948 -11.087 -21.567 1.00 24.28  ? 579  PHE   B CD1  1 
ATOM   20273 C CD2  . PHE   B  1 553 ? 54.757 -11.658 -20.853 1.00 23.79  ? 579  PHE   B CD2  1 
ATOM   20274 C CE1  . PHE   B  1 553 ? 56.412 -10.160 -22.453 1.00 25.19  ? 579  PHE   B CE1  1 
ATOM   20275 C CE2  . PHE   B  1 553 ? 54.229 -10.705 -21.707 1.00 24.17  ? 579  PHE   B CE2  1 
ATOM   20276 C CZ   . PHE   B  1 553 ? 55.057 -9.968  -22.507 1.00 24.52  ? 579  PHE   B CZ   1 
ATOM   20277 H H    . PHE   B  1 553 ? 54.893 -11.944 -18.378 0.00 30.56  ? 579  PHE   B H    1 
ATOM   20278 H HA   . PHE   B  1 553 ? 57.305 -13.161 -17.770 0.00 31.65  ? 579  PHE   B HA   1 
ATOM   20279 H HB2  . PHE   B  1 553 ? 57.648 -13.191 -20.205 0.00 29.54  ? 579  PHE   B HB2  1 
ATOM   20280 H HB3  . PHE   B  1 553 ? 56.002 -13.682 -19.740 0.00 29.55  ? 579  PHE   B HB3  1 
ATOM   20281 H HD1  . PHE   B  1 553 ? 58.015 -11.223 -21.518 0.00 29.13  ? 579  PHE   B HD1  1 
ATOM   20282 H HD2  . PHE   B  1 553 ? 54.099 -12.217 -20.209 0.00 28.61  ? 579  PHE   B HD2  1 
ATOM   20283 H HE1  . PHE   B  1 553 ? 57.064 -9.573  -23.077 0.00 29.33  ? 579  PHE   B HE1  1 
ATOM   20284 H HE2  . PHE   B  1 553 ? 53.162 -10.569 -21.769 0.00 28.21  ? 579  PHE   B HE2  1 
ATOM   20285 H HZ   . PHE   B  1 553 ? 54.642 -9.253  -23.196 0.00 28.15  ? 579  PHE   B HZ   1 
ATOM   20286 N N    . ILE   B  1 554 ? 57.731 -9.971  -18.386 1.00 26.20  ? 580  ILE   B N    1 
ATOM   20287 C CA   . ILE   B  1 554 ? 58.730 -8.885  -18.447 1.00 26.82  ? 580  ILE   B CA   1 
ATOM   20288 C C    . ILE   B  1 554 ? 59.821 -9.028  -17.353 1.00 27.51  ? 580  ILE   B C    1 
ATOM   20289 O O    . ILE   B  1 554 ? 60.992 -8.725  -17.592 1.00 27.03  ? 580  ILE   B O    1 
ATOM   20290 C CB   . ILE   B  1 554 ? 58.011 -7.498  -18.381 1.00 26.99  ? 580  ILE   B CB   1 
ATOM   20291 C CG1  . ILE   B  1 554 ? 57.184 -7.247  -19.679 1.00 28.12  ? 580  ILE   B CG1  1 
ATOM   20292 C CG2  . ILE   B  1 554 ? 59.013 -6.343  -18.155 1.00 27.16  ? 580  ILE   B CG2  1 
ATOM   20293 C CD1  . ILE   B  1 554 ? 56.044 -6.220  -19.500 1.00 29.72  ? 580  ILE   B CD1  1 
ATOM   20294 H H    . ILE   B  1 554 ? 56.775 -9.633  -18.344 0.00 31.88  ? 580  ILE   B H    1 
ATOM   20295 H HA   . ILE   B  1 554 ? 59.234 -8.941  -19.411 0.00 32.57  ? 580  ILE   B HA   1 
ATOM   20296 H HB   . ILE   B  1 554 ? 57.325 -7.506  -17.534 0.00 32.82  ? 580  ILE   B HB   1 
ATOM   20297 H HG12 . ILE   B  1 554 ? 57.856 -6.869  -20.448 0.00 33.24  ? 580  ILE   B HG12 1 
ATOM   20298 H HG13 . ILE   B  1 554 ? 56.735 -8.182  -20.011 0.00 33.41  ? 580  ILE   B HG13 1 
ATOM   20299 H HG21 . ILE   B  1 554 ? 58.545 -5.393  -18.408 0.00 32.65  ? 580  ILE   B HG21 1 
ATOM   20300 H HG22 . ILE   B  1 554 ? 59.305 -6.318  -17.106 0.00 33.35  ? 580  ILE   B HG22 1 
ATOM   20301 H HG23 . ILE   B  1 554 ? 59.889 -6.498  -18.782 0.00 32.92  ? 580  ILE   B HG23 1 
ATOM   20302 H HD11 . ILE   B  1 554 ? 55.406 -6.248  -20.382 0.00 34.76  ? 580  ILE   B HD11 1 
ATOM   20303 H HD12 . ILE   B  1 554 ? 55.471 -6.493  -18.616 0.00 35.34  ? 580  ILE   B HD12 1 
ATOM   20304 H HD13 . ILE   B  1 554 ? 56.461 -5.220  -19.383 0.00 35.07  ? 580  ILE   B HD13 1 
ATOM   20305 N N    . GLN   B  1 555 ? 59.421 -9.493  -16.175 1.00 28.70  ? 581  GLN   B N    1 
ATOM   20306 C CA   . GLN   B  1 555 ? 60.313 -9.682  -15.012 1.00 30.44  ? 581  GLN   B CA   1 
ATOM   20307 C C    . GLN   B  1 555 ? 61.407 -10.747 -15.194 1.00 31.78  ? 581  GLN   B C    1 
ATOM   20308 O O    . GLN   B  1 555 ? 62.442 -10.672 -14.530 1.00 31.81  ? 581  GLN   B O    1 
ATOM   20309 C CB   . GLN   B  1 555 ? 59.450 -10.071 -13.801 1.00 32.75  ? 581  GLN   B CB   1 
ATOM   20310 C CG   . GLN   B  1 555 ? 60.164 -10.164 -12.475 1.00 38.69  ? 581  GLN   B CG   1 
ATOM   20311 C CD   . GLN   B  1 555 ? 59.157 -10.425 -11.380 1.00 44.54  ? 581  GLN   B CD   1 
ATOM   20312 O OE1  . GLN   B  1 555 ? 58.229 -11.236 -11.548 1.00 45.37  ? 581  GLN   B OE1  1 
ATOM   20313 N NE2  . GLN   B  1 555 ? 59.316 -9.754  -10.235 1.00 45.54  ? 581  GLN   B NE2  1 
ATOM   20314 H H    . GLN   B  1 555 ? 58.453 -9.744  -16.001 0.00 35.96  ? 581  GLN   B H    1 
ATOM   20315 H HA   . GLN   B  1 555 ? 60.802 -8.736  -14.786 0.00 38.79  ? 581  GLN   B HA   1 
ATOM   20316 H HB2  . GLN   B  1 555 ? 58.660 -9.330  -13.687 0.00 41.65  ? 581  GLN   B HB2  1 
ATOM   20317 H HB3  . GLN   B  1 555 ? 59.008 -11.045 -14.012 0.00 41.92  ? 581  GLN   B HB3  1 
ATOM   20318 H HG2  . GLN   B  1 555 ? 60.866 -10.996 -12.481 0.00 50.03  ? 581  GLN   B HG2  1 
ATOM   20319 H HG3  . GLN   B  1 555 ? 60.679 -9.224  -12.282 0.00 49.73  ? 581  GLN   B HG3  1 
ATOM   20320 H HE21 . GLN   B  1 555 ? 60.085 -9.102  -10.119 0.00 58.73  ? 581  GLN   B HE21 1 
ATOM   20321 H HE22 . GLN   B  1 555 ? 58.660 -9.898  -9.474  0.00 58.83  ? 581  GLN   B HE22 1 
ATOM   20322 N N    . ASN   B  1 556 ? 61.158 -11.768 -16.020 1.00 32.40  ? 582  ASN   B N    1 
ATOM   20323 C CA   . ASN   B  1 556 ? 62.097 -12.883 -16.170 1.00 33.93  ? 582  ASN   B CA   1 
ATOM   20324 C C    . ASN   B  1 556 ? 63.407 -12.582 -16.907 1.00 34.00  ? 582  ASN   B C    1 
ATOM   20325 O O    . ASN   B  1 556 ? 64.356 -13.369 -16.797 1.00 35.72  ? 582  ASN   B O    1 
ATOM   20326 C CB   . ASN   B  1 556 ? 61.402 -14.035 -16.860 1.00 36.86  ? 582  ASN   B CB   1 
ATOM   20327 C CG   . ASN   B  1 556 ? 60.298 -14.620 -16.083 1.00 43.50  ? 582  ASN   B CG   1 
ATOM   20328 O OD1  . ASN   B  1 556 ? 59.239 -13.983 -15.932 1.00 44.01  ? 582  ASN   B OD1  1 
ATOM   20329 N ND2  . ASN   B  1 556 ? 60.530 -15.754 -15.429 1.00 47.84  ? 582  ASN   B ND2  1 
ATOM   20330 H H    . ASN   B  1 556 ? 60.329 -11.843 -16.600 0.00 40.98  ? 582  ASN   B H    1 
ATOM   20331 H HA   . ASN   B  1 556 ? 62.370 -13.232 -15.175 0.00 44.11  ? 582  ASN   B HA   1 
ATOM   20332 H HB2  . ASN   B  1 556 ? 60.993 -13.675 -17.803 0.00 46.49  ? 582  ASN   B HB2  1 
ATOM   20333 H HB3  . ASN   B  1 556 ? 62.130 -14.820 -17.060 0.00 47.30  ? 582  ASN   B HB3  1 
ATOM   20334 H HD21 . ASN   B  1 556 ? 59.652 -16.136 -15.725 0.00 60.75  ? 582  ASN   B HD21 1 
ATOM   20335 H HD22 . ASN   B  1 556 ? 61.421 -16.237 -15.404 0.00 61.28  ? 582  ASN   B HD22 1 
ATOM   20336 N N    . PHE   B  1 557 ? 63.479 -11.482 -17.653 1.00 32.24  ? 583  PHE   B N    1 
ATOM   20337 C CA   . PHE   B  1 557 ? 64.670 -11.159 -18.434 1.00 31.09  ? 583  PHE   B CA   1 
ATOM   20338 C C    . PHE   B  1 557 ? 65.733 -10.420 -17.632 1.00 30.62  ? 583  PHE   B C    1 
ATOM   20339 O O    . PHE   B  1 557 ? 65.440 -9.374  -17.054 1.00 30.81  ? 583  PHE   B O    1 
ATOM   20340 C CB   . PHE   B  1 557 ? 64.274 -10.310 -19.637 1.00 30.18  ? 583  PHE   B CB   1 
ATOM   20341 C CG   . PHE   B  1 557 ? 63.252 -10.971 -20.523 1.00 30.12  ? 583  PHE   B CG   1 
ATOM   20342 C CD1  . PHE   B  1 557 ? 63.615 -11.996 -21.383 1.00 30.21  ? 583  PHE   B CD1  1 
ATOM   20343 C CD2  . PHE   B  1 557 ? 61.929 -10.566 -20.504 1.00 30.56  ? 583  PHE   B CD2  1 
ATOM   20344 C CE1  . PHE   B  1 557 ? 62.674 -12.607 -22.198 1.00 30.57  ? 583  PHE   B CE1  1 
ATOM   20345 C CE2  . PHE   B  1 557 ? 60.989 -11.178 -21.328 1.00 31.04  ? 583  PHE   B CE2  1 
ATOM   20346 C CZ   . PHE   B  1 557 ? 61.372 -12.181 -22.185 1.00 30.53  ? 583  PHE   B CZ   1 
ATOM   20347 H H    . PHE   B  1 557 ? 62.743 -10.788 -17.735 0.00 40.71  ? 583  PHE   B H    1 
ATOM   20348 H HA   . PHE   B  1 557 ? 65.106 -12.076 -18.828 0.00 39.82  ? 583  PHE   B HA   1 
ATOM   20349 H HB2  . PHE   B  1 557 ? 63.869 -9.363  -19.282 0.00 37.69  ? 583  PHE   B HB2  1 
ATOM   20350 H HB3  . PHE   B  1 557 ? 65.170 -10.145 -20.234 0.00 37.86  ? 583  PHE   B HB3  1 
ATOM   20351 H HD1  . PHE   B  1 557 ? 64.639 -12.327 -21.415 0.00 37.87  ? 583  PHE   B HD1  1 
ATOM   20352 H HD2  . PHE   B  1 557 ? 61.621 -9.771  -19.846 0.00 37.54  ? 583  PHE   B HD2  1 
ATOM   20353 H HE1  . PHE   B  1 557 ? 62.972 -13.398 -22.868 0.00 37.76  ? 583  PHE   B HE1  1 
ATOM   20354 H HE2  . PHE   B  1 557 ? 59.963 -10.852 -21.307 0.00 37.55  ? 583  PHE   B HE2  1 
ATOM   20355 H HZ   . PHE   B  1 557 ? 60.641 -12.663 -22.815 0.00 37.06  ? 583  PHE   B HZ   1 
ATOM   20356 N N    . THR   B  1 558 ? 66.982 -10.919 -17.656 1.00 29.64  ? 584  THR   B N    1 
ATOM   20357 C CA   . THR   B  1 558 ? 68.090 -10.279 -16.942 1.00 29.65  ? 584  THR   B CA   1 
ATOM   20358 C C    . THR   B  1 558 ? 68.833 -9.249  -17.794 1.00 29.22  ? 584  THR   B C    1 
ATOM   20359 O O    . THR   B  1 558 ? 69.545 -8.428  -17.227 1.00 29.88  ? 584  THR   B O    1 
ATOM   20360 C CB   . THR   B  1 558 ? 69.049 -11.337 -16.367 1.00 31.46  ? 584  THR   B CB   1 
ATOM   20361 O OG1  . THR   B  1 558 ? 69.801 -11.935 -17.421 1.00 33.22  ? 584  THR   B OG1  1 
ATOM   20362 C CG2  . THR   B  1 558 ? 68.323 -12.400 -15.552 1.00 31.65  ? 584  THR   B CG2  1 
ATOM   20363 H H    . THR   B  1 558 ? 67.257 -11.758 -18.157 0.00 38.86  ? 584  THR   B H    1 
ATOM   20364 H HA   . THR   B  1 558 ? 67.693 -9.742  -16.082 0.00 39.34  ? 584  THR   B HA   1 
ATOM   20365 H HB   . THR   B  1 558 ? 69.744 -10.836 -15.695 0.00 42.55  ? 584  THR   B HB   1 
ATOM   20366 H HG1  . THR   B  1 558 ? 69.202 -12.473 -18.003 0.00 43.97  ? 584  THR   B HG1  1 
ATOM   20367 H HG21 . THR   B  1 558 ? 69.047 -13.021 -15.027 0.00 43.32  ? 584  THR   B HG21 1 
ATOM   20368 H HG22 . THR   B  1 558 ? 67.667 -11.928 -14.822 0.00 42.68  ? 584  THR   B HG22 1 
ATOM   20369 H HG23 . THR   B  1 558 ? 67.729 -13.037 -16.206 0.00 42.44  ? 584  THR   B HG23 1 
ATOM   20370 N N    . ASN   B  1 559 ? 68.714 -9.293  -19.133 1.00 28.25  ? 585  ASN   B N    1 
ATOM   20371 C CA   . ASN   B  1 559 ? 69.416 -8.346  -20.009 1.00 28.62  ? 585  ASN   B CA   1 
ATOM   20372 C C    . ASN   B  1 559 ? 68.441 -7.428  -20.793 1.00 27.70  ? 585  ASN   B C    1 
ATOM   20373 O O    . ASN   B  1 559 ? 68.901 -6.748  -21.705 1.00 28.02  ? 585  ASN   B O    1 
ATOM   20374 C CB   . ASN   B  1 559 ? 70.269 -9.097  -21.038 1.00 30.71  ? 585  ASN   B CB   1 
ATOM   20375 C CG   . ASN   B  1 559 ? 71.246 -10.095 -20.477 1.00 35.42  ? 585  ASN   B CG   1 
ATOM   20376 O OD1  . ASN   B  1 559 ? 71.055 -11.314 -20.580 1.00 36.94  ? 585  ASN   B OD1  1 
ATOM   20377 N ND2  . ASN   B  1 559 ? 72.329 -9.600  -19.893 1.00 35.34  ? 585  ASN   B ND2  1 
ATOM   20378 H H    . ASN   B  1 559 ? 68.156 -9.967  -19.648 0.00 36.55  ? 585  ASN   B H    1 
ATOM   20379 H HA   . ASN   B  1 559 ? 70.084 -7.704  -19.436 0.00 37.26  ? 585  ASN   B HA   1 
ATOM   20380 H HB2  . ASN   B  1 559 ? 69.604 -9.633  -21.713 0.00 39.20  ? 585  ASN   B HB2  1 
ATOM   20381 H HB3  . ASN   B  1 559 ? 70.857 -8.375  -21.603 0.00 39.39  ? 585  ASN   B HB3  1 
ATOM   20382 H HD21 . ASN   B  1 559 ? 73.022 -10.232 -19.508 0.00 46.80  ? 585  ASN   B HD21 1 
ATOM   20383 H HD22 . ASN   B  1 559 ? 72.467 -8.596  -19.843 0.00 46.15  ? 585  ASN   B HD22 1 
ATOM   20384 N N    . LEU   B  1 560 ? 67.125 -7.432  -20.486 1.00 26.34  ? 586  LEU   B N    1 
ATOM   20385 C CA   . LEU   B  1 560 ? 66.171 -6.604  -21.229 1.00 25.54  ? 586  LEU   B CA   1 
ATOM   20386 C C    . LEU   B  1 560 ? 66.415 -5.126  -20.928 1.00 25.67  ? 586  LEU   B C    1 
ATOM   20387 O O    . LEU   B  1 560 ? 66.317 -4.718  -19.767 1.00 26.15  ? 586  LEU   B O    1 
ATOM   20388 C CB   . LEU   B  1 560 ? 64.728 -6.995  -20.893 1.00 24.62  ? 586  LEU   B CB   1 
ATOM   20389 C CG   . LEU   B  1 560 ? 63.618 -6.351  -21.744 1.00 25.19  ? 586  LEU   B CG   1 
ATOM   20390 C CD1  . LEU   B  1 560 ? 63.687 -6.821  -23.212 1.00 25.15  ? 586  LEU   B CD1  1 
ATOM   20391 C CD2  . LEU   B  1 560 ? 62.248 -6.668  -21.159 1.00 25.85  ? 586  LEU   B CD2  1 
ATOM   20392 H H    . LEU   B  1 560 ? 66.690 -7.976  -19.748 0.00 33.43  ? 586  LEU   B H    1 
ATOM   20393 H HA   . LEU   B  1 560 ? 66.302 -6.791  -22.291 0.00 31.34  ? 586  LEU   B HA   1 
ATOM   20394 H HB2  . LEU   B  1 560 ? 64.634 -8.070  -21.040 0.00 30.41  ? 586  LEU   B HB2  1 
ATOM   20395 H HB3  . LEU   B  1 560 ? 64.533 -6.746  -19.851 0.00 30.56  ? 586  LEU   B HB3  1 
ATOM   20396 H HG   . LEU   B  1 560 ? 63.732 -5.268  -21.737 0.00 30.25  ? 586  LEU   B HG   1 
ATOM   20397 H HD11 . LEU   B  1 560 ? 62.765 -6.536  -23.716 0.00 29.58  ? 586  LEU   B HD11 1 
ATOM   20398 H HD12 . LEU   B  1 560 ? 64.530 -6.336  -23.702 0.00 29.94  ? 586  LEU   B HD12 1 
ATOM   20399 H HD13 . LEU   B  1 560 ? 63.808 -7.903  -23.241 0.00 30.16  ? 586  LEU   B HD13 1 
ATOM   20400 H HD21 . LEU   B  1 560 ? 61.484 -6.177  -21.760 0.00 30.67  ? 586  LEU   B HD21 1 
ATOM   20401 H HD22 . LEU   B  1 560 ? 62.099 -7.746  -21.177 0.00 31.20  ? 586  LEU   B HD22 1 
ATOM   20402 H HD23 . LEU   B  1 560 ? 62.207 -6.300  -20.135 0.00 31.34  ? 586  LEU   B HD23 1 
ATOM   20403 N N    . LYS   B  1 561 ? 66.721 -4.330  -21.966 1.00 24.75  ? 587  LYS   B N    1 
ATOM   20404 C CA   . LYS   B  1 561 ? 67.008 -2.899  -21.850 1.00 24.76  ? 587  LYS   B CA   1 
ATOM   20405 C C    . LYS   B  1 561 ? 65.854 -2.022  -22.353 1.00 24.28  ? 587  LYS   B C    1 
ATOM   20406 O O    . LYS   B  1 561 ? 65.562 -1.000  -21.737 1.00 24.43  ? 587  LYS   B O    1 
ATOM   20407 C CB   . LYS   B  1 561 ? 68.256 -2.528  -22.675 1.00 25.93  ? 587  LYS   B CB   1 
ATOM   20408 C CG   . LYS   B  1 561 ? 69.550 -3.120  -22.160 1.00 32.10  ? 587  LYS   B CG   1 
ATOM   20409 C CD   . LYS   B  1 561 ? 70.709 -2.769  -23.093 1.00 38.04  ? 587  LYS   B CD   1 
ATOM   20410 C CE   . LYS   B  1 561 ? 72.055 -3.274  -22.617 1.00 42.78  ? 587  LYS   B CE   1 
ATOM   20411 N NZ   . LYS   B  1 561 ? 72.015 -4.700  -22.188 1.00 45.94  ? 587  LYS   B NZ   1 
ATOM   20412 H H    . LYS   B  1 561 ? 66.773 -4.658  -22.925 0.00 30.03  ? 587  LYS   B H    1 
ATOM   20413 H HA   . LYS   B  1 561 ? 67.208 -2.632  -20.813 0.00 30.64  ? 587  LYS   B HA   1 
ATOM   20414 H HB2  . LYS   B  1 561 ? 68.118 -2.875  -23.698 0.00 31.39  ? 587  LYS   B HB2  1 
ATOM   20415 H HB3  . LYS   B  1 561 ? 68.365 -1.445  -22.669 0.00 31.67  ? 587  LYS   B HB3  1 
ATOM   20416 H HG2  . LYS   B  1 561 ? 69.768 -2.716  -21.173 0.00 40.09  ? 587  LYS   B HG2  1 
ATOM   20417 H HG3  . LYS   B  1 561 ? 69.448 -4.203  -22.115 0.00 39.84  ? 587  LYS   B HG3  1 
ATOM   20418 H HD2  . LYS   B  1 561 ? 70.516 -3.205  -24.071 0.00 46.58  ? 587  LYS   B HD2  1 
ATOM   20419 H HD3  . LYS   B  1 561 ? 70.772 -1.685  -23.178 0.00 46.80  ? 587  LYS   B HD3  1 
ATOM   20420 H HE2  . LYS   B  1 561 ? 72.774 -3.186  -23.430 0.00 53.22  ? 587  LYS   B HE2  1 
ATOM   20421 H HE3  . LYS   B  1 561 ? 72.379 -2.675  -21.767 0.00 53.58  ? 587  LYS   B HE3  1 
ATOM   20422 H HZ1  . LYS   B  1 561 ? 72.958 -5.073  -22.150 0.00 57.71  ? 587  LYS   B HZ1  1 
ATOM   20423 H HZ2  . LYS   B  1 561 ? 71.601 -4.779  -21.265 0.00 57.49  ? 587  LYS   B HZ2  1 
ATOM   20424 H HZ3  . LYS   B  1 561 ? 71.468 -5.246  -22.846 0.00 56.98  ? 587  LYS   B HZ3  1 
ATOM   20425 N N    . VAL   B  1 562 ? 65.265 -2.372  -23.505 1.00 23.01  ? 588  VAL   B N    1 
ATOM   20426 C CA   . VAL   B  1 562 ? 64.232 -1.550  -24.137 1.00 23.12  ? 588  VAL   B CA   1 
ATOM   20427 C C    . VAL   B  1 562 ? 62.986 -2.375  -24.412 1.00 22.42  ? 588  VAL   B C    1 
ATOM   20428 O O    . VAL   B  1 562 ? 63.065 -3.446  -25.031 1.00 22.59  ? 588  VAL   B O    1 
ATOM   20429 C CB   . VAL   B  1 562 ? 64.781 -0.929  -25.446 1.00 24.34  ? 588  VAL   B CB   1 
ATOM   20430 C CG1  . VAL   B  1 562 ? 63.738 -0.016  -26.105 1.00 24.42  ? 588  VAL   B CG1  1 
ATOM   20431 C CG2  . VAL   B  1 562 ? 66.105 -0.182  -25.194 1.00 24.29  ? 588  VAL   B CG2  1 
ATOM   20432 H H    . VAL   B  1 562 ? 65.481 -3.216  -24.025 0.00 27.13  ? 588  VAL   B H    1 
ATOM   20433 H HA   . VAL   B  1 562 ? 63.955 -0.723  -23.485 0.00 26.88  ? 588  VAL   B HA   1 
ATOM   20434 H HB   . VAL   B  1 562 ? 64.986 -1.738  -26.145 0.00 27.90  ? 588  VAL   B HB   1 
ATOM   20435 H HG11 . VAL   B  1 562 ? 64.223 0.596   -26.864 0.00 27.50  ? 588  VAL   B HG11 1 
ATOM   20436 H HG12 . VAL   B  1 562 ? 62.969 -0.624  -26.578 0.00 27.38  ? 588  VAL   B HG12 1 
ATOM   20437 H HG13 . VAL   B  1 562 ? 63.292 0.622   -25.343 0.00 27.71  ? 588  VAL   B HG13 1 
ATOM   20438 H HG21 . VAL   B  1 562 ? 66.364 0.401   -26.076 0.00 28.05  ? 588  VAL   B HG21 1 
ATOM   20439 H HG22 . VAL   B  1 562 ? 65.987 0.478   -24.336 0.00 28.45  ? 588  VAL   B HG22 1 
ATOM   20440 H HG23 . VAL   B  1 562 ? 66.893 -0.907  -24.998 0.00 28.56  ? 588  VAL   B HG23 1 
ATOM   20441 N N    . LEU   B  1 563 ? 61.833 -1.855  -23.983 1.00 20.97  ? 589  LEU   B N    1 
ATOM   20442 C CA   . LEU   B  1 563 ? 60.554 -2.498  -24.177 1.00 20.29  ? 589  LEU   B CA   1 
ATOM   20443 C C    . LEU   B  1 563 ? 59.586 -1.471  -24.718 1.00 19.62  ? 589  LEU   B C    1 
ATOM   20444 O O    . LEU   B  1 563 ? 59.388 -0.420  -24.108 1.00 19.98  ? 589  LEU   B O    1 
ATOM   20445 C CB   . LEU   B  1 563 ? 60.026 -3.064  -22.850 1.00 20.27  ? 589  LEU   B CB   1 
ATOM   20446 C CG   . LEU   B  1 563 ? 58.622 -3.674  -22.884 1.00 20.89  ? 589  LEU   B CG   1 
ATOM   20447 C CD1  . LEU   B  1 563 ? 58.535 -4.840  -23.873 1.00 20.41  ? 589  LEU   B CD1  1 
ATOM   20448 C CD2  . LEU   B  1 563 ? 58.209 -4.113  -21.488 1.00 21.00  ? 589  LEU   B CD2  1 
ATOM   20449 H H    . LEU   B  1 563 ? 61.754 -0.973  -23.486 0.00 23.85  ? 589  LEU   B H    1 
ATOM   20450 H HA   . LEU   B  1 563 ? 60.640 -3.313  -24.894 0.00 22.64  ? 589  LEU   B HA   1 
ATOM   20451 H HB2  . LEU   B  1 563 ? 60.709 -3.842  -22.514 0.00 23.33  ? 589  LEU   B HB2  1 
ATOM   20452 H HB3  . LEU   B  1 563 ? 60.006 -2.256  -22.121 0.00 23.18  ? 589  LEU   B HB3  1 
ATOM   20453 H HG   . LEU   B  1 563 ? 57.919 -2.912  -23.210 0.00 23.34  ? 589  LEU   B HG   1 
ATOM   20454 H HD11 . LEU   B  1 563 ? 57.584 -5.353  -23.733 0.00 22.83  ? 589  LEU   B HD11 1 
ATOM   20455 H HD12 . LEU   B  1 563 ? 58.595 -4.453  -24.889 0.00 22.57  ? 589  LEU   B HD12 1 
ATOM   20456 H HD13 . LEU   B  1 563 ? 59.363 -5.521  -23.683 0.00 23.13  ? 589  LEU   B HD13 1 
ATOM   20457 H HD21 . LEU   B  1 563 ? 57.198 -4.516  -21.527 0.00 24.00  ? 589  LEU   B HD21 1 
ATOM   20458 H HD22 . LEU   B  1 563 ? 58.900 -4.879  -21.137 0.00 24.41  ? 589  LEU   B HD22 1 
ATOM   20459 H HD23 . LEU   B  1 563 ? 58.241 -3.253  -20.821 0.00 24.24  ? 589  LEU   B HD23 1 
ATOM   20460 N N    . ASN   B  1 564 ? 58.957 -1.787  -25.835 1.00 18.41  ? 590  ASN   B N    1 
ATOM   20461 C CA   . ASN   B  1 564 ? 57.988 -0.893  -26.444 1.00 18.15  ? 590  ASN   B CA   1 
ATOM   20462 C C    . ASN   B  1 564 ? 56.615 -1.551  -26.420 1.00 18.40  ? 590  ASN   B C    1 
ATOM   20463 O O    . ASN   B  1 564 ? 56.380 -2.525  -27.125 1.00 18.13  ? 590  ASN   B O    1 
ATOM   20464 C CB   . ASN   B  1 564 ? 58.441 -0.467  -27.855 1.00 17.87  ? 590  ASN   B CB   1 
ATOM   20465 C CG   . ASN   B  1 564 ? 57.639 0.696   -28.425 1.00 19.81  ? 590  ASN   B CG   1 
ATOM   20466 O OD1  . ASN   B  1 564 ? 56.515 0.916   -27.998 1.00 20.22  ? 590  ASN   B OD1  1 
ATOM   20467 N ND2  . ASN   B  1 564 ? 58.101 1.400   -29.463 1.00 21.53  ? 590  ASN   B ND2  1 
ATOM   20468 H H    . ASN   B  1 564 ? 59.086 -2.652  -26.352 0.00 19.71  ? 590  ASN   B H    1 
ATOM   20469 H HA   . ASN   B  1 564 ? 57.914 0.020   -25.860 0.00 19.19  ? 590  ASN   B HA   1 
ATOM   20470 H HB2  . ASN   B  1 564 ? 59.489 -0.183  -27.769 0.00 18.63  ? 590  ASN   B HB2  1 
ATOM   20471 H HB3  . ASN   B  1 564 ? 58.337 -1.308  -28.538 0.00 18.38  ? 590  ASN   B HB3  1 
ATOM   20472 H HD21 . ASN   B  1 564 ? 57.553 2.140   -29.891 0.00 22.27  ? 590  ASN   B HD21 1 
ATOM   20473 N N    . LEU   B  1 565 ? 55.721 -1.032  -25.555 1.00 18.57  ? 591  LEU   B N    1 
ATOM   20474 C CA   . LEU   B  1 565 ? 54.328 -1.465  -25.469 1.00 19.14  ? 591  LEU   B CA   1 
ATOM   20475 C C    . LEU   B  1 565 ? 53.397 -0.431  -26.117 1.00 18.93  ? 591  LEU   B C    1 
ATOM   20476 O O    . LEU   B  1 565 ? 52.222 -0.405  -25.766 1.00 19.29  ? 591  LEU   B O    1 
ATOM   20477 C CB   . LEU   B  1 565 ? 53.917 -1.639  -23.988 1.00 19.33  ? 591  LEU   B CB   1 
ATOM   20478 C CG   . LEU   B  1 565 ? 54.781 -2.591  -23.163 1.00 21.00  ? 591  LEU   B CG   1 
ATOM   20479 C CD1  . LEU   B  1 565 ? 54.333 -2.629  -21.714 1.00 21.68  ? 591  LEU   B CD1  1 
ATOM   20480 C CD2  . LEU   B  1 565 ? 54.750 -4.004  -23.749 1.00 22.22  ? 591  LEU   B CD2  1 
ATOM   20481 H H    . LEU   B  1 565 ? 55.940 -0.302  -24.885 0.00 19.71  ? 591  LEU   B H    1 
ATOM   20482 H HA   . LEU   B  1 565 ? 54.179 -2.414  -25.980 0.00 20.10  ? 591  LEU   B HA   1 
ATOM   20483 H HB2  . LEU   B  1 565 ? 53.951 -0.664  -23.504 0.00 20.80  ? 591  LEU   B HB2  1 
ATOM   20484 H HB3  . LEU   B  1 565 ? 52.903 -2.034  -23.946 0.00 20.69  ? 591  LEU   B HB3  1 
ATOM   20485 H HG   . LEU   B  1 565 ? 55.801 -2.216  -23.175 0.00 23.16  ? 591  LEU   B HG   1 
ATOM   20486 H HD11 . LEU   B  1 565 ? 55.026 -3.246  -21.145 0.00 24.53  ? 591  LEU   B HD11 1 
ATOM   20487 H HD12 . LEU   B  1 565 ? 54.322 -1.614  -21.320 0.00 24.29  ? 591  LEU   B HD12 1 
ATOM   20488 H HD13 . LEU   B  1 565 ? 53.332 -3.055  -21.667 0.00 24.20  ? 591  LEU   B HD13 1 
ATOM   20489 H HD21 . LEU   B  1 565 ? 55.222 -4.688  -23.045 0.00 24.83  ? 591  LEU   B HD21 1 
ATOM   20490 H HD22 . LEU   B  1 565 ? 53.714 -4.298  -23.917 0.00 24.43  ? 591  LEU   B HD22 1 
ATOM   20491 H HD23 . LEU   B  1 565 ? 55.296 -4.014  -24.691 0.00 24.35  ? 591  LEU   B HD23 1 
ATOM   20492 N N    . SER   B  1 566 ? 53.884 0.395   -27.064 1.00 18.66  ? 592  SER   B N    1 
ATOM   20493 C CA   . SER   B  1 566 ? 53.062 1.445   -27.645 1.00 18.97  ? 592  SER   B CA   1 
ATOM   20494 C C    . SER   B  1 566 ? 51.845 0.973   -28.450 1.00 19.40  ? 592  SER   B C    1 
ATOM   20495 O O    . SER   B  1 566 ? 51.851 -0.111  -29.041 1.00 19.76  ? 592  SER   B O    1 
ATOM   20496 C CB   . SER   B  1 566 ? 53.888 2.398   -28.504 1.00 20.47  ? 592  SER   B CB   1 
ATOM   20497 O OG   . SER   B  1 566 ? 54.230 1.869   -29.776 1.00 22.59  ? 592  SER   B OG   1 
ATOM   20498 H H    . SER   B  1 566 ? 54.817 0.347   -27.462 0.00 19.10  ? 592  SER   B H    1 
ATOM   20499 H HA   . SER   B  1 566 ? 52.680 2.038   -26.815 0.00 19.45  ? 592  SER   B HA   1 
ATOM   20500 H HB2  . SER   B  1 566 ? 53.317 3.312   -28.658 0.00 20.90  ? 592  SER   B HB2  1 
ATOM   20501 H HB3  . SER   B  1 566 ? 54.812 2.632   -27.979 0.00 21.12  ? 592  SER   B HB3  1 
ATOM   20502 H HG   . SER   B  1 566 ? 54.472 0.909   -29.694 0.00 23.33  ? 592  SER   B HG   1 
ATOM   20503 N N    . HIS   B  1 567 ? 50.798 1.812   -28.440 1.00 18.39  ? 593  HIS   B N    1 
ATOM   20504 C CA   . HIS   B  1 567 ? 49.580 1.620   -29.221 1.00 19.16  ? 593  HIS   B CA   1 
ATOM   20505 C C    . HIS   B  1 567 ? 48.962 0.243   -29.033 1.00 19.36  ? 593  HIS   B C    1 
ATOM   20506 O O    . HIS   B  1 567 ? 48.522 -0.395  -29.986 1.00 19.39  ? 593  HIS   B O    1 
ATOM   20507 C CB   . HIS   B  1 567 ? 49.876 1.924   -30.688 1.00 20.47  ? 593  HIS   B CB   1 
ATOM   20508 C CG   . HIS   B  1 567 ? 50.422 3.306   -30.871 1.00 24.31  ? 593  HIS   B CG   1 
ATOM   20509 N ND1  . HIS   B  1 567 ? 49.602 4.413   -30.803 1.00 26.65  ? 593  HIS   B ND1  1 
ATOM   20510 C CD2  . HIS   B  1 567 ? 51.699 3.719   -31.050 1.00 25.98  ? 593  HIS   B CD2  1 
ATOM   20511 C CE1  . HIS   B  1 567 ? 50.398 5.462   -30.946 1.00 27.44  ? 593  HIS   B CE1  1 
ATOM   20512 N NE2  . HIS   B  1 567 ? 51.666 5.090   -31.116 1.00 27.61  ? 593  HIS   B NE2  1 
ATOM   20513 H H    . HIS   B  1 567 ? 50.766 2.660   -27.886 0.00 18.46  ? 593  HIS   B H    1 
ATOM   20514 H HA   . HIS   B  1 567 ? 48.842 2.346   -28.887 0.00 19.20  ? 593  HIS   B HA   1 
ATOM   20515 H HB2  . HIS   B  1 567 ? 50.610 1.215   -31.068 0.00 20.42  ? 593  HIS   B HB2  1 
ATOM   20516 H HB3  . HIS   B  1 567 ? 48.954 1.857   -31.265 0.00 20.39  ? 593  HIS   B HB3  1 
ATOM   20517 H HD2  . HIS   B  1 567 ? 52.573 3.095   -31.127 0.00 27.04  ? 593  HIS   B HD2  1 
ATOM   20518 H HE1  . HIS   B  1 567 ? 50.061 6.483   -30.929 0.00 28.91  ? 593  HIS   B HE1  1 
ATOM   20519 H HE2  . HIS   B  1 567 ? 52.460 5.705   -31.267 0.00 29.05  ? 593  HIS   B HE2  1 
ATOM   20520 N N    . ASN   B  1 568 ? 48.921 -0.194  -27.784 1.00 18.96  ? 594  ASN   B N    1 
ATOM   20521 C CA   . ASN   B  1 568 ? 48.312 -1.460  -27.404 1.00 19.19  ? 594  ASN   B CA   1 
ATOM   20522 C C    . ASN   B  1 568 ? 46.958 -1.274  -26.722 1.00 19.47  ? 594  ASN   B C    1 
ATOM   20523 O O    . ASN   B  1 568 ? 46.292 -2.272  -26.464 1.00 18.77  ? 594  ASN   B O    1 
ATOM   20524 C CB   . ASN   B  1 568 ? 49.261 -2.256  -26.519 1.00 19.89  ? 594  ASN   B CB   1 
ATOM   20525 C CG   . ASN   B  1 568 ? 50.223 -3.060  -27.331 1.00 21.15  ? 594  ASN   B CG   1 
ATOM   20526 O OD1  . ASN   B  1 568 ? 49.788 -3.716  -28.256 1.00 22.38  ? 594  ASN   B OD1  1 
ATOM   20527 N ND2  . ASN   B  1 568 ? 51.505 -3.062  -27.027 1.00 19.53  ? 594  ASN   B ND2  1 
ATOM   20528 H H    . ASN   B  1 568 ? 49.280 0.326   -26.991 0.00 19.34  ? 594  ASN   B H    1 
ATOM   20529 H HA   . ASN   B  1 568 ? 48.064 -2.019  -28.304 0.00 19.49  ? 594  ASN   B HA   1 
ATOM   20530 H HB2  . ASN   B  1 568 ? 49.807 -1.594  -25.849 0.00 20.77  ? 594  ASN   B HB2  1 
ATOM   20531 H HB3  . ASN   B  1 568 ? 48.687 -2.988  -25.955 0.00 20.83  ? 594  ASN   B HB3  1 
ATOM   20532 H HD21 . ASN   B  1 568 ? 52.150 -3.614  -27.582 0.00 20.22  ? 594  ASN   B HD21 1 
ATOM   20533 H HD22 . ASN   B  1 568 ? 51.852 -2.525  -26.239 0.00 20.38  ? 594  ASN   B HD22 1 
ATOM   20534 N N    . ASN   B  1 569 ? 46.522 -0.016  -26.443 1.00 20.35  ? 595  ASN   B N    1 
ATOM   20535 C CA   . ASN   B  1 569 ? 45.228 0.240   -25.810 1.00 21.81  ? 595  ASN   B CA   1 
ATOM   20536 C C    . ASN   B  1 569 ? 45.117 -0.513  -24.469 1.00 21.55  ? 595  ASN   B C    1 
ATOM   20537 O O    . ASN   B  1 569 ? 44.051 -1.015  -24.131 1.00 22.10  ? 595  ASN   B O    1 
ATOM   20538 C CB   . ASN   B  1 569 ? 44.096 -0.172  -26.792 1.00 25.16  ? 595  ASN   B CB   1 
ATOM   20539 C CG   . ASN   B  1 569 ? 43.218 0.954   -27.256 1.00 34.25  ? 595  ASN   B CG   1 
ATOM   20540 O OD1  . ASN   B  1 569 ? 43.710 1.998   -27.725 1.00 37.66  ? 595  ASN   B OD1  1 
ATOM   20541 N ND2  . ASN   B  1 569 ? 41.905 0.796   -27.130 1.00 35.79  ? 595  ASN   B ND2  1 
ATOM   20542 H H    . ASN   B  1 569 ? 47.038 0.836   -26.634 0.00 21.08  ? 595  ASN   B H    1 
ATOM   20543 H HA   . ASN   B  1 569 ? 45.174 1.303   -25.578 0.00 23.11  ? 595  ASN   B HA   1 
ATOM   20544 H HB2  . ASN   B  1 569 ? 44.560 -0.531  -27.707 0.00 26.82  ? 595  ASN   B HB2  1 
ATOM   20545 H HB3  . ASN   B  1 569 ? 43.475 -0.964  -26.379 0.00 27.14  ? 595  ASN   B HB3  1 
ATOM   20546 H HD21 . ASN   B  1 569 ? 41.284 1.539   -27.435 0.00 39.85  ? 595  ASN   B HD21 1 
ATOM   20547 H HD22 . ASN   B  1 569 ? 41.512 -0.036  -26.702 0.00 39.97  ? 595  ASN   B HD22 1 
ATOM   20548 N N    . ILE   B  1 570 ? 46.236 -0.608  -23.719 1.00 20.78  ? 596  ILE   B N    1 
ATOM   20549 C CA   . ILE   B  1 570 ? 46.267 -1.323  -22.444 1.00 20.52  ? 596  ILE   B CA   1 
ATOM   20550 C C    . ILE   B  1 570 ? 45.484 -0.536  -21.403 1.00 20.21  ? 596  ILE   B C    1 
ATOM   20551 O O    . ILE   B  1 570 ? 45.813 0.620   -21.137 1.00 20.82  ? 596  ILE   B O    1 
ATOM   20552 C CB   . ILE   B  1 570 ? 47.733 -1.559  -21.959 1.00 20.30  ? 596  ILE   B CB   1 
ATOM   20553 C CG1  . ILE   B  1 570 ? 48.519 -2.429  -22.992 1.00 19.75  ? 596  ILE   B CG1  1 
ATOM   20554 C CG2  . ILE   B  1 570 ? 47.738 -2.200  -20.546 1.00 20.73  ? 596  ILE   B CG2  1 
ATOM   20555 C CD1  . ILE   B  1 570 ? 50.057 -2.519  -22.801 1.00 19.90  ? 596  ILE   B CD1  1 
ATOM   20556 H H    . ILE   B  1 570 ? 47.122 -0.174  -23.957 0.00 22.18  ? 596  ILE   B H    1 
ATOM   20557 H HA   . ILE   B  1 570 ? 45.802 -2.300  -22.574 0.00 22.31  ? 596  ILE   B HA   1 
ATOM   20558 H HB   . ILE   B  1 570 ? 48.226 -0.590  -21.890 0.00 22.12  ? 596  ILE   B HB   1 
ATOM   20559 H HG12 . ILE   B  1 570 ? 48.117 -3.441  -22.980 0.00 21.36  ? 596  ILE   B HG12 1 
ATOM   20560 H HG13 . ILE   B  1 570 ? 48.361 -1.980  -23.970 0.00 21.03  ? 596  ILE   B HG13 1 
ATOM   20561 H HG21 . ILE   B  1 570 ? 48.700 -2.673  -20.354 0.00 23.15  ? 596  ILE   B HG21 1 
ATOM   20562 H HG22 . ILE   B  1 570 ? 47.575 -1.425  -19.798 0.00 23.22  ? 596  ILE   B HG22 1 
ATOM   20563 H HG23 . ILE   B  1 570 ? 46.943 -2.942  -20.492 0.00 23.11  ? 596  ILE   B HG23 1 
ATOM   20564 H HD11 . ILE   B  1 570 ? 50.498 -2.938  -23.704 0.00 21.37  ? 596  ILE   B HD11 1 
ATOM   20565 H HD12 . ILE   B  1 570 ? 50.453 -1.520  -22.623 0.00 21.55  ? 596  ILE   B HD12 1 
ATOM   20566 H HD13 . ILE   B  1 570 ? 50.283 -3.165  -21.954 0.00 21.81  ? 596  ILE   B HD13 1 
ATOM   20567 N N    . TYR   B  1 571 ? 44.422 -1.138  -20.856 1.00 19.54  ? 597  TYR   B N    1 
ATOM   20568 C CA   . TYR   B  1 571 ? 43.620 -0.519  -19.798 1.00 19.71  ? 597  TYR   B CA   1 
ATOM   20569 C C    . TYR   B  1 571 ? 43.241 -1.469  -18.683 1.00 19.82  ? 597  TYR   B C    1 
ATOM   20570 O O    . TYR   B  1 571 ? 42.637 -1.023  -17.725 1.00 19.79  ? 597  TYR   B O    1 
ATOM   20571 C CB   . TYR   B  1 571 ? 42.339 0.116   -20.353 1.00 19.74  ? 597  TYR   B CB   1 
ATOM   20572 C CG   . TYR   B  1 571 ? 41.266 -0.842  -20.808 1.00 20.69  ? 597  TYR   B CG   1 
ATOM   20573 C CD1  . TYR   B  1 571 ? 41.353 -1.463  -22.043 1.00 21.13  ? 597  TYR   B CD1  1 
ATOM   20574 C CD2  . TYR   B  1 571 ? 40.067 -0.956  -20.109 1.00 21.91  ? 597  TYR   B CD2  1 
ATOM   20575 C CE1  . TYR   B  1 571 ? 40.309 -2.218  -22.547 1.00 22.13  ? 597  TYR   B CE1  1 
ATOM   20576 C CE2  . TYR   B  1 571 ? 39.011 -1.715  -20.605 1.00 22.71  ? 597  TYR   B CE2  1 
ATOM   20577 C CZ   . TYR   B  1 571 ? 39.134 -2.332  -21.835 1.00 23.09  ? 597  TYR   B CZ   1 
ATOM   20578 O OH   . TYR   B  1 571 ? 38.102 -3.038  -22.392 1.00 24.16  ? 597  TYR   B OH   1 
ATOM   20579 H H    . TYR   B  1 571 ? 44.057 -2.028  -21.177 0.00 21.53  ? 597  TYR   B H    1 
ATOM   20580 H HA   . TYR   B  1 571 ? 44.195 0.285   -19.345 0.00 22.13  ? 597  TYR   B HA   1 
ATOM   20581 H HB2  . TYR   B  1 571 ? 41.916 0.798   -19.617 0.00 22.22  ? 597  TYR   B HB2  1 
ATOM   20582 H HB3  . TYR   B  1 571 ? 42.587 0.647   -21.268 0.00 21.75  ? 597  TYR   B HB3  1 
ATOM   20583 H HD1  . TYR   B  1 571 ? 42.250 -1.352  -22.626 0.00 23.17  ? 597  TYR   B HD1  1 
ATOM   20584 H HD2  . TYR   B  1 571 ? 39.946 -0.436  -19.174 0.00 25.11  ? 597  TYR   B HD2  1 
ATOM   20585 H HE1  . TYR   B  1 571 ? 40.411 -2.703  -23.492 0.00 24.43  ? 597  TYR   B HE1  1 
ATOM   20586 H HE2  . TYR   B  1 571 ? 38.091 -1.791  -20.050 0.00 26.09  ? 597  TYR   B HE2  1 
ATOM   20587 H HH   . TYR   B  1 571 ? 38.276 -3.245  -23.347 0.00 27.18  ? 597  TYR   B HH   1 
ATOM   20588 N N    . THR   B  1 572 ? 43.549 -2.779  -18.799 1.00 20.15  ? 598  THR   B N    1 
ATOM   20589 C CA   . THR   B  1 572 ? 43.200 -3.748  -17.767 1.00 19.96  ? 598  THR   B CA   1 
ATOM   20590 C C    . THR   B  1 572 ? 44.133 -4.947  -17.870 1.00 20.31  ? 598  THR   B C    1 
ATOM   20591 O O    . THR   B  1 572 ? 44.431 -5.409  -18.982 1.00 19.82  ? 598  THR   B O    1 
ATOM   20592 C CB   . THR   B  1 572 ? 41.709 -4.165  -17.883 1.00 20.38  ? 598  THR   B CB   1 
ATOM   20593 O OG1  . THR   B  1 572 ? 41.415 -5.117  -16.859 1.00 21.16  ? 598  THR   B OG1  1 
ATOM   20594 C CG2  . THR   B  1 572 ? 41.348 -4.744  -19.255 1.00 20.31  ? 598  THR   B CG2  1 
ATOM   20595 H H    . THR   B  1 572 ? 44.026 -3.191  -19.594 0.00 22.73  ? 598  THR   B H    1 
ATOM   20596 H HA   . THR   B  1 572 ? 43.343 -3.293  -16.788 0.00 23.33  ? 598  THR   B HA   1 
ATOM   20597 H HB   . THR   B  1 572 ? 41.089 -3.283  -17.725 0.00 23.68  ? 598  THR   B HB   1 
ATOM   20598 H HG1  . THR   B  1 572 ? 40.462 -5.393  -16.915 0.00 25.06  ? 598  THR   B HG1  1 
ATOM   20599 H HG21 . THR   B  1 572 ? 40.276 -4.931  -19.279 0.00 23.38  ? 598  THR   B HG21 1 
ATOM   20600 H HG22 . THR   B  1 572 ? 41.600 -4.044  -20.049 0.00 23.00  ? 598  THR   B HG22 1 
ATOM   20601 H HG23 . THR   B  1 572 ? 41.871 -5.684  -19.427 0.00 23.30  ? 598  THR   B HG23 1 
ATOM   20602 N N    . LEU   B  1 573 ? 44.616 -5.417  -16.717 1.00 20.77  ? 599  LEU   B N    1 
ATOM   20603 C CA   . LEU   B  1 573 ? 45.484 -6.583  -16.586 1.00 20.93  ? 599  LEU   B CA   1 
ATOM   20604 C C    . LEU   B  1 573 ? 44.846 -7.559  -15.578 1.00 21.84  ? 599  LEU   B C    1 
ATOM   20605 O O    . LEU   B  1 573 ? 44.045 -7.161  -14.728 1.00 22.35  ? 599  LEU   B O    1 
ATOM   20606 C CB   . LEU   B  1 573 ? 46.904 -6.175  -16.134 1.00 20.43  ? 599  LEU   B CB   1 
ATOM   20607 C CG   . LEU   B  1 573 ? 47.690 -5.245  -17.087 1.00 20.78  ? 599  LEU   B CG   1 
ATOM   20608 C CD1  . LEU   B  1 573 ? 49.039 -4.875  -16.496 1.00 21.14  ? 599  LEU   B CD1  1 
ATOM   20609 C CD2  . LEU   B  1 573 ? 47.918 -5.874  -18.464 1.00 21.06  ? 599  LEU   B CD2  1 
ATOM   20610 H H    . LEU   B  1 573 ? 44.408 -5.001  -15.814 0.00 24.70  ? 599  LEU   B H    1 
ATOM   20611 H HA   . LEU   B  1 573 ? 45.560 -7.110  -17.533 0.00 24.59  ? 599  LEU   B HA   1 
ATOM   20612 H HB2  . LEU   B  1 573 ? 46.822 -5.663  -15.177 0.00 24.57  ? 599  LEU   B HB2  1 
ATOM   20613 H HB3  . LEU   B  1 573 ? 47.494 -7.082  -16.008 0.00 24.48  ? 599  LEU   B HB3  1 
ATOM   20614 H HG   . LEU   B  1 573 ? 47.126 -4.324  -17.231 0.00 24.21  ? 599  LEU   B HG   1 
ATOM   20615 H HD11 . LEU   B  1 573 ? 49.534 -4.163  -17.155 0.00 24.72  ? 599  LEU   B HD11 1 
ATOM   20616 H HD12 . LEU   B  1 573 ? 48.886 -4.428  -15.516 0.00 25.25  ? 599  LEU   B HD12 1 
ATOM   20617 H HD13 . LEU   B  1 573 ? 49.641 -5.778  -16.406 0.00 25.13  ? 599  LEU   B HD13 1 
ATOM   20618 H HD21 . LEU   B  1 573 ? 48.588 -5.237  -19.039 0.00 24.13  ? 599  LEU   B HD21 1 
ATOM   20619 H HD22 . LEU   B  1 573 ? 48.360 -6.860  -18.332 0.00 24.52  ? 599  LEU   B HD22 1 
ATOM   20620 H HD23 . LEU   B  1 573 ? 46.964 -5.961  -18.982 0.00 24.19  ? 599  LEU   B HD23 1 
ATOM   20621 N N    . THR   B  1 574 ? 45.151 -8.850  -15.730 1.00 22.15  ? 600  THR   B N    1 
ATOM   20622 C CA   . THR   B  1 574 ? 44.596 -9.902  -14.894 1.00 22.94  ? 600  THR   B CA   1 
ATOM   20623 C C    . THR   B  1 574 ? 45.549 -10.248 -13.752 1.00 24.90  ? 600  THR   B C    1 
ATOM   20624 O O    . THR   B  1 574 ? 46.682 -10.654 -14.024 1.00 25.58  ? 600  THR   B O    1 
ATOM   20625 C CB   . THR   B  1 574 ? 44.377 -11.163 -15.752 1.00 23.32  ? 600  THR   B CB   1 
ATOM   20626 O OG1  . THR   B  1 574 ? 43.559 -10.825 -16.875 1.00 23.10  ? 600  THR   B OG1  1 
ATOM   20627 C CG2  . THR   B  1 574 ? 43.731 -12.293 -14.955 1.00 23.95  ? 600  THR   B CG2  1 
ATOM   20628 H H    . THR   B  1 574 ? 45.792 -9.197  -16.436 0.00 26.68  ? 600  THR   B H    1 
ATOM   20629 H HA   . THR   B  1 574 ? 43.631 -9.608  -14.487 0.00 28.32  ? 600  THR   B HA   1 
ATOM   20630 H HB   . THR   B  1 574 ? 45.337 -11.520 -16.119 0.00 28.62  ? 600  THR   B HB   1 
ATOM   20631 H HG1  . THR   B  1 574 ? 42.687 -10.465 -16.565 0.00 28.05  ? 600  THR   B HG1  1 
ATOM   20632 H HG21 . THR   B  1 574 ? 43.307 -13.026 -15.639 0.00 29.84  ? 600  THR   B HG21 1 
ATOM   20633 H HG22 . THR   B  1 574 ? 44.472 -12.794 -14.334 0.00 30.18  ? 600  THR   B HG22 1 
ATOM   20634 H HG23 . THR   B  1 574 ? 42.939 -11.900 -14.319 0.00 30.01  ? 600  THR   B HG23 1 
ATOM   20635 N N    . ASP   B  1 575 ? 45.094 -10.101 -12.491 1.00 25.75  ? 601  ASP   B N    1 
ATOM   20636 C CA   . ASP   B  1 575 ? 45.817 -10.498 -11.274 1.00 27.18  ? 601  ASP   B CA   1 
ATOM   20637 C C    . ASP   B  1 575 ? 47.111 -9.706  -10.961 1.00 28.09  ? 601  ASP   B C    1 
ATOM   20638 O O    . ASP   B  1 575 ? 47.254 -9.242  -9.822  1.00 28.86  ? 601  ASP   B O    1 
ATOM   20639 C CB   . ASP   B  1 575 ? 46.124 -12.009 -11.284 1.00 29.33  ? 601  ASP   B CB   1 
ATOM   20640 C CG   . ASP   B  1 575 ? 44.876 -12.878 -11.334 1.00 34.31  ? 601  ASP   B CG   1 
ATOM   20641 O OD1  . ASP   B  1 575 ? 43.841 -12.477 -10.744 1.00 35.44  ? 601  ASP   B OD1  1 
ATOM   20642 O OD2  . ASP   B  1 575 ? 44.928 -13.943 -11.967 1.00 36.69  ? 601  ASP   B OD2  1 
ATOM   20643 H H    . ASP   B  1 575 ? 44.192 -9.690  -12.275 0.00 32.45  ? 601  ASP   B H    1 
ATOM   20644 H HA   . ASP   B  1 575 ? 45.120 -10.333 -10.452 0.00 34.93  ? 601  ASP   B HA   1 
ATOM   20645 H HB2  . ASP   B  1 575 ? 46.742 -12.254 -12.147 0.00 37.29  ? 601  ASP   B HB2  1 
ATOM   20646 H HB3  . ASP   B  1 575 ? 46.660 -12.259 -10.369 0.00 37.94  ? 601  ASP   B HB3  1 
ATOM   20647 N N    . LYS   B  1 576 ? 48.076 -9.626  -11.897 1.00 27.64  ? 602  LYS   B N    1 
ATOM   20648 C CA   . LYS   B  1 576 ? 49.290 -8.855  -11.673 1.00 27.84  ? 602  LYS   B CA   1 
ATOM   20649 C C    . LYS   B  1 576 ? 49.106 -7.536  -12.392 1.00 27.33  ? 602  LYS   B C    1 
ATOM   20650 O O    . LYS   B  1 576 ? 49.012 -7.496  -13.615 1.00 27.05  ? 602  LYS   B O    1 
ATOM   20651 C CB   . LYS   B  1 576 ? 50.583 -9.554  -12.148 1.00 30.27  ? 602  LYS   B CB   1 
ATOM   20652 C CG   . LYS   B  1 576 ? 51.836 -8.819  -11.613 1.00 35.74  ? 602  LYS   B CG   1 
ATOM   20653 C CD   . LYS   B  1 576 ? 53.161 -9.509  -11.918 1.00 42.21  ? 602  LYS   B CD   1 
ATOM   20654 C CE   . LYS   B  1 576 ? 54.166 -9.434  -10.797 1.00 47.04  ? 602  LYS   B CE   1 
ATOM   20655 N NZ   . LYS   B  1 576 ? 54.370 -8.059  -10.268 1.00 50.32  ? 602  LYS   B NZ   1 
ATOM   20656 H H    . LYS   B  1 576 ? 48.036 -10.083 -12.803 0.00 34.68  ? 602  LYS   B H    1 
ATOM   20657 H HA   . LYS   B  1 576 ? 49.391 -8.663  -10.605 0.00 35.60  ? 602  LYS   B HA   1 
ATOM   20658 H HB2  . LYS   B  1 576 ? 50.599 -10.574 -11.768 0.00 38.48  ? 602  LYS   B HB2  1 
ATOM   20659 H HB3  . LYS   B  1 576 ? 50.623 -9.558  -13.236 0.00 37.76  ? 602  LYS   B HB3  1 
ATOM   20660 H HG2  . LYS   B  1 576 ? 51.886 -7.824  -12.053 0.00 44.58  ? 602  LYS   B HG2  1 
ATOM   20661 H HG3  . LYS   B  1 576 ? 51.747 -8.739  -10.531 0.00 45.30  ? 602  LYS   B HG3  1 
ATOM   20662 H HD2  . LYS   B  1 576 ? 52.968 -10.565 -12.097 0.00 52.94  ? 602  LYS   B HD2  1 
ATOM   20663 H HD3  . LYS   B  1 576 ? 53.605 -9.054  -12.802 0.00 52.50  ? 602  LYS   B HD3  1 
ATOM   20664 H HE2  . LYS   B  1 576 ? 53.820 -10.059 -9.974  0.00 59.59  ? 602  LYS   B HE2  1 
ATOM   20665 H HE3  . LYS   B  1 576 ? 55.125 -9.799  -11.160 0.00 59.30  ? 602  LYS   B HE3  1 
ATOM   20666 H HZ1  . LYS   B  1 576 ? 55.016 -8.105  -9.487  0.00 63.59  ? 602  LYS   B HZ1  1 
ATOM   20667 H HZ2  . LYS   B  1 576 ? 54.758 -7.463  -10.992 0.00 62.83  ? 602  LYS   B HZ2  1 
ATOM   20668 H HZ3  . LYS   B  1 576 ? 53.504 -7.652  -9.931  0.00 63.12  ? 602  LYS   B HZ3  1 
ATOM   20669 N N    . TYR   B  1 577 ? 49.020 -6.464  -11.626 1.00 26.48  ? 603  TYR   B N    1 
ATOM   20670 C CA   . TYR   B  1 577 ? 48.780 -5.139  -12.173 1.00 26.18  ? 603  TYR   B CA   1 
ATOM   20671 C C    . TYR   B  1 577 ? 50.057 -4.341  -12.466 1.00 26.62  ? 603  TYR   B C    1 
ATOM   20672 O O    . TYR   B  1 577 ? 49.975 -3.290  -13.113 1.00 27.52  ? 603  TYR   B O    1 
ATOM   20673 C CB   . TYR   B  1 577 ? 47.904 -4.369  -11.171 1.00 25.29  ? 603  TYR   B CB   1 
ATOM   20674 C CG   . TYR   B  1 577 ? 46.627 -5.103  -10.811 1.00 24.83  ? 603  TYR   B CG   1 
ATOM   20675 C CD1  . TYR   B  1 577 ? 45.788 -5.595  -11.796 1.00 24.86  ? 603  TYR   B CD1  1 
ATOM   20676 C CD2  . TYR   B  1 577 ? 46.302 -5.371  -9.487  1.00 25.83  ? 603  TYR   B CD2  1 
ATOM   20677 C CE1  . TYR   B  1 577 ? 44.615 -6.267  -11.478 1.00 25.72  ? 603  TYR   B CE1  1 
ATOM   20678 C CE2  . TYR   B  1 577 ? 45.128 -6.041  -9.154  1.00 26.46  ? 603  TYR   B CE2  1 
ATOM   20679 C CZ   . TYR   B  1 577 ? 44.285 -6.488  -10.155 1.00 26.73  ? 603  TYR   B CZ   1 
ATOM   20680 O OH   . TYR   B  1 577 ? 43.128 -7.174  -9.850  1.00 27.55  ? 603  TYR   B OH   1 
ATOM   20681 H H    . TYR   B  1 577 ? 49.130 -6.467  -10.617 0.00 33.66  ? 603  TYR   B H    1 
ATOM   20682 H HA   . TYR   B  1 577 ? 48.222 -5.208  -13.105 0.00 32.18  ? 603  TYR   B HA   1 
ATOM   20683 H HB2  . TYR   B  1 577 ? 48.476 -4.203  -10.259 0.00 32.13  ? 603  TYR   B HB2  1 
ATOM   20684 H HB3  . TYR   B  1 577 ? 47.625 -3.413  -11.611 0.00 31.51  ? 603  TYR   B HB3  1 
ATOM   20685 H HD1  . TYR   B  1 577 ? 46.018 -5.405  -12.831 0.00 30.64  ? 603  TYR   B HD1  1 
ATOM   20686 H HD2  . TYR   B  1 577 ? 46.940 -5.009  -8.698  0.00 33.39  ? 603  TYR   B HD2  1 
ATOM   20687 H HE1  . TYR   B  1 577 ? 43.971 -6.608  -12.271 0.00 31.99  ? 603  TYR   B HE1  1 
ATOM   20688 H HE2  . TYR   B  1 577 ? 44.881 -6.218  -8.120  0.00 34.42  ? 603  TYR   B HE2  1 
ATOM   20689 H HH   . TYR   B  1 577 ? 42.682 -7.507  -10.672 0.00 34.88  ? 603  TYR   B HH   1 
ATOM   20690 N N    . ASN   B  1 578 ? 51.225 -4.840  -12.034 1.00 26.00  ? 604  ASN   B N    1 
ATOM   20691 C CA   . ASN   B  1 578 ? 52.485 -4.134  -12.122 1.00 26.52  ? 604  ASN   B CA   1 
ATOM   20692 C C    . ASN   B  1 578 ? 53.487 -4.683  -13.111 1.00 27.54  ? 604  ASN   B C    1 
ATOM   20693 O O    . ASN   B  1 578 ? 53.577 -5.897  -13.294 1.00 28.87  ? 604  ASN   B O    1 
ATOM   20694 C CB   . ASN   B  1 578 ? 53.126 -4.139  -10.728 1.00 27.47  ? 604  ASN   B CB   1 
ATOM   20695 C CG   . ASN   B  1 578 ? 52.271 -3.481  -9.668  1.00 30.48  ? 604  ASN   B CG   1 
ATOM   20696 O OD1  . ASN   B  1 578 ? 51.659 -2.427  -9.907  1.00 31.26  ? 604  ASN   B OD1  1 
ATOM   20697 N ND2  . ASN   B  1 578 ? 52.222 -4.062  -8.468  1.00 30.27  ? 604  ASN   B ND2  1 
ATOM   20698 H H    . ASN   B  1 578 ? 51.336 -5.757  -11.613 0.00 32.80  ? 604  ASN   B H    1 
ATOM   20699 H HA   . ASN   B  1 578 ? 52.296 -3.104  -12.409 0.00 32.98  ? 604  ASN   B HA   1 
ATOM   20700 H HB2  . ASN   B  1 578 ? 53.309 -5.172  -10.437 0.00 35.20  ? 604  ASN   B HB2  1 
ATOM   20701 H HB3  . ASN   B  1 578 ? 54.070 -3.598  -10.775 0.00 35.03  ? 604  ASN   B HB3  1 
ATOM   20702 H HD21 . ASN   B  1 578 ? 51.660 -3.647  -7.732  0.00 39.40  ? 604  ASN   B HD21 1 
ATOM   20703 H HD22 . ASN   B  1 578 ? 52.748 -4.910  -8.279  0.00 39.37  ? 604  ASN   B HD22 1 
ATOM   20704 N N    . LEU   B  1 579 ? 54.278 -3.775  -13.716 1.00 26.41  ? 605  LEU   B N    1 
ATOM   20705 C CA   . LEU   B  1 579 ? 55.376 -4.130  -14.600 1.00 26.52  ? 605  LEU   B CA   1 
ATOM   20706 C C    . LEU   B  1 579 ? 56.631 -4.114  -13.746 1.00 26.78  ? 605  LEU   B C    1 
ATOM   20707 O O    . LEU   B  1 579 ? 56.844 -3.170  -12.982 1.00 27.60  ? 605  LEU   B O    1 
ATOM   20708 C CB   . LEU   B  1 579 ? 55.518 -3.136  -15.759 1.00 26.59  ? 605  LEU   B CB   1 
ATOM   20709 C CG   . LEU   B  1 579 ? 54.271 -2.880  -16.620 1.00 27.95  ? 605  LEU   B CG   1 
ATOM   20710 C CD1  . LEU   B  1 579 ? 54.635 -2.050  -17.835 1.00 28.30  ? 605  LEU   B CD1  1 
ATOM   20711 C CD2  . LEU   B  1 579 ? 53.584 -4.186  -17.045 1.00 28.17  ? 605  LEU   B CD2  1 
ATOM   20712 H H    . LEU   B  1 579 ? 54.167 -2.770  -13.624 0.00 32.58  ? 605  LEU   B H    1 
ATOM   20713 H HA   . LEU   B  1 579 ? 55.236 -5.128  -15.012 0.00 32.53  ? 605  LEU   B HA   1 
ATOM   20714 H HB2  . LEU   B  1 579 ? 55.828 -2.176  -15.348 0.00 32.34  ? 605  LEU   B HB2  1 
ATOM   20715 H HB3  . LEU   B  1 579 ? 56.295 -3.505  -16.427 0.00 32.11  ? 605  LEU   B HB3  1 
ATOM   20716 H HG   . LEU   B  1 579 ? 53.555 -2.307  -16.032 0.00 33.45  ? 605  LEU   B HG   1 
ATOM   20717 H HD11 . LEU   B  1 579 ? 53.732 -1.839  -18.407 0.00 33.07  ? 605  LEU   B HD11 1 
ATOM   20718 H HD12 . LEU   B  1 579 ? 55.092 -1.118  -17.505 0.00 33.48  ? 605  LEU   B HD12 1 
ATOM   20719 H HD13 . LEU   B  1 579 ? 55.339 -2.611  -18.447 0.00 33.28  ? 605  LEU   B HD13 1 
ATOM   20720 H HD21 . LEU   B  1 579 ? 52.856 -3.968  -17.826 0.00 33.16  ? 605  LEU   B HD21 1 
ATOM   20721 H HD22 . LEU   B  1 579 ? 54.339 -4.874  -17.419 0.00 33.52  ? 605  LEU   B HD22 1 
ATOM   20722 H HD23 . LEU   B  1 579 ? 53.077 -4.622  -16.186 0.00 33.79  ? 605  LEU   B HD23 1 
ATOM   20723 N N    . GLU   B  1 580 ? 57.433 -5.171  -13.828 1.00 26.29  ? 606  GLU   B N    1 
ATOM   20724 C CA   . GLU   B  1 580 ? 58.632 -5.292  -13.010 1.00 26.46  ? 606  GLU   B CA   1 
ATOM   20725 C C    . GLU   B  1 580 ? 59.809 -5.767  -13.836 1.00 26.20  ? 606  GLU   B C    1 
ATOM   20726 O O    . GLU   B  1 580 ? 59.662 -6.643  -14.665 1.00 26.08  ? 606  GLU   B O    1 
ATOM   20727 C CB   . GLU   B  1 580 ? 58.375 -6.268  -11.845 1.00 28.89  ? 606  GLU   B CB   1 
ATOM   20728 C CG   . GLU   B  1 580 ? 57.144 -5.887  -11.042 1.00 33.23  ? 606  GLU   B CG   1 
ATOM   20729 C CD   . GLU   B  1 580 ? 56.946 -6.631  -9.745  1.00 42.75  ? 606  GLU   B CD   1 
ATOM   20730 O OE1  . GLU   B  1 580 ? 57.344 -7.817  -9.673  1.00 45.22  ? 606  GLU   B OE1  1 
ATOM   20731 O OE2  . GLU   B  1 580 ? 56.355 -6.041  -8.811  1.00 46.23  ? 606  GLU   B OE2  1 
ATOM   20732 H H    . GLU   B  1 580 ? 57.287 -5.959  -14.451 0.00 32.87  ? 606  GLU   B H    1 
ATOM   20733 H HA   . GLU   B  1 580 ? 58.892 -4.327  -12.576 0.00 33.93  ? 606  GLU   B HA   1 
ATOM   20734 H HB2  . GLU   B  1 580 ? 58.222 -7.270  -12.245 0.00 37.20  ? 606  GLU   B HB2  1 
ATOM   20735 H HB3  . GLU   B  1 580 ? 59.232 -6.261  -11.174 0.00 37.70  ? 606  GLU   B HB3  1 
ATOM   20736 H HG2  . GLU   B  1 580 ? 57.186 -4.825  -10.810 0.00 42.50  ? 606  GLU   B HG2  1 
ATOM   20737 H HG3  . GLU   B  1 580 ? 56.263 -6.083  -11.651 0.00 42.13  ? 606  GLU   B HG3  1 
ATOM   20738 N N    . SER   B  1 581 ? 60.974 -5.181  -13.603 1.00 26.13  ? 607  SER   B N    1 
ATOM   20739 C CA   . SER   B  1 581 ? 62.220 -5.565  -14.258 1.00 26.09  ? 607  SER   B CA   1 
ATOM   20740 C C    . SER   B  1 581 ? 63.379 -4.943  -13.526 1.00 27.02  ? 607  SER   B C    1 
ATOM   20741 O O    . SER   B  1 581 ? 63.394 -3.722  -13.344 1.00 27.63  ? 607  SER   B O    1 
ATOM   20742 C CB   . SER   B  1 581 ? 62.267 -5.102  -15.715 1.00 26.24  ? 607  SER   B CB   1 
ATOM   20743 O OG   . SER   B  1 581 ? 63.571 -5.307  -16.258 1.00 27.42  ? 607  SER   B OG   1 
ATOM   20744 H H    . SER   B  1 581 ? 61.071 -4.407  -12.952 0.00 33.85  ? 607  SER   B H    1 
ATOM   20745 H HA   . SER   B  1 581 ? 62.320 -6.649  -14.237 0.00 33.82  ? 607  SER   B HA   1 
ATOM   20746 H HB2  . SER   B  1 581 ? 61.545 -5.675  -16.294 0.00 32.91  ? 607  SER   B HB2  1 
ATOM   20747 H HB3  . SER   B  1 581 ? 62.026 -4.041  -15.759 0.00 33.05  ? 607  SER   B HB3  1 
ATOM   20748 H HG   . SER   B  1 581 ? 63.901 -6.216  -16.032 0.00 34.99  ? 607  SER   B HG   1 
ATOM   20749 N N    . LYS   B  1 582 ? 64.377 -5.758  -13.166 1.00 26.48  ? 608  LYS   B N    1 
ATOM   20750 C CA   . LYS   B  1 582 ? 65.583 -5.246  -12.536 1.00 26.58  ? 608  LYS   B CA   1 
ATOM   20751 C C    . LYS   B  1 582 ? 66.540 -4.612  -13.570 1.00 26.29  ? 608  LYS   B C    1 
ATOM   20752 O O    . LYS   B  1 582 ? 67.363 -3.808  -13.169 1.00 26.56  ? 608  LYS   B O    1 
ATOM   20753 C CB   . LYS   B  1 582 ? 66.287 -6.369  -11.757 1.00 28.79  ? 608  LYS   B CB   1 
ATOM   20754 C CG   . LYS   B  1 582 ? 65.461 -6.870  -10.576 1.00 34.72  ? 608  LYS   B CG   1 
ATOM   20755 C CD   . LYS   B  1 582 ? 66.190 -7.947  -9.796  1.00 41.90  ? 608  LYS   B CD   1 
ATOM   20756 C CE   . LYS   B  1 582 ? 65.518 -8.268  -8.483  1.00 47.91  ? 608  LYS   B CE   1 
ATOM   20757 N NZ   . LYS   B  1 582 ? 66.284 -9.295  -7.721  1.00 52.95  ? 608  LYS   B NZ   1 
ATOM   20758 H H    . LYS   B  1 582 ? 64.365 -6.766  -13.288 0.00 35.21  ? 608  LYS   B H    1 
ATOM   20759 H HA   . LYS   B  1 582 ? 65.316 -4.472  -11.817 0.00 35.96  ? 608  LYS   B HA   1 
ATOM   20760 H HB2  . LYS   B  1 582 ? 66.475 -7.210  -12.424 0.00 39.02  ? 608  LYS   B HB2  1 
ATOM   20761 H HB3  . LYS   B  1 582 ? 67.230 -5.988  -11.368 0.00 39.56  ? 608  LYS   B HB3  1 
ATOM   20762 H HG2  . LYS   B  1 582 ? 65.259 -6.038  -9.903  0.00 46.76  ? 608  LYS   B HG2  1 
ATOM   20763 H HG3  . LYS   B  1 582 ? 64.527 -7.294  -10.941 0.00 46.23  ? 608  LYS   B HG3  1 
ATOM   20764 H HD2  . LYS   B  1 582 ? 66.222 -8.858  -10.392 0.00 55.83  ? 608  LYS   B HD2  1 
ATOM   20765 H HD3  . LYS   B  1 582 ? 67.201 -7.605  -9.582  0.00 56.33  ? 608  LYS   B HD3  1 
ATOM   20766 H HE2  . LYS   B  1 582 ? 65.460 -7.365  -7.876  0.00 63.78  ? 608  LYS   B HE2  1 
ATOM   20767 H HE3  . LYS   B  1 582 ? 64.520 -8.657  -8.674  0.00 63.29  ? 608  LYS   B HE3  1 
ATOM   20768 H HZ1  . LYS   B  1 582 ? 65.812 -9.502  -6.847  0.00 70.77  ? 608  LYS   B HZ1  1 
ATOM   20769 H HZ2  . LYS   B  1 582 ? 66.355 -10.149 -8.266  0.00 70.36  ? 608  LYS   B HZ2  1 
ATOM   20770 H HZ3  . LYS   B  1 582 ? 67.218 -8.954  -7.518  0.00 70.80  ? 608  LYS   B HZ3  1 
ATOM   20771 N N    . SER   B  1 583 ? 66.426 -4.932  -14.889 1.00 25.40  ? 609  SER   B N    1 
ATOM   20772 C CA   . SER   B  1 583 ? 67.332 -4.406  -15.931 1.00 24.77  ? 609  SER   B CA   1 
ATOM   20773 C C    . SER   B  1 583 ? 66.799 -3.286  -16.814 1.00 23.60  ? 609  SER   B C    1 
ATOM   20774 O O    . SER   B  1 583 ? 67.609 -2.508  -17.326 1.00 23.45  ? 609  SER   B O    1 
ATOM   20775 C CB   . SER   B  1 583 ? 67.763 -5.531  -16.871 1.00 26.32  ? 609  SER   B CB   1 
ATOM   20776 O OG   . SER   B  1 583 ? 66.649 -6.260  -17.362 1.00 28.60  ? 609  SER   B OG   1 
ATOM   20777 H H    . SER   B  1 583 ? 65.725 -5.560  -15.270 0.00 33.34  ? 609  SER   B H    1 
ATOM   20778 H HA   . SER   B  1 583 ? 68.243 -4.035  -15.464 0.00 33.08  ? 609  SER   B HA   1 
ATOM   20779 H HB2  . SER   B  1 583 ? 68.302 -5.099  -17.713 0.00 34.21  ? 609  SER   B HB2  1 
ATOM   20780 H HB3  . SER   B  1 583 ? 68.415 -6.212  -16.326 0.00 34.91  ? 609  SER   B HB3  1 
ATOM   20781 H HG   . SER   B  1 583 ? 66.288 -5.831  -18.181 0.00 36.26  ? 609  SER   B HG   1 
ATOM   20782 N N    . LEU   B  1 584 ? 65.484 -3.275  -17.117 1.00 23.00  ? 610  LEU   B N    1 
ATOM   20783 C CA   . LEU   B  1 584 ? 64.907 -2.343  -18.083 1.00 23.73  ? 610  LEU   B CA   1 
ATOM   20784 C C    . LEU   B  1 584 ? 65.327 -0.879  -17.901 1.00 24.65  ? 610  LEU   B C    1 
ATOM   20785 O O    . LEU   B  1 584 ? 65.207 -0.355  -16.796 1.00 25.30  ? 610  LEU   B O    1 
ATOM   20786 C CB   . LEU   B  1 584 ? 63.363 -2.455  -18.097 1.00 23.78  ? 610  LEU   B CB   1 
ATOM   20787 C CG   . LEU   B  1 584 ? 62.670 -1.879  -19.342 1.00 24.83  ? 610  LEU   B CG   1 
ATOM   20788 C CD1  . LEU   B  1 584 ? 62.854 -2.799  -20.556 1.00 24.85  ? 610  LEU   B CD1  1 
ATOM   20789 C CD2  . LEU   B  1 584 ? 61.175 -1.672  -19.098 1.00 26.10  ? 610  LEU   B CD2  1 
ATOM   20790 H H    . LEU   B  1 584 ? 64.805 -3.903  -16.698 0.00 29.46  ? 610  LEU   B H    1 
ATOM   20791 H HA   . LEU   B  1 584 ? 65.276 -2.661  -19.056 0.00 29.49  ? 610  LEU   B HA   1 
ATOM   20792 H HB2  . LEU   B  1 584 ? 63.078 -3.504  -18.031 0.00 29.45  ? 610  LEU   B HB2  1 
ATOM   20793 H HB3  . LEU   B  1 584 ? 62.980 -1.920  -17.229 0.00 29.60  ? 610  LEU   B HB3  1 
ATOM   20794 H HG   . LEU   B  1 584 ? 63.099 -0.909  -19.589 0.00 29.98  ? 610  LEU   B HG   1 
ATOM   20795 H HD11 . LEU   B  1 584 ? 62.207 -2.447  -21.358 0.00 29.34  ? 610  LEU   B HD11 1 
ATOM   20796 H HD12 . LEU   B  1 584 ? 63.890 -2.762  -20.888 0.00 29.89  ? 610  LEU   B HD12 1 
ATOM   20797 H HD13 . LEU   B  1 584 ? 62.585 -3.819  -20.286 0.00 29.88  ? 610  LEU   B HD13 1 
ATOM   20798 H HD21 . LEU   B  1 584 ? 60.741 -1.178  -19.967 0.00 30.91  ? 610  LEU   B HD21 1 
ATOM   20799 H HD22 . LEU   B  1 584 ? 60.703 -2.643  -18.954 0.00 31.33  ? 610  LEU   B HD22 1 
ATOM   20800 H HD23 . LEU   B  1 584 ? 61.033 -1.055  -18.213 0.00 31.55  ? 610  LEU   B HD23 1 
ATOM   20801 N N    . VAL   B  1 585 ? 65.824 -0.229  -18.976 1.00 24.53  ? 611  VAL   B N    1 
ATOM   20802 C CA   . VAL   B  1 585 ? 66.228 1.181   -18.925 1.00 25.14  ? 611  VAL   B CA   1 
ATOM   20803 C C    . VAL   B  1 585 ? 65.199 2.079   -19.642 1.00 24.79  ? 611  VAL   B C    1 
ATOM   20804 O O    . VAL   B  1 585 ? 65.035 3.232   -19.253 1.00 25.40  ? 611  VAL   B O    1 
ATOM   20805 C CB   . VAL   B  1 585 ? 67.668 1.435   -19.451 1.00 26.89  ? 611  VAL   B CB   1 
ATOM   20806 C CG1  . VAL   B  1 585 ? 68.658 0.445   -18.844 1.00 27.77  ? 611  VAL   B CG1  1 
ATOM   20807 C CG2  . VAL   B  1 585 ? 67.731 1.404   -20.961 1.00 27.90  ? 611  VAL   B CG2  1 
ATOM   20808 H H    . VAL   B  1 585 ? 65.954 -0.651  -19.890 0.00 30.21  ? 611  VAL   B H    1 
ATOM   20809 H HA   . VAL   B  1 585 ? 66.262 1.495   -17.884 0.00 31.69  ? 611  VAL   B HA   1 
ATOM   20810 H HB   . VAL   B  1 585 ? 67.990 2.431   -19.149 0.00 33.79  ? 611  VAL   B HB   1 
ATOM   20811 H HG11 . VAL   B  1 585 ? 69.670 0.770   -19.078 0.00 35.50  ? 611  VAL   B HG11 1 
ATOM   20812 H HG12 . VAL   B  1 585 ? 68.515 0.417   -17.765 0.00 35.52  ? 611  VAL   B HG12 1 
ATOM   20813 H HG13 . VAL   B  1 585 ? 68.478 -0.542  -19.271 0.00 35.03  ? 611  VAL   B HG13 1 
ATOM   20814 H HG21 . VAL   B  1 585 ? 68.758 1.201   -21.260 0.00 34.50  ? 611  VAL   B HG21 1 
ATOM   20815 H HG22 . VAL   B  1 585 ? 67.071 0.622   -21.335 0.00 34.02  ? 611  VAL   B HG22 1 
ATOM   20816 H HG23 . VAL   B  1 585 ? 67.430 2.373   -21.355 0.00 34.05  ? 611  VAL   B HG23 1 
ATOM   20817 N N    . GLU   B  1 586 ? 64.521 1.566   -20.688 1.00 23.35  ? 612  GLU   B N    1 
ATOM   20818 C CA   . GLU   B  1 586 ? 63.546 2.360   -21.442 1.00 22.08  ? 612  GLU   B CA   1 
ATOM   20819 C C    . GLU   B  1 586 ? 62.222 1.635   -21.614 1.00 21.20  ? 612  GLU   B C    1 
ATOM   20820 O O    . GLU   B  1 586 ? 62.199 0.492   -22.077 1.00 21.04  ? 612  GLU   B O    1 
ATOM   20821 C CB   . GLU   B  1 586 ? 64.123 2.720   -22.820 1.00 22.50  ? 612  GLU   B CB   1 
ATOM   20822 C CG   . GLU   B  1 586 ? 63.192 3.520   -23.725 1.00 23.72  ? 612  GLU   B CG   1 
ATOM   20823 C CD   . GLU   B  1 586 ? 63.787 3.858   -25.081 1.00 29.37  ? 612  GLU   B CD   1 
ATOM   20824 O OE1  . GLU   B  1 586 ? 64.886 3.348   -25.415 1.00 31.17  ? 612  GLU   B OE1  1 
ATOM   20825 O OE2  . GLU   B  1 586 ? 63.138 4.626   -25.825 1.00 29.22  ? 612  GLU   B OE2  1 
ATOM   20826 H H    . GLU   B  1 586 ? 64.625 0.621   -21.044 0.00 28.02  ? 612  GLU   B H    1 
ATOM   20827 H HA   . GLU   B  1 586 ? 63.346 3.299   -20.928 0.00 26.22  ? 612  GLU   B HA   1 
ATOM   20828 H HB2  . GLU   B  1 586 ? 65.032 3.303   -22.680 0.00 26.54  ? 612  GLU   B HB2  1 
ATOM   20829 H HB3  . GLU   B  1 586 ? 64.359 1.789   -23.335 0.00 26.18  ? 612  GLU   B HB3  1 
ATOM   20830 H HG2  . GLU   B  1 586 ? 62.288 2.948   -23.926 0.00 27.04  ? 612  GLU   B HG2  1 
ATOM   20831 H HG3  . GLU   B  1 586 ? 62.934 4.456   -23.233 0.00 27.41  ? 612  GLU   B HG3  1 
ATOM   20832 N N    . LEU   B  1 587 ? 61.115 2.318   -21.258 1.00 20.34  ? 613  LEU   B N    1 
ATOM   20833 C CA   . LEU   B  1 587 ? 59.771 1.806   -21.478 1.00 20.60  ? 613  LEU   B CA   1 
ATOM   20834 C C    . LEU   B  1 587 ? 59.012 2.812   -22.329 1.00 20.41  ? 613  LEU   B C    1 
ATOM   20835 O O    . LEU   B  1 587 ? 58.848 3.973   -21.915 1.00 21.19  ? 613  LEU   B O    1 
ATOM   20836 C CB   . LEU   B  1 587 ? 58.988 1.559   -20.171 1.00 20.53  ? 613  LEU   B CB   1 
ATOM   20837 C CG   . LEU   B  1 587 ? 57.505 1.109   -20.380 1.00 21.98  ? 613  LEU   B CG   1 
ATOM   20838 C CD1  . LEU   B  1 587 ? 57.432 -0.229  -21.120 1.00 21.75  ? 613  LEU   B CD1  1 
ATOM   20839 C CD2  . LEU   B  1 587 ? 56.758 1.020   -19.071 1.00 22.16  ? 613  LEU   B CD2  1 
ATOM   20840 H H    . LEU   B  1 587 ? 61.120 3.233   -20.820 0.00 23.71  ? 613  LEU   B H    1 
ATOM   20841 H HA   . LEU   B  1 587 ? 59.820 0.865   -22.022 0.00 23.42  ? 613  LEU   B HA   1 
ATOM   20842 H HB2  . LEU   B  1 587 ? 59.492 0.778   -19.605 0.00 24.05  ? 613  LEU   B HB2  1 
ATOM   20843 H HB3  . LEU   B  1 587 ? 58.973 2.483   -19.595 0.00 23.96  ? 613  LEU   B HB3  1 
ATOM   20844 H HG   . LEU   B  1 587 ? 56.971 1.845   -20.980 0.00 24.96  ? 613  LEU   B HG   1 
ATOM   20845 H HD11 . LEU   B  1 587 ? 56.416 -0.616  -21.053 0.00 24.64  ? 613  LEU   B HD11 1 
ATOM   20846 H HD12 . LEU   B  1 587 ? 57.693 -0.071  -22.165 0.00 24.46  ? 613  LEU   B HD12 1 
ATOM   20847 H HD13 . LEU   B  1 587 ? 58.131 -0.926  -20.661 0.00 25.01  ? 613  LEU   B HD13 1 
ATOM   20848 H HD21 . LEU   B  1 587 ? 55.711 0.800   -19.273 0.00 25.57  ? 613  LEU   B HD21 1 
ATOM   20849 H HD22 . LEU   B  1 587 ? 57.195 0.221   -18.475 0.00 26.04  ? 613  LEU   B HD22 1 
ATOM   20850 H HD23 . LEU   B  1 587 ? 56.849 1.971   -18.548 0.00 25.95  ? 613  LEU   B HD23 1 
ATOM   20851 N N    . VAL   B  1 588 ? 58.486 2.364   -23.467 1.00 19.31  ? 614  VAL   B N    1 
ATOM   20852 C CA   . VAL   B  1 588 ? 57.622 3.192   -24.279 1.00 19.25  ? 614  VAL   B CA   1 
ATOM   20853 C C    . VAL   B  1 588 ? 56.202 2.695   -24.029 1.00 19.28  ? 614  VAL   B C    1 
ATOM   20854 O O    . VAL   B  1 588 ? 55.865 1.577   -24.405 1.00 20.01  ? 614  VAL   B O    1 
ATOM   20855 C CB   . VAL   B  1 588 ? 57.993 3.205   -25.776 1.00 19.61  ? 614  VAL   B CB   1 
ATOM   20856 C CG1  . VAL   B  1 588 ? 57.091 4.158   -26.553 1.00 19.40  ? 614  VAL   B CG1  1 
ATOM   20857 C CG2  . VAL   B  1 588 ? 59.471 3.578   -25.958 1.00 19.96  ? 614  VAL   B CG2  1 
ATOM   20858 H H    . VAL   B  1 588 ? 58.645 1.441   -23.858 0.00 21.16  ? 614  VAL   B H    1 
ATOM   20859 H HA   . VAL   B  1 588 ? 57.683 4.220   -23.934 0.00 20.95  ? 614  VAL   B HA   1 
ATOM   20860 H HB   . VAL   B  1 588 ? 57.843 2.218   -26.206 0.00 20.80  ? 614  VAL   B HB   1 
ATOM   20861 H HG11 . VAL   B  1 588 ? 57.387 4.140   -27.601 0.00 20.19  ? 614  VAL   B HG11 1 
ATOM   20862 H HG12 . VAL   B  1 588 ? 56.051 3.852   -26.463 0.00 20.30  ? 614  VAL   B HG12 1 
ATOM   20863 H HG13 . VAL   B  1 588 ? 57.217 5.164   -26.157 0.00 20.54  ? 614  VAL   B HG13 1 
ATOM   20864 H HG21 . VAL   B  1 588 ? 59.671 3.724   -27.019 0.00 21.27  ? 614  VAL   B HG21 1 
ATOM   20865 H HG22 . VAL   B  1 588 ? 59.676 4.498   -25.413 0.00 21.69  ? 614  VAL   B HG22 1 
ATOM   20866 H HG23 . VAL   B  1 588 ? 60.096 2.771   -25.578 0.00 21.69  ? 614  VAL   B HG23 1 
ATOM   20867 N N    . PHE   B  1 589 ? 55.391 3.499   -23.351 1.00 18.90  ? 615  PHE   B N    1 
ATOM   20868 C CA   . PHE   B  1 589 ? 54.003 3.133   -23.025 1.00 18.87  ? 615  PHE   B CA   1 
ATOM   20869 C C    . PHE   B  1 589 ? 52.981 4.045   -23.748 1.00 18.97  ? 615  PHE   B C    1 
ATOM   20870 O O    . PHE   B  1 589 ? 51.817 4.123   -23.328 1.00 19.57  ? 615  PHE   B O    1 
ATOM   20871 C CB   . PHE   B  1 589 ? 53.796 3.230   -21.493 1.00 18.92  ? 615  PHE   B CB   1 
ATOM   20872 C CG   . PHE   B  1 589 ? 52.730 2.303   -20.931 1.00 20.19  ? 615  PHE   B CG   1 
ATOM   20873 C CD1  . PHE   B  1 589 ? 52.942 0.935   -20.867 1.00 21.05  ? 615  PHE   B CD1  1 
ATOM   20874 C CD2  . PHE   B  1 589 ? 51.521 2.802   -20.474 1.00 21.01  ? 615  PHE   B CD2  1 
ATOM   20875 C CE1  . PHE   B  1 589 ? 51.956 0.087   -20.374 1.00 22.13  ? 615  PHE   B CE1  1 
ATOM   20876 C CE2  . PHE   B  1 589 ? 50.544 1.950   -19.965 1.00 22.05  ? 615  PHE   B CE2  1 
ATOM   20877 C CZ   . PHE   B  1 589 ? 50.758 0.600   -19.939 1.00 21.71  ? 615  PHE   B CZ   1 
ATOM   20878 H H    . PHE   B  1 589 ? 55.650 4.418   -23.008 0.00 20.56  ? 615  PHE   B H    1 
ATOM   20879 H HA   . PHE   B  1 589 ? 53.803 2.112   -23.347 0.00 20.23  ? 615  PHE   B HA   1 
ATOM   20880 H HB2  . PHE   B  1 589 ? 54.736 2.978   -21.003 0.00 21.04  ? 615  PHE   B HB2  1 
ATOM   20881 H HB3  . PHE   B  1 589 ? 53.520 4.253   -21.243 0.00 20.90  ? 615  PHE   B HB3  1 
ATOM   20882 H HD1  . PHE   B  1 589 ? 53.870 0.522   -21.223 0.00 23.45  ? 615  PHE   B HD1  1 
ATOM   20883 H HD2  . PHE   B  1 589 ? 51.331 3.862   -20.512 0.00 23.46  ? 615  PHE   B HD2  1 
ATOM   20884 H HE1  . PHE   B  1 589 ? 52.132 -0.974  -20.330 0.00 24.91  ? 615  PHE   B HE1  1 
ATOM   20885 H HE2  . PHE   B  1 589 ? 49.607 2.351   -19.621 0.00 24.85  ? 615  PHE   B HE2  1 
ATOM   20886 H HZ   . PHE   B  1 589 ? 50.008 -0.057  -19.532 0.00 24.49  ? 615  PHE   B HZ   1 
ATOM   20887 N N    . SER   B  1 590 ? 53.398 4.744   -24.802 1.00 19.06  ? 616  SER   B N    1 
ATOM   20888 C CA   . SER   B  1 590 ? 52.500 5.658   -25.507 1.00 19.50  ? 616  SER   B CA   1 
ATOM   20889 C C    . SER   B  1 590 ? 51.330 4.927   -26.160 1.00 19.41  ? 616  SER   B C    1 
ATOM   20890 O O    . SER   B  1 590 ? 51.450 3.755   -26.495 1.00 19.39  ? 616  SER   B O    1 
ATOM   20891 C CB   . SER   B  1 590 ? 53.270 6.439   -26.565 1.00 21.53  ? 616  SER   B CB   1 
ATOM   20892 O OG   . SER   B  1 590 ? 53.889 5.552   -27.470 1.00 25.25  ? 616  SER   B OG   1 
ATOM   20893 H H    . SER   B  1 590 ? 54.326 4.699   -25.209 0.00 20.08  ? 616  SER   B H    1 
ATOM   20894 H HA   . SER   B  1 590 ? 52.095 6.373   -24.793 0.00 20.66  ? 616  SER   B HA   1 
ATOM   20895 H HB2  . SER   B  1 590 ? 52.580 7.083   -27.108 0.00 22.63  ? 616  SER   B HB2  1 
ATOM   20896 H HB3  . SER   B  1 590 ? 54.036 7.038   -26.075 0.00 22.94  ? 616  SER   B HB3  1 
ATOM   20897 H HG   . SER   B  1 590 ? 54.392 6.064   -28.157 0.00 26.90  ? 616  SER   B HG   1 
ATOM   20898 N N    . GLY   B  1 591 ? 50.209 5.619   -26.332 1.00 18.47  ? 617  GLY   B N    1 
ATOM   20899 C CA   . GLY   B  1 591 ? 49.050 5.056   -27.014 1.00 18.30  ? 617  GLY   B CA   1 
ATOM   20900 C C    . GLY   B  1 591 ? 48.350 3.965   -26.230 1.00 17.70  ? 617  GLY   B C    1 
ATOM   20901 O O    . GLY   B  1 591 ? 47.777 3.045   -26.822 1.00 18.15  ? 617  GLY   B O    1 
ATOM   20902 H H    . GLY   B  1 591 ? 50.067 6.564   -25.991 0.00 19.10  ? 617  GLY   B H    1 
ATOM   20903 H HA2  . GLY   B  1 591 ? 48.329 5.849   -27.207 0.00 18.60  ? 617  GLY   B HA2  1 
ATOM   20904 H HA3  . GLY   B  1 591 ? 49.361 4.644   -27.972 0.00 18.38  ? 617  GLY   B HA3  1 
ATOM   20905 N N    . ASN   B  1 592 ? 48.401 4.057   -24.902 1.00 17.05  ? 618  ASN   B N    1 
ATOM   20906 C CA   . ASN   B  1 592 ? 47.705 3.139   -24.020 1.00 17.22  ? 618  ASN   B CA   1 
ATOM   20907 C C    . ASN   B  1 592 ? 46.645 3.965   -23.253 1.00 18.69  ? 618  ASN   B C    1 
ATOM   20908 O O    . ASN   B  1 592 ? 46.328 5.086   -23.678 1.00 19.74  ? 618  ASN   B O    1 
ATOM   20909 C CB   . ASN   B  1 592 ? 48.735 2.391   -23.132 1.00 17.55  ? 618  ASN   B CB   1 
ATOM   20910 C CG   . ASN   B  1 592 ? 49.497 1.375   -23.955 1.00 19.70  ? 618  ASN   B CG   1 
ATOM   20911 O OD1  . ASN   B  1 592 ? 48.887 0.541   -24.625 1.00 20.53  ? 618  ASN   B OD1  1 
ATOM   20912 N ND2  . ASN   B  1 592 ? 50.825 1.434   -23.970 1.00 19.03  ? 618  ASN   B ND2  1 
ATOM   20913 H H    . ASN   B  1 592 ? 48.912 4.771   -24.394 0.00 17.64  ? 618  ASN   B H    1 
ATOM   20914 H HA   . ASN   B  1 592 ? 47.145 2.401   -24.592 0.00 17.75  ? 618  ASN   B HA   1 
ATOM   20915 H HB2  . ASN   B  1 592 ? 49.434 3.112   -22.710 0.00 18.61  ? 618  ASN   B HB2  1 
ATOM   20916 H HB3  . ASN   B  1 592 ? 48.225 1.853   -22.335 0.00 18.67  ? 618  ASN   B HB3  1 
ATOM   20917 H HD21 . ASN   B  1 592 ? 51.350 0.759   -24.517 0.00 19.99  ? 618  ASN   B HD21 1 
ATOM   20918 H HD22 . ASN   B  1 592 ? 51.320 2.144   -23.440 0.00 20.24  ? 618  ASN   B HD22 1 
ATOM   20919 N N    . ARG   B  1 593 ? 46.054 3.422   -22.189 1.00 18.75  ? 619  ARG   B N    1 
ATOM   20920 C CA   . ARG   B  1 593 ? 45.016 4.129   -21.459 1.00 19.49  ? 619  ARG   B CA   1 
ATOM   20921 C C    . ARG   B  1 593 ? 45.341 4.309   -19.991 1.00 19.85  ? 619  ARG   B C    1 
ATOM   20922 O O    . ARG   B  1 593 ? 44.569 3.887   -19.126 1.00 20.28  ? 619  ARG   B O    1 
ATOM   20923 C CB   . ARG   B  1 593 ? 43.665 3.424   -21.665 1.00 20.96  ? 619  ARG   B CB   1 
ATOM   20924 C CG   . ARG   B  1 593 ? 43.207 3.306   -23.135 1.00 22.35  ? 619  ARG   B CG   1 
ATOM   20925 C CD   . ARG   B  1 593 ? 42.896 4.651   -23.802 1.00 23.96  ? 619  ARG   B CD   1 
ATOM   20926 N NE   . ARG   B  1 593 ? 41.904 5.433   -23.053 1.00 24.59  ? 619  ARG   B NE   1 
ATOM   20927 C CZ   . ARG   B  1 593 ? 40.581 5.350   -23.194 1.00 23.84  ? 619  ARG   B CZ   1 
ATOM   20928 N NH1  . ARG   B  1 593 ? 40.047 4.510   -24.074 1.00 22.33  ? 619  ARG   B NH1  1 
ATOM   20929 N NH2  . ARG   B  1 593 ? 39.780 6.114   -22.457 1.00 21.67  ? 619  ARG   B NH2  1 
ATOM   20930 H H    . ARG   B  1 593 ? 46.253 2.500   -21.815 0.00 20.27  ? 619  ARG   B H    1 
ATOM   20931 H HA   . ARG   B  1 593 ? 44.911 5.143   -21.839 0.00 21.30  ? 619  ARG   B HA   1 
ATOM   20932 H HB2  . ARG   B  1 593 ? 43.809 2.424   -21.266 0.00 23.15  ? 619  ARG   B HB2  1 
ATOM   20933 H HB3  . ARG   B  1 593 ? 42.887 3.941   -21.106 0.00 23.30  ? 619  ARG   B HB3  1 
ATOM   20934 H HG2  . ARG   B  1 593 ? 43.983 2.815   -23.719 0.00 24.24  ? 619  ARG   B HG2  1 
ATOM   20935 H HG3  . ARG   B  1 593 ? 42.296 2.710   -23.166 0.00 24.48  ? 619  ARG   B HG3  1 
ATOM   20936 H HD2  . ARG   B  1 593 ? 43.810 5.243   -23.838 0.00 26.25  ? 619  ARG   B HD2  1 
ATOM   20937 H HD3  . ARG   B  1 593 ? 42.565 4.495   -24.827 0.00 26.09  ? 619  ARG   B HD3  1 
ATOM   20938 H HE   . ARG   B  1 593 ? 42.266 6.094   -22.374 0.00 27.52  ? 619  ARG   B HE   1 
ATOM   20939 H HH11 . ARG   B  1 593 ? 40.597 3.881   -24.648 0.00 24.34  ? 619  ARG   B HH11 1 
ATOM   20940 H HH12 . ARG   B  1 593 ? 39.037 4.458   -24.152 0.00 24.65  ? 619  ARG   B HH12 1 
ATOM   20941 H HH21 . ARG   B  1 593 ? 40.171 6.769   -21.788 0.00 24.42  ? 619  ARG   B HH21 1 
ATOM   20942 H HH22 . ARG   B  1 593 ? 38.772 6.053   -22.564 0.00 24.35  ? 619  ARG   B HH22 1 
ATOM   20943 N N    . LEU   B  1 594 ? 46.424 5.052   -19.699 1.00 19.42  ? 620  LEU   B N    1 
ATOM   20944 C CA   . LEU   B  1 594 ? 46.715 5.424   -18.315 1.00 19.59  ? 620  LEU   B CA   1 
ATOM   20945 C C    . LEU   B  1 594 ? 45.605 6.307   -17.715 1.00 19.74  ? 620  LEU   B C    1 
ATOM   20946 O O    . LEU   B  1 594 ? 45.489 6.368   -16.489 1.00 20.06  ? 620  LEU   B O    1 
ATOM   20947 C CB   . LEU   B  1 594 ? 48.087 6.083   -18.157 1.00 19.26  ? 620  LEU   B CB   1 
ATOM   20948 C CG   . LEU   B  1 594 ? 49.288 5.147   -18.266 1.00 20.26  ? 620  LEU   B CG   1 
ATOM   20949 C CD1  . LEU   B  1 594 ? 50.540 5.923   -18.560 1.00 20.31  ? 620  LEU   B CD1  1 
ATOM   20950 C CD2  . LEU   B  1 594 ? 49.467 4.329   -16.979 1.00 21.32  ? 620  LEU   B CD2  1 
ATOM   20951 H H    . LEU   B  1 594 ? 47.090 5.402   -20.380 0.00 21.57  ? 620  LEU   B H    1 
ATOM   20952 H HA   . LEU   B  1 594 ? 46.703 4.507   -17.736 0.00 22.51  ? 620  LEU   B HA   1 
ATOM   20953 H HB2  . LEU   B  1 594 ? 48.212 6.887   -18.878 0.00 21.95  ? 620  LEU   B HB2  1 
ATOM   20954 H HB3  . LEU   B  1 594 ? 48.122 6.513   -17.157 0.00 22.46  ? 620  LEU   B HB3  1 
ATOM   20955 H HG   . LEU   B  1 594 ? 49.139 4.450   -19.090 0.00 22.93  ? 620  LEU   B HG   1 
ATOM   20956 H HD11 . LEU   B  1 594 ? 51.364 5.213   -18.577 0.00 23.28  ? 620  LEU   B HD11 1 
ATOM   20957 H HD12 . LEU   B  1 594 ? 50.445 6.412   -19.528 0.00 23.02  ? 620  LEU   B HD12 1 
ATOM   20958 H HD13 . LEU   B  1 594 ? 50.696 6.664   -17.777 0.00 23.61  ? 620  LEU   B HD13 1 
ATOM   20959 H HD21 . LEU   B  1 594 ? 50.391 3.758   -17.051 0.00 24.86  ? 620  LEU   B HD21 1 
ATOM   20960 H HD22 . LEU   B  1 594 ? 49.520 5.002   -16.124 0.00 25.21  ? 620  LEU   B HD22 1 
ATOM   20961 H HD23 . LEU   B  1 594 ? 48.632 3.640   -16.859 0.00 24.85  ? 620  LEU   B HD23 1 
ATOM   20962 N N    . ASP   B  1 595 ? 44.749 6.947   -18.545 1.00 19.80  ? 621  ASP   B N    1 
ATOM   20963 C CA   . ASP   B  1 595 ? 43.585 7.680   -18.004 1.00 20.61  ? 621  ASP   B CA   1 
ATOM   20964 C C    . ASP   B  1 595 ? 42.645 6.694   -17.271 1.00 20.83  ? 621  ASP   B C    1 
ATOM   20965 O O    . ASP   B  1 595 ? 42.094 7.031   -16.223 1.00 20.69  ? 621  ASP   B O    1 
ATOM   20966 C CB   . ASP   B  1 595 ? 42.814 8.414   -19.118 1.00 21.50  ? 621  ASP   B CB   1 
ATOM   20967 C CG   . ASP   B  1 595 ? 42.175 7.513   -20.171 1.00 24.96  ? 621  ASP   B CG   1 
ATOM   20968 O OD1  . ASP   B  1 595 ? 42.870 6.593   -20.671 1.00 23.44  ? 621  ASP   B OD1  1 
ATOM   20969 O OD2  . ASP   B  1 595 ? 40.989 7.746   -20.514 1.00 26.48  ? 621  ASP   B OD2  1 
ATOM   20970 H H    . ASP   B  1 595 ? 44.845 7.005   -19.554 0.00 22.45  ? 621  ASP   B H    1 
ATOM   20971 H HA   . ASP   B  1 595 ? 43.919 8.419   -17.278 0.00 24.30  ? 621  ASP   B HA   1 
ATOM   20972 H HB2  . ASP   B  1 595 ? 42.015 8.993   -18.658 0.00 25.14  ? 621  ASP   B HB2  1 
ATOM   20973 H HB3  . ASP   B  1 595 ? 43.500 9.082   -19.635 0.00 24.77  ? 621  ASP   B HB3  1 
ATOM   20974 N N    . ILE   B  1 596 ? 42.514 5.456   -17.798 1.00 20.57  ? 622  ILE   B N    1 
ATOM   20975 C CA   . ILE   B  1 596 ? 41.702 4.418   -17.166 1.00 21.38  ? 622  ILE   B CA   1 
ATOM   20976 C C    . ILE   B  1 596 ? 42.494 3.730   -16.040 1.00 21.45  ? 622  ILE   B C    1 
ATOM   20977 O O    . ILE   B  1 596 ? 41.974 3.589   -14.932 1.00 20.82  ? 622  ILE   B O    1 
ATOM   20978 C CB   . ILE   B  1 596 ? 41.195 3.396   -18.223 1.00 22.72  ? 622  ILE   B CB   1 
ATOM   20979 C CG1  . ILE   B  1 596 ? 40.177 4.077   -19.177 1.00 23.69  ? 622  ILE   B CG1  1 
ATOM   20980 C CG2  . ILE   B  1 596 ? 40.589 2.152   -17.524 1.00 23.54  ? 622  ILE   B CG2  1 
ATOM   20981 C CD1  . ILE   B  1 596 ? 39.674 3.218   -20.351 1.00 24.70  ? 622  ILE   B CD1  1 
ATOM   20982 H H    . ILE   B  1 596 ? 42.939 5.158   -18.670 0.00 23.57  ? 622  ILE   B H    1 
ATOM   20983 H HA   . ILE   B  1 596 ? 40.820 4.873   -16.718 0.00 25.24  ? 622  ILE   B HA   1 
ATOM   20984 H HB   . ILE   B  1 596 ? 42.044 3.059   -18.817 0.00 26.04  ? 622  ILE   B HB   1 
ATOM   20985 H HG12 . ILE   B  1 596 ? 39.309 4.382   -18.595 0.00 27.57  ? 622  ILE   B HG12 1 
ATOM   20986 H HG13 . ILE   B  1 596 ? 40.645 4.959   -19.613 0.00 27.20  ? 622  ILE   B HG13 1 
ATOM   20987 H HG21 . ILE   B  1 596 ? 40.013 1.566   -18.238 0.00 27.31  ? 622  ILE   B HG21 1 
ATOM   20988 H HG22 . ILE   B  1 596 ? 41.392 1.526   -17.139 0.00 27.51  ? 622  ILE   B HG22 1 
ATOM   20989 H HG23 . ILE   B  1 596 ? 39.945 2.480   -16.710 0.00 27.77  ? 622  ILE   B HG23 1 
ATOM   20990 H HD11 . ILE   B  1 596 ? 39.278 3.874   -21.124 0.00 28.11  ? 622  ILE   B HD11 1 
ATOM   20991 H HD12 . ILE   B  1 596 ? 40.504 2.634   -20.746 0.00 28.03  ? 622  ILE   B HD12 1 
ATOM   20992 H HD13 . ILE   B  1 596 ? 38.883 2.557   -19.999 0.00 28.39  ? 622  ILE   B HD13 1 
ATOM   20993 N N    . LEU   B  1 597 ? 43.738 3.286   -16.314 1.00 21.11  ? 623  LEU   B N    1 
ATOM   20994 C CA   . LEU   B  1 597 ? 44.549 2.615   -15.281 1.00 21.41  ? 623  LEU   B CA   1 
ATOM   20995 C C    . LEU   B  1 597 ? 44.724 3.468   -14.023 1.00 21.94  ? 623  LEU   B C    1 
ATOM   20996 O O    . LEU   B  1 597 ? 44.667 2.941   -12.910 1.00 21.59  ? 623  LEU   B O    1 
ATOM   20997 C CB   . LEU   B  1 597 ? 45.933 2.211   -15.833 1.00 21.27  ? 623  LEU   B CB   1 
ATOM   20998 C CG   . LEU   B  1 597 ? 45.929 1.241   -17.025 1.00 21.93  ? 623  LEU   B CG   1 
ATOM   20999 C CD1  . LEU   B  1 597 ? 47.199 1.367   -17.897 1.00 22.37  ? 623  LEU   B CD1  1 
ATOM   21000 C CD2  . LEU   B  1 597 ? 45.784 -0.186  -16.541 1.00 22.38  ? 623  LEU   B CD2  1 
ATOM   21001 H H    . LEU   B  1 597 ? 44.197 3.391   -17.213 0.00 24.49  ? 623  LEU   B H    1 
ATOM   21002 H HA   . LEU   B  1 597 ? 44.036 1.701   -14.984 0.00 25.52  ? 623  LEU   B HA   1 
ATOM   21003 H HB2  . LEU   B  1 597 ? 46.501 3.104   -16.081 0.00 24.99  ? 623  LEU   B HB2  1 
ATOM   21004 H HB3  . LEU   B  1 597 ? 46.454 1.697   -15.027 0.00 25.30  ? 623  LEU   B HB3  1 
ATOM   21005 H HG   . LEU   B  1 597 ? 45.084 1.469   -17.672 0.00 25.24  ? 623  LEU   B HG   1 
ATOM   21006 H HD11 . LEU   B  1 597 ? 47.190 0.576   -18.646 0.00 25.47  ? 623  LEU   B HD11 1 
ATOM   21007 H HD12 . LEU   B  1 597 ? 47.200 2.338   -18.390 0.00 25.55  ? 623  LEU   B HD12 1 
ATOM   21008 H HD13 . LEU   B  1 597 ? 48.078 1.270   -17.262 0.00 25.91  ? 623  LEU   B HD13 1 
ATOM   21009 H HD21 . LEU   B  1 597 ? 45.696 -0.844  -17.404 0.00 25.88  ? 623  LEU   B HD21 1 
ATOM   21010 H HD22 . LEU   B  1 597 ? 46.665 -0.456  -15.961 0.00 26.33  ? 623  LEU   B HD22 1 
ATOM   21011 H HD23 . LEU   B  1 597 ? 44.892 -0.263  -15.921 0.00 26.35  ? 623  LEU   B HD23 1 
ATOM   21012 N N    . TRP   B  1 598 ? 44.922 4.786   -14.201 1.00 22.86  ? 624  TRP   B N    1 
ATOM   21013 C CA   . TRP   B  1 598 ? 45.092 5.717   -13.085 1.00 24.04  ? 624  TRP   B CA   1 
ATOM   21014 C C    . TRP   B  1 598 ? 43.826 6.511   -12.793 1.00 26.06  ? 624  TRP   B C    1 
ATOM   21015 O O    . TRP   B  1 598 ? 43.892 7.605   -12.236 1.00 27.10  ? 624  TRP   B O    1 
ATOM   21016 C CB   . TRP   B  1 598 ? 46.277 6.657   -13.349 1.00 23.55  ? 624  TRP   B CB   1 
ATOM   21017 C CG   . TRP   B  1 598 ? 47.622 5.996   -13.287 1.00 23.43  ? 624  TRP   B CG   1 
ATOM   21018 C CD1  . TRP   B  1 598 ? 47.980 4.916   -12.527 1.00 24.45  ? 624  TRP   B CD1  1 
ATOM   21019 C CD2  . TRP   B  1 598 ? 48.836 6.522   -13.831 1.00 23.39  ? 624  TRP   B CD2  1 
ATOM   21020 N NE1  . TRP   B  1 598 ? 49.326 4.669   -12.667 1.00 24.62  ? 624  TRP   B NE1  1 
ATOM   21021 C CE2  . TRP   B  1 598 ? 49.885 5.672   -13.418 1.00 24.39  ? 624  TRP   B CE2  1 
ATOM   21022 C CE3  . TRP   B  1 598 ? 49.141 7.639   -14.620 1.00 23.59  ? 624  TRP   B CE3  1 
ATOM   21023 C CZ2  . TRP   B  1 598 ? 51.198 5.851   -13.853 1.00 24.67  ? 624  TRP   B CZ2  1 
ATOM   21024 C CZ3  . TRP   B  1 598 ? 50.443 7.817   -15.043 1.00 24.53  ? 624  TRP   B CZ3  1 
ATOM   21025 C CH2  . TRP   B  1 598 ? 51.463 6.967   -14.609 1.00 24.99  ? 624  TRP   B CH2  1 
ATOM   21026 H H    . TRP   B  1 598 ? 44.975 5.238   -15.108 0.00 27.36  ? 624  TRP   B H    1 
ATOM   21027 H HA   . TRP   B  1 598 ? 45.315 5.166   -12.173 0.00 29.83  ? 624  TRP   B HA   1 
ATOM   21028 H HB2  . TRP   B  1 598 ? 46.169 7.098   -14.339 0.00 28.62  ? 624  TRP   B HB2  1 
ATOM   21029 H HB3  . TRP   B  1 598 ? 46.293 7.445   -12.599 0.00 29.31  ? 624  TRP   B HB3  1 
ATOM   21030 H HD1  . TRP   B  1 598 ? 47.295 4.285   -11.986 0.00 30.36  ? 624  TRP   B HD1  1 
ATOM   21031 H HE1  . TRP   B  1 598 ? 49.845 3.882   -12.226 0.00 30.55  ? 624  TRP   B HE1  1 
ATOM   21032 H HE3  . TRP   B  1 598 ? 48.365 8.315   -14.937 0.00 28.63  ? 624  TRP   B HE3  1 
ATOM   21033 H HZ2  . TRP   B  1 598 ? 51.986 5.187   -13.541 0.00 30.34  ? 624  TRP   B HZ2  1 
ATOM   21034 H HZ3  . TRP   B  1 598 ? 50.691 8.674   -15.648 0.00 29.64  ? 624  TRP   B HZ3  1 
ATOM   21035 H HH2  . TRP   B  1 598 ? 52.468 7.135   -14.959 0.00 30.40  ? 624  TRP   B HH2  1 
ATOM   21036 N N    . ASN   B  1 599 ? 42.649 5.926   -13.049 1.00 26.43  ? 625  ASN   B N    1 
ATOM   21037 C CA   . ASN   B  1 599 ? 41.371 6.561   -12.705 1.00 27.28  ? 625  ASN   B CA   1 
ATOM   21038 C C    . ASN   B  1 599 ? 41.340 6.818   -11.181 1.00 27.48  ? 625  ASN   B C    1 
ATOM   21039 O O    . ASN   B  1 599 ? 41.816 5.975   -10.416 1.00 27.20  ? 625  ASN   B O    1 
ATOM   21040 C CB   . ASN   B  1 599 ? 40.217 5.651   -13.105 1.00 29.22  ? 625  ASN   B CB   1 
ATOM   21041 C CG   . ASN   B  1 599 ? 38.878 6.170   -12.691 1.00 33.87  ? 625  ASN   B CG   1 
ATOM   21042 O OD1  . ASN   B  1 599 ? 38.397 5.881   -11.588 1.00 35.48  ? 625  ASN   B OD1  1 
ATOM   21043 N ND2  . ASN   B  1 599 ? 38.269 6.974   -13.546 1.00 34.07  ? 625  ASN   B ND2  1 
ATOM   21044 H H    . ASN   B  1 599 ? 42.546 5.015   -13.483 0.00 32.27  ? 625  ASN   B H    1 
ATOM   21045 H HA   . ASN   B  1 599 ? 41.276 7.508   -13.235 0.00 33.70  ? 625  ASN   B HA   1 
ATOM   21046 H HB2  . ASN   B  1 599 ? 40.222 5.524   -14.187 0.00 35.56  ? 625  ASN   B HB2  1 
ATOM   21047 H HB3  . ASN   B  1 599 ? 40.355 4.683   -12.624 0.00 36.02  ? 625  ASN   B HB3  1 
ATOM   21048 H HD21 . ASN   B  1 599 ? 37.359 7.352   -13.308 0.00 42.16  ? 625  ASN   B HD21 1 
ATOM   21049 H HD22 . ASN   B  1 599 ? 38.702 7.221   -14.430 0.00 41.62  ? 625  ASN   B HD22 1 
ATOM   21050 N N    . ASP   B  1 600 ? 40.874 8.004   -10.765 1.00 28.08  ? 626  ASP   B N    1 
ATOM   21051 C CA   . ASP   B  1 600 ? 40.854 8.411   -9.354  1.00 28.99  ? 626  ASP   B CA   1 
ATOM   21052 C C    . ASP   B  1 600 ? 40.205 7.399   -8.403  1.00 28.27  ? 626  ASP   B C    1 
ATOM   21053 O O    . ASP   B  1 600 ? 40.495 7.426   -7.213  1.00 28.27  ? 626  ASP   B O    1 
ATOM   21054 C CB   . ASP   B  1 600 ? 40.089 9.737   -9.195  1.00 32.62  ? 626  ASP   B CB   1 
ATOM   21055 C CG   . ASP   B  1 600 ? 40.779 10.956  -9.760  1.00 40.91  ? 626  ASP   B CG   1 
ATOM   21056 O OD1  . ASP   B  1 600 ? 42.021 10.922  -9.910  1.00 42.91  ? 626  ASP   B OD1  1 
ATOM   21057 O OD2  . ASP   B  1 600 ? 40.078 11.944  -10.065 1.00 44.39  ? 626  ASP   B OD2  1 
ATOM   21058 H H    . ASP   B  1 600 ? 40.491 8.702   -11.394 0.00 35.55  ? 626  ASP   B H    1 
ATOM   21059 H HA   . ASP   B  1 600 ? 41.879 8.554   -9.016  0.00 37.48  ? 626  ASP   B HA   1 
ATOM   21060 H HB2  . ASP   B  1 600 ? 39.123 9.644   -9.689  0.00 41.90  ? 626  ASP   B HB2  1 
ATOM   21061 H HB3  . ASP   B  1 600 ? 39.933 9.917   -8.133  0.00 42.53  ? 626  ASP   B HB3  1 
ATOM   21062 N N    . ASP   B  1 601 ? 39.271 6.579   -8.900  1.00 27.49  ? 627  ASP   B N    1 
ATOM   21063 C CA   . ASP   B  1 601 ? 38.546 5.619   -8.067  1.00 26.93  ? 627  ASP   B CA   1 
ATOM   21064 C C    . ASP   B  1 601 ? 39.171 4.213   -8.071  1.00 26.15  ? 627  ASP   B C    1 
ATOM   21065 O O    . ASP   B  1 601 ? 38.546 3.291   -7.560  1.00 25.66  ? 627  ASP   B O    1 
ATOM   21066 C CB   . ASP   B  1 601 ? 37.086 5.535   -8.543  1.00 27.90  ? 627  ASP   B CB   1 
ATOM   21067 C CG   . ASP   B  1 601 ? 36.402 6.888   -8.636  1.00 31.58  ? 627  ASP   B CG   1 
ATOM   21068 O OD1  . ASP   B  1 601 ? 36.388 7.607   -7.627  1.00 30.51  ? 627  ASP   B OD1  1 
ATOM   21069 O OD2  . ASP   B  1 601 ? 35.877 7.216   -9.726  1.00 35.56  ? 627  ASP   B OD2  1 
ATOM   21070 H H    . ASP   B  1 601 ? 38.994 6.547   -9.875  0.00 35.25  ? 627  ASP   B H    1 
ATOM   21071 H HA   . ASP   B  1 601 ? 38.520 5.966   -7.035  0.00 35.71  ? 627  ASP   B HA   1 
ATOM   21072 H HB2  . ASP   B  1 601 ? 37.058 5.074   -9.529  0.00 35.92  ? 627  ASP   B HB2  1 
ATOM   21073 H HB3  . ASP   B  1 601 ? 36.515 4.938   -7.834  0.00 36.63  ? 627  ASP   B HB3  1 
ATOM   21074 N N    . ASP   B  1 602 ? 40.382 4.039   -8.632  1.00 25.51  ? 628  ASP   B N    1 
ATOM   21075 C CA   . ASP   B  1 602 ? 41.043 2.738   -8.680  1.00 25.47  ? 628  ASP   B CA   1 
ATOM   21076 C C    . ASP   B  1 602 ? 42.474 2.857   -8.153  1.00 26.07  ? 628  ASP   B C    1 
ATOM   21077 O O    . ASP   B  1 602 ? 43.267 3.622   -8.697  1.00 26.74  ? 628  ASP   B O    1 
ATOM   21078 C CB   . ASP   B  1 602 ? 41.053 2.223   -10.135 1.00 25.82  ? 628  ASP   B CB   1 
ATOM   21079 C CG   . ASP   B  1 602 ? 41.500 0.786   -10.316 1.00 28.03  ? 628  ASP   B CG   1 
ATOM   21080 O OD1  . ASP   B  1 602 ? 41.819 0.127   -9.308  1.00 26.99  ? 628  ASP   B OD1  1 
ATOM   21081 O OD2  . ASP   B  1 602 ? 41.513 0.315   -11.466 1.00 31.92  ? 628  ASP   B OD2  1 
ATOM   21082 H H    . ASP   B  1 602 ? 40.937 4.772   -9.062  0.00 32.90  ? 628  ASP   B H    1 
ATOM   21083 H HA   . ASP   B  1 602 ? 40.513 2.015   -8.064  0.00 33.11  ? 628  ASP   B HA   1 
ATOM   21084 H HB2  . ASP   B  1 602 ? 40.041 2.295   -10.531 0.00 32.59  ? 628  ASP   B HB2  1 
ATOM   21085 H HB3  . ASP   B  1 602 ? 41.713 2.854   -10.728 0.00 32.44  ? 628  ASP   B HB3  1 
ATOM   21086 N N    . ASN   B  1 603 ? 42.812 2.084   -7.119  1.00 26.18  ? 629  ASN   B N    1 
ATOM   21087 C CA   . ASN   B  1 603 ? 44.174 2.074   -6.575  1.00 27.02  ? 629  ASN   B CA   1 
ATOM   21088 C C    . ASN   B  1 603 ? 45.029 0.916   -7.124  1.00 25.71  ? 629  ASN   B C    1 
ATOM   21089 O O    . ASN   B  1 603 ? 46.201 0.820   -6.746  1.00 25.37  ? 629  ASN   B O    1 
ATOM   21090 C CB   . ASN   B  1 603 ? 44.112 1.952   -5.040  1.00 29.85  ? 629  ASN   B CB   1 
ATOM   21091 C CG   . ASN   B  1 603 ? 43.530 3.170   -4.359  1.00 36.80  ? 629  ASN   B CG   1 
ATOM   21092 O OD1  . ASN   B  1 603 ? 43.581 4.285   -4.888  1.00 39.11  ? 629  ASN   B OD1  1 
ATOM   21093 N ND2  . ASN   B  1 603 ? 42.989 2.993   -3.148  1.00 38.73  ? 629  ASN   B ND2  1 
ATOM   21094 H H    . ASN   B  1 603 ? 42.176 1.454   -6.640  0.00 34.47  ? 629  ASN   B H    1 
ATOM   21095 H HA   . ASN   B  1 603 ? 44.693 3.001   -6.813  0.00 35.46  ? 629  ASN   B HA   1 
ATOM   21096 H HB2  . ASN   B  1 603 ? 43.504 1.088   -4.775  0.00 39.70  ? 629  ASN   B HB2  1 
ATOM   21097 H HB3  . ASN   B  1 603 ? 45.119 1.822   -4.647  0.00 39.81  ? 629  ASN   B HB3  1 
ATOM   21098 H HD21 . ASN   B  1 603 ? 42.588 3.784   -2.653  0.00 51.50  ? 629  ASN   B HD21 1 
ATOM   21099 H HD22 . ASN   B  1 603 ? 42.987 2.074   -2.718  0.00 51.36  ? 629  ASN   B HD22 1 
ATOM   21100 N N    . ARG   B  1 604 ? 44.475 0.029   -7.986  1.00 24.21  ? 630  ARG   B N    1 
ATOM   21101 C CA   . ARG   B  1 604 ? 45.210 -1.176  -8.390  1.00 23.76  ? 630  ARG   B CA   1 
ATOM   21102 C C    . ARG   B  1 604 ? 46.490 -0.949  -9.203  1.00 23.47  ? 630  ARG   B C    1 
ATOM   21103 O O    . ARG   B  1 604 ? 47.422 -1.738  -9.054  1.00 23.89  ? 630  ARG   B O    1 
ATOM   21104 C CB   . ARG   B  1 604 ? 44.296 -2.159  -9.138  1.00 24.62  ? 630  ARG   B CB   1 
ATOM   21105 C CG   . ARG   B  1 604 ? 43.166 -2.733  -8.250  1.00 26.14  ? 630  ARG   B CG   1 
ATOM   21106 C CD   . ARG   B  1 604 ? 42.139 -3.532  -9.045  1.00 27.60  ? 630  ARG   B CD   1 
ATOM   21107 N NE   . ARG   B  1 604 ? 41.545 -2.704  -10.090 1.00 27.93  ? 630  ARG   B NE   1 
ATOM   21108 C CZ   . ARG   B  1 604 ? 41.044 -3.145  -11.244 1.00 28.27  ? 630  ARG   B CZ   1 
ATOM   21109 N NH1  . ARG   B  1 604 ? 40.999 -4.449  -11.508 1.00 27.84  ? 630  ARG   B NH1  1 
ATOM   21110 N NH2  . ARG   B  1 604 ? 40.589 -2.284  -12.147 1.00 24.75  ? 630  ARG   B NH2  1 
ATOM   21111 H H    . ARG   B  1 604 ? 43.558 0.110   -8.412  0.00 31.32  ? 630  ARG   B H    1 
ATOM   21112 H HA   . ARG   B  1 604 ? 45.514 -1.675  -7.471  0.00 31.20  ? 630  ARG   B HA   1 
ATOM   21113 H HB2  . ARG   B  1 604 ? 43.855 -1.636  -9.985  0.00 31.19  ? 630  ARG   B HB2  1 
ATOM   21114 H HB3  . ARG   B  1 604 ? 44.897 -2.995  -9.492  0.00 31.43  ? 630  ARG   B HB3  1 
ATOM   21115 H HG2  . ARG   B  1 604 ? 43.603 -3.395  -7.504  0.00 34.08  ? 630  ARG   B HG2  1 
ATOM   21116 H HG3  . ARG   B  1 604 ? 42.642 -1.914  -7.759  0.00 33.93  ? 630  ARG   B HG3  1 
ATOM   21117 H HD2  . ARG   B  1 604 ? 42.672 -4.371  -9.489  0.00 35.09  ? 630  ARG   B HD2  1 
ATOM   21118 H HD3  . ARG   B  1 604 ? 41.347 -3.881  -8.384  0.00 35.53  ? 630  ARG   B HD3  1 
ATOM   21119 H HE   . ARG   B  1 604 ? 41.586 -1.699  -9.954  0.00 35.22  ? 630  ARG   B HE   1 
ATOM   21120 H HH11 . ARG   B  1 604 ? 41.323 -5.157  -10.858 0.00 34.97  ? 630  ARG   B HH11 1 
ATOM   21121 H HH12 . ARG   B  1 604 ? 40.590 -4.758  -12.385 0.00 34.44  ? 630  ARG   B HH12 1 
ATOM   21122 H HH21 . ARG   B  1 604 ? 40.615 -1.286  -11.964 0.00 30.69  ? 630  ARG   B HH21 1 
ATOM   21123 H HH22 . ARG   B  1 604 ? 40.183 -2.618  -13.016 0.00 30.40  ? 630  ARG   B HH22 1 
ATOM   21124 N N    . TYR   B  1 605 ? 46.550 0.097   -10.033 1.00 22.97  ? 631  TYR   B N    1 
ATOM   21125 C CA   . TYR   B  1 605 ? 47.711 0.367   -10.909 1.00 23.12  ? 631  TYR   B CA   1 
ATOM   21126 C C    . TYR   B  1 605 ? 48.556 1.552   -10.449 1.00 23.79  ? 631  TYR   B C    1 
ATOM   21127 O O    . TYR   B  1 605 ? 49.385 2.033   -11.217 1.00 23.18  ? 631  TYR   B O    1 
ATOM   21128 C CB   . TYR   B  1 605 ? 47.212 0.632   -12.341 1.00 22.08  ? 631  TYR   B CB   1 
ATOM   21129 C CG   . TYR   B  1 605 ? 46.402 -0.521  -12.887 1.00 22.30  ? 631  TYR   B CG   1 
ATOM   21130 C CD1  . TYR   B  1 605 ? 47.022 -1.602  -13.501 1.00 22.58  ? 631  TYR   B CD1  1 
ATOM   21131 C CD2  . TYR   B  1 605 ? 45.021 -0.562  -12.733 1.00 22.88  ? 631  TYR   B CD2  1 
ATOM   21132 C CE1  . TYR   B  1 605 ? 46.281 -2.667  -14.009 1.00 23.19  ? 631  TYR   B CE1  1 
ATOM   21133 C CE2  . TYR   B  1 605 ? 44.270 -1.624  -13.226 1.00 23.47  ? 631  TYR   B CE2  1 
ATOM   21134 C CZ   . TYR   B  1 605 ? 44.903 -2.679  -13.859 1.00 23.93  ? 631  TYR   B CZ   1 
ATOM   21135 O OH   . TYR   B  1 605 ? 44.175 -3.748  -14.334 1.00 24.59  ? 631  TYR   B OH   1 
ATOM   21136 H H    . TYR   B  1 605 ? 45.810 0.783   -10.133 0.00 29.14  ? 631  TYR   B H    1 
ATOM   21137 H HA   . TYR   B  1 605 ? 48.364 -0.502  -10.955 0.00 29.09  ? 631  TYR   B HA   1 
ATOM   21138 H HB2  . TYR   B  1 605 ? 46.581 1.520   -12.343 0.00 27.24  ? 631  TYR   B HB2  1 
ATOM   21139 H HB3  . TYR   B  1 605 ? 48.062 0.773   -13.007 0.00 27.02  ? 631  TYR   B HB3  1 
ATOM   21140 H HD1  . TYR   B  1 605 ? 48.092 -1.593  -13.628 0.00 27.43  ? 631  TYR   B HD1  1 
ATOM   21141 H HD2  . TYR   B  1 605 ? 44.520 0.258   -12.247 0.00 28.21  ? 631  TYR   B HD2  1 
ATOM   21142 H HE1  . TYR   B  1 605 ? 46.778 -3.490  -14.492 0.00 27.91  ? 631  TYR   B HE1  1 
ATOM   21143 H HE2  . TYR   B  1 605 ? 43.201 -1.623  -13.100 0.00 28.66  ? 631  TYR   B HE2  1 
ATOM   21144 H HH   . TYR   B  1 605 ? 43.205 -3.616  -14.175 0.00 29.73  ? 631  TYR   B HH   1 
ATOM   21145 N N    . ILE   B  1 606 ? 48.419 1.957   -9.182  1.00 25.22  ? 632  ILE   B N    1 
ATOM   21146 C CA   . ILE   B  1 606 ? 49.101 3.125   -8.637  1.00 26.94  ? 632  ILE   B CA   1 
ATOM   21147 C C    . ILE   B  1 606 ? 50.639 2.960   -8.604  1.00 26.60  ? 632  ILE   B C    1 
ATOM   21148 O O    . ILE   B  1 606 ? 51.338 3.968   -8.571  1.00 27.06  ? 632  ILE   B O    1 
ATOM   21149 C CB   . ILE   B  1 606 ? 48.498 3.502   -7.234  1.00 28.64  ? 632  ILE   B CB   1 
ATOM   21150 C CG1  . ILE   B  1 606 ? 48.614 5.012   -6.966  1.00 31.13  ? 632  ILE   B CG1  1 
ATOM   21151 C CG2  . ILE   B  1 606 ? 49.132 2.692   -6.100  1.00 29.07  ? 632  ILE   B CG2  1 
ATOM   21152 C CD1  . ILE   B  1 606 ? 47.491 5.874   -7.663  1.00 33.18  ? 632  ILE   B CD1  1 
ATOM   21153 H H    . ILE   B  1 606 ? 47.861 1.474   -8.485  0.00 32.61  ? 632  ILE   B H    1 
ATOM   21154 H HA   . ILE   B  1 606 ? 48.906 3.938   -9.335  0.00 34.48  ? 632  ILE   B HA   1 
ATOM   21155 H HB   . ILE   B  1 606 ? 47.433 3.270   -7.185  0.00 37.35  ? 632  ILE   B HB   1 
ATOM   21156 H HG12 . ILE   B  1 606 ? 48.542 5.181   -5.893  0.00 41.14  ? 632  ILE   B HG12 1 
ATOM   21157 H HG13 . ILE   B  1 606 ? 49.579 5.362   -7.328  0.00 40.56  ? 632  ILE   B HG13 1 
ATOM   21158 H HG21 . ILE   B  1 606 ? 48.485 2.756   -5.226  0.00 38.81  ? 632  ILE   B HG21 1 
ATOM   21159 H HG22 . ILE   B  1 606 ? 49.229 1.654   -6.414  0.00 38.26  ? 632  ILE   B HG22 1 
ATOM   21160 H HG23 . ILE   B  1 606 ? 50.108 3.109   -5.858  0.00 38.66  ? 632  ILE   B HG23 1 
ATOM   21161 H HD11 . ILE   B  1 606 ? 47.781 6.923   -7.637  0.00 42.93  ? 632  ILE   B HD11 1 
ATOM   21162 H HD12 . ILE   B  1 606 ? 47.359 5.540   -8.691  0.00 42.30  ? 632  ILE   B HD12 1 
ATOM   21163 H HD13 . ILE   B  1 606 ? 46.560 5.739   -7.115  0.00 42.99  ? 632  ILE   B HD13 1 
ATOM   21164 N N    . SER   B  1 607 ? 51.156 1.717   -8.626  1.00 25.45  ? 633  SER   B N    1 
ATOM   21165 C CA   . SER   B  1 607 ? 52.597 1.436   -8.663  1.00 25.16  ? 633  SER   B CA   1 
ATOM   21166 C C    . SER   B  1 607 ? 52.964 0.647   -9.939  1.00 24.42  ? 633  SER   B C    1 
ATOM   21167 O O    . SER   B  1 607 ? 53.948 -0.092  -9.927  1.00 24.92  ? 633  SER   B O    1 
ATOM   21168 C CB   . SER   B  1 607 ? 52.998 0.612   -7.443  1.00 27.08  ? 633  SER   B CB   1 
ATOM   21169 O OG   . SER   B  1 607 ? 52.638 1.263   -6.238  1.00 29.68  ? 633  SER   B OG   1 
ATOM   21170 H H    . SER   B  1 607 ? 50.600 0.867   -8.611  0.00 33.02  ? 633  SER   B H    1 
ATOM   21171 H HA   . SER   B  1 607 ? 53.181 2.355   -8.662  0.00 32.96  ? 633  SER   B HA   1 
ATOM   21172 H HB2  . SER   B  1 607 ? 52.496 -0.353  -7.487  0.00 35.68  ? 633  SER   B HB2  1 
ATOM   21173 H HB3  . SER   B  1 607 ? 54.077 0.471   -7.436  0.00 35.91  ? 633  SER   B HB3  1 
ATOM   21174 H HG   . SER   B  1 607 ? 52.568 2.243   -6.384  0.00 39.36  ? 633  SER   B HG   1 
ATOM   21175 N N    . ILE   B  1 608 ? 52.202 0.818   -11.037 1.00 22.52  ? 634  ILE   B N    1 
ATOM   21176 C CA   . ILE   B  1 608 ? 52.414 0.074   -12.282 1.00 21.84  ? 634  ILE   B CA   1 
ATOM   21177 C C    . ILE   B  1 608 ? 53.878 0.079   -12.787 1.00 21.86  ? 634  ILE   B C    1 
ATOM   21178 O O    . ILE   B  1 608 ? 54.332 -0.940  -13.304 1.00 22.69  ? 634  ILE   B O    1 
ATOM   21179 C CB   . ILE   B  1 608 ? 51.424 0.538   -13.392 1.00 22.47  ? 634  ILE   B CB   1 
ATOM   21180 C CG1  . ILE   B  1 608 ? 51.485 -0.406  -14.620 1.00 23.14  ? 634  ILE   B CG1  1 
ATOM   21181 C CG2  . ILE   B  1 608 ? 51.662 1.998   -13.812 1.00 23.04  ? 634  ILE   B CG2  1 
ATOM   21182 C CD1  . ILE   B  1 608 ? 50.324 -0.222  -15.611 1.00 24.34  ? 634  ILE   B CD1  1 
ATOM   21183 H H    . ILE   B  1 608 ? 51.429 1.472   -11.094 0.00 28.53  ? 634  ILE   B H    1 
ATOM   21184 H HA   . ILE   B  1 608 ? 52.154 -0.954  -12.049 0.00 27.40  ? 634  ILE   B HA   1 
ATOM   21185 H HB   . ILE   B  1 608 ? 50.416 0.471   -12.983 0.00 27.63  ? 634  ILE   B HB   1 
ATOM   21186 H HG12 . ILE   B  1 608 ? 52.407 -0.218  -15.169 0.00 27.80  ? 634  ILE   B HG12 1 
ATOM   21187 H HG13 . ILE   B  1 608 ? 51.465 -1.439  -14.274 0.00 28.08  ? 634  ILE   B HG13 1 
ATOM   21188 H HG21 . ILE   B  1 608 ? 50.818 2.338   -14.410 0.00 27.83  ? 634  ILE   B HG21 1 
ATOM   21189 H HG22 . ILE   B  1 608 ? 51.756 2.624   -12.926 0.00 28.48  ? 634  ILE   B HG22 1 
ATOM   21190 H HG23 . ILE   B  1 608 ? 52.574 2.059   -14.404 0.00 27.97  ? 634  ILE   B HG23 1 
ATOM   21191 H HD11 . ILE   B  1 608 ? 50.386 -0.996  -16.375 0.00 28.68  ? 634  ILE   B HD11 1 
ATOM   21192 H HD12 . ILE   B  1 608 ? 49.380 -0.306  -15.074 0.00 29.06  ? 634  ILE   B HD12 1 
ATOM   21193 H HD13 . ILE   B  1 608 ? 50.402 0.760   -16.076 0.00 28.75  ? 634  ILE   B HD13 1 
ATOM   21194 N N    . PHE   B  1 609 ? 54.599 1.189   -12.682 1.00 21.18  ? 635  PHE   B N    1 
ATOM   21195 C CA   . PHE   B  1 609 ? 55.987 1.278   -13.175 1.00 22.04  ? 635  PHE   B CA   1 
ATOM   21196 C C    . PHE   B  1 609 ? 57.053 1.282   -12.057 1.00 22.93  ? 635  PHE   B C    1 
ATOM   21197 O O    . PHE   B  1 609 ? 58.239 1.256   -12.371 1.00 23.26  ? 635  PHE   B O    1 
ATOM   21198 C CB   . PHE   B  1 609 ? 56.157 2.547   -14.022 1.00 21.75  ? 635  PHE   B CB   1 
ATOM   21199 C CG   . PHE   B  1 609 ? 55.137 2.693   -15.131 1.00 22.35  ? 635  PHE   B CG   1 
ATOM   21200 C CD1  . PHE   B  1 609 ? 54.878 1.647   -15.999 1.00 22.62  ? 635  PHE   B CD1  1 
ATOM   21201 C CD2  . PHE   B  1 609 ? 54.432 3.875   -15.294 1.00 23.00  ? 635  PHE   B CD2  1 
ATOM   21202 C CE1  . PHE   B  1 609 ? 53.932 1.782   -17.009 1.00 23.99  ? 635  PHE   B CE1  1 
ATOM   21203 C CE2  . PHE   B  1 609 ? 53.479 4.000   -16.291 1.00 23.39  ? 635  PHE   B CE2  1 
ATOM   21204 C CZ   . PHE   B  1 609 ? 53.252 2.964   -17.156 1.00 23.76  ? 635  PHE   B CZ   1 
ATOM   21205 H H    . PHE   B  1 609 ? 54.260 2.052   -12.269 0.00 26.76  ? 635  PHE   B H    1 
ATOM   21206 H HA   . PHE   B  1 609 ? 56.215 0.433   -13.823 0.00 27.43  ? 635  PHE   B HA   1 
ATOM   21207 H HB2  . PHE   B  1 609 ? 56.071 3.412   -13.366 0.00 27.28  ? 635  PHE   B HB2  1 
ATOM   21208 H HB3  . PHE   B  1 609 ? 57.144 2.534   -14.480 0.00 26.98  ? 635  PHE   B HB3  1 
ATOM   21209 H HD1  . PHE   B  1 609 ? 55.416 0.718   -15.899 0.00 27.22  ? 635  PHE   B HD1  1 
ATOM   21210 H HD2  . PHE   B  1 609 ? 54.605 4.700   -14.624 0.00 28.16  ? 635  PHE   B HD2  1 
ATOM   21211 H HE1  . PHE   B  1 609 ? 53.745 0.965   -17.686 0.00 28.05  ? 635  PHE   B HE1  1 
ATOM   21212 H HE2  . PHE   B  1 609 ? 52.945 4.928   -16.411 0.00 27.81  ? 635  PHE   B HE2  1 
ATOM   21213 H HZ   . PHE   B  1 609 ? 52.517 3.068   -17.936 0.00 27.61  ? 635  PHE   B HZ   1 
ATOM   21214 N N    . LYS   B  1 610 ? 56.649 1.301   -10.779 1.00 23.54  ? 636  LYS   B N    1 
ATOM   21215 C CA   . LYS   B  1 610 ? 57.588 1.354   -9.654  1.00 24.88  ? 636  LYS   B CA   1 
ATOM   21216 C C    . LYS   B  1 610 ? 58.636 0.225   -9.643  1.00 26.67  ? 636  LYS   B C    1 
ATOM   21217 O O    . LYS   B  1 610 ? 59.794 0.468   -9.297  1.00 27.16  ? 636  LYS   B O    1 
ATOM   21218 C CB   . LYS   B  1 610 ? 56.815 1.351   -8.327  1.00 26.27  ? 636  LYS   B CB   1 
ATOM   21219 C CG   . LYS   B  1 610 ? 57.701 1.626   -7.117  1.00 29.76  ? 636  LYS   B CG   1 
ATOM   21220 C CD   . LYS   B  1 610 ? 56.883 1.978   -5.889  1.00 33.85  ? 636  LYS   B CD   1 
ATOM   21221 C CE   . LYS   B  1 610 ? 57.764 2.426   -4.750  1.00 38.79  ? 636  LYS   B CE   1 
ATOM   21222 N NZ   . LYS   B  1 610 ? 56.960 2.919   -3.595  1.00 42.68  ? 636  LYS   B NZ   1 
ATOM   21223 H H    . LYS   B  1 610 ? 55.677 1.269   -10.488 0.00 30.53  ? 636  LYS   B H    1 
ATOM   21224 H HA   . LYS   B  1 610 ? 58.129 2.298   -9.711  0.00 32.92  ? 636  LYS   B HA   1 
ATOM   21225 H HB2  . LYS   B  1 610 ? 56.049 2.123   -8.362  0.00 34.83  ? 636  LYS   B HB2  1 
ATOM   21226 H HB3  . LYS   B  1 610 ? 56.353 0.374   -8.189  0.00 34.95  ? 636  LYS   B HB3  1 
ATOM   21227 H HG2  . LYS   B  1 610 ? 58.287 0.739   -6.881  0.00 40.12  ? 636  LYS   B HG2  1 
ATOM   21228 H HG3  . LYS   B  1 610 ? 58.359 2.464   -7.339  0.00 39.94  ? 636  LYS   B HG3  1 
ATOM   21229 H HD2  . LYS   B  1 610 ? 56.197 2.790   -6.124  0.00 45.05  ? 636  LYS   B HD2  1 
ATOM   21230 H HD3  . LYS   B  1 610 ? 56.328 1.099   -5.563  0.00 45.32  ? 636  LYS   B HD3  1 
ATOM   21231 H HE2  . LYS   B  1 610 ? 58.370 1.586   -4.411  0.00 52.23  ? 636  LYS   B HE2  1 
ATOM   21232 H HE3  . LYS   B  1 610 ? 58.405 3.239   -5.089  0.00 51.93  ? 636  LYS   B HE3  1 
ATOM   21233 H HZ1  . LYS   B  1 610 ? 57.575 3.255   -2.861  0.00 57.62  ? 636  LYS   B HZ1  1 
ATOM   21234 H HZ2  . LYS   B  1 610 ? 56.354 3.676   -3.892  0.00 56.85  ? 636  LYS   B HZ2  1 
ATOM   21235 H HZ3  . LYS   B  1 610 ? 56.388 2.166   -3.225  0.00 57.16  ? 636  LYS   B HZ3  1 
ATOM   21236 N N    . GLY   B  1 611 ? 58.218 -0.985  -10.013 1.00 26.99  ? 637  GLY   B N    1 
ATOM   21237 C CA   . GLY   B  1 611 ? 59.089 -2.155  -10.068 1.00 27.08  ? 637  GLY   B CA   1 
ATOM   21238 C C    . GLY   B  1 611 ? 60.097 -2.151  -11.203 1.00 26.31  ? 637  GLY   B C    1 
ATOM   21239 O O    . GLY   B  1 611 ? 60.933 -3.057  -11.279 1.00 26.64  ? 637  GLY   B O    1 
ATOM   21240 H H    . GLY   B  1 611 ? 57.263 -1.197  -10.283 0.00 35.04  ? 637  GLY   B H    1 
ATOM   21241 H HA2  . GLY   B  1 611 ? 59.641 -2.226  -9.133  0.00 36.18  ? 637  GLY   B HA2  1 
ATOM   21242 H HA3  . GLY   B  1 611 ? 58.476 -3.049  -10.163 0.00 35.51  ? 637  GLY   B HA3  1 
ATOM   21243 N N    . LEU   B  1 612 ? 60.059 -1.130  -12.085 1.00 25.08  ? 638  LEU   B N    1 
ATOM   21244 C CA   . LEU   B  1 612 ? 61.047 -0.981  -13.154 1.00 24.47  ? 638  LEU   B CA   1 
ATOM   21245 C C    . LEU   B  1 612 ? 62.195 -0.197  -12.491 1.00 24.79  ? 638  LEU   B C    1 
ATOM   21246 O O    . LEU   B  1 612 ? 62.419 0.986   -12.742 1.00 24.47  ? 638  LEU   B O    1 
ATOM   21247 C CB   . LEU   B  1 612 ? 60.424 -0.246  -14.355 1.00 23.81  ? 638  LEU   B CB   1 
ATOM   21248 C CG   . LEU   B  1 612 ? 59.167 -0.935  -14.931 1.00 24.99  ? 638  LEU   B CG   1 
ATOM   21249 C CD1  . LEU   B  1 612 ? 58.525 -0.097  -16.029 1.00 25.35  ? 638  LEU   B CD1  1 
ATOM   21250 C CD2  . LEU   B  1 612 ? 59.485 -2.331  -15.461 1.00 25.57  ? 638  LEU   B CD2  1 
ATOM   21251 H H    . LEU   B  1 612 ? 59.361 -0.394  -12.100 0.00 32.35  ? 638  LEU   B H    1 
ATOM   21252 H HA   . LEU   B  1 612 ? 61.424 -1.947  -13.486 0.00 31.53  ? 638  LEU   B HA   1 
ATOM   21253 H HB2  . LEU   B  1 612 ? 60.132 0.757   -14.049 0.00 30.15  ? 638  LEU   B HB2  1 
ATOM   21254 H HB3  . LEU   B  1 612 ? 61.165 -0.185  -15.150 0.00 29.94  ? 638  LEU   B HB3  1 
ATOM   21255 H HG   . LEU   B  1 612 ? 58.426 -1.050  -14.142 0.00 31.25  ? 638  LEU   B HG   1 
ATOM   21256 H HD11 . LEU   B  1 612 ? 57.585 -0.564  -16.321 0.00 30.69  ? 638  LEU   B HD11 1 
ATOM   21257 H HD12 . LEU   B  1 612 ? 58.342 0.907   -15.648 0.00 31.03  ? 638  LEU   B HD12 1 
ATOM   21258 H HD13 . LEU   B  1 612 ? 59.199 -0.050  -16.883 0.00 30.74  ? 638  LEU   B HD13 1 
ATOM   21259 H HD21 . LEU   B  1 612 ? 58.630 -2.694  -16.030 0.00 31.35  ? 638  LEU   B HD21 1 
ATOM   21260 H HD22 . LEU   B  1 612 ? 60.363 -2.273  -16.102 0.00 31.62  ? 638  LEU   B HD22 1 
ATOM   21261 H HD23 . LEU   B  1 612 ? 59.677 -2.998  -14.623 0.00 32.10  ? 638  LEU   B HD23 1 
ATOM   21262 N N    . LYS   B  1 613 ? 62.907 -0.902  -11.605 1.00 25.60  ? 639  LYS   B N    1 
ATOM   21263 C CA   . LYS   B  1 613 ? 63.914 -0.332  -10.710 1.00 26.58  ? 639  LYS   B CA   1 
ATOM   21264 C C    . LYS   B  1 613 ? 65.122 0.316   -11.396 1.00 26.69  ? 639  LYS   B C    1 
ATOM   21265 O O    . LYS   B  1 613 ? 65.742 1.181   -10.793 1.00 26.62  ? 639  LYS   B O    1 
ATOM   21266 C CB   . LYS   B  1 613 ? 64.384 -1.401  -9.700  1.00 28.77  ? 639  LYS   B CB   1 
ATOM   21267 C CG   . LYS   B  1 613 ? 63.244 -1.875  -8.803  1.00 34.46  ? 639  LYS   B CG   1 
ATOM   21268 C CD   . LYS   B  1 613 ? 63.694 -2.727  -7.633  1.00 41.72  ? 639  LYS   B CD   1 
ATOM   21269 C CE   . LYS   B  1 613 ? 62.541 -2.989  -6.688  1.00 46.45  ? 639  LYS   B CE   1 
ATOM   21270 N NZ   . LYS   B  1 613 ? 62.955 -3.807  -5.513  1.00 49.19  ? 639  LYS   B NZ   1 
ATOM   21271 H H    . LYS   B  1 613 ? 62.807 -1.907  -11.506 0.00 34.06  ? 639  LYS   B H    1 
ATOM   21272 H HA   . LYS   B  1 613 ? 63.431 0.462   -10.142 0.00 35.94  ? 639  LYS   B HA   1 
ATOM   21273 H HB2  . LYS   B  1 613 ? 64.775 -2.262  -10.242 0.00 38.99  ? 639  LYS   B HB2  1 
ATOM   21274 H HB3  . LYS   B  1 613 ? 65.159 -0.975  -9.066  0.00 39.60  ? 639  LYS   B HB3  1 
ATOM   21275 H HG2  . LYS   B  1 613 ? 62.727 -1.004  -8.402  0.00 46.10  ? 639  LYS   B HG2  1 
ATOM   21276 H HG3  . LYS   B  1 613 ? 62.553 -2.471  -9.399  0.00 45.62  ? 639  LYS   B HG3  1 
ATOM   21277 H HD2  . LYS   B  1 613 ? 64.064 -3.683  -8.001  0.00 55.48  ? 639  LYS   B HD2  1 
ATOM   21278 H HD3  . LYS   B  1 613 ? 64.476 -2.204  -7.084  0.00 55.98  ? 639  LYS   B HD3  1 
ATOM   21279 H HE2  . LYS   B  1 613 ? 62.152 -2.040  -6.324  0.00 61.40  ? 639  LYS   B HE2  1 
ATOM   21280 H HE3  . LYS   B  1 613 ? 61.761 -3.533  -7.220  0.00 60.94  ? 639  LYS   B HE3  1 
ATOM   21281 H HZ1  . LYS   B  1 613 ? 62.162 -3.957  -4.898  0.00 65.55  ? 639  LYS   B HZ1  1 
ATOM   21282 H HZ2  . LYS   B  1 613 ? 63.307 -4.707  -5.822  0.00 65.44  ? 639  LYS   B HZ2  1 
ATOM   21283 H HZ3  . LYS   B  1 613 ? 63.685 -3.326  -4.997  0.00 65.86  ? 639  LYS   B HZ3  1 
ATOM   21284 N N    . ASN   B  1 614 ? 65.442 -0.061  -12.633 1.00 26.50  ? 640  ASN   B N    1 
ATOM   21285 C CA   . ASN   B  1 614 ? 66.588 0.498   -13.350 1.00 26.35  ? 640  ASN   B CA   1 
ATOM   21286 C C    . ASN   B  1 614 ? 66.169 1.515   -14.449 1.00 25.49  ? 640  ASN   B C    1 
ATOM   21287 O O    . ASN   B  1 614 ? 67.019 1.933   -15.232 1.00 25.17  ? 640  ASN   B O    1 
ATOM   21288 C CB   . ASN   B  1 614 ? 67.345 -0.697  -13.993 1.00 28.37  ? 640  ASN   B CB   1 
ATOM   21289 C CG   . ASN   B  1 614 ? 68.770 -0.476  -14.264 1.00 31.31  ? 640  ASN   B CG   1 
ATOM   21290 O OD1  . ASN   B  1 614 ? 69.459 0.099   -13.426 1.00 30.91  ? 640  ASN   B OD1  1 
ATOM   21291 N ND2  . ASN   B  1 614 ? 69.347 -1.055  -15.302 1.00 33.40  ? 640  ASN   B ND2  1 
ATOM   21292 H H    . ASN   B  1 614 ? 64.942 -0.762  -13.171 0.00 34.92  ? 640  ASN   B H    1 
ATOM   21293 H HA   . ASN   B  1 614 ? 67.258 1.007   -12.659 0.00 35.60  ? 640  ASN   B HA   1 
ATOM   21294 H HB2  . ASN   B  1 614 ? 67.268 -1.555  -13.327 0.00 37.82  ? 640  ASN   B HB2  1 
ATOM   21295 H HB3  . ASN   B  1 614 ? 66.865 -0.930  -14.942 0.00 36.98  ? 640  ASN   B HB3  1 
ATOM   21296 H HD21 . ASN   B  1 614 ? 69.729 -0.158  -15.524 0.00 43.62  ? 640  ASN   B HD21 1 
ATOM   21297 H HD22 . ASN   B  1 614 ? 68.889 -1.713  -15.922 0.00 43.26  ? 640  ASN   B HD22 1 
ATOM   21298 N N    . LEU   B  1 615 ? 64.875 1.905   -14.514 1.00 24.24  ? 641  LEU   B N    1 
ATOM   21299 C CA   . LEU   B  1 615 ? 64.356 2.731   -15.597 1.00 24.39  ? 641  LEU   B CA   1 
ATOM   21300 C C    . LEU   B  1 615 ? 64.880 4.159   -15.615 1.00 24.90  ? 641  LEU   B C    1 
ATOM   21301 O O    . LEU   B  1 615 ? 64.810 4.846   -14.601 1.00 24.68  ? 641  LEU   B O    1 
ATOM   21302 C CB   . LEU   B  1 615 ? 62.810 2.759   -15.568 1.00 24.41  ? 641  LEU   B CB   1 
ATOM   21303 C CG   . LEU   B  1 615 ? 62.110 2.958   -16.928 1.00 25.23  ? 641  LEU   B CG   1 
ATOM   21304 C CD1  . LEU   B  1 615 ? 62.160 1.670   -17.761 1.00 25.31  ? 641  LEU   B CD1  1 
ATOM   21305 C CD2  . LEU   B  1 615 ? 60.685 3.372   -16.744 1.00 25.62  ? 641  LEU   B CD2  1 
ATOM   21306 H H    . LEU   B  1 615 ? 64.178 1.695   -13.806 0.00 31.70  ? 641  LEU   B H    1 
ATOM   21307 H HA   . LEU   B  1 615 ? 64.675 2.250   -16.519 0.00 30.89  ? 641  LEU   B HA   1 
ATOM   21308 H HB2  . LEU   B  1 615 ? 62.428 1.836   -15.134 0.00 30.93  ? 641  LEU   B HB2  1 
ATOM   21309 H HB3  . LEU   B  1 615 ? 62.531 3.606   -14.945 0.00 31.06  ? 641  LEU   B HB3  1 
ATOM   21310 H HG   . LEU   B  1 615 ? 62.623 3.744   -17.481 0.00 31.07  ? 641  LEU   B HG   1 
ATOM   21311 H HD11 . LEU   B  1 615 ? 61.493 1.777   -18.616 0.00 30.49  ? 641  LEU   B HD11 1 
ATOM   21312 H HD12 . LEU   B  1 615 ? 63.177 1.503   -18.112 0.00 31.04  ? 641  LEU   B HD12 1 
ATOM   21313 H HD13 . LEU   B  1 615 ? 61.838 0.834   -17.141 0.00 31.10  ? 641  LEU   B HD13 1 
ATOM   21314 H HD21 . LEU   B  1 615 ? 60.268 3.588   -17.726 0.00 30.97  ? 641  LEU   B HD21 1 
ATOM   21315 H HD22 . LEU   B  1 615 ? 60.133 2.558   -16.274 0.00 31.46  ? 641  LEU   B HD22 1 
ATOM   21316 H HD23 . LEU   B  1 615 ? 60.639 4.264   -16.121 0.00 31.67  ? 641  LEU   B HD23 1 
ATOM   21317 N N    . THR   B  1 616 ? 65.373 4.613   -16.782 1.00 25.26  ? 642  THR   B N    1 
ATOM   21318 C CA   . THR   B  1 616 ? 65.851 5.983   -16.968 1.00 25.93  ? 642  THR   B CA   1 
ATOM   21319 C C    . THR   B  1 616 ? 64.986 6.755   -17.980 1.00 24.99  ? 642  THR   B C    1 
ATOM   21320 O O    . THR   B  1 616 ? 64.892 7.968   -17.870 1.00 25.61  ? 642  THR   B O    1 
ATOM   21321 C CB   . THR   B  1 616 ? 67.359 6.018   -17.309 1.00 28.08  ? 642  THR   B CB   1 
ATOM   21322 O OG1  . THR   B  1 616 ? 67.597 5.330   -18.534 1.00 29.97  ? 642  THR   B OG1  1 
ATOM   21323 C CG2  . THR   B  1 616 ? 68.203 5.432   -16.196 1.00 28.96  ? 642  THR   B CG2  1 
ATOM   21324 H H    . THR   B  1 616 ? 65.462 4.044   -17.618 0.00 31.75  ? 642  THR   B H    1 
ATOM   21325 H HA   . THR   B  1 616 ? 65.777 6.520   -16.027 0.00 33.41  ? 642  THR   B HA   1 
ATOM   21326 H HB   . THR   B  1 616 ? 67.661 7.057   -17.433 0.00 35.98  ? 642  THR   B HB   1 
ATOM   21327 H HG1  . THR   B  1 616 ? 68.567 5.351   -18.750 0.00 37.89  ? 642  THR   B HG1  1 
ATOM   21328 H HG21 . THR   B  1 616 ? 69.258 5.546   -16.438 0.00 37.82  ? 642  THR   B HG21 1 
ATOM   21329 H HG22 . THR   B  1 616 ? 67.997 5.958   -15.265 0.00 37.95  ? 642  THR   B HG22 1 
ATOM   21330 H HG23 . THR   B  1 616 ? 67.981 4.372   -16.067 0.00 37.52  ? 642  THR   B HG23 1 
ATOM   21331 N N    . ARG   B  1 617 ? 64.351 6.080   -18.946 1.00 24.22  ? 643  ARG   B N    1 
ATOM   21332 C CA   . ARG   B  1 617 ? 63.533 6.758   -19.952 1.00 24.50  ? 643  ARG   B CA   1 
ATOM   21333 C C    . ARG   B  1 617 ? 62.128 6.169   -19.950 1.00 23.70  ? 643  ARG   B C    1 
ATOM   21334 O O    . ARG   B  1 617 ? 61.969 4.955   -20.117 1.00 23.28  ? 643  ARG   B O    1 
ATOM   21335 C CB   . ARG   B  1 617 ? 64.175 6.625   -21.342 1.00 26.66  ? 643  ARG   B CB   1 
ATOM   21336 C CG   . ARG   B  1 617 ? 63.409 7.404   -22.406 1.00 32.72  ? 643  ARG   B CG   1 
ATOM   21337 C CD   . ARG   B  1 617 ? 64.116 7.474   -23.763 1.00 37.18  ? 643  ARG   B CD   1 
ATOM   21338 N NE   . ARG   B  1 617 ? 63.420 8.390   -24.677 1.00 40.31  ? 643  ARG   B NE   1 
ATOM   21339 C CZ   . ARG   B  1 617 ? 62.284 8.115   -25.319 1.00 42.81  ? 643  ARG   B CZ   1 
ATOM   21340 N NH1  . ARG   B  1 617 ? 61.690 6.931   -25.166 1.00 41.43  ? 643  ARG   B NH1  1 
ATOM   21341 N NH2  . ARG   B  1 617 ? 61.725 9.026   -26.113 1.00 43.35  ? 643  ARG   B NH2  1 
ATOM   21342 H H    . ARG   B  1 617 ? 64.386 5.073   -19.074 0.00 29.73  ? 643  ARG   B H    1 
ATOM   21343 H HA   . ARG   B  1 617 ? 63.451 7.821   -19.733 0.00 29.81  ? 643  ARG   B HA   1 
ATOM   21344 H HB2  . ARG   B  1 617 ? 65.191 7.015   -21.305 0.00 32.18  ? 643  ARG   B HB2  1 
ATOM   21345 H HB3  . ARG   B  1 617 ? 64.191 5.574   -21.627 0.00 31.75  ? 643  ARG   B HB3  1 
ATOM   21346 H HG2  . ARG   B  1 617 ? 62.443 6.931   -22.575 0.00 38.43  ? 643  ARG   B HG2  1 
ATOM   21347 H HG3  . ARG   B  1 617 ? 63.262 8.425   -22.057 0.00 38.89  ? 643  ARG   B HG3  1 
ATOM   21348 H HD2  . ARG   B  1 617 ? 65.124 7.857   -23.610 0.00 44.11  ? 643  ARG   B HD2  1 
ATOM   21349 H HD3  . ARG   B  1 617 ? 64.164 6.481   -24.208 0.00 43.61  ? 643  ARG   B HD3  1 
ATOM   21350 H HE   . ARG   B  1 617 ? 63.833 9.307   -24.817 0.00 47.35  ? 643  ARG   B HE   1 
ATOM   21351 H HH11 . ARG   B  1 617 ? 62.071 6.205   -24.568 0.00 48.18  ? 643  ARG   B HH11 1 
ATOM   21352 H HH12 . ARG   B  1 617 ? 60.828 6.739   -25.665 0.00 47.69  ? 643  ARG   B HH12 1 
ATOM   21353 H HH21 . ARG   B  1 617 ? 62.166 9.930   -26.245 0.00 50.35  ? 643  ARG   B HH21 1 
ATOM   21354 H HH22 . ARG   B  1 617 ? 60.866 8.815   -26.611 0.00 49.92  ? 643  ARG   B HH22 1 
ATOM   21355 N N    . LEU   B  1 618 ? 61.110 7.029   -19.779 1.00 22.72  ? 644  LEU   B N    1 
ATOM   21356 C CA   . LEU   B  1 618 ? 59.718 6.591   -19.752 1.00 22.21  ? 644  LEU   B CA   1 
ATOM   21357 C C    . LEU   B  1 618 ? 58.867 7.483   -20.663 1.00 21.94  ? 644  LEU   B C    1 
ATOM   21358 O O    . LEU   B  1 618 ? 58.917 8.708   -20.544 1.00 22.66  ? 644  LEU   B O    1 
ATOM   21359 C CB   . LEU   B  1 618 ? 59.206 6.639   -18.307 1.00 21.95  ? 644  LEU   B CB   1 
ATOM   21360 C CG   . LEU   B  1 618 ? 57.729 6.279   -18.072 1.00 23.48  ? 644  LEU   B CG   1 
ATOM   21361 C CD1  . LEU   B  1 618 ? 57.411 4.834   -18.529 1.00 24.33  ? 644  LEU   B CD1  1 
ATOM   21362 C CD2  . LEU   B  1 618 ? 57.363 6.438   -16.604 1.00 23.50  ? 644  LEU   B CD2  1 
ATOM   21363 H H    . LEU   B  1 618 ? 61.214 8.032   -19.660 0.00 27.26  ? 644  LEU   B H    1 
ATOM   21364 H HA   . LEU   B  1 618 ? 59.645 5.566   -20.112 0.00 26.02  ? 644  LEU   B HA   1 
ATOM   21365 H HB2  . LEU   B  1 618 ? 59.780 5.901   -17.751 0.00 26.58  ? 644  LEU   B HB2  1 
ATOM   21366 H HB3  . LEU   B  1 618 ? 59.379 7.635   -17.902 0.00 26.60  ? 644  LEU   B HB3  1 
ATOM   21367 H HG   . LEU   B  1 618 ? 57.095 6.956   -18.641 0.00 27.76  ? 644  LEU   B HG   1 
ATOM   21368 H HD11 . LEU   B  1 618 ? 56.374 4.615   -18.281 0.00 28.64  ? 644  LEU   B HD11 1 
ATOM   21369 H HD12 . LEU   B  1 618 ? 57.548 4.747   -19.605 0.00 28.36  ? 644  LEU   B HD12 1 
ATOM   21370 H HD13 . LEU   B  1 618 ? 58.061 4.134   -18.006 0.00 28.96  ? 644  LEU   B HD13 1 
ATOM   21371 H HD21 . LEU   B  1 618 ? 56.312 6.183   -16.473 0.00 28.39  ? 644  LEU   B HD21 1 
ATOM   21372 H HD22 . LEU   B  1 618 ? 57.985 5.771   -16.010 0.00 28.77  ? 644  LEU   B HD22 1 
ATOM   21373 H HD23 . LEU   B  1 618 ? 57.533 7.473   -16.308 0.00 28.74  ? 644  LEU   B HD23 1 
ATOM   21374 N N    . ASP   B  1 619 ? 58.091 6.875   -21.572 1.00 20.92  ? 645  ASP   B N    1 
ATOM   21375 C CA   . ASP   B  1 619 ? 57.231 7.645   -22.465 1.00 20.78  ? 645  ASP   B CA   1 
ATOM   21376 C C    . ASP   B  1 619 ? 55.770 7.309   -22.184 1.00 21.43  ? 645  ASP   B C    1 
ATOM   21377 O O    . ASP   B  1 619 ? 55.318 6.204   -22.467 1.00 21.44  ? 645  ASP   B O    1 
ATOM   21378 C CB   . ASP   B  1 619 ? 57.620 7.395   -23.933 1.00 21.71  ? 645  ASP   B CB   1 
ATOM   21379 C CG   . ASP   B  1 619 ? 56.860 8.196   -24.965 1.00 25.57  ? 645  ASP   B CG   1 
ATOM   21380 O OD1  . ASP   B  1 619 ? 55.924 8.916   -24.586 1.00 25.34  ? 645  ASP   B OD1  1 
ATOM   21381 O OD2  . ASP   B  1 619 ? 57.208 8.100   -26.163 1.00 28.95  ? 645  ASP   B OD2  1 
ATOM   21382 H H    . ASP   B  1 619 ? 58.036 5.870   -21.711 0.00 23.73  ? 645  ASP   B H    1 
ATOM   21383 H HA   . ASP   B  1 619 ? 57.362 8.706   -22.271 0.00 23.55  ? 645  ASP   B HA   1 
ATOM   21384 H HB2  . ASP   B  1 619 ? 58.681 7.608   -24.060 0.00 24.21  ? 645  ASP   B HB2  1 
ATOM   21385 H HB3  . ASP   B  1 619 ? 57.419 6.355   -24.171 0.00 23.92  ? 645  ASP   B HB3  1 
ATOM   21386 N N    . LEU   B  1 620 ? 55.046 8.272   -21.583 1.00 21.25  ? 646  LEU   B N    1 
ATOM   21387 C CA   . LEU   B  1 620 ? 53.624 8.186   -21.258 1.00 20.62  ? 646  LEU   B CA   1 
ATOM   21388 C C    . LEU   B  1 620 ? 52.770 9.055   -22.184 1.00 21.19  ? 646  LEU   B C    1 
ATOM   21389 O O    . LEU   B  1 620 ? 51.636 9.387   -21.819 1.00 21.51  ? 646  LEU   B O    1 
ATOM   21390 C CB   . LEU   B  1 620 ? 53.407 8.657   -19.803 1.00 20.41  ? 646  LEU   B CB   1 
ATOM   21391 C CG   . LEU   B  1 620 ? 54.277 8.011   -18.731 1.00 22.29  ? 646  LEU   B CG   1 
ATOM   21392 C CD1  . LEU   B  1 620 ? 53.843 8.457   -17.342 1.00 22.64  ? 646  LEU   B CD1  1 
ATOM   21393 C CD2  . LEU   B  1 620 ? 54.247 6.486   -18.831 1.00 23.30  ? 646  LEU   B CD2  1 
ATOM   21394 H H    . LEU   B  1 620 ? 55.439 9.162   -21.294 0.00 24.25  ? 646  LEU   B H    1 
ATOM   21395 H HA   . LEU   B  1 620 ? 53.267 7.162   -21.353 0.00 23.07  ? 646  LEU   B HA   1 
ATOM   21396 H HB2  . LEU   B  1 620 ? 53.587 9.730   -19.764 0.00 23.62  ? 646  LEU   B HB2  1 
ATOM   21397 H HB3  . LEU   B  1 620 ? 52.374 8.452   -19.524 0.00 23.45  ? 646  LEU   B HB3  1 
ATOM   21398 H HG   . LEU   B  1 620 ? 55.300 8.352   -18.877 0.00 26.16  ? 646  LEU   B HG   1 
ATOM   21399 H HD11 . LEU   B  1 620 ? 54.542 8.059   -16.608 0.00 27.27  ? 646  LEU   B HD11 1 
ATOM   21400 H HD12 . LEU   B  1 620 ? 53.845 9.545   -17.306 0.00 27.13  ? 646  LEU   B HD12 1 
ATOM   21401 H HD13 . LEU   B  1 620 ? 52.841 8.077   -17.145 0.00 26.92  ? 646  LEU   B HD13 1 
ATOM   21402 H HD21 . LEU   B  1 620 ? 54.380 6.053   -17.841 0.00 27.43  ? 646  LEU   B HD21 1 
ATOM   21403 H HD22 . LEU   B  1 620 ? 53.296 6.174   -19.256 0.00 26.86  ? 646  LEU   B HD22 1 
ATOM   21404 H HD23 . LEU   B  1 620 ? 55.060 6.165   -19.480 0.00 26.96  ? 646  LEU   B HD23 1 
ATOM   21405 N N    . SER   B  1 621 ? 53.274 9.396   -23.386 1.00 21.10  ? 647  SER   B N    1 
ATOM   21406 C CA   . SER   B  1 621 ? 52.519 10.227  -24.310 1.00 21.15  ? 647  SER   B CA   1 
ATOM   21407 C C    . SER   B  1 621 ? 51.284 9.513   -24.844 1.00 21.05  ? 647  SER   B C    1 
ATOM   21408 O O    . SER   B  1 621 ? 51.207 8.291   -24.780 1.00 20.84  ? 647  SER   B O    1 
ATOM   21409 C CB   . SER   B  1 621 ? 53.407 10.677  -25.471 1.00 21.85  ? 647  SER   B CB   1 
ATOM   21410 O OG   . SER   B  1 621 ? 53.734 9.606   -26.338 1.00 23.41  ? 647  SER   B OG   1 
ATOM   21411 H H    . SER   B  1 621 ? 54.173 9.102   -23.756 0.00 23.23  ? 647  SER   B H    1 
ATOM   21412 H HA   . SER   B  1 621 ? 52.184 11.121  -23.787 0.00 23.43  ? 647  SER   B HA   1 
ATOM   21413 H HB2  . SER   B  1 621 ? 52.874 11.436  -26.043 0.00 23.78  ? 647  SER   B HB2  1 
ATOM   21414 H HB3  . SER   B  1 621 ? 54.325 11.103  -25.069 0.00 24.05  ? 647  SER   B HB3  1 
ATOM   21415 H HG   . SER   B  1 621 ? 54.550 9.139   -26.019 0.00 25.45  ? 647  SER   B HG   1 
ATOM   21416 N N    . LEU   B  1 622 ? 50.317 10.271  -25.373 1.00 20.54  ? 648  LEU   B N    1 
ATOM   21417 C CA   . LEU   B  1 622 ? 49.127 9.696   -26.012 1.00 20.79  ? 648  LEU   B CA   1 
ATOM   21418 C C    . LEU   B  1 622 ? 48.385 8.698   -25.132 1.00 20.34  ? 648  LEU   B C    1 
ATOM   21419 O O    . LEU   B  1 622 ? 47.969 7.652   -25.606 1.00 20.90  ? 648  LEU   B O    1 
ATOM   21420 C CB   . LEU   B  1 622 ? 49.501 9.068   -27.377 1.00 21.11  ? 648  LEU   B CB   1 
ATOM   21421 C CG   . LEU   B  1 622 ? 50.028 10.016  -28.442 1.00 23.89  ? 648  LEU   B CG   1 
ATOM   21422 C CD1  . LEU   B  1 622 ? 50.523 9.227   -29.674 1.00 24.96  ? 648  LEU   B CD1  1 
ATOM   21423 C CD2  . LEU   B  1 622 ? 48.959 11.023  -28.861 1.00 24.76  ? 648  LEU   B CD2  1 
ATOM   21424 H H    . LEU   B  1 622 ? 50.331 11.285  -25.376 0.00 22.26  ? 648  LEU   B H    1 
ATOM   21425 H HA   . LEU   B  1 622 ? 48.417 10.503  -26.188 0.00 22.26  ? 648  LEU   B HA   1 
ATOM   21426 H HB2  . LEU   B  1 622 ? 50.267 8.310   -27.220 0.00 22.16  ? 648  LEU   B HB2  1 
ATOM   21427 H HB3  . LEU   B  1 622 ? 48.615 8.601   -27.805 0.00 22.08  ? 648  LEU   B HB3  1 
ATOM   21428 H HG   . LEU   B  1 622 ? 50.876 10.567  -28.039 0.00 25.59  ? 648  LEU   B HG   1 
ATOM   21429 H HD11 . LEU   B  1 622 ? 50.911 9.926   -30.414 0.00 26.33  ? 648  LEU   B HD11 1 
ATOM   21430 H HD12 . LEU   B  1 622 ? 51.310 8.543   -29.361 0.00 26.38  ? 648  LEU   B HD12 1 
ATOM   21431 H HD13 . LEU   B  1 622 ? 49.688 8.670   -30.095 0.00 26.26  ? 648  LEU   B HD13 1 
ATOM   21432 H HD21 . LEU   B  1 622 ? 49.301 11.547  -29.753 0.00 26.45  ? 648  LEU   B HD21 1 
ATOM   21433 H HD22 . LEU   B  1 622 ? 48.030 10.498  -29.078 0.00 26.45  ? 648  LEU   B HD22 1 
ATOM   21434 H HD23 . LEU   B  1 622 ? 48.801 11.742  -28.061 0.00 26.81  ? 648  LEU   B HD23 1 
ATOM   21435 N N    . ASN   B  1 623 ? 48.195 9.029   -23.855 1.00 19.84  ? 649  ASN   B N    1 
ATOM   21436 C CA   . ASN   B  1 623 ? 47.456 8.162   -22.935 1.00 20.34  ? 649  ASN   B CA   1 
ATOM   21437 C C    . ASN   B  1 623 ? 46.134 8.810   -22.430 1.00 21.11  ? 649  ASN   B C    1 
ATOM   21438 O O    . ASN   B  1 623 ? 45.545 8.309   -21.467 1.00 21.27  ? 649  ASN   B O    1 
ATOM   21439 C CB   . ASN   B  1 623 ? 48.362 7.752   -21.778 1.00 20.31  ? 649  ASN   B CB   1 
ATOM   21440 C CG   . ASN   B  1 623 ? 49.093 6.439   -22.009 1.00 21.50  ? 649  ASN   B CG   1 
ATOM   21441 O OD1  . ASN   B  1 623 ? 48.680 5.381   -21.514 1.00 21.01  ? 649  ASN   B OD1  1 
ATOM   21442 N ND2  . ASN   B  1 623 ? 50.168 6.479   -22.796 1.00 21.09  ? 649  ASN   B ND2  1 
ATOM   21443 H H    . ASN   B  1 623 ? 48.524 9.891   -23.433 0.00 21.70  ? 649  ASN   B H    1 
ATOM   21444 H HA   . ASN   B  1 623 ? 47.120 7.271   -23.463 0.00 22.01  ? 649  ASN   B HA   1 
ATOM   21445 H HB2  . ASN   B  1 623 ? 49.109 8.527   -21.613 0.00 22.59  ? 649  ASN   B HB2  1 
ATOM   21446 H HB3  . ASN   B  1 623 ? 47.745 7.639   -20.889 0.00 22.69  ? 649  ASN   B HB3  1 
ATOM   21447 H HD21 . ASN   B  1 623 ? 50.691 5.629   -22.983 0.00 22.93  ? 649  ASN   B HD21 1 
ATOM   21448 H HD22 . ASN   B  1 623 ? 50.465 7.357   -23.209 0.00 23.00  ? 649  ASN   B HD22 1 
ATOM   21449 N N    . ARG   B  1 624 ? 45.676 9.901   -23.099 1.00 20.92  ? 650  ARG   B N    1 
ATOM   21450 C CA   . ARG   B  1 624 ? 44.434 10.619  -22.791 1.00 21.75  ? 650  ARG   B CA   1 
ATOM   21451 C C    . ARG   B  1 624 ? 44.370 11.123  -21.358 1.00 22.40  ? 650  ARG   B C    1 
ATOM   21452 O O    . ARG   B  1 624 ? 43.280 11.295  -20.818 1.00 22.79  ? 650  ARG   B O    1 
ATOM   21453 C CB   . ARG   B  1 624 ? 43.224 9.727   -23.109 1.00 22.91  ? 650  ARG   B CB   1 
ATOM   21454 C CG   . ARG   B  1 624 ? 43.366 9.013   -24.453 1.00 26.11  ? 650  ARG   B CG   1 
ATOM   21455 C CD   . ARG   B  1 624 ? 42.051 8.472   -24.977 1.00 30.24  ? 650  ARG   B CD   1 
ATOM   21456 N NE   . ARG   B  1 624 ? 42.286 7.478   -26.027 1.00 35.16  ? 650  ARG   B NE   1 
ATOM   21457 C CZ   . ARG   B  1 624 ? 41.326 6.829   -26.682 1.00 38.36  ? 650  ARG   B CZ   1 
ATOM   21458 N NH1  . ARG   B  1 624 ? 40.043 7.069   -26.410 1.00 37.61  ? 650  ARG   B NH1  1 
ATOM   21459 N NH2  . ARG   B  1 624 ? 41.638 5.935   -27.613 1.00 38.14  ? 650  ARG   B NH2  1 
ATOM   21460 H H    . ARG   B  1 624 ? 46.152 10.318  -23.893 0.00 22.99  ? 650  ARG   B H    1 
ATOM   21461 H HA   . ARG   B  1 624 ? 44.374 11.489  -23.442 0.00 24.37  ? 650  ARG   B HA   1 
ATOM   21462 H HB2  . ARG   B  1 624 ? 43.122 8.973   -22.331 0.00 25.75  ? 650  ARG   B HB2  1 
ATOM   21463 H HB3  . ARG   B  1 624 ? 42.329 10.345  -23.151 0.00 25.80  ? 650  ARG   B HB3  1 
ATOM   21464 H HG2  . ARG   B  1 624 ? 43.762 9.711   -25.190 0.00 28.97  ? 650  ARG   B HG2  1 
ATOM   21465 H HG3  . ARG   B  1 624 ? 44.049 8.174   -24.327 0.00 28.96  ? 650  ARG   B HG3  1 
ATOM   21466 H HD2  . ARG   B  1 624 ? 41.506 7.992   -24.165 0.00 34.15  ? 650  ARG   B HD2  1 
ATOM   21467 H HD3  . ARG   B  1 624 ? 41.464 9.286   -25.399 0.00 34.05  ? 650  ARG   B HD3  1 
ATOM   21468 H HE   . ARG   B  1 624 ? 43.249 7.262   -26.265 0.00 39.37  ? 650  ARG   B HE   1 
ATOM   21469 H HH11 . ARG   B  1 624 ? 39.763 7.740   -25.704 0.00 42.86  ? 650  ARG   B HH11 1 
ATOM   21470 H HH12 . ARG   B  1 624 ? 39.322 6.566   -26.919 0.00 42.59  ? 650  ARG   B HH12 1 
ATOM   21471 H HH21 . ARG   B  1 624 ? 42.610 5.742   -27.833 0.00 42.61  ? 650  ARG   B HH21 1 
ATOM   21472 H HH22 . ARG   B  1 624 ? 40.906 5.444   -28.114 0.00 42.73  ? 650  ARG   B HH22 1 
ATOM   21473 N N    . LEU   B  1 625 ? 45.528 11.367  -20.738 1.00 22.56  ? 651  LEU   B N    1 
ATOM   21474 C CA   . LEU   B  1 625 ? 45.578 11.791  -19.346 1.00 23.00  ? 651  LEU   B CA   1 
ATOM   21475 C C    . LEU   B  1 625 ? 45.099 13.224  -19.143 1.00 24.25  ? 651  LEU   B C    1 
ATOM   21476 O O    . LEU   B  1 625 ? 45.586 14.132  -19.804 1.00 23.65  ? 651  LEU   B O    1 
ATOM   21477 C CB   . LEU   B  1 625 ? 47.022 11.642  -18.807 1.00 22.92  ? 651  LEU   B CB   1 
ATOM   21478 C CG   . LEU   B  1 625 ? 47.488 10.199  -18.533 1.00 24.24  ? 651  LEU   B CG   1 
ATOM   21479 C CD1  . LEU   B  1 625 ? 49.002 10.113  -18.476 1.00 24.41  ? 651  LEU   B CD1  1 
ATOM   21480 C CD2  . LEU   B  1 625 ? 46.914 9.683   -17.221 1.00 24.93  ? 651  LEU   B CD2  1 
ATOM   21481 H H    . LEU   B  1 625 ? 46.441 11.292  -21.173 0.00 25.81  ? 651  LEU   B H    1 
ATOM   21482 H HA   . LEU   B  1 625 ? 44.924 11.140  -18.771 0.00 27.07  ? 651  LEU   B HA   1 
ATOM   21483 H HB2  . LEU   B  1 625 ? 47.724 12.089  -19.509 0.00 26.85  ? 651  LEU   B HB2  1 
ATOM   21484 H HB3  . LEU   B  1 625 ? 47.081 12.179  -17.861 0.00 27.39  ? 651  LEU   B HB3  1 
ATOM   21485 H HG   . LEU   B  1 625 ? 47.145 9.545   -19.334 0.00 28.08  ? 651  LEU   B HG   1 
ATOM   21486 H HD11 . LEU   B  1 625 ? 49.289 9.087   -18.250 0.00 28.59  ? 651  LEU   B HD11 1 
ATOM   21487 H HD12 . LEU   B  1 625 ? 49.411 10.408  -19.441 0.00 28.39  ? 651  LEU   B HD12 1 
ATOM   21488 H HD13 . LEU   B  1 625 ? 49.366 10.782  -17.698 0.00 29.02  ? 651  LEU   B HD13 1 
ATOM   21489 H HD21 . LEU   B  1 625 ? 47.249 8.658   -17.068 0.00 29.52  ? 651  LEU   B HD21 1 
ATOM   21490 H HD22 . LEU   B  1 625 ? 47.276 10.310  -16.408 0.00 29.98  ? 651  LEU   B HD22 1 
ATOM   21491 H HD23 . LEU   B  1 625 ? 45.827 9.711   -17.248 0.00 29.62  ? 651  LEU   B HD23 1 
ATOM   21492 N N    . LYS   B  1 626 ? 44.140 13.417  -18.230 1.00 25.60  ? 652  LYS   B N    1 
ATOM   21493 C CA   . LYS   B  1 626 ? 43.650 14.741  -17.840 1.00 27.57  ? 652  LYS   B CA   1 
ATOM   21494 C C    . LYS   B  1 626 ? 44.393 15.212  -16.567 1.00 29.21  ? 652  LYS   B C    1 
ATOM   21495 O O    . LYS   B  1 626 ? 44.603 16.406  -16.374 1.00 29.81  ? 652  LYS   B O    1 
ATOM   21496 C CB   . LYS   B  1 626 ? 42.127 14.723  -17.646 1.00 30.21  ? 652  LYS   B CB   1 
ATOM   21497 C CG   . LYS   B  1 626 ? 41.385 14.547  -18.965 1.00 35.85  ? 652  LYS   B CG   1 
ATOM   21498 C CD   . LYS   B  1 626 ? 39.881 14.623  -18.796 1.00 42.17  ? 652  LYS   B CD   1 
ATOM   21499 C CE   . LYS   B  1 626 ? 39.166 14.503  -20.116 1.00 47.71  ? 652  LYS   B CE   1 
ATOM   21500 N NZ   . LYS   B  1 626 ? 37.687 14.427  -19.936 1.00 51.87  ? 652  LYS   B NZ   1 
ATOM   21501 H H    . LYS   B  1 626 ? 43.676 12.666  -17.730 0.00 30.84  ? 652  LYS   B H    1 
ATOM   21502 H HA   . LYS   B  1 626 ? 43.875 15.465  -18.621 0.00 33.52  ? 652  LYS   B HA   1 
ATOM   21503 H HB2  . LYS   B  1 626 ? 41.852 13.903  -16.984 0.00 36.98  ? 652  LYS   B HB2  1 
ATOM   21504 H HB3  . LYS   B  1 626 ? 41.813 15.668  -17.207 0.00 37.32  ? 652  LYS   B HB3  1 
ATOM   21505 H HG2  . LYS   B  1 626 ? 41.688 15.333  -19.654 0.00 43.28  ? 652  LYS   B HG2  1 
ATOM   21506 H HG3  . LYS   B  1 626 ? 41.629 13.572  -19.382 0.00 42.96  ? 652  LYS   B HG3  1 
ATOM   21507 H HD2  . LYS   B  1 626 ? 39.550 13.809  -18.153 0.00 51.16  ? 652  LYS   B HD2  1 
ATOM   21508 H HD3  . LYS   B  1 626 ? 39.618 15.581  -18.349 0.00 51.51  ? 652  LYS   B HD3  1 
ATOM   21509 H HE2  . LYS   B  1 626 ? 39.392 15.375  -20.728 0.00 57.47  ? 652  LYS   B HE2  1 
ATOM   21510 H HE3  . LYS   B  1 626 ? 39.495 13.595  -20.620 0.00 57.08  ? 652  LYS   B HE3  1 
ATOM   21511 H HZ1  . LYS   B  1 626 ? 37.231 14.353  -20.840 0.00 62.49  ? 652  LYS   B HZ1  1 
ATOM   21512 H HZ2  . LYS   B  1 626 ? 37.449 13.614  -19.378 0.00 62.68  ? 652  LYS   B HZ2  1 
ATOM   21513 H HZ3  . LYS   B  1 626 ? 37.353 15.261  -19.463 0.00 63.05  ? 652  LYS   B HZ3  1 
ATOM   21514 N N    . HIS   B  1 627 ? 44.779 14.274  -15.708 1.00 29.96  ? 653  HIS   B N    1 
ATOM   21515 C CA   . HIS   B  1 627 ? 45.596 14.525  -14.530 1.00 31.62  ? 653  HIS   B CA   1 
ATOM   21516 C C    . HIS   B  1 627 ? 46.219 13.193  -14.069 1.00 31.66  ? 653  HIS   B C    1 
ATOM   21517 O O    . HIS   B  1 627 ? 45.681 12.125  -14.371 1.00 32.85  ? 653  HIS   B O    1 
ATOM   21518 C CB   . HIS   B  1 627 ? 44.751 15.142  -13.413 1.00 34.05  ? 653  HIS   B CB   1 
ATOM   21519 C CG   . HIS   B  1 627 ? 43.686 14.224  -12.918 1.00 38.94  ? 653  HIS   B CG   1 
ATOM   21520 N ND1  . HIS   B  1 627 ? 42.508 14.050  -13.615 1.00 41.90  ? 653  HIS   B ND1  1 
ATOM   21521 C CD2  . HIS   B  1 627 ? 43.679 13.414  -11.835 1.00 41.14  ? 653  HIS   B CD2  1 
ATOM   21522 C CE1  . HIS   B  1 627 ? 41.809 13.159  -12.932 1.00 42.89  ? 653  HIS   B CE1  1 
ATOM   21523 N NE2  . HIS   B  1 627 ? 42.477 12.746  -11.851 1.00 42.87  ? 653  HIS   B NE2  1 
ATOM   21524 H H    . HIS   B  1 627 ? 44.483 13.306  -15.791 0.00 36.80  ? 653  HIS   B H    1 
ATOM   21525 H HA   . HIS   B  1 627 ? 46.402 15.213  -14.781 0.00 39.55  ? 653  HIS   B HA   1 
ATOM   21526 H HB2  . HIS   B  1 627 ? 45.401 15.382  -12.572 0.00 43.36  ? 653  HIS   B HB2  1 
ATOM   21527 H HB3  . HIS   B  1 627 ? 44.271 16.047  -13.782 0.00 43.09  ? 653  HIS   B HB3  1 
ATOM   21528 H HD1  . HIS   B  1 627 ? 42.233 14.511  -14.477 0.00 51.97  ? 653  HIS   B HD1  1 
ATOM   21529 H HD2  . HIS   B  1 627 ? 44.463 13.308  -11.104 0.00 51.99  ? 653  HIS   B HD2  1 
ATOM   21530 H HE1  . HIS   B  1 627 ? 40.828 12.812  -13.211 0.00 53.35  ? 653  HIS   B HE1  1 
ATOM   21531 N N    . ILE   B  1 628 ? 47.354 13.252  -13.384 1.00 29.99  ? 654  ILE   B N    1 
ATOM   21532 C CA   . ILE   B  1 628 ? 48.004 12.055  -12.866 1.00 28.81  ? 654  ILE   B CA   1 
ATOM   21533 C C    . ILE   B  1 628 ? 47.787 12.093  -11.359 1.00 28.70  ? 654  ILE   B C    1 
ATOM   21534 O O    . ILE   B  1 628 ? 48.153 13.104  -10.747 1.00 29.34  ? 654  ILE   B O    1 
ATOM   21535 C CB   . ILE   B  1 628 ? 49.512 12.022  -13.210 1.00 28.33  ? 654  ILE   B CB   1 
ATOM   21536 C CG1  . ILE   B  1 628 ? 49.712 11.933  -14.749 1.00 28.99  ? 654  ILE   B CG1  1 
ATOM   21537 C CG2  . ILE   B  1 628 ? 50.185 10.829  -12.487 1.00 28.11  ? 654  ILE   B CG2  1 
ATOM   21538 C CD1  . ILE   B  1 628 ? 51.044 12.375  -15.243 1.00 30.04  ? 654  ILE   B CD1  1 
ATOM   21539 H H    . ILE   B  1 628 ? 47.847 14.113  -13.170 0.00 37.97  ? 654  ILE   B H    1 
ATOM   21540 H HA   . ILE   B  1 628 ? 47.569 11.158  -13.300 0.00 35.91  ? 654  ILE   B HA   1 
ATOM   21541 H HB   . ILE   B  1 628 ? 49.968 12.944  -12.854 0.00 35.93  ? 654  ILE   B HB   1 
ATOM   21542 H HG12 . ILE   B  1 628 ? 49.582 10.895  -15.051 0.00 35.49  ? 654  ILE   B HG12 1 
ATOM   21543 H HG13 . ILE   B  1 628 ? 48.968 12.550  -15.249 0.00 35.67  ? 654  ILE   B HG13 1 
ATOM   21544 H HG21 . ILE   B  1 628 ? 51.178 10.655  -12.896 0.00 35.33  ? 654  ILE   B HG21 1 
ATOM   21545 H HG22 . ILE   B  1 628 ? 50.272 11.044  -11.423 0.00 35.93  ? 654  ILE   B HG22 1 
ATOM   21546 H HG23 . ILE   B  1 628 ? 49.569 9.943   -12.631 0.00 35.20  ? 654  ILE   B HG23 1 
ATOM   21547 H HD11 . ILE   B  1 628 ? 51.231 11.895  -16.202 0.00 36.55  ? 654  ILE   B HD11 1 
ATOM   21548 H HD12 . ILE   B  1 628 ? 51.025 13.456  -15.373 0.00 37.21  ? 654  ILE   B HD12 1 
ATOM   21549 H HD13 . ILE   B  1 628 ? 51.825 12.105  -14.535 0.00 37.20  ? 654  ILE   B HD13 1 
ATOM   21550 N N    . PRO   B  1 629 ? 47.234 11.040  -10.703 1.00 27.95  ? 655  PRO   B N    1 
ATOM   21551 C CA   . PRO   B  1 629 ? 47.092 11.103  -9.234  1.00 27.34  ? 655  PRO   B CA   1 
ATOM   21552 C C    . PRO   B  1 629 ? 48.447 11.323  -8.573  1.00 26.96  ? 655  PRO   B C    1 
ATOM   21553 O O    . PRO   B  1 629 ? 49.444 10.770  -9.032  1.00 26.70  ? 655  PRO   B O    1 
ATOM   21554 C CB   . PRO   B  1 629 ? 46.511 9.732   -8.866  1.00 27.99  ? 655  PRO   B CB   1 
ATOM   21555 C CG   . PRO   B  1 629 ? 45.930 9.204   -10.108 1.00 28.53  ? 655  PRO   B CG   1 
ATOM   21556 C CD   . PRO   B  1 629 ? 46.741 9.753   -11.231 1.00 27.47  ? 655  PRO   B CD   1 
ATOM   21557 H HA   . PRO   B  1 629 ? 46.397 11.891  -8.945  0.00 36.05  ? 655  PRO   B HA   1 
ATOM   21558 H HB2  . PRO   B  1 629 ? 47.308 9.082   -8.506  0.00 36.57  ? 655  PRO   B HB2  1 
ATOM   21559 H HB3  . PRO   B  1 629 ? 45.743 9.853   -8.104  0.00 36.82  ? 655  PRO   B HB3  1 
ATOM   21560 H HG2  . PRO   B  1 629 ? 45.982 8.116   -10.099 0.00 36.36  ? 655  PRO   B HG2  1 
ATOM   21561 H HG3  . PRO   B  1 629 ? 44.894 9.532   -10.192 0.00 36.52  ? 655  PRO   B HG3  1 
ATOM   21562 H HD2  . PRO   B  1 629 ? 47.571 9.089   -11.468 0.00 34.69  ? 655  PRO   B HD2  1 
ATOM   21563 H HD3  . PRO   B  1 629 ? 46.092 9.908   -12.092 0.00 34.54  ? 655  PRO   B HD3  1 
ATOM   21564 N N    . ASN   B  1 630 ? 48.510 12.155  -7.531  1.00 26.84  ? 656  ASN   B N    1 
ATOM   21565 C CA   . ASN   B  1 630 ? 49.781 12.465  -6.870  1.00 27.08  ? 656  ASN   B CA   1 
ATOM   21566 C C    . ASN   B  1 630 ? 50.560 11.210  -6.438  1.00 27.96  ? 656  ASN   B C    1 
ATOM   21567 O O    . ASN   B  1 630 ? 51.762 11.119  -6.690  1.00 27.82  ? 656  ASN   B O    1 
ATOM   21568 C CB   . ASN   B  1 630 ? 49.532 13.387  -5.674  1.00 27.56  ? 656  ASN   B CB   1 
ATOM   21569 C CG   . ASN   B  1 630 ? 48.940 14.715  -6.089  1.00 29.85  ? 656  ASN   B CG   1 
ATOM   21570 O OD1  . ASN   B  1 630 ? 49.369 15.328  -7.076  1.00 30.48  ? 656  ASN   B OD1  1 
ATOM   21571 N ND2  . ASN   B  1 630 ? 47.943 15.196  -5.359  1.00 30.08  ? 656  ASN   B ND2  1 
ATOM   21572 H H    . ASN   B  1 630 ? 47.695 12.598  -7.120  0.00 36.47  ? 656  ASN   B H    1 
ATOM   21573 H HA   . ASN   B  1 630 ? 50.410 13.001  -7.579  0.00 36.79  ? 656  ASN   B HA   1 
ATOM   21574 H HB2  . ASN   B  1 630 ? 48.847 12.892  -4.988  0.00 38.49  ? 656  ASN   B HB2  1 
ATOM   21575 H HB3  . ASN   B  1 630 ? 50.480 13.584  -5.176  0.00 38.68  ? 656  ASN   B HB3  1 
ATOM   21576 H HD21 . ASN   B  1 630 ? 47.521 16.084  -5.612  0.00 41.90  ? 656  ASN   B HD21 1 
ATOM   21577 H HD22 . ASN   B  1 630 ? 47.596 14.689  -4.552  0.00 42.08  ? 656  ASN   B HD22 1 
ATOM   21578 N N    . GLU   B  1 631 ? 49.856 10.210  -5.889  1.00 28.50  ? 657  GLU   B N    1 
ATOM   21579 C CA   . GLU   B  1 631 ? 50.479 8.959   -5.453  1.00 29.80  ? 657  GLU   B CA   1 
ATOM   21580 C C    . GLU   B  1 631 ? 51.040 8.181   -6.649  1.00 29.46  ? 657  GLU   B C    1 
ATOM   21581 O O    . GLU   B  1 631 ? 52.099 7.568   -6.517  1.00 29.29  ? 657  GLU   B O    1 
ATOM   21582 C CB   . GLU   B  1 631 ? 49.449 8.103   -4.700  1.00 33.83  ? 657  GLU   B CB   1 
ATOM   21583 C CG   . GLU   B  1 631 ? 50.008 6.880   -3.992  1.00 41.21  ? 657  GLU   B CG   1 
ATOM   21584 C CD   . GLU   B  1 631 ? 48.982 6.108   -3.174  1.00 49.20  ? 657  GLU   B CD   1 
ATOM   21585 O OE1  . GLU   B  1 631 ? 47.765 6.380   -3.319  1.00 49.69  ? 657  GLU   B OE1  1 
ATOM   21586 O OE2  . GLU   B  1 631 ? 49.401 5.225   -2.388  1.00 51.20  ? 657  GLU   B OE2  1 
ATOM   21587 H H    . GLU   B  1 631 ? 48.852 10.238  -5.737  0.00 38.73  ? 657  GLU   B H    1 
ATOM   21588 H HA   . GLU   B  1 631 ? 51.301 9.182   -4.775  0.00 40.81  ? 657  GLU   B HA   1 
ATOM   21589 H HB2  . GLU   B  1 631 ? 48.971 8.722   -3.943  0.00 45.79  ? 657  GLU   B HB2  1 
ATOM   21590 H HB3  . GLU   B  1 631 ? 48.703 7.758   -5.415  0.00 44.90  ? 657  GLU   B HB3  1 
ATOM   21591 H HG2  . GLU   B  1 631 ? 50.412 6.192   -4.732  0.00 54.05  ? 657  GLU   B HG2  1 
ATOM   21592 H HG3  . GLU   B  1 631 ? 50.799 7.200   -3.316  0.00 54.93  ? 657  GLU   B HG3  1 
ATOM   21593 N N    . ALA   B  1 632 ? 50.337 8.195   -7.810  1.00 28.64  ? 658  ALA   B N    1 
ATOM   21594 C CA   . ALA   B  1 632 ? 50.835 7.500   -8.996  1.00 28.43  ? 658  ALA   B CA   1 
ATOM   21595 C C    . ALA   B  1 632 ? 52.088 8.177   -9.529  1.00 28.06  ? 658  ALA   B C    1 
ATOM   21596 O O    . ALA   B  1 632 ? 53.007 7.463   -9.933  1.00 28.75  ? 658  ALA   B O    1 
ATOM   21597 C CB   . ALA   B  1 632 ? 49.776 7.450   -10.087 1.00 29.01  ? 658  ALA   B CB   1 
ATOM   21598 H H    . ALA   B  1 632 ? 49.444 8.656   -7.948  0.00 37.66  ? 658  ALA   B H    1 
ATOM   21599 H HA   . ALA   B  1 632 ? 51.079 6.473   -8.727  0.00 36.90  ? 658  ALA   B HA   1 
ATOM   21600 H HB1  . ALA   B  1 632 ? 50.162 6.876   -10.928 0.00 36.61  ? 658  ALA   B HB1  1 
ATOM   21601 H HB2  . ALA   B  1 632 ? 48.878 6.978   -9.694  0.00 37.07  ? 658  ALA   B HB2  1 
ATOM   21602 H HB3  . ALA   B  1 632 ? 49.553 8.468   -10.405 0.00 36.99  ? 658  ALA   B HB3  1 
ATOM   21603 N N    . PHE   B  1 633 ? 52.156 9.529   -9.532  1.00 27.11  ? 659  PHE   B N    1 
ATOM   21604 C CA   . PHE   B  1 633 ? 53.365 10.217  -10.018 1.00 27.75  ? 659  PHE   B CA   1 
ATOM   21605 C C    . PHE   B  1 633 ? 54.544 9.903   -9.089  1.00 28.00  ? 659  PHE   B C    1 
ATOM   21606 O O    . PHE   B  1 633 ? 55.647 9.638   -9.557  1.00 27.47  ? 659  PHE   B O    1 
ATOM   21607 C CB   . PHE   B  1 633 ? 53.165 11.745  -10.098 1.00 27.87  ? 659  PHE   B CB   1 
ATOM   21608 C CG   . PHE   B  1 633 ? 54.256 12.452  -10.873 1.00 28.84  ? 659  PHE   B CG   1 
ATOM   21609 C CD1  . PHE   B  1 633 ? 55.417 12.874  -10.243 1.00 29.62  ? 659  PHE   B CD1  1 
ATOM   21610 C CD2  . PHE   B  1 633 ? 54.152 12.632  -12.241 1.00 29.84  ? 659  PHE   B CD2  1 
ATOM   21611 C CE1  . PHE   B  1 633 ? 56.448 13.461  -10.971 1.00 30.46  ? 659  PHE   B CE1  1 
ATOM   21612 C CE2  . PHE   B  1 633 ? 55.171 13.250  -12.959 1.00 30.66  ? 659  PHE   B CE2  1 
ATOM   21613 C CZ   . PHE   B  1 633 ? 56.314 13.655  -12.319 1.00 30.44  ? 659  PHE   B CZ   1 
ATOM   21614 H H    . PHE   B  1 633 ? 51.419 10.154  -9.224  0.00 35.61  ? 659  PHE   B H    1 
ATOM   21615 H HA   . PHE   B  1 633 ? 53.608 9.849   -11.014 0.00 35.76  ? 659  PHE   B HA   1 
ATOM   21616 H HB2  . PHE   B  1 633 ? 52.218 11.961  -10.589 0.00 36.31  ? 659  PHE   B HB2  1 
ATOM   21617 H HB3  . PHE   B  1 633 ? 53.157 12.150  -9.087  0.00 37.12  ? 659  PHE   B HB3  1 
ATOM   21618 H HD1  . PHE   B  1 633 ? 55.535 12.713  -9.184  0.00 39.60  ? 659  PHE   B HD1  1 
ATOM   21619 H HD2  . PHE   B  1 633 ? 53.263 12.309  -12.753 0.00 37.91  ? 659  PHE   B HD2  1 
ATOM   21620 H HE1  . PHE   B  1 633 ? 57.336 13.799  -10.466 0.00 40.51  ? 659  PHE   B HE1  1 
ATOM   21621 H HE2  . PHE   B  1 633 ? 55.071 13.394  -14.021 0.00 38.79  ? 659  PHE   B HE2  1 
ATOM   21622 H HZ   . PHE   B  1 633 ? 57.101 14.138  -12.876 0.00 39.44  ? 659  PHE   B HZ   1 
ATOM   21623 N N    . LEU   B  1 634 ? 54.301 9.920   -7.780  1.00 28.38  ? 660  LEU   B N    1 
ATOM   21624 C CA   . LEU   B  1 634 ? 55.331 9.602   -6.804  1.00 29.66  ? 660  LEU   B CA   1 
ATOM   21625 C C    . LEU   B  1 634 ? 55.839 8.170   -6.910  1.00 29.29  ? 660  LEU   B C    1 
ATOM   21626 O O    . LEU   B  1 634 ? 56.950 7.911   -6.452  1.00 29.96  ? 660  LEU   B O    1 
ATOM   21627 C CB   . LEU   B  1 634 ? 54.826 9.865   -5.369  1.00 30.49  ? 660  LEU   B CB   1 
ATOM   21628 C CG   . LEU   B  1 634 ? 54.678 11.331  -4.971  1.00 33.06  ? 660  LEU   B CG   1 
ATOM   21629 C CD1  . LEU   B  1 634 ? 54.160 11.463  -3.534  1.00 33.52  ? 660  LEU   B CD1  1 
ATOM   21630 C CD2  . LEU   B  1 634 ? 55.998 12.047  -5.086  1.00 33.89  ? 660  LEU   B CD2  1 
ATOM   21631 H H    . LEU   B  1 634 ? 53.410 10.173  -7.364  0.00 38.22  ? 660  LEU   B H    1 
ATOM   21632 H HA   . LEU   B  1 634 ? 56.189 10.239  -7.013  0.00 40.35  ? 660  LEU   B HA   1 
ATOM   21633 H HB2  . LEU   B  1 634 ? 53.851 9.395   -5.250  0.00 41.74  ? 660  LEU   B HB2  1 
ATOM   21634 H HB3  . LEU   B  1 634 ? 55.524 9.404   -4.671  0.00 42.30  ? 660  LEU   B HB3  1 
ATOM   21635 H HG   . LEU   B  1 634 ? 53.967 11.816  -5.638  0.00 45.06  ? 660  LEU   B HG   1 
ATOM   21636 H HD11 . LEU   B  1 634 ? 53.970 12.513  -3.317  0.00 46.97  ? 660  LEU   B HD11 1 
ATOM   21637 H HD12 . LEU   B  1 634 ? 53.239 10.890  -3.436  0.00 46.48  ? 660  LEU   B HD12 1 
ATOM   21638 H HD13 . LEU   B  1 634 ? 54.913 11.076  -2.850  0.00 47.09  ? 660  LEU   B HD13 1 
ATOM   21639 H HD21 . LEU   B  1 634 ? 56.127 12.731  -4.248  0.00 47.31  ? 660  LEU   B HD21 1 
ATOM   21640 H HD22 . LEU   B  1 634 ? 56.781 11.292  -5.077  0.00 46.70  ? 660  LEU   B HD22 1 
ATOM   21641 H HD23 . LEU   B  1 634 ? 56.028 12.587  -6.030  0.00 46.33  ? 660  LEU   B HD23 1 
ATOM   21642 N N    . ASN   B  1 635 ? 55.048 7.244   -7.489  1.00 28.03  ? 661  ASN   B N    1 
ATOM   21643 C CA   . ASN   B  1 635 ? 55.486 5.860   -7.662  1.00 27.31  ? 661  ASN   B CA   1 
ATOM   21644 C C    . ASN   B  1 635 ? 56.196 5.617   -8.995  1.00 26.95  ? 661  ASN   B C    1 
ATOM   21645 O O    . ASN   B  1 635 ? 56.529 4.466   -9.277  1.00 26.70  ? 661  ASN   B O    1 
ATOM   21646 C CB   . ASN   B  1 635 ? 54.330 4.872   -7.438  1.00 27.64  ? 661  ASN   B CB   1 
ATOM   21647 C CG   . ASN   B  1 635 ? 53.797 4.792   -6.017  1.00 29.97  ? 661  ASN   B CG   1 
ATOM   21648 O OD1  . ASN   B  1 635 ? 52.618 4.488   -5.805  1.00 31.32  ? 661  ASN   B OD1  1 
ATOM   21649 N ND2  . ASN   B  1 635 ? 54.615 5.017   -4.983  1.00 29.92  ? 661  ASN   B ND2  1 
ATOM   21650 H H    . ASN   B  1 635 ? 54.108 7.412   -7.834  0.00 37.28  ? 661  ASN   B H    1 
ATOM   21651 H HA   . ASN   B  1 635 ? 56.264 5.637   -6.935  0.00 37.01  ? 661  ASN   B HA   1 
ATOM   21652 H HB2  . ASN   B  1 635 ? 53.498 5.152   -8.084  0.00 36.40  ? 661  ASN   B HB2  1 
ATOM   21653 H HB3  . ASN   B  1 635 ? 54.663 3.868   -7.695  0.00 36.65  ? 661  ASN   B HB3  1 
ATOM   21654 H HD21 . ASN   B  1 635 ? 54.229 4.956   -4.046  0.00 41.20  ? 661  ASN   B HD21 1 
ATOM   21655 H HD22 . ASN   B  1 635 ? 55.608 5.200   -5.076  0.00 40.91  ? 661  ASN   B HD22 1 
ATOM   21656 N N    . LEU   B  1 636 ? 56.521 6.673   -9.764  1.00 26.62  ? 662  LEU   B N    1 
ATOM   21657 C CA   . LEU   B  1 636 ? 57.333 6.493   -10.962 1.00 27.43  ? 662  LEU   B CA   1 
ATOM   21658 C C    . LEU   B  1 636 ? 58.780 6.223   -10.459 1.00 28.14  ? 662  LEU   B C    1 
ATOM   21659 O O    . LEU   B  1 636 ? 59.154 6.697   -9.376  1.00 28.35  ? 662  LEU   B O    1 
ATOM   21660 C CB   . LEU   B  1 636 ? 57.280 7.718   -11.877 1.00 27.44  ? 662  LEU   B CB   1 
ATOM   21661 C CG   . LEU   B  1 636 ? 55.895 8.069   -12.446 1.00 29.03  ? 662  LEU   B CG   1 
ATOM   21662 C CD1  . LEU   B  1 636 ? 55.970 9.331   -13.309 1.00 30.08  ? 662  LEU   B CD1  1 
ATOM   21663 C CD2  . LEU   B  1 636 ? 55.309 6.915   -13.265 1.00 29.21  ? 662  LEU   B CD2  1 
ATOM   21664 H H    . LEU   B  1 636 ? 56.248 7.637   -9.602  0.00 35.11  ? 662  LEU   B H    1 
ATOM   21665 H HA   . LEU   B  1 636 ? 56.953 5.631   -11.505 0.00 35.15  ? 662  LEU   B HA   1 
ATOM   21666 H HB2  . LEU   B  1 636 ? 57.628 8.585   -11.316 0.00 35.66  ? 662  LEU   B HB2  1 
ATOM   21667 H HB3  . LEU   B  1 636 ? 57.944 7.545   -12.722 0.00 34.98  ? 662  LEU   B HB3  1 
ATOM   21668 H HG   . LEU   B  1 636 ? 55.216 8.268   -11.618 0.00 37.03  ? 662  LEU   B HG   1 
ATOM   21669 H HD11 . LEU   B  1 636 ? 54.968 9.593   -13.646 0.00 37.59  ? 662  LEU   B HD11 1 
ATOM   21670 H HD12 . LEU   B  1 636 ? 56.382 10.143  -12.712 0.00 38.25  ? 662  LEU   B HD12 1 
ATOM   21671 H HD13 . LEU   B  1 636 ? 56.615 9.138   -14.164 0.00 37.54  ? 662  LEU   B HD13 1 
ATOM   21672 H HD21 . LEU   B  1 636 ? 54.467 7.286   -13.846 0.00 36.12  ? 662  LEU   B HD21 1 
ATOM   21673 H HD22 . LEU   B  1 636 ? 56.079 6.522   -13.927 0.00 36.21  ? 662  LEU   B HD22 1 
ATOM   21674 H HD23 . LEU   B  1 636 ? 54.965 6.134   -12.589 0.00 36.57  ? 662  LEU   B HD23 1 
ATOM   21675 N N    . PRO   B  1 637 ? 59.576 5.405   -11.164 1.00 28.60  ? 663  PRO   B N    1 
ATOM   21676 C CA   . PRO   B  1 637 ? 60.940 5.101   -10.667 1.00 28.61  ? 663  PRO   B CA   1 
ATOM   21677 C C    . PRO   B  1 637 ? 61.780 6.340   -10.382 1.00 28.29  ? 663  PRO   B C    1 
ATOM   21678 O O    . PRO   B  1 637 ? 61.891 7.207   -11.247 1.00 27.94  ? 663  PRO   B O    1 
ATOM   21679 C CB   . PRO   B  1 637 ? 61.566 4.275   -11.799 1.00 29.38  ? 663  PRO   B CB   1 
ATOM   21680 C CG   . PRO   B  1 637 ? 60.426 3.782   -12.593 1.00 29.92  ? 663  PRO   B CG   1 
ATOM   21681 C CD   . PRO   B  1 637 ? 59.298 4.726   -12.447 1.00 28.12  ? 663  PRO   B CD   1 
ATOM   21682 H HA   . PRO   B  1 637 ? 60.877 4.482   -9.773  0.00 38.02  ? 663  PRO   B HA   1 
ATOM   21683 H HB2  . PRO   B  1 637 ? 62.217 4.901   -12.409 0.00 38.08  ? 663  PRO   B HB2  1 
ATOM   21684 H HB3  . PRO   B  1 637 ? 62.123 3.439   -11.374 0.00 38.45  ? 663  PRO   B HB3  1 
ATOM   21685 H HG2  . PRO   B  1 637 ? 60.700 3.716   -13.643 0.00 37.81  ? 663  PRO   B HG2  1 
ATOM   21686 H HG3  . PRO   B  1 637 ? 60.138 2.798   -12.224 0.00 38.27  ? 663  PRO   B HG3  1 
ATOM   21687 H HD2  . PRO   B  1 637 ? 59.289 5.444   -13.267 0.00 35.61  ? 663  PRO   B HD2  1 
ATOM   21688 H HD3  . PRO   B  1 637 ? 58.376 4.148   -12.407 0.00 35.73  ? 663  PRO   B HD3  1 
ATOM   21689 N N    . ALA   B  1 638 ? 62.348 6.444   -9.161  1.00 28.17  ? 664  ALA   B N    1 
ATOM   21690 C CA   . ALA   B  1 638 ? 63.198 7.584   -8.798  1.00 28.87  ? 664  ALA   B CA   1 
ATOM   21691 C C    . ALA   B  1 638 ? 64.500 7.665   -9.646  1.00 28.84  ? 664  ALA   B C    1 
ATOM   21692 O O    . ALA   B  1 638 ? 65.174 8.696   -9.644  1.00 29.16  ? 664  ALA   B O    1 
ATOM   21693 C CB   . ALA   B  1 638 ? 63.546 7.519   -7.317  1.00 29.22  ? 664  ALA   B CB   1 
ATOM   21694 H H    . ALA   B  1 638 ? 62.233 5.769   -8.412  0.00 38.57  ? 664  ALA   B H    1 
ATOM   21695 H HA   . ALA   B  1 638 ? 62.641 8.505   -8.967  0.00 39.51  ? 664  ALA   B HA   1 
ATOM   21696 H HB1  . ALA   B  1 638 ? 64.176 8.371   -7.065  0.00 41.29  ? 664  ALA   B HB1  1 
ATOM   21697 H HB2  . ALA   B  1 638 ? 62.625 7.554   -6.738  0.00 40.95  ? 664  ALA   B HB2  1 
ATOM   21698 H HB3  . ALA   B  1 638 ? 64.079 6.590   -7.119  0.00 41.04  ? 664  ALA   B HB3  1 
ATOM   21699 N N    . SER   B  1 639 ? 64.826 6.612   -10.394 1.00 28.36  ? 665  SER   B N    1 
ATOM   21700 C CA   . SER   B  1 639 ? 65.986 6.587   -11.276 1.00 29.03  ? 665  SER   B CA   1 
ATOM   21701 C C    . SER   B  1 639 ? 65.759 7.353   -12.602 1.00 28.41  ? 665  SER   B C    1 
ATOM   21702 O O    . SER   B  1 639 ? 66.716 7.536   -13.353 1.00 28.81  ? 665  SER   B O    1 
ATOM   21703 C CB   . SER   B  1 639 ? 66.355 5.139   -11.589 1.00 31.08  ? 665  SER   B CB   1 
ATOM   21704 O OG   . SER   B  1 639 ? 65.218 4.398   -12.008 1.00 33.12  ? 665  SER   B OG   1 
ATOM   21705 H H    . SER   B  1 639 ? 64.301 5.744   -10.412 0.00 38.36  ? 665  SER   B H    1 
ATOM   21706 H HA   . SER   B  1 639 ? 66.839 7.037   -10.768 0.00 39.82  ? 665  SER   B HA   1 
ATOM   21707 H HB2  . SER   B  1 639 ? 67.104 5.117   -12.379 0.00 41.45  ? 665  SER   B HB2  1 
ATOM   21708 H HB3  . SER   B  1 639 ? 66.758 4.678   -10.688 0.00 42.12  ? 665  SER   B HB3  1 
ATOM   21709 H HG   . SER   B  1 639 ? 65.077 4.516   -12.984 0.00 43.02  ? 665  SER   B HG   1 
ATOM   21710 N N    . LEU   B  1 640 ? 64.521 7.808   -12.904 1.00 27.71  ? 666  LEU   B N    1 
ATOM   21711 C CA   . LEU   B  1 640 ? 64.246 8.493   -14.175 1.00 27.54  ? 666  LEU   B CA   1 
ATOM   21712 C C    . LEU   B  1 640 ? 65.153 9.697   -14.509 1.00 27.47  ? 666  LEU   B C    1 
ATOM   21713 O O    . LEU   B  1 640 ? 65.377 10.562  -13.667 1.00 27.83  ? 666  LEU   B O    1 
ATOM   21714 C CB   . LEU   B  1 640 ? 62.778 8.949   -14.256 1.00 27.58  ? 666  LEU   B CB   1 
ATOM   21715 C CG   . LEU   B  1 640 ? 61.700 7.871   -14.432 1.00 28.81  ? 666  LEU   B CG   1 
ATOM   21716 C CD1  . LEU   B  1 640 ? 60.312 8.505   -14.407 1.00 28.52  ? 666  LEU   B CD1  1 
ATOM   21717 C CD2  . LEU   B  1 640 ? 61.881 7.096   -15.733 1.00 29.80  ? 666  LEU   B CD2  1 
ATOM   21718 H H    . LEU   B  1 640 ? 63.704 7.729   -12.305 0.00 36.72  ? 666  LEU   B H    1 
ATOM   21719 H HA   . LEU   B  1 640 ? 64.383 7.768   -14.970 0.00 35.52  ? 666  LEU   B HA   1 
ATOM   21720 H HB2  . LEU   B  1 640 ? 62.542 9.492   -13.342 0.00 36.03  ? 666  LEU   B HB2  1 
ATOM   21721 H HB3  . LEU   B  1 640 ? 62.689 9.632   -15.100 0.00 35.32  ? 666  LEU   B HB3  1 
ATOM   21722 H HG   . LEU   B  1 640 ? 61.760 7.160   -13.608 0.00 36.95  ? 666  LEU   B HG   1 
ATOM   21723 H HD11 . LEU   B  1 640 ? 59.559 7.718   -14.440 0.00 35.87  ? 666  LEU   B HD11 1 
ATOM   21724 H HD12 . LEU   B  1 640 ? 60.203 9.081   -13.490 0.00 36.55  ? 666  LEU   B HD12 1 
ATOM   21725 H HD13 . LEU   B  1 640 ? 60.208 9.160   -15.270 0.00 35.82  ? 666  LEU   B HD13 1 
ATOM   21726 H HD21 . LEU   B  1 640 ? 60.953 6.566   -15.932 0.00 36.96  ? 666  LEU   B HD21 1 
ATOM   21727 H HD22 . LEU   B  1 640 ? 62.103 7.795   -16.539 0.00 37.08  ? 666  LEU   B HD22 1 
ATOM   21728 H HD23 . LEU   B  1 640 ? 62.686 6.371   -15.620 0.00 37.44  ? 666  LEU   B HD23 1 
ATOM   21729 N N    . THR   B  1 641 ? 65.667 9.739   -15.741 1.00 26.90  ? 667  THR   B N    1 
ATOM   21730 C CA   . THR   B  1 641 ? 66.427 10.883  -16.264 1.00 27.01  ? 667  THR   B CA   1 
ATOM   21731 C C    . THR   B  1 641 ? 65.612 11.609  -17.371 1.00 26.74  ? 667  THR   B C    1 
ATOM   21732 O O    . THR   B  1 641 ? 65.821 12.800  -17.597 1.00 27.58  ? 667  THR   B O    1 
ATOM   21733 C CB   . THR   B  1 641 ? 67.820 10.479  -16.776 1.00 28.35  ? 667  THR   B CB   1 
ATOM   21734 O OG1  . THR   B  1 641 ? 67.689 9.714   -17.976 1.00 30.08  ? 667  THR   B OG1  1 
ATOM   21735 C CG2  . THR   B  1 641 ? 68.633 9.719   -15.733 1.00 28.16  ? 667  THR   B CG2  1 
ATOM   21736 H H    . THR   B  1 641 ? 65.593 8.978   -16.409 0.00 34.59  ? 667  THR   B H    1 
ATOM   21737 H HA   . THR   B  1 641 ? 66.615 11.601  -15.469 0.00 35.76  ? 667  THR   B HA   1 
ATOM   21738 H HB   . THR   B  1 641 ? 68.369 11.392  -17.010 0.00 37.18  ? 667  THR   B HB   1 
ATOM   21739 H HG1  . THR   B  1 641 ? 66.961 9.045   -17.895 0.00 38.19  ? 667  THR   B HG1  1 
ATOM   21740 H HG21 . THR   B  1 641 ? 69.639 9.540   -16.112 0.00 37.46  ? 667  THR   B HG21 1 
ATOM   21741 H HG22 . THR   B  1 641 ? 68.698 10.311  -14.823 0.00 37.84  ? 667  THR   B HG22 1 
ATOM   21742 H HG23 . THR   B  1 641 ? 68.166 8.761   -15.506 0.00 37.19  ? 667  THR   B HG23 1 
ATOM   21743 N N    . GLU   B  1 642 ? 64.702 10.904  -18.060 1.00 25.78  ? 668  GLU   B N    1 
ATOM   21744 C CA   . GLU   B  1 642 ? 63.906 11.460  -19.149 1.00 25.70  ? 668  GLU   B CA   1 
ATOM   21745 C C    . GLU   B  1 642 ? 62.463 10.988  -19.018 1.00 25.78  ? 668  GLU   B C    1 
ATOM   21746 O O    . GLU   B  1 642 ? 62.212 9.789   -18.986 1.00 26.07  ? 668  GLU   B O    1 
ATOM   21747 C CB   . GLU   B  1 642 ? 64.523 10.939  -20.437 1.00 28.25  ? 668  GLU   B CB   1 
ATOM   21748 C CG   . GLU   B  1 642 ? 63.880 11.393  -21.725 1.00 33.02  ? 668  GLU   B CG   1 
ATOM   21749 C CD   . GLU   B  1 642 ? 64.627 10.952  -22.968 1.00 37.49  ? 668  GLU   B CD   1 
ATOM   21750 O OE1  . GLU   B  1 642 ? 65.774 10.460  -22.841 1.00 37.99  ? 668  GLU   B OE1  1 
ATOM   21751 O OE2  . GLU   B  1 642 ? 64.071 11.122  -24.078 1.00 38.89  ? 668  GLU   B OE2  1 
ATOM   21752 H H    . GLU   B  1 642 ? 64.496 9.923   -17.900 0.00 32.50  ? 668  GLU   B H    1 
ATOM   21753 H HA   . GLU   B  1 642 ? 63.931 12.548  -19.157 0.00 32.19  ? 668  GLU   B HA   1 
ATOM   21754 H HB2  . GLU   B  1 642 ? 65.559 11.274  -20.450 0.00 34.95  ? 668  GLU   B HB2  1 
ATOM   21755 H HB3  . GLU   B  1 642 ? 64.494 9.851   -20.422 0.00 34.50  ? 668  GLU   B HB3  1 
ATOM   21756 H HG2  . GLU   B  1 642 ? 62.867 11.000  -21.794 0.00 39.58  ? 668  GLU   B HG2  1 
ATOM   21757 H HG3  . GLU   B  1 642 ? 63.863 12.481  -21.724 0.00 40.04  ? 668  GLU   B HG3  1 
ATOM   21758 N N    . LEU   B  1 643 ? 61.515 11.918  -18.929 1.00 25.23  ? 669  LEU   B N    1 
ATOM   21759 C CA   . LEU   B  1 643 ? 60.103 11.579  -18.772 1.00 24.37  ? 669  LEU   B CA   1 
ATOM   21760 C C    . LEU   B  1 643 ? 59.278 12.365  -19.785 1.00 24.33  ? 669  LEU   B C    1 
ATOM   21761 O O    . LEU   B  1 643 ? 59.304 13.604  -19.776 1.00 24.78  ? 669  LEU   B O    1 
ATOM   21762 C CB   . LEU   B  1 643 ? 59.670 11.928  -17.345 1.00 23.86  ? 669  LEU   B CB   1 
ATOM   21763 C CG   . LEU   B  1 643 ? 58.175 11.791  -16.976 1.00 24.89  ? 669  LEU   B CG   1 
ATOM   21764 C CD1  . LEU   B  1 643 ? 57.645 10.364  -17.248 1.00 25.17  ? 669  LEU   B CD1  1 
ATOM   21765 C CD2  . LEU   B  1 643 ? 57.956 12.181  -15.523 1.00 25.07  ? 669  LEU   B CD2  1 
ATOM   21766 H H    . LEU   B  1 643 ? 61.684 12.919  -18.957 0.00 31.30  ? 669  LEU   B H    1 
ATOM   21767 H HA   . LEU   B  1 643 ? 59.934 10.513  -18.928 0.00 29.57  ? 669  LEU   B HA   1 
ATOM   21768 H HB2  . LEU   B  1 643 ? 60.221 11.282  -16.662 0.00 29.98  ? 669  LEU   B HB2  1 
ATOM   21769 H HB3  . LEU   B  1 643 ? 59.945 12.965  -17.157 0.00 30.02  ? 669  LEU   B HB3  1 
ATOM   21770 H HG   . LEU   B  1 643 ? 57.591 12.485  -17.578 0.00 30.63  ? 669  LEU   B HG   1 
ATOM   21771 H HD11 . LEU   B  1 643 ? 56.624 10.288  -16.877 0.00 30.73  ? 669  LEU   B HD11 1 
ATOM   21772 H HD12 . LEU   B  1 643 ? 57.660 10.176  -18.321 0.00 30.33  ? 669  LEU   B HD12 1 
ATOM   21773 H HD13 . LEU   B  1 643 ? 58.282 9.645   -16.736 0.00 30.94  ? 669  LEU   B HD13 1 
ATOM   21774 H HD21 . LEU   B  1 643 ? 56.918 11.995  -15.253 0.00 31.56  ? 669  LEU   B HD21 1 
ATOM   21775 H HD22 . LEU   B  1 643 ? 58.615 11.584  -14.893 0.00 31.89  ? 669  LEU   B HD22 1 
ATOM   21776 H HD23 . LEU   B  1 643 ? 58.185 13.240  -15.404 0.00 31.92  ? 669  LEU   B HD23 1 
ATOM   21777 N N    . HIS   B  1 644 ? 58.549 11.645  -20.659 1.00 23.31  ? 670  HIS   B N    1 
ATOM   21778 C CA   . HIS   B  1 644 ? 57.669 12.275  -21.635 1.00 22.61  ? 670  HIS   B CA   1 
ATOM   21779 C C    . HIS   B  1 644 ? 56.226 12.003  -21.261 1.00 22.03  ? 670  HIS   B C    1 
ATOM   21780 O O    . HIS   B  1 644 ? 55.856 10.866  -20.998 1.00 21.34  ? 670  HIS   B O    1 
ATOM   21781 C CB   . HIS   B  1 644 ? 57.925 11.774  -23.065 1.00 23.44  ? 670  HIS   B CB   1 
ATOM   21782 C CG   . HIS   B  1 644 ? 59.325 11.977  -23.553 1.00 26.17  ? 670  HIS   B CG   1 
ATOM   21783 N ND1  . HIS   B  1 644 ? 59.629 12.966  -24.465 1.00 27.75  ? 670  HIS   B ND1  1 
ATOM   21784 C CD2  . HIS   B  1 644 ? 60.450 11.276  -23.274 1.00 27.20  ? 670  HIS   B CD2  1 
ATOM   21785 C CE1  . HIS   B  1 644 ? 60.931 12.865  -24.686 1.00 28.17  ? 670  HIS   B CE1  1 
ATOM   21786 N NE2  . HIS   B  1 644 ? 61.459 11.847  -24.005 1.00 28.02  ? 670  HIS   B NE2  1 
ATOM   21787 H H    . HIS   B  1 644 ? 58.548 10.631  -20.711 0.00 27.47  ? 670  HIS   B H    1 
ATOM   21788 H HA   . HIS   B  1 644 ? 57.821 13.352  -21.626 0.00 26.68  ? 670  HIS   B HA   1 
ATOM   21789 H HB2  . HIS   B  1 644 ? 57.699 10.714  -23.139 0.00 26.76  ? 670  HIS   B HB2  1 
ATOM   21790 H HB3  . HIS   B  1 644 ? 57.273 12.329  -23.737 0.00 26.78  ? 670  HIS   B HB3  1 
ATOM   21791 H HD2  . HIS   B  1 644 ? 60.536 10.431  -22.607 0.00 31.82  ? 670  HIS   B HD2  1 
ATOM   21792 H HE1  . HIS   B  1 644 ? 61.489 13.521  -25.334 0.00 32.79  ? 670  HIS   B HE1  1 
ATOM   21793 H HE2  . HIS   B  1 644 ? 62.427 11.542  -24.034 0.00 32.85  ? 670  HIS   B HE2  1 
ATOM   21794 N N    . ILE   B  1 645 ? 55.431 13.059  -21.176 1.00 22.15  ? 671  ILE   B N    1 
ATOM   21795 C CA   . ILE   B  1 645 ? 53.988 12.982  -20.930 1.00 22.62  ? 671  ILE   B CA   1 
ATOM   21796 C C    . ILE   B  1 645 ? 53.287 13.916  -21.967 1.00 23.06  ? 671  ILE   B C    1 
ATOM   21797 O O    . ILE   B  1 645 ? 52.230 14.480  -21.691 1.00 24.06  ? 671  ILE   B O    1 
ATOM   21798 C CB   . ILE   B  1 645 ? 53.609 13.372  -19.453 1.00 23.22  ? 671  ILE   B CB   1 
ATOM   21799 C CG1  . ILE   B  1 645 ? 54.736 13.003  -18.413 1.00 23.99  ? 671  ILE   B CG1  1 
ATOM   21800 C CG2  . ILE   B  1 645 ? 52.236 12.757  -19.061 1.00 23.35  ? 671  ILE   B CG2  1 
ATOM   21801 C CD1  . ILE   B  1 645 ? 54.440 13.431  -16.925 1.00 25.57  ? 671  ILE   B CD1  1 
ATOM   21802 H H    . ILE   B  1 645 ? 55.756 14.018  -21.256 0.00 26.13  ? 671  ILE   B H    1 
ATOM   21803 H HA   . ILE   B  1 645 ? 53.655 11.967  -21.143 0.00 26.18  ? 671  ILE   B HA   1 
ATOM   21804 H HB   . ILE   B  1 645 ? 53.487 14.453  -19.420 0.00 27.91  ? 671  ILE   B HB   1 
ATOM   21805 H HG12 . ILE   B  1 645 ? 54.881 11.924  -18.421 0.00 28.82  ? 671  ILE   B HG12 1 
ATOM   21806 H HG13 . ILE   B  1 645 ? 55.662 13.502  -18.694 0.00 29.09  ? 671  ILE   B HG13 1 
ATOM   21807 H HG21 . ILE   B  1 645 ? 51.966 13.072  -18.055 0.00 28.15  ? 671  ILE   B HG21 1 
ATOM   21808 H HG22 . ILE   B  1 645 ? 51.483 13.100  -19.769 0.00 27.54  ? 671  ILE   B HG22 1 
ATOM   21809 H HG23 . ILE   B  1 645 ? 52.313 11.671  -19.098 0.00 27.58  ? 671  ILE   B HG23 1 
ATOM   21810 H HD11 . ILE   B  1 645 ? 55.357 13.341  -16.345 0.00 31.78  ? 671  ILE   B HD11 1 
ATOM   21811 H HD12 . ILE   B  1 645 ? 54.090 14.462  -16.916 0.00 31.67  ? 671  ILE   B HD12 1 
ATOM   21812 H HD13 . ILE   B  1 645 ? 53.678 12.773  -16.509 0.00 31.44  ? 671  ILE   B HD13 1 
ATOM   21813 N N    . ASN   B  1 646 ? 53.878 14.055  -23.161 1.00 22.62  ? 672  ASN   B N    1 
ATOM   21814 C CA   . ASN   B  1 646 ? 53.386 14.923  -24.199 1.00 22.56  ? 672  ASN   B CA   1 
ATOM   21815 C C    . ASN   B  1 646 ? 52.131 14.362  -24.862 1.00 22.80  ? 672  ASN   B C    1 
ATOM   21816 O O    . ASN   B  1 646 ? 51.861 13.176  -24.771 1.00 22.53  ? 672  ASN   B O    1 
ATOM   21817 C CB   . ASN   B  1 646 ? 54.493 15.194  -25.246 1.00 22.95  ? 672  ASN   B CB   1 
ATOM   21818 C CG   . ASN   B  1 646 ? 55.042 13.945  -25.888 1.00 25.70  ? 672  ASN   B CG   1 
ATOM   21819 O OD1  . ASN   B  1 646 ? 55.625 13.084  -25.203 1.00 27.39  ? 672  ASN   B OD1  1 
ATOM   21820 N ND2  . ASN   B  1 646 ? 54.871 13.799  -27.190 1.00 25.32  ? 672  ASN   B ND2  1 
ATOM   21821 H H    . ASN   B  1 646 ? 54.709 13.538  -23.428 0.00 25.85  ? 672  ASN   B H    1 
ATOM   21822 H HA   . ASN   B  1 646 ? 53.122 15.883  -23.759 0.00 26.07  ? 672  ASN   B HA   1 
ATOM   21823 H HB2  . ASN   B  1 646 ? 54.091 15.847  -26.019 0.00 25.98  ? 672  ASN   B HB2  1 
ATOM   21824 H HB3  . ASN   B  1 646 ? 55.322 15.694  -24.747 0.00 26.37  ? 672  ASN   B HB3  1 
ATOM   21825 H HD21 . ASN   B  1 646 ? 55.230 12.970  -27.650 0.00 27.94  ? 672  ASN   B HD21 1 
ATOM   21826 H HD22 . ASN   B  1 646 ? 54.388 14.506  -27.734 0.00 28.14  ? 672  ASN   B HD22 1 
ATOM   21827 N N    . ASP   B  1 647 ? 51.368 15.224  -25.532 1.00 22.62  ? 673  ASP   B N    1 
ATOM   21828 C CA   . ASP   B  1 647 ? 50.173 14.819  -26.257 1.00 23.30  ? 673  ASP   B CA   1 
ATOM   21829 C C    . ASP   B  1 647 ? 49.175 14.016  -25.401 1.00 23.36  ? 673  ASP   B C    1 
ATOM   21830 O O    . ASP   B  1 647 ? 48.733 12.932  -25.761 1.00 23.98  ? 673  ASP   B O    1 
ATOM   21831 C CB   . ASP   B  1 647 ? 50.564 14.093  -27.547 1.00 25.40  ? 673  ASP   B CB   1 
ATOM   21832 C CG   . ASP   B  1 647 ? 51.449 14.958  -28.428 1.00 31.43  ? 673  ASP   B CG   1 
ATOM   21833 O OD1  . ASP   B  1 647 ? 51.164 16.173  -28.547 1.00 32.96  ? 673  ASP   B OD1  1 
ATOM   21834 O OD2  . ASP   B  1 647 ? 52.417 14.428  -28.998 1.00 34.06  ? 673  ASP   B OD2  1 
ATOM   21835 H H    . ASP   B  1 647 ? 51.560 16.219  -25.592 0.00 25.68  ? 673  ASP   B H    1 
ATOM   21836 H HA   . ASP   B  1 647 ? 49.641 15.725  -26.547 0.00 26.13  ? 673  ASP   B HA   1 
ATOM   21837 H HB2  . ASP   B  1 647 ? 51.099 13.174  -27.309 0.00 27.97  ? 673  ASP   B HB2  1 
ATOM   21838 H HB3  . ASP   B  1 647 ? 49.661 13.877  -28.115 0.00 27.92  ? 673  ASP   B HB3  1 
ATOM   21839 N N    . ASN   B  1 648 ? 48.844 14.582  -24.259 1.00 22.97  ? 674  ASN   B N    1 
ATOM   21840 C CA   . ASN   B  1 648 ? 47.790 14.119  -23.360 1.00 23.25  ? 674  ASN   B CA   1 
ATOM   21841 C C    . ASN   B  1 648 ? 46.825 15.350  -23.292 1.00 24.20  ? 674  ASN   B C    1 
ATOM   21842 O O    . ASN   B  1 648 ? 46.821 16.158  -24.228 1.00 23.82  ? 674  ASN   B O    1 
ATOM   21843 C CB   . ASN   B  1 648 ? 48.403 13.670  -22.006 1.00 22.87  ? 674  ASN   B CB   1 
ATOM   21844 C CG   . ASN   B  1 648 ? 48.970 12.274  -22.075 1.00 24.06  ? 674  ASN   B CG   1 
ATOM   21845 O OD1  . ASN   B  1 648 ? 48.210 11.305  -22.090 1.00 24.49  ? 674  ASN   B OD1  1 
ATOM   21846 N ND2  . ASN   B  1 648 ? 50.297 12.129  -22.145 1.00 22.12  ? 674  ASN   B ND2  1 
ATOM   21847 H H    . ASN   B  1 648 ? 49.299 15.417  -23.908 0.00 26.31  ? 674  ASN   B H    1 
ATOM   21848 H HA   . ASN   B  1 648 ? 47.235 13.289  -23.794 0.00 26.27  ? 674  ASN   B HA   1 
ATOM   21849 H HB2  . ASN   B  1 648 ? 49.201 14.359  -21.735 0.00 26.57  ? 674  ASN   B HB2  1 
ATOM   21850 H HB3  . ASN   B  1 648 ? 47.646 13.657  -21.225 0.00 26.57  ? 674  ASN   B HB3  1 
ATOM   21851 H HD21 . ASN   B  1 648 ? 50.701 11.200  -22.194 0.00 24.98  ? 674  ASN   B HD21 1 
ATOM   21852 H HD22 . ASN   B  1 648 ? 50.907 12.942  -22.155 0.00 25.30  ? 674  ASN   B HD22 1 
ATOM   21853 N N    . MET   B  1 649 ? 45.985 15.467  -22.262 1.00 25.44  ? 675  MET   B N    1 
ATOM   21854 C CA   . MET   B  1 649 ? 45.086 16.603  -22.072 1.00 27.57  ? 675  MET   B CA   1 
ATOM   21855 C C    . MET   B  1 649 ? 45.265 17.093  -20.629 1.00 28.21  ? 675  MET   B C    1 
ATOM   21856 O O    . MET   B  1 649 ? 44.279 17.329  -19.926 1.00 28.35  ? 675  MET   B O    1 
ATOM   21857 C CB   . MET   B  1 649 ? 43.632 16.162  -22.317 1.00 30.19  ? 675  MET   B CB   1 
ATOM   21858 C CG   . MET   B  1 649 ? 43.424 15.489  -23.660 1.00 36.38  ? 675  MET   B CG   1 
ATOM   21859 S SD   . MET   B  1 649 ? 41.659 15.340  -24.053 1.00 50.88  ? 675  MET   B SD   1 
ATOM   21860 C CE   . MET   B  1 649 ? 41.696 15.767  -25.791 1.00 52.12  ? 675  MET   B CE   1 
ATOM   21861 H H    . MET   B  1 649 ? 45.869 14.767  -21.537 0.00 29.85  ? 675  MET   B H    1 
ATOM   21862 H HA   . MET   B  1 649 ? 45.321 17.418  -22.755 0.00 32.74  ? 675  MET   B HA   1 
ATOM   21863 H HB2  . MET   B  1 649 ? 43.343 15.448  -21.547 0.00 35.84  ? 675  MET   B HB2  1 
ATOM   21864 H HB3  . MET   B  1 649 ? 42.984 17.036  -22.278 0.00 36.07  ? 675  MET   B HB3  1 
ATOM   21865 H HG2  . MET   B  1 649 ? 43.899 16.083  -24.439 0.00 42.66  ? 675  MET   B HG2  1 
ATOM   21866 H HG3  . MET   B  1 649 ? 43.851 14.487  -23.633 0.00 42.47  ? 675  MET   B HG3  1 
ATOM   21867 H HE1  . MET   B  1 649 ? 40.699 15.638  -26.208 0.00 61.38  ? 675  MET   B HE1  1 
ATOM   21868 H HE2  . MET   B  1 649 ? 42.010 16.805  -25.894 0.00 61.57  ? 675  MET   B HE2  1 
ATOM   21869 H HE3  . MET   B  1 649 ? 42.401 15.112  -26.301 0.00 61.04  ? 675  MET   B HE3  1 
ATOM   21870 N N    . LEU   B  1 650 ? 46.531 17.178  -20.152 1.00 28.04  ? 676  LEU   B N    1 
ATOM   21871 C CA   . LEU   B  1 650 ? 46.791 17.577  -18.775 1.00 28.42  ? 676  LEU   B CA   1 
ATOM   21872 C C    . LEU   B  1 650 ? 46.382 19.017  -18.512 1.00 30.01  ? 676  LEU   B C    1 
ATOM   21873 O O    . LEU   B  1 650 ? 46.851 19.910  -19.202 1.00 29.67  ? 676  LEU   B O    1 
ATOM   21874 C CB   . LEU   B  1 650 ? 48.277 17.411  -18.414 1.00 28.13  ? 676  LEU   B CB   1 
ATOM   21875 C CG   . LEU   B  1 650 ? 48.852 15.991  -18.418 1.00 29.09  ? 676  LEU   B CG   1 
ATOM   21876 C CD1  . LEU   B  1 650 ? 50.376 16.022  -18.237 1.00 29.13  ? 676  LEU   B CD1  1 
ATOM   21877 C CD2  . LEU   B  1 650 ? 48.210 15.125  -17.356 1.00 28.74  ? 676  LEU   B CD2  1 
ATOM   21878 H H    . LEU   B  1 650 ? 47.370 16.989  -20.690 0.00 33.70  ? 676  LEU   B H    1 
ATOM   21879 H HA   . LEU   B  1 650 ? 46.210 16.939  -18.112 0.00 34.98  ? 676  LEU   B HA   1 
ATOM   21880 H HB2  . LEU   B  1 650 ? 48.876 17.998  -19.106 0.00 34.57  ? 676  LEU   B HB2  1 
ATOM   21881 H HB3  . LEU   B  1 650 ? 48.418 17.803  -17.408 0.00 35.08  ? 676  LEU   B HB3  1 
ATOM   21882 H HG   . LEU   B  1 650 ? 48.645 15.538  -19.386 0.00 35.00  ? 676  LEU   B HG   1 
ATOM   21883 H HD11 . LEU   B  1 650 ? 50.762 15.009  -18.335 0.00 35.31  ? 676  LEU   B HD11 1 
ATOM   21884 H HD12 . LEU   B  1 650 ? 50.816 16.662  -19.000 0.00 35.51  ? 676  LEU   B HD12 1 
ATOM   21885 H HD13 . LEU   B  1 650 ? 50.605 16.410  -17.246 0.00 36.03  ? 676  LEU   B HD13 1 
ATOM   21886 H HD21 . LEU   B  1 650 ? 48.786 14.206  -17.258 0.00 34.98  ? 676  LEU   B HD21 1 
ATOM   21887 H HD22 . LEU   B  1 650 ? 48.201 15.661  -16.409 0.00 35.61  ? 676  LEU   B HD22 1 
ATOM   21888 H HD23 . LEU   B  1 650 ? 47.192 14.887  -17.658 0.00 35.01  ? 676  LEU   B HD23 1 
ATOM   21889 N N    . LYS   B  1 651 ? 45.513 19.234  -17.509 1.00 31.83  ? 677  LYS   B N    1 
ATOM   21890 C CA   . LYS   B  1 651 ? 45.092 20.566  -17.072 1.00 34.07  ? 677  LYS   B CA   1 
ATOM   21891 C C    . LYS   B  1 651 ? 45.909 21.019  -15.849 1.00 35.26  ? 677  LYS   B C    1 
ATOM   21892 O O    . LYS   B  1 651 ? 46.064 22.220  -15.646 1.00 36.51  ? 677  LYS   B O    1 
ATOM   21893 C CB   . LYS   B  1 651 ? 43.590 20.590  -16.742 1.00 37.53  ? 677  LYS   B CB   1 
ATOM   21894 C CG   . LYS   B  1 651 ? 42.708 20.454  -17.983 1.00 43.83  ? 677  LYS   B CG   1 
ATOM   21895 C CD   . LYS   B  1 651 ? 41.395 21.231  -17.879 1.00 50.08  ? 677  LYS   B CD   1 
ATOM   21896 C CE   . LYS   B  1 651 ? 40.670 21.295  -19.207 1.00 54.38  ? 677  LYS   B CE   1 
ATOM   21897 N NZ   . LYS   B  1 651 ? 39.274 21.797  -19.055 1.00 57.47  ? 677  LYS   B NZ   1 
ATOM   21898 H H    . LYS   B  1 651 ? 45.079 18.493  -16.969 0.00 39.92  ? 677  LYS   B H    1 
ATOM   21899 H HA   . LYS   B  1 651 ? 45.271 21.293  -17.862 0.00 43.17  ? 677  LYS   B HA   1 
ATOM   21900 H HB2  . LYS   B  1 651 ? 43.356 19.769  -16.066 0.00 47.53  ? 677  LYS   B HB2  1 
ATOM   21901 H HB3  . LYS   B  1 651 ? 43.357 21.535  -16.256 0.00 48.05  ? 677  LYS   B HB3  1 
ATOM   21902 H HG2  . LYS   B  1 651 ? 43.243 20.828  -18.854 0.00 54.53  ? 677  LYS   B HG2  1 
ATOM   21903 H HG3  . LYS   B  1 651 ? 42.461 19.404  -18.125 0.00 54.33  ? 677  LYS   B HG3  1 
ATOM   21904 H HD2  . LYS   B  1 651 ? 40.743 20.742  -17.156 0.00 62.70  ? 677  LYS   B HD2  1 
ATOM   21905 H HD3  . LYS   B  1 651 ? 41.599 22.253  -17.564 0.00 63.05  ? 677  LYS   B HD3  1 
ATOM   21906 H HE2  . LYS   B  1 651 ? 41.204 21.966  -19.877 0.00 67.44  ? 677  LYS   B HE2  1 
ATOM   21907 H HE3  . LYS   B  1 651 ? 40.625 20.296  -19.637 0.00 66.99  ? 677  LYS   B HE3  1 
ATOM   21908 H HZ1  . LYS   B  1 651 ? 38.823 21.852  -19.963 0.00 71.35  ? 677  LYS   B HZ1  1 
ATOM   21909 H HZ2  . LYS   B  1 651 ? 38.742 21.169  -18.460 0.00 71.55  ? 677  LYS   B HZ2  1 
ATOM   21910 H HZ3  . LYS   B  1 651 ? 39.283 22.720  -18.634 0.00 71.99  ? 677  LYS   B HZ3  1 
ATOM   21911 N N    . PHE   B  1 652 ? 46.426 20.072  -15.042 1.00 34.57  ? 678  PHE   B N    1 
ATOM   21912 C CA   . PHE   B  1 652 ? 47.244 20.361  -13.874 1.00 34.12  ? 678  PHE   B CA   1 
ATOM   21913 C C    . PHE   B  1 652 ? 48.498 19.468  -13.875 1.00 32.80  ? 678  PHE   B C    1 
ATOM   21914 O O    . PHE   B  1 652 ? 48.496 18.373  -14.435 1.00 31.99  ? 678  PHE   B O    1 
ATOM   21915 C CB   . PHE   B  1 652 ? 46.427 20.118  -12.585 1.00 34.42  ? 678  PHE   B CB   1 
ATOM   21916 H H    . PHE   B  1 652 ? 46.279 19.075  -15.163 0.00 43.99  ? 678  PHE   B H    1 
ATOM   21917 H HA   . PHE   B  1 652 ? 47.570 21.398  -13.885 0.00 44.69  ? 678  PHE   B HA   1 
ATOM   21918 N N    . PHE   B  1 653 ? 49.569 19.967  -13.265 1.00 32.14  ? 679  PHE   B N    1 
ATOM   21919 C CA   . PHE   B  1 653 ? 50.833 19.245  -13.095 1.00 31.77  ? 679  PHE   B CA   1 
ATOM   21920 C C    . PHE   B  1 653 ? 51.377 19.670  -11.753 1.00 31.89  ? 679  PHE   B C    1 
ATOM   21921 O O    . PHE   B  1 653 ? 51.571 20.866  -11.540 1.00 32.18  ? 679  PHE   B O    1 
ATOM   21922 C CB   . PHE   B  1 653 ? 51.852 19.556  -14.213 1.00 31.07  ? 679  PHE   B CB   1 
ATOM   21923 C CG   . PHE   B  1 653 ? 53.093 18.693  -14.108 1.00 31.05  ? 679  PHE   B CG   1 
ATOM   21924 C CD1  . PHE   B  1 653 ? 53.058 17.357  -14.460 1.00 31.63  ? 679  PHE   B CD1  1 
ATOM   21925 C CD2  . PHE   B  1 653 ? 54.265 19.197  -13.578 1.00 31.67  ? 679  PHE   B CD2  1 
ATOM   21926 C CE1  . PHE   B  1 653 ? 54.184 16.551  -14.320 1.00 32.11  ? 679  PHE   B CE1  1 
ATOM   21927 C CE2  . PHE   B  1 653 ? 55.384 18.385  -13.424 1.00 32.20  ? 679  PHE   B CE2  1 
ATOM   21928 C CZ   . PHE   B  1 653 ? 55.340 17.071  -13.806 1.00 31.86  ? 679  PHE   B CZ   1 
ATOM   21929 H H    . PHE   B  1 653 ? 49.589 20.912  -12.896 0.00 42.60  ? 679  PHE   B H    1 
ATOM   21930 H HA   . PHE   B  1 653 ? 50.657 18.172  -13.075 0.00 41.28  ? 679  PHE   B HA   1 
ATOM   21931 H HB2  . PHE   B  1 653 ? 51.391 19.366  -15.181 0.00 39.98  ? 679  PHE   B HB2  1 
ATOM   21932 H HB3  . PHE   B  1 653 ? 52.153 20.600  -14.150 0.00 40.82  ? 679  PHE   B HB3  1 
ATOM   21933 H HD1  . PHE   B  1 653 ? 52.152 16.940  -14.861 0.00 40.15  ? 679  PHE   B HD1  1 
ATOM   21934 H HD2  . PHE   B  1 653 ? 54.312 20.225  -13.269 0.00 41.99  ? 679  PHE   B HD2  1 
ATOM   21935 H HE1  . PHE   B  1 653 ? 54.148 15.517  -14.616 0.00 40.65  ? 679  PHE   B HE1  1 
ATOM   21936 H HE2  . PHE   B  1 653 ? 56.297 18.797  -13.031 0.00 42.54  ? 679  PHE   B HE2  1 
ATOM   21937 H HZ   . PHE   B  1 653 ? 56.214 16.448  -13.704 0.00 41.19  ? 679  PHE   B HZ   1 
ATOM   21938 N N    . ASN   B  1 654 ? 51.548 18.729  -10.821 1.00 31.78  ? 680  ASN   B N    1 
ATOM   21939 C CA   . ASN   B  1 654 ? 52.018 19.058  -9.479  1.00 31.94  ? 680  ASN   B CA   1 
ATOM   21940 C C    . ASN   B  1 654 ? 53.550 19.129  -9.519  1.00 32.22  ? 680  ASN   B C    1 
ATOM   21941 O O    . ASN   B  1 654 ? 54.229 18.108  -9.439  1.00 32.04  ? 680  ASN   B O    1 
ATOM   21942 C CB   . ASN   B  1 654 ? 51.472 18.034  -8.485  1.00 33.30  ? 680  ASN   B CB   1 
ATOM   21943 C CG   . ASN   B  1 654 ? 51.850 18.237  -7.061  1.00 36.82  ? 680  ASN   B CG   1 
ATOM   21944 O OD1  . ASN   B  1 654 ? 52.553 19.189  -6.725  1.00 36.11  ? 680  ASN   B OD1  1 
ATOM   21945 N ND2  . ASN   B  1 654 ? 51.262 17.441  -6.170  1.00 40.55  ? 680  ASN   B ND2  1 
ATOM   21946 H H    . ASN   B  1 654 ? 51.381 17.739  -10.964 0.00 42.13  ? 680  ASN   B H    1 
ATOM   21947 H HA   . ASN   B  1 654 ? 51.632 20.028  -9.172  0.00 43.85  ? 680  ASN   B HA   1 
ATOM   21948 H HB2  . ASN   B  1 654 ? 50.384 18.051  -8.537  0.00 45.07  ? 680  ASN   B HB2  1 
ATOM   21949 H HB3  . ASN   B  1 654 ? 51.832 17.046  -8.769  0.00 44.79  ? 680  ASN   B HB3  1 
ATOM   21950 H HD21 . ASN   B  1 654 ? 52.136 17.297  -5.705  0.00 55.10  ? 680  ASN   B HD21 1 
ATOM   21951 H HD22 . ASN   B  1 654 ? 50.585 16.725  -6.410  0.00 54.44  ? 680  ASN   B HD22 1 
ATOM   21952 N N    . TRP   B  1 655 ? 54.083 20.347  -9.711  1.00 32.52  ? 681  TRP   B N    1 
ATOM   21953 C CA   . TRP   B  1 655 ? 55.526 20.588  -9.834  1.00 33.32  ? 681  TRP   B CA   1 
ATOM   21954 C C    . TRP   B  1 655 ? 56.314 20.208  -8.580  1.00 33.84  ? 681  TRP   B C    1 
ATOM   21955 O O    . TRP   B  1 655 ? 57.494 19.878  -8.688  1.00 33.50  ? 681  TRP   B O    1 
ATOM   21956 C CB   . TRP   B  1 655 ? 55.796 22.064  -10.170 1.00 32.93  ? 681  TRP   B CB   1 
ATOM   21957 C CG   . TRP   B  1 655 ? 55.197 22.512  -11.470 1.00 32.71  ? 681  TRP   B CG   1 
ATOM   21958 C CD1  . TRP   B  1 655 ? 53.956 23.048  -11.663 1.00 33.22  ? 681  TRP   B CD1  1 
ATOM   21959 C CD2  . TRP   B  1 655 ? 55.775 22.357  -12.772 1.00 32.34  ? 681  TRP   B CD2  1 
ATOM   21960 N NE1  . TRP   B  1 655 ? 53.729 23.238  -13.009 1.00 33.37  ? 681  TRP   B NE1  1 
ATOM   21961 C CE2  . TRP   B  1 655 ? 54.834 22.829  -13.709 1.00 32.97  ? 681  TRP   B CE2  1 
ATOM   21962 C CE3  . TRP   B  1 655 ? 56.993 21.848  -13.240 1.00 32.71  ? 681  TRP   B CE3  1 
ATOM   21963 C CZ2  . TRP   B  1 655 ? 55.096 22.856  -15.078 1.00 33.42  ? 681  TRP   B CZ2  1 
ATOM   21964 C CZ3  . TRP   B  1 655 ? 57.250 21.878  -14.594 1.00 33.35  ? 681  TRP   B CZ3  1 
ATOM   21965 C CH2  . TRP   B  1 655 ? 56.301 22.359  -15.498 1.00 33.61  ? 681  TRP   B CH2  1 
ATOM   21966 H H    . TRP   B  1 655 ? 53.526 21.193  -9.764  0.00 44.84  ? 681  TRP   B H    1 
ATOM   21967 H HA   . TRP   B  1 655 ? 55.909 19.988  -10.657 0.00 45.26  ? 681  TRP   B HA   1 
ATOM   21968 H HB2  . TRP   B  1 655 ? 55.387 22.689  -9.378  0.00 46.25  ? 681  TRP   B HB2  1 
ATOM   21969 H HB3  . TRP   B  1 655 ? 56.873 22.199  -10.235 0.00 45.88  ? 681  TRP   B HB3  1 
ATOM   21970 H HD1  . TRP   B  1 655 ? 53.249 23.269  -10.879 0.00 45.86  ? 681  TRP   B HD1  1 
ATOM   21971 H HE1  . TRP   B  1 655 ? 52.871 23.664  -13.422 0.00 45.02  ? 681  TRP   B HE1  1 
ATOM   21972 H HE3  . TRP   B  1 655 ? 57.731 21.473  -12.550 0.00 44.41  ? 681  TRP   B HE3  1 
ATOM   21973 H HZ2  . TRP   B  1 655 ? 54.368 23.225  -15.782 0.00 44.06  ? 681  TRP   B HZ2  1 
ATOM   21974 H HZ3  . TRP   B  1 655 ? 58.187 21.495  -14.963 0.00 44.20  ? 681  TRP   B HZ3  1 
ATOM   21975 H HH2  . TRP   B  1 655 ? 56.532 22.362  -16.550 0.00 43.92  ? 681  TRP   B HH2  1 
ATOM   21976 N N    . THR   B  1 656 ? 55.678 20.268  -7.398  1.00 34.38  ? 682  THR   B N    1 
ATOM   21977 C CA   . THR   B  1 656 ? 56.332 19.924  -6.131  1.00 35.34  ? 682  THR   B CA   1 
ATOM   21978 C C    . THR   B  1 656 ? 56.887 18.496  -6.119  1.00 34.92  ? 682  THR   B C    1 
ATOM   21979 O O    . THR   B  1 656 ? 57.905 18.242  -5.480  1.00 34.39  ? 682  THR   B O    1 
ATOM   21980 C CB   . THR   B  1 656 ? 55.352 20.114  -4.958  1.00 38.03  ? 682  THR   B CB   1 
ATOM   21981 O OG1  . THR   B  1 656 ? 54.757 21.410  -5.050  1.00 39.94  ? 682  THR   B OG1  1 
ATOM   21982 C CG2  . THR   B  1 656 ? 56.026 19.966  -3.606  1.00 39.03  ? 682  THR   B CG2  1 
ATOM   21983 H H    . THR   B  1 656 ? 54.714 20.567  -7.290  0.00 48.20  ? 682  THR   B H    1 
ATOM   21984 H HA   . THR   B  1 656 ? 57.167 20.605  -5.976  0.00 50.42  ? 682  THR   B HA   1 
ATOM   21985 H HB   . THR   B  1 656 ? 54.570 19.360  -5.029  0.00 53.34  ? 682  THR   B HB   1 
ATOM   21986 H HG1  . THR   B  1 656 ? 55.461 22.103  -5.134  0.00 56.60  ? 682  THR   B HG1  1 
ATOM   21987 H HG21 . THR   B  1 656 ? 55.375 20.356  -2.826  0.00 56.20  ? 682  THR   B HG21 1 
ATOM   21988 H HG22 . THR   B  1 656 ? 56.226 18.917  -3.392  0.00 55.56  ? 682  THR   B HG22 1 
ATOM   21989 H HG23 . THR   B  1 656 ? 56.964 20.517  -3.593  0.00 56.10  ? 682  THR   B HG23 1 
ATOM   21990 N N    . LEU   B  1 657 ? 56.241 17.577  -6.851  1.00 34.95  ? 683  LEU   B N    1 
ATOM   21991 C CA   . LEU   B  1 657 ? 56.636 16.171  -6.888  1.00 35.38  ? 683  LEU   B CA   1 
ATOM   21992 C C    . LEU   B  1 657 ? 57.955 15.906  -7.607  1.00 36.36  ? 683  LEU   B C    1 
ATOM   21993 O O    . LEU   B  1 657 ? 58.508 14.811  -7.448  1.00 37.21  ? 683  LEU   B O    1 
ATOM   21994 C CB   . LEU   B  1 657 ? 55.492 15.339  -7.495  1.00 35.73  ? 683  LEU   B CB   1 
ATOM   21995 C CG   . LEU   B  1 657 ? 54.114 15.494  -6.806  1.00 37.25  ? 683  LEU   B CG   1 
ATOM   21996 C CD1  . LEU   B  1 657 ? 53.073 14.596  -7.432  1.00 38.02  ? 683  LEU   B CD1  1 
ATOM   21997 C CD2  . LEU   B  1 657 ? 54.181 15.270  -5.294  1.00 37.70  ? 683  LEU   B CD2  1 
ATOM   21998 H H    . LEU   B  1 657 ? 55.447 17.784  -7.448  0.00 48.05  ? 683  LEU   B H    1 
ATOM   21999 H HA   . LEU   B  1 657 ? 56.784 15.833  -5.863  0.00 49.06  ? 683  LEU   B HA   1 
ATOM   22000 H HB2  . LEU   B  1 657 ? 55.363 15.660  -8.528  0.00 47.87  ? 683  LEU   B HB2  1 
ATOM   22001 H HB3  . LEU   B  1 657 ? 55.771 14.287  -7.487  0.00 48.11  ? 683  LEU   B HB3  1 
ATOM   22002 H HG   . LEU   B  1 657 ? 53.769 16.515  -6.959  0.00 50.47  ? 683  LEU   B HG   1 
ATOM   22003 H HD11 . LEU   B  1 657 ? 52.103 14.812  -6.986  0.00 50.76  ? 683  LEU   B HD11 1 
ATOM   22004 H HD12 . LEU   B  1 657 ? 53.041 14.785  -8.504  0.00 50.12  ? 683  LEU   B HD12 1 
ATOM   22005 H HD13 . LEU   B  1 657 ? 53.346 13.559  -7.243  0.00 50.50  ? 683  LEU   B HD13 1 
ATOM   22006 H HD21 . LEU   B  1 657 ? 53.168 15.223  -4.898  0.00 51.65  ? 683  LEU   B HD21 1 
ATOM   22007 H HD22 . LEU   B  1 657 ? 54.701 14.334  -5.098  0.00 51.54  ? 683  LEU   B HD22 1 
ATOM   22008 H HD23 . LEU   B  1 657 ? 54.712 16.098  -4.828  0.00 52.12  ? 683  LEU   B HD23 1 
ATOM   22009 N N    . LEU   B  1 658 ? 58.506 16.892  -8.344  1.00 36.25  ? 684  LEU   B N    1 
ATOM   22010 C CA   . LEU   B  1 658 ? 59.814 16.699  -8.984  1.00 36.87  ? 684  LEU   B CA   1 
ATOM   22011 C C    . LEU   B  1 658 ? 60.957 16.543  -7.955  1.00 38.10  ? 684  LEU   B C    1 
ATOM   22012 O O    . LEU   B  1 658 ? 62.038 16.102  -8.338  1.00 38.72  ? 684  LEU   B O    1 
ATOM   22013 C CB   . LEU   B  1 658 ? 60.116 17.830  -9.977  1.00 36.64  ? 684  LEU   B CB   1 
ATOM   22014 C CG   . LEU   B  1 658 ? 59.122 17.988  -11.129 1.00 37.41  ? 684  LEU   B CG   1 
ATOM   22015 C CD1  . LEU   B  1 658 ? 59.520 19.137  -12.033 1.00 37.98  ? 684  LEU   B CD1  1 
ATOM   22016 C CD2  . LEU   B  1 658 ? 58.998 16.701  -11.949 1.00 37.78  ? 684  LEU   B CD2  1 
ATOM   22017 H H    . LEU   B  1 658 ? 58.094 17.804  -8.514  0.00 49.52  ? 684  LEU   B H    1 
ATOM   22018 H HA   . LEU   B  1 658 ? 59.788 15.765  -9.543  0.00 49.52  ? 684  LEU   B HA   1 
ATOM   22019 H HB2  . LEU   B  1 658 ? 60.132 18.773  -9.431  0.00 50.19  ? 684  LEU   B HB2  1 
ATOM   22020 H HB3  . LEU   B  1 658 ? 61.096 17.647  -10.415 0.00 49.58  ? 684  LEU   B HB3  1 
ATOM   22021 H HG   . LEU   B  1 658 ? 58.141 18.219  -10.716 0.00 49.97  ? 684  LEU   B HG   1 
ATOM   22022 H HD11 . LEU   B  1 658 ? 58.755 19.273  -12.796 0.00 50.11  ? 684  LEU   B HD11 1 
ATOM   22023 H HD12 . LEU   B  1 658 ? 59.610 20.043  -11.435 0.00 51.13  ? 684  LEU   B HD12 1 
ATOM   22024 H HD13 . LEU   B  1 658 ? 60.475 18.904  -12.501 0.00 50.44  ? 684  LEU   B HD13 1 
ATOM   22025 H HD21 . LEU   B  1 658 ? 58.511 16.926  -12.895 0.00 49.12  ? 684  LEU   B HD21 1 
ATOM   22026 H HD22 . LEU   B  1 658 ? 59.992 16.291  -12.122 0.00 49.57  ? 684  LEU   B HD22 1 
ATOM   22027 H HD23 . LEU   B  1 658 ? 58.395 15.985  -11.392 0.00 49.54  ? 684  LEU   B HD23 1 
ATOM   22028 N N    . GLN   B  1 659 ? 60.710 16.870  -6.663  1.00 38.67  ? 685  GLN   B N    1 
ATOM   22029 C CA   . GLN   B  1 659 ? 61.670 16.706  -5.564  1.00 39.63  ? 685  GLN   B CA   1 
ATOM   22030 C C    . GLN   B  1 659 ? 62.123 15.262  -5.418  1.00 39.56  ? 685  GLN   B C    1 
ATOM   22031 O O    . GLN   B  1 659 ? 63.266 15.021  -5.031  1.00 40.11  ? 685  GLN   B O    1 
ATOM   22032 C CB   . GLN   B  1 659 ? 61.036 17.109  -4.226  1.00 42.14  ? 685  GLN   B CB   1 
ATOM   22033 C CG   . GLN   B  1 659 ? 60.884 18.587  -4.027  1.00 47.05  ? 685  GLN   B CG   1 
ATOM   22034 C CD   . GLN   B  1 659 ? 60.302 18.874  -2.665  1.00 53.10  ? 685  GLN   B CD   1 
ATOM   22035 O OE1  . GLN   B  1 659 ? 59.097 18.728  -2.442  1.00 55.49  ? 685  GLN   B OE1  1 
ATOM   22036 N NE2  . GLN   B  1 659 ? 61.139 19.267  -1.719  1.00 54.16  ? 685  GLN   B NE2  1 
ATOM   22037 H H    . GLN   B  1 659 ? 59.839 17.287  -6.351  0.00 53.72  ? 685  GLN   B H    1 
ATOM   22038 H HA   . GLN   B  1 659 ? 62.547 17.327  -5.743  0.00 55.83  ? 685  GLN   B HA   1 
ATOM   22039 H HB2  . GLN   B  1 659 ? 60.049 16.655  -4.147  0.00 58.98  ? 685  GLN   B HB2  1 
ATOM   22040 H HB3  . GLN   B  1 659 ? 61.670 16.737  -3.423  0.00 59.79  ? 685  GLN   B HB3  1 
ATOM   22041 H HG2  . GLN   B  1 659 ? 61.868 19.046  -4.096  0.00 65.99  ? 685  GLN   B HG2  1 
ATOM   22042 H HG3  . GLN   B  1 659 ? 60.198 18.975  -4.779  0.00 65.19  ? 685  GLN   B HG3  1 
ATOM   22043 H HE21 . GLN   B  1 659 ? 62.131 19.365  -1.909  0.00 75.99  ? 685  GLN   B HE21 1 
ATOM   22044 H HE22 . GLN   B  1 659 ? 60.785 19.468  -0.790  0.00 76.36  ? 685  GLN   B HE22 1 
ATOM   22045 N N    . GLN   B  1 660 ? 61.210 14.306  -5.658  1.00 38.62  ? 686  GLN   B N    1 
ATOM   22046 C CA   . GLN   B  1 660 ? 61.506 12.877  -5.538  1.00 38.17  ? 686  GLN   B CA   1 
ATOM   22047 C C    . GLN   B  1 660 ? 62.229 12.296  -6.743  1.00 36.56  ? 686  GLN   B C    1 
ATOM   22048 O O    . GLN   B  1 660 ? 62.412 11.081  -6.774  1.00 36.64  ? 686  GLN   B O    1 
ATOM   22049 C CB   . GLN   B  1 660 ? 60.208 12.074  -5.354  1.00 41.22  ? 686  GLN   B CB   1 
ATOM   22050 C CG   . GLN   B  1 660 ? 59.219 12.613  -4.327  1.00 47.59  ? 686  GLN   B CG   1 
ATOM   22051 C CD   . GLN   B  1 660 ? 59.830 13.134  -3.067  1.00 54.54  ? 686  GLN   B CD   1 
ATOM   22052 O OE1  . GLN   B  1 660 ? 60.686 12.479  -2.469  1.00 57.06  ? 686  GLN   B OE1  1 
ATOM   22053 N NE2  . GLN   B  1 660 ? 59.404 14.310  -2.639  1.00 56.39  ? 686  GLN   B NE2  1 
ATOM   22054 H H    . GLN   B  1 660 ? 60.258 14.493  -5.957  0.00 53.26  ? 686  GLN   B H    1 
ATOM   22055 H HA   . GLN   B  1 660 ? 62.134 12.705  -4.665  0.00 53.48  ? 686  GLN   B HA   1 
ATOM   22056 H HB2  . GLN   B  1 660 ? 59.692 12.035  -6.312  0.00 55.55  ? 686  GLN   B HB2  1 
ATOM   22057 H HB3  . GLN   B  1 660 ? 60.465 11.064  -5.039  0.00 56.20  ? 686  GLN   B HB3  1 
ATOM   22058 H HG2  . GLN   B  1 660 ? 58.589 13.372  -4.788  0.00 64.06  ? 686  GLN   B HG2  1 
ATOM   22059 H HG3  . GLN   B  1 660 ? 58.622 11.769  -3.990  0.00 64.17  ? 686  GLN   B HG3  1 
ATOM   22060 H HE21 . GLN   B  1 660 ? 58.696 14.825  -3.153  0.00 75.86  ? 686  GLN   B HE21 1 
ATOM   22061 H HE22 . GLN   B  1 660 ? 59.788 14.704  -1.787  0.00 76.86  ? 686  GLN   B HE22 1 
ATOM   22062 N N    . PHE   B  1 661 ? 62.607 13.122  -7.738  1.00 34.80  ? 687  PHE   B N    1 
ATOM   22063 C CA   . PHE   B  1 661 ? 63.286 12.668  -8.947  1.00 34.40  ? 687  PHE   B CA   1 
ATOM   22064 C C    . PHE   B  1 661 ? 64.579 13.453  -9.103  1.00 33.94  ? 687  PHE   B C    1 
ATOM   22065 O O    . PHE   B  1 661 ? 64.660 14.357  -9.933  1.00 33.31  ? 687  PHE   B O    1 
ATOM   22066 C CB   . PHE   B  1 661 ? 62.355 12.844  -10.154 1.00 34.19  ? 687  PHE   B CB   1 
ATOM   22067 C CG   . PHE   B  1 661 ? 61.127 11.987  -10.005 1.00 34.34  ? 687  PHE   B CG   1 
ATOM   22068 C CD1  . PHE   B  1 661 ? 60.020 12.450  -9.316  1.00 34.99  ? 687  PHE   B CD1  1 
ATOM   22069 C CD2  . PHE   B  1 661 ? 61.129 10.670  -10.431 1.00 34.80  ? 687  PHE   B CD2  1 
ATOM   22070 C CE1  . PHE   B  1 661 ? 58.930 11.626  -9.086  1.00 35.80  ? 687  PHE   B CE1  1 
ATOM   22071 C CE2  . PHE   B  1 661 ? 60.028 9.856   -10.222 1.00 35.45  ? 687  PHE   B CE2  1 
ATOM   22072 C CZ   . PHE   B  1 661 ? 58.937 10.337  -9.548  1.00 35.46  ? 687  PHE   B CZ   1 
ATOM   22073 H H    . PHE   B  1 661 ? 62.464 14.127  -7.740  0.00 48.17  ? 687  PHE   B H    1 
ATOM   22074 H HA   . PHE   B  1 661 ? 63.530 11.608  -8.893  0.00 46.87  ? 687  PHE   B HA   1 
ATOM   22075 H HB2  . PHE   B  1 661 ? 62.049 13.885  -10.250 0.00 46.03  ? 687  PHE   B HB2  1 
ATOM   22076 H HB3  . PHE   B  1 661 ? 62.879 12.501  -11.044 0.00 45.57  ? 687  PHE   B HB3  1 
ATOM   22077 H HD1  . PHE   B  1 661 ? 60.015 13.456  -8.930  0.00 47.10  ? 687  PHE   B HD1  1 
ATOM   22078 H HD2  . PHE   B  1 661 ? 61.990 10.278  -10.947 0.00 45.76  ? 687  PHE   B HD2  1 
ATOM   22079 H HE1  . PHE   B  1 661 ? 58.063 12.009  -8.573  0.00 47.59  ? 687  PHE   B HE1  1 
ATOM   22080 H HE2  . PHE   B  1 661 ? 60.032 8.841   -10.584 0.00 46.08  ? 687  PHE   B HE2  1 
ATOM   22081 H HZ   . PHE   B  1 661 ? 58.075 9.708   -9.402  0.00 46.39  ? 687  PHE   B HZ   1 
ATOM   22082 N N    . PRO   B  1 662 ? 65.610 13.109  -8.297  1.00 34.18  ? 688  PRO   B N    1 
ATOM   22083 C CA   . PRO   B  1 662 ? 66.857 13.899  -8.309  1.00 34.25  ? 688  PRO   B CA   1 
ATOM   22084 C C    . PRO   B  1 662 ? 67.751 13.742  -9.530  1.00 34.13  ? 688  PRO   B C    1 
ATOM   22085 O O    . PRO   B  1 662 ? 68.714 14.491  -9.670  1.00 34.42  ? 688  PRO   B O    1 
ATOM   22086 C CB   . PRO   B  1 662 ? 67.572 13.436  -7.035  1.00 35.62  ? 688  PRO   B CB   1 
ATOM   22087 C CG   . PRO   B  1 662 ? 67.110 12.043  -6.841  1.00 36.25  ? 688  PRO   B CG   1 
ATOM   22088 C CD   . PRO   B  1 662 ? 65.660 12.050  -7.271  1.00 34.14  ? 688  PRO   B CD   1 
ATOM   22089 H HA   . PRO   B  1 662 ? 66.618 14.955  -8.196  0.00 48.59  ? 688  PRO   B HA   1 
ATOM   22090 H HB2  . PRO   B  1 662 ? 68.651 13.470  -7.178  0.00 51.10  ? 688  PRO   B HB2  1 
ATOM   22091 H HB3  . PRO   B  1 662 ? 67.275 14.065  -6.196  0.00 51.33  ? 688  PRO   B HB3  1 
ATOM   22092 H HG2  . PRO   B  1 662 ? 67.694 11.370  -7.466  0.00 51.01  ? 688  PRO   B HG2  1 
ATOM   22093 H HG3  . PRO   B  1 662 ? 67.199 11.769  -5.791  0.00 51.84  ? 688  PRO   B HG3  1 
ATOM   22094 H HD2  . PRO   B  1 662 ? 65.409 11.081  -7.697  0.00 47.62  ? 688  PRO   B HD2  1 
ATOM   22095 H HD3  . PRO   B  1 662 ? 65.014 12.301  -6.430  0.00 48.40  ? 688  PRO   B HD3  1 
ATOM   22096 N N    . ARG   B  1 663 ? 67.465 12.770  -10.395 1.00 33.52  ? 689  ARG   B N    1 
ATOM   22097 C CA   . ARG   B  1 663 ? 68.226 12.546  -11.619 1.00 33.54  ? 689  ARG   B CA   1 
ATOM   22098 C C    . ARG   B  1 663 ? 67.467 13.061  -12.871 1.00 32.09  ? 689  ARG   B C    1 
ATOM   22099 O O    . ARG   B  1 663 ? 67.988 12.912  -13.977 1.00 32.33  ? 689  ARG   B O    1 
ATOM   22100 C CB   . ARG   B  1 663 ? 68.496 11.041  -11.776 1.00 36.09  ? 689  ARG   B CB   1 
ATOM   22101 C CG   . ARG   B  1 663 ? 69.195 10.389  -10.578 1.00 41.78  ? 689  ARG   B CG   1 
ATOM   22102 C CD   . ARG   B  1 663 ? 70.704 10.436  -10.706 1.00 47.80  ? 689  ARG   B CD   1 
ATOM   22103 N NE   . ARG   B  1 663 ? 71.386 9.665   -9.662  1.00 54.00  ? 689  ARG   B NE   1 
ATOM   22104 C CZ   . ARG   B  1 663 ? 71.580 10.071  -8.407  1.00 58.80  ? 689  ARG   B CZ   1 
ATOM   22105 N NH1  . ARG   B  1 663 ? 72.218 9.291   -7.542  1.00 60.12  ? 689  ARG   B NH1  1 
ATOM   22106 N NH2  . ARG   B  1 663 ? 71.127 11.257  -8.003  1.00 59.09  ? 689  ARG   B NH2  1 
ATOM   22107 H H    . ARG   B  1 663 ? 66.712 12.099  -10.282 0.00 46.08  ? 689  ARG   B H    1 
ATOM   22108 H HA   . ARG   B  1 663 ? 69.190 13.050  -11.578 0.00 46.41  ? 689  ARG   B HA   1 
ATOM   22109 H HB2  . ARG   B  1 663 ? 67.549 10.527  -11.930 0.00 48.37  ? 689  ARG   B HB2  1 
ATOM   22110 H HB3  . ARG   B  1 663 ? 69.138 10.900  -12.643 0.00 48.58  ? 689  ARG   B HB3  1 
ATOM   22111 H HG2  . ARG   B  1 663 ? 68.923 10.893  -9.651  0.00 56.81  ? 689  ARG   B HG2  1 
ATOM   22112 H HG3  . ARG   B  1 663 ? 68.898 9.343   -10.526 0.00 56.15  ? 689  ARG   B HG3  1 
ATOM   22113 H HD2  . ARG   B  1 663 ? 70.989 9.991   -11.658 0.00 63.62  ? 689  ARG   B HD2  1 
ATOM   22114 H HD3  . ARG   B  1 663 ? 71.049 11.469  -10.673 0.00 64.35  ? 689  ARG   B HD3  1 
ATOM   22115 H HE   . ARG   B  1 663 ? 71.750 8.755   -9.928  0.00 72.05  ? 689  ARG   B HE   1 
ATOM   22116 H HH11 . ARG   B  1 663 ? 72.567 8.383   -7.832  0.00 80.77  ? 689  ARG   B HH11 1 
ATOM   22117 H HH12 . ARG   B  1 663 ? 72.356 9.594   -6.583  0.00 81.53  ? 689  ARG   B HH12 1 
ATOM   22118 H HH21 . ARG   B  1 663 ? 70.627 11.885  -8.623  0.00 78.88  ? 689  ARG   B HH21 1 
ATOM   22119 H HH22 . ARG   B  1 663 ? 71.276 11.544  -7.042  0.00 79.92  ? 689  ARG   B HH22 1 
ATOM   22120 N N    . LEU   B  1 664 ? 66.239 13.625  -12.720 1.00 30.68  ? 690  LEU   B N    1 
ATOM   22121 C CA   . LEU   B  1 664 ? 65.455 14.075  -13.869 1.00 30.57  ? 690  LEU   B CA   1 
ATOM   22122 C C    . LEU   B  1 664 ? 66.101 15.246  -14.607 1.00 31.07  ? 690  LEU   B C    1 
ATOM   22123 O O    . LEU   B  1 664 ? 66.192 16.345  -14.054 1.00 31.76  ? 690  LEU   B O    1 
ATOM   22124 C CB   . LEU   B  1 664 ? 64.029 14.439  -13.448 1.00 30.14  ? 690  LEU   B CB   1 
ATOM   22125 C CG   . LEU   B  1 664 ? 63.031 14.663  -14.599 1.00 30.49  ? 690  LEU   B CG   1 
ATOM   22126 C CD1  . LEU   B  1 664 ? 62.860 13.384  -15.445 1.00 30.31  ? 690  LEU   B CD1  1 
ATOM   22127 C CD2  . LEU   B  1 664 ? 61.684 15.131  -14.052 1.00 30.97  ? 690  LEU   B CD2  1 
ATOM   22128 H H    . LEU   B  1 664 ? 65.771 13.789  -11.834 0.00 41.97  ? 690  LEU   B H    1 
ATOM   22129 H HA   . LEU   B  1 664 ? 65.378 13.233  -14.553 0.00 40.38  ? 690  LEU   B HA   1 
ATOM   22130 H HB2  . LEU   B  1 664 ? 63.637 13.614  -12.856 0.00 40.27  ? 690  LEU   B HB2  1 
ATOM   22131 H HB3  . LEU   B  1 664 ? 64.049 15.345  -12.843 0.00 40.74  ? 690  LEU   B HB3  1 
ATOM   22132 H HG   . LEU   B  1 664 ? 63.399 15.450  -15.255 0.00 39.95  ? 690  LEU   B HG   1 
ATOM   22133 H HD11 . LEU   B  1 664 ? 61.935 13.461  -16.016 0.00 38.69  ? 690  LEU   B HD11 1 
ATOM   22134 H HD12 . LEU   B  1 664 ? 63.699 13.296  -16.133 0.00 38.99  ? 690  LEU   B HD12 1 
ATOM   22135 H HD13 . LEU   B  1 664 ? 62.820 12.516  -14.787 0.00 39.22  ? 690  LEU   B HD13 1 
ATOM   22136 H HD21 . LEU   B  1 664 ? 60.996 15.292  -14.880 0.00 40.15  ? 690  LEU   B HD21 1 
ATOM   22137 H HD22 . LEU   B  1 664 ? 61.289 14.371  -13.379 0.00 40.64  ? 690  LEU   B HD22 1 
ATOM   22138 H HD23 . LEU   B  1 664 ? 61.838 16.065  -13.514 0.00 41.09  ? 690  LEU   B HD23 1 
ATOM   22139 N N    . GLU   B  1 665 ? 66.514 15.004  -15.858 1.00 30.69  ? 691  GLU   B N    1 
ATOM   22140 C CA   . GLU   B  1 665 ? 67.166 15.974  -16.741 1.00 30.99  ? 691  GLU   B CA   1 
ATOM   22141 C C    . GLU   B  1 665 ? 66.225 16.540  -17.804 1.00 30.20  ? 691  GLU   B C    1 
ATOM   22142 O O    . GLU   B  1 665 ? 66.424 17.680  -18.234 1.00 30.28  ? 691  GLU   B O    1 
ATOM   22143 C CB   . GLU   B  1 665 ? 68.335 15.305  -17.475 1.00 34.92  ? 691  GLU   B CB   1 
ATOM   22144 C CG   . GLU   B  1 665 ? 69.471 14.902  -16.564 1.00 43.22  ? 691  GLU   B CG   1 
ATOM   22145 C CD   . GLU   B  1 665 ? 70.683 14.363  -17.296 1.00 53.35  ? 691  GLU   B CD   1 
ATOM   22146 O OE1  . GLU   B  1 665 ? 70.507 13.684  -18.333 1.00 55.18  ? 691  GLU   B OE1  1 
ATOM   22147 O OE2  . GLU   B  1 665 ? 71.814 14.599  -16.815 1.00 57.71  ? 691  GLU   B OE2  1 
ATOM   22148 H H    . GLU   B  1 665 ? 66.393 14.103  -16.312 0.00 40.20  ? 691  GLU   B H    1 
ATOM   22149 H HA   . GLU   B  1 665 ? 67.561 16.810  -16.164 0.00 41.53  ? 691  GLU   B HA   1 
ATOM   22150 H HB2  . GLU   B  1 665 ? 67.975 14.406  -17.975 0.00 45.08  ? 691  GLU   B HB2  1 
ATOM   22151 H HB3  . GLU   B  1 665 ? 68.732 16.010  -18.205 0.00 45.54  ? 691  GLU   B HB3  1 
ATOM   22152 H HG2  . GLU   B  1 665 ? 69.789 15.777  -15.997 0.00 56.72  ? 691  GLU   B HG2  1 
ATOM   22153 H HG3  . GLU   B  1 665 ? 69.120 14.124  -15.886 0.00 56.21  ? 691  GLU   B HG3  1 
ATOM   22154 N N    . LEU   B  1 666 ? 65.293 15.729  -18.322 1.00 28.82  ? 692  LEU   B N    1 
ATOM   22155 C CA   . LEU   B  1 666 ? 64.379 16.189  -19.369 1.00 28.34  ? 692  LEU   B CA   1 
ATOM   22156 C C    . LEU   B  1 666 ? 62.943 15.889  -18.990 1.00 27.38  ? 692  LEU   B C    1 
ATOM   22157 O O    . LEU   B  1 666 ? 62.616 14.745  -18.664 1.00 27.22  ? 692  LEU   B O    1 
ATOM   22158 C CB   . LEU   B  1 666 ? 64.698 15.519  -20.716 1.00 28.84  ? 692  LEU   B CB   1 
ATOM   22159 C CG   . LEU   B  1 666 ? 63.965 16.102  -21.943 1.00 31.07  ? 692  LEU   B CG   1 
ATOM   22160 C CD1  . LEU   B  1 666 ? 64.824 15.991  -23.189 1.00 32.21  ? 692  LEU   B CD1  1 
ATOM   22161 C CD2  . LEU   B  1 666 ? 62.621 15.427  -22.177 1.00 32.13  ? 692  LEU   B CD2  1 
ATOM   22162 H H    . LEU   B  1 666 ? 65.151 14.760  -18.056 0.00 37.06  ? 692  LEU   B H    1 
ATOM   22163 H HA   . LEU   B  1 666 ? 64.473 17.265  -19.508 0.00 36.33  ? 692  LEU   B HA   1 
ATOM   22164 H HB2  . LEU   B  1 666 ? 65.767 15.611  -20.897 0.00 36.34  ? 692  LEU   B HB2  1 
ATOM   22165 H HB3  . LEU   B  1 666 ? 64.433 14.466  -20.645 0.00 35.88  ? 692  LEU   B HB3  1 
ATOM   22166 H HG   . LEU   B  1 666 ? 63.766 17.164  -21.805 0.00 38.59  ? 692  LEU   B HG   1 
ATOM   22167 H HD11 . LEU   B  1 666 ? 64.264 16.371  -24.042 0.00 39.13  ? 692  LEU   B HD11 1 
ATOM   22168 H HD12 . LEU   B  1 666 ? 65.728 16.582  -23.051 0.00 39.84  ? 692  LEU   B HD12 1 
ATOM   22169 H HD13 . LEU   B  1 666 ? 65.083 14.946  -23.349 0.00 39.25  ? 692  LEU   B HD13 1 
ATOM   22170 H HD21 . LEU   B  1 666 ? 62.173 15.882  -23.058 0.00 38.84  ? 692  LEU   B HD21 1 
ATOM   22171 H HD22 . LEU   B  1 666 ? 62.768 14.365  -22.358 0.00 38.86  ? 692  LEU   B HD22 1 
ATOM   22172 H HD23 . LEU   B  1 666 ? 61.984 15.579  -21.307 0.00 39.32  ? 692  LEU   B HD23 1 
ATOM   22173 N N    . LEU   B  1 667 ? 62.090 16.914  -19.035 1.00 26.66  ? 693  LEU   B N    1 
ATOM   22174 C CA   . LEU   B  1 667 ? 60.667 16.776  -18.737 1.00 26.25  ? 693  LEU   B CA   1 
ATOM   22175 C C    . LEU   B  1 667 ? 59.931 17.320  -19.943 1.00 25.44  ? 693  LEU   B C    1 
ATOM   22176 O O    . LEU   B  1 667 ? 60.122 18.483  -20.314 1.00 25.65  ? 693  LEU   B O    1 
ATOM   22177 C CB   . LEU   B  1 667 ? 60.290 17.549  -17.459 1.00 26.64  ? 693  LEU   B CB   1 
ATOM   22178 C CG   . LEU   B  1 667 ? 58.807 17.528  -17.057 1.00 28.71  ? 693  LEU   B CG   1 
ATOM   22179 C CD1  . LEU   B  1 667 ? 58.240 16.085  -16.991 1.00 29.98  ? 693  LEU   B CD1  1 
ATOM   22180 C CD2  . LEU   B  1 667 ? 58.597 18.238  -15.745 1.00 29.32  ? 693  LEU   B CD2  1 
ATOM   22181 H H    . LEU   B  1 667 ? 62.352 17.865  -19.275 0.00 34.10  ? 693  LEU   B H    1 
ATOM   22182 H HA   . LEU   B  1 667 ? 60.406 15.727  -18.603 0.00 32.98  ? 693  LEU   B HA   1 
ATOM   22183 H HB2  . LEU   B  1 667 ? 60.855 17.132  -16.627 0.00 34.64  ? 693  LEU   B HB2  1 
ATOM   22184 H HB3  . LEU   B  1 667 ? 60.558 18.595  -17.603 0.00 34.58  ? 693  LEU   B HB3  1 
ATOM   22185 H HG   . LEU   B  1 667 ? 58.244 18.082  -17.805 0.00 36.47  ? 693  LEU   B HG   1 
ATOM   22186 H HD11 . LEU   B  1 667 ? 57.258 16.111  -16.523 0.00 37.85  ? 693  LEU   B HD11 1 
ATOM   22187 H HD12 . LEU   B  1 667 ? 58.150 15.691  -18.002 0.00 37.31  ? 693  LEU   B HD12 1 
ATOM   22188 H HD13 . LEU   B  1 667 ? 58.917 15.461  -16.410 0.00 38.00  ? 693  LEU   B HD13 1 
ATOM   22189 H HD21 . LEU   B  1 667 ? 57.540 18.212  -15.486 0.00 38.05  ? 693  LEU   B HD21 1 
ATOM   22190 H HD22 . LEU   B  1 667 ? 59.183 17.735  -14.977 0.00 38.39  ? 693  LEU   B HD22 1 
ATOM   22191 H HD23 . LEU   B  1 667 ? 58.927 19.271  -15.849 0.00 38.42  ? 693  LEU   B HD23 1 
ATOM   22192 N N    . ASP   B  1 668 ? 59.153 16.459  -20.607 1.00 24.30  ? 694  ASP   B N    1 
ATOM   22193 C CA   . ASP   B  1 668 ? 58.449 16.841  -21.816 1.00 24.35  ? 694  ASP   B CA   1 
ATOM   22194 C C    . ASP   B  1 668 ? 56.934 16.797  -21.590 1.00 24.90  ? 694  ASP   B C    1 
ATOM   22195 O O    . ASP   B  1 668 ? 56.346 15.722  -21.463 1.00 25.19  ? 694  ASP   B O    1 
ATOM   22196 C CB   . ASP   B  1 668 ? 58.930 15.954  -22.980 1.00 24.69  ? 694  ASP   B CB   1 
ATOM   22197 C CG   . ASP   B  1 668 ? 58.154 16.062  -24.262 1.00 27.76  ? 694  ASP   B CG   1 
ATOM   22198 O OD1  . ASP   B  1 668 ? 57.384 17.031  -24.407 1.00 27.60  ? 694  ASP   B OD1  1 
ATOM   22199 O OD2  . ASP   B  1 668 ? 58.346 15.189  -25.149 1.00 30.10  ? 694  ASP   B OD2  1 
ATOM   22200 H H    . ASP   B  1 668 ? 58.987 15.496  -20.330 0.00 29.73  ? 694  ASP   B H    1 
ATOM   22201 H HA   . ASP   B  1 668 ? 58.706 17.865  -22.074 0.00 29.74  ? 694  ASP   B HA   1 
ATOM   22202 H HB2  . ASP   B  1 668 ? 59.939 16.280  -23.221 0.00 29.57  ? 694  ASP   B HB2  1 
ATOM   22203 H HB3  . ASP   B  1 668 ? 58.968 14.909  -22.681 0.00 29.30  ? 694  ASP   B HB3  1 
ATOM   22204 N N    . LEU   B  1 669 ? 56.324 17.987  -21.487 1.00 24.62  ? 695  LEU   B N    1 
ATOM   22205 C CA   . LEU   B  1 669 ? 54.885 18.162  -21.274 1.00 25.12  ? 695  LEU   B CA   1 
ATOM   22206 C C    . LEU   B  1 669 ? 54.232 18.883  -22.465 1.00 25.15  ? 695  LEU   B C    1 
ATOM   22207 O O    . LEU   B  1 669 ? 53.171 19.469  -22.301 1.00 25.27  ? 695  LEU   B O    1 
ATOM   22208 C CB   . LEU   B  1 669 ? 54.642 18.972  -19.980 1.00 25.63  ? 695  LEU   B CB   1 
ATOM   22209 C CG   . LEU   B  1 669 ? 55.140 18.329  -18.684 1.00 27.86  ? 695  LEU   B CG   1 
ATOM   22210 C CD1  . LEU   B  1 669 ? 54.982 19.283  -17.494 1.00 28.27  ? 695  LEU   B CD1  1 
ATOM   22211 C CD2  . LEU   B  1 669 ? 54.433 17.028  -18.411 1.00 28.52  ? 695  LEU   B CD2  1 
ATOM   22212 H H    . LEU   B  1 669 ? 56.812 18.876  -21.541 0.00 30.27  ? 695  LEU   B H    1 
ATOM   22213 H HA   . LEU   B  1 669 ? 54.390 17.197  -21.173 0.00 30.31  ? 695  LEU   B HA   1 
ATOM   22214 H HB2  . LEU   B  1 669 ? 55.157 19.926  -20.080 0.00 32.11  ? 695  LEU   B HB2  1 
ATOM   22215 H HB3  . LEU   B  1 669 ? 53.574 19.143  -19.850 0.00 31.83  ? 695  LEU   B HB3  1 
ATOM   22216 H HG   . LEU   B  1 669 ? 56.198 18.104  -18.801 0.00 34.83  ? 695  LEU   B HG   1 
ATOM   22217 H HD11 . LEU   B  1 669 ? 55.407 18.817  -16.607 0.00 36.25  ? 695  LEU   B HD11 1 
ATOM   22218 H HD12 . LEU   B  1 669 ? 55.508 20.210  -17.716 0.00 36.25  ? 695  LEU   B HD12 1 
ATOM   22219 H HD13 . LEU   B  1 669 ? 53.923 19.483  -17.338 0.00 36.02  ? 695  LEU   B HD13 1 
ATOM   22220 H HD21 . LEU   B  1 669 ? 54.610 16.732  -17.377 0.00 35.62  ? 695  LEU   B HD21 1 
ATOM   22221 H HD22 . LEU   B  1 669 ? 53.365 17.149  -18.589 0.00 35.18  ? 695  LEU   B HD22 1 
ATOM   22222 H HD23 . LEU   B  1 669 ? 54.847 16.275  -19.079 0.00 34.91  ? 695  LEU   B HD23 1 
ATOM   22223 N N    . ARG   B  1 670 ? 54.814 18.783  -23.668 1.00 24.76  ? 696  ARG   B N    1 
ATOM   22224 C CA   . ARG   B  1 670 ? 54.252 19.425  -24.851 1.00 25.29  ? 696  ARG   B CA   1 
ATOM   22225 C C    . ARG   B  1 670 ? 52.868 18.879  -25.194 1.00 25.50  ? 696  ARG   B C    1 
ATOM   22226 O O    . ARG   B  1 670 ? 52.559 17.752  -24.843 1.00 25.23  ? 696  ARG   B O    1 
ATOM   22227 C CB   . ARG   B  1 670 ? 55.155 19.185  -26.062 1.00 26.86  ? 696  ARG   B CB   1 
ATOM   22228 C CG   . ARG   B  1 670 ? 56.533 19.830  -25.970 1.00 30.40  ? 696  ARG   B CG   1 
ATOM   22229 C CD   . ARG   B  1 670 ? 57.413 19.379  -27.133 1.00 33.78  ? 696  ARG   B CD   1 
ATOM   22230 N NE   . ARG   B  1 670 ? 57.659 17.936  -27.084 1.00 37.51  ? 696  ARG   B NE   1 
ATOM   22231 C CZ   . ARG   B  1 670 ? 58.241 17.232  -28.049 1.00 40.58  ? 696  ARG   B CZ   1 
ATOM   22232 N NH1  . ARG   B  1 670 ? 58.665 17.833  -29.158 1.00 40.12  ? 696  ARG   B NH1  1 
ATOM   22233 N NH2  . ARG   B  1 670 ? 58.405 15.920  -27.915 1.00 40.39  ? 696  ARG   B NH2  1 
ATOM   22234 H H    . ARG   B  1 670 ? 55.655 18.248  -23.858 0.00 29.43  ? 696  ARG   B H    1 
ATOM   22235 H HA   . ARG   B  1 670 ? 54.174 20.499  -24.684 0.00 30.36  ? 696  ARG   B HA   1 
ATOM   22236 H HB2  . ARG   B  1 670 ? 55.279 18.109  -26.181 0.00 31.25  ? 696  ARG   B HB2  1 
ATOM   22237 H HB3  . ARG   B  1 670 ? 54.664 19.593  -26.944 0.00 31.41  ? 696  ARG   B HB3  1 
ATOM   22238 H HG2  . ARG   B  1 670 ? 56.428 20.912  -26.022 0.00 36.40  ? 696  ARG   B HG2  1 
ATOM   22239 H HG3  . ARG   B  1 670 ? 57.019 19.537  -25.040 0.00 36.33  ? 696  ARG   B HG3  1 
ATOM   22240 H HD2  . ARG   B  1 670 ? 56.904 19.605  -28.068 0.00 39.60  ? 696  ARG   B HD2  1 
ATOM   22241 H HD3  . ARG   B  1 670 ? 58.371 19.895  -27.095 0.00 40.08  ? 696  ARG   B HD3  1 
ATOM   22242 H HE   . ARG   B  1 670 ? 57.356 17.438  -26.253 0.00 44.02  ? 696  ARG   B HE   1 
ATOM   22243 H HH11 . ARG   B  1 670 ? 58.547 18.830  -29.304 0.00 46.86  ? 696  ARG   B HH11 1 
ATOM   22244 H HH12 . ARG   B  1 670 ? 59.103 17.283  -29.890 0.00 46.41  ? 696  ARG   B HH12 1 
ATOM   22245 H HH21 . ARG   B  1 670 ? 58.097 15.448  -27.071 0.00 46.89  ? 696  ARG   B HH21 1 
ATOM   22246 H HH22 . ARG   B  1 670 ? 58.856 15.382  -28.647 0.00 46.58  ? 696  ARG   B HH22 1 
ATOM   22247 N N    . GLY   B  1 671 ? 52.059 19.677  -25.886 1.00 25.61  ? 697  GLY   B N    1 
ATOM   22248 C CA   . GLY   B  1 671 ? 50.748 19.238  -26.351 1.00 26.47  ? 697  GLY   B CA   1 
ATOM   22249 C C    . GLY   B  1 671 ? 49.790 18.823  -25.252 1.00 26.52  ? 697  GLY   B C    1 
ATOM   22250 O O    . GLY   B  1 671 ? 49.200 17.748  -25.312 1.00 27.35  ? 697  GLY   B O    1 
ATOM   22251 H H    . GLY   B  1 671 ? 52.281 20.636  -26.131 0.00 30.32  ? 697  GLY   B H    1 
ATOM   22252 H HA2  . GLY   B  1 671 ? 50.285 20.047  -26.916 0.00 30.95  ? 697  GLY   B HA2  1 
ATOM   22253 H HA3  . GLY   B  1 671 ? 50.874 18.391  -27.023 0.00 30.47  ? 697  GLY   B HA3  1 
ATOM   22254 N N    . ASN   B  1 672 ? 49.634 19.671  -24.249 1.00 25.69  ? 698  ASN   B N    1 
ATOM   22255 C CA   . ASN   B  1 672 ? 48.703 19.440  -23.144 1.00 26.11  ? 698  ASN   B CA   1 
ATOM   22256 C C    . ASN   B  1 672 ? 47.809 20.712  -23.002 1.00 26.90  ? 698  ASN   B C    1 
ATOM   22257 O O    . ASN   B  1 672 ? 47.681 21.455  -23.977 1.00 26.39  ? 698  ASN   B O    1 
ATOM   22258 C CB   . ASN   B  1 672 ? 49.514 19.065  -21.873 1.00 25.92  ? 698  ASN   B CB   1 
ATOM   22259 C CG   . ASN   B  1 672 ? 49.906 17.604  -21.851 1.00 27.13  ? 698  ASN   B CG   1 
ATOM   22260 O OD1  . ASN   B  1 672 ? 49.036 16.737  -21.821 1.00 26.91  ? 698  ASN   B OD1  1 
ATOM   22261 N ND2  . ASN   B  1 672 ? 51.204 17.289  -21.865 1.00 25.36  ? 698  ASN   B ND2  1 
ATOM   22262 H H    . ASN   B  1 672 ? 50.145 20.544  -24.168 0.00 30.86  ? 698  ASN   B H    1 
ATOM   22263 H HA   . ASN   B  1 672 ? 48.020 18.626  -23.379 0.00 31.05  ? 698  ASN   B HA   1 
ATOM   22264 H HB2  . ASN   B  1 672 ? 50.419 19.669  -21.858 0.00 31.55  ? 698  ASN   B HB2  1 
ATOM   22265 H HB3  . ASN   B  1 672 ? 48.930 19.267  -20.979 0.00 31.68  ? 698  ASN   B HB3  1 
ATOM   22266 H HD21 . ASN   B  1 672 ? 51.484 16.314  -21.851 0.00 30.01  ? 698  ASN   B HD21 1 
ATOM   22267 H HD22 . ASN   B  1 672 ? 51.914 18.014  -21.893 0.00 30.44  ? 698  ASN   B HD22 1 
ATOM   22268 N N    . LYS   B  1 673 ? 47.123 20.910  -21.877 1.00 28.31  ? 699  LYS   B N    1 
ATOM   22269 C CA   . LYS   B  1 673 ? 46.286 22.096  -21.670 1.00 29.87  ? 699  LYS   B CA   1 
ATOM   22270 C C    . LYS   B  1 673 ? 46.682 22.799  -20.370 1.00 30.78  ? 699  LYS   B C    1 
ATOM   22271 O O    . LYS   B  1 673 ? 45.809 23.352  -19.697 1.00 30.50  ? 699  LYS   B O    1 
ATOM   22272 C CB   . LYS   B  1 673 ? 44.803 21.681  -21.637 1.00 32.17  ? 699  LYS   B CB   1 
ATOM   22273 C CG   . LYS   B  1 673 ? 44.362 20.917  -22.885 1.00 37.29  ? 699  LYS   B CG   1 
ATOM   22274 C CD   . LYS   B  1 673 ? 42.892 20.541  -22.815 1.00 43.32  ? 699  LYS   B CD   1 
ATOM   22275 C CE   . LYS   B  1 673 ? 42.453 19.762  -24.029 1.00 48.34  ? 699  LYS   B CE   1 
ATOM   22276 N NZ   . LYS   B  1 673 ? 41.099 19.167  -23.838 1.00 52.04  ? 699  LYS   B NZ   1 
ATOM   22277 H H    . LYS   B  1 673 ? 47.080 20.262  -21.098 0.00 34.83  ? 699  LYS   B H    1 
ATOM   22278 H HA   . LYS   B  1 673 ? 46.414 22.815  -22.478 0.00 37.17  ? 699  LYS   B HA   1 
ATOM   22279 H HB2  . LYS   B  1 673 ? 44.633 21.041  -20.772 0.00 39.91  ? 699  LYS   B HB2  1 
ATOM   22280 H HB3  . LYS   B  1 673 ? 44.182 22.572  -21.570 0.00 40.23  ? 699  LYS   B HB3  1 
ATOM   22281 H HG2  . LYS   B  1 673 ? 44.514 21.543  -23.763 0.00 45.40  ? 699  LYS   B HG2  1 
ATOM   22282 H HG3  . LYS   B  1 673 ? 44.933 19.994  -22.977 0.00 45.09  ? 699  LYS   B HG3  1 
ATOM   22283 H HD2  . LYS   B  1 673 ? 42.723 19.922  -21.935 0.00 52.75  ? 699  LYS   B HD2  1 
ATOM   22284 H HD3  . LYS   B  1 673 ? 42.293 21.449  -22.758 0.00 53.07  ? 699  LYS   B HD3  1 
ATOM   22285 H HE2  . LYS   B  1 673 ? 42.414 20.428  -24.889 0.00 58.23  ? 699  LYS   B HE2  1 
ATOM   22286 H HE3  . LYS   B  1 673 ? 43.158 18.952  -24.211 0.00 57.87  ? 699  LYS   B HE3  1 
ATOM   22287 H HZ1  . LYS   B  1 673 ? 40.825 18.655  -24.670 0.00 62.37  ? 699  LYS   B HZ1  1 
ATOM   22288 H HZ2  . LYS   B  1 673 ? 41.109 18.530  -23.047 0.00 62.68  ? 699  LYS   B HZ2  1 
ATOM   22289 H HZ3  . LYS   B  1 673 ? 40.420 19.900  -23.662 0.00 63.02  ? 699  LYS   B HZ3  1 
ATOM   22290 N N    . LEU   B  1 674 ? 47.998 22.787  -20.015 1.00 31.88  ? 700  LEU   B N    1 
ATOM   22291 C CA   . LEU   B  1 674 ? 48.494 23.386  -18.777 1.00 33.58  ? 700  LEU   B CA   1 
ATOM   22292 C C    . LEU   B  1 674 ? 48.272 24.902  -18.811 1.00 35.81  ? 700  LEU   B C    1 
ATOM   22293 O O    . LEU   B  1 674 ? 48.546 25.545  -19.821 1.00 35.01  ? 700  LEU   B O    1 
ATOM   22294 C CB   . LEU   B  1 674 ? 49.978 23.027  -18.561 1.00 33.47  ? 700  LEU   B CB   1 
ATOM   22295 C CG   . LEU   B  1 674 ? 50.280 21.524  -18.426 1.00 34.87  ? 700  LEU   B CG   1 
ATOM   22296 C CD1  . LEU   B  1 674 ? 51.770 21.263  -18.364 1.00 35.36  ? 700  LEU   B CD1  1 
ATOM   22297 C CD2  . LEU   B  1 674 ? 49.593 20.924  -17.204 1.00 35.48  ? 700  LEU   B CD2  1 
ATOM   22298 H H    . LEU   B  1 674 ? 48.740 22.399  -20.589 0.00 39.95  ? 700  LEU   B H    1 
ATOM   22299 H HA   . LEU   B  1 674 ? 47.917 22.987  -17.945 0.00 43.09  ? 700  LEU   B HA   1 
ATOM   22300 H HB2  . LEU   B  1 674 ? 50.552 23.403  -19.407 0.00 42.63  ? 700  LEU   B HB2  1 
ATOM   22301 H HB3  . LEU   B  1 674 ? 50.320 23.507  -17.645 0.00 43.28  ? 700  LEU   B HB3  1 
ATOM   22302 H HG   . LEU   B  1 674 ? 49.897 21.011  -19.307 0.00 43.51  ? 700  LEU   B HG   1 
ATOM   22303 H HD11 . LEU   B  1 674 ? 51.944 20.188  -18.358 0.00 44.24  ? 700  LEU   B HD11 1 
ATOM   22304 H HD12 . LEU   B  1 674 ? 52.244 21.711  -19.235 0.00 44.44  ? 700  LEU   B HD12 1 
ATOM   22305 H HD13 . LEU   B  1 674 ? 52.167 21.704  -17.451 0.00 45.07  ? 700  LEU   B HD13 1 
ATOM   22306 H HD21 . LEU   B  1 674 ? 50.023 19.945  -17.000 0.00 44.71  ? 700  LEU   B HD21 1 
ATOM   22307 H HD22 . LEU   B  1 674 ? 49.741 21.581  -16.349 0.00 45.47  ? 700  LEU   B HD22 1 
ATOM   22308 H HD23 . LEU   B  1 674 ? 48.529 20.817  -17.410 0.00 44.82  ? 700  LEU   B HD23 1 
ATOM   22309 N N    . LEU   B  1 675 ? 47.704 25.442  -17.730 1.00 38.18  ? 701  LEU   B N    1 
ATOM   22310 C CA   . LEU   B  1 675 ? 47.308 26.845  -17.626 1.00 41.29  ? 701  LEU   B CA   1 
ATOM   22311 C C    . LEU   B  1 675 ? 48.310 27.731  -16.905 1.00 43.69  ? 701  LEU   B C    1 
ATOM   22312 O O    . LEU   B  1 675 ? 48.277 28.943  -17.104 1.00 43.81  ? 701  LEU   B O    1 
ATOM   22313 C CB   . LEU   B  1 675 ? 45.945 26.930  -16.910 1.00 42.02  ? 701  LEU   B CB   1 
ATOM   22314 C CG   . LEU   B  1 675 ? 44.757 26.331  -17.679 1.00 44.13  ? 701  LEU   B CG   1 
ATOM   22315 C CD1  . LEU   B  1 675 ? 43.613 26.000  -16.741 1.00 45.05  ? 701  LEU   B CD1  1 
ATOM   22316 C CD2  . LEU   B  1 675 ? 44.272 27.276  -18.758 1.00 45.10  ? 701  LEU   B CD2  1 
ATOM   22317 H H    . LEU   B  1 675 ? 47.519 24.923  -16.878 0.00 49.71  ? 701  LEU   B H    1 
ATOM   22318 H HA   . LEU   B  1 675 ? 47.178 27.261  -18.623 0.00 53.79  ? 701  LEU   B HA   1 
ATOM   22319 H HB2  . LEU   B  1 675 ? 46.017 26.412  -15.955 0.00 55.31  ? 701  LEU   B HB2  1 
ATOM   22320 H HB3  . LEU   B  1 675 ? 45.724 27.981  -16.726 0.00 55.70  ? 701  LEU   B HB3  1 
ATOM   22321 H HG   . LEU   B  1 675 ? 45.057 25.403  -18.164 0.00 56.65  ? 701  LEU   B HG   1 
ATOM   22322 H HD11 . LEU   B  1 675 ? 42.788 25.587  -17.319 0.00 58.27  ? 701  LEU   B HD11 1 
ATOM   22323 H HD12 . LEU   B  1 675 ? 43.953 25.269  -16.008 0.00 58.52  ? 701  LEU   B HD12 1 
ATOM   22324 H HD13 . LEU   B  1 675 ? 43.293 26.910  -16.236 0.00 59.16  ? 701  LEU   B HD13 1 
ATOM   22325 H HD21 . LEU   B  1 675 ? 43.391 26.847  -19.232 0.00 58.14  ? 701  LEU   B HD21 1 
ATOM   22326 H HD22 . LEU   B  1 675 ? 44.020 28.236  -18.310 0.00 59.01  ? 701  LEU   B HD22 1 
ATOM   22327 H HD23 . LEU   B  1 675 ? 45.054 27.408  -19.505 0.00 58.20  ? 701  LEU   B HD23 1 
ATOM   22328 N N    . PHE   B  1 676 ? 49.158 27.161  -16.047 1.00 45.48  ? 702  PHE   B N    1 
ATOM   22329 C CA   . PHE   B  1 676 ? 50.146 27.947  -15.324 1.00 47.95  ? 702  PHE   B CA   1 
ATOM   22330 C C    . PHE   B  1 676 ? 51.361 27.114  -14.931 1.00 48.93  ? 702  PHE   B C    1 
ATOM   22331 O O    . PHE   B  1 676 ? 51.338 25.882  -15.008 1.00 48.90  ? 702  PHE   B O    1 
ATOM   22332 C CB   . PHE   B  1 676 ? 49.506 28.648  -14.106 1.00 49.03  ? 702  PHE   B CB   1 
ATOM   22333 C CG   . PHE   B  1 676 ? 48.675 27.750  -13.223 1.00 51.00  ? 702  PHE   B CG   1 
ATOM   22334 C CD1  . PHE   B  1 676 ? 49.272 26.958  -12.254 1.00 52.44  ? 702  PHE   B CD1  1 
ATOM   22335 C CD2  . PHE   B  1 676 ? 47.296 27.725  -13.337 1.00 52.14  ? 702  PHE   B CD2  1 
ATOM   22336 C CE1  . PHE   B  1 676 ? 48.505 26.137  -11.438 1.00 53.38  ? 702  PHE   B CE1  1 
ATOM   22337 C CE2  . PHE   B  1 676 ? 46.534 26.896  -12.526 1.00 53.22  ? 702  PHE   B CE2  1 
ATOM   22338 C CZ   . PHE   B  1 676 ? 47.140 26.119  -11.573 1.00 53.22  ? 702  PHE   B CZ   1 
ATOM   22339 H H    . PHE   B  1 676 ? 49.185 26.174  -15.815 0.00 59.38  ? 702  PHE   B H    1 
ATOM   22340 H HA   . PHE   B  1 676 ? 50.520 28.730  -15.983 0.00 63.43  ? 702  PHE   B HA   1 
ATOM   22341 H HB2  . PHE   B  1 676 ? 50.296 29.071  -13.487 0.00 65.89  ? 702  PHE   B HB2  1 
ATOM   22342 H HB3  . PHE   B  1 676 ? 48.860 29.447  -14.466 0.00 65.64  ? 702  PHE   B HB3  1 
ATOM   22343 H HD1  . PHE   B  1 676 ? 50.344 26.963  -12.143 0.00 69.60  ? 702  PHE   B HD1  1 
ATOM   22344 H HD2  . PHE   B  1 676 ? 46.809 28.333  -14.081 0.00 69.01  ? 702  PHE   B HD2  1 
ATOM   22345 H HE1  . PHE   B  1 676 ? 48.985 25.522  -10.692 0.00 70.70  ? 702  PHE   B HE1  1 
ATOM   22346 H HE2  . PHE   B  1 676 ? 45.461 26.883  -12.630 0.00 70.26  ? 702  PHE   B HE2  1 
ATOM   22347 H HZ   . PHE   B  1 676 ? 46.544 25.485  -10.940 0.00 70.35  ? 702  PHE   B HZ   1 
ATOM   22348 N N    . LEU   B  1 677 ? 52.438 27.817  -14.545 1.00 49.40  ? 703  LEU   B N    1 
ATOM   22349 C CA   . LEU   B  1 677 ? 53.719 27.252  -14.137 1.00 50.32  ? 703  LEU   B CA   1 
ATOM   22350 C C    . LEU   B  1 677 ? 54.005 27.612  -12.685 1.00 51.03  ? 703  LEU   B C    1 
ATOM   22351 O O    . LEU   B  1 677 ? 53.594 28.675  -12.223 1.00 51.37  ? 703  LEU   B O    1 
ATOM   22352 C CB   . LEU   B  1 677 ? 54.824 27.852  -15.032 1.00 50.77  ? 703  LEU   B CB   1 
ATOM   22353 C CG   . LEU   B  1 677 ? 55.370 27.040  -16.220 1.00 52.66  ? 703  LEU   B CG   1 
ATOM   22354 C CD1  . LEU   B  1 677 ? 54.310 26.200  -16.899 1.00 52.97  ? 703  LEU   B CD1  1 
ATOM   22355 C CD2  . LEU   B  1 677 ? 56.004 27.968  -17.239 1.00 53.77  ? 703  LEU   B CD2  1 
ATOM   22356 H H    . LEU   B  1 677 ? 52.423 28.830  -14.484 0.00 65.91  ? 703  LEU   B H    1 
ATOM   22357 H HA   . LEU   B  1 677 ? 53.717 26.166  -14.211 0.00 66.06  ? 703  LEU   B HA   1 
ATOM   22358 H HB2  . LEU   B  1 677 ? 54.458 28.790  -15.449 0.00 67.26  ? 703  LEU   B HB2  1 
ATOM   22359 H HB3  . LEU   B  1 677 ? 55.677 28.068  -14.390 0.00 67.53  ? 703  LEU   B HB3  1 
ATOM   22360 H HG   . LEU   B  1 677 ? 56.145 26.365  -15.857 0.00 68.50  ? 703  LEU   B HG   1 
ATOM   22361 H HD11 . LEU   B  1 677 ? 54.654 25.918  -17.893 0.00 67.74  ? 703  LEU   B HD11 1 
ATOM   22362 H HD12 . LEU   B  1 677 ? 54.132 25.302  -16.310 0.00 68.06  ? 703  LEU   B HD12 1 
ATOM   22363 H HD13 . LEU   B  1 677 ? 53.395 26.786  -16.974 0.00 68.35  ? 703  LEU   B HD13 1 
ATOM   22364 H HD21 . LEU   B  1 677 ? 56.505 27.374  -18.002 0.00 69.46  ? 703  LEU   B HD21 1 
ATOM   22365 H HD22 . LEU   B  1 677 ? 55.228 28.581  -17.694 0.00 69.83  ? 703  LEU   B HD22 1 
ATOM   22366 H HD23 . LEU   B  1 677 ? 56.727 28.606  -16.732 0.00 70.51  ? 703  LEU   B HD23 1 
ATOM   22367 N N    . THR   B  1 678 ? 54.728 26.741  -11.971 1.00 51.31  ? 704  THR   B N    1 
ATOM   22368 C CA   . THR   B  1 678 ? 55.075 26.998  -10.572 1.00 51.91  ? 704  THR   B CA   1 
ATOM   22369 C C    . THR   B  1 678 ? 56.032 28.192  -10.475 1.00 52.20  ? 704  THR   B C    1 
ATOM   22370 O O    . THR   B  1 678 ? 56.869 28.390  -11.358 1.00 52.10  ? 704  THR   B O    1 
ATOM   22371 C CB   . THR   B  1 678 ? 55.694 25.739  -9.915  1.00 53.36  ? 704  THR   B CB   1 
ATOM   22372 O OG1  . THR   B  1 678 ? 55.704 25.894  -8.483  1.00 55.04  ? 704  THR   B OG1  1 
ATOM   22373 C CG2  . THR   B  1 678 ? 57.093 25.412  -10.463 1.00 53.62  ? 704  THR   B CG2  1 
ATOM   22374 H H    . THR   B  1 678 ? 55.070 25.855  -12.329 0.00 68.08  ? 704  THR   B H    1 
ATOM   22375 H HA   . THR   B  1 678 ? 54.157 27.254  -10.044 0.00 70.36  ? 704  THR   B HA   1 
ATOM   22376 H HB   . THR   B  1 678 ? 55.061 24.882  -10.139 0.00 71.19  ? 704  THR   B HB   1 
ATOM   22377 H HG1  . THR   B  1 678 ? 56.540 26.307  -8.143  0.00 74.88  ? 704  THR   B HG1  1 
ATOM   22378 H HG21 . THR   B  1 678 ? 57.415 24.440  -10.093 0.00 71.62  ? 704  THR   B HG21 1 
ATOM   22379 H HG22 . THR   B  1 678 ? 57.072 25.386  -11.552 0.00 71.24  ? 704  THR   B HG22 1 
ATOM   22380 H HG23 . THR   B  1 678 ? 57.825 26.150  -10.140 0.00 72.34  ? 704  THR   B HG23 1 
ATOM   22381 N N    . ASP   B  1 679 ? 55.902 28.978  -9.400  1.00 52.27  ? 705  ASP   B N    1 
ATOM   22382 C CA   . ASP   B  1 679 ? 56.752 30.145  -9.162  1.00 52.88  ? 705  ASP   B CA   1 
ATOM   22383 C C    . ASP   B  1 679 ? 58.004 29.821  -8.313  1.00 53.40  ? 705  ASP   B C    1 
ATOM   22384 O O    . ASP   B  1 679 ? 58.695 30.745  -7.896  1.00 53.57  ? 705  ASP   B O    1 
ATOM   22385 C CB   . ASP   B  1 679 ? 55.933 31.272  -8.498  1.00 54.36  ? 705  ASP   B CB   1 
ATOM   22386 C CG   . ASP   B  1 679 ? 55.449 30.983  -7.087  1.00 58.62  ? 705  ASP   B CG   1 
ATOM   22387 O OD1  . ASP   B  1 679 ? 55.438 29.795  -6.692  1.00 59.05  ? 705  ASP   B OD1  1 
ATOM   22388 O OD2  . ASP   B  1 679 ? 55.054 31.942  -6.389  1.00 60.80  ? 705  ASP   B OD2  1 
ATOM   22389 H H    . ASP   B  1 679 ? 55.214 28.812  -8.673  0.00 72.29  ? 705  ASP   B H    1 
ATOM   22390 H HA   . ASP   B  1 679 ? 57.098 30.542  -10.114 0.00 73.39  ? 705  ASP   B HA   1 
ATOM   22391 H HB2  . ASP   B  1 679 ? 56.539 32.176  -8.462  0.00 76.74  ? 705  ASP   B HB2  1 
ATOM   22392 H HB3  . ASP   B  1 679 ? 55.051 31.456  -9.110  0.00 75.85  ? 705  ASP   B HB3  1 
ATOM   22393 N N    . SER   B  1 680 ? 58.308 28.524  -8.072  1.00 53.40  ? 706  SER   B N    1 
ATOM   22394 C CA   . SER   B  1 680 ? 59.421 28.099  -7.218  1.00 53.60  ? 706  SER   B CA   1 
ATOM   22395 C C    . SER   B  1 680 ? 59.977 26.746  -7.703  1.00 53.33  ? 706  SER   B C    1 
ATOM   22396 O O    . SER   B  1 680 ? 60.146 25.814  -6.912  1.00 53.44  ? 706  SER   B O    1 
ATOM   22397 C CB   . SER   B  1 680 ? 58.954 27.990  -5.765  1.00 55.19  ? 706  SER   B CB   1 
ATOM   22398 O OG   . SER   B  1 680 ? 58.347 29.188  -5.309  1.00 58.25  ? 706  SER   B OG   1 
ATOM   22399 H H    . SER   B  1 680 ? 57.821 27.737  -8.485  0.00 73.67  ? 706  SER   B H    1 
ATOM   22400 H HA   . SER   B  1 680 ? 60.230 28.826  -7.263  0.00 75.47  ? 706  SER   B HA   1 
ATOM   22401 H HB2  . SER   B  1 680 ? 58.230 27.181  -5.686  0.00 77.09  ? 706  SER   B HB2  1 
ATOM   22402 H HB3  . SER   B  1 680 ? 59.815 27.779  -5.132  0.00 77.99  ? 706  SER   B HB3  1 
ATOM   22403 H HG   . SER   B  1 680 ? 57.390 29.209  -5.576  0.00 81.60  ? 706  SER   B HG   1 
ATOM   22404 N N    . LEU   B  1 681 ? 60.279 26.646  -9.001  1.00 52.73  ? 707  LEU   B N    1 
ATOM   22405 C CA   . LEU   B  1 681 ? 60.807 25.412  -9.590  1.00 52.54  ? 707  LEU   B CA   1 
ATOM   22406 C C    . LEU   B  1 681 ? 62.175 25.017  -9.018  1.00 52.01  ? 707  LEU   B C    1 
ATOM   22407 O O    . LEU   B  1 681 ? 62.460 23.825  -8.916  1.00 51.72  ? 707  LEU   B O    1 
ATOM   22408 C CB   . LEU   B  1 681 ? 60.869 25.541  -11.122 1.00 53.01  ? 707  LEU   B CB   1 
ATOM   22409 C CG   . LEU   B  1 681 ? 61.168 24.271  -11.938 1.00 54.63  ? 707  LEU   B CG   1 
ATOM   22410 C CD1  . LEU   B  1 681 ? 60.195 23.147  -11.610 1.00 55.15  ? 707  LEU   B CD1  1 
ATOM   22411 C CD2  . LEU   B  1 681 ? 61.085 24.559  -13.420 1.00 55.39  ? 707  LEU   B CD2  1 
ATOM   22412 H H    . LEU   B  1 681 ? 60.181 27.407  -9.665  0.00 72.52  ? 707  LEU   B H    1 
ATOM   22413 H HA   . LEU   B  1 681 ? 60.110 24.616  -9.338  0.00 71.29  ? 707  LEU   B HA   1 
ATOM   22414 H HB2  . LEU   B  1 681 ? 59.911 25.924  -11.471 0.00 71.29  ? 707  LEU   B HB2  1 
ATOM   22415 H HB3  . LEU   B  1 681 ? 61.646 26.264  -11.362 0.00 71.83  ? 707  LEU   B HB3  1 
ATOM   22416 H HG   . LEU   B  1 681 ? 62.175 23.922  -11.715 0.00 72.79  ? 707  LEU   B HG   1 
ATOM   22417 H HD11 . LEU   B  1 681 ? 60.279 22.375  -12.372 0.00 72.16  ? 707  LEU   B HD11 1 
ATOM   22418 H HD12 . LEU   B  1 681 ? 60.454 22.726  -10.639 0.00 73.14  ? 707  LEU   B HD12 1 
ATOM   22419 H HD13 . LEU   B  1 681 ? 59.182 23.548  -11.587 0.00 72.75  ? 707  LEU   B HD13 1 
ATOM   22420 H HD21 . LEU   B  1 681 ? 61.815 23.942  -13.940 0.00 72.59  ? 707  LEU   B HD21 1 
ATOM   22421 H HD22 . LEU   B  1 681 ? 60.084 24.310  -13.768 0.00 72.48  ? 707  LEU   B HD22 1 
ATOM   22422 H HD23 . LEU   B  1 681 ? 61.276 25.616  -13.601 0.00 73.29  ? 707  LEU   B HD23 1 
ATOM   22423 N N    . SER   B  1 682 ? 62.993 26.009  -8.604  1.00 51.68  ? 708  SER   B N    1 
ATOM   22424 C CA   . SER   B  1 682 ? 64.307 25.777  -7.993  1.00 51.59  ? 708  SER   B CA   1 
ATOM   22425 C C    . SER   B  1 682 ? 64.199 25.010  -6.662  1.00 50.89  ? 708  SER   B C    1 
ATOM   22426 O O    . SER   B  1 682 ? 65.128 24.291  -6.294  1.00 50.77  ? 708  SER   B O    1 
ATOM   22427 C CB   . SER   B  1 682 ? 65.033 27.104  -7.776  1.00 53.16  ? 708  SER   B CB   1 
ATOM   22428 O OG   . SER   B  1 682 ? 64.203 28.045  -7.109  1.00 55.59  ? 708  SER   B OG   1 
ATOM   22429 H H    . SER   B  1 682 ? 62.771 26.995  -8.697  0.00 72.14  ? 708  SER   B H    1 
ATOM   22430 H HA   . SER   B  1 682 ? 64.907 25.178  -8.677  0.00 71.83  ? 708  SER   B HA   1 
ATOM   22431 H HB2  . SER   B  1 682 ? 65.921 26.926  -7.172  0.00 75.54  ? 708  SER   B HB2  1 
ATOM   22432 H HB3  . SER   B  1 682 ? 65.319 27.512  -8.745  0.00 74.76  ? 708  SER   B HB3  1 
ATOM   22433 H HG   . SER   B  1 682 ? 64.691 28.900  -6.985  0.00 79.09  ? 708  SER   B HG   1 
ATOM   22434 N N    . ASP   B  1 683 ? 63.078 25.164  -5.942  1.00 50.44  ? 709  ASP   B N    1 
ATOM   22435 C CA   . ASP   B  1 683 ? 62.833 24.435  -4.694  1.00 50.39  ? 709  ASP   B CA   1 
ATOM   22436 C C    . ASP   B  1 683 ? 62.491 22.958  -4.949  1.00 49.61  ? 709  ASP   B C    1 
ATOM   22437 O O    . ASP   B  1 683 ? 62.650 22.140  -4.045  1.00 49.64  ? 709  ASP   B O    1 
ATOM   22438 C CB   . ASP   B  1 683 ? 61.668 25.072  -3.915  1.00 52.37  ? 709  ASP   B CB   1 
ATOM   22439 C CG   . ASP   B  1 683 ? 61.939 26.469  -3.392  1.00 57.54  ? 709  ASP   B CG   1 
ATOM   22440 O OD1  . ASP   B  1 683 ? 63.123 26.862  -3.334  1.00 58.83  ? 709  ASP   B OD1  1 
ATOM   22441 O OD2  . ASP   B  1 683 ? 60.966 27.163  -3.028  1.00 59.44  ? 709  ASP   B OD2  1 
ATOM   22442 H H    . ASP   B  1 683 ? 62.331 25.807  -6.183  0.00 71.43  ? 709  ASP   B H    1 
ATOM   22443 H HA   . ASP   B  1 683 ? 63.723 24.462  -4.068  0.00 72.40  ? 709  ASP   B HA   1 
ATOM   22444 H HB2  . ASP   B  1 683 ? 60.794 25.123  -4.563  0.00 74.04  ? 709  ASP   B HB2  1 
ATOM   22445 H HB3  . ASP   B  1 683 ? 61.446 24.439  -3.057  0.00 74.81  ? 709  ASP   B HB3  1 
ATOM   22446 N N    . PHE   B  1 684 ? 61.984 22.623  -6.154  1.00 48.77  ? 710  PHE   B N    1 
ATOM   22447 C CA   . PHE   B  1 684 ? 61.560 21.270  -6.487  1.00 48.25  ? 710  PHE   B CA   1 
ATOM   22448 C C    . PHE   B  1 684 ? 62.551 20.505  -7.354  1.00 47.63  ? 710  PHE   B C    1 
ATOM   22449 O O    . PHE   B  1 684 ? 62.460 19.278  -7.411  1.00 47.99  ? 710  PHE   B O    1 
ATOM   22450 C CB   . PHE   B  1 684 ? 60.168 21.291  -7.138  1.00 47.99  ? 710  PHE   B CB   1 
ATOM   22451 C CG   . PHE   B  1 684 ? 59.162 22.160  -6.412  1.00 48.42  ? 710  PHE   B CG   1 
ATOM   22452 C CD1  . PHE   B  1 684 ? 59.066 22.132  -5.029  1.00 49.18  ? 710  PHE   B CD1  1 
ATOM   22453 C CD2  . PHE   B  1 684 ? 58.299 22.985  -7.114  1.00 49.11  ? 710  PHE   B CD2  1 
ATOM   22454 C CE1  . PHE   B  1 684 ? 58.141 22.928  -4.365  1.00 49.94  ? 710  PHE   B CE1  1 
ATOM   22455 C CE2  . PHE   B  1 684 ? 57.382 23.787  -6.446  1.00 49.82  ? 710  PHE   B CE2  1 
ATOM   22456 C CZ   . PHE   B  1 684 ? 57.312 23.757  -5.078  1.00 49.74  ? 710  PHE   B CZ   1 
ATOM   22457 H H    . PHE   B  1 684 ? 61.840 23.271  -6.921  0.00 67.92  ? 710  PHE   B H    1 
ATOM   22458 H HA   . PHE   B  1 684 ? 61.456 20.706  -5.565  0.00 67.06  ? 710  PHE   B HA   1 
ATOM   22459 H HB2  . PHE   B  1 684 ? 60.265 21.666  -8.155  0.00 65.42  ? 710  PHE   B HB2  1 
ATOM   22460 H HB3  . PHE   B  1 684 ? 59.776 20.275  -7.159  0.00 65.37  ? 710  PHE   B HB3  1 
ATOM   22461 H HD1  . PHE   B  1 684 ? 59.710 21.486  -4.454  0.00 68.69  ? 710  PHE   B HD1  1 
ATOM   22462 H HD2  . PHE   B  1 684 ? 58.355 23.032  -8.188  0.00 66.86  ? 710  PHE   B HD2  1 
ATOM   22463 H HE1  . PHE   B  1 684 ? 58.082 22.899  -3.290  0.00 70.44  ? 710  PHE   B HE1  1 
ATOM   22464 H HE2  . PHE   B  1 684 ? 56.725 24.436  -7.004  0.00 68.59  ? 710  PHE   B HE2  1 
ATOM   22465 H HZ   . PHE   B  1 684 ? 56.590 24.370  -4.563  0.00 69.77  ? 710  PHE   B HZ   1 
ATOM   22466 N N    . THR   B  1 685 ? 63.482 21.191  -8.043  1.00 46.32  ? 711  THR   B N    1 
ATOM   22467 C CA   . THR   B  1 685 ? 64.461 20.490  -8.874  1.00 45.72  ? 711  THR   B CA   1 
ATOM   22468 C C    . THR   B  1 685 ? 65.742 21.279  -9.045  1.00 45.74  ? 711  THR   B C    1 
ATOM   22469 O O    . THR   B  1 685 ? 65.710 22.499  -9.165  1.00 46.27  ? 711  THR   B O    1 
ATOM   22470 C CB   . THR   B  1 685 ? 63.860 20.098  -10.249 1.00 46.07  ? 711  THR   B CB   1 
ATOM   22471 O OG1  . THR   B  1 685 ? 64.800 19.283  -10.949 1.00 46.16  ? 711  THR   B OG1  1 
ATOM   22472 C CG2  . THR   B  1 685 ? 63.475 21.303  -11.105 1.00 46.44  ? 711  THR   B CG2  1 
ATOM   22473 H H    . THR   B  1 685 ? 63.579 22.201  -8.059  0.00 64.40  ? 711  THR   B H    1 
ATOM   22474 H HA   . THR   B  1 685 ? 64.732 19.561  -8.373  0.00 62.95  ? 711  THR   B HA   1 
ATOM   22475 H HB   . THR   B  1 685 ? 62.957 19.515  -10.082 0.00 62.03  ? 711  THR   B HB   1 
ATOM   22476 H HG1  . THR   B  1 685 ? 64.344 18.783  -11.676 0.00 61.47  ? 711  THR   B HG1  1 
ATOM   22477 H HG21 . THR   B  1 685 ? 62.899 20.969  -11.967 0.00 61.99  ? 711  THR   B HG21 1 
ATOM   22478 H HG22 . THR   B  1 685 ? 62.871 22.002  -10.529 0.00 63.03  ? 711  THR   B HG22 1 
ATOM   22479 H HG23 . THR   B  1 685 ? 64.366 21.816  -11.462 0.00 62.85  ? 711  THR   B HG23 1 
ATOM   22480 N N    . SER   B  1 686 ? 66.872 20.565  -9.055  1.00 45.18  ? 712  SER   B N    1 
ATOM   22481 C CA   . SER   B  1 686 ? 68.200 21.119  -9.307  1.00 44.91  ? 712  SER   B CA   1 
ATOM   22482 C C    . SER   B  1 686 ? 68.941 20.337  -10.423 1.00 43.69  ? 712  SER   B C    1 
ATOM   22483 O O    . SER   B  1 686 ? 70.092 20.660  -10.707 1.00 44.06  ? 712  SER   B O    1 
ATOM   22484 C CB   . SER   B  1 686 ? 69.029 21.103  -8.029  1.00 47.02  ? 712  SER   B CB   1 
ATOM   22485 O OG   . SER   B  1 686 ? 69.307 19.773  -7.624  1.00 50.16  ? 712  SER   B OG   1 
ATOM   22486 H H    . SER   B  1 686 ? 66.903 19.568  -8.869  0.00 62.63  ? 712  SER   B H    1 
ATOM   22487 H HA   . SER   B  1 686 ? 68.119 22.153  -9.635  0.00 63.11  ? 712  SER   B HA   1 
ATOM   22488 H HB2  . SER   B  1 686 ? 69.967 21.627  -8.202  0.00 66.84  ? 712  SER   B HB2  1 
ATOM   22489 H HB3  . SER   B  1 686 ? 68.468 21.600  -7.239  0.00 66.86  ? 712  SER   B HB3  1 
ATOM   22490 H HG   . SER   B  1 686 ? 69.851 19.778  -6.794  0.00 70.78  ? 712  SER   B HG   1 
ATOM   22491 N N    . SER   B  1 687 ? 68.285 19.347  -11.079 1.00 42.04  ? 713  SER   B N    1 
ATOM   22492 C CA   . SER   B  1 687 ? 68.873 18.543  -12.147 1.00 40.69  ? 713  SER   B CA   1 
ATOM   22493 C C    . SER   B  1 687 ? 68.233 18.805  -13.516 1.00 39.29  ? 713  SER   B C    1 
ATOM   22494 O O    . SER   B  1 687 ? 68.846 18.496  -14.537 1.00 38.69  ? 713  SER   B O    1 
ATOM   22495 C CB   . SER   B  1 687 ? 68.724 17.062  -11.814 1.00 41.55  ? 713  SER   B CB   1 
ATOM   22496 O OG   . SER   B  1 687 ? 67.384 16.736  -11.479 1.00 42.43  ? 713  SER   B OG   1 
ATOM   22497 H H    . SER   B  1 687 ? 67.328 19.069  -10.886 0.00 57.81  ? 713  SER   B H    1 
ATOM   22498 H HA   . SER   B  1 687 ? 69.938 18.749  -12.237 0.00 56.24  ? 713  SER   B HA   1 
ATOM   22499 H HB2  . SER   B  1 687 ? 69.029 16.472  -12.677 0.00 56.18  ? 713  SER   B HB2  1 
ATOM   22500 H HB3  . SER   B  1 687 ? 69.365 16.829  -10.965 0.00 57.22  ? 713  SER   B HB3  1 
ATOM   22501 H HG   . SER   B  1 687 ? 66.869 16.512  -12.298 0.00 56.77  ? 713  SER   B HG   1 
ATOM   22502 N N    . LEU   B  1 688 ? 66.995 19.329  -13.549 1.00 38.21  ? 714  LEU   B N    1 
ATOM   22503 C CA   . LEU   B  1 688 ? 66.286 19.553  -14.806 1.00 37.46  ? 714  LEU   B CA   1 
ATOM   22504 C C    . LEU   B  1 688 ? 67.066 20.485  -15.737 1.00 36.61  ? 714  LEU   B C    1 
ATOM   22505 O O    . LEU   B  1 688 ? 67.388 21.603  -15.344 1.00 37.37  ? 714  LEU   B O    1 
ATOM   22506 C CB   . LEU   B  1 688 ? 64.887 20.128  -14.514 1.00 37.37  ? 714  LEU   B CB   1 
ATOM   22507 C CG   . LEU   B  1 688 ? 63.881 20.076  -15.648 1.00 38.43  ? 714  LEU   B CG   1 
ATOM   22508 C CD1  . LEU   B  1 688 ? 63.573 18.630  -16.043 1.00 38.77  ? 714  LEU   B CD1  1 
ATOM   22509 C CD2  . LEU   B  1 688 ? 62.605 20.783  -15.255 1.00 38.58  ? 714  LEU   B CD2  1 
ATOM   22510 H H    . LEU   B  1 688 ? 66.470 19.606  -12.726 0.00 52.23  ? 714  LEU   B H    1 
ATOM   22511 H HA   . LEU   B  1 688 ? 66.182 18.583  -15.290 0.00 49.76  ? 714  LEU   B HA   1 
ATOM   22512 H HB2  . LEU   B  1 688 ? 64.446 19.574  -13.687 0.00 50.22  ? 714  LEU   B HB2  1 
ATOM   22513 H HB3  . LEU   B  1 688 ? 64.999 21.173  -14.226 0.00 50.60  ? 714  LEU   B HB3  1 
ATOM   22514 H HG   . LEU   B  1 688 ? 64.289 20.587  -16.519 0.00 50.50  ? 714  LEU   B HG   1 
ATOM   22515 H HD11 . LEU   B  1 688 ? 62.646 18.619  -16.613 0.00 49.95  ? 714  LEU   B HD11 1 
ATOM   22516 H HD12 . LEU   B  1 688 ? 64.377 18.246  -16.668 0.00 50.21  ? 714  LEU   B HD12 1 
ATOM   22517 H HD13 . LEU   B  1 688 ? 63.467 18.020  -15.147 0.00 50.59  ? 714  LEU   B HD13 1 
ATOM   22518 H HD21 . LEU   B  1 688 ? 61.949 20.826  -16.121 0.00 50.42  ? 714  LEU   B HD21 1 
ATOM   22519 H HD22 . LEU   B  1 688 ? 62.126 20.227  -14.450 0.00 51.00  ? 714  LEU   B HD22 1 
ATOM   22520 H HD23 . LEU   B  1 688 ? 62.839 21.792  -14.919 0.00 51.44  ? 714  LEU   B HD23 1 
ATOM   22521 N N    . ARG   B  1 689 ? 67.414 19.993  -16.933 1.00 34.88  ? 715  ARG   B N    1 
ATOM   22522 C CA   . ARG   B  1 689 ? 68.169 20.726  -17.952 1.00 34.19  ? 715  ARG   B CA   1 
ATOM   22523 C C    . ARG   B  1 689 ? 67.277 21.132  -19.119 1.00 32.32  ? 715  ARG   B C    1 
ATOM   22524 O O    . ARG   B  1 689 ? 67.531 22.165  -19.726 1.00 32.80  ? 715  ARG   B O    1 
ATOM   22525 C CB   . ARG   B  1 689 ? 69.309 19.860  -18.500 1.00 36.61  ? 715  ARG   B CB   1 
ATOM   22526 C CG   . ARG   B  1 689 ? 70.398 19.526  -17.486 1.00 42.23  ? 715  ARG   B CG   1 
ATOM   22527 C CD   . ARG   B  1 689 ? 71.421 18.611  -18.146 1.00 48.22  ? 715  ARG   B CD   1 
ATOM   22528 N NE   . ARG   B  1 689 ? 72.530 18.264  -17.255 1.00 53.97  ? 715  ARG   B NE   1 
ATOM   22529 C CZ   . ARG   B  1 689 ? 73.554 17.483  -17.595 1.00 58.07  ? 715  ARG   B CZ   1 
ATOM   22530 N NH1  . ARG   B  1 689 ? 73.622 16.952  -18.815 1.00 58.29  ? 715  ARG   B NH1  1 
ATOM   22531 N NH2  . ARG   B  1 689 ? 74.519 17.223  -16.717 1.00 58.51  ? 715  ARG   B NH2  1 
ATOM   22532 H H    . ARG   B  1 689 ? 67.182 19.051  -17.234 0.00 46.22  ? 715  ARG   B H    1 
ATOM   22533 H HA   . ARG   B  1 689 ? 68.622 21.622  -17.532 0.00 46.43  ? 715  ARG   B HA   1 
ATOM   22534 H HB2  . ARG   B  1 689 ? 68.895 18.918  -18.859 0.00 48.06  ? 715  ARG   B HB2  1 
ATOM   22535 H HB3  . ARG   B  1 689 ? 69.782 20.394  -19.323 0.00 48.54  ? 715  ARG   B HB3  1 
ATOM   22536 H HG2  . ARG   B  1 689 ? 70.896 20.441  -17.168 0.00 56.56  ? 715  ARG   B HG2  1 
ATOM   22537 H HG3  . ARG   B  1 689 ? 69.963 19.002  -16.636 0.00 56.08  ? 715  ARG   B HG3  1 
ATOM   22538 H HD2  . ARG   B  1 689 ? 70.931 17.686  -18.449 0.00 62.46  ? 715  ARG   B HD2  1 
ATOM   22539 H HD3  . ARG   B  1 689 ? 71.836 19.120  -19.015 0.00 62.90  ? 715  ARG   B HD3  1 
ATOM   22540 H HE   . ARG   B  1 689 ? 72.513 18.653  -16.318 0.00 71.06  ? 715  ARG   B HE   1 
ATOM   22541 H HH11 . ARG   B  1 689 ? 72.905 17.126  -19.513 0.00 74.61  ? 715  ARG   B HH11 1 
ATOM   22542 H HH12 . ARG   B  1 689 ? 74.406 16.357  -19.061 0.00 75.15  ? 715  ARG   B HH12 1 
ATOM   22543 H HH21 . ARG   B  1 689 ? 74.481 17.617  -15.782 0.00 77.19  ? 715  ARG   B HH21 1 
ATOM   22544 H HH22 . ARG   B  1 689 ? 75.299 16.627  -16.975 0.00 76.72  ? 715  ARG   B HH22 1 
ATOM   22545 N N    . THR   B  1 690 ? 66.270 20.314  -19.464 1.00 29.98  ? 716  THR   B N    1 
ATOM   22546 C CA   . THR   B  1 690 ? 65.376 20.592  -20.591 1.00 28.88  ? 716  THR   B CA   1 
ATOM   22547 C C    . THR   B  1 690 ? 63.922 20.483  -20.158 1.00 27.62  ? 716  THR   B C    1 
ATOM   22548 O O    . THR   B  1 690 ? 63.526 19.481  -19.563 1.00 27.47  ? 716  THR   B O    1 
ATOM   22549 C CB   . THR   B  1 690 ? 65.664 19.628  -21.731 1.00 30.17  ? 716  THR   B CB   1 
ATOM   22550 O OG1  . THR   B  1 690 ? 67.024 19.816  -22.156 1.00 31.52  ? 716  THR   B OG1  1 
ATOM   22551 C CG2  . THR   B  1 690 ? 64.720 19.840  -22.904 1.00 30.43  ? 716  THR   B CG2  1 
ATOM   22552 H H    . THR   B  1 690 ? 66.052 19.440  -18.996 0.00 39.44  ? 716  THR   B H    1 
ATOM   22553 H HA   . THR   B  1 690 ? 65.541 21.599  -20.968 0.00 37.87  ? 716  THR   B HA   1 
ATOM   22554 H HB   . THR   B  1 690 ? 65.542 18.607  -21.374 0.00 38.41  ? 716  THR   B HB   1 
ATOM   22555 H HG1  . THR   B  1 690 ? 67.284 19.102  -22.795 0.00 40.08  ? 716  THR   B HG1  1 
ATOM   22556 H HG21 . THR   B  1 690 ? 65.164 19.437  -23.813 0.00 38.01  ? 716  THR   B HG21 1 
ATOM   22557 H HG22 . THR   B  1 690 ? 63.776 19.325  -22.730 0.00 38.06  ? 716  THR   B HG22 1 
ATOM   22558 H HG23 . THR   B  1 690 ? 64.526 20.902  -23.041 0.00 38.55  ? 716  THR   B HG23 1 
ATOM   22559 N N    . LEU   B  1 691 ? 63.137 21.530  -20.423 1.00 26.58  ? 717  LEU   B N    1 
ATOM   22560 C CA   . LEU   B  1 691 ? 61.729 21.576  -20.038 1.00 26.15  ? 717  LEU   B CA   1 
ATOM   22561 C C    . LEU   B  1 691 ? 60.938 21.943  -21.279 1.00 26.45  ? 717  LEU   B C    1 
ATOM   22562 O O    . LEU   B  1 691 ? 61.048 23.071  -21.765 1.00 26.70  ? 717  LEU   B O    1 
ATOM   22563 C CB   . LEU   B  1 691 ? 61.501 22.600  -18.904 1.00 25.90  ? 717  LEU   B CB   1 
ATOM   22564 C CG   . LEU   B  1 691 ? 60.042 22.797  -18.436 1.00 26.56  ? 717  LEU   B CG   1 
ATOM   22565 C CD1  . LEU   B  1 691 ? 59.382 21.469  -18.043 1.00 26.93  ? 717  LEU   B CD1  1 
ATOM   22566 C CD2  . LEU   B  1 691 ? 59.967 23.792  -17.271 1.00 27.05  ? 717  LEU   B CD2  1 
ATOM   22567 H H    . LEU   B  1 691 ? 63.440 22.361  -20.920 0.00 34.93  ? 717  LEU   B H    1 
ATOM   22568 H HA   . LEU   B  1 691 ? 61.395 20.598  -19.693 0.00 33.91  ? 717  LEU   B HA   1 
ATOM   22569 H HB2  . LEU   B  1 691 ? 62.078 22.278  -18.038 0.00 34.91  ? 717  LEU   B HB2  1 
ATOM   22570 H HB3  . LEU   B  1 691 ? 61.864 23.571  -19.239 0.00 34.85  ? 717  LEU   B HB3  1 
ATOM   22571 H HG   . LEU   B  1 691 ? 59.460 23.223  -19.251 0.00 35.10  ? 717  LEU   B HG   1 
ATOM   22572 H HD11 . LEU   B  1 691 ? 58.435 21.682  -17.548 0.00 35.53  ? 717  LEU   B HD11 1 
ATOM   22573 H HD12 . LEU   B  1 691 ? 59.197 20.886  -18.943 0.00 34.86  ? 717  LEU   B HD12 1 
ATOM   22574 H HD13 . LEU   B  1 691 ? 60.036 20.915  -17.373 0.00 35.62  ? 717  LEU   B HD13 1 
ATOM   22575 H HD21 . LEU   B  1 691 ? 58.926 23.945  -16.995 0.00 36.75  ? 717  LEU   B HD21 1 
ATOM   22576 H HD22 . LEU   B  1 691 ? 60.523 23.387  -16.426 0.00 37.04  ? 717  LEU   B HD22 1 
ATOM   22577 H HD23 . LEU   B  1 691 ? 60.407 24.737  -17.584 0.00 37.04  ? 717  LEU   B HD23 1 
ATOM   22578 N N    . LEU   B  1 692 ? 60.198 20.969  -21.837 1.00 26.06  ? 718  LEU   B N    1 
ATOM   22579 C CA   . LEU   B  1 692 ? 59.424 21.216  -23.048 1.00 26.55  ? 718  LEU   B CA   1 
ATOM   22580 C C    . LEU   B  1 692 ? 57.953 21.446  -22.709 1.00 26.85  ? 718  LEU   B C    1 
ATOM   22581 O O    . LEU   B  1 692 ? 57.294 20.554  -22.170 1.00 27.04  ? 718  LEU   B O    1 
ATOM   22582 C CB   . LEU   B  1 692 ? 59.605 20.099  -24.085 1.00 26.92  ? 718  LEU   B CB   1 
ATOM   22583 C CG   . LEU   B  1 692 ? 61.053 19.628  -24.356 1.00 28.67  ? 718  LEU   B CG   1 
ATOM   22584 C CD1  . LEU   B  1 692 ? 61.057 18.441  -25.305 1.00 28.89  ? 718  LEU   B CD1  1 
ATOM   22585 C CD2  . LEU   B  1 692 ? 61.912 20.772  -24.962 1.00 28.82  ? 718  LEU   B CD2  1 
ATOM   22586 H H    . LEU   B  1 692 ? 60.113 20.020  -21.484 0.00 32.78  ? 718  LEU   B H    1 
ATOM   22587 H HA   . LEU   B  1 692 ? 59.789 22.127  -23.511 0.00 33.30  ? 718  LEU   B HA   1 
ATOM   22588 H HB2  . LEU   B  1 692 ? 58.998 19.239  -23.811 0.00 32.67  ? 718  LEU   B HB2  1 
ATOM   22589 H HB3  . LEU   B  1 692 ? 59.237 20.490  -25.031 0.00 32.69  ? 718  LEU   B HB3  1 
ATOM   22590 H HG   . LEU   B  1 692 ? 61.515 19.309  -23.423 0.00 35.30  ? 718  LEU   B HG   1 
ATOM   22591 H HD11 . LEU   B  1 692 ? 62.048 17.989  -25.297 0.00 34.72  ? 718  LEU   B HD11 1 
ATOM   22592 H HD12 . LEU   B  1 692 ? 60.309 17.714  -24.991 0.00 34.47  ? 718  LEU   B HD12 1 
ATOM   22593 H HD13 . LEU   B  1 692 ? 60.829 18.799  -26.307 0.00 34.44  ? 718  LEU   B HD13 1 
ATOM   22594 H HD21 . LEU   B  1 692 ? 62.900 20.387  -25.208 0.00 35.46  ? 718  LEU   B HD21 1 
ATOM   22595 H HD22 . LEU   B  1 692 ? 61.423 21.137  -25.864 0.00 35.25  ? 718  LEU   B HD22 1 
ATOM   22596 H HD23 . LEU   B  1 692 ? 62.007 21.579  -24.236 0.00 35.97  ? 718  LEU   B HD23 1 
ATOM   22597 N N    . LEU   B  1 693 ? 57.453 22.667  -22.991 1.00 26.37  ? 719  LEU   B N    1 
ATOM   22598 C CA   . LEU   B  1 693 ? 56.080 23.048  -22.679 1.00 26.78  ? 719  LEU   B CA   1 
ATOM   22599 C C    . LEU   B  1 693 ? 55.317 23.609  -23.877 1.00 27.06  ? 719  LEU   B C    1 
ATOM   22600 O O    . LEU   B  1 693 ? 54.247 24.183  -23.671 1.00 27.46  ? 719  LEU   B O    1 
ATOM   22601 C CB   . LEU   B  1 693 ? 56.095 24.089  -21.546 1.00 27.20  ? 719  LEU   B CB   1 
ATOM   22602 C CG   . LEU   B  1 693 ? 56.488 23.584  -20.160 1.00 28.83  ? 719  LEU   B CG   1 
ATOM   22603 C CD1  . LEU   B  1 693 ? 56.940 24.740  -19.296 1.00 28.90  ? 719  LEU   B CD1  1 
ATOM   22604 C CD2  . LEU   B  1 693 ? 55.319 22.899  -19.487 1.00 29.87  ? 719  LEU   B CD2  1 
ATOM   22605 H H    . LEU   B  1 693 ? 57.977 23.415  -23.432 0.00 33.31  ? 719  LEU   B H    1 
ATOM   22606 H HA   . LEU   B  1 693 ? 55.520 22.177  -22.344 0.00 33.48  ? 719  LEU   B HA   1 
ATOM   22607 H HB2  . LEU   B  1 693 ? 56.802 24.873  -21.815 0.00 35.23  ? 719  LEU   B HB2  1 
ATOM   22608 H HB3  . LEU   B  1 693 ? 55.103 24.524  -21.434 0.00 35.07  ? 719  LEU   B HB3  1 
ATOM   22609 H HG   . LEU   B  1 693 ? 57.310 22.873  -20.238 0.00 37.07  ? 719  LEU   B HG   1 
ATOM   22610 H HD11 . LEU   B  1 693 ? 56.886 24.449  -18.249 0.00 38.40  ? 719  LEU   B HD11 1 
ATOM   22611 H HD12 . LEU   B  1 693 ? 57.966 24.992  -19.558 0.00 38.25  ? 719  LEU   B HD12 1 
ATOM   22612 H HD13 . LEU   B  1 693 ? 56.292 25.594  -19.493 0.00 38.31  ? 719  LEU   B HD13 1 
ATOM   22613 H HD21 . LEU   B  1 693 ? 55.685 22.357  -18.616 0.00 38.56  ? 719  LEU   B HD21 1 
ATOM   22614 H HD22 . LEU   B  1 693 ? 54.609 23.662  -19.170 0.00 38.70  ? 719  LEU   B HD22 1 
ATOM   22615 H HD23 . LEU   B  1 693 ? 54.830 22.214  -20.176 0.00 37.87  ? 719  LEU   B HD23 1 
ATOM   22616 N N    . SER   B  1 694 ? 55.817 23.428  -25.116 1.00 26.68  ? 720  SER   B N    1 
ATOM   22617 C CA   . SER   B  1 694 ? 55.122 23.961  -26.278 1.00 26.83  ? 720  SER   B CA   1 
ATOM   22618 C C    . SER   B  1 694 ? 53.729 23.343  -26.456 1.00 26.35  ? 720  SER   B C    1 
ATOM   22619 O O    . SER   B  1 694 ? 53.473 22.223  -26.016 1.00 25.82  ? 720  SER   B O    1 
ATOM   22620 C CB   . SER   B  1 694 ? 55.957 23.798  -27.540 1.00 28.55  ? 720  SER   B CB   1 
ATOM   22621 O OG   . SER   B  1 694 ? 56.157 22.439  -27.878 1.00 32.22  ? 720  SER   B OG   1 
ATOM   22622 H H    . SER   B  1 694 ? 56.675 22.938  -25.345 0.00 32.80  ? 720  SER   B H    1 
ATOM   22623 H HA   . SER   B  1 694 ? 54.984 25.030  -26.123 0.00 33.38  ? 720  SER   B HA   1 
ATOM   22624 H HB2  . SER   B  1 694 ? 55.445 24.293  -28.364 0.00 34.63  ? 720  SER   B HB2  1 
ATOM   22625 H HB3  . SER   B  1 694 ? 56.927 24.264  -27.378 0.00 34.96  ? 720  SER   B HB3  1 
ATOM   22626 H HG   . SER   B  1 694 ? 56.678 22.372  -28.721 0.00 38.36  ? 720  SER   B HG   1 
ATOM   22627 N N    . HIS   B  1 695 ? 52.825 24.099  -27.062 1.00 25.97  ? 721  HIS   B N    1 
ATOM   22628 C CA   . HIS   B  1 695 ? 51.454 23.651  -27.286 1.00 26.18  ? 721  HIS   B CA   1 
ATOM   22629 C C    . HIS   B  1 695 ? 50.735 23.390  -25.971 1.00 26.54  ? 721  HIS   B C    1 
ATOM   22630 O O    . HIS   B  1 695 ? 50.237 22.300  -25.716 1.00 27.04  ? 721  HIS   B O    1 
ATOM   22631 C CB   . HIS   B  1 695 ? 51.376 22.460  -28.266 1.00 26.27  ? 721  HIS   B CB   1 
ATOM   22632 C CG   . HIS   B  1 695 ? 51.650 22.876  -29.673 1.00 27.78  ? 721  HIS   B CG   1 
ATOM   22633 N ND1  . HIS   B  1 695 ? 50.686 23.515  -30.435 1.00 29.57  ? 721  HIS   B ND1  1 
ATOM   22634 C CD2  . HIS   B  1 695 ? 52.790 22.791  -30.394 1.00 28.39  ? 721  HIS   B CD2  1 
ATOM   22635 C CE1  . HIS   B  1 695 ? 51.256 23.766  -31.604 1.00 29.54  ? 721  HIS   B CE1  1 
ATOM   22636 N NE2  . HIS   B  1 695 ? 52.525 23.355  -31.623 1.00 29.36  ? 721  HIS   B NE2  1 
ATOM   22637 H H    . HIS   B  1 695 ? 53.003 25.045  -27.385 0.00 31.93  ? 721  HIS   B H    1 
ATOM   22638 H HA   . HIS   B  1 695 ? 50.923 24.472  -27.766 0.00 31.85  ? 721  HIS   B HA   1 
ATOM   22639 H HB2  . HIS   B  1 695 ? 52.099 21.693  -27.993 0.00 30.97  ? 721  HIS   B HB2  1 
ATOM   22640 H HB3  . HIS   B  1 695 ? 50.370 22.043  -28.249 0.00 31.01  ? 721  HIS   B HB3  1 
ATOM   22641 H HD2  . HIS   B  1 695 ? 53.725 22.364  -30.071 0.00 33.31  ? 721  HIS   B HD2  1 
ATOM   22642 H HE1  . HIS   B  1 695 ? 50.758 24.235  -32.436 0.00 34.84  ? 721  HIS   B HE1  1 
ATOM   22643 H HE2  . HIS   B  1 695 ? 53.173 23.438  -32.400 0.00 34.34  ? 721  HIS   B HE2  1 
ATOM   22644 N N    . ASN   B  1 696 ? 50.688 24.411  -25.137 1.00 26.34  ? 722  ASN   B N    1 
ATOM   22645 C CA   . ASN   B  1 696 ? 49.953 24.392  -23.868 1.00 26.74  ? 722  ASN   B CA   1 
ATOM   22646 C C    . ASN   B  1 696 ? 49.147 25.724  -23.807 1.00 28.79  ? 722  ASN   B C    1 
ATOM   22647 O O    . ASN   B  1 696 ? 48.973 26.363  -24.853 1.00 29.10  ? 722  ASN   B O    1 
ATOM   22648 C CB   . ASN   B  1 696 ? 50.925 24.154  -22.686 1.00 25.61  ? 722  ASN   B CB   1 
ATOM   22649 C CG   . ASN   B  1 696 ? 51.187 22.689  -22.421 1.00 25.65  ? 722  ASN   B CG   1 
ATOM   22650 O OD1  . ASN   B  1 696 ? 50.342 21.996  -21.866 1.00 25.73  ? 722  ASN   B OD1  1 
ATOM   22651 N ND2  . ASN   B  1 696 ? 52.341 22.179  -22.804 1.00 24.72  ? 722  ASN   B ND2  1 
ATOM   22652 H H    . ASN   B  1 696 ? 51.156 25.295  -25.308 0.00 32.97  ? 722  ASN   B H    1 
ATOM   22653 H HA   . ASN   B  1 696 ? 49.206 23.599  -23.878 0.00 33.22  ? 722  ASN   B HA   1 
ATOM   22654 H HB2  . ASN   B  1 696 ? 51.872 24.642  -22.909 0.00 32.55  ? 722  ASN   B HB2  1 
ATOM   22655 H HB3  . ASN   B  1 696 ? 50.517 24.566  -21.764 0.00 32.84  ? 722  ASN   B HB3  1 
ATOM   22656 H HD21 . ASN   B  1 696 ? 52.536 21.197  -22.638 0.00 30.40  ? 722  ASN   B HD21 1 
ATOM   22657 H HD22 . ASN   B  1 696 ? 53.035 22.756  -23.269 0.00 30.75  ? 722  ASN   B HD22 1 
ATOM   22658 N N    . ARG   B  1 697 ? 48.606 26.109  -22.646 1.00 30.15  ? 723  ARG   B N    1 
ATOM   22659 C CA   . ARG   B  1 697 ? 47.823 27.334  -22.535 1.00 31.49  ? 723  ARG   B CA   1 
ATOM   22660 C C    . ARG   B  1 697 ? 48.412 28.250  -21.473 1.00 32.42  ? 723  ARG   B C    1 
ATOM   22661 O O    . ARG   B  1 697 ? 47.664 28.864  -20.719 1.00 32.66  ? 723  ARG   B O    1 
ATOM   22662 C CB   . ARG   B  1 697 ? 46.357 26.974  -22.233 1.00 33.36  ? 723  ARG   B CB   1 
ATOM   22663 C CG   . ARG   B  1 697 ? 45.769 26.043  -23.283 1.00 36.92  ? 723  ARG   B CG   1 
ATOM   22664 C CD   . ARG   B  1 697 ? 44.364 25.631  -22.964 1.00 41.65  ? 723  ARG   B CD   1 
ATOM   22665 N NE   . ARG   B  1 697 ? 43.841 24.747  -24.005 1.00 46.26  ? 723  ARG   B NE   1 
ATOM   22666 C CZ   . ARG   B  1 697 ? 42.631 24.195  -23.992 1.00 49.21  ? 723  ARG   B CZ   1 
ATOM   22667 N NH1  . ARG   B  1 697 ? 41.794 24.426  -22.981 1.00 48.97  ? 723  ARG   B NH1  1 
ATOM   22668 N NH2  . ARG   B  1 697 ? 42.244 23.409  -24.989 1.00 49.32  ? 723  ARG   B NH2  1 
ATOM   22669 H H    . ARG   B  1 697 ? 48.659 25.590  -21.775 0.00 38.68  ? 723  ARG   B H    1 
ATOM   22670 H HA   . ARG   B  1 697 ? 47.832 27.889  -23.471 0.00 40.74  ? 723  ARG   B HA   1 
ATOM   22671 H HB2  . ARG   B  1 697 ? 46.300 26.479  -21.265 0.00 43.11  ? 723  ARG   B HB2  1 
ATOM   22672 H HB3  . ARG   B  1 697 ? 45.756 27.883  -22.227 0.00 43.44  ? 723  ARG   B HB3  1 
ATOM   22673 H HG2  . ARG   B  1 697 ? 45.762 26.553  -24.246 0.00 46.59  ? 723  ARG   B HG2  1 
ATOM   22674 H HG3  . ARG   B  1 697 ? 46.363 25.133  -23.347 0.00 46.23  ? 723  ARG   B HG3  1 
ATOM   22675 H HD2  . ARG   B  1 697 ? 44.348 25.095  -22.016 0.00 52.38  ? 723  ARG   B HD2  1 
ATOM   22676 H HD3  . ARG   B  1 697 ? 43.729 26.513  -22.912 0.00 52.76  ? 723  ARG   B HD3  1 
ATOM   22677 H HE   . ARG   B  1 697 ? 44.450 24.550  -24.793 0.00 56.97  ? 723  ARG   B HE   1 
ATOM   22678 H HH11 . ARG   B  1 697 ? 42.051 25.022  -22.201 0.00 61.28  ? 723  ARG   B HH11 1 
ATOM   22679 H HH12 . ARG   B  1 697 ? 40.875 23.997  -22.984 0.00 60.81  ? 723  ARG   B HH12 1 
ATOM   22680 H HH21 . ARG   B  1 697 ? 42.870 23.222  -25.766 0.00 60.07  ? 723  ARG   B HH21 1 
ATOM   22681 H HH22 . ARG   B  1 697 ? 41.323 22.984  -24.978 0.00 60.33  ? 723  ARG   B HH22 1 
ATOM   22682 N N    . ILE   B  1 698 ? 49.749 28.336  -21.399 1.00 33.06  ? 724  ILE   B N    1 
ATOM   22683 C CA   . ILE   B  1 698 ? 50.398 29.206  -20.423 1.00 34.59  ? 724  ILE   B CA   1 
ATOM   22684 C C    . ILE   B  1 698 ? 50.212 30.635  -20.929 1.00 35.63  ? 724  ILE   B C    1 
ATOM   22685 O O    . ILE   B  1 698 ? 50.713 30.956  -21.999 1.00 35.50  ? 724  ILE   B O    1 
ATOM   22686 C CB   . ILE   B  1 698 ? 51.909 28.878  -20.251 1.00 35.67  ? 724  ILE   B CB   1 
ATOM   22687 C CG1  . ILE   B  1 698 ? 52.171 27.378  -19.913 1.00 36.98  ? 724  ILE   B CG1  1 
ATOM   22688 C CG2  . ILE   B  1 698 ? 52.541 29.799  -19.205 1.00 36.28  ? 724  ILE   B CG2  1 
ATOM   22689 C CD1  . ILE   B  1 698 ? 51.403 26.829  -18.776 1.00 38.77  ? 724  ILE   B CD1  1 
ATOM   22690 H H    . ILE   B  1 698 ? 50.396 27.851  -22.012 0.00 43.02  ? 724  ILE   B H    1 
ATOM   22691 H HA   . ILE   B  1 698 ? 49.916 29.109  -19.452 0.00 46.26  ? 724  ILE   B HA   1 
ATOM   22692 H HB   . ILE   B  1 698 ? 52.401 29.079  -21.202 0.00 47.01  ? 724  ILE   B HB   1 
ATOM   22693 H HG12 . ILE   B  1 698 ? 51.918 26.782  -20.789 0.00 47.72  ? 724  ILE   B HG12 1 
ATOM   22694 H HG13 . ILE   B  1 698 ? 53.227 27.247  -19.684 0.00 48.36  ? 724  ILE   B HG13 1 
ATOM   22695 H HG21 . ILE   B  1 698 ? 53.549 29.448  -18.992 0.00 48.76  ? 724  ILE   B HG21 1 
ATOM   22696 H HG22 . ILE   B  1 698 ? 52.595 30.815  -19.592 0.00 49.12  ? 724  ILE   B HG22 1 
ATOM   22697 H HG23 . ILE   B  1 698 ? 51.940 29.777  -18.297 0.00 49.07  ? 724  ILE   B HG23 1 
ATOM   22698 H HD11 . ILE   B  1 698 ? 51.850 25.882  -18.475 0.00 50.30  ? 724  ILE   B HD11 1 
ATOM   22699 H HD12 . ILE   B  1 698 ? 51.421 27.532  -17.945 0.00 51.16  ? 724  ILE   B HD12 1 
ATOM   22700 H HD13 . ILE   B  1 698 ? 50.375 26.662  -19.094 0.00 50.36  ? 724  ILE   B HD13 1 
ATOM   22701 N N    . SER   B  1 699 ? 49.481 31.481  -20.178 1.00 36.50  ? 725  SER   B N    1 
ATOM   22702 C CA   . SER   B  1 699 ? 49.247 32.877  -20.555 1.00 37.73  ? 725  SER   B CA   1 
ATOM   22703 C C    . SER   B  1 699 ? 50.140 33.868  -19.794 1.00 38.76  ? 725  SER   B C    1 
ATOM   22704 O O    . SER   B  1 699 ? 50.129 35.043  -20.133 1.00 38.59  ? 725  SER   B O    1 
ATOM   22705 C CB   . SER   B  1 699 ? 47.786 33.244  -20.323 1.00 39.18  ? 725  SER   B CB   1 
ATOM   22706 O OG   . SER   B  1 699 ? 47.469 33.201  -18.940 1.00 41.49  ? 725  SER   B OG   1 
ATOM   22707 H H    . SER   B  1 699 ? 49.042 31.228  -19.299 0.00 49.59  ? 725  SER   B H    1 
ATOM   22708 H HA   . SER   B  1 699 ? 49.440 33.016  -21.617 0.00 51.19  ? 725  SER   B HA   1 
ATOM   22709 H HB2  . SER   B  1 699 ? 47.606 34.252  -20.695 0.00 53.92  ? 725  SER   B HB2  1 
ATOM   22710 H HB3  . SER   B  1 699 ? 47.155 32.533  -20.854 0.00 52.99  ? 725  SER   B HB3  1 
ATOM   22711 H HG   . SER   B  1 699 ? 46.515 33.439  -18.804 0.00 56.94  ? 725  SER   B HG   1 
ATOM   22712 N N    . HIS   B  1 700 ? 50.898 33.422  -18.784 1.00 40.07  ? 726  HIS   B N    1 
ATOM   22713 C CA   . HIS   B  1 700 ? 51.729 34.316  -17.991 1.00 42.21  ? 726  HIS   B CA   1 
ATOM   22714 C C    . HIS   B  1 700 ? 52.861 33.548  -17.316 1.00 43.66  ? 726  HIS   B C    1 
ATOM   22715 O O    . HIS   B  1 700 ? 52.650 32.434  -16.835 1.00 44.11  ? 726  HIS   B O    1 
ATOM   22716 C CB   . HIS   B  1 700 ? 50.836 34.996  -16.929 1.00 44.16  ? 726  HIS   B CB   1 
ATOM   22717 C CG   . HIS   B  1 700 ? 51.559 35.867  -15.951 1.00 48.75  ? 726  HIS   B CG   1 
ATOM   22718 N ND1  . HIS   B  1 700 ? 51.845 37.195  -16.237 1.00 51.34  ? 726  HIS   B ND1  1 
ATOM   22719 C CD2  . HIS   B  1 700 ? 51.965 35.596  -14.688 1.00 50.43  ? 726  HIS   B CD2  1 
ATOM   22720 C CE1  . HIS   B  1 700 ? 52.446 37.677  -15.159 1.00 51.82  ? 726  HIS   B CE1  1 
ATOM   22721 N NE2  . HIS   B  1 700 ? 52.539 36.752  -14.199 1.00 51.60  ? 726  HIS   B NE2  1 
ATOM   22722 H H    . HIS   B  1 700 ? 50.956 32.455  -18.483 0.00 54.82  ? 726  HIS   B H    1 
ATOM   22723 H HA   . HIS   B  1 700 ? 52.168 35.084  -18.625 0.00 58.76  ? 726  HIS   B HA   1 
ATOM   22724 H HB2  . HIS   B  1 700 ? 50.104 35.619  -17.440 0.00 61.80  ? 726  HIS   B HB2  1 
ATOM   22725 H HB3  . HIS   B  1 700 ? 50.327 34.220  -16.359 0.00 61.45  ? 726  HIS   B HB3  1 
ATOM   22726 H HD2  . HIS   B  1 700 ? 51.862 34.659  -14.166 0.00 70.17  ? 726  HIS   B HD2  1 
ATOM   22727 H HE1  . HIS   B  1 700 ? 52.812 38.685  -15.066 0.00 73.86  ? 726  HIS   B HE1  1 
ATOM   22728 H HE2  . HIS   B  1 700 ? 52.951 36.876  -13.280 0.00 73.30  ? 726  HIS   B HE2  1 
ATOM   22729 N N    . LEU   B  1 701 ? 54.054 34.145  -17.276 1.00 44.42  ? 727  LEU   B N    1 
ATOM   22730 C CA   . LEU   B  1 701 ? 55.194 33.556  -16.588 1.00 46.17  ? 727  LEU   B CA   1 
ATOM   22731 C C    . LEU   B  1 701 ? 55.251 34.174  -15.197 1.00 48.90  ? 727  LEU   B C    1 
ATOM   22732 O O    . LEU   B  1 701 ? 55.218 35.407  -15.108 1.00 48.92  ? 727  LEU   B O    1 
ATOM   22733 C CB   . LEU   B  1 701 ? 56.504 33.850  -17.334 1.00 45.86  ? 727  LEU   B CB   1 
ATOM   22734 C CG   . LEU   B  1 701 ? 56.637 33.245  -18.742 1.00 46.48  ? 727  LEU   B CG   1 
ATOM   22735 C CD1  . LEU   B  1 701 ? 58.013 33.503  -19.302 1.00 46.53  ? 727  LEU   B CD1  1 
ATOM   22736 C CD2  . LEU   B  1 701 ? 56.386 31.734  -18.739 1.00 46.98  ? 727  LEU   B CD2  1 
ATOM   22737 H H    . LEU   B  1 701 ? 54.263 35.039  -17.708 0.00 61.86  ? 727  LEU   B H    1 
ATOM   22738 H HA   . LEU   B  1 701 ? 55.080 32.477  -16.519 0.00 63.14  ? 727  LEU   B HA   1 
ATOM   22739 H HB2  . LEU   B  1 701 ? 56.609 34.930  -17.434 0.00 63.84  ? 727  LEU   B HB2  1 
ATOM   22740 H HB3  . LEU   B  1 701 ? 57.329 33.463  -16.739 0.00 63.41  ? 727  LEU   B HB3  1 
ATOM   22741 H HG   . LEU   B  1 701 ? 55.908 33.709  -19.404 0.00 63.07  ? 727  LEU   B HG   1 
ATOM   22742 H HD11 . LEU   B  1 701 ? 57.992 33.352  -20.380 0.00 62.79  ? 727  LEU   B HD11 1 
ATOM   22743 H HD12 . LEU   B  1 701 ? 58.313 34.522  -19.067 0.00 63.94  ? 727  LEU   B HD12 1 
ATOM   22744 H HD13 . LEU   B  1 701 ? 58.704 32.795  -18.847 0.00 63.17  ? 727  LEU   B HD13 1 
ATOM   22745 H HD21 . LEU   B  1 701 ? 56.714 31.322  -19.691 0.00 62.45  ? 727  LEU   B HD21 1 
ATOM   22746 H HD22 . LEU   B  1 701 ? 56.944 31.279  -17.921 0.00 63.14  ? 727  LEU   B HD22 1 
ATOM   22747 H HD23 . LEU   B  1 701 ? 55.320 31.545  -18.620 0.00 62.83  ? 727  LEU   B HD23 1 
ATOM   22748 N N    . PRO   B  1 702 ? 55.335 33.383  -14.099 1.00 50.91  ? 728  PRO   B N    1 
ATOM   22749 C CA   . PRO   B  1 702 ? 55.399 34.017  -12.768 1.00 52.66  ? 728  PRO   B CA   1 
ATOM   22750 C C    . PRO   B  1 702 ? 56.667 34.834  -12.540 1.00 55.13  ? 728  PRO   B C    1 
ATOM   22751 O O    . PRO   B  1 702 ? 57.672 34.637  -13.220 1.00 55.35  ? 728  PRO   B O    1 
ATOM   22752 C CB   . PRO   B  1 702 ? 55.314 32.847  -11.778 1.00 53.00  ? 728  PRO   B CB   1 
ATOM   22753 C CG   . PRO   B  1 702 ? 55.174 31.623  -12.565 1.00 52.92  ? 728  PRO   B CG   1 
ATOM   22754 C CD   . PRO   B  1 702 ? 55.376 31.908  -14.010 1.00 50.81  ? 728  PRO   B CD   1 
ATOM   22755 H HA   . PRO   B  1 702 ? 54.535 34.662  -12.619 0.00 73.76  ? 728  PRO   B HA   1 
ATOM   22756 H HB2  . PRO   B  1 702 ? 56.226 32.809  -11.185 0.00 74.01  ? 728  PRO   B HB2  1 
ATOM   22757 H HB3  . PRO   B  1 702 ? 54.450 32.979  -11.128 0.00 74.01  ? 728  PRO   B HB3  1 
ATOM   22758 H HG2  . PRO   B  1 702 ? 55.917 30.902  -12.226 0.00 72.41  ? 728  PRO   B HG2  1 
ATOM   22759 H HG3  . PRO   B  1 702 ? 54.175 31.221  -12.406 0.00 72.36  ? 728  PRO   B HG3  1 
ATOM   22760 H HD2  . PRO   B  1 702 ? 56.340 31.526  -14.343 0.00 69.33  ? 728  PRO   B HD2  1 
ATOM   22761 H HD3  . PRO   B  1 702 ? 54.550 31.460  -14.560 0.00 68.99  ? 728  PRO   B HD3  1 
ATOM   22762 N N    . SER   B  1 703 ? 56.601 35.788  -11.584 1.00 57.03  ? 729  SER   B N    1 
ATOM   22763 C CA   . SER   B  1 703 ? 57.745 36.630  -11.240 1.00 59.28  ? 729  SER   B CA   1 
ATOM   22764 C C    . SER   B  1 703 ? 58.857 35.720  -10.677 1.00 61.76  ? 729  SER   B C    1 
ATOM   22765 O O    . SER   B  1 703 ? 58.591 34.920  -9.784  1.00 61.76  ? 729  SER   B O    1 
ATOM   22766 C CB   . SER   B  1 703 ? 57.348 37.693  -10.213 1.00 60.81  ? 729  SER   B CB   1 
ATOM   22767 O OG   . SER   B  1 703 ? 56.045 38.231  -10.378 1.00 62.98  ? 729  SER   B OG   1 
ATOM   22768 H H    . SER   B  1 703 ? 55.764 35.999  -11.050 0.00 80.65  ? 729  SER   B H    1 
ATOM   22769 H HA   . SER   B  1 703 ? 58.110 37.133  -12.133 0.00 83.74  ? 729  SER   B HA   1 
ATOM   22770 H HB2  . SER   B  1 703 ? 57.435 37.253  -9.223  0.00 87.01  ? 729  SER   B HB2  1 
ATOM   22771 H HB3  . SER   B  1 703 ? 58.053 38.517  -10.289 0.00 87.34  ? 729  SER   B HB3  1 
ATOM   22772 H HG   . SER   B  1 703 ? 55.874 38.936  -9.699  0.00 90.24  ? 729  SER   B HG   1 
ATOM   22773 N N    . GLY   B  1 704 ? 60.053 35.798  -11.257 1.00 63.90  ? 730  GLY   B N    1 
ATOM   22774 C CA   . GLY   B  1 704 ? 61.183 34.952  -10.892 1.00 66.24  ? 730  GLY   B CA   1 
ATOM   22775 C C    . GLY   B  1 704 ? 61.062 33.539  -11.409 1.00 68.54  ? 730  GLY   B C    1 
ATOM   22776 O O    . GLY   B  1 704 ? 60.948 32.610  -10.607 1.00 68.45  ? 730  GLY   B O    1 
ATOM   22777 H H    . GLY   B  1 704 ? 60.309 36.506  -11.935 0.00 89.45  ? 730  GLY   B H    1 
ATOM   22778 H HA2  . GLY   B  1 704 ? 62.106 35.393  -11.266 0.00 92.24  ? 730  GLY   B HA2  1 
ATOM   22779 H HA3  . GLY   B  1 704 ? 61.245 34.861  -9.809  0.00 92.60  ? 730  GLY   B HA3  1 
ATOM   22780 N N    . PHE   B  1 705 ? 61.040 33.360  -12.745 1.00 70.47  ? 731  PHE   B N    1 
ATOM   22781 C CA   . PHE   B  1 705 ? 60.913 32.029  -13.336 1.00 72.48  ? 731  PHE   B CA   1 
ATOM   22782 C C    . PHE   B  1 705 ? 62.189 31.574  -14.066 1.00 74.24  ? 731  PHE   B C    1 
ATOM   22783 O O    . PHE   B  1 705 ? 62.742 30.522  -13.739 1.00 74.58  ? 731  PHE   B O    1 
ATOM   22784 C CB   . PHE   B  1 705 ? 59.680 31.956  -14.267 1.00 72.85  ? 731  PHE   B CB   1 
ATOM   22785 C CG   . PHE   B  1 705 ? 59.505 30.588  -14.889 1.00 73.96  ? 731  PHE   B CG   1 
ATOM   22786 C CD1  . PHE   B  1 705 ? 59.013 29.532  -14.148 1.00 74.97  ? 731  PHE   B CD1  1 
ATOM   22787 C CD2  . PHE   B  1 705 ? 59.923 30.336  -16.181 1.00 74.90  ? 731  PHE   B CD2  1 
ATOM   22788 C CE1  . PHE   B  1 705 ? 58.926 28.256  -14.688 1.00 75.76  ? 731  PHE   B CE1  1 
ATOM   22789 C CE2  . PHE   B  1 705 ? 59.817 29.061  -16.722 1.00 75.73  ? 731  PHE   B CE2  1 
ATOM   22790 C CZ   . PHE   B  1 705 ? 59.331 28.027  -15.969 1.00 75.61  ? 731  PHE   B CZ   1 
ATOM   22791 H H    . PHE   B  1 705 ? 61.018 34.111  -13.428 0.00 95.34  ? 731  PHE   B H    1 
ATOM   22792 H HA   . PHE   B  1 705 ? 60.717 31.309  -12.545 0.00 96.70  ? 731  PHE   B HA   1 
ATOM   22793 H HB2  . PHE   B  1 705 ? 58.785 32.171  -13.685 0.00 96.68  ? 731  PHE   B HB2  1 
ATOM   22794 H HB3  . PHE   B  1 705 ? 59.781 32.691  -15.062 0.00 96.49  ? 731  PHE   B HB3  1 
ATOM   22795 H HD1  . PHE   B  1 705 ? 58.715 29.697  -13.131 0.00 98.27  ? 731  PHE   B HD1  1 
ATOM   22796 H HD2  . PHE   B  1 705 ? 60.327 31.138  -16.774 0.00 97.52  ? 731  PHE   B HD2  1 
ATOM   22797 H HE1  . PHE   B  1 705 ? 58.528 27.446  -14.103 0.00 97.74  ? 731  PHE   B HE1  1 
ATOM   22798 H HE2  . PHE   B  1 705 ? 60.123 28.877  -17.733 0.00 97.05  ? 731  PHE   B HE2  1 
ATOM   22799 H HZ   . PHE   B  1 705 ? 59.228 27.042  -16.399 0.00 96.51  ? 731  PHE   B HZ   1 
ATOM   22800 N N    . LEU   B  1 706 ? 62.662 32.359  -15.044 1.00 75.16  ? 732  LEU   B N    1 
ATOM   22801 C CA   . LEU   B  1 706 ? 63.810 31.966  -15.864 1.00 76.33  ? 732  LEU   B CA   1 
ATOM   22802 C C    . LEU   B  1 706 ? 65.171 32.087  -15.160 1.00 76.83  ? 732  LEU   B C    1 
ATOM   22803 O O    . LEU   B  1 706 ? 66.126 31.428  -15.576 1.00 77.09  ? 732  LEU   B O    1 
ATOM   22804 C CB   . LEU   B  1 706 ? 63.839 32.792  -17.171 1.00 76.83  ? 732  LEU   B CB   1 
ATOM   22805 C CG   . LEU   B  1 706 ? 62.633 32.641  -18.130 1.00 78.75  ? 732  LEU   B CG   1 
ATOM   22806 C CD1  . LEU   B  1 706 ? 61.517 33.630  -17.802 1.00 79.39  ? 732  LEU   B CD1  1 
ATOM   22807 C CD2  . LEU   B  1 706 ? 63.053 32.850  -19.577 1.00 79.53  ? 732  LEU   B CD2  1 
ATOM   22808 H H    . LEU   B  1 706 ? 62.298 33.282  -15.261 0.00 99.90  ? 732  LEU   B H    1 
ATOM   22809 H HA   . LEU   B  1 706 ? 63.689 30.923  -16.153 0.00 100.04 ? 732  LEU   B HA   1 
ATOM   22810 H HB2  . LEU   B  1 706 ? 63.931 33.844  -16.903 0.00 101.82 ? 732  LEU   B HB2  1 
ATOM   22811 H HB3  . LEU   B  1 706 ? 64.728 32.493  -17.724 0.00 100.95 ? 732  LEU   B HB3  1 
ATOM   22812 H HG   . LEU   B  1 706 ? 62.218 31.637  -18.053 0.00 102.19 ? 732  LEU   B HG   1 
ATOM   22813 H HD11 . LEU   B  1 706 ? 60.836 33.687  -18.649 0.00 103.48 ? 732  LEU   B HD11 1 
ATOM   22814 H HD12 . LEU   B  1 706 ? 60.972 33.278  -16.930 0.00 104.06 ? 732  LEU   B HD12 1 
ATOM   22815 H HD13 . LEU   B  1 706 ? 61.937 34.616  -17.609 0.00 104.59 ? 732  LEU   B HD13 1 
ATOM   22816 H HD21 . LEU   B  1 706 ? 62.192 32.698  -20.227 0.00 102.69 ? 732  LEU   B HD21 1 
ATOM   22817 H HD22 . LEU   B  1 706 ? 63.429 33.866  -19.691 0.00 103.69 ? 732  LEU   B HD22 1 
ATOM   22818 H HD23 . LEU   B  1 706 ? 63.832 32.133  -19.833 0.00 102.86 ? 732  LEU   B HD23 1 
ATOM   22819 N N    . SER   B  1 707 ? 65.267 32.911  -14.111 1.00 76.69  ? 733  SER   B N    1 
ATOM   22820 C CA   . SER   B  1 707 ? 66.534 33.176  -13.434 1.00 77.14  ? 733  SER   B CA   1 
ATOM   22821 C C    . SER   B  1 707 ? 67.005 32.141  -12.395 1.00 76.96  ? 733  SER   B C    1 
ATOM   22822 O O    . SER   B  1 707 ? 68.197 31.819  -12.360 1.00 77.40  ? 733  SER   B O    1 
ATOM   22823 C CB   . SER   B  1 707 ? 66.470 34.545  -12.761 1.00 78.84  ? 733  SER   B CB   1 
ATOM   22824 O OG   . SER   B  1 707 ? 65.647 34.522  -11.605 1.00 81.61  ? 733  SER   B OG   1 
ATOM   22825 H H    . SER   B  1 707 ? 64.490 33.413  -13.693 0.00 103.06 ? 733  SER   B H    1 
ATOM   22826 H HA   . SER   B  1 707 ? 67.318 33.250  -14.186 0.00 103.96 ? 733  SER   B HA   1 
ATOM   22827 H HB2  . SER   B  1 707 ? 67.476 34.848  -12.474 0.00 107.75 ? 733  SER   B HB2  1 
ATOM   22828 H HB3  . SER   B  1 707 ? 66.056 35.263  -13.468 0.00 107.12 ? 733  SER   B HB3  1 
ATOM   22829 H HG   . SER   B  1 707 ? 64.789 34.058  -11.790 0.00 110.31 ? 733  SER   B HG   1 
ATOM   22830 N N    . GLU   B  1 708 ? 66.107 31.677  -11.513 1.00 75.96  ? 734  GLU   B N    1 
ATOM   22831 C CA   . GLU   B  1 708 ? 66.495 30.812  -10.398 1.00 75.40  ? 734  GLU   B CA   1 
ATOM   22832 C C    . GLU   B  1 708 ? 66.847 29.352  -10.752 1.00 74.17  ? 734  GLU   B C    1 
ATOM   22833 O O    . GLU   B  1 708 ? 67.670 28.769  -10.038 1.00 74.34  ? 734  GLU   B O    1 
ATOM   22834 C CB   . GLU   B  1 708 ? 65.412 30.834  -9.308  1.00 78.01  ? 734  GLU   B CB   1 
ATOM   22835 C CG   . GLU   B  1 708 ? 65.093 32.224  -8.770  1.00 83.37  ? 734  GLU   B CG   1 
ATOM   22836 C CD   . GLU   B  1 708 ? 66.279 33.016  -8.249  1.00 89.98  ? 734  GLU   B CD   1 
ATOM   22837 O OE1  . GLU   B  1 708 ? 66.521 32.988  -7.020  1.00 91.13  ? 734  GLU   B OE1  1 
ATOM   22838 O OE2  . GLU   B  1 708 ? 66.969 33.664  -9.070  1.00 92.23  ? 734  GLU   B OE2  1 
ATOM   22839 H H    . GLU   B  1 708 ? 65.112 31.874  -11.561 0.00 102.63 ? 734  GLU   B H    1 
ATOM   22840 H HA   . GLU   B  1 708 ? 67.398 31.234  -9.958  0.00 103.06 ? 734  GLU   B HA   1 
ATOM   22841 H HB2  . GLU   B  1 708 ? 64.495 30.417  -9.720  0.00 105.18 ? 734  GLU   B HB2  1 
ATOM   22842 H HB3  . GLU   B  1 708 ? 65.752 30.228  -8.469  0.00 106.07 ? 734  GLU   B HB3  1 
ATOM   22843 H HG2  . GLU   B  1 708 ? 64.630 32.806  -9.565  0.00 112.94 ? 734  GLU   B HG2  1 
ATOM   22844 H HG3  . GLU   B  1 708 ? 64.389 32.118  -7.946  0.00 113.42 ? 734  GLU   B HG3  1 
ATOM   22845 N N    . VAL   B  1 709 ? 66.256 28.753  -11.811 1.00 72.73  ? 735  VAL   B N    1 
ATOM   22846 C CA   . VAL   B  1 709 ? 66.581 27.358  -12.153 1.00 71.57  ? 735  VAL   B CA   1 
ATOM   22847 C C    . VAL   B  1 709 ? 67.949 27.341  -12.840 1.00 69.53  ? 735  VAL   B C    1 
ATOM   22848 O O    . VAL   B  1 709 ? 68.037 27.516  -14.054 1.00 69.84  ? 735  VAL   B O    1 
ATOM   22849 C CB   . VAL   B  1 709 ? 65.489 26.658  -13.005 1.00 72.63  ? 735  VAL   B CB   1 
ATOM   22850 C CG1  . VAL   B  1 709 ? 65.745 25.150  -13.097 1.00 73.27  ? 735  VAL   B CG1  1 
ATOM   22851 C CG2  . VAL   B  1 709 ? 64.104 26.918  -12.433 1.00 73.30  ? 735  VAL   B CG2  1 
ATOM   22852 H H    . VAL   B  1 709 ? 65.592 29.202  -12.435 0.00 97.14  ? 735  VAL   B H    1 
ATOM   22853 H HA   . VAL   B  1 709 ? 66.670 26.798  -11.222 0.00 95.59  ? 735  VAL   B HA   1 
ATOM   22854 H HB   . VAL   B  1 709 ? 65.496 27.063  -14.015 0.00 95.28  ? 735  VAL   B HB   1 
ATOM   22855 H HG11 . VAL   B  1 709 ? 64.989 24.699  -13.737 0.00 95.13  ? 735  VAL   B HG11 1 
ATOM   22856 H HG12 . VAL   B  1 709 ? 66.736 24.958  -13.505 0.00 95.79  ? 735  VAL   B HG12 1 
ATOM   22857 H HG13 . VAL   B  1 709 ? 65.677 24.724  -12.097 0.00 96.12  ? 735  VAL   B HG13 1 
ATOM   22858 H HG21 . VAL   B  1 709 ? 63.394 26.256  -12.924 0.00 95.77  ? 735  VAL   B HG21 1 
ATOM   22859 H HG22 . VAL   B  1 709 ? 64.124 26.717  -11.363 0.00 96.89  ? 735  VAL   B HG22 1 
ATOM   22860 H HG23 . VAL   B  1 709 ? 63.825 27.954  -12.619 0.00 96.73  ? 735  VAL   B HG23 1 
ATOM   22861 N N    . SER   B  1 710 ? 69.018 27.163  -12.051 1.00 67.23  ? 736  SER   B N    1 
ATOM   22862 C CA   . SER   B  1 710 ? 70.388 27.190  -12.558 1.00 65.11  ? 736  SER   B CA   1 
ATOM   22863 C C    . SER   B  1 710 ? 70.712 26.093  -13.572 1.00 61.98  ? 736  SER   B C    1 
ATOM   22864 O O    . SER   B  1 710 ? 71.430 26.364  -14.531 1.00 62.40  ? 736  SER   B O    1 
ATOM   22865 C CB   . SER   B  1 710 ? 71.386 27.147  -11.403 1.00 66.46  ? 736  SER   B CB   1 
ATOM   22866 O OG   . SER   B  1 710 ? 71.095 26.103  -10.490 1.00 68.84  ? 736  SER   B OG   1 
ATOM   22867 H H    . SER   B  1 710 ? 68.966 27.000  -11.050 0.00 91.25  ? 736  SER   B H    1 
ATOM   22868 H HA   . SER   B  1 710 ? 70.530 28.147  -13.058 0.00 88.63  ? 736  SER   B HA   1 
ATOM   22869 H HB2  . SER   B  1 710 ? 72.384 26.988  -11.808 0.00 91.07  ? 736  SER   B HB2  1 
ATOM   22870 H HB3  . SER   B  1 710 ? 71.350 28.098  -10.872 0.00 91.66  ? 736  SER   B HB3  1 
ATOM   22871 H HG   . SER   B  1 710 ? 71.792 26.066  -9.784  0.00 94.39  ? 736  SER   B HG   1 
ATOM   22872 N N    . SER   B  1 711 ? 70.207 24.865  -13.375 1.00 58.79  ? 737  SER   B N    1 
ATOM   22873 C CA   . SER   B  1 711 ? 70.499 23.765  -14.303 1.00 56.03  ? 737  SER   B CA   1 
ATOM   22874 C C    . SER   B  1 711 ? 69.740 23.847  -15.632 1.00 51.78  ? 737  SER   B C    1 
ATOM   22875 O O    . SER   B  1 711 ? 70.133 23.161  -16.573 1.00 52.04  ? 737  SER   B O    1 
ATOM   22876 C CB   . SER   B  1 711 ? 70.215 22.419  -13.642 1.00 57.73  ? 737  SER   B CB   1 
ATOM   22877 O OG   . SER   B  1 711 ? 68.877 22.351  -13.178 1.00 59.83  ? 737  SER   B OG   1 
ATOM   22878 H H    . SER   B  1 711 ? 69.609 24.603  -12.598 0.00 79.57  ? 737  SER   B H    1 
ATOM   22879 H HA   . SER   B  1 711 ? 71.563 23.778  -14.535 0.00 75.64  ? 737  SER   B HA   1 
ATOM   22880 H HB2  . SER   B  1 711 ? 70.387 21.623  -14.367 0.00 76.66  ? 737  SER   B HB2  1 
ATOM   22881 H HB3  . SER   B  1 711 ? 70.891 22.296  -12.797 0.00 77.81  ? 737  SER   B HB3  1 
ATOM   22882 H HG   . SER   B  1 711 ? 68.280 22.010  -13.894 0.00 78.88  ? 737  SER   B HG   1 
ATOM   22883 N N    . LEU   B  1 712 ? 68.658 24.647  -15.721 1.00 48.29  ? 738  LEU   B N    1 
ATOM   22884 C CA   . LEU   B  1 712 ? 67.858 24.710  -16.955 1.00 45.77  ? 738  LEU   B CA   1 
ATOM   22885 C C    . LEU   B  1 712 ? 68.599 25.382  -18.128 1.00 42.43  ? 738  LEU   B C    1 
ATOM   22886 O O    . LEU   B  1 712 ? 68.910 26.567  -18.072 1.00 42.14  ? 738  LEU   B O    1 
ATOM   22887 C CB   . LEU   B  1 712 ? 66.506 25.400  -16.694 1.00 46.05  ? 738  LEU   B CB   1 
ATOM   22888 C CG   . LEU   B  1 712 ? 65.384 25.157  -17.706 1.00 47.74  ? 738  LEU   B CG   1 
ATOM   22889 C CD1  . LEU   B  1 712 ? 65.019 23.674  -17.799 1.00 48.20  ? 738  LEU   B CD1  1 
ATOM   22890 C CD2  . LEU   B  1 712 ? 64.144 25.951  -17.336 1.00 48.41  ? 738  LEU   B CD2  1 
ATOM   22891 H H    . LEU   B  1 712 ? 68.316 25.253  -14.983 0.00 65.67  ? 738  LEU   B H    1 
ATOM   22892 H HA   . LEU   B  1 712 ? 67.647 23.681  -17.240 0.00 60.86  ? 738  LEU   B HA   1 
ATOM   22893 H HB2  . LEU   B  1 712 ? 66.128 25.052  -15.735 0.00 61.97  ? 738  LEU   B HB2  1 
ATOM   22894 H HB3  . LEU   B  1 712 ? 66.670 26.475  -16.645 0.00 62.25  ? 738  LEU   B HB3  1 
ATOM   22895 H HG   . LEU   B  1 712 ? 65.712 25.490  -18.689 0.00 62.78  ? 738  LEU   B HG   1 
ATOM   22896 H HD11 . LEU   B  1 712 ? 64.026 23.576  -18.236 0.00 62.44  ? 738  LEU   B HD11 1 
ATOM   22897 H HD12 . LEU   B  1 712 ? 65.740 23.169  -18.440 0.00 62.61  ? 738  LEU   B HD12 1 
ATOM   22898 H HD13 . LEU   B  1 712 ? 65.034 23.236  -16.803 0.00 63.16  ? 738  LEU   B HD13 1 
ATOM   22899 H HD21 . LEU   B  1 712 ? 63.378 25.804  -18.096 0.00 63.44  ? 738  LEU   B HD21 1 
ATOM   22900 H HD22 . LEU   B  1 712 ? 63.780 25.601  -16.372 0.00 64.20  ? 738  LEU   B HD22 1 
ATOM   22901 H HD23 . LEU   B  1 712 ? 64.405 27.006  -17.271 0.00 64.48  ? 738  LEU   B HD23 1 
ATOM   22902 N N    . LYS   B  1 713 ? 68.888 24.601  -19.176 1.00 39.83  ? 739  LYS   B N    1 
ATOM   22903 C CA   . LYS   B  1 713 ? 69.583 25.051  -20.380 1.00 38.17  ? 739  LYS   B CA   1 
ATOM   22904 C C    . LYS   B  1 713 ? 68.593 25.329  -21.525 1.00 36.17  ? 739  LYS   B C    1 
ATOM   22905 O O    . LYS   B  1 713 ? 68.794 26.274  -22.286 1.00 36.37  ? 739  LYS   B O    1 
ATOM   22906 C CB   . LYS   B  1 713 ? 70.586 23.972  -20.841 1.00 40.06  ? 739  LYS   B CB   1 
ATOM   22907 C CG   . LYS   B  1 713 ? 71.703 23.644  -19.836 1.00 44.82  ? 739  LYS   B CG   1 
ATOM   22908 C CD   . LYS   B  1 713 ? 72.658 24.818  -19.527 1.00 49.81  ? 739  LYS   B CD   1 
ATOM   22909 C CE   . LYS   B  1 713 ? 73.375 25.376  -20.741 1.00 53.68  ? 739  LYS   B CE   1 
ATOM   22910 N NZ   . LYS   B  1 713 ? 74.426 26.358  -20.366 1.00 55.63  ? 739  LYS   B NZ   1 
ATOM   22911 H H    . LYS   B  1 713 ? 68.643 23.616  -19.223 0.00 53.14  ? 739  LYS   B H    1 
ATOM   22912 H HA   . LYS   B  1 713 ? 70.135 25.970  -20.190 0.00 52.04  ? 739  LYS   B HA   1 
ATOM   22913 H HB2  . LYS   B  1 713 ? 70.038 23.047  -21.014 0.00 52.91  ? 739  LYS   B HB2  1 
ATOM   22914 H HB3  . LYS   B  1 713 ? 71.038 24.292  -21.779 0.00 53.33  ? 739  LYS   B HB3  1 
ATOM   22915 H HG2  . LYS   B  1 713 ? 71.253 23.329  -18.896 0.00 59.96  ? 739  LYS   B HG2  1 
ATOM   22916 H HG3  . LYS   B  1 713 ? 72.304 22.830  -20.237 0.00 59.57  ? 739  LYS   B HG3  1 
ATOM   22917 H HD2  . LYS   B  1 713 ? 72.106 25.630  -19.056 0.00 66.96  ? 739  LYS   B HD2  1 
ATOM   22918 H HD3  . LYS   B  1 713 ? 73.422 24.457  -18.840 0.00 67.07  ? 739  LYS   B HD3  1 
ATOM   22919 H HE2  . LYS   B  1 713 ? 73.847 24.560  -21.287 0.00 70.86  ? 739  LYS   B HE2  1 
ATOM   22920 H HE3  . LYS   B  1 713 ? 72.660 25.892  -21.380 0.00 70.91  ? 739  LYS   B HE3  1 
ATOM   22921 H HZ1  . LYS   B  1 713 ? 74.886 26.708  -21.200 0.00 74.39  ? 739  LYS   B HZ1  1 
ATOM   22922 H HZ2  . LYS   B  1 713 ? 74.009 27.138  -19.868 0.00 74.82  ? 739  LYS   B HZ2  1 
ATOM   22923 H HZ3  . LYS   B  1 713 ? 75.116 25.915  -19.768 0.00 74.78  ? 739  LYS   B HZ3  1 
ATOM   22924 N N    . HIS   B  1 714 ? 67.556 24.486  -21.672 1.00 33.84  ? 740  HIS   B N    1 
ATOM   22925 C CA   . HIS   B  1 714 ? 66.588 24.603  -22.763 1.00 32.43  ? 740  HIS   B CA   1 
ATOM   22926 C C    . HIS   B  1 714 ? 65.166 24.674  -22.204 1.00 30.57  ? 740  HIS   B C    1 
ATOM   22927 O O    . HIS   B  1 714 ? 64.710 23.734  -21.553 1.00 29.97  ? 740  HIS   B O    1 
ATOM   22928 C CB   . HIS   B  1 714 ? 66.746 23.385  -23.695 1.00 33.13  ? 740  HIS   B CB   1 
ATOM   22929 C CG   . HIS   B  1 714 ? 65.836 23.349  -24.891 1.00 35.99  ? 740  HIS   B CG   1 
ATOM   22930 N ND1  . HIS   B  1 714 ? 65.815 22.255  -25.731 1.00 38.05  ? 740  HIS   B ND1  1 
ATOM   22931 C CD2  . HIS   B  1 714 ? 64.951 24.263  -25.350 1.00 37.58  ? 740  HIS   B CD2  1 
ATOM   22932 C CE1  . HIS   B  1 714 ? 64.914 22.526  -26.662 1.00 38.72  ? 740  HIS   B CE1  1 
ATOM   22933 N NE2  . HIS   B  1 714 ? 64.373 23.727  -26.476 1.00 38.82  ? 740  HIS   B NE2  1 
ATOM   22934 H H    . HIS   B  1 714 ? 67.365 23.699  -21.060 0.00 44.92  ? 740  HIS   B H    1 
ATOM   22935 H HA   . HIS   B  1 714 ? 66.777 25.497  -23.356 0.00 42.88  ? 740  HIS   B HA   1 
ATOM   22936 H HB2  . HIS   B  1 714 ? 67.770 23.365  -24.065 0.00 42.96  ? 740  HIS   B HB2  1 
ATOM   22937 H HB3  . HIS   B  1 714 ? 66.549 22.486  -23.114 0.00 42.71  ? 740  HIS   B HB3  1 
ATOM   22938 H HD2  . HIS   B  1 714 ? 64.738 25.224  -24.916 0.00 48.00  ? 740  HIS   B HD2  1 
ATOM   22939 H HE1  . HIS   B  1 714 ? 64.653 21.864  -27.469 0.00 47.42  ? 740  HIS   B HE1  1 
ATOM   22940 H HE2  . HIS   B  1 714 ? 63.660 24.162  -27.052 0.00 48.23  ? 740  HIS   B HE2  1 
ATOM   22941 N N    . LEU   B  1 715 ? 64.481 25.802  -22.454 1.00 29.17  ? 741  LEU   B N    1 
ATOM   22942 C CA   . LEU   B  1 715 ? 63.095 26.014  -22.056 1.00 28.49  ? 741  LEU   B CA   1 
ATOM   22943 C C    . LEU   B  1 715 ? 62.312 26.292  -23.334 1.00 28.12  ? 741  LEU   B C    1 
ATOM   22944 O O    . LEU   B  1 715 ? 62.650 27.228  -24.062 1.00 28.49  ? 741  LEU   B O    1 
ATOM   22945 C CB   . LEU   B  1 715 ? 62.996 27.200  -21.086 1.00 28.50  ? 741  LEU   B CB   1 
ATOM   22946 C CG   . LEU   B  1 715 ? 61.598 27.728  -20.755 1.00 29.63  ? 741  LEU   B CG   1 
ATOM   22947 C CD1  . LEU   B  1 715 ? 60.694 26.624  -20.199 1.00 29.51  ? 741  LEU   B CD1  1 
ATOM   22948 C CD2  . LEU   B  1 715 ? 61.699 28.882  -19.768 1.00 29.96  ? 741  LEU   B CD2  1 
ATOM   22949 H H    . LEU   B  1 715 ? 64.871 26.607  -22.936 0.00 39.13  ? 741  LEU   B H    1 
ATOM   22950 H HA   . LEU   B  1 715 ? 62.686 25.130  -21.569 0.00 37.80  ? 741  LEU   B HA   1 
ATOM   22951 H HB2  . LEU   B  1 715 ? 63.459 26.906  -20.145 0.00 39.18  ? 741  LEU   B HB2  1 
ATOM   22952 H HB3  . LEU   B  1 715 ? 63.558 28.031  -21.511 0.00 39.14  ? 741  LEU   B HB3  1 
ATOM   22953 H HG   . LEU   B  1 715 ? 61.130 28.122  -21.657 0.00 40.06  ? 741  LEU   B HG   1 
ATOM   22954 H HD11 . LEU   B  1 715 ? 59.770 27.076  -19.845 0.00 39.94  ? 741  LEU   B HD11 1 
ATOM   22955 H HD12 . LEU   B  1 715 ? 60.473 25.905  -20.987 0.00 39.16  ? 741  LEU   B HD12 1 
ATOM   22956 H HD13 . LEU   B  1 715 ? 61.207 26.128  -19.376 0.00 39.97  ? 741  LEU   B HD13 1 
ATOM   22957 H HD21 . LEU   B  1 715 ? 60.739 29.392  -19.722 0.00 41.67  ? 741  LEU   B HD21 1 
ATOM   22958 H HD22 . LEU   B  1 715 ? 61.965 28.486  -18.789 0.00 41.84  ? 741  LEU   B HD22 1 
ATOM   22959 H HD23 . LEU   B  1 715 ? 62.466 29.577  -20.108 0.00 41.91  ? 741  LEU   B HD23 1 
ATOM   22960 N N    . ASP   B  1 716 ? 61.301 25.474  -23.631 1.00 26.76  ? 742  ASP   B N    1 
ATOM   22961 C CA   . ASP   B  1 716 ? 60.504 25.658  -24.830 1.00 26.89  ? 742  ASP   B CA   1 
ATOM   22962 C C    . ASP   B  1 716 ? 59.091 26.076  -24.433 1.00 26.41  ? 742  ASP   B C    1 
ATOM   22963 O O    . ASP   B  1 716 ? 58.319 25.271  -23.921 1.00 26.06  ? 742  ASP   B O    1 
ATOM   22964 C CB   . ASP   B  1 716 ? 60.537 24.376  -25.684 1.00 28.83  ? 742  ASP   B CB   1 
ATOM   22965 C CG   . ASP   B  1 716 ? 59.557 24.308  -26.822 1.00 34.97  ? 742  ASP   B CG   1 
ATOM   22966 O OD1  . ASP   B  1 716 ? 59.155 25.385  -27.333 1.00 34.73  ? 742  ASP   B OD1  1 
ATOM   22967 O OD2  . ASP   B  1 716 ? 59.216 23.177  -27.238 1.00 39.15  ? 742  ASP   B OD2  1 
ATOM   22968 H H    . ASP   B  1 716 ? 61.012 24.683  -23.065 0.00 34.75  ? 742  ASP   B H    1 
ATOM   22969 H HA   . ASP   B  1 716 ? 60.931 26.450  -25.442 0.00 34.81  ? 742  ASP   B HA   1 
ATOM   22970 H HB2  . ASP   B  1 716 ? 61.533 24.288  -26.116 0.00 36.22  ? 742  ASP   B HB2  1 
ATOM   22971 H HB3  . ASP   B  1 716 ? 60.352 23.517  -25.048 0.00 36.10  ? 742  ASP   B HB3  1 
ATOM   22972 N N    . LEU   B  1 717 ? 58.786 27.361  -24.631 1.00 26.38  ? 743  LEU   B N    1 
ATOM   22973 C CA   . LEU   B  1 717 ? 57.473 27.938  -24.349 1.00 26.94  ? 743  LEU   B CA   1 
ATOM   22974 C C    . LEU   B  1 717 ? 56.749 28.316  -25.652 1.00 27.05  ? 743  LEU   B C    1 
ATOM   22975 O O    . LEU   B  1 717 ? 55.849 29.152  -25.613 1.00 27.30  ? 743  LEU   B O    1 
ATOM   22976 C CB   . LEU   B  1 717 ? 57.642 29.188  -23.460 1.00 27.18  ? 743  LEU   B CB   1 
ATOM   22977 C CG   . LEU   B  1 717 ? 58.031 28.940  -22.001 1.00 28.81  ? 743  LEU   B CG   1 
ATOM   22978 C CD1  . LEU   B  1 717 ? 58.565 30.222  -21.373 1.00 28.96  ? 743  LEU   B CD1  1 
ATOM   22979 C CD2  . LEU   B  1 717 ? 56.853 28.410  -21.199 1.00 29.73  ? 743  LEU   B CD2  1 
ATOM   22980 H H    . LEU   B  1 717 ? 59.441 28.045  -24.995 0.00 34.76  ? 743  LEU   B H    1 
ATOM   22981 H HA   . LEU   B  1 717 ? 56.841 27.222  -23.827 0.00 35.17  ? 743  LEU   B HA   1 
ATOM   22982 H HB2  . LEU   B  1 717 ? 58.415 29.819  -23.895 0.00 36.71  ? 743  LEU   B HB2  1 
ATOM   22983 H HB3  . LEU   B  1 717 ? 56.705 29.742  -23.432 0.00 36.65  ? 743  LEU   B HB3  1 
ATOM   22984 H HG   . LEU   B  1 717 ? 58.821 28.192  -21.965 0.00 38.64  ? 743  LEU   B HG   1 
ATOM   22985 H HD11 . LEU   B  1 717 ? 58.605 30.114  -20.290 0.00 40.24  ? 743  LEU   B HD11 1 
ATOM   22986 H HD12 . LEU   B  1 717 ? 59.566 30.407  -21.760 0.00 39.98  ? 743  LEU   B HD12 1 
ATOM   22987 H HD13 . LEU   B  1 717 ? 57.911 31.047  -21.650 0.00 40.11  ? 743  LEU   B HD13 1 
ATOM   22988 H HD21 . LEU   B  1 717 ? 57.144 28.332  -20.153 0.00 40.24  ? 743  LEU   B HD21 1 
ATOM   22989 H HD22 . LEU   B  1 717 ? 56.015 29.099  -21.295 0.00 40.01  ? 743  LEU   B HD22 1 
ATOM   22990 H HD23 . LEU   B  1 717 ? 56.569 27.425  -21.564 0.00 39.29  ? 743  LEU   B HD23 1 
ATOM   22991 N N    . SER   B  1 718 ? 57.102 27.692  -26.800 1.00 27.11  ? 744  SER   B N    1 
ATOM   22992 C CA   . SER   B  1 718 ? 56.478 28.045  -28.070 1.00 28.00  ? 744  SER   B CA   1 
ATOM   22993 C C    . SER   B  1 718 ? 55.027 27.575  -28.148 1.00 28.54  ? 744  SER   B C    1 
ATOM   22994 O O    . SER   B  1 718 ? 54.624 26.701  -27.398 1.00 29.15  ? 744  SER   B O    1 
ATOM   22995 C CB   . SER   B  1 718 ? 57.301 27.513  -29.241 1.00 30.02  ? 744  SER   B CB   1 
ATOM   22996 O OG   . SER   B  1 718 ? 57.333 26.099  -29.292 1.00 32.34  ? 744  SER   B OG   1 
ATOM   22997 H H    . SER   B  1 718 ? 57.785 26.947  -26.881 0.00 34.45  ? 744  SER   B H    1 
ATOM   22998 H HA   . SER   B  1 718 ? 56.469 29.130  -28.162 0.00 35.97  ? 744  SER   B HA   1 
ATOM   22999 H HB2  . SER   B  1 718 ? 56.866 27.886  -30.168 0.00 37.39  ? 744  SER   B HB2  1 
ATOM   23000 H HB3  . SER   B  1 718 ? 58.321 27.881  -29.141 0.00 37.76  ? 744  SER   B HB3  1 
ATOM   23001 H HG   . SER   B  1 718 ? 57.938 25.749  -28.587 0.00 39.83  ? 744  SER   B HG   1 
ATOM   23002 N N    . SER   B  1 719 ? 54.217 28.227  -28.975 1.00 27.95  ? 745  SER   B N    1 
ATOM   23003 C CA   . SER   B  1 719 ? 52.813 27.883  -29.148 1.00 27.89  ? 745  SER   B CA   1 
ATOM   23004 C C    . SER   B  1 719 ? 52.025 27.803  -27.841 1.00 27.39  ? 745  SER   B C    1 
ATOM   23005 O O    . SER   B  1 719 ? 51.313 26.835  -27.590 1.00 27.15  ? 745  SER   B O    1 
ATOM   23006 C CB   . SER   B  1 719 ? 52.677 26.592  -29.952 1.00 28.99  ? 745  SER   B CB   1 
ATOM   23007 O OG   . SER   B  1 719 ? 53.377 26.708  -31.178 1.00 31.12  ? 745  SER   B OG   1 
ATOM   23008 H H    . SER   B  1 719 ? 54.508 29.013  -29.548 0.00 35.41  ? 745  SER   B H    1 
ATOM   23009 H HA   . SER   B  1 719 ? 52.352 28.675  -29.737 0.00 35.10  ? 745  SER   B HA   1 
ATOM   23010 H HB2  . SER   B  1 719 ? 53.097 25.759  -29.391 0.00 35.34  ? 745  SER   B HB2  1 
ATOM   23011 H HB3  . SER   B  1 719 ? 51.624 26.406  -30.161 0.00 35.41  ? 745  SER   B HB3  1 
ATOM   23012 H HG   . SER   B  1 719 ? 53.276 25.872  -31.705 0.00 37.46  ? 745  SER   B HG   1 
ATOM   23013 N N    . ASN   B  1 720 ? 52.166 28.824  -27.003 1.00 27.05  ? 746  ASN   B N    1 
ATOM   23014 C CA   . ASN   B  1 720 ? 51.400 28.950  -25.768 1.00 27.65  ? 746  ASN   B CA   1 
ATOM   23015 C C    . ASN   B  1 720 ? 50.498 30.222  -25.931 1.00 28.91  ? 746  ASN   B C    1 
ATOM   23016 O O    . ASN   B  1 720 ? 50.187 30.572  -27.077 1.00 29.11  ? 746  ASN   B O    1 
ATOM   23017 C CB   . ASN   B  1 720 ? 52.367 28.966  -24.548 1.00 27.31  ? 746  ASN   B CB   1 
ATOM   23018 C CG   . ASN   B  1 720 ? 52.636 27.580  -24.007 1.00 28.47  ? 746  ASN   B CG   1 
ATOM   23019 O OD1  . ASN   B  1 720 ? 51.882 27.081  -23.163 1.00 28.84  ? 746  ASN   B OD1  1 
ATOM   23020 N ND2  . ASN   B  1 720 ? 53.691 26.926  -24.483 1.00 26.43  ? 746  ASN   B ND2  1 
ATOM   23021 H H    . ASN   B  1 720 ? 52.803 29.598  -27.159 0.00 35.13  ? 746  ASN   B H    1 
ATOM   23022 H HA   . ASN   B  1 720 ? 50.703 28.120  -25.661 0.00 35.58  ? 746  ASN   B HA   1 
ATOM   23023 H HB2  . ASN   B  1 720 ? 53.316 29.401  -24.858 0.00 36.01  ? 746  ASN   B HB2  1 
ATOM   23024 H HB3  . ASN   B  1 720 ? 51.964 29.548  -23.722 0.00 36.37  ? 746  ASN   B HB3  1 
ATOM   23025 H HD21 . ASN   B  1 720 ? 53.902 25.993  -24.143 0.00 33.76  ? 746  ASN   B HD21 1 
ATOM   23026 H HD22 . ASN   B  1 720 ? 54.283 27.348  -25.192 0.00 34.01  ? 746  ASN   B HD22 1 
ATOM   23027 N N    . LEU   B  1 721 ? 50.028 30.862  -24.845 1.00 29.52  ? 747  LEU   B N    1 
ATOM   23028 C CA   . LEU   B  1 721 ? 49.172 32.044  -24.949 1.00 30.62  ? 747  LEU   B CA   1 
ATOM   23029 C C    . LEU   B  1 721 ? 49.820 33.252  -24.257 1.00 31.47  ? 747  LEU   B C    1 
ATOM   23030 O O    . LEU   B  1 721 ? 49.114 34.071  -23.682 1.00 31.71  ? 747  LEU   B O    1 
ATOM   23031 C CB   . LEU   B  1 721 ? 47.796 31.719  -24.334 1.00 30.55  ? 747  LEU   B CB   1 
ATOM   23032 C CG   . LEU   B  1 721 ? 47.053 30.535  -24.986 1.00 31.34  ? 747  LEU   B CG   1 
ATOM   23033 C CD1  . LEU   B  1 721 ? 45.799 30.194  -24.220 1.00 31.21  ? 747  LEU   B CD1  1 
ATOM   23034 C CD2  . LEU   B  1 721 ? 46.703 30.831  -26.443 1.00 32.19  ? 747  LEU   B CD2  1 
ATOM   23035 H H    . LEU   B  1 721 ? 50.167 30.575  -23.881 0.00 39.42  ? 747  LEU   B H    1 
ATOM   23036 H HA   . LEU   B  1 721 ? 49.016 32.327  -25.988 0.00 41.02  ? 747  LEU   B HA   1 
ATOM   23037 H HB2  . LEU   B  1 721 ? 47.932 31.485  -23.279 0.00 41.32  ? 747  LEU   B HB2  1 
ATOM   23038 H HB3  . LEU   B  1 721 ? 47.149 32.590  -24.435 0.00 41.56  ? 747  LEU   B HB3  1 
ATOM   23039 H HG   . LEU   B  1 721 ? 47.693 29.654  -24.975 0.00 40.93  ? 747  LEU   B HG   1 
ATOM   23040 H HD11 . LEU   B  1 721 ? 45.338 29.312  -24.661 0.00 40.85  ? 747  LEU   B HD11 1 
ATOM   23041 H HD12 . LEU   B  1 721 ? 46.062 29.995  -23.182 0.00 41.52  ? 747  LEU   B HD12 1 
ATOM   23042 H HD13 . LEU   B  1 721 ? 45.111 31.037  -24.271 0.00 41.77  ? 747  LEU   B HD13 1 
ATOM   23043 H HD21 . LEU   B  1 721 ? 46.013 30.067  -26.802 0.00 41.76  ? 747  LEU   B HD21 1 
ATOM   23044 H HD22 . LEU   B  1 721 ? 46.237 31.813  -26.506 0.00 42.64  ? 747  LEU   B HD22 1 
ATOM   23045 H HD23 . LEU   B  1 721 ? 47.612 30.811  -27.042 0.00 41.95  ? 747  LEU   B HD23 1 
ATOM   23046 N N    . LEU   B  1 722 ? 51.162 33.379  -24.332 1.00 32.13  ? 748  LEU   B N    1 
ATOM   23047 C CA   . LEU   B  1 722 ? 51.849 34.503  -23.711 1.00 32.70  ? 748  LEU   B CA   1 
ATOM   23048 C C    . LEU   B  1 722 ? 51.587 35.767  -24.496 1.00 33.53  ? 748  LEU   B C    1 
ATOM   23049 O O    . LEU   B  1 722 ? 51.789 35.798  -25.712 1.00 33.29  ? 748  LEU   B O    1 
ATOM   23050 C CB   . LEU   B  1 722 ? 53.364 34.289  -23.652 1.00 32.64  ? 748  LEU   B CB   1 
ATOM   23051 C CG   . LEU   B  1 722 ? 53.884 33.127  -22.821 1.00 33.78  ? 748  LEU   B CG   1 
ATOM   23052 C CD1  . LEU   B  1 722 ? 55.372 32.986  -23.013 1.00 33.96  ? 748  LEU   B CD1  1 
ATOM   23053 C CD2  . LEU   B  1 722 ? 53.563 33.318  -21.326 1.00 34.49  ? 748  LEU   B CD2  1 
ATOM   23054 H H    . LEU   B  1 722 ? 51.784 32.742  -24.819 0.00 43.33  ? 748  LEU   B H    1 
ATOM   23055 H HA   . LEU   B  1 722 ? 51.478 34.638  -22.696 0.00 45.65  ? 748  LEU   B HA   1 
ATOM   23056 H HB2  . LEU   B  1 722 ? 53.724 34.148  -24.670 0.00 44.73  ? 748  LEU   B HB2  1 
ATOM   23057 H HB3  . LEU   B  1 722 ? 53.809 35.194  -23.240 0.00 45.73  ? 748  LEU   B HB3  1 
ATOM   23058 H HG   . LEU   B  1 722 ? 53.409 32.207  -23.157 0.00 45.55  ? 748  LEU   B HG   1 
ATOM   23059 H HD11 . LEU   B  1 722 ? 55.731 32.149  -22.416 0.00 46.04  ? 748  LEU   B HD11 1 
ATOM   23060 H HD12 . LEU   B  1 722 ? 55.583 32.810  -24.067 0.00 45.84  ? 748  LEU   B HD12 1 
ATOM   23061 H HD13 . LEU   B  1 722 ? 55.856 33.906  -22.688 0.00 46.86  ? 748  LEU   B HD13 1 
ATOM   23062 H HD21 . LEU   B  1 722 ? 54.078 32.547  -20.754 0.00 47.39  ? 748  LEU   B HD21 1 
ATOM   23063 H HD22 . LEU   B  1 722 ? 53.903 34.304  -21.011 0.00 48.20  ? 748  LEU   B HD22 1 
ATOM   23064 H HD23 . LEU   B  1 722 ? 52.489 33.227  -21.172 0.00 47.52  ? 748  LEU   B HD23 1 
ATOM   23065 N N    . LYS   B  1 723 ? 51.143 36.810  -23.798 1.00 34.35  ? 749  LYS   B N    1 
ATOM   23066 C CA   . LYS   B  1 723 ? 50.922 38.137  -24.377 1.00 35.67  ? 749  LYS   B CA   1 
ATOM   23067 C C    . LYS   B  1 723 ? 52.179 39.006  -24.163 1.00 36.61  ? 749  LYS   B C    1 
ATOM   23068 O O    . LYS   B  1 723 ? 52.472 39.883  -24.972 1.00 36.92  ? 749  LYS   B O    1 
ATOM   23069 C CB   . LYS   B  1 723 ? 49.721 38.822  -23.708 1.00 38.74  ? 749  LYS   B CB   1 
ATOM   23070 C CG   . LYS   B  1 723 ? 48.392 38.080  -23.879 1.00 44.93  ? 749  LYS   B CG   1 
ATOM   23071 C CD   . LYS   B  1 723 ? 47.289 38.635  -22.975 1.00 51.44  ? 749  LYS   B CD   1 
ATOM   23072 C CE   . LYS   B  1 723 ? 47.015 40.108  -23.195 1.00 56.68  ? 749  LYS   B CE   1 
ATOM   23073 N NZ   . LYS   B  1 723 ? 45.654 40.515  -22.739 1.00 59.76  ? 749  LYS   B NZ   1 
ATOM   23074 H H    . LYS   B  1 723 ? 50.896 36.769  -22.815 0.00 48.77  ? 749  LYS   B H    1 
ATOM   23075 H HA   . LYS   B  1 723 ? 50.720 38.060  -25.444 0.00 50.30  ? 749  LYS   B HA   1 
ATOM   23076 H HB2  . LYS   B  1 723 ? 49.915 38.913  -22.640 0.00 55.36  ? 749  LYS   B HB2  1 
ATOM   23077 H HB3  . LYS   B  1 723 ? 49.615 39.813  -24.148 0.00 55.45  ? 749  LYS   B HB3  1 
ATOM   23078 H HG2  . LYS   B  1 723 ? 48.063 38.185  -24.912 0.00 61.71  ? 749  LYS   B HG2  1 
ATOM   23079 H HG3  . LYS   B  1 723 ? 48.523 37.026  -23.636 0.00 61.40  ? 749  LYS   B HG3  1 
ATOM   23080 H HD2  . LYS   B  1 723 ? 46.367 38.087  -23.168 0.00 70.06  ? 749  LYS   B HD2  1 
ATOM   23081 H HD3  . LYS   B  1 723 ? 47.585 38.501  -21.936 0.00 70.64  ? 749  LYS   B HD3  1 
ATOM   23082 H HE2  . LYS   B  1 723 ? 47.745 40.692  -22.637 0.00 78.06  ? 749  LYS   B HE2  1 
ATOM   23083 H HE3  . LYS   B  1 723 ? 47.098 40.329  -24.257 0.00 77.35  ? 749  LYS   B HE3  1 
ATOM   23084 H HZ1  . LYS   B  1 723 ? 45.521 41.509  -22.890 0.00 82.32  ? 749  LYS   B HZ1  1 
ATOM   23085 H HZ2  . LYS   B  1 723 ? 44.946 40.006  -23.260 0.00 81.29  ? 749  LYS   B HZ2  1 
ATOM   23086 H HZ3  . LYS   B  1 723 ? 45.545 40.311  -21.751 0.00 81.91  ? 749  LYS   B HZ3  1 
ATOM   23087 N N    . THR   B  1 724 ? 52.875 38.827  -23.030 1.00 36.64  ? 750  THR   B N    1 
ATOM   23088 C CA   . THR   B  1 724 ? 54.059 39.618  -22.712 1.00 37.65  ? 750  THR   B CA   1 
ATOM   23089 C C    . THR   B  1 724 ? 54.954 38.852  -21.725 1.00 38.58  ? 750  THR   B C    1 
ATOM   23090 O O    . THR   B  1 724 ? 54.548 37.816  -21.206 1.00 38.45  ? 750  THR   B O    1 
ATOM   23091 C CB   . THR   B  1 724 ? 53.597 40.985  -22.117 1.00 38.88  ? 750  THR   B CB   1 
ATOM   23092 O OG1  . THR   B  1 724 ? 54.732 41.844  -21.963 1.00 39.73  ? 750  THR   B OG1  1 
ATOM   23093 C CG2  . THR   B  1 724 ? 52.875 40.823  -20.788 1.00 39.27  ? 750  THR   B CG2  1 
ATOM   23094 H H    . THR   B  1 724 ? 52.632 38.162  -22.302 0.00 52.53  ? 750  THR   B H    1 
ATOM   23095 H HA   . THR   B  1 724 ? 54.641 39.807  -23.612 0.00 54.38  ? 750  THR   B HA   1 
ATOM   23096 H HB   . THR   B  1 724 ? 52.904 41.459  -22.811 0.00 57.09  ? 750  THR   B HB   1 
ATOM   23097 H HG1  . THR   B  1 724 ? 54.449 42.717  -21.585 0.00 59.43  ? 750  THR   B HG1  1 
ATOM   23098 H HG21 . THR   B  1 724 ? 52.405 41.767  -20.516 0.00 58.57  ? 750  THR   B HG21 1 
ATOM   23099 H HG22 . THR   B  1 724 ? 52.105 40.056  -20.854 0.00 57.35  ? 750  THR   B HG22 1 
ATOM   23100 H HG23 . THR   B  1 724 ? 53.577 40.555  -20.000 0.00 58.01  ? 750  THR   B HG23 1 
ATOM   23101 N N    . ILE   B  1 725 ? 56.164 39.364  -21.464 1.00 39.69  ? 751  ILE   B N    1 
ATOM   23102 C CA   . ILE   B  1 725 ? 57.063 38.790  -20.473 1.00 41.92  ? 751  ILE   B CA   1 
ATOM   23103 C C    . ILE   B  1 725 ? 57.567 39.974  -19.631 1.00 44.46  ? 751  ILE   B C    1 
ATOM   23104 O O    . ILE   B  1 725 ? 58.252 40.840  -20.165 1.00 44.38  ? 751  ILE   B O    1 
ATOM   23105 C CB   . ILE   B  1 725 ? 58.212 37.973  -21.121 1.00 42.21  ? 751  ILE   B CB   1 
ATOM   23106 C CG1  . ILE   B  1 725 ? 57.648 36.838  -22.020 1.00 43.20  ? 751  ILE   B CG1  1 
ATOM   23107 C CG2  . ILE   B  1 725 ? 59.098 37.390  -20.025 1.00 42.66  ? 751  ILE   B CG2  1 
ATOM   23108 C CD1  . ILE   B  1 725 ? 58.695 36.090  -22.882 1.00 44.26  ? 751  ILE   B CD1  1 
ATOM   23109 H H    . ILE   B  1 725 ? 56.545 40.180  -21.931 0.00 57.77  ? 751  ILE   B H    1 
ATOM   23110 H HA   . ILE   B  1 725 ? 56.516 38.122  -19.810 0.00 60.00  ? 751  ILE   B HA   1 
ATOM   23111 H HB   . ILE   B  1 725 ? 58.811 38.641  -21.737 0.00 60.16  ? 751  ILE   B HB   1 
ATOM   23112 H HG12 . ILE   B  1 725 ? 57.166 36.101  -21.380 0.00 59.83  ? 751  ILE   B HG12 1 
ATOM   23113 H HG13 . ILE   B  1 725 ? 56.916 37.254  -22.710 0.00 59.99  ? 751  ILE   B HG13 1 
ATOM   23114 H HG21 . ILE   B  1 725 ? 59.861 36.749  -20.464 0.00 60.22  ? 751  ILE   B HG21 1 
ATOM   23115 H HG22 . ILE   B  1 725 ? 59.586 38.195  -19.478 0.00 61.40  ? 751  ILE   B HG22 1 
ATOM   23116 H HG23 . ILE   B  1 725 ? 58.474 36.816  -19.343 0.00 60.49  ? 751  ILE   B HG23 1 
ATOM   23117 H HD11 . ILE   B  1 725 ? 58.174 35.527  -23.654 0.00 60.11  ? 751  ILE   B HD11 1 
ATOM   23118 H HD12 . ILE   B  1 725 ? 59.366 36.816  -23.338 0.00 61.07  ? 751  ILE   B HD12 1 
ATOM   23119 H HD13 . ILE   B  1 725 ? 59.258 35.405  -22.250 0.00 60.66  ? 751  ILE   B HD13 1 
ATOM   23120 N N    . ASN   B  1 726 ? 57.190 40.036  -18.337 1.00 46.77  ? 752  ASN   B N    1 
ATOM   23121 C CA   . ASN   B  1 726 ? 57.574 41.144  -17.444 1.00 49.55  ? 752  ASN   B CA   1 
ATOM   23122 C C    . ASN   B  1 726 ? 59.038 41.095  -17.034 1.00 52.33  ? 752  ASN   B C    1 
ATOM   23123 O O    . ASN   B  1 726 ? 59.596 40.013  -16.899 1.00 52.29  ? 752  ASN   B O    1 
ATOM   23124 C CB   . ASN   B  1 726 ? 56.734 41.123  -16.153 1.00 50.75  ? 752  ASN   B CB   1 
ATOM   23125 C CG   . ASN   B  1 726 ? 55.265 41.365  -16.362 1.00 54.58  ? 752  ASN   B CG   1 
ATOM   23126 O OD1  . ASN   B  1 726 ? 54.851 42.042  -17.313 1.00 56.15  ? 752  ASN   B OD1  1 
ATOM   23127 N ND2  . ASN   B  1 726 ? 54.438 40.824  -15.471 1.00 55.45  ? 752  ASN   B ND2  1 
ATOM   23128 H H    . ASN   B  1 726 ? 56.626 39.327  -17.878 0.00 67.34  ? 752  ASN   B H    1 
ATOM   23129 H HA   . ASN   B  1 726 ? 57.401 42.091  -17.954 0.00 72.48  ? 752  ASN   B HA   1 
ATOM   23130 H HB2  . ASN   B  1 726 ? 56.858 40.151  -15.679 0.00 73.62  ? 752  ASN   B HB2  1 
ATOM   23131 H HB3  . ASN   B  1 726 ? 57.103 41.903  -15.488 0.00 74.85  ? 752  ASN   B HB3  1 
ATOM   23132 H HD21 . ASN   B  1 726 ? 53.436 40.958  -15.568 0.00 79.50  ? 752  ASN   B HD21 1 
ATOM   23133 H HD22 . ASN   B  1 726 ? 54.800 40.284  -14.692 0.00 79.60  ? 752  ASN   B HD22 1 
ATOM   23134 N N    . LYS   B  1 727 ? 59.623 42.262  -16.724 1.00 54.82  ? 753  LYS   B N    1 
ATOM   23135 C CA   . LYS   B  1 727 ? 61.007 42.373  -16.242 1.00 57.55  ? 753  LYS   B CA   1 
ATOM   23136 C C    . LYS   B  1 727 ? 61.237 41.490  -14.995 1.00 59.75  ? 753  LYS   B C    1 
ATOM   23137 O O    . LYS   B  1 727 ? 62.326 40.939  -14.831 1.00 60.42  ? 753  LYS   B O    1 
ATOM   23138 C CB   . LYS   B  1 727 ? 61.333 43.843  -15.902 1.00 60.13  ? 753  LYS   B CB   1 
ATOM   23139 C CG   . LYS   B  1 727 ? 62.818 44.132  -15.666 1.00 65.21  ? 753  LYS   B CG   1 
ATOM   23140 C CD   . LYS   B  1 727 ? 63.018 45.446  -14.907 1.00 70.96  ? 753  LYS   B CD   1 
ATOM   23141 C CE   . LYS   B  1 727 ? 64.474 45.732  -14.603 1.00 75.98  ? 753  LYS   B CE   1 
ATOM   23142 N NZ   . LYS   B  1 727 ? 65.188 46.320  -15.768 1.00 78.73  ? 753  LYS   B NZ   1 
ATOM   23143 H H    . LYS   B  1 727 ? 59.148 43.157  -16.796 0.00 80.23  ? 753  LYS   B H    1 
ATOM   23144 H HA   . LYS   B  1 727 ? 61.687 42.042  -17.023 0.00 83.03  ? 753  LYS   B HA   1 
ATOM   23145 H HB2  . LYS   B  1 727 ? 61.011 44.478  -16.726 0.00 87.81  ? 753  LYS   B HB2  1 
ATOM   23146 H HB3  . LYS   B  1 727 ? 60.791 44.119  -14.999 0.00 88.32  ? 753  LYS   B HB3  1 
ATOM   23147 H HG2  . LYS   B  1 727 ? 63.274 43.334  -15.081 0.00 94.25  ? 753  LYS   B HG2  1 
ATOM   23148 H HG3  . LYS   B  1 727 ? 63.318 44.221  -16.629 0.00 94.19  ? 753  LYS   B HG3  1 
ATOM   23149 H HD2  . LYS   B  1 727 ? 62.631 46.267  -15.508 0.00 102.94 ? 753  LYS   B HD2  1 
ATOM   23150 H HD3  . LYS   B  1 727 ? 62.487 45.395  -13.958 0.00 103.00 ? 753  LYS   B HD3  1 
ATOM   23151 H HE2  . LYS   B  1 727 ? 64.532 46.439  -13.777 0.00 110.28 ? 753  LYS   B HE2  1 
ATOM   23152 H HE3  . LYS   B  1 727 ? 64.976 44.803  -14.335 0.00 108.90 ? 753  LYS   B HE3  1 
ATOM   23153 H HZ1  . LYS   B  1 727 ? 66.168 46.457  -15.540 0.00 113.20 ? 753  LYS   B HZ1  1 
ATOM   23154 H HZ2  . LYS   B  1 727 ? 65.118 45.699  -16.567 0.00 111.96 ? 753  LYS   B HZ2  1 
ATOM   23155 H HZ3  . LYS   B  1 727 ? 64.778 47.217  -16.008 0.00 113.28 ? 753  LYS   B HZ3  1 
ATOM   23156 N N    . SER   B  1 728 ? 60.213 41.363  -14.132 1.00 60.74  ? 754  SER   B N    1 
ATOM   23157 C CA   . SER   B  1 728 ? 60.288 40.550  -12.919 1.00 62.26  ? 754  SER   B CA   1 
ATOM   23158 C C    . SER   B  1 728 ? 60.456 39.070  -13.233 1.00 63.88  ? 754  SER   B C    1 
ATOM   23159 O O    . SER   B  1 728 ? 61.169 38.377  -12.509 1.00 64.05  ? 754  SER   B O    1 
ATOM   23160 C CB   . SER   B  1 728 ? 59.041 40.753  -12.064 1.00 63.21  ? 754  SER   B CB   1 
ATOM   23161 O OG   . SER   B  1 728 ? 57.887 40.156  -12.633 1.00 64.63  ? 754  SER   B OG   1 
ATOM   23162 H H    . SER   B  1 728 ? 59.315 41.823  -14.246 0.00 87.65  ? 754  SER   B H    1 
ATOM   23163 H HA   . SER   B  1 728 ? 61.151 40.868  -12.335 0.00 90.06  ? 754  SER   B HA   1 
ATOM   23164 H HB2  . SER   B  1 728 ? 59.226 40.322  -11.081 0.00 91.11  ? 754  SER   B HB2  1 
ATOM   23165 H HB3  . SER   B  1 728 ? 58.861 41.821  -11.956 0.00 91.65  ? 754  SER   B HB3  1 
ATOM   23166 H HG   . SER   B  1 728 ? 57.097 40.323  -12.055 0.00 92.05  ? 754  SER   B HG   1 
ATOM   23167 N N    . ALA   B  1 729 ? 59.792 38.582  -14.296 1.00 64.98  ? 755  ALA   B N    1 
ATOM   23168 C CA   . ALA   B  1 729 ? 59.876 37.183  -14.712 1.00 66.42  ? 755  ALA   B CA   1 
ATOM   23169 C C    . ALA   B  1 729 ? 61.279 36.777  -15.181 1.00 67.93  ? 755  ALA   B C    1 
ATOM   23170 O O    . ALA   B  1 729 ? 61.691 35.649  -14.924 1.00 68.05  ? 755  ALA   B O    1 
ATOM   23171 C CB   . ALA   B  1 729 ? 58.863 36.905  -15.812 1.00 66.71  ? 755  ALA   B CB   1 
ATOM   23172 H H    . ALA   B  1 729 ? 59.171 39.133  -14.881 0.00 90.67  ? 755  ALA   B H    1 
ATOM   23173 H HA   . ALA   B  1 729 ? 59.596 36.538  -13.882 0.00 91.40  ? 755  ALA   B HA   1 
ATOM   23174 H HB1  . ALA   B  1 729 ? 58.929 35.855  -16.095 0.00 90.25  ? 755  ALA   B HB1  1 
ATOM   23175 H HB2  . ALA   B  1 729 ? 57.865 37.128  -15.439 0.00 91.12  ? 755  ALA   B HB2  1 
ATOM   23176 H HB3  . ALA   B  1 729 ? 59.091 37.536  -16.669 0.00 90.97  ? 755  ALA   B HB3  1 
ATOM   23177 N N    . LEU   B  1 730 ? 62.009 37.673  -15.872 1.00 69.07  ? 756  LEU   B N    1 
ATOM   23178 C CA   . LEU   B  1 730 ? 63.337 37.341  -16.409 1.00 70.59  ? 756  LEU   B CA   1 
ATOM   23179 C C    . LEU   B  1 730 ? 64.486 37.257  -15.368 1.00 72.04  ? 756  LEU   B C    1 
ATOM   23180 O O    . LEU   B  1 730 ? 65.141 36.219  -15.267 1.00 72.45  ? 756  LEU   B O    1 
ATOM   23181 C CB   . LEU   B  1 730 ? 63.754 38.336  -17.523 1.00 70.79  ? 756  LEU   B CB   1 
ATOM   23182 C CG   . LEU   B  1 730 ? 63.071 38.328  -18.911 1.00 71.97  ? 756  LEU   B CG   1 
ATOM   23183 C CD1  . LEU   B  1 730 ? 62.575 36.951  -19.330 1.00 72.51  ? 756  LEU   B CD1  1 
ATOM   23184 C CD2  . LEU   B  1 730 ? 62.005 39.383  -18.995 1.00 72.47  ? 756  LEU   B CD2  1 
ATOM   23185 H H    . LEU   B  1 730 ? 61.706 38.618  -16.084 0.00 95.14  ? 756  LEU   B H    1 
ATOM   23186 H HA   . LEU   B  1 730 ? 63.262 36.361  -16.878 0.00 95.57  ? 756  LEU   B HA   1 
ATOM   23187 H HB2  . LEU   B  1 730 ? 63.643 39.343  -17.124 0.00 97.52  ? 756  LEU   B HB2  1 
ATOM   23188 H HB3  . LEU   B  1 730 ? 64.812 38.164  -17.715 0.00 96.76  ? 756  LEU   B HB3  1 
ATOM   23189 H HG   . LEU   B  1 730 ? 63.824 38.606  -19.645 0.00 97.43  ? 756  LEU   B HG   1 
ATOM   23190 H HD11 . LEU   B  1 730 ? 62.256 36.992  -20.370 0.00 96.56  ? 756  LEU   B HD11 1 
ATOM   23191 H HD12 . LEU   B  1 730 ? 63.384 36.231  -19.214 0.00 96.81  ? 756  LEU   B HD12 1 
ATOM   23192 H HD13 . LEU   B  1 730 ? 61.733 36.672  -18.698 0.00 96.97  ? 756  LEU   B HD13 1 
ATOM   23193 H HD21 . LEU   B  1 730 ? 61.532 39.336  -19.974 0.00 97.95  ? 756  LEU   B HD21 1 
ATOM   23194 H HD22 . LEU   B  1 730 ? 61.268 39.204  -18.213 0.00 98.54  ? 756  LEU   B HD22 1 
ATOM   23195 H HD23 . LEU   B  1 730 ? 62.461 40.362  -18.858 0.00 99.20  ? 756  LEU   B HD23 1 
ATOM   23196 N N    . GLU   B  1 731 ? 64.770 38.361  -14.654 1.00 72.61  ? 757  GLU   B N    1 
ATOM   23197 C CA   . GLU   B  1 731 ? 65.887 38.454  -13.707 1.00 73.69  ? 757  GLU   B CA   1 
ATOM   23198 C C    . GLU   B  1 731 ? 65.420 38.576  -12.257 1.00 74.32  ? 757  GLU   B C    1 
ATOM   23199 O O    . GLU   B  1 731 ? 64.290 38.997  -12.002 1.00 74.38  ? 757  GLU   B O    1 
ATOM   23200 C CB   . GLU   B  1 731 ? 66.755 39.678  -14.059 1.00 75.91  ? 757  GLU   B CB   1 
ATOM   23201 C CG   . GLU   B  1 731 ? 67.414 39.603  -15.431 1.00 80.03  ? 757  GLU   B CG   1 
ATOM   23202 C CD   . GLU   B  1 731 ? 68.074 40.889  -15.894 1.00 84.63  ? 757  GLU   B CD   1 
ATOM   23203 O OE1  . GLU   B  1 731 ? 68.194 41.833  -15.080 1.00 85.66  ? 757  GLU   B OE1  1 
ATOM   23204 O OE2  . GLU   B  1 731 ? 68.469 40.953  -17.081 1.00 85.92  ? 757  GLU   B OE2  1 
ATOM   23205 H H    . GLU   B  1 731 ? 64.219 39.212  -14.710 0.00 100.88 ? 757  GLU   B H    1 
ATOM   23206 H HA   . GLU   B  1 731 ? 66.526 37.574  -13.773 0.00 102.21 ? 757  GLU   B HA   1 
ATOM   23207 H HB2  . GLU   B  1 731 ? 66.124 40.566  -14.036 0.00 106.45 ? 757  GLU   B HB2  1 
ATOM   23208 H HB3  . GLU   B  1 731 ? 67.549 39.766  -13.319 0.00 106.66 ? 757  GLU   B HB3  1 
ATOM   23209 H HG2  . GLU   B  1 731 ? 68.181 38.831  -15.406 0.00 110.09 ? 757  GLU   B HG2  1 
ATOM   23210 H HG3  . GLU   B  1 731 ? 66.663 39.344  -16.176 0.00 109.72 ? 757  GLU   B HG3  1 
ATOM   23211 N N    . THR   B  1 732 ? 66.296 38.198  -11.304 1.00 74.70  ? 758  THR   B N    1 
ATOM   23212 C CA   . THR   B  1 732 ? 66.020 38.302  -9.867  1.00 75.61  ? 758  THR   B CA   1 
ATOM   23213 C C    . THR   B  1 732 ? 67.359 38.547  -9.101  1.00 76.05  ? 758  THR   B C    1 
ATOM   23214 O O    . THR   B  1 732 ? 67.641 39.698  -8.760  1.00 76.41  ? 758  THR   B O    1 
ATOM   23215 C CB   . THR   B  1 732 ? 65.168 37.103  -9.370  1.00 77.15  ? 758  THR   B CB   1 
ATOM   23216 O OG1  . THR   B  1 732 ? 63.929 37.076  -10.081 1.00 78.30  ? 758  THR   B OG1  1 
ATOM   23217 C CG2  . THR   B  1 732 ? 64.910 37.152  -7.866  1.00 77.57  ? 758  THR   B CG2  1 
ATOM   23218 H H    . THR   B  1 732 ? 67.213 37.812  -11.506 0.00 104.91 ? 758  THR   B H    1 
ATOM   23219 H HA   . THR   B  1 732 ? 65.406 39.187  -9.707  0.00 107.36 ? 758  THR   B HA   1 
ATOM   23220 H HB   . THR   B  1 732 ? 65.708 36.182  -9.581  0.00 107.53 ? 758  THR   B HB   1 
ATOM   23221 H HG1  . THR   B  1 732 ? 63.411 37.903  -9.896  0.00 109.24 ? 758  THR   B HG1  1 
ATOM   23222 H HG21 . THR   B  1 732 ? 64.150 36.420  -7.597  0.00 108.88 ? 758  THR   B HG21 1 
ATOM   23223 H HG22 . THR   B  1 732 ? 65.821 36.922  -7.317  0.00 109.75 ? 758  THR   B HG22 1 
ATOM   23224 H HG23 . THR   B  1 732 ? 64.563 38.144  -7.579  0.00 110.04 ? 758  THR   B HG23 1 
ATOM   23225 N N    . LYS   B  1 733 ? 68.188 37.496  -8.866  1.00 75.84  ? 759  LYS   B N    1 
ATOM   23226 C CA   . LYS   B  1 733 ? 69.471 37.622  -8.154  1.00 76.17  ? 759  LYS   B CA   1 
ATOM   23227 C C    . LYS   B  1 733 ? 70.623 37.015  -8.972  1.00 75.74  ? 759  LYS   B C    1 
ATOM   23228 O O    . LYS   B  1 733 ? 71.665 37.654  -9.130  1.00 75.95  ? 759  LYS   B O    1 
ATOM   23229 C CB   . LYS   B  1 733 ? 69.397 37.006  -6.736  1.00 78.58  ? 759  LYS   B CB   1 
ATOM   23230 C CG   . LYS   B  1 733 ? 68.804 35.596  -6.659  1.00 83.33  ? 759  LYS   B CG   1 
ATOM   23231 C CD   . LYS   B  1 733 ? 68.800 35.048  -5.223  1.00 88.14  ? 759  LYS   B CD   1 
ATOM   23232 C CE   . LYS   B  1 733 ? 69.955 34.119  -4.908  1.00 91.99  ? 759  LYS   B CE   1 
ATOM   23233 N NZ   . LYS   B  1 733 ? 71.264 34.824  -4.865  1.00 94.37  ? 759  LYS   B NZ   1 
ATOM   23234 H H    . LYS   B  1 733 ? 67.972 36.549  -9.159  0.00 107.21 ? 759  LYS   B H    1 
ATOM   23235 H HA   . LYS   B  1 733 ? 69.700 38.677  -8.014  0.00 110.01 ? 759  LYS   B HA   1 
ATOM   23236 H HB2  . LYS   B  1 733 ? 70.404 36.963  -6.326  0.00 113.11 ? 759  LYS   B HB2  1 
ATOM   23237 H HB3  . LYS   B  1 733 ? 68.781 37.654  -6.114  0.00 113.06 ? 759  LYS   B HB3  1 
ATOM   23238 H HG2  . LYS   B  1 733 ? 67.772 35.618  -7.004  0.00 116.73 ? 759  LYS   B HG2  1 
ATOM   23239 H HG3  . LYS   B  1 733 ? 69.391 34.921  -7.279  0.00 116.74 ? 759  LYS   B HG3  1 
ATOM   23240 H HD2  . LYS   B  1 733 ? 68.855 35.885  -4.528  0.00 124.52 ? 759  LYS   B HD2  1 
ATOM   23241 H HD3  . LYS   B  1 733 ? 67.877 34.495  -5.061  0.00 123.10 ? 759  LYS   B HD3  1 
ATOM   23242 H HE2  . LYS   B  1 733 ? 69.787 33.671  -3.929  0.00 128.56 ? 759  LYS   B HE2  1 
ATOM   23243 H HE3  . LYS   B  1 733 ? 70.013 33.341  -5.667  0.00 127.34 ? 759  LYS   B HE3  1 
ATOM   23244 H HZ1  . LYS   B  1 733 ? 71.990 34.178  -4.573  0.00 131.96 ? 759  LYS   B HZ1  1 
ATOM   23245 H HZ2  . LYS   B  1 733 ? 71.498 35.186  -5.784  0.00 131.58 ? 759  LYS   B HZ2  1 
ATOM   23246 H HZ3  . LYS   B  1 733 ? 71.222 35.595  -4.206  0.00 132.74 ? 759  LYS   B HZ3  1 
ATOM   23247 N N    . THR   B  1 734 ? 70.426 35.800  -9.508  1.00 74.89  ? 760  THR   B N    1 
ATOM   23248 C CA   . THR   B  1 734 ? 71.413 35.117  -10.342 1.00 74.51  ? 760  THR   B CA   1 
ATOM   23249 C C    . THR   B  1 734 ? 70.889 35.129  -11.777 1.00 73.57  ? 760  THR   B C    1 
ATOM   23250 O O    . THR   B  1 734 ? 69.766 34.681  -12.004 1.00 73.76  ? 760  THR   B O    1 
ATOM   23251 C CB   . THR   B  1 734 ? 71.611 33.675  -9.856  1.00 75.96  ? 760  THR   B CB   1 
ATOM   23252 O OG1  . THR   B  1 734 ? 70.362 32.979  -9.923  1.00 76.97  ? 760  THR   B OG1  1 
ATOM   23253 C CG2  . THR   B  1 734 ? 72.183 33.608  -8.446  1.00 76.32  ? 760  THR   B CG2  1 
ATOM   23254 H H    . THR   B  1 734 ? 69.574 35.263  -9.390  0.00 105.62 ? 760  THR   B H    1 
ATOM   23255 H HA   . THR   B  1 734 ? 72.378 35.620  -10.312 0.00 105.70 ? 760  THR   B HA   1 
ATOM   23256 H HB   . THR   B  1 734 ? 72.319 33.181  -10.519 0.00 105.92 ? 760  THR   B HB   1 
ATOM   23257 H HG1  . THR   B  1 734 ? 70.476 32.042  -9.615  0.00 106.46 ? 760  THR   B HG1  1 
ATOM   23258 H HG21 . THR   B  1 734 ? 72.350 32.569  -8.164  0.00 107.34 ? 760  THR   B HG21 1 
ATOM   23259 H HG22 . THR   B  1 734 ? 73.131 34.142  -8.405  0.00 108.32 ? 760  THR   B HG22 1 
ATOM   23260 H HG23 . THR   B  1 734 ? 71.495 34.058  -7.734  0.00 108.15 ? 760  THR   B HG23 1 
ATOM   23261 N N    . THR   B  1 735 ? 71.671 35.649  -12.741 1.00 72.35  ? 761  THR   B N    1 
ATOM   23262 C CA   . THR   B  1 735 ? 71.228 35.704  -14.140 1.00 71.67  ? 761  THR   B CA   1 
ATOM   23263 C C    . THR   B  1 735 ? 70.952 34.295  -14.716 1.00 69.94  ? 761  THR   B C    1 
ATOM   23264 O O    . THR   B  1 735 ? 71.362 33.285  -14.141 1.00 70.39  ? 761  THR   B O    1 
ATOM   23265 C CB   . THR   B  1 735 ? 72.218 36.526  -15.007 1.00 73.57  ? 761  THR   B CB   1 
ATOM   23266 O OG1  . THR   B  1 735 ? 71.602 36.831  -16.267 1.00 74.61  ? 761  THR   B OG1  1 
ATOM   23267 C CG2  . THR   B  1 735 ? 73.536 35.790  -15.254 1.00 74.30  ? 761  THR   B CG2  1 
ATOM   23268 H H    . THR   B  1 735 ? 72.587 36.057  -12.582 0.00 101.87 ? 761  THR   B H    1 
ATOM   23269 H HA   . THR   B  1 735 ? 70.274 36.230  -14.143 0.00 99.76  ? 761  THR   B HA   1 
ATOM   23270 H HB   . THR   B  1 735 ? 72.448 37.460  -14.498 0.00 103.29 ? 761  THR   B HB   1 
ATOM   23271 H HG1  . THR   B  1 735 ? 72.010 37.646  -16.660 0.00 103.44 ? 761  THR   B HG1  1 
ATOM   23272 H HG21 . THR   B  1 735 ? 74.267 36.480  -15.673 0.00 103.65 ? 761  THR   B HG21 1 
ATOM   23273 H HG22 . THR   B  1 735 ? 73.920 35.387  -14.318 0.00 103.79 ? 761  THR   B HG22 1 
ATOM   23274 H HG23 . THR   B  1 735 ? 73.388 34.974  -15.960 0.00 102.47 ? 761  THR   B HG23 1 
ATOM   23275 N N    . THR   B  1 736 ? 70.246 34.241  -15.847 1.00 67.68  ? 762  THR   B N    1 
ATOM   23276 C CA   . THR   B  1 736 ? 69.829 32.985  -16.473 1.00 65.85  ? 762  THR   B CA   1 
ATOM   23277 C C    . THR   B  1 736 ? 70.966 32.123  -17.035 1.00 63.45  ? 762  THR   B C    1 
ATOM   23278 O O    . THR   B  1 736 ? 71.772 32.615  -17.823 1.00 63.66  ? 762  THR   B O    1 
ATOM   23279 C CB   . THR   B  1 736 ? 68.860 33.287  -17.631 1.00 67.17  ? 762  THR   B CB   1 
ATOM   23280 O OG1  . THR   B  1 736 ? 69.515 34.154  -18.563 1.00 68.25  ? 762  THR   B OG1  1 
ATOM   23281 C CG2  . THR   B  1 736 ? 67.569 33.944  -17.166 1.00 67.60  ? 762  THR   B CG2  1 
ATOM   23282 H H    . THR   B  1 736 ? 69.981 35.075  -16.363 0.00 93.20  ? 762  THR   B H    1 
ATOM   23283 H HA   . THR   B  1 736 ? 69.285 32.400  -15.733 0.00 89.66  ? 762  THR   B HA   1 
ATOM   23284 H HB   . THR   B  1 736 ? 68.595 32.350  -18.120 0.00 89.99  ? 762  THR   B HB   1 
ATOM   23285 H HG1  . THR   B  1 736 ? 69.988 33.634  -19.265 0.00 91.97  ? 762  THR   B HG1  1 
ATOM   23286 H HG21 . THR   B  1 736 ? 66.914 34.122  -18.017 0.00 90.87  ? 762  THR   B HG21 1 
ATOM   23287 H HG22 . THR   B  1 736 ? 67.048 33.282  -16.476 0.00 91.21  ? 762  THR   B HG22 1 
ATOM   23288 H HG23 . THR   B  1 736 ? 67.775 34.892  -16.670 0.00 92.12  ? 762  THR   B HG23 1 
ATOM   23289 N N    . LYS   B  1 737 ? 70.987 30.821  -16.693 1.00 60.91  ? 763  LYS   B N    1 
ATOM   23290 C CA   . LYS   B  1 737 ? 71.934 29.871  -17.302 1.00 58.72  ? 763  LYS   B CA   1 
ATOM   23291 C C    . LYS   B  1 737 ? 71.290 29.175  -18.552 1.00 54.99  ? 763  LYS   B C    1 
ATOM   23292 O O    . LYS   B  1 737 ? 71.820 28.180  -19.054 1.00 54.97  ? 763  LYS   B O    1 
ATOM   23293 C CB   . LYS   B  1 737 ? 72.437 28.835  -16.275 1.00 61.56  ? 763  LYS   B CB   1 
ATOM   23294 C CG   . LYS   B  1 737 ? 73.523 29.363  -15.334 1.00 67.16  ? 763  LYS   B CG   1 
ATOM   23295 C CD   . LYS   B  1 737 ? 73.014 30.444  -14.387 1.00 72.34  ? 763  LYS   B CD   1 
ATOM   23296 C CE   . LYS   B  1 737 ? 73.165 30.064  -12.939 1.00 76.35  ? 763  LYS   B CE   1 
ATOM   23297 N NZ   . LYS   B  1 737 ? 72.515 31.056  -12.047 1.00 78.62  ? 763  LYS   B NZ   1 
ATOM   23298 H H    . LYS   B  1 737 ? 70.359 30.399  -16.018 0.00 83.11  ? 763  LYS   B H    1 
ATOM   23299 H HA   . LYS   B  1 737 ? 72.803 30.412  -17.673 0.00 80.51  ? 763  LYS   B HA   1 
ATOM   23300 H HB2  . LYS   B  1 737 ? 71.602 28.499  -15.664 0.00 83.63  ? 763  LYS   B HB2  1 
ATOM   23301 H HB3  . LYS   B  1 737 ? 72.867 27.981  -16.796 0.00 83.29  ? 763  LYS   B HB3  1 
ATOM   23302 H HG2  . LYS   B  1 737 ? 73.907 28.540  -14.733 0.00 91.62  ? 763  LYS   B HG2  1 
ATOM   23303 H HG3  . LYS   B  1 737 ? 74.326 29.795  -15.929 0.00 91.71  ? 763  LYS   B HG3  1 
ATOM   23304 H HD2  . LYS   B  1 737 ? 73.580 31.359  -14.555 0.00 99.08  ? 763  LYS   B HD2  1 
ATOM   23305 H HD3  . LYS   B  1 737 ? 71.956 30.622  -14.573 0.00 98.16  ? 763  LYS   B HD3  1 
ATOM   23306 H HE2  . LYS   B  1 737 ? 72.694 29.096  -12.769 0.00 103.43 ? 763  LYS   B HE2  1 
ATOM   23307 H HE3  . LYS   B  1 737 ? 74.224 30.018  -12.688 0.00 104.47 ? 763  LYS   B HE3  1 
ATOM   23308 H HZ1  . LYS   B  1 737 ? 72.631 30.782  -11.077 0.00 107.79 ? 763  LYS   B HZ1  1 
ATOM   23309 H HZ2  . LYS   B  1 737 ? 72.936 31.969  -12.188 0.00 107.89 ? 763  LYS   B HZ2  1 
ATOM   23310 H HZ3  . LYS   B  1 737 ? 71.524 31.115  -12.257 0.00 106.93 ? 763  LYS   B HZ3  1 
ATOM   23311 N N    . LEU   B  1 738 ? 70.177 29.729  -19.079 1.00 51.74  ? 764  LEU   B N    1 
ATOM   23312 C CA   . LEU   B  1 738 ? 69.555 29.226  -20.286 1.00 49.03  ? 764  LEU   B CA   1 
ATOM   23313 C C    . LEU   B  1 738 ? 70.456 29.518  -21.475 1.00 45.95  ? 764  LEU   B C    1 
ATOM   23314 O O    . LEU   B  1 738 ? 71.145 30.537  -21.507 1.00 45.97  ? 764  LEU   B O    1 
ATOM   23315 C CB   . LEU   B  1 738 ? 68.214 29.932  -20.556 1.00 49.24  ? 764  LEU   B CB   1 
ATOM   23316 C CG   . LEU   B  1 738 ? 67.017 29.509  -19.735 1.00 50.87  ? 764  LEU   B CG   1 
ATOM   23317 C CD1  . LEU   B  1 738 ? 65.911 30.543  -19.852 1.00 51.66  ? 764  LEU   B CD1  1 
ATOM   23318 C CD2  . LEU   B  1 738 ? 66.509 28.130  -20.156 1.00 51.28  ? 764  LEU   B CD2  1 
ATOM   23319 H H    . LEU   B  1 738 ? 69.688 30.527  -18.686 0.00 70.74  ? 764  LEU   B H    1 
ATOM   23320 H HA   . LEU   B  1 738 ? 69.393 28.153  -20.201 0.00 65.74  ? 764  LEU   B HA   1 
ATOM   23321 H HB2  . LEU   B  1 738 ? 68.348 31.004  -20.411 0.00 66.82  ? 764  LEU   B HB2  1 
ATOM   23322 H HB3  . LEU   B  1 738 ? 67.957 29.756  -21.599 0.00 65.68  ? 764  LEU   B HB3  1 
ATOM   23323 H HG   . LEU   B  1 738 ? 67.309 29.451  -18.688 0.00 68.58  ? 764  LEU   B HG   1 
ATOM   23324 H HD11 . LEU   B  1 738 ? 65.037 30.193  -19.304 0.00 68.82  ? 764  LEU   B HD11 1 
ATOM   23325 H HD12 . LEU   B  1 738 ? 66.258 31.485  -19.431 0.00 69.86  ? 764  LEU   B HD12 1 
ATOM   23326 H HD13 . LEU   B  1 738 ? 65.658 30.675  -20.903 0.00 68.90  ? 764  LEU   B HD13 1 
ATOM   23327 H HD21 . LEU   B  1 738 ? 65.581 27.919  -19.626 0.00 67.62  ? 764  LEU   B HD21 1 
ATOM   23328 H HD22 . LEU   B  1 738 ? 66.324 28.123  -21.229 0.00 67.20  ? 764  LEU   B HD22 1 
ATOM   23329 H HD23 . LEU   B  1 738 ? 67.248 27.372  -19.900 0.00 67.66  ? 764  LEU   B HD23 1 
ATOM   23330 N N    . SER   B  1 739 ? 70.432 28.626  -22.449 1.00 43.16  ? 765  SER   B N    1 
ATOM   23331 C CA   . SER   B  1 739 ? 71.120 28.783  -23.719 1.00 41.03  ? 765  SER   B CA   1 
ATOM   23332 C C    . SER   B  1 739 ? 70.095 28.773  -24.886 1.00 38.24  ? 765  SER   B C    1 
ATOM   23333 O O    . SER   B  1 739 ? 70.442 29.226  -25.969 1.00 37.43  ? 765  SER   B O    1 
ATOM   23334 C CB   . SER   B  1 739 ? 72.169 27.693  -23.903 1.00 42.81  ? 765  SER   B CB   1 
ATOM   23335 O OG   . SER   B  1 739 ? 71.587 26.403  -23.967 1.00 45.57  ? 765  SER   B OG   1 
ATOM   23336 H H    . SER   B  1 739 ? 69.947 27.737  -22.375 0.00 57.80  ? 765  SER   B H    1 
ATOM   23337 H HA   . SER   B  1 739 ? 71.639 29.739  -23.757 0.00 56.03  ? 765  SER   B HA   1 
ATOM   23338 H HB2  . SER   B  1 739 ? 72.708 27.879  -24.830 0.00 57.29  ? 765  SER   B HB2  1 
ATOM   23339 H HB3  . SER   B  1 739 ? 72.860 27.724  -23.061 0.00 57.95  ? 765  SER   B HB3  1 
ATOM   23340 H HG   . SER   B  1 739 ? 72.293 25.716  -24.097 0.00 59.93  ? 765  SER   B HG   1 
ATOM   23341 N N    . MET   B  1 740 ? 68.842 28.278  -24.673 1.00 36.66  ? 766  MET   B N    1 
ATOM   23342 C CA   . MET   B  1 740 ? 67.795 28.265  -25.693 1.00 36.01  ? 766  MET   B CA   1 
ATOM   23343 C C    . MET   B  1 740 ? 66.421 28.492  -25.060 1.00 34.41  ? 766  MET   B C    1 
ATOM   23344 O O    . MET   B  1 740 ? 65.998 27.742  -24.180 1.00 33.80  ? 766  MET   B O    1 
ATOM   23345 C CB   . MET   B  1 740 ? 67.780 26.949  -26.480 1.00 37.52  ? 766  MET   B CB   1 
ATOM   23346 C CG   . MET   B  1 740 ? 66.758 26.955  -27.609 1.00 42.04  ? 766  MET   B CG   1 
ATOM   23347 S SD   . MET   B  1 740 ? 66.918 25.561  -28.727 1.00 54.41  ? 766  MET   B SD   1 
ATOM   23348 C CE   . MET   B  1 740 ? 68.358 26.084  -29.676 1.00 52.01  ? 766  MET   B CE   1 
ATOM   23349 H H    . MET   B  1 740 ? 68.530 27.859  -23.804 0.00 49.14  ? 766  MET   B H    1 
ATOM   23350 H HA   . MET   B  1 740 ? 67.987 29.065  -26.407 0.00 47.83  ? 766  MET   B HA   1 
ATOM   23351 H HB2  . MET   B  1 740 ? 68.767 26.790  -26.913 0.00 48.75  ? 766  MET   B HB2  1 
ATOM   23352 H HB3  . MET   B  1 740 ? 67.535 26.129  -25.806 0.00 48.56  ? 766  MET   B HB3  1 
ATOM   23353 H HG2  . MET   B  1 740 ? 65.753 26.900  -27.192 0.00 53.46  ? 766  MET   B HG2  1 
ATOM   23354 H HG3  . MET   B  1 740 ? 66.872 27.872  -28.185 0.00 53.77  ? 766  MET   B HG3  1 
ATOM   23355 H HE1  . MET   B  1 740 ? 68.454 25.441  -30.550 0.00 64.48  ? 766  MET   B HE1  1 
ATOM   23356 H HE2  . MET   B  1 740 ? 68.224 27.119  -29.989 0.00 65.19  ? 766  MET   B HE2  1 
ATOM   23357 H HE3  . MET   B  1 740 ? 69.245 25.995  -29.050 0.00 65.31  ? 766  MET   B HE3  1 
ATOM   23358 N N    . LEU   B  1 741 ? 65.721 29.520  -25.544 1.00 33.23  ? 767  LEU   B N    1 
ATOM   23359 C CA   . LEU   B  1 741 ? 64.390 29.903  -25.100 1.00 32.19  ? 767  LEU   B CA   1 
ATOM   23360 C C    . LEU   B  1 741 ? 63.526 30.008  -26.360 1.00 31.03  ? 767  LEU   B C    1 
ATOM   23361 O O    . LEU   B  1 741 ? 63.736 30.909  -27.171 1.00 31.06  ? 767  LEU   B O    1 
ATOM   23362 C CB   . LEU   B  1 741 ? 64.475 31.256  -24.376 1.00 31.97  ? 767  LEU   B CB   1 
ATOM   23363 C CG   . LEU   B  1 741 ? 63.155 31.892  -23.926 1.00 32.82  ? 767  LEU   B CG   1 
ATOM   23364 C CD1  . LEU   B  1 741 ? 62.448 31.028  -22.896 1.00 32.95  ? 767  LEU   B CD1  1 
ATOM   23365 C CD2  . LEU   B  1 741 ? 63.394 33.274  -23.361 1.00 33.01  ? 767  LEU   B CD2  1 
ATOM   23366 H H    . LEU   B  1 741 ? 66.061 30.134  -26.277 0.00 44.59  ? 767  LEU   B H    1 
ATOM   23367 H HA   . LEU   B  1 741 ? 63.965 29.159  -24.428 0.00 43.10  ? 767  LEU   B HA   1 
ATOM   23368 H HB2  . LEU   B  1 741 ? 65.083 31.120  -23.483 0.00 44.26  ? 767  LEU   B HB2  1 
ATOM   23369 H HB3  . LEU   B  1 741 ? 64.968 31.968  -25.036 0.00 44.10  ? 767  LEU   B HB3  1 
ATOM   23370 H HG   . LEU   B  1 741 ? 62.495 32.009  -24.783 0.00 44.79  ? 767  LEU   B HG   1 
ATOM   23371 H HD11 . LEU   B  1 741 ? 61.583 31.566  -22.512 0.00 45.36  ? 767  LEU   B HD11 1 
ATOM   23372 H HD12 . LEU   B  1 741 ? 62.119 30.104  -23.370 0.00 44.47  ? 767  LEU   B HD12 1 
ATOM   23373 H HD13 . LEU   B  1 741 ? 63.139 30.804  -22.085 0.00 45.43  ? 767  LEU   B HD13 1 
ATOM   23374 H HD21 . LEU   B  1 741 ? 62.446 33.696  -23.032 0.00 46.44  ? 767  LEU   B HD21 1 
ATOM   23375 H HD22 . LEU   B  1 741 ? 64.080 33.197  -22.520 0.00 46.66  ? 767  LEU   B HD22 1 
ATOM   23376 H HD23 . LEU   B  1 741 ? 63.828 33.902  -24.138 0.00 46.41  ? 767  LEU   B HD23 1 
ATOM   23377 N N    . GLU   B  1 742 ? 62.597 29.068  -26.552 1.00 29.84  ? 768  GLU   B N    1 
ATOM   23378 C CA   . GLU   B  1 742 ? 61.743 29.073  -27.739 1.00 29.10  ? 768  GLU   B CA   1 
ATOM   23379 C C    . GLU   B  1 742 ? 60.438 29.792  -27.410 1.00 28.19  ? 768  GLU   B C    1 
ATOM   23380 O O    . GLU   B  1 742 ? 59.849 29.533  -26.360 1.00 27.95  ? 768  GLU   B O    1 
ATOM   23381 C CB   . GLU   B  1 742 ? 61.475 27.650  -28.245 1.00 30.51  ? 768  GLU   B CB   1 
ATOM   23382 C CG   . GLU   B  1 742 ? 62.714 26.772  -28.308 1.00 34.67  ? 768  GLU   B CG   1 
ATOM   23383 C CD   . GLU   B  1 742 ? 62.460 25.463  -29.022 1.00 40.95  ? 768  GLU   B CD   1 
ATOM   23384 O OE1  . GLU   B  1 742 ? 62.086 25.510  -30.215 1.00 43.08  ? 768  GLU   B OE1  1 
ATOM   23385 O OE2  . GLU   B  1 742 ? 62.619 24.394  -28.391 1.00 42.48  ? 768  GLU   B OE2  1 
ATOM   23386 H H    . GLU   B  1 742 ? 62.407 28.304  -25.911 0.00 39.17  ? 768  GLU   B H    1 
ATOM   23387 H HA   . GLU   B  1 742 ? 62.237 29.601  -28.553 0.00 38.02  ? 768  GLU   B HA   1 
ATOM   23388 H HB2  . GLU   B  1 742 ? 60.739 27.169  -27.604 0.00 38.77  ? 768  GLU   B HB2  1 
ATOM   23389 H HB3  . GLU   B  1 742 ? 61.074 27.727  -29.255 0.00 38.58  ? 768  GLU   B HB3  1 
ATOM   23390 H HG2  . GLU   B  1 742 ? 63.501 27.302  -28.841 0.00 43.86  ? 768  GLU   B HG2  1 
ATOM   23391 H HG3  . GLU   B  1 742 ? 63.040 26.536  -27.296 0.00 43.94  ? 768  GLU   B HG3  1 
ATOM   23392 N N    . LEU   B  1 743 ? 60.031 30.737  -28.275 1.00 27.62  ? 769  LEU   B N    1 
ATOM   23393 C CA   . LEU   B  1 743 ? 58.834 31.551  -28.067 1.00 27.99  ? 769  LEU   B CA   1 
ATOM   23394 C C    . LEU   B  1 743 ? 57.994 31.757  -29.324 1.00 27.95  ? 769  LEU   B C    1 
ATOM   23395 O O    . LEU   B  1 743 ? 57.000 32.487  -29.248 1.00 28.62  ? 769  LEU   B O    1 
ATOM   23396 C CB   . LEU   B  1 743 ? 59.237 32.923  -27.489 1.00 28.35  ? 769  LEU   B CB   1 
ATOM   23397 C CG   . LEU   B  1 743 ? 59.882 32.906  -26.100 1.00 30.57  ? 769  LEU   B CG   1 
ATOM   23398 C CD1  . LEU   B  1 743 ? 60.666 34.178  -25.864 1.00 31.24  ? 769  LEU   B CD1  1 
ATOM   23399 C CD2  . LEU   B  1 743 ? 58.840 32.736  -25.005 1.00 31.17  ? 769  LEU   B CD2  1 
ATOM   23400 H H    . LEU   B  1 743 ? 60.534 30.977  -29.124 0.00 36.46  ? 769  LEU   B H    1 
ATOM   23401 H HA   . LEU   B  1 743 ? 58.181 31.065  -27.344 0.00 37.19  ? 769  LEU   B HA   1 
ATOM   23402 H HB2  . LEU   B  1 743 ? 59.951 33.381  -28.172 0.00 38.69  ? 769  LEU   B HB2  1 
ATOM   23403 H HB3  . LEU   B  1 743 ? 58.354 33.555  -27.414 0.00 38.82  ? 769  LEU   B HB3  1 
ATOM   23404 H HG   . LEU   B  1 743 ? 60.575 32.070  -26.031 0.00 41.41  ? 769  LEU   B HG   1 
ATOM   23405 H HD11 . LEU   B  1 743 ? 61.053 34.173  -24.846 0.00 43.70  ? 769  LEU   B HD11 1 
ATOM   23406 H HD12 . LEU   B  1 743 ? 61.492 34.223  -26.572 0.00 43.24  ? 769  LEU   B HD12 1 
ATOM   23407 H HD13 . LEU   B  1 743 ? 60.006 35.032  -26.007 0.00 43.64  ? 769  LEU   B HD13 1 
ATOM   23408 H HD21 . LEU   B  1 743 ? 59.341 32.739  -24.038 0.00 42.94  ? 769  LEU   B HD21 1 
ATOM   23409 H HD22 . LEU   B  1 743 ? 58.130 33.560  -25.056 0.00 42.89  ? 769  LEU   B HD22 1 
ATOM   23410 H HD23 . LEU   B  1 743 ? 58.320 31.789  -25.145 0.00 42.01  ? 769  LEU   B HD23 1 
ATOM   23411 N N    . HIS   B  1 744 ? 58.327 31.109  -30.464 1.00 26.86  ? 770  HIS   B N    1 
ATOM   23412 C CA   . HIS   B  1 744 ? 57.505 31.259  -31.665 1.00 26.93  ? 770  HIS   B CA   1 
ATOM   23413 C C    . HIS   B  1 744 ? 56.055 30.779  -31.420 1.00 26.94  ? 770  HIS   B C    1 
ATOM   23414 O O    . HIS   B  1 744 ? 55.837 29.884  -30.621 1.00 26.98  ? 770  HIS   B O    1 
ATOM   23415 C CB   . HIS   B  1 744 ? 58.144 30.528  -32.863 1.00 27.07  ? 770  HIS   B CB   1 
ATOM   23416 C CG   . HIS   B  1 744 ? 58.020 29.035  -32.829 1.00 29.41  ? 770  HIS   B CG   1 
ATOM   23417 N ND1  . HIS   B  1 744 ? 59.043 28.239  -32.351 1.00 30.90  ? 770  HIS   B ND1  1 
ATOM   23418 C CD2  . HIS   B  1 744 ? 56.998 28.239  -33.226 1.00 30.86  ? 770  HIS   B CD2  1 
ATOM   23419 C CE1  . HIS   B  1 744 ? 58.623 26.992  -32.485 1.00 31.42  ? 770  HIS   B CE1  1 
ATOM   23420 N NE2  . HIS   B  1 744 ? 57.395 26.944  -33.003 1.00 32.00  ? 770  HIS   B NE2  1 
ATOM   23421 H H    . HIS   B  1 744 ? 59.124 30.492  -30.581 0.00 34.81  ? 770  HIS   B H    1 
ATOM   23422 H HA   . HIS   B  1 744 ? 57.459 32.317  -31.919 0.00 35.29  ? 770  HIS   B HA   1 
ATOM   23423 H HB2  . HIS   B  1 744 ? 57.660 30.876  -33.774 0.00 34.41  ? 770  HIS   B HB2  1 
ATOM   23424 H HB3  . HIS   B  1 744 ? 59.205 30.772  -32.899 0.00 34.67  ? 770  HIS   B HB3  1 
ATOM   23425 H HD2  . HIS   B  1 744 ? 56.056 28.561  -33.637 0.00 37.90  ? 770  HIS   B HD2  1 
ATOM   23426 H HE1  . HIS   B  1 744 ? 59.201 26.125  -32.211 0.00 38.16  ? 770  HIS   B HE1  1 
ATOM   23427 H HE2  . HIS   B  1 744 ? 56.854 26.107  -33.195 0.00 38.44  ? 770  HIS   B HE2  1 
ATOM   23428 N N    . GLY   B  1 745 ? 55.083 31.426  -32.042 1.00 27.39  ? 771  GLY   B N    1 
ATOM   23429 C CA   . GLY   B  1 745 ? 53.682 31.036  -31.919 1.00 27.97  ? 771  GLY   B CA   1 
ATOM   23430 C C    . GLY   B  1 745 ? 52.907 31.564  -30.728 1.00 28.47  ? 771  GLY   B C    1 
ATOM   23431 O O    . GLY   B  1 745 ? 51.778 31.134  -30.517 1.00 29.57  ? 771  GLY   B O    1 
ATOM   23432 H H    . GLY   B  1 745 ? 55.228 32.232  -32.642 0.00 35.53  ? 771  GLY   B H    1 
ATOM   23433 H HA2  . GLY   B  1 745 ? 53.163 31.384  -32.811 0.00 35.74  ? 771  GLY   B HA2  1 
ATOM   23434 H HA3  . GLY   B  1 745 ? 53.608 29.950  -31.910 0.00 35.30  ? 771  GLY   B HA3  1 
ATOM   23435 N N    . ASN   B  1 746 ? 53.464 32.494  -29.949 1.00 27.93  ? 772  ASN   B N    1 
ATOM   23436 C CA   . ASN   B  1 746 ? 52.744 33.107  -28.828 1.00 28.39  ? 772  ASN   B CA   1 
ATOM   23437 C C    . ASN   B  1 746 ? 52.085 34.414  -29.303 1.00 29.08  ? 772  ASN   B C    1 
ATOM   23438 O O    . ASN   B  1 746 ? 52.684 35.158  -30.078 1.00 29.11  ? 772  ASN   B O    1 
ATOM   23439 C CB   . ASN   B  1 746 ? 53.681 33.396  -27.650 1.00 28.72  ? 772  ASN   B CB   1 
ATOM   23440 C CG   . ASN   B  1 746 ? 54.005 32.165  -26.843 1.00 29.13  ? 772  ASN   B CG   1 
ATOM   23441 O OD1  . ASN   B  1 746 ? 53.197 31.736  -26.013 1.00 28.61  ? 772  ASN   B OD1  1 
ATOM   23442 N ND2  . ASN   B  1 746 ? 55.165 31.549  -27.087 1.00 28.52  ? 772  ASN   B ND2  1 
ATOM   23443 H H    . ASN   B  1 746 ? 54.409 32.842  -30.064 0.00 37.02  ? 772  ASN   B H    1 
ATOM   23444 H HA   . ASN   B  1 746 ? 51.972 32.420  -28.484 0.00 37.71  ? 772  ASN   B HA   1 
ATOM   23445 H HB2  . ASN   B  1 746 ? 54.609 33.832  -28.017 0.00 38.99  ? 772  ASN   B HB2  1 
ATOM   23446 H HB3  . ASN   B  1 746 ? 53.189 34.105  -26.986 0.00 39.35  ? 772  ASN   B HB3  1 
ATOM   23447 H HD21 . ASN   B  1 746 ? 55.413 30.719  -26.557 0.00 37.67  ? 772  ASN   B HD21 1 
ATOM   23448 H HD22 . ASN   B  1 746 ? 55.800 31.901  -27.796 0.00 37.90  ? 772  ASN   B HD22 1 
ATOM   23449 N N    . PRO   B  1 747 ? 50.852 34.711  -28.861 1.00 29.70  ? 773  PRO   B N    1 
ATOM   23450 C CA   . PRO   B  1 747 ? 50.177 35.931  -29.326 1.00 30.22  ? 773  PRO   B CA   1 
ATOM   23451 C C    . PRO   B  1 747 ? 50.664 37.197  -28.591 1.00 30.90  ? 773  PRO   B C    1 
ATOM   23452 O O    . PRO   B  1 747 ? 49.959 37.740  -27.744 1.00 30.40  ? 773  PRO   B O    1 
ATOM   23453 C CB   . PRO   B  1 747 ? 48.707 35.609  -29.041 1.00 30.87  ? 773  PRO   B CB   1 
ATOM   23454 C CG   . PRO   B  1 747 ? 48.761 34.808  -27.784 1.00 31.14  ? 773  PRO   B CG   1 
ATOM   23455 C CD   . PRO   B  1 747 ? 49.987 33.940  -27.942 1.00 29.48  ? 773  PRO   B CD   1 
ATOM   23456 H HA   . PRO   B  1 747 ? 50.302 36.065  -30.400 0.00 41.37  ? 773  PRO   B HA   1 
ATOM   23457 H HB2  . PRO   B  1 747 ? 48.112 36.513  -28.927 0.00 42.84  ? 773  PRO   B HB2  1 
ATOM   23458 H HB3  . PRO   B  1 747 ? 48.313 34.999  -29.853 0.00 41.79  ? 773  PRO   B HB3  1 
ATOM   23459 H HG2  . PRO   B  1 747 ? 48.863 35.474  -26.929 0.00 43.04  ? 773  PRO   B HG2  1 
ATOM   23460 H HG3  . PRO   B  1 747 ? 47.863 34.197  -27.696 0.00 42.21  ? 773  PRO   B HG3  1 
ATOM   23461 H HD2  . PRO   B  1 747 ? 50.489 33.815  -26.983 0.00 40.11  ? 773  PRO   B HD2  1 
ATOM   23462 H HD3  . PRO   B  1 747 ? 49.716 32.981  -28.382 0.00 39.35  ? 773  PRO   B HD3  1 
ATOM   23463 N N    . PHE   B  1 748 ? 51.871 37.675  -28.925 1.00 31.57  ? 774  PHE   B N    1 
ATOM   23464 C CA   . PHE   B  1 748 ? 52.469 38.820  -28.234 1.00 32.54  ? 774  PHE   B CA   1 
ATOM   23465 C C    . PHE   B  1 748 ? 51.773 40.136  -28.480 1.00 34.00  ? 774  PHE   B C    1 
ATOM   23466 O O    . PHE   B  1 748 ? 51.328 40.419  -29.594 1.00 34.18  ? 774  PHE   B O    1 
ATOM   23467 C CB   . PHE   B  1 748 ? 53.962 38.976  -28.591 1.00 32.39  ? 774  PHE   B CB   1 
ATOM   23468 C CG   . PHE   B  1 748 ? 54.863 37.979  -27.905 1.00 32.94  ? 774  PHE   B CG   1 
ATOM   23469 C CD1  . PHE   B  1 748 ? 55.185 38.118  -26.567 1.00 34.04  ? 774  PHE   B CD1  1 
ATOM   23470 C CD2  . PHE   B  1 748 ? 55.336 36.870  -28.581 1.00 33.39  ? 774  PHE   B CD2  1 
ATOM   23471 C CE1  . PHE   B  1 748 ? 55.984 37.180  -25.925 1.00 34.76  ? 774  PHE   B CE1  1 
ATOM   23472 C CE2  . PHE   B  1 748 ? 56.166 35.956  -27.945 1.00 34.12  ? 774  PHE   B CE2  1 
ATOM   23473 C CZ   . PHE   B  1 748 ? 56.462 36.102  -26.618 1.00 34.11  ? 774  PHE   B CZ   1 
ATOM   23474 H H    . PHE   B  1 748 ? 52.447 37.284  -29.663 0.00 43.79  ? 774  PHE   B H    1 
ATOM   23475 H HA   . PHE   B  1 748 ? 52.397 38.615  -27.167 0.00 46.38  ? 774  PHE   B HA   1 
ATOM   23476 H HB2  . PHE   B  1 748 ? 54.091 38.874  -29.667 0.00 45.72  ? 774  PHE   B HB2  1 
ATOM   23477 H HB3  . PHE   B  1 748 ? 54.283 39.970  -28.282 0.00 46.74  ? 774  PHE   B HB3  1 
ATOM   23478 H HD1  . PHE   B  1 748 ? 54.806 38.961  -26.014 0.00 48.78  ? 774  PHE   B HD1  1 
ATOM   23479 H HD2  . PHE   B  1 748 ? 55.101 36.737  -29.623 0.00 45.73  ? 774  PHE   B HD2  1 
ATOM   23480 H HE1  . PHE   B  1 748 ? 56.239 37.309  -24.887 0.00 49.11  ? 774  PHE   B HE1  1 
ATOM   23481 H HE2  . PHE   B  1 748 ? 56.526 35.095  -28.482 0.00 46.10  ? 774  PHE   B HE2  1 
ATOM   23482 H HZ   . PHE   B  1 748 ? 57.096 35.384  -26.126 0.00 46.95  ? 774  PHE   B HZ   1 
ATOM   23483 N N    . GLU   B  1 749 ? 51.704 40.953  -27.420 1.00 34.66  ? 775  GLU   B N    1 
ATOM   23484 C CA   . GLU   B  1 749 ? 51.132 42.283  -27.449 1.00 35.85  ? 775  GLU   B CA   1 
ATOM   23485 C C    . GLU   B  1 749 ? 52.322 43.215  -27.692 1.00 36.80  ? 775  GLU   B C    1 
ATOM   23486 O O    . GLU   B  1 749 ? 53.214 43.301  -26.843 1.00 37.16  ? 775  GLU   B O    1 
ATOM   23487 C CB   . GLU   B  1 749 ? 50.449 42.605  -26.108 1.00 38.97  ? 775  GLU   B CB   1 
ATOM   23488 C CG   . GLU   B  1 749 ? 49.653 43.905  -26.145 1.00 46.20  ? 775  GLU   B CG   1 
ATOM   23489 C CD   . GLU   B  1 749 ? 48.596 44.074  -25.067 1.00 56.11  ? 775  GLU   B CD   1 
ATOM   23490 O OE1  . GLU   B  1 749 ? 48.119 45.219  -24.891 1.00 58.80  ? 775  GLU   B OE1  1 
ATOM   23491 O OE2  . GLU   B  1 749 ? 48.233 43.072  -24.408 1.00 59.65  ? 775  GLU   B OE2  1 
ATOM   23492 H H    . GLU   B  1 749 ? 52.056 40.715  -26.498 0.00 50.38  ? 775  GLU   B H    1 
ATOM   23493 H HA   . GLU   B  1 749 ? 50.404 42.372  -28.255 0.00 52.42  ? 775  GLU   B HA   1 
ATOM   23494 H HB2  . GLU   B  1 749 ? 49.777 41.784  -25.865 0.00 56.46  ? 775  GLU   B HB2  1 
ATOM   23495 H HB3  . GLU   B  1 749 ? 51.202 42.698  -25.326 0.00 57.20  ? 775  GLU   B HB3  1 
ATOM   23496 H HG2  . GLU   B  1 749 ? 50.352 44.734  -26.045 0.00 67.03  ? 775  GLU   B HG2  1 
ATOM   23497 H HG3  . GLU   B  1 749 ? 49.144 43.974  -27.104 0.00 66.24  ? 775  GLU   B HG3  1 
ATOM   23498 N N    . CYS   B  1 750 ? 52.378 43.848  -28.872 1.00 37.00  ? 776  CYS   B N    1 
ATOM   23499 C CA   . CYS   B  1 750 ? 53.488 44.711  -29.251 1.00 38.41  ? 776  CYS   B CA   1 
ATOM   23500 C C    . CYS   B  1 750 ? 53.194 46.178  -29.052 1.00 40.02  ? 776  CYS   B C    1 
ATOM   23501 O O    . CYS   B  1 750 ? 52.995 46.937  -29.997 1.00 40.29  ? 776  CYS   B O    1 
ATOM   23502 C CB   . CYS   B  1 750 ? 53.942 44.409  -30.672 1.00 38.88  ? 776  CYS   B CB   1 
ATOM   23503 S SG   . CYS   B  1 750 ? 54.633 42.745  -30.865 1.00 41.01  ? 776  CYS   B SG   1 
ATOM   23504 H H    . CYS   B  1 750 ? 51.661 43.779  -29.588 0.00 54.36  ? 776  CYS   B H    1 
ATOM   23505 H HA   . CYS   B  1 750 ? 54.346 44.487  -28.619 0.00 56.79  ? 776  CYS   B HA   1 
ATOM   23506 H HB2  . CYS   B  1 750 ? 53.090 44.500  -31.344 0.00 56.66  ? 776  CYS   B HB2  1 
ATOM   23507 H HB3  . CYS   B  1 750 ? 54.715 45.121  -30.955 0.00 57.19  ? 776  CYS   B HB3  1 
ATOM   23508 N N    . THR   B  1 751 ? 53.149 46.550  -27.788 1.00 41.09  ? 777  THR   B N    1 
ATOM   23509 C CA   . THR   B  1 751 ? 53.017 47.920  -27.304 1.00 42.62  ? 777  THR   B CA   1 
ATOM   23510 C C    . THR   B  1 751 ? 54.353 48.196  -26.542 1.00 43.33  ? 777  THR   B C    1 
ATOM   23511 O O    . THR   B  1 751 ? 55.242 47.333  -26.533 1.00 43.05  ? 777  THR   B O    1 
ATOM   23512 C CB   . THR   B  1 751 ? 51.772 48.017  -26.396 1.00 44.41  ? 777  THR   B CB   1 
ATOM   23513 O OG1  . THR   B  1 751 ? 51.958 47.139  -25.281 1.00 45.94  ? 777  THR   B OG1  1 
ATOM   23514 C CG2  . THR   B  1 751 ? 50.480 47.667  -27.126 1.00 44.99  ? 777  THR   B CG2  1 
ATOM   23515 H H    . THR   B  1 751 ? 53.203 45.884  -27.024 0.00 61.42  ? 777  THR   B H    1 
ATOM   23516 H HA   . THR   B  1 751 ? 52.917 48.629  -28.124 0.00 64.94  ? 777  THR   B HA   1 
ATOM   23517 H HB   . THR   B  1 751 ? 51.681 49.039  -26.030 0.00 68.02  ? 777  THR   B HB   1 
ATOM   23518 H HG1  . THR   B  1 751 ? 51.164 47.172  -24.686 0.00 68.87  ? 777  THR   B HG1  1 
ATOM   23519 H HG21 . THR   B  1 751 ? 49.627 47.841  -26.471 0.00 67.72  ? 777  THR   B HG21 1 
ATOM   23520 H HG22 . THR   B  1 751 ? 50.377 48.286  -28.016 0.00 67.62  ? 777  THR   B HG22 1 
ATOM   23521 H HG23 . THR   B  1 751 ? 50.484 46.619  -27.421 0.00 66.53  ? 777  THR   B HG23 1 
ATOM   23522 N N    . CYS   B  1 752 ? 54.505 49.370  -25.903 1.00 43.59  ? 778  CYS   B N    1 
ATOM   23523 C CA   . CYS   B  1 752 ? 55.704 49.646  -25.110 1.00 43.96  ? 778  CYS   B CA   1 
ATOM   23524 C C    . CYS   B  1 752 ? 55.866 48.645  -23.928 1.00 43.28  ? 778  CYS   B C    1 
ATOM   23525 O O    . CYS   B  1 752 ? 56.965 48.527  -23.391 1.00 43.35  ? 778  CYS   B O    1 
ATOM   23526 C CB   . CYS   B  1 752 ? 55.712 51.099  -24.650 1.00 45.41  ? 778  CYS   B CB   1 
ATOM   23527 S SG   . CYS   B  1 752 ? 55.797 52.281  -26.023 1.00 51.31  ? 778  CYS   B SG   1 
ATOM   23528 H H    . CYS   B  1 752 ? 53.828 50.126  -25.917 0.00 67.92  ? 778  CYS   B H    1 
ATOM   23529 H HA   . CYS   B  1 752 ? 56.572 49.518  -25.754 0.00 68.08  ? 778  CYS   B HA   1 
ATOM   23530 H HB2  . CYS   B  1 752 ? 54.800 51.298  -24.088 0.00 71.67  ? 778  CYS   B HB2  1 
ATOM   23531 H HB3  . CYS   B  1 752 ? 56.583 51.265  -24.017 0.00 71.77  ? 778  CYS   B HB3  1 
ATOM   23532 H HG   . CYS   B  1 752 ? 55.779 53.525  -25.530 0.00 80.14  ? 778  CYS   B HG   1 
ATOM   23533 N N    . ASP   B  1 753 ? 54.816 47.853  -23.601 1.00 42.64  ? 779  ASP   B N    1 
ATOM   23534 C CA   . ASP   B  1 753 ? 54.877 46.824  -22.556 1.00 42.45  ? 779  ASP   B CA   1 
ATOM   23535 C C    . ASP   B  1 753 ? 55.848 45.681  -22.926 1.00 41.47  ? 779  ASP   B C    1 
ATOM   23536 O O    . ASP   B  1 753 ? 56.297 44.973  -22.027 1.00 41.27  ? 779  ASP   B O    1 
ATOM   23537 C CB   . ASP   B  1 753 ? 53.478 46.244  -22.285 1.00 44.53  ? 779  ASP   B CB   1 
ATOM   23538 C CG   . ASP   B  1 753 ? 52.480 47.245  -21.735 1.00 50.41  ? 779  ASP   B CG   1 
ATOM   23539 O OD1  . ASP   B  1 753 ? 51.275 47.101  -22.030 1.00 52.10  ? 779  ASP   B OD1  1 
ATOM   23540 O OD2  . ASP   B  1 753 ? 52.905 48.176  -21.015 1.00 52.65  ? 779  ASP   B OD2  1 
ATOM   23541 H H    . ASP   B  1 753 ? 53.908 47.898  -24.050 0.00 65.71  ? 779  ASP   B H    1 
ATOM   23542 H HA   . ASP   B  1 753 ? 55.250 47.273  -21.637 0.00 65.94  ? 779  ASP   B HA   1 
ATOM   23543 H HB2  . ASP   B  1 753 ? 53.078 45.839  -23.214 0.00 66.76  ? 779  ASP   B HB2  1 
ATOM   23544 H HB3  . ASP   B  1 753 ? 53.573 45.441  -21.554 0.00 67.07  ? 779  ASP   B HB3  1 
ATOM   23545 N N    . ILE   B  1 754 ? 56.156 45.493  -24.233 1.00 40.67  ? 780  ILE   B N    1 
ATOM   23546 C CA   . ILE   B  1 754 ? 57.136 44.495  -24.690 1.00 40.43  ? 780  ILE   B CA   1 
ATOM   23547 C C    . ILE   B  1 754 ? 58.598 45.030  -24.613 1.00 40.03  ? 780  ILE   B C    1 
ATOM   23548 O O    . ILE   B  1 754 ? 59.515 44.287  -24.949 1.00 39.52  ? 780  ILE   B O    1 
ATOM   23549 C CB   . ILE   B  1 754 ? 56.804 43.991  -26.135 1.00 40.82  ? 780  ILE   B CB   1 
ATOM   23550 C CG1  . ILE   B  1 754 ? 57.433 42.596  -26.431 1.00 41.75  ? 780  ILE   B CG1  1 
ATOM   23551 C CG2  . ILE   B  1 754 ? 57.264 45.003  -27.194 1.00 41.15  ? 780  ILE   B CG2  1 
ATOM   23552 C CD1  . ILE   B  1 754 ? 56.788 41.433  -25.705 1.00 42.98  ? 780  ILE   B CD1  1 
ATOM   23553 H H    . ILE   B  1 754 ? 55.734 46.004  -25.001 0.00 61.71  ? 780  ILE   B H    1 
ATOM   23554 H HA   . ILE   B  1 754 ? 57.079 43.641  -24.016 0.00 60.21  ? 780  ILE   B HA   1 
ATOM   23555 H HB   . ILE   B  1 754 ? 55.726 43.874  -26.241 0.00 60.03  ? 780  ILE   B HB   1 
ATOM   23556 H HG12 . ILE   B  1 754 ? 57.346 42.401  -27.499 0.00 59.88  ? 780  ILE   B HG12 1 
ATOM   23557 H HG13 . ILE   B  1 754 ? 58.485 42.613  -26.151 0.00 60.51  ? 780  ILE   B HG13 1 
ATOM   23558 H HG21 . ILE   B  1 754 ? 56.720 44.807  -28.117 0.00 60.52  ? 780  ILE   B HG21 1 
ATOM   23559 H HG22 . ILE   B  1 754 ? 57.050 46.013  -26.848 0.00 61.77  ? 780  ILE   B HG22 1 
ATOM   23560 H HG23 . ILE   B  1 754 ? 58.331 44.883  -27.378 0.00 60.91  ? 780  ILE   B HG23 1 
ATOM   23561 H HD11 . ILE   B  1 754 ? 57.106 40.507  -26.180 0.00 60.53  ? 780  ILE   B HD11 1 
ATOM   23562 H HD12 . ILE   B  1 754 ? 57.104 41.430  -24.663 0.00 61.59  ? 780  ILE   B HD12 1 
ATOM   23563 H HD13 . ILE   B  1 754 ? 55.705 41.531  -25.767 0.00 61.17  ? 780  ILE   B HD13 1 
ATOM   23564 N N    . GLY   B  1 755 ? 58.792 46.303  -24.235 1.00 39.92  ? 781  GLY   B N    1 
ATOM   23565 C CA   . GLY   B  1 755 ? 60.100 46.932  -24.145 1.00 40.40  ? 781  GLY   B CA   1 
ATOM   23566 C C    . GLY   B  1 755 ? 61.053 46.265  -23.179 1.00 40.67  ? 781  GLY   B C    1 
ATOM   23567 O O    . GLY   B  1 755 ? 62.221 46.073  -23.514 1.00 40.95  ? 781  GLY   B O    1 
ATOM   23568 H H    . GLY   B  1 755 ? 58.049 46.956  -24.013 0.00 62.00  ? 781  GLY   B H    1 
ATOM   23569 H HA2  . GLY   B  1 755 ? 60.559 46.924  -25.133 0.00 62.41  ? 781  GLY   B HA2  1 
ATOM   23570 H HA3  . GLY   B  1 755 ? 59.977 47.969  -23.835 0.00 63.58  ? 781  GLY   B HA3  1 
ATOM   23571 N N    . ASP   B  1 756 ? 60.572 45.889  -21.987 1.00 40.42  ? 782  ASP   B N    1 
ATOM   23572 C CA   . ASP   B  1 756 ? 61.423 45.227  -20.996 1.00 40.44  ? 782  ASP   B CA   1 
ATOM   23573 C C    . ASP   B  1 756 ? 61.988 43.906  -21.529 1.00 38.73  ? 782  ASP   B C    1 
ATOM   23574 O O    . ASP   B  1 756 ? 63.184 43.652  -21.377 1.00 39.08  ? 782  ASP   B O    1 
ATOM   23575 C CB   . ASP   B  1 756 ? 60.660 44.990  -19.684 1.00 43.24  ? 782  ASP   B CB   1 
ATOM   23576 C CG   . ASP   B  1 756 ? 60.343 46.255  -18.920 1.00 50.27  ? 782  ASP   B CG   1 
ATOM   23577 O OD1  . ASP   B  1 756 ? 61.254 47.103  -18.768 1.00 51.10  ? 782  ASP   B OD1  1 
ATOM   23578 O OD2  . ASP   B  1 756 ? 59.190 46.392  -18.456 1.00 53.88  ? 782  ASP   B OD2  1 
ATOM   23579 H H    . ASP   B  1 756 ? 59.611 46.024  -21.690 0.00 62.96  ? 782  ASP   B H    1 
ATOM   23580 H HA   . ASP   B  1 756 ? 62.267 45.882  -20.785 0.00 63.62  ? 782  ASP   B HA   1 
ATOM   23581 H HB2  . ASP   B  1 756 ? 59.718 44.489  -19.906 0.00 66.00  ? 782  ASP   B HB2  1 
ATOM   23582 H HB3  . ASP   B  1 756 ? 61.272 44.360  -19.040 0.00 66.48  ? 782  ASP   B HB3  1 
ATOM   23583 N N    . PHE   B  1 757 ? 61.150 43.104  -22.195 1.00 37.01  ? 783  PHE   B N    1 
ATOM   23584 C CA   . PHE   B  1 757 ? 61.607 41.840  -22.765 1.00 35.81  ? 783  PHE   B CA   1 
ATOM   23585 C C    . PHE   B  1 757 ? 62.568 42.091  -23.921 1.00 35.77  ? 783  PHE   B C    1 
ATOM   23586 O O    . PHE   B  1 757 ? 63.570 41.392  -24.029 1.00 35.30  ? 783  PHE   B O    1 
ATOM   23587 C CB   . PHE   B  1 757 ? 60.431 40.969  -23.213 1.00 34.62  ? 783  PHE   B CB   1 
ATOM   23588 C CG   . PHE   B  1 757 ? 60.890 39.642  -23.773 1.00 33.78  ? 783  PHE   B CG   1 
ATOM   23589 C CD1  . PHE   B  1 757 ? 61.705 38.802  -23.029 1.00 34.05  ? 783  PHE   B CD1  1 
ATOM   23590 C CD2  . PHE   B  1 757 ? 60.556 39.261  -25.059 1.00 33.91  ? 783  PHE   B CD2  1 
ATOM   23591 C CE1  . PHE   B  1 757 ? 62.173 37.608  -23.563 1.00 34.45  ? 783  PHE   B CE1  1 
ATOM   23592 C CE2  . PHE   B  1 757 ? 60.988 38.043  -25.571 1.00 34.28  ? 783  PHE   B CE2  1 
ATOM   23593 C CZ   . PHE   B  1 757 ? 61.823 37.245  -24.834 1.00 33.91  ? 783  PHE   B CZ   1 
ATOM   23594 H H    . PHE   B  1 757 ? 60.164 43.291  -22.347 0.00 56.78  ? 783  PHE   B H    1 
ATOM   23595 H HA   . PHE   B  1 757 ? 62.150 41.297  -21.993 0.00 54.49  ? 783  PHE   B HA   1 
ATOM   23596 H HB2  . PHE   B  1 757 ? 59.788 40.771  -22.357 0.00 52.24  ? 783  PHE   B HB2  1 
ATOM   23597 H HB3  . PHE   B  1 757 ? 59.872 41.498  -23.984 0.00 52.12  ? 783  PHE   B HB3  1 
ATOM   23598 H HD1  . PHE   B  1 757 ? 62.015 39.096  -22.043 0.00 50.98  ? 783  PHE   B HD1  1 
ATOM   23599 H HD2  . PHE   B  1 757 ? 59.918 39.888  -25.658 0.00 49.70  ? 783  PHE   B HD2  1 
ATOM   23600 H HE1  . PHE   B  1 757 ? 62.803 36.964  -22.973 0.00 50.00  ? 783  PHE   B HE1  1 
ATOM   23601 H HE2  . PHE   B  1 757 ? 60.717 37.755  -26.573 0.00 48.70  ? 783  PHE   B HE2  1 
ATOM   23602 H HZ   . PHE   B  1 757 ? 62.155 36.302  -25.234 0.00 48.09  ? 783  PHE   B HZ   1 
ATOM   23603 N N    . ARG   B  1 758 ? 62.300 43.107  -24.755 1.00 36.38  ? 784  ARG   B N    1 
ATOM   23604 C CA   . ARG   B  1 758 ? 63.210 43.463  -25.853 1.00 37.84  ? 784  ARG   B CA   1 
ATOM   23605 C C    . ARG   B  1 758 ? 64.584 43.892  -25.303 1.00 39.41  ? 784  ARG   B C    1 
ATOM   23606 O O    . ARG   B  1 758 ? 65.596 43.494  -25.867 1.00 40.06  ? 784  ARG   B O    1 
ATOM   23607 C CB   . ARG   B  1 758 ? 62.616 44.587  -26.726 1.00 38.97  ? 784  ARG   B CB   1 
ATOM   23608 C CG   . ARG   B  1 758 ? 61.542 44.111  -27.716 1.00 41.22  ? 784  ARG   B CG   1 
ATOM   23609 C CD   . ARG   B  1 758 ? 62.120 43.590  -29.029 1.00 43.06  ? 784  ARG   B CD   1 
ATOM   23610 N NE   . ARG   B  1 758 ? 62.931 44.593  -29.734 1.00 44.81  ? 784  ARG   B NE   1 
ATOM   23611 C CZ   . ARG   B  1 758 ? 62.446 45.634  -30.411 1.00 46.60  ? 784  ARG   B CZ   1 
ATOM   23612 N NH1  . ARG   B  1 758 ? 61.133 45.829  -30.498 1.00 45.80  ? 784  ARG   B NH1  1 
ATOM   23613 N NH2  . ARG   B  1 758 ? 63.270 46.491  -31.002 1.00 47.29  ? 784  ARG   B NH2  1 
ATOM   23614 H H    . ARG   B  1 758 ? 61.462 43.677  -24.713 0.00 55.61  ? 784  ARG   B H    1 
ATOM   23615 H HA   . ARG   B  1 758 ? 63.368 42.584  -26.476 0.00 56.32  ? 784  ARG   B HA   1 
ATOM   23616 H HB2  . ARG   B  1 758 ? 62.164 45.339  -26.082 0.00 59.49  ? 784  ARG   B HB2  1 
ATOM   23617 H HB3  . ARG   B  1 758 ? 63.430 45.045  -27.286 0.00 59.07  ? 784  ARG   B HB3  1 
ATOM   23618 H HG2  . ARG   B  1 758 ? 60.974 43.303  -27.257 0.00 60.29  ? 784  ARG   B HG2  1 
ATOM   23619 H HG3  . ARG   B  1 758 ? 60.881 44.945  -27.947 0.00 61.17  ? 784  ARG   B HG3  1 
ATOM   23620 H HD2  . ARG   B  1 758 ? 62.767 42.742  -28.808 0.00 61.87  ? 784  ARG   B HD2  1 
ATOM   23621 H HD3  . ARG   B  1 758 ? 61.310 43.268  -29.682 0.00 61.76  ? 784  ARG   B HD3  1 
ATOM   23622 H HE   . ARG   B  1 758 ? 63.939 44.483  -29.690 0.00 65.00  ? 784  ARG   B HE   1 
ATOM   23623 H HH11 . ARG   B  1 758 ? 60.466 45.207  -30.056 0.00 66.15  ? 784  ARG   B HH11 1 
ATOM   23624 H HH12 . ARG   B  1 758 ? 60.781 46.628  -31.016 0.00 66.89  ? 784  ARG   B HH12 1 
ATOM   23625 H HH21 . ARG   B  1 758 ? 64.275 46.354  -30.949 0.00 68.94  ? 784  ARG   B HH21 1 
ATOM   23626 H HH22 . ARG   B  1 758 ? 62.902 47.281  -31.522 0.00 69.24  ? 784  ARG   B HH22 1 
ATOM   23627 N N    . ARG   B  1 759 ? 64.627 44.649  -24.190 1.00 39.92  ? 785  ARG   B N    1 
ATOM   23628 C CA   . ARG   B  1 759 ? 65.892 45.058  -23.576 1.00 41.08  ? 785  ARG   B CA   1 
ATOM   23629 C C    . ARG   B  1 759 ? 66.610 43.844  -22.982 1.00 41.92  ? 785  ARG   B C    1 
ATOM   23630 O O    . ARG   B  1 759 ? 67.826 43.732  -23.130 1.00 42.44  ? 785  ARG   B O    1 
ATOM   23631 C CB   . ARG   B  1 759 ? 65.671 46.158  -22.522 1.00 42.71  ? 785  ARG   B CB   1 
ATOM   23632 C CG   . ARG   B  1 759 ? 65.279 47.498  -23.145 1.00 45.91  ? 785  ARG   B CG   1 
ATOM   23633 C CD   . ARG   B  1 759 ? 64.834 48.540  -22.135 1.00 49.10  ? 785  ARG   B CD   1 
ATOM   23634 N NE   . ARG   B  1 759 ? 63.652 49.259  -22.634 1.00 51.91  ? 785  ARG   B NE   1 
ATOM   23635 C CZ   . ARG   B  1 759 ? 62.444 49.324  -22.065 1.00 53.90  ? 785  ARG   B CZ   1 
ATOM   23636 N NH1  . ARG   B  1 759 ? 62.210 48.728  -20.898 1.00 54.00  ? 785  ARG   B NH1  1 
ATOM   23637 N NH2  . ARG   B  1 759 ? 61.464 50.002  -22.652 1.00 54.11  ? 785  ARG   B NH2  1 
ATOM   23638 H H    . ARG   B  1 759 ? 63.809 45.004  -23.707 0.00 61.49  ? 785  ARG   B H    1 
ATOM   23639 H HA   . ARG   B  1 759 ? 66.538 45.465  -24.353 0.00 63.47  ? 785  ARG   B HA   1 
ATOM   23640 H HB2  . ARG   B  1 759 ? 64.882 45.844  -21.840 0.00 66.35  ? 785  ARG   B HB2  1 
ATOM   23641 H HB3  . ARG   B  1 759 ? 66.598 46.306  -21.970 0.00 66.97  ? 785  ARG   B HB3  1 
ATOM   23642 H HG2  . ARG   B  1 759 ? 66.136 47.899  -23.684 0.00 71.19  ? 785  ARG   B HG2  1 
ATOM   23643 H HG3  . ARG   B  1 759 ? 64.457 47.334  -23.840 0.00 70.39  ? 785  ARG   B HG3  1 
ATOM   23644 H HD2  . ARG   B  1 759 ? 64.693 48.056  -21.173 0.00 75.87  ? 785  ARG   B HD2  1 
ATOM   23645 H HD3  . ARG   B  1 759 ? 65.631 49.276  -22.044 0.00 76.60  ? 785  ARG   B HD3  1 
ATOM   23646 H HE   . ARG   B  1 759 ? 63.766 49.728  -23.526 0.00 79.37  ? 785  ARG   B HE   1 
ATOM   23647 H HH11 . ARG   B  1 759 ? 62.893 48.188  -20.380 0.00 81.85  ? 785  ARG   B HH11 1 
ATOM   23648 H HH12 . ARG   B  1 759 ? 61.280 48.809  -20.499 0.00 82.01  ? 785  ARG   B HH12 1 
ATOM   23649 H HH21 . ARG   B  1 759 ? 61.625 50.469  -23.539 0.00 82.24  ? 785  ARG   B HH21 1 
ATOM   23650 H HH22 . ARG   B  1 759 ? 60.545 50.062  -22.223 0.00 82.30  ? 785  ARG   B HH22 1 
ATOM   23651 N N    . TRP   B  1 760 ? 65.861 42.902  -22.379 1.00 41.72  ? 786  TRP   B N    1 
ATOM   23652 C CA   . TRP   B  1 760 ? 66.441 41.670  -21.845 1.00 41.66  ? 786  TRP   B CA   1 
ATOM   23653 C C    . TRP   B  1 760 ? 67.081 40.847  -22.971 1.00 41.11  ? 786  TRP   B C    1 
ATOM   23654 O O    . TRP   B  1 760 ? 68.158 40.281  -22.781 1.00 41.02  ? 786  TRP   B O    1 
ATOM   23655 C CB   . TRP   B  1 760 ? 65.366 40.835  -21.146 1.00 41.73  ? 786  TRP   B CB   1 
ATOM   23656 C CG   . TRP   B  1 760 ? 65.896 39.577  -20.530 1.00 42.34  ? 786  TRP   B CG   1 
ATOM   23657 C CD1  . TRP   B  1 760 ? 66.384 39.428  -19.268 1.00 43.49  ? 786  TRP   B CD1  1 
ATOM   23658 C CD2  . TRP   B  1 760 ? 65.959 38.280  -21.142 1.00 42.37  ? 786  TRP   B CD2  1 
ATOM   23659 N NE1  . TRP   B  1 760 ? 66.697 38.108  -19.035 1.00 43.83  ? 786  TRP   B NE1  1 
ATOM   23660 C CE2  . TRP   B  1 760 ? 66.480 37.389  -20.183 1.00 43.22  ? 786  TRP   B CE2  1 
ATOM   23661 C CE3  . TRP   B  1 760 ? 65.650 37.789  -22.417 1.00 42.71  ? 786  TRP   B CE3  1 
ATOM   23662 C CZ2  . TRP   B  1 760 ? 66.698 36.040  -20.458 1.00 43.64  ? 786  TRP   B CZ2  1 
ATOM   23663 C CZ3  . TRP   B  1 760 ? 65.871 36.453  -22.688 1.00 43.52  ? 786  TRP   B CZ3  1 
ATOM   23664 C CH2  . TRP   B  1 760 ? 66.389 35.594  -21.716 1.00 43.68  ? 786  TRP   B CH2  1 
ATOM   23665 H H    . TRP   B  1 760 ? 64.858 42.966  -22.238 0.00 63.01  ? 786  TRP   B H    1 
ATOM   23666 H HA   . TRP   B  1 760 ? 67.214 41.917  -21.120 0.00 63.23  ? 786  TRP   B HA   1 
ATOM   23667 H HB2  . TRP   B  1 760 ? 64.917 41.434  -20.355 0.00 62.83  ? 786  TRP   B HB2  1 
ATOM   23668 H HB3  . TRP   B  1 760 ? 64.607 40.556  -21.874 0.00 61.59  ? 786  TRP   B HB3  1 
ATOM   23669 H HD1  . TRP   B  1 760 ? 66.417 40.208  -18.526 0.00 65.29  ? 786  TRP   B HD1  1 
ATOM   23670 H HE1  . TRP   B  1 760 ? 67.102 37.731  -18.154 0.00 64.55  ? 786  TRP   B HE1  1 
ATOM   23671 H HE3  . TRP   B  1 760 ? 65.244 38.442  -23.171 0.00 61.12  ? 786  TRP   B HE3  1 
ATOM   23672 H HZ2  . TRP   B  1 760 ? 67.116 35.379  -19.722 0.00 62.33  ? 786  TRP   B HZ2  1 
ATOM   23673 H HZ3  . TRP   B  1 760 ? 65.619 36.059  -23.658 0.00 60.65  ? 786  TRP   B HZ3  1 
ATOM   23674 H HH2  . TRP   B  1 760 ? 66.531 34.553  -21.953 0.00 60.89  ? 786  TRP   B HH2  1 
ATOM   23675 N N    . MET   B  1 761 ? 66.429 40.775  -24.138 1.00 40.51  ? 787  MET   B N    1 
ATOM   23676 C CA   . MET   B  1 761 ? 66.980 40.045  -25.279 1.00 40.83  ? 787  MET   B CA   1 
ATOM   23677 C C    . MET   B  1 761 ? 68.338 40.646  -25.705 1.00 41.66  ? 787  MET   B C    1 
ATOM   23678 O O    . MET   B  1 761 ? 69.267 39.908  -26.025 1.00 41.55  ? 787  MET   B O    1 
ATOM   23679 C CB   . MET   B  1 761 ? 66.003 40.086  -26.468 1.00 40.65  ? 787  MET   B CB   1 
ATOM   23680 C CG   . MET   B  1 761 ? 64.765 39.212  -26.289 1.00 41.38  ? 787  MET   B CG   1 
ATOM   23681 S SD   . MET   B  1 761 ? 63.544 39.350  -27.642 1.00 41.12  ? 787  MET   B SD   1 
ATOM   23682 C CE   . MET   B  1 761 ? 64.580 39.093  -29.063 1.00 41.08  ? 787  MET   B CE   1 
ATOM   23683 H H    . MET   B  1 761 ? 65.520 41.189  -24.317 0.00 59.77  ? 787  MET   B H    1 
ATOM   23684 H HA   . MET   B  1 761 ? 67.130 39.005  -24.994 0.00 58.92  ? 787  MET   B HA   1 
ATOM   23685 H HB2  . MET   B  1 761 ? 65.673 41.111  -26.630 0.00 59.10  ? 787  MET   B HB2  1 
ATOM   23686 H HB3  . MET   B  1 761 ? 66.544 39.733  -27.344 0.00 58.20  ? 787  MET   B HB3  1 
ATOM   23687 H HG2  . MET   B  1 761 ? 65.077 38.171  -26.230 0.00 58.24  ? 787  MET   B HG2  1 
ATOM   23688 H HG3  . MET   B  1 761 ? 64.267 39.498  -25.364 0.00 59.17  ? 787  MET   B HG3  1 
ATOM   23689 H HE1  . MET   B  1 761 ? 63.950 38.906  -29.931 0.00 56.97  ? 787  MET   B HE1  1 
ATOM   23690 H HE2  . MET   B  1 761 ? 65.181 39.986  -29.229 0.00 58.00  ? 787  MET   B HE2  1 
ATOM   23691 H HE3  . MET   B  1 761 ? 65.229 38.237  -28.883 0.00 57.09  ? 787  MET   B HE3  1 
ATOM   23692 N N    . ASP   B  1 762 ? 68.455 41.977  -25.683 1.00 42.58  ? 788  ASP   B N    1 
ATOM   23693 C CA   . ASP   B  1 762 ? 69.704 42.670  -26.032 1.00 44.15  ? 788  ASP   B CA   1 
ATOM   23694 C C    . ASP   B  1 762 ? 70.809 42.408  -24.987 1.00 44.94  ? 788  ASP   B C    1 
ATOM   23695 O O    . ASP   B  1 762 ? 71.975 42.267  -25.352 1.00 45.00  ? 788  ASP   B O    1 
ATOM   23696 C CB   . ASP   B  1 762 ? 69.461 44.189  -26.160 1.00 45.98  ? 788  ASP   B CB   1 
ATOM   23697 C CG   . ASP   B  1 762 ? 68.544 44.590  -27.306 1.00 51.03  ? 788  ASP   B CG   1 
ATOM   23698 O OD1  . ASP   B  1 762 ? 68.288 43.747  -28.187 1.00 51.99  ? 788  ASP   B OD1  1 
ATOM   23699 O OD2  . ASP   B  1 762 ? 68.064 45.737  -27.308 1.00 54.06  ? 788  ASP   B OD2  1 
ATOM   23700 H H    . ASP   B  1 762 ? 67.703 42.608  -25.425 0.00 63.20  ? 788  ASP   B H    1 
ATOM   23701 H HA   . ASP   B  1 762 ? 70.068 42.297  -26.989 0.00 64.88  ? 788  ASP   B HA   1 
ATOM   23702 H HB2  . ASP   B  1 762 ? 69.019 44.554  -25.234 0.00 68.94  ? 788  ASP   B HB2  1 
ATOM   23703 H HB3  . ASP   B  1 762 ? 70.421 44.678  -26.320 0.00 68.96  ? 788  ASP   B HB3  1 
ATOM   23704 N N    . GLU   B  1 763 ? 70.442 42.342  -23.706 1.00 45.44  ? 789  GLU   B N    1 
ATOM   23705 C CA   . GLU   B  1 763 ? 71.391 42.083  -22.618 1.00 46.63  ? 789  GLU   B CA   1 
ATOM   23706 C C    . GLU   B  1 763 ? 71.760 40.595  -22.466 1.00 46.68  ? 789  GLU   B C    1 
ATOM   23707 O O    . GLU   B  1 763 ? 72.679 40.293  -21.702 1.00 47.01  ? 789  GLU   B O    1 
ATOM   23708 C CB   . GLU   B  1 763 ? 70.809 42.574  -21.282 1.00 49.96  ? 789  GLU   B CB   1 
ATOM   23709 C CG   . GLU   B  1 763 ? 70.592 44.076  -21.204 1.00 56.38  ? 789  GLU   B CG   1 
ATOM   23710 C CD   . GLU   B  1 763 ? 69.778 44.545  -20.011 1.00 64.77  ? 789  GLU   B CD   1 
ATOM   23711 O OE1  . GLU   B  1 763 ? 69.200 43.691  -19.300 1.00 65.71  ? 789  GLU   B OE1  1 
ATOM   23712 O OE2  . GLU   B  1 763 ? 69.711 45.777  -19.793 1.00 68.68  ? 789  GLU   B OE2  1 
ATOM   23713 H H    . GLU   B  1 763 ? 69.491 42.479  -23.379 0.00 67.78  ? 789  GLU   B H    1 
ATOM   23714 H HA   . GLU   B  1 763 ? 72.310 42.639  -22.797 0.00 70.31  ? 789  GLU   B HA   1 
ATOM   23715 H HB2  . GLU   B  1 763 ? 69.852 42.076  -21.128 0.00 73.96  ? 789  GLU   B HB2  1 
ATOM   23716 H HB3  . GLU   B  1 763 ? 71.492 42.305  -20.478 0.00 74.84  ? 789  GLU   B HB3  1 
ATOM   23717 H HG2  . GLU   B  1 763 ? 71.565 44.563  -21.148 0.00 83.77  ? 789  GLU   B HG2  1 
ATOM   23718 H HG3  . GLU   B  1 763 ? 70.071 44.409  -22.100 0.00 82.85  ? 789  GLU   B HG3  1 
ATOM   23719 N N    . HIS   B  1 764 ? 71.027 39.673  -23.130 1.00 45.86  ? 790  HIS   B N    1 
ATOM   23720 C CA   . HIS   B  1 764 ? 71.271 38.233  -23.020 1.00 45.87  ? 790  HIS   B CA   1 
ATOM   23721 C C    . HIS   B  1 764 ? 71.383 37.607  -24.407 1.00 45.32  ? 790  HIS   B C    1 
ATOM   23722 O O    . HIS   B  1 764 ? 70.595 36.735  -24.766 1.00 45.06  ? 790  HIS   B O    1 
ATOM   23723 C CB   . HIS   B  1 764 ? 70.154 37.564  -22.193 1.00 46.85  ? 790  HIS   B CB   1 
ATOM   23724 C CG   . HIS   B  1 764 ? 70.072 38.080  -20.790 1.00 49.20  ? 790  HIS   B CG   1 
ATOM   23725 N ND1  . HIS   B  1 764 ? 69.346 39.215  -20.479 1.00 51.37  ? 790  HIS   B ND1  1 
ATOM   23726 C CD2  . HIS   B  1 764 ? 70.660 37.616  -19.663 1.00 50.45  ? 790  HIS   B CD2  1 
ATOM   23727 C CE1  . HIS   B  1 764 ? 69.506 39.407  -19.178 1.00 51.94  ? 790  HIS   B CE1  1 
ATOM   23728 N NE2  . HIS   B  1 764 ? 70.291 38.470  -18.643 1.00 51.76  ? 790  HIS   B NE2  1 
ATOM   23729 H H    . HIS   B  1 764 ? 70.252 39.885  -23.750 0.00 66.73  ? 790  HIS   B H    1 
ATOM   23730 H HA   . HIS   B  1 764 ? 72.213 38.042  -22.509 0.00 66.71  ? 790  HIS   B HA   1 
ATOM   23731 H HB2  . HIS   B  1 764 ? 69.196 37.750  -22.676 0.00 66.80  ? 790  HIS   B HB2  1 
ATOM   23732 H HB3  . HIS   B  1 764 ? 70.341 36.492  -22.139 0.00 66.64  ? 790  HIS   B HB3  1 
ATOM   23733 H HD1  . HIS   B  1 764 ? 68.798 39.783  -21.117 0.00 73.96  ? 790  HIS   B HD1  1 
ATOM   23734 H HD2  . HIS   B  1 764 ? 71.293 36.748  -19.579 0.00 72.44  ? 790  HIS   B HD2  1 
ATOM   23735 H HE1  . HIS   B  1 764 ? 69.060 40.216  -18.624 0.00 76.05  ? 790  HIS   B HE1  1 
ATOM   23736 N N    . LEU   B  1 765 ? 72.385 38.049  -25.187 1.00 44.99  ? 791  LEU   B N    1 
ATOM   23737 C CA   . LEU   B  1 765 ? 72.626 37.514  -26.527 1.00 45.25  ? 791  LEU   B CA   1 
ATOM   23738 C C    . LEU   B  1 765 ? 73.068 36.043  -26.513 1.00 44.96  ? 791  LEU   B C    1 
ATOM   23739 O O    . LEU   B  1 765 ? 72.985 35.387  -27.552 1.00 45.20  ? 791  LEU   B O    1 
ATOM   23740 C CB   . LEU   B  1 765 ? 73.671 38.365  -27.270 1.00 45.66  ? 791  LEU   B CB   1 
ATOM   23741 C CG   . LEU   B  1 765 ? 73.280 39.814  -27.564 1.00 47.27  ? 791  LEU   B CG   1 
ATOM   23742 C CD1  . LEU   B  1 765 ? 74.457 40.579  -28.149 1.00 47.79  ? 791  LEU   B CD1  1 
ATOM   23743 C CD2  . LEU   B  1 765 ? 72.079 39.889  -28.508 1.00 47.71  ? 791  LEU   B CD2  1 
ATOM   23744 H H    . LEU   B  1 765 ? 73.040 38.772  -24.909 0.00 65.36  ? 791  LEU   B H    1 
ATOM   23745 H HA   . LEU   B  1 765 ? 71.693 37.547  -27.086 0.00 63.79  ? 791  LEU   B HA   1 
ATOM   23746 H HB2  . LEU   B  1 765 ? 74.581 38.389  -26.673 0.00 65.76  ? 791  LEU   B HB2  1 
ATOM   23747 H HB3  . LEU   B  1 765 ? 73.883 37.887  -28.225 0.00 64.71  ? 791  LEU   B HB3  1 
ATOM   23748 H HG   . LEU   B  1 765 ? 72.999 40.300  -26.631 0.00 68.31  ? 791  LEU   B HG   1 
ATOM   23749 H HD11 . LEU   B  1 765 ? 74.163 41.615  -28.312 0.00 69.50  ? 791  LEU   B HD11 1 
ATOM   23750 H HD12 . LEU   B  1 765 ? 75.290 40.534  -27.450 0.00 69.53  ? 791  LEU   B HD12 1 
ATOM   23751 H HD13 . LEU   B  1 765 ? 74.739 40.120  -29.096 0.00 68.53  ? 791  LEU   B HD13 1 
ATOM   23752 H HD21 . LEU   B  1 765 ? 71.989 40.905  -28.888 0.00 68.15  ? 791  LEU   B HD21 1 
ATOM   23753 H HD22 . LEU   B  1 765 ? 72.230 39.194  -29.333 0.00 67.07  ? 791  LEU   B HD22 1 
ATOM   23754 H HD23 . LEU   B  1 765 ? 71.175 39.628  -27.959 0.00 67.45  ? 791  LEU   B HD23 1 
ATOM   23755 N N    . ASN   B  1 766 ? 73.535 35.523  -25.357 1.00 44.68  ? 792  ASN   B N    1 
ATOM   23756 C CA   . ASN   B  1 766 ? 73.918 34.115  -25.226 1.00 45.11  ? 792  ASN   B CA   1 
ATOM   23757 C C    . ASN   B  1 766 ? 72.675 33.190  -25.148 1.00 43.64  ? 792  ASN   B C    1 
ATOM   23758 O O    . ASN   B  1 766 ? 72.799 31.992  -25.406 1.00 44.12  ? 792  ASN   B O    1 
ATOM   23759 C CB   . ASN   B  1 766 ? 74.804 33.921  -24.000 1.00 48.41  ? 792  ASN   B CB   1 
ATOM   23760 C CG   . ASN   B  1 766 ? 75.604 32.637  -24.026 1.00 55.06  ? 792  ASN   B CG   1 
ATOM   23761 O OD1  . ASN   B  1 766 ? 76.568 32.501  -24.797 1.00 57.26  ? 792  ASN   B OD1  1 
ATOM   23762 N ND2  . ASN   B  1 766 ? 75.241 31.667  -23.183 1.00 56.64  ? 792  ASN   B ND2  1 
ATOM   23763 H H    . ASN   B  1 766 ? 73.669 36.048  -24.499 0.00 63.83  ? 792  ASN   B H    1 
ATOM   23764 H HA   . ASN   B  1 766 ? 74.494 33.826  -26.105 0.00 62.86  ? 792  ASN   B HA   1 
ATOM   23765 H HB2  . ASN   B  1 766 ? 75.519 34.741  -23.951 0.00 68.44  ? 792  ASN   B HB2  1 
ATOM   23766 H HB3  . ASN   B  1 766 ? 74.179 33.935  -23.109 0.00 67.91  ? 792  ASN   B HB3  1 
ATOM   23767 H HD21 . ASN   B  1 766 ? 75.759 30.794  -23.174 0.00 76.88  ? 792  ASN   B HD21 1 
ATOM   23768 H HD22 . ASN   B  1 766 ? 74.456 31.791  -22.552 0.00 77.19  ? 792  ASN   B HD22 1 
ATOM   23769 N N    . VAL   B  1 767 ? 71.485 33.732  -24.801 1.00 41.58  ? 793  VAL   B N    1 
ATOM   23770 C CA   . VAL   B  1 767 ? 70.252 32.945  -24.771 1.00 40.26  ? 793  VAL   B CA   1 
ATOM   23771 C C    . VAL   B  1 767 ? 69.678 32.967  -26.185 1.00 38.74  ? 793  VAL   B C    1 
ATOM   23772 O O    . VAL   B  1 767 ? 69.141 33.990  -26.603 1.00 39.41  ? 793  VAL   B O    1 
ATOM   23773 C CB   . VAL   B  1 767 ? 69.224 33.503  -23.754 1.00 40.52  ? 793  VAL   B CB   1 
ATOM   23774 C CG1  . VAL   B  1 767 ? 67.954 32.650  -23.753 1.00 40.83  ? 793  VAL   B CG1  1 
ATOM   23775 C CG2  . VAL   B  1 767 ? 69.824 33.588  -22.349 1.00 40.64  ? 793  VAL   B CG2  1 
ATOM   23776 H H    . VAL   B  1 767 ? 71.342 34.700  -24.530 0.00 58.70  ? 793  VAL   B H    1 
ATOM   23777 H HA   . VAL   B  1 767 ? 70.465 31.915  -24.490 0.00 55.51  ? 793  VAL   B HA   1 
ATOM   23778 H HB   . VAL   B  1 767 ? 68.947 34.515  -24.047 0.00 56.86  ? 793  VAL   B HB   1 
ATOM   23779 H HG11 . VAL   B  1 767 ? 67.428 32.792  -22.810 0.00 56.47  ? 793  VAL   B HG11 1 
ATOM   23780 H HG12 . VAL   B  1 767 ? 67.310 32.965  -24.573 0.00 55.89  ? 793  VAL   B HG12 1 
ATOM   23781 H HG13 . VAL   B  1 767 ? 68.221 31.601  -23.873 0.00 55.69  ? 793  VAL   B HG13 1 
ATOM   23782 H HG21 . VAL   B  1 767 ? 69.087 34.030  -21.680 0.00 57.70  ? 793  VAL   B HG21 1 
ATOM   23783 H HG22 . VAL   B  1 767 ? 70.073 32.582  -22.014 0.00 57.12  ? 793  VAL   B HG22 1 
ATOM   23784 H HG23 . VAL   B  1 767 ? 70.720 34.207  -22.366 0.00 57.98  ? 793  VAL   B HG23 1 
ATOM   23785 N N    . LYS   B  1 768 ? 69.812 31.869  -26.928 1.00 37.01  ? 794  LYS   B N    1 
ATOM   23786 C CA   . LYS   B  1 768 ? 69.314 31.785  -28.299 1.00 36.21  ? 794  LYS   B CA   1 
ATOM   23787 C C    . LYS   B  1 768 ? 67.787 31.702  -28.319 1.00 34.77  ? 794  LYS   B C    1 
ATOM   23788 O O    . LYS   B  1 768 ? 67.209 30.916  -27.571 1.00 34.18  ? 794  LYS   B O    1 
ATOM   23789 C CB   . LYS   B  1 768 ? 69.880 30.540  -29.007 1.00 38.30  ? 794  LYS   B CB   1 
ATOM   23790 C CG   . LYS   B  1 768 ? 71.398 30.511  -29.107 1.00 44.20  ? 794  LYS   B CG   1 
ATOM   23791 C CD   . LYS   B  1 768 ? 71.903 29.401  -30.049 1.00 50.51  ? 794  LYS   B CD   1 
ATOM   23792 C CE   . LYS   B  1 768 ? 71.766 27.992  -29.497 1.00 55.41  ? 794  LYS   B CE   1 
ATOM   23793 N NZ   . LYS   B  1 768 ? 72.621 27.766  -28.294 1.00 58.09  ? 794  LYS   B NZ   1 
ATOM   23794 H H    . LYS   B  1 768 ? 70.249 31.013  -26.603 0.00 50.40  ? 794  LYS   B H    1 
ATOM   23795 H HA   . LYS   B  1 768 ? 69.635 32.665  -28.855 0.00 49.31  ? 794  LYS   B HA   1 
ATOM   23796 H HB2  . LYS   B  1 768 ? 69.561 29.658  -28.454 0.00 50.58  ? 794  LYS   B HB2  1 
ATOM   23797 H HB3  . LYS   B  1 768 ? 69.475 30.505  -30.018 0.00 50.45  ? 794  LYS   B HB3  1 
ATOM   23798 H HG2  . LYS   B  1 768 ? 71.745 31.467  -29.499 0.00 58.70  ? 794  LYS   B HG2  1 
ATOM   23799 H HG3  . LYS   B  1 768 ? 71.818 30.343  -28.116 0.00 58.66  ? 794  LYS   B HG3  1 
ATOM   23800 H HD2  . LYS   B  1 768 ? 71.341 29.451  -30.979 0.00 64.84  ? 794  LYS   B HD2  1 
ATOM   23801 H HD3  . LYS   B  1 768 ? 72.960 29.572  -30.250 0.00 65.56  ? 794  LYS   B HD3  1 
ATOM   23802 H HE2  . LYS   B  1 768 ? 70.730 27.805  -29.218 0.00 70.45  ? 794  LYS   B HE2  1 
ATOM   23803 H HE3  . LYS   B  1 768 ? 72.075 27.283  -30.264 0.00 70.27  ? 794  LYS   B HE3  1 
ATOM   23804 H HZ1  . LYS   B  1 768 ? 72.601 26.785  -28.033 0.00 74.17  ? 794  LYS   B HZ1  1 
ATOM   23805 H HZ2  . LYS   B  1 768 ? 73.579 28.033  -28.497 0.00 74.75  ? 794  LYS   B HZ2  1 
ATOM   23806 H HZ3  . LYS   B  1 768 ? 72.285 28.318  -27.512 0.00 74.87  ? 794  LYS   B HZ3  1 
ATOM   23807 N N    . ILE   B  1 769 ? 67.151 32.536  -29.147 1.00 33.84  ? 795  ILE   B N    1 
ATOM   23808 C CA   . ILE   B  1 769 ? 65.712 32.560  -29.367 1.00 33.24  ? 795  ILE   B CA   1 
ATOM   23809 C C    . ILE   B  1 769 ? 65.594 32.306  -30.878 1.00 33.31  ? 795  ILE   B C    1 
ATOM   23810 O O    . ILE   B  1 769 ? 65.773 33.245  -31.659 1.00 33.99  ? 795  ILE   B O    1 
ATOM   23811 C CB   . ILE   B  1 769 ? 65.098 33.921  -28.938 1.00 33.27  ? 795  ILE   B CB   1 
ATOM   23812 C CG1  . ILE   B  1 769 ? 65.344 34.168  -27.420 1.00 33.98  ? 795  ILE   B CG1  1 
ATOM   23813 C CG2  . ILE   B  1 769 ? 63.593 33.961  -29.261 1.00 33.46  ? 795  ILE   B CG2  1 
ATOM   23814 C CD1  . ILE   B  1 769 ? 64.920 35.533  -26.923 1.00 34.74  ? 795  ILE   B CD1  1 
ATOM   23815 H H    . ILE   B  1 769 ? 67.628 33.239  -29.703 0.00 46.02  ? 795  ILE   B H    1 
ATOM   23816 H HA   . ILE   B  1 769 ? 65.200 31.781  -28.804 0.00 44.38  ? 795  ILE   B HA   1 
ATOM   23817 H HB   . ILE   B  1 769 ? 65.590 34.720  -29.491 0.00 45.73  ? 795  ILE   B HB   1 
ATOM   23818 H HG12 . ILE   B  1 769 ? 64.785 33.425  -26.854 0.00 46.57  ? 795  ILE   B HG12 1 
ATOM   23819 H HG13 . ILE   B  1 769 ? 66.407 34.069  -27.204 0.00 47.10  ? 795  ILE   B HG13 1 
ATOM   23820 H HG21 . ILE   B  1 769 ? 63.195 34.946  -29.020 0.00 45.79  ? 795  ILE   B HG21 1 
ATOM   23821 H HG22 . ILE   B  1 769 ? 63.428 33.766  -30.319 0.00 44.88  ? 795  ILE   B HG22 1 
ATOM   23822 H HG23 . ILE   B  1 769 ? 63.087 33.204  -28.663 0.00 44.98  ? 795  ILE   B HG23 1 
ATOM   23823 H HD11 . ILE   B  1 769 ? 65.329 35.686  -25.926 0.00 49.04  ? 795  ILE   B HD11 1 
ATOM   23824 H HD12 . ILE   B  1 769 ? 65.303 36.292  -27.603 0.00 48.81  ? 795  ILE   B HD12 1 
ATOM   23825 H HD13 . ILE   B  1 769 ? 63.833 35.581  -26.882 0.00 48.40  ? 795  ILE   B HD13 1 
ATOM   23826 N N    . PRO   B  1 770 ? 65.429 31.046  -31.324 1.00 32.40  ? 796  PRO   B N    1 
ATOM   23827 C CA   . PRO   B  1 770 ? 65.361 30.802  -32.775 1.00 32.28  ? 796  PRO   B CA   1 
ATOM   23828 C C    . PRO   B  1 770 ? 64.068 31.302  -33.402 1.00 32.14  ? 796  PRO   B C    1 
ATOM   23829 O O    . PRO   B  1 770 ? 63.063 31.515  -32.707 1.00 32.05  ? 796  PRO   B O    1 
ATOM   23830 C CB   . PRO   B  1 770 ? 65.483 29.274  -32.910 1.00 32.91  ? 796  PRO   B CB   1 
ATOM   23831 C CG   . PRO   B  1 770 ? 65.634 28.731  -31.514 1.00 33.42  ? 796  PRO   B CG   1 
ATOM   23832 C CD   . PRO   B  1 770 ? 65.239 29.803  -30.552 1.00 31.66  ? 796  PRO   B CD   1 
ATOM   23833 H HA   . PRO   B  1 770 ? 66.210 31.262  -33.280 0.00 42.00  ? 796  PRO   B HA   1 
ATOM   23834 H HB2  . PRO   B  1 770 ? 64.582 28.879  -33.377 0.00 41.44  ? 796  PRO   B HB2  1 
ATOM   23835 H HB3  . PRO   B  1 770 ? 66.360 29.033  -33.509 0.00 41.77  ? 796  PRO   B HB3  1 
ATOM   23836 H HG2  . PRO   B  1 770 ? 64.988 27.863  -31.395 0.00 42.18  ? 796  PRO   B HG2  1 
ATOM   23837 H HG3  . PRO   B  1 770 ? 66.674 28.449  -31.352 0.00 42.74  ? 796  PRO   B HG3  1 
ATOM   23838 H HD2  . PRO   B  1 770 ? 64.195 29.689  -30.263 0.00 40.97  ? 796  PRO   B HD2  1 
ATOM   23839 H HD3  . PRO   B  1 770 ? 65.901 29.769  -29.689 0.00 41.47  ? 796  PRO   B HD3  1 
ATOM   23840 N N    . ARG   B  1 771 ? 64.102 31.461  -34.729 1.00 31.46  ? 797  ARG   B N    1 
ATOM   23841 C CA   . ARG   B  1 771 ? 62.950 31.834  -35.541 1.00 31.60  ? 797  ARG   B CA   1 
ATOM   23842 C C    . ARG   B  1 771 ? 62.242 33.106  -35.048 1.00 30.07  ? 797  ARG   B C    1 
ATOM   23843 O O    . ARG   B  1 771 ? 61.028 33.094  -34.832 1.00 28.45  ? 797  ARG   B O    1 
ATOM   23844 C CB   . ARG   B  1 771 ? 61.960 30.650  -35.631 1.00 33.89  ? 797  ARG   B CB   1 
ATOM   23845 C CG   . ARG   B  1 771 ? 62.519 29.378  -36.294 1.00 38.24  ? 797  ARG   B CG   1 
ATOM   23846 C CD   . ARG   B  1 771 ? 62.617 29.423  -37.815 1.00 42.83  ? 797  ARG   B CD   1 
ATOM   23847 N NE   . ARG   B  1 771 ? 61.311 29.527  -38.482 1.00 45.67  ? 797  ARG   B NE   1 
ATOM   23848 C CZ   . ARG   B  1 771 ? 61.058 29.202  -39.753 1.00 45.98  ? 797  ARG   B CZ   1 
ATOM   23849 N NH1  . ARG   B  1 771 ? 62.017 28.704  -40.528 1.00 45.64  ? 797  ARG   B NH1  1 
ATOM   23850 N NH2  . ARG   B  1 771 ? 59.836 29.354  -40.251 1.00 44.21  ? 797  ARG   B NH2  1 
ATOM   23851 H H    . ARG   B  1 771 ? 64.944 31.335  -35.281 0.00 40.40  ? 797  ARG   B H    1 
ATOM   23852 H HA   . ARG   B  1 771 ? 63.301 32.034  -36.553 0.00 40.40  ? 797  ARG   B HA   1 
ATOM   23853 H HB2  . ARG   B  1 771 ? 61.643 30.380  -34.625 0.00 42.59  ? 797  ARG   B HB2  1 
ATOM   23854 H HB3  . ARG   B  1 771 ? 61.092 30.968  -36.205 0.00 42.48  ? 797  ARG   B HB3  1 
ATOM   23855 H HG2  . ARG   B  1 771 ? 63.518 29.183  -35.908 0.00 47.29  ? 797  ARG   B HG2  1 
ATOM   23856 H HG3  . ARG   B  1 771 ? 61.866 28.545  -36.036 0.00 46.80  ? 797  ARG   B HG3  1 
ATOM   23857 H HD2  . ARG   B  1 771 ? 63.223 30.279  -38.112 0.00 52.83  ? 797  ARG   B HD2  1 
ATOM   23858 H HD3  . ARG   B  1 771 ? 63.099 28.496  -38.121 0.00 52.08  ? 797  ARG   B HD3  1 
ATOM   23859 H HE   . ARG   B  1 771 ? 60.533 29.886  -37.939 0.00 55.76  ? 797  ARG   B HE   1 
ATOM   23860 H HH11 . ARG   B  1 771 ? 62.975 28.591  -40.212 0.00 55.23  ? 797  ARG   B HH11 1 
ATOM   23861 H HH12 . ARG   B  1 771 ? 61.802 28.472  -41.492 0.00 54.90  ? 797  ARG   B HH12 1 
ATOM   23862 H HH21 . ARG   B  1 771 ? 59.085 29.711  -39.669 0.00 53.59  ? 797  ARG   B HH21 1 
ATOM   23863 H HH22 . ARG   B  1 771 ? 59.638 29.094  -41.212 0.00 53.24  ? 797  ARG   B HH22 1 
ATOM   23864 N N    . LEU   B  1 772 ? 63.003 34.212  -34.883 1.00 30.12  ? 798  LEU   B N    1 
ATOM   23865 C CA   . LEU   B  1 772 ? 62.430 35.501  -34.485 1.00 30.19  ? 798  LEU   B CA   1 
ATOM   23866 C C    . LEU   B  1 772 ? 61.349 35.959  -35.469 1.00 30.10  ? 798  LEU   B C    1 
ATOM   23867 O O    . LEU   B  1 772 ? 60.398 36.610  -35.040 1.00 29.69  ? 798  LEU   B O    1 
ATOM   23868 C CB   . LEU   B  1 772 ? 63.509 36.583  -34.391 1.00 30.65  ? 798  LEU   B CB   1 
ATOM   23869 C CG   . LEU   B  1 772 ? 64.445 36.514  -33.190 1.00 32.45  ? 798  LEU   B CG   1 
ATOM   23870 C CD1  . LEU   B  1 772 ? 65.506 37.610  -33.286 1.00 33.29  ? 798  LEU   B CD1  1 
ATOM   23871 C CD2  . LEU   B  1 772 ? 63.675 36.650  -31.859 1.00 33.05  ? 798  LEU   B CD2  1 
ATOM   23872 H H    . LEU   B  1 772 ? 64.009 34.230  -35.015 0.00 40.06  ? 798  LEU   B H    1 
ATOM   23873 H HA   . LEU   B  1 772 ? 61.944 35.385  -33.519 0.00 40.80  ? 798  LEU   B HA   1 
ATOM   23874 H HB2  . LEU   B  1 772 ? 64.120 36.535  -35.291 0.00 41.84  ? 798  LEU   B HB2  1 
ATOM   23875 H HB3  . LEU   B  1 772 ? 63.011 37.550  -34.350 0.00 42.44  ? 798  LEU   B HB3  1 
ATOM   23876 H HG   . LEU   B  1 772 ? 64.954 35.552  -33.188 0.00 44.09  ? 798  LEU   B HG   1 
ATOM   23877 H HD11 . LEU   B  1 772 ? 66.310 37.387  -32.587 0.00 46.51  ? 798  LEU   B HD11 1 
ATOM   23878 H HD12 . LEU   B  1 772 ? 65.903 37.641  -34.300 0.00 46.09  ? 798  LEU   B HD12 1 
ATOM   23879 H HD13 . LEU   B  1 772 ? 65.051 38.567  -33.037 0.00 46.76  ? 798  LEU   B HD13 1 
ATOM   23880 H HD21 . LEU   B  1 772 ? 64.380 36.916  -31.073 0.00 45.99  ? 798  LEU   B HD21 1 
ATOM   23881 H HD22 . LEU   B  1 772 ? 62.917 37.426  -31.960 0.00 45.80  ? 798  LEU   B HD22 1 
ATOM   23882 H HD23 . LEU   B  1 772 ? 63.207 35.698  -31.614 0.00 45.01  ? 798  LEU   B HD23 1 
ATOM   23883 N N    . VAL   B  1 773 ? 61.459 35.579  -36.767 1.00 30.05  ? 799  VAL   B N    1 
ATOM   23884 C CA   . VAL   B  1 773 ? 60.429 35.876  -37.778 1.00 30.46  ? 799  VAL   B CA   1 
ATOM   23885 C C    . VAL   B  1 773 ? 59.069 35.319  -37.400 1.00 30.40  ? 799  VAL   B C    1 
ATOM   23886 O O    . VAL   B  1 773 ? 58.066 35.825  -37.903 1.00 31.13  ? 799  VAL   B O    1 
ATOM   23887 C CB   . VAL   B  1 773 ? 60.783 35.341  -39.193 1.00 31.27  ? 799  VAL   B CB   1 
ATOM   23888 C CG1  . VAL   B  1 773 ? 61.964 36.068  -39.776 1.00 31.79  ? 799  VAL   B CG1  1 
ATOM   23889 C CG2  . VAL   B  1 773 ? 61.021 33.830  -39.187 1.00 31.97  ? 799  VAL   B CG2  1 
ATOM   23890 H H    . VAL   B  1 773 ? 62.269 35.097  -37.143 0.00 39.78  ? 799  VAL   B H    1 
ATOM   23891 H HA   . VAL   B  1 773 ? 60.321 36.958  -37.846 0.00 40.94  ? 799  VAL   B HA   1 
ATOM   23892 H HB   . VAL   B  1 773 ? 59.935 35.529  -39.849 0.00 40.85  ? 799  VAL   B HB   1 
ATOM   23893 H HG11 . VAL   B  1 773 ? 62.136 35.683  -40.780 0.00 41.60  ? 799  VAL   B HG11 1 
ATOM   23894 H HG12 . VAL   B  1 773 ? 61.742 37.134  -39.816 0.00 42.45  ? 799  VAL   B HG12 1 
ATOM   23895 H HG13 . VAL   B  1 773 ? 62.839 35.892  -39.152 0.00 42.03  ? 799  VAL   B HG13 1 
ATOM   23896 H HG21 . VAL   B  1 773 ? 60.426 33.380  -39.980 0.00 40.64  ? 799  VAL   B HG21 1 
ATOM   23897 H HG22 . VAL   B  1 773 ? 62.079 33.655  -39.373 0.00 41.00  ? 799  VAL   B HG22 1 
ATOM   23898 H HG23 . VAL   B  1 773 ? 60.752 33.392  -38.227 0.00 40.90  ? 799  VAL   B HG23 1 
ATOM   23899 N N    . ASP   B  1 774 ? 59.042 34.208  -36.627 1.00 29.49  ? 800  ASP   B N    1 
ATOM   23900 C CA   . ASP   B  1 774 ? 57.838 33.535  -36.160 1.00 29.39  ? 800  ASP   B CA   1 
ATOM   23901 C C    . ASP   B  1 774 ? 57.438 33.924  -34.720 1.00 29.53  ? 800  ASP   B C    1 
ATOM   23902 O O    . ASP   B  1 774 ? 56.395 33.464  -34.255 1.00 29.96  ? 800  ASP   B O    1 
ATOM   23903 C CB   . ASP   B  1 774 ? 57.990 32.004  -36.294 1.00 31.27  ? 800  ASP   B CB   1 
ATOM   23904 C CG   . ASP   B  1 774 ? 58.176 31.520  -37.719 1.00 35.98  ? 800  ASP   B CG   1 
ATOM   23905 O OD1  . ASP   B  1 774 ? 57.791 32.253  -38.649 1.00 36.10  ? 800  ASP   B OD1  1 
ATOM   23906 O OD2  . ASP   B  1 774 ? 58.683 30.395  -37.901 1.00 38.22  ? 800  ASP   B OD2  1 
ATOM   23907 H H    . ASP   B  1 774 ? 59.876 33.734  -36.296 0.00 38.34  ? 800  ASP   B H    1 
ATOM   23908 H HA   . ASP   B  1 774 ? 56.997 33.822  -36.789 0.00 38.01  ? 800  ASP   B HA   1 
ATOM   23909 H HB2  . ASP   B  1 774 ? 58.851 31.677  -35.712 0.00 39.54  ? 800  ASP   B HB2  1 
ATOM   23910 H HB3  . ASP   B  1 774 ? 57.086 31.529  -35.918 0.00 39.33  ? 800  ASP   B HB3  1 
ATOM   23911 N N    . VAL   B  1 775 ? 58.215 34.779  -34.029 1.00 29.00  ? 801  VAL   B N    1 
ATOM   23912 C CA   . VAL   B  1 775 ? 57.866 35.307  -32.707 1.00 29.43  ? 801  VAL   B CA   1 
ATOM   23913 C C    . VAL   B  1 775 ? 57.141 36.603  -33.063 1.00 30.56  ? 801  VAL   B C    1 
ATOM   23914 O O    . VAL   B  1 775 ? 57.750 37.664  -33.144 1.00 30.93  ? 801  VAL   B O    1 
ATOM   23915 C CB   . VAL   B  1 775 ? 59.129 35.542  -31.834 1.00 29.12  ? 801  VAL   B CB   1 
ATOM   23916 C CG1  . VAL   B  1 775 ? 58.735 36.043  -30.448 1.00 29.41  ? 801  VAL   B CG1  1 
ATOM   23917 C CG2  . VAL   B  1 775 ? 59.963 34.262  -31.724 1.00 28.88  ? 801  VAL   B CG2  1 
ATOM   23918 H H    . VAL   B  1 775 ? 59.113 35.127  -34.351 0.00 38.77  ? 801  VAL   B H    1 
ATOM   23919 H HA   . VAL   B  1 775 ? 57.193 34.640  -32.171 0.00 39.37  ? 801  VAL   B HA   1 
ATOM   23920 H HB   . VAL   B  1 775 ? 59.760 36.298  -32.299 0.00 40.02  ? 801  VAL   B HB   1 
ATOM   23921 H HG11 . VAL   B  1 775 ? 59.625 36.075  -29.820 0.00 40.87  ? 801  VAL   B HG11 1 
ATOM   23922 H HG12 . VAL   B  1 775 ? 58.307 37.040  -30.525 0.00 41.08  ? 801  VAL   B HG12 1 
ATOM   23923 H HG13 . VAL   B  1 775 ? 58.007 35.354  -30.024 0.00 40.27  ? 801  VAL   B HG13 1 
ATOM   23924 H HG21 . VAL   B  1 775 ? 60.836 34.467  -31.105 0.00 39.18  ? 801  VAL   B HG21 1 
ATOM   23925 H HG22 . VAL   B  1 775 ? 59.360 33.484  -31.259 0.00 38.48  ? 801  VAL   B HG22 1 
ATOM   23926 H HG23 . VAL   B  1 775 ? 60.287 33.944  -32.713 0.00 38.49  ? 801  VAL   B HG23 1 
ATOM   23927 N N    . ILE   B  1 776 ? 55.849 36.478  -33.365 1.00 31.41  ? 802  ILE   B N    1 
ATOM   23928 C CA   . ILE   B  1 776 ? 55.014 37.504  -33.992 1.00 32.79  ? 802  ILE   B CA   1 
ATOM   23929 C C    . ILE   B  1 776 ? 54.049 38.246  -33.061 1.00 33.61  ? 802  ILE   B C    1 
ATOM   23930 O O    . ILE   B  1 776 ? 53.569 37.698  -32.074 1.00 33.71  ? 802  ILE   B O    1 
ATOM   23931 C CB   . ILE   B  1 776 ? 54.238 36.802  -35.177 1.00 33.88  ? 802  ILE   B CB   1 
ATOM   23932 C CG1  . ILE   B  1 776 ? 55.204 36.476  -36.335 1.00 34.89  ? 802  ILE   B CG1  1 
ATOM   23933 C CG2  . ILE   B  1 776 ? 53.068 37.645  -35.703 1.00 34.99  ? 802  ILE   B CG2  1 
ATOM   23934 C CD1  . ILE   B  1 776 ? 54.700 35.349  -37.305 1.00 36.36  ? 802  ILE   B CD1  1 
ATOM   23935 H H    . ILE   B  1 776 ? 55.326 35.632  -33.159 0.00 41.95  ? 802  ILE   B H    1 
ATOM   23936 H HA   . ILE   B  1 776 ? 55.664 38.259  -34.433 0.00 44.81  ? 802  ILE   B HA   1 
ATOM   23937 H HB   . ILE   B  1 776 ? 53.792 35.866  -34.840 0.00 44.71  ? 802  ILE   B HB   1 
ATOM   23938 H HG12 . ILE   B  1 776 ? 55.348 37.377  -36.928 0.00 46.39  ? 802  ILE   B HG12 1 
ATOM   23939 H HG13 . ILE   B  1 776 ? 56.161 36.151  -35.930 0.00 45.89  ? 802  ILE   B HG13 1 
ATOM   23940 H HG21 . ILE   B  1 776 ? 52.696 37.233  -36.639 0.00 46.51  ? 802  ILE   B HG21 1 
ATOM   23941 H HG22 . ILE   B  1 776 ? 52.256 37.633  -34.978 0.00 46.99  ? 802  ILE   B HG22 1 
ATOM   23942 H HG23 . ILE   B  1 776 ? 53.409 38.667  -35.863 0.00 47.42  ? 802  ILE   B HG23 1 
ATOM   23943 H HD11 . ILE   B  1 776 ? 55.501 35.108  -38.001 0.00 46.77  ? 802  ILE   B HD11 1 
ATOM   23944 H HD12 . ILE   B  1 776 ? 54.435 34.469  -36.720 0.00 46.64  ? 802  ILE   B HD12 1 
ATOM   23945 H HD13 . ILE   B  1 776 ? 53.837 35.697  -37.869 0.00 47.12  ? 802  ILE   B HD13 1 
ATOM   23946 N N    . CYS   B  1 777 ? 53.717 39.489  -33.454 1.00 34.26  ? 803  CYS   B N    1 
ATOM   23947 C CA   . CYS   B  1 777 ? 52.748 40.333  -32.772 1.00 35.69  ? 803  CYS   B CA   1 
ATOM   23948 C C    . CYS   B  1 777 ? 51.340 39.895  -33.188 1.00 36.54  ? 803  CYS   B C    1 
ATOM   23949 O O    . CYS   B  1 777 ? 51.041 39.867  -34.380 1.00 36.77  ? 803  CYS   B O    1 
ATOM   23950 C CB   . CYS   B  1 777 ? 52.954 41.802  -33.141 1.00 36.78  ? 803  CYS   B CB   1 
ATOM   23951 S SG   . CYS   B  1 777 ? 54.623 42.439  -32.864 1.00 41.31  ? 803  CYS   B SG   1 
ATOM   23952 H H    . CYS   B  1 777 ? 54.118 39.945  -34.268 0.00 47.57  ? 803  CYS   B H    1 
ATOM   23953 H HA   . CYS   B  1 777 ? 52.860 40.228  -31.694 0.00 50.00  ? 803  CYS   B HA   1 
ATOM   23954 H HB2  . CYS   B  1 777 ? 52.730 41.931  -34.199 0.00 51.84  ? 803  CYS   B HB2  1 
ATOM   23955 H HB3  . CYS   B  1 777 ? 52.270 42.406  -32.548 0.00 52.49  ? 803  CYS   B HB3  1 
ATOM   23956 N N    . ALA   B  1 778 ? 50.461 39.656  -32.223 1.00 36.92  ? 804  ALA   B N    1 
ATOM   23957 C CA   . ALA   B  1 778 ? 49.039 39.399  -32.485 1.00 37.74  ? 804  ALA   B CA   1 
ATOM   23958 C C    . ALA   B  1 778 ? 48.217 40.698  -32.348 1.00 38.81  ? 804  ALA   B C    1 
ATOM   23959 O O    . ALA   B  1 778 ? 47.114 40.765  -32.880 1.00 38.33  ? 804  ALA   B O    1 
ATOM   23960 C CB   . ALA   B  1 778 ? 48.503 38.362  -31.521 1.00 37.65  ? 804  ALA   B CB   1 
ATOM   23961 H H    . ALA   B  1 778 ? 50.699 39.639  -31.237 0.00 51.27  ? 804  ALA   B H    1 
ATOM   23962 H HA   . ALA   B  1 778 ? 48.894 39.008  -33.491 0.00 51.51  ? 804  ALA   B HA   1 
ATOM   23963 H HB1  . ALA   B  1 778 ? 47.425 38.282  -31.655 0.00 51.44  ? 804  ALA   B HB1  1 
ATOM   23964 H HB2  . ALA   B  1 778 ? 48.975 37.407  -31.745 0.00 50.81  ? 804  ALA   B HB2  1 
ATOM   23965 H HB3  . ALA   B  1 778 ? 48.728 38.665  -30.499 0.00 51.82  ? 804  ALA   B HB3  1 
ATOM   23966 N N    . SER   B  1 779 ? 48.740 41.715  -31.618 1.00 40.44  ? 805  SER   B N    1 
ATOM   23967 C CA   . SER   B  1 779 ? 48.066 42.989  -31.380 1.00 42.22  ? 805  SER   B CA   1 
ATOM   23968 C C    . SER   B  1 779 ? 49.099 44.093  -31.103 1.00 43.47  ? 805  SER   B C    1 
ATOM   23969 O O    . SER   B  1 779 ? 50.183 43.777  -30.618 1.00 43.85  ? 805  SER   B O    1 
ATOM   23970 C CB   . SER   B  1 779 ? 47.148 42.856  -30.166 1.00 44.61  ? 805  SER   B CB   1 
ATOM   23971 O OG   . SER   B  1 779 ? 47.865 42.691  -28.954 1.00 49.01  ? 805  SER   B OG   1 
ATOM   23972 H H    . SER   B  1 779 ? 49.638 41.669  -31.148 0.00 56.80  ? 805  SER   B H    1 
ATOM   23973 H HA   . SER   B  1 779 ? 47.468 43.259  -32.249 0.00 59.89  ? 805  SER   B HA   1 
ATOM   23974 H HB2  . SER   B  1 779 ? 46.533 43.748  -30.061 0.00 63.64  ? 805  SER   B HB2  1 
ATOM   23975 H HB3  . SER   B  1 779 ? 46.511 41.984  -30.301 0.00 62.42  ? 805  SER   B HB3  1 
ATOM   23976 H HG   . SER   B  1 779 ? 48.353 41.826  -28.956 0.00 67.77  ? 805  SER   B HG   1 
ATOM   23977 N N    . PRO   B  1 780 ? 48.778 45.394  -31.298 1.00 43.89  ? 806  PRO   B N    1 
ATOM   23978 C CA   . PRO   B  1 780 ? 47.562 45.941  -31.928 1.00 44.13  ? 806  PRO   B CA   1 
ATOM   23979 C C    . PRO   B  1 780 ? 47.532 45.663  -33.441 1.00 44.84  ? 806  PRO   B C    1 
ATOM   23980 O O    . PRO   B  1 780 ? 48.469 45.077  -33.992 1.00 45.06  ? 806  PRO   B O    1 
ATOM   23981 C CB   . PRO   B  1 780 ? 47.645 47.432  -31.577 1.00 44.75  ? 806  PRO   B CB   1 
ATOM   23982 C CG   . PRO   B  1 780 ? 49.110 47.718  -31.531 1.00 45.14  ? 806  PRO   B CG   1 
ATOM   23983 C CD   . PRO   B  1 780 ? 49.763 46.459  -31.013 1.00 43.44  ? 806  PRO   B CD   1 
ATOM   23984 H HA   . PRO   B  1 780 ? 46.661 45.530  -31.477 0.00 63.96  ? 806  PRO   B HA   1 
ATOM   23985 H HB2  . PRO   B  1 780 ? 47.160 48.026  -32.350 0.00 66.27  ? 806  PRO   B HB2  1 
ATOM   23986 H HB3  . PRO   B  1 780 ? 47.183 47.610  -30.607 0.00 66.34  ? 806  PRO   B HB3  1 
ATOM   23987 H HG2  . PRO   B  1 780 ? 49.466 47.952  -32.533 0.00 66.46  ? 806  PRO   B HG2  1 
ATOM   23988 H HG3  . PRO   B  1 780 ? 49.297 48.552  -30.855 0.00 67.30  ? 806  PRO   B HG3  1 
ATOM   23989 H HD2  . PRO   B  1 780 ? 50.694 46.272  -31.545 0.00 63.37  ? 806  PRO   B HD2  1 
ATOM   23990 H HD3  . PRO   B  1 780 ? 49.934 46.540  -29.941 0.00 63.98  ? 806  PRO   B HD3  1 
ATOM   23991 N N    . GLY   B  1 781 ? 46.447 46.056  -34.102 1.00 45.06  ? 807  GLY   B N    1 
ATOM   23992 C CA   . GLY   B  1 781 ? 46.265 45.833  -35.536 1.00 45.68  ? 807  GLY   B CA   1 
ATOM   23993 C C    . GLY   B  1 781 ? 47.421 46.273  -36.413 1.00 46.18  ? 807  GLY   B C    1 
ATOM   23994 O O    . GLY   B  1 781 ? 47.834 45.540  -37.310 1.00 46.23  ? 807  GLY   B O    1 
ATOM   23995 H H    . GLY   B  1 781 ? 45.667 46.538  -33.667 0.00 65.45  ? 807  GLY   B H    1 
ATOM   23996 H HA2  . GLY   B  1 781 ? 46.099 44.771  -35.708 0.00 64.57  ? 807  GLY   B HA2  1 
ATOM   23997 H HA3  . GLY   B  1 781 ? 45.375 46.370  -35.864 0.00 65.75  ? 807  GLY   B HA3  1 
ATOM   23998 N N    . ASP   B  1 782 ? 47.955 47.468  -36.156 1.00 46.58  ? 808  ASP   B N    1 
ATOM   23999 C CA   . ASP   B  1 782 ? 49.089 48.007  -36.921 1.00 47.41  ? 808  ASP   B CA   1 
ATOM   24000 C C    . ASP   B  1 782 ? 50.386 47.171  -36.829 1.00 47.07  ? 808  ASP   B C    1 
ATOM   24001 O O    . ASP   B  1 782 ? 51.226 47.277  -37.725 1.00 47.02  ? 808  ASP   B O    1 
ATOM   24002 C CB   . ASP   B  1 782 ? 49.376 49.460  -36.514 1.00 50.30  ? 808  ASP   B CB   1 
ATOM   24003 C CG   . ASP   B  1 782 ? 49.500 49.683  -35.018 1.00 57.66  ? 808  ASP   B CG   1 
ATOM   24004 O OD1  . ASP   B  1 782 ? 48.464 49.598  -34.318 1.00 59.23  ? 808  ASP   B OD1  1 
ATOM   24005 O OD2  . ASP   B  1 782 ? 50.628 49.963  -34.549 1.00 60.46  ? 808  ASP   B OD2  1 
ATOM   24006 H H    . ASP   B  1 782 ? 47.583 48.092  -35.448 0.00 67.89  ? 808  ASP   B H    1 
ATOM   24007 H HA   . ASP   B  1 782 ? 48.801 48.026  -37.971 0.00 68.35  ? 808  ASP   B HA   1 
ATOM   24008 H HB2  . ASP   B  1 782 ? 50.314 49.771  -36.972 0.00 73.14  ? 808  ASP   B HB2  1 
ATOM   24009 H HB3  . ASP   B  1 782 ? 48.565 50.091  -36.875 0.00 73.54  ? 808  ASP   B HB3  1 
ATOM   24010 N N    . GLN   B  1 783 ? 50.551 46.357  -35.761 1.00 46.30  ? 809  GLN   B N    1 
ATOM   24011 C CA   . GLN   B  1 783 ? 51.738 45.519  -35.568 1.00 45.91  ? 809  GLN   B CA   1 
ATOM   24012 C C    . GLN   B  1 783 ? 51.511 44.036  -35.886 1.00 45.50  ? 809  GLN   B C    1 
ATOM   24013 O O    . GLN   B  1 783 ? 52.487 43.293  -35.960 1.00 45.24  ? 809  GLN   B O    1 
ATOM   24014 C CB   . GLN   B  1 783 ? 52.266 45.659  -34.129 1.00 46.99  ? 809  GLN   B CB   1 
ATOM   24015 C CG   . GLN   B  1 783 ? 52.569 47.097  -33.709 1.00 49.22  ? 809  GLN   B CG   1 
ATOM   24016 C CD   . GLN   B  1 783 ? 53.591 47.758  -34.608 1.00 52.26  ? 809  GLN   B CD   1 
ATOM   24017 O OE1  . GLN   B  1 783 ? 54.531 47.118  -35.097 1.00 52.99  ? 809  GLN   B OE1  1 
ATOM   24018 N NE2  . GLN   B  1 783 ? 53.442 49.052  -34.843 1.00 52.39  ? 809  GLN   B NE2  1 
ATOM   24019 H H    . GLN   B  1 783 ? 49.883 46.265  -35.003 0.00 66.14  ? 809  GLN   B H    1 
ATOM   24020 H HA   . GLN   B  1 783 ? 52.529 45.852  -36.237 0.00 65.03  ? 809  GLN   B HA   1 
ATOM   24021 H HB2  . GLN   B  1 783 ? 51.515 45.258  -33.450 0.00 66.49  ? 809  GLN   B HB2  1 
ATOM   24022 H HB3  . GLN   B  1 783 ? 53.184 45.081  -34.034 0.00 66.21  ? 809  GLN   B HB3  1 
ATOM   24023 H HG2  . GLN   B  1 783 ? 51.648 47.677  -33.732 0.00 70.81  ? 809  GLN   B HG2  1 
ATOM   24024 H HG3  . GLN   B  1 783 ? 52.973 47.088  -32.697 0.00 70.57  ? 809  GLN   B HG3  1 
ATOM   24025 H HE21 . GLN   B  1 783 ? 52.675 49.570  -34.426 0.00 75.86  ? 809  GLN   B HE21 1 
ATOM   24026 H HE22 . GLN   B  1 783 ? 54.106 49.533  -35.441 0.00 75.61  ? 809  GLN   B HE22 1 
ATOM   24027 N N    . ARG   B  1 784 ? 50.250 43.601  -36.068 1.00 45.30  ? 810  ARG   B N    1 
ATOM   24028 C CA   . ARG   B  1 784 ? 49.919 42.206  -36.383 1.00 45.70  ? 810  ARG   B CA   1 
ATOM   24029 C C    . ARG   B  1 784 ? 50.716 41.667  -37.586 1.00 44.44  ? 810  ARG   B C    1 
ATOM   24030 O O    . ARG   B  1 784 ? 50.890 42.373  -38.580 1.00 44.77  ? 810  ARG   B O    1 
ATOM   24031 C CB   . ARG   B  1 784 ? 48.401 42.067  -36.609 1.00 48.27  ? 810  ARG   B CB   1 
ATOM   24032 C CG   . ARG   B  1 784 ? 47.930 40.711  -37.156 1.00 53.28  ? 810  ARG   B CG   1 
ATOM   24033 C CD   . ARG   B  1 784 ? 46.604 40.211  -36.586 1.00 58.13  ? 810  ARG   B CD   1 
ATOM   24034 N NE   . ARG   B  1 784 ? 45.583 41.250  -36.391 1.00 62.94  ? 810  ARG   B NE   1 
ATOM   24035 C CZ   . ARG   B  1 784 ? 44.406 41.046  -35.804 1.00 66.43  ? 810  ARG   B CZ   1 
ATOM   24036 N NH1  . ARG   B  1 784 ? 43.547 42.047  -35.658 1.00 66.41  ? 810  ARG   B NH1  1 
ATOM   24037 N NH2  . ARG   B  1 784 ? 44.079 39.844  -35.353 1.00 67.08  ? 810  ARG   B NH2  1 
ATOM   24038 H H    . ARG   B  1 784 ? 49.430 44.193  -35.979 0.00 63.38  ? 810  ARG   B H    1 
ATOM   24039 H HA   . ARG   B  1 784 ? 50.173 41.603  -35.513 0.00 62.20  ? 810  ARG   B HA   1 
ATOM   24040 H HB2  . ARG   B  1 784 ? 47.906 42.233  -35.653 0.00 65.83  ? 810  ARG   B HB2  1 
ATOM   24041 H HB3  . ARG   B  1 784 ? 48.084 42.828  -37.321 0.00 65.96  ? 810  ARG   B HB3  1 
ATOM   24042 H HG2  . ARG   B  1 784 ? 47.818 40.789  -38.236 0.00 70.59  ? 810  ARG   B HG2  1 
ATOM   24043 H HG3  . ARG   B  1 784 ? 48.672 39.951  -36.915 0.00 70.18  ? 810  ARG   B HG3  1 
ATOM   24044 H HD2  . ARG   B  1 784 ? 46.191 39.468  -37.265 0.00 75.92  ? 810  ARG   B HD2  1 
ATOM   24045 H HD3  . ARG   B  1 784 ? 46.796 39.754  -35.617 0.00 76.26  ? 810  ARG   B HD3  1 
ATOM   24046 H HE   . ARG   B  1 784 ? 45.783 42.187  -36.725 0.00 83.49  ? 810  ARG   B HE   1 
ATOM   24047 H HH11 . ARG   B  1 784 ? 43.776 42.977  -35.993 0.00 88.55  ? 810  ARG   B HH11 1 
ATOM   24048 H HH12 . ARG   B  1 784 ? 42.652 41.888  -35.207 0.00 88.14  ? 810  ARG   B HH12 1 
ATOM   24049 H HH21 . ARG   B  1 784 ? 44.713 39.057  -35.439 0.00 86.87  ? 810  ARG   B HH21 1 
ATOM   24050 H HH22 . ARG   B  1 784 ? 43.180 39.720  -34.899 0.00 87.56  ? 810  ARG   B HH22 1 
ATOM   24051 N N    . GLY   B  1 785 ? 51.238 40.449  -37.445 1.00 42.84  ? 811  GLY   B N    1 
ATOM   24052 C CA   . GLY   B  1 785 ? 52.040 39.794  -38.472 1.00 41.57  ? 811  GLY   B CA   1 
ATOM   24053 C C    . GLY   B  1 785 ? 53.532 40.072  -38.398 1.00 40.09  ? 811  GLY   B C    1 
ATOM   24054 O O    . GLY   B  1 785 ? 54.326 39.308  -38.953 1.00 40.58  ? 811  GLY   B O    1 
ATOM   24055 H H    . GLY   B  1 785 ? 51.119 39.873  -36.617 0.00 57.49  ? 811  GLY   B H    1 
ATOM   24056 H HA2  . GLY   B  1 785 ? 51.904 38.718  -38.379 0.00 55.01  ? 811  GLY   B HA2  1 
ATOM   24057 H HA3  . GLY   B  1 785 ? 51.689 40.085  -39.461 0.00 55.69  ? 811  GLY   B HA3  1 
ATOM   24058 N N    . LYS   B  1 786 ? 53.940 41.157  -37.734 1.00 38.50  ? 812  LYS   B N    1 
ATOM   24059 C CA   . LYS   B  1 786 ? 55.355 41.524  -37.641 1.00 37.96  ? 812  LYS   B CA   1 
ATOM   24060 C C    . LYS   B  1 786 ? 56.058 40.825  -36.489 1.00 36.97  ? 812  LYS   B C    1 
ATOM   24061 O O    . LYS   B  1 786 ? 55.413 40.438  -35.520 1.00 36.85  ? 812  LYS   B O    1 
ATOM   24062 C CB   . LYS   B  1 786 ? 55.489 43.041  -37.449 1.00 40.30  ? 812  LYS   B CB   1 
ATOM   24063 C CG   . LYS   B  1 786 ? 54.872 43.870  -38.568 1.00 45.90  ? 812  LYS   B CG   1 
ATOM   24064 C CD   . LYS   B  1 786 ? 55.078 45.361  -38.325 1.00 51.69  ? 812  LYS   B CD   1 
ATOM   24065 C CE   . LYS   B  1 786 ? 54.798 46.178  -39.561 1.00 56.97  ? 812  LYS   B CE   1 
ATOM   24066 N NZ   . LYS   B  1 786 ? 56.033 46.393  -40.371 1.00 60.25  ? 812  LYS   B NZ   1 
ATOM   24067 H H    . LYS   B  1 786 ? 53.328 41.811  -37.256 0.00 53.30  ? 812  LYS   B H    1 
ATOM   24068 H HA   . LYS   B  1 786 ? 55.871 41.266  -38.565 0.00 52.10  ? 812  LYS   B HA   1 
ATOM   24069 H HB2  . LYS   B  1 786 ? 55.001 43.323  -36.518 0.00 56.53  ? 812  LYS   B HB2  1 
ATOM   24070 H HB3  . LYS   B  1 786 ? 56.548 43.290  -37.397 0.00 56.37  ? 812  LYS   B HB3  1 
ATOM   24071 H HG2  . LYS   B  1 786 ? 55.345 43.608  -39.513 0.00 62.97  ? 812  LYS   B HG2  1 
ATOM   24072 H HG3  . LYS   B  1 786 ? 53.801 43.682  -38.616 0.00 63.15  ? 812  LYS   B HG3  1 
ATOM   24073 H HD2  . LYS   B  1 786 ? 54.408 45.697  -37.536 0.00 71.61  ? 812  LYS   B HD2  1 
ATOM   24074 H HD3  . LYS   B  1 786 ? 56.112 45.534  -38.031 0.00 71.43  ? 812  LYS   B HD3  1 
ATOM   24075 H HE2  . LYS   B  1 786 ? 54.073 45.652  -40.180 0.00 77.55  ? 812  LYS   B HE2  1 
ATOM   24076 H HE3  . LYS   B  1 786 ? 54.408 47.151  -39.268 0.00 78.71  ? 812  LYS   B HE3  1 
ATOM   24077 H HZ1  . LYS   B  1 786 ? 55.804 46.894  -41.224 0.00 82.20  ? 812  LYS   B HZ1  1 
ATOM   24078 H HZ2  . LYS   B  1 786 ? 56.706 46.938  -39.841 0.00 82.41  ? 812  LYS   B HZ2  1 
ATOM   24079 H HZ3  . LYS   B  1 786 ? 56.449 45.499  -40.613 0.00 81.32  ? 812  LYS   B HZ3  1 
ATOM   24080 N N    . SER   B  1 787 ? 57.386 40.700  -36.569 1.00 36.31  ? 813  SER   B N    1 
ATOM   24081 C CA   . SER   B  1 787 ? 58.163 40.125  -35.475 1.00 36.33  ? 813  SER   B CA   1 
ATOM   24082 C C    . SER   B  1 787 ? 58.222 41.136  -34.317 1.00 36.85  ? 813  SER   B C    1 
ATOM   24083 O O    . SER   B  1 787 ? 58.184 42.347  -34.545 1.00 36.76  ? 813  SER   B O    1 
ATOM   24084 C CB   . SER   B  1 787 ? 59.579 39.790  -35.934 1.00 36.33  ? 813  SER   B CB   1 
ATOM   24085 O OG   . SER   B  1 787 ? 60.356 39.254  -34.874 1.00 36.58  ? 813  SER   B OG   1 
ATOM   24086 H H    . SER   B  1 787 ? 57.942 40.983  -37.369 0.00 50.19  ? 813  SER   B H    1 
ATOM   24087 H HA   . SER   B  1 787 ? 57.688 39.210  -35.124 0.00 49.56  ? 813  SER   B HA   1 
ATOM   24088 H HB2  . SER   B  1 787 ? 59.525 39.058  -36.738 0.00 49.28  ? 813  SER   B HB2  1 
ATOM   24089 H HB3  . SER   B  1 787 ? 60.057 40.700  -36.294 0.00 50.37  ? 813  SER   B HB3  1 
ATOM   24090 H HG   . SER   B  1 787 ? 59.794 38.710  -34.263 0.00 49.73  ? 813  SER   B HG   1 
ATOM   24091 N N    . ILE   B  1 788 ? 58.319 40.640  -33.079 1.00 36.97  ? 814  ILE   B N    1 
ATOM   24092 C CA   . ILE   B  1 788 ? 58.409 41.515  -31.905 1.00 37.73  ? 814  ILE   B CA   1 
ATOM   24093 C C    . ILE   B  1 788 ? 59.657 42.416  -31.946 1.00 39.21  ? 814  ILE   B C    1 
ATOM   24094 O O    . ILE   B  1 788 ? 59.659 43.471  -31.318 1.00 39.24  ? 814  ILE   B O    1 
ATOM   24095 C CB   . ILE   B  1 788 ? 58.349 40.714  -30.579 1.00 37.76  ? 814  ILE   B CB   1 
ATOM   24096 C CG1  . ILE   B  1 788 ? 59.594 39.817  -30.386 1.00 38.34  ? 814  ILE   B CG1  1 
ATOM   24097 C CG2  . ILE   B  1 788 ? 57.056 39.907  -30.497 1.00 38.00  ? 814  ILE   B CG2  1 
ATOM   24098 C CD1  . ILE   B  1 788 ? 59.746 39.278  -28.963 1.00 39.76  ? 814  ILE   B CD1  1 
ATOM   24099 H H    . ILE   B  1 788 ? 58.355 39.646  -32.877 0.00 51.09  ? 814  ILE   B H    1 
ATOM   24100 H HA   . ILE   B  1 788 ? 57.543 42.175  -31.915 0.00 53.72  ? 814  ILE   B HA   1 
ATOM   24101 H HB   . ILE   B  1 788 ? 58.338 41.435  -29.763 0.00 53.89  ? 814  ILE   B HB   1 
ATOM   24102 H HG12 . ILE   B  1 788 ? 59.515 38.964  -31.058 0.00 52.85  ? 814  ILE   B HG12 1 
ATOM   24103 H HG13 . ILE   B  1 788 ? 60.506 40.370  -30.606 0.00 53.89  ? 814  ILE   B HG13 1 
ATOM   24104 H HG21 . ILE   B  1 788 ? 56.932 39.530  -29.483 0.00 52.99  ? 814  ILE   B HG21 1 
ATOM   24105 H HG22 . ILE   B  1 788 ? 56.219 40.553  -30.757 0.00 53.26  ? 814  ILE   B HG22 1 
ATOM   24106 H HG23 . ILE   B  1 788 ? 57.113 39.074  -31.195 0.00 52.31  ? 814  ILE   B HG23 1 
ATOM   24107 H HD11 . ILE   B  1 788 ? 60.701 38.761  -28.882 0.00 55.15  ? 814  ILE   B HD11 1 
ATOM   24108 H HD12 . ILE   B  1 788 ? 59.712 40.111  -28.263 0.00 56.03  ? 814  ILE   B HD12 1 
ATOM   24109 H HD13 . ILE   B  1 788 ? 58.933 38.583  -28.756 0.00 54.91  ? 814  ILE   B HD13 1 
ATOM   24110 N N    . VAL   B  1 789 ? 60.710 41.991  -32.677 1.00 40.30  ? 815  VAL   B N    1 
ATOM   24111 C CA   . VAL   B  1 789 ? 61.959 42.737  -32.829 1.00 42.18  ? 815  VAL   B CA   1 
ATOM   24112 C C    . VAL   B  1 789 ? 61.795 43.983  -33.752 1.00 44.15  ? 815  VAL   B C    1 
ATOM   24113 O O    . VAL   B  1 789 ? 62.730 44.767  -33.859 1.00 44.10  ? 815  VAL   B O    1 
ATOM   24114 C CB   . VAL   B  1 789 ? 63.111 41.774  -33.291 1.00 43.09  ? 815  VAL   B CB   1 
ATOM   24115 C CG1  . VAL   B  1 789 ? 62.988 41.428  -34.771 1.00 43.28  ? 815  VAL   B CG1  1 
ATOM   24116 C CG2  . VAL   B  1 789 ? 64.490 42.359  -32.994 1.00 44.22  ? 815  VAL   B CG2  1 
ATOM   24117 H H    . VAL   B  1 789 ? 60.733 41.104  -33.168 0.00 56.09  ? 815  VAL   B H    1 
ATOM   24118 H HA   . VAL   B  1 789 ? 62.218 43.118  -31.842 0.00 60.11  ? 815  VAL   B HA   1 
ATOM   24119 H HB   . VAL   B  1 789 ? 63.058 40.838  -32.737 0.00 59.64  ? 815  VAL   B HB   1 
ATOM   24120 H HG11 . VAL   B  1 789 ? 63.573 40.531  -34.970 0.00 59.24  ? 815  VAL   B HG11 1 
ATOM   24121 H HG12 . VAL   B  1 789 ? 61.941 41.253  -35.012 0.00 59.49  ? 815  VAL   B HG12 1 
ATOM   24122 H HG13 . VAL   B  1 789 ? 63.377 42.252  -35.368 0.00 60.20  ? 815  VAL   B HG13 1 
ATOM   24123 H HG21 . VAL   B  1 789 ? 65.249 41.635  -33.286 0.00 61.68  ? 815  VAL   B HG21 1 
ATOM   24124 H HG22 . VAL   B  1 789 ? 64.618 43.278  -33.564 0.00 62.56  ? 815  VAL   B HG22 1 
ATOM   24125 H HG23 . VAL   B  1 789 ? 64.564 42.567  -31.928 0.00 62.50  ? 815  VAL   B HG23 1 
ATOM   24126 N N    . SER   B  1 790 ? 60.616 44.178  -34.394 1.00 45.82  ? 816  SER   B N    1 
ATOM   24127 C CA   . SER   B  1 790 ? 60.312 45.358  -35.220 1.00 47.88  ? 816  SER   B CA   1 
ATOM   24128 C C    . SER   B  1 790 ? 59.600 46.426  -34.354 1.00 49.45  ? 816  SER   B C    1 
ATOM   24129 O O    . SER   B  1 790 ? 59.070 46.097  -33.294 1.00 49.54  ? 816  SER   B O    1 
ATOM   24130 C CB   . SER   B  1 790 ? 59.428 44.962  -36.397 1.00 49.55  ? 816  SER   B CB   1 
ATOM   24131 O OG   . SER   B  1 790 ? 60.074 43.966  -37.174 1.00 52.64  ? 816  SER   B OG   1 
ATOM   24132 H H    . SER   B  1 790 ? 59.839 43.526  -34.371 0.00 63.87  ? 816  SER   B H    1 
ATOM   24133 H HA   . SER   B  1 790 ? 61.226 45.792  -35.621 0.00 67.73  ? 816  SER   B HA   1 
ATOM   24134 H HB2  . SER   B  1 790 ? 58.485 44.567  -36.022 0.00 68.64  ? 816  SER   B HB2  1 
ATOM   24135 H HB3  . SER   B  1 790 ? 59.247 45.837  -37.019 0.00 69.36  ? 816  SER   B HB3  1 
ATOM   24136 H HG   . SER   B  1 790 ? 59.502 43.711  -37.944 0.00 71.49  ? 816  SER   B HG   1 
ATOM   24137 N N    . LEU   B  1 791 ? 59.574 47.696  -34.795 1.00 50.79  ? 817  LEU   B N    1 
ATOM   24138 C CA   . LEU   B  1 791 ? 58.993 48.811  -34.003 1.00 52.51  ? 817  LEU   B CA   1 
ATOM   24139 C C    . LEU   B  1 791 ? 59.921 49.083  -32.796 1.00 52.55  ? 817  LEU   B C    1 
ATOM   24140 O O    . LEU   B  1 791 ? 60.205 48.155  -32.036 1.00 52.07  ? 817  LEU   B O    1 
ATOM   24141 C CB   . LEU   B  1 791 ? 57.498 48.552  -33.573 1.00 53.88  ? 817  LEU   B CB   1 
ATOM   24142 C CG   . LEU   B  1 791 ? 57.138 48.357  -32.055 1.00 56.54  ? 817  LEU   B CG   1 
ATOM   24143 C CD1  . LEU   B  1 791 ? 56.980 49.682  -31.354 1.00 57.31  ? 817  LEU   B CD1  1 
ATOM   24144 C CD2  . LEU   B  1 791 ? 55.863 47.574  -31.883 1.00 57.57  ? 817  LEU   B CD2  1 
ATOM   24145 H H    . LEU   B  1 791 ? 59.940 47.989  -35.695 0.00 72.65  ? 817  LEU   B H    1 
ATOM   24146 H HA   . LEU   B  1 791 ? 58.992 49.703  -34.627 0.00 76.15  ? 817  LEU   B HA   1 
ATOM   24147 H HB2  . LEU   B  1 791 ? 56.920 49.412  -33.908 0.00 77.68  ? 817  LEU   B HB2  1 
ATOM   24148 H HB3  . LEU   B  1 791 ? 57.133 47.672  -34.101 0.00 76.35  ? 817  LEU   B HB3  1 
ATOM   24149 H HG   . LEU   B  1 791 ? 57.921 47.791  -31.552 0.00 80.19  ? 817  LEU   B HG   1 
ATOM   24150 H HD11 . LEU   B  1 791 ? 56.786 49.502  -30.297 0.00 82.65  ? 817  LEU   B HD11 1 
ATOM   24151 H HD12 . LEU   B  1 791 ? 57.898 50.256  -31.471 0.00 83.00  ? 817  LEU   B HD12 1 
ATOM   24152 H HD13 . LEU   B  1 791 ? 56.144 50.222  -31.797 0.00 82.84  ? 817  LEU   B HD13 1 
ATOM   24153 H HD21 . LEU   B  1 791 ? 55.656 47.465  -30.819 0.00 81.29  ? 817  LEU   B HD21 1 
ATOM   24154 H HD22 . LEU   B  1 791 ? 55.049 48.111  -32.368 0.00 81.41  ? 817  LEU   B HD22 1 
ATOM   24155 H HD23 . LEU   B  1 791 ? 55.984 46.591  -32.337 0.00 80.32  ? 817  LEU   B HD23 1 
ATOM   24156 N N    . GLU   B  1 792 ? 60.401 50.330  -32.624 1.00 53.02  ? 818  GLU   B N    1 
ATOM   24157 C CA   . GLU   B  1 792 ? 61.298 50.639  -31.507 1.00 53.63  ? 818  GLU   B CA   1 
ATOM   24158 C C    . GLU   B  1 792 ? 60.551 51.405  -30.437 1.00 53.60  ? 818  GLU   B C    1 
ATOM   24159 O O    . GLU   B  1 792 ? 60.775 51.179  -29.247 1.00 53.64  ? 818  GLU   B O    1 
ATOM   24160 C CB   . GLU   B  1 792 ? 62.578 51.366  -31.971 1.00 56.67  ? 818  GLU   B CB   1 
ATOM   24161 C CG   . GLU   B  1 792 ? 62.367 52.709  -32.654 1.00 62.56  ? 818  GLU   B CG   1 
ATOM   24162 C CD   . GLU   B  1 792 ? 63.657 53.368  -33.100 1.00 69.11  ? 818  GLU   B CD   1 
ATOM   24163 O OE1  . GLU   B  1 792 ? 64.233 52.916  -34.116 1.00 70.21  ? 818  GLU   B OE1  1 
ATOM   24164 O OE2  . GLU   B  1 792 ? 64.090 54.339  -32.436 1.00 71.24  ? 818  GLU   B OE2  1 
ATOM   24165 H H    . GLU   B  1 792 ? 60.169 51.122  -33.214 0.00 78.27  ? 818  GLU   B H    1 
ATOM   24166 H HA   . GLU   B  1 792 ? 61.644 49.713  -31.050 0.00 78.64  ? 818  GLU   B HA   1 
ATOM   24167 H HB2  . GLU   B  1 792 ? 63.209 51.539  -31.101 0.00 83.86  ? 818  GLU   B HB2  1 
ATOM   24168 H HB3  . GLU   B  1 792 ? 63.101 50.722  -32.676 0.00 82.76  ? 818  GLU   B HB3  1 
ATOM   24169 H HG2  . GLU   B  1 792 ? 61.747 52.563  -33.537 0.00 90.91  ? 818  GLU   B HG2  1 
ATOM   24170 H HG3  . GLU   B  1 792 ? 61.876 53.393  -31.964 0.00 92.02  ? 818  GLU   B HG3  1 
HETATM 24171 C C1   . NAG   C  2 .   ? 20.472 -4.065  -15.082 1.00 21.49  ? 1    NAG   C C1   1 
HETATM 24172 C C2   . NAG   C  2 .   ? 21.309 -2.857  -15.520 1.00 21.68  ? 1    NAG   C C2   1 
HETATM 24173 C C3   . NAG   C  2 .   ? 20.413 -1.645  -15.777 1.00 22.49  ? 1    NAG   C C3   1 
HETATM 24174 C C4   . NAG   C  2 .   ? 19.276 -2.000  -16.733 1.00 23.25  ? 1    NAG   C C4   1 
HETATM 24175 C C5   . NAG   C  2 .   ? 18.549 -3.249  -16.243 1.00 22.91  ? 1    NAG   C C5   1 
HETATM 24176 C C6   . NAG   C  2 .   ? 17.471 -3.737  -17.189 1.00 23.06  ? 1    NAG   C C6   1 
HETATM 24177 C C7   . NAG   C  2 .   ? 23.551 -2.282  -14.675 1.00 21.05  ? 1    NAG   C C7   1 
HETATM 24178 C C8   . NAG   C  2 .   ? 24.313 -1.747  -13.501 1.00 21.03  ? 1    NAG   C C8   1 
HETATM 24179 N N2   . NAG   C  2 .   ? 22.261 -2.554  -14.460 1.00 20.94  ? 1    NAG   C N2   1 
HETATM 24180 O O3   . NAG   C  2 .   ? 21.250 -0.608  -16.297 1.00 22.10  ? 1    NAG   C O3   1 
HETATM 24181 O O4   . NAG   C  2 .   ? 18.319 -0.944  -16.803 1.00 25.03  ? 1    NAG   C O4   1 
HETATM 24182 O O5   . NAG   C  2 .   ? 19.489 -4.319  -16.094 1.00 22.25  ? 1    NAG   C O5   1 
HETATM 24183 O O6   . NAG   C  2 .   ? 17.990 -4.003  -18.488 1.00 23.92  ? 1    NAG   C O6   1 
HETATM 24184 O O7   . NAG   C  2 .   ? 24.076 -2.437  -15.771 1.00 21.55  ? 1    NAG   C O7   1 
HETATM 24185 H H2   . NAG   C  2 .   ? 21.820 -3.120  -16.444 0.00 23.35  ? 1    NAG   C H2   1 
HETATM 24186 H H3   . NAG   C  2 .   ? 19.976 -1.303  -14.840 0.00 24.98  ? 1    NAG   C H3   1 
HETATM 24187 H H4   . NAG   C  2 .   ? 19.715 -2.207  -17.708 0.00 25.50  ? 1    NAG   C H4   1 
HETATM 24188 H H5   . NAG   C  2 .   ? 18.084 -3.047  -15.279 0.00 25.87  ? 1    NAG   C H5   1 
HETATM 24189 H H61  . NAG   C  2 .   ? 16.727 -2.962  -17.363 0.00 26.10  ? 1    NAG   C H61  1 
HETATM 24190 H H62  . NAG   C  2 .   ? 16.949 -4.604  -16.786 0.00 26.17  ? 1    NAG   C H62  1 
HETATM 24191 H H81  . NAG   C  2 .   ? 25.109 -1.057  -13.776 0.00 22.49  ? 1    NAG   C H81  1 
HETATM 24192 H H82  . NAG   C  2 .   ? 24.785 -2.552  -12.941 0.00 22.71  ? 1    NAG   C H82  1 
HETATM 24193 H H83  . NAG   C  2 .   ? 23.665 -1.222  -12.799 0.00 22.91  ? 1    NAG   C H83  1 
HETATM 24194 H HN2  . NAG   C  2 .   ? 21.888 -2.567  -13.515 0.00 22.97  ? 1    NAG   C HN2  1 
HETATM 24195 H HO3  . NAG   C  2 .   ? 20.679 0.204   -16.342 0.00 24.14  ? 1    NAG   C HO3  1 
HETATM 24196 H HO6  . NAG   C  2 .   ? 18.887 -4.415  -18.382 0.00 26.47  ? 1    NAG   C HO6  1 
HETATM 24197 C C1   . NAG   C  2 .   ? 18.528 0.074   -17.761 1.00 27.08  ? 2    NAG   C C1   1 
HETATM 24198 C C2   . NAG   C  2 .   ? 17.228 0.832   -18.028 1.00 27.42  ? 2    NAG   C C2   1 
HETATM 24199 C C3   . NAG   C  2 .   ? 17.504 1.861   -19.126 1.00 28.77  ? 2    NAG   C C3   1 
HETATM 24200 C C4   . NAG   C  2 .   ? 18.649 2.785   -18.723 1.00 30.96  ? 2    NAG   C C4   1 
HETATM 24201 C C5   . NAG   C  2 .   ? 19.861 1.949   -18.318 1.00 30.34  ? 2    NAG   C C5   1 
HETATM 24202 C C6   . NAG   C  2 .   ? 21.008 2.765   -17.774 1.00 31.19  ? 2    NAG   C C6   1 
HETATM 24203 C C7   . NAG   C  2 .   ? 14.897 0.052   -18.144 1.00 25.19  ? 2    NAG   C C7   1 
HETATM 24204 C C8   . NAG   C  2 .   ? 13.955 -0.898  -18.815 1.00 25.24  ? 2    NAG   C C8   1 
HETATM 24205 N N2   . NAG   C  2 .   ? 16.190 -0.090  -18.460 1.00 26.18  ? 2    NAG   C N2   1 
HETATM 24206 O O3   . NAG   C  2 .   ? 16.322 2.608   -19.382 1.00 27.81  ? 2    NAG   C O3   1 
HETATM 24207 O O4   . NAG   C  2 .   ? 19.038 3.583   -19.836 1.00 33.65  ? 2    NAG   C O4   1 
HETATM 24208 O O5   . NAG   C  2 .   ? 19.484 1.020   -17.289 1.00 28.43  ? 2    NAG   C O5   1 
HETATM 24209 O O6   . NAG   C  2 .   ? 20.609 3.575   -16.680 1.00 31.47  ? 2    NAG   C O6   1 
HETATM 24210 O O7   . NAG   C  2 .   ? 14.505 0.907   -17.357 1.00 24.21  ? 2    NAG   C O7   1 
HETATM 24211 H H2   . NAG   C  2 .   ? 16.935 1.359   -17.121 0.00 31.42  ? 2    NAG   C H2   1 
HETATM 24212 H H3   . NAG   C  2 .   ? 17.782 1.332   -20.037 0.00 32.42  ? 2    NAG   C H3   1 
HETATM 24213 H H4   . NAG   C  2 .   ? 18.313 3.380   -17.874 0.00 35.33  ? 2    NAG   C H4   1 
HETATM 24214 H H5   . NAG   C  2 .   ? 20.236 1.393   -19.177 0.00 33.77  ? 2    NAG   C H5   1 
HETATM 24215 H H61  . NAG   C  2 .   ? 21.351 3.484   -18.518 0.00 34.76  ? 2    NAG   C H61  1 
HETATM 24216 H H62  . NAG   C  2 .   ? 21.857 2.135   -17.512 0.00 34.69  ? 2    NAG   C H62  1 
HETATM 24217 H H81  . NAG   C  2 .   ? 12.916 -0.763  -18.522 0.00 29.82  ? 2    NAG   C H81  1 
HETATM 24218 H H82  . NAG   C  2 .   ? 14.207 -1.930  -18.574 0.00 29.34  ? 2    NAG   C H82  1 
HETATM 24219 H H83  . NAG   C  2 .   ? 14.001 -0.811  -19.900 0.00 29.29  ? 2    NAG   C H83  1 
HETATM 24220 H HN2  . NAG   C  2 .   ? 16.497 -0.872  -19.029 0.00 29.72  ? 2    NAG   C HN2  1 
HETATM 24221 H HO3  . NAG   C  2 .   ? 16.620 3.463   -19.788 0.00 31.81  ? 2    NAG   C HO3  1 
HETATM 24222 H HO6  . NAG   C  2 .   ? 21.394 4.114   -16.400 0.00 35.48  ? 2    NAG   C HO6  1 
HETATM 24223 C C1   . BMA   C  2 .   ? 18.764 4.959   -19.825 1.00 36.45  ? 3    BMA   C C1   1 
HETATM 24224 C C2   . BMA   C  2 .   ? 19.431 5.584   -21.052 1.00 37.69  ? 3    BMA   C C2   1 
HETATM 24225 C C3   . BMA   C  2 .   ? 19.069 7.060   -21.169 1.00 38.88  ? 3    BMA   C C3   1 
HETATM 24226 C C4   . BMA   C  2 .   ? 17.561 7.261   -21.085 1.00 39.99  ? 3    BMA   C C4   1 
HETATM 24227 C C5   . BMA   C  2 .   ? 17.013 6.577   -19.836 1.00 40.35  ? 3    BMA   C C5   1 
HETATM 24228 C C6   . BMA   C  2 .   ? 15.507 6.662   -19.701 1.00 42.77  ? 3    BMA   C C6   1 
HETATM 24229 O O2   . BMA   C  2 .   ? 19.057 4.879   -22.232 1.00 37.72  ? 3    BMA   C O2   1 
HETATM 24230 O O3   . BMA   C  2 .   ? 19.556 7.574   -22.409 1.00 39.22  ? 3    BMA   C O3   1 
HETATM 24231 O O4   . BMA   C  2 .   ? 17.278 8.655   -21.002 1.00 40.68  ? 3    BMA   C O4   1 
HETATM 24232 O O5   . BMA   C  2 .   ? 17.357 5.185   -19.866 1.00 38.05  ? 3    BMA   C O5   1 
HETATM 24233 O O6   . BMA   C  2 .   ? 14.823 6.067   -20.801 1.00 45.51  ? 3    BMA   C O6   1 
HETATM 24234 H H2   . BMA   C  2 .   ? 20.511 5.520   -20.922 0.00 42.68  ? 3    BMA   C H2   1 
HETATM 24235 H H3   . BMA   C  2 .   ? 19.568 7.610   -20.372 0.00 44.72  ? 3    BMA   C H3   1 
HETATM 24236 H H4   . BMA   C  2 .   ? 17.078 6.845   -21.969 0.00 46.49  ? 3    BMA   C H4   1 
HETATM 24237 H H5   . BMA   C  2 .   ? 17.454 7.025   -18.946 0.00 47.16  ? 3    BMA   C H5   1 
HETATM 24238 H H61  . BMA   C  2 .   ? 15.179 7.683   -19.510 0.00 50.83  ? 3    BMA   C H61  1 
HETATM 24239 H H62  . BMA   C  2 .   ? 15.181 6.070   -18.847 0.00 50.65  ? 3    BMA   C H62  1 
HETATM 24240 H HO2  . BMA   C  2 .   ? 19.489 3.987   -22.163 0.00 42.68  ? 3    BMA   C HO2  1 
HETATM 24241 H HO4  . BMA   C  2 .   ? 16.353 8.831   -21.318 0.00 47.95  ? 3    BMA   C HO4  1 
HETATM 24242 C C1   . MAN   C  2 .   ? 20.549 8.588   -22.408 1.00 39.72  ? 4    MAN   C C1   1 
HETATM 24243 C C2   . MAN   C  2 .   ? 20.638 9.222   -23.799 1.00 40.30  ? 4    MAN   C C2   1 
HETATM 24244 C C3   . MAN   C  2 .   ? 21.237 8.244   -24.798 1.00 40.28  ? 4    MAN   C C3   1 
HETATM 24245 C C4   . MAN   C  2 .   ? 22.574 7.724   -24.293 1.00 40.05  ? 4    MAN   C C4   1 
HETATM 24246 C C5   . MAN   C  2 .   ? 22.410 7.119   -22.901 1.00 39.37  ? 4    MAN   C C5   1 
HETATM 24247 C C6   . MAN   C  2 .   ? 23.727 6.726   -22.278 1.00 39.07  ? 4    MAN   C C6   1 
HETATM 24248 O O2   . MAN   C  2 .   ? 21.440 10.399  -23.739 1.00 40.75  ? 4    MAN   C O2   1 
HETATM 24249 O O3   . MAN   C  2 .   ? 21.422 8.881   -26.060 1.00 40.75  ? 4    MAN   C O3   1 
HETATM 24250 O O4   . MAN   C  2 .   ? 23.058 6.726   -25.186 1.00 40.60  ? 4    MAN   C O4   1 
HETATM 24251 O O5   . MAN   C  2 .   ? 21.819 8.076   -22.009 1.00 39.18  ? 4    MAN   C O5   1 
HETATM 24252 O O6   . MAN   C  2 .   ? 24.534 7.868   -22.003 1.00 38.70  ? 4    MAN   C O6   1 
HETATM 24253 H H2   . MAN   C  2 .   ? 19.646 9.518   -24.137 0.00 46.37  ? 4    MAN   C H2   1 
HETATM 24254 H H3   . MAN   C  2 .   ? 20.545 7.422   -24.977 0.00 45.69  ? 4    MAN   C H3   1 
HETATM 24255 H H4   . MAN   C  2 .   ? 23.278 8.554   -24.241 0.00 44.97  ? 4    MAN   C H4   1 
HETATM 24256 H H5   . MAN   C  2 .   ? 21.788 6.226   -22.958 0.00 44.27  ? 4    MAN   C H5   1 
HETATM 24257 H H61  . MAN   C  2 .   ? 24.251 5.986   -22.882 0.00 43.35  ? 4    MAN   C H61  1 
HETATM 24258 H H62  . MAN   C  2 .   ? 23.556 6.279   -21.300 0.00 43.70  ? 4    MAN   C H62  1 
HETATM 24259 H HO2  . MAN   C  2 .   ? 21.812 10.582  -24.641 0.00 46.50  ? 4    MAN   C HO2  1 
HETATM 24260 H HO3  . MAN   C  2 .   ? 22.235 8.539   -26.517 0.00 45.89  ? 4    MAN   C HO3  1 
HETATM 24261 H HO4  . MAN   C  2 .   ? 24.042 6.654   -25.078 0.00 45.11  ? 4    MAN   C HO4  1 
HETATM 24262 H HO6  . MAN   C  2 .   ? 25.460 7.540   -21.855 0.00 42.99  ? 4    MAN   C HO6  1 
HETATM 24263 C C1   . MAN   C  2 .   ? 12.957 4.773   -21.712 1.00 49.76  ? 5    MAN   C C1   1 
HETATM 24264 C C2   . MAN   C  2 .   ? 13.343 6.020   -20.913 1.00 48.41  ? 5    MAN   C C2   1 
HETATM 24265 C C3   . MAN   C  2 .   ? 12.772 7.261   -21.586 1.00 49.82  ? 5    MAN   C C3   1 
HETATM 24266 C C4   . MAN   C  2 .   ? 13.253 7.332   -23.030 1.00 50.59  ? 5    MAN   C C4   1 
HETATM 24267 C C5   . MAN   C  2 .   ? 12.836 6.060   -23.765 1.00 50.95  ? 5    MAN   C C5   1 
HETATM 24268 C C6   . MAN   C  2 .   ? 13.359 6.000   -25.185 1.00 51.81  ? 5    MAN   C C6   1 
HETATM 24269 O O1   . MAN   C  2 .   ? 11.575 4.572   -21.620 1.00 50.26  ? 5    MAN   C O1   1 
HETATM 24270 O O3   . MAN   C  2 .   ? 13.145 8.435   -20.871 1.00 50.13  ? 5    MAN   C O3   1 
HETATM 24271 O O4   . MAN   C  2 .   ? 12.695 8.473   -23.678 1.00 50.68  ? 5    MAN   C O4   1 
HETATM 24272 O O5   . MAN   C  2 .   ? 13.365 4.909   -23.078 1.00 50.41  ? 5    MAN   C O5   1 
HETATM 24273 O O6   . MAN   C  2 .   ? 12.986 4.791   -25.842 1.00 52.38  ? 5    MAN   C O6   1 
HETATM 24274 H H1   . MAN   C  2 .   ? 13.519 3.897   -21.393 0.00 59.06  ? 5    MAN   C H1   1 
HETATM 24275 H H3   . MAN   C  2 .   ? 11.684 7.238   -21.548 0.00 60.29  ? 5    MAN   C H3   1 
HETATM 24276 H H4   . MAN   C  2 .   ? 14.341 7.393   -23.035 0.00 60.12  ? 5    MAN   C H4   1 
HETATM 24277 H H5   . MAN   C  2 .   ? 11.750 6.005   -23.814 0.00 61.27  ? 5    MAN   C H5   1 
HETATM 24278 H H61  . MAN   C  2 .   ? 14.433 6.182   -25.219 0.00 61.24  ? 5    MAN   C H61  1 
HETATM 24279 H H62  . MAN   C  2 .   ? 12.887 6.777   -25.784 0.00 61.89  ? 5    MAN   C H62  1 
HETATM 24280 H HO1  . MAN   C  2 .   ? 11.308 3.931   -22.330 0.00 60.43  ? 5    MAN   C HO1  1 
HETATM 24281 H HO3  . MAN   C  2 .   ? 12.925 9.254   -21.388 0.00 60.57  ? 5    MAN   C HO3  1 
HETATM 24282 H HO4  . MAN   C  2 .   ? 13.269 8.712   -24.452 0.00 60.78  ? 5    MAN   C HO4  1 
HETATM 24283 H HO6  . MAN   C  2 .   ? 13.761 4.172   -25.786 0.00 61.89  ? 5    MAN   C HO6  1 
HETATM 24284 C C1   . NAG   D  3 .   ? 31.694 -5.171  -38.742 1.00 21.63  ? 1    NAG   D C1   1 
HETATM 24285 C C2   . NAG   D  3 .   ? 30.763 -4.002  -38.418 1.00 22.20  ? 1    NAG   D C2   1 
HETATM 24286 C C3   . NAG   D  3 .   ? 31.559 -2.831  -37.841 1.00 24.02  ? 1    NAG   D C3   1 
HETATM 24287 C C4   . NAG   D  3 .   ? 32.420 -3.288  -36.667 1.00 26.44  ? 1    NAG   D C4   1 
HETATM 24288 C C5   . NAG   D  3 .   ? 33.281 -4.473  -37.087 1.00 24.20  ? 1    NAG   D C5   1 
HETATM 24289 C C6   . NAG   D  3 .   ? 34.090 -5.073  -35.957 1.00 23.55  ? 1    NAG   D C6   1 
HETATM 24290 C C7   . NAG   D  3 .   ? 28.738 -3.723  -39.811 1.00 22.80  ? 1    NAG   D C7   1 
HETATM 24291 C C8   . NAG   D  3 .   ? 28.239 -3.423  -41.191 1.00 22.84  ? 1    NAG   D C8   1 
HETATM 24292 N N2   . NAG   D  3 .   ? 30.063 -3.594  -39.629 1.00 21.95  ? 1    NAG   D N2   1 
HETATM 24293 O O3   . NAG   D  3 .   ? 30.649 -1.828  -37.406 1.00 24.12  ? 1    NAG   D O3   1 
HETATM 24294 O O4   . NAG   D  3 .   ? 33.269 -2.233  -36.223 1.00 31.21  ? 1    NAG   D O4   1 
HETATM 24295 O O5   . NAG   D  3 .   ? 32.416 -5.508  -37.553 1.00 22.54  ? 1    NAG   D O5   1 
HETATM 24296 O O6   . NAG   D  3 .   ? 33.250 -5.541  -34.906 1.00 23.32  ? 1    NAG   D O6   1 
HETATM 24297 O O7   . NAG   D  3 .   ? 27.976 -4.079  -38.906 1.00 22.94  ? 1    NAG   D O7   1 
HETATM 24298 H H2   . NAG   D  3 .   ? 30.058 -4.327  -37.654 0.00 21.78  ? 1    NAG   D H2   1 
HETATM 24299 H H3   . NAG   D  3 .   ? 32.206 -2.412  -38.611 0.00 23.64  ? 1    NAG   D H3   1 
HETATM 24300 H H4   . NAG   D  3 .   ? 31.740 -3.624  -35.884 0.00 26.50  ? 1    NAG   D H4   1 
HETATM 24301 H H5   . NAG   D  3 .   ? 33.960 -4.178  -37.886 0.00 23.80  ? 1    NAG   D H5   1 
HETATM 24302 H H61  . NAG   D  3 .   ? 34.709 -4.316  -35.478 0.00 22.86  ? 1    NAG   D H61  1 
HETATM 24303 H H62  . NAG   D  3 .   ? 34.754 -5.859  -36.315 0.00 23.06  ? 1    NAG   D H62  1 
HETATM 24304 H H81  . NAG   D  3 .   ? 27.154 -3.458  -41.220 0.00 23.29  ? 1    NAG   D H81  1 
HETATM 24305 H H82  . NAG   D  3 .   ? 28.588 -4.167  -41.906 0.00 23.19  ? 1    NAG   D H82  1 
HETATM 24306 H H83  . NAG   D  3 .   ? 28.569 -2.454  -41.561 0.00 23.01  ? 1    NAG   D H83  1 
HETATM 24307 H HN2  . NAG   D  3 .   ? 30.640 -3.191  -40.360 0.00 21.56  ? 1    NAG   D HN2  1 
HETATM 24308 H HO3  . NAG   D  3 .   ? 31.207 -1.098  -37.029 0.00 23.71  ? 1    NAG   D HO3  1 
HETATM 24309 H HO6  . NAG   D  3 .   ? 32.409 -5.874  -35.316 0.00 22.89  ? 1    NAG   D HO6  1 
HETATM 24310 C C1   . NAG   D  3 .   ? 32.908 -1.549  -35.041 1.00 36.84  ? 2    NAG   D C1   1 
HETATM 24311 C C2   . NAG   D  3 .   ? 34.150 -0.884  -34.449 1.00 39.75  ? 2    NAG   D C2   1 
HETATM 24312 C C3   . NAG   D  3 .   ? 33.748 -0.129  -33.181 1.00 42.05  ? 2    NAG   D C3   1 
HETATM 24313 C C4   . NAG   D  3 .   ? 32.590 0.832   -33.448 1.00 43.92  ? 2    NAG   D C4   1 
HETATM 24314 C C5   . NAG   D  3 .   ? 31.442 0.099   -34.139 1.00 42.15  ? 2    NAG   D C5   1 
HETATM 24315 C C6   . NAG   D  3 .   ? 30.318 1.011   -34.584 1.00 42.87  ? 2    NAG   D C6   1 
HETATM 24316 C C7   . NAG   D  3 .   ? 36.235 -2.143  -34.840 1.00 40.82  ? 2    NAG   D C7   1 
HETATM 24317 C C8   . NAG   D  3 .   ? 37.213 -3.109  -34.237 1.00 40.92  ? 2    NAG   D C8   1 
HETATM 24318 N N2   . NAG   D  3 .   ? 35.128 -1.915  -34.128 1.00 40.44  ? 2    NAG   D N2   1 
HETATM 24319 O O3   . NAG   D  3 .   ? 34.876 0.599   -32.711 1.00 42.34  ? 2    NAG   D O3   1 
HETATM 24320 O O4   . NAG   D  3 .   ? 32.126 1.352   -32.198 1.00 47.25  ? 2    NAG   D O4   1 
HETATM 24321 O O5   . NAG   D  3 .   ? 31.930 -0.554  -35.322 1.00 39.42  ? 2    NAG   D O5   1 
HETATM 24322 O O6   . NAG   D  3 .   ? 30.758 1.923   -35.587 1.00 43.48  ? 2    NAG   D O6   1 
HETATM 24323 O O7   . NAG   D  3 .   ? 36.441 -1.598  -35.920 1.00 41.23  ? 2    NAG   D O7   1 
HETATM 24324 H H2   . NAG   D  3 .   ? 34.551 -0.166  -35.164 0.00 42.07  ? 2    NAG   D H2   1 
HETATM 24325 H H3   . NAG   D  3 .   ? 33.451 -0.845  -32.415 0.00 44.88  ? 2    NAG   D H3   1 
HETATM 24326 H H4   . NAG   D  3 .   ? 32.949 1.622   -34.106 0.00 47.15  ? 2    NAG   D H4   1 
HETATM 24327 H H5   . NAG   D  3 .   ? 31.026 -0.647  -33.463 0.00 45.21  ? 2    NAG   D H5   1 
HETATM 24328 H H61  . NAG   D  3 .   ? 30.001 1.658   -33.767 0.00 46.20  ? 2    NAG   D H61  1 
HETATM 24329 H H62  . NAG   D  3 .   ? 29.446 0.446   -34.910 0.00 46.30  ? 2    NAG   D H62  1 
HETATM 24330 H H81  . NAG   D  3 .   ? 37.920 -3.520  -34.955 0.00 43.56  ? 2    NAG   D H81  1 
HETATM 24331 H H82  . NAG   D  3 .   ? 36.700 -3.960  -33.794 0.00 43.58  ? 2    NAG   D H82  1 
HETATM 24332 H H83  . NAG   D  3 .   ? 37.795 -2.650  -33.440 0.00 43.48  ? 2    NAG   D H83  1 
HETATM 24333 H HN2  . NAG   D  3 .   ? 34.927 -2.478  -33.308 0.00 42.94  ? 2    NAG   D HN2  1 
HETATM 24334 H HO3  . NAG   D  3 .   ? 34.544 1.168   -31.967 0.00 45.15  ? 2    NAG   D HO3  1 
HETATM 24335 H HO6  . NAG   D  3 .   ? 31.273 1.407   -36.261 0.00 46.86  ? 2    NAG   D HO6  1 
HETATM 24336 C C1   . BMA   D  3 .   ? 31.793 2.732   -32.099 1.00 49.78  ? 3    BMA   D C1   1 
HETATM 24337 C C2   . BMA   D  3 .   ? 30.725 2.898   -31.026 1.00 50.85  ? 3    BMA   D C2   1 
HETATM 24338 C C3   . BMA   D  3 .   ? 30.350 4.369   -30.884 1.00 51.81  ? 3    BMA   D C3   1 
HETATM 24339 C C4   . BMA   D  3 .   ? 31.586 5.238   -30.683 1.00 52.13  ? 3    BMA   D C4   1 
HETATM 24340 C C5   . BMA   D  3 .   ? 32.638 4.933   -31.749 1.00 51.93  ? 3    BMA   D C5   1 
HETATM 24341 C C6   . BMA   D  3 .   ? 33.951 5.645   -31.502 1.00 52.56  ? 3    BMA   D C6   1 
HETATM 24342 O O2   . BMA   D  3 .   ? 31.200 2.381   -29.787 1.00 50.84  ? 3    BMA   D O2   1 
HETATM 24343 O O3   . BMA   D  3 .   ? 29.449 4.552   -29.793 1.00 52.18  ? 3    BMA   D O3   1 
HETATM 24344 O O4   . BMA   D  3 .   ? 31.215 6.611   -30.781 1.00 52.31  ? 3    BMA   D O4   1 
HETATM 24345 O O5   . BMA   D  3 .   ? 32.927 3.525   -31.764 1.00 50.93  ? 3    BMA   D O5   1 
HETATM 24346 O O6   . BMA   D  3 .   ? 34.949 5.279   -32.453 1.00 52.97  ? 3    BMA   D O6   1 
HETATM 24347 H H2   . BMA   D  3 .   ? 29.833 2.355   -31.336 0.00 55.81  ? 3    BMA   D H2   1 
HETATM 24348 H H3   . BMA   D  3 .   ? 29.767 4.689   -31.746 0.00 57.10  ? 3    BMA   D H3   1 
HETATM 24349 H H4   . BMA   D  3 .   ? 32.018 5.055   -29.700 0.00 57.32  ? 3    BMA   D H4   1 
HETATM 24350 H H5   . BMA   D  3 .   ? 32.271 5.225   -32.731 0.00 57.00  ? 3    BMA   D H5   1 
HETATM 24351 H H61  . BMA   D  3 .   ? 34.287 5.522   -30.474 0.00 57.68  ? 3    BMA   D H61  1 
HETATM 24352 H H62  . BMA   D  3 .   ? 33.824 6.716   -31.658 0.00 57.79  ? 3    BMA   D H62  1 
HETATM 24353 H HO2  . BMA   D  3 .   ? 30.480 2.554   -29.126 0.00 55.79  ? 3    BMA   D HO2  1 
HETATM 24354 H HO3  . BMA   D  3 .   ? 29.148 5.498   -29.780 0.00 57.75  ? 3    BMA   D HO3  1 
HETATM 24355 H HO4  . BMA   D  3 .   ? 31.888 7.176   -30.317 0.00 57.75  ? 3    BMA   D HO4  1 
HETATM 24356 H HO6  . BMA   D  3 .   ? 35.742 5.856   -32.293 0.00 58.08  ? 3    BMA   D HO6  1 
HETATM 24357 C C1   . NAG   E  3 .   ? 32.483 3.839   -45.441 1.00 20.10  ? 1    NAG   E C1   1 
HETATM 24358 C C2   . NAG   E  3 .   ? 32.377 4.001   -43.916 1.00 20.33  ? 1    NAG   E C2   1 
HETATM 24359 C C3   . NAG   E  3 .   ? 30.919 3.799   -43.498 1.00 20.40  ? 1    NAG   E C3   1 
HETATM 24360 C C4   . NAG   E  3 .   ? 30.010 4.753   -44.264 1.00 21.41  ? 1    NAG   E C4   1 
HETATM 24361 C C5   . NAG   E  3 .   ? 30.203 4.550   -45.766 1.00 20.23  ? 1    NAG   E C5   1 
HETATM 24362 C C6   . NAG   E  3 .   ? 29.408 5.510   -46.638 1.00 20.05  ? 1    NAG   E C6   1 
HETATM 24363 C C7   . NAG   E  3 .   ? 34.208 3.206   -42.441 1.00 22.80  ? 1    NAG   E C7   1 
HETATM 24364 C C8   . NAG   E  3 .   ? 34.879 1.987   -41.879 1.00 22.74  ? 1    NAG   E C8   1 
HETATM 24365 N N2   . NAG   E  3 .   ? 33.215 2.974   -43.313 1.00 21.36  ? 1    NAG   E N2   1 
HETATM 24366 O O3   . NAG   E  3 .   ? 30.798 4.041   -42.097 1.00 20.12  ? 1    NAG   E O3   1 
HETATM 24367 O O4   . NAG   E  3 .   ? 28.650 4.517   -43.902 1.00 23.27  ? 1    NAG   E O4   1 
HETATM 24368 O O5   . NAG   E  3 .   ? 31.582 4.764   -46.083 1.00 19.90  ? 1    NAG   E O5   1 
HETATM 24369 O O6   . NAG   E  3 .   ? 29.596 6.875   -46.262 1.00 19.88  ? 1    NAG   E O6   1 
HETATM 24370 O O7   . NAG   E  3 .   ? 34.551 4.343   -42.124 1.00 23.45  ? 1    NAG   E O7   1 
HETATM 24371 H H2   . NAG   E  3 .   ? 32.686 5.003   -43.623 0.00 19.70  ? 1    NAG   E H2   1 
HETATM 24372 H H3   . NAG   E  3 .   ? 30.612 2.776   -43.711 0.00 19.98  ? 1    NAG   E H3   1 
HETATM 24373 H H4   . NAG   E  3 .   ? 30.339 5.759   -44.005 0.00 21.44  ? 1    NAG   E H4   1 
HETATM 24374 H H5   . NAG   E  3 .   ? 29.934 3.530   -46.038 0.00 20.28  ? 1    NAG   E H5   1 
HETATM 24375 H H61  . NAG   E  3 .   ? 28.340 5.353   -46.489 0.00 20.54  ? 1    NAG   E H61  1 
HETATM 24376 H H62  . NAG   E  3 .   ? 29.616 5.358   -47.696 0.00 20.51  ? 1    NAG   E H62  1 
HETATM 24377 H H81  . NAG   E  3 .   ? 35.661 2.212   -41.155 0.00 21.95  ? 1    NAG   E H81  1 
HETATM 24378 H H82  . NAG   E  3 .   ? 35.352 1.402   -42.666 0.00 22.12  ? 1    NAG   E H82  1 
HETATM 24379 H H83  . NAG   E  3 .   ? 34.165 1.326   -41.389 0.00 22.08  ? 1    NAG   E H83  1 
HETATM 24380 H HN2  . NAG   E  3 .   ? 33.008 2.020   -43.592 0.00 20.79  ? 1    NAG   E HN2  1 
HETATM 24381 H HO3  . NAG   E  3 .   ? 29.836 3.919   -41.881 0.00 19.58  ? 1    NAG   E HO3  1 
HETATM 24382 H HO6  . NAG   E  3 .   ? 29.357 7.440   -47.043 0.00 20.42  ? 1    NAG   E HO6  1 
HETATM 24383 C C1   . NAG   E  3 .   ? 27.843 5.640   -43.654 1.00 25.42  ? 2    NAG   E C1   1 
HETATM 24384 C C2   . NAG   E  3 .   ? 26.381 5.200   -43.594 1.00 26.39  ? 2    NAG   E C2   1 
HETATM 24385 C C3   . NAG   E  3 .   ? 25.527 6.441   -43.334 1.00 27.69  ? 2    NAG   E C3   1 
HETATM 24386 C C4   . NAG   E  3 .   ? 25.995 7.158   -42.071 1.00 29.89  ? 2    NAG   E C4   1 
HETATM 24387 C C5   . NAG   E  3 .   ? 27.480 7.493   -42.189 1.00 28.81  ? 2    NAG   E C5   1 
HETATM 24388 C C6   . NAG   E  3 .   ? 28.057 8.114   -40.934 1.00 29.90  ? 2    NAG   E C6   1 
HETATM 24389 C C7   . NAG   E  3 .   ? 25.872 3.269   -45.033 1.00 26.22  ? 2    NAG   E C7   1 
HETATM 24390 C C8   . NAG   E  3 .   ? 25.499 2.826   -46.419 1.00 26.19  ? 2    NAG   E C8   1 
HETATM 24391 N N2   . NAG   E  3 .   ? 26.003 4.586   -44.858 1.00 25.83  ? 2    NAG   E N2   1 
HETATM 24392 O O3   . NAG   E  3 .   ? 24.173 6.025   -43.201 1.00 27.38  ? 2    NAG   E O3   1 
HETATM 24393 O O4   . NAG   E  3 .   ? 25.266 8.370   -41.902 1.00 33.34  ? 2    NAG   E O4   1 
HETATM 24394 O O5   . NAG   E  3 .   ? 28.223 6.289   -42.440 1.00 26.69  ? 2    NAG   E O5   1 
HETATM 24395 O O6   . NAG   E  3 .   ? 29.412 8.500   -41.116 1.00 30.90  ? 2    NAG   E O6   1 
HETATM 24396 O O7   . NAG   E  3 .   ? 26.062 2.468   -44.121 1.00 26.42  ? 2    NAG   E O7   1 
HETATM 24397 H H2   . NAG   E  3 .   ? 26.239 4.515   -42.760 0.00 27.94  ? 2    NAG   E H2   1 
HETATM 24398 H H3   . NAG   E  3 .   ? 25.606 7.124   -44.179 0.00 30.09  ? 2    NAG   E H3   1 
HETATM 24399 H H4   . NAG   E  3 .   ? 25.864 6.465   -41.241 0.00 32.20  ? 2    NAG   E H4   1 
HETATM 24400 H H5   . NAG   E  3 .   ? 27.637 8.182   -43.017 0.00 30.94  ? 2    NAG   E H5   1 
HETATM 24401 H H61  . NAG   E  3 .   ? 28.116 7.370   -40.141 0.00 31.73  ? 2    NAG   E H61  1 
HETATM 24402 H H62  . NAG   E  3 .   ? 27.454 8.942   -40.567 0.00 32.11  ? 2    NAG   E H62  1 
HETATM 24403 H H81  . NAG   E  3 .   ? 25.089 1.818   -46.453 0.00 28.46  ? 2    NAG   E H81  1 
HETATM 24404 H H82  . NAG   E  3 .   ? 26.365 2.828   -47.079 0.00 28.31  ? 2    NAG   E H82  1 
HETATM 24405 H H83  . NAG   E  3 .   ? 24.764 3.489   -46.871 0.00 28.69  ? 2    NAG   E H83  1 
HETATM 24406 H HN2  . NAG   E  3 .   ? 25.836 5.223   -45.631 0.00 27.86  ? 2    NAG   E HN2  1 
HETATM 24407 H HO3  . NAG   E  3 .   ? 23.722 6.723   -42.659 0.00 29.93  ? 2    NAG   E HO3  1 
HETATM 24408 H HO6  . NAG   E  3 .   ? 29.902 7.728   -41.502 0.00 32.78  ? 2    NAG   E HO6  1 
HETATM 24409 C C1   . BMA   E  3 .   ? 24.646 8.587   -40.647 1.00 37.10  ? 3    BMA   E C1   1 
HETATM 24410 C C2   . BMA   E  3 .   ? 24.412 10.081  -40.471 1.00 38.76  ? 3    BMA   E C2   1 
HETATM 24411 C C3   . BMA   E  3 .   ? 23.698 10.346  -39.152 1.00 40.43  ? 3    BMA   E C3   1 
HETATM 24412 C C4   . BMA   E  3 .   ? 22.427 9.514   -39.050 1.00 40.75  ? 3    BMA   E C4   1 
HETATM 24413 C C5   . BMA   E  3 .   ? 22.743 8.041   -39.302 1.00 40.27  ? 3    BMA   E C5   1 
HETATM 24414 C C6   . BMA   E  3 .   ? 21.510 7.171   -39.356 1.00 40.83  ? 3    BMA   E C6   1 
HETATM 24415 O O2   . BMA   E  3 .   ? 23.637 10.569  -41.558 1.00 38.82  ? 3    BMA   E O2   1 
HETATM 24416 O O3   . BMA   E  3 .   ? 23.386 11.730  -39.022 1.00 41.30  ? 3    BMA   E O3   1 
HETATM 24417 O O4   . BMA   E  3 .   ? 21.887 9.656   -37.739 1.00 41.34  ? 3    BMA   E O4   1 
HETATM 24418 O O5   . BMA   E  3 .   ? 23.405 7.889   -40.568 1.00 38.83  ? 3    BMA   E O5   1 
HETATM 24419 O O6   . BMA   E  3 .   ? 20.674 7.539   -40.446 1.00 41.43  ? 3    BMA   E O6   1 
HETATM 24420 H H2   . BMA   E  3 .   ? 25.376 10.588  -40.442 0.00 43.46  ? 3    BMA   E H2   1 
HETATM 24421 H H3   . BMA   E  3 .   ? 24.368 10.155  -38.315 0.00 45.44  ? 3    BMA   E H3   1 
HETATM 24422 H H4   . BMA   E  3 .   ? 21.696 9.863   -39.779 0.00 46.63  ? 3    BMA   E H4   1 
HETATM 24423 H H5   . BMA   E  3 .   ? 23.399 7.660   -38.522 0.00 45.11  ? 3    BMA   E H5   1 
HETATM 24424 H H61  . BMA   E  3 .   ? 20.981 7.153   -38.405 0.00 46.38  ? 3    BMA   E H61  1 
HETATM 24425 H H62  . BMA   E  3 .   ? 21.787 6.141   -39.576 0.00 46.15  ? 3    BMA   E H62  1 
HETATM 24426 H HO2  . BMA   E  3 .   ? 23.445 11.520  -41.350 0.00 44.32  ? 3    BMA   E HO2  1 
HETATM 24427 H HO3  . BMA   E  3 .   ? 22.546 11.822  -38.500 0.00 47.33  ? 3    BMA   E HO3  1 
HETATM 24428 H HO4  . BMA   E  3 .   ? 20.920 9.430   -37.752 0.00 47.31  ? 3    BMA   E HO4  1 
HETATM 24429 H HO6  . BMA   E  3 .   ? 21.189 7.397   -41.283 0.00 47.40  ? 3    BMA   E HO6  1 
HETATM 24430 C C1   . NAG   F  2 .   ? 71.404 4.148   -61.101 1.00 22.33  ? 1    NAG   F C1   1 
HETATM 24431 C C2   . NAG   F  2 .   ? 70.555 5.138   -60.295 1.00 22.56  ? 1    NAG   F C2   1 
HETATM 24432 C C3   . NAG   F  2 .   ? 71.435 6.203   -59.639 1.00 22.99  ? 1    NAG   F C3   1 
HETATM 24433 C C4   . NAG   F  2 .   ? 72.572 5.563   -58.851 1.00 24.00  ? 1    NAG   F C4   1 
HETATM 24434 C C5   . NAG   F  2 .   ? 73.316 4.556   -59.725 1.00 23.78  ? 1    NAG   F C5   1 
HETATM 24435 C C6   . NAG   F  2 .   ? 74.399 3.790   -58.985 1.00 24.84  ? 1    NAG   F C6   1 
HETATM 24436 C C7   . NAG   F  2 .   ? 68.309 5.940   -60.915 1.00 21.86  ? 1    NAG   F C7   1 
HETATM 24437 C C8   . NAG   F  2 .   ? 67.544 6.830   -61.850 1.00 21.72  ? 1    NAG   F C8   1 
HETATM 24438 N N2   . NAG   F  2 .   ? 69.603 5.765   -61.201 1.00 21.82  ? 1    NAG   F N2   1 
HETATM 24439 O O3   . NAG   F  2 .   ? 70.589 6.998   -58.809 1.00 22.41  ? 1    NAG   F O3   1 
HETATM 24440 O O4   . NAG   F  2 .   ? 73.515 6.548   -58.422 1.00 25.43  ? 1    NAG   F O4   1 
HETATM 24441 O O5   . NAG   F  2 .   ? 72.387 3.587   -60.226 1.00 22.81  ? 1    NAG   F O5   1 
HETATM 24442 O O6   . NAG   F  2 .   ? 73.879 3.100   -57.849 1.00 25.77  ? 1    NAG   F O6   1 
HETATM 24443 O O7   . NAG   F  2 .   ? 67.783 5.419   -59.937 1.00 21.66  ? 1    NAG   F O7   1 
HETATM 24444 H H2   . NAG   F  2 .   ? 70.042 4.577   -59.515 0.00 24.31  ? 1    NAG   F H2   1 
HETATM 24445 H H3   . NAG   F  2 .   ? 71.871 6.843   -60.406 0.00 25.21  ? 1    NAG   F H3   1 
HETATM 24446 H H4   . NAG   F  2 .   ? 72.133 5.040   -58.003 0.00 26.21  ? 1    NAG   F H4   1 
HETATM 24447 H H5   . NAG   F  2 .   ? 73.782 5.076   -60.560 0.00 26.61  ? 1    NAG   F H5   1 
HETATM 24448 H H61  . NAG   F  2 .   ? 75.133 4.471   -58.557 0.00 27.97  ? 1    NAG   F H61  1 
HETATM 24449 H H62  . NAG   F  2 .   ? 74.931 3.111   -59.650 0.00 28.12  ? 1    NAG   F H62  1 
HETATM 24450 H H81  . NAG   F  2 .   ? 66.738 7.382   -61.369 0.00 23.08  ? 1    NAG   F H81  1 
HETATM 24451 H H82  . NAG   F  2 .   ? 67.082 6.251   -62.649 0.00 23.34  ? 1    NAG   F H82  1 
HETATM 24452 H H83  . NAG   F  2 .   ? 68.187 7.565   -62.331 0.00 23.42  ? 1    NAG   F H83  1 
HETATM 24453 H HN2  . NAG   F  2 .   ? 69.976 6.074   -62.092 0.00 23.75  ? 1    NAG   F HN2  1 
HETATM 24454 H HO3  . NAG   F  2 .   ? 71.145 7.759   -58.497 0.00 24.15  ? 1    NAG   F HO3  1 
HETATM 24455 H HO6  . NAG   F  2 .   ? 72.991 2.733   -58.101 0.00 28.65  ? 1    NAG   F HO6  1 
HETATM 24456 C C1   . NAG   F  2 .   ? 73.289 7.186   -57.181 1.00 26.85  ? 2    NAG   F C1   1 
HETATM 24457 C C2   . NAG   F  2 .   ? 74.581 7.827   -56.673 1.00 27.08  ? 2    NAG   F C2   1 
HETATM 24458 C C3   . NAG   F  2 .   ? 74.285 8.434   -55.300 1.00 28.76  ? 2    NAG   F C3   1 
HETATM 24459 C C4   . NAG   F  2 .   ? 73.132 9.432   -55.387 1.00 30.94  ? 2    NAG   F C4   1 
HETATM 24460 C C5   . NAG   F  2 .   ? 71.930 8.767   -56.054 1.00 30.50  ? 2    NAG   F C5   1 
HETATM 24461 C C6   . NAG   F  2 .   ? 70.775 9.707   -56.308 1.00 31.94  ? 2    NAG   F C6   1 
HETATM 24462 C C7   . NAG   F  2 .   ? 76.923 7.074   -56.806 1.00 25.96  ? 2    NAG   F C7   1 
HETATM 24463 C C8   . NAG   F  2 .   ? 77.875 5.962   -56.484 1.00 25.35  ? 2    NAG   F C8   1 
HETATM 24464 N N2   . NAG   F  2 .   ? 75.629 6.825   -56.566 1.00 26.07  ? 2    NAG   F N2   1 
HETATM 24465 O O3   . NAG   F  2 .   ? 75.459 9.067   -54.803 1.00 28.27  ? 2    NAG   F O3   1 
HETATM 24466 O O4   . NAG   F  2 .   ? 72.727 9.818   -54.077 1.00 33.74  ? 2    NAG   F O4   1 
HETATM 24467 O O5   . NAG   F  2 .   ? 72.320 8.221   -57.322 1.00 28.47  ? 2    NAG   F O5   1 
HETATM 24468 O O6   . NAG   F  2 .   ? 71.168 10.840  -57.067 1.00 32.99  ? 2    NAG   F O6   1 
HETATM 24469 O O7   . NAG   F  2 .   ? 77.309 8.154   -57.252 1.00 26.56  ? 2    NAG   F O7   1 
HETATM 24470 H H2   . NAG   F  2 .   ? 74.871 8.629   -57.350 0.00 30.43  ? 2    NAG   F H2   1 
HETATM 24471 H H3   . NAG   F  2 .   ? 74.010 7.632   -54.617 0.00 32.04  ? 2    NAG   F H3   1 
HETATM 24472 H H4   . NAG   F  2 .   ? 73.463 10.277  -55.989 0.00 34.71  ? 2    NAG   F H4   1 
HETATM 24473 H H5   . NAG   F  2 .   ? 71.556 7.955   -55.430 0.00 33.65  ? 2    NAG   F H5   1 
HETATM 24474 H H61  . NAG   F  2 .   ? 70.418 10.140  -55.375 0.00 35.24  ? 2    NAG   F H61  1 
HETATM 24475 H H62  . NAG   F  2 .   ? 69.934 9.192   -56.772 0.00 35.22  ? 2    NAG   F H62  1 
HETATM 24476 H H81  . NAG   F  2 .   ? 78.915 6.196   -56.707 0.00 29.39  ? 2    NAG   F H81  1 
HETATM 24477 H H82  . NAG   F  2 .   ? 77.637 5.064   -57.053 0.00 29.07  ? 2    NAG   F H82  1 
HETATM 24478 H H83  . NAG   F  2 .   ? 77.826 5.681   -55.433 0.00 29.00  ? 2    NAG   F H83  1 
HETATM 24479 H HN2  . NAG   F  2 .   ? 75.332 5.893   -56.291 0.00 29.25  ? 2    NAG   F HN2  1 
HETATM 24480 H HO3  . NAG   F  2 .   ? 75.146 9.739   -54.143 0.00 31.77  ? 2    NAG   F HO3  1 
HETATM 24481 H HO6  . NAG   F  2 .   ? 70.377 11.434  -57.161 0.00 36.72  ? 2    NAG   F HO6  1 
HETATM 24482 C C1   . BMA   F  2 .   ? 72.984 11.123  -53.634 1.00 35.89  ? 3    BMA   F C1   1 
HETATM 24483 C C2   . BMA   F  2 .   ? 72.305 11.303  -52.277 1.00 36.52  ? 3    BMA   F C2   1 
HETATM 24484 C C3   . BMA   F  2 .   ? 72.649 12.663  -51.679 1.00 37.70  ? 3    BMA   F C3   1 
HETATM 24485 C C4   . BMA   F  2 .   ? 74.154 12.898  -51.681 1.00 38.75  ? 3    BMA   F C4   1 
HETATM 24486 C C5   . BMA   F  2 .   ? 74.714 12.666  -53.081 1.00 39.91  ? 3    BMA   F C5   1 
HETATM 24487 C C6   . BMA   F  2 .   ? 76.221 12.804  -53.166 1.00 43.14  ? 3    BMA   F C6   1 
HETATM 24488 O O2   . BMA   F  2 .   ? 72.685 10.252  -51.392 1.00 35.96  ? 3    BMA   F O2   1 
HETATM 24489 O O3   . BMA   F  2 .   ? 72.155 12.736  -50.340 1.00 37.90  ? 3    BMA   F O3   1 
HETATM 24490 O O4   . BMA   F  2 .   ? 74.420 14.243  -51.299 1.00 38.83  ? 3    BMA   F O4   1 
HETATM 24491 O O5   . BMA   F  2 .   ? 74.385 11.335  -53.509 1.00 37.56  ? 3    BMA   F O5   1 
HETATM 24492 O O6   . BMA   F  2 .   ? 76.909 11.888  -52.319 1.00 46.37  ? 3    BMA   F O6   1 
HETATM 24493 H H2   . BMA   F  2 .   ? 71.227 11.276  -52.429 0.00 40.82  ? 3    BMA   F H2   1 
HETATM 24494 H H3   . BMA   F  2 .   ? 72.146 13.440  -52.254 0.00 42.64  ? 3    BMA   F H3   1 
HETATM 24495 H H4   . BMA   F  2 .   ? 74.637 12.219  -50.980 0.00 44.35  ? 3    BMA   F H4   1 
HETATM 24496 H H5   . BMA   F  2 .   ? 74.274 13.378  -53.778 0.00 45.80  ? 3    BMA   F H5   1 
HETATM 24497 H H61  . BMA   F  2 .   ? 76.541 13.832  -53.008 0.00 50.29  ? 3    BMA   F H61  1 
HETATM 24498 H H62  . BMA   F  2 .   ? 76.558 12.529  -54.164 0.00 50.18  ? 3    BMA   F H62  1 
HETATM 24499 H HO2  . BMA   F  2 .   ? 72.262 9.429   -51.753 0.00 40.24  ? 3    BMA   F HO2  1 
HETATM 24500 H HO4  . BMA   F  2 .   ? 75.343 14.316  -50.938 0.00 44.86  ? 3    BMA   F HO4  1 
HETATM 24501 C C1   . MAN   F  2 .   ? 71.146 13.682  -50.016 1.00 38.33  ? 4    MAN   F C1   1 
HETATM 24502 C C2   . MAN   F  2 .   ? 71.044 13.823  -48.499 1.00 38.41  ? 4    MAN   F C2   1 
HETATM 24503 C C3   . MAN   F  2 .   ? 70.458 12.561  -47.881 1.00 39.12  ? 4    MAN   F C3   1 
HETATM 24504 C C4   . MAN   F  2 .   ? 69.130 12.220  -48.534 1.00 39.32  ? 4    MAN   F C4   1 
HETATM 24505 C C5   . MAN   F  2 .   ? 69.303 12.110  -50.049 1.00 38.44  ? 4    MAN   F C5   1 
HETATM 24506 C C6   . MAN   F  2 .   ? 67.993 11.930  -50.774 1.00 37.85  ? 4    MAN   F C6   1 
HETATM 24507 O O2   . MAN   F  2 .   ? 70.231 14.948  -48.180 1.00 37.98  ? 4    MAN   F O2   1 
HETATM 24508 O O3   . MAN   F  2 .   ? 70.271 12.736  -46.479 1.00 39.83  ? 4    MAN   F O3   1 
HETATM 24509 O O4   . MAN   F  2 .   ? 68.658 10.977  -48.019 1.00 40.10  ? 4    MAN   F O4   1 
HETATM 24510 O O5   . MAN   F  2 .   ? 69.883 13.315  -50.572 1.00 38.22  ? 4    MAN   F O5   1 
HETATM 24511 O O6   . MAN   F  2 .   ? 67.172 13.087  -50.658 1.00 37.49  ? 4    MAN   F O6   1 
HETATM 24512 H H2   . MAN   F  2 .   ? 72.031 14.003  -48.075 0.00 43.56  ? 4    MAN   F H2   1 
HETATM 24513 H H3   . MAN   F  2 .   ? 71.160 11.734  -47.976 0.00 43.97  ? 4    MAN   F H3   1 
HETATM 24514 H H4   . MAN   F  2 .   ? 68.415 13.012  -48.313 0.00 43.80  ? 4    MAN   F H4   1 
HETATM 24515 H H5   . MAN   F  2 .   ? 69.934 11.255  -50.284 0.00 42.83  ? 4    MAN   F H5   1 
HETATM 24516 H H61  . MAN   F  2 .   ? 67.478 11.025  -50.454 0.00 41.68  ? 4    MAN   F H61  1 
HETATM 24517 H H62  . MAN   F  2 .   ? 68.172 11.836  -51.844 0.00 41.90  ? 4    MAN   F H62  1 
HETATM 24518 H HO2  . MAN   F  2 .   ? 69.855 14.818  -47.270 0.00 42.73  ? 4    MAN   F HO2  1 
HETATM 24519 H HO3  . MAN   F  2 .   ? 69.454 12.266  -46.166 0.00 44.59  ? 4    MAN   F HO3  1 
HETATM 24520 H HO4  . MAN   F  2 .   ? 67.676 10.932  -48.159 0.00 44.40  ? 4    MAN   F HO4  1 
HETATM 24521 H HO6  . MAN   F  2 .   ? 66.251 12.820  -50.914 0.00 41.25  ? 4    MAN   F HO6  1 
HETATM 24522 C C1   . MAN   F  2 .   ? 78.773 10.373  -51.859 1.00 51.04  ? 5    MAN   F C1   1 
HETATM 24523 C C2   . MAN   F  2 .   ? 78.381 11.808  -52.207 1.00 49.42  ? 5    MAN   F C2   1 
HETATM 24524 C C3   . MAN   F  2 .   ? 78.938 12.763  -51.163 1.00 50.94  ? 5    MAN   F C3   1 
HETATM 24525 C C4   . MAN   F  2 .   ? 78.446 12.357  -49.780 1.00 51.80  ? 5    MAN   F C4   1 
HETATM 24526 C C5   . MAN   F  2 .   ? 78.866 10.917  -49.496 1.00 52.25  ? 5    MAN   F C5   1 
HETATM 24527 C C6   . MAN   F  2 .   ? 78.331 10.394  -48.180 1.00 53.18  ? 5    MAN   F C6   1 
HETATM 24528 O O1   . MAN   F  2 .   ? 80.153 10.219  -52.000 1.00 51.65  ? 5    MAN   F O1   1 
HETATM 24529 O O3   . MAN   F  2 .   ? 78.564 14.103  -51.463 1.00 51.56  ? 5    MAN   F O3   1 
HETATM 24530 O O4   . MAN   F  2 .   ? 78.987 13.228  -48.789 1.00 52.12  ? 5    MAN   F O4   1 
HETATM 24531 O O5   . MAN   F  2 .   ? 78.354 10.051  -50.526 1.00 51.80  ? 5    MAN   F O5   1 
HETATM 24532 O O6   . MAN   F  2 .   ? 78.699 9.036   -47.955 1.00 53.83  ? 5    MAN   F O6   1 
HETATM 24533 H H1   . MAN   F  2 .   ? 78.224 9.645   -52.455 0.00 59.89  ? 5    MAN   F H1   1 
HETATM 24534 H H3   . MAN   F  2 .   ? 80.027 12.760  -51.196 0.00 60.59  ? 5    MAN   F H3   1 
HETATM 24535 H H4   . MAN   F  2 .   ? 77.358 12.409  -49.766 0.00 60.79  ? 5    MAN   F H4   1 
HETATM 24536 H H5   . MAN   F  2 .   ? 79.952 10.853  -49.457 0.00 62.03  ? 5    MAN   F H5   1 
HETATM 24537 H H61  . MAN   F  2 .   ? 77.257 10.552  -48.097 0.00 62.31  ? 5    MAN   F H61  1 
HETATM 24538 H H62  . MAN   F  2 .   ? 78.795 10.933  -47.355 0.00 62.86  ? 5    MAN   F H62  1 
HETATM 24539 H HO1  . MAN   F  2 .   ? 80.421 9.383   -51.536 0.00 61.31  ? 5    MAN   F HO1  1 
HETATM 24540 H HO3  . MAN   F  2 .   ? 78.770 14.711  -50.704 0.00 61.17  ? 5    MAN   F HO3  1 
HETATM 24541 H HO4  . MAN   F  2 .   ? 78.406 13.196  -47.984 0.00 61.65  ? 5    MAN   F HO4  1 
HETATM 24542 H HO6  . MAN   F  2 .   ? 77.928 8.467   -48.218 0.00 63.18  ? 5    MAN   F HO6  1 
HETATM 24543 C C1   . NAG   G  3 .   ? 60.233 -4.978  -39.282 1.00 23.50  ? 1    NAG   G C1   1 
HETATM 24544 C C2   . NAG   G  3 .   ? 61.152 -3.758  -39.180 1.00 24.50  ? 1    NAG   G C2   1 
HETATM 24545 C C3   . NAG   G  3 .   ? 60.343 -2.465  -39.321 1.00 25.96  ? 1    NAG   G C3   1 
HETATM 24546 C C4   . NAG   G  3 .   ? 59.499 -2.495  -40.591 1.00 27.57  ? 1    NAG   G C4   1 
HETATM 24547 C C5   . NAG   G  3 .   ? 58.632 -3.748  -40.600 1.00 25.16  ? 1    NAG   G C5   1 
HETATM 24548 C C6   . NAG   G  3 .   ? 57.820 -3.910  -41.870 1.00 24.26  ? 1    NAG   G C6   1 
HETATM 24549 C C7   . NAG   G  3 .   ? 63.193 -3.958  -37.782 1.00 24.63  ? 1    NAG   G C7   1 
HETATM 24550 C C8   . NAG   G  3 .   ? 63.686 -4.337  -36.416 1.00 25.21  ? 1    NAG   G C8   1 
HETATM 24551 N N2   . NAG   G  3 .   ? 61.854 -3.787  -37.904 1.00 24.40  ? 1    NAG   G N2   1 
HETATM 24552 O O3   . NAG   G  3 .   ? 61.234 -1.360  -39.385 1.00 26.06  ? 1    NAG   G O3   1 
HETATM 24553 O O4   . NAG   G  3 .   ? 58.643 -1.356  -40.667 1.00 31.94  ? 1    NAG   G O4   1 
HETATM 24554 O O5   . NAG   G  3 .   ? 59.486 -4.891  -40.508 1.00 23.72  ? 1    NAG   G O5   1 
HETATM 24555 O O6   . NAG   G  3 .   ? 58.646 -4.103  -43.007 1.00 23.79  ? 1    NAG   G O6   1 
HETATM 24556 O O7   . NAG   G  3 .   ? 63.961 -3.823  -38.734 1.00 24.55  ? 1    NAG   G O7   1 
HETATM 24557 H H2   . NAG   G  3 .   ? 61.858 -3.790  -40.008 0.00 25.45  ? 1    NAG   G H2   1 
HETATM 24558 H H3   . NAG   G  3 .   ? 59.686 -2.346  -38.461 0.00 26.90  ? 1    NAG   G H3   1 
HETATM 24559 H H4   . NAG   G  3 .   ? 60.183 -2.551  -41.438 0.00 28.71  ? 1    NAG   G H4   1 
HETATM 24560 H H5   . NAG   G  3 .   ? 57.956 -3.739  -39.746 0.00 25.83  ? 1    NAG   G H5   1 
HETATM 24561 H H61  . NAG   G  3 .   ? 57.268 -3.000  -42.103 0.00 24.53  ? 1    NAG   G H61  1 
HETATM 24562 H H62  . NAG   G  3 .   ? 57.091 -4.713  -41.773 0.00 24.75  ? 1    NAG   G H62  1 
HETATM 24563 H H81  . NAG   G  3 .   ? 64.422 -3.650  -36.001 0.00 27.10  ? 1    NAG   G H81  1 
HETATM 24564 H H82  . NAG   G  3 .   ? 64.170 -5.312  -36.440 0.00 27.21  ? 1    NAG   G H82  1 
HETATM 24565 H H83  . NAG   G  3 .   ? 62.880 -4.414  -35.689 0.00 26.95  ? 1    NAG   G H83  1 
HETATM 24566 H HN2  . NAG   G  3 .   ? 61.273 -3.657  -37.082 0.00 25.48  ? 1    NAG   G HN2  1 
HETATM 24567 H HO3  . NAG   G  3 .   ? 60.672 -0.566  -39.586 0.00 26.87  ? 1    NAG   G HO3  1 
HETATM 24568 H HO6  . NAG   G  3 .   ? 59.465 -4.581  -42.710 0.00 24.33  ? 1    NAG   G HO6  1 
HETATM 24569 C C1   . NAG   G  3 .   ? 58.979 -0.326  -41.571 1.00 36.76  ? 2    NAG   G C1   1 
HETATM 24570 C C2   . NAG   G  3 .   ? 57.729 0.487   -41.910 1.00 39.15  ? 2    NAG   G C2   1 
HETATM 24571 C C3   . NAG   G  3 .   ? 58.122 1.629   -42.850 1.00 41.42  ? 2    NAG   G C3   1 
HETATM 24572 C C4   . NAG   G  3 .   ? 59.267 2.457   -42.273 1.00 43.38  ? 2    NAG   G C4   1 
HETATM 24573 C C5   . NAG   G  3 .   ? 60.423 1.547   -41.861 1.00 41.82  ? 2    NAG   G C5   1 
HETATM 24574 C C6   . NAG   G  3 .   ? 61.536 2.270   -41.130 1.00 42.69  ? 2    NAG   G C6   1 
HETATM 24575 C C7   . NAG   G  3 .   ? 55.647 -0.834  -41.968 1.00 39.18  ? 2    NAG   G C7   1 
HETATM 24576 C C8   . NAG   G  3 .   ? 54.682 -1.561  -42.858 1.00 39.03  ? 2    NAG   G C8   1 
HETATM 24577 N N2   . NAG   G  3 .   ? 56.756 -0.380  -42.559 1.00 39.19  ? 2    NAG   G N2   1 
HETATM 24578 O O3   . NAG   G  3 .   ? 56.989 2.465   -43.055 1.00 41.82  ? 2    NAG   G O3   1 
HETATM 24579 O O4   . NAG   G  3 .   ? 59.723 3.370   -43.277 1.00 46.84  ? 2    NAG   G O4   1 
HETATM 24580 O O5   . NAG   G  3 .   ? 59.942 0.531   -40.969 1.00 39.32  ? 2    NAG   G O5   1 
HETATM 24581 O O6   . NAG   G  3 .   ? 61.087 2.789   -39.881 1.00 43.51  ? 2    NAG   G O6   1 
HETATM 24582 O O7   . NAG   G  3 .   ? 55.430 -0.668  -40.771 1.00 39.37  ? 2    NAG   G O7   1 
HETATM 24583 H H2   . NAG   G  3 .   ? 57.320 0.922   -40.999 0.00 42.09  ? 2    NAG   G H2   1 
HETATM 24584 H H3   . NAG   G  3 .   ? 58.428 1.212   -43.810 0.00 44.78  ? 2    NAG   G H3   1 
HETATM 24585 H H4   . NAG   G  3 .   ? 58.899 2.980   -41.390 0.00 47.19  ? 2    NAG   G H4   1 
HETATM 24586 H H5   . NAG   G  3 .   ? 60.848 1.072   -42.744 0.00 45.52  ? 2    NAG   G H5   1 
HETATM 24587 H H61  . NAG   G  3 .   ? 61.845 3.158   -41.680 0.00 46.64  ? 2    NAG   G H61  1 
HETATM 24588 H H62  . NAG   G  3 .   ? 62.412 1.636   -41.003 0.00 46.81  ? 2    NAG   G H62  1 
HETATM 24589 H H81  . NAG   G  3 .   ? 53.982 -2.196  -42.317 0.00 42.02  ? 2    NAG   G H81  1 
HETATM 24590 H H82  . NAG   G  3 .   ? 55.205 -2.211  -43.557 0.00 42.05  ? 2    NAG   G H82  1 
HETATM 24591 H H83  . NAG   G  3 .   ? 54.096 -0.868  -43.460 0.00 41.90  ? 2    NAG   G H83  1 
HETATM 24592 H HN2  . NAG   G  3 .   ? 56.965 -0.638  -43.518 0.00 42.15  ? 2    NAG   G HN2  1 
HETATM 24593 H HO3  . NAG   G  3 .   ? 57.314 3.245   -43.575 0.00 45.13  ? 2    NAG   G HO3  1 
HETATM 24594 H HO6  . NAG   G  3 .   ? 60.571 2.075   -39.422 0.00 47.66  ? 2    NAG   G HO6  1 
HETATM 24595 C C1   . BMA   G  3 .   ? 60.040 4.706   -42.909 1.00 49.65  ? 3    BMA   G C1   1 
HETATM 24596 C C2   . BMA   G  3 .   ? 61.111 5.233   -43.856 1.00 50.74  ? 3    BMA   G C2   1 
HETATM 24597 C C3   . BMA   G  3 .   ? 61.466 6.671   -43.494 1.00 51.98  ? 3    BMA   G C3   1 
HETATM 24598 C C4   . BMA   G  3 .   ? 60.219 7.544   -43.405 1.00 52.45  ? 3    BMA   G C4   1 
HETATM 24599 C C5   . BMA   G  3 .   ? 59.164 6.890   -42.513 1.00 52.31  ? 3    BMA   G C5   1 
HETATM 24600 C C6   . BMA   G  3 .   ? 57.843 7.628   -42.529 1.00 53.11  ? 3    BMA   G C6   1 
HETATM 24601 O O2   . BMA   G  3 .   ? 60.648 5.156   -45.200 1.00 50.56  ? 3    BMA   G O2   1 
HETATM 24602 O O3   . BMA   G  3 .   ? 62.375 7.217   -44.448 1.00 52.48  ? 3    BMA   G O3   1 
HETATM 24603 O O4   . BMA   G  3 .   ? 60.569 8.808   -42.848 1.00 52.89  ? 3    BMA   G O4   1 
HETATM 24604 O O5   . BMA   G  3 .   ? 58.896 5.553   -42.968 1.00 51.12  ? 3    BMA   G O5   1 
HETATM 24605 O O6   . BMA   G  3 .   ? 56.842 6.955   -41.770 1.00 53.71  ? 3    BMA   G O6   1 
HETATM 24606 H H2   . BMA   G  3 .   ? 62.007 4.627   -43.736 0.00 56.21  ? 3    BMA   G H2   1 
HETATM 24607 H H3   . BMA   G  3 .   ? 62.040 6.691   -42.568 0.00 57.78  ? 3    BMA   G H3   1 
HETATM 24608 H H4   . BMA   G  3 .   ? 59.798 7.694   -44.399 0.00 58.11  ? 3    BMA   G H4   1 
HETATM 24609 H H5   . BMA   G  3 .   ? 59.522 6.842   -41.486 0.00 57.99  ? 3    BMA   G H5   1 
HETATM 24610 H H61  . BMA   G  3 .   ? 57.517 7.853   -43.544 0.00 58.78  ? 3    BMA   G H61  1 
HETATM 24611 H H62  . BMA   G  3 .   ? 57.953 8.586   -42.022 0.00 58.91  ? 3    BMA   G H62  1 
HETATM 24612 H HO2  . BMA   G  3 .   ? 61.373 5.545   -45.756 0.00 55.89  ? 3    BMA   G HO2  1 
HETATM 24613 H HO3  . BMA   G  3 .   ? 62.659 8.119   -44.144 0.00 58.45  ? 3    BMA   G HO3  1 
HETATM 24614 H HO4  . BMA   G  3 .   ? 59.894 9.489   -43.108 0.00 58.80  ? 3    BMA   G HO4  1 
HETATM 24615 H HO6  . BMA   G  3 .   ? 56.044 7.545   -41.730 0.00 59.49  ? 3    BMA   G HO6  1 
HETATM 24616 C C1   . NAG   H  3 .   ? 59.438 1.291   -29.999 1.00 21.67  ? 1    NAG   H C1   1 
HETATM 24617 C C2   . NAG   H  3 .   ? 59.547 1.904   -31.404 1.00 21.83  ? 1    NAG   H C2   1 
HETATM 24618 C C3   . NAG   H  3 .   ? 61.004 1.895   -31.860 1.00 21.81  ? 1    NAG   H C3   1 
HETATM 24619 C C4   . NAG   H  3 .   ? 61.890 2.575   -30.830 1.00 22.68  ? 1    NAG   H C4   1 
HETATM 24620 C C5   . NAG   H  3 .   ? 61.704 1.911   -29.469 1.00 21.91  ? 1    NAG   H C5   1 
HETATM 24621 C C6   . NAG   H  3 .   ? 62.514 2.549   -28.358 1.00 21.52  ? 1    NAG   H C6   1 
HETATM 24622 C C7   . NAG   H  3 .   ? 57.757 1.662   -33.075 1.00 23.08  ? 1    NAG   H C7   1 
HETATM 24623 C C8   . NAG   H  3 .   ? 57.064 0.718   -34.015 1.00 22.77  ? 1    NAG   H C8   1 
HETATM 24624 N N2   . NAG   H  3 .   ? 58.730 1.134   -32.328 1.00 21.88  ? 1    NAG   H N2   1 
HETATM 24625 O O3   . NAG   H  3 .   ? 61.130 2.574   -33.105 1.00 21.12  ? 1    NAG   H O3   1 
HETATM 24626 O O4   . NAG   H  3 .   ? 63.249 2.460   -31.248 1.00 24.20  ? 1    NAG   H O4   1 
HETATM 24627 O O5   . NAG   H  3 .   ? 60.317 1.997   -29.095 1.00 21.78  ? 1    NAG   H O5   1 
HETATM 24628 O O6   . NAG   H  3 .   ? 62.265 3.948   -28.219 1.00 21.19  ? 1    NAG   H O6   1 
HETATM 24629 O O7   . NAG   H  3 .   ? 57.461 2.851   -33.011 1.00 23.91  ? 1    NAG   H O7   1 
HETATM 24630 H H2   . NAG   H  3 .   ? 59.225 2.943   -31.361 0.00 22.54  ? 1    NAG   H H2   1 
HETATM 24631 H H3   . NAG   H  3 .   ? 61.338 0.866   -31.985 0.00 22.73  ? 1    NAG   H H3   1 
HETATM 24632 H H4   . NAG   H  3 .   ? 61.556 3.610   -30.761 0.00 24.00  ? 1    NAG   H H4   1 
HETATM 24633 H H5   . NAG   H  3 .   ? 61.985 0.861   -29.537 0.00 23.44  ? 1    NAG   H H5   1 
HETATM 24634 H H61  . NAG   H  3 .   ? 63.577 2.504   -28.592 0.00 23.43  ? 1    NAG   H H61  1 
HETATM 24635 H H62  . NAG   H  3 .   ? 62.369 2.028   -27.413 0.00 23.49  ? 1    NAG   H H62  1 
HETATM 24636 H H81  . NAG   H  3 .   ? 56.248 1.175   -34.573 0.00 22.91  ? 1    NAG   H H81  1 
HETATM 24637 H H82  . NAG   H  3 .   ? 56.631 -0.123  -33.477 0.00 23.15  ? 1    NAG   H H82  1 
HETATM 24638 H H83  . NAG   H  3 .   ? 57.757 0.296   -34.742 0.00 23.05  ? 1    NAG   H H83  1 
HETATM 24639 H HN2  . NAG   H  3 .   ? 58.937 0.142   -32.386 0.00 22.46  ? 1    NAG   H HN2  1 
HETATM 24640 H HO3  . NAG   H  3 .   ? 62.102 2.602   -33.303 0.00 21.74  ? 1    NAG   H HO3  1 
HETATM 24641 H HO6  . NAG   H  3 .   ? 62.763 4.267   -27.421 0.00 23.17  ? 1    NAG   H HO6  1 
HETATM 24642 C C1   . NAG   H  3 .   ? 64.049 3.598   -31.132 1.00 26.38  ? 2    NAG   H C1   1 
HETATM 24643 C C2   . NAG   H  3 .   ? 65.514 3.212   -31.325 1.00 27.21  ? 2    NAG   H C2   1 
HETATM 24644 C C3   . NAG   H  3 .   ? 66.352 4.480   -31.167 1.00 29.17  ? 2    NAG   H C3   1 
HETATM 24645 C C4   . NAG   H  3 .   ? 65.879 5.559   -32.137 1.00 31.28  ? 2    NAG   H C4   1 
HETATM 24646 C C5   . NAG   H  3 .   ? 64.388 5.818   -31.933 1.00 30.21  ? 2    NAG   H C5   1 
HETATM 24647 C C6   . NAG   H  3 .   ? 63.801 6.794   -32.933 1.00 31.54  ? 2    NAG   H C6   1 
HETATM 24648 C C7   . NAG   H  3 .   ? 66.036 0.916   -30.598 1.00 26.27  ? 2    NAG   H C7   1 
HETATM 24649 C C8   . NAG   H  3 .   ? 66.414 0.044   -29.436 1.00 25.90  ? 2    NAG   H C8   1 
HETATM 24650 N N2   . NAG   H  3 .   ? 65.896 2.223   -30.331 1.00 26.11  ? 2    NAG   H N2   1 
HETATM 24651 O O3   . NAG   H  3 .   ? 67.713 4.146   -31.420 1.00 28.85  ? 2    NAG   H O3   1 
HETATM 24652 O O4   . NAG   H  3 .   ? 66.586 6.773   -31.916 1.00 34.75  ? 2    NAG   H O4   1 
HETATM 24653 O O5   . NAG   H  3 .   ? 63.669 4.586   -32.087 1.00 27.85  ? 2    NAG   H O5   1 
HETATM 24654 O O6   . NAG   H  3 .   ? 62.440 7.093   -32.631 1.00 32.28  ? 2    NAG   H O6   1 
HETATM 24655 O O7   . NAG   H  3 .   ? 65.859 0.457   -31.722 1.00 26.51  ? 2    NAG   H O7   1 
HETATM 24656 H H2   . NAG   H  3 .   ? 65.668 2.835   -32.335 0.00 29.88  ? 2    NAG   H H2   1 
HETATM 24657 H H3   . NAG   H  3 .   ? 66.261 4.854   -30.148 0.00 32.83  ? 2    NAG   H H3   1 
HETATM 24658 H H4   . NAG   H  3 .   ? 66.022 5.170   -33.145 0.00 34.69  ? 2    NAG   H H4   1 
HETATM 24659 H H5   . NAG   H  3 .   ? 64.218 6.205   -30.929 0.00 33.53  ? 2    NAG   H H5   1 
HETATM 24660 H H61  . NAG   H  3 .   ? 63.757 6.340   -33.922 0.00 34.47  ? 2    NAG   H H61  1 
HETATM 24661 H H62  . NAG   H  3 .   ? 64.394 7.704   -33.015 0.00 34.82  ? 2    NAG   H H62  1 
HETATM 24662 H H81  . NAG   H  3 .   ? 66.830 -0.917  -29.732 0.00 29.26  ? 2    NAG   H H81  1 
HETATM 24663 H H82  . NAG   H  3 .   ? 65.546 -0.178  -28.817 0.00 29.13  ? 2    NAG   H H82  1 
HETATM 24664 H H83  . NAG   H  3 .   ? 67.143 0.528   -28.788 0.00 29.48  ? 2    NAG   H H83  1 
HETATM 24665 H HN2  . NAG   H  3 .   ? 66.057 2.573   -29.392 0.00 29.27  ? 2    NAG   H HN2  1 
HETATM 24666 H HO3  . NAG   H  3 .   ? 68.155 4.991   -31.696 0.00 32.54  ? 2    NAG   H HO3  1 
HETATM 24667 H HO6  . NAG   H  3 .   ? 61.961 6.230   -32.520 0.00 35.30  ? 2    NAG   H HO6  1 
HETATM 24668 C C1   . BMA   H  3 .   ? 67.206 7.385   -33.032 1.00 38.55  ? 3    BMA   H C1   1 
HETATM 24669 C C2   . BMA   H  3 .   ? 67.417 8.861   -32.725 1.00 40.69  ? 3    BMA   H C2   1 
HETATM 24670 C C3   . BMA   H  3 .   ? 68.130 9.537   -33.891 1.00 42.38  ? 3    BMA   H C3   1 
HETATM 24671 C C4   . BMA   H  3 .   ? 69.421 8.805   -34.226 1.00 42.40  ? 3    BMA   H C4   1 
HETATM 24672 C C5   . BMA   H  3 .   ? 69.133 7.322   -34.453 1.00 41.78  ? 3    BMA   H C5   1 
HETATM 24673 C C6   . BMA   H  3 .   ? 70.385 6.500   -34.655 1.00 42.18  ? 3    BMA   H C6   1 
HETATM 24674 O O2   . BMA   H  3 .   ? 68.178 8.994   -31.530 1.00 41.04  ? 3    BMA   H O2   1 
HETATM 24675 O O3   . BMA   H  3 .   ? 68.405 10.904  -33.594 1.00 43.65  ? 3    BMA   H O3   1 
HETATM 24676 O O4   . BMA   H  3 .   ? 69.969 9.353   -35.420 1.00 43.01  ? 3    BMA   H O4   1 
HETATM 24677 O O5   . BMA   H  3 .   ? 68.460 6.767   -33.310 1.00 40.25  ? 3    BMA   H O5   1 
HETATM 24678 O O6   . BMA   H  3 .   ? 71.203 6.519   -33.494 1.00 42.38  ? 3    BMA   H O6   1 
HETATM 24679 H H2   . BMA   H  3 .   ? 66.445 9.336   -32.600 0.00 46.42  ? 3    BMA   H H2   1 
HETATM 24680 H H3   . BMA   H  3 .   ? 67.469 9.604   -34.754 0.00 48.28  ? 3    BMA   H H3   1 
HETATM 24681 H H4   . BMA   H  3 .   ? 70.138 8.920   -33.414 0.00 49.14  ? 3    BMA   H H4   1 
HETATM 24682 H H5   . BMA   H  3 .   ? 68.489 7.196   -35.322 0.00 47.51  ? 3    BMA   H H5   1 
HETATM 24683 H H61  . BMA   H  3 .   ? 70.926 6.793   -35.554 0.00 48.53  ? 3    BMA   H H61  1 
HETATM 24684 H H62  . BMA   H  3 .   ? 70.126 5.450   -34.774 0.00 48.42  ? 3    BMA   H H62  1 
HETATM 24685 H HO2  . BMA   H  3 .   ? 68.348 9.967   -31.428 0.00 47.58  ? 3    BMA   H HO2  1 
HETATM 24686 H HO3  . BMA   H  3 .   ? 69.258 11.165  -34.030 0.00 50.55  ? 3    BMA   H HO3  1 
HETATM 24687 H HO4  . BMA   H  3 .   ? 70.942 9.156   -35.463 0.00 49.70  ? 3    BMA   H HO4  1 
HETATM 24688 H HO6  . BMA   H  3 .   ? 70.682 6.109   -32.755 0.00 49.23  ? 3    BMA   H HO6  1 
HETATM 24689 C C1   . NAG   I  4 .   ? 6.993  33.814  -19.078 1.00 62.63  ? 901  NAG   A C1   1 
HETATM 24690 C C2   . NAG   I  4 .   ? 7.225  35.312  -18.869 1.00 63.38  ? 901  NAG   A C2   1 
HETATM 24691 C C3   . NAG   I  4 .   ? 6.087  36.040  -19.581 1.00 63.75  ? 901  NAG   A C3   1 
HETATM 24692 C C4   . NAG   I  4 .   ? 6.083  35.696  -21.065 1.00 63.75  ? 901  NAG   A C4   1 
HETATM 24693 C C5   . NAG   I  4 .   ? 6.008  34.182  -21.247 1.00 63.54  ? 901  NAG   A C5   1 
HETATM 24694 C C6   . NAG   I  4 .   ? 6.191  33.760  -22.688 1.00 63.79  ? 901  NAG   A C6   1 
HETATM 24695 C C7   . NAG   I  4 .   ? 8.355  35.774  -16.722 1.00 63.98  ? 901  NAG   A C7   1 
HETATM 24696 C C8   . NAG   I  4 .   ? 8.159  36.190  -15.295 1.00 64.13  ? 901  NAG   A C8   1 
HETATM 24697 N N2   . NAG   I  4 .   ? 7.240  35.665  -17.457 1.00 63.73  ? 901  NAG   A N2   1 
HETATM 24698 O O3   . NAG   I  4 .   ? 6.244  37.443  -19.403 1.00 63.92  ? 901  NAG   A O3   1 
HETATM 24699 O O4   . NAG   I  4 .   ? 4.953  36.301  -21.690 1.00 63.93  ? 901  NAG   A O4   1 
HETATM 24700 O O5   . NAG   I  4 .   ? 7.044  33.537  -20.483 1.00 63.15  ? 901  NAG   A O5   1 
HETATM 24701 O O6   . NAG   I  4 .   ? 6.145  32.349  -22.841 1.00 64.20  ? 901  NAG   A O6   1 
HETATM 24702 O O7   . NAG   I  4 .   ? 9.468  35.549  -17.185 1.00 64.07  ? 901  NAG   A O7   1 
HETATM 24703 H H2   . NAG   I  4 .   ? 8.154  35.615  -19.350 0.00 90.46  ? 901  NAG   A H2   1 
HETATM 24704 H H3   . NAG   I  4 .   ? 5.135  35.735  -19.149 0.00 92.60  ? 901  NAG   A H3   1 
HETATM 24705 H H4   . NAG   I  4 .   ? 7.013  36.063  -21.498 0.00 91.53  ? 901  NAG   A H4   1 
HETATM 24706 H H5   . NAG   I  4 .   ? 5.040  33.821  -20.902 0.00 90.90  ? 901  NAG   A H5   1 
HETATM 24707 H H61  . NAG   I  4 .   ? 7.187  34.020  -23.037 0.00 89.98  ? 901  NAG   A H61  1 
HETATM 24708 H H62  . NAG   I  4 .   ? 5.475  34.250  -23.346 0.00 91.02  ? 901  NAG   A H62  1 
HETATM 24709 H H81  . NAG   I  4 .   ? 9.090  36.368  -14.758 0.00 92.20  ? 901  NAG   A H81  1 
HETATM 24710 H H82  . NAG   I  4 .   ? 7.626  35.423  -14.734 0.00 92.21  ? 901  NAG   A H82  1 
HETATM 24711 H H83  . NAG   I  4 .   ? 7.563  37.098  -15.219 0.00 93.35  ? 901  NAG   A H83  1 
HETATM 24712 H HN2  . NAG   I  4 .   ? 6.333  35.837  -17.033 0.00 92.32  ? 901  NAG   A HN2  1 
HETATM 24713 H HO3  . NAG   I  4 .   ? 5.585  37.872  -20.011 0.00 93.96  ? 901  NAG   A HO3  1 
HETATM 24714 H HO4  . NAG   I  4 .   ? 5.157  36.392  -22.658 0.00 92.86  ? 901  NAG   A HO4  1 
HETATM 24715 H HO6  . NAG   I  4 .   ? 5.280  32.031  -22.472 0.00 90.25  ? 901  NAG   A HO6  1 
HETATM 24716 C C1   . NAG   J  4 .   ? 29.302 29.161  -0.096  1.00 37.12  ? 902  NAG   A C1   1 
HETATM 24717 C C2   . NAG   J  4 .   ? 30.327 29.029  1.035   1.00 37.66  ? 902  NAG   A C2   1 
HETATM 24718 C C3   . NAG   J  4 .   ? 29.988 30.030  2.144   1.00 37.41  ? 902  NAG   A C3   1 
HETATM 24719 C C4   . NAG   J  4 .   ? 29.868 31.444  1.587   1.00 38.07  ? 902  NAG   A C4   1 
HETATM 24720 C C5   . NAG   J  4 .   ? 28.894 31.457  0.415   1.00 38.47  ? 902  NAG   A C5   1 
HETATM 24721 C C6   . NAG   J  4 .   ? 28.816 32.787  -0.294  1.00 39.72  ? 902  NAG   A C6   1 
HETATM 24722 C C7   . NAG   J  4 .   ? 31.463 26.943  1.703   1.00 39.02  ? 902  NAG   A C7   1 
HETATM 24723 C C8   . NAG   J  4 .   ? 31.301 25.618  2.388   1.00 39.46  ? 902  NAG   A C8   1 
HETATM 24724 N N2   . NAG   J  4 .   ? 30.349 27.681  1.581   1.00 38.19  ? 902  NAG   A N2   1 
HETATM 24725 O O3   . NAG   J  4 .   ? 31.009 29.999  3.139   1.00 36.46  ? 902  NAG   A O3   1 
HETATM 24726 O O4   . NAG   J  4 .   ? 29.381 32.321  2.597   1.00 38.50  ? 902  NAG   A O4   1 
HETATM 24727 O O5   . NAG   J  4 .   ? 29.353 30.515  -0.554  1.00 37.59  ? 902  NAG   A O5   1 
HETATM 24728 O O6   . NAG   J  4 .   ? 28.105 32.675  -1.523  1.00 40.54  ? 902  NAG   A O6   1 
HETATM 24729 O O7   . NAG   J  4 .   ? 32.547 27.321  1.272   1.00 39.21  ? 902  NAG   A O7   1 
HETATM 24730 H H2   . NAG   J  4 .   ? 31.306 29.304  0.648   0.00 54.98  ? 902  NAG   A H2   1 
HETATM 24731 H H3   . NAG   J  4 .   ? 29.034 29.750  2.588   0.00 55.95  ? 902  NAG   A H3   1 
HETATM 24732 H H4   . NAG   J  4 .   ? 30.853 31.755  1.240   0.00 57.17  ? 902  NAG   A H4   1 
HETATM 24733 H H5   . NAG   J  4 .   ? 27.897 31.182  0.757   0.00 57.40  ? 902  NAG   A H5   1 
HETATM 24734 H H61  . NAG   J  4 .   ? 29.809 33.115  -0.599  0.00 59.26  ? 902  NAG   A H61  1 
HETATM 24735 H H62  . NAG   J  4 .   ? 28.395 33.562  0.345   0.00 60.11  ? 902  NAG   A H62  1 
HETATM 24736 H H81  . NAG   J  4 .   ? 32.155 24.955  2.261   0.00 55.58  ? 902  NAG   A H81  1 
HETATM 24737 H H82  . NAG   J  4 .   ? 30.441 25.079  1.994   0.00 55.61  ? 902  NAG   A H82  1 
HETATM 24738 H H83  . NAG   J  4 .   ? 31.135 25.734  3.459   0.00 56.55  ? 902  NAG   A H83  1 
HETATM 24739 H HN2  . NAG   J  4 .   ? 29.454 27.305  1.877   0.00 55.15  ? 902  NAG   A HN2  1 
HETATM 24740 H HO3  . NAG   J  4 .   ? 30.639 30.444  3.945   0.00 55.72  ? 902  NAG   A HO3  1 
HETATM 24741 H HO4  . NAG   J  4 .   ? 29.659 33.245  2.358   0.00 59.21  ? 902  NAG   A HO4  1 
HETATM 24742 H HO6  . NAG   J  4 .   ? 27.466 31.919  -1.442  0.00 59.45  ? 902  NAG   A HO6  1 
HETATM 24743 C C1   . NAG   K  4 .   ? -0.009 1.446   -9.293  1.00 45.54  ? 903  NAG   A C1   1 
HETATM 24744 C C2   . NAG   K  4 .   ? -0.355 2.741   -8.557  1.00 46.21  ? 903  NAG   A C2   1 
HETATM 24745 C C3   . NAG   K  4 .   ? -1.808 3.051   -8.910  1.00 46.96  ? 903  NAG   A C3   1 
HETATM 24746 C C4   . NAG   K  4 .   ? -1.940 3.273   -10.412 1.00 47.25  ? 903  NAG   A C4   1 
HETATM 24747 C C5   . NAG   K  4 .   ? -1.374 2.070   -11.164 1.00 47.18  ? 903  NAG   A C5   1 
HETATM 24748 C C6   . NAG   K  4 .   ? -1.270 2.302   -12.655 1.00 47.53  ? 903  NAG   A C6   1 
HETATM 24749 C C7   . NAG   K  4 .   ? 0.400  3.529   -6.351  1.00 46.37  ? 903  NAG   A C7   1 
HETATM 24750 C C8   . NAG   K  4 .   ? 0.455  3.229   -4.884  1.00 46.05  ? 903  NAG   A C8   1 
HETATM 24751 N N2   . NAG   K  4 .   ? -0.196 2.604   -7.117  1.00 46.38  ? 903  NAG   A N2   1 
HETATM 24752 O O3   . NAG   K  4 .   ? -2.239 4.209   -8.203  1.00 47.19  ? 903  NAG   A O3   1 
HETATM 24753 O O4   . NAG   K  4 .   ? -3.313 3.449   -10.752 1.00 47.61  ? 903  NAG   A O4   1 
HETATM 24754 O O5   . NAG   K  4 .   ? -0.047 1.768   -10.687 1.00 46.61  ? 903  NAG   A O5   1 
HETATM 24755 O O6   . NAG   K  4 .   ? -0.552 1.257   -13.308 1.00 47.79  ? 903  NAG   A O6   1 
HETATM 24756 O O7   . NAG   K  4 .   ? 0.864  4.564   -6.820  1.00 46.49  ? 903  NAG   A O7   1 
HETATM 24757 H H2   . NAG   K  4 .   ? 0.264  3.544   -8.952  0.00 62.51  ? 903  NAG   A H2   1 
HETATM 24758 H H3   . NAG   K  4 .   ? -2.435 2.207   -8.625  0.00 64.82  ? 903  NAG   A H3   1 
HETATM 24759 H H4   . NAG   K  4 .   ? -1.362 4.160   -10.669 0.00 64.45  ? 903  NAG   A H4   1 
HETATM 24760 H H5   . NAG   K  4 .   ? -2.010 1.202   -10.995 0.00 64.30  ? 903  NAG   A H5   1 
HETATM 24761 H H61  . NAG   K  4 .   ? -0.690 3.199   -12.863 0.00 63.91  ? 903  NAG   A H61  1 
HETATM 24762 H H62  . NAG   K  4 .   ? -2.253 2.443   -13.102 0.00 64.68  ? 903  NAG   A H62  1 
HETATM 24763 H H81  . NAG   K  4 .   ? 0.833  4.055   -4.284  0.00 63.17  ? 903  NAG   A H81  1 
HETATM 24764 H H82  . NAG   K  4 .   ? 1.108  2.381   -4.682  0.00 62.69  ? 903  NAG   A H82  1 
HETATM 24765 H H83  . NAG   K  4 .   ? -0.526 2.964   -4.490  0.00 63.67  ? 903  NAG   A H83  1 
HETATM 24766 H HN2  . NAG   K  4 .   ? -0.564 1.755   -6.701  0.00 63.40  ? 903  NAG   A HN2  1 
HETATM 24767 H HO3  . NAG   K  4 .   ? -3.188 4.348   -8.463  0.00 65.87  ? 903  NAG   A HO3  1 
HETATM 24768 H HO4  . NAG   K  4 .   ? -3.352 3.940   -11.614 0.00 65.86  ? 903  NAG   A HO4  1 
HETATM 24769 H HO6  . NAG   K  4 .   ? -0.867 0.392   -12.935 0.00 64.01  ? 903  NAG   A HO6  1 
HETATM 24770 C C1   . NAG   L  4 .   ? 5.953  -14.015 -31.782 1.00 33.52  ? 904  NAG   A C1   1 
HETATM 24771 C C2   . NAG   L  4 .   ? 4.898  -14.231 -30.696 1.00 33.93  ? 904  NAG   A C2   1 
HETATM 24772 C C3   . NAG   L  4 .   ? 3.547  -13.787 -31.256 1.00 34.12  ? 904  NAG   A C3   1 
HETATM 24773 C C4   . NAG   L  4 .   ? 3.611  -12.353 -31.774 1.00 34.38  ? 904  NAG   A C4   1 
HETATM 24774 C C5   . NAG   L  4 .   ? 4.749  -12.215 -32.782 1.00 34.69  ? 904  NAG   A C5   1 
HETATM 24775 C C6   . NAG   L  4 .   ? 4.960  -10.798 -33.271 1.00 35.53  ? 904  NAG   A C6   1 
HETATM 24776 C C7   . NAG   L  4 .   ? 5.184  -16.151 -29.163 1.00 35.15  ? 904  NAG   A C7   1 
HETATM 24777 C C8   . NAG   L  4 .   ? 5.133  -17.646 -29.042 1.00 35.13  ? 904  NAG   A C8   1 
HETATM 24778 N N2   . NAG   L  4 .   ? 4.862  -15.648 -30.366 1.00 34.74  ? 904  NAG   A N2   1 
HETATM 24779 O O3   . NAG   L  4 .   ? 2.578  -13.872 -30.221 1.00 34.11  ? 904  NAG   A O3   1 
HETATM 24780 O O4   . NAG   L  4 .   ? 2.384  -12.026 -32.415 1.00 34.27  ? 904  NAG   A O4   1 
HETATM 24781 O O5   . NAG   L  4 .   ? 5.981  -12.640 -32.174 1.00 33.95  ? 904  NAG   A O5   1 
HETATM 24782 O O6   . NAG   L  4 .   ? 5.058  -9.872  -32.190 1.00 36.29  ? 904  NAG   A O6   1 
HETATM 24783 O O7   . NAG   L  4 .   ? 5.487  -15.434 -28.216 1.00 35.54  ? 904  NAG   A O7   1 
HETATM 24784 H H2   . NAG   L  4 .   ? 5.128  -13.614 -29.829 0.00 44.33  ? 904  NAG   A H2   1 
HETATM 24785 H H3   . NAG   L  4 .   ? 3.258  -14.445 -32.074 0.00 45.88  ? 904  NAG   A H3   1 
HETATM 24786 H H4   . NAG   L  4 .   ? 3.794  -11.699 -30.922 0.00 45.32  ? 904  NAG   A H4   1 
HETATM 24787 H H5   . NAG   L  4 .   ? 4.545  -12.844 -33.648 0.00 45.76  ? 904  NAG   A H5   1 
HETATM 24788 H H61  . NAG   L  4 .   ? 4.083  -10.454 -33.817 0.00 46.67  ? 904  NAG   A H61  1 
HETATM 24789 H H62  . NAG   L  4 .   ? 5.808  -10.744 -33.953 0.00 45.87  ? 904  NAG   A H62  1 
HETATM 24790 H H81  . NAG   L  4 .   ? 5.493  -18.027 -28.087 0.00 46.46  ? 904  NAG   A H81  1 
HETATM 24791 H H82  . NAG   L  4 .   ? 5.744  -18.121 -29.808 0.00 46.47  ? 904  NAG   A H82  1 
HETATM 24792 H H83  . NAG   L  4 .   ? 4.121  -18.023 -29.179 0.00 47.20  ? 904  NAG   A H83  1 
HETATM 24793 H HN2  . NAG   L  4 .   ? 4.577  -16.270 -31.115 0.00 46.23  ? 904  NAG   A HN2  1 
HETATM 24794 H HO3  . NAG   L  4 .   ? 1.779  -13.383 -30.553 0.00 46.14  ? 904  NAG   A HO3  1 
HETATM 24795 H HO4  . NAG   L  4 .   ? 2.325  -11.035 -32.438 0.00 46.08  ? 904  NAG   A HO4  1 
HETATM 24796 H HO6  . NAG   L  4 .   ? 5.829  -9.262  -32.338 0.00 46.31  ? 904  NAG   A HO6  1 
HETATM 24797 C C1   . NAG   M  4 .   ? 15.672 -29.230 -37.223 1.00 61.01  ? 905  NAG   A C1   1 
HETATM 24798 C C2   . NAG   M  4 .   ? 16.104 -30.518 -36.515 1.00 62.06  ? 905  NAG   A C2   1 
HETATM 24799 C C3   . NAG   M  4 .   ? 14.837 -31.237 -36.053 1.00 62.54  ? 905  NAG   A C3   1 
HETATM 24800 C C4   . NAG   M  4 .   ? 14.017 -30.338 -35.135 1.00 62.59  ? 905  NAG   A C4   1 
HETATM 24801 C C5   . NAG   M  4 .   ? 13.697 -29.031 -35.856 1.00 62.27  ? 905  NAG   A C5   1 
HETATM 24802 C C6   . NAG   M  4 .   ? 13.003 -28.014 -34.973 1.00 62.46  ? 905  NAG   A C6   1 
HETATM 24803 C C7   . NAG   M  4 .   ? 18.195 -31.258 -37.595 1.00 62.86  ? 905  NAG   A C7   1 
HETATM 24804 C C8   . NAG   M  4 .   ? 18.807 -32.229 -38.560 1.00 62.93  ? 905  NAG   A C8   1 
HETATM 24805 N N2   . NAG   M  4 .   ? 16.877 -31.384 -37.393 1.00 62.59  ? 905  NAG   A N2   1 
HETATM 24806 O O3   . NAG   M  4 .   ? 15.185 -32.444 -35.383 1.00 62.75  ? 905  NAG   A O3   1 
HETATM 24807 O O4   . NAG   M  4 .   ? 12.801 -31.000 -34.792 1.00 62.81  ? 905  NAG   A O4   1 
HETATM 24808 O O5   . NAG   M  4 .   ? 14.912 -28.418 -36.324 1.00 61.64  ? 905  NAG   A O5   1 
HETATM 24809 O O6   . NAG   M  4 .   ? 12.468 -26.930 -35.723 1.00 62.65  ? 905  NAG   A O6   1 
HETATM 24810 O O7   . NAG   M  4 .   ? 18.858 -30.392 -37.037 1.00 62.92  ? 905  NAG   A O7   1 
HETATM 24811 H H2   . NAG   M  4 .   ? 16.684 -30.272 -35.627 0.00 80.00  ? 905  NAG   A H2   1 
HETATM 24812 H H3   . NAG   M  4 .   ? 14.230 -31.486 -36.922 0.00 82.16  ? 905  NAG   A H3   1 
HETATM 24813 H H4   . NAG   M  4 .   ? 14.611 -30.122 -34.248 0.00 81.01  ? 905  NAG   A H4   1 
HETATM 24814 H H5   . NAG   M  4 .   ? 13.063 -29.248 -36.715 0.00 81.06  ? 905  NAG   A H5   1 
HETATM 24815 H H61  . NAG   M  4 .   ? 13.727 -27.533 -34.317 0.00 79.91  ? 905  NAG   A H61  1 
HETATM 24816 H H62  . NAG   M  4 .   ? 12.242 -28.470 -34.340 0.00 80.87  ? 905  NAG   A H62  1 
HETATM 24817 H H81  . NAG   M  4 .   ? 19.895 -32.184 -38.597 0.00 81.66  ? 905  NAG   A H81  1 
HETATM 24818 H H82  . NAG   M  4 .   ? 18.460 -32.041 -39.575 0.00 82.10  ? 905  NAG   A H82  1 
HETATM 24819 H H83  . NAG   M  4 .   ? 18.533 -33.257 -38.326 0.00 82.57  ? 905  NAG   A H83  1 
HETATM 24820 H HN2  . NAG   M  4 .   ? 16.357 -32.117 -37.864 0.00 82.04  ? 905  NAG   A HN2  1 
HETATM 24821 H HO3  . NAG   M  4 .   ? 15.733 -32.180 -34.598 0.00 81.99  ? 905  NAG   A HO3  1 
HETATM 24822 H HO4  . NAG   M  4 .   ? 12.473 -30.604 -33.942 0.00 82.20  ? 905  NAG   A HO4  1 
HETATM 24823 H HO6  . NAG   M  4 .   ? 12.993 -26.851 -36.562 0.00 80.40  ? 905  NAG   A HO6  1 
HETATM 24824 C C1   . NAG   N  4 .   ? 40.360 -14.103 -62.224 1.00 38.22  ? 906  NAG   A C1   1 
HETATM 24825 C C2   . NAG   N  4 .   ? 41.218 -14.455 -63.442 1.00 39.81  ? 906  NAG   A C2   1 
HETATM 24826 C C3   . NAG   N  4 .   ? 40.597 -15.614 -64.219 1.00 40.28  ? 906  NAG   A C3   1 
HETATM 24827 C C4   . NAG   N  4 .   ? 40.327 -16.793 -63.295 1.00 40.68  ? 906  NAG   A C4   1 
HETATM 24828 C C5   . NAG   N  4 .   ? 39.503 -16.327 -62.097 1.00 40.55  ? 906  NAG   A C5   1 
HETATM 24829 C C6   . NAG   N  4 .   ? 39.231 -17.426 -61.087 1.00 41.61  ? 906  NAG   A C6   1 
HETATM 24830 C C7   . NAG   N  4 .   ? 42.566 -12.760 -64.617 1.00 41.92  ? 906  NAG   A C7   1 
HETATM 24831 C C8   . NAG   N  4 .   ? 42.551 -11.702 -65.680 1.00 42.19  ? 906  NAG   A C8   1 
HETATM 24832 N N2   . NAG   N  4 .   ? 41.378 -13.300 -64.312 1.00 40.86  ? 906  NAG   A N2   1 
HETATM 24833 O O3   . NAG   N  4 .   ? 41.504 -16.008 -65.242 1.00 40.42  ? 906  NAG   A O3   1 
HETATM 24834 O O4   . NAG   N  4 .   ? 39.611 -17.791 -64.016 1.00 41.26  ? 906  NAG   A O4   1 
HETATM 24835 O O5   . NAG   N  4 .   ? 40.212 -15.274 -61.416 1.00 39.03  ? 906  NAG   A O5   1 
HETATM 24836 O O6   . NAG   N  4 .   ? 40.434 -17.890 -60.480 1.00 42.59  ? 906  NAG   A O6   1 
HETATM 24837 O O7   . NAG   N  4 .   ? 43.607 -13.120 -64.075 1.00 42.43  ? 906  NAG   A O7   1 
HETATM 24838 H H2   . NAG   N  4 .   ? 42.192 -14.777 -63.081 0.00 50.00  ? 906  NAG   A H2   1 
HETATM 24839 H H3   . NAG   N  4 .   ? 39.663 -15.286 -64.672 0.00 51.36  ? 906  NAG   A H3   1 
HETATM 24840 H H4   . NAG   N  4 .   ? 41.284 -17.175 -62.942 0.00 51.80  ? 906  NAG   A H4   1 
HETATM 24841 H H5   . NAG   N  4 .   ? 38.543 -15.948 -62.444 0.00 51.09  ? 906  NAG   A H5   1 
HETATM 24842 H H61  . NAG   N  4 .   ? 38.848 -18.315 -61.586 0.00 52.88  ? 906  NAG   A H61  1 
HETATM 24843 H H62  . NAG   N  4 .   ? 38.486 -17.135 -60.349 0.00 52.02  ? 906  NAG   A H62  1 
HETATM 24844 H H81  . NAG   N  4 .   ? 43.525 -11.523 -66.133 0.00 53.05  ? 906  NAG   A H81  1 
HETATM 24845 H H82  . NAG   N  4 .   ? 42.220 -10.746 -65.276 0.00 52.49  ? 906  NAG   A H82  1 
HETATM 24846 H H83  . NAG   N  4 .   ? 41.860 -11.949 -66.485 0.00 53.30  ? 906  NAG   A H83  1 
HETATM 24847 H HN2  . NAG   N  4 .   ? 40.523 -12.905 -64.692 0.00 51.31  ? 906  NAG   A HN2  1 
HETATM 24848 H HO3  . NAG   N  4 .   ? 41.055 -16.742 -65.737 0.00 52.43  ? 906  NAG   A HO3  1 
HETATM 24849 H HO4  . NAG   N  4 .   ? 39.774 -18.665 -63.572 0.00 53.32  ? 906  NAG   A HO4  1 
HETATM 24850 H HO6  . NAG   N  4 .   ? 41.014 -17.100 -60.319 0.00 53.14  ? 906  NAG   A HO6  1 
HETATM 24851 C C1   . NAG   O  4 .   ? 32.262 -7.526  -66.058 1.00 45.93  ? 907  NAG   A C1   1 
HETATM 24852 C C2   . NAG   O  4 .   ? 31.988 -8.866  -66.743 1.00 46.82  ? 907  NAG   A C2   1 
HETATM 24853 C C3   . NAG   O  4 .   ? 32.882 -8.914  -67.979 1.00 47.02  ? 907  NAG   A C3   1 
HETATM 24854 C C4   . NAG   O  4 .   ? 32.507 -7.785  -68.925 1.00 47.09  ? 907  NAG   A C4   1 
HETATM 24855 C C5   . NAG   O  4 .   ? 32.561 -6.438  -68.203 1.00 47.21  ? 907  NAG   A C5   1 
HETATM 24856 C C6   . NAG   O  4 .   ? 31.933 -5.331  -69.025 1.00 47.65  ? 907  NAG   A C6   1 
HETATM 24857 C C7   . NAG   O  4 .   ? 31.335 -10.548 -65.074 1.00 48.19  ? 907  NAG   A C7   1 
HETATM 24858 C C8   . NAG   O  4 .   ? 31.770 -11.758 -64.302 1.00 48.43  ? 907  NAG   A C8   1 
HETATM 24859 N N2   . NAG   O  4 .   ? 32.255 -10.004 -65.876 1.00 47.36  ? 907  NAG   A N2   1 
HETATM 24860 O O3   . NAG   O  4 .   ? 32.713 -10.167 -68.637 1.00 47.23  ? 907  NAG   A O3   1 
HETATM 24861 O O4   . NAG   O  4 .   ? 33.412 -7.773  -70.026 1.00 47.31  ? 907  NAG   A O4   1 
HETATM 24862 O O5   . NAG   O  4 .   ? 31.839 -6.490  -66.954 1.00 46.74  ? 907  NAG   A O5   1 
HETATM 24863 O O6   . NAG   O  4 .   ? 32.277 -4.043  -68.548 1.00 48.13  ? 907  NAG   A O6   1 
HETATM 24864 O O7   . NAG   O  4 .   ? 30.204 -10.081 -64.969 1.00 48.66  ? 907  NAG   A O7   1 
HETATM 24865 H H2   . NAG   O  4 .   ? 30.958 -8.897  -67.096 0.00 59.48  ? 907  NAG   A H2   1 
HETATM 24866 H H3   . NAG   O  4 .   ? 33.924 -8.800  -67.685 0.00 59.45  ? 907  NAG   A H3   1 
HETATM 24867 H H4   . NAG   O  4 .   ? 31.487 -7.964  -69.264 0.00 60.49  ? 907  NAG   A H4   1 
HETATM 24868 H H5   . NAG   O  4 .   ? 33.599 -6.189  -67.986 0.00 59.37  ? 907  NAG   A H5   1 
HETATM 24869 H H61  . NAG   O  4 .   ? 30.849 -5.357  -68.920 0.00 60.69  ? 907  NAG   A H61  1 
HETATM 24870 H H62  . NAG   O  4 .   ? 32.159 -5.431  -70.085 0.00 60.97  ? 907  NAG   A H62  1 
HETATM 24871 H H81  . NAG   O  4 .   ? 30.943 -12.321 -63.871 0.00 60.85  ? 907  NAG   A H81  1 
HETATM 24872 H H82  . NAG   O  4 .   ? 32.412 -11.476 -63.470 0.00 60.23  ? 907  NAG   A H82  1 
HETATM 24873 H H83  . NAG   O  4 .   ? 32.344 -12.448 -64.919 0.00 61.08  ? 907  NAG   A H83  1 
HETATM 24874 H HN2  . NAG   O  4 .   ? 33.197 -10.381 -65.907 0.00 59.56  ? 907  NAG   A HN2  1 
HETATM 24875 H HO3  . NAG   O  4 .   ? 33.418 -10.205 -69.336 0.00 60.85  ? 907  NAG   A HO3  1 
HETATM 24876 H HO4  . NAG   O  4 .   ? 32.960 -7.317  -70.784 0.00 61.08  ? 907  NAG   A HO4  1 
HETATM 24877 H HO6  . NAG   O  4 .   ? 32.125 -4.031  -67.567 0.00 60.22  ? 907  NAG   A HO6  1 
HETATM 24878 C C1   . NAG   P  4 .   ? 21.185 6.234   -60.040 1.00 30.04  ? 908  NAG   A C1   1 
HETATM 24879 C C2   . NAG   P  4 .   ? 20.735 4.872   -60.581 1.00 30.06  ? 908  NAG   A C2   1 
HETATM 24880 C C3   . NAG   P  4 .   ? 19.256 4.683   -60.230 1.00 31.19  ? 908  NAG   A C3   1 
HETATM 24881 C C4   . NAG   P  4 .   ? 19.027 4.836   -58.733 1.00 31.77  ? 908  NAG   A C4   1 
HETATM 24882 C C5   . NAG   P  4 .   ? 19.514 6.214   -58.301 1.00 31.48  ? 908  NAG   A C5   1 
HETATM 24883 C C6   . NAG   P  4 .   ? 19.409 6.453   -56.810 1.00 31.34  ? 908  NAG   A C6   1 
HETATM 24884 C C7   . NAG   P  4 .   ? 21.388 3.692   -62.658 1.00 28.13  ? 908  NAG   A C7   1 
HETATM 24885 C C8   . NAG   P  4 .   ? 21.492 3.793   -64.152 1.00 27.97  ? 908  NAG   A C8   1 
HETATM 24886 N N2   . NAG   P  4 .   ? 20.922 4.783   -62.023 1.00 28.85  ? 908  NAG   A N2   1 
HETATM 24887 O O3   . NAG   P  4 .   ? 18.820 3.393   -60.639 1.00 31.34  ? 908  NAG   A O3   1 
HETATM 24888 O O4   . NAG   P  4 .   ? 17.642 4.712   -58.418 1.00 32.27  ? 908  NAG   A O4   1 
HETATM 24889 O O5   . NAG   P  4 .   ? 20.903 6.324   -58.637 1.00 30.57  ? 908  NAG   A O5   1 
HETATM 24890 O O6   . NAG   P  4 .   ? 20.089 5.443   -56.072 1.00 31.27  ? 908  NAG   A O6   1 
HETATM 24891 O O7   . NAG   P  4 .   ? 21.722 2.678   -62.054 1.00 27.74  ? 908  NAG   A O7   1 
HETATM 24892 H H2   . NAG   P  4 .   ? 21.296 4.090   -60.073 0.00 38.15  ? 908  NAG   A H2   1 
HETATM 24893 H H3   . NAG   P  4 .   ? 18.670 5.442   -60.746 0.00 40.83  ? 908  NAG   A H3   1 
HETATM 24894 H H4   . NAG   P  4 .   ? 19.617 4.064   -58.240 0.00 40.15  ? 908  NAG   A H4   1 
HETATM 24895 H H5   . NAG   P  4 .   ? 18.958 6.988   -58.826 0.00 40.49  ? 908  NAG   A H5   1 
HETATM 24896 H H61  . NAG   P  4 .   ? 18.376 6.360   -56.479 0.00 39.69  ? 908  NAG   A H61  1 
HETATM 24897 H H62  . NAG   P  4 .   ? 19.746 7.454   -56.547 0.00 39.31  ? 908  NAG   A H62  1 
HETATM 24898 H H81  . NAG   P  4 .   ? 21.907 2.903   -64.622 0.00 37.19  ? 908  NAG   A H81  1 
HETATM 24899 H H82  . NAG   P  4 .   ? 22.135 4.622   -64.444 0.00 37.09  ? 908  NAG   A H82  1 
HETATM 24900 H H83  . NAG   P  4 .   ? 20.521 3.977   -64.611 0.00 37.73  ? 908  NAG   A H83  1 
HETATM 24901 H HN2  . NAG   P  4 .   ? 20.677 5.612   -62.554 0.00 37.95  ? 908  NAG   A HN2  1 
HETATM 24902 H HO3  . NAG   P  4 .   ? 17.847 3.410   -60.444 0.00 41.09  ? 908  NAG   A HO3  1 
HETATM 24903 H HO4  . NAG   P  4 .   ? 17.571 4.413   -57.473 0.00 41.32  ? 908  NAG   A HO4  1 
HETATM 24904 H HO6  . NAG   P  4 .   ? 20.449 5.842   -55.237 0.00 38.35  ? 908  NAG   A HO6  1 
HETATM 24905 C C1   . NAG   Q  4 .   ? 40.543 27.694  -63.944 1.00 38.01  ? 909  NAG   A C1   1 
HETATM 24906 C C2   . NAG   Q  4 .   ? 41.652 28.745  -64.010 1.00 39.32  ? 909  NAG   A C2   1 
HETATM 24907 C C3   . NAG   Q  4 .   ? 41.691 29.292  -65.438 1.00 39.51  ? 909  NAG   A C3   1 
HETATM 24908 C C4   . NAG   Q  4 .   ? 41.915 28.165  -66.441 1.00 38.98  ? 909  NAG   A C4   1 
HETATM 24909 C C5   . NAG   Q  4 .   ? 40.882 27.060  -66.244 1.00 38.34  ? 909  NAG   A C5   1 
HETATM 24910 C C6   . NAG   Q  4 .   ? 41.184 25.821  -67.057 1.00 37.81  ? 909  NAG   A C6   1 
HETATM 24911 C C7   . NAG   Q  4 .   ? 42.290 30.345  -62.249 1.00 41.69  ? 909  NAG   A C7   1 
HETATM 24912 C C8   . NAG   Q  4 .   ? 41.794 31.396  -61.300 1.00 41.69  ? 909  NAG   A C8   1 
HETATM 24913 N N2   . NAG   Q  4 .   ? 41.372 29.819  -63.071 1.00 40.62  ? 909  NAG   A N2   1 
HETATM 24914 O O3   . NAG   Q  4 .   ? 42.750 30.237  -65.553 1.00 40.03  ? 909  NAG   A O3   1 
HETATM 24915 O O4   . NAG   Q  4 .   ? 41.787 28.666  -67.769 1.00 38.94  ? 909  NAG   A O4   1 
HETATM 24916 O O5   . NAG   Q  4 .   ? 40.863 26.652  -64.870 1.00 38.00  ? 909  NAG   A O5   1 
HETATM 24917 O O6   . NAG   Q  4 .   ? 40.151 24.856  -66.935 1.00 37.40  ? 909  NAG   A O6   1 
HETATM 24918 O O7   . NAG   Q  4 .   ? 43.462 29.979  -62.258 1.00 42.27  ? 909  NAG   A O7   1 
HETATM 24919 H H2   . NAG   Q  4 .   ? 42.608 28.269  -63.798 0.00 51.83  ? 909  NAG   A H2   1 
HETATM 24920 H H3   . NAG   Q  4 .   ? 40.744 29.783  -65.662 0.00 53.51  ? 909  NAG   A H3   1 
HETATM 24921 H H4   . NAG   Q  4 .   ? 42.910 27.754  -66.273 0.00 52.02  ? 909  NAG   A H4   1 
HETATM 24922 H H5   . NAG   Q  4 .   ? 39.890 27.423  -66.514 0.00 51.48  ? 909  NAG   A H5   1 
HETATM 24923 H H61  . NAG   Q  4 .   ? 42.057 25.309  -66.655 0.00 49.87  ? 909  NAG   A H61  1 
HETATM 24924 H H62  . NAG   Q  4 .   ? 41.390 26.054  -68.101 0.00 50.74  ? 909  NAG   A H62  1 
HETATM 24925 H H81  . NAG   Q  4 .   ? 42.507 31.643  -60.515 0.00 55.24  ? 909  NAG   A H81  1 
HETATM 24926 H H82  . NAG   Q  4 .   ? 40.886 31.069  -60.795 0.00 55.16  ? 909  NAG   A H82  1 
HETATM 24927 H H83  . NAG   Q  4 .   ? 41.546 32.323  -61.816 0.00 56.02  ? 909  NAG   A H83  1 
HETATM 24928 H HN2  . NAG   Q  4 .   ? 40.418 30.168  -63.060 0.00 54.17  ? 909  NAG   A HN2  1 
HETATM 24929 H HO3  . NAG   Q  4 .   ? 42.641 30.660  -66.445 0.00 54.64  ? 909  NAG   A HO3  1 
HETATM 24930 H HO4  . NAG   Q  4 .   ? 42.287 28.058  -68.375 0.00 52.92  ? 909  NAG   A HO4  1 
HETATM 24931 H HO6  . NAG   Q  4 .   ? 40.365 24.102  -67.544 0.00 49.41  ? 909  NAG   A HO6  1 
HETATM 24932 S S    . SO4   R  5 .   ? 56.156 9.564   -47.806 1.00 99.68  ? 910  SO4   A S    1 
HETATM 24933 O O1   . SO4   R  5 .   ? 57.493 8.991   -47.932 1.00 99.68  ? 910  SO4   A O1   1 
HETATM 24934 O O2   . SO4   R  5 .   ? 55.290 9.010   -48.853 1.00 99.64  ? 910  SO4   A O2   1 
HETATM 24935 O O3   . SO4   R  5 .   ? 55.610 9.242   -46.483 1.00 99.65  ? 910  SO4   A O3   1 
HETATM 24936 O O4   . SO4   R  5 .   ? 56.234 11.017  -47.959 1.00 99.70  ? 910  SO4   A O4   1 
HETATM 24937 S S    . SO4   S  5 .   ? 31.881 -5.052  -16.712 1.00 42.01  ? 911  SO4   A S    1 
HETATM 24938 O O1   . SO4   S  5 .   ? 31.865 -5.024  -18.196 1.00 42.30  ? 911  SO4   A O1   1 
HETATM 24939 O O2   . SO4   S  5 .   ? 30.598 -5.437  -16.285 1.00 42.40  ? 911  SO4   A O2   1 
HETATM 24940 O O3   . SO4   S  5 .   ? 32.812 -6.046  -16.215 1.00 41.70  ? 911  SO4   A O3   1 
HETATM 24941 O O4   . SO4   S  5 .   ? 32.187 -3.707  -16.189 1.00 41.99  ? 911  SO4   A O4   1 
HETATM 24942 N N1   . A1BLN T  6 .   ? 50.358 -13.848 -56.724 1.00 22.34  ? 912  A1BLN A N1   1 
HETATM 24943 N N3   . A1BLN T  6 .   ? 50.310 -9.437  -58.009 1.00 20.65  ? 912  A1BLN A N3   1 
HETATM 24944 C C4   . A1BLN T  6 .   ? 49.540 -13.028 -56.103 1.00 21.86  ? 912  A1BLN A C4   1 
HETATM 24945 C C5   . A1BLN T  6 .   ? 50.054 -15.537 -61.137 1.00 29.22  ? 912  A1BLN A C5   1 
HETATM 24946 C C6   . A1BLN T  6 .   ? 51.600 -14.195 -59.818 1.00 25.62  ? 912  A1BLN A C6   1 
HETATM 24947 C C7   . A1BLN T  6 .   ? 49.622 -11.674 -56.641 1.00 21.54  ? 912  A1BLN A C7   1 
HETATM 24948 C C8   . A1BLN T  6 .   ? 50.575 -11.799 -57.659 1.00 22.17  ? 912  A1BLN A C8   1 
HETATM 24949 C C10  . A1BLN T  6 .   ? 50.884 -10.593 -58.379 1.00 21.52  ? 912  A1BLN A C10  1 
HETATM 24950 C C13  . A1BLN T  6 .   ? 44.093 -15.879 -61.600 1.00 39.83  ? 912  A1BLN A C13  1 
HETATM 24951 C C15  . A1BLN T  6 .   ? 45.235 -14.879 -61.603 1.00 39.81  ? 912  A1BLN A C15  1 
HETATM 24952 C C17  . A1BLN T  6 .   ? 54.181 -12.791 -61.970 1.00 23.33  ? 912  A1BLN A C17  1 
HETATM 24953 C C20  . A1BLN T  6 .   ? 54.543 -9.404  -59.386 1.00 20.71  ? 912  A1BLN A C20  1 
HETATM 24954 C C21  . A1BLN T  6 .   ? 53.221 -8.657  -59.400 1.00 21.06  ? 912  A1BLN A C21  1 
HETATM 24955 C C22  . A1BLN T  6 .   ? 52.403 -9.628  -61.619 1.00 22.60  ? 912  A1BLN A C22  1 
HETATM 24956 C C24  . A1BLN T  6 .   ? 52.083 -9.350  -60.150 1.00 21.68  ? 912  A1BLN A C24  1 
HETATM 24957 C C1   . A1BLN T  6 .   ? 50.734 -15.166 -62.285 1.00 27.73  ? 912  A1BLN A C1   1 
HETATM 24958 C C2   . A1BLN T  6 .   ? 51.825 -14.318 -62.228 1.00 26.45  ? 912  A1BLN A C2   1 
HETATM 24959 C C3   . A1BLN T  6 .   ? 50.505 -15.052 -59.914 1.00 27.28  ? 912  A1BLN A C3   1 
HETATM 24960 C C9   . A1BLN T  6 .   ? 52.257 -13.834 -60.999 1.00 25.08  ? 912  A1BLN A C9   1 
HETATM 24961 C C11  . A1BLN T  6 .   ? 49.419 -9.437  -56.996 1.00 20.40  ? 912  A1BLN A C11  1 
HETATM 24962 C C12  . A1BLN T  6 .   ? 45.881 -17.128 -61.077 1.00 39.49  ? 912  A1BLN A C12  1 
HETATM 24963 C C14  . A1BLN T  6 .   ? 46.433 -15.705 -61.004 1.00 38.65  ? 912  A1BLN A C14  1 
HETATM 24964 C C16  . A1BLN T  6 .   ? 55.564 -8.772  -58.410 1.00 20.79  ? 912  A1BLN A C16  1 
HETATM 24965 C C18  . A1BLN T  6 .   ? 52.069 -13.705 -58.465 1.00 23.78  ? 912  A1BLN A C18  1 
HETATM 24966 C C19  . A1BLN T  6 .   ? 48.802 -16.375 -61.224 1.00 32.60  ? 912  A1BLN A C19  1 
HETATM 24967 C C23  . A1BLN T  6 .   ? 51.240 -10.215 -62.387 1.00 23.49  ? 912  A1BLN A C23  1 
HETATM 24968 N N2   . A1BLN T  6 .   ? 49.028 -10.517 -56.288 1.00 20.72  ? 912  A1BLN A N2   1 
HETATM 24969 N N4   . A1BLN T  6 .   ? 51.004 -13.099 -57.671 1.00 22.92  ? 912  A1BLN A N4   1 
HETATM 24970 N N5   . A1BLN T  6 .   ? 48.908 -8.256  -56.639 1.00 19.88  ? 912  A1BLN A N5   1 
HETATM 24971 N N6   . A1BLN T  6 .   ? 51.694 -10.576 -59.460 1.00 21.46  ? 912  A1BLN A N6   1 
HETATM 24972 N N7   . A1BLN T  6 .   ? 47.685 -15.593 -61.768 1.00 35.78  ? 912  A1BLN A N7   1 
HETATM 24973 O O1   . A1BLN T  6 .   ? 44.507 -16.968 -60.786 1.00 39.95  ? 912  A1BLN A O1   1 
HETATM 24974 O O2   . A1BLN T  6 .   ? 44.885 -13.749 -60.795 1.00 40.75  ? 912  A1BLN A O2   1 
HETATM 24975 O O3   . A1BLN T  6 .   ? 51.625 -10.593 -63.701 1.00 24.61  ? 912  A1BLN A O3   1 
HETATM 24976 O O4   . A1BLN T  6 .   ? 53.338 -13.014 -60.840 1.00 24.06  ? 912  A1BLN A O4   1 
HETATM 24977 H H4   . A1BLN T  6 .   ? 48.892 -13.342 -55.288 0.00 26.23  ? 912  A1BLN A H4   1 
HETATM 24978 H H8   . A1BLN T  6 .   ? 43.881 -16.259 -62.598 0.00 47.80  ? 912  A1BLN A H8   1 
HETATM 24979 H H7   . A1BLN T  6 .   ? 43.165 -15.525 -61.153 0.00 47.80  ? 912  A1BLN A H7   1 
HETATM 24980 H H10  . A1BLN T  6 .   ? 45.426 -14.535 -62.619 0.00 47.77  ? 912  A1BLN A H10  1 
HETATM 24981 H H14  . A1BLN T  6 .   ? 54.940 -12.116 -61.583 0.00 27.99  ? 912  A1BLN A H14  1 
HETATM 24982 H H15  . A1BLN T  6 .   ? 53.668 -12.300 -62.796 0.00 27.99  ? 912  A1BLN A H15  1 
HETATM 24983 H H16  . A1BLN T  6 .   ? 54.665 -13.700 -62.324 0.00 27.99  ? 912  A1BLN A H16  1 
HETATM 24984 H H22  . A1BLN T  6 .   ? 54.976 -9.442  -60.384 0.00 24.86  ? 912  A1BLN A H22  1 
HETATM 24985 H H21  . A1BLN T  6 .   ? 54.389 -10.444 -59.108 0.00 24.86  ? 912  A1BLN A H21  1 
HETATM 24986 H H23  . A1BLN T  6 .   ? 52.893 -8.533  -58.372 0.00 25.28  ? 912  A1BLN A H23  1 
HETATM 24987 H H24  . A1BLN T  6 .   ? 53.388 -7.651  -59.779 0.00 25.28  ? 912  A1BLN A H24  1 
HETATM 24988 H H26  . A1BLN T  6 .   ? 52.738 -8.711  -62.101 0.00 27.12  ? 912  A1BLN A H26  1 
HETATM 24989 H H25  . A1BLN T  6 .   ? 53.259 -10.295 -61.693 0.00 27.12  ? 912  A1BLN A H25  1 
HETATM 24990 H H29  . A1BLN T  6 .   ? 51.243 -8.658  -60.164 0.00 26.02  ? 912  A1BLN A H29  1 
HETATM 24991 H H1   . A1BLN T  6 .   ? 50.411 -15.546 -63.253 0.00 33.27  ? 912  A1BLN A H1   1 
HETATM 24992 H H2   . A1BLN T  6 .   ? 52.291 -14.061 -63.178 0.00 31.74  ? 912  A1BLN A H2   1 
HETATM 24993 H H3   . A1BLN T  6 .   ? 49.988 -15.349 -59.002 0.00 32.73  ? 912  A1BLN A H3   1 
HETATM 24994 H H5   . A1BLN T  6 .   ? 46.290 -17.847 -60.369 0.00 47.39  ? 912  A1BLN A H5   1 
HETATM 24995 H H6   . A1BLN T  6 .   ? 45.976 -17.562 -62.071 0.00 47.39  ? 912  A1BLN A H6   1 
HETATM 24996 H H9   . A1BLN T  6 .   ? 46.609 -15.465 -59.954 0.00 46.39  ? 912  A1BLN A H9   1 
HETATM 24997 H H11  . A1BLN T  6 .   ? 55.838 -7.759  -58.699 0.00 24.95  ? 912  A1BLN A H11  1 
HETATM 24998 H H13  . A1BLN T  6 .   ? 56.488 -9.347  -58.368 0.00 24.95  ? 912  A1BLN A H13  1 
HETATM 24999 H H12  . A1BLN T  6 .   ? 55.185 -8.710  -57.392 0.00 24.95  ? 912  A1BLN A H12  1 
HETATM 25000 H H17  . A1BLN T  6 .   ? 52.865 -12.974 -58.551 0.00 28.54  ? 912  A1BLN A H17  1 
HETATM 25001 H H18  . A1BLN T  6 .   ? 52.480 -14.539 -57.900 0.00 28.54  ? 912  A1BLN A H18  1 
HETATM 25002 H H19  . A1BLN T  6 .   ? 49.028 -17.275 -61.793 0.00 39.12  ? 912  A1BLN A H19  1 
HETATM 25003 H H20  . A1BLN T  6 .   ? 48.531 -16.741 -60.235 0.00 39.12  ? 912  A1BLN A H20  1 
HETATM 25004 H H27  . A1BLN T  6 .   ? 50.777 -11.060 -61.880 0.00 28.18  ? 912  A1BLN A H27  1 
HETATM 25005 H H28  . A1BLN T  6 .   ? 50.448 -9.491  -62.570 0.00 28.18  ? 912  A1BLN A H28  1 
HETATM 25006 H H31  . A1BLN T  6 .   ? 49.158 -7.402  -57.125 0.00 23.86  ? 912  A1BLN A H31  1 
HETATM 25007 H H30  . A1BLN T  6 .   ? 48.254 -8.183  -55.867 0.00 23.86  ? 912  A1BLN A H30  1 
HETATM 25008 H H32  . A1BLN T  6 .   ? 52.051 -11.448 -59.836 0.00 25.75  ? 912  A1BLN A H32  1 
HETATM 25009 H H33  . A1BLN T  6 .   ? 47.935 -14.647 -62.035 0.00 42.93  ? 912  A1BLN A H33  1 
HETATM 25010 H H34  . A1BLN T  6 .   ? 44.112 -13.320 -61.248 0.00 48.90  ? 912  A1BLN A H34  1 
HETATM 25011 H H35  . A1BLN T  6 .   ? 50.834 -10.998 -64.143 0.00 29.53  ? 912  A1BLN A H35  1 
HETATM 25012 C C1   . NAG   U  4 .   ? 84.410 38.752  -44.691 1.00 55.60  ? 901  NAG   B C1   1 
HETATM 25013 C C2   . NAG   U  4 .   ? 84.173 40.236  -44.400 1.00 56.21  ? 901  NAG   B C2   1 
HETATM 25014 C C3   . NAG   U  4 .   ? 85.299 40.691  -43.475 1.00 56.55  ? 901  NAG   B C3   1 
HETATM 25015 C C4   . NAG   U  4 .   ? 85.288 39.878  -42.186 1.00 56.67  ? 901  NAG   B C4   1 
HETATM 25016 C C5   . NAG   U  4 .   ? 85.370 38.388  -42.510 1.00 56.60  ? 901  NAG   B C5   1 
HETATM 25017 C C6   . NAG   U  4 .   ? 85.174 37.514  -41.291 1.00 56.99  ? 901  NAG   B C6   1 
HETATM 25018 C C7   . NAG   U  4 .   ? 83.063 41.376  -46.290 1.00 56.60  ? 901  NAG   B C7   1 
HETATM 25019 C C8   . NAG   U  4 .   ? 83.270 42.237  -47.499 1.00 56.64  ? 901  NAG   B C8   1 
HETATM 25020 N N2   . NAG   U  4 .   ? 84.171 41.036  -45.617 1.00 56.37  ? 901  NAG   B N2   1 
HETATM 25021 O O3   . NAG   U  4 .   ? 85.136 42.074  -43.183 1.00 56.83  ? 901  NAG   B O3   1 
HETATM 25022 O O4   . NAG   U  4 .   ? 86.408 40.244  -41.382 1.00 56.70  ? 901  NAG   B O4   1 
HETATM 25023 O O5   . NAG   U  4 .   ? 84.346 38.028  -43.457 1.00 56.15  ? 901  NAG   B O5   1 
HETATM 25024 O O6   . NAG   U  4 .   ? 85.226 36.131  -41.611 1.00 57.31  ? 901  NAG   B O6   1 
HETATM 25025 O O7   . NAG   U  4 .   ? 81.945 41.005  -45.940 1.00 56.78  ? 901  NAG   B O7   1 
HETATM 25026 H H2   . NAG   U  4 .   ? 83.237 40.362  -43.857 0.00 77.84  ? 901  NAG   B H2   1 
HETATM 25027 H H3   . NAG   U  4 .   ? 86.257 40.546  -43.971 0.00 79.51  ? 901  NAG   B H3   1 
HETATM 25028 H H4   . NAG   U  4 .   ? 84.352 40.081  -41.668 0.00 79.09  ? 901  NAG   B H4   1 
HETATM 25029 H H5   . NAG   U  4 .   ? 86.343 38.162  -42.944 0.00 78.52  ? 901  NAG   B H5   1 
HETATM 25030 H H61  . NAG   U  4 .   ? 84.172 37.646  -40.887 0.00 78.26  ? 901  NAG   B H61  1 
HETATM 25031 H H62  . NAG   U  4 .   ? 85.880 37.763  -40.499 0.00 79.09  ? 901  NAG   B H62  1 
HETATM 25032 H H81  . NAG   U  4 .   ? 82.344 42.579  -47.959 0.00 78.71  ? 901  NAG   B H81  1 
HETATM 25033 H H82  . NAG   U  4 .   ? 83.814 41.698  -48.273 0.00 78.63  ? 901  NAG   B H82  1 
HETATM 25034 H H83  . NAG   U  4 .   ? 83.862 43.121  -47.265 0.00 79.64  ? 901  NAG   B H83  1 
HETATM 25035 H HN2  . NAG   U  4 .   ? 85.081 41.337  -45.950 0.00 78.94  ? 901  NAG   B HN2  1 
HETATM 25036 H HO3  . NAG   U  4 .   ? 85.785 42.280  -42.461 0.00 80.96  ? 901  NAG   B HO3  1 
HETATM 25037 H HO4  . NAG   U  4 .   ? 86.192 40.012  -40.440 0.00 80.11  ? 901  NAG   B HO4  1 
HETATM 25038 H HO6  . NAG   U  4 .   ? 86.097 35.954  -42.053 0.00 78.29  ? 901  NAG   B HO6  1 
HETATM 25039 C C1   . NAG   V  4 .   ? 62.356 40.476  -64.460 1.00 60.75  ? 902  NAG   B C1   1 
HETATM 25040 C C2   . NAG   V  4 .   ? 61.345 40.702  -65.588 1.00 62.04  ? 902  NAG   B C2   1 
HETATM 25041 C C3   . NAG   V  4 .   ? 61.696 42.000  -66.320 1.00 62.70  ? 902  NAG   B C3   1 
HETATM 25042 C C4   . NAG   V  4 .   ? 61.790 43.170  -65.344 1.00 62.72  ? 902  NAG   B C4   1 
HETATM 25043 C C5   . NAG   V  4 .   ? 62.744 42.817  -64.209 1.00 62.38  ? 902  NAG   B C5   1 
HETATM 25044 C C6   . NAG   V  4 .   ? 62.801 43.853  -63.111 1.00 62.64  ? 902  NAG   B C6   1 
HETATM 25045 C C7   . NAG   V  4 .   ? 60.229 38.927  -66.893 1.00 63.34  ? 902  NAG   B C7   1 
HETATM 25046 C C8   . NAG   V  4 .   ? 60.407 37.889  -67.962 1.00 63.37  ? 902  NAG   B C8   1 
HETATM 25047 N N2   . NAG   V  4 .   ? 61.338 39.591  -66.528 1.00 62.75  ? 902  NAG   B N2   1 
HETATM 25048 O O3   . NAG   V  4 .   ? 60.701 42.270  -67.302 1.00 63.14  ? 902  NAG   B O3   1 
HETATM 25049 O O4   . NAG   V  4 .   ? 62.280 44.324  -66.021 1.00 62.94  ? 902  NAG   B O4   1 
HETATM 25050 O O5   . NAG   V  4 .   ? 62.278 41.613  -63.596 1.00 61.65  ? 902  NAG   B O5   1 
HETATM 25051 O O6   . NAG   V  4 .   ? 63.500 43.363  -61.966 1.00 62.94  ? 902  NAG   B O6   1 
HETATM 25052 O O7   . NAG   V  4 .   ? 59.136 39.150  -66.381 1.00 63.57  ? 902  NAG   B O7   1 
HETATM 25053 H H2   . NAG   V  4 .   ? 60.358 40.838  -65.148 0.00 81.15  ? 902  NAG   B H2   1 
HETATM 25054 H H3   . NAG   V  4 .   ? 62.659 41.881  -66.814 0.00 82.79  ? 902  NAG   B H3   1 
HETATM 25055 H H4   . NAG   V  4 .   ? 60.798 43.348  -64.930 0.00 83.36  ? 902  NAG   B H4   1 
HETATM 25056 H H5   . NAG   V  4 .   ? 63.749 42.669  -64.601 0.00 82.52  ? 902  NAG   B H5   1 
HETATM 25057 H H61  . NAG   V  4 .   ? 61.799 44.056  -62.734 0.00 83.35  ? 902  NAG   B H61  1 
HETATM 25058 H H62  . NAG   V  4 .   ? 63.222 44.793  -63.463 0.00 83.93  ? 902  NAG   B H62  1 
HETATM 25059 H H81  . NAG   V  4 .   ? 59.558 37.215  -68.065 0.00 81.47  ? 902  NAG   B H81  1 
HETATM 25060 H H82  . NAG   V  4 .   ? 61.273 37.261  -67.759 0.00 81.38  ? 902  NAG   B H82  1 
HETATM 25061 H H83  . NAG   V  4 .   ? 60.580 38.340  -68.938 0.00 82.18  ? 902  NAG   B H83  1 
HETATM 25062 H HN2  . NAG   V  4 .   ? 62.237 39.339  -66.925 0.00 81.43  ? 902  NAG   B HN2  1 
HETATM 25063 H HO3  . NAG   V  4 .   ? 61.070 42.965  -67.908 0.00 84.16  ? 902  NAG   B HO3  1 
HETATM 25064 H HO4  . NAG   V  4 .   ? 61.994 45.120  -65.500 0.00 84.78  ? 902  NAG   B HO4  1 
HETATM 25065 H HO6  . NAG   V  4 .   ? 64.144 42.671  -62.270 0.00 82.88  ? 902  NAG   B HO6  1 
HETATM 25066 C C1   . NAG   W  4 .   ? 91.846 11.491  -64.617 1.00 48.00  ? 903  NAG   B C1   1 
HETATM 25067 C C2   . NAG   W  4 .   ? 92.188 12.959  -64.876 1.00 48.90  ? 903  NAG   B C2   1 
HETATM 25068 C C3   . NAG   W  4 .   ? 93.644 13.125  -64.444 1.00 49.47  ? 903  NAG   B C3   1 
HETATM 25069 C C4   . NAG   W  4 .   ? 93.779 12.832  -62.954 1.00 49.61  ? 903  NAG   B C4   1 
HETATM 25070 C C5   . NAG   W  4 .   ? 93.206 11.451  -62.642 1.00 49.29  ? 903  NAG   B C5   1 
HETATM 25071 C C6   . NAG   W  4 .   ? 93.101 11.175  -61.157 1.00 49.31  ? 903  NAG   B C6   1 
HETATM 25072 C C7   . NAG   W  4 .   ? 91.420 14.441  -66.686 1.00 49.50  ? 903  NAG   B C7   1 
HETATM 25073 C C8   . NAG   W  4 .   ? 91.369 14.652  -68.170 1.00 49.45  ? 903  NAG   B C8   1 
HETATM 25074 N N2   . NAG   W  4 .   ? 92.024 13.318  -66.276 1.00 49.26  ? 903  NAG   B N2   1 
HETATM 25075 O O3   . NAG   W  4 .   ? 94.084 14.446  -64.735 1.00 49.69  ? 903  NAG   B O3   1 
HETATM 25076 O O4   . NAG   W  4 .   ? 95.153 12.867  -62.581 1.00 49.99  ? 903  NAG   B O4   1 
HETATM 25077 O O5   . NAG   W  4 .   ? 91.881 11.327  -63.194 1.00 48.85  ? 903  NAG   B O5   1 
HETATM 25078 O O6   . NAG   W  4 .   ? 92.381 9.974   -60.887 1.00 49.22  ? 903  NAG   B O6   1 
HETATM 25079 O O7   . NAG   W  4 .   ? 90.951 15.255  -65.896 1.00 49.78  ? 903  NAG   B O7   1 
HETATM 25080 H H2   . NAG   W  4 .   ? 91.566 13.585  -64.237 0.00 63.14  ? 903  NAG   B H2   1 
HETATM 25081 H H3   . NAG   W  4 .   ? 94.269 12.424  -64.994 0.00 65.07  ? 903  NAG   B H3   1 
HETATM 25082 H H4   . NAG   W  4 .   ? 93.202 13.584  -62.415 0.00 64.59  ? 903  NAG   B H4   1 
HETATM 25083 H H5   . NAG   W  4 .   ? 93.841 10.687  -63.089 0.00 64.41  ? 903  NAG   B H5   1 
HETATM 25084 H H61  . NAG   W  4 .   ? 92.514 11.951  -60.667 0.00 63.69  ? 903  NAG   B H61  1 
HETATM 25085 H H62  . NAG   W  4 .   ? 94.081 11.164  -60.684 0.00 64.40  ? 903  NAG   B H62  1 
HETATM 25086 H H81  . NAG   W  4 .   ? 90.984 15.628  -68.461 0.00 64.28  ? 903  NAG   B H81  1 
HETATM 25087 H H82  . NAG   W  4 .   ? 90.723 13.916  -68.647 0.00 64.05  ? 903  NAG   B H82  1 
HETATM 25088 H H83  . NAG   W  4 .   ? 92.352 14.544  -68.627 0.00 64.78  ? 903  NAG   B H83  1 
HETATM 25089 H HN2  . NAG   W  4 .   ? 92.399 12.661  -66.953 0.00 64.20  ? 903  NAG   B HN2  1 
HETATM 25090 H HO3  . NAG   W  4 .   ? 95.027 14.496  -64.430 0.00 65.78  ? 903  NAG   B HO3  1 
HETATM 25091 H HO4  . NAG   W  4 .   ? 95.192 13.053  -61.606 0.00 65.92  ? 903  NAG   B HO4  1 
HETATM 25092 H HO6  . NAG   W  4 .   ? 92.693 9.283   -61.527 0.00 63.64  ? 903  NAG   B HO6  1 
HETATM 25093 C C1   . NAG   X  4 .   ? 86.026 -10.798 -48.689 1.00 37.62  ? 904  NAG   B C1   1 
HETATM 25094 C C2   . NAG   X  4 .   ? 87.080 -10.627 -49.784 1.00 37.80  ? 904  NAG   B C2   1 
HETATM 25095 C C3   . NAG   X  4 .   ? 88.431 -10.400 -49.107 1.00 38.23  ? 904  NAG   B C3   1 
HETATM 25096 C C4   . NAG   X  4 .   ? 88.365 -9.228  -48.137 1.00 38.50  ? 904  NAG   B C4   1 
HETATM 25097 C C5   . NAG   X  4 .   ? 87.225 -9.437  -47.144 1.00 38.91  ? 904  NAG   B C5   1 
HETATM 25098 C C6   . NAG   X  4 .   ? 87.011 -8.263  -46.213 1.00 40.05  ? 904  NAG   B C6   1 
HETATM 25099 C C7   . NAG   X  4 .   ? 86.810 -11.913 -51.874 1.00 37.56  ? 904  NAG   B C7   1 
HETATM 25100 C C8   . NAG   X  4 .   ? 86.871 -13.278 -52.491 1.00 37.39  ? 904  NAG   B C8   1 
HETATM 25101 N N2   . NAG   X  4 .   ? 87.117 -11.848 -50.575 1.00 37.62  ? 904  NAG   B N2   1 
HETATM 25102 O O3   . NAG   X  4 .   ? 89.407 -10.134 -50.108 1.00 38.07  ? 904  NAG   B O3   1 
HETATM 25103 O O4   . NAG   X  4 .   ? 89.598 -9.154  -47.431 1.00 38.26  ? 904  NAG   B O4   1 
HETATM 25104 O O5   . NAG   X  4 .   ? 85.994 -9.635  -47.862 1.00 38.15  ? 904  NAG   B O5   1 
HETATM 25105 O O6   . NAG   X  4 .   ? 86.909 -7.029  -46.930 1.00 40.61  ? 904  NAG   B O6   1 
HETATM 25106 O O7   . NAG   X  4 .   ? 86.509 -10.920 -52.525 1.00 38.07  ? 904  NAG   B O7   1 
HETATM 25107 H H2   . NAG   X  4 .   ? 86.851 -9.753  -50.392 0.00 49.47  ? 904  NAG   B H2   1 
HETATM 25108 H H3   . NAG   X  4 .   ? 88.719 -11.297 -48.559 0.00 51.38  ? 904  NAG   B H3   1 
HETATM 25109 H H4   . NAG   X  4 .   ? 88.182 -8.323  -48.717 0.00 50.64  ? 904  NAG   B H4   1 
HETATM 25110 H H5   . NAG   X  4 .   ? 87.427 -10.318 -46.537 0.00 51.42  ? 904  NAG   B H5   1 
HETATM 25111 H H61  . NAG   X  4 .   ? 87.885 -8.119  -45.580 0.00 52.53  ? 904  NAG   B H61  1 
HETATM 25112 H H62  . NAG   X  4 .   ? 86.163 -8.440  -45.552 0.00 51.84  ? 904  NAG   B H62  1 
HETATM 25113 H H81  . NAG   X  4 .   ? 86.516 -13.305 -53.520 0.00 49.89  ? 904  NAG   B H81  1 
HETATM 25114 H H82  . NAG   X  4 .   ? 86.262 -13.987 -51.934 0.00 49.98  ? 904  NAG   B H82  1 
HETATM 25115 H H83  . NAG   X  4 .   ? 87.886 -13.672 -52.486 0.00 50.62  ? 904  NAG   B H83  1 
HETATM 25116 H HN2  . NAG   X  4 .   ? 87.413 -12.684 -50.080 0.00 50.37  ? 904  NAG   B HN2  1 
HETATM 25117 H HO3  . NAG   X  4 .   ? 90.202 -9.779  -49.631 0.00 51.23  ? 904  NAG   B HO3  1 
HETATM 25118 H HO4  . NAG   X  4 .   ? 89.645 -8.236  -47.059 0.00 51.20  ? 904  NAG   B HO4  1 
HETATM 25119 H HO6  . NAG   X  4 .   ? 86.141 -6.504  -46.579 0.00 51.89  ? 904  NAG   B HO6  1 
HETATM 25120 C C1   . NAG   Y  4 .   ? 76.423 -27.020 -48.748 1.00 60.58  ? 905  NAG   B C1   1 
HETATM 25121 C C2   . NAG   Y  4 .   ? 76.003 -27.997 -49.851 1.00 61.39  ? 905  NAG   B C2   1 
HETATM 25122 C C3   . NAG   Y  4 .   ? 77.276 -28.508 -50.524 1.00 61.94  ? 905  NAG   B C3   1 
HETATM 25123 C C4   . NAG   Y  4 .   ? 78.091 -27.346 -51.080 1.00 62.08  ? 905  NAG   B C4   1 
HETATM 25124 C C5   . NAG   Y  4 .   ? 78.399 -26.356 -49.960 1.00 61.89  ? 905  NAG   B C5   1 
HETATM 25125 C C6   . NAG   Y  4 .   ? 79.086 -25.095 -50.445 1.00 62.22  ? 905  NAG   B C6   1 
HETATM 25126 C C7   . NAG   Y  4 .   ? 73.917 -29.075 -49.093 1.00 61.80  ? 905  NAG   B C7   1 
HETATM 25127 C C8   . NAG   Y  4 .   ? 73.312 -30.320 -48.514 1.00 62.00  ? 905  NAG   B C8   1 
HETATM 25128 N N2   . NAG   Y  4 .   ? 75.236 -29.115 -49.321 1.00 61.65  ? 905  NAG   B N2   1 
HETATM 25129 O O3   . NAG   Y  4 .   ? 76.937 -29.420 -51.563 1.00 62.11  ? 905  NAG   B O3   1 
HETATM 25130 O O4   . NAG   Y  4 .   ? 79.315 -27.845 -51.615 1.00 62.34  ? 905  NAG   B O4   1 
HETATM 25131 O O5   . NAG   Y  4 .   ? 77.177 -25.947 -49.318 1.00 61.22  ? 905  NAG   B O5   1 
HETATM 25132 O O6   . NAG   Y  4 .   ? 79.613 -24.324 -49.370 1.00 62.41  ? 905  NAG   B O6   1 
HETATM 25133 O O7   . NAG   Y  4 .   ? 73.247 -28.076 -49.328 1.00 61.80  ? 905  NAG   B O7   1 
HETATM 25134 H H2   . NAG   Y  4 .   ? 75.422 -27.469 -50.606 0.00 80.77  ? 905  NAG   B H2   1 
HETATM 25135 H H3   . NAG   Y  4 .   ? 77.884 -29.032 -49.788 0.00 83.07  ? 905  NAG   B H3   1 
HETATM 25136 H H4   . NAG   Y  4 .   ? 77.497 -26.848 -51.845 0.00 81.97  ? 905  NAG   B H4   1 
HETATM 25137 H H5   . NAG   Y  4 .   ? 79.033 -26.846 -49.222 0.00 82.18  ? 905  NAG   B H5   1 
HETATM 25138 H H61  . NAG   Y  4 .   ? 78.359 -24.426 -50.902 0.00 81.11  ? 905  NAG   B H61  1 
HETATM 25139 H H62  . NAG   Y  4 .   ? 79.852 -25.304 -51.191 0.00 82.10  ? 905  NAG   B H62  1 
HETATM 25140 H H81  . NAG   Y  4 .   ? 72.225 -30.297 -48.467 0.00 82.10  ? 905  NAG   B H81  1 
HETATM 25141 H H82  . NAG   Y  4 .   ? 73.656 -30.482 -47.494 0.00 82.57  ? 905  NAG   B H82  1 
HETATM 25142 H H83  . NAG   Y  4 .   ? 73.594 -31.206 -49.081 0.00 83.06  ? 905  NAG   B H83  1 
HETATM 25143 H HN2  . NAG   Y  4 .   ? 75.761 -29.960 -49.123 0.00 82.54  ? 905  NAG   B HN2  1 
HETATM 25144 H HO3  . NAG   Y  4 .   ? 76.391 -28.909 -52.217 0.00 82.84  ? 905  NAG   B HO3  1 
HETATM 25145 H HO4  . NAG   Y  4 .   ? 79.640 -27.185 -52.283 0.00 83.23  ? 905  NAG   B HO4  1 
HETATM 25146 H HO6  . NAG   Y  4 .   ? 79.086 -24.539 -48.556 0.00 81.61  ? 905  NAG   B HO6  1 
HETATM 25147 C C1   . NAG   Z  4 .   ? 51.711 -21.284 -20.116 1.00 43.68  ? 906  NAG   B C1   1 
HETATM 25148 C C2   . NAG   Z  4 .   ? 50.867 -22.026 -19.077 1.00 45.01  ? 906  NAG   B C2   1 
HETATM 25149 C C3   . NAG   Z  4 .   ? 51.497 -23.374 -18.733 1.00 45.58  ? 906  NAG   B C3   1 
HETATM 25150 C C4   . NAG   Z  4 .   ? 51.762 -24.179 -19.997 1.00 45.70  ? 906  NAG   B C4   1 
HETATM 25151 C C5   . NAG   Z  4 .   ? 52.574 -23.337 -20.978 1.00 45.30  ? 906  NAG   B C5   1 
HETATM 25152 C C6   . NAG   Z  4 .   ? 52.843 -24.036 -22.296 1.00 45.69  ? 906  NAG   B C6   1 
HETATM 25153 C C7   . NAG   Z  4 .   ? 49.523 -20.829 -17.392 1.00 46.61  ? 906  NAG   B C7   1 
HETATM 25154 C C8   . NAG   Z  4 .   ? 49.548 -20.182 -16.040 1.00 46.57  ? 906  NAG   B C8   1 
HETATM 25155 N N2   . NAG   Z  4 .   ? 50.710 -21.227 -17.872 1.00 45.85  ? 906  NAG   B N2   1 
HETATM 25156 O O3   . NAG   Z  4 .   ? 50.608 -24.090 -17.884 1.00 45.98  ? 906  NAG   B O3   1 
HETATM 25157 O O4   . NAG   Z  4 .   ? 52.491 -25.356 -19.648 1.00 46.17  ? 906  NAG   B O4   1 
HETATM 25158 O O5   . NAG   Z  4 .   ? 51.856 -22.121 -21.267 1.00 44.32  ? 906  NAG   B O5   1 
HETATM 25159 O O6   . NAG   Z  4 .   ? 51.642 -24.275 -23.020 1.00 46.16  ? 906  NAG   B O6   1 
HETATM 25160 O O7   . NAG   Z  4 .   ? 48.478 -20.991 -18.015 1.00 47.28  ? 906  NAG   B O7   1 
HETATM 25161 H H2   . NAG   Z  4 .   ? 49.892 -22.218 -19.514 0.00 56.95  ? 906  NAG   B H2   1 
HETATM 25162 H H3   . NAG   Z  4 .   ? 52.434 -23.208 -18.204 0.00 58.58  ? 906  NAG   B H3   1 
HETATM 25163 H H4   . NAG   Z  4 .   ? 50.803 -24.428 -20.449 0.00 58.49  ? 906  NAG   B H4   1 
HETATM 25164 H H5   . NAG   Z  4 .   ? 53.535 -23.087 -20.531 0.00 57.71  ? 906  NAG   B H5   1 
HETATM 25165 H H61  . NAG   Z  4 .   ? 53.230 -25.039 -22.124 0.00 58.57  ? 906  NAG   B H61  1 
HETATM 25166 H H62  . NAG   Z  4 .   ? 53.583 -23.514 -22.900 0.00 57.78  ? 906  NAG   B H62  1 
HETATM 25167 H H81  . NAG   Z  4 .   ? 48.579 -20.170 -15.543 0.00 59.09  ? 906  NAG   B H81  1 
HETATM 25168 H H82  . NAG   Z  4 .   ? 49.861 -19.141 -16.113 0.00 58.66  ? 906  NAG   B H82  1 
HETATM 25169 H H83  . NAG   Z  4 .   ? 50.250 -20.674 -15.369 0.00 59.44  ? 906  NAG   B H83  1 
HETATM 25170 H HN2  . NAG   Z  4 .   ? 51.565 -20.972 -17.390 0.00 58.21  ? 906  NAG   B HN2  1 
HETATM 25171 H HO3  . NAG   Z  4 .   ? 51.063 -24.946 -17.669 0.00 59.80  ? 906  NAG   B HO3  1 
HETATM 25172 H HO4  . NAG   Z  4 .   ? 52.326 -26.031 -20.358 0.00 59.92  ? 906  NAG   B HO4  1 
HETATM 25173 H HO6  . NAG   Z  4 .   ? 51.053 -23.484 -22.902 0.00 58.12  ? 906  NAG   B HO6  1 
HETATM 25174 C C1   . NAG   AA 4 .   ? 59.774 -16.263 -14.327 1.00 49.81  ? 907  NAG   B C1   1 
HETATM 25175 C C2   . NAG   AA 4 .   ? 60.048 -17.754 -14.120 1.00 51.03  ? 907  NAG   B C2   1 
HETATM 25176 C C3   . NAG   AA 4 .   ? 59.143 -18.204 -12.977 1.00 51.38  ? 907  NAG   B C3   1 
HETATM 25177 C C4   . NAG   AA 4 .   ? 59.507 -17.449 -11.709 1.00 51.52  ? 907  NAG   B C4   1 
HETATM 25178 C C5   . NAG   AA 4 .   ? 59.453 -15.940 -11.947 1.00 51.39  ? 907  NAG   B C5   1 
HETATM 25179 C C6   . NAG   AA 4 .   ? 60.070 -15.164 -10.801 1.00 51.97  ? 907  NAG   B C6   1 
HETATM 25180 C C7   . NAG   AA 4 .   ? 60.722 -18.790 -16.246 1.00 52.45  ? 907  NAG   B C7   1 
HETATM 25181 C C8   . NAG   AA 4 .   ? 60.295 -19.673 -17.382 1.00 52.45  ? 907  NAG   B C8   1 
HETATM 25182 N N2   . NAG   AA 4 .   ? 59.795 -18.547 -15.313 1.00 51.75  ? 907  NAG   B N2   1 
HETATM 25183 O O3   . NAG   AA 4 .   ? 59.309 -19.602 -12.765 1.00 51.69  ? 907  NAG   B O3   1 
HETATM 25184 O O4   . NAG   AA 4 .   ? 58.592 -17.802 -10.677 1.00 52.03  ? 907  NAG   B O4   1 
HETATM 25185 O O5   . NAG   AA 4 .   ? 60.183 -15.576 -13.138 1.00 50.49  ? 907  NAG   B O5   1 
HETATM 25186 O O6   . NAG   AA 4 .   ? 59.725 -13.788 -10.826 1.00 52.63  ? 907  NAG   B O6   1 
HETATM 25187 O O7   . NAG   AA 4 .   ? 61.852 -18.310 -16.181 1.00 52.85  ? 907  NAG   B O7   1 
HETATM 25188 H H2   . NAG   AA 4 .   ? 61.076 -17.893 -13.790 0.00 66.13  ? 907  NAG   B H2   1 
HETATM 25189 H H3   . NAG   AA 4 .   ? 58.102 -18.002 -13.226 0.00 66.15  ? 907  NAG   B H3   1 
HETATM 25190 H H4   . NAG   AA 4 .   ? 60.525 -17.728 -11.438 0.00 67.45  ? 907  NAG   B H4   1 
HETATM 25191 H H5   . NAG   AA 4 .   ? 58.416 -15.633 -12.076 0.00 65.97  ? 907  NAG   B H5   1 
HETATM 25192 H H61  . NAG   AA 4 .   ? 61.154 -15.152 -10.902 0.00 67.63  ? 907  NAG   B H61  1 
HETATM 25193 H H62  . NAG   AA 4 .   ? 59.839 -15.609 -9.835  0.00 67.88  ? 907  NAG   B H62  1 
HETATM 25194 H H81  . NAG   AA 4 .   ? 61.125 -20.055 -17.975 0.00 67.12  ? 907  NAG   B H81  1 
HETATM 25195 H H82  . NAG   AA 4 .   ? 59.647 -19.139 -18.075 0.00 66.45  ? 907  NAG   B H82  1 
HETATM 25196 H H83  . NAG   AA 4 .   ? 59.728 -20.533 -17.028 0.00 67.30  ? 907  NAG   B H83  1 
HETATM 25197 H HN2  . NAG   AA 4 .   ? 58.855 -18.916 -15.416 0.00 66.25  ? 907  NAG   B HN2  1 
HETATM 25198 H HO3  . NAG   AA 4 .   ? 58.597 -19.870 -12.125 0.00 67.66  ? 907  NAG   B HO3  1 
HETATM 25199 H HO4  . NAG   AA 4 .   ? 59.034 -17.620 -9.806  0.00 68.36  ? 907  NAG   B HO4  1 
HETATM 25200 H HO6  . NAG   AA 4 .   ? 59.886 -13.454 -11.747 0.00 67.34  ? 907  NAG   B HO6  1 
HETATM 25201 C C1   . NAG   BA 4 .   ? 70.761 -1.206  -15.507 1.00 34.25  ? 908  NAG   B C1   1 
HETATM 25202 C C2   . NAG   BA 4 .   ? 71.214 -2.669  -15.443 1.00 34.72  ? 908  NAG   B C2   1 
HETATM 25203 C C3   . NAG   BA 4 .   ? 72.690 -2.739  -15.845 1.00 35.77  ? 908  NAG   B C3   1 
HETATM 25204 C C4   . NAG   BA 4 .   ? 72.900 -2.117  -17.220 1.00 36.19  ? 908  NAG   B C4   1 
HETATM 25205 C C5   . NAG   BA 4 .   ? 72.418 -0.671  -17.176 1.00 35.64  ? 908  NAG   B C5   1 
HETATM 25206 C C6   . NAG   BA 4 .   ? 72.518 0.045   -18.503 1.00 35.88  ? 908  NAG   B C6   1 
HETATM 25207 C C7   . NAG   BA 4 .   ? 70.590 -4.467  -13.858 1.00 33.55  ? 908  NAG   B C7   1 
HETATM 25208 C C8   . NAG   BA 4 .   ? 70.486 -4.853  -12.411 1.00 33.41  ? 908  NAG   B C8   1 
HETATM 25209 N N2   . NAG   BA 4 .   ? 71.036 -3.224  -14.108 1.00 34.00  ? 908  NAG   B N2   1 
HETATM 25210 O O3   . NAG   BA 4 .   ? 73.135 -4.089  -15.854 1.00 35.92  ? 908  NAG   B O3   1 
HETATM 25211 O O4   . NAG   BA 4 .   ? 74.279 -2.156  -17.574 1.00 36.80  ? 908  NAG   B O4   1 
HETATM 25212 O O5   . NAG   BA 4 .   ? 71.033 -0.675  -16.814 1.00 34.81  ? 908  NAG   B O5   1 
HETATM 25213 O O6   . NAG   BA 4 .   ? 71.817 -0.660  -19.527 1.00 36.55  ? 908  NAG   B O6   1 
HETATM 25214 O O7   . NAG   BA 4 .   ? 70.268 -5.238  -14.756 1.00 33.37  ? 908  NAG   B O7   1 
HETATM 25215 H H2   . NAG   BA 4 .   ? 70.647 -3.242  -16.174 0.00 45.44  ? 908  NAG   B H2   1 
HETATM 25216 H H3   . NAG   BA 4 .   ? 73.282 -2.185  -15.119 0.00 48.03  ? 908  NAG   B H3   1 
HETATM 25217 H H4   . NAG   BA 4 .   ? 72.297 -2.679  -17.932 0.00 47.05  ? 908  NAG   B H4   1 
HETATM 25218 H H5   . NAG   BA 4 .   ? 72.984 -0.112  -16.432 0.00 47.08  ? 908  NAG   B H5   1 
HETATM 25219 H H61  . NAG   BA 4 .   ? 73.547 0.056   -18.858 0.00 46.59  ? 908  NAG   B H61  1 
HETATM 25220 H H62  . NAG   BA 4 .   ? 72.189 1.080   -18.419 0.00 46.24  ? 908  NAG   B H62  1 
HETATM 25221 H H81  . NAG   BA 4 .   ? 70.076 -5.849  -12.252 0.00 45.65  ? 908  NAG   B H81  1 
HETATM 25222 H H82  . NAG   BA 4 .   ? 69.835 -4.169  -11.868 0.00 45.55  ? 908  NAG   B H82  1 
HETATM 25223 H H83  . NAG   BA 4 .   ? 71.455 -4.817  -11.916 0.00 46.18  ? 908  NAG   B H83  1 
HETATM 25224 H HN2  . NAG   BA 4 .   ? 71.281 -2.609  -13.338 0.00 45.97  ? 908  NAG   B HN2  1 
HETATM 25225 H HO3  . NAG   BA 4 .   ? 74.099 -4.031  -16.082 0.00 48.26  ? 908  NAG   B HO3  1 
HETATM 25226 H HO4  . NAG   BA 4 .   ? 74.340 -2.112  -18.565 0.00 48.25  ? 908  NAG   B HO4  1 
HETATM 25227 H HO6  . NAG   BA 4 .   ? 71.459 -0.003  -20.180 0.00 46.13  ? 908  NAG   B HO6  1 
HETATM 25228 C C1   . NAG   CA 4 .   ? 51.194 17.634  -4.753  1.00 42.27  ? 909  NAG   B C1   1 
HETATM 25229 C C2   . NAG   CA 4 .   ? 50.075 18.590  -4.337  1.00 43.46  ? 909  NAG   B C2   1 
HETATM 25230 C C3   . NAG   CA 4 .   ? 50.054 18.640  -2.808  1.00 43.68  ? 909  NAG   B C3   1 
HETATM 25231 C C4   . NAG   CA 4 .   ? 49.857 17.248  -2.222  1.00 43.80  ? 909  NAG   B C4   1 
HETATM 25232 C C5   . NAG   CA 4 .   ? 50.898 16.281  -2.778  1.00 43.24  ? 909  NAG   B C5   1 
HETATM 25233 C C6   . NAG   CA 4 .   ? 50.620 14.839  -2.411  1.00 42.89  ? 909  NAG   B C6   1 
HETATM 25234 C C7   . NAG   CA 4 .   ? 49.390 20.665  -5.472  1.00 45.51  ? 909  NAG   B C7   1 
HETATM 25235 C C8   . NAG   CA 4 .   ? 49.858 21.974  -6.039  1.00 45.66  ? 909  NAG   B C8   1 
HETATM 25236 N N2   . NAG   CA 4 .   ? 50.326 19.916  -4.879  1.00 44.31  ? 909  NAG   B N2   1 
HETATM 25237 O O3   . NAG   CA 4 .   ? 48.993 19.484  -2.382  1.00 44.24  ? 909  NAG   B O3   1 
HETATM 25238 O O4   . NAG   CA 4 .   ? 50.002 17.300  -0.804  1.00 44.37  ? 909  NAG   B O4   1 
HETATM 25239 O O5   . NAG   CA 4 .   ? 50.902 16.343  -4.211  1.00 42.71  ? 909  NAG   B O5   1 
HETATM 25240 O O6   . NAG   CA 4 .   ? 51.663 13.982  -2.845  1.00 42.77  ? 909  NAG   B O6   1 
HETATM 25241 O O7   . NAG   CA 4 .   ? 48.221 20.301  -5.557  1.00 46.23  ? 909  NAG   B O7   1 
HETATM 25242 H H2   . NAG   CA 4 .   ? 49.122 18.193  -4.683  0.00 59.11  ? 909  NAG   B H2   1 
HETATM 25243 H H3   . NAG   CA 4 .   ? 50.994 19.049  -2.442  0.00 61.00  ? 909  NAG   B H3   1 
HETATM 25244 H H4   . NAG   CA 4 .   ? 48.865 16.897  -2.503  0.00 60.28  ? 909  NAG   B H4   1 
HETATM 25245 H H5   . NAG   CA 4 .   ? 51.888 16.548  -2.413  0.00 59.85  ? 909  NAG   B H5   1 
HETATM 25246 H H61  . NAG   CA 4 .   ? 49.748 14.474  -2.953  0.00 58.39  ? 909  NAG   B H61  1 
HETATM 25247 H H62  . NAG   CA 4 .   ? 50.423 14.718  -1.347  0.00 59.38  ? 909  NAG   B H62  1 
HETATM 25248 H H81  . NAG   CA 4 .   ? 49.134 22.452  -6.698  0.00 62.15  ? 909  NAG   B H81  1 
HETATM 25249 H H82  . NAG   CA 4 .   ? 50.764 21.843  -6.628  0.00 62.08  ? 909  NAG   B H82  1 
HETATM 25250 H H83  . NAG   CA 4 .   ? 50.101 22.688  -5.253  0.00 63.04  ? 909  NAG   B H83  1 
HETATM 25251 H HN2  . NAG   CA 4 .   ? 51.274 20.263  -4.785  0.00 60.90  ? 909  NAG   B HN2  1 
HETATM 25252 H HO3  . NAG   CA 4 .   ? 49.104 19.594  -1.401  0.00 62.26  ? 909  NAG   B HO3  1 
HETATM 25253 H HO4  . NAG   CA 4 .   ? 49.522 16.517  -0.424  0.00 62.08  ? 909  NAG   B HO4  1 
HETATM 25254 H HO6  . NAG   CA 4 .   ? 51.457 13.066  -2.524  0.00 58.31  ? 909  NAG   B HO6  1 
HETATM 25255 S S    . SO4   DA 5 .   ? 60.048 2.704   -59.909 1.00 41.81  ? 910  SO4   B S    1 
HETATM 25256 O O1   . SO4   DA 5 .   ? 61.384 2.766   -60.381 1.00 42.12  ? 910  SO4   B O1   1 
HETATM 25257 O O2   . SO4   DA 5 .   ? 59.295 1.767   -60.727 1.00 41.35  ? 910  SO4   B O2   1 
HETATM 25258 O O3   . SO4   DA 5 .   ? 60.047 2.239   -58.498 1.00 42.27  ? 910  SO4   B O3   1 
HETATM 25259 O O4   . SO4   DA 5 .   ? 59.495 4.067   -59.978 1.00 42.18  ? 910  SO4   B O4   1 
HETATM 25260 N N1   . A1BLN EA 6 .   ? 41.705 -19.265 -25.214 1.00 21.58  ? 911  A1BLN B N1   1 
HETATM 25261 N N3   . A1BLN EA 6 .   ? 41.711 -15.543 -22.549 1.00 19.93  ? 911  A1BLN B N3   1 
HETATM 25262 C C4   . A1BLN EA 6 .   ? 42.489 -18.262 -25.540 1.00 20.84  ? 911  A1BLN B C4   1 
HETATM 25263 C C5   . A1BLN EA 6 .   ? 42.118 -22.231 -21.618 1.00 30.95  ? 911  A1BLN B C5   1 
HETATM 25264 C C6   . A1BLN EA 6 .   ? 40.479 -20.625 -22.426 1.00 27.05  ? 911  A1BLN B C6   1 
HETATM 25265 C C7   . A1BLN EA 6 .   ? 42.368 -17.163 -24.604 1.00 20.47  ? 911  A1BLN B C7   1 
HETATM 25266 C C8   . A1BLN EA 6 .   ? 41.439 -17.633 -23.670 1.00 21.19  ? 911  A1BLN B C8   1 
HETATM 25267 C C10  . A1BLN EA 6 .   ? 41.134 -16.757 -22.595 1.00 20.51  ? 911  A1BLN B C10  1 
HETATM 25268 C C13  . A1BLN EA 6 .   ? 47.700 -22.754 -20.874 1.00 40.63  ? 911  A1BLN B C13  1 
HETATM 25269 C C15  . A1BLN EA 6 .   ? 46.827 -21.521 -21.033 1.00 40.21  ? 911  A1BLN B C15  1 
HETATM 25270 C C17  . A1BLN EA 6 .   ? 37.913 -20.071 -19.896 1.00 26.10  ? 911  A1BLN B C17  1 
HETATM 25271 C C20  . A1BLN EA 6 .   ? 37.443 -15.984 -21.283 1.00 20.08  ? 911  A1BLN B C20  1 
HETATM 25272 C C21  . A1BLN EA 6 .   ? 38.757 -15.289 -20.996 1.00 20.60  ? 911  A1BLN B C21  1 
HETATM 25273 C C22  . A1BLN EA 6 .   ? 39.619 -16.926 -19.228 1.00 24.00  ? 911  A1BLN B C22  1 
HETATM 25274 C C24  . A1BLN EA 6 .   ? 39.912 -16.175 -20.527 1.00 21.87  ? 911  A1BLN B C24  1 
HETATM 25275 C C1   . A1BLN EA 6 .   ? 41.411 -22.329 -20.429 1.00 29.64  ? 911  A1BLN B C1   1 
HETATM 25276 C C2   . A1BLN EA 6 .   ? 40.258 -21.595 -20.218 1.00 28.35  ? 911  A1BLN B C2   1 
HETATM 25277 C C3   . A1BLN EA 6 .   ? 41.634 -21.379 -22.604 1.00 28.89  ? 911  A1BLN B C3   1 
HETATM 25278 C C9   . A1BLN EA 6 .   ? 39.798 -20.738 -21.210 1.00 27.19  ? 911  A1BLN B C9   1 
HETATM 25279 C C11  . A1BLN EA 6 .   ? 42.571 -15.180 -23.526 1.00 19.42  ? 911  A1BLN B C11  1 
HETATM 25280 C C12  . A1BLN EA 6 .   ? 46.364 -23.188 -22.635 1.00 40.21  ? 911  A1BLN B C12  1 
HETATM 25281 C C14  . A1BLN EA 6 .   ? 45.655 -22.044 -21.913 1.00 39.13  ? 911  A1BLN B C14  1 
HETATM 25282 C C16  . A1BLN EA 6 .   ? 36.420 -15.057 -21.999 1.00 19.87  ? 911  A1BLN B C16  1 
HETATM 25283 C C18  . A1BLN EA 6 .   ? 39.990 -19.728 -23.539 1.00 24.34  ? 911  A1BLN B C18  1 
HETATM 25284 C C19  . A1BLN EA 6 .   ? 43.375 -23.032 -21.851 1.00 33.79  ? 911  A1BLN B C19  1 
HETATM 25285 C C23  . A1BLN EA 6 .   ? 40.768 -17.789 -18.756 1.00 25.52  ? 911  A1BLN B C23  1 
HETATM 25286 N N2   . A1BLN EA 6 .   ? 42.936 -15.941 -24.573 1.00 19.59  ? 911  A1BLN B N2   1 
HETATM 25287 N N4   . A1BLN EA 6 .   ? 41.045 -18.878 -24.079 1.00 22.32  ? 911  A1BLN B N4   1 
HETATM 25288 N N5   . A1BLN EA 6 .   ? 43.097 -13.954 -23.453 1.00 18.99  ? 911  A1BLN B N5   1 
HETATM 25289 N N6   . A1BLN EA 6 .   ? 40.307 -17.098 -21.589 1.00 21.14  ? 911  A1BLN B N6   1 
HETATM 25290 N N7   . A1BLN EA 6 .   ? 44.519 -22.507 -21.096 1.00 36.71  ? 911  A1BLN B N7   1 
HETATM 25291 O O1   . A1BLN EA 6 .   ? 47.082 -23.819 -21.599 1.00 40.91  ? 911  A1BLN B O1   1 
HETATM 25292 O O2   . A1BLN EA 6 .   ? 47.579 -20.486 -21.680 1.00 40.48  ? 911  A1BLN B O2   1 
HETATM 25293 O O3   . A1BLN EA 6 .   ? 40.525 -18.305 -17.452 1.00 27.16  ? 911  A1BLN B O3   1 
HETATM 25294 O O4   . A1BLN EA 6 .   ? 38.686 -19.952 -21.089 1.00 26.47  ? 911  A1BLN B O4   1 
HETATM 25295 H H4   . A1BLN EA 6 .   ? 43.111 -18.263 -26.432 0.00 25.01  ? 911  A1BLN B H4   1 
HETATM 25296 H H8   . A1BLN EA 6 .   ? 47.795 -23.060 -19.834 0.00 48.75  ? 911  A1BLN B H8   1 
HETATM 25297 H H7   . A1BLN EA 6 .   ? 48.688 -22.679 -21.325 0.00 48.75  ? 911  A1BLN B H7   1 
HETATM 25298 H H10  . A1BLN EA 6 .   ? 46.509 -21.160 -20.052 0.00 48.25  ? 911  A1BLN B H10  1 
HETATM 25299 H H14  . A1BLN EA 6 .   ? 37.128 -19.330 -20.039 0.00 31.32  ? 911  A1BLN B H14  1 
HETATM 25300 H H15  . A1BLN EA 6 .   ? 38.475 -19.821 -18.997 0.00 31.32  ? 911  A1BLN B H15  1 
HETATM 25301 H H16  . A1BLN EA 6 .   ? 37.454 -21.052 -19.782 0.00 31.32  ? 911  A1BLN B H16  1 
HETATM 25302 H H22  . A1BLN EA 6 .   ? 37.005 -16.362 -20.361 0.00 24.09  ? 911  A1BLN B H22  1 
HETATM 25303 H H21  . A1BLN EA 6 .   ? 37.603 -16.870 -21.895 0.00 24.09  ? 911  A1BLN B H21  1 
HETATM 25304 H H23  . A1BLN EA 6 .   ? 39.088 -14.829 -21.922 0.00 24.72  ? 911  A1BLN B H23  1 
HETATM 25305 H H24  . A1BLN EA 6 .   ? 38.579 -14.470 -20.302 0.00 24.72  ? 911  A1BLN B H24  1 
HETATM 25306 H H26  . A1BLN EA 6 .   ? 39.345 -16.218 -18.447 0.00 28.80  ? 911  A1BLN B H26  1 
HETATM 25307 H H25  . A1BLN EA 6 .   ? 38.730 -17.540 -19.350 0.00 28.80  ? 911  A1BLN B H25  1 
HETATM 25308 H H29  . A1BLN EA 6 .   ? 40.743 -15.513 -20.293 0.00 26.24  ? 911  A1BLN B H29  1 
HETATM 25309 H H1   . A1BLN EA 6 .   ? 41.766 -22.996 -19.644 0.00 35.57  ? 911  A1BLN B H1   1 
HETATM 25310 H H2   . A1BLN EA 6 .   ? 39.761 -21.737 -19.259 0.00 34.01  ? 911  A1BLN B H2   1 
HETATM 25311 H H3   . A1BLN EA 6 .   ? 42.173 -21.301 -23.547 0.00 34.67  ? 911  A1BLN B H3   1 
HETATM 25312 H H5   . A1BLN EA 6 .   ? 47.083 -22.900 -23.400 0.00 48.26  ? 911  A1BLN B H5   1 
HETATM 25313 H H6   . A1BLN EA 6 .   ? 45.702 -23.925 -23.084 0.00 48.26  ? 911  A1BLN B H6   1 
HETATM 25314 H H9   . A1BLN EA 6 .   ? 45.326 -21.304 -22.644 0.00 46.96  ? 911  A1BLN B H9   1 
HETATM 25315 H H11  . A1BLN EA 6 .   ? 36.168 -14.181 -21.403 0.00 23.84  ? 911  A1BLN B H11  1 
HETATM 25316 H H13  . A1BLN EA 6 .   ? 35.485 -15.575 -22.206 0.00 23.84  ? 911  A1BLN B H13  1 
HETATM 25317 H H12  . A1BLN EA 6 .   ? 36.793 -14.687 -22.953 0.00 23.84  ? 911  A1BLN B H12  1 
HETATM 25318 H H17  . A1BLN EA 6 .   ? 39.173 -19.085 -23.228 0.00 29.21  ? 911  A1BLN B H17  1 
HETATM 25319 H H18  . A1BLN EA 6 .   ? 39.606 -20.336 -24.356 0.00 29.21  ? 911  A1BLN B H18  1 
HETATM 25320 H H19  . A1BLN EA 6 .   ? 43.157 -24.079 -21.644 0.00 40.54  ? 911  A1BLN B H19  1 
HETATM 25321 H H20  . A1BLN EA 6 .   ? 43.610 -23.010 -22.912 0.00 40.54  ? 911  A1BLN B H20  1 
HETATM 25322 H H27  . A1BLN EA 6 .   ? 40.989 -18.601 -19.447 0.00 30.63  ? 911  A1BLN B H27  1 
HETATM 25323 H H28  . A1BLN EA 6 .   ? 41.693 -17.230 -18.625 0.00 30.63  ? 911  A1BLN B H28  1 
HETATM 25324 H H31  . A1BLN EA 6 .   ? 42.872 -13.323 -22.691 0.00 22.79  ? 911  A1BLN B H31  1 
HETATM 25325 H H30  . A1BLN EA 6 .   ? 43.741 -13.626 -24.165 0.00 22.79  ? 911  A1BLN B H30  1 
HETATM 25326 H H32  . A1BLN EA 6 .   ? 39.939 -18.041 -21.526 0.00 25.37  ? 911  A1BLN B H32  1 
HETATM 25327 H H33  . A1BLN EA 6 .   ? 44.258 -21.885 -20.337 0.00 44.05  ? 911  A1BLN B H33  1 
HETATM 25328 H H34  . A1BLN EA 6 .   ? 48.222 -20.136 -21.009 0.00 48.57  ? 911  A1BLN B H34  1 
HETATM 25329 H H35  . A1BLN EA 6 .   ? 41.251 -18.947 -17.240 0.00 32.59  ? 911  A1BLN B H35  1 
HETATM 25330 O O    . HOH   FA 7 .   ? 47.187 7.455   -47.677 1.00 44.42  ? 1001 HOH   A O    1 
HETATM 25331 O O    . HOH   FA 7 .   ? 40.383 40.738  -42.345 1.00 42.89  ? 1002 HOH   A O    1 
HETATM 25332 O O    . HOH   FA 7 .   ? 37.066 -20.555 -45.984 1.00 41.38  ? 1003 HOH   A O    1 
HETATM 25333 O O    . HOH   FA 7 .   ? 44.175 30.470  -52.139 1.00 42.55  ? 1004 HOH   A O    1 
HETATM 25334 O O    . HOH   FA 7 .   ? 9.661  -21.237 -19.900 1.00 39.62  ? 1005 HOH   A O    1 
HETATM 25335 O O    . HOH   FA 7 .   ? 6.709  -7.729  -3.230  1.00 44.55  ? 1006 HOH   A O    1 
HETATM 25336 O O    . HOH   FA 7 .   ? 50.353 9.212   -60.805 1.00 28.71  ? 1007 HOH   A O    1 
HETATM 25337 O O    . HOH   FA 7 .   ? 7.211  -15.748 -16.232 1.00 26.23  ? 1008 HOH   A O    1 
HETATM 25338 O O    . HOH   FA 7 .   ? 20.344 -5.435  -18.756 1.00 25.78  ? 1009 HOH   A O    1 
HETATM 25339 O O    . HOH   FA 7 .   ? 28.822 -4.653  -35.443 1.00 48.76  ? 1010 HOH   A O    1 
HETATM 25340 O O    . HOH   FA 7 .   ? 35.715 -15.680 -61.811 1.00 37.04  ? 1011 HOH   A O    1 
HETATM 25341 O O    . HOH   FA 7 .   ? 32.053 -7.683  -14.572 1.00 31.18  ? 1012 HOH   A O    1 
HETATM 25342 O O    . HOH   FA 7 .   ? 39.604 36.952  -49.887 1.00 48.70  ? 1013 HOH   A O    1 
HETATM 25343 O O    . HOH   FA 7 .   ? 18.720 31.156  -0.272  1.00 49.36  ? 1014 HOH   A O    1 
HETATM 25344 O O    . HOH   FA 7 .   ? 26.870 31.899  -9.833  1.00 46.05  ? 1015 HOH   A O    1 
HETATM 25345 O O    . HOH   FA 7 .   ? 12.745 -25.205 -29.409 1.00 27.69  ? 1016 HOH   A O    1 
HETATM 25346 O O    . HOH   FA 7 .   ? 28.916 -26.693 -29.093 1.00 32.48  ? 1017 HOH   A O    1 
HETATM 25347 O O    . HOH   FA 7 .   ? 32.813 -19.858 -50.965 1.00 43.93  ? 1018 HOH   A O    1 
HETATM 25348 O O    . HOH   FA 7 .   ? 19.633 35.055  -15.954 1.00 58.88  ? 1019 HOH   A O    1 
HETATM 25349 O O    . HOH   FA 7 .   ? 32.122 -20.659 -54.001 1.00 59.65  ? 1020 HOH   A O    1 
HETATM 25350 O O    . HOH   FA 7 .   ? 32.067 10.509  -7.343  1.00 37.46  ? 1021 HOH   A O    1 
HETATM 25351 O O    . HOH   FA 7 .   ? 41.905 36.400  -47.925 1.00 35.09  ? 1022 HOH   A O    1 
HETATM 25352 O O    . HOH   FA 7 .   ? 23.974 34.648  -32.965 1.00 43.88  ? 1023 HOH   A O    1 
HETATM 25353 O O    . HOH   FA 7 .   ? 22.705 -22.301 -41.978 1.00 34.02  ? 1024 HOH   A O    1 
HETATM 25354 O O    . HOH   FA 7 .   ? 50.164 16.172  -66.810 1.00 42.99  ? 1025 HOH   A O    1 
HETATM 25355 O O    . HOH   FA 7 .   ? 38.986 -0.889  -16.702 1.00 38.31  ? 1026 HOH   A O    1 
HETATM 25356 O O    . HOH   FA 7 .   ? 37.671 -23.154 -46.606 1.00 44.86  ? 1027 HOH   A O    1 
HETATM 25357 O O    . HOH   FA 7 .   ? 11.861 -7.568  -26.385 1.00 40.54  ? 1028 HOH   A O    1 
HETATM 25358 O O    . HOH   FA 7 .   ? 27.905 24.831  -59.125 1.00 35.12  ? 1029 HOH   A O    1 
HETATM 25359 O O    . HOH   FA 7 .   ? 25.489 -23.334 -12.281 1.00 29.94  ? 1030 HOH   A O    1 
HETATM 25360 O O    . HOH   FA 7 .   ? 31.376 14.742  -8.151  1.00 31.66  ? 1031 HOH   A O    1 
HETATM 25361 O O    . HOH   FA 7 .   ? 22.850 33.689  -49.504 1.00 46.90  ? 1032 HOH   A O    1 
HETATM 25362 O O    . HOH   FA 7 .   ? 40.732 30.021  -52.830 1.00 42.96  ? 1033 HOH   A O    1 
HETATM 25363 O O    . HOH   FA 7 .   ? 20.767 -16.996 -3.636  1.00 35.69  ? 1034 HOH   A O    1 
HETATM 25364 O O    . HOH   FA 7 .   ? 15.341 21.189  3.184   1.00 39.77  ? 1035 HOH   A O    1 
HETATM 25365 O O    . HOH   FA 7 .   ? 41.824 23.197  -60.168 1.00 33.70  ? 1036 HOH   A O    1 
HETATM 25366 O O    . HOH   FA 7 .   ? 41.959 8.832   -66.305 1.00 18.72  ? 1037 HOH   A O    1 
HETATM 25367 O O    . HOH   FA 7 .   ? 22.393 15.026  2.422   1.00 32.08  ? 1038 HOH   A O    1 
HETATM 25368 O O    . HOH   FA 7 .   ? 30.451 11.753  -65.703 1.00 31.13  ? 1039 HOH   A O    1 
HETATM 25369 O O    . HOH   FA 7 .   ? 55.444 -4.563  -61.219 1.00 27.77  ? 1040 HOH   A O    1 
HETATM 25370 O O    . HOH   FA 7 .   ? 18.826 -25.234 -9.361  1.00 38.38  ? 1041 HOH   A O    1 
HETATM 25371 O O    . HOH   FA 7 .   ? 8.488  17.681  -5.362  1.00 33.44  ? 1042 HOH   A O    1 
HETATM 25372 O O    . HOH   FA 7 .   ? 5.408  -0.731  -6.494  1.00 31.87  ? 1043 HOH   A O    1 
HETATM 25373 O O    . HOH   FA 7 .   ? 22.515 -14.271 -49.867 1.00 27.10  ? 1044 HOH   A O    1 
HETATM 25374 O O    . HOH   FA 7 .   ? 28.611 -0.544  -60.663 1.00 33.28  ? 1045 HOH   A O    1 
HETATM 25375 O O    . HOH   FA 7 .   ? 21.723 -30.310 -20.978 1.00 43.06  ? 1046 HOH   A O    1 
HETATM 25376 O O    . HOH   FA 7 .   ? 48.459 -11.559 -60.953 1.00 34.19  ? 1047 HOH   A O    1 
HETATM 25377 O O    . HOH   FA 7 .   ? 50.800 6.933   -48.440 1.00 34.38  ? 1048 HOH   A O    1 
HETATM 25378 O O    . HOH   FA 7 .   ? 42.610 30.767  -37.516 1.00 43.15  ? 1049 HOH   A O    1 
HETATM 25379 O O    . HOH   FA 7 .   ? 3.270  3.482   -9.858  1.00 32.29  ? 1050 HOH   A O    1 
HETATM 25380 O O    . HOH   FA 7 .   ? 22.014 1.697   -48.626 1.00 38.29  ? 1051 HOH   A O    1 
HETATM 25381 O O    . HOH   FA 7 .   ? 48.353 18.142  -59.040 1.00 37.75  ? 1052 HOH   A O    1 
HETATM 25382 O O    . HOH   FA 7 .   ? 25.880 -14.892 -58.796 1.00 39.20  ? 1053 HOH   A O    1 
HETATM 25383 O O    . HOH   FA 7 .   ? 29.094 -23.227 -44.417 1.00 36.06  ? 1054 HOH   A O    1 
HETATM 25384 O O    . HOH   FA 7 .   ? 50.200 4.865   -50.799 1.00 31.47  ? 1055 HOH   A O    1 
HETATM 25385 O O    . HOH   FA 7 .   ? 25.097 29.198  -55.501 1.00 163.92 ? 1056 HOH   A O    1 
HETATM 25386 O O    . HOH   FA 7 .   ? 45.429 -3.950  -50.789 1.00 18.45  ? 1057 HOH   A O    1 
HETATM 25387 O O    . HOH   FA 7 .   ? 30.375 -7.026  -21.296 1.00 28.24  ? 1058 HOH   A O    1 
HETATM 25388 O O    . HOH   FA 7 .   ? 10.090 -9.002  -0.769  1.00 36.09  ? 1059 HOH   A O    1 
HETATM 25389 O O    . HOH   FA 7 .   ? 24.271 -9.860  -54.277 1.00 22.34  ? 1060 HOH   A O    1 
HETATM 25390 O O    . HOH   FA 7 .   ? 19.230 35.046  -13.509 1.00 48.51  ? 1061 HOH   A O    1 
HETATM 25391 O O    . HOH   FA 7 .   ? 16.839 -23.525 -11.759 1.00 33.11  ? 1062 HOH   A O    1 
HETATM 25392 O O    . HOH   FA 7 .   ? 25.156 35.117  -11.581 1.00 47.39  ? 1063 HOH   A O    1 
HETATM 25393 O O    . HOH   FA 7 .   ? 21.999 -19.315 -48.860 1.00 46.76  ? 1064 HOH   A O    1 
HETATM 25394 O O    . HOH   FA 7 .   ? 30.577 6.593   -13.188 1.00 21.85  ? 1065 HOH   A O    1 
HETATM 25395 O O    . HOH   FA 7 .   ? 30.508 -6.331  -35.094 1.00 27.70  ? 1066 HOH   A O    1 
HETATM 25396 O O    . HOH   FA 7 .   ? 23.075 6.130   -12.780 1.00 58.44  ? 1067 HOH   A O    1 
HETATM 25397 O O    . HOH   FA 7 .   ? 31.338 -6.736  -1.834  1.00 32.64  ? 1068 HOH   A O    1 
HETATM 25398 O O    . HOH   FA 7 .   ? 41.449 -16.303 -53.874 1.00 32.54  ? 1069 HOH   A O    1 
HETATM 25399 O O    . HOH   FA 7 .   ? 33.841 -14.439 6.572   1.00 36.62  ? 1070 HOH   A O    1 
HETATM 25400 O O    . HOH   FA 7 .   ? 24.163 6.273   -64.998 1.00 31.53  ? 1071 HOH   A O    1 
HETATM 25401 O O    . HOH   FA 7 .   ? 40.699 -15.080 -34.462 1.00 28.02  ? 1072 HOH   A O    1 
HETATM 25402 O O    . HOH   FA 7 .   ? 14.916 -18.647 -35.043 1.00 26.71  ? 1073 HOH   A O    1 
HETATM 25403 O O    . HOH   FA 7 .   ? 50.659 6.570   -59.858 1.00 18.25  ? 1074 HOH   A O    1 
HETATM 25404 O O    . HOH   FA 7 .   ? 26.711 19.075  -60.287 1.00 24.94  ? 1075 HOH   A O    1 
HETATM 25405 O O    . HOH   FA 7 .   ? 39.617 -18.257 -54.418 1.00 57.61  ? 1076 HOH   A O    1 
HETATM 25406 O O    . HOH   FA 7 .   ? 10.254 -15.521 -4.568  1.00 25.17  ? 1077 HOH   A O    1 
HETATM 25407 O O    . HOH   FA 7 .   ? 33.085 25.375  -20.196 1.00 36.12  ? 1078 HOH   A O    1 
HETATM 25408 O O    . HOH   FA 7 .   ? 1.797  -13.227 -5.720  1.00 45.39  ? 1079 HOH   A O    1 
HETATM 25409 O O    . HOH   FA 7 .   ? 34.264 34.785  -24.610 1.00 52.38  ? 1080 HOH   A O    1 
HETATM 25410 O O    . HOH   FA 7 .   ? 14.212 -20.725 -33.609 1.00 22.93  ? 1081 HOH   A O    1 
HETATM 25411 O O    . HOH   FA 7 .   ? 18.065 -26.556 -12.348 1.00 43.39  ? 1082 HOH   A O    1 
HETATM 25412 O O    . HOH   FA 7 .   ? 38.516 0.940   -13.309 1.00 35.43  ? 1083 HOH   A O    1 
HETATM 25413 O O    . HOH   FA 7 .   ? 22.015 -7.408  3.124   1.00 39.98  ? 1084 HOH   A O    1 
HETATM 25414 O O    . HOH   FA 7 .   ? 16.880 -9.672  -34.220 1.00 38.96  ? 1085 HOH   A O    1 
HETATM 25415 O O    . HOH   FA 7 .   ? 50.384 4.543   -61.620 1.00 21.07  ? 1086 HOH   A O    1 
HETATM 25416 O O    . HOH   FA 7 .   ? 31.815 -8.416  -11.882 1.00 34.44  ? 1087 HOH   A O    1 
HETATM 25417 O O    . HOH   FA 7 .   ? 34.771 -12.805 -55.294 1.00 20.67  ? 1088 HOH   A O    1 
HETATM 25418 O O    . HOH   FA 7 .   ? 4.499  13.738  -9.253  1.00 41.17  ? 1089 HOH   A O    1 
HETATM 25419 O O    . HOH   FA 7 .   ? 22.863 41.471  -33.111 1.00 46.37  ? 1090 HOH   A O    1 
HETATM 25420 O O    . HOH   FA 7 .   ? 25.689 6.479   -47.022 1.00 28.90  ? 1091 HOH   A O    1 
HETATM 25421 O O    . HOH   FA 7 .   ? 44.867 -15.241 -47.586 1.00 27.90  ? 1092 HOH   A O    1 
HETATM 25422 O O    . HOH   FA 7 .   ? 29.533 28.037  -35.363 1.00 39.29  ? 1093 HOH   A O    1 
HETATM 25423 O O    . HOH   FA 7 .   ? 30.715 -0.937  -43.017 1.00 28.02  ? 1094 HOH   A O    1 
HETATM 25424 O O    . HOH   FA 7 .   ? 26.226 -25.594 -19.850 1.00 24.76  ? 1095 HOH   A O    1 
HETATM 25425 O O    . HOH   FA 7 .   ? 26.355 47.882  -41.028 1.00 46.48  ? 1096 HOH   A O    1 
HETATM 25426 O O    . HOH   FA 7 .   ? 37.662 12.943  -43.590 1.00 33.05  ? 1097 HOH   A O    1 
HETATM 25427 O O    . HOH   FA 7 .   ? 32.282 10.502  -46.356 1.00 24.69  ? 1098 HOH   A O    1 
HETATM 25428 O O    . HOH   FA 7 .   ? 44.323 10.731  -69.688 1.00 38.56  ? 1099 HOH   A O    1 
HETATM 25429 O O    . HOH   FA 7 .   ? 10.031 -17.060 -23.399 1.00 22.03  ? 1100 HOH   A O    1 
HETATM 25430 O O    . HOH   FA 7 .   ? 6.306  -18.436 -13.806 1.00 38.42  ? 1101 HOH   A O    1 
HETATM 25431 O O    . HOH   FA 7 .   ? 38.679 -11.780 -64.913 1.00 37.39  ? 1102 HOH   A O    1 
HETATM 25432 O O    . HOH   FA 7 .   ? 34.121 12.616  0.172   1.00 41.49  ? 1103 HOH   A O    1 
HETATM 25433 O O    . HOH   FA 7 .   ? 32.302 52.206  -36.935 1.00 58.63  ? 1104 HOH   A O    1 
HETATM 25434 O O    . HOH   FA 7 .   ? 21.303 -8.281  -23.001 1.00 31.83  ? 1105 HOH   A O    1 
HETATM 25435 O O    . HOH   FA 7 .   ? 39.384 -8.638  -9.202  1.00 36.99  ? 1106 HOH   A O    1 
HETATM 25436 O O    . HOH   FA 7 .   ? 34.729 -10.359 -13.077 1.00 36.67  ? 1107 HOH   A O    1 
HETATM 25437 O O    . HOH   FA 7 .   ? 18.216 -1.855  -39.310 1.00 41.04  ? 1108 HOH   A O    1 
HETATM 25438 O O    . HOH   FA 7 .   ? 28.579 0.001   -64.763 1.00 30.49  ? 1109 HOH   A O    1 
HETATM 25439 O O    . HOH   FA 7 .   ? 44.404 7.413   -68.775 1.00 24.47  ? 1110 HOH   A O    1 
HETATM 25440 O O    . HOH   FA 7 .   ? 22.886 34.180  -30.289 1.00 43.44  ? 1111 HOH   A O    1 
HETATM 25441 O O    . HOH   FA 7 .   ? 42.402 -7.966  -17.681 1.00 18.44  ? 1112 HOH   A O    1 
HETATM 25442 O O    . HOH   FA 7 .   ? 30.081 -6.305  -10.443 1.00 23.66  ? 1113 HOH   A O    1 
HETATM 25443 O O    . HOH   FA 7 .   ? 30.465 -5.236  -7.936  1.00 28.08  ? 1114 HOH   A O    1 
HETATM 25444 O O    . HOH   FA 7 .   ? 39.044 14.115  -41.639 1.00 34.27  ? 1115 HOH   A O    1 
HETATM 25445 O O    . HOH   FA 7 .   ? 28.279 -4.741  -4.184  1.00 29.23  ? 1116 HOH   A O    1 
HETATM 25446 O O    . HOH   FA 7 .   ? 28.018 6.296   -60.798 1.00 21.72  ? 1117 HOH   A O    1 
HETATM 25447 O O    . HOH   FA 7 .   ? 20.606 0.671   -60.183 1.00 31.69  ? 1118 HOH   A O    1 
HETATM 25448 O O    . HOH   FA 7 .   ? 28.027 -6.491  -38.310 1.00 25.96  ? 1119 HOH   A O    1 
HETATM 25449 O O    . HOH   FA 7 .   ? 8.236  -16.456 -5.814  1.00 30.22  ? 1120 HOH   A O    1 
HETATM 25450 O O    . HOH   FA 7 .   ? 19.263 14.899  2.693   1.00 53.28  ? 1121 HOH   A O    1 
HETATM 25451 O O    . HOH   FA 7 .   ? 19.603 24.791  -2.022  1.00 34.79  ? 1122 HOH   A O    1 
HETATM 25452 O O    . HOH   FA 7 .   ? 30.070 31.038  -35.125 1.00 31.48  ? 1123 HOH   A O    1 
HETATM 25453 O O    . HOH   FA 7 .   ? 10.176 -24.989 -28.451 1.00 34.08  ? 1124 HOH   A O    1 
HETATM 25454 O O    . HOH   FA 7 .   ? 16.689 21.107  -22.218 1.00 43.75  ? 1125 HOH   A O    1 
HETATM 25455 O O    . HOH   FA 7 .   ? 23.002 -12.518 -57.151 1.00 37.47  ? 1126 HOH   A O    1 
HETATM 25456 O O    . HOH   FA 7 .   ? 15.917 20.113  -0.109  1.00 25.95  ? 1127 HOH   A O    1 
HETATM 25457 O O    . HOH   FA 7 .   ? 28.282 -9.117  -21.675 1.00 29.39  ? 1128 HOH   A O    1 
HETATM 25458 O O    . HOH   FA 7 .   ? 21.814 0.401   -11.645 1.00 17.83  ? 1129 HOH   A O    1 
HETATM 25459 O O    . HOH   FA 7 .   ? 28.703 36.748  -53.900 1.00 72.73  ? 1130 HOH   A O    1 
HETATM 25460 O O    . HOH   FA 7 .   ? 5.760  -5.971  -9.095  1.00 27.21  ? 1131 HOH   A O    1 
HETATM 25461 O O    . HOH   FA 7 .   ? 35.395 -14.823 -9.975  1.00 22.43  ? 1132 HOH   A O    1 
HETATM 25462 O O    . HOH   FA 7 .   ? 39.409 13.761  -62.310 1.00 22.24  ? 1133 HOH   A O    1 
HETATM 25463 O O    . HOH   FA 7 .   ? 26.225 7.532   -0.921  1.00 29.99  ? 1134 HOH   A O    1 
HETATM 25464 O O    . HOH   FA 7 .   ? 26.338 13.655  2.863   1.00 36.22  ? 1135 HOH   A O    1 
HETATM 25465 O O    . HOH   FA 7 .   ? 44.821 26.288  -42.338 1.00 43.15  ? 1136 HOH   A O    1 
HETATM 25466 O O    . HOH   FA 7 .   ? -0.371 1.781   -1.335  1.00 56.97  ? 1137 HOH   A O    1 
HETATM 25467 O O    . HOH   FA 7 .   ? 32.885 26.800  -30.820 1.00 44.75  ? 1138 HOH   A O    1 
HETATM 25468 O O    . HOH   FA 7 .   ? 13.286 -17.206 -42.470 1.00 39.41  ? 1139 HOH   A O    1 
HETATM 25469 O O    . HOH   FA 7 .   ? 6.664  -12.835 6.665   1.00 63.13  ? 1140 HOH   A O    1 
HETATM 25470 O O    . HOH   FA 7 .   ? 49.478 -11.378 -65.078 1.00 39.82  ? 1141 HOH   A O    1 
HETATM 25471 O O    . HOH   FA 7 .   ? 25.712 -0.027  -62.878 1.00 48.65  ? 1142 HOH   A O    1 
HETATM 25472 O O    . HOH   FA 7 .   ? 26.968 12.099  -14.784 1.00 40.72  ? 1143 HOH   A O    1 
HETATM 25473 O O    . HOH   FA 7 .   ? 37.956 24.017  -58.784 1.00 24.82  ? 1144 HOH   A O    1 
HETATM 25474 O O    . HOH   FA 7 .   ? 30.123 -27.557 -21.926 1.00 37.62  ? 1145 HOH   A O    1 
HETATM 25475 O O    . HOH   FA 7 .   ? 15.782 -10.124 -31.267 1.00 41.01  ? 1146 HOH   A O    1 
HETATM 25476 O O    . HOH   FA 7 .   ? 42.007 -0.880  -62.251 1.00 32.48  ? 1147 HOH   A O    1 
HETATM 25477 O O    . HOH   FA 7 .   ? 6.730  -10.747 -23.138 1.00 35.00  ? 1148 HOH   A O    1 
HETATM 25478 O O    . HOH   FA 7 .   ? 5.720  -10.413 -13.823 1.00 23.42  ? 1149 HOH   A O    1 
HETATM 25479 O O    . HOH   FA 7 .   ? 44.854 -9.937  -62.642 1.00 30.93  ? 1150 HOH   A O    1 
HETATM 25480 O O    . HOH   FA 7 .   ? 1.359  -6.827  -8.206  1.00 49.84  ? 1151 HOH   A O    1 
HETATM 25481 O O    . HOH   FA 7 .   ? 50.415 1.119   -63.621 1.00 23.10  ? 1152 HOH   A O    1 
HETATM 25482 O O    . HOH   FA 7 .   ? 7.869  30.303  -23.010 1.00 40.36  ? 1153 HOH   A O    1 
HETATM 25483 O O    . HOH   FA 7 .   ? 46.667 11.829  -63.571 1.00 21.80  ? 1154 HOH   A O    1 
HETATM 25484 O O    . HOH   FA 7 .   ? 31.667 -13.970 -60.935 1.00 31.32  ? 1155 HOH   A O    1 
HETATM 25485 O O    . HOH   FA 7 .   ? 32.818 45.903  -39.688 1.00 55.74  ? 1156 HOH   A O    1 
HETATM 25486 O O    . HOH   FA 7 .   ? 42.714 -8.083  -40.311 1.00 23.41  ? 1157 HOH   A O    1 
HETATM 25487 O O    . HOH   FA 7 .   ? 45.231 41.850  -27.839 1.00 42.66  ? 1158 HOH   A O    1 
HETATM 25488 O O    . HOH   FA 7 .   ? 39.464 -7.016  -30.850 1.00 25.55  ? 1159 HOH   A O    1 
HETATM 25489 O O    . HOH   FA 7 .   ? 53.562 3.046   -50.237 1.00 28.47  ? 1160 HOH   A O    1 
HETATM 25490 O O    . HOH   FA 7 .   ? 26.362 10.408  -19.491 1.00 48.46  ? 1161 HOH   A O    1 
HETATM 25491 O O    . HOH   FA 7 .   ? 35.821 9.405   -44.902 1.00 35.16  ? 1162 HOH   A O    1 
HETATM 25492 O O    . HOH   FA 7 .   ? 55.851 18.376  -60.739 1.00 54.45  ? 1163 HOH   A O    1 
HETATM 25493 O O    . HOH   FA 7 .   ? 37.932 -19.802 -52.887 1.00 42.57  ? 1164 HOH   A O    1 
HETATM 25494 O O    . HOH   FA 7 .   ? 40.431 -7.107  -57.950 1.00 21.66  ? 1165 HOH   A O    1 
HETATM 25495 O O    . HOH   FA 7 .   ? 18.411 -6.403  2.248   1.00 31.30  ? 1166 HOH   A O    1 
HETATM 25496 O O    . HOH   FA 7 .   ? 35.336 -6.126  -64.608 1.00 36.48  ? 1167 HOH   A O    1 
HETATM 25497 O O    . HOH   FA 7 .   ? 27.028 0.129   3.966   1.00 42.49  ? 1168 HOH   A O    1 
HETATM 25498 O O    . HOH   FA 7 .   ? 20.231 3.768   -12.335 1.00 42.63  ? 1169 HOH   A O    1 
HETATM 25499 O O    . HOH   FA 7 .   ? 5.869  -0.489  -0.218  1.00 39.87  ? 1170 HOH   A O    1 
HETATM 25500 O O    . HOH   FA 7 .   ? 37.088 -4.017  -37.627 1.00 28.28  ? 1171 HOH   A O    1 
HETATM 25501 O O    . HOH   FA 7 .   ? 10.097 28.229  -12.272 1.00 37.85  ? 1172 HOH   A O    1 
HETATM 25502 O O    . HOH   FA 7 .   ? 33.764 -1.970  -40.451 1.00 34.47  ? 1173 HOH   A O    1 
HETATM 25503 O O    . HOH   FA 7 .   ? 6.780  -22.957 -21.905 1.00 38.74  ? 1174 HOH   A O    1 
HETATM 25504 O O    . HOH   FA 7 .   ? 45.717 -3.887  -45.043 1.00 16.65  ? 1175 HOH   A O    1 
HETATM 25505 O O    . HOH   FA 7 .   ? 32.380 -14.804 -6.586  1.00 21.99  ? 1176 HOH   A O    1 
HETATM 25506 O O    . HOH   FA 7 .   ? 52.659 0.640   -60.078 1.00 18.97  ? 1177 HOH   A O    1 
HETATM 25507 O O    . HOH   FA 7 .   ? 24.726 -4.769  -57.886 1.00 24.05  ? 1178 HOH   A O    1 
HETATM 25508 O O    . HOH   FA 7 .   ? 30.556 4.345   -66.741 1.00 31.12  ? 1179 HOH   A O    1 
HETATM 25509 O O    . HOH   FA 7 .   ? 49.392 0.346   -65.947 1.00 26.75  ? 1180 HOH   A O    1 
HETATM 25510 O O    . HOH   FA 7 .   ? 11.624 -2.046  1.602   1.00 43.31  ? 1181 HOH   A O    1 
HETATM 25511 O O    . HOH   FA 7 .   ? 20.190 0.485   -45.132 1.00 27.09  ? 1182 HOH   A O    1 
HETATM 25512 O O    . HOH   FA 7 .   ? 24.912 20.539  -1.217  1.00 40.65  ? 1183 HOH   A O    1 
HETATM 25513 O O    . HOH   FA 7 .   ? 19.645 18.341  2.866   1.00 37.44  ? 1184 HOH   A O    1 
HETATM 25514 O O    . HOH   FA 7 .   ? 13.295 -9.469  -32.632 1.00 45.31  ? 1185 HOH   A O    1 
HETATM 25515 O O    . HOH   FA 7 .   ? 13.944 3.950   4.960   1.00 33.94  ? 1186 HOH   A O    1 
HETATM 25516 O O    . HOH   FA 7 .   ? 56.417 19.911  -63.814 1.00 42.61  ? 1187 HOH   A O    1 
HETATM 25517 O O    . HOH   FA 7 .   ? 13.004 19.173  1.817   1.00 65.63  ? 1188 HOH   A O    1 
HETATM 25518 O O    . HOH   FA 7 .   ? 46.458 9.935   -47.612 1.00 23.32  ? 1189 HOH   A O    1 
HETATM 25519 O O    . HOH   FA 7 .   ? 28.392 -17.295 -20.749 1.00 18.80  ? 1190 HOH   A O    1 
HETATM 25520 O O    . HOH   FA 7 .   ? 29.680 14.484  2.251   1.00 34.89  ? 1191 HOH   A O    1 
HETATM 25521 O O    . HOH   FA 7 .   ? 10.491 -17.546 -29.607 1.00 24.10  ? 1192 HOH   A O    1 
HETATM 25522 O O    . HOH   FA 7 .   ? 33.480 -7.756  -31.417 1.00 28.21  ? 1193 HOH   A O    1 
HETATM 25523 O O    . HOH   FA 7 .   ? 1.975  -15.342 -28.023 1.00 55.08  ? 1194 HOH   A O    1 
HETATM 25524 O O    . HOH   FA 7 .   ? 12.167 -18.426 4.200   1.00 48.47  ? 1195 HOH   A O    1 
HETATM 25525 O O    . HOH   FA 7 .   ? 43.966 -4.141  -42.117 1.00 31.28  ? 1196 HOH   A O    1 
HETATM 25526 O O    . HOH   FA 7 .   ? 7.951  5.790   9.318   1.00 53.87  ? 1197 HOH   A O    1 
HETATM 25527 O O    . HOH   FA 7 .   ? 30.025 -21.253 -14.634 1.00 28.46  ? 1198 HOH   A O    1 
HETATM 25528 O O    . HOH   FA 7 .   ? 1.366  -2.088  -1.514  1.00 33.21  ? 1199 HOH   A O    1 
HETATM 25529 O O    . HOH   FA 7 .   ? 19.149 33.402  -23.477 1.00 41.83  ? 1200 HOH   A O    1 
HETATM 25530 O O    . HOH   FA 7 .   ? 39.944 -22.863 -36.079 1.00 38.37  ? 1201 HOH   A O    1 
HETATM 25531 O O    . HOH   FA 7 .   ? 45.839 18.313  -66.987 1.00 54.09  ? 1202 HOH   A O    1 
HETATM 25532 O O    . HOH   FA 7 .   ? 30.033 -19.012 -51.279 1.00 27.77  ? 1203 HOH   A O    1 
HETATM 25533 O O    . HOH   FA 7 .   ? 6.536  11.567  -4.640  1.00 29.27  ? 1204 HOH   A O    1 
HETATM 25534 O O    . HOH   FA 7 .   ? 36.069 -9.251  -17.061 1.00 24.36  ? 1205 HOH   A O    1 
HETATM 25535 O O    . HOH   FA 7 .   ? 43.632 30.103  -69.159 1.00 50.40  ? 1206 HOH   A O    1 
HETATM 25536 O O    . HOH   FA 7 .   ? 9.442  -14.697 -37.167 1.00 55.03  ? 1207 HOH   A O    1 
HETATM 25537 O O    . HOH   FA 7 .   ? 52.315 -4.010  -47.269 1.00 23.29  ? 1208 HOH   A O    1 
HETATM 25538 O O    . HOH   FA 7 .   ? 45.877 21.856  -44.305 1.00 30.63  ? 1209 HOH   A O    1 
HETATM 25539 O O    . HOH   FA 7 .   ? 32.941 9.279   -18.428 1.00 69.48  ? 1210 HOH   A O    1 
HETATM 25540 O O    . HOH   FA 7 .   ? 47.903 1.747   -55.169 1.00 15.55  ? 1211 HOH   A O    1 
HETATM 25541 O O    . HOH   FA 7 .   ? 23.305 -5.526  -17.028 1.00 17.49  ? 1212 HOH   A O    1 
HETATM 25542 O O    . HOH   FA 7 .   ? 36.241 7.138   -64.741 1.00 20.87  ? 1213 HOH   A O    1 
HETATM 25543 O O    . HOH   FA 7 .   ? 7.678  -14.682 -8.067  1.00 28.18  ? 1214 HOH   A O    1 
HETATM 25544 O O    . HOH   FA 7 .   ? 7.900  8.552   6.801   1.00 47.84  ? 1215 HOH   A O    1 
HETATM 25545 O O    . HOH   FA 7 .   ? 37.468 -13.303 -44.757 1.00 31.25  ? 1216 HOH   A O    1 
HETATM 25546 O O    . HOH   FA 7 .   ? 19.201 -8.463  -39.544 1.00 21.80  ? 1217 HOH   A O    1 
HETATM 25547 O O    . HOH   FA 7 .   ? 47.433 15.326  -63.470 1.00 25.14  ? 1218 HOH   A O    1 
HETATM 25548 O O    . HOH   FA 7 .   ? 24.508 7.488   -50.275 1.00 36.76  ? 1219 HOH   A O    1 
HETATM 25549 O O    . HOH   FA 7 .   ? 14.965 -14.262 -48.887 1.00 44.34  ? 1220 HOH   A O    1 
HETATM 25550 O O    . HOH   FA 7 .   ? 22.562 14.808  -59.961 1.00 41.29  ? 1221 HOH   A O    1 
HETATM 25551 O O    . HOH   FA 7 .   ? 52.831 -10.564 -49.724 1.00 26.10  ? 1222 HOH   A O    1 
HETATM 25552 O O    . HOH   FA 7 .   ? 23.838 -28.318 -26.166 1.00 35.61  ? 1223 HOH   A O    1 
HETATM 25553 O O    . HOH   FA 7 .   ? 14.887 31.162  -0.821  1.00 50.44  ? 1224 HOH   A O    1 
HETATM 25554 O O    . HOH   FA 7 .   ? 44.288 23.599  -42.267 1.00 42.60  ? 1225 HOH   A O    1 
HETATM 25555 O O    . HOH   FA 7 .   ? -0.946 -9.353  -13.894 1.00 33.79  ? 1226 HOH   A O    1 
HETATM 25556 O O    . HOH   FA 7 .   ? 47.712 -7.754  -64.039 1.00 27.15  ? 1227 HOH   A O    1 
HETATM 25557 O O    . HOH   FA 7 .   ? 9.381  6.996   -14.036 1.00 56.18  ? 1228 HOH   A O    1 
HETATM 25558 O O    . HOH   FA 7 .   ? 20.570 -3.771  -22.552 1.00 36.56  ? 1229 HOH   A O    1 
HETATM 25559 O O    . HOH   FA 7 .   ? 12.024 5.042   3.081   1.00 33.63  ? 1230 HOH   A O    1 
HETATM 25560 O O    . HOH   FA 7 .   ? 15.935 2.240   8.517   1.00 35.28  ? 1231 HOH   A O    1 
HETATM 25561 O O    . HOH   FA 7 .   ? 20.894 -3.019  -36.118 1.00 44.31  ? 1232 HOH   A O    1 
HETATM 25562 O O    . HOH   FA 7 .   ? 49.122 -5.420  -43.169 1.00 45.01  ? 1233 HOH   A O    1 
HETATM 25563 O O    . HOH   FA 7 .   ? 41.161 -23.983 -41.000 1.00 52.37  ? 1234 HOH   A O    1 
HETATM 25564 O O    . HOH   FA 7 .   ? 29.813 31.139  -9.652  1.00 30.47  ? 1235 HOH   A O    1 
HETATM 25565 O O    . HOH   FA 7 .   ? 54.279 12.010  -62.214 1.00 64.48  ? 1236 HOH   A O    1 
HETATM 25566 O O    . HOH   FA 7 .   ? 8.262  -14.876 -18.615 1.00 24.62  ? 1237 HOH   A O    1 
HETATM 25567 O O    . HOH   FA 7 .   ? 22.209 24.717  -46.458 1.00 43.12  ? 1238 HOH   A O    1 
HETATM 25568 O O    . HOH   FA 7 .   ? 30.606 53.459  -28.589 1.00 41.39  ? 1239 HOH   A O    1 
HETATM 25569 O O    . HOH   FA 7 .   ? 35.296 -13.226 -14.842 1.00 35.19  ? 1240 HOH   A O    1 
HETATM 25570 O O    . HOH   FA 7 .   ? 25.688 1.519   -15.008 1.00 34.07  ? 1241 HOH   A O    1 
HETATM 25571 O O    . HOH   FA 7 .   ? 13.527 -13.594 5.313   1.00 34.92  ? 1242 HOH   A O    1 
HETATM 25572 O O    . HOH   FA 7 .   ? 45.515 37.776  -29.723 1.00 39.84  ? 1243 HOH   A O    1 
HETATM 25573 O O    . HOH   FA 7 .   ? 19.933 -5.041  -55.048 1.00 26.88  ? 1244 HOH   A O    1 
HETATM 25574 O O    . HOH   FA 7 .   ? 17.458 2.881   -56.342 1.00 47.77  ? 1245 HOH   A O    1 
HETATM 25575 O O    . HOH   FA 7 .   ? 21.046 19.663  -56.806 1.00 45.23  ? 1246 HOH   A O    1 
HETATM 25576 O O    . HOH   FA 7 .   ? 17.695 -11.889 -45.916 1.00 24.22  ? 1247 HOH   A O    1 
HETATM 25577 O O    . HOH   FA 7 .   ? 45.074 -0.915  -44.032 1.00 24.63  ? 1248 HOH   A O    1 
HETATM 25578 O O    . HOH   FA 7 .   ? 47.037 -5.579  -55.172 1.00 19.84  ? 1249 HOH   A O    1 
HETATM 25579 O O    . HOH   FA 7 .   ? 37.182 34.356  -32.553 1.00 27.67  ? 1250 HOH   A O    1 
HETATM 25580 O O    . HOH   FA 7 .   ? 37.885 25.881  -68.173 1.00 44.74  ? 1251 HOH   A O    1 
HETATM 25581 O O    . HOH   FA 7 .   ? 45.373 2.573   -44.064 1.00 30.14  ? 1252 HOH   A O    1 
HETATM 25582 O O    . HOH   FA 7 .   ? 24.761 3.319   -13.550 1.00 25.12  ? 1253 HOH   A O    1 
HETATM 25583 O O    . HOH   FA 7 .   ? 15.103 -18.967 1.989   1.00 44.47  ? 1254 HOH   A O    1 
HETATM 25584 O O    . HOH   FA 7 .   ? 36.913 40.914  -44.499 1.00 34.04  ? 1255 HOH   A O    1 
HETATM 25585 O O    . HOH   FA 7 .   ? 18.156 31.537  -7.764  1.00 49.59  ? 1256 HOH   A O    1 
HETATM 25586 O O    . HOH   FA 7 .   ? 44.959 18.579  -43.622 1.00 33.94  ? 1257 HOH   A O    1 
HETATM 25587 O O    . HOH   FA 7 .   ? 24.353 -20.820 -48.608 1.00 37.07  ? 1258 HOH   A O    1 
HETATM 25588 O O    . HOH   FA 7 .   ? 22.068 3.576   -57.453 1.00 27.41  ? 1259 HOH   A O    1 
HETATM 25589 O O    . HOH   FA 7 .   ? 21.042 32.455  -1.364  1.00 46.49  ? 1260 HOH   A O    1 
HETATM 25590 O O    . HOH   FA 7 .   ? 34.721 -21.674 -41.027 1.00 35.18  ? 1261 HOH   A O    1 
HETATM 25591 O O    . HOH   FA 7 .   ? 35.688 -7.536  -30.068 1.00 24.90  ? 1262 HOH   A O    1 
HETATM 25592 O O    . HOH   FA 7 .   ? 24.898 33.610  -9.445  1.00 36.68  ? 1263 HOH   A O    1 
HETATM 25593 O O    . HOH   FA 7 .   ? 8.088  -13.190 -28.703 1.00 22.28  ? 1264 HOH   A O    1 
HETATM 25594 O O    . HOH   FA 7 .   ? 47.076 -12.708 -44.058 1.00 48.32  ? 1265 HOH   A O    1 
HETATM 25595 O O    . HOH   FA 7 .   ? 35.662 -0.656  -64.260 1.00 38.67  ? 1266 HOH   A O    1 
HETATM 25596 O O    . HOH   FA 7 .   ? 34.872 3.056   -1.553  1.00 38.69  ? 1267 HOH   A O    1 
HETATM 25597 O O    . HOH   FA 7 .   ? 32.237 17.272  -1.153  1.00 40.56  ? 1268 HOH   A O    1 
HETATM 25598 O O    . HOH   FA 7 .   ? 37.219 0.410   -39.430 1.00 52.53  ? 1269 HOH   A O    1 
HETATM 25599 O O    . HOH   FA 7 .   ? 32.399 26.733  -4.721  1.00 46.45  ? 1270 HOH   A O    1 
HETATM 25600 O O    . HOH   FA 7 .   ? 16.070 -8.242  -36.077 1.00 43.04  ? 1271 HOH   A O    1 
HETATM 25601 O O    . HOH   FA 7 .   ? 40.713 -9.367  -56.097 1.00 21.29  ? 1272 HOH   A O    1 
HETATM 25602 O O    . HOH   FA 7 .   ? 11.593 -11.506 -32.795 1.00 33.28  ? 1273 HOH   A O    1 
HETATM 25603 O O    . HOH   FA 7 .   ? 56.388 14.181  -60.861 1.00 36.48  ? 1274 HOH   A O    1 
HETATM 25604 O O    . HOH   FA 7 .   ? 47.312 -12.553 -52.473 1.00 25.75  ? 1275 HOH   A O    1 
HETATM 25605 O O    . HOH   FA 7 .   ? 37.187 -15.155 -28.635 1.00 21.48  ? 1276 HOH   A O    1 
HETATM 25606 O O    . HOH   FA 7 .   ? 26.784 32.778  -27.549 1.00 45.87  ? 1277 HOH   A O    1 
HETATM 25607 O O    . HOH   FA 7 .   ? 30.721 -21.307 -50.192 1.00 27.30  ? 1278 HOH   A O    1 
HETATM 25608 O O    . HOH   FA 7 .   ? 51.245 15.852  -51.044 1.00 41.67  ? 1279 HOH   A O    1 
HETATM 25609 O O    . HOH   FA 7 .   ? 36.695 -23.136 -38.596 1.00 35.11  ? 1280 HOH   A O    1 
HETATM 25610 O O    . HOH   FA 7 .   ? 39.077 49.356  -29.281 1.00 35.62  ? 1281 HOH   A O    1 
HETATM 25611 O O    . HOH   FA 7 .   ? 49.773 -10.513 -46.852 1.00 41.02  ? 1282 HOH   A O    1 
HETATM 25612 O O    . HOH   FA 7 .   ? 34.254 26.909  -65.922 1.00 62.50  ? 1283 HOH   A O    1 
HETATM 25613 O O    . HOH   FA 7 .   ? 30.814 -1.047  -18.923 1.00 32.91  ? 1284 HOH   A O    1 
HETATM 25614 O O    . HOH   FA 7 .   ? 50.330 16.594  -71.430 1.00 49.07  ? 1285 HOH   A O    1 
HETATM 25615 O O    . HOH   FA 7 .   ? 32.992 31.177  -1.432  1.00 45.02  ? 1286 HOH   A O    1 
HETATM 25616 O O    . HOH   FA 7 .   ? 45.519 15.212  -46.346 1.00 18.34  ? 1287 HOH   A O    1 
HETATM 25617 O O    . HOH   FA 7 .   ? 25.847 -9.563  -23.299 1.00 46.86  ? 1288 HOH   A O    1 
HETATM 25618 O O    . HOH   FA 7 .   ? 3.205  -1.288  -12.831 1.00 30.55  ? 1289 HOH   A O    1 
HETATM 25619 O O    . HOH   FA 7 .   ? 16.876 -6.034  -48.961 1.00 34.21  ? 1290 HOH   A O    1 
HETATM 25620 O O    . HOH   FA 7 .   ? 44.102 -5.460  -67.166 1.00 51.12  ? 1291 HOH   A O    1 
HETATM 25621 O O    . HOH   FA 7 .   ? 28.599 -7.097  -2.614  1.00 26.91  ? 1292 HOH   A O    1 
HETATM 25622 O O    . HOH   FA 7 .   ? 37.407 12.245  -62.651 1.00 23.77  ? 1293 HOH   A O    1 
HETATM 25623 O O    . HOH   FA 7 .   ? 22.636 0.327   -63.384 1.00 25.15  ? 1294 HOH   A O    1 
HETATM 25624 O O    . HOH   FA 7 .   ? 37.287 30.874  -30.335 1.00 35.36  ? 1295 HOH   A O    1 
HETATM 25625 O O    . HOH   FA 7 .   ? 27.900 20.099  -66.638 1.00 34.58  ? 1296 HOH   A O    1 
HETATM 25626 O O    . HOH   FA 7 .   ? 40.919 0.843   -38.496 1.00 40.33  ? 1297 HOH   A O    1 
HETATM 25627 O O    . HOH   FA 7 .   ? 1.938  4.784   -2.001  1.00 60.38  ? 1298 HOH   A O    1 
HETATM 25628 O O    . HOH   FA 7 .   ? 33.033 13.144  -6.532  1.00 36.33  ? 1299 HOH   A O    1 
HETATM 25629 O O    . HOH   FA 7 .   ? 44.785 27.472  -62.629 1.00 51.39  ? 1300 HOH   A O    1 
HETATM 25630 O O    . HOH   FA 7 .   ? 17.020 25.346  -3.278  1.00 37.12  ? 1301 HOH   A O    1 
HETATM 25631 O O    . HOH   FA 7 .   ? 50.195 23.155  -49.269 1.00 43.50  ? 1302 HOH   A O    1 
HETATM 25632 O O    . HOH   FA 7 .   ? 4.118  24.658  -10.939 1.00 68.59  ? 1303 HOH   A O    1 
HETATM 25633 O O    . HOH   FA 7 .   ? 24.212 22.833  -44.003 1.00 36.29  ? 1304 HOH   A O    1 
HETATM 25634 O O    . HOH   FA 7 .   ? 35.427 15.122  -4.009  1.00 60.41  ? 1305 HOH   A O    1 
HETATM 25635 O O    . HOH   FA 7 .   ? 20.556 6.042   -53.311 1.00 33.60  ? 1306 HOH   A O    1 
HETATM 25636 O O    . HOH   FA 7 .   ? 25.036 -17.372 -0.423  1.00 28.12  ? 1307 HOH   A O    1 
HETATM 25637 O O    . HOH   FA 7 .   ? 39.673 0.350   -62.573 1.00 28.02  ? 1308 HOH   A O    1 
HETATM 25638 O O    . HOH   FA 7 .   ? 26.763 29.838  -3.105  1.00 35.69  ? 1309 HOH   A O    1 
HETATM 25639 O O    . HOH   FA 7 .   ? 2.963  -10.278 -20.396 1.00 28.99  ? 1310 HOH   A O    1 
HETATM 25640 O O    . HOH   FA 7 .   ? 30.419 -11.238 2.626   1.00 38.14  ? 1311 HOH   A O    1 
HETATM 25641 O O    . HOH   FA 7 .   ? 35.540 5.899   -44.105 1.00 31.47  ? 1312 HOH   A O    1 
HETATM 25642 O O    . HOH   FA 7 .   ? 23.669 23.177  -24.355 1.00 50.41  ? 1313 HOH   A O    1 
HETATM 25643 O O    . HOH   FA 7 .   ? 19.606 1.009   3.146   1.00 26.73  ? 1314 HOH   A O    1 
HETATM 25644 O O    . HOH   FA 7 .   ? 24.831 -6.763  -60.957 1.00 35.25  ? 1315 HOH   A O    1 
HETATM 25645 O O    . HOH   FA 7 .   ? 23.458 21.487  -48.538 1.00 39.98  ? 1316 HOH   A O    1 
HETATM 25646 O O    . HOH   FA 7 .   ? 53.316 12.906  -47.922 1.00 44.05  ? 1317 HOH   A O    1 
HETATM 25647 O O    . HOH   FA 7 .   ? 43.209 -3.100  -39.744 1.00 37.00  ? 1318 HOH   A O    1 
HETATM 25648 O O    . HOH   FA 7 .   ? 18.934 -7.840  -27.064 1.00 24.61  ? 1319 HOH   A O    1 
HETATM 25649 O O    . HOH   FA 7 .   ? 28.568 -24.314 -13.314 1.00 36.46  ? 1320 HOH   A O    1 
HETATM 25650 O O    . HOH   FA 7 .   ? 57.425 -2.422  -55.111 1.00 22.63  ? 1321 HOH   A O    1 
HETATM 25651 O O    . HOH   FA 7 .   ? 25.522 -13.516 0.617   1.00 29.67  ? 1322 HOH   A O    1 
HETATM 25652 O O    . HOH   FA 7 .   ? 16.797 -19.431 -39.329 1.00 36.61  ? 1323 HOH   A O    1 
HETATM 25653 O O    . HOH   FA 7 .   ? 31.665 -0.242  -5.388  1.00 35.36  ? 1324 HOH   A O    1 
HETATM 25654 O O    . HOH   FA 7 .   ? 17.007 6.618   10.757  1.00 41.35  ? 1325 HOH   A O    1 
HETATM 25655 O O    . HOH   FA 7 .   ? 41.641 -2.000  -5.192  1.00 44.62  ? 1326 HOH   A O    1 
HETATM 25656 O O    . HOH   FA 7 .   ? 39.881 -27.015 -20.409 1.00 37.29  ? 1327 HOH   A O    1 
HETATM 25657 O O    . HOH   FA 7 .   ? 17.197 -7.086  4.501   1.00 53.33  ? 1328 HOH   A O    1 
HETATM 25658 O O    . HOH   FA 7 .   ? 16.809 -17.565 -45.615 1.00 35.42  ? 1329 HOH   A O    1 
HETATM 25659 O O    . HOH   FA 7 .   ? 41.856 -20.055 -35.197 1.00 36.95  ? 1330 HOH   A O    1 
HETATM 25660 O O    . HOH   FA 7 .   ? 40.792 -9.450  -53.275 1.00 17.13  ? 1331 HOH   A O    1 
HETATM 25661 O O    . HOH   FA 7 .   ? 36.339 1.044   -19.947 1.00 53.86  ? 1332 HOH   A O    1 
HETATM 25662 O O    . HOH   FA 7 .   ? 35.161 26.321  -24.227 1.00 53.12  ? 1333 HOH   A O    1 
HETATM 25663 O O    . HOH   FA 7 .   ? 34.342 -7.290  -18.339 1.00 23.35  ? 1334 HOH   A O    1 
HETATM 25664 O O    . HOH   FA 7 .   ? 33.914 -23.354 -38.901 1.00 28.80  ? 1335 HOH   A O    1 
HETATM 25665 O O    . HOH   FA 7 .   ? 44.816 20.673  -65.807 1.00 35.02  ? 1336 HOH   A O    1 
HETATM 25666 O O    . HOH   FA 7 .   ? 19.853 6.829   -63.779 1.00 34.51  ? 1337 HOH   A O    1 
HETATM 25667 O O    . HOH   FA 7 .   ? 30.558 3.406   -19.826 1.00 36.07  ? 1338 HOH   A O    1 
HETATM 25668 O O    . HOH   FA 7 .   ? 23.968 -19.494 -5.911  1.00 22.34  ? 1339 HOH   A O    1 
HETATM 25669 O O    . HOH   FA 7 .   ? 8.572  -22.258 -35.445 1.00 67.55  ? 1340 HOH   A O    1 
HETATM 25670 O O    . HOH   FA 7 .   ? 29.702 -25.310 -42.004 1.00 45.53  ? 1341 HOH   A O    1 
HETATM 25671 O O    . HOH   FA 7 .   ? 7.608  -10.090 -2.833  1.00 25.47  ? 1342 HOH   A O    1 
HETATM 25672 O O    . HOH   FA 7 .   ? 31.008 -12.722 -4.357  1.00 23.13  ? 1343 HOH   A O    1 
HETATM 25673 O O    . HOH   FA 7 .   ? 42.496 22.936  -56.197 1.00 28.32  ? 1344 HOH   A O    1 
HETATM 25674 O O    . HOH   FA 7 .   ? 20.887 6.363   -11.942 1.00 155.05 ? 1345 HOH   A O    1 
HETATM 25675 O O    . HOH   FA 7 .   ? 35.728 6.831   -67.568 1.00 36.27  ? 1346 HOH   A O    1 
HETATM 25676 O O    . HOH   FA 7 .   ? 34.121 -22.266 -19.532 1.00 24.64  ? 1347 HOH   A O    1 
HETATM 25677 O O    . HOH   FA 7 .   ? 26.408 -1.167  -34.521 1.00 36.74  ? 1348 HOH   A O    1 
HETATM 25678 O O    . HOH   FA 7 .   ? 34.941 -18.965 -13.335 1.00 27.76  ? 1349 HOH   A O    1 
HETATM 25679 O O    . HOH   FA 7 .   ? 43.775 40.694  -46.101 1.00 65.23  ? 1350 HOH   A O    1 
HETATM 25680 O O    . HOH   FA 7 .   ? 33.219 5.593   -13.335 1.00 34.93  ? 1351 HOH   A O    1 
HETATM 25681 O O    . HOH   FA 7 .   ? 56.354 0.443   -53.224 1.00 23.00  ? 1352 HOH   A O    1 
HETATM 25682 O O    . HOH   FA 7 .   ? 35.992 4.419   1.221   1.00 54.94  ? 1353 HOH   A O    1 
HETATM 25683 O O    . HOH   FA 7 .   ? 31.729 36.114  -54.504 1.00 44.20  ? 1354 HOH   A O    1 
HETATM 25684 O O    . HOH   FA 7 .   ? 35.521 -2.073  -4.860  1.00 45.59  ? 1355 HOH   A O    1 
HETATM 25685 O O    . HOH   FA 7 .   ? -1.725 0.281   -6.213  1.00 49.01  ? 1356 HOH   A O    1 
HETATM 25686 O O    . HOH   FA 7 .   ? 34.539 -13.315 -7.067  1.00 26.65  ? 1357 HOH   A O    1 
HETATM 25687 O O    . HOH   FA 7 .   ? 32.561 -30.366 -24.092 1.00 33.28  ? 1358 HOH   A O    1 
HETATM 25688 O O    . HOH   FA 7 .   ? 22.219 20.541  2.821   1.00 36.77  ? 1359 HOH   A O    1 
HETATM 25689 O O    . HOH   FA 7 .   ? 25.596 37.951  -17.080 1.00 46.92  ? 1360 HOH   A O    1 
HETATM 25690 O O    . HOH   FA 7 .   ? 36.009 9.885   4.708   1.00 52.53  ? 1361 HOH   A O    1 
HETATM 25691 O O    . HOH   FA 7 .   ? 22.145 9.230   -58.284 1.00 38.89  ? 1362 HOH   A O    1 
HETATM 25692 O O    . HOH   FA 7 .   ? 5.742  -18.652 -4.312  1.00 42.84  ? 1363 HOH   A O    1 
HETATM 25693 O O    . HOH   FA 7 .   ? 45.133 -4.443  -53.697 1.00 22.99  ? 1364 HOH   A O    1 
HETATM 25694 O O    . HOH   FA 7 .   ? 27.849 12.410  -64.235 1.00 37.90  ? 1365 HOH   A O    1 
HETATM 25695 O O    . HOH   FA 7 .   ? 16.375 15.068  8.616   1.00 32.90  ? 1366 HOH   A O    1 
HETATM 25696 O O    . HOH   FA 7 .   ? 26.446 22.775  -2.301  1.00 33.56  ? 1367 HOH   A O    1 
HETATM 25697 O O    . HOH   FA 7 .   ? 27.730 29.895  -65.668 1.00 50.23  ? 1368 HOH   A O    1 
HETATM 25698 O O    . HOH   FA 7 .   ? 43.277 19.612  -41.656 1.00 31.74  ? 1369 HOH   A O    1 
HETATM 25699 O O    . HOH   FA 7 .   ? 47.242 -7.233  -66.711 1.00 40.49  ? 1370 HOH   A O    1 
HETATM 25700 O O    . HOH   FA 7 .   ? 48.752 17.928  -54.874 1.00 28.73  ? 1371 HOH   A O    1 
HETATM 25701 O O    . HOH   FA 7 .   ? 25.075 1.722   4.665   1.00 44.23  ? 1372 HOH   A O    1 
HETATM 25702 O O    . HOH   FA 7 .   ? 34.516 16.592  -68.250 1.00 42.73  ? 1373 HOH   A O    1 
HETATM 25703 O O    . HOH   FA 7 .   ? 4.619  -6.860  -20.542 1.00 31.65  ? 1374 HOH   A O    1 
HETATM 25704 O O    . HOH   FA 7 .   ? 34.319 14.416  -45.422 1.00 39.04  ? 1375 HOH   A O    1 
HETATM 25705 O O    . HOH   FA 7 .   ? 8.039  -3.178  -20.843 1.00 44.58  ? 1376 HOH   A O    1 
HETATM 25706 O O    . HOH   FA 7 .   ? 41.492 10.527  -69.540 1.00 41.84  ? 1377 HOH   A O    1 
HETATM 25707 O O    . HOH   FA 7 .   ? 40.468 23.791  -57.898 1.00 27.62  ? 1378 HOH   A O    1 
HETATM 25708 O O    . HOH   FA 7 .   ? 19.933 -6.018  -62.910 1.00 46.89  ? 1379 HOH   A O    1 
HETATM 25709 O O    . HOH   FA 7 .   ? 2.896  20.513  -3.912  1.00 48.07  ? 1380 HOH   A O    1 
HETATM 25710 O O    . HOH   FA 7 .   ? 16.368 3.504   5.962   1.00 29.98  ? 1381 HOH   A O    1 
HETATM 25711 O O    . HOH   FA 7 .   ? 40.387 35.913  -31.311 1.00 37.89  ? 1382 HOH   A O    1 
HETATM 25712 O O    . HOH   FA 7 .   ? 5.525  -9.293  -20.790 1.00 36.12  ? 1383 HOH   A O    1 
HETATM 25713 O O    . HOH   FA 7 .   ? 32.633 38.333  -23.655 1.00 42.11  ? 1384 HOH   A O    1 
HETATM 25714 O O    . HOH   FA 7 .   ? 38.792 -2.707  -3.692  1.00 34.73  ? 1385 HOH   A O    1 
HETATM 25715 O O    . HOH   FA 7 .   ? 19.477 -7.658  -31.624 1.00 51.13  ? 1386 HOH   A O    1 
HETATM 25716 O O    . HOH   FA 7 .   ? 21.942 2.175   3.856   1.00 37.17  ? 1387 HOH   A O    1 
HETATM 25717 O O    . HOH   FA 7 .   ? 28.513 27.153  3.899   1.00 48.06  ? 1388 HOH   A O    1 
HETATM 25718 O O    . HOH   FA 7 .   ? 44.490 -15.714 -53.094 1.00 27.97  ? 1389 HOH   A O    1 
HETATM 25719 O O    . HOH   FA 7 .   ? 38.729 1.053   -1.017  1.00 35.89  ? 1390 HOH   A O    1 
HETATM 25720 O O    . HOH   FA 7 .   ? 21.099 3.285   6.170   1.00 36.43  ? 1391 HOH   A O    1 
HETATM 25721 O O    . HOH   FA 7 .   ? 25.696 -32.318 -34.539 1.00 59.59  ? 1392 HOH   A O    1 
HETATM 25722 O O    . HOH   FA 7 .   ? 33.504 31.689  3.081   1.00 36.44  ? 1393 HOH   A O    1 
HETATM 25723 O O    . HOH   FA 7 .   ? 24.638 -23.767 -50.047 1.00 41.91  ? 1394 HOH   A O    1 
HETATM 25724 O O    . HOH   FA 7 .   ? 40.409 -12.617 -33.891 1.00 65.66  ? 1395 HOH   A O    1 
HETATM 25725 O O    . HOH   FA 7 .   ? 39.480 -5.888  -8.722  1.00 40.20  ? 1396 HOH   A O    1 
HETATM 25726 O O    . HOH   FA 7 .   ? 36.083 -24.464 -48.260 1.00 56.95  ? 1397 HOH   A O    1 
HETATM 25727 O O    . HOH   FA 7 .   ? 42.470 -15.700 -57.254 1.00 33.86  ? 1398 HOH   A O    1 
HETATM 25728 O O    . HOH   FA 7 .   ? 18.040 37.106  -16.874 1.00 70.54  ? 1399 HOH   A O    1 
HETATM 25729 O O    . HOH   FA 7 .   ? 38.730 9.424   -3.482  1.00 35.60  ? 1400 HOH   A O    1 
HETATM 25730 O O    . HOH   FA 7 .   ? 36.567 5.526   -19.895 1.00 47.58  ? 1401 HOH   A O    1 
HETATM 25731 O O    . HOH   FA 7 .   ? 19.524 -20.204 -48.442 1.00 44.84  ? 1402 HOH   A O    1 
HETATM 25732 O O    . HOH   FA 7 .   ? 34.237 -9.950  6.946   1.00 55.02  ? 1403 HOH   A O    1 
HETATM 25733 O O    . HOH   FA 7 .   ? 47.110 -13.402 -58.350 1.00 45.44  ? 1404 HOH   A O    1 
HETATM 25734 O O    . HOH   FA 7 .   ? 20.908 -18.512 4.938   1.00 41.42  ? 1405 HOH   A O    1 
HETATM 25735 O O    . HOH   FA 7 .   ? 25.419 33.821  -0.610  1.00 42.60  ? 1406 HOH   A O    1 
HETATM 25736 O O    . HOH   FA 7 .   ? 21.677 14.156  -16.803 1.00 42.31  ? 1407 HOH   A O    1 
HETATM 25737 O O    . HOH   FA 7 .   ? 42.587 -8.946  -63.599 1.00 27.16  ? 1408 HOH   A O    1 
HETATM 25738 O O    . HOH   FA 7 .   ? 29.152 -0.253  -2.940  1.00 53.52  ? 1409 HOH   A O    1 
HETATM 25739 O O    . HOH   FA 7 .   ? 37.398 33.735  -24.030 1.00 51.07  ? 1410 HOH   A O    1 
HETATM 25740 O O    . HOH   FA 7 .   ? 12.308 21.536  0.677   1.00 49.19  ? 1411 HOH   A O    1 
HETATM 25741 O O    . HOH   FA 7 .   ? -1.847 -1.647  -8.023  1.00 36.75  ? 1412 HOH   A O    1 
HETATM 25742 O O    . HOH   FA 7 .   ? 42.284 3.198   -68.337 1.00 36.11  ? 1413 HOH   A O    1 
HETATM 25743 O O    . HOH   FA 7 .   ? 25.875 5.536   -38.713 1.00 33.98  ? 1414 HOH   A O    1 
HETATM 25744 O O    . HOH   FA 7 .   ? 8.671  24.695  -1.996  1.00 38.76  ? 1415 HOH   A O    1 
HETATM 25745 O O    . HOH   FA 7 .   ? 14.089 12.107  -15.296 1.00 47.40  ? 1416 HOH   A O    1 
HETATM 25746 O O    . HOH   FA 7 .   ? 36.772 29.980  -27.798 1.00 46.65  ? 1417 HOH   A O    1 
HETATM 25747 O O    . HOH   FA 7 .   ? 1.869  -6.374  0.585   1.00 34.02  ? 1418 HOH   A O    1 
HETATM 25748 O O    . HOH   FA 7 .   ? 36.280 0.533   -62.181 1.00 32.10  ? 1419 HOH   A O    1 
HETATM 25749 O O    . HOH   FA 7 .   ? 22.712 8.372   -64.653 1.00 28.62  ? 1420 HOH   A O    1 
HETATM 25750 O O    . HOH   FA 7 .   ? 27.967 2.689   -41.526 1.00 43.20  ? 1421 HOH   A O    1 
HETATM 25751 O O    . HOH   FA 7 .   ? 38.348 3.953   -69.416 1.00 68.10  ? 1422 HOH   A O    1 
HETATM 25752 O O    . HOH   FA 7 .   ? 28.647 -7.096  -66.051 1.00 41.70  ? 1423 HOH   A O    1 
HETATM 25753 O O    . HOH   FA 7 .   ? 19.455 -31.427 -22.105 1.00 42.04  ? 1424 HOH   A O    1 
HETATM 25754 O O    . HOH   FA 7 .   ? 51.806 17.844  -58.539 1.00 46.24  ? 1425 HOH   A O    1 
HETATM 25755 O O    . HOH   FA 7 .   ? 27.817 -26.814 -42.488 1.00 46.68  ? 1426 HOH   A O    1 
HETATM 25756 O O    . HOH   FA 7 .   ? 31.577 5.151   6.936   1.00 53.20  ? 1427 HOH   A O    1 
HETATM 25757 O O    . HOH   FA 7 .   ? 14.820 -19.006 -41.173 1.00 170.34 ? 1428 HOH   A O    1 
HETATM 25758 O O    . HOH   FA 7 .   ? 25.238 26.202  -60.653 1.00 32.44  ? 1429 HOH   A O    1 
HETATM 25759 O O    . HOH   FA 7 .   ? 20.111 -1.357  -20.707 1.00 22.32  ? 1430 HOH   A O    1 
HETATM 25760 O O    . HOH   FA 7 .   ? 35.194 -30.941 -23.041 1.00 38.25  ? 1431 HOH   A O    1 
HETATM 25761 O O    . HOH   FA 7 .   ? 21.699 -5.113  -34.545 1.00 35.53  ? 1432 HOH   A O    1 
HETATM 25762 O O    . HOH   FA 7 .   ? 32.625 -4.691  -6.042  1.00 29.40  ? 1433 HOH   A O    1 
HETATM 25763 O O    . HOH   FA 7 .   ? 45.877 23.623  -60.452 1.00 53.22  ? 1434 HOH   A O    1 
HETATM 25764 O O    . HOH   FA 7 .   ? 6.655  -23.207 -1.082  1.00 44.31  ? 1435 HOH   A O    1 
HETATM 25765 O O    . HOH   FA 7 .   ? 45.314 6.482   -44.582 1.00 43.12  ? 1436 HOH   A O    1 
HETATM 25766 O O    . HOH   FA 7 .   ? 43.703 25.954  -38.984 1.00 56.06  ? 1437 HOH   A O    1 
HETATM 25767 O O    . HOH   FA 7 .   ? 32.614 27.726  -2.137  1.00 29.78  ? 1438 HOH   A O    1 
HETATM 25768 O O    . HOH   FA 7 .   ? 33.329 17.991  -14.531 1.00 43.76  ? 1439 HOH   A O    1 
HETATM 25769 O O    . HOH   FA 7 .   ? 26.518 31.008  3.174   1.00 44.66  ? 1440 HOH   A O    1 
HETATM 25770 O O    . HOH   FA 7 .   ? 30.462 1.451   -47.770 1.00 26.71  ? 1441 HOH   A O    1 
HETATM 25771 O O    . HOH   FA 7 .   ? 30.770 14.433  -66.266 1.00 36.05  ? 1442 HOH   A O    1 
HETATM 25772 O O    . HOH   FA 7 .   ? 34.483 29.083  -0.574  1.00 70.00  ? 1443 HOH   A O    1 
HETATM 25773 O O    . HOH   FA 7 .   ? 42.149 -20.839 -28.492 1.00 44.87  ? 1444 HOH   A O    1 
HETATM 25774 O O    . HOH   FA 7 .   ? 7.746  24.976  -5.921  1.00 41.80  ? 1445 HOH   A O    1 
HETATM 25775 O O    . HOH   FA 7 .   ? 13.766 -4.304  -23.531 1.00 36.25  ? 1446 HOH   A O    1 
HETATM 25776 O O    . HOH   FA 7 .   ? 21.026 -19.142 -5.032  1.00 42.51  ? 1447 HOH   A O    1 
HETATM 25777 O O    . HOH   FA 7 .   ? 32.145 3.170   2.100   1.00 44.16  ? 1448 HOH   A O    1 
HETATM 25778 O O    . HOH   FA 7 .   ? 31.127 -22.749 -12.248 1.00 41.03  ? 1449 HOH   A O    1 
HETATM 25779 O O    . HOH   FA 7 .   ? 16.998 -29.660 -41.371 1.00 107.13 ? 1450 HOH   A O    1 
HETATM 25780 O O    . HOH   FA 7 .   ? 17.273 -24.548 -7.507  1.00 52.36  ? 1451 HOH   A O    1 
HETATM 25781 O O    . HOH   FA 7 .   ? 9.122  -1.507  1.414   1.00 30.00  ? 1452 HOH   A O    1 
HETATM 25782 O O    . HOH   FA 7 .   ? 24.799 17.074  -19.081 1.00 39.88  ? 1453 HOH   A O    1 
HETATM 25783 O O    . HOH   FA 7 .   ? 11.911 -10.799 6.067   1.00 44.95  ? 1454 HOH   A O    1 
HETATM 25784 O O    . HOH   FA 7 .   ? 38.407 -25.599 -14.284 1.00 39.72  ? 1455 HOH   A O    1 
HETATM 25785 O O    . HOH   FA 7 .   ? 40.382 8.316   -69.944 1.00 50.22  ? 1456 HOH   A O    1 
HETATM 25786 O O    . HOH   FA 7 .   ? 39.408 31.338  -58.666 1.00 41.02  ? 1457 HOH   A O    1 
HETATM 25787 O O    . HOH   FA 7 .   ? 31.964 -9.352  -29.546 1.00 44.88  ? 1458 HOH   A O    1 
HETATM 25788 O O    . HOH   FA 7 .   ? 15.848 -10.801 -41.488 1.00 40.96  ? 1459 HOH   A O    1 
HETATM 25789 O O    . HOH   FA 7 .   ? 14.503 -6.412  -43.311 1.00 49.90  ? 1460 HOH   A O    1 
HETATM 25790 O O    . HOH   FA 7 .   ? 28.977 37.462  -56.353 1.00 62.69  ? 1461 HOH   A O    1 
HETATM 25791 O O    . HOH   FA 7 .   ? 32.911 0.786   -38.745 1.00 50.39  ? 1462 HOH   A O    1 
HETATM 25792 O O    . HOH   FA 7 .   ? 23.508 24.179  -40.416 1.00 59.67  ? 1463 HOH   A O    1 
HETATM 25793 O O    . HOH   FA 7 .   ? 35.598 -18.061 -8.000  1.00 45.24  ? 1464 HOH   A O    1 
HETATM 25794 O O    . HOH   FA 7 .   ? 29.374 1.384   -18.700 1.00 35.60  ? 1465 HOH   A O    1 
HETATM 25795 O O    . HOH   FA 7 .   ? 11.010 -12.645 -35.179 1.00 52.39  ? 1466 HOH   A O    1 
HETATM 25796 O O    . HOH   FA 7 .   ? 28.791 33.939  -66.015 1.00 62.34  ? 1467 HOH   A O    1 
HETATM 25797 O O    . HOH   FA 7 .   ? 25.735 11.666  9.042   1.00 48.66  ? 1468 HOH   A O    1 
HETATM 25798 O O    . HOH   FA 7 .   ? 30.239 1.683   -66.179 1.00 38.39  ? 1469 HOH   A O    1 
HETATM 25799 O O    . HOH   FA 7 .   ? 45.651 10.252  -44.845 1.00 45.92  ? 1470 HOH   A O    1 
HETATM 25800 O O    . HOH   FA 7 .   ? 42.136 31.072  -57.405 1.00 55.32  ? 1471 HOH   A O    1 
HETATM 25801 O O    . HOH   FA 7 .   ? 40.346 3.736   -0.292  1.00 50.82  ? 1472 HOH   A O    1 
HETATM 25802 O O    . HOH   FA 7 .   ? -1.996 -15.619 -18.435 1.00 41.78  ? 1473 HOH   A O    1 
HETATM 25803 O O    . HOH   FA 7 .   ? 6.161  -11.926 -27.396 1.00 42.02  ? 1474 HOH   A O    1 
HETATM 25804 O O    . HOH   FA 7 .   ? 32.519 24.915  -1.169  1.00 53.69  ? 1475 HOH   A O    1 
HETATM 25805 O O    . HOH   FA 7 .   ? 22.087 -6.707  -24.914 1.00 52.11  ? 1476 HOH   A O    1 
HETATM 25806 O O    . HOH   FA 7 .   ? 32.682 -24.817 -19.068 1.00 51.07  ? 1477 HOH   A O    1 
HETATM 25807 O O    . HOH   FA 7 .   ? 31.246 -4.645  -3.244  1.00 44.43  ? 1478 HOH   A O    1 
HETATM 25808 O O    . HOH   FA 7 .   ? 31.133 -20.302 -58.530 1.00 44.88  ? 1479 HOH   A O    1 
HETATM 25809 O O    . HOH   FA 7 .   ? 25.870 -7.889  -25.519 1.00 47.70  ? 1480 HOH   A O    1 
HETATM 25810 O O    . HOH   FA 7 .   ? 0.632  -13.813 -7.931  1.00 44.80  ? 1481 HOH   A O    1 
HETATM 25811 O O    . HOH   FA 7 .   ? 33.556 -4.932  -32.225 1.00 41.46  ? 1482 HOH   A O    1 
HETATM 25812 O O    . HOH   FA 7 .   ? 48.423 19.283  -64.519 1.00 45.12  ? 1483 HOH   A O    1 
HETATM 25813 O O    . HOH   FA 7 .   ? 43.102 28.684  -58.273 1.00 44.90  ? 1484 HOH   A O    1 
HETATM 25814 O O    . HOH   FA 7 .   ? 16.909 -30.551 -16.760 1.00 48.72  ? 1485 HOH   A O    1 
HETATM 25815 O O    . HOH   FA 7 .   ? 30.034 10.808  -68.017 1.00 54.43  ? 1486 HOH   A O    1 
HETATM 25816 O O    . HOH   FA 7 .   ? 33.720 8.095   -68.640 1.00 39.37  ? 1487 HOH   A O    1 
HETATM 25817 O O    . HOH   FA 7 .   ? 28.740 -2.217  -35.537 1.00 29.11  ? 1488 HOH   A O    1 
HETATM 25818 O O    . HOH   FA 7 .   ? 37.076 28.641  -31.916 1.00 41.76  ? 1489 HOH   A O    1 
HETATM 25819 O O    . HOH   FA 7 .   ? 45.120 -17.485 -36.022 1.00 37.73  ? 1490 HOH   A O    1 
HETATM 25820 O O    . HOH   FA 7 .   ? 33.157 -7.107  -20.809 1.00 25.62  ? 1491 HOH   A O    1 
HETATM 25821 O O    . HOH   FA 7 .   ? 26.408 32.447  -65.689 1.00 50.93  ? 1492 HOH   A O    1 
HETATM 25822 O O    . HOH   FA 7 .   ? 21.505 -16.897 -50.527 1.00 46.83  ? 1493 HOH   A O    1 
HETATM 25823 O O    . HOH   FA 7 .   ? 5.902  -2.810  -18.566 1.00 40.06  ? 1494 HOH   A O    1 
HETATM 25824 O O    . HOH   FA 7 .   ? 21.578 -8.104  -61.928 1.00 41.08  ? 1495 HOH   A O    1 
HETATM 25825 O O    . HOH   FA 7 .   ? 34.526 -9.090  -15.027 1.00 31.61  ? 1496 HOH   A O    1 
HETATM 25826 O O    . HOH   FA 7 .   ? 47.361 -10.370 -62.800 1.00 48.75  ? 1497 HOH   A O    1 
HETATM 25827 O O    . HOH   FA 7 .   ? 35.576 -1.392  -19.111 1.00 44.19  ? 1498 HOH   A O    1 
HETATM 25828 O O    . HOH   FA 7 .   ? 43.952 22.233  -67.851 1.00 43.39  ? 1499 HOH   A O    1 
HETATM 25829 O O    . HOH   FA 7 .   ? 46.293 -5.298  -41.739 1.00 42.65  ? 1500 HOH   A O    1 
HETATM 25830 O O    . HOH   FA 7 .   ? 9.998  -16.431 -41.554 1.00 53.02  ? 1501 HOH   A O    1 
HETATM 25831 O O    . HOH   FA 7 .   ? 37.334 -3.226  -67.907 1.00 41.51  ? 1502 HOH   A O    1 
HETATM 25832 O O    . HOH   FA 7 .   ? 35.188 -28.051 -53.405 1.00 56.74  ? 1503 HOH   A O    1 
HETATM 25833 O O    . HOH   FA 7 .   ? 34.039 -6.620  -25.061 1.00 38.67  ? 1504 HOH   A O    1 
HETATM 25834 O O    . HOH   FA 7 .   ? 33.468 -4.443  -21.751 1.00 32.15  ? 1505 HOH   A O    1 
HETATM 25835 O O    . HOH   FA 7 .   ? 35.121 -1.016  -38.557 1.00 42.31  ? 1506 HOH   A O    1 
HETATM 25836 O O    . HOH   FA 7 .   ? 36.061 -16.972 -11.974 1.00 31.51  ? 1507 HOH   A O    1 
HETATM 25837 O O    . HOH   FA 7 .   ? 0.085  -8.263  -3.450  1.00 31.66  ? 1508 HOH   A O    1 
HETATM 25838 O O    . HOH   FA 7 .   ? 15.302 3.703   -16.733 1.00 31.37  ? 1509 HOH   A O    1 
HETATM 25839 O O    . HOH   FA 7 .   ? 31.362 -27.057 -19.565 1.00 40.37  ? 1510 HOH   A O    1 
HETATM 25840 O O    . HOH   FA 7 .   ? 17.829 38.772  -42.321 1.00 79.59  ? 1511 HOH   A O    1 
HETATM 25841 O O    . HOH   FA 7 .   ? 45.531 -24.255 -31.580 1.00 49.74  ? 1512 HOH   A O    1 
HETATM 25842 O O    . HOH   FA 7 .   ? 54.028 9.451   -42.592 1.00 80.12  ? 1513 HOH   A O    1 
HETATM 25843 O O    . HOH   FA 7 .   ? 51.638 -2.806  -44.821 1.00 37.43  ? 1514 HOH   A O    1 
HETATM 25844 O O    . HOH   FA 7 .   ? 36.173 -7.281  -66.555 1.00 48.30  ? 1515 HOH   A O    1 
HETATM 25845 O O    . HOH   FA 7 .   ? 0.421  -7.768  -1.049  1.00 41.99  ? 1516 HOH   A O    1 
HETATM 25846 O O    . HOH   FA 7 .   ? 12.151 -28.941 -14.403 1.00 52.63  ? 1517 HOH   A O    1 
HETATM 25847 O O    . HOH   FA 7 .   ? 42.268 -7.986  -66.033 1.00 39.40  ? 1518 HOH   A O    1 
HETATM 25848 O O    . HOH   FA 7 .   ? 28.196 4.766   -39.935 1.00 52.10  ? 1519 HOH   A O    1 
HETATM 25849 O O    . HOH   FA 7 .   ? 25.032 18.664  -66.227 1.00 43.92  ? 1520 HOH   A O    1 
HETATM 25850 O O    . HOH   FA 7 .   ? 31.810 8.243   -44.957 1.00 22.84  ? 1521 HOH   A O    1 
HETATM 25851 O O    . HOH   FA 7 .   ? 46.189 -24.878 -28.858 1.00 55.30  ? 1522 HOH   A O    1 
HETATM 25852 O O    . HOH   FA 7 .   ? 24.128 10.691  -21.081 1.00 55.78  ? 1523 HOH   A O    1 
HETATM 25853 O O    . HOH   FA 7 .   ? 22.591 4.633   -45.087 1.00 36.87  ? 1524 HOH   A O    1 
HETATM 25854 O O    . HOH   FA 7 .   ? 46.547 13.537  -44.459 1.00 36.04  ? 1525 HOH   A O    1 
HETATM 25855 O O    . HOH   FA 7 .   ? 38.111 -17.542 -10.021 1.00 47.62  ? 1526 HOH   A O    1 
HETATM 25856 O O    . HOH   FA 7 .   ? 22.241 7.917   -43.372 1.00 37.22  ? 1527 HOH   A O    1 
HETATM 25857 O O    . HOH   FA 7 .   ? 45.236 34.084  -27.054 1.00 51.26  ? 1528 HOH   A O    1 
HETATM 25858 O O    . HOH   FA 7 .   ? 17.342 -1.921  -20.573 1.00 30.61  ? 1529 HOH   A O    1 
HETATM 25859 O O    . HOH   FA 7 .   ? 31.290 6.505   -41.081 1.00 29.92  ? 1530 HOH   A O    1 
HETATM 25860 O O    . HOH   FA 7 .   ? 39.393 -12.886 -4.187  1.00 49.59  ? 1531 HOH   A O    1 
HETATM 25861 O O    . HOH   FA 7 .   ? 11.374 1.696   -25.546 1.00 52.01  ? 1532 HOH   A O    1 
HETATM 25862 O O    . HOH   FA 7 .   ? 19.685 12.776  -22.551 1.00 51.78  ? 1533 HOH   A O    1 
HETATM 25863 O O    . HOH   FA 7 .   ? 16.560 3.237   -22.939 1.00 46.75  ? 1534 HOH   A O    1 
HETATM 25864 O O    . HOH   FA 7 .   ? 17.723 8.436   -41.888 1.00 54.99  ? 1535 HOH   A O    1 
HETATM 25865 O O    . HOH   FA 7 .   ? 21.956 12.979  -24.080 1.00 48.16  ? 1536 HOH   A O    1 
HETATM 25866 O O    . HOH   FA 7 .   ? 16.942 9.610   -23.528 1.00 53.78  ? 1537 HOH   A O    1 
HETATM 25867 O O    . HOH   FA 7 .   ? 32.236 7.623   -34.076 1.00 69.17  ? 1538 HOH   A O    1 
HETATM 25868 O O    . HOH   FA 7 .   ? 24.248 14.883  -38.645 1.00 61.00  ? 1539 HOH   A O    1 
HETATM 25869 O O    . HOH   GA 7 .   ? 79.182 -20.624 -54.609 1.00 22.46  ? 1001 HOH   B O    1 
HETATM 25870 O O    . HOH   GA 7 .   ? 60.681 5.693   -74.422 1.00 35.68  ? 1002 HOH   B O    1 
HETATM 25871 O O    . HOH   GA 7 .   ? 63.914 16.640  -10.262 1.00 51.93  ? 1003 HOH   B O    1 
HETATM 25872 O O    . HOH   GA 7 .   ? 54.505 -24.653 -37.968 1.00 41.44  ? 1004 HOH   B O    1 
HETATM 25873 O O    . HOH   GA 7 .   ? 72.096 21.753  -81.002 1.00 58.74  ? 1005 HOH   B O    1 
HETATM 25874 O O    . HOH   GA 7 .   ? 60.055 0.804   -62.827 1.00 25.27  ? 1006 HOH   B O    1 
HETATM 25875 O O    . HOH   GA 7 .   ? 79.853 31.317  -72.041 1.00 46.26  ? 1007 HOH   B O    1 
HETATM 25876 O O    . HOH   GA 7 .   ? 54.861 -21.995 -37.575 1.00 38.89  ? 1008 HOH   B O    1 
HETATM 25877 O O    . HOH   GA 7 .   ? 85.957 12.892  -73.715 1.00 47.12  ? 1009 HOH   B O    1 
HETATM 25878 O O    . HOH   GA 7 .   ? 62.978 -3.606  -42.297 1.00 41.45  ? 1010 HOH   B O    1 
HETATM 25879 O O    . HOH   GA 7 .   ? 41.427 1.016   -13.813 1.00 27.22  ? 1011 HOH   B O    1 
HETATM 25880 O O    . HOH   GA 7 .   ? 72.964 42.366  -63.449 1.00 51.32  ? 1012 HOH   B O    1 
HETATM 25881 O O    . HOH   GA 7 .   ? 84.198 2.522   -77.508 1.00 85.70  ? 1013 HOH   B O    1 
HETATM 25882 O O    . HOH   GA 7 .   ? 68.249 35.654  -34.449 1.00 39.89  ? 1014 HOH   B O    1 
HETATM 25883 O O    . HOH   GA 7 .   ? 84.854 -7.194  -63.885 1.00 30.83  ? 1015 HOH   B O    1 
HETATM 25884 O O    . HOH   GA 7 .   ? 66.557 -13.006 -70.339 1.00 30.14  ? 1016 HOH   B O    1 
HETATM 25885 O O    . HOH   GA 7 .   ? 65.137 10.804  -10.939 1.00 23.71  ? 1017 HOH   B O    1 
HETATM 25886 O O    . HOH   GA 7 .   ? 59.088 -22.873 -32.936 1.00 33.47  ? 1018 HOH   B O    1 
HETATM 25887 O O    . HOH   GA 7 .   ? 77.378 -16.155 -47.369 1.00 29.33  ? 1019 HOH   B O    1 
HETATM 25888 O O    . HOH   GA 7 .   ? 52.541 1.454   -68.027 1.00 36.93  ? 1020 HOH   B O    1 
HETATM 25889 O O    . HOH   GA 7 .   ? 77.547 -24.812 -53.587 1.00 48.62  ? 1021 HOH   B O    1 
HETATM 25890 O O    . HOH   GA 7 .   ? 57.784 17.065  -53.854 1.00 57.09  ? 1022 HOH   B O    1 
HETATM 25891 O O    . HOH   GA 7 .   ? 60.342 24.162  -61.467 1.00 28.77  ? 1023 HOH   B O    1 
HETATM 25892 O O    . HOH   GA 7 .   ? 46.553 -7.920  -27.639 1.00 22.25  ? 1024 HOH   B O    1 
HETATM 25893 O O    . HOH   GA 7 .   ? 56.634 -22.742 -21.300 1.00 40.56  ? 1025 HOH   B O    1 
HETATM 25894 O O    . HOH   GA 7 .   ? 86.970 23.284  -60.183 1.00 36.12  ? 1026 HOH   B O    1 
HETATM 25895 O O    . HOH   GA 7 .   ? 51.124 37.245  -20.781 1.00 34.45  ? 1027 HOH   B O    1 
HETATM 25896 O O    . HOH   GA 7 .   ? 66.139 3.192   -27.577 1.00 27.80  ? 1028 HOH   B O    1 
HETATM 25897 O O    . HOH   GA 7 .   ? 58.416 17.022  -75.238 1.00 59.90  ? 1029 HOH   B O    1 
HETATM 25898 O O    . HOH   GA 7 .   ? 86.356 10.336  -68.012 1.00 23.51  ? 1030 HOH   B O    1 
HETATM 25899 O O    . HOH   GA 7 .   ? 53.023 6.243   -58.571 1.00 32.86  ? 1031 HOH   B O    1 
HETATM 25900 O O    . HOH   GA 7 .   ? 74.946 25.600  -46.231 1.00 37.36  ? 1032 HOH   B O    1 
HETATM 25901 O O    . HOH   GA 7 .   ? 43.605 -18.320 -20.309 1.00 35.83  ? 1033 HOH   B O    1 
HETATM 25902 O O    . HOH   GA 7 .   ? 61.902 27.204  -71.227 1.00 29.39  ? 1034 HOH   B O    1 
HETATM 25903 O O    . HOH   GA 7 .   ? 54.964 43.293  -19.515 1.00 46.61  ? 1035 HOH   B O    1 
HETATM 25904 O O    . HOH   GA 7 .   ? 65.855 -17.710 -63.953 1.00 23.38  ? 1036 HOH   B O    1 
HETATM 25905 O O    . HOH   GA 7 .   ? 54.390 37.142  -40.270 1.00 46.28  ? 1037 HOH   B O    1 
HETATM 25906 O O    . HOH   GA 7 .   ? 67.686 -14.600 -26.215 1.00 22.97  ? 1038 HOH   B O    1 
HETATM 25907 O O    . HOH   GA 7 .   ? 71.703 1.515   -57.893 1.00 28.03  ? 1039 HOH   B O    1 
HETATM 25908 O O    . HOH   GA 7 .   ? 63.273 -21.993 -55.598 1.00 30.76  ? 1040 HOH   B O    1 
HETATM 25909 O O    . HOH   GA 7 .   ? 83.274 28.060  -63.077 1.00 23.06  ? 1041 HOH   B O    1 
HETATM 25910 O O    . HOH   GA 7 .   ? 87.527 18.501  -73.523 1.00 37.70  ? 1042 HOH   B O    1 
HETATM 25911 O O    . HOH   GA 7 .   ? 61.523 2.074   -8.333  1.00 33.22  ? 1043 HOH   B O    1 
HETATM 25912 O O    . HOH   GA 7 .   ? 50.003 -1.006  -8.587  1.00 24.76  ? 1044 HOH   B O    1 
HETATM 25913 O O    . HOH   GA 7 .   ? 74.268 -3.347  -81.441 1.00 42.85  ? 1045 HOH   B O    1 
HETATM 25914 O O    . HOH   GA 7 .   ? 81.876 -10.757 -57.645 1.00 24.42  ? 1046 HOH   B O    1 
HETATM 25915 O O    . HOH   GA 7 .   ? 61.220 14.652  -59.466 1.00 23.41  ? 1047 HOH   B O    1 
HETATM 25916 O O    . HOH   GA 7 .   ? 72.672 36.760  -41.211 1.00 44.53  ? 1048 HOH   B O    1 
HETATM 25917 O O    . HOH   GA 7 .   ? 70.549 -22.707 -64.500 1.00 33.76  ? 1049 HOH   B O    1 
HETATM 25918 O O    . HOH   GA 7 .   ? 76.164 34.163  -70.068 1.00 35.98  ? 1050 HOH   B O    1 
HETATM 25919 O O    . HOH   GA 7 .   ? 69.285 -22.048 -41.969 1.00 28.38  ? 1051 HOH   B O    1 
HETATM 25920 O O    . HOH   GA 7 .   ? 56.953 -1.092  -65.201 1.00 31.02  ? 1052 HOH   B O    1 
HETATM 25921 O O    . HOH   GA 7 .   ? 64.352 34.577  -37.603 1.00 41.04  ? 1053 HOH   B O    1 
HETATM 25922 O O    . HOH   GA 7 .   ? 62.932 -24.213 -40.123 1.00 36.48  ? 1054 HOH   B O    1 
HETATM 25923 O O    . HOH   GA 7 .   ? 82.162 15.276  -58.110 1.00 44.24  ? 1055 HOH   B O    1 
HETATM 25924 O O    . HOH   GA 7 .   ? 68.227 41.350  -29.125 1.00 34.91  ? 1056 HOH   B O    1 
HETATM 25925 O O    . HOH   GA 7 .   ? 59.521 7.330   -26.992 1.00 27.07  ? 1057 HOH   B O    1 
HETATM 25926 O O    . HOH   GA 7 .   ? 64.747 39.847  -54.120 1.00 44.62  ? 1058 HOH   B O    1 
HETATM 25927 O O    . HOH   GA 7 .   ? 59.695 20.621  -63.686 1.00 41.37  ? 1059 HOH   B O    1 
HETATM 25928 O O    . HOH   GA 7 .   ? 69.460 28.001  -71.379 1.00 25.07  ? 1060 HOH   B O    1 
HETATM 25929 O O    . HOH   GA 7 .   ? 38.277 -1.320  -25.609 1.00 30.59  ? 1061 HOH   B O    1 
HETATM 25930 O O    . HOH   GA 7 .   ? 77.936 18.345  -77.243 1.00 26.50  ? 1062 HOH   B O    1 
HETATM 25931 O O    . HOH   GA 7 .   ? 79.905 11.569  -76.245 1.00 34.01  ? 1063 HOH   B O    1 
HETATM 25932 O O    . HOH   GA 7 .   ? 61.528 5.297   -68.202 1.00 28.95  ? 1064 HOH   B O    1 
HETATM 25933 O O    . HOH   GA 7 .   ? 72.402 35.577  -63.875 1.00 26.66  ? 1065 HOH   B O    1 
HETATM 25934 O O    . HOH   GA 7 .   ? 63.382 -7.797  -17.281 1.00 30.78  ? 1066 HOH   B O    1 
HETATM 25935 O O    . HOH   GA 7 .   ? 75.705 32.019  -67.123 1.00 28.16  ? 1067 HOH   B O    1 
HETATM 25936 O O    . HOH   GA 7 .   ? 63.673 -2.846  -56.683 1.00 28.69  ? 1068 HOH   B O    1 
HETATM 25937 O O    . HOH   GA 7 .   ? 76.672 14.612  -55.977 1.00 43.59  ? 1069 HOH   B O    1 
HETATM 25938 O O    . HOH   GA 7 .   ? 36.585 -11.893 -17.812 1.00 21.68  ? 1070 HOH   B O    1 
HETATM 25939 O O    . HOH   GA 7 .   ? 85.688 -8.725  -66.874 1.00 47.79  ? 1071 HOH   B O    1 
HETATM 25940 O O    . HOH   GA 7 .   ? 42.973 10.032  -12.245 1.00 43.19  ? 1072 HOH   B O    1 
HETATM 25941 O O    . HOH   GA 7 .   ? 52.575 12.105  -30.149 1.00 37.75  ? 1073 HOH   B O    1 
HETATM 25942 O O    . HOH   GA 7 .   ? 61.407 30.559  -30.948 1.00 30.26  ? 1074 HOH   B O    1 
HETATM 25943 O O    . HOH   GA 7 .   ? 67.524 -2.771  -10.792 1.00 33.42  ? 1075 HOH   B O    1 
HETATM 25944 O O    . HOH   GA 7 .   ? 68.608 28.825  -16.225 1.00 47.79  ? 1076 HOH   B O    1 
HETATM 25945 O O    . HOH   GA 7 .   ? 61.895 3.434   -66.294 1.00 26.54  ? 1077 HOH   B O    1 
HETATM 25946 O O    . HOH   GA 7 .   ? 85.172 22.712  -65.683 1.00 25.24  ? 1078 HOH   B O    1 
HETATM 25947 O O    . HOH   GA 7 .   ? 75.013 -9.225  -30.148 1.00 33.54  ? 1079 HOH   B O    1 
HETATM 25948 O O    . HOH   GA 7 .   ? 54.260 37.051  -18.731 1.00 38.76  ? 1080 HOH   B O    1 
HETATM 25949 O O    . HOH   GA 7 .   ? 78.312 37.498  -46.227 1.00 38.26  ? 1081 HOH   B O    1 
HETATM 25950 O O    . HOH   GA 7 .   ? 54.516 32.026  -35.356 1.00 38.06  ? 1082 HOH   B O    1 
HETATM 25951 O O    . HOH   GA 7 .   ? 87.746 18.776  -61.201 1.00 43.27  ? 1083 HOH   B O    1 
HETATM 25952 O O    . HOH   GA 7 .   ? 52.209 27.759  -33.262 1.00 41.92  ? 1084 HOH   B O    1 
HETATM 25953 O O    . HOH   GA 7 .   ? 45.861 -9.565  -7.638  1.00 42.04  ? 1085 HOH   B O    1 
HETATM 25954 O O    . HOH   GA 7 .   ? 53.238 9.035   -61.156 1.00 40.02  ? 1086 HOH   B O    1 
HETATM 25955 O O    . HOH   GA 7 .   ? 52.536 5.079   -10.890 1.00 24.27  ? 1087 HOH   B O    1 
HETATM 25956 O O    . HOH   GA 7 .   ? 61.214 -4.981  -43.150 1.00 28.66  ? 1088 HOH   B O    1 
HETATM 25957 O O    . HOH   GA 7 .   ? 83.835 23.366  -77.723 1.00 32.58  ? 1089 HOH   B O    1 
HETATM 25958 O O    . HOH   GA 7 .   ? 41.570 -11.276 -11.229 1.00 24.08  ? 1090 HOH   B O    1 
HETATM 25959 O O    . HOH   GA 7 .   ? 57.348 -17.805 -26.227 1.00 23.06  ? 1091 HOH   B O    1 
HETATM 25960 O O    . HOH   GA 7 .   ? 86.231 -1.097  -64.329 1.00 24.46  ? 1092 HOH   B O    1 
HETATM 25961 O O    . HOH   GA 7 .   ? 58.194 43.217  -21.571 1.00 42.17  ? 1093 HOH   B O    1 
HETATM 25962 O O    . HOH   GA 7 .   ? 79.954 -2.575  -52.125 1.00 45.48  ? 1094 HOH   B O    1 
HETATM 25963 O O    . HOH   GA 7 .   ? 66.663 -20.474 -23.303 1.00 32.21  ? 1095 HOH   B O    1 
HETATM 25964 O O    . HOH   GA 7 .   ? 90.289 -0.953  -72.968 1.00 48.07  ? 1096 HOH   B O    1 
HETATM 25965 O O    . HOH   GA 7 .   ? 50.860 -20.620 -28.802 1.00 42.39  ? 1097 HOH   B O    1 
HETATM 25966 O O    . HOH   GA 7 .   ? 41.230 -1.042  -15.501 1.00 19.41  ? 1098 HOH   B O    1 
HETATM 25967 O O    . HOH   GA 7 .   ? 59.995 24.332  -31.298 1.00 45.67  ? 1099 HOH   B O    1 
HETATM 25968 O O    . HOH   GA 7 .   ? 59.621 -24.506 -30.481 1.00 51.44  ? 1100 HOH   B O    1 
HETATM 25969 O O    . HOH   GA 7 .   ? 40.735 10.615  -20.829 1.00 38.27  ? 1101 HOH   B O    1 
HETATM 25970 O O    . HOH   GA 7 .   ? 45.334 30.097  -20.662 1.00 47.35  ? 1102 HOH   B O    1 
HETATM 25971 O O    . HOH   GA 7 .   ? 86.216 4.605   -67.236 1.00 26.30  ? 1103 HOH   B O    1 
HETATM 25972 O O    . HOH   GA 7 .   ? 67.570 -13.455 -18.966 1.00 35.26  ? 1104 HOH   B O    1 
HETATM 25973 O O    . HOH   GA 7 .   ? 47.549 -0.237  -4.738  1.00 42.60  ? 1105 HOH   B O    1 
HETATM 25974 O O    . HOH   GA 7 .   ? 68.333 47.919  -25.847 1.00 55.09  ? 1106 HOH   B O    1 
HETATM 25975 O O    . HOH   GA 7 .   ? 49.226 -8.266  -38.790 1.00 26.61  ? 1107 HOH   B O    1 
HETATM 25976 O O    . HOH   GA 7 .   ? 70.060 9.445   -62.789 1.00 19.36  ? 1108 HOH   B O    1 
HETATM 25977 O O    . HOH   GA 7 .   ? 65.457 19.726  -70.696 1.00 25.75  ? 1109 HOH   B O    1 
HETATM 25978 O O    . HOH   GA 7 .   ? 61.976 27.676  -31.727 1.00 45.40  ? 1110 HOH   B O    1 
HETATM 25979 O O    . HOH   GA 7 .   ? 69.177 -17.932 -24.577 1.00 43.15  ? 1111 HOH   B O    1 
HETATM 25980 O O    . HOH   GA 7 .   ? 76.923 -17.093 -32.874 1.00 38.62  ? 1112 HOH   B O    1 
HETATM 25981 O O    . HOH   GA 7 .   ? 89.969 -10.812 -52.606 1.00 41.51  ? 1113 HOH   B O    1 
HETATM 25982 O O    . HOH   GA 7 .   ? 78.736 24.716  -81.076 1.00 36.99  ? 1114 HOH   B O    1 
HETATM 25983 O O    . HOH   GA 7 .   ? 67.155 -10.770 -21.220 1.00 25.52  ? 1115 HOH   B O    1 
HETATM 25984 O O    . HOH   GA 7 .   ? 51.584 -13.332 -21.869 1.00 22.85  ? 1116 HOH   B O    1 
HETATM 25985 O O    . HOH   GA 7 .   ? 65.051 14.501  -77.965 1.00 37.80  ? 1117 HOH   B O    1 
HETATM 25986 O O    . HOH   GA 7 .   ? 80.403 -8.993  -46.954 1.00 36.85  ? 1118 HOH   B O    1 
HETATM 25987 O O    . HOH   GA 7 .   ? 75.035 8.807   -80.351 1.00 46.32  ? 1119 HOH   B O    1 
HETATM 25988 O O    . HOH   GA 7 .   ? 60.942 53.570  -28.105 1.00 35.19  ? 1120 HOH   B O    1 
HETATM 25989 O O    . HOH   GA 7 .   ? 62.237 -1.331  -31.321 1.00 37.47  ? 1121 HOH   B O    1 
HETATM 25990 O O    . HOH   GA 7 .   ? 49.553 -0.612  -60.102 1.00 20.37  ? 1122 HOH   B O    1 
HETATM 25991 O O    . HOH   GA 7 .   ? 74.743 -7.888  -26.459 1.00 46.96  ? 1123 HOH   B O    1 
HETATM 25992 O O    . HOH   GA 7 .   ? 53.284 -19.866 -16.930 1.00 43.56  ? 1124 HOH   B O    1 
HETATM 25993 O O    . HOH   GA 7 .   ? 88.764 13.056  -63.667 1.00 38.26  ? 1125 HOH   B O    1 
HETATM 25994 O O    . HOH   GA 7 .   ? 47.245 -15.071 -12.620 1.00 42.88  ? 1126 HOH   B O    1 
HETATM 25995 O O    . HOH   GA 7 .   ? 60.341 0.104   -65.318 1.00 33.96  ? 1127 HOH   B O    1 
HETATM 25996 O O    . HOH   GA 7 .   ? 61.218 -24.113 -33.837 1.00 44.86  ? 1128 HOH   B O    1 
HETATM 25997 O O    . HOH   GA 7 .   ? 45.202 2.706   -10.283 1.00 21.80  ? 1129 HOH   B O    1 
HETATM 25998 O O    . HOH   GA 7 .   ? 55.908 6.576   -28.877 1.00 32.24  ? 1130 HOH   B O    1 
HETATM 25999 O O    . HOH   GA 7 .   ? 91.476 21.706  -66.546 1.00 38.52  ? 1131 HOH   B O    1 
HETATM 26000 O O    . HOH   GA 7 .   ? 71.292 12.270  -61.283 1.00 43.18  ? 1132 HOH   B O    1 
HETATM 26001 O O    . HOH   GA 7 .   ? 53.827 15.891  -10.867 1.00 25.62  ? 1133 HOH   B O    1 
HETATM 26002 O O    . HOH   GA 7 .   ? 47.181 -17.442 -34.284 1.00 34.80  ? 1134 HOH   B O    1 
HETATM 26003 O O    . HOH   GA 7 .   ? 79.586 16.818  -83.051 1.00 43.38  ? 1135 HOH   B O    1 
HETATM 26004 O O    . HOH   GA 7 .   ? 60.391 -20.586 -21.372 1.00 32.63  ? 1136 HOH   B O    1 
HETATM 26005 O O    . HOH   GA 7 .   ? 82.830 36.897  -61.072 1.00 42.31  ? 1137 HOH   B O    1 
HETATM 26006 O O    . HOH   GA 7 .   ? 71.510 -4.263  -76.184 1.00 28.80  ? 1138 HOH   B O    1 
HETATM 26007 O O    . HOH   GA 7 .   ? 61.485 -1.024  -56.372 1.00 25.60  ? 1139 HOH   B O    1 
HETATM 26008 O O    . HOH   GA 7 .   ? 47.925 -5.113  -35.530 1.00 34.28  ? 1140 HOH   B O    1 
HETATM 26009 O O    . HOH   GA 7 .   ? 83.764 34.598  -67.677 1.00 82.14  ? 1141 HOH   B O    1 
HETATM 26010 O O    . HOH   GA 7 .   ? 91.859 6.228   -66.300 1.00 31.81  ? 1142 HOH   B O    1 
HETATM 26011 O O    . HOH   GA 7 .   ? 54.130 10.322  -28.886 1.00 31.58  ? 1143 HOH   B O    1 
HETATM 26012 O O    . HOH   GA 7 .   ? 67.305 3.102   -24.295 1.00 37.16  ? 1144 HOH   B O    1 
HETATM 26013 O O    . HOH   GA 7 .   ? 77.775 -17.858 -49.309 1.00 28.11  ? 1145 HOH   B O    1 
HETATM 26014 O O    . HOH   GA 7 .   ? 88.580 24.411  -67.493 1.00 47.26  ? 1146 HOH   B O    1 
HETATM 26015 O O    . HOH   GA 7 .   ? 70.651 -2.419  -55.086 1.00 35.61  ? 1147 HOH   B O    1 
HETATM 26016 O O    . HOH   GA 7 .   ? 81.382 35.642  -53.102 1.00 25.17  ? 1148 HOH   B O    1 
HETATM 26017 O O    . HOH   GA 7 .   ? 70.088 -1.596  -27.552 1.00 41.30  ? 1149 HOH   B O    1 
HETATM 26018 O O    . HOH   GA 7 .   ? 83.108 -1.492  -51.357 1.00 47.56  ? 1150 HOH   B O    1 
HETATM 26019 O O    . HOH   GA 7 .   ? 58.305 30.487  -46.807 1.00 39.96  ? 1151 HOH   B O    1 
HETATM 26020 O O    . HOH   GA 7 .   ? 40.845 3.163   -26.438 1.00 44.20  ? 1152 HOH   B O    1 
HETATM 26021 O O    . HOH   GA 7 .   ? 57.652 24.839  -70.046 1.00 36.80  ? 1153 HOH   B O    1 
HETATM 26022 O O    . HOH   GA 7 .   ? 80.616 26.584  -49.395 1.00 43.17  ? 1154 HOH   B O    1 
HETATM 26023 O O    . HOH   GA 7 .   ? 58.021 -2.642  -36.694 1.00 32.15  ? 1155 HOH   B O    1 
HETATM 26024 O O    . HOH   GA 7 .   ? 94.950 16.035  -62.751 1.00 60.43  ? 1156 HOH   B O    1 
HETATM 26025 O O    . HOH   GA 7 .   ? 50.015 14.822  -9.635  1.00 35.09  ? 1157 HOH   B O    1 
HETATM 26026 O O    . HOH   GA 7 .   ? 63.931 -1.426  -14.687 1.00 22.97  ? 1158 HOH   B O    1 
HETATM 26027 O O    . HOH   GA 7 .   ? 56.109 -4.292  -48.219 1.00 24.80  ? 1159 HOH   B O    1 
HETATM 26028 O O    . HOH   GA 7 .   ? 84.114 -4.370  -73.946 1.00 37.57  ? 1160 HOH   B O    1 
HETATM 26029 O O    . HOH   GA 7 .   ? 89.959 3.979   -68.699 1.00 37.52  ? 1161 HOH   B O    1 
HETATM 26030 O O    . HOH   GA 7 .   ? 73.233 40.162  -56.281 1.00 43.92  ? 1162 HOH   B O    1 
HETATM 26031 O O    . HOH   GA 7 .   ? 66.283 9.296   -59.366 1.00 30.84  ? 1163 HOH   B O    1 
HETATM 26032 O O    . HOH   GA 7 .   ? 56.336 -3.405  -8.269  1.00 35.77  ? 1164 HOH   B O    1 
HETATM 26033 O O    . HOH   GA 7 .   ? 77.999 10.650  -78.994 1.00 57.87  ? 1165 HOH   B O    1 
HETATM 26034 O O    . HOH   GA 7 .   ? 64.276 5.894   -53.401 1.00 36.18  ? 1166 HOH   B O    1 
HETATM 26035 O O    . HOH   GA 7 .   ? 55.666 25.110  -31.161 1.00 38.05  ? 1167 HOH   B O    1 
HETATM 26036 O O    . HOH   GA 7 .   ? 58.471 26.180  -2.756  1.00 54.74  ? 1168 HOH   B O    1 
HETATM 26037 O O    . HOH   GA 7 .   ? 69.726 24.612  -24.738 1.00 48.57  ? 1169 HOH   B O    1 
HETATM 26038 O O    . HOH   GA 7 .   ? 85.253 -4.726  -55.741 1.00 45.43  ? 1170 HOH   B O    1 
HETATM 26039 O O    . HOH   GA 7 .   ? 82.285 24.710  -74.576 1.00 55.55  ? 1171 HOH   B O    1 
HETATM 26040 O O    . HOH   GA 7 .   ? 69.298 7.084   -12.724 1.00 41.36  ? 1172 HOH   B O    1 
HETATM 26041 O O    . HOH   GA 7 .   ? 51.356 -14.901 -24.128 1.00 21.49  ? 1173 HOH   B O    1 
HETATM 26042 O O    . HOH   GA 7 .   ? 44.876 -19.142 -23.286 1.00 41.40  ? 1174 HOH   B O    1 
HETATM 26043 O O    . HOH   GA 7 .   ? 44.026 -4.045  -21.570 1.00 19.90  ? 1175 HOH   B O    1 
HETATM 26044 O O    . HOH   GA 7 .   ? 61.291 -2.391  -33.920 1.00 34.34  ? 1176 HOH   B O    1 
HETATM 26045 O O    . HOH   GA 7 .   ? 58.144 28.000  -36.781 1.00 44.21  ? 1177 HOH   B O    1 
HETATM 26046 O O    . HOH   GA 7 .   ? 42.493 -8.968  -11.764 1.00 27.57  ? 1178 HOH   B O    1 
HETATM 26047 O O    . HOH   GA 7 .   ? 46.857 -2.700  -32.815 1.00 25.77  ? 1179 HOH   B O    1 
HETATM 26048 O O    . HOH   GA 7 .   ? 56.500 -4.480  -69.658 1.00 26.18  ? 1180 HOH   B O    1 
HETATM 26049 O O    . HOH   GA 7 .   ? 75.944 -1.050  -15.757 1.00 49.30  ? 1181 HOH   B O    1 
HETATM 26050 O O    . HOH   GA 7 .   ? 63.948 -6.007  -40.095 1.00 29.51  ? 1182 HOH   B O    1 
HETATM 26051 O O    . HOH   GA 7 .   ? 59.204 4.790   -78.150 1.00 42.91  ? 1183 HOH   B O    1 
HETATM 26052 O O    . HOH   GA 7 .   ? 83.532 22.057  -80.454 1.00 39.97  ? 1184 HOH   B O    1 
HETATM 26053 O O    . HOH   GA 7 .   ? 61.842 -22.463 -32.089 1.00 32.90  ? 1185 HOH   B O    1 
HETATM 26054 O O    . HOH   GA 7 .   ? 71.749 -1.739  -31.349 1.00 27.66  ? 1186 HOH   B O    1 
HETATM 26055 O O    . HOH   GA 7 .   ? 47.727 -3.211  -6.800  1.00 24.47  ? 1187 HOH   B O    1 
HETATM 26056 O O    . HOH   GA 7 .   ? 55.956 -1.406  -61.094 1.00 26.13  ? 1188 HOH   B O    1 
HETATM 26057 O O    . HOH   GA 7 .   ? 69.800 -2.886  -18.881 1.00 35.32  ? 1189 HOH   B O    1 
HETATM 26058 O O    . HOH   GA 7 .   ? 88.793 41.492  -41.732 1.00 60.90  ? 1190 HOH   B O    1 
HETATM 26059 O O    . HOH   GA 7 .   ? 46.248 -5.935  -32.920 1.00 18.50  ? 1191 HOH   B O    1 
HETATM 26060 O O    . HOH   GA 7 .   ? 45.720 18.377  -25.342 1.00 34.85  ? 1192 HOH   B O    1 
HETATM 26061 O O    . HOH   GA 7 .   ? 55.696 -2.096  -10.764 1.00 24.65  ? 1193 HOH   B O    1 
HETATM 26062 O O    . HOH   GA 7 .   ? 86.454 -1.071  -83.582 1.00 70.86  ? 1194 HOH   B O    1 
HETATM 26063 O O    . HOH   GA 7 .   ? 81.910 6.295   -58.547 1.00 43.87  ? 1195 HOH   B O    1 
HETATM 26064 O O    . HOH   GA 7 .   ? 71.475 -6.518  -17.068 1.00 36.76  ? 1196 HOH   B O    1 
HETATM 26065 O O    . HOH   GA 7 .   ? 41.470 -3.603  -14.585 1.00 23.18  ? 1197 HOH   B O    1 
HETATM 26066 O O    . HOH   GA 7 .   ? 46.504 0.370   -31.643 1.00 32.45  ? 1198 HOH   B O    1 
HETATM 26067 O O    . HOH   GA 7 .   ? 61.584 -0.044  -53.539 1.00 42.33  ? 1199 HOH   B O    1 
HETATM 26068 O O    . HOH   GA 7 .   ? 68.166 -22.447 -58.799 1.00 33.34  ? 1200 HOH   B O    1 
HETATM 26069 O O    . HOH   GA 7 .   ? 91.939 -10.972 -49.560 1.00 28.06  ? 1201 HOH   B O    1 
HETATM 26070 O O    . HOH   GA 7 .   ? 81.512 -13.475 -51.915 1.00 25.85  ? 1202 HOH   B O    1 
HETATM 26071 O O    . HOH   GA 7 .   ? 51.898 -20.929 -47.657 1.00 43.17  ? 1203 HOH   B O    1 
HETATM 26072 O O    . HOH   GA 7 .   ? 79.651 18.880  -75.244 1.00 25.73  ? 1204 HOH   B O    1 
HETATM 26073 O O    . HOH   GA 7 .   ? 56.630 -9.515  -7.661  1.00 46.65  ? 1205 HOH   B O    1 
HETATM 26074 O O    . HOH   GA 7 .   ? 71.307 1.986   -54.158 1.00 33.08  ? 1206 HOH   B O    1 
HETATM 26075 O O    . HOH   GA 7 .   ? 39.282 -6.752  -17.349 1.00 17.58  ? 1207 HOH   B O    1 
HETATM 26076 O O    . HOH   GA 7 .   ? 44.676 -16.512 -28.818 1.00 27.12  ? 1208 HOH   B O    1 
HETATM 26077 O O    . HOH   GA 7 .   ? 59.588 28.513  -11.095 1.00 47.92  ? 1209 HOH   B O    1 
HETATM 26078 O O    . HOH   GA 7 .   ? 67.121 11.714  -60.170 1.00 29.95  ? 1210 HOH   B O    1 
HETATM 26079 O O    . HOH   GA 7 .   ? 71.888 31.211  -70.789 1.00 33.11  ? 1211 HOH   B O    1 
HETATM 26080 O O    . HOH   GA 7 .   ? 84.381 -3.398  -71.257 1.00 28.28  ? 1212 HOH   B O    1 
HETATM 26081 O O    . HOH   GA 7 .   ? 84.977 -15.996 -63.635 1.00 46.90  ? 1213 HOH   B O    1 
HETATM 26082 O O    . HOH   GA 7 .   ? 90.545 -0.287  -76.155 1.00 54.89  ? 1214 HOH   B O    1 
HETATM 26083 O O    . HOH   GA 7 .   ? 70.571 43.178  -62.076 1.00 53.70  ? 1215 HOH   B O    1 
HETATM 26084 O O    . HOH   GA 7 .   ? 45.483 6.154   -26.057 1.00 22.80  ? 1216 HOH   B O    1 
HETATM 26085 O O    . HOH   GA 7 .   ? 66.923 31.991  -65.901 1.00 36.92  ? 1217 HOH   B O    1 
HETATM 26086 O O    . HOH   GA 7 .   ? 66.884 16.403  -78.053 1.00 36.58  ? 1218 HOH   B O    1 
HETATM 26087 O O    . HOH   GA 7 .   ? 54.740 -3.552  -39.998 1.00 24.73  ? 1219 HOH   B O    1 
HETATM 26088 O O    . HOH   GA 7 .   ? 47.388 -17.975 -18.389 1.00 38.06  ? 1220 HOH   B O    1 
HETATM 26089 O O    . HOH   GA 7 .   ? 65.921 28.346  -37.620 1.00 49.97  ? 1221 HOH   B O    1 
HETATM 26090 O O    . HOH   GA 7 .   ? 69.521 20.968  -22.117 1.00 40.20  ? 1222 HOH   B O    1 
HETATM 26091 O O    . HOH   GA 7 .   ? 54.272 -23.361 -30.607 1.00 44.91  ? 1223 HOH   B O    1 
HETATM 26092 O O    . HOH   GA 7 .   ? 90.452 10.885  -73.290 1.00 42.62  ? 1224 HOH   B O    1 
HETATM 26093 O O    . HOH   GA 7 .   ? 39.151 -13.872 -30.730 1.00 27.31  ? 1225 HOH   B O    1 
HETATM 26094 O O    . HOH   GA 7 .   ? 54.135 34.416  -32.303 1.00 28.96  ? 1226 HOH   B O    1 
HETATM 26095 O O    . HOH   GA 7 .   ? 72.738 -8.221  -39.553 1.00 24.35  ? 1227 HOH   B O    1 
HETATM 26096 O O    . HOH   GA 7 .   ? 74.831 -10.427 -25.438 1.00 48.01  ? 1228 HOH   B O    1 
HETATM 26097 O O    . HOH   GA 7 .   ? 72.545 -14.199 -31.173 1.00 27.22  ? 1229 HOH   B O    1 
HETATM 26098 O O    . HOH   GA 7 .   ? 63.574 -10.326 -60.239 1.00 19.96  ? 1230 HOH   B O    1 
HETATM 26099 O O    . HOH   GA 7 .   ? 92.602 -0.096  -64.086 1.00 29.73  ? 1231 HOH   B O    1 
HETATM 26100 O O    . HOH   GA 7 .   ? 69.459 -17.410 -31.753 1.00 25.80  ? 1232 HOH   B O    1 
HETATM 26101 O O    . HOH   GA 7 .   ? 51.283 -12.946 -46.773 1.00 26.96  ? 1233 HOH   B O    1 
HETATM 26102 O O    . HOH   GA 7 .   ? 65.606 43.446  -28.794 1.00 37.55  ? 1234 HOH   B O    1 
HETATM 26103 O O    . HOH   GA 7 .   ? 70.168 6.979   -79.465 1.00 34.05  ? 1235 HOH   B O    1 
HETATM 26104 O O    . HOH   GA 7 .   ? 75.574 11.340  -80.213 1.00 38.81  ? 1236 HOH   B O    1 
HETATM 26105 O O    . HOH   GA 7 .   ? 63.794 9.724   -57.978 1.00 36.30  ? 1237 HOH   B O    1 
HETATM 26106 O O    . HOH   GA 7 .   ? 44.196 -15.895 -16.536 1.00 39.93  ? 1238 HOH   B O    1 
HETATM 26107 O O    . HOH   GA 7 .   ? 53.167 -6.797  -8.115  1.00 45.06  ? 1239 HOH   B O    1 
HETATM 26108 O O    . HOH   GA 7 .   ? 66.130 34.504  -35.690 1.00 44.01  ? 1240 HOH   B O    1 
HETATM 26109 O O    . HOH   GA 7 .   ? 63.620 -8.584  -13.135 1.00 30.74  ? 1241 HOH   B O    1 
HETATM 26110 O O    . HOH   GA 7 .   ? 75.327 -13.281 -70.778 1.00 31.18  ? 1242 HOH   B O    1 
HETATM 26111 O O    . HOH   GA 7 .   ? 71.991 -10.098 -24.081 1.00 31.52  ? 1243 HOH   B O    1 
HETATM 26112 O O    . HOH   GA 7 .   ? 68.590 2.251   -59.804 1.00 21.01  ? 1244 HOH   B O    1 
HETATM 26113 O O    . HOH   GA 7 .   ? 57.010 15.175  -71.545 1.00 34.25  ? 1245 HOH   B O    1 
HETATM 26114 O O    . HOH   GA 7 .   ? 83.744 -7.027  -61.493 1.00 26.27  ? 1246 HOH   B O    1 
HETATM 26115 O O    . HOH   GA 7 .   ? 85.367 -15.953 -60.962 1.00 40.29  ? 1247 HOH   B O    1 
HETATM 26116 O O    . HOH   GA 7 .   ? 81.705 -19.953 -55.369 1.00 33.03  ? 1248 HOH   B O    1 
HETATM 26117 O O    . HOH   GA 7 .   ? 85.592 13.245  -57.563 1.00 43.85  ? 1249 HOH   B O    1 
HETATM 26118 O O    . HOH   GA 7 .   ? 82.949 -22.054 -59.686 1.00 50.21  ? 1250 HOH   B O    1 
HETATM 26119 O O    . HOH   GA 7 .   ? 74.281 -13.648 -34.654 1.00 25.25  ? 1251 HOH   B O    1 
HETATM 26120 O O    . HOH   GA 7 .   ? 74.775 35.869  -62.451 1.00 30.29  ? 1252 HOH   B O    1 
HETATM 26121 O O    . HOH   GA 7 .   ? 41.458 -7.434  -13.716 1.00 22.47  ? 1253 HOH   B O    1 
HETATM 26122 O O    . HOH   GA 7 .   ? 59.682 -3.278  -72.823 1.00 23.16  ? 1254 HOH   B O    1 
HETATM 26123 O O    . HOH   GA 7 .   ? 58.812 23.216  -63.594 1.00 31.44  ? 1255 HOH   B O    1 
HETATM 26124 O O    . HOH   GA 7 .   ? 79.495 -22.818 -47.016 1.00 61.25  ? 1256 HOH   B O    1 
HETATM 26125 O O    . HOH   GA 7 .   ? 75.296 18.410  -78.506 1.00 26.79  ? 1257 HOH   B O    1 
HETATM 26126 O O    . HOH   GA 7 .   ? 83.856 -8.945  -51.283 1.00 26.73  ? 1258 HOH   B O    1 
HETATM 26127 O O    . HOH   GA 7 .   ? 71.337 -6.970  -75.404 1.00 35.43  ? 1259 HOH   B O    1 
HETATM 26128 O O    . HOH   GA 7 .   ? 70.745 12.732  -14.443 1.00 36.94  ? 1260 HOH   B O    1 
HETATM 26129 O O    . HOH   GA 7 .   ? 56.564 -4.789  -64.707 1.00 31.07  ? 1261 HOH   B O    1 
HETATM 26130 O O    . HOH   GA 7 .   ? 45.070 -10.954 -23.913 1.00 20.70  ? 1262 HOH   B O    1 
HETATM 26131 O O    . HOH   GA 7 .   ? 51.140 0.652   -37.493 1.00 40.57  ? 1263 HOH   B O    1 
HETATM 26132 O O    . HOH   GA 7 .   ? 67.561 20.177  -25.024 1.00 36.63  ? 1264 HOH   B O    1 
HETATM 26133 O O    . HOH   GA 7 .   ? 57.301 -21.241 -42.737 1.00 29.19  ? 1265 HOH   B O    1 
HETATM 26134 O O    . HOH   GA 7 .   ? 58.498 -4.835  -47.064 1.00 23.70  ? 1266 HOH   B O    1 
HETATM 26135 O O    . HOH   GA 7 .   ? 88.692 7.389   -62.380 1.00 26.88  ? 1267 HOH   B O    1 
HETATM 26136 O O    . HOH   GA 7 .   ? 89.064 -3.362  -58.127 1.00 31.80  ? 1268 HOH   B O    1 
HETATM 26137 O O    . HOH   GA 7 .   ? 61.771 -5.203  -9.672  1.00 31.98  ? 1269 HOH   B O    1 
HETATM 26138 O O    . HOH   GA 7 .   ? 70.638 6.957   -9.701  1.00 50.80  ? 1270 HOH   B O    1 
HETATM 26139 O O    . HOH   GA 7 .   ? 49.113 29.262  -29.319 1.00 43.01  ? 1271 HOH   B O    1 
HETATM 26140 O O    . HOH   GA 7 .   ? 87.369 -1.685  -81.192 1.00 50.51  ? 1272 HOH   B O    1 
HETATM 26141 O O    . HOH   GA 7 .   ? 54.516 3.506   -10.989 1.00 24.92  ? 1273 HOH   B O    1 
HETATM 26142 O O    . HOH   GA 7 .   ? 61.291 -19.644 -40.032 1.00 45.88  ? 1274 HOH   B O    1 
HETATM 26143 O O    . HOH   GA 7 .   ? 63.361 40.111  -47.050 1.00 34.92  ? 1275 HOH   B O    1 
HETATM 26144 O O    . HOH   GA 7 .   ? 56.293 3.552   -30.683 1.00 37.82  ? 1276 HOH   B O    1 
HETATM 26145 O O    . HOH   GA 7 .   ? 70.038 20.922  -53.719 1.00 38.31  ? 1277 HOH   B O    1 
HETATM 26146 O O    . HOH   GA 7 .   ? 50.092 -8.852  -15.833 1.00 28.10  ? 1278 HOH   B O    1 
HETATM 26147 O O    . HOH   GA 7 .   ? 62.078 -12.119 -67.421 1.00 20.25  ? 1279 HOH   B O    1 
HETATM 26148 O O    . HOH   GA 7 .   ? 54.755 -11.037 -52.119 1.00 20.38  ? 1280 HOH   B O    1 
HETATM 26149 O O    . HOH   GA 7 .   ? 63.615 7.230   -71.725 1.00 26.38  ? 1281 HOH   B O    1 
HETATM 26150 O O    . HOH   GA 7 .   ? 66.641 0.278   -79.027 1.00 32.23  ? 1282 HOH   B O    1 
HETATM 26151 O O    . HOH   GA 7 .   ? 66.631 42.710  -51.790 1.00 43.48  ? 1283 HOH   B O    1 
HETATM 26152 O O    . HOH   GA 7 .   ? 39.269 7.072   -16.353 1.00 38.99  ? 1284 HOH   B O    1 
HETATM 26153 O O    . HOH   GA 7 .   ? 63.834 9.955   -4.603  1.00 43.17  ? 1285 HOH   B O    1 
HETATM 26154 O O    . HOH   GA 7 .   ? 76.223 -13.259 -27.473 1.00 40.02  ? 1286 HOH   B O    1 
HETATM 26155 O O    . HOH   GA 7 .   ? 65.527 26.714  -72.337 1.00 32.39  ? 1287 HOH   B O    1 
HETATM 26156 O O    . HOH   GA 7 .   ? 75.184 -18.917 -36.788 1.00 34.87  ? 1288 HOH   B O    1 
HETATM 26157 O O    . HOH   GA 7 .   ? 71.215 0.681   -21.950 1.00 44.41  ? 1289 HOH   B O    1 
HETATM 26158 O O    . HOH   GA 7 .   ? 50.430 9.117   -69.851 1.00 47.73  ? 1290 HOH   B O    1 
HETATM 26159 O O    . HOH   GA 7 .   ? 46.245 11.601  -25.493 1.00 18.20  ? 1291 HOH   B O    1 
HETATM 26160 O O    . HOH   GA 7 .   ? 65.523 0.134   -41.925 1.00 29.68  ? 1292 HOH   B O    1 
HETATM 26161 O O    . HOH   GA 7 .   ? 75.945 17.868  -81.116 1.00 34.54  ? 1293 HOH   B O    1 
HETATM 26162 O O    . HOH   GA 7 .   ? 71.598 24.659  -48.297 1.00 44.98  ? 1294 HOH   B O    1 
HETATM 26163 O O    . HOH   GA 7 .   ? 34.602 -7.957  -22.924 1.00 19.45  ? 1295 HOH   B O    1 
HETATM 26164 O O    . HOH   GA 7 .   ? 44.474 6.105   -9.360  1.00 29.24  ? 1296 HOH   B O    1 
HETATM 26165 O O    . HOH   GA 7 .   ? 62.482 -26.436 -33.835 1.00 61.88  ? 1297 HOH   B O    1 
HETATM 26166 O O    . HOH   GA 7 .   ? 86.979 -5.823  -50.352 1.00 51.18  ? 1298 HOH   B O    1 
HETATM 26167 O O    . HOH   GA 7 .   ? 72.356 24.460  -80.539 1.00 46.17  ? 1299 HOH   B O    1 
HETATM 26168 O O    . HOH   GA 7 .   ? 67.669 -23.170 -35.260 1.00 48.89  ? 1300 HOH   B O    1 
HETATM 26169 O O    . HOH   GA 7 .   ? 45.308 -16.541 -50.158 1.00 42.53  ? 1301 HOH   B O    1 
HETATM 26170 O O    . HOH   GA 7 .   ? 59.249 5.931   -6.629  1.00 42.61  ? 1302 HOH   B O    1 
HETATM 26171 O O    . HOH   GA 7 .   ? 71.256 2.382   -46.358 1.00 47.71  ? 1303 HOH   B O    1 
HETATM 26172 O O    . HOH   GA 7 .   ? 83.495 34.737  -59.637 1.00 36.98  ? 1304 HOH   B O    1 
HETATM 26173 O O    . HOH   GA 7 .   ? 47.395 20.787  -26.742 1.00 44.69  ? 1305 HOH   B O    1 
HETATM 26174 O O    . HOH   GA 7 .   ? 75.570 30.051  -77.128 1.00 41.44  ? 1306 HOH   B O    1 
HETATM 26175 O O    . HOH   GA 7 .   ? 67.719 27.094  -43.373 1.00 38.37  ? 1307 HOH   B O    1 
HETATM 26176 O O    . HOH   GA 7 .   ? 57.308 11.144  -26.461 1.00 34.41  ? 1308 HOH   B O    1 
HETATM 26177 O O    . HOH   GA 7 .   ? 82.237 13.171  -79.361 1.00 36.35  ? 1309 HOH   B O    1 
HETATM 26178 O O    . HOH   GA 7 .   ? 53.448 13.162  -72.779 1.00 32.73  ? 1310 HOH   B O    1 
HETATM 26179 O O    . HOH   GA 7 .   ? 66.015 -3.792  -55.296 1.00 45.37  ? 1311 HOH   B O    1 
HETATM 26180 O O    . HOH   GA 7 .   ? 63.293 5.355   -73.922 1.00 28.83  ? 1312 HOH   B O    1 
HETATM 26181 O O    . HOH   GA 7 .   ? 78.513 -17.889 -40.094 1.00 41.70  ? 1313 HOH   B O    1 
HETATM 26182 O O    . HOH   GA 7 .   ? 58.649 13.152  -53.099 1.00 47.84  ? 1314 HOH   B O    1 
HETATM 26183 O O    . HOH   GA 7 .   ? 77.788 19.159  -55.510 1.00 42.72  ? 1315 HOH   B O    1 
HETATM 26184 O O    . HOH   GA 7 .   ? 60.485 19.711  -78.814 1.00 44.07  ? 1316 HOH   B O    1 
HETATM 26185 O O    . HOH   GA 7 .   ? 60.528 6.788   -76.730 1.00 37.41  ? 1317 HOH   B O    1 
HETATM 26186 O O    . HOH   GA 7 .   ? 48.604 -3.340  -37.446 1.00 47.58  ? 1318 HOH   B O    1 
HETATM 26187 O O    . HOH   GA 7 .   ? 79.068 -19.996 -68.904 1.00 60.21  ? 1319 HOH   B O    1 
HETATM 26188 O O    . HOH   GA 7 .   ? 50.116 -17.628 -47.566 1.00 46.11  ? 1320 HOH   B O    1 
HETATM 26189 O O    . HOH   GA 7 .   ? 48.534 17.320  -28.448 1.00 37.92  ? 1321 HOH   B O    1 
HETATM 26190 O O    . HOH   GA 7 .   ? 56.558 -14.744 -15.241 1.00 40.39  ? 1322 HOH   B O    1 
HETATM 26191 O O    . HOH   GA 7 .   ? 73.379 7.788   -78.318 1.00 34.01  ? 1323 HOH   B O    1 
HETATM 26192 O O    . HOH   GA 7 .   ? 41.504 18.025  -20.182 1.00 41.16  ? 1324 HOH   B O    1 
HETATM 26193 O O    . HOH   GA 7 .   ? 52.357 -7.856  -15.005 1.00 35.20  ? 1325 HOH   B O    1 
HETATM 26194 O O    . HOH   GA 7 .   ? 38.507 7.361   -19.119 1.00 36.17  ? 1326 HOH   B O    1 
HETATM 26195 O O    . HOH   GA 7 .   ? 65.144 23.480  -77.085 1.00 35.10  ? 1327 HOH   B O    1 
HETATM 26196 O O    . HOH   GA 7 .   ? 90.684 -4.756  -60.468 1.00 64.50  ? 1328 HOH   B O    1 
HETATM 26197 O O    . HOH   GA 7 .   ? 40.881 16.359  -14.147 1.00 57.42  ? 1329 HOH   B O    1 
HETATM 26198 O O    . HOH   GA 7 .   ? 57.452 -1.974  -71.858 1.00 26.11  ? 1330 HOH   B O    1 
HETATM 26199 O O    . HOH   GA 7 .   ? 57.919 -14.774 -63.190 1.00 23.52  ? 1331 HOH   B O    1 
HETATM 26200 O O    . HOH   GA 7 .   ? 61.095 9.738   -54.013 1.00 38.42  ? 1332 HOH   B O    1 
HETATM 26201 O O    . HOH   GA 7 .   ? 61.123 13.520  -71.648 1.00 39.33  ? 1333 HOH   B O    1 
HETATM 26202 O O    . HOH   GA 7 .   ? 82.159 -13.296 -44.545 1.00 51.07  ? 1334 HOH   B O    1 
HETATM 26203 O O    . HOH   GA 7 .   ? 69.755 2.386   -16.031 1.00 31.18  ? 1335 HOH   B O    1 
HETATM 26204 O O    . HOH   GA 7 .   ? 71.379 -5.048  -19.393 1.00 51.92  ? 1336 HOH   B O    1 
HETATM 26205 O O    . HOH   GA 7 .   ? 64.503 9.459   -79.133 1.00 45.88  ? 1337 HOH   B O    1 
HETATM 26206 O O    . HOH   GA 7 .   ? 88.231 30.584  -58.693 1.00 48.65  ? 1338 HOH   B O    1 
HETATM 26207 O O    . HOH   GA 7 .   ? 51.248 15.979  -11.663 1.00 34.56  ? 1339 HOH   B O    1 
HETATM 26208 O O    . HOH   GA 7 .   ? 66.692 -29.098 -52.128 1.00 43.33  ? 1340 HOH   B O    1 
HETATM 26209 O O    . HOH   GA 7 .   ? 50.565 -1.534  -67.338 1.00 31.24  ? 1341 HOH   B O    1 
HETATM 26210 O O    . HOH   GA 7 .   ? 57.087 38.119  -39.373 1.00 43.11  ? 1342 HOH   B O    1 
HETATM 26211 O O    . HOH   GA 7 .   ? 70.666 18.272  -78.653 1.00 31.38  ? 1343 HOH   B O    1 
HETATM 26212 O O    . HOH   GA 7 .   ? 73.009 -3.533  -51.034 1.00 23.94  ? 1344 HOH   B O    1 
HETATM 26213 O O    . HOH   GA 7 .   ? 56.359 29.962  -42.592 1.00 44.43  ? 1345 HOH   B O    1 
HETATM 26214 O O    . HOH   GA 7 .   ? 84.984 8.962   -59.218 1.00 36.36  ? 1346 HOH   B O    1 
HETATM 26215 O O    . HOH   GA 7 .   ? 72.181 -1.844  -11.830 1.00 47.41  ? 1347 HOH   B O    1 
HETATM 26216 O O    . HOH   GA 7 .   ? 38.562 8.855   -24.670 1.00 53.94  ? 1348 HOH   B O    1 
HETATM 26217 O O    . HOH   GA 7 .   ? 58.621 13.662  -59.698 1.00 38.24  ? 1349 HOH   B O    1 
HETATM 26218 O O    . HOH   GA 7 .   ? 84.078 2.941   -74.264 1.00 31.10  ? 1350 HOH   B O    1 
HETATM 26219 O O    . HOH   GA 7 .   ? 53.223 20.545  -67.779 1.00 37.01  ? 1351 HOH   B O    1 
HETATM 26220 O O    . HOH   GA 7 .   ? 87.776 -11.372 -56.696 1.00 36.41  ? 1352 HOH   B O    1 
HETATM 26221 O O    . HOH   GA 7 .   ? 65.088 33.836  -64.436 1.00 33.03  ? 1353 HOH   B O    1 
HETATM 26222 O O    . HOH   GA 7 .   ? 68.011 -7.430  -74.953 1.00 24.57  ? 1354 HOH   B O    1 
HETATM 26223 O O    . HOH   GA 7 .   ? 82.737 12.624  -75.921 1.00 35.20  ? 1355 HOH   B O    1 
HETATM 26224 O O    . HOH   GA 7 .   ? 59.285 29.027  -67.179 1.00 47.51  ? 1356 HOH   B O    1 
HETATM 26225 O O    . HOH   GA 7 .   ? 43.322 11.333  -16.369 1.00 34.50  ? 1357 HOH   B O    1 
HETATM 26226 O O    . HOH   GA 7 .   ? 69.652 16.362  -77.016 1.00 31.92  ? 1358 HOH   B O    1 
HETATM 26227 O O    . HOH   GA 7 .   ? 51.242 -13.918 -27.133 1.00 16.45  ? 1359 HOH   B O    1 
HETATM 26228 O O    . HOH   GA 7 .   ? 52.532 4.172   -67.464 1.00 35.99  ? 1360 HOH   B O    1 
HETATM 26229 O O    . HOH   GA 7 .   ? 60.618 8.767   -68.500 1.00 35.55  ? 1361 HOH   B O    1 
HETATM 26230 O O    . HOH   GA 7 .   ? 65.910 16.252  -4.974  1.00 51.99  ? 1362 HOH   B O    1 
HETATM 26231 O O    . HOH   GA 7 .   ? 58.228 -22.374 -45.185 1.00 30.58  ? 1363 HOH   B O    1 
HETATM 26232 O O    . HOH   GA 7 .   ? 82.011 -2.924  -74.464 1.00 26.10  ? 1364 HOH   B O    1 
HETATM 26233 O O    . HOH   GA 7 .   ? 88.577 16.821  -71.985 1.00 30.25  ? 1365 HOH   B O    1 
HETATM 26234 O O    . HOH   GA 7 .   ? 62.120 -25.076 -43.225 1.00 45.89  ? 1366 HOH   B O    1 
HETATM 26235 O O    . HOH   GA 7 .   ? 46.999 10.229  -5.269  1.00 37.55  ? 1367 HOH   B O    1 
HETATM 26236 O O    . HOH   GA 7 .   ? 72.558 42.096  -49.678 1.00 58.04  ? 1368 HOH   B O    1 
HETATM 26237 O O    . HOH   GA 7 .   ? 35.580 -4.672  -23.751 1.00 23.51  ? 1369 HOH   B O    1 
HETATM 26238 O O    . HOH   GA 7 .   ? 72.982 -23.802 -63.917 1.00 36.20  ? 1370 HOH   B O    1 
HETATM 26239 O O    . HOH   GA 7 .   ? 68.306 12.863  -20.085 1.00 52.71  ? 1371 HOH   B O    1 
HETATM 26240 O O    . HOH   GA 7 .   ? 60.999 -0.634  -74.191 1.00 21.16  ? 1372 HOH   B O    1 
HETATM 26241 O O    . HOH   GA 7 .   ? 52.282 -19.642 -63.927 1.00 37.83  ? 1373 HOH   B O    1 
HETATM 26242 O O    . HOH   GA 7 .   ? 84.257 -20.022 -58.513 1.00 38.05  ? 1374 HOH   B O    1 
HETATM 26243 O O    . HOH   GA 7 .   ? 74.595 22.507  -81.918 1.00 42.62  ? 1375 HOH   B O    1 
HETATM 26244 O O    . HOH   GA 7 .   ? 87.260 -0.082  -56.775 1.00 36.18  ? 1376 HOH   B O    1 
HETATM 26245 O O    . HOH   GA 7 .   ? 67.415 -3.692  -79.256 1.00 33.86  ? 1377 HOH   B O    1 
HETATM 26246 O O    . HOH   GA 7 .   ? 43.884 46.927  -32.941 1.00 37.48  ? 1378 HOH   B O    1 
HETATM 26247 O O    . HOH   GA 7 .   ? 56.254 -9.464  -13.537 1.00 42.65  ? 1379 HOH   B O    1 
HETATM 26248 O O    . HOH   GA 7 .   ? 51.077 36.372  -32.944 1.00 34.12  ? 1380 HOH   B O    1 
HETATM 26249 O O    . HOH   GA 7 .   ? 53.271 9.069   -71.487 1.00 34.22  ? 1381 HOH   B O    1 
HETATM 26250 O O    . HOH   GA 7 .   ? 49.350 15.623  -13.773 1.00 29.73  ? 1382 HOH   B O    1 
HETATM 26251 O O    . HOH   GA 7 .   ? 35.531 5.370   -12.093 1.00 32.15  ? 1383 HOH   B O    1 
HETATM 26252 O O    . HOH   GA 7 .   ? 76.834 -5.300  -81.070 1.00 35.66  ? 1384 HOH   B O    1 
HETATM 26253 O O    . HOH   GA 7 .   ? 55.616 7.204   -54.983 1.00 42.44  ? 1385 HOH   B O    1 
HETATM 26254 O O    . HOH   GA 7 .   ? 68.607 17.494  -21.216 1.00 46.74  ? 1386 HOH   B O    1 
HETATM 26255 O O    . HOH   GA 7 .   ? 64.770 16.884  -7.493  1.00 61.64  ? 1387 HOH   B O    1 
HETATM 26256 O O    . HOH   GA 7 .   ? 55.977 -26.407 -36.735 1.00 44.47  ? 1388 HOH   B O    1 
HETATM 26257 O O    . HOH   GA 7 .   ? 69.344 33.510  -69.659 1.00 44.30  ? 1389 HOH   B O    1 
HETATM 26258 O O    . HOH   GA 7 .   ? 72.193 15.116  -76.431 1.00 28.85  ? 1390 HOH   B O    1 
HETATM 26259 O O    . HOH   GA 7 .   ? 83.004 35.739  -63.543 1.00 39.09  ? 1391 HOH   B O    1 
HETATM 26260 O O    . HOH   GA 7 .   ? 49.867 -21.308 -25.469 1.00 59.02  ? 1392 HOH   B O    1 
HETATM 26261 O O    . HOH   GA 7 .   ? 46.724 4.140   -30.059 1.00 50.99  ? 1393 HOH   B O    1 
HETATM 26262 O O    . HOH   GA 7 .   ? 64.345 -15.084 -19.241 1.00 51.86  ? 1394 HOH   B O    1 
HETATM 26263 O O    . HOH   GA 7 .   ? 57.163 -9.437  -67.800 1.00 24.92  ? 1395 HOH   B O    1 
HETATM 26264 O O    . HOH   GA 7 .   ? 47.266 13.955  -2.728  1.00 41.31  ? 1396 HOH   B O    1 
HETATM 26265 O O    . HOH   GA 7 .   ? 56.938 -24.243 -62.393 1.00 32.56  ? 1397 HOH   B O    1 
HETATM 26266 O O    . HOH   GA 7 .   ? 97.056 14.185  -64.917 1.00 35.33  ? 1398 HOH   B O    1 
HETATM 26267 O O    . HOH   GA 7 .   ? 49.615 -6.981  -8.739  1.00 38.83  ? 1399 HOH   B O    1 
HETATM 26268 O O    . HOH   GA 7 .   ? 46.853 -9.312  -24.951 1.00 24.03  ? 1400 HOH   B O    1 
HETATM 26269 O O    . HOH   GA 7 .   ? 65.244 5.754   -27.660 1.00 47.50  ? 1401 HOH   B O    1 
HETATM 26270 O O    . HOH   GA 7 .   ? 61.823 39.574  -54.961 1.00 41.87  ? 1402 HOH   B O    1 
HETATM 26271 O O    . HOH   GA 7 .   ? 83.723 -20.420 -49.030 1.00 45.71  ? 1403 HOH   B O    1 
HETATM 26272 O O    . HOH   GA 7 .   ? 37.073 4.226   -23.668 1.00 47.62  ? 1404 HOH   B O    1 
HETATM 26273 O O    . HOH   GA 7 .   ? 76.342 -6.637  -48.068 1.00 46.63  ? 1405 HOH   B O    1 
HETATM 26274 O O    . HOH   GA 7 .   ? 67.457 -25.746 -34.805 1.00 53.13  ? 1406 HOH   B O    1 
HETATM 26275 O O    . HOH   GA 7 .   ? 86.491 -2.721  -57.435 1.00 32.55  ? 1407 HOH   B O    1 
HETATM 26276 O O    . HOH   GA 7 .   ? 70.074 -21.224 -33.851 1.00 37.28  ? 1408 HOH   B O    1 
HETATM 26277 O O    . HOH   GA 7 .   ? 55.803 22.331  -75.696 1.00 67.87  ? 1409 HOH   B O    1 
HETATM 26278 O O    . HOH   GA 7 .   ? 59.839 -23.982 -61.479 1.00 30.90  ? 1410 HOH   B O    1 
HETATM 26279 O O    . HOH   GA 7 .   ? 60.757 5.475   -56.404 1.00 34.38  ? 1411 HOH   B O    1 
HETATM 26280 O O    . HOH   GA 7 .   ? 69.571 35.605  -66.967 1.00 35.47  ? 1412 HOH   B O    1 
HETATM 26281 O O    . HOH   GA 7 .   ? 66.898 22.985  -50.539 1.00 28.40  ? 1413 HOH   B O    1 
HETATM 26282 O O    . HOH   GA 7 .   ? 75.135 -18.379 -43.357 1.00 39.06  ? 1414 HOH   B O    1 
HETATM 26283 O O    . HOH   GA 7 .   ? 68.237 -19.686 -70.137 1.00 43.43  ? 1415 HOH   B O    1 
HETATM 26284 O O    . HOH   GA 7 .   ? 40.172 9.994   -12.969 1.00 37.37  ? 1416 HOH   B O    1 
HETATM 26285 O O    . HOH   GA 7 .   ? 61.545 4.395   -7.043  1.00 32.95  ? 1417 HOH   B O    1 
HETATM 26286 O O    . HOH   GA 7 .   ? 65.850 -1.675  -51.347 1.00 60.29  ? 1418 HOH   B O    1 
HETATM 26287 O O    . HOH   GA 7 .   ? 69.997 37.756  -41.029 1.00 43.13  ? 1419 HOH   B O    1 
HETATM 26288 O O    . HOH   GA 7 .   ? 53.391 -24.202 -54.108 1.00 37.30  ? 1420 HOH   B O    1 
HETATM 26289 O O    . HOH   GA 7 .   ? 66.030 5.139   -35.762 1.00 44.50  ? 1421 HOH   B O    1 
HETATM 26290 O O    . HOH   GA 7 .   ? 58.014 21.505  -79.207 1.00 71.05  ? 1422 HOH   B O    1 
HETATM 26291 O O    . HOH   GA 7 .   ? 64.574 4.873   -48.691 1.00 41.47  ? 1423 HOH   B O    1 
HETATM 26292 O O    . HOH   GA 7 .   ? 45.805 12.525  -6.126  1.00 46.43  ? 1424 HOH   B O    1 
HETATM 26293 O O    . HOH   GA 7 .   ? 50.393 -0.651  -5.386  1.00 51.65  ? 1425 HOH   B O    1 
HETATM 26294 O O    . HOH   GA 7 .   ? 75.583 -7.028  -43.062 1.00 43.00  ? 1426 HOH   B O    1 
HETATM 26295 O O    . HOH   GA 7 .   ? 56.413 9.414   -70.339 1.00 45.53  ? 1427 HOH   B O    1 
HETATM 26296 O O    . HOH   GA 7 .   ? 79.214 33.542  -67.449 1.00 34.14  ? 1428 HOH   B O    1 
HETATM 26297 O O    . HOH   GA 7 .   ? 44.836 -17.250 -18.447 1.00 58.48  ? 1429 HOH   B O    1 
HETATM 26298 O O    . HOH   GA 7 .   ? 85.886 16.428  -76.810 1.00 104.32 ? 1430 HOH   B O    1 
HETATM 26299 O O    . HOH   GA 7 .   ? 72.327 41.355  -47.085 1.00 56.31  ? 1431 HOH   B O    1 
HETATM 26300 O O    . HOH   GA 7 .   ? 63.419 -4.153  -50.013 1.00 49.32  ? 1432 HOH   B O    1 
HETATM 26301 O O    . HOH   GA 7 .   ? 47.601 -19.957 -29.195 1.00 33.50  ? 1433 HOH   B O    1 
HETATM 26302 O O    . HOH   GA 7 .   ? 69.186 -8.118  -14.179 1.00 33.84  ? 1434 HOH   B O    1 
HETATM 26303 O O    . HOH   GA 7 .   ? 36.985 6.926   -23.492 1.00 49.44  ? 1435 HOH   B O    1 
HETATM 26304 O O    . HOH   GA 7 .   ? 60.475 10.882  -69.157 1.00 32.50  ? 1436 HOH   B O    1 
HETATM 26305 O O    . HOH   GA 7 .   ? 47.107 -15.412 -45.837 1.00 37.74  ? 1437 HOH   B O    1 
HETATM 26306 O O    . HOH   GA 7 .   ? 70.349 -3.488  -43.910 1.00 41.36  ? 1438 HOH   B O    1 
HETATM 26307 O O    . HOH   GA 7 .   ? 55.785 -7.559  -15.244 1.00 28.55  ? 1439 HOH   B O    1 
HETATM 26308 O O    . HOH   GA 7 .   ? 43.672 9.461   -14.726 1.00 41.11  ? 1440 HOH   B O    1 
HETATM 26309 O O    . HOH   GA 7 .   ? 37.432 -5.066  -30.225 1.00 42.55  ? 1441 HOH   B O    1 
HETATM 26310 O O    . HOH   GA 7 .   ? 37.663 2.848   -11.567 1.00 51.02  ? 1442 HOH   B O    1 
HETATM 26311 O O    . HOH   GA 7 .   ? 57.600 -0.323  -59.144 1.00 25.49  ? 1443 HOH   B O    1 
HETATM 26312 O O    . HOH   GA 7 .   ? 92.560 15.274  -71.918 1.00 54.48  ? 1444 HOH   B O    1 
HETATM 26313 O O    . HOH   GA 7 .   ? 54.696 31.989  -38.281 1.00 39.47  ? 1445 HOH   B O    1 
HETATM 26314 O O    . HOH   GA 7 .   ? 51.827 -3.319  -5.454  1.00 41.59  ? 1446 HOH   B O    1 
HETATM 26315 O O    . HOH   GA 7 .   ? 49.170 -17.907 -50.364 1.00 47.47  ? 1447 HOH   B O    1 
HETATM 26316 O O    . HOH   GA 7 .   ? 45.953 7.791   -28.008 1.00 47.12  ? 1448 HOH   B O    1 
HETATM 26317 O O    . HOH   GA 7 .   ? 73.793 39.310  -38.420 1.00 45.91  ? 1449 HOH   B O    1 
HETATM 26318 O O    . HOH   GA 7 .   ? 63.457 -22.312 -66.128 1.00 63.63  ? 1450 HOH   B O    1 
HETATM 26319 O O    . HOH   GA 7 .   ? 77.484 -13.058 -74.402 1.00 43.83  ? 1451 HOH   B O    1 
HETATM 26320 O O    . HOH   GA 7 .   ? 45.843 14.847  -9.445  1.00 53.65  ? 1452 HOH   B O    1 
HETATM 26321 O O    . HOH   GA 7 .   ? 51.958 49.720  -31.128 1.00 42.15  ? 1453 HOH   B O    1 
HETATM 26322 O O    . HOH   GA 7 .   ? 70.820 33.868  -34.928 1.00 41.62  ? 1454 HOH   B O    1 
HETATM 26323 O O    . HOH   GA 7 .   ? 64.249 -26.609 -42.762 1.00 56.57  ? 1455 HOH   B O    1 
HETATM 26324 O O    . HOH   GA 7 .   ? 78.875 -6.470  -46.835 1.00 46.16  ? 1456 HOH   B O    1 
HETATM 26325 O O    . HOH   GA 7 .   ? 89.119 17.145  -69.308 1.00 27.85  ? 1457 HOH   B O    1 
HETATM 26326 O O    . HOH   GA 7 .   ? 46.182 35.318  -24.133 1.00 47.19  ? 1458 HOH   B O    1 
HETATM 26327 O O    . HOH   GA 7 .   ? 49.283 -16.778 -17.033 1.00 35.92  ? 1459 HOH   B O    1 
HETATM 26328 O O    . HOH   GA 7 .   ? 87.829 8.913   -59.448 1.00 46.39  ? 1460 HOH   B O    1 
HETATM 26329 O O    . HOH   GA 7 .   ? 42.458 -0.488  -30.992 1.00 51.51  ? 1461 HOH   B O    1 
HETATM 26330 O O    . HOH   GA 7 .   ? 56.924 -9.521  -72.202 1.00 49.20  ? 1462 HOH   B O    1 
HETATM 26331 O O    . HOH   GA 7 .   ? 64.879 6.248   -50.981 1.00 38.85  ? 1463 HOH   B O    1 
HETATM 26332 O O    . HOH   GA 7 .   ? 61.553 -1.674  -28.545 1.00 26.43  ? 1464 HOH   B O    1 
HETATM 26333 O O    . HOH   GA 7 .   ? 69.702 26.567  -81.171 1.00 47.47  ? 1465 HOH   B O    1 
HETATM 26334 O O    . HOH   GA 7 .   ? 71.685 4.984   -54.757 1.00 22.50  ? 1466 HOH   B O    1 
HETATM 26335 O O    . HOH   GA 7 .   ? 66.923 -3.454  -52.979 1.00 44.44  ? 1467 HOH   B O    1 
HETATM 26336 O O    . HOH   GA 7 .   ? 53.541 7.762   -31.534 1.00 50.73  ? 1468 HOH   B O    1 
HETATM 26337 O O    . HOH   GA 7 .   ? 64.347 1.228   -34.134 1.00 40.72  ? 1469 HOH   B O    1 
HETATM 26338 O O    . HOH   GA 7 .   ? 66.807 -7.544  -4.975  1.00 42.12  ? 1470 HOH   B O    1 
HETATM 26339 O O    . HOH   GA 7 .   ? 63.487 -16.138 -13.987 1.00 48.28  ? 1471 HOH   B O    1 
HETATM 26340 O O    . HOH   GA 7 .   ? 65.697 -5.428  -6.440  1.00 43.64  ? 1472 HOH   B O    1 
HETATM 26341 O O    . HOH   GA 7 .   ? 69.219 -0.908  -10.271 1.00 35.49  ? 1473 HOH   B O    1 
HETATM 26342 O O    . HOH   GA 7 .   ? 58.693 -2.705  -45.270 1.00 35.86  ? 1474 HOH   B O    1 
HETATM 26343 O O    . HOH   GA 7 .   ? 58.282 24.937  -53.958 1.00 60.22  ? 1475 HOH   B O    1 
HETATM 26344 O O    . HOH   GA 7 .   ? 79.564 36.097  -68.424 1.00 71.65  ? 1476 HOH   B O    1 
HETATM 26345 O O    . HOH   GA 7 .   ? 60.156 -5.771  -49.510 1.00 34.29  ? 1477 HOH   B O    1 
HETATM 26346 O O    . HOH   GA 7 .   ? 56.560 11.938  -29.391 1.00 44.71  ? 1478 HOH   B O    1 
HETATM 26347 O O    . HOH   GA 7 .   ? 61.853 10.183  -78.897 1.00 57.51  ? 1479 HOH   B O    1 
HETATM 26348 O O    . HOH   GA 7 .   ? 92.247 12.240  -71.837 1.00 46.35  ? 1480 HOH   B O    1 
HETATM 26349 O O    . HOH   GA 7 .   ? 75.037 39.887  -24.263 1.00 58.38  ? 1481 HOH   B O    1 
HETATM 26350 O O    . HOH   GA 7 .   ? 85.816 -7.246  -52.167 1.00 38.74  ? 1482 HOH   B O    1 
HETATM 26351 O O    . HOH   GA 7 .   ? 90.812 -3.177  -68.511 1.00 34.62  ? 1483 HOH   B O    1 
HETATM 26352 O O    . HOH   GA 7 .   ? 69.647 37.332  -69.180 1.00 53.83  ? 1484 HOH   B O    1 
HETATM 26353 O O    . HOH   GA 7 .   ? 52.647 23.118  -8.389  1.00 36.61  ? 1485 HOH   B O    1 
HETATM 26354 O O    . HOH   GA 7 .   ? 62.544 8.205   -55.867 1.00 41.61  ? 1486 HOH   B O    1 
HETATM 26355 O O    . HOH   GA 7 .   ? 61.840 -7.567  -10.993 1.00 47.12  ? 1487 HOH   B O    1 
HETATM 26356 O O    . HOH   GA 7 .   ? 72.651 45.769  -47.759 1.00 56.23  ? 1488 HOH   B O    1 
HETATM 26357 O O    . HOH   GA 7 .   ? 73.692 39.827  -35.815 1.00 48.62  ? 1489 HOH   B O    1 
HETATM 26358 O O    . HOH   GA 7 .   ? 54.734 29.360  -34.767 1.00 32.85  ? 1490 HOH   B O    1 
HETATM 26359 O O    . HOH   GA 7 .   ? 65.978 26.830  -78.631 1.00 44.05  ? 1491 HOH   B O    1 
HETATM 26360 O O    . HOH   GA 7 .   ? 73.880 -11.375 -22.560 1.00 41.70  ? 1492 HOH   B O    1 
HETATM 26361 O O    . HOH   GA 7 .   ? 91.720 -2.235  -70.949 1.00 36.90  ? 1493 HOH   B O    1 
HETATM 26362 O O    . HOH   GA 7 .   ? 59.533 -17.201 -64.390 1.00 52.54  ? 1494 HOH   B O    1 
HETATM 26363 O O    . HOH   GA 7 .   ? 63.146 -1.163  -41.332 1.00 32.48  ? 1495 HOH   B O    1 
HETATM 26364 O O    . HOH   GA 7 .   ? 75.335 -21.637 -68.145 1.00 50.11  ? 1496 HOH   B O    1 
HETATM 26365 O O    . HOH   GA 7 .   ? 61.064 -12.799 -69.932 1.00 47.15  ? 1497 HOH   B O    1 
HETATM 26366 O O    . HOH   GA 7 .   ? 93.502 0.675   -69.274 1.00 87.76  ? 1498 HOH   B O    1 
HETATM 26367 O O    . HOH   GA 7 .   ? 49.393 36.772  -34.999 1.00 55.50  ? 1499 HOH   B O    1 
HETATM 26368 O O    . HOH   GA 7 .   ? 87.190 32.429  -60.399 1.00 36.95  ? 1500 HOH   B O    1 
HETATM 26369 O O    . HOH   GA 7 .   ? 48.350 20.178  -9.139  1.00 42.61  ? 1501 HOH   B O    1 
HETATM 26370 O O    . HOH   GA 7 .   ? 76.573 -14.682 -35.586 1.00 33.70  ? 1502 HOH   B O    1 
HETATM 26371 O O    . HOH   GA 7 .   ? 52.107 -3.188  -40.500 1.00 41.74  ? 1503 HOH   B O    1 
HETATM 26372 O O    . HOH   GA 7 .   ? 72.872 20.340  -14.207 1.00 74.27  ? 1504 HOH   B O    1 
HETATM 26373 O O    . HOH   GA 7 .   ? 54.676 -3.956  -71.305 1.00 40.58  ? 1505 HOH   B O    1 
HETATM 26374 O O    . HOH   GA 7 .   ? 73.278 35.606  -21.640 1.00 52.40  ? 1506 HOH   B O    1 
HETATM 26375 O O    . HOH   GA 7 .   ? 58.785 -0.850  -56.829 1.00 24.22  ? 1507 HOH   B O    1 
HETATM 26376 O O    . HOH   GA 7 .   ? 76.687 10.899  -56.977 1.00 40.15  ? 1508 HOH   B O    1 
HETATM 26377 O O    . HOH   GA 7 .   ? 46.737 -15.433 -56.622 1.00 36.60  ? 1509 HOH   B O    1 
HETATM 26378 O O    . HOH   GA 7 .   ? 91.549 2.189   -78.418 1.00 54.91  ? 1510 HOH   B O    1 
HETATM 26379 O O    . HOH   GA 7 .   ? 65.923 6.546   -46.462 1.00 44.68  ? 1511 HOH   B O    1 
HETATM 26380 O O    . HOH   GA 7 .   ? 57.992 -1.731  -52.667 1.00 37.87  ? 1512 HOH   B O    1 
HETATM 26381 O O    . HOH   GA 7 .   ? 61.689 9.037   -71.075 1.00 45.02  ? 1513 HOH   B O    1 
HETATM 26382 O O    . HOH   GA 7 .   ? 45.435 -20.625 -25.780 1.00 37.33  ? 1514 HOH   B O    1 
HETATM 26383 O O    . HOH   GA 7 .   ? 48.203 -18.186 -46.103 1.00 39.85  ? 1515 HOH   B O    1 
HETATM 26384 O O    . HOH   GA 7 .   ? 72.694 -25.957 -58.900 1.00 45.11  ? 1516 HOH   B O    1 
HETATM 26385 O O    . HOH   GA 7 .   ? 74.351 -6.353  -40.690 1.00 31.87  ? 1517 HOH   B O    1 
HETATM 26386 O O    . HOH   GA 7 .   ? 55.823 -7.300  -68.476 1.00 28.81  ? 1518 HOH   B O    1 
HETATM 26387 O O    . HOH   GA 7 .   ? 49.655 -16.529 -14.474 1.00 44.16  ? 1519 HOH   B O    1 
HETATM 26388 O O    . HOH   GA 7 .   ? 49.890 -4.660  -40.471 1.00 39.50  ? 1520 HOH   B O    1 
HETATM 26389 O O    . HOH   GA 7 .   ? 53.013 0.246   -39.840 1.00 42.89  ? 1521 HOH   B O    1 
HETATM 26390 O O    . HOH   GA 7 .   ? 72.932 29.547  -79.912 1.00 62.25  ? 1522 HOH   B O    1 
HETATM 26391 O O    . HOH   GA 7 .   ? 54.568 -2.033  -47.116 1.00 36.32  ? 1523 HOH   B O    1 
HETATM 26392 O O    . HOH   GA 7 .   ? 61.659 7.666   -30.143 1.00 48.07  ? 1524 HOH   B O    1 
HETATM 26393 O O    . HOH   GA 7 .   ? 57.011 -0.918  -45.408 1.00 45.14  ? 1525 HOH   B O    1 
HETATM 26394 O O    . HOH   GA 7 .   ? 60.115 5.516   -28.989 1.00 22.78  ? 1526 HOH   B O    1 
HETATM 26395 O O    . HOH   GA 7 .   ? 58.809 1.709   -38.620 1.00 68.35  ? 1527 HOH   B O    1 
HETATM 26396 O O    . HOH   GA 7 .   ? 72.263 4.065   -32.961 1.00 62.30  ? 1528 HOH   B O    1 
HETATM 26397 O O    . HOH   GA 7 .   ? 69.642 5.924   -30.761 1.00 43.02  ? 1529 HOH   B O    1 
HETATM 26398 O O    . HOH   GA 7 .   ? 57.383 -2.527  -50.165 1.00 32.95  ? 1530 HOH   B O    1 
HETATM 26399 O O    . HOH   GA 7 .   ? 69.469 2.024   -29.932 1.00 45.06  ? 1531 HOH   B O    1 
HETATM 26400 O O    . HOH   GA 7 .   ? 44.696 -25.604 -25.536 1.00 58.28  ? 1532 HOH   B O    1 
HETATM 26401 O O    . HOH   GA 7 .   ? 74.613 4.464   -55.215 1.00 29.37  ? 1533 HOH   B O    1 
HETATM 26402 O O    . HOH   GA 7 .   ? 37.803 6.175   -31.593 1.00 56.99  ? 1534 HOH   B O    1 
HETATM 26403 O O    . HOH   GA 7 .   ? 63.963 8.756   -47.300 1.00 49.73  ? 1535 HOH   B O    1 
HETATM 26404 O O    . HOH   GA 7 .   ? 60.497 5.276   -33.124 1.00 32.07  ? 1536 HOH   B O    1 
HETATM 26405 O O    . HOH   GA 7 .   ? 73.985 7.000   -32.717 1.00 67.94  ? 1537 HOH   B O    1 
HETATM 26406 O O    . HOH   GA 7 .   ? 76.858 7.459   -49.396 1.00 61.75  ? 1538 HOH   B O    1 
HETATM 26407 O O    . HOH   GA 7 .   ? 69.747 17.325  -47.010 1.00 51.66  ? 1539 HOH   B O    1 
HETATM 26408 O O    . HOH   GA 7 .   ? 68.138 13.762  -33.248 1.00 64.40  ? 1540 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . ARG A  6   ? 0.5923 0.3582 0.5630 0.1483  0.0348  0.0433  32  ARG A N   
2     C CA  . ARG A  6   ? 0.5918 0.3716 0.5632 0.1377  0.0293  0.0408  32  ARG A CA  
3     C C   . ARG A  6   ? 0.5921 0.3742 0.5604 0.1329  0.0318  0.0321  32  ARG A C   
4     O O   . ARG A  6   ? 0.5995 0.3650 0.5575 0.1291  0.0355  0.0259  32  ARG A O   
5     C CB  . ARG A  6   ? 0.6084 0.3774 0.5713 0.1289  0.0264  0.0412  32  ARG A CB  
6     C CG  . ARG A  6   ? 0.6105 0.3960 0.5768 0.1205  0.0196  0.0424  32  ARG A CG  
7     C CD  . ARG A  6   ? 0.6224 0.3967 0.5806 0.1131  0.0173  0.0436  32  ARG A CD  
8     N NE  . ARG A  6   ? 0.6230 0.3977 0.5841 0.1173  0.0146  0.0522  32  ARG A NE  
9     C CZ  . ARG A  6   ? 0.6159 0.4078 0.5841 0.1161  0.0090  0.0575  32  ARG A CZ  
10    N NH1 . ARG A  6   ? 0.5954 0.4054 0.5690 0.1113  0.0057  0.0549  32  ARG A NH1 
11    N NH2 . ARG A  6   ? 0.5975 0.3884 0.5672 0.1200  0.0067  0.0653  32  ARG A NH2 
24    N N   . SER A  7   ? 0.5823 0.3846 0.5591 0.1330  0.0297  0.0316  33  SER A N   
25    C CA  . SER A  7   ? 0.5862 0.3925 0.5610 0.1292  0.0318  0.0242  33  SER A CA  
26    C C   . SER A  7   ? 0.5843 0.3845 0.5495 0.1176  0.0302  0.0182  33  SER A C   
27    O O   . SER A  7   ? 0.5826 0.3874 0.5477 0.1110  0.0252  0.0202  33  SER A O   
28    C CB  . SER A  7   ? 0.6023 0.4323 0.5881 0.1303  0.0290  0.0260  33  SER A CB  
29    O OG  . SER A  7   ? 0.6463 0.4806 0.6298 0.1264  0.0307  0.0193  33  SER A OG  
35    N N   . TYR A  8   ? 0.5797 0.3705 0.5371 0.1151  0.0344  0.0108  34  TYR A N   
36    C CA  . TYR A  8   ? 0.5843 0.3700 0.5326 0.1043  0.0332  0.0046  34  TYR A CA  
37    C C   . TYR A  8   ? 0.5813 0.3668 0.5257 0.1033  0.0371  -0.0027 34  TYR A C   
38    O O   . TYR A  8   ? 0.5821 0.3577 0.5241 0.1099  0.0428  -0.0046 34  TYR A O   
39    C CB  . TYR A  8   ? 0.5964 0.3604 0.5341 0.1007  0.0349  0.0033  34  TYR A CB  
40    C CG  . TYR A  8   ? 0.6151 0.3750 0.5440 0.0891  0.0334  -0.0028 34  TYR A CG  
41    C CD1 . TYR A  8   ? 0.6214 0.3898 0.5515 0.0814  0.0277  -0.0010 34  TYR A CD1 
42    C CD2 . TYR A  8   ? 0.6351 0.3848 0.5550 0.0859  0.0375  -0.0105 34  TYR A CD2 
43    C CE1 . TYR A  8   ? 0.6364 0.4030 0.5594 0.0710  0.0262  -0.0064 34  TYR A CE1 
44    C CE2 . TYR A  8   ? 0.6503 0.3989 0.5629 0.0751  0.0356  -0.0160 34  TYR A CE2 
45    C CZ  . TYR A  8   ? 0.6589 0.4164 0.5735 0.0679  0.0300  -0.0138 34  TYR A CZ  
46    O OH  . TYR A  8   ? 0.6883 0.4456 0.5963 0.0575  0.0281  -0.0188 34  TYR A OH  
56    N N   . PRO A  9   ? 0.5732 0.3684 0.5160 0.0954  0.0345  -0.0069 35  PRO A N   
57    C CA  . PRO A  9   ? 0.5661 0.3727 0.5108 0.0872  0.0283  -0.0057 35  PRO A CA  
58    C C   . PRO A  9   ? 0.5612 0.3891 0.5177 0.0891  0.0242  -0.0009 35  PRO A C   
59    O O   . PRO A  9   ? 0.5604 0.3972 0.5186 0.0828  0.0194  0.0001  35  PRO A O   
60    C CB  . PRO A  9   ? 0.5749 0.3803 0.5118 0.0792  0.0288  -0.0131 35  PRO A CB  
61    C CG  . PRO A  9   ? 0.5817 0.3870 0.5182 0.0846  0.0337  -0.0166 35  PRO A CG  
62    C CD  . PRO A  9   ? 0.5651 0.3598 0.5032 0.0943  0.0381  -0.0137 35  PRO A CD  
70    N N   . CYS A  10  ? 0.5579 0.3938 0.5222 0.0975  0.0261  0.0019  36  CYS A N   
71    C CA  . CYS A  10  ? 0.5627 0.4188 0.5380 0.0991  0.0225  0.0061  36  CYS A CA  
72    C C   . CYS A  10  ? 0.5858 0.4461 0.5681 0.1030  0.0194  0.0136  36  CYS A C   
73    O O   . CYS A  10  ? 0.5846 0.4328 0.5647 0.1074  0.0213  0.0162  36  CYS A O   
74    C CB  . CYS A  10  ? 0.5554 0.4200 0.5358 0.1051  0.0260  0.0050  36  CYS A CB  
75    S SG  . CYS A  10  ? 0.5665 0.4210 0.5370 0.1036  0.0316  -0.0035 36  CYS A SG  
80    N N   . ASP A  11  ? 0.6029 0.4804 0.5933 0.1013  0.0149  0.0172  37  ASP A N   
81    C CA  . ASP A  11  ? 0.6279 0.5130 0.6257 0.1045  0.0115  0.0244  37  ASP A CA  
82    C C   . ASP A  11  ? 0.6485 0.5476 0.6567 0.1119  0.0126  0.0274  37  ASP A C   
83    O O   . ASP A  11  ? 0.6435 0.5546 0.6553 0.1099  0.0122  0.0254  37  ASP A O   
84    C CB  . ASP A  11  ? 0.6430 0.5376 0.6421 0.0967  0.0058  0.0258  37  ASP A CB  
85    C CG  . ASP A  11  ? 0.7079 0.5904 0.6980 0.0895  0.0044  0.0238  37  ASP A CG  
86    O OD1 . ASP A  11  ? 0.7214 0.5921 0.7080 0.0913  0.0048  0.0265  37  ASP A OD1 
87    O OD2 . ASP A  11  ? 0.7405 0.6255 0.7272 0.0821  0.0029  0.0198  37  ASP A OD2 
92    N N   . GLU A  12  ? 0.6707 0.5687 0.6837 0.1202  0.0139  0.0324  38  GLU A N   
93    C CA  . GLU A  12  ? 0.6923 0.6041 0.7156 0.1276  0.0153  0.0355  38  GLU A CA  
94    C C   . GLU A  12  ? 0.7182 0.6473 0.7515 0.1282  0.0102  0.0420  38  GLU A C   
95    O O   . GLU A  12  ? 0.7235 0.6506 0.7584 0.1311  0.0081  0.0474  38  GLU A O   
96    C CB  . GLU A  12  ? 0.7177 0.6191 0.7412 0.1375  0.0204  0.0369  38  GLU A CB  
97    C CG  . GLU A  12  ? 0.7749 0.6611 0.7896 0.1380  0.0264  0.0300  38  GLU A CG  
98    C CD  . GLU A  12  ? 0.8484 0.7217 0.8621 0.1476  0.0320  0.0311  38  GLU A CD  
99    O OE1 . GLU A  12  ? 0.8612 0.7334 0.8790 0.1534  0.0309  0.0374  38  GLU A OE1 
100   O OE2 . GLU A  12  ? 0.8731 0.7370 0.8814 0.1494  0.0376  0.0255  38  GLU A OE2 
107   N N   . LYS A  13  ? 0.7319 0.6780 0.7718 0.1257  0.0085  0.0416  39  LYS A N   
108   C CA  . LYS A  13  ? 0.7494 0.7133 0.7989 0.1257  0.0040  0.0470  39  LYS A CA  
109   C C   . LYS A  13  ? 0.7638 0.7400 0.8232 0.1335  0.0066  0.0495  39  LYS A C   
110   O O   . LYS A  13  ? 0.7649 0.7411 0.8243 0.1354  0.0109  0.0455  39  LYS A O   
111   C CB  . LYS A  13  ? 0.7779 0.7519 0.8274 0.1166  0.0004  0.0448  39  LYS A CB  
112   C CG  . LYS A  13  ? 0.8449 0.8117 0.8873 0.1090  -0.0033 0.0440  39  LYS A CG  
113   C CD  . LYS A  13  ? 0.9017 0.8823 0.9481 0.1027  -0.0083 0.0459  39  LYS A CD  
114   C CE  . LYS A  13  ? 0.9517 0.9395 0.9984 0.0976  -0.0079 0.0415  39  LYS A CE  
115   N NZ  . LYS A  13  ? 0.9788 0.9791 1.0293 0.0919  -0.0123 0.0432  39  LYS A NZ  
129   N N   . LYS A  14  ? 0.7716 0.7589 0.8396 0.1379  0.0040  0.0561  40  LYS A N   
130   C CA  . LYS A  14  ? 0.7799 0.7807 0.8586 0.1455  0.0061  0.0592  40  LYS A CA  
131   C C   . LYS A  14  ? 0.7806 0.8023 0.8678 0.1411  0.0022  0.0611  40  LYS A C   
132   O O   . LYS A  14  ? 0.7812 0.8123 0.8725 0.1407  0.0044  0.0587  40  LYS A O   
133   C CB  . LYS A  14  ? 0.8090 0.8082 0.8922 0.1546  0.0063  0.0657  40  LYS A CB  
134   C CG  . LYS A  14  ? 0.8815 0.8590 0.9553 0.1570  0.0081  0.0655  40  LYS A CG  
135   C CD  . LYS A  14  ? 0.9545 0.9150 1.0197 0.1579  0.0142  0.0586  40  LYS A CD  
136   C CE  . LYS A  14  ? 1.0158 0.9542 1.0707 0.1582  0.0156  0.0579  40  LYS A CE  
137   N NZ  . LYS A  14  ? 1.0469 0.9781 1.1043 0.1690  0.0189  0.0625  40  LYS A NZ  
151   N N   . ASP A  17  ? 0.7601 0.8545 0.8911 0.1553  0.0134  0.0639  43  ASP A N   
152   C CA  . ASP A  17  ? 0.7646 0.8554 0.8978 0.1647  0.0200  0.0631  43  ASP A CA  
153   C C   . ASP A  17  ? 0.7698 0.8403 0.8906 0.1638  0.0245  0.0563  43  ASP A C   
154   O O   . ASP A  17  ? 0.7734 0.8438 0.8936 0.1655  0.0298  0.0524  43  ASP A O   
155   C CB  . ASP A  17  ? 0.7830 0.8925 0.9265 0.1663  0.0227  0.0636  43  ASP A CB  
156   C CG  . ASP A  17  ? 0.8386 0.9695 0.9944 0.1662  0.0182  0.0699  43  ASP A CG  
157   O OD1 . ASP A  17  ? 0.8465 0.9881 1.0041 0.1578  0.0145  0.0697  43  ASP A OD1 
158   O OD2 . ASP A  17  ? 0.8617 0.9988 1.0254 0.1746  0.0185  0.0752  43  ASP A OD2 
162   N N   . SER A  18  ? 0.7651 0.8190 0.8760 0.1609  0.0224  0.0549  44  SER A N   
163   C CA  . SER A  18  ? 0.7672 0.8018 0.8658 0.1590  0.0260  0.0485  44  SER A CA  
164   C C   . SER A  18  ? 0.7600 0.7778 0.8496 0.1568  0.0232  0.0485  44  SER A C   
165   O O   . SER A  18  ? 0.7641 0.7858 0.8563 0.1553  0.0181  0.0532  44  SER A O   
166   C CB  . SER A  18  ? 0.7861 0.8235 0.8803 0.1505  0.0257  0.0433  44  SER A CB  
167   O OG  . SER A  18  ? 0.8180 0.8632 0.9133 0.1425  0.0196  0.0451  44  SER A OG  
173   N N   . VAL A  19  ? 0.7462 0.7454 0.8249 0.1562  0.0268  0.0432  45  VAL A N   
174   C CA  . VAL A  19  ? 0.7367 0.7186 0.8056 0.1532  0.0249  0.0423  45  VAL A CA  
175   C C   . VAL A  19  ? 0.7135 0.6851 0.7715 0.1455  0.0259  0.0351  45  VAL A C   
176   O O   . VAL A  19  ? 0.7204 0.6857 0.7741 0.1473  0.0311  0.0303  45  VAL A O   
177   C CB  . VAL A  19  ? 0.7553 0.7228 0.8221 0.1618  0.0282  0.0445  45  VAL A CB  
178   C CG1 . VAL A  19  ? 0.7646 0.7307 0.8340 0.1705  0.0353  0.0427  45  VAL A CG1 
179   C CG2 . VAL A  19  ? 0.7721 0.7184 0.8262 0.1577  0.0283  0.0411  45  VAL A CG2 
189   N N   . ILE A  20  ? 0.6837 0.6545 0.7374 0.1370  0.0210  0.0345  46  ILE A N   
190   C CA  . ILE A  20  ? 0.6640 0.6280 0.7086 0.1291  0.0209  0.0285  46  ILE A CA  
191   C C   . ILE A  20  ? 0.6413 0.5861 0.6750 0.1265  0.0211  0.0258  46  ILE A C   
192   O O   . ILE A  20  ? 0.6426 0.5832 0.6759 0.1260  0.0179  0.0294  46  ILE A O   
193   C CB  . ILE A  20  ? 0.6674 0.6440 0.7148 0.1212  0.0154  0.0295  46  ILE A CB  
194   C CG1 . ILE A  20  ? 0.6726 0.6684 0.7307 0.1228  0.0150  0.0322  46  ILE A CG1 
195   C CG2 . ILE A  20  ? 0.6782 0.6489 0.7168 0.1134  0.0152  0.0237  46  ILE A CG2 
196   C CD1 . ILE A  20  ? 0.6828 0.6910 0.7451 0.1162  0.0094  0.0347  46  ILE A CD1 
208   N N   . ALA A  21  ? 0.6144 0.5481 0.6391 0.1242  0.0246  0.0196  47  ALA A N   
209   C CA  . ALA A  21  ? 0.5987 0.5149 0.6125 0.1200  0.0248  0.0162  47  ALA A CA  
210   C C   . ALA A  21  ? 0.5719 0.4915 0.5813 0.1102  0.0211  0.0129  47  ALA A C   
211   O O   . ALA A  21  ? 0.5692 0.4908 0.5753 0.1075  0.0229  0.0084  47  ALA A O   
212   C CB  . ALA A  21  ? 0.6051 0.5071 0.6114 0.1234  0.0310  0.0111  47  ALA A CB  
218   N N   . GLU A  22  ? 0.5482 0.4699 0.5581 0.1054  0.0161  0.0157  48  GLU A N   
219   C CA  . GLU A  22  ? 0.5341 0.4592 0.5405 0.0966  0.0126  0.0132  48  GLU A CA  
220   C C   . GLU A  22  ? 0.5124 0.4215 0.5077 0.0923  0.0140  0.0084  48  GLU A C   
221   O O   . GLU A  22  ? 0.5120 0.4104 0.5036 0.0919  0.0133  0.0097  48  GLU A O   
222   C CB  . GLU A  22  ? 0.5754 0.5082 0.5863 0.0933  0.0072  0.0179  48  GLU A CB  
223   C CG  . GLU A  22  ? 0.6608 0.6101 0.6825 0.0966  0.0055  0.0225  48  GLU A CG  
224   C CD  . GLU A  22  ? 0.7730 0.7307 0.7985 0.0924  0.0002  0.0264  48  GLU A CD  
225   O OE1 . GLU A  22  ? 0.7906 0.7599 0.8197 0.0885  -0.0019 0.0263  48  GLU A OE1 
226   O OE2 . GLU A  22  ? 0.8127 0.7645 0.8370 0.0930  -0.0016 0.0296  48  GLU A OE2 
233   N N   . CYS A  23  ? 0.4915 0.3987 0.4812 0.0894  0.0162  0.0029  49  CYS A N   
234   C CA  . CYS A  23  ? 0.4867 0.3792 0.4653 0.0850  0.0179  -0.0024 49  CYS A CA  
235   C C   . CYS A  23  ? 0.4679 0.3657 0.4426 0.0769  0.0155  -0.0062 49  CYS A C   
236   O O   . CYS A  23  ? 0.4711 0.3600 0.4371 0.0732  0.0172  -0.0113 49  CYS A O   
237   C CB  . CYS A  23  ? 0.5019 0.3847 0.4761 0.0902  0.0239  -0.0060 49  CYS A CB  
238   S SG  . CYS A  23  ? 0.5656 0.4251 0.5294 0.0904  0.0272  -0.0088 49  CYS A SG  
243   N N   . SER A  24  ? 0.4463 0.3580 0.4270 0.0741  0.0116  -0.0037 50  SER A N   
244   C CA  . SER A  24  ? 0.4447 0.3624 0.4227 0.0673  0.0094  -0.0066 50  SER A CA  
245   C C   . SER A  24  ? 0.4538 0.3660 0.4265 0.0603  0.0063  -0.0077 50  SER A C   
246   O O   . SER A  24  ? 0.4558 0.3632 0.4291 0.0600  0.0048  -0.0049 50  SER A O   
247   C CB  . SER A  24  ? 0.4512 0.3850 0.4375 0.0673  0.0068  -0.0034 50  SER A CB  
248   O OG  . SER A  24  ? 0.4768 0.4149 0.4680 0.0659  0.0031  0.0009  50  SER A OG  
254   N N   . ASN A  25  ? 0.4549 0.3691 0.4229 0.0545  0.0054  -0.0115 51  ASN A N   
255   C CA  . ASN A  25  ? 0.4689 0.3812 0.4327 0.0473  0.0024  -0.0128 51  ASN A CA  
256   C C   . ASN A  25  ? 0.4687 0.3669 0.4270 0.0455  0.0028  -0.0133 51  ASN A C   
257   O O   . ASN A  25  ? 0.4673 0.3657 0.4268 0.0423  -0.0001 -0.0109 51  ASN A O   
258   C CB  . ASN A  25  ? 0.4943 0.4191 0.4652 0.0451  -0.0017 -0.0090 51  ASN A CB  
259   C CG  . ASN A  25  ? 0.5673 0.4946 0.5351 0.0377  -0.0047 -0.0107 51  ASN A CG  
260   O OD1 . ASN A  25  ? 0.5857 0.5165 0.5503 0.0347  -0.0048 -0.0139 51  ASN A OD1 
261   N ND2 . ASN A  25  ? 0.5841 0.5102 0.5529 0.0348  -0.0072 -0.0085 51  ASN A ND2 
268   N N   . ARG A  26  ? 0.4635 0.3488 0.4151 0.0473  0.0067  -0.0166 52  ARG A N   
269   C CA  . ARG A  26  ? 0.4755 0.3456 0.4209 0.0454  0.0077  -0.0174 52  ARG A CA  
270   C C   . ARG A  26  ? 0.4838 0.3424 0.4186 0.0410  0.0103  -0.0238 52  ARG A C   
271   O O   . ARG A  26  ? 0.4922 0.3353 0.4208 0.0414  0.0129  -0.0253 52  ARG A O   
272   C CB  . ARG A  26  ? 0.4883 0.3509 0.4366 0.0528  0.0098  -0.0135 52  ARG A CB  
273   C CG  . ARG A  26  ? 0.5051 0.3685 0.4566 0.0610  0.0136  -0.0132 52  ARG A CG  
274   C CD  . ARG A  26  ? 0.5281 0.3922 0.4867 0.0679  0.0135  -0.0071 52  ARG A CD  
275   N NE  . ARG A  26  ? 0.5453 0.4257 0.5133 0.0682  0.0095  -0.0025 52  ARG A NE  
276   C CZ  . ARG A  26  ? 0.5659 0.4500 0.5405 0.0721  0.0077  0.0033  52  ARG A CZ  
277   N NH1 . ARG A  26  ? 0.5449 0.4177 0.5180 0.0766  0.0095  0.0057  52  ARG A NH1 
278   N NH2 . ARG A  26  ? 0.5618 0.4607 0.5440 0.0715  0.0042  0.0068  52  ARG A NH2 
292   N N   . ARG A  27  ? 0.4764 0.3423 0.4086 0.0364  0.0092  -0.0275 53  ARG A N   
293   C CA  . ARG A  27  ? 0.4904 0.3482 0.4124 0.0305  0.0107  -0.0337 53  ARG A CA  
294   C C   . ARG A  27  ? 0.5049 0.3492 0.4201 0.0343  0.0161  -0.0375 53  ARG A C   
295   O O   . ARG A  27  ? 0.5161 0.3480 0.4219 0.0297  0.0179  -0.0423 53  ARG A O   
296   C CB  . ARG A  27  ? 0.5007 0.3516 0.4182 0.0232  0.0085  -0.0344 53  ARG A CB  
297   C CG  . ARG A  27  ? 0.5179 0.3813 0.4423 0.0200  0.0036  -0.0304 53  ARG A CG  
298   C CD  . ARG A  27  ? 0.5390 0.3957 0.4597 0.0132  0.0019  -0.0305 53  ARG A CD  
299   N NE  . ARG A  27  ? 0.5560 0.3976 0.4741 0.0160  0.0042  -0.0287 53  ARG A NE  
300   C CZ  . ARG A  27  ? 0.5613 0.4034 0.4855 0.0210  0.0036  -0.0231 53  ARG A CZ  
301   N NH1 . ARG A  27  ? 0.5437 0.4005 0.4768 0.0236  0.0007  -0.0191 53  ARG A NH1 
302   N NH2 . ARG A  27  ? 0.5594 0.3871 0.4805 0.0234  0.0058  -0.0215 53  ARG A NH2 
316   N N   . LEU A  28  ? 0.5070 0.3538 0.4269 0.0424  0.0189  -0.0358 54  LEU A N   
317   C CA  . LEU A  28  ? 0.5246 0.3590 0.4387 0.0469  0.0245  -0.0393 54  LEU A CA  
318   C C   . LEU A  28  ? 0.5354 0.3712 0.4422 0.0430  0.0260  -0.0453 54  LEU A C   
319   O O   . LEU A  28  ? 0.5279 0.3781 0.4385 0.0426  0.0241  -0.0448 54  LEU A O   
320   C CB  . LEU A  28  ? 0.5235 0.3624 0.4459 0.0568  0.0270  -0.0352 54  LEU A CB  
321   C CG  . LEU A  28  ? 0.5351 0.3747 0.4656 0.0613  0.0253  -0.0287 54  LEU A CG  
322   C CD1 . LEU A  28  ? 0.5319 0.3799 0.4715 0.0703  0.0271  -0.0247 54  LEU A CD1 
323   C CD2 . LEU A  28  ? 0.5505 0.3714 0.4750 0.0617  0.0275  -0.0290 54  LEU A CD2 
335   N N   . GLN A  29  ? 0.5501 0.3710 0.4458 0.0396  0.0293  -0.0510 55  GLN A N   
336   C CA  . GLN A  29  ? 0.5721 0.3925 0.4590 0.0353  0.0309  -0.0574 55  GLN A CA  
337   C C   . GLN A  29  ? 0.5783 0.3955 0.4636 0.0424  0.0366  -0.0595 55  GLN A C   
338   O O   . GLN A  29  ? 0.5758 0.3970 0.4559 0.0403  0.0377  -0.0637 55  GLN A O   
339   C CB  . GLN A  29  ? 0.6194 0.4250 0.4944 0.0274  0.0318  -0.0630 55  GLN A CB  
340   C CG  . GLN A  29  ? 0.6951 0.5059 0.5708 0.0190  0.0262  -0.0619 55  GLN A CG  
341   C CD  . GLN A  29  ? 0.7998 0.5949 0.6650 0.0116  0.0273  -0.0664 55  GLN A CD  
342   O OE1 . GLN A  29  ? 0.8479 0.6272 0.7039 0.0117  0.0322  -0.0713 55  GLN A OE1 
343   N NE2 . GLN A  29  ? 0.8116 0.6105 0.6778 0.0046  0.0229  -0.0652 55  GLN A NE2 
352   N N   . GLU A  30  ? 0.5813 0.3910 0.4707 0.0508  0.0402  -0.0568 56  GLU A N   
353   C CA  . GLU A  30  ? 0.5891 0.3960 0.4784 0.0586  0.0460  -0.0581 56  GLU A CA  
354   C C   . GLU A  30  ? 0.5761 0.3890 0.4777 0.0680  0.0463  -0.0512 56  GLU A C   
355   O O   . GLU A  30  ? 0.5722 0.3866 0.4799 0.0682  0.0429  -0.0462 56  GLU A O   
356   C CB  . GLU A  30  ? 0.6411 0.4265 0.5191 0.0590  0.0520  -0.0638 56  GLU A CB  
357   C CG  . GLU A  30  ? 0.7448 0.5236 0.6098 0.0494  0.0520  -0.0712 56  GLU A CG  
358   C CD  . GLU A  30  ? 0.8742 0.6398 0.7285 0.0511  0.0589  -0.0779 56  GLU A CD  
359   O OE1 . GLU A  30  ? 0.9045 0.6787 0.7569 0.0512  0.0601  -0.0806 56  GLU A OE1 
360   O OE2 . GLU A  30  ? 0.9105 0.6568 0.7581 0.0523  0.0633  -0.0805 56  GLU A OE2 
367   N N   . VAL A  31  ? 0.5676 0.3838 0.4727 0.0756  0.0507  -0.0510 57  VAL A N   
368   C CA  . VAL A  31  ? 0.5648 0.3870 0.4815 0.0847  0.0515  -0.0447 57  VAL A CA  
369   C C   . VAL A  31  ? 0.5864 0.3914 0.5012 0.0889  0.0543  -0.0435 57  VAL A C   
370   O O   . VAL A  31  ? 0.5898 0.3784 0.4949 0.0894  0.0594  -0.0486 57  VAL A O   
371   C CB  . VAL A  31  ? 0.5610 0.3905 0.4813 0.0917  0.0561  -0.0452 57  VAL A CB  
372   C CG1 . VAL A  31  ? 0.5568 0.3919 0.4892 0.1013  0.0572  -0.0388 57  VAL A CG1 
373   C CG2 . VAL A  31  ? 0.5548 0.4010 0.4770 0.0876  0.0533  -0.0456 57  VAL A CG2 
383   N N   . PRO A  32  ? 0.5927 0.3998 0.5151 0.0912  0.0509  -0.0372 58  PRO A N   
384   C CA  . PRO A  32  ? 0.6093 0.3992 0.5290 0.0951  0.0535  -0.0357 58  PRO A CA  
385   C C   . PRO A  32  ? 0.6304 0.4133 0.5517 0.1055  0.0602  -0.0356 58  PRO A C   
386   O O   . PRO A  32  ? 0.6229 0.4191 0.5539 0.1122  0.0610  -0.0322 58  PRO A O   
387   C CB  . PRO A  32  ? 0.6094 0.4073 0.5386 0.0961  0.0482  -0.0282 58  PRO A CB  
388   C CG  . PRO A  32  ? 0.6043 0.4220 0.5401 0.0918  0.0429  -0.0263 58  PRO A CG  
389   C CD  . PRO A  32  ? 0.5775 0.4021 0.5107 0.0904  0.0449  -0.0311 58  PRO A CD  
397   N N   . GLN A  33  ? 0.6517 0.4135 0.5637 0.1069  0.0653  -0.0391 59  GLN A N   
398   C CA  . GLN A  33  ? 0.6764 0.4290 0.5893 0.1173  0.0722  -0.0389 59  GLN A CA  
399   C C   . GLN A  33  ? 0.6889 0.4374 0.6091 0.1249  0.0718  -0.0314 59  GLN A C   
400   O O   . GLN A  33  ? 0.6957 0.4308 0.6143 0.1329  0.0776  -0.0313 59  GLN A O   
401   C CB  . GLN A  33  ? 0.7115 0.4425 0.6098 0.1152  0.0786  -0.0470 59  GLN A CB  
402   C CG  . GLN A  33  ? 0.7631 0.4981 0.6534 0.1079  0.0791  -0.0544 59  GLN A CG  
403   C CD  . GLN A  33  ? 0.8145 0.5659 0.7118 0.1131  0.0809  -0.0541 59  GLN A CD  
404   O OE1 . GLN A  33  ? 0.8235 0.5928 0.7253 0.1088  0.0763  -0.0532 59  GLN A OE1 
405   N NE2 . GLN A  33  ? 0.8207 0.5664 0.7192 0.1226  0.0878  -0.0546 59  GLN A NE2 
414   N N   . THR A  34  ? 0.6866 0.4470 0.6148 0.1228  0.0650  -0.0251 60  THR A N   
415   C CA  . THR A  34  ? 0.6962 0.4549 0.6315 0.1292  0.0637  -0.0175 60  THR A CA  
416   C C   . THR A  34  ? 0.6954 0.4774 0.6452 0.1329  0.0590  -0.0105 60  THR A C   
417   O O   . THR A  34  ? 0.6961 0.4814 0.6518 0.1345  0.0551  -0.0039 60  THR A O   
418   C CB  . THR A  34  ? 0.7166 0.4629 0.6450 0.1221  0.0604  -0.0168 60  THR A CB  
419   O OG1 . THR A  34  ? 0.7238 0.4819 0.6521 0.1120  0.0542  -0.0179 60  THR A OG1 
420   C CG2 . THR A  34  ? 0.7338 0.4552 0.6481 0.1194  0.0657  -0.0230 60  THR A CG2 
428   N N   . VAL A  35  ? 0.6900 0.4879 0.6455 0.1341  0.0594  -0.0117 61  VAL A N   
429   C CA  . VAL A  35  ? 0.6865 0.5064 0.6556 0.1374  0.0555  -0.0056 61  VAL A CA  
430   C C   . VAL A  35  ? 0.6892 0.5093 0.6665 0.1495  0.0591  -0.0003 61  VAL A C   
431   O O   . VAL A  35  ? 0.6956 0.5038 0.6690 0.1557  0.0658  -0.0031 61  VAL A O   
432   C CB  . VAL A  35  ? 0.6893 0.5251 0.6611 0.1345  0.0552  -0.0086 61  VAL A CB  
433   C CG1 . VAL A  35  ? 0.6839 0.5416 0.6696 0.1376  0.0516  -0.0024 61  VAL A CG1 
434   C CG2 . VAL A  35  ? 0.6974 0.5330 0.6612 0.1232  0.0517  -0.0135 61  VAL A CG2 
444   N N   . GLY A  36  ? 0.6832 0.5166 0.6714 0.1527  0.0548  0.0072  62  GLY A N   
445   C CA  . GLY A  36  ? 0.6870 0.5230 0.6841 0.1641  0.0573  0.0131  62  GLY A CA  
446   C C   . GLY A  36  ? 0.6892 0.5348 0.6926 0.1713  0.0623  0.0120  62  GLY A C   
447   O O   . GLY A  36  ? 0.6863 0.5467 0.6931 0.1677  0.0611  0.0100  62  GLY A O   
451   N N   . LYS A  37  ? 0.6928 0.5299 0.6979 0.1818  0.0682  0.0134  63  LYS A N   
452   C CA  . LYS A  37  ? 0.6947 0.5400 0.7064 0.1902  0.0740  0.0128  63  LYS A CA  
453   C C   . LYS A  37  ? 0.6765 0.5482 0.7028 0.1922  0.0702  0.0183  63  LYS A C   
454   O O   . LYS A  37  ? 0.6739 0.5569 0.7047 0.1943  0.0734  0.0163  63  LYS A O   
455   C CB  . LYS A  37  ? 0.7300 0.5622 0.7427 0.2021  0.0800  0.0155  63  LYS A CB  
456   C CG  . LYS A  37  ? 0.7950 0.6321 0.8168 0.2081  0.0761  0.0249  63  LYS A CG  
457   C CD  . LYS A  37  ? 0.8680 0.6915 0.8907 0.2205  0.0823  0.0279  63  LYS A CD  
458   C CE  . LYS A  37  ? 0.9128 0.7538 0.9498 0.2315  0.0849  0.0328  63  LYS A CE  
459   N NZ  . LYS A  37  ? 0.9525 0.7810 0.9913 0.2442  0.0906  0.0366  63  LYS A NZ  
473   N N   . TYR A  38  ? 0.6612 0.5425 0.6949 0.1917  0.0638  0.0253  64  TYR A N   
474   C CA  . TYR A  38  ? 0.6488 0.5549 0.6963 0.1928  0.0597  0.0309  64  TYR A CA  
475   C C   . TYR A  38  ? 0.6251 0.5443 0.6726 0.1820  0.0543  0.0288  64  TYR A C   
476   O O   . TYR A  38  ? 0.6183 0.5577 0.6763 0.1821  0.0517  0.0322  64  TYR A O   
477   C CB  . TYR A  38  ? 0.6589 0.5697 0.7141 0.1976  0.0553  0.0396  64  TYR A CB  
478   C CG  . TYR A  38  ? 0.6913 0.5890 0.7385 0.1916  0.0508  0.0407  64  TYR A CG  
479   C CD1 . TYR A  38  ? 0.7056 0.6096 0.7506 0.1809  0.0444  0.0400  64  TYR A CD1 
480   C CD2 . TYR A  38  ? 0.7196 0.5981 0.7611 0.1967  0.0533  0.0424  64  TYR A CD2 
481   C CE1 . TYR A  38  ? 0.7283 0.6207 0.7659 0.1753  0.0406  0.0408  64  TYR A CE1 
482   C CE2 . TYR A  38  ? 0.7416 0.6079 0.7754 0.1908  0.0494  0.0434  64  TYR A CE2 
483   C CZ  . TYR A  38  ? 0.7541 0.6279 0.7861 0.1800  0.0430  0.0425  64  TYR A CZ  
484   O OH  . TYR A  38  ? 0.7876 0.6500 0.8123 0.1743  0.0394  0.0436  64  TYR A OH  
494   N N   . VAL A  39  ? 0.6086 0.5167 0.6446 0.1727  0.0528  0.0233  65  VAL A N   
495   C CA  . VAL A  39  ? 0.5884 0.5076 0.6239 0.1627  0.0480  0.0213  65  VAL A CA  
496   C C   . VAL A  39  ? 0.5634 0.4970 0.6039 0.1633  0.0506  0.0191  65  VAL A C   
497   O O   . VAL A  39  ? 0.5703 0.4977 0.6072 0.1670  0.0569  0.0148  65  VAL A O   
498   C CB  . VAL A  39  ? 0.6071 0.5108 0.6290 0.1537  0.0471  0.0153  65  VAL A CB  
499   C CG1 . VAL A  39  ? 0.6109 0.5253 0.6316 0.1446  0.0437  0.0123  65  VAL A CG1 
500   C CG2 . VAL A  39  ? 0.6187 0.5119 0.6368 0.1512  0.0432  0.0182  65  VAL A CG2 
510   N N   . THR A  40  ? 0.5355 0.4878 0.5840 0.1593  0.0461  0.0220  66  THR A N   
511   C CA  . THR A  40  ? 0.5181 0.4853 0.5719 0.1588  0.0479  0.0206  66  THR A CA  
512   C C   . THR A  40  ? 0.4994 0.4701 0.5479 0.1486  0.0447  0.0170  66  THR A C   
513   O O   . THR A  40  ? 0.4988 0.4771 0.5480 0.1474  0.0471  0.0144  66  THR A O   
514   C CB  . THR A  40  ? 0.5259 0.5130 0.5940 0.1630  0.0459  0.0272  66  THR A CB  
515   O OG1 . THR A  40  ? 0.5338 0.5282 0.6049 0.1571  0.0387  0.0310  66  THR A OG1 
516   C CG2 . THR A  40  ? 0.5361 0.5222 0.6108 0.1740  0.0491  0.0314  66  THR A CG2 
524   N N   . GLU A  41  ? 0.4862 0.4523 0.5300 0.1415  0.0393  0.0171  67  GLU A N   
525   C CA  . GLU A  41  ? 0.4754 0.4447 0.5144 0.1322  0.0363  0.0140  67  GLU A CA  
526   C C   . GLU A  41  ? 0.4700 0.4230 0.4978 0.1269  0.0347  0.0105  67  GLU A C   
527   O O   . GLU A  41  ? 0.4745 0.4216 0.5019 0.1268  0.0318  0.0133  67  GLU A O   
528   C CB  . GLU A  41  ? 0.4904 0.4757 0.5377 0.1281  0.0306  0.0185  67  GLU A CB  
529   C CG  . GLU A  41  ? 0.5341 0.5361 0.5934 0.1332  0.0316  0.0225  67  GLU A CG  
530   C CD  . GLU A  41  ? 0.5852 0.6035 0.6520 0.1283  0.0267  0.0260  67  GLU A CD  
531   O OE1 . GLU A  41  ? 0.6001 0.6169 0.6629 0.1210  0.0224  0.0253  67  GLU A OE1 
532   O OE2 . GLU A  41  ? 0.5895 0.6221 0.6663 0.1317  0.0274  0.0294  67  GLU A OE2 
539   N N   . LEU A  42  ? 0.4538 0.3995 0.4722 0.1227  0.0368  0.0046  68  LEU A N   
540   C CA  . LEU A  42  ? 0.4537 0.3844 0.4612 0.1173  0.0358  0.0007  68  LEU A CA  
541   C C   . LEU A  42  ? 0.4372 0.3730 0.4410 0.1085  0.0320  -0.0015 68  LEU A C   
542   O O   . LEU A  42  ? 0.4413 0.3826 0.4435 0.1067  0.0336  -0.0044 68  LEU A O   
543   C CB  . LEU A  42  ? 0.4702 0.3864 0.4689 0.1203  0.0420  -0.0047 68  LEU A CB  
544   C CG  . LEU A  42  ? 0.5025 0.4018 0.4885 0.1146  0.0421  -0.0098 68  LEU A CG  
545   C CD1 . LEU A  42  ? 0.5124 0.4037 0.4975 0.1128  0.0385  -0.0068 68  LEU A CD1 
546   C CD2 . LEU A  42  ? 0.5177 0.4028 0.4961 0.1189  0.0489  -0.0146 68  LEU A CD2 
558   N N   . ASP A  43  ? 0.4147 0.3493 0.4176 0.1031  0.0270  0.0001  69  ASP A N   
559   C CA  . ASP A  43  ? 0.4005 0.3398 0.4004 0.0950  0.0232  -0.0016 69  ASP A CA  
560   C C   . ASP A  43  ? 0.3954 0.3209 0.3843 0.0898  0.0230  -0.0061 69  ASP A C   
561   O O   . ASP A  43  ? 0.3978 0.3160 0.3847 0.0879  0.0208  -0.0049 69  ASP A O   
562   C CB  . ASP A  43  ? 0.4070 0.3565 0.4140 0.0924  0.0178  0.0033  69  ASP A CB  
563   C CG  . ASP A  43  ? 0.4641 0.4197 0.4693 0.0847  0.0141  0.0021  69  ASP A CG  
564   O OD1 . ASP A  43  ? 0.4601 0.4125 0.4585 0.0813  0.0153  -0.0023 69  ASP A OD1 
565   O OD2 . ASP A  43  ? 0.4895 0.4533 0.5001 0.0824  0.0101  0.0056  69  ASP A OD2 
570   N N   . LEU A  44  ? 0.3881 0.3105 0.3698 0.0872  0.0253  -0.0113 70  LEU A N   
571   C CA  . LEU A  44  ? 0.4000 0.3108 0.3709 0.0814  0.0251  -0.0161 70  LEU A CA  
572   C C   . LEU A  44  ? 0.3892 0.3076 0.3578 0.0739  0.0215  -0.0177 70  LEU A C   
573   O O   . LEU A  44  ? 0.3944 0.3061 0.3540 0.0690  0.0218  -0.0224 70  LEU A O   
574   C CB  . LEU A  44  ? 0.4104 0.3105 0.3734 0.0839  0.0308  -0.0213 70  LEU A CB  
575   C CG  . LEU A  44  ? 0.4414 0.3287 0.4035 0.0903  0.0349  -0.0210 70  LEU A CG  
576   C CD1 . LEU A  44  ? 0.4536 0.3350 0.4108 0.0943  0.0411  -0.0254 70  LEU A CD1 
577   C CD2 . LEU A  44  ? 0.4540 0.3263 0.4085 0.0863  0.0338  -0.0226 70  LEU A CD2 
589   N N   . SER A  45  ? 0.3718 0.3039 0.3481 0.0729  0.0181  -0.0140 71  SER A N   
590   C CA  . SER A  45  ? 0.3805 0.3204 0.3554 0.0668  0.0150  -0.0149 71  SER A CA  
591   C C   . SER A  45  ? 0.3921 0.3267 0.3621 0.0602  0.0115  -0.0161 71  SER A C   
592   O O   . SER A  45  ? 0.3920 0.3197 0.3621 0.0603  0.0105  -0.0147 71  SER A O   
593   C CB  . SER A  45  ? 0.3891 0.3434 0.3734 0.0675  0.0126  -0.0104 71  SER A CB  
594   O OG  . SER A  45  ? 0.4178 0.3736 0.4074 0.0670  0.0093  -0.0065 71  SER A OG  
600   N N   . ASP A  46  ? 0.3981 0.3363 0.3638 0.0547  0.0097  -0.0186 72  ASP A N   
601   C CA  . ASP A  46  ? 0.4137 0.3493 0.3755 0.0481  0.0063  -0.0198 72  ASP A CA  
602   C C   . ASP A  46  ? 0.4222 0.3432 0.3762 0.0461  0.0075  -0.0230 72  ASP A C   
603   O O   . ASP A  46  ? 0.4214 0.3384 0.3749 0.0427  0.0052  -0.0221 72  ASP A O   
604   C CB  . ASP A  46  ? 0.4470 0.3894 0.4160 0.0469  0.0024  -0.0152 72  ASP A CB  
605   C CG  . ASP A  46  ? 0.5411 0.4969 0.5170 0.0480  0.0012  -0.0124 72  ASP A CG  
606   O OD1 . ASP A  46  ? 0.5613 0.5230 0.5354 0.0446  -0.0001 -0.0137 72  ASP A OD1 
607   O OD2 . ASP A  46  ? 0.5908 0.5512 0.5738 0.0520  0.0014  -0.0088 72  ASP A OD2 
612   N N   . ASN A  47  ? 0.4304 0.3430 0.3778 0.0477  0.0115  -0.0271 73  ASN A N   
613   C CA  . ASN A  47  ? 0.4469 0.3444 0.3856 0.0452  0.0132  -0.0309 73  ASN A CA  
614   C C   . ASN A  47  ? 0.4653 0.3615 0.3948 0.0396  0.0137  -0.0366 73  ASN A C   
615   O O   . ASN A  47  ? 0.4615 0.3692 0.3923 0.0372  0.0115  -0.0365 73  ASN A O   
616   C CB  . ASN A  47  ? 0.4573 0.3445 0.3960 0.0523  0.0179  -0.0307 73  ASN A CB  
617   C CG  . ASN A  47  ? 0.4772 0.3621 0.4222 0.0558  0.0167  -0.0256 73  ASN A CG  
618   O OD1 . ASN A  47  ? 0.4834 0.3626 0.4264 0.0518  0.0145  -0.0249 73  ASN A OD1 
619   N ND2 . ASN A  47  ? 0.4687 0.3585 0.4214 0.0630  0.0182  -0.0218 73  ASN A ND2 
626   N N   . PHE A  48  ? 0.4837 0.3662 0.4038 0.0369  0.0160  -0.0413 74  PHE A N   
627   C CA  . PHE A  48  ? 0.5040 0.3845 0.4144 0.0312  0.0165  -0.0470 74  PHE A CA  
628   C C   . PHE A  48  ? 0.5010 0.3730 0.4048 0.0348  0.0221  -0.0513 74  PHE A C   
629   O O   . PHE A  48  ? 0.5112 0.3750 0.4048 0.0301  0.0236  -0.0569 74  PHE A O   
630   C CB  . PHE A  48  ? 0.5245 0.3960 0.4281 0.0236  0.0148  -0.0498 74  PHE A CB  
631   C CG  . PHE A  48  ? 0.5446 0.4228 0.4541 0.0200  0.0100  -0.0460 74  PHE A CG  
632   C CD1 . PHE A  48  ? 0.5586 0.4528 0.4754 0.0196  0.0063  -0.0426 74  PHE A CD1 
633   C CD2 . PHE A  48  ? 0.5693 0.4372 0.4758 0.0162  0.0094  -0.0462 74  PHE A CD2 
634   C CE1 . PHE A  48  ? 0.5677 0.4676 0.4891 0.0160  0.0022  -0.0395 74  PHE A CE1 
635   C CE2 . PHE A  48  ? 0.5790 0.4534 0.4902 0.0123  0.0052  -0.0431 74  PHE A CE2 
636   C CZ  . PHE A  48  ? 0.5694 0.4599 0.4882 0.0125  0.0017  -0.0398 74  PHE A CZ  
646   N N   . ILE A  49  ? 0.4844 0.3581 0.3938 0.0428  0.0252  -0.0488 75  ILE A N   
647   C CA  . ILE A  49  ? 0.4779 0.3441 0.3818 0.0470  0.0310  -0.0526 75  ILE A CA  
648   C C   . ILE A  49  ? 0.4736 0.3475 0.3720 0.0437  0.0311  -0.0561 75  ILE A C   
649   O O   . ILE A  49  ? 0.4638 0.3523 0.3681 0.0437  0.0283  -0.0531 75  ILE A O   
650   C CB  . ILE A  49  ? 0.4677 0.3365 0.3804 0.0566  0.0341  -0.0486 75  ILE A CB  
651   C CG1 . ILE A  49  ? 0.4639 0.3252 0.3818 0.0603  0.0339  -0.0446 75  ILE A CG1 
652   C CG2 . ILE A  49  ? 0.4725 0.3344 0.3795 0.0610  0.0405  -0.0527 75  ILE A CG2 
653   C CD1 . ILE A  49  ? 0.4615 0.3317 0.3912 0.0681  0.0342  -0.0387 75  ILE A CD1 
665   N N   . THR A  50  ? 0.4720 0.3357 0.3589 0.0407  0.0343  -0.0625 76  THR A N   
666   C CA  . THR A  50  ? 0.4764 0.3461 0.3562 0.0371  0.0346  -0.0664 76  THR A CA  
667   C C   . THR A  50  ? 0.4736 0.3393 0.3495 0.0425  0.0408  -0.0693 76  THR A C   
668   O O   . THR A  50  ? 0.4780 0.3516 0.3502 0.0411  0.0412  -0.0711 76  THR A O   
669   C CB  . THR A  50  ? 0.5024 0.3652 0.3710 0.0280  0.0330  -0.0719 76  THR A CB  
670   O OG1 . THR A  50  ? 0.5198 0.3639 0.3811 0.0281  0.0372  -0.0760 76  THR A OG1 
671   C CG2 . THR A  50  ? 0.5109 0.3808 0.3832 0.0218  0.0266  -0.0692 76  THR A CG2 
679   N N   . HIS A  51  ? 0.4720 0.3256 0.3482 0.0487  0.0459  -0.0699 77  HIS A N   
680   C CA  . HIS A  51  ? 0.4850 0.3338 0.3573 0.0542  0.0525  -0.0730 77  HIS A CA  
681   C C   . HIS A  51  ? 0.4936 0.3418 0.3758 0.0641  0.0560  -0.0687 77  HIS A C   
682   O O   . HIS A  51  ? 0.4992 0.3406 0.3860 0.0667  0.0555  -0.0659 77  HIS A O   
683   C CB  . HIS A  51  ? 0.5023 0.3325 0.3609 0.0511  0.0569  -0.0805 77  HIS A CB  
684   C CG  . HIS A  51  ? 0.5247 0.3554 0.3719 0.0416  0.0546  -0.0858 77  HIS A CG  
685   N ND1 . HIS A  51  ? 0.5443 0.3749 0.3893 0.0335  0.0492  -0.0862 77  HIS A ND1 
686   C CD2 . HIS A  51  ? 0.5370 0.3687 0.3747 0.0390  0.0570  -0.0909 77  HIS A CD2 
687   C CE1 . HIS A  51  ? 0.5522 0.3844 0.3868 0.0263  0.0483  -0.0913 77  HIS A CE1 
688   N NE2 . HIS A  51  ? 0.5524 0.3852 0.3820 0.0292  0.0528  -0.0943 77  HIS A NE2 
696   N N   . ILE A  52  ? 0.4898 0.3447 0.3746 0.0697  0.0600  -0.0684 78  ILE A N   
697   C CA  . ILE A  52  ? 0.4930 0.3483 0.3866 0.0795  0.0642  -0.0650 78  ILE A CA  
698   C C   . ILE A  52  ? 0.5156 0.3631 0.4011 0.0830  0.0717  -0.0705 78  ILE A C   
699   O O   . ILE A  52  ? 0.5135 0.3676 0.3939 0.0804  0.0727  -0.0732 78  ILE A O   
700   C CB  . ILE A  52  ? 0.4801 0.3541 0.3868 0.0831  0.0617  -0.0585 78  ILE A CB  
701   C CG1 . ILE A  52  ? 0.4745 0.3572 0.3884 0.0789  0.0543  -0.0534 78  ILE A CG1 
702   C CG2 . ILE A  52  ? 0.4793 0.3540 0.3951 0.0931  0.0663  -0.0552 78  ILE A CG2 
703   C CD1 . ILE A  52  ? 0.4871 0.3620 0.4053 0.0805  0.0525  -0.0505 78  ILE A CD1 
715   N N   . THR A  53  ? 0.5348 0.3680 0.4188 0.0888  0.0772  -0.0721 79  THR A N   
716   C CA  . THR A  53  ? 0.5568 0.3809 0.4332 0.0930  0.0852  -0.0775 79  THR A CA  
717   C C   . THR A  53  ? 0.5648 0.3897 0.4516 0.1045  0.0902  -0.0736 79  THR A C   
718   O O   . THR A  53  ? 0.5525 0.3847 0.4515 0.1084  0.0871  -0.0669 79  THR A O   
719   C CB  . THR A  53  ? 0.5922 0.3952 0.4541 0.0885  0.0879  -0.0847 79  THR A CB  
720   O OG1 . THR A  53  ? 0.6133 0.4035 0.4784 0.0929  0.0891  -0.0825 79  THR A OG1 
721   C CG2 . THR A  53  ? 0.5954 0.3988 0.4486 0.0769  0.0822  -0.0878 79  THR A CG2 
729   N N   . ASN A  54  ? 0.5793 0.3973 0.4612 0.1099  0.0982  -0.0778 80  ASN A N   
730   C CA  . ASN A  54  ? 0.5955 0.4138 0.4869 0.1212  0.1035  -0.0744 80  ASN A CA  
731   C C   . ASN A  54  ? 0.6055 0.4088 0.4990 0.1258  0.1046  -0.0725 80  ASN A C   
732   O O   . ASN A  54  ? 0.6087 0.4134 0.5117 0.1354  0.1079  -0.0684 80  ASN A O   
733   C CB  . ASN A  54  ? 0.6281 0.4431 0.5138 0.1259  0.1121  -0.0795 80  ASN A CB  
734   C CG  . ASN A  54  ? 0.7077 0.5014 0.5772 0.1236  0.1178  -0.0880 80  ASN A CG  
735   O OD1 . ASN A  54  ? 0.7383 0.5180 0.5997 0.1181  0.1156  -0.0908 80  ASN A OD1 
736   N ND2 . ASN A  54  ? 0.7311 0.5220 0.5950 0.1274  0.1254  -0.0927 80  ASN A ND2 
743   N N   . GLU A  55  ? 0.6102 0.4001 0.4951 0.1190  0.1016  -0.0751 81  GLU A N   
744   C CA  . GLU A  55  ? 0.6213 0.3966 0.5072 0.1221  0.1018  -0.0729 81  GLU A CA  
745   C C   . GLU A  55  ? 0.6073 0.3913 0.5022 0.1190  0.0934  -0.0661 81  GLU A C   
746   O O   . GLU A  55  ? 0.6113 0.3854 0.5084 0.1218  0.0930  -0.0631 81  GLU A O   
747   C CB  . GLU A  55  ? 0.6783 0.4312 0.5480 0.1164  0.1047  -0.0805 81  GLU A CB  
748   C CG  . GLU A  55  ? 0.7733 0.5148 0.6331 0.1197  0.1136  -0.0876 81  GLU A CG  
749   C CD  . GLU A  55  ? 0.9088 0.6257 0.7530 0.1152  0.1173  -0.0948 81  GLU A CD  
750   O OE1 . GLU A  55  ? 0.9341 0.6365 0.7717 0.1207  0.1257  -0.0994 81  GLU A OE1 
751   O OE2 . GLU A  55  ? 0.9568 0.6687 0.7953 0.1060  0.1121  -0.0960 81  GLU A OE2 
758   N N   . SER A  56  ? 0.5870 0.3888 0.4867 0.1134  0.0871  -0.0636 82  SER A N   
759   C CA  . SER A  56  ? 0.5820 0.3921 0.4895 0.1100  0.0794  -0.0577 82  SER A CA  
760   C C   . SER A  56  ? 0.5808 0.3982 0.5025 0.1186  0.0787  -0.0498 82  SER A C   
761   O O   . SER A  56  ? 0.5813 0.3944 0.5061 0.1184  0.0753  -0.0460 82  SER A O   
762   C CB  . SER A  56  ? 0.5762 0.4038 0.4860 0.1030  0.0737  -0.0568 82  SER A CB  
763   O OG  . SER A  56  ? 0.5908 0.4130 0.4880 0.0942  0.0729  -0.0631 82  SER A OG  
769   N N   . PHE A  57  ? 0.5780 0.4072 0.5084 0.1260  0.0818  -0.0474 83  PHE A N   
770   C CA  . PHE A  57  ? 0.5824 0.4207 0.5269 0.1343  0.0811  -0.0399 83  PHE A CA  
771   C C   . PHE A  57  ? 0.6093 0.4388 0.5551 0.1449  0.0890  -0.0403 83  PHE A C   
772   O O   . PHE A  57  ? 0.5979 0.4393 0.5552 0.1526  0.0905  -0.0356 83  PHE A O   
773   C CB  . PHE A  57  ? 0.5589 0.4200 0.5140 0.1340  0.0779  -0.0359 83  PHE A CB  
774   C CG  . PHE A  57  ? 0.5556 0.4249 0.5095 0.1243  0.0707  -0.0354 83  PHE A CG  
775   C CD1 . PHE A  57  ? 0.5581 0.4295 0.5167 0.1215  0.0645  -0.0308 83  PHE A CD1 
776   C CD2 . PHE A  57  ? 0.5607 0.4349 0.5083 0.1179  0.0702  -0.0396 83  PHE A CD2 
777   C CE1 . PHE A  57  ? 0.5616 0.4399 0.5190 0.1129  0.0584  -0.0305 83  PHE A CE1 
778   C CE2 . PHE A  57  ? 0.5627 0.4440 0.5092 0.1095  0.0637  -0.0389 83  PHE A CE2 
779   C CZ  . PHE A  57  ? 0.5586 0.4419 0.5102 0.1072  0.0580  -0.0345 83  PHE A CZ  
789   N N   . GLN A  58  ? 0.6415 0.4500 0.5755 0.1451  0.0940  -0.0459 84  GLN A N   
790   C CA  . GLN A  58  ? 0.6725 0.4700 0.6059 0.1551  0.1022  -0.0471 84  GLN A CA  
791   C C   . GLN A  58  ? 0.6852 0.4822 0.6293 0.1637  0.1016  -0.0396 84  GLN A C   
792   O O   . GLN A  58  ? 0.6921 0.4834 0.6359 0.1605  0.0968  -0.0367 84  GLN A O   
793   C CB  . GLN A  58  ? 0.7191 0.4923 0.6361 0.1520  0.1073  -0.0552 84  GLN A CB  
794   C CG  . GLN A  58  ? 0.7962 0.5616 0.7072 0.1577  0.1166  -0.0609 84  GLN A CG  
795   C CD  . GLN A  58  ? 0.8942 0.6333 0.7897 0.1559  0.1221  -0.0682 84  GLN A CD  
796   O OE1 . GLN A  58  ? 0.9159 0.6423 0.8093 0.1644  0.1300  -0.0699 84  GLN A OE1 
797   N NE2 . GLN A  58  ? 0.9202 0.6505 0.8042 0.1448  0.1184  -0.0727 84  GLN A NE2 
806   N N   . GLY A  59  ? 0.6859 0.4899 0.6396 0.1743  0.1062  -0.0364 85  GLY A N   
807   C CA  . GLY A  59  ? 0.6931 0.4986 0.6577 0.1835  0.1059  -0.0288 85  GLY A CA  
808   C C   . GLY A  59  ? 0.6902 0.5151 0.6676 0.1820  0.0977  -0.0209 85  GLY A C   
809   O O   . GLY A  59  ? 0.6970 0.5218 0.6817 0.1875  0.0959  -0.0145 85  GLY A O   
813   N N   . LEU A  60  ? 0.6743 0.5159 0.6543 0.1745  0.0928  -0.0212 86  LEU A N   
814   C CA  . LEU A  60  ? 0.6596 0.5197 0.6510 0.1722  0.0853  -0.0143 86  LEU A CA  
815   C C   . LEU A  60  ? 0.6420 0.5237 0.6444 0.1756  0.0863  -0.0120 86  LEU A C   
816   O O   . LEU A  60  ? 0.6306 0.5265 0.6358 0.1691  0.0817  -0.0115 86  LEU A O   
817   C CB  . LEU A  60  ? 0.6635 0.5243 0.6485 0.1601  0.0785  -0.0162 86  LEU A CB  
818   C CG  . LEU A  60  ? 0.6904 0.5318 0.6644 0.1548  0.0769  -0.0188 86  LEU A CG  
819   C CD1 . LEU A  60  ? 0.6955 0.5416 0.6652 0.1434  0.0703  -0.0203 86  LEU A CD1 
820   C CD2 . LEU A  60  ? 0.7004 0.5362 0.6794 0.1599  0.0751  -0.0125 86  LEU A CD2 
832   N N   . GLN A  61  ? 0.6364 0.5203 0.6452 0.1860  0.0923  -0.0105 87  GLN A N   
833   C CA  . GLN A  61  ? 0.6258 0.5296 0.6454 0.1899  0.0943  -0.0084 87  GLN A CA  
834   C C   . GLN A  61  ? 0.6019 0.5272 0.6356 0.1894  0.0878  -0.0008 87  GLN A C   
835   O O   . GLN A  61  ? 0.5966 0.5392 0.6373 0.1888  0.0879  0.0002  87  GLN A O   
836   C CB  . GLN A  61  ? 0.6555 0.5561 0.6789 0.2018  0.1027  -0.0083 87  GLN A CB  
837   C CG  . GLN A  61  ? 0.7264 0.6081 0.7360 0.2024  0.1104  -0.0166 87  GLN A CG  
838   C CD  . GLN A  61  ? 0.8009 0.6880 0.8037 0.1948  0.1111  -0.0224 87  GLN A CD  
839   O OE1 . GLN A  61  ? 0.8120 0.7183 0.8230 0.1945  0.1106  -0.0204 87  GLN A OE1 
840   N NE2 . GLN A  61  ? 0.8224 0.6933 0.8099 0.1880  0.1122  -0.0295 87  GLN A NE2 
849   N N   . ASN A  62  ? 0.5878 0.5119 0.6252 0.1893  0.0823  0.0044  88  ASN A N   
850   C CA  . ASN A  62  ? 0.5734 0.5173 0.6232 0.1879  0.0759  0.0113  88  ASN A CA  
851   C C   . ASN A  62  ? 0.5410 0.4934 0.5884 0.1766  0.0699  0.0099  88  ASN A C   
852   O O   . ASN A  62  ? 0.5325 0.5019 0.5895 0.1746  0.0650  0.0147  88  ASN A O   
853   C CB  . ASN A  62  ? 0.6198 0.5597 0.6736 0.1913  0.0719  0.0174  88  ASN A CB  
854   C CG  . ASN A  62  ? 0.7177 0.6592 0.7801 0.2033  0.0760  0.0220  88  ASN A CG  
855   O OD1 . ASN A  62  ? 0.7247 0.6856 0.7999 0.2075  0.0755  0.0266  88  ASN A OD1 
856   N ND2 . ASN A  62  ? 0.7823 0.7057 0.8398 0.2094  0.0792  0.0222  88  ASN A ND2 
863   N N   . LEU A  63  ? 0.5208 0.4619 0.5555 0.1692  0.0701  0.0035  89  LEU A N   
864   C CA  . LEU A  63  ? 0.5009 0.4495 0.5333 0.1590  0.0646  0.0024  89  LEU A CA  
865   C C   . LEU A  63  ? 0.4684 0.4356 0.5079 0.1579  0.0651  0.0031  89  LEU A C   
866   O O   . LEU A  63  ? 0.4679 0.4352 0.5046 0.1599  0.0706  -0.0007 89  LEU A O   
867   C CB  . LEU A  63  ? 0.5150 0.4487 0.5327 0.1518  0.0650  -0.0045 89  LEU A CB  
868   C CG  . LEU A  63  ? 0.5376 0.4535 0.5469 0.1493  0.0632  -0.0057 89  LEU A CG  
869   C CD1 . LEU A  63  ? 0.5540 0.4571 0.5492 0.1422  0.0643  -0.0130 89  LEU A CD1 
870   C CD2 . LEU A  63  ? 0.5360 0.4574 0.5498 0.1449  0.0557  -0.0008 89  LEU A CD2 
882   N N   . THR A  64  ? 0.4450 0.4273 0.4929 0.1542  0.0594  0.0078  90  THR A N   
883   C CA  . THR A  64  ? 0.4279 0.4277 0.4822 0.1515  0.0587  0.0089  90  THR A CA  
884   C C   . THR A  64  ? 0.4100 0.4106 0.4581 0.1412  0.0541  0.0066  90  THR A C   
885   O O   . THR A  64  ? 0.4097 0.4213 0.4599 0.1381  0.0544  0.0063  90  THR A O   
886   C CB  . THR A  64  ? 0.4378 0.4547 0.5064 0.1546  0.0559  0.0158  90  THR A CB  
887   O OG1 . THR A  64  ? 0.4533 0.4712 0.5231 0.1497  0.0489  0.0190  90  THR A OG1 
888   C CG2 . THR A  64  ? 0.4435 0.4608 0.5193 0.1652  0.0599  0.0188  90  THR A CG2 
896   N N   . LYS A  65  ? 0.4003 0.3899 0.4411 0.1362  0.0500  0.0055  91  LYS A N   
897   C CA  . LYS A  65  ? 0.3878 0.3784 0.4234 0.1271  0.0456  0.0038  91  LYS A CA  
898   C C   . LYS A  65  ? 0.3806 0.3543 0.4043 0.1232  0.0448  -0.0004 91  LYS A C   
899   O O   . LYS A  65  ? 0.3936 0.3575 0.4160 0.1254  0.0440  0.0006  91  LYS A O   
900   C CB  . LYS A  65  ? 0.4026 0.4045 0.4463 0.1237  0.0394  0.0090  91  LYS A CB  
901   C CG  . LYS A  65  ? 0.4638 0.4658 0.5024 0.1147  0.0346  0.0077  91  LYS A CG  
902   C CD  . LYS A  65  ? 0.5126 0.5268 0.5596 0.1117  0.0294  0.0125  91  LYS A CD  
903   C CE  . LYS A  65  ? 0.5594 0.5728 0.6016 0.1035  0.0250  0.0114  91  LYS A CE  
904   N NZ  . LYS A  65  ? 0.5719 0.5939 0.6209 0.1007  0.0200  0.0158  91  LYS A NZ  
918   N N   . ILE A  66  ? 0.3631 0.3339 0.3783 0.1172  0.0447  -0.0048 92  ILE A N   
919   C CA  . ILE A  66  ? 0.3636 0.3206 0.3677 0.1120  0.0432  -0.0089 92  ILE A CA  
920   C C   . ILE A  66  ? 0.3519 0.3154 0.3541 0.1040  0.0386  -0.0092 92  ILE A C   
921   O O   . ILE A  66  ? 0.3474 0.3196 0.3500 0.1023  0.0394  -0.0099 92  ILE A O   
922   C CB  . ILE A  66  ? 0.3775 0.3220 0.3710 0.1132  0.0488  -0.0151 92  ILE A CB  
923   C CG1 . ILE A  66  ? 0.3904 0.3252 0.3847 0.1213  0.0536  -0.0151 92  ILE A CG1 
924   C CG2 . ILE A  66  ? 0.3878 0.3210 0.3697 0.1057  0.0464  -0.0195 92  ILE A CG2 
925   C CD1 . ILE A  66  ? 0.4140 0.3397 0.4002 0.1241  0.0604  -0.0207 92  ILE A CD1 
937   N N   . ASN A  67  ? 0.3443 0.3027 0.3436 0.0991  0.0340  -0.0088 93  ASN A N   
938   C CA  . ASN A  67  ? 0.3332 0.2965 0.3301 0.0917  0.0297  -0.0093 93  ASN A CA  
939   C C   . ASN A  67  ? 0.3371 0.2877 0.3226 0.0869  0.0293  -0.0141 93  ASN A C   
940   O O   . ASN A  67  ? 0.3420 0.2831 0.3249 0.0861  0.0279  -0.0143 93  ASN A O   
941   C CB  . ASN A  67  ? 0.3325 0.3035 0.3371 0.0896  0.0245  -0.0043 93  ASN A CB  
942   C CG  . ASN A  67  ? 0.3589 0.3337 0.3612 0.0824  0.0202  -0.0047 93  ASN A CG  
943   O OD1 . ASN A  67  ? 0.3734 0.3447 0.3680 0.0785  0.0204  -0.0085 93  ASN A OD1 
944   N ND2 . ASN A  67  ? 0.3525 0.3349 0.3612 0.0805  0.0162  -0.0008 93  ASN A ND2 
951   N N   . LEU A  68  ? 0.3342 0.2848 0.3128 0.0838  0.0307  -0.0181 94  LEU A N   
952   C CA  . LEU A  68  ? 0.3376 0.2782 0.3053 0.0785  0.0301  -0.0230 94  LEU A CA  
953   C C   . LEU A  68  ? 0.3402 0.2884 0.3061 0.0717  0.0258  -0.0231 94  LEU A C   
954   O O   . LEU A  68  ? 0.3560 0.2997 0.3131 0.0671  0.0256  -0.0271 94  LEU A O   
955   C CB  . LEU A  68  ? 0.3357 0.2689 0.2954 0.0806  0.0357  -0.0281 94  LEU A CB  
956   C CG  . LEU A  68  ? 0.3449 0.2641 0.3013 0.0853  0.0399  -0.0301 94  LEU A CG  
957   C CD1 . LEU A  68  ? 0.3505 0.2666 0.3025 0.0894  0.0462  -0.0338 94  LEU A CD1 
958   C CD2 . LEU A  68  ? 0.3551 0.2606 0.3025 0.0802  0.0384  -0.0335 94  LEU A CD2 
970   N N   . ASN A  69  ? 0.3306 0.2897 0.3047 0.0707  0.0223  -0.0186 95  ASN A N   
971   C CA  . ASN A  69  ? 0.3335 0.2998 0.3068 0.0651  0.0184  -0.0181 95  ASN A CA  
972   C C   . ASN A  69  ? 0.3474 0.3072 0.3145 0.0594  0.0153  -0.0203 95  ASN A C   
973   O O   . ASN A  69  ? 0.3401 0.2922 0.3068 0.0592  0.0145  -0.0202 95  ASN A O   
974   C CB  . ASN A  69  ? 0.3296 0.3065 0.3128 0.0653  0.0154  -0.0129 95  ASN A CB  
975   C CG  . ASN A  69  ? 0.3374 0.3236 0.3275 0.0694  0.0177  -0.0101 95  ASN A CG  
976   O OD1 . ASN A  69  ? 0.3524 0.3464 0.3507 0.0700  0.0158  -0.0061 95  ASN A OD1 
977   N ND2 . ASN A  69  ? 0.3023 0.2880 0.2899 0.0725  0.0220  -0.0123 95  ASN A ND2 
984   N N   . HIS A  70  ? 0.3603 0.3243 0.3230 0.0546  0.0133  -0.0219 96  HIS A N   
985   C CA  . HIS A  70  ? 0.3863 0.3471 0.3443 0.0487  0.0099  -0.0236 96  HIS A CA  
986   C C   . HIS A  70  ? 0.4073 0.3547 0.3572 0.0473  0.0116  -0.0279 96  HIS A C   
987   O O   . HIS A  70  ? 0.4042 0.3454 0.3539 0.0454  0.0099  -0.0277 96  HIS A O   
988   C CB  . HIS A  70  ? 0.4060 0.3709 0.3709 0.0471  0.0060  -0.0196 96  HIS A CB  
989   C CG  . HIS A  70  ? 0.4559 0.4314 0.4297 0.0496  0.0051  -0.0151 96  HIS A CG  
990   N ND1 . HIS A  70  ? 0.4863 0.4710 0.4612 0.0481  0.0042  -0.0140 96  HIS A ND1 
991   C CD2 . HIS A  70  ? 0.4710 0.4489 0.4526 0.0528  0.0050  -0.0114 96  HIS A CD2 
992   C CE1 . HIS A  70  ? 0.4867 0.4782 0.4696 0.0504  0.0039  -0.0101 96  HIS A CE1 
993   N NE2 . HIS A  70  ? 0.4823 0.4706 0.4695 0.0531  0.0041  -0.0085 96  HIS A NE2 
1001  N N   . ASN A  71  ? 0.4253 0.3680 0.3681 0.0481  0.0152  -0.0320 97  ASN A N   
1002  C CA  . ASN A  71  ? 0.4590 0.3881 0.3927 0.0466  0.0176  -0.0369 97  ASN A CA  
1003  C C   . ASN A  71  ? 0.5072 0.4362 0.4312 0.0427  0.0186  -0.0417 97  ASN A C   
1004  O O   . ASN A  71  ? 0.5059 0.4395 0.4292 0.0455  0.0211  -0.0421 97  ASN A O   
1005  C CB  . ASN A  71  ? 0.4614 0.3827 0.3962 0.0535  0.0226  -0.0371 97  ASN A CB  
1006  C CG  . ASN A  71  ? 0.4778 0.3918 0.4167 0.0560  0.0223  -0.0346 97  ASN A CG  
1007  O OD1 . ASN A  71  ? 0.4903 0.4088 0.4381 0.0611  0.0224  -0.0302 97  ASN A OD1 
1008  N ND2 . ASN A  71  ? 0.4647 0.3677 0.3970 0.0519  0.0217  -0.0374 97  ASN A ND2 
1015  N N   . PRO A  72  ? 0.5447 0.4684 0.4606 0.0362  0.0168  -0.0455 98  PRO A N   
1016  C CA  . PRO A  72  ? 0.5736 0.4914 0.4887 0.0317  0.0139  -0.0457 98  PRO A CA  
1017  C C   . PRO A  72  ? 0.6056 0.5344 0.5283 0.0293  0.0088  -0.0412 98  PRO A C   
1018  O O   . PRO A  72  ? 0.6060 0.5467 0.5338 0.0306  0.0073  -0.0383 98  PRO A O   
1019  C CB  . PRO A  72  ? 0.5874 0.4988 0.4909 0.0251  0.0140  -0.0517 98  PRO A CB  
1020  C CG  . PRO A  72  ? 0.5888 0.5012 0.4864 0.0269  0.0175  -0.0549 98  PRO A CG  
1021  C CD  . PRO A  72  ? 0.5509 0.4753 0.4572 0.0322  0.0174  -0.0501 98  PRO A CD  
1029  N N   . ASN A  73  ? 0.6302 0.5546 0.5533 0.0257  0.0064  -0.0408 99  ASN A N   
1030  C CA  . ASN A  73  ? 0.6521 0.5852 0.5817 0.0231  0.0019  -0.0370 99  ASN A CA  
1031  C C   . ASN A  73  ? 0.6615 0.6001 0.6013 0.0286  0.0016  -0.0316 99  ASN A C   
1032  O O   . ASN A  73  ? 0.6694 0.6023 0.6123 0.0303  0.0017  -0.0296 99  ASN A O   
1033  C CB  . ASN A  73  ? 0.6719 0.6168 0.6007 0.0190  -0.0011 -0.0373 99  ASN A CB  
1034  C CG  . ASN A  73  ? 0.7323 0.6736 0.6510 0.0131  -0.0013 -0.0425 99  ASN A CG  
1035  O OD1 . ASN A  73  ? 0.7587 0.6883 0.6711 0.0105  0.0002  -0.0462 99  ASN A OD1 
1036  N ND2 . ASN A  73  ? 0.7438 0.6952 0.6608 0.0107  -0.0031 -0.0430 99  ASN A ND2 
1043  N N   . GLY A  87  ? 0.5518 0.4888 0.4327 0.0209  0.0171  -0.0601 113 GLY A N   
1044  C CA  . GLY A  87  ? 0.5456 0.4844 0.4347 0.0286  0.0201  -0.0564 113 GLY A CA  
1045  C C   . GLY A  87  ? 0.5406 0.4662 0.4277 0.0330  0.0257  -0.0592 113 GLY A C   
1046  O O   . GLY A  87  ? 0.5571 0.4711 0.4348 0.0303  0.0279  -0.0647 113 GLY A O   
1049  N N   . LEU A  88  ? 0.5138 0.4412 0.4098 0.0401  0.0281  -0.0554 114 LEU A N   
1050  C CA  . LEU A  88  ? 0.4966 0.4129 0.3924 0.0457  0.0335  -0.0570 114 LEU A CA  
1051  C C   . LEU A  88  ? 0.4849 0.3983 0.3725 0.0474  0.0387  -0.0614 114 LEU A C   
1052  O O   . LEU A  88  ? 0.4787 0.4023 0.3677 0.0488  0.0393  -0.0598 114 LEU A O   
1053  C CB  . LEU A  88  ? 0.4861 0.4082 0.3947 0.0525  0.0339  -0.0512 114 LEU A CB  
1054  C CG  . LEU A  88  ? 0.4996 0.4121 0.4107 0.0593  0.0390  -0.0514 114 LEU A CG  
1055  C CD1 . LEU A  88  ? 0.5023 0.4005 0.4095 0.0576  0.0388  -0.0535 114 LEU A CD1 
1056  C CD2 . LEU A  88  ? 0.4991 0.4206 0.4232 0.0653  0.0387  -0.0452 114 LEU A CD2 
1068  N N   . ASN A  89  ? 0.4766 0.3757 0.3554 0.0471  0.0428  -0.0670 115 ASN A N   
1069  C CA  . ASN A  89  ? 0.4702 0.3649 0.3401 0.0487  0.0484  -0.0718 115 ASN A CA  
1070  C C   . ASN A  89  ? 0.4606 0.3483 0.3352 0.0573  0.0545  -0.0712 115 ASN A C   
1071  O O   . ASN A  89  ? 0.4566 0.3315 0.3306 0.0592  0.0564  -0.0725 115 ASN A O   
1072  C CB  . ASN A  89  ? 0.4883 0.3727 0.3436 0.0414  0.0488  -0.0790 115 ASN A CB  
1073  C CG  . ASN A  89  ? 0.5381 0.4104 0.3833 0.0432  0.0556  -0.0852 115 ASN A CG  
1074  O OD1 . ASN A  89  ? 0.5365 0.4107 0.3840 0.0497  0.0605  -0.0847 115 ASN A OD1 
1075  N ND2 . ASN A  89  ? 0.5717 0.4323 0.4043 0.0372  0.0565  -0.0918 115 ASN A ND2 
1082  N N   . ILE A  90  ? 0.4551 0.3519 0.3351 0.0627  0.0573  -0.0687 116 ILE A N   
1083  C CA  . ILE A  90  ? 0.4627 0.3565 0.3486 0.0714  0.0631  -0.0676 116 ILE A CA  
1084  C C   . ILE A  90  ? 0.4872 0.3766 0.3636 0.0730  0.0696  -0.0730 116 ILE A C   
1085  O O   . ILE A  90  ? 0.4881 0.3872 0.3617 0.0710  0.0696  -0.0732 116 ILE A O   
1086  C CB  . ILE A  90  ? 0.4495 0.3586 0.3495 0.0760  0.0614  -0.0604 116 ILE A CB  
1087  C CG1 . ILE A  90  ? 0.4544 0.3689 0.3628 0.0734  0.0546  -0.0553 116 ILE A CG1 
1088  C CG2 . ILE A  90  ? 0.4496 0.3570 0.3567 0.0851  0.0672  -0.0588 116 ILE A CG2 
1089  C CD1 . ILE A  90  ? 0.4620 0.3911 0.3832 0.0766  0.0525  -0.0487 116 ILE A CD1 
1101  N N   . THR A  91  ? 0.5007 0.3756 0.3722 0.0768  0.0755  -0.0771 117 THR A N   
1102  C CA  . THR A  91  ? 0.5210 0.3903 0.3831 0.0787  0.0824  -0.0827 117 THR A CA  
1103  C C   . THR A  91  ? 0.5188 0.3982 0.3898 0.0866  0.0868  -0.0793 117 THR A C   
1104  O O   . THR A  91  ? 0.5001 0.3871 0.3846 0.0917  0.0855  -0.0732 117 THR A O   
1105  C CB  . THR A  91  ? 0.5653 0.4145 0.4195 0.0805  0.0876  -0.0882 117 THR A CB  
1106  O OG1 . THR A  91  ? 0.5880 0.4343 0.4534 0.0883  0.0890  -0.0838 117 THR A OG1 
1107  C CG2 . THR A  91  ? 0.5794 0.4177 0.4231 0.0718  0.0840  -0.0925 117 THR A CG2 
1115  N N   . ASP A  92  ? 0.5354 0.4153 0.3988 0.0873  0.0922  -0.0834 118 ASP A N   
1116  C CA  . ASP A  92  ? 0.5524 0.4416 0.4227 0.0943  0.0973  -0.0810 118 ASP A CA  
1117  C C   . ASP A  92  ? 0.5536 0.4362 0.4322 0.1036  0.1023  -0.0795 118 ASP A C   
1118  O O   . ASP A  92  ? 0.5692 0.4355 0.4409 0.1054  0.1064  -0.0842 118 ASP A O   
1119  C CB  . ASP A  92  ? 0.6118 0.4986 0.4692 0.0929  0.1030  -0.0871 118 ASP A CB  
1120  C CG  . ASP A  92  ? 0.7214 0.6179 0.5842 0.0993  0.1089  -0.0854 118 ASP A CG  
1121  O OD1 . ASP A  92  ? 0.7433 0.6488 0.6205 0.1053  0.1090  -0.0794 118 ASP A OD1 
1122  O OD2 . ASP A  92  ? 0.7725 0.6678 0.6247 0.0980  0.1136  -0.0902 118 ASP A OD2 
1127  N N   . GLY A  93  ? 0.5404 0.4354 0.4336 0.1093  0.1018  -0.0730 119 GLY A N   
1128  C CA  . GLY A  93  ? 0.5420 0.4340 0.4449 0.1186  0.1060  -0.0704 119 GLY A CA  
1129  C C   . GLY A  93  ? 0.5486 0.4303 0.4546 0.1195  0.1028  -0.0687 119 GLY A C   
1130  O O   . GLY A  93  ? 0.5566 0.4302 0.4663 0.1269  0.1073  -0.0684 119 GLY A O   
1134  N N   . ALA A  94  ? 0.5451 0.4273 0.4503 0.1124  0.0952  -0.0672 120 ALA A N   
1135  C CA  . ALA A  94  ? 0.5506 0.4231 0.4583 0.1126  0.0921  -0.0654 120 ALA A CA  
1136  C C   . ALA A  94  ? 0.5427 0.4222 0.4658 0.1205  0.0917  -0.0584 120 ALA A C   
1137  O O   . ALA A  94  ? 0.5546 0.4229 0.4792 0.1250  0.0934  -0.0578 120 ALA A O   
1138  C CB  . ALA A  94  ? 0.5494 0.4239 0.4545 0.1035  0.0842  -0.0646 120 ALA A CB  
1144  N N   . PHE A  95  ? 0.5200 0.4176 0.4542 0.1218  0.0894  -0.0530 121 PHE A N   
1145  C CA  . PHE A  95  ? 0.5089 0.4160 0.4582 0.1284  0.0883  -0.0461 121 PHE A CA  
1146  C C   . PHE A  95  ? 0.5142 0.4274 0.4701 0.1372  0.0953  -0.0452 121 PHE A C   
1147  O O   . PHE A  95  ? 0.5050 0.4287 0.4741 0.1426  0.0946  -0.0394 121 PHE A O   
1148  C CB  . PHE A  95  ? 0.4868 0.4109 0.4447 0.1239  0.0815  -0.0407 121 PHE A CB  
1149  C CG  . PHE A  95  ? 0.4830 0.4049 0.4366 0.1155  0.0744  -0.0406 121 PHE A CG  
1150  C CD1 . PHE A  95  ? 0.4879 0.4080 0.4471 0.1152  0.0697  -0.0368 121 PHE A CD1 
1151  C CD2 . PHE A  95  ? 0.4845 0.4092 0.4302 0.1081  0.0721  -0.0435 121 PHE A CD2 
1152  C CE1 . PHE A  95  ? 0.4906 0.4100 0.4466 0.1076  0.0633  -0.0365 121 PHE A CE1 
1153  C CE2 . PHE A  95  ? 0.4919 0.4160 0.4347 0.1008  0.0656  -0.0431 121 PHE A CE2 
1154  C CZ  . PHE A  95  ? 0.4899 0.4113 0.4380 0.1005  0.0614  -0.0397 121 PHE A CZ  
1164  N N   . LEU A  96  ? 0.5318 0.4397 0.4790 0.1384  0.1019  -0.0508 122 LEU A N   
1165  C CA  . LEU A  96  ? 0.5408 0.4553 0.4936 0.1463  0.1089  -0.0504 122 LEU A CA  
1166  C C   . LEU A  96  ? 0.5542 0.4649 0.5159 0.1564  0.1127  -0.0475 122 LEU A C   
1167  O O   . LEU A  96  ? 0.5471 0.4709 0.5206 0.1628  0.1152  -0.0434 122 LEU A O   
1168  C CB  . LEU A  96  ? 0.5482 0.4544 0.4875 0.1452  0.1156  -0.0580 122 LEU A CB  
1169  C CG  . LEU A  96  ? 0.5610 0.4764 0.5044 0.1515  0.1229  -0.0582 122 LEU A CG  
1170  C CD1 . LEU A  96  ? 0.5539 0.4899 0.5055 0.1486  0.1197  -0.0537 122 LEU A CD1 
1171  C CD2 . LEU A  96  ? 0.5750 0.4790 0.5032 0.1503  0.1296  -0.0663 122 LEU A CD2 
1183  N N   . ASN A  97  ? 0.5756 0.4689 0.5320 0.1578  0.1131  -0.0493 123 ASN A N   
1184  C CA  . ASN A  97  ? 0.5933 0.4810 0.5572 0.1679  0.1168  -0.0464 123 ASN A CA  
1185  C C   . ASN A  97  ? 0.5868 0.4877 0.5664 0.1710  0.1112  -0.0377 123 ASN A C   
1186  O O   . ASN A  97  ? 0.5914 0.4924 0.5795 0.1801  0.1142  -0.0341 123 ASN A O   
1187  C CB  . ASN A  97  ? 0.6359 0.4995 0.5883 0.1681  0.1191  -0.0509 123 ASN A CB  
1188  C CG  . ASN A  97  ? 0.7088 0.5660 0.6617 0.1641  0.1121  -0.0478 123 ASN A CG  
1189  O OD1 . ASN A  97  ? 0.7383 0.5865 0.6947 0.1701  0.1130  -0.0450 123 ASN A OD1 
1190  N ND2 . ASN A  97  ? 0.7227 0.5847 0.6723 0.1542  0.1050  -0.0479 123 ASN A ND2 
1197  N N   . LEU A  98  ? 0.5752 0.4863 0.5580 0.1636  0.1032  -0.0345 124 LEU A N   
1198  C CA  . LEU A  98  ? 0.5644 0.4879 0.5609 0.1653  0.0975  -0.0267 124 LEU A CA  
1199  C C   . LEU A  98  ? 0.5558 0.5002 0.5649 0.1691  0.0988  -0.0226 124 LEU A C   
1200  O O   . LEU A  98  ? 0.5563 0.5137 0.5676 0.1632  0.0955  -0.0216 124 LEU A O   
1201  C CB  . LEU A  98  ? 0.5635 0.4887 0.5575 0.1555  0.0891  -0.0256 124 LEU A CB  
1202  C CG  . LEU A  98  ? 0.5844 0.4905 0.5660 0.1505  0.0873  -0.0296 124 LEU A CG  
1203  C CD1 . LEU A  98  ? 0.5866 0.4973 0.5665 0.1409  0.0794  -0.0285 124 LEU A CD1 
1204  C CD2 . LEU A  98  ? 0.5894 0.4834 0.5730 0.1568  0.0884  -0.0272 124 LEU A CD2 
1216  N N   . LYS A  99  ? 0.5438 0.4914 0.5617 0.1791  0.1038  -0.0199 125 LYS A N   
1217  C CA  . LYS A  99  ? 0.5340 0.5009 0.5641 0.1838  0.1064  -0.0164 125 LYS A CA  
1218  C C   . LYS A  99  ? 0.5109 0.4970 0.5546 0.1820  0.0998  -0.0091 125 LYS A C   
1219  O O   . LYS A  99  ? 0.5052 0.5082 0.5572 0.1827  0.1012  -0.0070 125 LYS A O   
1220  C CB  . LYS A  99  ? 0.5737 0.5379 0.6090 0.1955  0.1141  -0.0158 125 LYS A CB  
1221  C CG  . LYS A  99  ? 0.6588 0.6063 0.6812 0.1978  0.1222  -0.0235 125 LYS A CG  
1222  C CD  . LYS A  99  ? 0.7327 0.6895 0.7532 0.1966  0.1273  -0.0270 125 LYS A CD  
1223  C CE  . LYS A  99  ? 0.7941 0.7628 0.8264 0.2068  0.1338  -0.0242 125 LYS A CE  
1224  N NZ  . LYS A  99  ? 0.8337 0.8108 0.8634 0.2054  0.1392  -0.0277 125 LYS A NZ  
1238  N N   . ASN A  100 ? 0.4993 0.4835 0.5455 0.1795  0.0930  -0.0054 126 ASN A N   
1239  C CA  . ASN A  100 ? 0.4871 0.4891 0.5452 0.1769  0.0865  0.0011  126 ASN A CA  
1240  C C   . ASN A  100 ? 0.4710 0.4730 0.5234 0.1659  0.0796  0.0003  126 ASN A C   
1241  O O   . ASN A  100 ? 0.4608 0.4739 0.5210 0.1629  0.0736  0.0052  126 ASN A O   
1242  C CB  . ASN A  100 ? 0.5132 0.5160 0.5804 0.1831  0.0840  0.0071  126 ASN A CB  
1243  C CG  . ASN A  100 ? 0.5602 0.5840 0.6417 0.1828  0.0790  0.0141  126 ASN A CG  
1244  O OD1 . ASN A  100 ? 0.5621 0.5974 0.6456 0.1754  0.0751  0.0147  126 ASN A OD1 
1245  N ND2 . ASN A  100 ? 0.5659 0.5951 0.6578 0.1906  0.0788  0.0196  126 ASN A ND2 
1252  N N   . LEU A  101 ? 0.4650 0.4555 0.5041 0.1599  0.0802  -0.0056 127 LEU A N   
1253  C CA  . LEU A  101 ? 0.4561 0.4470 0.4901 0.1501  0.0739  -0.0063 127 LEU A CA  
1254  C C   . LEU A  101 ? 0.4414 0.4502 0.4820 0.1464  0.0723  -0.0040 127 LEU A C   
1255  O O   . LEU A  101 ? 0.4439 0.4572 0.4829 0.1471  0.0770  -0.0063 127 LEU A O   
1256  C CB  . LEU A  101 ? 0.4654 0.4410 0.4841 0.1450  0.0752  -0.0131 127 LEU A CB  
1257  C CG  . LEU A  101 ? 0.4756 0.4501 0.4884 0.1353  0.0687  -0.0138 127 LEU A CG  
1258  C CD1 . LEU A  101 ? 0.4785 0.4478 0.4932 0.1339  0.0632  -0.0108 127 LEU A CD1 
1259  C CD2 . LEU A  101 ? 0.4923 0.4548 0.4906 0.1305  0.0706  -0.0205 127 LEU A CD2 
1271  N N   . ARG A  102 ? 0.4222 0.4410 0.4700 0.1425  0.0661  0.0007  128 ARG A N   
1272  C CA  . ARG A  102 ? 0.4110 0.4460 0.4653 0.1384  0.0641  0.0034  128 ARG A CA  
1273  C C   . ARG A  102 ? 0.3958 0.4292 0.4435 0.1292  0.0590  0.0021  128 ARG A C   
1274  O O   . ARG A  102 ? 0.3944 0.4351 0.4412 0.1252  0.0594  0.0015  128 ARG A O   
1275  C CB  . ARG A  102 ? 0.4271 0.4759 0.4953 0.1409  0.0609  0.0098  128 ARG A CB  
1276  C CG  . ARG A  102 ? 0.4863 0.5399 0.5633 0.1505  0.0654  0.0122  128 ARG A CG  
1277  C CD  . ARG A  102 ? 0.5552 0.6191 0.6360 0.1533  0.0714  0.0113  128 ARG A CD  
1278  N NE  . ARG A  102 ? 0.6277 0.6955 0.7165 0.1631  0.0764  0.0132  128 ARG A NE  
1279  C CZ  . ARG A  102 ? 0.6719 0.7465 0.7638 0.1675  0.0829  0.0121  128 ARG A CZ  
1280  N NH1 . ARG A  102 ? 0.6662 0.7445 0.7535 0.1627  0.0852  0.0092  128 ARG A NH1 
1281  N NH2 . ARG A  102 ? 0.6808 0.7589 0.7805 0.1770  0.0874  0.0140  128 ARG A NH2 
1295  N N   . GLU A  103 ? 0.3855 0.4099 0.4291 0.1259  0.0542  0.0021  129 GLU A N   
1296  C CA  . GLU A  103 ? 0.3765 0.4000 0.4149 0.1177  0.0492  0.0013  129 GLU A CA  
1297  C C   . GLU A  103 ? 0.3758 0.3835 0.4016 0.1147  0.0490  -0.0036 129 GLU A C   
1298  O O   . GLU A  103 ? 0.3908 0.3877 0.4140 0.1171  0.0489  -0.0043 129 GLU A O   
1299  C CB  . GLU A  103 ? 0.3944 0.4239 0.4401 0.1153  0.0432  0.0060  129 GLU A CB  
1300  C CG  . GLU A  103 ? 0.4614 0.4918 0.5034 0.1071  0.0381  0.0059  129 GLU A CG  
1301  C CD  . GLU A  103 ? 0.5503 0.5883 0.5999 0.1046  0.0328  0.0105  129 GLU A CD  
1302  O OE1 . GLU A  103 ? 0.5675 0.6121 0.6259 0.1088  0.0326  0.0142  129 GLU A OE1 
1303  O OE2 . GLU A  103 ? 0.5713 0.6088 0.6179 0.0984  0.0288  0.0104  129 GLU A OE2 
1310  N N   . LEU A  104 ? 0.3569 0.3633 0.3747 0.1094  0.0489  -0.0068 130 LEU A N   
1311  C CA  . LEU A  104 ? 0.3524 0.3456 0.3580 0.1056  0.0483  -0.0116 130 LEU A CA  
1312  C C   . LEU A  104 ? 0.3359 0.3326 0.3385 0.0980  0.0434  -0.0114 130 LEU A C   
1313  O O   . LEU A  104 ? 0.3293 0.3339 0.3316 0.0956  0.0438  -0.0112 130 LEU A O   
1314  C CB  . LEU A  104 ? 0.3636 0.3510 0.3610 0.1076  0.0543  -0.0166 130 LEU A CB  
1315  C CG  . LEU A  104 ? 0.3923 0.3661 0.3763 0.1036  0.0544  -0.0222 130 LEU A CG  
1316  C CD1 . LEU A  104 ? 0.4005 0.3616 0.3820 0.1038  0.0525  -0.0229 130 LEU A CD1 
1317  C CD2 . LEU A  104 ? 0.4043 0.3728 0.3809 0.1064  0.0610  -0.0270 130 LEU A CD2 
1329  N N   . LEU A  105 ? 0.3280 0.3188 0.3284 0.0943  0.0387  -0.0111 131 LEU A N   
1330  C CA  . LEU A  105 ? 0.3227 0.3165 0.3207 0.0876  0.0340  -0.0108 131 LEU A CA  
1331  C C   . LEU A  105 ? 0.3270 0.3098 0.3133 0.0836  0.0337  -0.0156 131 LEU A C   
1332  O O   . LEU A  105 ? 0.3259 0.2981 0.3084 0.0839  0.0334  -0.0174 131 LEU A O   
1333  C CB  . LEU A  105 ? 0.3215 0.3187 0.3264 0.0858  0.0290  -0.0066 131 LEU A CB  
1334  C CG  . LEU A  105 ? 0.3349 0.3413 0.3511 0.0900  0.0291  -0.0020 131 LEU A CG  
1335  C CD1 . LEU A  105 ? 0.3365 0.3451 0.3576 0.0874  0.0239  0.0015  131 LEU A CD1 
1336  C CD2 . LEU A  105 ? 0.3360 0.3547 0.3572 0.0901  0.0308  -0.0003 131 LEU A CD2 
1348  N N   . LEU A  106 ? 0.3303 0.3158 0.3107 0.0800  0.0338  -0.0177 132 LEU A N   
1349  C CA  . LEU A  106 ? 0.3444 0.3217 0.3136 0.0757  0.0333  -0.0224 132 LEU A CA  
1350  C C   . LEU A  106 ? 0.3470 0.3307 0.3143 0.0699  0.0291  -0.0215 132 LEU A C   
1351  O O   . LEU A  106 ? 0.3604 0.3446 0.3203 0.0673  0.0298  -0.0240 132 LEU A O   
1352  C CB  . LEU A  106 ? 0.3491 0.3223 0.3109 0.0779  0.0388  -0.0267 132 LEU A CB  
1353  C CG  . LEU A  106 ? 0.3803 0.3444 0.3414 0.0836  0.0437  -0.0288 132 LEU A CG  
1354  C CD1 . LEU A  106 ? 0.3898 0.3540 0.3462 0.0865  0.0496  -0.0319 132 LEU A CD1 
1355  C CD2 . LEU A  106 ? 0.4001 0.3499 0.3533 0.0815  0.0431  -0.0326 132 LEU A CD2 
1367  N N   . GLU A  107 ? 0.3336 0.3221 0.3073 0.0680  0.0249  -0.0178 133 GLU A N   
1368  C CA  . GLU A  107 ? 0.3315 0.3261 0.3046 0.0632  0.0210  -0.0164 133 GLU A CA  
1369  C C   . GLU A  107 ? 0.3420 0.3304 0.3081 0.0583  0.0179  -0.0191 133 GLU A C   
1370  O O   . GLU A  107 ? 0.3481 0.3282 0.3126 0.0581  0.0174  -0.0206 133 GLU A O   
1371  C CB  . GLU A  107 ? 0.3275 0.3294 0.3103 0.0631  0.0180  -0.0115 133 GLU A CB  
1372  C CG  . GLU A  107 ? 0.3404 0.3492 0.3313 0.0673  0.0206  -0.0085 133 GLU A CG  
1373  C CD  . GLU A  107 ? 0.3562 0.3725 0.3559 0.0664  0.0177  -0.0040 133 GLU A CD  
1374  O OE1 . GLU A  107 ? 0.3633 0.3793 0.3629 0.0626  0.0137  -0.0032 133 GLU A OE1 
1375  O OE2 . GLU A  107 ? 0.3397 0.3624 0.3466 0.0693  0.0194  -0.0014 133 GLU A OE2 
1382  N N   . ASP A  108 ? 0.3416 0.3346 0.3038 0.0543  0.0157  -0.0194 134 ASP A N   
1383  C CA  . ASP A  108 ? 0.3536 0.3434 0.3102 0.0492  0.0123  -0.0215 134 ASP A CA  
1384  C C   . ASP A  108 ? 0.3602 0.3393 0.3080 0.0480  0.0140  -0.0267 134 ASP A C   
1385  O O   . ASP A  108 ? 0.3669 0.3397 0.3129 0.0453  0.0119  -0.0280 134 ASP A O   
1386  C CB  . ASP A  108 ? 0.3834 0.3743 0.3464 0.0476  0.0084  -0.0186 134 ASP A CB  
1387  C CG  . ASP A  108 ? 0.4728 0.4640 0.4323 0.0423  0.0045  -0.0195 134 ASP A CG  
1388  O OD1 . ASP A  108 ? 0.4947 0.4883 0.4481 0.0397  0.0040  -0.0214 134 ASP A OD1 
1389  O OD2 . ASP A  108 ? 0.5100 0.4994 0.4728 0.0407  0.0020  -0.0183 134 ASP A OD2 
1394  N N   . ASN A  109 ? 0.3549 0.3315 0.2969 0.0497  0.0179  -0.0296 135 ASN A N   
1395  C CA  . ASN A  109 ? 0.3672 0.3327 0.2999 0.0487  0.0203  -0.0351 135 ASN A CA  
1396  C C   . ASN A  109 ? 0.3760 0.3425 0.2985 0.0447  0.0205  -0.0388 135 ASN A C   
1397  O O   . ASN A  109 ? 0.3803 0.3378 0.2941 0.0437  0.0231  -0.0438 135 ASN A O   
1398  C CB  . ASN A  109 ? 0.3813 0.3414 0.3153 0.0548  0.0257  -0.0360 135 ASN A CB  
1399  C CG  . ASN A  109 ? 0.4277 0.3845 0.3699 0.0587  0.0259  -0.0331 135 ASN A CG  
1400  O OD1 . ASN A  109 ? 0.4530 0.4129 0.4018 0.0641  0.0286  -0.0307 135 ASN A OD1 
1401  N ND2 . ASN A  109 ? 0.4220 0.3723 0.3636 0.0562  0.0234  -0.0335 135 ASN A ND2 
1408  N N   . GLN A  110 ? 0.3800 0.3569 0.3029 0.0425  0.0178  -0.0365 136 GLN A N   
1409  C CA  . GLN A  110 ? 0.4001 0.3797 0.3137 0.0390  0.0176  -0.0392 136 GLN A CA  
1410  C C   . GLN A  110 ? 0.4043 0.3794 0.3109 0.0415  0.0230  -0.0429 136 GLN A C   
1411  O O   . GLN A  110 ? 0.4137 0.3856 0.3099 0.0380  0.0236  -0.0474 136 GLN A O   
1412  C CB  . GLN A  110 ? 0.4449 0.4208 0.3516 0.0327  0.0142  -0.0426 136 GLN A CB  
1413  C CG  . GLN A  110 ? 0.5261 0.5076 0.4394 0.0301  0.0090  -0.0391 136 GLN A CG  
1414  C CD  . GLN A  110 ? 0.6380 0.6213 0.5449 0.0235  0.0052  -0.0414 136 GLN A CD  
1415  O OE1 . GLN A  110 ? 0.6844 0.6632 0.5814 0.0202  0.0062  -0.0463 136 GLN A OE1 
1416  N NE2 . GLN A  110 ? 0.6586 0.6490 0.5710 0.0214  0.0008  -0.0381 136 GLN A NE2 
1425  N N   . LEU A  111 ? 0.3892 0.3647 0.3015 0.0473  0.0271  -0.0411 137 LEU A N   
1426  C CA  . LEU A  111 ? 0.3932 0.3647 0.2995 0.0501  0.0328  -0.0445 137 LEU A CA  
1427  C C   . LEU A  111 ? 0.3986 0.3779 0.2989 0.0482  0.0331  -0.0445 137 LEU A C   
1428  O O   . LEU A  111 ? 0.3865 0.3759 0.2922 0.0485  0.0310  -0.0398 137 LEU A O   
1429  C CB  . LEU A  111 ? 0.3902 0.3626 0.3053 0.0569  0.0369  -0.0419 137 LEU A CB  
1430  C CG  . LEU A  111 ? 0.4098 0.3744 0.3307 0.0599  0.0373  -0.0416 137 LEU A CG  
1431  C CD1 . LEU A  111 ? 0.4114 0.3807 0.3428 0.0664  0.0402  -0.0378 137 LEU A CD1 
1432  C CD2 . LEU A  111 ? 0.4300 0.3808 0.3421 0.0598  0.0405  -0.0475 137 LEU A CD2 
1444  N N   . PRO A  112 ? 0.4113 0.3858 0.2998 0.0461  0.0356  -0.0498 138 PRO A N   
1445  C CA  . PRO A  112 ? 0.4099 0.3921 0.2920 0.0444  0.0359  -0.0495 138 PRO A CA  
1446  C C   . PRO A  112 ? 0.4109 0.3969 0.2951 0.0494  0.0412  -0.0480 138 PRO A C   
1447  O O   . PRO A  112 ? 0.4100 0.4038 0.2912 0.0485  0.0413  -0.0462 138 PRO A O   
1448  C CB  . PRO A  112 ? 0.4302 0.4050 0.2984 0.0399  0.0368  -0.0562 138 PRO A CB  
1449  C CG  . PRO A  112 ? 0.4443 0.4060 0.3118 0.0425  0.0409  -0.0604 138 PRO A CG  
1450  C CD  . PRO A  112 ? 0.4166 0.3781 0.2967 0.0453  0.0388  -0.0562 138 PRO A CD  
1458  N N   . GLN A  113 ? 0.4035 0.3841 0.2926 0.0546  0.0459  -0.0488 139 GLN A N   
1459  C CA  . GLN A  113 ? 0.4092 0.3934 0.3011 0.0596  0.0515  -0.0477 139 GLN A CA  
1460  C C   . GLN A  113 ? 0.4077 0.3909 0.3116 0.0653  0.0534  -0.0451 139 GLN A C   
1461  O O   . GLN A  113 ? 0.4025 0.3788 0.3095 0.0657  0.0518  -0.0458 139 GLN A O   
1462  C CB  . GLN A  113 ? 0.4359 0.4122 0.3163 0.0602  0.0573  -0.0541 139 GLN A CB  
1463  C CG  . GLN A  113 ? 0.5222 0.4993 0.3891 0.0547  0.0562  -0.0575 139 GLN A CG  
1464  C CD  . GLN A  113 ? 0.6163 0.6050 0.4827 0.0543  0.0562  -0.0536 139 GLN A CD  
1465  O OE1 . GLN A  113 ? 0.6424 0.6378 0.5175 0.0583  0.0583  -0.0492 139 GLN A OE1 
1466  N NE2 . GLN A  113 ? 0.6301 0.6217 0.4863 0.0491  0.0535  -0.0549 139 GLN A NE2 
1475  N N   . ILE A  114 ? 0.4096 0.3991 0.3195 0.0699  0.0576  -0.0425 140 ILE A N   
1476  C CA  . ILE A  114 ? 0.4154 0.4046 0.3362 0.0757  0.0602  -0.0405 140 ILE A CA  
1477  C C   . ILE A  114 ? 0.4335 0.4103 0.3482 0.0787  0.0650  -0.0462 140 ILE A C   
1478  O O   . ILE A  114 ? 0.4439 0.4172 0.3486 0.0783  0.0692  -0.0506 140 ILE A O   
1479  C CB  . ILE A  114 ? 0.4123 0.4119 0.3403 0.0795  0.0639  -0.0368 140 ILE A CB  
1480  C CG1 . ILE A  114 ? 0.4107 0.4212 0.3440 0.0764  0.0595  -0.0312 140 ILE A CG1 
1481  C CG2 . ILE A  114 ? 0.4121 0.4117 0.3509 0.0859  0.0671  -0.0352 140 ILE A CG2 
1482  C CD1 . ILE A  114 ? 0.4139 0.4350 0.3544 0.0790  0.0627  -0.0272 140 ILE A CD1 
1494  N N   . PRO A  115 ? 0.4371 0.4061 0.3562 0.0812  0.0647  -0.0465 141 PRO A N   
1495  C CA  . PRO A  115 ? 0.4424 0.3983 0.3550 0.0841  0.0697  -0.0520 141 PRO A CA  
1496  C C   . PRO A  115 ? 0.4505 0.4080 0.3634 0.0899  0.0773  -0.0533 141 PRO A C   
1497  O O   . PRO A  115 ? 0.4488 0.4164 0.3722 0.0940  0.0786  -0.0488 141 PRO A O   
1498  C CB  . PRO A  115 ? 0.4476 0.3979 0.3683 0.0871  0.0679  -0.0499 141 PRO A CB  
1499  C CG  . PRO A  115 ? 0.4526 0.4103 0.3795 0.0830  0.0608  -0.0452 141 PRO A CG  
1500  C CD  . PRO A  115 ? 0.4245 0.3958 0.3542 0.0816  0.0599  -0.0420 141 PRO A CD  
1508  N N   . SER A  116 ? 0.4565 0.4044 0.3576 0.0899  0.0823  -0.0596 142 SER A N   
1509  C CA  . SER A  116 ? 0.4590 0.4077 0.3595 0.0956  0.0901  -0.0615 142 SER A CA  
1510  C C   . SER A  116 ? 0.4554 0.3966 0.3623 0.1032  0.0945  -0.0617 142 SER A C   
1511  O O   . SER A  116 ? 0.4545 0.3847 0.3604 0.1032  0.0928  -0.0630 142 SER A O   
1512  C CB  . SER A  116 ? 0.4873 0.4291 0.3721 0.0925  0.0941  -0.0683 142 SER A CB  
1513  O OG  . SER A  116 ? 0.5261 0.4665 0.4006 0.0844  0.0890  -0.0704 142 SER A OG  
1519  N N   . GLY A  117 ? 0.4522 0.3997 0.3656 0.1097  0.1003  -0.0603 143 GLY A N   
1520  C CA  . GLY A  117 ? 0.4578 0.3999 0.3780 0.1180  0.1052  -0.0601 143 GLY A CA  
1521  C C   . GLY A  117 ? 0.4543 0.4001 0.3879 0.1208  0.1007  -0.0542 143 GLY A C   
1522  O O   . GLY A  117 ? 0.4626 0.3980 0.3978 0.1249  0.1019  -0.0548 143 GLY A O   
1526  N N   . LEU A  118 ? 0.4376 0.3977 0.3807 0.1184  0.0955  -0.0483 144 LEU A N   
1527  C CA  . LEU A  118 ? 0.4327 0.3977 0.3887 0.1207  0.0911  -0.0425 144 LEU A CA  
1528  C C   . LEU A  118 ? 0.4379 0.4094 0.4055 0.1295  0.0961  -0.0395 144 LEU A C   
1529  O O   . LEU A  118 ? 0.4390 0.4171 0.4073 0.1324  0.1016  -0.0403 144 LEU A O   
1530  C CB  . LEU A  118 ? 0.4251 0.4030 0.3870 0.1152  0.0844  -0.0375 144 LEU A CB  
1531  C CG  . LEU A  118 ? 0.4455 0.4186 0.3998 0.1073  0.0780  -0.0387 144 LEU A CG  
1532  C CD1 . LEU A  118 ? 0.4494 0.4357 0.4086 0.1026  0.0731  -0.0342 144 LEU A CD1 
1533  C CD2 . LEU A  118 ? 0.4538 0.4175 0.4095 0.1072  0.0743  -0.0383 144 LEU A CD2 
1545  N N   . PRO A  119 ? 0.4378 0.4082 0.4146 0.1340  0.0943  -0.0359 145 PRO A N   
1546  C CA  . PRO A  119 ? 0.4381 0.4152 0.4263 0.1428  0.0990  -0.0328 145 PRO A CA  
1547  C C   . PRO A  119 ? 0.4368 0.4335 0.4362 0.1430  0.0984  -0.0279 145 PRO A C   
1548  O O   . PRO A  119 ? 0.4249 0.4304 0.4291 0.1379  0.0923  -0.0240 145 PRO A O   
1549  C CB  . PRO A  119 ? 0.4453 0.4170 0.4399 0.1462  0.0957  -0.0296 145 PRO A CB  
1550  C CG  . PRO A  119 ? 0.4498 0.4175 0.4399 0.1383  0.0883  -0.0292 145 PRO A CG  
1551  C CD  . PRO A  119 ? 0.4347 0.3972 0.4115 0.1314  0.0884  -0.0346 145 PRO A CD  
1559  N N   . GLU A  120 ? 0.4394 0.4425 0.4435 0.1491  0.1052  -0.0279 146 GLU A N   
1560  C CA  . GLU A  120 ? 0.4430 0.4649 0.4580 0.1501  0.1063  -0.0236 146 GLU A CA  
1561  C C   . GLU A  120 ? 0.4351 0.4689 0.4653 0.1519  0.1016  -0.0167 146 GLU A C   
1562  O O   . GLU A  120 ? 0.4301 0.4795 0.4689 0.1500  0.1004  -0.0128 146 GLU A O   
1563  C CB  . GLU A  120 ? 0.4870 0.5112 0.5032 0.1573  0.1154  -0.0258 146 GLU A CB  
1564  C CG  . GLU A  120 ? 0.5702 0.6120 0.5937 0.1570  0.1181  -0.0231 146 GLU A CG  
1565  C CD  . GLU A  120 ? 0.6803 0.7232 0.7032 0.1637  0.1275  -0.0260 146 GLU A CD  
1566  O OE1 . GLU A  120 ? 0.7097 0.7464 0.7203 0.1612  0.1315  -0.0311 146 GLU A OE1 
1567  O OE2 . GLU A  120 ? 0.7100 0.7601 0.7446 0.1716  0.1310  -0.0231 146 GLU A OE2 
1574  N N   . SER A  121 ? 0.4294 0.4559 0.4627 0.1552  0.0990  -0.0152 147 SER A N   
1575  C CA  . SER A  121 ? 0.4181 0.4553 0.4648 0.1566  0.0941  -0.0087 147 SER A CA  
1576  C C   . SER A  121 ? 0.4046 0.4461 0.4516 0.1480  0.0860  -0.0062 147 SER A C   
1577  O O   . SER A  121 ? 0.3962 0.4476 0.4538 0.1480  0.0817  -0.0009 147 SER A O   
1578  C CB  . SER A  121 ? 0.4406 0.4677 0.4893 0.1629  0.0940  -0.0078 147 SER A CB  
1579  O OG  . SER A  121 ? 0.4779 0.4883 0.5152 0.1585  0.0907  -0.0111 147 SER A OG  
1585  N N   . LEU A  122 ? 0.4012 0.4354 0.4368 0.1407  0.0838  -0.0097 148 LEU A N   
1586  C CA  . LEU A  122 ? 0.3921 0.4294 0.4276 0.1330  0.0765  -0.0074 148 LEU A CA  
1587  C C   . LEU A  122 ? 0.3771 0.4317 0.4223 0.1303  0.0746  -0.0029 148 LEU A C   
1588  O O   . LEU A  122 ? 0.3775 0.4394 0.4227 0.1301  0.0786  -0.0035 148 LEU A O   
1589  C CB  . LEU A  122 ? 0.4009 0.4289 0.4227 0.1262  0.0750  -0.0120 148 LEU A CB  
1590  C CG  . LEU A  122 ? 0.4283 0.4387 0.4392 0.1257  0.0746  -0.0164 148 LEU A CG  
1591  C CD1 . LEU A  122 ? 0.4378 0.4422 0.4358 0.1187  0.0734  -0.0207 148 LEU A CD1 
1592  C CD2 . LEU A  122 ? 0.4322 0.4382 0.4467 0.1250  0.0690  -0.0137 148 LEU A CD2 
1604  N N   . THR A  123 ? 0.3626 0.4232 0.4152 0.1278  0.0687  0.0014  149 THR A N   
1605  C CA  . THR A  123 ? 0.3500 0.4254 0.4109 0.1238  0.0659  0.0056  149 THR A CA  
1606  C C   . THR A  123 ? 0.3390 0.4112 0.3942 0.1156  0.0600  0.0055  149 THR A C   
1607  O O   . THR A  123 ? 0.3350 0.4162 0.3930 0.1110  0.0586  0.0076  149 THR A O   
1608  C CB  . THR A  123 ? 0.3653 0.4514 0.4396 0.1272  0.0640  0.0107  149 THR A CB  
1609  O OG1 . THR A  123 ? 0.3898 0.4683 0.4634 0.1267  0.0589  0.0117  149 THR A OG1 
1610  C CG2 . THR A  123 ? 0.3663 0.4574 0.4475 0.1358  0.0698  0.0113  149 THR A CG2 
1618  N N   . GLU A  124 ? 0.3325 0.3920 0.3801 0.1137  0.0567  0.0034  150 GLU A N   
1619  C CA  . GLU A  124 ? 0.3312 0.3878 0.3739 0.1065  0.0514  0.0033  150 GLU A CA  
1620  C C   . GLU A  124 ? 0.3247 0.3671 0.3547 0.1047  0.0514  -0.0015 150 GLU A C   
1621  O O   . GLU A  124 ? 0.3246 0.3570 0.3515 0.1077  0.0520  -0.0035 150 GLU A O   
1622  C CB  . GLU A  124 ? 0.3775 0.4361 0.4268 0.1053  0.0458  0.0069  150 GLU A CB  
1623  C CG  . GLU A  124 ? 0.4737 0.5473 0.5347 0.1051  0.0448  0.0117  150 GLU A CG  
1624  C CD  . GLU A  124 ? 0.6025 0.6803 0.6727 0.1084  0.0423  0.0153  150 GLU A CD  
1625  O OE1 . GLU A  124 ? 0.6336 0.7185 0.7114 0.1141  0.0455  0.0171  150 GLU A OE1 
1626  O OE2 . GLU A  124 ? 0.6300 0.7045 0.6998 0.1053  0.0372  0.0166  150 GLU A OE2 
1633  N N   . LEU A  125 ? 0.3136 0.3553 0.3361 0.0996  0.0509  -0.0034 151 LEU A N   
1634  C CA  . LEU A  125 ? 0.3140 0.3441 0.3243 0.0969  0.0505  -0.0079 151 LEU A CA  
1635  C C   . LEU A  125 ? 0.3067 0.3380 0.3139 0.0903  0.0455  -0.0070 151 LEU A C   
1636  O O   . LEU A  125 ? 0.3077 0.3469 0.3161 0.0878  0.0455  -0.0052 151 LEU A O   
1637  C CB  . LEU A  125 ? 0.3162 0.3449 0.3193 0.0984  0.0562  -0.0115 151 LEU A CB  
1638  C CG  . LEU A  125 ? 0.3367 0.3553 0.3263 0.0948  0.0561  -0.0164 151 LEU A CG  
1639  C CD1 . LEU A  125 ? 0.3498 0.3553 0.3345 0.0957  0.0553  -0.0196 151 LEU A CD1 
1640  C CD2 . LEU A  125 ? 0.3428 0.3616 0.3259 0.0963  0.0620  -0.0196 151 LEU A CD2 
1652  N N   . SER A  126 ? 0.3050 0.3286 0.3085 0.0875  0.0413  -0.0080 152 SER A N   
1653  C CA  . SER A  126 ? 0.3042 0.3288 0.3046 0.0815  0.0367  -0.0073 152 SER A CA  
1654  C C   . SER A  126 ? 0.3062 0.3218 0.2950 0.0785  0.0362  -0.0117 152 SER A C   
1655  O O   . SER A  126 ? 0.3120 0.3181 0.2967 0.0790  0.0359  -0.0144 152 SER A O   
1656  C CB  . SER A  126 ? 0.3152 0.3405 0.3215 0.0797  0.0317  -0.0044 152 SER A CB  
1657  O OG  . SER A  126 ? 0.3281 0.3554 0.3321 0.0744  0.0279  -0.0035 152 SER A OG  
1663  N N   . LEU A  127 ? 0.2974 0.3162 0.2809 0.0752  0.0360  -0.0122 153 LEU A N   
1664  C CA  . LEU A  127 ? 0.3027 0.3153 0.2751 0.0716  0.0350  -0.0160 153 LEU A CA  
1665  C C   . LEU A  127 ? 0.2940 0.3110 0.2656 0.0666  0.0303  -0.0139 153 LEU A C   
1666  O O   . LEU A  127 ? 0.2962 0.3128 0.2598 0.0637  0.0297  -0.0156 153 LEU A O   
1667  C CB  . LEU A  127 ? 0.3131 0.3258 0.2789 0.0731  0.0400  -0.0188 153 LEU A CB  
1668  C CG  . LEU A  127 ? 0.3440 0.3506 0.3087 0.0781  0.0452  -0.0218 153 LEU A CG  
1669  C CD1 . LEU A  127 ? 0.3526 0.3634 0.3147 0.0803  0.0505  -0.0228 153 LEU A CD1 
1670  C CD2 . LEU A  127 ? 0.3654 0.3596 0.3208 0.0768  0.0451  -0.0269 153 LEU A CD2 
1682  N N   . ILE A  128 ? 0.2829 0.3035 0.2623 0.0657  0.0268  -0.0103 154 ILE A N   
1683  C CA  . ILE A  128 ? 0.2780 0.3022 0.2577 0.0615  0.0225  -0.0081 154 ILE A CA  
1684  C C   . ILE A  128 ? 0.2861 0.3043 0.2581 0.0580  0.0196  -0.0110 154 ILE A C   
1685  O O   . ILE A  128 ? 0.3016 0.3123 0.2713 0.0583  0.0195  -0.0138 154 ILE A O   
1686  C CB  . ILE A  128 ? 0.2737 0.3018 0.2632 0.0614  0.0198  -0.0042 154 ILE A CB  
1687  C CG1 . ILE A  128 ? 0.2757 0.3116 0.2726 0.0637  0.0223  -0.0010 154 ILE A CG1 
1688  C CG2 . ILE A  128 ? 0.2760 0.3056 0.2654 0.0573  0.0154  -0.0026 154 ILE A CG2 
1689  C CD1 . ILE A  128 ? 0.2812 0.3205 0.2877 0.0641  0.0203  0.0022  154 ILE A CD1 
1701  N N   . GLN A  129 ? 0.2674 0.2891 0.2359 0.0547  0.0171  -0.0103 155 GLN A N   
1702  C CA  . GLN A  129 ? 0.2787 0.2969 0.2411 0.0508  0.0138  -0.0125 155 GLN A CA  
1703  C C   . GLN A  129 ? 0.2984 0.3093 0.2516 0.0502  0.0155  -0.0177 155 GLN A C   
1704  O O   . GLN A  129 ? 0.3061 0.3106 0.2566 0.0482  0.0139  -0.0203 155 GLN A O   
1705  C CB  . GLN A  129 ? 0.2775 0.2939 0.2452 0.0493  0.0101  -0.0113 155 GLN A CB  
1706  C CG  . GLN A  129 ? 0.2785 0.3015 0.2517 0.0478  0.0072  -0.0072 155 GLN A CG  
1707  C CD  . GLN A  129 ? 0.3207 0.3469 0.2888 0.0446  0.0047  -0.0072 155 GLN A CD  
1708  O OE1 . GLN A  129 ? 0.3318 0.3557 0.2920 0.0429  0.0046  -0.0103 155 GLN A OE1 
1709  N NE2 . GLN A  129 ? 0.3228 0.3543 0.2950 0.0437  0.0026  -0.0037 155 GLN A NE2 
1718  N N   . ASN A  130 ? 0.2985 0.3105 0.2461 0.0512  0.0188  -0.0193 156 ASN A N   
1719  C CA  . ASN A  130 ? 0.3094 0.3149 0.2468 0.0500  0.0206  -0.0245 156 ASN A CA  
1720  C C   . ASN A  130 ? 0.3079 0.3187 0.2377 0.0472  0.0198  -0.0247 156 ASN A C   
1721  O O   . ASN A  130 ? 0.3019 0.3200 0.2348 0.0460  0.0170  -0.0208 156 ASN A O   
1722  C CB  . ASN A  130 ? 0.3220 0.3227 0.2593 0.0545  0.0261  -0.0266 156 ASN A CB  
1723  C CG  . ASN A  130 ? 0.3327 0.3263 0.2747 0.0567  0.0264  -0.0272 156 ASN A CG  
1724  O OD1 . ASN A  130 ? 0.3465 0.3322 0.2839 0.0544  0.0251  -0.0303 156 ASN A OD1 
1725  N ND2 . ASN A  130 ? 0.3259 0.3224 0.2769 0.0609  0.0280  -0.0241 156 ASN A ND2 
1732  N N   . ASN A  131 ? 0.3122 0.3191 0.2318 0.0460  0.0221  -0.0292 157 ASN A N   
1733  C CA  . ASN A  131 ? 0.3262 0.3381 0.2377 0.0434  0.0214  -0.0296 157 ASN A CA  
1734  C C   . ASN A  131 ? 0.3319 0.3445 0.2395 0.0463  0.0269  -0.0306 157 ASN A C   
1735  O O   . ASN A  131 ? 0.3447 0.3564 0.2421 0.0443  0.0281  -0.0338 157 ASN A O   
1736  C CB  . ASN A  131 ? 0.3484 0.3558 0.2501 0.0385  0.0192  -0.0343 157 ASN A CB  
1737  C CG  . ASN A  131 ? 0.3924 0.3995 0.2979 0.0354  0.0142  -0.0336 157 ASN A CG  
1738  O OD1 . ASN A  131 ? 0.3908 0.4038 0.3043 0.0358  0.0113  -0.0289 157 ASN A OD1 
1739  N ND2 . ASN A  131 ? 0.4167 0.4166 0.3161 0.0319  0.0134  -0.0383 157 ASN A ND2 
1746  N N   . ILE A  132 ? 0.3281 0.3427 0.2438 0.0508  0.0300  -0.0278 158 ILE A N   
1747  C CA  . ILE A  132 ? 0.3399 0.3556 0.2535 0.0539  0.0356  -0.0284 158 ILE A CA  
1748  C C   . ILE A  132 ? 0.3480 0.3730 0.2615 0.0534  0.0353  -0.0241 158 ILE A C   
1749  O O   . ILE A  132 ? 0.3367 0.3672 0.2589 0.0542  0.0337  -0.0192 158 ILE A O   
1750  C CB  . ILE A  132 ? 0.3429 0.3571 0.2659 0.0590  0.0392  -0.0275 158 ILE A CB  
1751  C CG1 . ILE A  132 ? 0.3648 0.3686 0.2869 0.0600  0.0399  -0.0317 158 ILE A CG1 
1752  C CG2 . ILE A  132 ? 0.3485 0.3658 0.2706 0.0623  0.0451  -0.0276 158 ILE A CG2 
1753  C CD1 . ILE A  132 ? 0.3791 0.3821 0.3120 0.0648  0.0417  -0.0296 158 ILE A CD1 
1765  N N   . TYR A  133 ? 0.3548 0.3809 0.2580 0.0518  0.0370  -0.0261 159 TYR A N   
1766  C CA  . TYR A  133 ? 0.3629 0.3971 0.2643 0.0512  0.0370  -0.0219 159 TYR A CA  
1767  C C   . TYR A  133 ? 0.3920 0.4278 0.2902 0.0537  0.0431  -0.0225 159 TYR A C   
1768  O O   . TYR A  133 ? 0.4049 0.4466 0.3001 0.0531  0.0437  -0.0194 159 TYR A O   
1769  C CB  . TYR A  133 ? 0.3564 0.3927 0.2481 0.0468  0.0329  -0.0225 159 TYR A CB  
1770  C CG  . TYR A  133 ? 0.3677 0.4025 0.2615 0.0440  0.0272  -0.0229 159 TYR A CG  
1771  C CD1 . TYR A  133 ? 0.3697 0.4062 0.2743 0.0449  0.0244  -0.0190 159 TYR A CD1 
1772  C CD2 . TYR A  133 ? 0.3817 0.4128 0.2666 0.0401  0.0250  -0.0276 159 TYR A CD2 
1773  C CE1 . TYR A  133 ? 0.3798 0.4144 0.2865 0.0425  0.0198  -0.0197 159 TYR A CE1 
1774  C CE2 . TYR A  133 ? 0.3894 0.4193 0.2766 0.0373  0.0201  -0.0280 159 TYR A CE2 
1775  C CZ  . TYR A  133 ? 0.3946 0.4263 0.2928 0.0387  0.0177  -0.0240 159 TYR A CZ  
1776  O OH  . TYR A  133 ? 0.4176 0.4483 0.3183 0.0360  0.0132  -0.0244 159 TYR A OH  
1786  N N   . ASN A  134 ? 0.4027 0.4332 0.3014 0.0567  0.0479  -0.0264 160 ASN A N   
1787  C CA  . ASN A  134 ? 0.4215 0.4531 0.3170 0.0593  0.0542  -0.0276 160 ASN A CA  
1788  C C   . ASN A  134 ? 0.4177 0.4480 0.3235 0.0642  0.0581  -0.0275 160 ASN A C   
1789  O O   . ASN A  134 ? 0.4250 0.4482 0.3325 0.0656  0.0581  -0.0307 160 ASN A O   
1790  C CB  . ASN A  134 ? 0.4596 0.4848 0.3414 0.0576  0.0565  -0.0341 160 ASN A CB  
1791  C CG  . ASN A  134 ? 0.5390 0.5665 0.4135 0.0587  0.0622  -0.0354 160 ASN A CG  
1792  O OD1 . ASN A  134 ? 0.5601 0.5949 0.4388 0.0602  0.0645  -0.0311 160 ASN A OD1 
1793  N ND2 . ASN A  134 ? 0.5726 0.5937 0.4355 0.0575  0.0650  -0.0416 160 ASN A ND2 
1800  N N   . ILE A  135 ? 0.4052 0.4427 0.3182 0.0666  0.0611  -0.0235 161 ILE A N   
1801  C CA  . ILE A  135 ? 0.4065 0.4453 0.3301 0.0713  0.0649  -0.0227 161 ILE A CA  
1802  C C   . ILE A  135 ? 0.4183 0.4584 0.3372 0.0739  0.0720  -0.0250 161 ILE A C   
1803  O O   . ILE A  135 ? 0.4145 0.4616 0.3324 0.0731  0.0740  -0.0221 161 ILE A O   
1804  C CB  . ILE A  135 ? 0.3999 0.4469 0.3356 0.0715  0.0629  -0.0164 161 ILE A CB  
1805  C CG1 . ILE A  135 ? 0.4121 0.4586 0.3500 0.0680  0.0558  -0.0138 161 ILE A CG1 
1806  C CG2 . ILE A  135 ? 0.3963 0.4454 0.3436 0.0760  0.0658  -0.0155 161 ILE A CG2 
1807  C CD1 . ILE A  135 ? 0.4331 0.4725 0.3716 0.0678  0.0525  -0.0165 161 ILE A CD1 
1819  N N   . THR A  136 ? 0.4274 0.4602 0.3426 0.0768  0.0760  -0.0303 162 THR A N   
1820  C CA  . THR A  136 ? 0.4402 0.4729 0.3495 0.0793  0.0832  -0.0335 162 THR A CA  
1821  C C   . THR A  136 ? 0.4371 0.4709 0.3558 0.0854  0.0887  -0.0337 162 THR A C   
1822  O O   . THR A  136 ? 0.4283 0.4598 0.3559 0.0881  0.0870  -0.0330 162 THR A O   
1823  C CB  . THR A  136 ? 0.4725 0.4953 0.3672 0.0773  0.0842  -0.0402 162 THR A CB  
1824  O OG1 . THR A  136 ? 0.4935 0.5066 0.3899 0.0795  0.0841  -0.0438 162 THR A OG1 
1825  C CG2 . THR A  136 ? 0.4797 0.5023 0.3650 0.0711  0.0785  -0.0400 162 THR A CG2 
1833  N N   . LYS A  137 ? 0.4452 0.4828 0.3616 0.0879  0.0955  -0.0348 163 LYS A N   
1834  C CA  . LYS A  137 ? 0.4621 0.5018 0.3866 0.0942  0.1018  -0.0353 163 LYS A CA  
1835  C C   . LYS A  137 ? 0.4851 0.5131 0.4071 0.0978  0.1037  -0.0406 163 LYS A C   
1836  O O   . LYS A  137 ? 0.4809 0.5093 0.4132 0.1030  0.1055  -0.0396 163 LYS A O   
1837  C CB  . LYS A  137 ? 0.4762 0.5213 0.3961 0.0954  0.1089  -0.0362 163 LYS A CB  
1838  C CG  . LYS A  137 ? 0.5146 0.5717 0.4392 0.0927  0.1081  -0.0302 163 LYS A CG  
1839  C CD  . LYS A  137 ? 0.5806 0.6440 0.5024 0.0943  0.1157  -0.0306 163 LYS A CD  
1840  C CE  . LYS A  137 ? 0.6287 0.7041 0.5578 0.0921  0.1152  -0.0242 163 LYS A CE  
1841  N NZ  . LYS A  137 ? 0.6635 0.7449 0.5884 0.0926  0.1224  -0.0243 163 LYS A NZ  
1855  N N   . GLU A  138 ? 0.5076 0.5250 0.4157 0.0949  0.1033  -0.0461 164 GLU A N   
1856  C CA  . GLU A  138 ? 0.5304 0.5347 0.4342 0.0973  0.1051  -0.0516 164 GLU A CA  
1857  C C   . GLU A  138 ? 0.5269 0.5282 0.4406 0.0985  0.0999  -0.0491 164 GLU A C   
1858  O O   . GLU A  138 ? 0.5307 0.5257 0.4486 0.1036  0.1026  -0.0507 164 GLU A O   
1859  C CB  . GLU A  138 ? 0.5888 0.5834 0.4757 0.0919  0.1037  -0.0574 164 GLU A CB  
1860  C CG  . GLU A  138 ? 0.6990 0.6791 0.5784 0.0942  0.1079  -0.0643 164 GLU A CG  
1861  C CD  . GLU A  138 ? 0.8337 0.8029 0.7037 0.0888  0.1028  -0.0681 164 GLU A CD  
1862  O OE1 . GLU A  138 ? 0.8509 0.8230 0.7136 0.0823  0.0980  -0.0679 164 GLU A OE1 
1863  O OE2 . GLU A  138 ? 0.8918 0.8495 0.7619 0.0912  0.1039  -0.0712 164 GLU A OE2 
1870  N N   . GLY A  139 ? 0.5198 0.5258 0.4370 0.0940  0.0927  -0.0450 165 GLY A N   
1871  C CA  . GLY A  139 ? 0.5245 0.5284 0.4503 0.0942  0.0873  -0.0424 165 GLY A CA  
1872  C C   . GLY A  139 ? 0.5194 0.5315 0.4609 0.0989  0.0876  -0.0372 165 GLY A C   
1873  O O   . GLY A  139 ? 0.5210 0.5281 0.4683 0.1023  0.0869  -0.0371 165 GLY A O   
1877  N N   . ILE A  140 ? 0.5101 0.5350 0.4588 0.0989  0.0883  -0.0326 166 ILE A N   
1878  C CA  . ILE A  140 ? 0.5096 0.5435 0.4734 0.1023  0.0877  -0.0274 166 ILE A CA  
1879  C C   . ILE A  140 ? 0.5126 0.5568 0.4838 0.1067  0.0939  -0.0255 166 ILE A C   
1880  O O   . ILE A  140 ? 0.5062 0.5579 0.4902 0.1096  0.0935  -0.0216 166 ILE A O   
1881  C CB  . ILE A  140 ? 0.5121 0.5527 0.4814 0.0973  0.0809  -0.0224 166 ILE A CB  
1882  C CG1 . ILE A  140 ? 0.5215 0.5697 0.4870 0.0933  0.0811  -0.0203 166 ILE A CG1 
1883  C CG2 . ILE A  140 ? 0.5216 0.5533 0.4858 0.0936  0.0747  -0.0238 166 ILE A CG2 
1884  C CD1 . ILE A  140 ? 0.5354 0.5914 0.5086 0.0898  0.0760  -0.0148 166 ILE A CD1 
1896  N N   . SER A  141 ? 0.5201 0.5657 0.4839 0.1068  0.0995  -0.0280 167 SER A N   
1897  C CA  . SER A  141 ? 0.5260 0.5824 0.4974 0.1107  0.1055  -0.0259 167 SER A CA  
1898  C C   . SER A  141 ? 0.5183 0.5737 0.4971 0.1185  0.1105  -0.0272 167 SER A C   
1899  O O   . SER A  141 ? 0.5129 0.5796 0.5030 0.1220  0.1135  -0.0238 167 SER A O   
1900  C CB  . SER A  141 ? 0.5649 0.6234 0.5263 0.1087  0.1103  -0.0280 167 SER A CB  
1901  O OG  . SER A  141 ? 0.6054 0.6685 0.5637 0.1023  0.1058  -0.0248 167 SER A OG  
1907  N N   . ARG A  142 ? 0.5196 0.5620 0.4930 0.1213  0.1112  -0.0315 168 ARG A N   
1908  C CA  . ARG A  142 ? 0.5217 0.5622 0.5027 0.1294  0.1156  -0.0321 168 ARG A CA  
1909  C C   . ARG A  142 ? 0.5058 0.5507 0.5004 0.1313  0.1104  -0.0270 168 ARG A C   
1910  O O   . ARG A  142 ? 0.5013 0.5483 0.5050 0.1382  0.1134  -0.0258 168 ARG A O   
1911  C CB  . ARG A  142 ? 0.5659 0.5894 0.5355 0.1317  0.1187  -0.0387 168 ARG A CB  
1912  C CG  . ARG A  142 ? 0.6424 0.6628 0.6020 0.1335  0.1268  -0.0439 168 ARG A CG  
1913  C CD  . ARG A  142 ? 0.7260 0.7285 0.6712 0.1333  0.1290  -0.0510 168 ARG A CD  
1914  N NE  . ARG A  142 ? 0.7930 0.7900 0.7258 0.1248  0.1237  -0.0532 168 ARG A NE  
1915  C CZ  . ARG A  142 ? 0.8462 0.8302 0.7637 0.1219  0.1252  -0.0598 168 ARG A CZ  
1916  N NH1 . ARG A  142 ? 0.8534 0.8269 0.7652 0.1268  0.1323  -0.0652 168 ARG A NH1 
1917  N NH2 . ARG A  142 ? 0.8555 0.8370 0.7632 0.1141  0.1198  -0.0610 168 ARG A NH2 
1931  N N   . LEU A  143 ? 0.4941 0.5411 0.4904 0.1254  0.1028  -0.0239 169 LEU A N   
1932  C CA  . LEU A  143 ? 0.4791 0.5301 0.4871 0.1265  0.0977  -0.0193 169 LEU A CA  
1933  C C   . LEU A  143 ? 0.4601 0.5284 0.4812 0.1266  0.0976  -0.0137 169 LEU A C   
1934  O O   . LEU A  143 ? 0.4562 0.5306 0.4815 0.1216  0.0921  -0.0100 169 LEU A O   
1935  C CB  . LEU A  143 ? 0.4839 0.5282 0.4870 0.1202  0.0900  -0.0190 169 LEU A CB  
1936  C CG  . LEU A  143 ? 0.5133 0.5417 0.5027 0.1182  0.0894  -0.0246 169 LEU A CG  
1937  C CD1 . LEU A  143 ? 0.5233 0.5479 0.5100 0.1120  0.0817  -0.0235 169 LEU A CD1 
1938  C CD2 . LEU A  143 ? 0.5241 0.5419 0.5131 0.1247  0.0930  -0.0274 169 LEU A CD2 
1950  N N   . ILE A  144 ? 0.4501 0.5259 0.4779 0.1325  0.1039  -0.0132 170 ILE A N   
1951  C CA  . ILE A  144 ? 0.4408 0.5338 0.4808 0.1328  0.1051  -0.0084 170 ILE A CA  
1952  C C   . ILE A  144 ? 0.4166 0.5183 0.4703 0.1333  0.0999  -0.0030 170 ILE A C   
1953  O O   . ILE A  144 ? 0.4085 0.5239 0.4709 0.1307  0.0990  0.0010  170 ILE A O   
1954  C CB  . ILE A  144 ? 0.4545 0.5540 0.4982 0.1392  0.1137  -0.0095 170 ILE A CB  
1955  C CG1 . ILE A  144 ? 0.4718 0.5707 0.5241 0.1482  0.1165  -0.0091 170 ILE A CG1 
1956  C CG2 . ILE A  144 ? 0.4741 0.5652 0.5035 0.1385  0.1191  -0.0150 170 ILE A CG2 
1957  C CD1 . ILE A  144 ? 0.5033 0.5861 0.5491 0.1510  0.1152  -0.0122 170 ILE A CD1 
1969  N N   . ASN A  145 ? 0.4026 0.4963 0.4578 0.1358  0.0963  -0.0029 171 ASN A N   
1970  C CA  . ASN A  145 ? 0.3876 0.4890 0.4546 0.1359  0.0910  0.0021  171 ASN A CA  
1971  C C   . ASN A  145 ? 0.3866 0.4848 0.4502 0.1281  0.0832  0.0034  171 ASN A C   
1972  O O   . ASN A  145 ? 0.3871 0.4900 0.4587 0.1274  0.0783  0.0072  171 ASN A O   
1973  C CB  . ASN A  145 ? 0.3961 0.4913 0.4670 0.1433  0.0914  0.0022  171 ASN A CB  
1974  C CG  . ASN A  145 ? 0.4271 0.5270 0.5035 0.1519  0.0989  0.0018  171 ASN A CG  
1975  O OD1 . ASN A  145 ? 0.4344 0.5501 0.5213 0.1535  0.1013  0.0050  171 ASN A OD1 
1976  N ND2 . ASN A  145 ? 0.4294 0.5160 0.4993 0.1575  0.1030  -0.0021 171 ASN A ND2 
1983  N N   . LEU A  146 ? 0.3770 0.4674 0.4287 0.1225  0.0821  0.0005  172 LEU A N   
1984  C CA  . LEU A  146 ? 0.3716 0.4590 0.4203 0.1156  0.0752  0.0017  172 LEU A CA  
1985  C C   . LEU A  146 ? 0.3543 0.4552 0.4126 0.1117  0.0722  0.0066  172 LEU A C   
1986  O O   . LEU A  146 ? 0.3461 0.4567 0.4074 0.1106  0.0755  0.0079  172 LEU A O   
1987  C CB  . LEU A  146 ? 0.3780 0.4574 0.4132 0.1104  0.0749  -0.0018 172 LEU A CB  
1988  C CG  . LEU A  146 ? 0.4028 0.4667 0.4266 0.1101  0.0737  -0.0063 172 LEU A CG  
1989  C CD1 . LEU A  146 ? 0.4175 0.4770 0.4296 0.1043  0.0726  -0.0087 172 LEU A CD1 
1990  C CD2 . LEU A  146 ? 0.4022 0.4606 0.4286 0.1093  0.0678  -0.0050 172 LEU A CD2 
2002  N N   . LYS A  147 ? 0.3424 0.4434 0.4051 0.1093  0.0662  0.0092  173 LYS A N   
2003  C CA  . LYS A  147 ? 0.3344 0.4462 0.4053 0.1049  0.0626  0.0135  173 LYS A CA  
2004  C C   . LYS A  147 ? 0.3216 0.4271 0.3855 0.0980  0.0576  0.0131  173 LYS A C   
2005  O O   . LYS A  147 ? 0.3208 0.4323 0.3857 0.0931  0.0567  0.0151  173 LYS A O   
2006  C CB  . LYS A  147 ? 0.3710 0.4882 0.4525 0.1078  0.0596  0.0167  173 LYS A CB  
2007  C CG  . LYS A  147 ? 0.4480 0.5788 0.5394 0.1037  0.0568  0.0211  173 LYS A CG  
2008  C CD  . LYS A  147 ? 0.5216 0.6569 0.6221 0.1057  0.0527  0.0242  173 LYS A CD  
2009  C CE  . LYS A  147 ? 0.5891 0.7166 0.6854 0.1010  0.0464  0.0244  173 LYS A CE  
2010  N NZ  . LYS A  147 ? 0.6215 0.7545 0.7262 0.1022  0.0423  0.0278  173 LYS A NZ  
2024  N N   . ASN A  148 ? 0.3126 0.4062 0.3695 0.0976  0.0544  0.0109  174 ASN A N   
2025  C CA  . ASN A  148 ? 0.3162 0.4043 0.3669 0.0916  0.0497  0.0106  174 ASN A CA  
2026  C C   . ASN A  148 ? 0.3224 0.3984 0.3606 0.0912  0.0504  0.0062  174 ASN A C   
2027  O O   . ASN A  148 ? 0.3308 0.3986 0.3658 0.0945  0.0510  0.0036  174 ASN A O   
2028  C CB  . ASN A  148 ? 0.3309 0.4175 0.3858 0.0902  0.0441  0.0125  174 ASN A CB  
2029  C CG  . ASN A  148 ? 0.3714 0.4697 0.4382 0.0902  0.0427  0.0167  174 ASN A CG  
2030  O OD1 . ASN A  148 ? 0.3762 0.4847 0.4483 0.0890  0.0448  0.0187  174 ASN A OD1 
2031  N ND2 . ASN A  148 ? 0.3863 0.4835 0.4572 0.0910  0.0389  0.0182  174 ASN A ND2 
2038  N N   . LEU A  149 ? 0.3130 0.3882 0.3443 0.0869  0.0503  0.0055  175 LEU A N   
2039  C CA  . LEU A  149 ? 0.3165 0.3820 0.3358 0.0858  0.0505  0.0016  175 LEU A CA  
2040  C C   . LEU A  149 ? 0.3157 0.3787 0.3307 0.0801  0.0456  0.0024  175 LEU A C   
2041  O O   . LEU A  149 ? 0.3141 0.3829 0.3300 0.0770  0.0453  0.0048  175 LEU A O   
2042  C CB  . LEU A  149 ? 0.3174 0.3848 0.3313 0.0868  0.0560  -0.0002 175 LEU A CB  
2043  C CG  . LEU A  149 ? 0.3336 0.3923 0.3344 0.0851  0.0565  -0.0043 175 LEU A CG  
2044  C CD1 . LEU A  149 ? 0.3354 0.3831 0.3313 0.0872  0.0560  -0.0083 175 LEU A CD1 
2045  C CD2 . LEU A  149 ? 0.3375 0.3992 0.3334 0.0863  0.0623  -0.0057 175 LEU A CD2 
2057  N N   . TYR A  150 ? 0.3124 0.3669 0.3229 0.0789  0.0420  0.0004  176 TYR A N   
2058  C CA  . TYR A  150 ? 0.3174 0.3697 0.3241 0.0741  0.0373  0.0010  176 TYR A CA  
2059  C C   . TYR A  150 ? 0.3288 0.3741 0.3241 0.0724  0.0373  -0.0027 176 TYR A C   
2060  O O   . TYR A  150 ? 0.3374 0.3749 0.3280 0.0737  0.0376  -0.0061 176 TYR A O   
2061  C CB  . TYR A  150 ? 0.3187 0.3681 0.3295 0.0730  0.0327  0.0020  176 TYR A CB  
2062  C CG  . TYR A  150 ? 0.3257 0.3816 0.3475 0.0747  0.0322  0.0053  176 TYR A CG  
2063  C CD1 . TYR A  150 ? 0.3380 0.3938 0.3642 0.0796  0.0345  0.0050  176 TYR A CD1 
2064  C CD2 . TYR A  150 ? 0.3375 0.3993 0.3648 0.0715  0.0294  0.0087  176 TYR A CD2 
2065  C CE1 . TYR A  150 ? 0.3499 0.4128 0.3863 0.0811  0.0337  0.0083  176 TYR A CE1 
2066  C CE2 . TYR A  150 ? 0.3491 0.4174 0.3860 0.0725  0.0287  0.0116  176 TYR A CE2 
2067  C CZ  . TYR A  150 ? 0.3653 0.4348 0.4069 0.0773  0.0307  0.0116  176 TYR A CZ  
2068  O OH  . TYR A  150 ? 0.3984 0.4753 0.4496 0.0782  0.0296  0.0147  176 TYR A OH  
2078  N N   . LEU A  151 ? 0.3221 0.3700 0.3125 0.0695  0.0371  -0.0018 177 LEU A N   
2079  C CA  . LEU A  151 ? 0.3257 0.3689 0.3052 0.0673  0.0365  -0.0048 177 LEU A CA  
2080  C C   . LEU A  151 ? 0.3198 0.3642 0.2974 0.0631  0.0319  -0.0027 177 LEU A C   
2081  O O   . LEU A  151 ? 0.3264 0.3697 0.2958 0.0610  0.0313  -0.0038 177 LEU A O   
2082  C CB  . LEU A  151 ? 0.3332 0.3791 0.3077 0.0685  0.0414  -0.0056 177 LEU A CB  
2083  C CG  . LEU A  151 ? 0.3567 0.4004 0.3309 0.0729  0.0466  -0.0086 177 LEU A CG  
2084  C CD1 . LEU A  151 ? 0.3637 0.4135 0.3369 0.0742  0.0516  -0.0078 177 LEU A CD1 
2085  C CD2 . LEU A  151 ? 0.3777 0.4121 0.3421 0.0728  0.0470  -0.0138 177 LEU A CD2 
2097  N N   . ALA A  152 ? 0.2989 0.3455 0.2838 0.0619  0.0287  0.0004  178 ALA A N   
2098  C CA  . ALA A  152 ? 0.2936 0.3416 0.2778 0.0585  0.0249  0.0026  178 ALA A CA  
2099  C C   . ALA A  152 ? 0.2899 0.3327 0.2679 0.0562  0.0213  0.0002  178 ALA A C   
2100  O O   . ALA A  152 ? 0.2993 0.3365 0.2750 0.0568  0.0211  -0.0032 178 ALA A O   
2101  C CB  . ALA A  152 ? 0.2931 0.3443 0.2866 0.0578  0.0230  0.0060  178 ALA A CB  
2107  N N   . TRP A  153 ? 0.2731 0.3178 0.2482 0.0536  0.0187  0.0019  179 TRP A N   
2108  C CA  . TRP A  153 ? 0.2749 0.3169 0.2456 0.0511  0.0148  0.0003  179 TRP A CA  
2109  C C   . TRP A  153 ? 0.2911 0.3288 0.2525 0.0504  0.0154  -0.0042 179 TRP A C   
2110  O O   . TRP A  153 ? 0.3022 0.3352 0.2616 0.0489  0.0132  -0.0069 179 TRP A O   
2111  C CB  . TRP A  153 ? 0.2606 0.3000 0.2371 0.0503  0.0119  0.0004  179 TRP A CB  
2112  C CG  . TRP A  153 ? 0.2524 0.2956 0.2365 0.0499  0.0107  0.0044  179 TRP A CG  
2113  C CD1 . TRP A  153 ? 0.2610 0.3063 0.2526 0.0513  0.0121  0.0063  179 TRP A CD1 
2114  C CD2 . TRP A  153 ? 0.2461 0.2912 0.2311 0.0477  0.0076  0.0067  179 TRP A CD2 
2115  N NE1 . TRP A  153 ? 0.2563 0.3041 0.2526 0.0497  0.0102  0.0094  179 TRP A NE1 
2116  C CE2 . TRP A  153 ? 0.2480 0.2953 0.2406 0.0477  0.0075  0.0096  179 TRP A CE2 
2117  C CE3 . TRP A  153 ? 0.2539 0.2995 0.2342 0.0458  0.0049  0.0065  179 TRP A CE3 
2118  C CZ2 . TRP A  153 ? 0.2474 0.2962 0.2424 0.0460  0.0054  0.0121  179 TRP A CZ2 
2119  C CZ3 . TRP A  153 ? 0.2579 0.3057 0.2413 0.0445  0.0027  0.0094  179 TRP A CZ3 
2120  C CH2 . TRP A  153 ? 0.2531 0.3019 0.2436 0.0447  0.0031  0.0120  179 TRP A CH2 
2131  N N   . ASN A  154 ? 0.2899 0.3289 0.2452 0.0512  0.0184  -0.0051 180 ASN A N   
2132  C CA  . ASN A  154 ? 0.3013 0.3366 0.2467 0.0499  0.0189  -0.0095 180 ASN A CA  
2133  C C   . ASN A  154 ? 0.3181 0.3575 0.2569 0.0471  0.0163  -0.0084 180 ASN A C   
2134  O O   . ASN A  154 ? 0.3318 0.3688 0.2630 0.0447  0.0147  -0.0118 180 ASN A O   
2135  C CB  . ASN A  154 ? 0.3098 0.3429 0.2517 0.0525  0.0242  -0.0122 180 ASN A CB  
2136  C CG  . ASN A  154 ? 0.3406 0.3676 0.2861 0.0551  0.0262  -0.0148 180 ASN A CG  
2137  O OD1 . ASN A  154 ? 0.3394 0.3597 0.2787 0.0550  0.0276  -0.0193 180 ASN A OD1 
2138  N ND2 . ASN A  154 ? 0.3499 0.3788 0.3054 0.0572  0.0262  -0.0119 180 ASN A ND2 
2145  N N   . CYS A  155 ? 0.3113 0.3567 0.2527 0.0474  0.0158  -0.0037 181 CYS A N   
2146  C CA  . CYS A  155 ? 0.3212 0.3709 0.2568 0.0454  0.0133  -0.0019 181 CYS A CA  
2147  C C   . CYS A  155 ? 0.3138 0.3680 0.2559 0.0458  0.0115  0.0037  181 CYS A C   
2148  O O   . CYS A  155 ? 0.3096 0.3660 0.2549 0.0474  0.0142  0.0069  181 CYS A O   
2149  C CB  . CYS A  155 ? 0.3411 0.3927 0.2683 0.0457  0.0163  -0.0025 181 CYS A CB  
2150  S SG  . CYS A  155 ? 0.4105 0.4682 0.3299 0.0435  0.0130  0.0001  181 CYS A SG  
2155  N N   . TYR A  156 ? 0.3080 0.3633 0.2522 0.0441  0.0073  0.0047  182 TYR A N   
2156  C CA  . TYR A  156 ? 0.3097 0.3678 0.2604 0.0447  0.0059  0.0095  182 TYR A CA  
2157  C C   . TYR A  156 ? 0.3119 0.3726 0.2621 0.0429  0.0014  0.0105  182 TYR A C   
2158  O O   . TYR A  156 ? 0.3131 0.3733 0.2594 0.0409  -0.0009 0.0071  182 TYR A O   
2159  C CB  . TYR A  156 ? 0.3053 0.3605 0.2650 0.0455  0.0067  0.0096  182 TYR A CB  
2160  C CG  . TYR A  156 ? 0.3129 0.3641 0.2737 0.0442  0.0046  0.0059  182 TYR A CG  
2161  C CD1 . TYR A  156 ? 0.3265 0.3734 0.2843 0.0445  0.0063  0.0017  182 TYR A CD1 
2162  C CD2 . TYR A  156 ? 0.3266 0.3782 0.2904 0.0426  0.0010  0.0065  182 TYR A CD2 
2163  C CE1 . TYR A  156 ? 0.3378 0.3802 0.2955 0.0431  0.0045  -0.0017 182 TYR A CE1 
2164  C CE2 . TYR A  156 ? 0.3383 0.3862 0.3024 0.0410  -0.0009 0.0032  182 TYR A CE2 
2165  C CZ  . TYR A  156 ? 0.3503 0.3933 0.3112 0.0412  0.0008  -0.0008 182 TYR A CZ  
2166  O OH  . TYR A  156 ? 0.3772 0.4156 0.3380 0.0395  -0.0009 -0.0039 182 TYR A OH  
2176  N N   . PHE A  157 ? 0.3059 0.3695 0.2603 0.0438  0.0003  0.0152  183 PHE A N   
2177  C CA  . PHE A  157 ? 0.3083 0.3751 0.2638 0.0429  -0.0035 0.0169  183 PHE A CA  
2178  C C   . PHE A  157 ? 0.3185 0.3897 0.2659 0.0414  -0.0059 0.0158  183 PHE A C   
2179  O O   . PHE A  157 ? 0.3182 0.3913 0.2597 0.0421  -0.0044 0.0169  183 PHE A O   
2180  C CB  . PHE A  157 ? 0.2990 0.3631 0.2605 0.0416  -0.0054 0.0147  183 PHE A CB  
2181  C CG  . PHE A  157 ? 0.3009 0.3618 0.2703 0.0426  -0.0038 0.0160  183 PHE A CG  
2182  C CD1 . PHE A  157 ? 0.3130 0.3740 0.2849 0.0443  -0.0009 0.0193  183 PHE A CD1 
2183  C CD2 . PHE A  157 ? 0.3080 0.3659 0.2819 0.0414  -0.0051 0.0139  183 PHE A CD2 
2184  C CE1 . PHE A  157 ? 0.3182 0.3766 0.2969 0.0446  0.0004  0.0202  183 PHE A CE1 
2185  C CE2 . PHE A  157 ? 0.3142 0.3697 0.2947 0.0420  -0.0038 0.0151  183 PHE A CE2 
2186  C CZ  . PHE A  157 ? 0.3136 0.3697 0.2966 0.0435  -0.0012 0.0181  183 PHE A CZ  
2196  N N   . ASN A  158 ? 0.3261 0.3990 0.2728 0.0391  -0.0095 0.0135  184 ASN A N   
2197  C CA  . ASN A  158 ? 0.3340 0.4116 0.2730 0.0370  -0.0120 0.0121  184 ASN A CA  
2198  C C   . ASN A  158 ? 0.3489 0.4224 0.2821 0.0341  -0.0117 0.0059  184 ASN A C   
2199  O O   . ASN A  158 ? 0.3561 0.4328 0.2834 0.0312  -0.0143 0.0037  184 ASN A O   
2200  C CB  . ASN A  158 ? 0.3378 0.4214 0.2794 0.0360  -0.0162 0.0140  184 ASN A CB  
2201  C CG  . ASN A  158 ? 0.3583 0.4456 0.3048 0.0391  -0.0164 0.0201  184 ASN A CG  
2202  O OD1 . ASN A  158 ? 0.3471 0.4354 0.3002 0.0396  -0.0179 0.0217  184 ASN A OD1 
2203  N ND2 . ASN A  158 ? 0.3675 0.4568 0.3105 0.0414  -0.0148 0.0238  184 ASN A ND2 
2210  N N   . LYS A  159 ? 0.3519 0.4184 0.2861 0.0350  -0.0082 0.0032  185 LYS A N   
2211  C CA  . LYS A  159 ? 0.3579 0.4192 0.2860 0.0328  -0.0071 -0.0026 185 LYS A CA  
2212  C C   . LYS A  159 ? 0.3695 0.4335 0.2875 0.0320  -0.0063 -0.0038 185 LYS A C   
2213  O O   . LYS A  159 ? 0.3591 0.4264 0.2759 0.0342  -0.0046 -0.0002 185 LYS A O   
2214  C CB  . LYS A  159 ? 0.3577 0.4119 0.2894 0.0350  -0.0032 -0.0043 185 LYS A CB  
2215  C CG  . LYS A  159 ? 0.3774 0.4247 0.3035 0.0335  -0.0016 -0.0103 185 LYS A CG  
2216  C CD  . LYS A  159 ? 0.3963 0.4377 0.3263 0.0366  0.0026  -0.0112 185 LYS A CD  
2217  C CE  . LYS A  159 ? 0.4269 0.4611 0.3501 0.0358  0.0050  -0.0169 185 LYS A CE  
2218  N NZ  . LYS A  159 ? 0.4445 0.4732 0.3726 0.0393  0.0088  -0.0176 185 LYS A NZ  
2232  N N   . VAL A  160 ? 0.3913 0.4540 0.3016 0.0284  -0.0076 -0.0086 186 VAL A N   
2233  C CA  . VAL A  160 ? 0.4153 0.4803 0.3151 0.0270  -0.0068 -0.0104 186 VAL A CA  
2234  C C   . VAL A  160 ? 0.4350 0.4926 0.3325 0.0290  -0.0015 -0.0134 186 VAL A C   
2235  O O   . VAL A  160 ? 0.4462 0.4961 0.3435 0.0282  0.0001  -0.0180 186 VAL A O   
2236  C CB  . VAL A  160 ? 0.4363 0.5024 0.3283 0.0218  -0.0100 -0.0149 186 VAL A CB  
2237  C CG1 . VAL A  160 ? 0.4449 0.5132 0.3251 0.0200  -0.0090 -0.0170 186 VAL A CG1 
2238  C CG2 . VAL A  160 ? 0.4403 0.5147 0.3362 0.0200  -0.0153 -0.0118 186 VAL A CG2 
2248  N N   . CYS A  161 ? 0.4356 0.4952 0.3324 0.0319  0.0016  -0.0104 187 CYS A N   
2249  C CA  . CYS A  161 ? 0.4442 0.4981 0.3402 0.0344  0.0070  -0.0126 187 CYS A CA  
2250  C C   . CYS A  161 ? 0.4626 0.5206 0.3537 0.0360  0.0099  -0.0100 187 CYS A C   
2251  O O   . CYS A  161 ? 0.4659 0.5305 0.3568 0.0362  0.0079  -0.0051 187 CYS A O   
2252  C CB  . CYS A  161 ? 0.4358 0.4863 0.3430 0.0374  0.0086  -0.0109 187 CYS A CB  
2253  S SG  . CYS A  161 ? 0.4226 0.4792 0.3396 0.0395  0.0069  -0.0033 187 CYS A SG  
2258  N N   . GLU A  162 ? 0.4714 0.5251 0.3583 0.0372  0.0148  -0.0133 188 GLU A N   
2259  C CA  . GLU A  162 ? 0.4803 0.5372 0.3619 0.0386  0.0183  -0.0115 188 GLU A CA  
2260  C C   . GLU A  162 ? 0.4735 0.5315 0.3641 0.0423  0.0215  -0.0070 188 GLU A C   
2261  O O   . GLU A  162 ? 0.4674 0.5222 0.3671 0.0441  0.0223  -0.0070 188 GLU A O   
2262  C CB  . GLU A  162 ? 0.5268 0.5785 0.3993 0.0381  0.0227  -0.0176 188 GLU A CB  
2263  C CG  . GLU A  162 ? 0.6199 0.6731 0.4792 0.0342  0.0211  -0.0208 188 GLU A CG  
2264  C CD  . GLU A  162 ? 0.7208 0.7728 0.5778 0.0301  0.0161  -0.0240 188 GLU A CD  
2265  O OE1 . GLU A  162 ? 0.7485 0.7948 0.6117 0.0303  0.0156  -0.0262 188 GLU A OE1 
2266  O OE2 . GLU A  162 ? 0.7475 0.8045 0.5963 0.0266  0.0128  -0.0242 188 GLU A OE2 
2273  N N   . LYS A  163 ? 0.4749 0.5375 0.3624 0.0433  0.0235  -0.0032 189 LYS A N   
2274  C CA  . LYS A  163 ? 0.4790 0.5429 0.3738 0.0461  0.0272  0.0008  189 LYS A CA  
2275  C C   . LYS A  163 ? 0.4702 0.5297 0.3667 0.0481  0.0325  -0.0033 189 LYS A C   
2276  O O   . LYS A  163 ? 0.4714 0.5277 0.3598 0.0475  0.0345  -0.0084 189 LYS A O   
2277  C CB  . LYS A  163 ? 0.5141 0.5830 0.4032 0.0463  0.0288  0.0053  189 LYS A CB  
2278  C CG  . LYS A  163 ? 0.5923 0.6658 0.4813 0.0454  0.0242  0.0107  189 LYS A CG  
2279  C CD  . LYS A  163 ? 0.6755 0.7534 0.5585 0.0458  0.0260  0.0154  189 LYS A CD  
2280  C CE  . LYS A  163 ? 0.7399 0.8218 0.6239 0.0459  0.0218  0.0216  189 LYS A CE  
2281  N NZ  . LYS A  163 ? 0.7732 0.8538 0.6685 0.0476  0.0217  0.0257  189 LYS A NZ  
2295  N N   . THR A  164 ? 0.4608 0.5200 0.3677 0.0505  0.0345  -0.0014 190 THR A N   
2296  C CA  . THR A  164 ? 0.4664 0.5224 0.3765 0.0530  0.0393  -0.0047 190 THR A CA  
2297  C C   . THR A  164 ? 0.4747 0.5331 0.3802 0.0543  0.0450  -0.0047 190 THR A C   
2298  O O   . THR A  164 ? 0.4809 0.5442 0.3889 0.0546  0.0465  0.0001  190 THR A O   
2299  C CB  . THR A  164 ? 0.4781 0.5345 0.4013 0.0549  0.0393  -0.0022 190 THR A CB  
2300  O OG1 . THR A  164 ? 0.4849 0.5397 0.4122 0.0534  0.0340  -0.0015 190 THR A OG1 
2301  C CG2 . THR A  164 ? 0.4888 0.5421 0.4164 0.0578  0.0433  -0.0056 190 THR A CG2 
2309  N N   . ASN A  165 ? 0.4711 0.5257 0.3700 0.0551  0.0486  -0.0100 191 ASN A N   
2310  C CA  . ASN A  165 ? 0.4728 0.5295 0.3671 0.0565  0.0546  -0.0107 191 ASN A CA  
2311  C C   . ASN A  165 ? 0.4598 0.5159 0.3634 0.0603  0.0592  -0.0116 191 ASN A C   
2312  O O   . ASN A  165 ? 0.4637 0.5142 0.3680 0.0619  0.0604  -0.0162 191 ASN A O   
2313  C CB  . ASN A  165 ? 0.5010 0.5539 0.3818 0.0550  0.0562  -0.0163 191 ASN A CB  
2314  C CG  . ASN A  165 ? 0.5588 0.6135 0.4342 0.0566  0.0629  -0.0175 191 ASN A CG  
2315  O OD1 . ASN A  165 ? 0.5747 0.6353 0.4503 0.0565  0.0646  -0.0130 191 ASN A OD1 
2316  N ND2 . ASN A  165 ? 0.5883 0.6376 0.4593 0.0581  0.0672  -0.0235 191 ASN A ND2 
2323  N N   . ILE A  166 ? 0.4443 0.5063 0.3553 0.0616  0.0618  -0.0071 192 ILE A N   
2324  C CA  . ILE A  166 ? 0.4392 0.5030 0.3597 0.0651  0.0663  -0.0073 192 ILE A CA  
2325  C C   . ILE A  166 ? 0.4459 0.5116 0.3601 0.0665  0.0730  -0.0093 192 ILE A C   
2326  O O   . ILE A  166 ? 0.4458 0.5162 0.3562 0.0650  0.0746  -0.0060 192 ILE A O   
2327  C CB  . ILE A  166 ? 0.4370 0.5069 0.3692 0.0650  0.0653  -0.0014 192 ILE A CB  
2328  C CG1 . ILE A  166 ? 0.4526 0.5209 0.3896 0.0630  0.0587  0.0010  192 ILE A CG1 
2329  C CG2 . ILE A  166 ? 0.4388 0.5118 0.3814 0.0684  0.0695  -0.0015 192 ILE A CG2 
2330  C CD1 . ILE A  166 ? 0.4696 0.5337 0.4125 0.0643  0.0562  -0.0015 192 ILE A CD1 
2342  N N   . GLU A  167 ? 0.4464 0.5079 0.3586 0.0694  0.0771  -0.0145 193 GLU A N   
2343  C CA  . GLU A  167 ? 0.4575 0.5206 0.3635 0.0710  0.0840  -0.0168 193 GLU A CA  
2344  C C   . GLU A  167 ? 0.4504 0.5222 0.3660 0.0728  0.0882  -0.0125 193 GLU A C   
2345  O O   . GLU A  167 ? 0.4421 0.5165 0.3701 0.0750  0.0879  -0.0106 193 GLU A O   
2346  C CB  . GLU A  167 ? 0.4941 0.5501 0.3968 0.0742  0.0879  -0.0234 193 GLU A CB  
2347  C CG  . GLU A  167 ? 0.5518 0.6078 0.4444 0.0751  0.0946  -0.0269 193 GLU A CG  
2348  C CD  . GLU A  167 ? 0.6326 0.6814 0.5227 0.0789  0.0996  -0.0333 193 GLU A CD  
2349  O OE1 . GLU A  167 ? 0.6349 0.6760 0.5262 0.0797  0.0969  -0.0362 193 GLU A OE1 
2350  O OE2 . GLU A  167 ? 0.6561 0.7066 0.5428 0.0813  0.1066  -0.0353 193 GLU A OE2 
2357  N N   . ASP A  168 ? 0.4472 0.5237 0.3569 0.0716  0.0920  -0.0107 194 ASP A N   
2358  C CA  . ASP A  168 ? 0.4437 0.5289 0.3617 0.0724  0.0961  -0.0063 194 ASP A CA  
2359  C C   . ASP A  168 ? 0.4344 0.5225 0.3631 0.0771  0.1009  -0.0080 194 ASP A C   
2360  O O   . ASP A  168 ? 0.4407 0.5255 0.3652 0.0802  0.1053  -0.0129 194 ASP A O   
2361  C CB  . ASP A  168 ? 0.4719 0.5606 0.3800 0.0707  0.1005  -0.0054 194 ASP A CB  
2362  C CG  . ASP A  168 ? 0.5401 0.6375 0.4560 0.0703  0.1040  -0.0001 194 ASP A CG  
2363  O OD1 . ASP A  168 ? 0.5480 0.6479 0.4691 0.0677  0.1002  0.0051  194 ASP A OD1 
2364  O OD2 . ASP A  168 ? 0.5655 0.6673 0.4823 0.0724  0.1108  -0.0013 194 ASP A OD2 
2369  N N   . GLY A  169 ? 0.4226 0.5167 0.3648 0.0776  0.0998  -0.0039 195 GLY A N   
2370  C CA  . GLY A  169 ? 0.4159 0.5145 0.3696 0.0820  0.1037  -0.0045 195 GLY A CA  
2371  C C   . GLY A  169 ? 0.4182 0.5105 0.3757 0.0856  0.1016  -0.0081 195 GLY A C   
2372  O O   . GLY A  169 ? 0.4225 0.5176 0.3880 0.0902  0.1054  -0.0092 195 GLY A O   
2376  N N   . VAL A  170 ? 0.4111 0.4950 0.3633 0.0836  0.0957  -0.0097 196 VAL A N   
2377  C CA  . VAL A  170 ? 0.4128 0.4895 0.3676 0.0866  0.0937  -0.0130 196 VAL A CA  
2378  C C   . VAL A  170 ? 0.4062 0.4883 0.3765 0.0894  0.0927  -0.0101 196 VAL A C   
2379  O O   . VAL A  170 ? 0.4042 0.4839 0.3789 0.0942  0.0950  -0.0125 196 VAL A O   
2380  C CB  . VAL A  170 ? 0.4262 0.4942 0.3733 0.0832  0.0872  -0.0147 196 VAL A CB  
2381  C CG1 . VAL A  170 ? 0.4252 0.4962 0.3783 0.0796  0.0808  -0.0098 196 VAL A CG1 
2382  C CG2 . VAL A  170 ? 0.4357 0.4946 0.3824 0.0860  0.0866  -0.0192 196 VAL A CG2 
2392  N N   . PHE A  171 ? 0.3963 0.4852 0.3744 0.0865  0.0894  -0.0049 197 PHE A N   
2393  C CA  . PHE A  171 ? 0.3937 0.4886 0.3861 0.0883  0.0879  -0.0019 197 PHE A CA  
2394  C C   . PHE A  171 ? 0.4117 0.5178 0.4133 0.0908  0.0935  0.0002  197 PHE A C   
2395  O O   . PHE A  171 ? 0.4076 0.5194 0.4211 0.0932  0.0931  0.0022  197 PHE A O   
2396  C CB  . PHE A  171 ? 0.3742 0.4709 0.3707 0.0835  0.0817  0.0023  197 PHE A CB  
2397  C CG  . PHE A  171 ? 0.3675 0.4551 0.3558 0.0806  0.0760  0.0010  197 PHE A CG  
2398  C CD1 . PHE A  171 ? 0.3683 0.4483 0.3560 0.0823  0.0730  -0.0019 197 PHE A CD1 
2399  C CD2 . PHE A  171 ? 0.3689 0.4559 0.3505 0.0761  0.0737  0.0029  197 PHE A CD2 
2400  C CE1 . PHE A  171 ? 0.3771 0.4497 0.3579 0.0793  0.0679  -0.0030 197 PHE A CE1 
2401  C CE2 . PHE A  171 ? 0.3790 0.4590 0.3542 0.0736  0.0683  0.0020  197 PHE A CE2 
2402  C CZ  . PHE A  171 ? 0.3760 0.4492 0.3510 0.0750  0.0655  -0.0011 197 PHE A CZ  
2412  N N   . GLU A  172 ? 0.4275 0.5375 0.4238 0.0900  0.0987  0.0002  198 GLU A N   
2413  C CA  . GLU A  172 ? 0.4411 0.5627 0.4454 0.0915  0.1044  0.0025  198 GLU A CA  
2414  C C   . GLU A  172 ? 0.4514 0.5772 0.4654 0.0979  0.1081  0.0012  198 GLU A C   
2415  O O   . GLU A  172 ? 0.4557 0.5929 0.4818 0.0986  0.1096  0.0045  198 GLU A O   
2416  C CB  . GLU A  172 ? 0.4828 0.6051 0.4769 0.0904  0.1100  0.0012  198 GLU A CB  
2417  C CG  . GLU A  172 ? 0.5342 0.6687 0.5350 0.0899  0.1153  0.0044  198 GLU A CG  
2418  C CD  . GLU A  172 ? 0.5907 0.7252 0.5802 0.0880  0.1202  0.0036  198 GLU A CD  
2419  O OE1 . GLU A  172 ? 0.5995 0.7259 0.5773 0.0895  0.1218  -0.0009 198 GLU A OE1 
2420  O OE2 . GLU A  172 ? 0.6042 0.7466 0.5960 0.0847  0.1224  0.0075  198 GLU A OE2 
2427  N N   . THR A  173 ? 0.4547 0.5720 0.4635 0.1025  0.1099  -0.0036 199 THR A N   
2428  C CA  . THR A  173 ? 0.4569 0.5769 0.4742 0.1095  0.1139  -0.0049 199 THR A CA  
2429  C C   . THR A  173 ? 0.4435 0.5624 0.4703 0.1115  0.1087  -0.0033 199 THR A C   
2430  O O   . THR A  173 ? 0.4365 0.5584 0.4716 0.1176  0.1113  -0.0035 199 THR A O   
2431  C CB  . THR A  173 ? 0.5004 0.6107 0.5071 0.1135  0.1189  -0.0109 199 THR A CB  
2432  O OG1 . THR A  173 ? 0.5333 0.6299 0.5299 0.1115  0.1142  -0.0140 199 THR A OG1 
2433  C CG2 . THR A  173 ? 0.5100 0.6227 0.5079 0.1121  0.1249  -0.0124 199 THR A CG2 
2441  N N   . LEU A  174 ? 0.4371 0.5522 0.4631 0.1068  0.1014  -0.0015 200 LEU A N   
2442  C CA  . LEU A  174 ? 0.4345 0.5490 0.4691 0.1081  0.0962  0.0003  200 LEU A CA  
2443  C C   . LEU A  174 ? 0.4208 0.5498 0.4689 0.1065  0.0952  0.0056  200 LEU A C   
2444  O O   . LEU A  174 ? 0.4227 0.5534 0.4731 0.1013  0.0899  0.0086  200 LEU A O   
2445  C CB  . LEU A  174 ? 0.4401 0.5443 0.4675 0.1036  0.0893  -0.0004 200 LEU A CB  
2446  C CG  . LEU A  174 ? 0.4784 0.5680 0.4944 0.1049  0.0888  -0.0054 200 LEU A CG  
2447  C CD1 . LEU A  174 ? 0.4979 0.5834 0.5036 0.1065  0.0948  -0.0097 200 LEU A CD1 
2448  C CD2 . LEU A  174 ? 0.4887 0.5712 0.4980 0.0993  0.0822  -0.0055 200 LEU A CD2 
2460  N N   . THR A  175 ? 0.4033 0.5426 0.4604 0.1111  0.1005  0.0066  201 THR A N   
2461  C CA  . THR A  175 ? 0.3891 0.5438 0.4590 0.1095  0.1007  0.0113  201 THR A CA  
2462  C C   . THR A  175 ? 0.3726 0.5323 0.4541 0.1102  0.0954  0.0145  201 THR A C   
2463  O O   . THR A  175 ? 0.3611 0.5341 0.4535 0.1084  0.0950  0.0183  201 THR A O   
2464  C CB  . THR A  175 ? 0.3983 0.5631 0.4733 0.1140  0.1086  0.0111  201 THR A CB  
2465  O OG1 . THR A  175 ? 0.4116 0.5749 0.4909 0.1221  0.1111  0.0094  201 THR A OG1 
2466  C CG2 . THR A  175 ? 0.4112 0.5720 0.4743 0.1125  0.1138  0.0083  201 THR A CG2 
2474  N N   . ASN A  176 ? 0.3679 0.5173 0.4468 0.1122  0.0911  0.0131  202 ASN A N   
2475  C CA  . ASN A  176 ? 0.3588 0.5115 0.4468 0.1119  0.0854  0.0162  202 ASN A CA  
2476  C C   . ASN A  176 ? 0.3364 0.4799 0.4179 0.1058  0.0785  0.0161  202 ASN A C   
2477  O O   . ASN A  176 ? 0.3281 0.4718 0.4148 0.1051  0.0733  0.0181  202 ASN A O   
2478  C CB  . ASN A  176 ? 0.3989 0.5479 0.4906 0.1198  0.0861  0.0152  202 ASN A CB  
2479  C CG  . ASN A  176 ? 0.4687 0.6264 0.5674 0.1268  0.0930  0.0152  202 ASN A CG  
2480  O OD1 . ASN A  176 ? 0.5057 0.6554 0.6001 0.1329  0.0971  0.0119  202 ASN A OD1 
2481  N ND2 . ASN A  176 ? 0.4765 0.6507 0.5863 0.1260  0.0947  0.0188  202 ASN A ND2 
2488  N N   . LEU A  177 ? 0.3203 0.4559 0.3902 0.1015  0.0784  0.0141  203 LEU A N   
2489  C CA  . LEU A  177 ? 0.3122 0.4391 0.3756 0.0963  0.0725  0.0139  203 LEU A CA  
2490  C C   . LEU A  177 ? 0.2962 0.4311 0.3662 0.0906  0.0688  0.0179  203 LEU A C   
2491  O O   . LEU A  177 ? 0.2817 0.4238 0.3531 0.0875  0.0712  0.0197  203 LEU A O   
2492  C CB  . LEU A  177 ? 0.3153 0.4337 0.3653 0.0936  0.0738  0.0110  203 LEU A CB  
2493  C CG  . LEU A  177 ? 0.3325 0.4403 0.3742 0.0896  0.0683  0.0099  203 LEU A CG  
2494  C CD1 . LEU A  177 ? 0.3495 0.4478 0.3891 0.0928  0.0659  0.0073  203 LEU A CD1 
2495  C CD2 . LEU A  177 ? 0.3352 0.4378 0.3649 0.0868  0.0699  0.0079  203 LEU A CD2 
2507  N N   . GLU A  178 ? 0.2930 0.4259 0.3664 0.0892  0.0632  0.0192  204 GLU A N   
2508  C CA  . GLU A  178 ? 0.2928 0.4317 0.3720 0.0837  0.0592  0.0226  204 GLU A CA  
2509  C C   . GLU A  178 ? 0.2950 0.4242 0.3662 0.0787  0.0546  0.0220  204 GLU A C   
2510  O O   . GLU A  178 ? 0.2934 0.4257 0.3658 0.0734  0.0529  0.0242  204 GLU A O   
2511  C CB  . GLU A  178 ? 0.3150 0.4604 0.4049 0.0858  0.0563  0.0248  204 GLU A CB  
2512  C CG  . GLU A  178 ? 0.3729 0.5303 0.4725 0.0905  0.0606  0.0263  204 GLU A CG  
2513  C CD  . GLU A  178 ? 0.4700 0.6356 0.5807 0.0926  0.0575  0.0291  204 GLU A CD  
2514  O OE1 . GLU A  178 ? 0.4975 0.6569 0.6069 0.0917  0.0523  0.0293  204 GLU A OE1 
2515  O OE2 . GLU A  178 ? 0.5131 0.6917 0.6336 0.0952  0.0602  0.0312  204 GLU A OE2 
2522  N N   . LEU A  179 ? 0.2883 0.4061 0.3516 0.0803  0.0526  0.0191  205 LEU A N   
2523  C CA  . LEU A  179 ? 0.2835 0.3929 0.3396 0.0759  0.0484  0.0186  205 LEU A CA  
2524  C C   . LEU A  179 ? 0.2871 0.3872 0.3316 0.0767  0.0498  0.0152  205 LEU A C   
2525  O O   . LEU A  179 ? 0.2961 0.3909 0.3373 0.0808  0.0514  0.0123  205 LEU A O   
2526  C CB  . LEU A  179 ? 0.2841 0.3896 0.3429 0.0758  0.0432  0.0189  205 LEU A CB  
2527  C CG  . LEU A  179 ? 0.3164 0.4144 0.3693 0.0714  0.0385  0.0185  205 LEU A CG  
2528  C CD1 . LEU A  179 ? 0.3213 0.4198 0.3798 0.0701  0.0338  0.0201  205 LEU A CD1 
2529  C CD2 . LEU A  179 ? 0.3384 0.4257 0.3812 0.0725  0.0381  0.0150  205 LEU A CD2 
2541  N N   . LEU A  180 ? 0.2792 0.3773 0.3173 0.0727  0.0494  0.0156  206 LEU A N   
2542  C CA  . LEU A  180 ? 0.2840 0.3744 0.3107 0.0726  0.0501  0.0128  206 LEU A CA  
2543  C C   . LEU A  180 ? 0.2812 0.3669 0.3036 0.0683  0.0454  0.0137  206 LEU A C   
2544  O O   . LEU A  180 ? 0.2913 0.3806 0.3156 0.0649  0.0447  0.0167  206 LEU A O   
2545  C CB  . LEU A  180 ? 0.2877 0.3819 0.3105 0.0726  0.0552  0.0129  206 LEU A CB  
2546  C CG  . LEU A  180 ? 0.3177 0.4051 0.3279 0.0718  0.0558  0.0104  206 LEU A CG  
2547  C CD1 . LEU A  180 ? 0.3255 0.4053 0.3302 0.0751  0.0562  0.0059  206 LEU A CD1 
2548  C CD2 . LEU A  180 ? 0.3219 0.4141 0.3288 0.0716  0.0610  0.0112  206 LEU A CD2 
2560  N N   . SER A  181 ? 0.2627 0.3403 0.2795 0.0684  0.0424  0.0112  207 SER A N   
2561  C CA  . SER A  181 ? 0.2569 0.3306 0.2696 0.0647  0.0380  0.0119  207 SER A CA  
2562  C C   . SER A  181 ? 0.2678 0.3358 0.2696 0.0643  0.0380  0.0092  207 SER A C   
2563  O O   . SER A  181 ? 0.2649 0.3272 0.2624 0.0660  0.0379  0.0057  207 SER A O   
2564  C CB  . SER A  181 ? 0.2445 0.3150 0.2611 0.0641  0.0336  0.0118  207 SER A CB  
2565  O OG  . SER A  181 ? 0.2534 0.3200 0.2655 0.0609  0.0298  0.0121  207 SER A OG  
2571  N N   . LEU A  182 ? 0.2728 0.3420 0.2698 0.0618  0.0382  0.0110  208 LEU A N   
2572  C CA  . LEU A  182 ? 0.2762 0.3415 0.2626 0.0609  0.0376  0.0092  208 LEU A CA  
2573  C C   . LEU A  182 ? 0.2631 0.3271 0.2474 0.0577  0.0333  0.0113  208 LEU A C   
2574  O O   . LEU A  182 ? 0.2553 0.3179 0.2316 0.0566  0.0326  0.0110  208 LEU A O   
2575  C CB  . LEU A  182 ? 0.2952 0.3638 0.2767 0.0613  0.0421  0.0098  208 LEU A CB  
2576  C CG  . LEU A  182 ? 0.3270 0.3971 0.3092 0.0647  0.0472  0.0074  208 LEU A CG  
2577  C CD1 . LEU A  182 ? 0.3286 0.4044 0.3095 0.0645  0.0518  0.0095  208 LEU A CD1 
2578  C CD2 . LEU A  182 ? 0.3512 0.4149 0.3246 0.0660  0.0477  0.0024  208 LEU A CD2 
2590  N N   . SER A  183 ? 0.2538 0.3181 0.2449 0.0565  0.0303  0.0133  209 SER A N   
2591  C CA  . SER A  183 ? 0.2541 0.3171 0.2441 0.0539  0.0266  0.0153  209 SER A CA  
2592  C C   . SER A  183 ? 0.2575 0.3163 0.2404 0.0533  0.0235  0.0129  209 SER A C   
2593  O O   . SER A  183 ? 0.2634 0.3189 0.2437 0.0543  0.0233  0.0092  209 SER A O   
2594  C CB  . SER A  183 ? 0.2490 0.3122 0.2473 0.0529  0.0241  0.0167  209 SER A CB  
2595  O OG  . SER A  183 ? 0.2560 0.3239 0.2608 0.0529  0.0268  0.0190  209 SER A OG  
2601  N N   . PHE A  184 ? 0.2458 0.3048 0.2256 0.0515  0.0210  0.0149  210 PHE A N   
2602  C CA  . PHE A  184 ? 0.2577 0.3143 0.2315 0.0504  0.0176  0.0131  210 PHE A CA  
2603  C C   . PHE A  184 ? 0.2728 0.3282 0.2382 0.0509  0.0190  0.0096  210 PHE A C   
2604  O O   . PHE A  184 ? 0.2751 0.3269 0.2374 0.0505  0.0176  0.0059  210 PHE A O   
2605  C CB  . PHE A  184 ? 0.2518 0.3054 0.2298 0.0496  0.0142  0.0115  210 PHE A CB  
2606  C CG  . PHE A  184 ? 0.2465 0.3014 0.2312 0.0486  0.0126  0.0148  210 PHE A CG  
2607  C CD1 . PHE A  184 ? 0.2478 0.3036 0.2398 0.0489  0.0140  0.0161  210 PHE A CD1 
2608  C CD2 . PHE A  184 ? 0.2540 0.3093 0.2374 0.0472  0.0098  0.0167  210 PHE A CD2 
2609  C CE1 . PHE A  184 ? 0.2537 0.3102 0.2511 0.0475  0.0127  0.0188  210 PHE A CE1 
2610  C CE2 . PHE A  184 ? 0.2576 0.3131 0.2466 0.0464  0.0087  0.0194  210 PHE A CE2 
2611  C CZ  . PHE A  184 ? 0.2516 0.3074 0.2471 0.0463  0.0103  0.0203  210 PHE A CZ  
2621  N N   . ASN A  185 ? 0.2840 0.3419 0.2454 0.0516  0.0222  0.0109  211 ASN A N   
2622  C CA  . ASN A  185 ? 0.2949 0.3525 0.2471 0.0519  0.0242  0.0083  211 ASN A CA  
2623  C C   . ASN A  185 ? 0.3145 0.3761 0.2623 0.0514  0.0250  0.0122  211 ASN A C   
2624  O O   . ASN A  185 ? 0.3143 0.3780 0.2672 0.0515  0.0257  0.0163  211 ASN A O   
2625  C CB  . ASN A  185 ? 0.2955 0.3523 0.2487 0.0541  0.0289  0.0057  211 ASN A CB  
2626  C CG  . ASN A  185 ? 0.3173 0.3692 0.2729 0.0551  0.0284  0.0017  211 ASN A CG  
2627  O OD1 . ASN A  185 ? 0.3351 0.3830 0.2852 0.0538  0.0262  -0.0017 211 ASN A OD1 
2628  N ND2 . ASN A  185 ? 0.3025 0.3548 0.2661 0.0572  0.0304  0.0021  211 ASN A ND2 
2635  N N   . SER A  186 ? 0.3239 0.3862 0.2620 0.0506  0.0249  0.0110  212 SER A N   
2636  C CA  . SER A  186 ? 0.3432 0.4092 0.2765 0.0504  0.0258  0.0151  212 SER A CA  
2637  C C   . SER A  186 ? 0.3527 0.4199 0.2834 0.0516  0.0313  0.0147  212 SER A C   
2638  O O   . SER A  186 ? 0.3585 0.4251 0.2811 0.0515  0.0330  0.0113  212 SER A O   
2639  C CB  . SER A  186 ? 0.3780 0.4454 0.3021 0.0488  0.0224  0.0145  212 SER A CB  
2640  O OG  . SER A  186 ? 0.4308 0.5018 0.3495 0.0489  0.0235  0.0187  212 SER A OG  
2646  N N   . LEU A  187 ? 0.3494 0.4183 0.2867 0.0524  0.0342  0.0180  213 LEU A N   
2647  C CA  . LEU A  187 ? 0.3566 0.4276 0.2929 0.0534  0.0398  0.0180  213 LEU A CA  
2648  C C   . LEU A  187 ? 0.3732 0.4473 0.3041 0.0528  0.0417  0.0225  213 LEU A C   
2649  O O   . LEU A  187 ? 0.3791 0.4547 0.3043 0.0532  0.0457  0.0216  213 LEU A O   
2650  C CB  . LEU A  187 ? 0.3485 0.4206 0.2957 0.0544  0.0423  0.0187  213 LEU A CB  
2651  C CG  . LEU A  187 ? 0.3600 0.4297 0.3141 0.0555  0.0407  0.0153  213 LEU A CG  
2652  C CD1 . LEU A  187 ? 0.3560 0.4286 0.3200 0.0565  0.0436  0.0166  213 LEU A CD1 
2653  C CD2 . LEU A  187 ? 0.3697 0.4362 0.3182 0.0567  0.0416  0.0098  213 LEU A CD2 
2665  N N   . SER A  188 ? 0.3810 0.4555 0.3140 0.0519  0.0394  0.0275  214 SER A N   
2666  C CA  . SER A  188 ? 0.3995 0.4759 0.3277 0.0514  0.0412  0.0327  214 SER A CA  
2667  C C   . SER A  188 ? 0.4061 0.4843 0.3387 0.0512  0.0464  0.0352  214 SER A C   
2668  O O   . SER A  188 ? 0.4173 0.4957 0.3500 0.0504  0.0473  0.0403  214 SER A O   
2669  C CB  . SER A  188 ? 0.4324 0.5103 0.3484 0.0512  0.0413  0.0319  214 SER A CB  
2670  O OG  . SER A  188 ? 0.4828 0.5603 0.3946 0.0507  0.0361  0.0310  214 SER A OG  
2676  N N   . HIS A  189 ? 0.4016 0.4813 0.3376 0.0520  0.0501  0.0318  215 HIS A N   
2677  C CA  . HIS A  189 ? 0.4115 0.4942 0.3524 0.0516  0.0551  0.0339  215 HIS A CA  
2678  C C   . HIS A  189 ? 0.3917 0.4758 0.3420 0.0527  0.0566  0.0306  215 HIS A C   
2679  O O   . HIS A  189 ? 0.3869 0.4695 0.3369 0.0543  0.0554  0.0260  215 HIS A O   
2680  C CB  . HIS A  189 ? 0.4493 0.5346 0.3817 0.0518  0.0599  0.0340  215 HIS A CB  
2681  C CG  . HIS A  189 ? 0.5366 0.6211 0.4585 0.0510  0.0585  0.0372  215 HIS A CG  
2682  N ND1 . HIS A  189 ? 0.5775 0.6625 0.4981 0.0497  0.0601  0.0431  215 HIS A ND1 
2683  C CD2 . HIS A  189 ? 0.5652 0.6486 0.4777 0.0513  0.0555  0.0354  215 HIS A CD2 
2684  C CE1 . HIS A  189 ? 0.5896 0.6740 0.5002 0.0497  0.0580  0.0451  215 HIS A CE1 
2685  N NE2 . HIS A  189 ? 0.5866 0.6706 0.4922 0.0505  0.0551  0.0405  215 HIS A NE2 
2693  N N   . VAL A  190 ? 0.3816 0.4689 0.3400 0.0518  0.0595  0.0330  216 VAL A N   
2694  C CA  . VAL A  190 ? 0.3818 0.4722 0.3497 0.0530  0.0611  0.0305  216 VAL A CA  
2695  C C   . VAL A  190 ? 0.3916 0.4844 0.3556 0.0554  0.0656  0.0269  216 VAL A C   
2696  O O   . VAL A  190 ? 0.3873 0.4822 0.3454 0.0549  0.0694  0.0283  216 VAL A O   
2697  C CB  . VAL A  190 ? 0.3824 0.4771 0.3592 0.0509  0.0635  0.0340  216 VAL A CB  
2698  C CG1 . VAL A  190 ? 0.3787 0.4785 0.3651 0.0524  0.0657  0.0317  216 VAL A CG1 
2699  C CG2 . VAL A  190 ? 0.3838 0.4751 0.3642 0.0485  0.0595  0.0370  216 VAL A CG2 
2709  N N   . PRO A  191 ? 0.3978 0.4895 0.3640 0.0581  0.0653  0.0223  217 PRO A N   
2710  C CA  . PRO A  191 ? 0.4010 0.4940 0.3628 0.0606  0.0700  0.0187  217 PRO A CA  
2711  C C   . PRO A  191 ? 0.4019 0.5021 0.3692 0.0610  0.0759  0.0204  217 PRO A C   
2712  O O   . PRO A  191 ? 0.3988 0.5033 0.3769 0.0608  0.0761  0.0221  217 PRO A O   
2713  C CB  . PRO A  191 ? 0.4090 0.4989 0.3743 0.0634  0.0685  0.0141  217 PRO A CB  
2714  C CG  . PRO A  191 ? 0.4108 0.4976 0.3808 0.0621  0.0625  0.0152  217 PRO A CG  
2715  C CD  . PRO A  191 ? 0.3881 0.4769 0.3605 0.0589  0.0610  0.0203  217 PRO A CD  
2723  N N   . PRO A  192 ? 0.3986 0.5008 0.3586 0.0614  0.0808  0.0198  218 PRO A N   
2724  C CA  . PRO A  192 ? 0.3934 0.5033 0.3590 0.0619  0.0869  0.0212  218 PRO A CA  
2725  C C   . PRO A  192 ? 0.3866 0.4993 0.3590 0.0661  0.0899  0.0173  218 PRO A C   
2726  O O   . PRO A  192 ? 0.3899 0.4972 0.3606 0.0687  0.0878  0.0132  218 PRO A O   
2727  C CB  . PRO A  192 ? 0.4121 0.5223 0.3663 0.0610  0.0909  0.0217  218 PRO A CB  
2728  C CG  . PRO A  192 ? 0.4227 0.5259 0.3655 0.0616  0.0880  0.0183  218 PRO A CG  
2729  C CD  . PRO A  192 ? 0.3994 0.4976 0.3456 0.0613  0.0812  0.0178  218 PRO A CD  
2737  N N   . LYS A  193 ? 0.3755 0.4965 0.3556 0.0668  0.0949  0.0187  219 LYS A N   
2738  C CA  . LYS A  193 ? 0.3750 0.5004 0.3623 0.0713  0.0987  0.0157  219 LYS A CA  
2739  C C   . LYS A  193 ? 0.3649 0.4886 0.3611 0.0736  0.0945  0.0144  219 LYS A C   
2740  O O   . LYS A  193 ? 0.3643 0.4844 0.3599 0.0778  0.0951  0.0104  219 LYS A O   
2741  C CB  . LYS A  193 ? 0.4042 0.5261 0.3816 0.0745  0.1031  0.0110  219 LYS A CB  
2742  C CG  . LYS A  193 ? 0.4590 0.5838 0.4280 0.0725  0.1080  0.0123  219 LYS A CG  
2743  C CD  . LYS A  193 ? 0.5057 0.6257 0.4629 0.0749  0.1117  0.0073  219 LYS A CD  
2744  C CE  . LYS A  193 ? 0.5398 0.6627 0.4877 0.0726  0.1163  0.0089  219 LYS A CE  
2745  N NZ  . LYS A  193 ? 0.5691 0.6878 0.5053 0.0748  0.1204  0.0036  219 LYS A NZ  
2759  N N   . LEU A  194 ? 0.3540 0.4802 0.3583 0.0708  0.0904  0.0180  220 LEU A N   
2760  C CA  . LEU A  194 ? 0.3523 0.4779 0.3654 0.0725  0.0863  0.0174  220 LEU A CA  
2761  C C   . LEU A  194 ? 0.3492 0.4854 0.3748 0.0750  0.0899  0.0183  220 LEU A C   
2762  O O   . LEU A  194 ? 0.3432 0.4879 0.3726 0.0731  0.0937  0.0210  220 LEU A O   
2763  C CB  . LEU A  194 ? 0.3487 0.4720 0.3641 0.0681  0.0804  0.0205  220 LEU A CB  
2764  C CG  . LEU A  194 ? 0.3759 0.4898 0.3805 0.0660  0.0763  0.0199  220 LEU A CG  
2765  C CD1 . LEU A  194 ? 0.3823 0.4948 0.3904 0.0620  0.0713  0.0232  220 LEU A CD1 
2766  C CD2 . LEU A  194 ? 0.3858 0.4919 0.3852 0.0691  0.0741  0.0154  220 LEU A CD2 
2778  N N   . PRO A  195 ? 0.3547 0.4909 0.3867 0.0794  0.0888  0.0164  221 PRO A N   
2779  C CA  . PRO A  195 ? 0.3571 0.5045 0.4015 0.0823  0.0921  0.0177  221 PRO A CA  
2780  C C   . PRO A  195 ? 0.3615 0.5172 0.4164 0.0782  0.0892  0.0220  221 PRO A C   
2781  O O   . PRO A  195 ? 0.3723 0.5235 0.4275 0.0752  0.0834  0.0231  221 PRO A O   
2782  C CB  . PRO A  195 ? 0.3661 0.5092 0.4130 0.0882  0.0911  0.0147  221 PRO A CB  
2783  C CG  . PRO A  195 ? 0.3712 0.5026 0.4109 0.0862  0.0850  0.0133  221 PRO A CG  
2784  C CD  . PRO A  195 ? 0.3509 0.4773 0.3794 0.0817  0.0847  0.0134  221 PRO A CD  
2792  N N   . SER A  196 ? 0.3516 0.5196 0.4149 0.0777  0.0934  0.0243  222 SER A N   
2793  C CA  . SER A  196 ? 0.3523 0.5295 0.4257 0.0732  0.0914  0.0282  222 SER A CA  
2794  C C   . SER A  196 ? 0.3385 0.5191 0.4221 0.0749  0.0869  0.0289  222 SER A C   
2795  O O   . SER A  196 ? 0.3418 0.5290 0.4330 0.0706  0.0842  0.0318  222 SER A O   
2796  C CB  . SER A  196 ? 0.3784 0.5687 0.4582 0.0723  0.0975  0.0302  222 SER A CB  
2797  O OG  . SER A  196 ? 0.4242 0.6202 0.5086 0.0790  0.1020  0.0283  222 SER A OG  
2803  N N   . SER A  197 ? 0.3199 0.4959 0.4034 0.0810  0.0860  0.0262  223 SER A N   
2804  C CA  . SER A  197 ? 0.3032 0.4807 0.3948 0.0829  0.0814  0.0270  223 SER A CA  
2805  C C   . SER A  197 ? 0.2978 0.4660 0.3849 0.0786  0.0746  0.0272  223 SER A C   
2806  O O   . SER A  197 ? 0.2974 0.4676 0.3912 0.0785  0.0702  0.0285  223 SER A O   
2807  C CB  . SER A  197 ? 0.3060 0.4792 0.3972 0.0908  0.0829  0.0241  223 SER A CB  
2808  O OG  . SER A  197 ? 0.3133 0.4728 0.3915 0.0918  0.0833  0.0204  223 SER A OG  
2814  N N   . LEU A  198 ? 0.2919 0.4500 0.3678 0.0753  0.0736  0.0261  224 LEU A N   
2815  C CA  . LEU A  198 ? 0.2921 0.4414 0.3636 0.0718  0.0676  0.0262  224 LEU A CA  
2816  C C   . LEU A  198 ? 0.2735 0.4285 0.3527 0.0668  0.0639  0.0293  224 LEU A C   
2817  O O   . LEU A  198 ? 0.2590 0.4219 0.3423 0.0630  0.0660  0.0318  224 LEU A O   
2818  C CB  . LEU A  198 ? 0.3066 0.4468 0.3660 0.0687  0.0676  0.0254  224 LEU A CB  
2819  C CG  . LEU A  198 ? 0.3396 0.4699 0.3885 0.0722  0.0683  0.0216  224 LEU A CG  
2820  C CD1 . LEU A  198 ? 0.3506 0.4746 0.3886 0.0687  0.0681  0.0217  224 LEU A CD1 
2821  C CD2 . LEU A  198 ? 0.3441 0.4669 0.3924 0.0743  0.0636  0.0196  224 LEU A CD2 
2833  N N   . ARG A  199 ? 0.2696 0.4199 0.3500 0.0666  0.0586  0.0291  225 ARG A N   
2834  C CA  . ARG A  199 ? 0.2711 0.4247 0.3573 0.0619  0.0544  0.0314  225 ARG A CA  
2835  C C   . ARG A  199 ? 0.2549 0.3973 0.3330 0.0583  0.0502  0.0309  225 ARG A C   
2836  O O   . ARG A  199 ? 0.2536 0.3966 0.3326 0.0529  0.0486  0.0327  225 ARG A O   
2837  C CB  . ARG A  199 ? 0.3141 0.4731 0.4091 0.0650  0.0517  0.0319  225 ARG A CB  
2838  C CG  . ARG A  199 ? 0.3795 0.5524 0.4847 0.0677  0.0554  0.0335  225 ARG A CG  
2839  C CD  . ARG A  199 ? 0.4606 0.6394 0.5747 0.0716  0.0529  0.0345  225 ARG A CD  
2840  N NE  . ARG A  199 ? 0.5222 0.7165 0.6471 0.0732  0.0561  0.0366  225 ARG A NE  
2841  C CZ  . ARG A  199 ? 0.5774 0.7801 0.7116 0.0776  0.0551  0.0381  225 ARG A CZ  
2842  N NH1 . ARG A  199 ? 0.5938 0.7901 0.7273 0.0807  0.0510  0.0377  225 ARG A NH1 
2843  N NH2 . ARG A  199 ? 0.5802 0.7980 0.7246 0.0789  0.0582  0.0403  225 ARG A NH2 
2857  N N   . LYS A  200 ? 0.2441 0.3764 0.3145 0.0611  0.0488  0.0283  226 LYS A N   
2858  C CA  . LYS A  200 ? 0.2468 0.3693 0.3101 0.0582  0.0449  0.0277  226 LYS A CA  
2859  C C   . LYS A  200 ? 0.2474 0.3621 0.3001 0.0597  0.0464  0.0256  226 LYS A C   
2860  O O   . LYS A  200 ? 0.2480 0.3594 0.2976 0.0640  0.0475  0.0229  226 LYS A O   
2861  C CB  . LYS A  200 ? 0.2510 0.3697 0.3163 0.0594  0.0401  0.0268  226 LYS A CB  
2862  C CG  . LYS A  200 ? 0.2689 0.3962 0.3445 0.0582  0.0383  0.0289  226 LYS A CG  
2863  C CD  . LYS A  200 ? 0.2983 0.4212 0.3747 0.0573  0.0330  0.0287  226 LYS A CD  
2864  C CE  . LYS A  200 ? 0.3306 0.4631 0.4168 0.0556  0.0313  0.0311  226 LYS A CE  
2865  N NZ  . LYS A  200 ? 0.3588 0.4874 0.4453 0.0535  0.0262  0.0312  226 LYS A NZ  
2879  N N   . LEU A  201 ? 0.2463 0.3578 0.2932 0.0561  0.0466  0.0268  227 LEU A N   
2880  C CA  . LEU A  201 ? 0.2471 0.3520 0.2836 0.0570  0.0476  0.0253  227 LEU A CA  
2881  C C   . LEU A  201 ? 0.2387 0.3362 0.2699 0.0544  0.0433  0.0255  227 LEU A C   
2882  O O   . LEU A  201 ? 0.2467 0.3442 0.2788 0.0507  0.0424  0.0281  227 LEU A O   
2883  C CB  . LEU A  201 ? 0.2489 0.3577 0.2828 0.0556  0.0523  0.0270  227 LEU A CB  
2884  C CG  . LEU A  201 ? 0.2700 0.3735 0.2928 0.0561  0.0538  0.0261  227 LEU A CG  
2885  C CD1 . LEU A  201 ? 0.2712 0.3711 0.2891 0.0603  0.0544  0.0221  227 LEU A CD1 
2886  C CD2 . LEU A  201 ? 0.2767 0.3851 0.2980 0.0547  0.0588  0.0284  227 LEU A CD2 
2898  N N   . PHE A  202 ? 0.2243 0.3152 0.2503 0.0563  0.0407  0.0228  228 PHE A N   
2899  C CA  . PHE A  202 ? 0.2240 0.3085 0.2452 0.0542  0.0367  0.0229  228 PHE A CA  
2900  C C   . PHE A  202 ? 0.2337 0.3142 0.2448 0.0544  0.0373  0.0221  228 PHE A C   
2901  O O   . PHE A  202 ? 0.2360 0.3139 0.2420 0.0568  0.0379  0.0191  228 PHE A O   
2902  C CB  . PHE A  202 ? 0.2188 0.2994 0.2418 0.0550  0.0325  0.0209  228 PHE A CB  
2903  C CG  . PHE A  202 ? 0.2293 0.3140 0.2617 0.0547  0.0313  0.0219  228 PHE A CG  
2904  C CD1 . PHE A  202 ? 0.2380 0.3272 0.2757 0.0578  0.0335  0.0213  228 PHE A CD1 
2905  C CD2 . PHE A  202 ? 0.2343 0.3179 0.2698 0.0517  0.0278  0.0233  228 PHE A CD2 
2906  C CE1 . PHE A  202 ? 0.2425 0.3360 0.2886 0.0578  0.0318  0.0224  228 PHE A CE1 
2907  C CE2 . PHE A  202 ? 0.2407 0.3283 0.2840 0.0513  0.0263  0.0241  228 PHE A CE2 
2908  C CZ  . PHE A  202 ? 0.2364 0.3293 0.2851 0.0543  0.0282  0.0238  228 PHE A CZ  
2918  N N   . LEU A  203 ? 0.2318 0.3114 0.2398 0.0519  0.0369  0.0249  229 LEU A N   
2919  C CA  . LEU A  203 ? 0.2429 0.3197 0.2415 0.0518  0.0371  0.0251  229 LEU A CA  
2920  C C   . LEU A  203 ? 0.2520 0.3250 0.2485 0.0498  0.0334  0.0270  229 LEU A C   
2921  O O   . LEU A  203 ? 0.2529 0.3252 0.2445 0.0490  0.0340  0.0296  229 LEU A O   
2922  C CB  . LEU A  203 ? 0.2451 0.3256 0.2417 0.0513  0.0417  0.0275  229 LEU A CB  
2923  C CG  . LEU A  203 ? 0.2632 0.3483 0.2618 0.0534  0.0461  0.0259  229 LEU A CG  
2924  C CD1 . LEU A  203 ? 0.2664 0.3560 0.2655 0.0519  0.0505  0.0290  229 LEU A CD1 
2925  C CD2 . LEU A  203 ? 0.2763 0.3588 0.2672 0.0560  0.0469  0.0222  229 LEU A CD2 
2937  N N   . SER A  204 ? 0.2470 0.3176 0.2471 0.0494  0.0296  0.0259  230 SER A N   
2938  C CA  . SER A  204 ? 0.2434 0.3108 0.2423 0.0478  0.0263  0.0275  230 SER A CA  
2939  C C   . SER A  204 ? 0.2471 0.3120 0.2379 0.0487  0.0243  0.0263  230 SER A C   
2940  O O   . SER A  204 ? 0.2615 0.3257 0.2493 0.0499  0.0239  0.0229  230 SER A O   
2941  C CB  . SER A  204 ? 0.2472 0.3132 0.2521 0.0469  0.0232  0.0264  230 SER A CB  
2942  O OG  . SER A  204 ? 0.2697 0.3326 0.2731 0.0457  0.0202  0.0277  230 SER A OG  
2948  N N   . ASN A  205 ? 0.2362 0.3000 0.2234 0.0479  0.0230  0.0290  231 ASN A N   
2949  C CA  . ASN A  205 ? 0.2420 0.3048 0.2222 0.0485  0.0204  0.0283  231 ASN A CA  
2950  C C   . ASN A  205 ? 0.2561 0.3202 0.2292 0.0496  0.0222  0.0260  231 ASN A C   
2951  O O   . ASN A  205 ? 0.2558 0.3187 0.2253 0.0498  0.0204  0.0225  231 ASN A O   
2952  C CB  . ASN A  205 ? 0.2371 0.2979 0.2193 0.0480  0.0164  0.0257  231 ASN A CB  
2953  C CG  . ASN A  205 ? 0.2480 0.3074 0.2349 0.0470  0.0143  0.0280  231 ASN A CG  
2954  O OD1 . ASN A  205 ? 0.2731 0.3321 0.2576 0.0469  0.0118  0.0290  231 ASN A OD1 
2955  N ND2 . ASN A  205 ? 0.2250 0.2841 0.2186 0.0461  0.0154  0.0287  231 ASN A ND2 
2962  N N   . THR A  206 ? 0.2575 0.3236 0.2287 0.0499  0.0261  0.0279  232 THR A N   
2963  C CA  . THR A  206 ? 0.2750 0.3425 0.2393 0.0509  0.0286  0.0260  232 THR A CA  
2964  C C   . THR A  206 ? 0.2947 0.3636 0.2512 0.0507  0.0295  0.0291  232 THR A C   
2965  O O   . THR A  206 ? 0.3028 0.3731 0.2531 0.0513  0.0322  0.0279  232 THR A O   
2966  C CB  . THR A  206 ? 0.2940 0.3634 0.2624 0.0517  0.0331  0.0249  232 THR A CB  
2967  O OG1 . THR A  206 ? 0.2977 0.3690 0.2709 0.0507  0.0353  0.0290  232 THR A OG1 
2968  C CG2 . THR A  206 ? 0.3015 0.3698 0.2760 0.0526  0.0323  0.0214  232 THR A CG2 
2976  N N   . GLN A  207 ? 0.2965 0.3650 0.2528 0.0502  0.0274  0.0332  233 GLN A N   
2977  C CA  . GLN A  207 ? 0.3241 0.3939 0.2733 0.0504  0.0280  0.0371  233 GLN A CA  
2978  C C   . GLN A  207 ? 0.3326 0.4037 0.2804 0.0503  0.0331  0.0396  233 GLN A C   
2979  O O   . GLN A  207 ? 0.3406 0.4132 0.2804 0.0506  0.0344  0.0413  233 GLN A O   
2980  C CB  . GLN A  207 ? 0.3651 0.4364 0.3054 0.0507  0.0256  0.0351  233 GLN A CB  
2981  C CG  . GLN A  207 ? 0.4337 0.5044 0.3753 0.0503  0.0206  0.0331  233 GLN A CG  
2982  C CD  . GLN A  207 ? 0.5266 0.5994 0.4594 0.0498  0.0181  0.0307  233 GLN A CD  
2983  O OE1 . GLN A  207 ? 0.5576 0.6318 0.4829 0.0497  0.0202  0.0296  233 GLN A OE1 
2984  N NE2 . GLN A  207 ? 0.5599 0.6331 0.4933 0.0492  0.0137  0.0297  233 GLN A NE2 
2993  N N   . ILE A  208 ? 0.3320 0.4029 0.2873 0.0496  0.0358  0.0400  234 ILE A N   
2994  C CA  . ILE A  208 ? 0.3471 0.4198 0.3020 0.0490  0.0408  0.0426  234 ILE A CA  
2995  C C   . ILE A  208 ? 0.3657 0.4360 0.3215 0.0479  0.0410  0.0482  234 ILE A C   
2996  O O   . ILE A  208 ? 0.3892 0.4573 0.3519 0.0469  0.0400  0.0490  234 ILE A O   
2997  C CB  . ILE A  208 ? 0.3505 0.4253 0.3133 0.0486  0.0438  0.0402  234 ILE A CB  
2998  C CG1 . ILE A  208 ? 0.3585 0.4346 0.3204 0.0502  0.0436  0.0347  234 ILE A CG1 
2999  C CG2 . ILE A  208 ? 0.3599 0.4375 0.3225 0.0475  0.0491  0.0430  234 ILE A CG2 
3000  C CD1 . ILE A  208 ? 0.3707 0.4496 0.3408 0.0507  0.0465  0.0324  234 ILE A CD1 
3012  N N   . LYS A  209 ? 0.3542 0.4244 0.3025 0.0482  0.0424  0.0520  235 LYS A N   
3013  C CA  . LYS A  209 ? 0.3575 0.4243 0.3054 0.0477  0.0427  0.0577  235 LYS A CA  
3014  C C   . LYS A  209 ? 0.3588 0.4251 0.3089 0.0457  0.0478  0.0607  235 LYS A C   
3015  O O   . LYS A  209 ? 0.3540 0.4161 0.3059 0.0446  0.0485  0.0647  235 LYS A O   
3016  C CB  . LYS A  209 ? 0.3812 0.4482 0.3195 0.0494  0.0411  0.0609  235 LYS A CB  
3017  C CG  . LYS A  209 ? 0.4438 0.5123 0.3797 0.0508  0.0359  0.0582  235 LYS A CG  
3018  C CD  . LYS A  209 ? 0.5201 0.5907 0.4463 0.0522  0.0343  0.0612  235 LYS A CD  
3019  C CE  . LYS A  209 ? 0.5840 0.6574 0.5073 0.0529  0.0295  0.0577  235 LYS A CE  
3020  N NZ  . LYS A  209 ? 0.6070 0.6789 0.5360 0.0537  0.0254  0.0584  235 LYS A NZ  
3034  N N   . TYR A  210 ? 0.3612 0.4315 0.3107 0.0450  0.0516  0.0589  236 TYR A N   
3035  C CA  . TYR A  210 ? 0.3679 0.4388 0.3190 0.0427  0.0568  0.0617  236 TYR A CA  
3036  C C   . TYR A  210 ? 0.3475 0.4234 0.3056 0.0418  0.0594  0.0578  236 TYR A C   
3037  O O   . TYR A  210 ? 0.3465 0.4257 0.3036 0.0436  0.0591  0.0536  236 TYR A O   
3038  C CB  . TYR A  210 ? 0.3931 0.4649 0.3343 0.0431  0.0596  0.0650  236 TYR A CB  
3039  C CG  . TYR A  210 ? 0.4268 0.5002 0.3688 0.0406  0.0655  0.0675  236 TYR A CG  
3040  C CD1 . TYR A  210 ? 0.4499 0.5194 0.3955 0.0380  0.0674  0.0716  236 TYR A CD1 
3041  C CD2 . TYR A  210 ? 0.4440 0.5225 0.3822 0.0407  0.0694  0.0660  236 TYR A CD2 
3042  C CE1 . TYR A  210 ? 0.4627 0.5339 0.4091 0.0351  0.0729  0.0739  236 TYR A CE1 
3043  C CE2 . TYR A  210 ? 0.4621 0.5426 0.4008 0.0382  0.0749  0.0686  236 TYR A CE2 
3044  C CZ  . TYR A  210 ? 0.4803 0.5573 0.4231 0.0352  0.0766  0.0726  236 TYR A CZ  
3045  O OH  . TYR A  210 ? 0.5149 0.5939 0.4583 0.0321  0.0822  0.0753  236 TYR A OH  
3055  N N   . ILE A  211 ? 0.3327 0.4090 0.2979 0.0390  0.0620  0.0593  237 ILE A N   
3056  C CA  . ILE A  211 ? 0.3294 0.4118 0.3022 0.0379  0.0648  0.0565  237 ILE A CA  
3057  C C   . ILE A  211 ? 0.3316 0.4164 0.3029 0.0355  0.0704  0.0598  237 ILE A C   
3058  O O   . ILE A  211 ? 0.3306 0.4121 0.3028 0.0324  0.0719  0.0637  237 ILE A O   
3059  C CB  . ILE A  211 ? 0.3332 0.4156 0.3162 0.0362  0.0627  0.0551  237 ILE A CB  
3060  C CG1 . ILE A  211 ? 0.3433 0.4222 0.3272 0.0382  0.0570  0.0525  237 ILE A CG1 
3061  C CG2 . ILE A  211 ? 0.3307 0.4207 0.3216 0.0355  0.0654  0.0526  237 ILE A CG2 
3062  C CD1 . ILE A  211 ? 0.3594 0.4411 0.3420 0.0416  0.0553  0.0478  237 ILE A CD1 
3074  N N   . SER A  212 ? 0.3290 0.4191 0.2973 0.0367  0.0739  0.0583  238 SER A N   
3075  C CA  . SER A  212 ? 0.3342 0.4275 0.3006 0.0344  0.0797  0.0611  238 SER A CA  
3076  C C   . SER A  212 ? 0.3278 0.4277 0.3050 0.0319  0.0827  0.0602  238 SER A C   
3077  O O   . SER A  212 ? 0.3262 0.4287 0.3118 0.0325  0.0804  0.0571  238 SER A O   
3078  C CB  . SER A  212 ? 0.3560 0.4526 0.3142 0.0369  0.0822  0.0595  238 SER A CB  
3079  O OG  . SER A  212 ? 0.3752 0.4775 0.3382 0.0390  0.0832  0.0545  238 SER A OG  
3085  N N   . GLU A  213 ? 0.3293 0.4324 0.3061 0.0290  0.0880  0.0631  239 GLU A N   
3086  C CA  . GLU A  213 ? 0.3294 0.4403 0.3162 0.0261  0.0915  0.0626  239 GLU A CA  
3087  C C   . GLU A  213 ? 0.3369 0.4563 0.3289 0.0295  0.0925  0.0579  239 GLU A C   
3088  O O   . GLU A  213 ? 0.3475 0.4730 0.3500 0.0286  0.0924  0.0564  239 GLU A O   
3089  C CB  . GLU A  213 ? 0.3511 0.4637 0.3346 0.0224  0.0974  0.0668  239 GLU A CB  
3090  C CG  . GLU A  213 ? 0.3848 0.5056 0.3785 0.0182  0.1011  0.0671  239 GLU A CG  
3091  C CD  . GLU A  213 ? 0.4310 0.5522 0.4215 0.0135  0.1067  0.0716  239 GLU A CD  
3092  O OE1 . GLU A  213 ? 0.4562 0.5700 0.4362 0.0135  0.1076  0.0750  239 GLU A OE1 
3093  O OE2 . GLU A  213 ? 0.4412 0.5704 0.4397 0.0098  0.1103  0.0719  239 GLU A OE2 
3100  N N   . GLU A  214 ? 0.3335 0.4531 0.3182 0.0335  0.0933  0.0556  240 GLU A N   
3101  C CA  . GLU A  214 ? 0.3403 0.4665 0.3284 0.0372  0.0950  0.0511  240 GLU A CA  
3102  C C   . GLU A  214 ? 0.3345 0.4584 0.3251 0.0410  0.0901  0.0468  240 GLU A C   
3103  O O   . GLU A  214 ? 0.3319 0.4607 0.3264 0.0442  0.0917  0.0433  240 GLU A O   
3104  C CB  . GLU A  214 ? 0.3945 0.5212 0.3720 0.0392  0.0990  0.0505  240 GLU A CB  
3105  C CG  . GLU A  214 ? 0.5038 0.6330 0.4773 0.0359  0.1046  0.0546  240 GLU A CG  
3106  C CD  . GLU A  214 ? 0.6502 0.7882 0.6249 0.0367  0.1112  0.0532  240 GLU A CD  
3107  O OE1 . GLU A  214 ? 0.6791 0.8239 0.6628 0.0391  0.1123  0.0498  240 GLU A OE1 
3108  O OE2 . GLU A  214 ? 0.6911 0.8295 0.6578 0.0352  0.1156  0.0558  240 GLU A OE2 
3115  N N   . ASP A  215 ? 0.3393 0.4556 0.3272 0.0410  0.0845  0.0470  241 ASP A N   
3116  C CA  . ASP A  215 ? 0.3506 0.4641 0.3398 0.0443  0.0799  0.0429  241 ASP A CA  
3117  C C   . ASP A  215 ? 0.3518 0.4710 0.3529 0.0455  0.0794  0.0405  241 ASP A C   
3118  O O   . ASP A  215 ? 0.3668 0.4856 0.3684 0.0492  0.0782  0.0366  241 ASP A O   
3119  C CB  . ASP A  215 ? 0.3654 0.4708 0.3512 0.0435  0.0742  0.0441  241 ASP A CB  
3120  C CG  . ASP A  215 ? 0.4315 0.5316 0.4050 0.0443  0.0733  0.0451  241 ASP A CG  
3121  O OD1 . ASP A  215 ? 0.4455 0.5475 0.4123 0.0459  0.0764  0.0437  241 ASP A OD1 
3122  O OD2 . ASP A  215 ? 0.4669 0.5615 0.4375 0.0433  0.0696  0.0474  241 ASP A OD2 
3127  N N   . PHE A  216 ? 0.3411 0.4655 0.3513 0.0424  0.0805  0.0427  242 PHE A N   
3128  C CA  . PHE A  216 ? 0.3453 0.4763 0.3672 0.0434  0.0798  0.0410  242 PHE A CA  
3129  C C   . PHE A  216 ? 0.3738 0.5157 0.4037 0.0417  0.0849  0.0424  242 PHE A C   
3130  O O   . PHE A  216 ? 0.3764 0.5248 0.4169 0.0409  0.0839  0.0424  242 PHE A O   
3131  C CB  . PHE A  216 ? 0.3307 0.4586 0.3578 0.0406  0.0747  0.0420  242 PHE A CB  
3132  C CG  . PHE A  216 ? 0.3289 0.4466 0.3490 0.0411  0.0698  0.0415  242 PHE A CG  
3133  C CD1 . PHE A  216 ? 0.3356 0.4497 0.3525 0.0452  0.0670  0.0381  242 PHE A CD1 
3134  C CD2 . PHE A  216 ? 0.3328 0.4448 0.3500 0.0375  0.0680  0.0445  242 PHE A CD2 
3135  C CE1 . PHE A  216 ? 0.3408 0.4467 0.3518 0.0454  0.0625  0.0377  242 PHE A CE1 
3136  C CE2 . PHE A  216 ? 0.3437 0.4474 0.3553 0.0384  0.0637  0.0442  242 PHE A CE2 
3137  C CZ  . PHE A  216 ? 0.3404 0.4418 0.3491 0.0422  0.0609  0.0408  242 PHE A CZ  
3147  N N   . LYS A  217 ? 0.3912 0.5358 0.4165 0.0407  0.0902  0.0440  243 LYS A N   
3148  C CA  . LYS A  217 ? 0.4054 0.5607 0.4382 0.0382  0.0953  0.0459  243 LYS A CA  
3149  C C   . LYS A  217 ? 0.4021 0.5685 0.4464 0.0411  0.0968  0.0438  243 LYS A C   
3150  O O   . LYS A  217 ? 0.4093 0.5848 0.4631 0.0378  0.0984  0.0458  243 LYS A O   
3151  C CB  . LYS A  217 ? 0.4448 0.6014 0.4698 0.0376  0.1012  0.0473  243 LYS A CB  
3152  C CG  . LYS A  217 ? 0.5047 0.6574 0.5251 0.0318  0.1025  0.0518  243 LYS A CG  
3153  C CD  . LYS A  217 ? 0.5531 0.7062 0.5646 0.0314  0.1080  0.0534  243 LYS A CD  
3154  C CE  . LYS A  217 ? 0.5955 0.7413 0.6002 0.0267  0.1079  0.0580  243 LYS A CE  
3155  N NZ  . LYS A  217 ? 0.6251 0.7720 0.6219 0.0252  0.1137  0.0606  243 LYS A NZ  
3169  N N   . GLY A  218 ? 0.3847 0.5508 0.4281 0.0471  0.0969  0.0402  244 GLY A N   
3170  C CA  . GLY A  218 ? 0.3665 0.5426 0.4205 0.0510  0.0986  0.0385  244 GLY A CA  
3171  C C   . GLY A  218 ? 0.3508 0.5272 0.4129 0.0524  0.0931  0.0375  244 GLY A C   
3172  O O   . GLY A  218 ? 0.3543 0.5393 0.4259 0.0557  0.0940  0.0367  244 GLY A O   
3176  N N   . LEU A  219 ? 0.3308 0.4982 0.3894 0.0500  0.0875  0.0379  245 LEU A N   
3177  C CA  . LEU A  219 ? 0.3147 0.4809 0.3793 0.0512  0.0820  0.0369  245 LEU A CA  
3178  C C   . LEU A  219 ? 0.3010 0.4756 0.3765 0.0465  0.0804  0.0396  245 LEU A C   
3179  O O   . LEU A  219 ? 0.3005 0.4703 0.3761 0.0430  0.0758  0.0404  245 LEU A O   
3180  C CB  . LEU A  219 ? 0.3183 0.4715 0.3741 0.0508  0.0769  0.0359  245 LEU A CB  
3181  C CG  . LEU A  219 ? 0.3345 0.4794 0.3788 0.0545  0.0780  0.0332  245 LEU A CG  
3182  C CD1 . LEU A  219 ? 0.3399 0.4737 0.3771 0.0539  0.0726  0.0323  245 LEU A CD1 
3183  C CD2 . LEU A  219 ? 0.3402 0.4876 0.3865 0.0607  0.0801  0.0298  245 LEU A CD2 
3195  N N   . ILE A  220 ? 0.2884 0.4760 0.3732 0.0468  0.0841  0.0406  246 ILE A N   
3196  C CA  . ILE A  220 ? 0.2898 0.4877 0.3853 0.0420  0.0832  0.0430  246 ILE A CA  
3197  C C   . ILE A  220 ? 0.2847 0.4853 0.3882 0.0433  0.0778  0.0426  246 ILE A C   
3198  O O   . ILE A  220 ? 0.2838 0.4914 0.3947 0.0383  0.0760  0.0445  246 ILE A O   
3199  C CB  . ILE A  220 ? 0.3013 0.5137 0.4045 0.0417  0.0891  0.0444  246 ILE A CB  
3200  C CG1 . ILE A  220 ? 0.3104 0.5311 0.4204 0.0494  0.0911  0.0427  246 ILE A CG1 
3201  C CG2 . ILE A  220 ? 0.3164 0.5259 0.4112 0.0394  0.0945  0.0454  246 ILE A CG2 
3202  C CD1 . ILE A  220 ? 0.3357 0.5727 0.4551 0.0494  0.0970  0.0442  246 ILE A CD1 
3214  N N   . ASN A  221 ? 0.2778 0.4735 0.3799 0.0495  0.0754  0.0401  247 ASN A N   
3215  C CA  . ASN A  221 ? 0.2734 0.4706 0.3821 0.0508  0.0701  0.0399  247 ASN A CA  
3216  C C   . ASN A  221 ? 0.2597 0.4431 0.3606 0.0494  0.0647  0.0388  247 ASN A C   
3217  O O   . ASN A  221 ? 0.2597 0.4425 0.3643 0.0508  0.0602  0.0384  247 ASN A O   
3218  C CB  . ASN A  221 ? 0.3024 0.5034 0.4155 0.0589  0.0711  0.0384  247 ASN A CB  
3219  C CG  . ASN A  221 ? 0.3706 0.5872 0.4945 0.0609  0.0751  0.0398  247 ASN A CG  
3220  O OD1 . ASN A  221 ? 0.3620 0.5890 0.4923 0.0557  0.0762  0.0423  247 ASN A OD1 
3221  N ND2 . ASN A  221 ? 0.4349 0.6546 0.5625 0.0685  0.0768  0.0386  247 ASN A ND2 
3228  N N   . LEU A  222 ? 0.2458 0.4189 0.3364 0.0470  0.0651  0.0384  248 LEU A N   
3229  C CA  . LEU A  222 ? 0.2386 0.3993 0.3220 0.0462  0.0603  0.0374  248 LEU A CA  
3230  C C   . LEU A  222 ? 0.2272 0.3884 0.3149 0.0409  0.0561  0.0388  248 LEU A C   
3231  O O   . LEU A  222 ? 0.2290 0.3937 0.3188 0.0353  0.0574  0.0409  248 LEU A O   
3232  C CB  . LEU A  222 ? 0.2418 0.3930 0.3138 0.0447  0.0619  0.0373  248 LEU A CB  
3233  C CG  . LEU A  222 ? 0.2587 0.3976 0.3221 0.0462  0.0580  0.0355  248 LEU A CG  
3234  C CD1 . LEU A  222 ? 0.2622 0.3986 0.3231 0.0525  0.0582  0.0323  248 LEU A CD1 
3235  C CD2 . LEU A  222 ? 0.2686 0.3999 0.3222 0.0437  0.0590  0.0365  248 LEU A CD2 
3247  N N   . THR A  223 ? 0.2129 0.3706 0.3019 0.0425  0.0513  0.0377  249 THR A N   
3248  C CA  . THR A  223 ? 0.2109 0.3681 0.3030 0.0379  0.0469  0.0386  249 THR A CA  
3249  C C   . THR A  223 ? 0.2171 0.3610 0.3004 0.0367  0.0437  0.0375  249 THR A C   
3250  O O   . THR A  223 ? 0.2250 0.3663 0.3085 0.0319  0.0411  0.0383  249 THR A O   
3251  C CB  . THR A  223 ? 0.2172 0.3814 0.3177 0.0402  0.0438  0.0385  249 THR A CB  
3252  O OG1 . THR A  223 ? 0.2272 0.3841 0.3238 0.0457  0.0418  0.0364  249 THR A OG1 
3253  C CG2 . THR A  223 ? 0.2116 0.3902 0.3218 0.0419  0.0469  0.0399  249 THR A CG2 
3261  N N   . LEU A  224 ? 0.2082 0.3438 0.2837 0.0408  0.0438  0.0357  250 LEU A N   
3262  C CA  . LEU A  224 ? 0.2041 0.3285 0.2718 0.0399  0.0408  0.0348  250 LEU A CA  
3263  C C   . LEU A  224 ? 0.2187 0.3372 0.2774 0.0415  0.0433  0.0343  250 LEU A C   
3264  O O   . LEU A  224 ? 0.2271 0.3470 0.2840 0.0456  0.0458  0.0330  250 LEU A O   
3265  C CB  . LEU A  224 ? 0.1976 0.3178 0.2652 0.0429  0.0365  0.0328  250 LEU A CB  
3266  C CG  . LEU A  224 ? 0.2115 0.3211 0.2717 0.0421  0.0333  0.0318  250 LEU A CG  
3267  C CD1 . LEU A  224 ? 0.2163 0.3241 0.2793 0.0420  0.0288  0.0310  250 LEU A CD1 
3268  C CD2 . LEU A  224 ? 0.2207 0.3242 0.2729 0.0459  0.0342  0.0298  250 LEU A CD2 
3280  N N   . LEU A  225 ? 0.2101 0.3217 0.2628 0.0385  0.0426  0.0354  251 LEU A N   
3281  C CA  . LEU A  225 ? 0.2122 0.3178 0.2558 0.0398  0.0441  0.0354  251 LEU A CA  
3282  C C   . LEU A  225 ? 0.2250 0.3219 0.2635 0.0389  0.0402  0.0353  251 LEU A C   
3283  O O   . LEU A  225 ? 0.2295 0.3243 0.2696 0.0352  0.0389  0.0368  251 LEU A O   
3284  C CB  . LEU A  225 ? 0.2071 0.3148 0.2489 0.0371  0.0484  0.0381  251 LEU A CB  
3285  C CG  . LEU A  225 ? 0.2335 0.3356 0.2654 0.0383  0.0500  0.0388  251 LEU A CG  
3286  C CD1 . LEU A  225 ? 0.2386 0.3412 0.2663 0.0430  0.0511  0.0361  251 LEU A CD1 
3287  C CD2 . LEU A  225 ? 0.2386 0.3426 0.2690 0.0352  0.0544  0.0419  251 LEU A CD2 
3299  N N   . ASP A  226 ? 0.2268 0.3189 0.2593 0.0420  0.0386  0.0333  252 ASP A N   
3300  C CA  . ASP A  226 ? 0.2357 0.3205 0.2635 0.0415  0.0350  0.0331  252 ASP A CA  
3301  C C   . ASP A  226 ? 0.2421 0.3233 0.2611 0.0426  0.0361  0.0337  252 ASP A C   
3302  O O   . ASP A  226 ? 0.2471 0.3278 0.2616 0.0455  0.0364  0.0316  252 ASP A O   
3303  C CB  . ASP A  226 ? 0.2350 0.3178 0.2641 0.0435  0.0312  0.0303  252 ASP A CB  
3304  C CG  . ASP A  226 ? 0.2766 0.3529 0.3009 0.0434  0.0276  0.0296  252 ASP A CG  
3305  O OD1 . ASP A  226 ? 0.2809 0.3542 0.3021 0.0416  0.0275  0.0317  252 ASP A OD1 
3306  O OD2 . ASP A  226 ? 0.2850 0.3591 0.3089 0.0450  0.0249  0.0272  252 ASP A OD2 
3311  N N   . LEU A  227 ? 0.2398 0.3182 0.2560 0.0404  0.0368  0.0367  253 LEU A N   
3312  C CA  . LEU A  227 ? 0.2446 0.3196 0.2523 0.0413  0.0375  0.0382  253 LEU A CA  
3313  C C   . LEU A  227 ? 0.2433 0.3125 0.2481 0.0411  0.0339  0.0391  253 LEU A C   
3314  O O   . LEU A  227 ? 0.2450 0.3114 0.2440 0.0414  0.0343  0.0415  253 LEU A O   
3315  C CB  . LEU A  227 ? 0.2491 0.3253 0.2553 0.0394  0.0417  0.0417  253 LEU A CB  
3316  C CG  . LEU A  227 ? 0.2805 0.3627 0.2877 0.0400  0.0460  0.0413  253 LEU A CG  
3317  C CD1 . LEU A  227 ? 0.2821 0.3653 0.2892 0.0370  0.0500  0.0451  253 LEU A CD1 
3318  C CD2 . LEU A  227 ? 0.2934 0.3757 0.2931 0.0432  0.0466  0.0396  253 LEU A CD2 
3330  N N   . SER A  228 ? 0.2342 0.3019 0.2429 0.0408  0.0304  0.0371  254 SER A N   
3331  C CA  . SER A  228 ? 0.2309 0.2939 0.2377 0.0406  0.0273  0.0378  254 SER A CA  
3332  C C   . SER A  228 ? 0.2380 0.2996 0.2379 0.0430  0.0253  0.0371  254 SER A C   
3333  O O   . SER A  228 ? 0.2370 0.3005 0.2339 0.0447  0.0255  0.0349  254 SER A O   
3334  C CB  . SER A  228 ? 0.2297 0.2920 0.2421 0.0396  0.0243  0.0358  254 SER A CB  
3335  O OG  . SER A  228 ? 0.2363 0.3004 0.2497 0.0413  0.0226  0.0325  254 SER A OG  
3341  N N   . GLY A  229 ? 0.2381 0.2964 0.2354 0.0431  0.0235  0.0391  255 GLY A N   
3342  C CA  . GLY A  229 ? 0.2455 0.3035 0.2368 0.0450  0.0211  0.0388  255 GLY A CA  
3343  C C   . GLY A  229 ? 0.2446 0.3041 0.2288 0.0463  0.0230  0.0405  255 GLY A C   
3344  O O   . GLY A  229 ? 0.2501 0.3106 0.2289 0.0476  0.0209  0.0397  255 GLY A O   
3348  N N   . ASN A  230 ? 0.2417 0.3019 0.2255 0.0456  0.0269  0.0430  256 ASN A N   
3349  C CA  . ASN A  230 ? 0.2443 0.3059 0.2209 0.0466  0.0291  0.0451  256 ASN A CA  
3350  C C   . ASN A  230 ? 0.2574 0.3158 0.2320 0.0466  0.0297  0.0502  256 ASN A C   
3351  O O   . ASN A  230 ? 0.2729 0.3288 0.2516 0.0449  0.0319  0.0522  256 ASN A O   
3352  C CB  . ASN A  230 ? 0.2501 0.3146 0.2278 0.0459  0.0333  0.0445  256 ASN A CB  
3353  C CG  . ASN A  230 ? 0.2703 0.3373 0.2493 0.0468  0.0327  0.0396  256 ASN A CG  
3354  O OD1 . ASN A  230 ? 0.2848 0.3521 0.2586 0.0482  0.0309  0.0372  256 ASN A OD1 
3355  N ND2 . ASN A  230 ? 0.2633 0.3321 0.2494 0.0461  0.0341  0.0380  256 ASN A ND2 
3362  N N   . CYS A  231 ? 0.2459 0.3042 0.2146 0.0485  0.0276  0.0522  257 CYS A N   
3363  C CA  . CYS A  231 ? 0.2551 0.3101 0.2222 0.0494  0.0273  0.0570  257 CYS A CA  
3364  C C   . CYS A  231 ? 0.2624 0.3143 0.2358 0.0490  0.0251  0.0561  257 CYS A C   
3365  O O   . CYS A  231 ? 0.2613 0.3089 0.2382 0.0478  0.0270  0.0581  257 CYS A O   
3366  C CB  . CYS A  231 ? 0.2670 0.3192 0.2327 0.0485  0.0317  0.0614  257 CYS A CB  
3367  S SG  . CYS A  231 ? 0.3411 0.3968 0.2980 0.0492  0.0344  0.0633  257 CYS A SG  
3372  N N   . PRO A  232 ? 0.2627 0.3166 0.2373 0.0497  0.0212  0.0529  258 PRO A N   
3373  C CA  . PRO A  232 ? 0.2650 0.3163 0.2455 0.0490  0.0193  0.0516  258 PRO A CA  
3374  C C   . PRO A  232 ? 0.2625 0.3104 0.2434 0.0505  0.0188  0.0554  258 PRO A C   
3375  O O   . PRO A  232 ? 0.2637 0.3121 0.2398 0.0527  0.0187  0.0591  258 PRO A O   
3376  C CB  . PRO A  232 ? 0.2744 0.3291 0.2549 0.0493  0.0155  0.0474  258 PRO A CB  
3377  C CG  . PRO A  232 ? 0.2801 0.3385 0.2534 0.0508  0.0146  0.0480  258 PRO A CG  
3378  C CD  . PRO A  232 ? 0.2509 0.3092 0.2212 0.0505  0.0186  0.0499  258 PRO A CD  
3386  N N   . ARG A  233 ? 0.2563 0.3006 0.2427 0.0492  0.0186  0.0544  259 ARG A N   
3387  C CA  . ARG A  233 ? 0.2631 0.3036 0.2507 0.0507  0.0183  0.0571  259 ARG A CA  
3388  C C   . ARG A  233 ? 0.2590 0.3034 0.2475 0.0519  0.0139  0.0546  259 ARG A C   
3389  O O   . ARG A  233 ? 0.2407 0.2858 0.2330 0.0501  0.0124  0.0506  259 ARG A O   
3390  C CB  . ARG A  233 ? 0.2806 0.3152 0.2730 0.0482  0.0205  0.0566  259 ARG A CB  
3391  C CG  . ARG A  233 ? 0.3094 0.3404 0.3043 0.0493  0.0195  0.0572  259 ARG A CG  
3392  C CD  . ARG A  233 ? 0.3375 0.3617 0.3356 0.0467  0.0224  0.0573  259 ARG A CD  
3393  N NE  . ARG A  233 ? 0.3669 0.3880 0.3672 0.0479  0.0214  0.0571  259 ARG A NE  
3394  C CZ  . ARG A  233 ? 0.3509 0.3645 0.3524 0.0470  0.0241  0.0581  259 ARG A CZ  
3395  N NH1 . ARG A  233 ? 0.2935 0.3018 0.2943 0.0443  0.0279  0.0594  259 ARG A NH1 
3396  N NH2 . ARG A  233 ? 0.3515 0.3628 0.3549 0.0485  0.0234  0.0577  259 ARG A NH2 
3410  N N   . CYS A  234 ? 0.2589 0.3062 0.2441 0.0548  0.0120  0.0571  260 CYS A N   
3411  C CA  . CYS A  234 ? 0.2757 0.3282 0.2611 0.0555  0.0079  0.0548  260 CYS A CA  
3412  C C   . CYS A  234 ? 0.2739 0.3260 0.2629 0.0571  0.0063  0.0557  260 CYS A C   
3413  O O   . CYS A  234 ? 0.2748 0.3315 0.2646 0.0570  0.0030  0.0533  260 CYS A O   
3414  C CB  . CYS A  234 ? 0.3030 0.3612 0.2822 0.0571  0.0062  0.0562  260 CYS A CB  
3415  S SG  . CYS A  234 ? 0.3728 0.4327 0.3477 0.0550  0.0075  0.0532  260 CYS A SG  
3420  N N   . PHE A  235 ? 0.2614 0.3080 0.2523 0.0584  0.0088  0.0590  261 PHE A N   
3421  C CA  . PHE A  235 ? 0.2530 0.2994 0.2473 0.0603  0.0077  0.0597  261 PHE A CA  
3422  C C   . PHE A  235 ? 0.2331 0.2797 0.2319 0.0576  0.0060  0.0547  261 PHE A C   
3423  O O   . PHE A  235 ? 0.2316 0.2746 0.2324 0.0545  0.0074  0.0520  261 PHE A O   
3424  C CB  . PHE A  235 ? 0.2614 0.3003 0.2566 0.0622  0.0113  0.0637  261 PHE A CB  
3425  C CG  . PHE A  235 ? 0.2692 0.3074 0.2681 0.0644  0.0107  0.0641  261 PHE A CG  
3426  C CD1 . PHE A  235 ? 0.2750 0.3198 0.2738 0.0681  0.0081  0.0665  261 PHE A CD1 
3427  C CD2 . PHE A  235 ? 0.2809 0.3132 0.2837 0.0624  0.0125  0.0618  261 PHE A CD2 
3428  C CE1 . PHE A  235 ? 0.2810 0.3263 0.2838 0.0701  0.0076  0.0666  261 PHE A CE1 
3429  C CE2 . PHE A  235 ? 0.2846 0.3165 0.2908 0.0645  0.0122  0.0619  261 PHE A CE2 
3430  C CZ  . PHE A  235 ? 0.2793 0.3179 0.2858 0.0685  0.0099  0.0643  261 PHE A CZ  
3440  N N   . ASN A  236 ? 0.2233 0.2752 0.2237 0.0584  0.0028  0.0535  262 ASN A N   
3441  C CA  . ASN A  236 ? 0.2239 0.2763 0.2281 0.0559  0.0011  0.0492  262 ASN A CA  
3442  C C   . ASN A  236 ? 0.2374 0.2903 0.2411 0.0524  0.0001  0.0448  262 ASN A C   
3443  O O   . ASN A  236 ? 0.2385 0.2892 0.2454 0.0499  -0.0001 0.0417  262 ASN A O   
3444  C CB  . ASN A  236 ? 0.2255 0.2714 0.2336 0.0554  0.0036  0.0492  262 ASN A CB  
3445  C CG  . ASN A  236 ? 0.2224 0.2698 0.2342 0.0538  0.0017  0.0457  262 ASN A CG  
3446  O OD1 . ASN A  236 ? 0.2221 0.2756 0.2345 0.0549  -0.0011 0.0454  262 ASN A OD1 
3447  N ND2 . ASN A  236 ? 0.2254 0.2680 0.2396 0.0508  0.0029  0.0431  262 ASN A ND2 
3454  N N   . ALA A  237 ? 0.2367 0.2924 0.2363 0.0523  -0.0004 0.0447  263 ALA A N   
3455  C CA  . ALA A  237 ? 0.2508 0.3066 0.2499 0.0496  -0.0009 0.0408  263 ALA A CA  
3456  C C   . ALA A  237 ? 0.2531 0.3120 0.2533 0.0481  -0.0042 0.0371  263 ALA A C   
3457  O O   . ALA A  237 ? 0.2532 0.3169 0.2516 0.0490  -0.0066 0.0375  263 ALA A O   
3458  C CB  . ALA A  237 ? 0.2597 0.3177 0.2536 0.0502  -0.0003 0.0414  263 ALA A CB  
3464  N N   . PRO A  238 ? 0.2597 0.3163 0.2623 0.0456  -0.0044 0.0336  264 PRO A N   
3465  C CA  . PRO A  238 ? 0.2633 0.3220 0.2662 0.0439  -0.0073 0.0301  264 PRO A CA  
3466  C C   . PRO A  238 ? 0.2813 0.3419 0.2797 0.0432  -0.0085 0.0276  264 PRO A C   
3467  O O   . PRO A  238 ? 0.2900 0.3501 0.2884 0.0413  -0.0100 0.0242  264 PRO A O   
3468  C CB  . PRO A  238 ? 0.2705 0.3251 0.2776 0.0418  -0.0067 0.0281  264 PRO A CB  
3469  C CG  . PRO A  238 ? 0.2757 0.3275 0.2832 0.0419  -0.0039 0.0291  264 PRO A CG  
3470  C CD  . PRO A  238 ? 0.2563 0.3086 0.2615 0.0442  -0.0021 0.0329  264 PRO A CD  
3478  N N   . PHE A  239 ? 0.2817 0.3440 0.2758 0.0446  -0.0074 0.0292  265 PHE A N   
3479  C CA  . PHE A  239 ? 0.2946 0.3585 0.2835 0.0440  -0.0080 0.0268  265 PHE A CA  
3480  C C   . PHE A  239 ? 0.2951 0.3628 0.2789 0.0458  -0.0079 0.0298  265 PHE A C   
3481  O O   . PHE A  239 ? 0.2839 0.3517 0.2687 0.0477  -0.0066 0.0338  265 PHE A O   
3482  C CB  . PHE A  239 ? 0.3012 0.3614 0.2904 0.0435  -0.0055 0.0249  265 PHE A CB  
3483  C CG  . PHE A  239 ? 0.3196 0.3781 0.3104 0.0447  -0.0023 0.0280  265 PHE A CG  
3484  C CD1 . PHE A  239 ? 0.3342 0.3900 0.3305 0.0443  -0.0012 0.0292  265 PHE A CD1 
3485  C CD2 . PHE A  239 ? 0.3341 0.3939 0.3207 0.0460  -0.0003 0.0299  265 PHE A CD2 
3486  C CE1 . PHE A  239 ? 0.3407 0.3949 0.3383 0.0447  0.0018  0.0319  265 PHE A CE1 
3487  C CE2 . PHE A  239 ? 0.3441 0.4023 0.3321 0.0467  0.0028  0.0329  265 PHE A CE2 
3488  C CZ  . PHE A  239 ? 0.3401 0.3954 0.3337 0.0459  0.0039  0.0338  265 PHE A CZ  
3498  N N   . PRO A  240 ? 0.3114 0.3819 0.2892 0.0451  -0.0091 0.0279  266 PRO A N   
3499  C CA  . PRO A  240 ? 0.3265 0.4011 0.2989 0.0466  -0.0090 0.0309  266 PRO A CA  
3500  C C   . PRO A  240 ? 0.3440 0.4157 0.3156 0.0481  -0.0052 0.0333  266 PRO A C   
3501  O O   . PRO A  240 ? 0.3547 0.4235 0.3258 0.0474  -0.0030 0.0309  266 PRO A O   
3502  C CB  . PRO A  240 ? 0.3371 0.4142 0.3031 0.0447  -0.0107 0.0271  266 PRO A CB  
3503  C CG  . PRO A  240 ? 0.3376 0.4128 0.3063 0.0422  -0.0125 0.0229  266 PRO A CG  
3504  C CD  . PRO A  240 ? 0.3117 0.3814 0.2867 0.0427  -0.0103 0.0229  266 PRO A CD  
3512  N N   . CYS A  241 ? 0.3479 0.4201 0.3200 0.0503  -0.0042 0.0383  267 CYS A N   
3513  C CA  . CYS A  241 ? 0.3573 0.4262 0.3294 0.0514  -0.0003 0.0411  267 CYS A CA  
3514  C C   . CYS A  241 ? 0.3716 0.4434 0.3376 0.0532  0.0002  0.0453  267 CYS A C   
3515  O O   . CYS A  241 ? 0.3741 0.4491 0.3396 0.0550  -0.0017 0.0486  267 CYS A O   
3516  C CB  . CYS A  241 ? 0.3569 0.4217 0.3354 0.0519  0.0010  0.0433  267 CYS A CB  
3517  S SG  . CYS A  241 ? 0.3829 0.4427 0.3628 0.0518  0.0059  0.0458  267 CYS A SG  
3522  N N   . VAL A  242 ? 0.3810 0.4523 0.3426 0.0530  0.0029  0.0454  268 VAL A N   
3523  C CA  . VAL A  242 ? 0.3868 0.4606 0.3418 0.0546  0.0037  0.0494  268 VAL A CA  
3524  C C   . VAL A  242 ? 0.3784 0.4477 0.3348 0.0552  0.0081  0.0530  268 VAL A C   
3525  O O   . VAL A  242 ? 0.3739 0.4412 0.3309 0.0538  0.0110  0.0508  268 VAL A O   
3526  C CB  . VAL A  242 ? 0.4061 0.4832 0.3535 0.0534  0.0036  0.0465  268 VAL A CB  
3527  C CG1 . VAL A  242 ? 0.4186 0.4983 0.3588 0.0548  0.0046  0.0510  268 VAL A CG1 
3528  C CG2 . VAL A  242 ? 0.4104 0.4913 0.3561 0.0519  -0.0006 0.0425  268 VAL A CG2 
3538  N N   . PRO A  243 ? 0.3745 0.4421 0.3317 0.0572  0.0089  0.0584  269 PRO A N   
3539  C CA  . PRO A  243 ? 0.3760 0.4386 0.3339 0.0572  0.0133  0.0616  269 PRO A CA  
3540  C C   . PRO A  243 ? 0.3799 0.4440 0.3305 0.0575  0.0156  0.0640  269 PRO A C   
3541  O O   . PRO A  243 ? 0.3862 0.4552 0.3304 0.0584  0.0135  0.0645  269 PRO A O   
3542  C CB  . PRO A  243 ? 0.3860 0.4455 0.3462 0.0596  0.0132  0.0666  269 PRO A CB  
3543  C CG  . PRO A  243 ? 0.3958 0.4610 0.3537 0.0618  0.0091  0.0677  269 PRO A CG  
3544  C CD  . PRO A  243 ? 0.3737 0.4438 0.3308 0.0597  0.0060  0.0619  269 PRO A CD  
3552  N N   . CYS A  244 ? 0.3769 0.4370 0.3280 0.0566  0.0200  0.0658  270 CYS A N   
3553  C CA  . CYS A  244 ? 0.3830 0.4440 0.3271 0.0568  0.0227  0.0690  270 CYS A CA  
3554  C C   . CYS A  244 ? 0.4064 0.4670 0.3464 0.0597  0.0219  0.0755  270 CYS A C   
3555  O O   . CYS A  244 ? 0.4032 0.4612 0.3472 0.0614  0.0205  0.0776  270 CYS A O   
3556  C CB  . CYS A  244 ? 0.3714 0.4286 0.3179 0.0547  0.0277  0.0695  270 CYS A CB  
3557  S SG  . CYS A  244 ? 0.3638 0.4239 0.3129 0.0522  0.0292  0.0628  270 CYS A SG  
3562  N N   . ASP A  245 ? 0.4249 0.4884 0.3566 0.0607  0.0224  0.0787  271 ASP A N   
3563  C CA  . ASP A  245 ? 0.4523 0.5165 0.3796 0.0639  0.0212  0.0853  271 ASP A CA  
3564  C C   . ASP A  245 ? 0.4588 0.5153 0.3900 0.0655  0.0237  0.0904  271 ASP A C   
3565  O O   . ASP A  245 ? 0.4645 0.5152 0.3971 0.0636  0.0281  0.0911  271 ASP A O   
3566  C CB  . ASP A  245 ? 0.4987 0.5664 0.4162 0.0642  0.0223  0.0882  271 ASP A CB  
3567  C CG  . ASP A  245 ? 0.5943 0.6699 0.5064 0.0632  0.0189  0.0838  271 ASP A CG  
3568  O OD1 . ASP A  245 ? 0.5985 0.6766 0.5146 0.0624  0.0157  0.0787  271 ASP A OD1 
3569  O OD2 . ASP A  245 ? 0.6380 0.7168 0.5415 0.0630  0.0197  0.0855  271 ASP A OD2 
3574  N N   . GLY A  246 ? 0.4593 0.5158 0.3929 0.0686  0.0210  0.0931  272 GLY A N   
3575  C CA  . GLY A  246 ? 0.4665 0.5151 0.4038 0.0705  0.0233  0.0975  272 GLY A CA  
3576  C C   . GLY A  246 ? 0.4646 0.5072 0.4099 0.0679  0.0250  0.0933  272 GLY A C   
3577  O O   . GLY A  246 ? 0.4744 0.5088 0.4220 0.0680  0.0284  0.0960  272 GLY A O   
3581  N N   . GLY A  247 ? 0.4502 0.4967 0.3995 0.0655  0.0228  0.0868  273 GLY A N   
3582  C CA  . GLY A  247 ? 0.4367 0.4787 0.3931 0.0626  0.0241  0.0825  273 GLY A CA  
3583  C C   . GLY A  247 ? 0.4195 0.4565 0.3763 0.0594  0.0289  0.0826  273 GLY A C   
3584  O O   . GLY A  247 ? 0.4114 0.4430 0.3735 0.0573  0.0309  0.0812  273 GLY A O   
3588  N N   . ALA A  248 ? 0.4043 0.4435 0.3553 0.0588  0.0310  0.0842  274 ALA A N   
3589  C CA  . ALA A  248 ? 0.3924 0.4280 0.3432 0.0557  0.0358  0.0849  274 ALA A CA  
3590  C C   . ALA A  248 ? 0.3711 0.4077 0.3283 0.0520  0.0366  0.0791  274 ALA A C   
3591  O O   . ALA A  248 ? 0.3615 0.4028 0.3213 0.0519  0.0336  0.0743  274 ALA A O   
3592  C CB  . ALA A  248 ? 0.3962 0.4355 0.3392 0.0559  0.0374  0.0871  274 ALA A CB  
3598  N N   . SER A  249 ? 0.3602 0.3924 0.3196 0.0489  0.0408  0.0800  275 SER A N   
3599  C CA  . SER A  249 ? 0.3526 0.3863 0.3182 0.0452  0.0421  0.0755  275 SER A CA  
3600  C C   . SER A  249 ? 0.3402 0.3809 0.3039 0.0445  0.0429  0.0729  275 SER A C   
3601  O O   . SER A  249 ? 0.3347 0.3775 0.2917 0.0458  0.0441  0.0754  275 SER A O   
3602  C CB  . SER A  249 ? 0.3805 0.4080 0.3480 0.0418  0.0466  0.0779  275 SER A CB  
3603  O OG  . SER A  249 ? 0.4185 0.4485 0.3923 0.0379  0.0478  0.0740  275 SER A OG  
3609  N N   . ILE A  250 ? 0.3282 0.3724 0.2979 0.0424  0.0428  0.0682  276 ILE A N   
3610  C CA  . ILE A  250 ? 0.3230 0.3733 0.2921 0.0416  0.0448  0.0658  276 ILE A CA  
3611  C C   . ILE A  250 ? 0.3234 0.3721 0.2910 0.0391  0.0500  0.0695  276 ILE A C   
3612  O O   . ILE A  250 ? 0.3237 0.3673 0.2942 0.0367  0.0518  0.0717  276 ILE A O   
3613  C CB  . ILE A  250 ? 0.3221 0.3761 0.2988 0.0401  0.0438  0.0606  276 ILE A CB  
3614  C CG1 . ILE A  250 ? 0.3299 0.3902 0.3054 0.0406  0.0455  0.0578  276 ILE A CG1 
3615  C CG2 . ILE A  250 ? 0.3241 0.3760 0.3077 0.0364  0.0460  0.0610  276 ILE A CG2 
3616  C CD1 . ILE A  250 ? 0.3216 0.3859 0.3045 0.0402  0.0443  0.0530  276 ILE A CD1 
3628  N N   . ASN A  251 ? 0.3215 0.3741 0.2840 0.0395  0.0525  0.0702  277 ASN A N   
3629  C CA  . ASN A  251 ? 0.3391 0.3907 0.2995 0.0370  0.0577  0.0739  277 ASN A CA  
3630  C C   . ASN A  251 ? 0.3359 0.3937 0.3019 0.0345  0.0605  0.0706  277 ASN A C   
3631  O O   . ASN A  251 ? 0.3378 0.4012 0.3016 0.0360  0.0611  0.0682  277 ASN A O   
3632  C CB  . ASN A  251 ? 0.3709 0.4230 0.3214 0.0391  0.0588  0.0774  277 ASN A CB  
3633  C CG  . ASN A  251 ? 0.4427 0.4930 0.3898 0.0367  0.0642  0.0818  277 ASN A CG  
3634  O OD1 . ASN A  251 ? 0.4681 0.5182 0.4206 0.0330  0.0676  0.0817  277 ASN A OD1 
3635  N ND2 . ASN A  251 ? 0.4570 0.5065 0.3950 0.0384  0.0651  0.0859  277 ASN A ND2 
3642  N N   . ILE A  252 ? 0.3339 0.3909 0.3072 0.0309  0.0622  0.0704  278 ILE A N   
3643  C CA  . ILE A  252 ? 0.3383 0.4024 0.3180 0.0285  0.0647  0.0677  278 ILE A CA  
3644  C C   . ILE A  252 ? 0.3603 0.4244 0.3388 0.0249  0.0702  0.0713  278 ILE A C   
3645  O O   . ILE A  252 ? 0.3792 0.4373 0.3584 0.0217  0.0716  0.0742  278 ILE A O   
3646  C CB  . ILE A  252 ? 0.3325 0.3978 0.3218 0.0266  0.0624  0.0644  278 ILE A CB  
3647  C CG1 . ILE A  252 ? 0.3364 0.4021 0.3267 0.0301  0.0572  0.0606  278 ILE A CG1 
3648  C CG2 . ILE A  252 ? 0.3300 0.4036 0.3264 0.0241  0.0653  0.0624  278 ILE A CG2 
3649  C CD1 . ILE A  252 ? 0.3418 0.4057 0.3395 0.0284  0.0541  0.0586  278 ILE A CD1 
3661  N N   . ASP A  253 ? 0.3546 0.4251 0.3313 0.0251  0.0737  0.0709  279 ASP A N   
3662  C CA  . ASP A  253 ? 0.3595 0.4313 0.3353 0.0213  0.0792  0.0743  279 ASP A CA  
3663  C C   . ASP A  253 ? 0.3589 0.4323 0.3439 0.0162  0.0809  0.0738  279 ASP A C   
3664  O O   . ASP A  253 ? 0.3516 0.4299 0.3446 0.0161  0.0786  0.0699  279 ASP A O   
3665  C CB  . ASP A  253 ? 0.3772 0.4571 0.3508 0.0226  0.0826  0.0730  279 ASP A CB  
3666  C CG  . ASP A  253 ? 0.4388 0.5201 0.4103 0.0188  0.0886  0.0768  279 ASP A CG  
3667  O OD1 . ASP A  253 ? 0.4606 0.5363 0.4230 0.0190  0.0903  0.0811  279 ASP A OD1 
3668  O OD2 . ASP A  253 ? 0.4328 0.5208 0.4118 0.0156  0.0917  0.0756  279 ASP A OD2 
3673  N N   . ARG A  254 ? 0.3648 0.4337 0.3481 0.0118  0.0846  0.0778  280 ARG A N   
3674  C CA  . ARG A  254 ? 0.3754 0.4453 0.3663 0.0058  0.0867  0.0778  280 ARG A CA  
3675  C C   . ARG A  254 ? 0.3566 0.4393 0.3567 0.0044  0.0877  0.0742  280 ARG A C   
3676  O O   . ARG A  254 ? 0.3611 0.4466 0.3695 0.0013  0.0863  0.0722  280 ARG A O   
3677  C CB  . ARG A  254 ? 0.4213 0.4852 0.4070 0.0014  0.0918  0.0830  280 ARG A CB  
3678  C CG  . ARG A  254 ? 0.5082 0.5773 0.4999 -0.0054 0.0965  0.0834  280 ARG A CG  
3679  C CD  . ARG A  254 ? 0.5809 0.6473 0.5795 -0.0102 0.0949  0.0819  280 ARG A CD  
3680  N NE  . ARG A  254 ? 0.6324 0.7054 0.6373 -0.0172 0.0989  0.0820  280 ARG A NE  
3681  C CZ  . ARG A  254 ? 0.6482 0.7346 0.6622 -0.0185 0.0989  0.0789  280 ARG A CZ  
3682  N NH1 . ARG A  254 ? 0.6203 0.7143 0.6379 -0.0129 0.0955  0.0754  280 ARG A NH1 
3683  N NH2 . ARG A  254 ? 0.6540 0.7465 0.6736 -0.0253 0.1026  0.0794  280 ARG A NH2 
3697  N N   . PHE A  255 ? 0.3405 0.4311 0.3393 0.0072  0.0900  0.0733  281 PHE A N   
3698  C CA  . PHE A  255 ? 0.3365 0.4397 0.3439 0.0068  0.0916  0.0703  281 PHE A CA  
3699  C C   . PHE A  255 ? 0.3108 0.4191 0.3213 0.0125  0.0879  0.0657  281 PHE A C   
3700  O O   . PHE A  255 ? 0.2926 0.4110 0.3096 0.0132  0.0896  0.0635  281 PHE A O   
3701  C CB  . PHE A  255 ? 0.3557 0.4645 0.3599 0.0059  0.0976  0.0723  281 PHE A CB  
3702  C CG  . PHE A  255 ? 0.3836 0.4891 0.3861 -0.0003 0.1020  0.0767  281 PHE A CG  
3703  C CD1 . PHE A  255 ? 0.4007 0.5085 0.4112 -0.0063 0.1028  0.0768  281 PHE A CD1 
3704  C CD2 . PHE A  255 ? 0.4111 0.5115 0.4036 -0.0005 0.1056  0.0806  281 PHE A CD2 
3705  C CE1 . PHE A  255 ? 0.4132 0.5178 0.4220 -0.0127 0.1072  0.0806  281 PHE A CE1 
3706  C CE2 . PHE A  255 ? 0.4266 0.5235 0.4173 -0.0065 0.1101  0.0848  281 PHE A CE2 
3707  C CZ  . PHE A  255 ? 0.4224 0.5207 0.4212 -0.0126 0.1108  0.0846  281 PHE A CZ  
3717  N N   . ALA A  256 ? 0.3068 0.4082 0.3130 0.0163  0.0832  0.0644  282 ALA A N   
3718  C CA  . ALA A  256 ? 0.3060 0.4107 0.3141 0.0213  0.0798  0.0601  282 ALA A CA  
3719  C C   . ALA A  256 ? 0.2964 0.4088 0.3157 0.0209  0.0782  0.0571  282 ALA A C   
3720  O O   . ALA A  256 ? 0.2951 0.4127 0.3168 0.0249  0.0776  0.0539  282 ALA A O   
3721  C CB  . ALA A  256 ? 0.3100 0.4059 0.3126 0.0241  0.0747  0.0596  282 ALA A CB  
3727  N N   . PHE A  257 ? 0.2971 0.4097 0.3229 0.0164  0.0773  0.0579  283 PHE A N   
3728  C CA  . PHE A  257 ? 0.3033 0.4236 0.3396 0.0158  0.0752  0.0553  283 PHE A CA  
3729  C C   . PHE A  257 ? 0.2982 0.4279 0.3423 0.0108  0.0791  0.0567  283 PHE A C   
3730  O O   . PHE A  257 ? 0.2885 0.4243 0.3414 0.0086  0.0772  0.0555  283 PHE A O   
3731  C CB  . PHE A  257 ? 0.3201 0.4339 0.3581 0.0144  0.0702  0.0546  283 PHE A CB  
3732  C CG  . PHE A  257 ? 0.3524 0.4564 0.3830 0.0181  0.0664  0.0539  283 PHE A CG  
3733  C CD1 . PHE A  257 ? 0.3742 0.4786 0.4008 0.0236  0.0653  0.0518  283 PHE A CD1 
3734  C CD2 . PHE A  257 ? 0.3781 0.4733 0.4063 0.0161  0.0639  0.0549  283 PHE A CD2 
3735  C CE1 . PHE A  257 ? 0.3915 0.4881 0.4120 0.0266  0.0616  0.0510  283 PHE A CE1 
3736  C CE2 . PHE A  257 ? 0.3949 0.4827 0.4175 0.0196  0.0603  0.0542  283 PHE A CE2 
3737  C CZ  . PHE A  257 ? 0.3934 0.4823 0.4123 0.0246  0.0591  0.0523  283 PHE A CZ  
3747  N N   . GLN A  258 ? 0.2967 0.4285 0.3376 0.0089  0.0844  0.0592  284 GLN A N   
3748  C CA  . GLN A  258 ? 0.2968 0.4376 0.3447 0.0034  0.0883  0.0607  284 GLN A CA  
3749  C C   . GLN A  258 ? 0.3042 0.4595 0.3629 0.0051  0.0888  0.0585  284 GLN A C   
3750  O O   . GLN A  258 ? 0.3054 0.4691 0.3724 0.0001  0.0900  0.0592  284 GLN A O   
3751  C CB  . GLN A  258 ? 0.3074 0.4472 0.3489 0.0011  0.0942  0.0639  284 GLN A CB  
3752  C CG  . GLN A  258 ? 0.3300 0.4761 0.3691 0.0060  0.0976  0.0630  284 GLN A CG  
3753  C CD  . GLN A  258 ? 0.3576 0.5015 0.3890 0.0037  0.1031  0.0665  284 GLN A CD  
3754  O OE1 . GLN A  258 ? 0.3492 0.4906 0.3802 -0.0025 0.1056  0.0696  284 GLN A OE1 
3755  N NE2 . GLN A  258 ? 0.3536 0.4978 0.3782 0.0084  0.1052  0.0659  284 GLN A NE2 
3764  N N   . ASN A  259 ? 0.3129 0.4713 0.3715 0.0118  0.0882  0.0559  285 ASN A N   
3765  C CA  . ASN A  259 ? 0.3232 0.4946 0.3917 0.0147  0.0888  0.0540  285 ASN A CA  
3766  C C   . ASN A  259 ? 0.3046 0.4759 0.3781 0.0181  0.0831  0.0514  285 ASN A C   
3767  O O   . ASN A  259 ? 0.3065 0.4875 0.3876 0.0217  0.0833  0.0498  285 ASN A O   
3768  C CB  . ASN A  259 ? 0.3808 0.5558 0.4460 0.0203  0.0929  0.0528  285 ASN A CB  
3769  C CG  . ASN A  259 ? 0.5015 0.6785 0.5624 0.0174  0.0990  0.0553  285 ASN A CG  
3770  O OD1 . ASN A  259 ? 0.5437 0.7275 0.6100 0.0117  0.1018  0.0576  285 ASN A OD1 
3771  N ND2 . ASN A  259 ? 0.5330 0.7045 0.5837 0.0209  0.1013  0.0550  285 ASN A ND2 
3778  N N   . LEU A  260 ? 0.2906 0.4513 0.3599 0.0172  0.0783  0.0510  286 LEU A N   
3779  C CA  . LEU A  260 ? 0.2773 0.4371 0.3505 0.0201  0.0729  0.0486  286 LEU A CA  
3780  C C   . LEU A  260 ? 0.2582 0.4242 0.3405 0.0150  0.0706  0.0493  286 LEU A C   
3781  O O   . LEU A  260 ? 0.2444 0.4039 0.3258 0.0127  0.0665  0.0489  286 LEU A O   
3782  C CB  . LEU A  260 ? 0.2850 0.4312 0.3491 0.0220  0.0690  0.0477  286 LEU A CB  
3783  C CG  . LEU A  260 ? 0.3182 0.4584 0.3728 0.0269  0.0705  0.0468  286 LEU A CG  
3784  C CD1 . LEU A  260 ? 0.3354 0.4639 0.3825 0.0284  0.0661  0.0460  286 LEU A CD1 
3785  C CD2 . LEU A  260 ? 0.3253 0.4718 0.3828 0.0328  0.0715  0.0441  286 LEU A CD2 
3797  N N   . THR A  261 ? 0.2505 0.4299 0.3417 0.0132  0.0734  0.0501  287 THR A N   
3798  C CA  . THR A  261 ? 0.2504 0.4385 0.3509 0.0076  0.0718  0.0509  287 THR A CA  
3799  C C   . THR A  261 ? 0.2304 0.4208 0.3366 0.0099  0.0662  0.0493  287 THR A C   
3800  O O   . THR A  261 ? 0.2332 0.4260 0.3437 0.0046  0.0634  0.0497  287 THR A O   
3801  C CB  . THR A  261 ? 0.2839 0.4876 0.3931 0.0061  0.0763  0.0523  287 THR A CB  
3802  O OG1 . THR A  261 ? 0.3125 0.5136 0.4159 0.0035  0.0817  0.0540  287 THR A OG1 
3803  C CG2 . THR A  261 ? 0.2954 0.5096 0.4143 -0.0004 0.0747  0.0532  287 THR A CG2 
3811  N N   . GLN A  262 ? 0.2117 0.4012 0.3174 0.0174  0.0647  0.0475  288 GLN A N   
3812  C CA  . GLN A  262 ? 0.2096 0.4009 0.3201 0.0201  0.0596  0.0462  288 GLN A CA  
3813  C C   . GLN A  262 ? 0.2149 0.3924 0.3180 0.0211  0.0551  0.0447  288 GLN A C   
3814  O O   . GLN A  262 ? 0.2217 0.3996 0.3278 0.0236  0.0509  0.0437  288 GLN A O   
3815  C CB  . GLN A  262 ? 0.2193 0.4186 0.3350 0.0277  0.0609  0.0453  288 GLN A CB  
3816  C CG  . GLN A  262 ? 0.2402 0.4549 0.3646 0.0273  0.0656  0.0469  288 GLN A CG  
3817  C CD  . GLN A  262 ? 0.2749 0.5008 0.4085 0.0206  0.0641  0.0488  288 GLN A CD  
3818  O OE1 . GLN A  262 ? 0.3066 0.5371 0.4415 0.0144  0.0671  0.0503  288 GLN A OE1 
3819  N NE2 . GLN A  262 ? 0.2603 0.4904 0.3998 0.0215  0.0593  0.0486  288 GLN A NE2 
3828  N N   . LEU A  263 ? 0.2097 0.3753 0.3033 0.0191  0.0557  0.0449  289 LEU A N   
3829  C CA  . LEU A  263 ? 0.2257 0.3790 0.3125 0.0202  0.0517  0.0435  289 LEU A CA  
3830  C C   . LEU A  263 ? 0.2210 0.3737 0.3113 0.0157  0.0474  0.0435  289 LEU A C   
3831  O O   . LEU A  263 ? 0.2167 0.3722 0.3096 0.0093  0.0482  0.0448  289 LEU A O   
3832  C CB  . LEU A  263 ? 0.2420 0.3840 0.3185 0.0192  0.0535  0.0442  289 LEU A CB  
3833  C CG  . LEU A  263 ? 0.2670 0.3981 0.3355 0.0235  0.0507  0.0426  289 LEU A CG  
3834  C CD1 . LEU A  263 ? 0.2697 0.4026 0.3364 0.0299  0.0520  0.0409  289 LEU A CD1 
3835  C CD2 . LEU A  263 ? 0.2804 0.4014 0.3401 0.0214  0.0516  0.0440  289 LEU A CD2 
3847  N N   . ARG A  264 ? 0.2217 0.3717 0.3124 0.0189  0.0430  0.0418  290 ARG A N   
3848  C CA  . ARG A  264 ? 0.2199 0.3681 0.3125 0.0155  0.0385  0.0414  290 ARG A CA  
3849  C C   . ARG A  264 ? 0.2191 0.3537 0.3033 0.0163  0.0360  0.0402  290 ARG A C   
3850  O O   . ARG A  264 ? 0.2170 0.3471 0.3001 0.0120  0.0338  0.0400  290 ARG A O   
3851  C CB  . ARG A  264 ? 0.2261 0.3824 0.3260 0.0186  0.0353  0.0408  290 ARG A CB  
3852  C CG  . ARG A  264 ? 0.2389 0.4093 0.3487 0.0151  0.0353  0.0423  290 ARG A CG  
3853  C CD  . ARG A  264 ? 0.2557 0.4363 0.3704 0.0171  0.0398  0.0435  290 ARG A CD  
3854  N NE  . ARG A  264 ? 0.2702 0.4657 0.3950 0.0136  0.0399  0.0451  290 ARG A NE  
3855  C CZ  . ARG A  264 ? 0.2995 0.5069 0.4307 0.0146  0.0437  0.0463  290 ARG A CZ  
3856  N NH1 . ARG A  264 ? 0.2829 0.4881 0.4107 0.0191  0.0480  0.0461  290 ARG A NH1 
3857  N NH2 . ARG A  264 ? 0.2913 0.5132 0.4322 0.0111  0.0433  0.0479  290 ARG A NH2 
3871  N N   . TYR A  265 ? 0.2199 0.3483 0.2982 0.0217  0.0364  0.0391  291 TYR A N   
3872  C CA  . TYR A  265 ? 0.2224 0.3393 0.2932 0.0228  0.0339  0.0380  291 TYR A CA  
3873  C C   . TYR A  265 ? 0.2167 0.3273 0.2798 0.0243  0.0367  0.0386  291 TYR A C   
3874  O O   . TYR A  265 ? 0.2118 0.3252 0.2737 0.0278  0.0392  0.0384  291 TYR A O   
3875  C CB  . TYR A  265 ? 0.2346 0.3502 0.3053 0.0279  0.0307  0.0360  291 TYR A CB  
3876  C CG  . TYR A  265 ? 0.2622 0.3833 0.3398 0.0272  0.0274  0.0357  291 TYR A CG  
3877  C CD1 . TYR A  265 ? 0.2785 0.4105 0.3639 0.0285  0.0283  0.0364  291 TYR A CD1 
3878  C CD2 . TYR A  265 ? 0.2892 0.4050 0.3654 0.0255  0.0234  0.0349  291 TYR A CD2 
3879  C CE1 . TYR A  265 ? 0.2939 0.4316 0.3855 0.0280  0.0250  0.0366  291 TYR A CE1 
3880  C CE2 . TYR A  265 ? 0.3020 0.4230 0.3839 0.0246  0.0203  0.0349  291 TYR A CE2 
3881  C CZ  . TYR A  265 ? 0.3151 0.4472 0.4047 0.0258  0.0209  0.0359  291 TYR A CZ  
3882  O OH  . TYR A  265 ? 0.3573 0.4952 0.4525 0.0252  0.0176  0.0363  291 TYR A OH  
3892  N N   . LEU A  266 ? 0.2131 0.3152 0.2706 0.0219  0.0363  0.0394  292 LEU A N   
3893  C CA  . LEU A  266 ? 0.2128 0.3087 0.2626 0.0234  0.0385  0.0404  292 LEU A CA  
3894  C C   . LEU A  266 ? 0.2035 0.2903 0.2479 0.0243  0.0354  0.0398  292 LEU A C   
3895  O O   . LEU A  266 ? 0.2036 0.2864 0.2487 0.0210  0.0339  0.0401  292 LEU A O   
3896  C CB  . LEU A  266 ? 0.2285 0.3239 0.2772 0.0191  0.0424  0.0431  292 LEU A CB  
3897  C CG  . LEU A  266 ? 0.2544 0.3431 0.2946 0.0204  0.0447  0.0450  292 LEU A CG  
3898  C CD1 . LEU A  266 ? 0.2579 0.3495 0.2948 0.0252  0.0461  0.0443  292 LEU A CD1 
3899  C CD2 . LEU A  266 ? 0.2645 0.3525 0.3041 0.0159  0.0487  0.0479  292 LEU A CD2 
3911  N N   . ASN A  267 ? 0.1942 0.2777 0.2332 0.0285  0.0345  0.0388  293 ASN A N   
3912  C CA  . ASN A  267 ? 0.2078 0.2839 0.2420 0.0296  0.0315  0.0384  293 ASN A CA  
3913  C C   . ASN A  267 ? 0.2179 0.2894 0.2446 0.0309  0.0333  0.0403  293 ASN A C   
3914  O O   . ASN A  267 ? 0.2171 0.2899 0.2398 0.0339  0.0342  0.0398  293 ASN A O   
3915  C CB  . ASN A  267 ? 0.2090 0.2852 0.2432 0.0330  0.0282  0.0355  293 ASN A CB  
3916  C CG  . ASN A  267 ? 0.2234 0.2936 0.2551 0.0331  0.0246  0.0347  293 ASN A CG  
3917  O OD1 . ASN A  267 ? 0.2177 0.2831 0.2462 0.0319  0.0248  0.0363  293 ASN A OD1 
3918  N ND2 . ASN A  267 ? 0.2336 0.3036 0.2661 0.0349  0.0216  0.0323  293 ASN A ND2 
3924  N N   . LEU A  268 ? 0.2237 0.2897 0.2482 0.0287  0.0338  0.0425  294 LEU A N   
3925  C CA  . LEU A  268 ? 0.2307 0.2918 0.2481 0.0301  0.0351  0.0450  294 LEU A CA  
3926  C C   . LEU A  268 ? 0.2223 0.2772 0.2372 0.0311  0.0320  0.0451  294 LEU A C   
3927  O O   . LEU A  268 ? 0.2273 0.2770 0.2381 0.0312  0.0331  0.0479  294 LEU A O   
3928  C CB  . LEU A  268 ? 0.2437 0.3033 0.2604 0.0270  0.0392  0.0483  294 LEU A CB  
3929  C CG  . LEU A  268 ? 0.2774 0.3437 0.2958 0.0261  0.0428  0.0487  294 LEU A CG  
3930  C CD1 . LEU A  268 ? 0.2876 0.3526 0.3071 0.0216  0.0466  0.0515  294 LEU A CD1 
3931  C CD2 . LEU A  268 ? 0.2879 0.3553 0.3000 0.0296  0.0442  0.0494  294 LEU A CD2 
3943  N N   . SER A  269 ? 0.2134 0.2688 0.2306 0.0320  0.0284  0.0422  295 SER A N   
3944  C CA  . SER A  269 ? 0.2214 0.2721 0.2367 0.0330  0.0256  0.0421  295 SER A CA  
3945  C C   . SER A  269 ? 0.2281 0.2779 0.2371 0.0364  0.0249  0.0432  295 SER A C   
3946  O O   . SER A  269 ? 0.2223 0.2755 0.2287 0.0383  0.0250  0.0422  295 SER A O   
3947  C CB  . SER A  269 ? 0.2353 0.2874 0.2540 0.0332  0.0220  0.0388  295 SER A CB  
3948  O OG  . SER A  269 ? 0.2670 0.3204 0.2914 0.0300  0.0221  0.0379  295 SER A OG  
3954  N N   . SER A  270 ? 0.2272 0.2724 0.2334 0.0373  0.0243  0.0453  296 SER A N   
3955  C CA  . SER A  270 ? 0.2361 0.2812 0.2366 0.0404  0.0232  0.0468  296 SER A CA  
3956  C C   . SER A  270 ? 0.2424 0.2897 0.2379 0.0416  0.0256  0.0487  296 SER A C   
3957  O O   . SER A  270 ? 0.2466 0.2972 0.2384 0.0435  0.0242  0.0476  296 SER A O   
3958  C CB  . SER A  270 ? 0.2512 0.2986 0.2515 0.0420  0.0192  0.0437  296 SER A CB  
3959  O OG  . SER A  270 ? 0.2692 0.3162 0.2651 0.0444  0.0174  0.0454  296 SER A OG  
3965  N N   . THR A  271 ? 0.2400 0.2858 0.2356 0.0399  0.0293  0.0513  297 THR A N   
3966  C CA  . THR A  271 ? 0.2449 0.2918 0.2353 0.0406  0.0322  0.0541  297 THR A CA  
3967  C C   . THR A  271 ? 0.2572 0.2985 0.2434 0.0414  0.0339  0.0592  297 THR A C   
3968  O O   . THR A  271 ? 0.2649 0.3062 0.2467 0.0415  0.0368  0.0623  297 THR A O   
3969  C CB  . THR A  271 ? 0.2553 0.3053 0.2488 0.0381  0.0356  0.0534  297 THR A CB  
3970  O OG1 . THR A  271 ? 0.2575 0.3042 0.2554 0.0347  0.0374  0.0545  297 THR A OG1 
3971  C CG2 . THR A  271 ? 0.2609 0.3164 0.2580 0.0384  0.0342  0.0490  297 THR A CG2 
3979  N N   . SER A  272 ? 0.2628 0.2997 0.2501 0.0422  0.0321  0.0601  298 SER A N   
3980  C CA  . SER A  272 ? 0.2798 0.3108 0.2638 0.0437  0.0335  0.0648  298 SER A CA  
3981  C C   . SER A  272 ? 0.2961 0.3220 0.2795 0.0410  0.0382  0.0679  298 SER A C   
3982  O O   . SER A  272 ? 0.3058 0.3281 0.2842 0.0425  0.0403  0.0725  298 SER A O   
3983  C CB  . SER A  272 ? 0.2954 0.3289 0.2729 0.0475  0.0319  0.0675  298 SER A CB  
3984  O OG  . SER A  272 ? 0.3185 0.3556 0.2968 0.0495  0.0275  0.0649  298 SER A OG  
3990  N N   . LEU A  273 ? 0.2904 0.3164 0.2789 0.0368  0.0399  0.0655  299 LEU A N   
3991  C CA  . LEU A  273 ? 0.2907 0.3122 0.2790 0.0333  0.0444  0.0680  299 LEU A CA  
3992  C C   . LEU A  273 ? 0.3009 0.3127 0.2889 0.0326  0.0460  0.0703  299 LEU A C   
3993  O O   . LEU A  273 ? 0.2947 0.3041 0.2861 0.0323  0.0440  0.0680  299 LEU A O   
3994  C CB  . LEU A  273 ? 0.2850 0.3107 0.2793 0.0288  0.0455  0.0646  299 LEU A CB  
3995  C CG  . LEU A  273 ? 0.3030 0.3374 0.2981 0.0288  0.0459  0.0629  299 LEU A CG  
3996  C CD1 . LEU A  273 ? 0.3082 0.3478 0.3107 0.0254  0.0455  0.0591  299 LEU A CD1 
3997  C CD2 . LEU A  273 ? 0.3061 0.3403 0.2967 0.0280  0.0502  0.0666  299 LEU A CD2 
4009  N N   A ARG A  274 ? 0.3055 0.3111 0.2889 0.0324  0.0498  0.0750  300 ARG A N   
4010  N N   B ARG A  274 ? 0.3058 0.3115 0.2892 0.0324  0.0498  0.0750  300 ARG A N   
4011  C CA  A ARG A  274 ? 0.3174 0.3120 0.2996 0.0314  0.0525  0.0777  300 ARG A CA  
4012  C CA  B ARG A  274 ? 0.3181 0.3128 0.3003 0.0315  0.0525  0.0778  300 ARG A CA  
4013  C C   A ARG A  274 ? 0.3358 0.3269 0.3194 0.0252  0.0569  0.0777  300 ARG A C   
4014  C C   B ARG A  274 ? 0.3356 0.3263 0.3187 0.0254  0.0571  0.0782  300 ARG A C   
4015  O O   A ARG A  274 ? 0.3429 0.3261 0.3278 0.0222  0.0588  0.0774  300 ARG A O   
4016  O O   B ARG A  274 ? 0.3425 0.3244 0.3263 0.0227  0.0593  0.0784  300 ARG A O   
4017  C CB  A ARG A  274 ? 0.3272 0.3163 0.3028 0.0359  0.0538  0.0836  300 ARG A CB  
4018  C CB  B ARG A  274 ? 0.3297 0.3195 0.3053 0.0364  0.0533  0.0834  300 ARG A CB  
4019  C CG  A ARG A  274 ? 0.3300 0.3199 0.3047 0.0417  0.0500  0.0843  300 ARG A CG  
4020  C CG  B ARG A  274 ? 0.3369 0.3292 0.3124 0.0419  0.0490  0.0833  300 ARG A CG  
4021  C CD  A ARG A  274 ? 0.3299 0.3306 0.3039 0.0443  0.0460  0.0825  300 ARG A CD  
4022  C CD  B ARG A  274 ? 0.3558 0.3457 0.3252 0.0471  0.0491  0.0891  300 ARG A CD  
4023  N NE  A ARG A  274 ? 0.3300 0.3321 0.3022 0.0497  0.0426  0.0843  300 ARG A NE  
4024  N NE  B ARG A  274 ? 0.3591 0.3540 0.3291 0.0519  0.0445  0.0885  300 ARG A NE  
4025  C CZ  A ARG A  274 ? 0.3270 0.3370 0.2964 0.0526  0.0394  0.0844  300 ARG A CZ  
4026  C CZ  B ARG A  274 ? 0.3464 0.3380 0.3193 0.0540  0.0431  0.0879  300 ARG A CZ  
4027  N NH1 A ARG A  274 ? 0.3271 0.3389 0.2954 0.0571  0.0363  0.0861  300 ARG A NH1 
4028  N NH1 B ARG A  274 ? 0.3385 0.3362 0.3120 0.0580  0.0389  0.0874  300 ARG A NH1 
4029  N NH2 A ARG A  274 ? 0.2900 0.3065 0.2577 0.0511  0.0393  0.0826  300 ARG A NH2 
4030  N NH2 B ARG A  274 ? 0.3257 0.3081 0.3009 0.0518  0.0460  0.0874  300 ARG A NH2 
4057  N N   . LYS A  275 ? 0.3412 0.3383 0.3245 0.0230  0.0587  0.0780  301 LYS A N   
4058  C CA  . LYS A  275 ? 0.3629 0.3588 0.3477 0.0169  0.0629  0.0783  301 LYS A CA  
4059  C C   . LYS A  275 ? 0.3614 0.3692 0.3518 0.0146  0.0617  0.0743  301 LYS A C   
4060  O O   . LYS A  275 ? 0.3637 0.3793 0.3538 0.0181  0.0594  0.0732  301 LYS A O   
4061  C CB  . LYS A  275 ? 0.4107 0.4030 0.3892 0.0170  0.0672  0.0836  301 LYS A CB  
4062  C CG  . LYS A  275 ? 0.5143 0.4952 0.4866 0.0204  0.0686  0.0886  301 LYS A CG  
4063  C CD  . LYS A  275 ? 0.6045 0.5734 0.5770 0.0163  0.0720  0.0893  301 LYS A CD  
4064  C CE  . LYS A  275 ? 0.6693 0.6264 0.6353 0.0201  0.0743  0.0949  301 LYS A CE  
4065  N NZ  . LYS A  275 ? 0.7104 0.6544 0.6754 0.0156  0.0787  0.0959  301 LYS A NZ  
4079  N N   . ILE A  276 ? 0.3549 0.3641 0.3504 0.0087  0.0633  0.0722  302 ILE A N   
4080  C CA  . ILE A  276 ? 0.3553 0.3758 0.3566 0.0064  0.0626  0.0690  302 ILE A CA  
4081  C C   . ILE A  276 ? 0.3565 0.3776 0.3575 0.0013  0.0677  0.0713  302 ILE A C   
4082  O O   . ILE A  276 ? 0.3596 0.3736 0.3604 -0.0037 0.0704  0.0723  302 ILE A O   
4083  C CB  . ILE A  276 ? 0.3688 0.3922 0.3770 0.0036  0.0597  0.0646  302 ILE A CB  
4084  C CG1 . ILE A  276 ? 0.3875 0.4101 0.3956 0.0086  0.0549  0.0625  302 ILE A CG1 
4085  C CG2 . ILE A  276 ? 0.3728 0.4086 0.3876 0.0013  0.0594  0.0621  302 ILE A CG2 
4086  C CD1 . ILE A  276 ? 0.4101 0.4337 0.4234 0.0062  0.0521  0.0588  302 ILE A CD1 
4098  N N   . ASN A  277 ? 0.3471 0.3763 0.3477 0.0024  0.0692  0.0721  303 ASN A N   
4099  C CA  . ASN A  277 ? 0.3369 0.3682 0.3376 -0.0025 0.0741  0.0742  303 ASN A CA  
4100  C C   . ASN A  277 ? 0.3260 0.3656 0.3354 -0.0079 0.0741  0.0708  303 ASN A C   
4101  O O   . ASN A  277 ? 0.3174 0.3678 0.3321 -0.0060 0.0719  0.0679  303 ASN A O   
4102  C CB  . ASN A  277 ? 0.3444 0.3819 0.3415 0.0008  0.0758  0.0759  303 ASN A CB  
4103  C CG  . ASN A  277 ? 0.3823 0.4210 0.3781 -0.0038 0.0814  0.0789  303 ASN A CG  
4104  O OD1 . ASN A  277 ? 0.3934 0.4303 0.3923 -0.0101 0.0840  0.0791  303 ASN A OD1 
4105  N ND2 . ASN A  277 ? 0.3887 0.4303 0.3793 -0.0010 0.0835  0.0812  303 ASN A ND2 
4112  N N   . ALA A  278 ? 0.3279 0.3628 0.3389 -0.0145 0.0765  0.0712  304 ALA A N   
4113  C CA  . ALA A  278 ? 0.3324 0.3758 0.3517 -0.0205 0.0763  0.0683  304 ALA A CA  
4114  C C   . ALA A  278 ? 0.3344 0.3917 0.3584 -0.0211 0.0782  0.0681  304 ALA A C   
4115  O O   . ALA A  278 ? 0.3376 0.4058 0.3697 -0.0228 0.0763  0.0652  304 ALA A O   
4116  C CB  . ALA A  278 ? 0.3375 0.3727 0.3558 -0.0282 0.0797  0.0694  304 ALA A CB  
4122  N N   . ALA A  279 ? 0.3279 0.3851 0.3471 -0.0197 0.0819  0.0713  305 ALA A N   
4123  C CA  . ALA A  279 ? 0.3228 0.3926 0.3457 -0.0198 0.0844  0.0714  305 ALA A CA  
4124  C C   . ALA A  279 ? 0.3137 0.3938 0.3407 -0.0138 0.0809  0.0683  305 ALA A C   
4125  O O   . ALA A  279 ? 0.3080 0.4002 0.3411 -0.0144 0.0823  0.0671  305 ALA A O   
4126  C CB  . ALA A  279 ? 0.3313 0.3973 0.3465 -0.0190 0.0890  0.0755  305 ALA A CB  
4132  N N   . TRP A  280 ? 0.3156 0.3910 0.3399 -0.0082 0.0765  0.0667  306 TRP A N   
4133  C CA  . TRP A  280 ? 0.3206 0.4042 0.3485 -0.0028 0.0731  0.0635  306 TRP A CA  
4134  C C   . TRP A  280 ? 0.3181 0.4118 0.3563 -0.0053 0.0713  0.0606  306 TRP A C   
4135  O O   . TRP A  280 ? 0.3102 0.4134 0.3529 -0.0019 0.0705  0.0586  306 TRP A O   
4136  C CB  . TRP A  280 ? 0.3247 0.4007 0.3485 0.0022  0.0684  0.0622  306 TRP A CB  
4137  C CG  . TRP A  280 ? 0.3436 0.4121 0.3579 0.0062  0.0690  0.0648  306 TRP A CG  
4138  C CD1 . TRP A  280 ? 0.3570 0.4264 0.3658 0.0074  0.0726  0.0674  306 TRP A CD1 
4139  C CD2 . TRP A  280 ? 0.3525 0.4124 0.3618 0.0097  0.0656  0.0651  306 TRP A CD2 
4140  N NE1 . TRP A  280 ? 0.3684 0.4301 0.3688 0.0112  0.0715  0.0695  306 TRP A NE1 
4141  C CE2 . TRP A  280 ? 0.3672 0.4234 0.3682 0.0129  0.0672  0.0681  306 TRP A CE2 
4142  C CE3 . TRP A  280 ? 0.3594 0.4147 0.3705 0.0104  0.0615  0.0631  306 TRP A CE3 
4143  C CZ2 . TRP A  280 ? 0.3789 0.4276 0.3738 0.0167  0.0646  0.0695  306 TRP A CZ2 
4144  C CZ3 . TRP A  280 ? 0.3727 0.4206 0.3780 0.0142  0.0593  0.0642  306 TRP A CZ3 
4145  C CH2 . TRP A  280 ? 0.3776 0.4225 0.3751 0.0174  0.0607  0.0674  306 TRP A CH2 
4156  N N   . PHE A  281 ? 0.3301 0.4216 0.3718 -0.0112 0.0707  0.0603  307 PHE A N   
4157  C CA  . PHE A  281 ? 0.3402 0.4412 0.3913 -0.0142 0.0685  0.0578  307 PHE A CA  
4158  C C   . PHE A  281 ? 0.3529 0.4630 0.4100 -0.0207 0.0721  0.0588  307 PHE A C   
4159  O O   . PHE A  281 ? 0.3516 0.4700 0.4165 -0.0242 0.0703  0.0571  307 PHE A O   
4160  C CB  . PHE A  281 ? 0.3400 0.4333 0.3910 -0.0166 0.0648  0.0563  307 PHE A CB  
4161  C CG  . PHE A  281 ? 0.3489 0.4330 0.3941 -0.0108 0.0615  0.0555  307 PHE A CG  
4162  C CD1 . PHE A  281 ? 0.3520 0.4409 0.3995 -0.0052 0.0577  0.0532  307 PHE A CD1 
4163  C CD2 . PHE A  281 ? 0.3627 0.4339 0.4000 -0.0105 0.0625  0.0575  307 PHE A CD2 
4164  C CE1 . PHE A  281 ? 0.3632 0.4444 0.4055 -0.0003 0.0547  0.0525  307 PHE A CE1 
4165  C CE2 . PHE A  281 ? 0.3747 0.4390 0.4074 -0.0051 0.0595  0.0570  307 PHE A CE2 
4166  C CZ  . PHE A  281 ? 0.3667 0.4364 0.4019 -0.0003 0.0556  0.0544  307 PHE A CZ  
4176  N N   . LYS A  282 ? 0.3595 0.4689 0.4130 -0.0227 0.0772  0.0616  308 LYS A N   
4177  C CA  . LYS A  282 ? 0.3707 0.4886 0.4293 -0.0295 0.0813  0.0628  308 LYS A CA  
4178  C C   . LYS A  282 ? 0.3581 0.4935 0.4272 -0.0284 0.0807  0.0611  308 LYS A C   
4179  O O   . LYS A  282 ? 0.3613 0.5056 0.4376 -0.0346 0.0814  0.0609  308 LYS A O   
4180  C CB  . LYS A  282 ? 0.4205 0.5343 0.4725 -0.0305 0.0869  0.0663  308 LYS A CB  
4181  C CG  . LYS A  282 ? 0.5109 0.6294 0.5661 -0.0389 0.0916  0.0681  308 LYS A CG  
4182  C CD  . LYS A  282 ? 0.6005 0.7169 0.6494 -0.0387 0.0972  0.0715  308 LYS A CD  
4183  C CE  . LYS A  282 ? 0.6742 0.7900 0.7232 -0.0479 0.1023  0.0740  308 LYS A CE  
4184  N NZ  . LYS A  282 ? 0.7290 0.8268 0.7691 -0.0512 0.1033  0.0761  308 LYS A NZ  
4198  N N   . ASN A  283 ? 0.3430 0.4835 0.4128 -0.0207 0.0795  0.0599  309 ASN A N   
4199  C CA  . ASN A  283 ? 0.3250 0.4814 0.4044 -0.0184 0.0794  0.0586  309 ASN A CA  
4200  C C   . ASN A  283 ? 0.2969 0.4555 0.3800 -0.0129 0.0739  0.0558  309 ASN A C   
4201  O O   . ASN A  283 ? 0.2827 0.4507 0.3706 -0.0077 0.0739  0.0547  309 ASN A O   
4202  C CB  . ASN A  283 ? 0.3552 0.5170 0.4329 -0.0144 0.0839  0.0596  309 ASN A CB  
4203  C CG  . ASN A  283 ? 0.4249 0.5849 0.4988 -0.0198 0.0896  0.0626  309 ASN A CG  
4204  O OD1 . ASN A  283 ? 0.4405 0.6071 0.5200 -0.0269 0.0917  0.0636  309 ASN A OD1 
4205  N ND2 . ASN A  283 ? 0.4498 0.6010 0.5139 -0.0171 0.0921  0.0643  309 ASN A ND2 
4212  N N   . MET A  284 ? 0.2881 0.4379 0.3691 -0.0142 0.0695  0.0546  310 MET A N   
4213  C CA  . MET A  284 ? 0.2790 0.4299 0.3631 -0.0100 0.0641  0.0522  310 MET A CA  
4214  C C   . MET A  284 ? 0.2710 0.4265 0.3616 -0.0163 0.0613  0.0515  310 MET A C   
4215  O O   . MET A  284 ? 0.2782 0.4247 0.3656 -0.0183 0.0581  0.0505  310 MET A O   
4216  C CB  . MET A  284 ? 0.2933 0.4298 0.3686 -0.0062 0.0613  0.0513  310 MET A CB  
4217  C CG  . MET A  284 ? 0.3283 0.4619 0.3982 0.0010  0.0619  0.0509  310 MET A CG  
4218  S SD  . MET A  284 ? 0.3628 0.4817 0.4243 0.0044  0.0576  0.0498  310 MET A SD  
4219  C CE  . MET A  284 ? 0.3086 0.4228 0.3613 0.0091  0.0606  0.0510  310 MET A CE  
4229  N N   . PRO A  285 ? 0.2506 0.4207 0.3505 -0.0197 0.0624  0.0519  311 PRO A N   
4230  C CA  . PRO A  285 ? 0.2433 0.4187 0.3491 -0.0264 0.0597  0.0513  311 PRO A CA  
4231  C C   . PRO A  285 ? 0.2382 0.4152 0.3472 -0.0234 0.0538  0.0494  311 PRO A C   
4232  O O   . PRO A  285 ? 0.2433 0.4208 0.3543 -0.0290 0.0511  0.0487  311 PRO A O   
4233  C CB  . PRO A  285 ? 0.2427 0.4350 0.3578 -0.0298 0.0626  0.0526  311 PRO A CB  
4234  C CG  . PRO A  285 ? 0.2457 0.4441 0.3625 -0.0221 0.0649  0.0531  311 PRO A CG  
4235  C CD  . PRO A  285 ? 0.2358 0.4188 0.3413 -0.0178 0.0664  0.0531  311 PRO A CD  
4243  N N   . HIS A  286 ? 0.2288 0.4063 0.3379 -0.0149 0.0521  0.0486  312 HIS A N   
4244  C CA  . HIS A  286 ? 0.2279 0.4070 0.3400 -0.0116 0.0467  0.0471  312 HIS A CA  
4245  C C   . HIS A  286 ? 0.2338 0.3978 0.3373 -0.0080 0.0439  0.0456  312 HIS A C   
4246  O O   . HIS A  286 ? 0.2441 0.4087 0.3492 -0.0044 0.0398  0.0444  312 HIS A O   
4247  C CB  . HIS A  286 ? 0.2217 0.4120 0.3404 -0.0044 0.0466  0.0472  312 HIS A CB  
4248  C CG  . HIS A  286 ? 0.2404 0.4469 0.3683 -0.0063 0.0497  0.0488  312 HIS A CG  
4249  N ND1 . HIS A  286 ? 0.2545 0.4740 0.3915 -0.0106 0.0474  0.0494  312 HIS A ND1 
4250  C CD2 . HIS A  286 ? 0.2512 0.4634 0.3805 -0.0043 0.0547  0.0498  312 HIS A CD2 
4251  C CE1 . HIS A  286 ? 0.2567 0.4897 0.4009 -0.0111 0.0510  0.0509  312 HIS A CE1 
4252  N NE2 . HIS A  286 ? 0.2631 0.4921 0.4029 -0.0073 0.0557  0.0512  312 HIS A NE2 
4260  N N   . LEU A  287 ? 0.2269 0.3779 0.3213 -0.0086 0.0460  0.0458  313 LEU A N   
4261  C CA  . LEU A  287 ? 0.2219 0.3601 0.3088 -0.0048 0.0434  0.0446  313 LEU A CA  
4262  C C   . LEU A  287 ? 0.2101 0.3455 0.2980 -0.0075 0.0388  0.0431  313 LEU A C   
4263  O O   . LEU A  287 ? 0.2038 0.3382 0.2922 -0.0143 0.0389  0.0432  313 LEU A O   
4264  C CB  . LEU A  287 ? 0.2297 0.3555 0.3075 -0.0055 0.0462  0.0456  313 LEU A CB  
4265  C CG  . LEU A  287 ? 0.2595 0.3741 0.3300 -0.0003 0.0439  0.0446  313 LEU A CG  
4266  C CD1 . LEU A  287 ? 0.2642 0.3818 0.3341 0.0070  0.0436  0.0439  313 LEU A CD1 
4267  C CD2 . LEU A  287 ? 0.2802 0.3832 0.3425 -0.0017 0.0463  0.0461  313 LEU A CD2 
4279  N N   . LYS A  288 ? 0.2015 0.3361 0.2896 -0.0025 0.0350  0.0417  314 LYS A N   
4280  C CA  . LYS A  288 ? 0.2070 0.3401 0.2962 -0.0042 0.0305  0.0403  314 LYS A CA  
4281  C C   . LYS A  288 ? 0.2002 0.3202 0.2818 -0.0021 0.0285  0.0390  314 LYS A C   
4282  O O   . LYS A  288 ? 0.2015 0.3171 0.2819 -0.0059 0.0262  0.0381  314 LYS A O   
4283  C CB  . LYS A  288 ? 0.2479 0.3912 0.3439 0.0000  0.0276  0.0400  314 LYS A CB  
4284  C CG  . LYS A  288 ? 0.3293 0.4750 0.4282 -0.0026 0.0230  0.0393  314 LYS A CG  
4285  C CD  . LYS A  288 ? 0.4110 0.5674 0.5170 0.0018  0.0205  0.0397  314 LYS A CD  
4286  C CE  . LYS A  288 ? 0.4939 0.6434 0.5962 0.0087  0.0185  0.0386  314 LYS A CE  
4287  N NZ  . LYS A  288 ? 0.5385 0.6972 0.6473 0.0136  0.0166  0.0393  314 LYS A NZ  
4301  N N   . VAL A  289 ? 0.1934 0.3081 0.2704 0.0038  0.0290  0.0388  315 VAL A N   
4302  C CA  . VAL A  289 ? 0.2073 0.3109 0.2776 0.0062  0.0270  0.0377  315 VAL A CA  
4303  C C   . VAL A  289 ? 0.2207 0.3171 0.2843 0.0082  0.0301  0.0388  315 VAL A C   
4304  O O   . VAL A  289 ? 0.2327 0.3323 0.2959 0.0117  0.0322  0.0394  315 VAL A O   
4305  C CB  . VAL A  289 ? 0.2148 0.3193 0.2858 0.0116  0.0235  0.0362  315 VAL A CB  
4306  C CG1 . VAL A  289 ? 0.2301 0.3240 0.2946 0.0134  0.0215  0.0351  315 VAL A CG1 
4307  C CG2 . VAL A  289 ? 0.2134 0.3257 0.2911 0.0100  0.0205  0.0358  315 VAL A CG2 
4317  N N   . LEU A  290 ? 0.2064 0.2932 0.2648 0.0059  0.0306  0.0392  316 LEU A N   
4318  C CA  . LEU A  290 ? 0.2048 0.2843 0.2565 0.0077  0.0332  0.0407  316 LEU A CA  
4319  C C   . LEU A  290 ? 0.2077 0.2784 0.2544 0.0103  0.0306  0.0399  316 LEU A C   
4320  O O   . LEU A  290 ? 0.2023 0.2678 0.2484 0.0074  0.0295  0.0393  316 LEU A O   
4321  C CB  . LEU A  290 ? 0.2022 0.2786 0.2526 0.0025  0.0369  0.0427  316 LEU A CB  
4322  C CG  . LEU A  290 ? 0.2223 0.2907 0.2656 0.0041  0.0400  0.0451  316 LEU A CG  
4323  C CD1 . LEU A  290 ? 0.2250 0.2972 0.2663 0.0091  0.0411  0.0458  316 LEU A CD1 
4324  C CD2 . LEU A  290 ? 0.2315 0.2971 0.2741 -0.0015 0.0440  0.0471  316 LEU A CD2 
4336  N N   . ASP A  291 ? 0.2080 0.2776 0.2513 0.0154  0.0298  0.0396  317 ASP A N   
4337  C CA  . ASP A  291 ? 0.2255 0.2884 0.2644 0.0181  0.0273  0.0389  317 ASP A CA  
4338  C C   . ASP A  291 ? 0.2284 0.2853 0.2610 0.0196  0.0296  0.0413  317 ASP A C   
4339  O O   . ASP A  291 ? 0.2285 0.2876 0.2585 0.0220  0.0314  0.0424  317 ASP A O   
4340  C CB  . ASP A  291 ? 0.2680 0.3341 0.3073 0.0224  0.0245  0.0369  317 ASP A CB  
4341  C CG  . ASP A  291 ? 0.3923 0.4539 0.4299 0.0235  0.0209  0.0353  317 ASP A CG  
4342  O OD1 . ASP A  291 ? 0.4205 0.4759 0.4550 0.0227  0.0210  0.0361  317 ASP A OD1 
4343  O OD2 . ASP A  291 ? 0.4381 0.5023 0.4775 0.0254  0.0183  0.0334  317 ASP A OD2 
4348  N N   . LEU A  292 ? 0.2216 0.2709 0.2515 0.0182  0.0299  0.0423  318 LEU A N   
4349  C CA  . LEU A  292 ? 0.2234 0.2664 0.2475 0.0199  0.0319  0.0451  318 LEU A CA  
4350  C C   . LEU A  292 ? 0.2208 0.2579 0.2421 0.0222  0.0296  0.0448  318 LEU A C   
4351  O O   . LEU A  292 ? 0.2291 0.2593 0.2470 0.0224  0.0312  0.0470  318 LEU A O   
4352  C CB  . LEU A  292 ? 0.2300 0.2687 0.2536 0.0156  0.0358  0.0473  318 LEU A CB  
4353  C CG  . LEU A  292 ? 0.2535 0.2979 0.2792 0.0131  0.0389  0.0483  318 LEU A CG  
4354  C CD1 . LEU A  292 ? 0.2657 0.3061 0.2924 0.0072  0.0420  0.0494  318 LEU A CD1 
4355  C CD2 . LEU A  292 ? 0.2595 0.3041 0.2803 0.0163  0.0411  0.0509  318 LEU A CD2 
4367  N N   . GLU A  293 ? 0.2170 0.2569 0.2396 0.0243  0.0260  0.0423  319 GLU A N   
4368  C CA  . GLU A  293 ? 0.2209 0.2567 0.2416 0.0263  0.0236  0.0418  319 GLU A CA  
4369  C C   . GLU A  293 ? 0.2181 0.2525 0.2337 0.0304  0.0236  0.0440  319 GLU A C   
4370  O O   . GLU A  293 ? 0.2184 0.2563 0.2318 0.0320  0.0244  0.0447  319 GLU A O   
4371  C CB  . GLU A  293 ? 0.2480 0.2875 0.2713 0.0272  0.0197  0.0386  319 GLU A CB  
4372  C CG  . GLU A  293 ? 0.3130 0.3552 0.3413 0.0237  0.0189  0.0365  319 GLU A CG  
4373  C CD  . GLU A  293 ? 0.3890 0.4351 0.4193 0.0251  0.0155  0.0339  319 GLU A CD  
4374  O OE1 . GLU A  293 ? 0.3965 0.4478 0.4285 0.0262  0.0154  0.0333  319 GLU A OE1 
4375  O OE2 . GLU A  293 ? 0.3989 0.4427 0.4289 0.0254  0.0131  0.0326  319 GLU A OE2 
4382  N N   . PHE A  294 ? 0.2152 0.2454 0.2289 0.0322  0.0226  0.0448  320 PHE A N   
4383  C CA  . PHE A  294 ? 0.2268 0.2571 0.2361 0.0363  0.0218  0.0469  320 PHE A CA  
4384  C C   . PHE A  294 ? 0.2310 0.2601 0.2363 0.0372  0.0249  0.0506  320 PHE A C   
4385  O O   . PHE A  294 ? 0.2270 0.2596 0.2287 0.0397  0.0244  0.0515  320 PHE A O   
4386  C CB  . PHE A  294 ? 0.2289 0.2650 0.2376 0.0383  0.0184  0.0444  320 PHE A CB  
4387  C CG  . PHE A  294 ? 0.2420 0.2784 0.2538 0.0377  0.0153  0.0413  320 PHE A CG  
4388  C CD1 . PHE A  294 ? 0.2521 0.2868 0.2631 0.0395  0.0137  0.0418  320 PHE A CD1 
4389  C CD2 . PHE A  294 ? 0.2492 0.2881 0.2647 0.0356  0.0141  0.0383  320 PHE A CD2 
4390  C CE1 . PHE A  294 ? 0.2614 0.2966 0.2751 0.0387  0.0110  0.0391  320 PHE A CE1 
4391  C CE2 . PHE A  294 ? 0.2624 0.3014 0.2802 0.0350  0.0112  0.0358  320 PHE A CE2 
4392  C CZ  . PHE A  294 ? 0.2574 0.2944 0.2741 0.0363  0.0099  0.0361  320 PHE A CZ  
4402  N N   . ASN A  295 ? 0.2315 0.2553 0.2369 0.0349  0.0284  0.0526  321 ASN A N   
4403  C CA  . ASN A  295 ? 0.2409 0.2620 0.2422 0.0354  0.0318  0.0567  321 ASN A CA  
4404  C C   . ASN A  295 ? 0.2591 0.2716 0.2583 0.0364  0.0337  0.0598  321 ASN A C   
4405  O O   . ASN A  295 ? 0.2677 0.2781 0.2682 0.0379  0.0318  0.0588  321 ASN A O   
4406  C CB  . ASN A  295 ? 0.2409 0.2634 0.2442 0.0312  0.0348  0.0563  321 ASN A CB  
4407  C CG  . ASN A  295 ? 0.2444 0.2750 0.2489 0.0313  0.0341  0.0544  321 ASN A CG  
4408  O OD1 . ASN A  295 ? 0.2484 0.2831 0.2576 0.0286  0.0339  0.0517  321 ASN A OD1 
4409  N ND2 . ASN A  295 ? 0.2233 0.2568 0.2234 0.0346  0.0335  0.0555  321 ASN A ND2 
4416  N N   . TYR A  296 ? 0.2635 0.2707 0.2593 0.0360  0.0375  0.0638  322 TYR A N   
4417  C CA  . TYR A  296 ? 0.2814 0.2793 0.2750 0.0373  0.0399  0.0670  322 TYR A CA  
4418  C C   . TYR A  296 ? 0.2902 0.2812 0.2842 0.0322  0.0443  0.0675  322 TYR A C   
4419  O O   . TYR A  296 ? 0.2999 0.2842 0.2901 0.0324  0.0479  0.0716  322 TYR A O   
4420  C CB  . TYR A  296 ? 0.2850 0.2824 0.2731 0.0419  0.0405  0.0721  322 TYR A CB  
4421  C CG  . TYR A  296 ? 0.3007 0.3058 0.2877 0.0462  0.0362  0.0717  322 TYR A CG  
4422  C CD1 . TYR A  296 ? 0.3140 0.3190 0.3023 0.0495  0.0335  0.0715  322 TYR A CD1 
4423  C CD2 . TYR A  296 ? 0.3153 0.3276 0.2997 0.0469  0.0350  0.0717  322 TYR A CD2 
4424  C CE1 . TYR A  296 ? 0.3300 0.3424 0.3171 0.0530  0.0296  0.0714  322 TYR A CE1 
4425  C CE2 . TYR A  296 ? 0.3249 0.3440 0.3077 0.0503  0.0311  0.0711  322 TYR A CE2 
4426  C CZ  . TYR A  296 ? 0.3417 0.3609 0.3258 0.0532  0.0284  0.0712  322 TYR A CZ  
4427  O OH  . TYR A  296 ? 0.3567 0.3829 0.3390 0.0561  0.0245  0.0709  322 TYR A OH  
4437  N N   . LEU A  297 ? 0.2873 0.2802 0.2860 0.0275  0.0438  0.0634  323 LEU A N   
4438  C CA  . LEU A  297 ? 0.2930 0.2818 0.2926 0.0216  0.0475  0.0631  323 LEU A CA  
4439  C C   . LEU A  297 ? 0.3072 0.2861 0.3071 0.0185  0.0495  0.0622  323 LEU A C   
4440  O O   . LEU A  297 ? 0.3063 0.2837 0.3080 0.0126  0.0516  0.0606  323 LEU A O   
4441  C CB  . LEU A  297 ? 0.2850 0.2832 0.2896 0.0179  0.0458  0.0594  323 LEU A CB  
4442  C CG  . LEU A  297 ? 0.2942 0.3014 0.2984 0.0200  0.0449  0.0601  323 LEU A CG  
4443  C CD1 . LEU A  297 ? 0.2957 0.3122 0.3055 0.0178  0.0426  0.0561  323 LEU A CD1 
4444  C CD2 . LEU A  297 ? 0.3029 0.3083 0.3037 0.0185  0.0493  0.0638  323 LEU A CD2 
4456  N N   . VAL A  298 ? 0.3173 0.2892 0.3152 0.0223  0.0496  0.0634  324 VAL A N   
4457  C CA  . VAL A  298 ? 0.3293 0.2903 0.3265 0.0195  0.0524  0.0624  324 VAL A CA  
4458  C C   . VAL A  298 ? 0.3370 0.2892 0.3310 0.0152  0.0578  0.0650  324 VAL A C   
4459  O O   . VAL A  298 ? 0.3329 0.2805 0.3278 0.0091  0.0598  0.0625  324 VAL A O   
4460  C CB  . VAL A  298 ? 0.3360 0.2910 0.3316 0.0252  0.0521  0.0639  324 VAL A CB  
4461  C CG1 . VAL A  298 ? 0.3449 0.2859 0.3379 0.0234  0.0567  0.0644  324 VAL A CG1 
4462  C CG2 . VAL A  298 ? 0.3415 0.3036 0.3409 0.0270  0.0474  0.0601  324 VAL A CG2 
4472  N N   . GLY A  299 ? 0.3479 0.2983 0.3380 0.0180  0.0599  0.0698  325 GLY A N   
4473  C CA  . GLY A  299 ? 0.3579 0.3001 0.3444 0.0141  0.0651  0.0727  325 GLY A CA  
4474  C C   . GLY A  299 ? 0.3578 0.3062 0.3474 0.0068  0.0657  0.0701  325 GLY A C   
4475  O O   . GLY A  299 ? 0.3671 0.3087 0.3562 0.0006  0.0692  0.0692  325 GLY A O   
4479  N N   . GLU A  300 ? 0.3409 0.3025 0.3340 0.0075  0.0624  0.0686  326 GLU A N   
4480  C CA  . GLU A  300 ? 0.3298 0.2995 0.3270 0.0014  0.0626  0.0662  326 GLU A CA  
4481  C C   . GLU A  300 ? 0.3245 0.2950 0.3261 -0.0040 0.0613  0.0614  326 GLU A C   
4482  O O   . GLU A  300 ? 0.3247 0.2970 0.3284 -0.0107 0.0631  0.0601  326 GLU A O   
4483  C CB  . GLU A  300 ? 0.3500 0.3332 0.3499 0.0044  0.0593  0.0655  326 GLU A CB  
4484  C CG  . GLU A  300 ? 0.4058 0.3906 0.4017 0.0064  0.0617  0.0697  326 GLU A CG  
4485  C CD  . GLU A  300 ? 0.4684 0.4541 0.4648 0.0004  0.0659  0.0708  326 GLU A CD  
4486  O OE1 . GLU A  300 ? 0.4988 0.4857 0.4993 -0.0058 0.0665  0.0679  326 GLU A OE1 
4487  O OE2 . GLU A  300 ? 0.4788 0.4645 0.4712 0.0016  0.0685  0.0745  326 GLU A OE2 
4494  N N   . ILE A  301 ? 0.3129 0.2826 0.3159 -0.0015 0.0581  0.0588  327 ILE A N   
4495  C CA  . ILE A  301 ? 0.3113 0.2811 0.3176 -0.0066 0.0568  0.0543  327 ILE A CA  
4496  C C   . ILE A  301 ? 0.3298 0.2870 0.3327 -0.0121 0.0615  0.0544  327 ILE A C   
4497  O O   . ILE A  301 ? 0.3299 0.2882 0.3351 -0.0190 0.0618  0.0513  327 ILE A O   
4498  C CB  . ILE A  301 ? 0.3007 0.2722 0.3085 -0.0024 0.0526  0.0518  327 ILE A CB  
4499  C CG1 . ILE A  301 ? 0.2993 0.2837 0.3108 0.0013  0.0481  0.0508  327 ILE A CG1 
4500  C CG2 . ILE A  301 ? 0.3032 0.2726 0.3130 -0.0080 0.0520  0.0475  327 ILE A CG2 
4501  C CD1 . ILE A  301 ? 0.3099 0.2960 0.3220 0.0066  0.0441  0.0494  327 ILE A CD1 
4513  N N   . ALA A  302 ? 0.3431 0.2883 0.3406 -0.0091 0.0650  0.0579  328 ALA A N   
4514  C CA  . ALA A  302 ? 0.3642 0.2954 0.3576 -0.0139 0.0701  0.0582  328 ALA A CA  
4515  C C   . ALA A  302 ? 0.3887 0.3187 0.3809 -0.0202 0.0741  0.0600  328 ALA A C   
4516  O O   . ALA A  302 ? 0.3907 0.3115 0.3807 -0.0267 0.0777  0.0588  328 ALA A O   
4517  C CB  . ALA A  302 ? 0.3671 0.2857 0.3553 -0.0076 0.0726  0.0618  328 ALA A CB  
4523  N N   . SER A  303 ? 0.4102 0.3486 0.4033 -0.0185 0.0738  0.0629  329 SER A N   
4524  C CA  . SER A  303 ? 0.4447 0.3817 0.4362 -0.0241 0.0781  0.0651  329 SER A CA  
4525  C C   . SER A  303 ? 0.4668 0.4192 0.4626 -0.0244 0.0763  0.0655  329 SER A C   
4526  O O   . SER A  303 ? 0.4898 0.4423 0.4831 -0.0248 0.0794  0.0692  329 SER A O   
4527  C CB  . SER A  303 ? 0.4798 0.4040 0.4642 -0.0206 0.0825  0.0706  329 SER A CB  
4528  O OG  . SER A  303 ? 0.5198 0.4500 0.5032 -0.0129 0.0805  0.0741  329 SER A OG  
4534  N N   . GLY A  304 ? 0.4581 0.4229 0.4600 -0.0246 0.0718  0.0618  330 GLY A N   
4535  C CA  . GLY A  304 ? 0.4607 0.4403 0.4672 -0.0238 0.0699  0.0617  330 GLY A CA  
4536  C C   . GLY A  304 ? 0.4529 0.4390 0.4625 -0.0311 0.0725  0.0616  330 GLY A C   
4537  O O   . GLY A  304 ? 0.4588 0.4508 0.4734 -0.0369 0.0713  0.0583  330 GLY A O   
4541  N N   . ALA A  305 ? 0.4418 0.4283 0.4488 -0.0307 0.0759  0.0654  331 ALA A N   
4542  C CA  . ALA A  305 ? 0.4328 0.4273 0.4431 -0.0371 0.0786  0.0657  331 ALA A CA  
4543  C C   . ALA A  305 ? 0.4125 0.4245 0.4307 -0.0359 0.0749  0.0631  331 ALA A C   
4544  O O   . ALA A  305 ? 0.4074 0.4284 0.4312 -0.0420 0.0755  0.0615  331 ALA A O   
4545  C CB  . ALA A  305 ? 0.4386 0.4296 0.4438 -0.0360 0.0831  0.0705  331 ALA A CB  
4551  N N   . PHE A  306 ? 0.4005 0.4175 0.4192 -0.0281 0.0712  0.0626  332 PHE A N   
4552  C CA  . PHE A  306 ? 0.3970 0.4291 0.4226 -0.0261 0.0678  0.0602  332 PHE A CA  
4553  C C   . PHE A  306 ? 0.3965 0.4347 0.4288 -0.0304 0.0646  0.0563  332 PHE A C   
4554  O O   . PHE A  306 ? 0.3997 0.4509 0.4386 -0.0310 0.0629  0.0548  332 PHE A O   
4555  C CB  . PHE A  306 ? 0.3922 0.4261 0.4159 -0.0174 0.0644  0.0602  332 PHE A CB  
4556  C CG  . PHE A  306 ? 0.3983 0.4276 0.4219 -0.0145 0.0602  0.0578  332 PHE A CG  
4557  C CD1 . PHE A  306 ? 0.4116 0.4280 0.4295 -0.0131 0.0608  0.0591  332 PHE A CD1 
4558  C CD2 . PHE A  306 ? 0.4040 0.4418 0.4331 -0.0131 0.0559  0.0544  332 PHE A CD2 
4559  C CE1 . PHE A  306 ? 0.4217 0.4345 0.4397 -0.0105 0.0573  0.0568  332 PHE A CE1 
4560  C CE2 . PHE A  306 ? 0.4125 0.4463 0.4412 -0.0107 0.0522  0.0523  332 PHE A CE2 
4561  C CZ  . PHE A  306 ? 0.4173 0.4389 0.4406 -0.0096 0.0530  0.0534  332 PHE A CZ  
4571  N N   . LEU A  307 ? 0.3983 0.4269 0.4284 -0.0331 0.0638  0.0547  333 LEU A N   
4572  C CA  . LEU A  307 ? 0.3969 0.4303 0.4321 -0.0375 0.0608  0.0511  333 LEU A CA  
4573  C C   . LEU A  307 ? 0.3892 0.4305 0.4294 -0.0460 0.0627  0.0505  333 LEU A C   
4574  O O   . LEU A  307 ? 0.3907 0.4412 0.4368 -0.0491 0.0596  0.0478  333 LEU A O   
4575  C CB  . LEU A  307 ? 0.4118 0.4319 0.4425 -0.0388 0.0604  0.0496  333 LEU A CB  
4576  C CG  . LEU A  307 ? 0.4396 0.4527 0.4663 -0.0309 0.0582  0.0499  333 LEU A CG  
4577  C CD1 . LEU A  307 ? 0.4578 0.4556 0.4788 -0.0323 0.0601  0.0497  333 LEU A CD1 
4578  C CD2 . LEU A  307 ? 0.4442 0.4658 0.4754 -0.0275 0.0528  0.0471  333 LEU A CD2 
4590  N N   . THR A  308 ? 0.3737 0.4119 0.4114 -0.0500 0.0677  0.0531  334 THR A N   
4591  C CA  . THR A  308 ? 0.3649 0.4115 0.4075 -0.0586 0.0698  0.0527  334 THR A CA  
4592  C C   . THR A  308 ? 0.3496 0.4141 0.3998 -0.0565 0.0689  0.0532  334 THR A C   
4593  O O   . THR A  308 ? 0.3432 0.4185 0.3996 -0.0627 0.0694  0.0525  334 THR A O   
4594  C CB  . THR A  308 ? 0.3846 0.4204 0.4214 -0.0641 0.0758  0.0553  334 THR A CB  
4595  O OG1 . THR A  308 ? 0.4030 0.4396 0.4374 -0.0595 0.0786  0.0590  334 THR A OG1 
4596  C CG2 . THR A  308 ? 0.4003 0.4170 0.4291 -0.0648 0.0774  0.0553  334 THR A CG2 
4604  N N   . MET A  309 ? 0.3445 0.4123 0.3943 -0.0480 0.0677  0.0543  335 MET A N   
4605  C CA  . MET A  309 ? 0.3309 0.4138 0.3868 -0.0449 0.0675  0.0547  335 MET A CA  
4606  C C   . MET A  309 ? 0.3138 0.4077 0.3766 -0.0412 0.0623  0.0521  335 MET A C   
4607  O O   . MET A  309 ? 0.3119 0.4177 0.3798 -0.0376 0.0620  0.0523  335 MET A O   
4608  C CB  . MET A  309 ? 0.3416 0.4206 0.3920 -0.0373 0.0691  0.0571  335 MET A CB  
4609  C CG  . MET A  309 ? 0.3804 0.4477 0.4230 -0.0392 0.0740  0.0605  335 MET A CG  
4610  S SD  . MET A  309 ? 0.4439 0.5163 0.4891 -0.0486 0.0796  0.0623  335 MET A SD  
4611  C CE  . MET A  309 ? 0.3582 0.4490 0.4104 -0.0449 0.0799  0.0624  335 MET A CE  
4621  N N   . LEU A  310 ? 0.2960 0.3859 0.3589 -0.0420 0.0584  0.0496  336 LEU A N   
4622  C CA  . LEU A  310 ? 0.2823 0.3804 0.3503 -0.0379 0.0533  0.0475  336 LEU A CA  
4623  C C   . LEU A  310 ? 0.2712 0.3754 0.3445 -0.0440 0.0503  0.0452  336 LEU A C   
4624  O O   . LEU A  310 ? 0.2707 0.3707 0.3428 -0.0430 0.0466  0.0432  336 LEU A O   
4625  C CB  . LEU A  310 ? 0.2915 0.3782 0.3531 -0.0315 0.0509  0.0468  336 LEU A CB  
4626  C CG  . LEU A  310 ? 0.3207 0.4023 0.3769 -0.0250 0.0530  0.0489  336 LEU A CG  
4627  C CD1 . LEU A  310 ? 0.3302 0.4014 0.3806 -0.0197 0.0505  0.0483  336 LEU A CD1 
4628  C CD2 . LEU A  310 ? 0.3321 0.4256 0.3926 -0.0202 0.0529  0.0492  336 LEU A CD2 
4640  N N   . PRO A  311 ? 0.2605 0.3757 0.3399 -0.0504 0.0517  0.0455  337 PRO A N   
4641  C CA  . PRO A  311 ? 0.2580 0.3798 0.3422 -0.0569 0.0486  0.0435  337 PRO A CA  
4642  C C   . PRO A  311 ? 0.2529 0.3865 0.3438 -0.0528 0.0434  0.0423  337 PRO A C   
4643  O O   . PRO A  311 ? 0.2520 0.3884 0.3449 -0.0573 0.0401  0.0406  337 PRO A O   
4644  C CB  . PRO A  311 ? 0.2626 0.3937 0.3514 -0.0648 0.0520  0.0446  337 PRO A CB  
4645  C CG  . PRO A  311 ? 0.2669 0.4037 0.3575 -0.0598 0.0552  0.0471  337 PRO A CG  
4646  C CD  . PRO A  311 ? 0.2514 0.3737 0.3334 -0.0527 0.0562  0.0478  337 PRO A CD  
4654  N N   . ARG A  312 ? 0.2459 0.3857 0.3397 -0.0446 0.0426  0.0433  338 ARG A N   
4655  C CA  . ARG A  312 ? 0.2430 0.3926 0.3426 -0.0397 0.0380  0.0425  338 ARG A CA  
4656  C C   . ARG A  312 ? 0.2302 0.3698 0.3246 -0.0325 0.0352  0.0414  338 ARG A C   
4657  O O   . ARG A  312 ? 0.2322 0.3779 0.3303 -0.0278 0.0315  0.0409  338 ARG A O   
4658  C CB  . ARG A  312 ? 0.2709 0.4351 0.3782 -0.0355 0.0393  0.0442  338 ARG A CB  
4659  C CG  . ARG A  312 ? 0.3549 0.5368 0.4724 -0.0391 0.0375  0.0446  338 ARG A CG  
4660  C CD  . ARG A  312 ? 0.4257 0.6189 0.5488 -0.0417 0.0417  0.0464  338 ARG A CD  
4661  N NE  . ARG A  312 ? 0.5061 0.6932 0.6252 -0.0503 0.0454  0.0467  338 ARG A NE  
4662  C CZ  . ARG A  312 ? 0.5371 0.7322 0.6598 -0.0548 0.0496  0.0482  338 ARG A CZ  
4663  N NH1 . ARG A  312 ? 0.5385 0.7490 0.6695 -0.0511 0.0508  0.0497  338 ARG A NH1 
4664  N NH2 . ARG A  312 ? 0.5304 0.7180 0.6485 -0.0628 0.0530  0.0484  338 ARG A NH2 
4678  N N   . LEU A  313 ? 0.2128 0.3373 0.2985 -0.0315 0.0368  0.0412  339 LEU A N   
4679  C CA  . LEU A  313 ? 0.2079 0.3237 0.2888 -0.0252 0.0343  0.0402  339 LEU A CA  
4680  C C   . LEU A  313 ? 0.2012 0.3157 0.2825 -0.0270 0.0298  0.0382  339 LEU A C   
4681  O O   . LEU A  313 ? 0.2027 0.3142 0.2829 -0.0338 0.0299  0.0372  339 LEU A O   
4682  C CB  . LEU A  313 ? 0.2135 0.3148 0.2858 -0.0241 0.0372  0.0409  339 LEU A CB  
4683  C CG  . LEU A  313 ? 0.2296 0.3230 0.2969 -0.0170 0.0352  0.0404  339 LEU A CG  
4684  C CD1 . LEU A  313 ? 0.2348 0.3326 0.3025 -0.0105 0.0364  0.0415  339 LEU A CD1 
4685  C CD2 . LEU A  313 ? 0.2332 0.3123 0.2927 -0.0178 0.0371  0.0408  339 LEU A CD2 
4697  N N   . GLU A  314 ? 0.1892 0.3059 0.2718 -0.0212 0.0262  0.0374  340 GLU A N   
4698  C CA  . GLU A  314 ? 0.1849 0.3008 0.2677 -0.0222 0.0219  0.0357  340 GLU A CA  
4699  C C   . GLU A  314 ? 0.1900 0.2934 0.2660 -0.0185 0.0206  0.0345  340 GLU A C   
4700  O O   . GLU A  314 ? 0.1910 0.2894 0.2645 -0.0215 0.0186  0.0330  340 GLU A O   
4701  C CB  . GLU A  314 ? 0.2032 0.3315 0.2930 -0.0189 0.0185  0.0361  340 GLU A CB  
4702  C CG  . GLU A  314 ? 0.2759 0.4183 0.3735 -0.0231 0.0190  0.0373  340 GLU A CG  
4703  C CD  . GLU A  314 ? 0.3607 0.5160 0.4659 -0.0188 0.0161  0.0382  340 GLU A CD  
4704  O OE1 . GLU A  314 ? 0.3930 0.5455 0.4971 -0.0136 0.0131  0.0377  340 GLU A OE1 
4705  O OE2 . GLU A  314 ? 0.3757 0.5439 0.4882 -0.0205 0.0171  0.0397  340 GLU A OE2 
4712  N N   . ILE A  315 ? 0.1858 0.2847 0.2586 -0.0122 0.0217  0.0351  341 ILE A N   
4713  C CA  . ILE A  315 ? 0.2010 0.2893 0.2677 -0.0086 0.0205  0.0342  341 ILE A CA  
4714  C C   . ILE A  315 ? 0.2050 0.2849 0.2661 -0.0068 0.0240  0.0354  341 ILE A C   
4715  O O   . ILE A  315 ? 0.2132 0.2962 0.2746 -0.0038 0.0261  0.0367  341 ILE A O   
4716  C CB  . ILE A  315 ? 0.2117 0.3027 0.2796 -0.0024 0.0172  0.0335  341 ILE A CB  
4717  C CG1 . ILE A  315 ? 0.2190 0.3191 0.2928 -0.0038 0.0137  0.0330  341 ILE A CG1 
4718  C CG2 . ILE A  315 ? 0.2298 0.3105 0.2917 0.0003  0.0158  0.0324  341 ILE A CG2 
4719  C CD1 . ILE A  315 ? 0.2402 0.3427 0.3153 0.0021  0.0108  0.0326  341 ILE A CD1 
4731  N N   . LEU A  316 ? 0.2022 0.2717 0.2581 -0.0084 0.0248  0.0350  342 LEU A N   
4732  C CA  . LEU A  316 ? 0.2012 0.2622 0.2515 -0.0065 0.0279  0.0366  342 LEU A CA  
4733  C C   . LEU A  316 ? 0.2012 0.2545 0.2471 -0.0025 0.0259  0.0358  342 LEU A C   
4734  O O   . LEU A  316 ? 0.2050 0.2538 0.2500 -0.0048 0.0246  0.0343  342 LEU A O   
4735  C CB  . LEU A  316 ? 0.2032 0.2583 0.2514 -0.0125 0.0314  0.0374  342 LEU A CB  
4736  C CG  . LEU A  316 ? 0.2236 0.2685 0.2656 -0.0108 0.0350  0.0396  342 LEU A CG  
4737  C CD1 . LEU A  316 ? 0.2206 0.2692 0.2619 -0.0064 0.0366  0.0419  342 LEU A CD1 
4738  C CD2 . LEU A  316 ? 0.2343 0.2731 0.2746 -0.0174 0.0388  0.0403  342 LEU A CD2 
4750  N N   . ASP A  317 ? 0.2021 0.2547 0.2455 0.0032  0.0256  0.0366  343 ASP A N   
4751  C CA  . ASP A  317 ? 0.2052 0.2517 0.2448 0.0069  0.0237  0.0360  343 ASP A CA  
4752  C C   . ASP A  317 ? 0.2097 0.2490 0.2440 0.0091  0.0264  0.0383  343 ASP A C   
4753  O O   . ASP A  317 ? 0.2058 0.2468 0.2383 0.0122  0.0276  0.0399  343 ASP A O   
4754  C CB  . ASP A  317 ? 0.2132 0.2647 0.2540 0.0115  0.0205  0.0348  343 ASP A CB  
4755  C CG  . ASP A  317 ? 0.2761 0.3230 0.3144 0.0138  0.0178  0.0335  343 ASP A CG  
4756  O OD1 . ASP A  317 ? 0.2849 0.3247 0.3197 0.0139  0.0189  0.0342  343 ASP A OD1 
4757  O OD2 . ASP A  317 ? 0.2989 0.3491 0.3389 0.0156  0.0147  0.0318  343 ASP A OD2 
4762  N N   . LEU A  318 ? 0.2116 0.2425 0.2431 0.0076  0.0274  0.0385  344 LEU A N   
4763  C CA  . LEU A  318 ? 0.2264 0.2496 0.2529 0.0100  0.0300  0.0411  344 LEU A CA  
4764  C C   . LEU A  318 ? 0.2281 0.2470 0.2523 0.0138  0.0279  0.0406  344 LEU A C   
4765  O O   . LEU A  318 ? 0.2347 0.2461 0.2555 0.0151  0.0299  0.0424  344 LEU A O   
4766  C CB  . LEU A  318 ? 0.2284 0.2446 0.2535 0.0053  0.0339  0.0422  344 LEU A CB  
4767  C CG  . LEU A  318 ? 0.2460 0.2655 0.2722 0.0019  0.0369  0.0437  344 LEU A CG  
4768  C CD1 . LEU A  318 ? 0.2581 0.2724 0.2844 -0.0048 0.0396  0.0432  344 LEU A CD1 
4769  C CD2 . LEU A  318 ? 0.2541 0.2712 0.2762 0.0054  0.0395  0.0473  344 LEU A CD2 
4781  N N   . SER A  319 ? 0.2208 0.2445 0.2470 0.0156  0.0241  0.0383  345 SER A N   
4782  C CA  . SER A  319 ? 0.2235 0.2443 0.2482 0.0186  0.0221  0.0376  345 SER A CA  
4783  C C   . SER A  319 ? 0.2348 0.2544 0.2558 0.0236  0.0223  0.0401  345 SER A C   
4784  O O   . SER A  319 ? 0.2515 0.2743 0.2712 0.0254  0.0229  0.0416  345 SER A O   
4785  C CB  . SER A  319 ? 0.2231 0.2494 0.2504 0.0191  0.0181  0.0348  345 SER A CB  
4786  O OG  . SER A  319 ? 0.2361 0.2638 0.2666 0.0146  0.0174  0.0328  345 SER A OG  
4792  N N   . PHE A  320 ? 0.2201 0.2354 0.2395 0.0258  0.0219  0.0404  346 PHE A N   
4793  C CA  . PHE A  320 ? 0.2306 0.2454 0.2470 0.0306  0.0216  0.0428  346 PHE A CA  
4794  C C   . PHE A  320 ? 0.2399 0.2523 0.2529 0.0321  0.0246  0.0466  346 PHE A C   
4795  O O   . PHE A  320 ? 0.2414 0.2576 0.2521 0.0351  0.0238  0.0483  346 PHE A O   
4796  C CB  . PHE A  320 ? 0.2313 0.2532 0.2481 0.0330  0.0177  0.0412  346 PHE A CB  
4797  C CG  . PHE A  320 ? 0.2487 0.2713 0.2678 0.0325  0.0150  0.0383  346 PHE A CG  
4798  C CD1 . PHE A  320 ? 0.2652 0.2853 0.2837 0.0346  0.0146  0.0389  346 PHE A CD1 
4799  C CD2 . PHE A  320 ? 0.2630 0.2889 0.2849 0.0298  0.0130  0.0353  346 PHE A CD2 
4800  C CE1 . PHE A  320 ? 0.2764 0.2971 0.2968 0.0336  0.0125  0.0362  346 PHE A CE1 
4801  C CE2 . PHE A  320 ? 0.2718 0.2979 0.2953 0.0290  0.0107  0.0329  346 PHE A CE2 
4802  C CZ  . PHE A  320 ? 0.2727 0.2963 0.2954 0.0307  0.0105  0.0333  346 PHE A CZ  
4812  N N   . ASN A  321 ? 0.2412 0.2468 0.2535 0.0297  0.0282  0.0481  347 ASN A N   
4813  C CA  . ASN A  321 ? 0.2536 0.2550 0.2623 0.0309  0.0316  0.0522  347 ASN A CA  
4814  C C   . ASN A  321 ? 0.2695 0.2625 0.2756 0.0338  0.0336  0.0548  347 ASN A C   
4815  O O   . ASN A  321 ? 0.2716 0.2587 0.2745 0.0346  0.0370  0.0585  347 ASN A O   
4816  C CB  . ASN A  321 ? 0.2541 0.2535 0.2634 0.0258  0.0348  0.0522  347 ASN A CB  
4817  C CG  . ASN A  321 ? 0.2769 0.2845 0.2873 0.0250  0.0341  0.0517  347 ASN A CG  
4818  O OD1 . ASN A  321 ? 0.2851 0.2933 0.2926 0.0263  0.0360  0.0546  347 ASN A OD1 
4819  N ND2 . ASN A  321 ? 0.2794 0.2934 0.2939 0.0230  0.0316  0.0483  347 ASN A ND2 
4826  N N   . TYR A  322 ? 0.2681 0.2608 0.2757 0.0358  0.0316  0.0532  348 TYR A N   
4827  C CA  . TYR A  322 ? 0.2755 0.2610 0.2815 0.0390  0.0335  0.0555  348 TYR A CA  
4828  C C   . TYR A  322 ? 0.2992 0.2841 0.3017 0.0442  0.0345  0.0607  348 TYR A C   
4829  O O   . TYR A  322 ? 0.2998 0.2919 0.3011 0.0461  0.0322  0.0619  348 TYR A O   
4830  C CB  . TYR A  322 ? 0.2646 0.2526 0.2733 0.0407  0.0308  0.0530  348 TYR A CB  
4831  C CG  . TYR A  322 ? 0.2553 0.2525 0.2645 0.0446  0.0266  0.0532  348 TYR A CG  
4832  C CD1 . TYR A  322 ? 0.2518 0.2565 0.2631 0.0427  0.0229  0.0497  348 TYR A CD1 
4833  C CD2 . TYR A  322 ? 0.2598 0.2578 0.2675 0.0500  0.0263  0.0568  348 TYR A CD2 
4834  C CE1 . TYR A  322 ? 0.2571 0.2694 0.2685 0.0456  0.0193  0.0495  348 TYR A CE1 
4835  C CE2 . TYR A  322 ? 0.2638 0.2707 0.2718 0.0528  0.0224  0.0568  348 TYR A CE2 
4836  C CZ  . TYR A  322 ? 0.2683 0.2819 0.2781 0.0503  0.0189  0.0529  348 TYR A CZ  
4837  O OH  . TYR A  322 ? 0.2868 0.3083 0.2964 0.0526  0.0152  0.0526  348 TYR A OH  
4847  N N   . ILE A  323 ? 0.3091 0.2851 0.3096 0.0464  0.0379  0.0638  349 ILE A N   
4848  C CA  . ILE A  323 ? 0.3315 0.3062 0.3287 0.0519  0.0389  0.0693  349 ILE A CA  
4849  C C   . ILE A  323 ? 0.3396 0.3181 0.3386 0.0570  0.0362  0.0696  349 ILE A C   
4850  O O   . ILE A  323 ? 0.3303 0.3037 0.3312 0.0574  0.0376  0.0682  349 ILE A O   
4851  C CB  . ILE A  323 ? 0.3493 0.3114 0.3431 0.0519  0.0444  0.0729  349 ILE A CB  
4852  C CG1 . ILE A  323 ? 0.3723 0.3319 0.3640 0.0467  0.0469  0.0731  349 ILE A CG1 
4853  C CG2 . ILE A  323 ? 0.3573 0.3177 0.3480 0.0588  0.0452  0.0791  349 ILE A CG2 
4854  C CD1 . ILE A  323 ? 0.3965 0.3420 0.3855 0.0439  0.0528  0.0747  349 ILE A CD1 
4866  N N   . LYS A  324 ? 0.3491 0.3370 0.3477 0.0606  0.0326  0.0712  350 LYS A N   
4867  C CA  . LYS A  324 ? 0.3676 0.3611 0.3684 0.0653  0.0298  0.0718  350 LYS A CA  
4868  C C   . LYS A  324 ? 0.3813 0.3669 0.3816 0.0700  0.0332  0.0759  350 LYS A C   
4869  O O   . LYS A  324 ? 0.3877 0.3673 0.3844 0.0721  0.0362  0.0806  350 LYS A O   
4870  C CB  . LYS A  324 ? 0.4010 0.4049 0.3999 0.0682  0.0260  0.0740  350 LYS A CB  
4871  C CG  . LYS A  324 ? 0.4659 0.4773 0.4671 0.0726  0.0227  0.0748  350 LYS A CG  
4872  C CD  . LYS A  324 ? 0.5155 0.5370 0.5142 0.0752  0.0191  0.0773  350 LYS A CD  
4873  C CE  . LYS A  324 ? 0.5621 0.5904 0.5631 0.0800  0.0166  0.0794  350 LYS A CE  
4874  N NZ  . LYS A  324 ? 0.5940 0.6328 0.5923 0.0822  0.0128  0.0818  350 LYS A NZ  
4888  N N   . GLY A  325 ? 0.3798 0.3646 0.3836 0.0714  0.0331  0.0740  351 GLY A N   
4889  C CA  . GLY A  325 ? 0.3858 0.3632 0.3897 0.0763  0.0366  0.0775  351 GLY A CA  
4890  C C   . GLY A  325 ? 0.3865 0.3494 0.3888 0.0736  0.0422  0.0766  351 GLY A C   
4891  O O   . GLY A  325 ? 0.3932 0.3484 0.3956 0.0775  0.0456  0.0787  351 GLY A O   
4895  N N   . SER A  326 ? 0.3682 0.3274 0.3692 0.0669  0.0432  0.0733  352 SER A N   
4896  C CA  . SER A  326 ? 0.3658 0.3117 0.3650 0.0631  0.0483  0.0719  352 SER A CA  
4897  C C   . SER A  326 ? 0.3554 0.3014 0.3573 0.0574  0.0475  0.0654  352 SER A C   
4898  O O   . SER A  326 ? 0.3459 0.2992 0.3493 0.0530  0.0443  0.0621  352 SER A O   
4899  C CB  . SER A  326 ? 0.3908 0.3325 0.3863 0.0592  0.0504  0.0736  352 SER A CB  
4900  O OG  . SER A  326 ? 0.4306 0.3598 0.4242 0.0546  0.0552  0.0720  352 SER A OG  
4906  N N   . TYR A  327 ? 0.3495 0.2870 0.3517 0.0575  0.0508  0.0637  353 TYR A N   
4907  C CA  . TYR A  327 ? 0.3447 0.2814 0.3487 0.0522  0.0504  0.0577  353 TYR A CA  
4908  C C   . TYR A  327 ? 0.3563 0.2780 0.3568 0.0485  0.0562  0.0567  353 TYR A C   
4909  O O   . TYR A  327 ? 0.3671 0.2804 0.3669 0.0508  0.0598  0.0563  353 TYR A O   
4910  C CB  . TYR A  327 ? 0.3329 0.2744 0.3403 0.0565  0.0488  0.0565  353 TYR A CB  
4911  C CG  . TYR A  327 ? 0.3247 0.2670 0.3339 0.0520  0.0479  0.0506  353 TYR A CG  
4912  C CD1 . TYR A  327 ? 0.3273 0.2708 0.3363 0.0446  0.0465  0.0465  353 TYR A CD1 
4913  C CD2 . TYR A  327 ? 0.3291 0.2729 0.3407 0.0553  0.0480  0.0494  353 TYR A CD2 
4914  C CE1 . TYR A  327 ? 0.3314 0.2767 0.3418 0.0406  0.0452  0.0415  353 TYR A CE1 
4915  C CE2 . TYR A  327 ? 0.3336 0.2784 0.3465 0.0512  0.0473  0.0442  353 TYR A CE2 
4916  C CZ  . TYR A  327 ? 0.3396 0.2851 0.3517 0.0438  0.0457  0.0403  353 TYR A CZ  
4917  O OH  . TYR A  327 ? 0.3455 0.2922 0.3584 0.0397  0.0448  0.0355  353 TYR A OH  
4927  N N   . PRO A  328 ? 0.3611 0.2791 0.3592 0.0432  0.0577  0.0567  354 PRO A N   
4928  C CA  . PRO A  328 ? 0.3747 0.2779 0.3688 0.0391  0.0635  0.0560  354 PRO A CA  
4929  C C   . PRO A  328 ? 0.3901 0.2890 0.3843 0.0336  0.0646  0.0500  354 PRO A C   
4930  O O   . PRO A  328 ? 0.3779 0.2860 0.3753 0.0313  0.0605  0.0462  354 PRO A O   
4931  C CB  . PRO A  328 ? 0.3850 0.2888 0.3773 0.0341  0.0637  0.0571  354 PRO A CB  
4932  C CG  . PRO A  328 ? 0.3782 0.2975 0.3744 0.0329  0.0578  0.0554  354 PRO A CG  
4933  C CD  . PRO A  328 ? 0.3477 0.2745 0.3462 0.0404  0.0546  0.0572  354 PRO A CD  
4941  N N   . GLN A  329 ? 0.4043 0.2884 0.3946 0.0314  0.0703  0.0493  355 GLN A N   
4942  C CA  . GLN A  329 ? 0.4151 0.2937 0.4043 0.0257  0.0719  0.0436  355 GLN A CA  
4943  C C   . GLN A  329 ? 0.4019 0.2862 0.3917 0.0166  0.0694  0.0396  355 GLN A C   
4944  O O   . GLN A  329 ? 0.3977 0.2868 0.3892 0.0129  0.0670  0.0350  355 GLN A O   
4945  C CB  . GLN A  329 ? 0.4697 0.3299 0.4537 0.0250  0.0792  0.0437  355 GLN A CB  
4946  C CG  . GLN A  329 ? 0.5451 0.3989 0.5288 0.0342  0.0822  0.0468  355 GLN A CG  
4947  C CD  . GLN A  329 ? 0.6483 0.4835 0.6269 0.0330  0.0895  0.0454  355 GLN A CD  
4948  O OE1 . GLN A  329 ? 0.6816 0.5064 0.6557 0.0261  0.0930  0.0438  355 GLN A OE1 
4949  N NE2 . GLN A  329 ? 0.6678 0.4981 0.6468 0.0397  0.0921  0.0459  355 GLN A NE2 
4958  N N   . HIS A  330 ? 0.3868 0.2713 0.3755 0.0130  0.0698  0.0416  356 HIS A N   
4959  C CA  . HIS A  330 ? 0.3879 0.2779 0.3776 0.0043  0.0678  0.0382  356 HIS A CA  
4960  C C   . HIS A  330 ? 0.3706 0.2725 0.3632 0.0042  0.0642  0.0407  356 HIS A C   
4961  O O   . HIS A  330 ? 0.3717 0.2749 0.3641 0.0098  0.0643  0.0454  356 HIS A O   
4962  C CB  . HIS A  330 ? 0.4168 0.2933 0.4017 -0.0028 0.0734  0.0367  356 HIS A CB  
4963  C CG  . HIS A  330 ? 0.4660 0.3290 0.4471 -0.0027 0.0778  0.0341  356 HIS A CG  
4964  N ND1 . HIS A  330 ? 0.5003 0.3474 0.4765 -0.0002 0.0840  0.0367  356 HIS A ND1 
4965  C CD2 . HIS A  330 ? 0.4799 0.3434 0.4614 -0.0039 0.0768  0.0296  356 HIS A CD2 
4966  C CE1 . HIS A  330 ? 0.5124 0.3506 0.4863 -0.0002 0.0869  0.0333  356 HIS A CE1 
4967  N NE2 . HIS A  330 ? 0.5065 0.3543 0.4833 -0.0025 0.0827  0.0289  356 HIS A NE2 
4975  N N   . ILE A  331 ? 0.3501 0.2611 0.3454 -0.0020 0.0610  0.0375  357 ILE A N   
4976  C CA  . ILE A  331 ? 0.3429 0.2646 0.3410 -0.0031 0.0583  0.0392  357 ILE A CA  
4977  C C   . ILE A  331 ? 0.3500 0.2649 0.3453 -0.0089 0.0626  0.0405  357 ILE A C   
4978  O O   . ILE A  331 ? 0.3551 0.2615 0.3478 -0.0151 0.0656  0.0378  357 ILE A O   
4979  C CB  . ILE A  331 ? 0.3393 0.2747 0.3422 -0.0063 0.0529  0.0358  357 ILE A CB  
4980  C CG1 . ILE A  331 ? 0.3339 0.2804 0.3398 -0.0054 0.0503  0.0380  357 ILE A CG1 
4981  C CG2 . ILE A  331 ? 0.3487 0.2829 0.3514 -0.0151 0.0533  0.0314  357 ILE A CG2 
4982  C CD1 . ILE A  331 ? 0.3363 0.2964 0.3471 -0.0057 0.0447  0.0356  357 ILE A CD1 
4994  N N   . ASN A  332 ? 0.3418 0.2598 0.3371 -0.0069 0.0630  0.0445  358 ASN A N   
4995  C CA  . ASN A  332 ? 0.3572 0.2694 0.3499 -0.0121 0.0672  0.0462  358 ASN A CA  
4996  C C   . ASN A  332 ? 0.3503 0.2759 0.3471 -0.0163 0.0645  0.0458  358 ASN A C   
4997  O O   . ASN A  332 ? 0.3440 0.2770 0.3422 -0.0122 0.0630  0.0488  358 ASN A O   
4998  C CB  . ASN A  332 ? 0.3749 0.2781 0.3634 -0.0066 0.0709  0.0518  358 ASN A CB  
4999  C CG  . ASN A  332 ? 0.4372 0.3311 0.4218 -0.0120 0.0761  0.0537  358 ASN A CG  
5000  O OD1 . ASN A  332 ? 0.4618 0.3571 0.4472 -0.0204 0.0769  0.0509  358 ASN A OD1 
5001  N ND2 . ASN A  332 ? 0.4587 0.3431 0.4390 -0.0075 0.0798  0.0588  358 ASN A ND2 
5008  N N   . ILE A  333 ? 0.3490 0.2777 0.3478 -0.0243 0.0640  0.0419  359 ILE A N   
5009  C CA  . ILE A  333 ? 0.3509 0.2928 0.3544 -0.0290 0.0616  0.0410  359 ILE A CA  
5010  C C   . ILE A  333 ? 0.3488 0.2862 0.3503 -0.0358 0.0661  0.0423  359 ILE A C   
5011  O O   . ILE A  333 ? 0.3515 0.2794 0.3500 -0.0421 0.0692  0.0403  359 ILE A O   
5012  C CB  . ILE A  333 ? 0.3639 0.3128 0.3709 -0.0336 0.0579  0.0361  359 ILE A CB  
5013  C CG1 . ILE A  333 ? 0.3766 0.3300 0.3854 -0.0273 0.0535  0.0349  359 ILE A CG1 
5014  C CG2 . ILE A  333 ? 0.3734 0.3359 0.3856 -0.0388 0.0556  0.0353  359 ILE A CG2 
5015  C CD1 . ILE A  333 ? 0.3937 0.3574 0.4057 -0.0204 0.0501  0.0372  359 ILE A CD1 
5027  N N   . SER A  334 ? 0.3426 0.2871 0.3459 -0.0349 0.0664  0.0454  360 SER A N   
5028  C CA  . SER A  334 ? 0.3493 0.2909 0.3511 -0.0415 0.0707  0.0470  360 SER A CA  
5029  C C   . SER A  334 ? 0.3594 0.3060 0.3642 -0.0513 0.0703  0.0431  360 SER A C   
5030  O O   . SER A  334 ? 0.3478 0.3067 0.3579 -0.0522 0.0657  0.0403  360 SER A O   
5031  C CB  . SER A  334 ? 0.3475 0.2993 0.3517 -0.0388 0.0703  0.0504  360 SER A CB  
5032  O OG  . SER A  334 ? 0.3519 0.3022 0.3552 -0.0454 0.0745  0.0519  360 SER A OG  
5038  N N   . ARG A  335 ? 0.3746 0.3125 0.3760 -0.0588 0.0751  0.0432  361 ARG A N   
5039  C CA  . ARG A  335 ? 0.3880 0.3318 0.3922 -0.0691 0.0750  0.0399  361 ARG A CA  
5040  C C   . ARG A  335 ? 0.3736 0.3367 0.3854 -0.0700 0.0720  0.0406  361 ARG A C   
5041  O O   . ARG A  335 ? 0.3803 0.3539 0.3969 -0.0762 0.0695  0.0376  361 ARG A O   
5042  C CB  . ARG A  335 ? 0.4348 0.3658 0.4337 -0.0771 0.0812  0.0404  361 ARG A CB  
5043  C CG  . ARG A  335 ? 0.5324 0.4448 0.5243 -0.0791 0.0845  0.0382  361 ARG A CG  
5044  C CD  . ARG A  335 ? 0.6242 0.5258 0.6114 -0.0893 0.0901  0.0375  361 ARG A CD  
5045  N NE  . ARG A  335 ? 0.7132 0.5962 0.6933 -0.0917 0.0938  0.0349  361 ARG A NE  
5046  C CZ  . ARG A  335 ? 0.7800 0.6457 0.7537 -0.0859 0.0980  0.0375  361 ARG A CZ  
5047  N NH1 . ARG A  335 ? 0.7940 0.6431 0.7615 -0.0885 0.1016  0.0347  361 ARG A NH1 
5048  N NH2 . ARG A  335 ? 0.7918 0.6570 0.7653 -0.0773 0.0987  0.0430  361 ARG A NH2 
5062  N N   . ASN A  336 ? 0.3541 0.3221 0.3670 -0.0637 0.0722  0.0445  362 ASN A N   
5063  C CA  . ASN A  336 ? 0.3419 0.3273 0.3616 -0.0633 0.0699  0.0454  362 ASN A CA  
5064  C C   . ASN A  336 ? 0.3218 0.3207 0.3478 -0.0601 0.0638  0.0427  362 ASN A C   
5065  O O   . ASN A  336 ? 0.3141 0.3279 0.3466 -0.0609 0.0618  0.0428  362 ASN A O   
5066  C CB  . ASN A  336 ? 0.3545 0.3404 0.3726 -0.0568 0.0718  0.0499  362 ASN A CB  
5067  C CG  . ASN A  336 ? 0.4103 0.3868 0.4236 -0.0608 0.0778  0.0531  362 ASN A CG  
5068  O OD1 . ASN A  336 ? 0.4096 0.3843 0.4229 -0.0699 0.0806  0.0520  362 ASN A OD1 
5069  N ND2 . ASN A  336 ? 0.4373 0.4082 0.4462 -0.0545 0.0798  0.0572  362 ASN A ND2 
5076  N N   . PHE A  337 ? 0.3070 0.3011 0.3314 -0.0565 0.0609  0.0406  363 PHE A N   
5077  C CA  . PHE A  337 ? 0.3011 0.3069 0.3309 -0.0544 0.0552  0.0381  363 PHE A CA  
5078  C C   . PHE A  337 ? 0.3055 0.3208 0.3401 -0.0633 0.0537  0.0353  363 PHE A C   
5079  O O   . PHE A  337 ? 0.3008 0.3297 0.3415 -0.0623 0.0495  0.0342  363 PHE A O   
5080  C CB  . PHE A  337 ? 0.2952 0.2934 0.3220 -0.0499 0.0529  0.0362  363 PHE A CB  
5081  C CG  . PHE A  337 ? 0.2944 0.2920 0.3201 -0.0401 0.0513  0.0383  363 PHE A CG  
5082  C CD1 . PHE A  337 ? 0.3005 0.2873 0.3208 -0.0358 0.0546  0.0413  363 PHE A CD1 
5083  C CD2 . PHE A  337 ? 0.2946 0.3030 0.3247 -0.0353 0.0466  0.0375  363 PHE A CD2 
5084  C CE1 . PHE A  337 ? 0.3065 0.2937 0.3258 -0.0272 0.0529  0.0431  363 PHE A CE1 
5085  C CE2 . PHE A  337 ? 0.3012 0.3091 0.3300 -0.0270 0.0451  0.0391  363 PHE A CE2 
5086  C CZ  . PHE A  337 ? 0.3003 0.2982 0.3238 -0.0232 0.0482  0.0418  363 PHE A CZ  
5096  N N   . SER A  338 ? 0.3027 0.3107 0.3342 -0.0720 0.0572  0.0341  364 SER A N   
5097  C CA  . SER A  338 ? 0.3021 0.3191 0.3376 -0.0814 0.0561  0.0317  364 SER A CA  
5098  C C   . SER A  338 ? 0.2941 0.3280 0.3372 -0.0832 0.0556  0.0335  364 SER A C   
5099  O O   . SER A  338 ? 0.2942 0.3396 0.3424 -0.0898 0.0536  0.0318  364 SER A O   
5100  C CB  . SER A  338 ? 0.3258 0.3298 0.3554 -0.0904 0.0608  0.0302  364 SER A CB  
5101  O OG  . SER A  338 ? 0.3542 0.3538 0.3820 -0.0924 0.0658  0.0332  364 SER A OG  
5107  N N   . LYS A  339 ? 0.2844 0.3199 0.3280 -0.0775 0.0576  0.0370  365 LYS A N   
5108  C CA  . LYS A  339 ? 0.2747 0.3256 0.3252 -0.0780 0.0577  0.0388  365 LYS A CA  
5109  C C   . LYS A  339 ? 0.2596 0.3246 0.3167 -0.0709 0.0528  0.0388  365 LYS A C   
5110  O O   . LYS A  339 ? 0.2466 0.3259 0.3104 -0.0710 0.0525  0.0400  365 LYS A O   
5111  C CB  . LYS A  339 ? 0.3093 0.3547 0.3564 -0.0755 0.0626  0.0426  365 LYS A CB  
5112  C CG  . LYS A  339 ? 0.3904 0.4203 0.4304 -0.0817 0.0681  0.0433  365 LYS A CG  
5113  C CD  . LYS A  339 ? 0.4690 0.5034 0.5115 -0.0934 0.0698  0.0417  365 LYS A CD  
5114  C CE  . LYS A  339 ? 0.5392 0.5577 0.5743 -0.0995 0.0759  0.0427  365 LYS A CE  
5115  N NZ  . LYS A  339 ? 0.5790 0.5983 0.6147 -0.1116 0.0769  0.0398  365 LYS A NZ  
5129  N N   . LEU A  340 ? 0.2533 0.3143 0.3086 -0.0647 0.0492  0.0375  366 LEU A N   
5130  C CA  . LEU A  340 ? 0.2449 0.3175 0.3057 -0.0582 0.0446  0.0373  366 LEU A CA  
5131  C C   . LEU A  340 ? 0.2451 0.3285 0.3115 -0.0633 0.0406  0.0350  366 LEU A C   
5132  O O   . LEU A  340 ? 0.2389 0.3217 0.3050 -0.0612 0.0367  0.0331  366 LEU A O   
5133  C CB  . LEU A  340 ? 0.2459 0.3095 0.3022 -0.0504 0.0426  0.0369  366 LEU A CB  
5134  C CG  . LEU A  340 ? 0.2675 0.3208 0.3180 -0.0448 0.0458  0.0394  366 LEU A CG  
5135  C CD1 . LEU A  340 ? 0.2776 0.3227 0.3239 -0.0383 0.0434  0.0386  366 LEU A CD1 
5136  C CD2 . LEU A  340 ? 0.2651 0.3275 0.3187 -0.0405 0.0468  0.0418  366 LEU A CD2 
5148  N N   . LEU A  341 ? 0.2455 0.3402 0.3174 -0.0697 0.0416  0.0354  367 LEU A N   
5149  C CA  . LEU A  341 ? 0.2408 0.3474 0.3182 -0.0759 0.0382  0.0337  367 LEU A CA  
5150  C C   . LEU A  341 ? 0.2281 0.3446 0.3104 -0.0702 0.0325  0.0332  367 LEU A C   
5151  O O   . LEU A  341 ? 0.2349 0.3535 0.3175 -0.0738 0.0290  0.0312  367 LEU A O   
5152  C CB  . LEU A  341 ? 0.2412 0.3614 0.3252 -0.0821 0.0401  0.0350  367 LEU A CB  
5153  C CG  . LEU A  341 ? 0.2813 0.3938 0.3615 -0.0891 0.0458  0.0357  367 LEU A CG  
5154  C CD1 . LEU A  341 ? 0.2859 0.4148 0.3740 -0.0954 0.0469  0.0368  367 LEU A CD1 
5155  C CD2 . LEU A  341 ? 0.3022 0.4000 0.3748 -0.0965 0.0472  0.0331  367 LEU A CD2 
5167  N N   . SER A  342 ? 0.2189 0.3409 0.3045 -0.0615 0.0318  0.0350  368 SER A N   
5168  C CA  . SER A  342 ? 0.2139 0.3449 0.3042 -0.0557 0.0269  0.0349  368 SER A CA  
5169  C C   . SER A  342 ? 0.2130 0.3329 0.2977 -0.0492 0.0247  0.0338  368 SER A C   
5170  O O   . SER A  342 ? 0.2085 0.3343 0.2963 -0.0439 0.0210  0.0339  368 SER A O   
5171  C CB  . SER A  342 ? 0.2321 0.3753 0.3292 -0.0499 0.0274  0.0372  368 SER A CB  
5172  O OG  . SER A  342 ? 0.2677 0.4228 0.3708 -0.0555 0.0294  0.0383  368 SER A OG  
5178  N N   . LEU A  343 ? 0.2091 0.3135 0.2859 -0.0494 0.0271  0.0330  369 LEU A N   
5179  C CA  . LEU A  343 ? 0.2088 0.3035 0.2806 -0.0432 0.0252  0.0322  369 LEU A CA  
5180  C C   . LEU A  343 ? 0.2053 0.3026 0.2780 -0.0438 0.0205  0.0302  369 LEU A C   
5181  O O   . LEU A  343 ? 0.2101 0.3077 0.2824 -0.0508 0.0196  0.0286  369 LEU A O   
5182  C CB  . LEU A  343 ? 0.2179 0.2962 0.2816 -0.0439 0.0286  0.0318  369 LEU A CB  
5183  C CG  . LEU A  343 ? 0.2434 0.3129 0.3025 -0.0362 0.0278  0.0318  369 LEU A CG  
5184  C CD1 . LEU A  343 ? 0.2398 0.3137 0.3006 -0.0290 0.0283  0.0340  369 LEU A CD1 
5185  C CD2 . LEU A  343 ? 0.2613 0.3155 0.3130 -0.0373 0.0311  0.0316  369 LEU A CD2 
5197  N N   . ARG A  344 ? 0.2007 0.2999 0.2745 -0.0367 0.0175  0.0305  370 ARG A N   
5198  C CA  . ARG A  344 ? 0.2046 0.3059 0.2789 -0.0359 0.0129  0.0291  370 ARG A CA  
5199  C C   . ARG A  344 ? 0.2140 0.3032 0.2821 -0.0319 0.0124  0.0279  370 ARG A C   
5200  O O   . ARG A  344 ? 0.2192 0.3055 0.2850 -0.0339 0.0100  0.0262  370 ARG A O   
5201  C CB  . ARG A  344 ? 0.2177 0.3313 0.2986 -0.0308 0.0099  0.0305  370 ARG A CB  
5202  C CG  . ARG A  344 ? 0.2658 0.3938 0.3543 -0.0342 0.0097  0.0319  370 ARG A CG  
5203  C CD  . ARG A  344 ? 0.3160 0.4549 0.4107 -0.0284 0.0064  0.0333  370 ARG A CD  
5204  N NE  . ARG A  344 ? 0.3653 0.5196 0.4683 -0.0303 0.0064  0.0351  370 ARG A NE  
5205  C CZ  . ARG A  344 ? 0.4207 0.5852 0.5280 -0.0361 0.0038  0.0353  370 ARG A CZ  
5206  N NH1 . ARG A  344 ? 0.4349 0.5952 0.5384 -0.0412 0.0013  0.0335  370 ARG A NH1 
5207  N NH2 . ARG A  344 ? 0.4297 0.6092 0.5453 -0.0371 0.0040  0.0372  370 ARG A NH2 
5221  N N   . ALA A  345 ? 0.2066 0.2896 0.2718 -0.0261 0.0144  0.0289  371 ALA A N   
5222  C CA  . ALA A  345 ? 0.2127 0.2856 0.2727 -0.0220 0.0138  0.0279  371 ALA A CA  
5223  C C   . ALA A  345 ? 0.2233 0.2870 0.2787 -0.0198 0.0176  0.0290  371 ALA A C   
5224  O O   . ALA A  345 ? 0.2304 0.2970 0.2870 -0.0173 0.0197  0.0308  371 ALA A O   
5225  C CB  . ALA A  345 ? 0.2086 0.2857 0.2705 -0.0155 0.0106  0.0282  371 ALA A CB  
5231  N N   . LEU A  346 ? 0.2147 0.2676 0.2648 -0.0205 0.0188  0.0280  372 LEU A N   
5232  C CA  . LEU A  346 ? 0.2120 0.2555 0.2574 -0.0179 0.0222  0.0293  372 LEU A CA  
5233  C C   . LEU A  346 ? 0.2084 0.2460 0.2505 -0.0128 0.0207  0.0287  372 LEU A C   
5234  O O   . LEU A  346 ? 0.2053 0.2389 0.2457 -0.0144 0.0194  0.0268  372 LEU A O   
5235  C CB  . LEU A  346 ? 0.2182 0.2534 0.2603 -0.0238 0.0259  0.0289  372 LEU A CB  
5236  C CG  . LEU A  346 ? 0.2501 0.2743 0.2870 -0.0214 0.0299  0.0307  372 LEU A CG  
5237  C CD1 . LEU A  346 ? 0.2537 0.2815 0.2914 -0.0178 0.0316  0.0337  372 LEU A CD1 
5238  C CD2 . LEU A  346 ? 0.2642 0.2796 0.2978 -0.0278 0.0336  0.0301  372 LEU A CD2 
5250  N N   . HIS A  347 ? 0.1996 0.2372 0.2407 -0.0068 0.0208  0.0303  373 HIS A N   
5251  C CA  . HIS A  347 ? 0.2056 0.2388 0.2439 -0.0020 0.0193  0.0299  373 HIS A CA  
5252  C C   . HIS A  347 ? 0.2100 0.2344 0.2437 0.0001  0.0225  0.0317  373 HIS A C   
5253  O O   . HIS A  347 ? 0.2111 0.2357 0.2438 0.0020  0.0246  0.0340  373 HIS A O   
5254  C CB  . HIS A  347 ? 0.2106 0.2502 0.2506 0.0030  0.0165  0.0301  373 HIS A CB  
5255  C CG  . HIS A  347 ? 0.2343 0.2822 0.2790 0.0016  0.0136  0.0289  373 HIS A CG  
5256  N ND1 . HIS A  347 ? 0.2528 0.3015 0.2981 0.0015  0.0103  0.0271  373 HIS A ND1 
5257  C CD2 . HIS A  347 ? 0.2467 0.3025 0.2956 0.0004  0.0138  0.0295  373 HIS A CD2 
5258  C CE1 . HIS A  347 ? 0.2585 0.3152 0.3082 0.0003  0.0084  0.0270  373 HIS A CE1 
5259  N NE2 . HIS A  347 ? 0.2598 0.3214 0.3120 -0.0002 0.0104  0.0284  373 HIS A NE2 
5267  N N   . LEU A  348 ? 0.2082 0.2250 0.2391 -0.0002 0.0231  0.0308  374 LEU A N   
5268  C CA  . LEU A  348 ? 0.2286 0.2365 0.2553 0.0023  0.0262  0.0327  374 LEU A CA  
5269  C C   . LEU A  348 ? 0.2341 0.2393 0.2594 0.0064  0.0244  0.0320  374 LEU A C   
5270  O O   . LEU A  348 ? 0.2448 0.2421 0.2675 0.0064  0.0265  0.0319  374 LEU A O   
5271  C CB  . LEU A  348 ? 0.2453 0.2450 0.2699 -0.0029 0.0300  0.0325  374 LEU A CB  
5272  C CG  . LEU A  348 ? 0.2717 0.2720 0.2967 -0.0066 0.0329  0.0340  374 LEU A CG  
5273  C CD1 . LEU A  348 ? 0.2833 0.2768 0.3067 -0.0134 0.0358  0.0325  374 LEU A CD1 
5274  C CD2 . LEU A  348 ? 0.2829 0.2790 0.3048 -0.0027 0.0359  0.0377  374 LEU A CD2 
5286  N N   . ARG A  349 ? 0.2292 0.2409 0.2561 0.0098  0.0209  0.0315  375 ARG A N   
5287  C CA  . ARG A  349 ? 0.2355 0.2457 0.2612 0.0137  0.0193  0.0311  375 ARG A CA  
5288  C C   . ARG A  349 ? 0.2295 0.2360 0.2523 0.0182  0.0213  0.0342  375 ARG A C   
5289  O O   . ARG A  349 ? 0.2296 0.2369 0.2516 0.0189  0.0228  0.0364  375 ARG A O   
5290  C CB  . ARG A  349 ? 0.2604 0.2780 0.2880 0.0158  0.0152  0.0299  375 ARG A CB  
5291  C CG  . ARG A  349 ? 0.3411 0.3629 0.3715 0.0122  0.0128  0.0275  375 ARG A CG  
5292  C CD  . ARG A  349 ? 0.4206 0.4465 0.4519 0.0145  0.0091  0.0261  375 ARG A CD  
5293  N NE  . ARG A  349 ? 0.4867 0.5168 0.5180 0.0182  0.0081  0.0272  375 ARG A NE  
5294  C CZ  . ARG A  349 ? 0.5460 0.5786 0.5769 0.0208  0.0054  0.0263  375 ARG A CZ  
5295  N NH1 . ARG A  349 ? 0.5442 0.5762 0.5753 0.0201  0.0034  0.0246  375 ARG A NH1 
5296  N NH2 . ARG A  349 ? 0.5594 0.5952 0.5897 0.0237  0.0049  0.0270  375 ARG A NH2 
5310  N N   . GLY A  350 ? 0.2201 0.2234 0.2416 0.0213  0.0212  0.0346  376 GLY A N   
5311  C CA  . GLY A  350 ? 0.2251 0.2266 0.2442 0.0263  0.0224  0.0378  376 GLY A CA  
5312  C C   . GLY A  350 ? 0.2281 0.2236 0.2446 0.0265  0.0265  0.0410  376 GLY A C   
5313  O O   . GLY A  350 ? 0.2238 0.2206 0.2385 0.0301  0.0268  0.0441  376 GLY A O   
5317  N N   . TYR A  351 ? 0.2273 0.2159 0.2432 0.0223  0.0296  0.0404  377 TYR A N   
5318  C CA  . TYR A  351 ? 0.2492 0.2296 0.2621 0.0221  0.0342  0.0434  377 TYR A CA  
5319  C C   . TYR A  351 ? 0.2530 0.2264 0.2640 0.0265  0.0359  0.0450  377 TYR A C   
5320  O O   . TYR A  351 ? 0.2518 0.2218 0.2602 0.0306  0.0378  0.0490  377 TYR A O   
5321  C CB  . TYR A  351 ? 0.2580 0.2334 0.2709 0.0154  0.0368  0.0415  377 TYR A CB  
5322  C CG  . TYR A  351 ? 0.2674 0.2329 0.2767 0.0144  0.0419  0.0443  377 TYR A CG  
5323  C CD1 . TYR A  351 ? 0.2799 0.2346 0.2863 0.0158  0.0452  0.0450  377 TYR A CD1 
5324  C CD2 . TYR A  351 ? 0.2762 0.2427 0.2849 0.0116  0.0436  0.0460  377 TYR A CD2 
5325  C CE1 . TYR A  351 ? 0.2915 0.2358 0.2942 0.0148  0.0501  0.0477  377 TYR A CE1 
5326  C CE2 . TYR A  351 ? 0.2932 0.2501 0.2984 0.0100  0.0485  0.0485  377 TYR A CE2 
5327  C CZ  . TYR A  351 ? 0.3069 0.2522 0.3089 0.0117  0.0517  0.0495  377 TYR A CZ  
5328  O OH  . TYR A  351 ? 0.3388 0.2730 0.3367 0.0100  0.0568  0.0519  377 TYR A OH  
5338  N N   . VAL A  352 ? 0.2520 0.2237 0.2642 0.0258  0.0352  0.0420  378 VAL A N   
5339  C CA  . VAL A  352 ? 0.2677 0.2344 0.2791 0.0299  0.0365  0.0427  378 VAL A CA  
5340  C C   . VAL A  352 ? 0.2804 0.2344 0.2888 0.0287  0.0419  0.0435  378 VAL A C   
5341  O O   . VAL A  352 ? 0.2866 0.2351 0.2925 0.0308  0.0449  0.0473  378 VAL A O   
5342  C CB  . VAL A  352 ? 0.2749 0.2466 0.2864 0.0368  0.0348  0.0462  378 VAL A CB  
5343  C CG1 . VAL A  352 ? 0.2871 0.2551 0.2989 0.0412  0.0360  0.0468  378 VAL A CG1 
5344  C CG2 . VAL A  352 ? 0.2702 0.2535 0.2842 0.0372  0.0297  0.0448  378 VAL A CG2 
5354  N N   . PHE A  353 ? 0.2833 0.2323 0.2915 0.0251  0.0433  0.0399  379 PHE A N   
5355  C CA  . PHE A  353 ? 0.2996 0.2354 0.3045 0.0233  0.0486  0.0396  379 PHE A CA  
5356  C C   . PHE A  353 ? 0.3119 0.2447 0.3170 0.0219  0.0492  0.0356  379 PHE A C   
5357  O O   . PHE A  353 ? 0.3105 0.2513 0.3181 0.0203  0.0453  0.0326  379 PHE A O   
5358  C CB  . PHE A  353 ? 0.2908 0.2221 0.2937 0.0165  0.0510  0.0389  379 PHE A CB  
5359  C CG  . PHE A  353 ? 0.2796 0.2173 0.2845 0.0095  0.0481  0.0346  379 PHE A CG  
5360  C CD1 . PHE A  353 ? 0.2729 0.2227 0.2811 0.0091  0.0436  0.0346  379 PHE A CD1 
5361  C CD2 . PHE A  353 ? 0.2830 0.2144 0.2861 0.0033  0.0502  0.0308  379 PHE A CD2 
5362  C CE1 . PHE A  353 ? 0.2785 0.2345 0.2889 0.0032  0.0410  0.0313  379 PHE A CE1 
5363  C CE2 . PHE A  353 ? 0.2877 0.2259 0.2927 -0.0031 0.0473  0.0274  379 PHE A CE2 
5364  C CZ  . PHE A  353 ? 0.2815 0.2322 0.2904 -0.0028 0.0427  0.0278  379 PHE A CZ  
5374  N N   . GLN A  354 ? 0.3170 0.2376 0.3190 0.0230  0.0542  0.0357  380 GLN A N   
5375  C CA  . GLN A  354 ? 0.3271 0.2439 0.3288 0.0227  0.0555  0.0321  380 GLN A CA  
5376  C C   . GLN A  354 ? 0.3333 0.2456 0.3328 0.0145  0.0567  0.0271  380 GLN A C   
5377  O O   . GLN A  354 ? 0.3305 0.2448 0.3306 0.0132  0.0556  0.0236  380 GLN A O   
5378  C CB  . GLN A  354 ? 0.3520 0.2577 0.3516 0.0286  0.0608  0.0345  380 GLN A CB  
5379  C CG  . GLN A  354 ? 0.3798 0.2898 0.3814 0.0372  0.0598  0.0401  380 GLN A CG  
5380  C CD  . GLN A  354 ? 0.4560 0.3544 0.4554 0.0430  0.0654  0.0431  380 GLN A CD  
5381  O OE1 . GLN A  354 ? 0.4856 0.3753 0.4834 0.0426  0.0692  0.0404  380 GLN A OE1 
5382  N NE2 . GLN A  354 ? 0.4520 0.3499 0.4511 0.0488  0.0660  0.0488  380 GLN A NE2 
5391  N N   . GLU A  355 ? 0.3428 0.2487 0.3394 0.0087  0.0591  0.0266  381 GLU A N   
5392  C CA  . GLU A  355 ? 0.3631 0.2641 0.3570 0.0003  0.0606  0.0217  381 GLU A CA  
5393  C C   . GLU A  355 ? 0.3669 0.2712 0.3608 -0.0069 0.0594  0.0212  381 GLU A C   
5394  O O   . GLU A  355 ? 0.3691 0.2703 0.3621 -0.0065 0.0613  0.0245  381 GLU A O   
5395  C CB  . GLU A  355 ? 0.4142 0.2985 0.4029 0.0002  0.0674  0.0209  381 GLU A CB  
5396  C CG  . GLU A  355 ? 0.5307 0.4081 0.5154 -0.0082 0.0696  0.0154  381 GLU A CG  
5397  C CD  . GLU A  355 ? 0.6523 0.5117 0.6312 -0.0087 0.0769  0.0143  381 GLU A CD  
5398  O OE1 . GLU A  355 ? 0.6716 0.5231 0.6494 -0.0027 0.0806  0.0185  381 GLU A OE1 
5399  O OE2 . GLU A  355 ? 0.6877 0.5408 0.6626 -0.0153 0.0791  0.0093  381 GLU A OE2 
5406  N N   . LEU A  356 ? 0.3634 0.2734 0.3579 -0.0137 0.0566  0.0172  382 LEU A N   
5407  C CA  . LEU A  356 ? 0.3666 0.2807 0.3616 -0.0211 0.0555  0.0165  382 LEU A CA  
5408  C C   . LEU A  356 ? 0.3828 0.2863 0.3727 -0.0291 0.0595  0.0126  382 LEU A C   
5409  O O   . LEU A  356 ? 0.3683 0.2709 0.3566 -0.0322 0.0590  0.0086  382 LEU A O   
5410  C CB  . LEU A  356 ? 0.3572 0.2865 0.3568 -0.0230 0.0492  0.0152  382 LEU A CB  
5411  C CG  . LEU A  356 ? 0.3612 0.2975 0.3628 -0.0295 0.0476  0.0151  382 LEU A CG  
5412  C CD1 . LEU A  356 ? 0.3605 0.2976 0.3633 -0.0268 0.0489  0.0195  382 LEU A CD1 
5413  C CD2 . LEU A  356 ? 0.3595 0.3099 0.3655 -0.0308 0.0416  0.0139  382 LEU A CD2 
5425  N N   . ARG A  357 ? 0.4158 0.3110 0.4029 -0.0327 0.0636  0.0137  383 ARG A N   
5426  C CA  . ARG A  357 ? 0.4510 0.3350 0.4326 -0.0411 0.0678  0.0100  383 ARG A CA  
5427  C C   . ARG A  357 ? 0.4669 0.3591 0.4502 -0.0499 0.0655  0.0087  383 ARG A C   
5428  O O   . ARG A  357 ? 0.4595 0.3621 0.4474 -0.0487 0.0627  0.0118  383 ARG A O   
5429  C CB  . ARG A  357 ? 0.4828 0.3502 0.4596 -0.0395 0.0746  0.0122  383 ARG A CB  
5430  C CG  . ARG A  357 ? 0.5379 0.3974 0.5136 -0.0297 0.0773  0.0146  383 ARG A CG  
5431  C CD  . ARG A  357 ? 0.5958 0.4387 0.5666 -0.0284 0.0841  0.0172  383 ARG A CD  
5432  N NE  . ARG A  357 ? 0.6298 0.4757 0.6021 -0.0275 0.0839  0.0221  383 ARG A NE  
5433  C CZ  . ARG A  357 ? 0.6747 0.5079 0.6430 -0.0267 0.0892  0.0254  383 ARG A CZ  
5434  N NH1 . ARG A  357 ? 0.6891 0.5048 0.6517 -0.0261 0.0954  0.0244  383 ARG A NH1 
5435  N NH2 . ARG A  357 ? 0.6618 0.4993 0.6316 -0.0262 0.0887  0.0297  383 ARG A NH2 
5449  N N   . GLU A  358 ? 0.4888 0.3764 0.4682 -0.0590 0.0671  0.0042  384 GLU A N   
5450  C CA  . GLU A  358 ? 0.5077 0.4038 0.4888 -0.0682 0.0649  0.0028  384 GLU A CA  
5451  C C   . GLU A  358 ? 0.5170 0.4112 0.4987 -0.0698 0.0676  0.0063  384 GLU A C   
5452  O O   . GLU A  358 ? 0.5229 0.4302 0.5096 -0.0720 0.0642  0.0078  384 GLU A O   
5453  C CB  . GLU A  358 ? 0.5568 0.4464 0.5323 -0.0780 0.0668  -0.0028 384 GLU A CB  
5454  C CG  . GLU A  358 ? 0.6353 0.5347 0.6127 -0.0881 0.0643  -0.0043 384 GLU A CG  
5455  C CD  . GLU A  358 ? 0.7327 0.6336 0.7067 -0.0968 0.0628  -0.0098 384 GLU A CD  
5456  O OE1 . GLU A  358 ? 0.7545 0.6418 0.7217 -0.0983 0.0667  -0.0134 384 GLU A OE1 
5457  O OE2 . GLU A  358 ? 0.7633 0.6791 0.7414 -0.1020 0.0579  -0.0105 384 GLU A OE2 
5464  N N   . ASP A  359 ? 0.5188 0.3971 0.4955 -0.0682 0.0737  0.0078  385 ASP A N   
5465  C CA  . ASP A  359 ? 0.5251 0.4003 0.5016 -0.0696 0.0767  0.0115  385 ASP A CA  
5466  C C   . ASP A  359 ? 0.4990 0.3862 0.4815 -0.0622 0.0733  0.0166  385 ASP A C   
5467  O O   . ASP A  359 ? 0.4976 0.3888 0.4817 -0.0648 0.0739  0.0191  385 ASP A O   
5468  C CB  . ASP A  359 ? 0.5764 0.4310 0.5460 -0.0675 0.0840  0.0129  385 ASP A CB  
5469  C CG  . ASP A  359 ? 0.6759 0.5160 0.6385 -0.0769 0.0891  0.0084  385 ASP A CG  
5470  O OD1 . ASP A  359 ? 0.6958 0.5422 0.6585 -0.0856 0.0867  0.0038  385 ASP A OD1 
5471  O OD2 . ASP A  359 ? 0.7223 0.5446 0.6790 -0.0754 0.0954  0.0095  385 ASP A OD2 
5476  N N   . ASP A  360 ? 0.4736 0.3663 0.4589 -0.0533 0.0700  0.0180  386 ASP A N   
5477  C CA  . ASP A  360 ? 0.4588 0.3616 0.4488 -0.0461 0.0672  0.0225  386 ASP A CA  
5478  C C   . ASP A  360 ? 0.4344 0.3547 0.4306 -0.0490 0.0621  0.0225  386 ASP A C   
5479  O O   . ASP A  360 ? 0.4252 0.3517 0.4241 -0.0457 0.0615  0.0262  386 ASP A O   
5480  C CB  . ASP A  360 ? 0.4761 0.3799 0.4672 -0.0363 0.0651  0.0238  386 ASP A CB  
5481  C CG  . ASP A  360 ? 0.5541 0.4419 0.5401 -0.0319 0.0701  0.0246  386 ASP A CG  
5482  O OD1 . ASP A  360 ? 0.5545 0.4305 0.5364 -0.0331 0.0753  0.0267  386 ASP A OD1 
5483  O OD2 . ASP A  360 ? 0.6033 0.4904 0.5895 -0.0273 0.0690  0.0233  386 ASP A OD2 
5488  N N   . PHE A  361 ? 0.4188 0.3471 0.4171 -0.0549 0.0588  0.0186  387 PHE A N   
5489  C CA  . PHE A  361 ? 0.4035 0.3487 0.4081 -0.0572 0.0540  0.0188  387 PHE A CA  
5490  C C   . PHE A  361 ? 0.3996 0.3480 0.4047 -0.0676 0.0550  0.0171  387 PHE A C   
5491  O O   . PHE A  361 ? 0.3902 0.3530 0.4006 -0.0705 0.0510  0.0166  387 PHE A O   
5492  C CB  . PHE A  361 ? 0.3889 0.3437 0.3966 -0.0548 0.0485  0.0166  387 PHE A CB  
5493  C CG  . PHE A  361 ? 0.3842 0.3445 0.3948 -0.0452 0.0455  0.0190  387 PHE A CG  
5494  C CD1 . PHE A  361 ? 0.3983 0.3549 0.4083 -0.0386 0.0475  0.0228  387 PHE A CD1 
5495  C CD2 . PHE A  361 ? 0.3844 0.3537 0.3981 -0.0432 0.0405  0.0175  387 PHE A CD2 
5496  C CE1 . PHE A  361 ? 0.4011 0.3633 0.4135 -0.0305 0.0445  0.0248  387 PHE A CE1 
5497  C CE2 . PHE A  361 ? 0.3873 0.3616 0.4034 -0.0351 0.0378  0.0194  387 PHE A CE2 
5498  C CZ  . PHE A  361 ? 0.3893 0.3601 0.4047 -0.0290 0.0397  0.0229  387 PHE A CZ  
5508  N N   . GLN A  362 ? 0.4060 0.3414 0.4057 -0.0729 0.0605  0.0166  388 GLN A N   
5509  C CA  . GLN A  362 ? 0.4121 0.3501 0.4120 -0.0836 0.0619  0.0150  388 GLN A CA  
5510  C C   . GLN A  362 ? 0.3947 0.3472 0.4011 -0.0840 0.0600  0.0181  388 GLN A C   
5511  O O   . GLN A  362 ? 0.3937 0.3577 0.4039 -0.0910 0.0576  0.0164  388 GLN A O   
5512  C CB  . GLN A  362 ? 0.4606 0.3807 0.4533 -0.0887 0.0687  0.0145  388 GLN A CB  
5513  C CG  . GLN A  362 ? 0.5645 0.4697 0.5505 -0.0897 0.0713  0.0109  388 GLN A CG  
5514  C CD  . GLN A  362 ? 0.6697 0.5782 0.6544 -0.0991 0.0694  0.0055  388 GLN A CD  
5515  O OE1 . GLN A  362 ? 0.7055 0.6169 0.6900 -0.1089 0.0702  0.0038  388 GLN A OE1 
5516  N NE2 . GLN A  362 ? 0.6886 0.5971 0.6722 -0.0966 0.0670  0.0027  388 GLN A NE2 
5525  N N   . PRO A  363 ? 0.3811 0.3343 0.3889 -0.0768 0.0610  0.0225  389 PRO A N   
5526  C CA  . PRO A  363 ? 0.3659 0.3333 0.3798 -0.0772 0.0595  0.0250  389 PRO A CA  
5527  C C   . PRO A  363 ? 0.3566 0.3424 0.3779 -0.0762 0.0533  0.0241  389 PRO A C   
5528  O O   . PRO A  363 ? 0.3541 0.3523 0.3808 -0.0793 0.0523  0.0251  389 PRO A O   
5529  C CB  . PRO A  363 ? 0.3749 0.3383 0.3877 -0.0683 0.0614  0.0295  389 PRO A CB  
5530  C CG  . PRO A  363 ? 0.3918 0.3364 0.3971 -0.0661 0.0656  0.0298  389 PRO A CG  
5531  C CD  . PRO A  363 ? 0.3777 0.3198 0.3817 -0.0679 0.0634  0.0254  389 PRO A CD  
5539  N N   . LEU A  364 ? 0.3520 0.3397 0.3739 -0.0719 0.0494  0.0224  390 LEU A N   
5540  C CA  . LEU A  364 ? 0.3519 0.3557 0.3803 -0.0702 0.0436  0.0217  390 LEU A CA  
5541  C C   . LEU A  364 ? 0.3551 0.3654 0.3849 -0.0784 0.0409  0.0182  390 LEU A C   
5542  O O   . LEU A  364 ? 0.3512 0.3758 0.3869 -0.0778 0.0362  0.0181  390 LEU A O   
5543  C CB  . LEU A  364 ? 0.3520 0.3543 0.3799 -0.0615 0.0408  0.0218  390 LEU A CB  
5544  C CG  . LEU A  364 ? 0.3662 0.3624 0.3922 -0.0528 0.0426  0.0250  390 LEU A CG  
5545  C CD1 . LEU A  364 ? 0.3650 0.3577 0.3894 -0.0461 0.0402  0.0242  390 LEU A CD1 
5546  C CD2 . LEU A  364 ? 0.3646 0.3721 0.3956 -0.0490 0.0414  0.0279  390 LEU A CD2 
5558  N N   . MET A  365 ? 0.3571 0.3565 0.3811 -0.0855 0.0437  0.0152  391 MET A N   
5559  C CA  . MET A  365 ? 0.3669 0.3707 0.3906 -0.0930 0.0410  0.0114  391 MET A CA  
5560  C C   . MET A  365 ? 0.3672 0.3854 0.3961 -0.1012 0.0390  0.0111  391 MET A C   
5561  O O   . MET A  365 ? 0.3692 0.3952 0.3993 -0.1058 0.0352  0.0087  391 MET A O   
5562  C CB  . MET A  365 ? 0.3881 0.3747 0.4032 -0.0982 0.0451  0.0080  391 MET A CB  
5563  C CG  . MET A  365 ? 0.4255 0.4011 0.4363 -0.0907 0.0456  0.0074  391 MET A CG  
5564  S SD  . MET A  365 ? 0.5164 0.4698 0.5170 -0.0946 0.0518  0.0041  391 MET A SD  
5565  C CE  . MET A  365 ? 0.4610 0.4078 0.4601 -0.0831 0.0512  0.0050  391 MET A CE  
5575  N N   . GLN A  366 ? 0.3652 0.3879 0.3974 -0.1029 0.0413  0.0136  392 GLN A N   
5576  C CA  . GLN A  366 ? 0.3793 0.4174 0.4174 -0.1104 0.0394  0.0136  392 GLN A CA  
5577  C C   . GLN A  366 ? 0.3617 0.4174 0.4091 -0.1039 0.0358  0.0170  392 GLN A C   
5578  O O   . GLN A  366 ? 0.3608 0.4309 0.4144 -0.1088 0.0345  0.0177  392 GLN A O   
5579  C CB  . GLN A  366 ? 0.4257 0.4575 0.4613 -0.1182 0.0450  0.0138  392 GLN A CB  
5580  C CG  . GLN A  366 ? 0.5302 0.5710 0.5677 -0.1305 0.0442  0.0115  392 GLN A CG  
5581  C CD  . GLN A  366 ? 0.6558 0.6884 0.6899 -0.1386 0.0501  0.0115  392 GLN A CD  
5582  O OE1 . GLN A  366 ? 0.7038 0.7201 0.7321 -0.1359 0.0552  0.0126  392 GLN A OE1 
5583  N NE2 . GLN A  366 ? 0.6717 0.7158 0.7095 -0.1488 0.0495  0.0105  392 GLN A NE2 
5592  N N   . LEU A  367 ? 0.3403 0.3952 0.3886 -0.0932 0.0343  0.0189  393 LEU A N   
5593  C CA  . LEU A  367 ? 0.3185 0.3883 0.3747 -0.0868 0.0312  0.0217  393 LEU A CA  
5594  C C   . LEU A  367 ? 0.3095 0.3920 0.3701 -0.0879 0.0254  0.0204  393 LEU A C   
5595  O O   . LEU A  367 ? 0.3165 0.3937 0.3736 -0.0860 0.0230  0.0186  393 LEU A O   
5596  C CB  . LEU A  367 ? 0.3101 0.3735 0.3646 -0.0760 0.0318  0.0237  393 LEU A CB  
5597  C CG  . LEU A  367 ? 0.3267 0.3776 0.3764 -0.0744 0.0373  0.0255  393 LEU A CG  
5598  C CD1 . LEU A  367 ? 0.3310 0.3774 0.3792 -0.0641 0.0371  0.0274  393 LEU A CD1 
5599  C CD2 . LEU A  367 ? 0.3350 0.3931 0.3884 -0.0782 0.0402  0.0277  393 LEU A CD2 
5611  N N   . PRO A  368 ? 0.2950 0.3941 0.3630 -0.0918 0.0232  0.0213  394 PRO A N   
5612  C CA  . PRO A  368 ? 0.2830 0.3941 0.3547 -0.0941 0.0177  0.0203  394 PRO A CA  
5613  C C   . PRO A  368 ? 0.2663 0.3826 0.3410 -0.0849 0.0134  0.0216  394 PRO A C   
5614  O O   . PRO A  368 ? 0.2687 0.3882 0.3428 -0.0863 0.0093  0.0202  394 PRO A O   
5615  C CB  . PRO A  368 ? 0.2856 0.4137 0.3651 -0.1001 0.0170  0.0216  394 PRO A CB  
5616  C CG  . PRO A  368 ? 0.2942 0.4223 0.3761 -0.0971 0.0213  0.0242  394 PRO A CG  
5617  C CD  . PRO A  368 ? 0.2838 0.3919 0.3570 -0.0950 0.0258  0.0234  394 PRO A CD  
5625  N N   . ASN A  369 ? 0.2497 0.3667 0.3270 -0.0760 0.0142  0.0241  395 ASN A N   
5626  C CA  . ASN A  369 ? 0.2397 0.3612 0.3196 -0.0675 0.0102  0.0252  395 ASN A CA  
5627  C C   . ASN A  369 ? 0.2265 0.3341 0.3004 -0.0606 0.0111  0.0247  395 ASN A C   
5628  O O   . ASN A  369 ? 0.2113 0.3217 0.2871 -0.0534 0.0084  0.0257  395 ASN A O   
5629  C CB  . ASN A  369 ? 0.2493 0.3846 0.3376 -0.0625 0.0097  0.0282  395 ASN A CB  
5630  C CG  . ASN A  369 ? 0.2993 0.4503 0.3946 -0.0687 0.0082  0.0290  395 ASN A CG  
5631  O OD1 . ASN A  369 ? 0.3132 0.4686 0.4084 -0.0748 0.0052  0.0276  395 ASN A OD1 
5632  N ND2 . ASN A  369 ? 0.3217 0.4842 0.4240 -0.0672 0.0095  0.0313  395 ASN A ND2 
5639  N N   . LEU A  370 ? 0.2288 0.3215 0.2955 -0.0626 0.0147  0.0232  396 LEU A N   
5640  C CA  . LEU A  370 ? 0.2372 0.3177 0.2986 -0.0562 0.0155  0.0228  396 LEU A CA  
5641  C C   . LEU A  370 ? 0.2475 0.3265 0.3067 -0.0557 0.0117  0.0209  396 LEU A C   
5642  O O   . LEU A  370 ? 0.2586 0.3316 0.3134 -0.0615 0.0120  0.0184  396 LEU A O   
5643  C CB  . LEU A  370 ? 0.2438 0.3094 0.2985 -0.0585 0.0206  0.0221  396 LEU A CB  
5644  C CG  . LEU A  370 ? 0.2708 0.3239 0.3202 -0.0517 0.0218  0.0221  396 LEU A CG  
5645  C CD1 . LEU A  370 ? 0.2696 0.3269 0.3217 -0.0430 0.0207  0.0245  396 LEU A CD1 
5646  C CD2 . LEU A  370 ? 0.2836 0.3232 0.3273 -0.0537 0.0271  0.0222  396 LEU A CD2 
5658  N N   . SER A  371 ? 0.2444 0.3295 0.3067 -0.0494 0.0081  0.0220  397 SER A N   
5659  C CA  . SER A  371 ? 0.2490 0.3340 0.3096 -0.0487 0.0043  0.0206  397 SER A CA  
5660  C C   . SER A  371 ? 0.2396 0.3144 0.2958 -0.0424 0.0045  0.0201  397 SER A C   
5661  O O   . SER A  371 ? 0.2427 0.3141 0.2957 -0.0431 0.0025  0.0185  397 SER A O   
5662  C CB  . SER A  371 ? 0.2848 0.3839 0.3519 -0.0468 -0.0002 0.0223  397 SER A CB  
5663  O OG  . SER A  371 ? 0.3330 0.4353 0.4036 -0.0388 -0.0005 0.0244  397 SER A OG  
5669  N N   . THR A  372 ? 0.2261 0.2965 0.2818 -0.0365 0.0068  0.0216  398 THR A N   
5670  C CA  . THR A  372 ? 0.2321 0.2940 0.2840 -0.0307 0.0069  0.0212  398 THR A CA  
5671  C C   . THR A  372 ? 0.2225 0.2735 0.2700 -0.0298 0.0113  0.0214  398 THR A C   
5672  O O   . THR A  372 ? 0.2103 0.2618 0.2589 -0.0292 0.0140  0.0231  398 THR A O   
5673  C CB  . THR A  372 ? 0.2604 0.3280 0.3157 -0.0235 0.0048  0.0230  398 THR A CB  
5674  O OG1 . THR A  372 ? 0.2808 0.3569 0.3395 -0.0237 0.0007  0.0231  398 THR A OG1 
5675  C CG2 . THR A  372 ? 0.2724 0.3320 0.3238 -0.0178 0.0050  0.0227  398 THR A CG2 
5683  N N   . ILE A  373 ? 0.2216 0.2627 0.2641 -0.0293 0.0122  0.0198  399 ILE A N   
5684  C CA  . ILE A  373 ? 0.2350 0.2652 0.2732 -0.0272 0.0161  0.0203  399 ILE A CA  
5685  C C   . ILE A  373 ? 0.2265 0.2533 0.2628 -0.0211 0.0147  0.0202  399 ILE A C   
5686  O O   . ILE A  373 ? 0.2249 0.2508 0.2600 -0.0218 0.0127  0.0183  399 ILE A O   
5687  C CB  . ILE A  373 ? 0.2639 0.2845 0.2976 -0.0331 0.0196  0.0185  399 ILE A CB  
5688  C CG1 . ILE A  373 ? 0.2931 0.3019 0.3224 -0.0295 0.0237  0.0195  399 ILE A CG1 
5689  C CG2 . ILE A  373 ? 0.2767 0.2956 0.3081 -0.0368 0.0178  0.0154  399 ILE A CG2 
5690  C CD1 . ILE A  373 ? 0.3276 0.3367 0.3578 -0.0264 0.0260  0.0226  399 ILE A CD1 
5702  N N   . ASN A  374 ? 0.2144 0.2402 0.2507 -0.0153 0.0156  0.0222  400 ASN A N   
5703  C CA  . ASN A  374 ? 0.2187 0.2425 0.2536 -0.0097 0.0141  0.0223  400 ASN A CA  
5704  C C   . ASN A  374 ? 0.2194 0.2340 0.2505 -0.0067 0.0175  0.0234  400 ASN A C   
5705  O O   . ASN A  374 ? 0.2105 0.2242 0.2412 -0.0045 0.0196  0.0257  400 ASN A O   
5706  C CB  . ASN A  374 ? 0.2215 0.2532 0.2595 -0.0053 0.0114  0.0235  400 ASN A CB  
5707  C CG  . ASN A  374 ? 0.2673 0.2977 0.3040 0.0005  0.0102  0.0239  400 ASN A CG  
5708  O OD1 . ASN A  374 ? 0.2799 0.3049 0.3140 0.0016  0.0104  0.0231  400 ASN A OD1 
5709  N ND2 . ASN A  374 ? 0.2758 0.3113 0.3141 0.0042  0.0090  0.0250  400 ASN A ND2 
5716  N N   . LEU A  375 ? 0.2188 0.2268 0.2471 -0.0069 0.0182  0.0219  401 LEU A N   
5717  C CA  . LEU A  375 ? 0.2227 0.2223 0.2478 -0.0036 0.0213  0.0230  401 LEU A CA  
5718  C C   . LEU A  375 ? 0.2229 0.2229 0.2477 0.0012  0.0193  0.0226  401 LEU A C   
5719  O O   . LEU A  375 ? 0.2287 0.2221 0.2511 0.0028  0.0214  0.0225  401 LEU A O   
5720  C CB  . LEU A  375 ? 0.2274 0.2176 0.2492 -0.0079 0.0250  0.0216  401 LEU A CB  
5721  C CG  . LEU A  375 ? 0.2583 0.2465 0.2797 -0.0132 0.0277  0.0219  401 LEU A CG  
5722  C CD1 . LEU A  375 ? 0.2783 0.2584 0.2963 -0.0191 0.0304  0.0192  401 LEU A CD1 
5723  C CD2 . LEU A  375 ? 0.2650 0.2486 0.2849 -0.0100 0.0311  0.0253  401 LEU A CD2 
5735  N N   . GLY A  376 ? 0.2255 0.2331 0.2526 0.0036  0.0156  0.0227  402 GLY A N   
5736  C CA  . GLY A  376 ? 0.2282 0.2370 0.2552 0.0077  0.0136  0.0224  402 GLY A CA  
5737  C C   . GLY A  376 ? 0.2208 0.2268 0.2463 0.0128  0.0153  0.0249  402 GLY A C   
5738  O O   . GLY A  376 ? 0.2158 0.2214 0.2408 0.0140  0.0169  0.0271  402 GLY A O   
5742  N N   . ILE A  377 ? 0.2081 0.2126 0.2328 0.0157  0.0150  0.0246  403 ILE A N   
5743  C CA  . ILE A  377 ? 0.2167 0.2206 0.2406 0.0211  0.0158  0.0272  403 ILE A CA  
5744  C C   . ILE A  377 ? 0.2198 0.2171 0.2417 0.0223  0.0199  0.0298  403 ILE A C   
5745  O O   . ILE A  377 ? 0.2314 0.2300 0.2526 0.0251  0.0203  0.0325  403 ILE A O   
5746  C CB  . ILE A  377 ? 0.2286 0.2399 0.2534 0.0240  0.0126  0.0282  403 ILE A CB  
5747  C CG1 . ILE A  377 ? 0.2381 0.2549 0.2647 0.0222  0.0089  0.0256  403 ILE A CG1 
5748  C CG2 . ILE A  377 ? 0.2364 0.2489 0.2605 0.0292  0.0124  0.0302  403 ILE A CG2 
5749  C CD1 . ILE A  377 ? 0.2576 0.2805 0.2847 0.0243  0.0063  0.0261  403 ILE A CD1 
5761  N N   . ASN A  378 ? 0.2182 0.2078 0.2386 0.0199  0.0232  0.0289  404 ASN A N   
5762  C CA  . ASN A  378 ? 0.2302 0.2116 0.2482 0.0209  0.0276  0.0313  404 ASN A CA  
5763  C C   . ASN A  378 ? 0.2383 0.2129 0.2550 0.0240  0.0304  0.0317  404 ASN A C   
5764  O O   . ASN A  378 ? 0.2412 0.2076 0.2555 0.0252  0.0345  0.0338  404 ASN A O   
5765  C CB  . ASN A  378 ? 0.2337 0.2106 0.2506 0.0147  0.0299  0.0300  404 ASN A CB  
5766  C CG  . ASN A  378 ? 0.2396 0.2215 0.2576 0.0130  0.0290  0.0312  404 ASN A CG  
5767  O OD1 . ASN A  378 ? 0.2496 0.2307 0.2664 0.0159  0.0303  0.0344  404 ASN A OD1 
5768  N ND2 . ASN A  378 ? 0.2239 0.2111 0.2439 0.0085  0.0268  0.0290  404 ASN A ND2 
5775  N N   . PHE A  379 ? 0.2356 0.2132 0.2536 0.0255  0.0286  0.0299  405 PHE A N   
5776  C CA  . PHE A  379 ? 0.2448 0.2169 0.2622 0.0285  0.0314  0.0299  405 PHE A CA  
5777  C C   . PHE A  379 ? 0.2540 0.2148 0.2685 0.0248  0.0361  0.0283  405 PHE A C   
5778  O O   . PHE A  379 ? 0.2577 0.2106 0.2706 0.0279  0.0401  0.0297  405 PHE A O   
5779  C CB  . PHE A  379 ? 0.2470 0.2199 0.2648 0.0356  0.0321  0.0342  405 PHE A CB  
5780  C CG  . PHE A  379 ? 0.2487 0.2328 0.2691 0.0384  0.0274  0.0349  405 PHE A CG  
5781  C CD1 . PHE A  379 ? 0.2441 0.2329 0.2666 0.0398  0.0256  0.0333  405 PHE A CD1 
5782  C CD2 . PHE A  379 ? 0.2534 0.2431 0.2737 0.0389  0.0248  0.0367  405 PHE A CD2 
5783  C CE1 . PHE A  379 ? 0.2422 0.2409 0.2667 0.0413  0.0212  0.0334  405 PHE A CE1 
5784  C CE2 . PHE A  379 ? 0.2539 0.2531 0.2759 0.0407  0.0206  0.0367  405 PHE A CE2 
5785  C CZ  . PHE A  379 ? 0.2428 0.2463 0.2669 0.0418  0.0188  0.0350  405 PHE A CZ  
5795  N N   . ILE A  380 ? 0.2534 0.2135 0.2670 0.0181  0.0356  0.0253  406 ILE A N   
5796  C CA  . ILE A  380 ? 0.2622 0.2122 0.2725 0.0133  0.0397  0.0231  406 ILE A CA  
5797  C C   . ILE A  380 ? 0.2857 0.2323 0.2951 0.0134  0.0411  0.0201  406 ILE A C   
5798  O O   . ILE A  380 ? 0.2922 0.2457 0.3033 0.0122  0.0377  0.0179  406 ILE A O   
5799  C CB  . ILE A  380 ? 0.2501 0.2026 0.2602 0.0057  0.0382  0.0207  406 ILE A CB  
5800  C CG1 . ILE A  380 ? 0.2556 0.2114 0.2667 0.0054  0.0375  0.0235  406 ILE A CG1 
5801  C CG2 . ILE A  380 ? 0.2556 0.1978 0.2617 0.0000  0.0423  0.0177  406 ILE A CG2 
5802  C CD1 . ILE A  380 ? 0.2701 0.2338 0.2832 -0.0003 0.0342  0.0218  406 ILE A CD1 
5814  N N   . LYS A  381 ? 0.2956 0.2312 0.3022 0.0147  0.0463  0.0201  407 LYS A N   
5815  C CA  . LYS A  381 ? 0.3179 0.2490 0.3232 0.0151  0.0487  0.0172  407 LYS A CA  
5816  C C   . LYS A  381 ? 0.3459 0.2698 0.3471 0.0073  0.0510  0.0126  407 LYS A C   
5817  O O   . LYS A  381 ? 0.3475 0.2706 0.3475 0.0057  0.0515  0.0092  407 LYS A O   
5818  C CB  . LYS A  381 ? 0.3528 0.2750 0.3571 0.0216  0.0537  0.0198  407 LYS A CB  
5819  C CG  . LYS A  381 ? 0.3946 0.3237 0.4026 0.0297  0.0519  0.0245  407 LYS A CG  
5820  C CD  . LYS A  381 ? 0.4505 0.3702 0.4573 0.0359  0.0572  0.0274  407 LYS A CD  
5821  C CE  . LYS A  381 ? 0.5094 0.4367 0.5200 0.0442  0.0554  0.0321  407 LYS A CE  
5822  N NZ  . LYS A  381 ? 0.5335 0.4515 0.5431 0.0508  0.0606  0.0356  407 LYS A NZ  
5836  N N   . GLN A  382 ? 0.3593 0.2775 0.3579 0.0023  0.0528  0.0125  408 GLN A N   
5837  C CA  . GLN A  382 ? 0.3803 0.2914 0.3745 -0.0057 0.0551  0.0082  408 GLN A CA  
5838  C C   . GLN A  382 ? 0.3841 0.2978 0.3780 -0.0124 0.0535  0.0080  408 GLN A C   
5839  O O   . GLN A  382 ? 0.3777 0.2912 0.3726 -0.0109 0.0539  0.0114  408 GLN A O   
5840  C CB  . GLN A  382 ? 0.4251 0.3203 0.4145 -0.0049 0.0622  0.0076  408 GLN A CB  
5841  C CG  . GLN A  382 ? 0.4899 0.3802 0.4779 -0.0015 0.0652  0.0053  408 GLN A CG  
5846  N N   . ILE A  383 ? 0.3886 0.3044 0.3809 -0.0201 0.0519  0.0041  409 ILE A N   
5847  C CA  . ILE A  383 ? 0.3954 0.3146 0.3877 -0.0271 0.0504  0.0036  409 ILE A CA  
5848  C C   . ILE A  383 ? 0.3966 0.3080 0.3835 -0.0357 0.0532  -0.0010 409 ILE A C   
5849  O O   . ILE A  383 ? 0.3913 0.3020 0.3760 -0.0376 0.0530  -0.0044 409 ILE A O   
5850  C CB  . ILE A  383 ? 0.4019 0.3366 0.3991 -0.0280 0.0437  0.0041  409 ILE A CB  
5851  C CG1 . ILE A  383 ? 0.4170 0.3589 0.4189 -0.0200 0.0411  0.0083  409 ILE A CG1 
5852  C CG2 . ILE A  383 ? 0.4058 0.3455 0.4035 -0.0357 0.0420  0.0033  409 ILE A CG2 
5853  C CD1 . ILE A  383 ? 0.4287 0.3842 0.4351 -0.0198 0.0352  0.0092  409 ILE A CD1 
5865  N N   . ASP A  384 ? 0.4046 0.3107 0.3894 -0.0412 0.0558  -0.0011 410 ASP A N   
5866  C CA  . ASP A  384 ? 0.4277 0.3277 0.4073 -0.0507 0.0579  -0.0056 410 ASP A CA  
5867  C C   . ASP A  384 ? 0.4144 0.3294 0.3975 -0.0562 0.0518  -0.0064 410 ASP A C   
5868  O O   . ASP A  384 ? 0.4030 0.3235 0.3887 -0.0593 0.0504  -0.0046 410 ASP A O   
5869  C CB  . ASP A  384 ? 0.4854 0.3741 0.4614 -0.0548 0.0631  -0.0051 410 ASP A CB  
5870  C CG  . ASP A  384 ? 0.6171 0.4879 0.5876 -0.0518 0.0702  -0.0055 410 ASP A CG  
5871  O OD1 . ASP A  384 ? 0.6492 0.5164 0.6187 -0.0465 0.0714  -0.0065 410 ASP A OD1 
5872  O OD2 . ASP A  384 ? 0.6701 0.5304 0.6373 -0.0547 0.0748  -0.0048 410 ASP A OD2 
5877  N N   . PHE A  385 ? 0.4139 0.3361 0.3976 -0.0567 0.0480  -0.0085 411 PHE A N   
5878  C CA  . PHE A  385 ? 0.4211 0.3581 0.4086 -0.0606 0.0418  -0.0085 411 PHE A CA  
5879  C C   . PHE A  385 ? 0.4317 0.3710 0.4176 -0.0707 0.0414  -0.0107 411 PHE A C   
5880  O O   . PHE A  385 ? 0.4272 0.3794 0.4177 -0.0728 0.0367  -0.0093 411 PHE A O   
5881  C CB  . PHE A  385 ? 0.4196 0.3620 0.4068 -0.0597 0.0385  -0.0105 411 PHE A CB  
5882  C CG  . PHE A  385 ? 0.4269 0.3728 0.4177 -0.0504 0.0368  -0.0078 411 PHE A CG  
5883  C CD1 . PHE A  385 ? 0.4305 0.3885 0.4272 -0.0468 0.0317  -0.0048 411 PHE A CD1 
5884  C CD2 . PHE A  385 ? 0.4410 0.3779 0.4294 -0.0453 0.0405  -0.0084 411 PHE A CD2 
5885  C CE1 . PHE A  385 ? 0.4342 0.3951 0.4339 -0.0389 0.0302  -0.0025 411 PHE A CE1 
5886  C CE2 . PHE A  385 ? 0.4466 0.3877 0.4388 -0.0372 0.0388  -0.0059 411 PHE A CE2 
5887  C CZ  . PHE A  385 ? 0.4379 0.3908 0.4354 -0.0343 0.0336  -0.0031 411 PHE A CZ  
5897  N N   . LYS A  386 ? 0.4398 0.3668 0.4192 -0.0768 0.0464  -0.0139 412 LYS A N   
5898  C CA  . LYS A  386 ? 0.4515 0.3806 0.4291 -0.0872 0.0463  -0.0161 412 LYS A CA  
5899  C C   . LYS A  386 ? 0.4473 0.3835 0.4302 -0.0879 0.0452  -0.0125 412 LYS A C   
5900  O O   . LYS A  386 ? 0.4447 0.3886 0.4287 -0.0957 0.0431  -0.0135 412 LYS A O   
5901  C CB  . LYS A  386 ? 0.4945 0.4068 0.4638 -0.0933 0.0527  -0.0202 412 LYS A CB  
5902  C CG  . LYS A  386 ? 0.5766 0.4748 0.5440 -0.0897 0.0589  -0.0182 412 LYS A CG  
5903  C CD  . LYS A  386 ? 0.6690 0.5491 0.6274 -0.0950 0.0657  -0.0226 412 LYS A CD  
5904  C CE  . LYS A  386 ? 0.7403 0.6051 0.6964 -0.0906 0.0721  -0.0203 412 LYS A CE  
5905  N NZ  . LYS A  386 ? 0.7851 0.6312 0.7321 -0.0959 0.0791  -0.0247 412 LYS A NZ  
5919  N N   . LEU A  387 ? 0.4421 0.3764 0.4283 -0.0800 0.0466  -0.0084 413 LEU A N   
5920  C CA  . LEU A  387 ? 0.4388 0.3793 0.4295 -0.0804 0.0461  -0.0049 413 LEU A CA  
5921  C C   . LEU A  387 ? 0.4278 0.3869 0.4256 -0.0808 0.0397  -0.0032 413 LEU A C   
5922  O O   . LEU A  387 ? 0.4217 0.3875 0.4226 -0.0851 0.0392  -0.0020 413 LEU A O   
5923  C CB  . LEU A  387 ? 0.4462 0.3804 0.4380 -0.0714 0.0490  -0.0008 413 LEU A CB  
5924  C CG  . LEU A  387 ? 0.4662 0.4086 0.4630 -0.0616 0.0452  0.0022  413 LEU A CG  
5925  C CD1 . LEU A  387 ? 0.4652 0.4212 0.4685 -0.0600 0.0415  0.0056  413 LEU A CD1 
5926  C CD2 . LEU A  387 ? 0.4836 0.4156 0.4786 -0.0535 0.0490  0.0047  413 LEU A CD2 
5938  N N   . PHE A  388 ? 0.4197 0.3870 0.4200 -0.0765 0.0351  -0.0032 414 PHE A N   
5939  C CA  . PHE A  388 ? 0.4158 0.3998 0.4228 -0.0758 0.0292  -0.0012 414 PHE A CA  
5940  C C   . PHE A  388 ? 0.4364 0.4297 0.4443 -0.0851 0.0265  -0.0031 414 PHE A C   
5941  O O   . PHE A  388 ? 0.4389 0.4451 0.4529 -0.0856 0.0233  -0.0008 414 PHE A O   
5942  C CB  . PHE A  388 ? 0.3994 0.3882 0.4082 -0.0691 0.0254  -0.0007 414 PHE A CB  
5943  C CG  . PHE A  388 ? 0.3963 0.3796 0.4057 -0.0597 0.0271  0.0018  414 PHE A CG  
5944  C CD1 . PHE A  388 ? 0.4003 0.3880 0.4142 -0.0548 0.0269  0.0055  414 PHE A CD1 
5945  C CD2 . PHE A  388 ? 0.4017 0.3765 0.4074 -0.0559 0.0287  0.0004  414 PHE A CD2 
5946  C CE1 . PHE A  388 ? 0.4092 0.3924 0.4232 -0.0466 0.0282  0.0077  414 PHE A CE1 
5947  C CE2 . PHE A  388 ? 0.4072 0.3785 0.4140 -0.0475 0.0299  0.0029  414 PHE A CE2 
5948  C CZ  . PHE A  388 ? 0.4030 0.3787 0.4138 -0.0430 0.0294  0.0065  414 PHE A CZ  
5958  N N   . GLN A  389 ? 0.4515 0.4387 0.4534 -0.0927 0.0279  -0.0073 415 GLN A N   
5959  C CA  . GLN A  389 ? 0.4713 0.4676 0.4735 -0.1023 0.0253  -0.0092 415 GLN A CA  
5960  C C   . GLN A  389 ? 0.4834 0.4802 0.4869 -0.1083 0.0280  -0.0085 415 GLN A C   
5961  O O   . GLN A  389 ? 0.4777 0.4868 0.4846 -0.1148 0.0249  -0.0086 415 GLN A O   
5962  C CB  . GLN A  389 ? 0.5125 0.5021 0.5070 -0.1091 0.0260  -0.0141 415 GLN A CB  
5963  C CG  . GLN A  389 ? 0.5899 0.5633 0.5767 -0.1152 0.0324  -0.0177 415 GLN A CG  
5964  C CD  . GLN A  389 ? 0.6724 0.6364 0.6509 -0.1190 0.0340  -0.0225 415 GLN A CD  
5965  O OE1 . GLN A  389 ? 0.7079 0.6555 0.6803 -0.1181 0.0397  -0.0247 415 GLN A OE1 
5966  N NE2 . GLN A  389 ? 0.6773 0.6511 0.6552 -0.1233 0.0293  -0.0243 415 GLN A NE2 
5975  N N   . ASN A  390 ? 0.4956 0.4798 0.4968 -0.1062 0.0335  -0.0077 416 ASN A N   
5976  C CA  . ASN A  390 ? 0.5141 0.4984 0.5164 -0.1119 0.0363  -0.0067 416 ASN A CA  
5977  C C   . ASN A  390 ? 0.4910 0.4887 0.5021 -0.1071 0.0339  -0.0020 416 ASN A C   
5978  O O   . ASN A  390 ? 0.4939 0.4935 0.5068 -0.1114 0.0361  -0.0008 416 ASN A O   
5979  C CB  . ASN A  390 ? 0.5794 0.5443 0.5751 -0.1124 0.0436  -0.0076 416 ASN A CB  
5980  C CG  . ASN A  390 ? 0.7044 0.6658 0.6978 -0.1223 0.0470  -0.0089 416 ASN A CG  
5981  O OD1 . ASN A  390 ? 0.7275 0.6989 0.7220 -0.1312 0.0443  -0.0110 416 ASN A OD1 
5982  N ND2 . ASN A  390 ? 0.7728 0.7226 0.7638 -0.1218 0.0526  -0.0073 416 ASN A ND2 
5989  N N   . PHE A  391 ? 0.4653 0.4719 0.4814 -0.0985 0.0298  0.0005  417 PHE A N   
5990  C CA  . PHE A  391 ? 0.4490 0.4689 0.4731 -0.0941 0.0273  0.0045  417 PHE A CA  
5991  C C   . PHE A  391 ? 0.4390 0.4756 0.4683 -0.1003 0.0228  0.0042  417 PHE A C   
5992  O O   . PHE A  391 ? 0.4371 0.4761 0.4642 -0.1050 0.0201  0.0015  417 PHE A O   
5993  C CB  . PHE A  391 ? 0.4333 0.4562 0.4604 -0.0833 0.0245  0.0068  417 PHE A CB  
5994  C CG  . PHE A  391 ? 0.4359 0.4483 0.4611 -0.0758 0.0282  0.0089  417 PHE A CG  
5995  C CD1 . PHE A  391 ? 0.4510 0.4482 0.4696 -0.0742 0.0318  0.0074  417 PHE A CD1 
5996  C CD2 . PHE A  391 ? 0.4376 0.4559 0.4676 -0.0702 0.0282  0.0126  417 PHE A CD2 
5997  C CE1 . PHE A  391 ? 0.4623 0.4510 0.4795 -0.0670 0.0348  0.0098  417 PHE A CE1 
5998  C CE2 . PHE A  391 ? 0.4486 0.4580 0.4765 -0.0634 0.0311  0.0147  417 PHE A CE2 
5999  C CZ  . PHE A  391 ? 0.4545 0.4495 0.4762 -0.0618 0.0343  0.0134  417 PHE A CZ  
6009  N N   . SER A  392 ? 0.4329 0.4817 0.4692 -0.1001 0.0219  0.0071  418 SER A N   
6010  C CA  . SER A  392 ? 0.4297 0.4957 0.4719 -0.1057 0.0176  0.0073  418 SER A CA  
6011  C C   . SER A  392 ? 0.4119 0.4884 0.4573 -0.1017 0.0116  0.0078  418 SER A C   
6012  O O   . SER A  392 ? 0.4149 0.4982 0.4598 -0.1080 0.0084  0.0060  418 SER A O   
6013  C CB  . SER A  392 ? 0.4550 0.5323 0.5046 -0.1055 0.0182  0.0105  418 SER A CB  
6014  O OG  . SER A  392 ? 0.5036 0.5975 0.5587 -0.1120 0.0145  0.0105  418 SER A OG  
6020  N N   . ASN A  393 ? 0.3927 0.4707 0.4411 -0.0916 0.0100  0.0103  419 ASN A N   
6021  C CA  . ASN A  393 ? 0.3750 0.4619 0.4262 -0.0874 0.0046  0.0111  419 ASN A CA  
6022  C C   . ASN A  393 ? 0.3421 0.4232 0.3928 -0.0769 0.0043  0.0126  419 ASN A C   
6023  O O   . ASN A  393 ? 0.3327 0.4224 0.3891 -0.0705 0.0020  0.0154  419 ASN A O   
6024  C CB  . ASN A  393 ? 0.3988 0.5046 0.4588 -0.0880 0.0009  0.0138  419 ASN A CB  
6025  C CG  . ASN A  393 ? 0.4611 0.5766 0.5241 -0.0843 -0.0048 0.0150  419 ASN A CG  
6026  O OD1 . ASN A  393 ? 0.4803 0.5906 0.5382 -0.0849 -0.0067 0.0132  419 ASN A OD1 
6027  N ND2 . ASN A  393 ? 0.4695 0.5993 0.5409 -0.0803 -0.0075 0.0183  419 ASN A ND2 
6034  N N   . LEU A  394 ? 0.3279 0.3945 0.3718 -0.0753 0.0067  0.0106  420 LEU A N   
6035  C CA  . LEU A  394 ? 0.3139 0.3757 0.3571 -0.0662 0.0062  0.0117  420 LEU A CA  
6036  C C   . LEU A  394 ? 0.2899 0.3590 0.3345 -0.0641 0.0010  0.0118  420 LEU A C   
6037  O O   . LEU A  394 ? 0.2915 0.3617 0.3334 -0.0697 -0.0009 0.0097  420 LEU A O   
6038  C CB  . LEU A  394 ? 0.3237 0.3693 0.3597 -0.0649 0.0100  0.0097  420 LEU A CB  
6039  C CG  . LEU A  394 ? 0.3407 0.3771 0.3752 -0.0625 0.0150  0.0108  420 LEU A CG  
6040  C CD1 . LEU A  394 ? 0.3560 0.3771 0.3836 -0.0619 0.0187  0.0087  420 LEU A CD1 
6041  C CD2 . LEU A  394 ? 0.3418 0.3825 0.3807 -0.0540 0.0144  0.0141  420 LEU A CD2 
6053  N N   . GLU A  395 ? 0.2686 0.3426 0.3172 -0.0564 -0.0013 0.0142  421 GLU A N   
6054  C CA  . GLU A  395 ? 0.2609 0.3404 0.3106 -0.0534 -0.0059 0.0149  421 GLU A CA  
6055  C C   . GLU A  395 ? 0.2452 0.3162 0.2919 -0.0465 -0.0055 0.0147  421 GLU A C   
6056  O O   . GLU A  395 ? 0.2376 0.3089 0.2827 -0.0453 -0.0084 0.0143  421 GLU A O   
6057  C CB  . GLU A  395 ? 0.3029 0.3964 0.3603 -0.0504 -0.0091 0.0180  421 GLU A CB  
6058  C CG  . GLU A  395 ? 0.4152 0.5198 0.4768 -0.0569 -0.0100 0.0185  421 GLU A CG  
6059  C CD  . GLU A  395 ? 0.5776 0.6961 0.6475 -0.0530 -0.0124 0.0218  421 GLU A CD  
6060  O OE1 . GLU A  395 ? 0.6216 0.7433 0.6935 -0.0470 -0.0153 0.0235  421 GLU A OE1 
6061  O OE2 . GLU A  395 ? 0.6225 0.7485 0.6969 -0.0560 -0.0111 0.0228  421 GLU A OE2 
6068  N N   . ILE A  396 ? 0.2349 0.2990 0.2810 -0.0419 -0.0022 0.0153  422 ILE A N   
6069  C CA  . ILE A  396 ? 0.2322 0.2892 0.2757 -0.0356 -0.0017 0.0153  422 ILE A CA  
6070  C C   . ILE A  396 ? 0.2312 0.2767 0.2705 -0.0354 0.0029  0.0143  422 ILE A C   
6071  O O   . ILE A  396 ? 0.2363 0.2807 0.2768 -0.0343 0.0056  0.0157  422 ILE A O   
6072  C CB  . ILE A  396 ? 0.2367 0.2991 0.2847 -0.0286 -0.0031 0.0179  422 ILE A CB  
6073  C CG1 . ILE A  396 ? 0.2462 0.3185 0.2979 -0.0277 -0.0076 0.0191  422 ILE A CG1 
6074  C CG2 . ILE A  396 ? 0.2397 0.2944 0.2848 -0.0225 -0.0022 0.0178  422 ILE A CG2 
6075  C CD1 . ILE A  396 ? 0.2634 0.3418 0.3200 -0.0215 -0.0085 0.0215  422 ILE A CD1 
6087  N N   . ILE A  397 ? 0.2205 0.2576 0.2548 -0.0363 0.0040  0.0122  423 ILE A N   
6088  C CA  . ILE A  397 ? 0.2209 0.2467 0.2511 -0.0353 0.0084  0.0114  423 ILE A CA  
6089  C C   . ILE A  397 ? 0.2262 0.2493 0.2557 -0.0286 0.0076  0.0119  423 ILE A C   
6090  O O   . ILE A  397 ? 0.2217 0.2432 0.2490 -0.0287 0.0062  0.0104  423 ILE A O   
6091  C CB  . ILE A  397 ? 0.2401 0.2582 0.2652 -0.0417 0.0107  0.0083  423 ILE A CB  
6092  C CG1 . ILE A  397 ? 0.2470 0.2693 0.2727 -0.0496 0.0108  0.0074  423 ILE A CG1 
6093  C CG2 . ILE A  397 ? 0.2536 0.2592 0.2746 -0.0395 0.0157  0.0079  423 ILE A CG2 
6094  C CD1 . ILE A  397 ? 0.2723 0.2895 0.2927 -0.0568 0.0117  0.0038  423 ILE A CD1 
6106  N N   . TYR A  398 ? 0.2202 0.2438 0.2516 -0.0229 0.0082  0.0142  424 TYR A N   
6107  C CA  . TYR A  398 ? 0.2219 0.2443 0.2530 -0.0168 0.0071  0.0148  424 TYR A CA  
6108  C C   . TYR A  398 ? 0.2158 0.2292 0.2438 -0.0139 0.0108  0.0150  424 TYR A C   
6109  O O   . TYR A  398 ? 0.2088 0.2198 0.2369 -0.0121 0.0133  0.0168  424 TYR A O   
6110  C CB  . TYR A  398 ? 0.2263 0.2561 0.2613 -0.0124 0.0049  0.0170  424 TYR A CB  
6111  C CG  . TYR A  398 ? 0.2452 0.2749 0.2799 -0.0070 0.0032  0.0173  424 TYR A CG  
6112  C CD1 . TYR A  398 ? 0.2582 0.2916 0.2935 -0.0066 -0.0003 0.0166  424 TYR A CD1 
6113  C CD2 . TYR A  398 ? 0.2608 0.2872 0.2944 -0.0023 0.0049  0.0186  424 TYR A CD2 
6114  C CE1 . TYR A  398 ? 0.2732 0.3065 0.3081 -0.0021 -0.0018 0.0169  424 TYR A CE1 
6115  C CE2 . TYR A  398 ? 0.2738 0.3011 0.3073 0.0021  0.0032  0.0188  424 TYR A CE2 
6116  C CZ  . TYR A  398 ? 0.2930 0.3237 0.3271 0.0021  -0.0002 0.0179  424 TYR A CZ  
6117  O OH  . TYR A  398 ? 0.3421 0.3732 0.3757 0.0058  -0.0017 0.0179  424 TYR A OH  
6127  N N   . LEU A  399 ? 0.2099 0.2183 0.2351 -0.0136 0.0113  0.0133  425 LEU A N   
6128  C CA  . LEU A  399 ? 0.2222 0.2223 0.2448 -0.0106 0.0148  0.0135  425 LEU A CA  
6129  C C   . LEU A  399 ? 0.2335 0.2347 0.2563 -0.0056 0.0132  0.0136  425 LEU A C   
6130  O O   . LEU A  399 ? 0.2493 0.2447 0.2701 -0.0036 0.0157  0.0132  425 LEU A O   
6131  C CB  . LEU A  399 ? 0.2268 0.2190 0.2456 -0.0154 0.0179  0.0109  425 LEU A CB  
6132  C CG  . LEU A  399 ? 0.2620 0.2528 0.2799 -0.0217 0.0195  0.0101  425 LEU A CG  
6133  C CD1 . LEU A  399 ? 0.2700 0.2536 0.2835 -0.0271 0.0220  0.0068  425 LEU A CD1 
6134  C CD2 . LEU A  399 ? 0.2823 0.2696 0.3005 -0.0201 0.0227  0.0126  425 LEU A CD2 
6146  N N   . SER A  400 ? 0.2153 0.2239 0.2406 -0.0036 0.0093  0.0142  426 SER A N   
6147  C CA  . SER A  400 ? 0.2149 0.2252 0.2404 0.0001  0.0075  0.0142  426 SER A CA  
6148  C C   . SER A  400 ? 0.2260 0.2341 0.2514 0.0054  0.0093  0.0161  426 SER A C   
6149  O O   . SER A  400 ? 0.2269 0.2347 0.2527 0.0071  0.0106  0.0181  426 SER A O   
6150  C CB  . SER A  400 ? 0.2103 0.2281 0.2382 0.0011  0.0034  0.0147  426 SER A CB  
6151  O OG  . SER A  400 ? 0.2132 0.2326 0.2411 0.0041  0.0016  0.0145  426 SER A OG  
6157  N N   . GLU A  401 ? 0.2195 0.2263 0.2442 0.0079  0.0096  0.0156  427 GLU A N   
6158  C CA  . GLU A  401 ? 0.2238 0.2302 0.2489 0.0132  0.0107  0.0176  427 GLU A CA  
6159  C C   . GLU A  401 ? 0.2374 0.2371 0.2610 0.0146  0.0149  0.0191  427 GLU A C   
6160  O O   . GLU A  401 ? 0.2460 0.2458 0.2698 0.0172  0.0157  0.0216  427 GLU A O   
6161  C CB  . GLU A  401 ? 0.2467 0.2592 0.2733 0.0160  0.0079  0.0193  427 GLU A CB  
6162  C CG  . GLU A  401 ? 0.2822 0.2967 0.3091 0.0210  0.0076  0.0209  427 GLU A CG  
6163  C CD  . GLU A  401 ? 0.3185 0.3350 0.3459 0.0213  0.0062  0.0194  427 GLU A CD  
6164  O OE1 . GLU A  401 ? 0.3641 0.3775 0.3912 0.0226  0.0086  0.0193  427 GLU A OE1 
6165  O OE2 . GLU A  401 ? 0.3182 0.3391 0.3462 0.0203  0.0030  0.0183  427 GLU A OE2 
6172  N N   . ASN A  402 ? 0.2312 0.2246 0.2531 0.0129  0.0179  0.0176  428 ASN A N   
6173  C CA  . ASN A  402 ? 0.2417 0.2268 0.2616 0.0144  0.0225  0.0188  428 ASN A CA  
6174  C C   . ASN A  402 ? 0.2617 0.2432 0.2810 0.0167  0.0247  0.0178  428 ASN A C   
6175  O O   . ASN A  402 ? 0.2632 0.2503 0.2842 0.0184  0.0223  0.0173  428 ASN A O   
6176  C CB  . ASN A  402 ? 0.2395 0.2193 0.2574 0.0087  0.0246  0.0176  428 ASN A CB  
6177  C CG  . ASN A  402 ? 0.2286 0.2110 0.2475 0.0084  0.0240  0.0198  428 ASN A CG  
6178  O OD1 . ASN A  402 ? 0.2196 0.1999 0.2381 0.0123  0.0257  0.0228  428 ASN A OD1 
6179  N ND2 . ASN A  402 ? 0.2186 0.2063 0.2388 0.0043  0.0214  0.0187  428 ASN A ND2 
6186  N N   . ARG A  403 ? 0.2744 0.2466 0.2913 0.0169  0.0295  0.0177  429 ARG A N   
6187  C CA  . ARG A  403 ? 0.2890 0.2570 0.3054 0.0193  0.0325  0.0166  429 ARG A CA  
6188  C C   . ARG A  403 ? 0.2881 0.2474 0.3007 0.0139  0.0359  0.0130  429 ARG A C   
6189  O O   . ARG A  403 ? 0.2832 0.2341 0.2938 0.0156  0.0406  0.0125  429 ARG A O   
6190  C CB  . ARG A  403 ? 0.3081 0.2717 0.3248 0.0257  0.0358  0.0201  429 ARG A CB  
6191  C CG  . ARG A  403 ? 0.3777 0.3493 0.3972 0.0307  0.0327  0.0238  429 ARG A CG  
6192  C CD  . ARG A  403 ? 0.4499 0.4307 0.4725 0.0334  0.0295  0.0236  429 ARG A CD  
6193  N NE  . ARG A  403 ? 0.5117 0.4902 0.5352 0.0377  0.0326  0.0240  429 ARG A NE  
6194  C CZ  . ARG A  403 ? 0.5380 0.5245 0.5647 0.0410  0.0307  0.0245  429 ARG A CZ  
6195  N NH1 . ARG A  403 ? 0.5344 0.5191 0.5624 0.0452  0.0339  0.0250  429 ARG A NH1 
6196  N NH2 . ARG A  403 ? 0.5297 0.5259 0.5583 0.0404  0.0257  0.0245  429 ARG A NH2 
6210  N N   . ILE A  404 ? 0.2866 0.2479 0.2981 0.0074  0.0336  0.0105  430 ILE A N   
6211  C CA  . ILE A  404 ? 0.3047 0.2587 0.3122 0.0014  0.0364  0.0070  430 ILE A CA  
6212  C C   . ILE A  404 ? 0.3239 0.2771 0.3302 0.0015  0.0374  0.0042  430 ILE A C   
6213  O O   . ILE A  404 ? 0.3178 0.2791 0.3263 0.0023  0.0338  0.0040  430 ILE A O   
6214  C CB  . ILE A  404 ? 0.3123 0.2705 0.3194 -0.0053 0.0332  0.0057  430 ILE A CB  
6215  C CG1 . ILE A  404 ? 0.3241 0.2823 0.3323 -0.0053 0.0333  0.0084  430 ILE A CG1 
6216  C CG2 . ILE A  404 ? 0.3204 0.2723 0.3230 -0.0122 0.0355  0.0016  430 ILE A CG2 
6217  C CD1 . ILE A  404 ? 0.3319 0.2988 0.3421 -0.0095 0.0289  0.0084  430 ILE A CD1 
6229  N N   . SER A  405 ? 0.3417 0.2847 0.3445 0.0012  0.0427  0.0024  431 SER A N   
6230  C CA  . SER A  405 ? 0.3718 0.3130 0.3732 0.0017  0.0447  -0.0003 431 SER A CA  
6231  C C   . SER A  405 ? 0.3981 0.3322 0.3939 -0.0058 0.0472  -0.0049 431 SER A C   
6232  O O   . SER A  405 ? 0.4039 0.3347 0.3973 -0.0109 0.0472  -0.0056 431 SER A O   
6233  C CB  . SER A  405 ? 0.3925 0.3283 0.3950 0.0090  0.0493  0.0016  431 SER A CB  
6234  O OG  . SER A  405 ? 0.4361 0.3593 0.4348 0.0083  0.0547  0.0013  431 SER A OG  
6240  N N   . PRO A  406 ? 0.4182 0.3507 0.4116 -0.0070 0.0489  -0.0082 432 PRO A N   
6241  C CA  . PRO A  406 ? 0.4477 0.3734 0.4348 -0.0146 0.0512  -0.0128 432 PRO A CA  
6242  C C   . PRO A  406 ? 0.4906 0.4033 0.4733 -0.0170 0.0565  -0.0140 432 PRO A C   
6243  O O   . PRO A  406 ? 0.4973 0.4020 0.4803 -0.0117 0.0612  -0.0124 432 PRO A O   
6244  C CB  . PRO A  406 ? 0.4494 0.3741 0.4349 -0.0132 0.0537  -0.0155 432 PRO A CB  
6245  C CG  . PRO A  406 ? 0.4366 0.3725 0.4282 -0.0075 0.0498  -0.0124 432 PRO A CG  
6246  C CD  . PRO A  406 ? 0.4089 0.3457 0.4048 -0.0019 0.0492  -0.0080 432 PRO A CD  
6254  N N   . LEU A  407 ? 0.5152 0.4262 0.4942 -0.0252 0.0556  -0.0164 433 LEU A N   
6255  C CA  . LEU A  407 ? 0.5519 0.4511 0.5263 -0.0292 0.0601  -0.0178 433 LEU A CA  
6256  C C   . LEU A  407 ? 0.5774 0.4626 0.5460 -0.0291 0.0673  -0.0213 433 LEU A C   
6257  O O   . LEU A  407 ? 0.5876 0.4732 0.5539 -0.0300 0.0681  -0.0245 433 LEU A O   
6258  C CB  . LEU A  407 ? 0.5634 0.4659 0.5351 -0.0389 0.0570  -0.0201 433 LEU A CB  
6259  C CG  . LEU A  407 ? 0.6008 0.4947 0.5693 -0.0440 0.0600  -0.0206 433 LEU A CG  
6260  C CD1 . LEU A  407 ? 0.6078 0.5109 0.5772 -0.0514 0.0549  -0.0209 433 LEU A CD1 
6261  C CD2 . LEU A  407 ? 0.6231 0.5019 0.5838 -0.0483 0.0667  -0.0253 433 LEU A CD2 
6273  N N   . PHE A  433 ? 0.5027 0.5263 0.4758 0.0314  -0.0102 -0.0076 459 PHE A N   
6274  C CA  . PHE A  433 ? 0.4963 0.5262 0.4732 0.0336  -0.0095 -0.0040 459 PHE A CA  
6275  C C   . PHE A  433 ? 0.4748 0.5071 0.4589 0.0336  -0.0109 -0.0009 459 PHE A C   
6276  O O   . PHE A  433 ? 0.4852 0.5139 0.4723 0.0331  -0.0114 -0.0011 459 PHE A O   
6277  C CB  . PHE A  433 ? 0.5013 0.5303 0.4784 0.0370  -0.0060 -0.0037 459 PHE A CB  
6278  C CG  . PHE A  433 ? 0.5143 0.5374 0.4930 0.0389  -0.0041 -0.0051 459 PHE A CG  
6279  C CD1 . PHE A  433 ? 0.5253 0.5490 0.5112 0.0405  -0.0039 -0.0026 459 PHE A CD1 
6280  C CD2 . PHE A  433 ? 0.5287 0.5461 0.5018 0.0394  -0.0023 -0.0086 459 PHE A CD2 
6281  C CE1 . PHE A  433 ? 0.5359 0.5551 0.5237 0.0428  -0.0022 -0.0033 459 PHE A CE1 
6282  C CE2 . PHE A  433 ? 0.5401 0.5522 0.5151 0.0420  -0.0002 -0.0095 459 PHE A CE2 
6283  C CZ  . PHE A  433 ? 0.5359 0.5493 0.5185 0.0439  -0.0003 -0.0066 459 PHE A CZ  
6292  N N   . GLU A  434 ? 0.4439 0.4818 0.4305 0.0341  -0.0112 0.0021  460 GLU A N   
6293  C CA  . GLU A  434 ? 0.4156 0.4556 0.4082 0.0339  -0.0121 0.0049  460 GLU A CA  
6294  C C   . GLU A  434 ? 0.3865 0.4261 0.3842 0.0359  -0.0101 0.0069  460 GLU A C   
6295  O O   . GLU A  434 ? 0.3805 0.4197 0.3827 0.0351  -0.0109 0.0081  460 GLU A O   
6296  C CB  . GLU A  434 ? 0.4209 0.4665 0.4134 0.0340  -0.0129 0.0073  460 GLU A CB  
6297  C CG  . GLU A  434 ? 0.4522 0.4995 0.4501 0.0340  -0.0133 0.0101  460 GLU A CG  
6298  C CD  . GLU A  434 ? 0.4824 0.5344 0.4803 0.0350  -0.0135 0.0129  460 GLU A CD  
6299  O OE1 . GLU A  434 ? 0.4989 0.5514 0.5009 0.0354  -0.0130 0.0152  460 GLU A OE1 
6300  O OE2 . GLU A  434 ? 0.4622 0.5171 0.4557 0.0353  -0.0139 0.0128  460 GLU A OE2 
6307  N N   . PHE A  435 ? 0.3612 0.4016 0.3581 0.0380  -0.0076 0.0075  461 PHE A N   
6308  C CA  . PHE A  435 ? 0.3402 0.3816 0.3421 0.0395  -0.0056 0.0096  461 PHE A CA  
6309  C C   . PHE A  435 ? 0.3313 0.3701 0.3342 0.0411  -0.0041 0.0081  461 PHE A C   
6310  O O   . PHE A  435 ? 0.3373 0.3743 0.3358 0.0423  -0.0027 0.0061  461 PHE A O   
6311  C CB  . PHE A  435 ? 0.3312 0.3761 0.3322 0.0407  -0.0036 0.0118  461 PHE A CB  
6312  C CG  . PHE A  435 ? 0.3263 0.3735 0.3268 0.0398  -0.0048 0.0139  461 PHE A CG  
6313  C CD1 . PHE A  435 ? 0.3320 0.3798 0.3372 0.0392  -0.0050 0.0162  461 PHE A CD1 
6314  C CD2 . PHE A  435 ? 0.3350 0.3840 0.3305 0.0397  -0.0059 0.0136  461 PHE A CD2 
6315  C CE1 . PHE A  435 ? 0.3386 0.3880 0.3434 0.0389  -0.0058 0.0181  461 PHE A CE1 
6316  C CE2 . PHE A  435 ? 0.3425 0.3942 0.3380 0.0395  -0.0071 0.0159  461 PHE A CE2 
6317  C CZ  . PHE A  435 ? 0.3347 0.3862 0.3350 0.0394  -0.0069 0.0182  461 PHE A CZ  
6327  N N   . ASP A  436 ? 0.3106 0.3492 0.3189 0.0413  -0.0042 0.0092  462 ASP A N   
6328  C CA  . ASP A  436 ? 0.3014 0.3384 0.3117 0.0433  -0.0028 0.0085  462 ASP A CA  
6329  C C   . ASP A  436 ? 0.2931 0.3335 0.3042 0.0456  0.0004  0.0094  462 ASP A C   
6330  O O   . ASP A  436 ? 0.2852 0.3298 0.3002 0.0452  0.0012  0.0119  462 ASP A O   
6331  C CB  . ASP A  436 ? 0.3161 0.3537 0.3323 0.0427  -0.0042 0.0101  462 ASP A CB  
6332  C CG  . ASP A  436 ? 0.3688 0.4058 0.3881 0.0452  -0.0031 0.0102  462 ASP A CG  
6333  O OD1 . ASP A  436 ? 0.3533 0.3889 0.3704 0.0478  -0.0008 0.0088  462 ASP A OD1 
6334  O OD2 . ASP A  436 ? 0.4114 0.4496 0.4353 0.0447  -0.0044 0.0117  462 ASP A OD2 
6339  N N   . PRO A  437 ? 0.2918 0.3303 0.2993 0.0478  0.0026  0.0074  463 PRO A N   
6340  C CA  . PRO A  437 ? 0.2931 0.3353 0.3013 0.0499  0.0060  0.0082  463 PRO A CA  
6341  C C   . PRO A  437 ? 0.2795 0.3256 0.2950 0.0515  0.0075  0.0102  463 PRO A C   
6342  O O   . PRO A  437 ? 0.2738 0.3242 0.2909 0.0526  0.0103  0.0115  463 PRO A O   
6343  C CB  . PRO A  437 ? 0.3106 0.3490 0.3125 0.0517  0.0080  0.0050  463 PRO A CB  
6344  C CG  . PRO A  437 ? 0.3202 0.3525 0.3198 0.0510  0.0059  0.0026  463 PRO A CG  
6345  C CD  . PRO A  437 ? 0.2931 0.3257 0.2952 0.0481  0.0023  0.0041  463 PRO A CD  
6353  N N   . HIS A  438 ? 0.2752 0.3203 0.2952 0.0516  0.0057  0.0107  464 HIS A N   
6354  C CA  . HIS A  438 ? 0.2797 0.3296 0.3070 0.0529  0.0065  0.0128  464 HIS A CA  
6355  C C   . HIS A  438 ? 0.2900 0.3439 0.3220 0.0498  0.0047  0.0154  464 HIS A C   
6356  O O   . HIS A  438 ? 0.2897 0.3480 0.3279 0.0501  0.0047  0.0172  464 HIS A O   
6357  C CB  . HIS A  438 ? 0.2956 0.3422 0.3246 0.0553  0.0058  0.0120  464 HIS A CB  
6358  C CG  . HIS A  438 ? 0.3354 0.3771 0.3597 0.0584  0.0082  0.0093  464 HIS A CG  
6359  N ND1 . HIS A  438 ? 0.3599 0.4046 0.3858 0.0619  0.0120  0.0092  464 HIS A ND1 
6360  C CD2 . HIS A  438 ? 0.3571 0.3911 0.3747 0.0581  0.0076  0.0064  464 HIS A CD2 
6361  C CE1 . HIS A  438 ? 0.3721 0.4103 0.3921 0.0639  0.0136  0.0061  464 HIS A CE1 
6362  N NE2 . HIS A  438 ? 0.3745 0.4060 0.3893 0.0615  0.0110  0.0043  464 HIS A NE2 
6370  N N   . SER A  439 ? 0.2976 0.3501 0.3267 0.0469  0.0033  0.0156  465 SER A N   
6371  C CA  . SER A  439 ? 0.3098 0.3647 0.3424 0.0438  0.0019  0.0176  465 SER A CA  
6372  C C   . SER A  439 ? 0.2950 0.3523 0.3265 0.0428  0.0040  0.0191  465 SER A C   
6373  O O   . SER A  439 ? 0.2907 0.3476 0.3182 0.0442  0.0059  0.0185  465 SER A O   
6374  C CB  . SER A  439 ? 0.3621 0.4129 0.3922 0.0416  -0.0011 0.0169  465 SER A CB  
6375  O OG  . SER A  439 ? 0.4367 0.4850 0.4677 0.0419  -0.0032 0.0160  465 SER A OG  
6381  N N   . ASN A  440 ? 0.2859 0.3450 0.3206 0.0401  0.0037  0.0209  466 ASN A N   
6382  C CA  . ASN A  440 ? 0.2798 0.3399 0.3134 0.0387  0.0057  0.0226  466 ASN A CA  
6383  C C   . ASN A  440 ? 0.2838 0.3397 0.3121 0.0385  0.0044  0.0221  466 ASN A C   
6384  O O   . ASN A  440 ? 0.2870 0.3403 0.3150 0.0373  0.0020  0.0214  466 ASN A O   
6385  C CB  . ASN A  440 ? 0.2792 0.3413 0.3174 0.0355  0.0057  0.0242  466 ASN A CB  
6386  C CG  . ASN A  440 ? 0.2712 0.3342 0.3090 0.0341  0.0085  0.0262  466 ASN A CG  
6387  O OD1 . ASN A  440 ? 0.2612 0.3209 0.2951 0.0338  0.0089  0.0269  466 ASN A OD1 
6388  N ND2 . ASN A  440 ? 0.2729 0.3409 0.3150 0.0331  0.0104  0.0273  466 ASN A ND2 
6395  N N   . PHE A  441 ? 0.2732 0.3290 0.2974 0.0396  0.0062  0.0227  467 PHE A N   
6396  C CA  . PHE A  441 ? 0.2717 0.3249 0.2909 0.0398  0.0050  0.0227  467 PHE A CA  
6397  C C   . PHE A  441 ? 0.2753 0.3272 0.2953 0.0381  0.0049  0.0249  467 PHE A C   
6398  O O   . PHE A  441 ? 0.2873 0.3373 0.3051 0.0380  0.0031  0.0247  467 PHE A O   
6399  C CB  . PHE A  441 ? 0.2680 0.3221 0.2822 0.0417  0.0069  0.0230  467 PHE A CB  
6400  C CG  . PHE A  441 ? 0.2741 0.3271 0.2829 0.0421  0.0055  0.0232  467 PHE A CG  
6401  C CD1 . PHE A  441 ? 0.2809 0.3326 0.2868 0.0424  0.0031  0.0207  467 PHE A CD1 
6402  C CD2 . PHE A  441 ? 0.2842 0.3376 0.2906 0.0424  0.0069  0.0259  467 PHE A CD2 
6403  C CE1 . PHE A  441 ? 0.2937 0.3458 0.2948 0.0426  0.0016  0.0209  467 PHE A CE1 
6404  C CE2 . PHE A  441 ? 0.2980 0.3515 0.2996 0.0432  0.0054  0.0265  467 PHE A CE2 
6405  C CZ  . PHE A  441 ? 0.2947 0.3481 0.2940 0.0432  0.0026  0.0239  467 PHE A CZ  
6415  N N   . TYR A  442 ? 0.2667 0.3193 0.2896 0.0366  0.0071  0.0268  468 TYR A N   
6416  C CA  . TYR A  442 ? 0.2673 0.3173 0.2901 0.0351  0.0078  0.0288  468 TYR A CA  
6417  C C   . TYR A  442 ? 0.2809 0.3292 0.3072 0.0325  0.0065  0.0282  468 TYR A C   
6418  O O   . TYR A  442 ? 0.2858 0.3309 0.3113 0.0317  0.0067  0.0293  468 TYR A O   
6419  C CB  . TYR A  442 ? 0.2533 0.3039 0.2760 0.0345  0.0112  0.0313  468 TYR A CB  
6420  C CG  . TYR A  442 ? 0.2507 0.3021 0.2685 0.0370  0.0125  0.0323  468 TYR A CG  
6421  C CD1 . TYR A  442 ? 0.2556 0.3049 0.2691 0.0385  0.0118  0.0336  468 TYR A CD1 
6422  C CD2 . TYR A  442 ? 0.2588 0.3136 0.2761 0.0381  0.0140  0.0316  468 TYR A CD2 
6423  C CE1 . TYR A  442 ? 0.2702 0.3209 0.2786 0.0406  0.0125  0.0344  468 TYR A CE1 
6424  C CE2 . TYR A  442 ? 0.2698 0.3254 0.2819 0.0402  0.0151  0.0321  468 TYR A CE2 
6425  C CZ  . TYR A  442 ? 0.2830 0.3366 0.2904 0.0413  0.0143  0.0337  468 TYR A CZ  
6426  O OH  . TYR A  442 ? 0.3107 0.3656 0.3124 0.0431  0.0150  0.0342  468 TYR A OH  
6436  N N   . HIS A  443 ? 0.2856 0.3358 0.3155 0.0313  0.0051  0.0267  469 HIS A N   
6437  C CA  . HIS A  443 ? 0.2897 0.3385 0.3221 0.0287  0.0035  0.0260  469 HIS A CA  
6438  C C   . HIS A  443 ? 0.2947 0.3454 0.3293 0.0287  0.0010  0.0242  469 HIS A C   
6439  O O   . HIS A  443 ? 0.2843 0.3377 0.3197 0.0305  0.0012  0.0238  469 HIS A O   
6440  C CB  . HIS A  443 ? 0.2951 0.3441 0.3302 0.0254  0.0055  0.0272  469 HIS A CB  
6441  C CG  . HIS A  443 ? 0.3134 0.3674 0.3519 0.0249  0.0068  0.0277  469 HIS A CG  
6442  N ND1 . HIS A  443 ? 0.3309 0.3863 0.3690 0.0251  0.0098  0.0293  469 HIS A ND1 
6443  C CD2 . HIS A  443 ? 0.3238 0.3822 0.3663 0.0242  0.0054  0.0269  469 HIS A CD2 
6444  C CE1 . HIS A  443 ? 0.3362 0.3972 0.3784 0.0246  0.0103  0.0293  469 HIS A CE1 
6445  N NE2 . HIS A  443 ? 0.3367 0.3999 0.3819 0.0242  0.0076  0.0280  469 HIS A NE2 
6453  N N   . PHE A  444 ? 0.3016 0.3506 0.3369 0.0269  -0.0010 0.0233  470 PHE A N   
6454  C CA  . PHE A  444 ? 0.3134 0.3636 0.3506 0.0267  -0.0035 0.0221  470 PHE A CA  
6455  C C   . PHE A  444 ? 0.2976 0.3521 0.3392 0.0253  -0.0030 0.0229  470 PHE A C   
6456  O O   . PHE A  444 ? 0.2919 0.3475 0.3351 0.0229  -0.0014 0.0239  470 PHE A O   
6457  C CB  . PHE A  444 ? 0.3347 0.3821 0.3712 0.0246  -0.0055 0.0212  470 PHE A CB  
6458  C CG  . PHE A  444 ? 0.3728 0.4172 0.4060 0.0256  -0.0060 0.0205  470 PHE A CG  
6459  C CD1 . PHE A  444 ? 0.3996 0.4438 0.4302 0.0280  -0.0069 0.0197  470 PHE A CD1 
6460  C CD2 . PHE A  444 ? 0.3947 0.4366 0.4271 0.0239  -0.0057 0.0206  470 PHE A CD2 
6461  C CE1 . PHE A  444 ? 0.4166 0.4593 0.4445 0.0285  -0.0077 0.0191  470 PHE A CE1 
6462  C CE2 . PHE A  444 ? 0.4110 0.4513 0.4410 0.0251  -0.0063 0.0202  470 PHE A CE2 
6463  C CZ  . PHE A  444 ? 0.4137 0.4550 0.4417 0.0272  -0.0075 0.0195  470 PHE A CZ  
6473  N N   . THR A  445 ? 0.2987 0.3558 0.3423 0.0269  -0.0043 0.0225  471 THR A N   
6474  C CA  . THR A  445 ? 0.3149 0.3776 0.3635 0.0261  -0.0042 0.0236  471 THR A CA  
6475  C C   . THR A  445 ? 0.3168 0.3808 0.3676 0.0238  -0.0069 0.0236  471 THR A C   
6476  O O   . THR A  445 ? 0.3136 0.3833 0.3688 0.0228  -0.0073 0.0247  471 THR A O   
6477  C CB  . THR A  445 ? 0.3408 0.4066 0.3909 0.0300  -0.0031 0.0237  471 THR A CB  
6478  O OG1 . THR A  445 ? 0.3688 0.4309 0.4163 0.0324  -0.0048 0.0224  471 THR A OG1 
6479  C CG2 . THR A  445 ? 0.3450 0.4107 0.3930 0.0315  -0.0001 0.0239  471 THR A CG2 
6487  N N   . ARG A  446 ? 0.3213 0.3808 0.3692 0.0228  -0.0089 0.0225  472 ARG A N   
6488  C CA  . ARG A  446 ? 0.3316 0.3920 0.3808 0.0204  -0.0115 0.0226  472 ARG A CA  
6489  C C   . ARG A  446 ? 0.3190 0.3818 0.3699 0.0159  -0.0110 0.0231  472 ARG A C   
6490  O O   . ARG A  446 ? 0.3079 0.3687 0.3575 0.0145  -0.0088 0.0229  472 ARG A O   
6491  C CB  . ARG A  446 ? 0.3644 0.4194 0.4097 0.0201  -0.0132 0.0213  472 ARG A CB  
6492  C CG  . ARG A  446 ? 0.4280 0.4791 0.4703 0.0181  -0.0121 0.0204  472 ARG A CG  
6493  C CD  . ARG A  446 ? 0.4877 0.5353 0.5274 0.0169  -0.0139 0.0193  472 ARG A CD  
6494  N NE  . ARG A  446 ? 0.5429 0.5870 0.5801 0.0158  -0.0126 0.0185  472 ARG A NE  
6495  C CZ  . ARG A  446 ? 0.5764 0.6196 0.6136 0.0128  -0.0115 0.0183  472 ARG A CZ  
6496  N NH1 . ARG A  446 ? 0.5650 0.6107 0.6043 0.0100  -0.0116 0.0188  472 ARG A NH1 
6497  N NH2 . ARG A  446 ? 0.5805 0.6203 0.6157 0.0127  -0.0101 0.0177  472 ARG A NH2 
6511  N N   . PRO A  447 ? 0.3148 0.3812 0.3679 0.0133  -0.0131 0.0236  473 PRO A N   
6512  C CA  . PRO A  447 ? 0.2992 0.3675 0.3531 0.0083  -0.0126 0.0236  473 PRO A CA  
6513  C C   . PRO A  447 ? 0.2855 0.3470 0.3351 0.0058  -0.0115 0.0220  473 PRO A C   
6514  O O   . PRO A  447 ? 0.2848 0.3417 0.3313 0.0072  -0.0124 0.0211  473 PRO A O   
6515  C CB  . PRO A  447 ? 0.3116 0.3847 0.3677 0.0062  -0.0157 0.0244  473 PRO A CB  
6516  C CG  . PRO A  447 ? 0.3239 0.3989 0.3817 0.0110  -0.0173 0.0255  473 PRO A CG  
6517  C CD  . PRO A  447 ? 0.3118 0.3806 0.3664 0.0147  -0.0159 0.0244  473 PRO A CD  
6525  N N   . LEU A  448 ? 0.2716 0.3321 0.3209 0.0024  -0.0093 0.0218  474 LEU A N   
6526  C CA  . LEU A  448 ? 0.2714 0.3249 0.3167 0.0004  -0.0077 0.0204  474 LEU A CA  
6527  C C   . LEU A  448 ? 0.2695 0.3215 0.3128 -0.0024 -0.0098 0.0191  474 LEU A C   
6528  O O   . LEU A  448 ? 0.2684 0.3153 0.3086 -0.0018 -0.0095 0.0179  474 LEU A O   
6529  C CB  . LEU A  448 ? 0.2682 0.3205 0.3135 -0.0032 -0.0047 0.0204  474 LEU A CB  
6530  C CG  . LEU A  448 ? 0.2735 0.3261 0.3198 -0.0009 -0.0020 0.0217  474 LEU A CG  
6531  C CD1 . LEU A  448 ? 0.2861 0.3374 0.3323 -0.0053 0.0008  0.0218  474 LEU A CD1 
6532  C CD2 . LEU A  448 ? 0.2824 0.3295 0.3257 0.0034  -0.0007 0.0219  474 LEU A CD2 
6544  N N   . ILE A  449 ? 0.2639 0.3212 0.3092 -0.0055 -0.0119 0.0194  475 ILE A N   
6545  C CA  . ILE A  449 ? 0.2760 0.3330 0.3192 -0.0088 -0.0141 0.0185  475 ILE A CA  
6546  C C   . ILE A  449 ? 0.2736 0.3358 0.3190 -0.0068 -0.0176 0.0200  475 ILE A C   
6547  O O   . ILE A  449 ? 0.2760 0.3442 0.3256 -0.0048 -0.0182 0.0217  475 ILE A O   
6548  C CB  . ILE A  449 ? 0.2932 0.3514 0.3360 -0.0150 -0.0132 0.0176  475 ILE A CB  
6549  C CG1 . ILE A  449 ? 0.3079 0.3581 0.3475 -0.0161 -0.0092 0.0160  475 ILE A CG1 
6550  C CG2 . ILE A  449 ? 0.2977 0.3575 0.3385 -0.0191 -0.0159 0.0168  475 ILE A CG2 
6551  C CD1 . ILE A  449 ? 0.3281 0.3759 0.3656 -0.0219 -0.0074 0.0144  475 ILE A CD1 
6563  N N   . LYS A  450 ? 0.2651 0.3251 0.3078 -0.0069 -0.0196 0.0195  476 LYS A N   
6564  C CA  . LYS A  450 ? 0.2694 0.3331 0.3136 -0.0049 -0.0228 0.0212  476 LYS A CA  
6565  C C   . LYS A  450 ? 0.2619 0.3340 0.3098 -0.0070 -0.0248 0.0230  476 LYS A C   
6566  O O   . LYS A  450 ? 0.2564 0.3304 0.3034 -0.0122 -0.0248 0.0222  476 LYS A O   
6567  C CB  . LYS A  450 ? 0.3000 0.3602 0.3401 -0.0063 -0.0246 0.0205  476 LYS A CB  
6568  C CG  . LYS A  450 ? 0.3982 0.4520 0.4355 -0.0036 -0.0236 0.0194  476 LYS A CG  
6569  C CD  . LYS A  450 ? 0.4768 0.5286 0.5108 -0.0050 -0.0257 0.0193  476 LYS A CD  
6570  C CE  . LYS A  450 ? 0.5491 0.5952 0.5801 -0.0038 -0.0246 0.0177  476 LYS A CE  
6571  N NZ  . LYS A  450 ? 0.5903 0.6346 0.6178 -0.0063 -0.0261 0.0174  476 LYS A NZ  
6585  N N   . PRO A  451 ? 0.2660 0.3435 0.3182 -0.0032 -0.0260 0.0253  477 PRO A N   
6586  C CA  . PRO A  451 ? 0.2650 0.3521 0.3216 -0.0051 -0.0279 0.0273  477 PRO A CA  
6587  C C   . PRO A  451 ? 0.2653 0.3551 0.3199 -0.0095 -0.0310 0.0278  477 PRO A C   
6588  O O   . PRO A  451 ? 0.2630 0.3597 0.3196 -0.0137 -0.0320 0.0282  477 PRO A O   
6589  C CB  . PRO A  451 ? 0.2700 0.3610 0.3308 0.0009  -0.0288 0.0298  477 PRO A CB  
6590  C CG  . PRO A  451 ? 0.2810 0.3647 0.3399 0.0052  -0.0264 0.0285  477 PRO A CG  
6591  C CD  . PRO A  451 ? 0.2593 0.3348 0.3126 0.0029  -0.0257 0.0261  477 PRO A CD  
6599  N N   . GLN A  452 ? 0.2669 0.3516 0.3173 -0.0089 -0.0325 0.0276  478 GLN A N   
6600  C CA  . GLN A  452 ? 0.2700 0.3570 0.3177 -0.0129 -0.0355 0.0281  478 GLN A CA  
6601  C C   . GLN A  452 ? 0.2649 0.3505 0.3090 -0.0197 -0.0343 0.0254  478 GLN A C   
6602  O O   . GLN A  452 ? 0.2639 0.3545 0.3070 -0.0243 -0.0366 0.0258  478 GLN A O   
6603  C CB  . GLN A  452 ? 0.2963 0.3771 0.3399 -0.0109 -0.0368 0.0284  478 GLN A CB  
6604  C CG  . GLN A  452 ? 0.3287 0.4103 0.3750 -0.0047 -0.0382 0.0313  478 GLN A CG  
6605  C CD  . GLN A  452 ? 0.3609 0.4360 0.4071 0.0000  -0.0356 0.0300  478 GLN A CD  
6606  O OE1 . GLN A  452 ? 0.3673 0.4402 0.4138 -0.0001 -0.0328 0.0280  478 GLN A OE1 
6607  N NE2 . GLN A  452 ? 0.3719 0.4434 0.4174 0.0041  -0.0365 0.0314  478 GLN A NE2 
6616  N N   . CYS A  453 ? 0.2636 0.3423 0.3056 -0.0203 -0.0307 0.0226  479 CYS A N   
6617  C CA  . CYS A  453 ? 0.2709 0.3464 0.3093 -0.0261 -0.0287 0.0198  479 CYS A CA  
6618  C C   . CYS A  453 ? 0.2772 0.3582 0.3191 -0.0292 -0.0277 0.0199  479 CYS A C   
6619  O O   . CYS A  453 ? 0.2829 0.3673 0.3234 -0.0352 -0.0285 0.0190  479 CYS A O   
6620  C CB  . CYS A  453 ? 0.2746 0.3405 0.3097 -0.0245 -0.0253 0.0174  479 CYS A CB  
6621  S SG  . CYS A  453 ? 0.2885 0.3477 0.3176 -0.0307 -0.0224 0.0137  479 CYS A SG  
6626  N N   . ALA A  454 ? 0.2780 0.3603 0.3242 -0.0254 -0.0259 0.0209  480 ALA A N   
6627  C CA  . ALA A  454 ? 0.2790 0.3667 0.3288 -0.0282 -0.0246 0.0211  480 ALA A CA  
6628  C C   . ALA A  454 ? 0.2745 0.3739 0.3283 -0.0310 -0.0280 0.0232  480 ALA A C   
6629  O O   . ALA A  454 ? 0.2704 0.3742 0.3253 -0.0364 -0.0274 0.0225  480 ALA A O   
6630  C CB  . ALA A  454 ? 0.2763 0.3636 0.3298 -0.0230 -0.0222 0.0221  480 ALA A CB  
6636  N N   . ALA A  455 ? 0.2720 0.3765 0.3278 -0.0276 -0.0316 0.0258  481 ALA A N   
6637  C CA  . ALA A  455 ? 0.2726 0.3893 0.3326 -0.0294 -0.0353 0.0285  481 ALA A CA  
6638  C C   . ALA A  455 ? 0.2738 0.3933 0.3302 -0.0376 -0.0369 0.0270  481 ALA A C   
6639  O O   . ALA A  455 ? 0.2791 0.4096 0.3392 -0.0410 -0.0393 0.0286  481 ALA A O   
6640  C CB  . ALA A  455 ? 0.2772 0.3962 0.3384 -0.0241 -0.0386 0.0315  481 ALA A CB  
6646  N N   . TYR A  456 ? 0.2601 0.3701 0.3093 -0.0408 -0.0357 0.0240  482 TYR A N   
6647  C CA  . TYR A  456 ? 0.2525 0.3635 0.2970 -0.0488 -0.0367 0.0219  482 TYR A CA  
6648  C C   . TYR A  456 ? 0.2389 0.3501 0.2832 -0.0551 -0.0340 0.0194  482 TYR A C   
6649  O O   . TYR A  456 ? 0.2335 0.3486 0.2751 -0.0623 -0.0354 0.0181  482 TYR A O   
6650  C CB  . TYR A  456 ? 0.2554 0.3561 0.2921 -0.0500 -0.0358 0.0194  482 TYR A CB  
6651  C CG  . TYR A  456 ? 0.2606 0.3634 0.2959 -0.0476 -0.0396 0.0217  482 TYR A CG  
6652  C CD1 . TYR A  456 ? 0.2619 0.3734 0.2964 -0.0517 -0.0437 0.0234  482 TYR A CD1 
6653  C CD2 . TYR A  456 ? 0.2684 0.3648 0.3029 -0.0414 -0.0391 0.0225  482 TYR A CD2 
6654  C CE1 . TYR A  456 ? 0.2695 0.3825 0.3021 -0.0494 -0.0471 0.0260  482 TYR A CE1 
6655  C CE2 . TYR A  456 ? 0.2803 0.3777 0.3130 -0.0395 -0.0423 0.0247  482 TYR A CE2 
6656  C CZ  . TYR A  456 ? 0.2863 0.3916 0.3179 -0.0434 -0.0463 0.0266  482 TYR A CZ  
6657  O OH  . TYR A  456 ? 0.3096 0.4155 0.3392 -0.0412 -0.0493 0.0293  482 TYR A OH  
6667  N N   . GLY A  457 ? 0.2296 0.3364 0.2761 -0.0527 -0.0302 0.0187  483 GLY A N   
6668  C CA  . GLY A  457 ? 0.2324 0.3383 0.2785 -0.0586 -0.0272 0.0165  483 GLY A CA  
6669  C C   . GLY A  457 ? 0.2353 0.3288 0.2786 -0.0566 -0.0220 0.0144  483 GLY A C   
6670  O O   . GLY A  457 ? 0.2438 0.3330 0.2883 -0.0496 -0.0210 0.0154  483 GLY A O   
6674  N N   . LYS A  458 ? 0.2259 0.3136 0.2653 -0.0629 -0.0189 0.0114  484 LYS A N   
6675  C CA  . LYS A  458 ? 0.2274 0.3031 0.2640 -0.0615 -0.0137 0.0096  484 LYS A CA  
6676  C C   . LYS A  458 ? 0.2257 0.2917 0.2584 -0.0563 -0.0125 0.0087  484 LYS A C   
6677  O O   . LYS A  458 ? 0.2219 0.2849 0.2500 -0.0582 -0.0136 0.0070  484 LYS A O   
6678  C CB  . LYS A  458 ? 0.2530 0.3231 0.2847 -0.0699 -0.0106 0.0062  484 LYS A CB  
6679  C CG  . LYS A  458 ? 0.3097 0.3773 0.3432 -0.0716 -0.0067 0.0062  484 LYS A CG  
6680  C CD  . LYS A  458 ? 0.3938 0.4553 0.4218 -0.0807 -0.0038 0.0027  484 LYS A CD  
6681  C CE  . LYS A  458 ? 0.4552 0.5205 0.4861 -0.0857 -0.0019 0.0030  484 LYS A CE  
6682  N NZ  . LYS A  458 ? 0.4717 0.5503 0.5052 -0.0929 -0.0057 0.0031  484 LYS A NZ  
6696  N N   . ALA A  459 ? 0.2185 0.2799 0.2530 -0.0499 -0.0102 0.0099  485 ALA A N   
6697  C CA  . ALA A  459 ? 0.2209 0.2749 0.2529 -0.0444 -0.0094 0.0095  485 ALA A CA  
6698  C C   . ALA A  459 ? 0.2122 0.2550 0.2409 -0.0432 -0.0045 0.0080  485 ALA A C   
6699  O O   . ALA A  459 ? 0.2082 0.2496 0.2386 -0.0429 -0.0018 0.0088  485 ALA A O   
6700  C CB  . ALA A  459 ? 0.2235 0.2822 0.2599 -0.0373 -0.0115 0.0124  485 ALA A CB  
6706  N N   . LEU A  460 ? 0.2013 0.2366 0.2256 -0.0422 -0.0032 0.0062  486 LEU A N   
6707  C CA  . LEU A  460 ? 0.2047 0.2295 0.2260 -0.0401 0.0013  0.0051  486 LEU A CA  
6708  C C   . LEU A  460 ? 0.2037 0.2267 0.2250 -0.0337 0.0006  0.0058  486 LEU A C   
6709  O O   . LEU A  460 ? 0.1924 0.2157 0.2116 -0.0343 -0.0012 0.0047  486 LEU A O   
6710  C CB  . LEU A  460 ? 0.2174 0.2347 0.2330 -0.0459 0.0040  0.0016  486 LEU A CB  
6711  C CG  . LEU A  460 ? 0.2304 0.2359 0.2423 -0.0435 0.0090  0.0003  486 LEU A CG  
6712  C CD1 . LEU A  460 ? 0.2437 0.2455 0.2575 -0.0409 0.0122  0.0021  486 LEU A CD1 
6713  C CD2 . LEU A  460 ? 0.2326 0.2309 0.2387 -0.0497 0.0118  -0.0034 486 LEU A CD2 
6725  N N   . ASP A  461 ? 0.2107 0.2324 0.2344 -0.0280 0.0018  0.0077  487 ASP A N   
6726  C CA  . ASP A  461 ? 0.2127 0.2334 0.2365 -0.0223 0.0010  0.0084  487 ASP A CA  
6727  C C   . ASP A  461 ? 0.2117 0.2238 0.2331 -0.0198 0.0052  0.0077  487 ASP A C   
6728  O O   . ASP A  461 ? 0.2090 0.2183 0.2311 -0.0175 0.0076  0.0090  487 ASP A O   
6729  C CB  . ASP A  461 ? 0.2264 0.2530 0.2545 -0.0175 -0.0011 0.0110  487 ASP A CB  
6730  C CG  . ASP A  461 ? 0.2887 0.3154 0.3169 -0.0124 -0.0026 0.0115  487 ASP A CG  
6731  O OD1 . ASP A  461 ? 0.2789 0.3007 0.3047 -0.0114 -0.0010 0.0104  487 ASP A OD1 
6732  O OD2 . ASP A  461 ? 0.3325 0.3644 0.3634 -0.0096 -0.0051 0.0130  487 ASP A OD2 
6737  N N   . LEU A  462 ? 0.2073 0.2153 0.2256 -0.0203 0.0060  0.0057  488 LEU A N   
6738  C CA  . LEU A  462 ? 0.2151 0.2156 0.2314 -0.0174 0.0099  0.0051  488 LEU A CA  
6739  C C   . LEU A  462 ? 0.2155 0.2181 0.2328 -0.0126 0.0084  0.0057  488 LEU A C   
6740  O O   . LEU A  462 ? 0.2274 0.2254 0.2430 -0.0109 0.0110  0.0047  488 LEU A O   
6741  C CB  . LEU A  462 ? 0.2265 0.2202 0.2382 -0.0222 0.0129  0.0020  488 LEU A CB  
6742  C CG  . LEU A  462 ? 0.2516 0.2404 0.2613 -0.0268 0.0158  0.0011  488 LEU A CG  
6743  C CD1 . LEU A  462 ? 0.2596 0.2441 0.2645 -0.0332 0.0173  -0.0025 488 LEU A CD1 
6744  C CD2 . LEU A  462 ? 0.2629 0.2440 0.2723 -0.0231 0.0203  0.0023  488 LEU A CD2 
6756  N N   . SER A  463 ? 0.1971 0.2065 0.2172 -0.0104 0.0046  0.0073  489 SER A N   
6757  C CA  . SER A  463 ? 0.1929 0.2045 0.2138 -0.0066 0.0031  0.0077  489 SER A CA  
6758  C C   . SER A  463 ? 0.1921 0.2015 0.2140 -0.0014 0.0053  0.0091  489 SER A C   
6759  O O   . SER A  463 ? 0.1753 0.1826 0.1977 0.0000  0.0071  0.0105  489 SER A O   
6760  C CB  . SER A  463 ? 0.1944 0.2126 0.2176 -0.0057 -0.0012 0.0090  489 SER A CB  
6761  O OG  . SER A  463 ? 0.2161 0.2365 0.2417 -0.0032 -0.0015 0.0110  489 SER A OG  
6767  N N   . LEU A  464 ? 0.1953 0.2055 0.2173 0.0012  0.0051  0.0089  490 LEU A N   
6768  C CA  . LEU A  464 ? 0.2118 0.2215 0.2350 0.0064  0.0066  0.0105  490 LEU A CA  
6769  C C   . LEU A  464 ? 0.2200 0.2231 0.2421 0.0075  0.0111  0.0108  490 LEU A C   
6770  O O   . LEU A  464 ? 0.2274 0.2296 0.2504 0.0108  0.0123  0.0130  490 LEU A O   
6771  C CB  . LEU A  464 ? 0.2199 0.2343 0.2453 0.0094  0.0042  0.0126  490 LEU A CB  
6772  C CG  . LEU A  464 ? 0.2343 0.2542 0.2605 0.0090  0.0001  0.0123  490 LEU A CG  
6773  C CD1 . LEU A  464 ? 0.2410 0.2641 0.2685 0.0103  -0.0019 0.0138  490 LEU A CD1 
6774  C CD2 . LEU A  464 ? 0.2444 0.2666 0.2711 0.0115  -0.0005 0.0122  490 LEU A CD2 
6786  N N   . ASN A  465 ? 0.2116 0.2096 0.2313 0.0046  0.0137  0.0086  491 ASN A N   
6787  C CA  . ASN A  465 ? 0.2173 0.2073 0.2353 0.0056  0.0186  0.0085  491 ASN A CA  
6788  C C   . ASN A  465 ? 0.2314 0.2196 0.2487 0.0070  0.0208  0.0069  491 ASN A C   
6789  O O   . ASN A  465 ? 0.2313 0.2254 0.2503 0.0084  0.0183  0.0069  491 ASN A O   
6790  C CB  . ASN A  465 ? 0.2273 0.2120 0.2426 0.0002  0.0203  0.0070  491 ASN A CB  
6791  C CG  . ASN A  465 ? 0.2566 0.2419 0.2730 0.0004  0.0199  0.0092  491 ASN A CG  
6792  O OD1 . ASN A  465 ? 0.2811 0.2618 0.2974 0.0034  0.0229  0.0111  491 ASN A OD1 
6793  N ND2 . ASN A  465 ? 0.2262 0.2173 0.2440 -0.0026 0.0165  0.0093  491 ASN A ND2 
6800  N N   . SER A  466 ? 0.2475 0.2275 0.2623 0.0068  0.0255  0.0056  492 SER A N   
6801  C CA  . SER A  466 ? 0.2609 0.2386 0.2750 0.0084  0.0284  0.0040  492 SER A CA  
6802  C C   . SER A  466 ? 0.2641 0.2345 0.2735 0.0029  0.0315  0.0002  492 SER A C   
6803  O O   . SER A  466 ? 0.2655 0.2286 0.2730 0.0043  0.0364  -0.0010 492 SER A O   
6804  C CB  . SER A  466 ? 0.2924 0.2665 0.3081 0.0148  0.0321  0.0064  492 SER A CB  
6805  O OG  . SER A  466 ? 0.3437 0.3251 0.3632 0.0193  0.0290  0.0098  492 SER A OG  
6811  N N   . ILE A  467 ? 0.2604 0.2327 0.2678 -0.0033 0.0287  -0.0016 493 ILE A N   
6812  C CA  . ILE A  467 ? 0.2652 0.2316 0.2675 -0.0093 0.0310  -0.0053 493 ILE A CA  
6813  C C   . ILE A  467 ? 0.2745 0.2449 0.2763 -0.0098 0.0301  -0.0071 493 ILE A C   
6814  O O   . ILE A  467 ? 0.2799 0.2556 0.2807 -0.0139 0.0263  -0.0080 493 ILE A O   
6815  C CB  . ILE A  467 ? 0.2651 0.2330 0.2658 -0.0156 0.0282  -0.0060 493 ILE A CB  
6816  C CG1 . ILE A  467 ? 0.2728 0.2380 0.2749 -0.0146 0.0291  -0.0037 493 ILE A CG1 
6817  C CG2 . ILE A  467 ? 0.2753 0.2376 0.2701 -0.0225 0.0304  -0.0101 493 ILE A CG2 
6818  C CD1 . ILE A  467 ? 0.2775 0.2467 0.2794 -0.0203 0.0259  -0.0038 493 ILE A CD1 
6830  N N   A PHE A  468 ? 0.2692 0.2376 0.2719 -0.0052 0.0335  -0.0072 494 PHE A N   
6831  N N   B PHE A  468 ? 0.2785 0.2467 0.2811 -0.0052 0.0336  -0.0073 494 PHE A N   
6832  C CA  A PHE A  468 ? 0.2704 0.2430 0.2731 -0.0050 0.0332  -0.0087 494 PHE A CA  
6833  C CA  B PHE A  468 ? 0.2896 0.2615 0.2922 -0.0048 0.0337  -0.0088 494 PHE A CA  
6834  C C   A PHE A  468 ? 0.2942 0.2622 0.2911 -0.0109 0.0355  -0.0129 494 PHE A C   
6835  C C   B PHE A  468 ? 0.3036 0.2717 0.3005 -0.0111 0.0353  -0.0129 494 PHE A C   
6836  O O   A PHE A  468 ? 0.2944 0.2662 0.2906 -0.0118 0.0350  -0.0142 494 PHE A O   
6837  O O   B PHE A  468 ? 0.3050 0.2772 0.3012 -0.0122 0.0345  -0.0141 494 PHE A O   
6838  C CB  A PHE A  468 ? 0.2591 0.2323 0.2654 0.0020  0.0363  -0.0073 494 PHE A CB  
6839  C CB  B PHE A  468 ? 0.2935 0.2627 0.2982 0.0014  0.0384  -0.0083 494 PHE A CB  
6840  C CG  A PHE A  468 ? 0.2622 0.2254 0.2665 0.0044  0.0429  -0.0084 494 PHE A CG  
6841  C CG  B PHE A  468 ? 0.3062 0.2774 0.3157 0.0081  0.0383  -0.0043 494 PHE A CG  
6842  C CD1 A PHE A  468 ? 0.2714 0.2294 0.2720 0.0027  0.0472  -0.0119 494 PHE A CD1 
6843  C CD1 B PHE A  468 ? 0.3158 0.2965 0.3296 0.0105  0.0335  -0.0015 494 PHE A CD1 
6844  C CD2 A PHE A  468 ? 0.2696 0.2281 0.2755 0.0087  0.0449  -0.0058 494 PHE A CD2 
6845  C CD2 B PHE A  468 ? 0.3245 0.2878 0.3338 0.0121  0.0432  -0.0033 494 PHE A CD2 
6846  C CE1 A PHE A  468 ? 0.2843 0.2322 0.2829 0.0052  0.0537  -0.0130 494 PHE A CE1 
6847  C CE1 B PHE A  468 ? 0.3248 0.3078 0.3425 0.0164  0.0332  0.0021  494 PHE A CE1 
6848  C CE2 A PHE A  468 ? 0.2799 0.2281 0.2837 0.0113  0.0513  -0.0065 494 PHE A CE2 
6849  C CE2 B PHE A  468 ? 0.3361 0.3018 0.3496 0.0185  0.0428  0.0007  494 PHE A CE2 
6850  C CZ  A PHE A  468 ? 0.2797 0.2224 0.2799 0.0096  0.0557  -0.0102 494 PHE A CZ  
6851  C CZ  B PHE A  468 ? 0.3260 0.3019 0.3436 0.0205  0.0378  0.0034  494 PHE A CZ  
6870  N N   . PHE A  469 ? 0.3106 0.2703 0.3029 -0.0150 0.0383  -0.0151 495 PHE A N   
6871  C CA  . PHE A  469 ? 0.3455 0.3003 0.3314 -0.0213 0.0404  -0.0194 495 PHE A CA  
6872  C C   . PHE A  469 ? 0.3625 0.3125 0.3449 -0.0270 0.0402  -0.0205 495 PHE A C   
6873  O O   . PHE A  469 ? 0.3739 0.3185 0.3573 -0.0249 0.0425  -0.0192 495 PHE A O   
6874  C CB  . PHE A  469 ? 0.3593 0.3057 0.3428 -0.0186 0.0473  -0.0218 495 PHE A CB  
6875  C CG  . PHE A  469 ? 0.3840 0.3235 0.3599 -0.0250 0.0507  -0.0267 495 PHE A CG  
6876  C CD1 . PHE A  469 ? 0.3989 0.3424 0.3723 -0.0278 0.0501  -0.0290 495 PHE A CD1 
6877  C CD2 . PHE A  469 ? 0.4039 0.3321 0.3748 -0.0282 0.0551  -0.0293 495 PHE A CD2 
6878  C CE1 . PHE A  469 ? 0.4144 0.3512 0.3800 -0.0337 0.0535  -0.0337 495 PHE A CE1 
6879  C CE2 . PHE A  469 ? 0.4225 0.3439 0.3857 -0.0343 0.0586  -0.0343 495 PHE A CE2 
6880  C CZ  . PHE A  469 ? 0.4190 0.3451 0.3795 -0.0372 0.0575  -0.0365 495 PHE A CZ  
6890  N N   . ILE A  470 ? 0.3601 0.3130 0.3387 -0.0340 0.0372  -0.0224 496 ILE A N   
6891  C CA  . ILE A  470 ? 0.3701 0.3204 0.3455 -0.0405 0.0365  -0.0237 496 ILE A CA  
6892  C C   . ILE A  470 ? 0.4061 0.3462 0.3739 -0.0454 0.0418  -0.0285 496 ILE A C   
6893  O O   . ILE A  470 ? 0.4030 0.3442 0.3666 -0.0491 0.0418  -0.0313 496 ILE A O   
6894  C CB  . ILE A  470 ? 0.3590 0.3193 0.3348 -0.0452 0.0299  -0.0227 496 ILE A CB  
6895  C CG1 . ILE A  470 ? 0.3619 0.3312 0.3448 -0.0399 0.0251  -0.0181 496 ILE A CG1 
6896  C CG2 . ILE A  470 ? 0.3619 0.3207 0.3344 -0.0524 0.0292  -0.0243 496 ILE A CG2 
6897  C CD1 . ILE A  470 ? 0.3710 0.3500 0.3548 -0.0426 0.0190  -0.0168 496 ILE A CD1 
6909  N N   . GLY A  471 ? 0.4358 0.3658 0.4019 -0.0452 0.0467  -0.0295 497 GLY A N   
6910  C CA  . GLY A  471 ? 0.4758 0.3941 0.4343 -0.0498 0.0525  -0.0343 497 GLY A CA  
6911  C C   . GLY A  471 ? 0.5031 0.4210 0.4565 -0.0595 0.0507  -0.0369 497 GLY A C   
6912  O O   . GLY A  471 ? 0.5037 0.4299 0.4603 -0.0618 0.0453  -0.0344 497 GLY A O   
6916  N N   . PRO A  472 ? 0.5228 0.4309 0.4681 -0.0655 0.0553  -0.0419 498 PRO A N   
6917  C CA  . PRO A  472 ? 0.5331 0.4416 0.4730 -0.0756 0.0534  -0.0447 498 PRO A CA  
6918  C C   . PRO A  472 ? 0.5389 0.4467 0.4809 -0.0783 0.0523  -0.0430 498 PRO A C   
6919  O O   . PRO A  472 ? 0.5508 0.4644 0.4909 -0.0860 0.0486  -0.0439 498 PRO A O   
6920  C CB  . PRO A  472 ? 0.5540 0.4500 0.4844 -0.0805 0.0598  -0.0508 498 PRO A CB  
6921  C CG  . PRO A  472 ? 0.5632 0.4497 0.4947 -0.0722 0.0661  -0.0507 498 PRO A CG  
6922  C CD  . PRO A  472 ? 0.5305 0.4275 0.4709 -0.0635 0.0623  -0.0456 498 PRO A CD  
6930  N N   . ASN A  473 ? 0.5322 0.4343 0.4782 -0.0723 0.0553  -0.0403 499 ASN A N   
6931  C CA  . ASN A  473 ? 0.5301 0.4312 0.4779 -0.0749 0.0548  -0.0384 499 ASN A CA  
6932  C C   . ASN A  473 ? 0.5023 0.4142 0.4592 -0.0689 0.0500  -0.0326 499 ASN A C   
6933  O O   . ASN A  473 ? 0.5053 0.4166 0.4643 -0.0700 0.0499  -0.0307 499 ASN A O   
6934  C CB  . ASN A  473 ? 0.5692 0.4541 0.5137 -0.0733 0.0624  -0.0397 499 ASN A CB  
6935  C CG  . ASN A  473 ? 0.6436 0.5157 0.5789 -0.0784 0.0684  -0.0456 499 ASN A CG  
6936  O OD1 . ASN A  473 ? 0.6572 0.5310 0.5868 -0.0872 0.0669  -0.0496 499 ASN A OD1 
6937  N ND2 . ASN A  473 ? 0.6725 0.5313 0.6058 -0.0728 0.0753  -0.0464 499 ASN A ND2 
6944  N N   . GLN A  474 ? 0.4777 0.3990 0.4396 -0.0629 0.0461  -0.0300 500 GLN A N   
6945  C CA  . GLN A  474 ? 0.4586 0.3891 0.4284 -0.0569 0.0420  -0.0248 500 GLN A CA  
6946  C C   . GLN A  474 ? 0.4485 0.3876 0.4211 -0.0615 0.0374  -0.0230 500 GLN A C   
6947  O O   . GLN A  474 ? 0.4473 0.3878 0.4244 -0.0582 0.0370  -0.0197 500 GLN A O   
6948  C CB  . GLN A  474 ? 0.4579 0.3976 0.4314 -0.0518 0.0381  -0.0230 500 GLN A CB  
6949  C CG  . GLN A  474 ? 0.4560 0.4043 0.4371 -0.0452 0.0342  -0.0181 500 GLN A CG  
6950  C CD  . GLN A  474 ? 0.4779 0.4196 0.4614 -0.0384 0.0382  -0.0157 500 GLN A CD  
6951  O OE1 . GLN A  474 ? 0.4803 0.4156 0.4627 -0.0341 0.0422  -0.0164 500 GLN A OE1 
6952  N NE2 . GLN A  474 ? 0.4653 0.4087 0.4521 -0.0372 0.0372  -0.0128 500 GLN A NE2 
6961  N N   . PHE A  475 ? 0.4373 0.3828 0.4076 -0.0687 0.0338  -0.0250 501 PHE A N   
6962  C CA  . PHE A  475 ? 0.4344 0.3901 0.4081 -0.0728 0.0290  -0.0231 501 PHE A CA  
6963  C C   . PHE A  475 ? 0.4530 0.4050 0.4222 -0.0820 0.0306  -0.0260 501 PHE A C   
6964  O O   . PHE A  475 ? 0.4546 0.4164 0.4256 -0.0873 0.0263  -0.0253 501 PHE A O   
6965  C CB  . PHE A  475 ? 0.4200 0.3882 0.3957 -0.0733 0.0227  -0.0220 501 PHE A CB  
6966  C CG  . PHE A  475 ? 0.4176 0.3895 0.3978 -0.0647 0.0209  -0.0190 501 PHE A CG  
6967  C CD1 . PHE A  475 ? 0.4203 0.3951 0.4068 -0.0582 0.0201  -0.0151 501 PHE A CD1 
6968  C CD2 . PHE A  475 ? 0.4256 0.3982 0.4035 -0.0634 0.0202  -0.0202 501 PHE A CD2 
6969  C CE1 . PHE A  475 ? 0.4252 0.4033 0.4154 -0.0509 0.0185  -0.0127 501 PHE A CE1 
6970  C CE2 . PHE A  475 ? 0.4325 0.4087 0.4146 -0.0561 0.0187  -0.0176 501 PHE A CE2 
6971  C CZ  . PHE A  475 ? 0.4252 0.4041 0.4133 -0.0500 0.0178  -0.0140 501 PHE A CZ  
6981  N N   . GLU A  476 ? 0.4675 0.4056 0.4314 -0.0839 0.0370  -0.0288 502 GLU A N   
6982  C CA  . GLU A  476 ? 0.4868 0.4194 0.4457 -0.0931 0.0394  -0.0320 502 GLU A CA  
6983  C C   . GLU A  476 ? 0.4916 0.4278 0.4555 -0.0937 0.0386  -0.0289 502 GLU A C   
6984  O O   . GLU A  476 ? 0.4983 0.4344 0.4674 -0.0861 0.0392  -0.0250 502 GLU A O   
6985  C CB  . GLU A  476 ? 0.5304 0.4453 0.4821 -0.0939 0.0471  -0.0359 502 GLU A CB  
6986  C CG  . GLU A  476 ? 0.6316 0.5390 0.5761 -0.1046 0.0501  -0.0404 502 GLU A CG  
6987  C CD  . GLU A  476 ? 0.7645 0.6528 0.7015 -0.1052 0.0583  -0.0442 502 GLU A CD  
6988  O OE1 . GLU A  476 ? 0.7887 0.6694 0.7268 -0.0964 0.0620  -0.0428 502 GLU A OE1 
6989  O OE2 . GLU A  476 ? 0.8066 0.6873 0.7364 -0.1145 0.0612  -0.0487 502 GLU A OE2 
6996  N N   . ASN A  477 ? 0.4854 0.4248 0.4475 -0.1031 0.0375  -0.0306 503 ASN A N   
6997  C CA  . ASN A  477 ? 0.4874 0.4303 0.4536 -0.1054 0.0373  -0.0282 503 ASN A CA  
6998  C C   . ASN A  477 ? 0.4805 0.4378 0.4561 -0.0993 0.0320  -0.0229 503 ASN A C   
6999  O O   . ASN A  477 ? 0.4805 0.4389 0.4602 -0.0977 0.0329  -0.0200 503 ASN A O   
7000  C CB  . ASN A  477 ? 0.5134 0.4406 0.4770 -0.1032 0.0443  -0.0282 503 ASN A CB  
7001  C CG  . ASN A  477 ? 0.5724 0.4834 0.5267 -0.1078 0.0503  -0.0334 503 ASN A CG  
7002  O OD1 . ASN A  477 ? 0.5857 0.4962 0.5344 -0.1175 0.0502  -0.0376 503 ASN A OD1 
7003  N ND2 . ASN A  477 ? 0.5968 0.4942 0.5488 -0.1011 0.0558  -0.0332 503 ASN A ND2 
7010  N N   . LEU A  478 ? 0.4718 0.4398 0.4502 -0.0965 0.0268  -0.0217 504 LEU A N   
7011  C CA  . LEU A  478 ? 0.4713 0.4522 0.4579 -0.0905 0.0219  -0.0170 504 LEU A CA  
7012  C C   . LEU A  478 ? 0.4602 0.4554 0.4500 -0.0968 0.0167  -0.0164 504 LEU A C   
7013  O O   . LEU A  478 ? 0.4664 0.4634 0.4517 -0.1044 0.0154  -0.0195 504 LEU A O   
7014  C CB  . LEU A  478 ? 0.4832 0.4664 0.4705 -0.0838 0.0194  -0.0162 504 LEU A CB  
7015  C CG  . LEU A  478 ? 0.5111 0.4970 0.5043 -0.0737 0.0183  -0.0122 504 LEU A CG  
7016  C CD1 . LEU A  478 ? 0.5238 0.5009 0.5178 -0.0695 0.0230  -0.0108 504 LEU A CD1 
7017  C CD2 . LEU A  478 ? 0.5213 0.5050 0.5127 -0.0691 0.0179  -0.0129 504 LEU A CD2 
7029  N N   . PRO A  479 ? 0.4405 0.4467 0.4379 -0.0938 0.0136  -0.0124 505 PRO A N   
7030  C CA  . PRO A  479 ? 0.4243 0.4457 0.4256 -0.0989 0.0084  -0.0113 505 PRO A CA  
7031  C C   . PRO A  479 ? 0.4121 0.4414 0.4133 -0.0975 0.0032  -0.0110 505 PRO A C   
7032  O O   . PRO A  479 ? 0.4160 0.4387 0.4139 -0.0933 0.0040  -0.0119 505 PRO A O   
7033  C CB  . PRO A  479 ? 0.4331 0.4625 0.4425 -0.0942 0.0073  -0.0071 505 PRO A CB  
7034  C CG  . PRO A  479 ? 0.4443 0.4662 0.4547 -0.0847 0.0096  -0.0053 505 PRO A CG  
7035  C CD  . PRO A  479 ? 0.4326 0.4389 0.4355 -0.0853 0.0145  -0.0086 505 PRO A CD  
7043  N N   . ASP A  480 ? 0.3918 0.4353 0.3963 -0.1014 -0.0020 -0.0096 506 ASP A N   
7044  C CA  . ASP A  480 ? 0.3808 0.4320 0.3849 -0.1005 -0.0070 -0.0088 506 ASP A CA  
7045  C C   . ASP A  480 ? 0.3454 0.3997 0.3549 -0.0903 -0.0091 -0.0050 506 ASP A C   
7046  O O   . ASP A  480 ? 0.3436 0.4093 0.3599 -0.0873 -0.0127 -0.0013 506 ASP A O   
7047  C CB  . ASP A  480 ? 0.4097 0.4759 0.4164 -0.1072 -0.0120 -0.0078 506 ASP A CB  
7048  C CG  . ASP A  480 ? 0.4743 0.5484 0.4797 -0.1071 -0.0173 -0.0068 506 ASP A CG  
7049  O OD1 . ASP A  480 ? 0.4934 0.5620 0.4966 -0.1015 -0.0172 -0.0066 506 ASP A OD1 
7050  O OD2 . ASP A  480 ? 0.4929 0.5792 0.4996 -0.1127 -0.0215 -0.0059 506 ASP A OD2 
7055  N N   . ILE A  481 ? 0.3175 0.3616 0.3238 -0.0851 -0.0066 -0.0059 507 ILE A N   
7056  C CA  . ILE A  481 ? 0.2982 0.3439 0.3087 -0.0759 -0.0081 -0.0028 507 ILE A CA  
7057  C C   . ILE A  481 ? 0.2845 0.3386 0.2955 -0.0751 -0.0134 -0.0012 507 ILE A C   
7058  O O   . ILE A  481 ? 0.3026 0.3544 0.3078 -0.0790 -0.0139 -0.0035 507 ILE A O   
7059  C CB  . ILE A  481 ? 0.3032 0.3360 0.3102 -0.0711 -0.0037 -0.0043 507 ILE A CB  
7060  C CG1 . ILE A  481 ? 0.3057 0.3297 0.3124 -0.0710 0.0016  -0.0052 507 ILE A CG1 
7061  C CG2 . ILE A  481 ? 0.3033 0.3382 0.3141 -0.0625 -0.0056 -0.0014 507 ILE A CG2 
7062  C CD1 . ILE A  481 ? 0.3042 0.3333 0.3175 -0.0675 0.0014  -0.0019 507 ILE A CD1 
7074  N N   . ALA A  482 ? 0.2589 0.3221 0.2764 -0.0699 -0.0169 0.0027  508 ALA A N   
7075  C CA  . ALA A  482 ? 0.2521 0.3229 0.2709 -0.0676 -0.0218 0.0052  508 ALA A CA  
7076  C C   . ALA A  482 ? 0.2450 0.3112 0.2645 -0.0596 -0.0216 0.0066  508 ALA A C   
7077  O O   . ALA A  482 ? 0.2329 0.3008 0.2508 -0.0582 -0.0244 0.0075  508 ALA A O   
7078  C CB  . ALA A  482 ? 0.2424 0.3263 0.2681 -0.0670 -0.0255 0.0087  508 ALA A CB  
7084  N N   . CYS A  483 ? 0.2334 0.2945 0.2555 -0.0544 -0.0186 0.0070  509 CYS A N   
7085  C CA  . CYS A  483 ? 0.2390 0.2967 0.2623 -0.0470 -0.0185 0.0083  509 CYS A CA  
7086  C C   . CYS A  483 ? 0.2443 0.2911 0.2645 -0.0455 -0.0137 0.0059  509 CYS A C   
7087  O O   . CYS A  483 ? 0.2539 0.2977 0.2752 -0.0456 -0.0106 0.0056  509 CYS A O   
7088  C CB  . CYS A  483 ? 0.2408 0.3048 0.2708 -0.0417 -0.0199 0.0116  509 CYS A CB  
7089  S SG  . CYS A  483 ? 0.2854 0.3440 0.3169 -0.0332 -0.0185 0.0127  509 CYS A SG  
7094  N N   . LEU A  484 ? 0.2414 0.2825 0.2577 -0.0442 -0.0129 0.0045  510 LEU A N   
7095  C CA  . LEU A  484 ? 0.2410 0.2725 0.2546 -0.0425 -0.0084 0.0025  510 LEU A CA  
7096  C C   . LEU A  484 ? 0.2339 0.2635 0.2482 -0.0364 -0.0087 0.0035  510 LEU A C   
7097  O O   . LEU A  484 ? 0.2318 0.2633 0.2447 -0.0362 -0.0110 0.0037  510 LEU A O   
7098  C CB  . LEU A  484 ? 0.2500 0.2758 0.2572 -0.0482 -0.0062 -0.0011 510 LEU A CB  
7099  C CG  . LEU A  484 ? 0.2865 0.3020 0.2906 -0.0464 -0.0012 -0.0033 510 LEU A CG  
7100  C CD1 . LEU A  484 ? 0.2990 0.3097 0.3048 -0.0449 0.0025  -0.0030 510 LEU A CD1 
7101  C CD2 . LEU A  484 ? 0.3015 0.3117 0.2989 -0.0522 0.0009  -0.0071 510 LEU A CD2 
7113  N N   . ASN A  485 ? 0.2237 0.2496 0.2400 -0.0316 -0.0061 0.0041  511 ASN A N   
7114  C CA  . ASN A  485 ? 0.2214 0.2460 0.2385 -0.0262 -0.0063 0.0049  511 ASN A CA  
7115  C C   . ASN A  485 ? 0.2227 0.2395 0.2374 -0.0247 -0.0020 0.0032  511 ASN A C   
7116  O O   . ASN A  485 ? 0.2222 0.2350 0.2374 -0.0234 0.0011  0.0033  511 ASN A O   
7117  C CB  . ASN A  485 ? 0.2236 0.2521 0.2453 -0.0212 -0.0078 0.0076  511 ASN A CB  
7118  C CG  . ASN A  485 ? 0.2334 0.2617 0.2559 -0.0163 -0.0085 0.0084  511 ASN A CG  
7119  O OD1 . ASN A  485 ? 0.2189 0.2447 0.2388 -0.0164 -0.0083 0.0072  511 ASN A OD1 
7120  N ND2 . ASN A  485 ? 0.2429 0.2742 0.2685 -0.0123 -0.0099 0.0103  511 ASN A ND2 
7127  N N   . LEU A  486 ? 0.2206 0.2352 0.2325 -0.0250 -0.0016 0.0017  512 LEU A N   
7128  C CA  . LEU A  486 ? 0.2306 0.2390 0.2407 -0.0229 0.0024  0.0002  512 LEU A CA  
7129  C C   . LEU A  486 ? 0.2268 0.2374 0.2386 -0.0182 0.0012  0.0013  512 LEU A C   
7130  O O   . LEU A  486 ? 0.2361 0.2438 0.2465 -0.0171 0.0035  0.0000  512 LEU A O   
7131  C CB  . LEU A  486 ? 0.2430 0.2471 0.2480 -0.0278 0.0045  -0.0030 512 LEU A CB  
7132  C CG  . LEU A  486 ? 0.2815 0.2817 0.2840 -0.0329 0.0067  -0.0047 512 LEU A CG  
7133  C CD1 . LEU A  486 ? 0.2947 0.2926 0.2916 -0.0387 0.0075  -0.0079 512 LEU A CD1 
7134  C CD2 . LEU A  486 ? 0.2989 0.2912 0.3012 -0.0304 0.0117  -0.0051 512 LEU A CD2 
7146  N N   . SER A  487 ? 0.2108 0.2266 0.2258 -0.0156 -0.0022 0.0035  513 SER A N   
7147  C CA  . SER A  487 ? 0.2015 0.2195 0.2179 -0.0119 -0.0036 0.0044  513 SER A CA  
7148  C C   . SER A  487 ? 0.1954 0.2108 0.2131 -0.0076 -0.0005 0.0046  513 SER A C   
7149  O O   . SER A  487 ? 0.1998 0.2128 0.2184 -0.0060 0.0015  0.0053  513 SER A O   
7150  C CB  . SER A  487 ? 0.2197 0.2424 0.2389 -0.0097 -0.0070 0.0066  513 SER A CB  
7151  O OG  . SER A  487 ? 0.2586 0.2829 0.2787 -0.0066 -0.0083 0.0072  513 SER A OG  
7157  N N   . ALA A  488 ? 0.1877 0.2040 0.2055 -0.0056 -0.0003 0.0043  514 ALA A N   
7158  C CA  . ALA A  488 ? 0.1895 0.2052 0.2091 -0.0011 0.0019  0.0050  514 ALA A CA  
7159  C C   . ALA A  488 ? 0.2002 0.2103 0.2191 -0.0001 0.0063  0.0045  514 ALA A C   
7160  O O   . ALA A  488 ? 0.2139 0.2230 0.2345 0.0033  0.0076  0.0061  514 ALA A O   
7161  C CB  . ALA A  488 ? 0.1910 0.2103 0.2134 0.0026  -0.0003 0.0072  514 ALA A CB  
7167  N N   . ASN A  489 ? 0.1987 0.2047 0.2147 -0.0032 0.0088  0.0022  515 ASN A N   
7168  C CA  . ASN A  489 ? 0.2092 0.2084 0.2237 -0.0025 0.0137  0.0012  515 ASN A CA  
7169  C C   . ASN A  489 ? 0.2226 0.2205 0.2367 -0.0008 0.0167  -0.0002 515 ASN A C   
7170  O O   . ASN A  489 ? 0.2277 0.2191 0.2398 -0.0007 0.0211  -0.0016 515 ASN A O   
7171  C CB  . ASN A  489 ? 0.2096 0.2041 0.2205 -0.0081 0.0148  -0.0008 515 ASN A CB  
7172  C CG  . ASN A  489 ? 0.2305 0.2240 0.2423 -0.0084 0.0145  0.0007  515 ASN A CG  
7173  O OD1 . ASN A  489 ? 0.2369 0.2250 0.2486 -0.0064 0.0179  0.0013  515 ASN A OD1 
7174  N ND2 . ASN A  489 ? 0.2253 0.2241 0.2384 -0.0104 0.0105  0.0017  515 ASN A ND2 
7181  N N   . SER A  490 ? 0.2329 0.2368 0.2489 0.0007  0.0145  0.0002  516 SER A N   
7182  C CA  . SER A  490 ? 0.2420 0.2465 0.2584 0.0023  0.0171  -0.0009 516 SER A CA  
7183  C C   . SER A  490 ? 0.2423 0.2414 0.2542 -0.0017 0.0204  -0.0041 516 SER A C   
7184  O O   . SER A  490 ? 0.2363 0.2326 0.2480 0.0002  0.0246  -0.0053 516 SER A O   
7185  C CB  A SER A  490 ? 0.2747 0.2788 0.2943 0.0085  0.0200  0.0009  516 SER A CB  
7186  C CB  B SER A  490 ? 0.2527 0.2567 0.2723 0.0085  0.0200  0.0010  516 SER A CB  
7187  O OG  A SER A  490 ? 0.3257 0.3217 0.3436 0.0095  0.0245  0.0005  516 SER A OG  
7188  O OG  B SER A  490 ? 0.2603 0.2694 0.2832 0.0117  0.0169  0.0038  516 SER A OG  
7197  N N   . ASN A  491 ? 0.2374 0.2354 0.2458 -0.0074 0.0184  -0.0055 517 ASN A N   
7198  C CA  . ASN A  491 ? 0.2441 0.2371 0.2474 -0.0121 0.0210  -0.0088 517 ASN A CA  
7199  C C   . ASN A  491 ? 0.2357 0.2318 0.2374 -0.0137 0.0210  -0.0103 517 ASN A C   
7200  O O   . ASN A  491 ? 0.2308 0.2322 0.2326 -0.0157 0.0169  -0.0094 517 ASN A O   
7201  C CB  . ASN A  491 ? 0.2613 0.2531 0.2615 -0.0176 0.0186  -0.0094 517 ASN A CB  
7202  C CG  . ASN A  491 ? 0.2905 0.2760 0.2848 -0.0228 0.0218  -0.0129 517 ASN A CG  
7203  O OD1 . ASN A  491 ? 0.3006 0.2848 0.2921 -0.0240 0.0241  -0.0152 517 ASN A OD1 
7204  N ND2 . ASN A  491 ? 0.3053 0.2866 0.2974 -0.0261 0.0224  -0.0137 517 ASN A ND2 
7211  N N   . ALA A  492 ? 0.2389 0.2313 0.2391 -0.0129 0.0259  -0.0125 518 ALA A N   
7212  C CA  . ALA A  492 ? 0.2560 0.2513 0.2547 -0.0144 0.0267  -0.0141 518 ALA A CA  
7213  C C   . ALA A  492 ? 0.2600 0.2493 0.2519 -0.0197 0.0300  -0.0179 518 ALA A C   
7214  O O   . ALA A  492 ? 0.2624 0.2523 0.2526 -0.0203 0.0326  -0.0198 518 ALA A O   
7215  C CB  . ALA A  492 ? 0.2621 0.2596 0.2652 -0.0086 0.0300  -0.0134 518 ALA A CB  
7221  N N   . GLN A  493 ? 0.2607 0.2449 0.2486 -0.0238 0.0298  -0.0192 519 GLN A N   
7222  C CA  . GLN A  493 ? 0.2695 0.2476 0.2503 -0.0292 0.0331  -0.0232 519 GLN A CA  
7223  C C   . GLN A  493 ? 0.2806 0.2628 0.2568 -0.0353 0.0297  -0.0242 519 GLN A C   
7224  O O   . GLN A  493 ? 0.2799 0.2689 0.2582 -0.0358 0.0243  -0.0215 519 GLN A O   
7225  C CB  . GLN A  493 ? 0.2866 0.2573 0.2646 -0.0319 0.0346  -0.0245 519 GLN A CB  
7226  C CG  . GLN A  493 ? 0.3175 0.2911 0.2932 -0.0377 0.0295  -0.0240 519 GLN A CG  
7227  C CD  . GLN A  493 ? 0.3459 0.3132 0.3200 -0.0398 0.0312  -0.0249 519 GLN A CD  
7228  O OE1 . GLN A  493 ? 0.3293 0.2981 0.3078 -0.0373 0.0293  -0.0221 519 GLN A OE1 
7229  N NE2 . GLN A  493 ? 0.3505 0.3101 0.3181 -0.0446 0.0352  -0.0289 519 GLN A NE2 
7238  N N   . VAL A  494 ? 0.2851 0.2627 0.2546 -0.0400 0.0330  -0.0280 520 VAL A N   
7239  C CA  . VAL A  494 ? 0.2937 0.2741 0.2574 -0.0465 0.0303  -0.0292 520 VAL A CA  
7240  C C   . VAL A  494 ? 0.3100 0.2873 0.2695 -0.0519 0.0287  -0.0304 520 VAL A C   
7241  O O   . VAL A  494 ? 0.3255 0.2951 0.2801 -0.0548 0.0331  -0.0340 520 VAL A O   
7242  C CB  . VAL A  494 ? 0.3045 0.2818 0.2626 -0.0487 0.0352  -0.0330 520 VAL A CB  
7243  C CG1 . VAL A  494 ? 0.3078 0.2875 0.2586 -0.0561 0.0324  -0.0343 520 VAL A CG1 
7244  C CG2 . VAL A  494 ? 0.3075 0.2890 0.2704 -0.0433 0.0369  -0.0317 520 VAL A CG2 
7254  N N   . LEU A  495 ? 0.2973 0.2805 0.2589 -0.0535 0.0226  -0.0273 521 LEU A N   
7255  C CA  . LEU A  495 ? 0.3025 0.2850 0.2607 -0.0591 0.0204  -0.0281 521 LEU A CA  
7256  C C   . LEU A  495 ? 0.3146 0.2963 0.2642 -0.0664 0.0208  -0.0313 521 LEU A C   
7257  O O   . LEU A  495 ? 0.3029 0.2885 0.2506 -0.0671 0.0195  -0.0308 521 LEU A O   
7258  C CB  . LEU A  495 ? 0.2955 0.2858 0.2584 -0.0585 0.0139  -0.0238 521 LEU A CB  
7259  C CG  . LEU A  495 ? 0.3110 0.3022 0.2817 -0.0519 0.0134  -0.0208 521 LEU A CG  
7260  C CD1 . LEU A  495 ? 0.3163 0.3154 0.2913 -0.0506 0.0073  -0.0168 521 LEU A CD1 
7261  C CD2 . LEU A  495 ? 0.3267 0.3120 0.2977 -0.0523 0.0163  -0.0221 521 LEU A CD2 
7273  N N   . SER A  496 ? 0.3293 0.3055 0.2732 -0.0718 0.0231  -0.0347 522 SER A N   
7274  C CA  . SER A  496 ? 0.3579 0.3321 0.2927 -0.0789 0.0244  -0.0385 522 SER A CA  
7275  C C   . SER A  496 ? 0.3629 0.3383 0.2926 -0.0869 0.0216  -0.0399 522 SER A C   
7276  O O   . SER A  496 ? 0.3681 0.3401 0.2893 -0.0933 0.0237  -0.0439 522 SER A O   
7277  C CB  . SER A  496 ? 0.3970 0.3612 0.3279 -0.0781 0.0323  -0.0431 522 SER A CB  
7278  O OG  . SER A  496 ? 0.4477 0.4041 0.3791 -0.0778 0.0356  -0.0447 522 SER A OG  
7284  N N   . GLY A  497 ? 0.3552 0.3364 0.2899 -0.0867 0.0167  -0.0365 523 GLY A N   
7285  C CA  . GLY A  497 ? 0.3647 0.3494 0.2957 -0.0942 0.0133  -0.0371 523 GLY A CA  
7286  C C   . GLY A  497 ? 0.3672 0.3454 0.2964 -0.0979 0.0164  -0.0401 523 GLY A C   
7287  O O   . GLY A  497 ? 0.3691 0.3501 0.2940 -0.1054 0.0141  -0.0415 523 GLY A O   
7291  N N   . THR A  498 ? 0.3648 0.3345 0.2970 -0.0932 0.0216  -0.0411 524 THR A N   
7292  C CA  . THR A  498 ? 0.3823 0.3444 0.3127 -0.0967 0.0251  -0.0437 524 THR A CA  
7293  C C   . THR A  498 ? 0.3748 0.3357 0.3133 -0.0904 0.0256  -0.0405 524 THR A C   
7294  O O   . THR A  498 ? 0.3893 0.3458 0.3274 -0.0934 0.0274  -0.0417 524 THR A O   
7295  C CB  . THR A  498 ? 0.4220 0.3710 0.3452 -0.0982 0.0328  -0.0492 524 THR A CB  
7296  O OG1 . THR A  498 ? 0.4364 0.3816 0.3637 -0.0895 0.0365  -0.0481 524 THR A OG1 
7297  C CG2 . THR A  498 ? 0.4400 0.3886 0.3534 -0.1056 0.0332  -0.0534 524 THR A CG2 
7305  N N   . GLU A  499 ? 0.3537 0.3182 0.2994 -0.0821 0.0244  -0.0367 525 GLU A N   
7306  C CA  . GLU A  499 ? 0.3510 0.3142 0.3039 -0.0756 0.0252  -0.0337 525 GLU A CA  
7307  C C   . GLU A  499 ? 0.3535 0.3227 0.3106 -0.0775 0.0212  -0.0310 525 GLU A C   
7308  O O   . GLU A  499 ? 0.3603 0.3252 0.3206 -0.0749 0.0235  -0.0300 525 GLU A O   
7309  C CB  . GLU A  499 ? 0.3609 0.3287 0.3201 -0.0672 0.0237  -0.0301 525 GLU A CB  
7310  C CG  . GLU A  499 ? 0.4101 0.3721 0.3673 -0.0636 0.0286  -0.0321 525 GLU A CG  
7311  C CD  . GLU A  499 ? 0.4347 0.3981 0.3858 -0.0676 0.0284  -0.0347 525 GLU A CD  
7312  O OE1 . GLU A  499 ? 0.4137 0.3847 0.3633 -0.0720 0.0232  -0.0337 525 GLU A OE1 
7313  O OE2 . GLU A  499 ? 0.4751 0.4321 0.4230 -0.0663 0.0336  -0.0375 525 GLU A OE2 
7320  N N   . PHE A  500 ? 0.3501 0.3293 0.3073 -0.0816 0.0154  -0.0295 526 PHE A N   
7321  C CA  . PHE A  500 ? 0.3504 0.3372 0.3124 -0.0831 0.0113  -0.0267 526 PHE A CA  
7322  C C   . PHE A  500 ? 0.3675 0.3557 0.3247 -0.0927 0.0104  -0.0293 526 PHE A C   
7323  O O   . PHE A  500 ? 0.3724 0.3694 0.3335 -0.0948 0.0062  -0.0268 526 PHE A O   
7324  C CB  . PHE A  500 ? 0.3410 0.3393 0.3084 -0.0796 0.0050  -0.0222 526 PHE A CB  
7325  C CG  . PHE A  500 ? 0.3420 0.3396 0.3145 -0.0707 0.0056  -0.0196 526 PHE A CG  
7326  C CD1 . PHE A  500 ? 0.3452 0.3427 0.3239 -0.0653 0.0061  -0.0170 526 PHE A CD1 
7327  C CD2 . PHE A  500 ? 0.3485 0.3454 0.3191 -0.0683 0.0059  -0.0200 526 PHE A CD2 
7328  C CE1 . PHE A  500 ? 0.3497 0.3468 0.3326 -0.0576 0.0065  -0.0149 526 PHE A CE1 
7329  C CE2 . PHE A  500 ? 0.3558 0.3525 0.3310 -0.0608 0.0064  -0.0178 526 PHE A CE2 
7330  C CZ  . PHE A  500 ? 0.3486 0.3456 0.3298 -0.0556 0.0065  -0.0153 526 PHE A CZ  
7340  N N   . SER A  501 ? 0.3845 0.3640 0.3335 -0.0985 0.0146  -0.0342 527 SER A N   
7341  C CA  . SER A  501 ? 0.4000 0.3803 0.3434 -0.1085 0.0140  -0.0373 527 SER A CA  
7342  C C   . SER A  501 ? 0.3964 0.3768 0.3430 -0.1113 0.0145  -0.0368 527 SER A C   
7343  O O   . SER A  501 ? 0.4038 0.3904 0.3486 -0.1190 0.0116  -0.0376 527 SER A O   
7344  C CB  . SER A  501 ? 0.4476 0.4167 0.3810 -0.1136 0.0194  -0.0432 527 SER A CB  
7345  O OG  . SER A  501 ? 0.5081 0.4640 0.4411 -0.1088 0.0263  -0.0450 527 SER A OG  
7351  N N   . ALA A  502 ? 0.3888 0.3629 0.3400 -0.1053 0.0179  -0.0353 528 ALA A N   
7352  C CA  . ALA A  502 ? 0.3826 0.3566 0.3369 -0.1078 0.0186  -0.0344 528 ALA A CA  
7353  C C   . ALA A  502 ? 0.3662 0.3546 0.3292 -0.1054 0.0125  -0.0293 528 ALA A C   
7354  O O   . ALA A  502 ? 0.3572 0.3493 0.3227 -0.1094 0.0118  -0.0286 528 ALA A O   
7355  C CB  . ALA A  502 ? 0.3913 0.3528 0.3466 -0.1023 0.0248  -0.0344 528 ALA A CB  
7361  N N   . ILE A  503 ? 0.3593 0.3557 0.3270 -0.0991 0.0084  -0.0258 529 ILE A N   
7362  C CA  . ILE A  503 ? 0.3532 0.3628 0.3287 -0.0962 0.0028  -0.0210 529 ILE A CA  
7363  C C   . ILE A  503 ? 0.3550 0.3736 0.3294 -0.0970 -0.0024 -0.0199 529 ILE A C   
7364  O O   . ILE A  503 ? 0.3473 0.3688 0.3250 -0.0903 -0.0045 -0.0171 529 ILE A O   
7365  C CB  . ILE A  503 ? 0.3625 0.3712 0.3450 -0.0865 0.0036  -0.0173 529 ILE A CB  
7366  C CG1 . ILE A  503 ? 0.3817 0.3830 0.3626 -0.0801 0.0061  -0.0178 529 ILE A CG1 
7367  C CG2 . ILE A  503 ? 0.3696 0.3725 0.3539 -0.0867 0.0076  -0.0174 529 ILE A CG2 
7368  C CD1 . ILE A  503 ? 0.3965 0.3994 0.3841 -0.0710 0.0057  -0.0140 529 ILE A CD1 
7380  N N   . PRO A  504 ? 0.3592 0.3814 0.3281 -0.1054 -0.0043 -0.0222 530 PRO A N   
7381  C CA  . PRO A  504 ? 0.3601 0.3895 0.3266 -0.1063 -0.0089 -0.0212 530 PRO A CA  
7382  C C   . PRO A  504 ? 0.3528 0.3968 0.3260 -0.1041 -0.0155 -0.0161 530 PRO A C   
7383  O O   . PRO A  504 ? 0.3621 0.4118 0.3335 -0.1042 -0.0194 -0.0145 530 PRO A O   
7384  C CB  . PRO A  504 ? 0.3734 0.4008 0.3309 -0.1165 -0.0081 -0.0258 530 PRO A CB  
7385  C CG  . PRO A  504 ? 0.3796 0.4060 0.3379 -0.1219 -0.0063 -0.0274 530 PRO A CG  
7386  C CD  . PRO A  504 ? 0.3581 0.3772 0.3218 -0.1148 -0.0022 -0.0261 530 PRO A CD  
7394  N N   . HIS A  505 ? 0.3338 0.3837 0.3145 -0.1021 -0.0167 -0.0133 531 HIS A N   
7395  C CA  . HIS A  505 ? 0.3187 0.3824 0.3063 -0.0995 -0.0226 -0.0083 531 HIS A CA  
7396  C C   . HIS A  505 ? 0.2941 0.3581 0.2887 -0.0895 -0.0229 -0.0045 531 HIS A C   
7397  O O   . HIS A  505 ? 0.2894 0.3629 0.2909 -0.0863 -0.0263 -0.0006 531 HIS A O   
7398  C CB  . HIS A  505 ? 0.3349 0.4074 0.3262 -0.1050 -0.0242 -0.0078 531 HIS A CB  
7399  C CG  . HIS A  505 ? 0.3928 0.4647 0.3767 -0.1156 -0.0237 -0.0119 531 HIS A CG  
7400  N ND1 . HIS A  505 ? 0.4259 0.5038 0.4047 -0.1204 -0.0276 -0.0122 531 HIS A ND1 
7401  C CD2 . HIS A  505 ? 0.4212 0.4861 0.4012 -0.1222 -0.0195 -0.0161 531 HIS A CD2 
7402  C CE1 . HIS A  505 ? 0.4401 0.5151 0.4122 -0.1299 -0.0258 -0.0167 531 HIS A CE1 
7403  N NE2 . HIS A  505 ? 0.4412 0.5080 0.4137 -0.1315 -0.0209 -0.0192 531 HIS A NE2 
7411  N N   . VAL A  506 ? 0.2792 0.3331 0.2717 -0.0844 -0.0196 -0.0056 532 VAL A N   
7412  C CA  . VAL A  506 ? 0.2713 0.3254 0.2695 -0.0754 -0.0202 -0.0024 532 VAL A CA  
7413  C C   . VAL A  506 ? 0.2613 0.3241 0.2609 -0.0733 -0.0256 0.0011  532 VAL A C   
7414  O O   . VAL A  506 ? 0.2652 0.3283 0.2594 -0.0768 -0.0272 0.0002  532 VAL A O   
7415  C CB  . VAL A  506 ? 0.2786 0.3212 0.2740 -0.0711 -0.0157 -0.0044 532 VAL A CB  
7416  C CG1 . VAL A  506 ? 0.2799 0.3236 0.2802 -0.0627 -0.0170 -0.0012 532 VAL A CG1 
7417  C CG2 . VAL A  506 ? 0.2850 0.3187 0.2794 -0.0720 -0.0103 -0.0071 532 VAL A CG2 
7427  N N   . LYS A  507 ? 0.2468 0.3165 0.2534 -0.0682 -0.0283 0.0051  533 LYS A N   
7428  C CA  . LYS A  507 ? 0.2506 0.3282 0.2595 -0.0653 -0.0332 0.0089  533 LYS A CA  
7429  C C   . LYS A  507 ? 0.2506 0.3234 0.2608 -0.0578 -0.0328 0.0105  533 LYS A C   
7430  O O   . LYS A  507 ? 0.2568 0.3314 0.2655 -0.0564 -0.0356 0.0124  533 LYS A O   
7431  C CB  . LYS A  507 ? 0.2730 0.3617 0.2892 -0.0641 -0.0362 0.0124  533 LYS A CB  
7432  C CG  . LYS A  507 ? 0.3318 0.4272 0.3480 -0.0717 -0.0370 0.0113  533 LYS A CG  
7433  C CD  . LYS A  507 ? 0.3788 0.4814 0.3910 -0.0774 -0.0412 0.0118  533 LYS A CD  
7434  C CE  . LYS A  507 ? 0.4230 0.5343 0.4359 -0.0852 -0.0425 0.0110  533 LYS A CE  
7435  N NZ  . LYS A  507 ? 0.4410 0.5644 0.4631 -0.0826 -0.0451 0.0150  533 LYS A NZ  
7449  N N   . TYR A  508 ? 0.2408 0.3079 0.2539 -0.0532 -0.0294 0.0099  534 TYR A N   
7450  C CA  . TYR A  508 ? 0.2395 0.3025 0.2542 -0.0463 -0.0288 0.0111  534 TYR A CA  
7451  C C   . TYR A  508 ? 0.2257 0.2790 0.2379 -0.0454 -0.0240 0.0080  534 TYR A C   
7452  O O   . TYR A  508 ? 0.2166 0.2673 0.2306 -0.0451 -0.0211 0.0070  534 TYR A O   
7453  C CB  . TYR A  508 ? 0.2413 0.3093 0.2631 -0.0408 -0.0300 0.0143  534 TYR A CB  
7454  C CG  . TYR A  508 ? 0.2571 0.3224 0.2805 -0.0342 -0.0305 0.0160  534 TYR A CG  
7455  C CD1 . TYR A  508 ? 0.2749 0.3322 0.2964 -0.0315 -0.0274 0.0141  534 TYR A CD1 
7456  C CD2 . TYR A  508 ? 0.2693 0.3401 0.2965 -0.0303 -0.0336 0.0194  534 TYR A CD2 
7457  C CE1 . TYR A  508 ? 0.2880 0.3433 0.3109 -0.0260 -0.0278 0.0154  534 TYR A CE1 
7458  C CE2 . TYR A  508 ? 0.2862 0.3537 0.3145 -0.0245 -0.0336 0.0206  534 TYR A CE2 
7459  C CZ  . TYR A  508 ? 0.3018 0.3617 0.3278 -0.0227 -0.0309 0.0185  534 TYR A CZ  
7460  O OH  . TYR A  508 ? 0.3274 0.3841 0.3540 -0.0178 -0.0310 0.0194  534 TYR A OH  
7470  N N   . LEU A  509 ? 0.2201 0.2682 0.2279 -0.0452 -0.0231 0.0066  535 LEU A N   
7471  C CA  . LEU A  509 ? 0.2270 0.2666 0.2324 -0.0441 -0.0187 0.0038  535 LEU A CA  
7472  C C   . LEU A  509 ? 0.2195 0.2569 0.2266 -0.0381 -0.0185 0.0050  535 LEU A C   
7473  O O   . LEU A  509 ? 0.2127 0.2510 0.2179 -0.0378 -0.0205 0.0058  535 LEU A O   
7474  C CB  . LEU A  509 ? 0.2281 0.2640 0.2269 -0.0495 -0.0171 0.0007  535 LEU A CB  
7475  C CG  . LEU A  509 ? 0.2429 0.2701 0.2388 -0.0484 -0.0122 -0.0023 535 LEU A CG  
7476  C CD1 . LEU A  509 ? 0.2475 0.2700 0.2455 -0.0468 -0.0084 -0.0033 535 LEU A CD1 
7477  C CD2 . LEU A  509 ? 0.2497 0.2737 0.2387 -0.0540 -0.0106 -0.0055 535 LEU A CD2 
7489  N N   . ASP A  510 ? 0.2137 0.2479 0.2237 -0.0338 -0.0159 0.0049  536 ASP A N   
7490  C CA  . ASP A  510 ? 0.2116 0.2439 0.2231 -0.0286 -0.0156 0.0057  536 ASP A CA  
7491  C C   . ASP A  510 ? 0.2076 0.2335 0.2166 -0.0281 -0.0115 0.0032  536 ASP A C   
7492  O O   . ASP A  510 ? 0.1971 0.2194 0.2066 -0.0275 -0.0083 0.0022  536 ASP A O   
7493  C CB  . ASP A  510 ? 0.2242 0.2588 0.2407 -0.0237 -0.0162 0.0079  536 ASP A CB  
7494  C CG  . ASP A  510 ? 0.2567 0.2899 0.2746 -0.0187 -0.0162 0.0087  536 ASP A CG  
7495  O OD1 . ASP A  510 ? 0.2813 0.3110 0.2971 -0.0184 -0.0144 0.0072  536 ASP A OD1 
7496  O OD2 . ASP A  510 ? 0.2557 0.2914 0.2768 -0.0152 -0.0177 0.0106  536 ASP A OD2 
7501  N N   . LEU A  511 ? 0.2114 0.2360 0.2175 -0.0286 -0.0114 0.0023  537 LEU A N   
7502  C CA  . LEU A  511 ? 0.2232 0.2429 0.2276 -0.0277 -0.0075 0.0001  537 LEU A CA  
7503  C C   . LEU A  511 ? 0.2195 0.2401 0.2259 -0.0234 -0.0079 0.0012  537 LEU A C   
7504  O O   . LEU A  511 ? 0.2156 0.2341 0.2205 -0.0230 -0.0056 -0.0003 537 LEU A O   
7505  C CB  . LEU A  511 ? 0.2328 0.2502 0.2318 -0.0326 -0.0061 -0.0024 537 LEU A CB  
7506  C CG  . LEU A  511 ? 0.2616 0.2764 0.2573 -0.0376 -0.0044 -0.0046 537 LEU A CG  
7507  C CD1 . LEU A  511 ? 0.2671 0.2813 0.2569 -0.0430 -0.0043 -0.0068 537 LEU A CD1 
7508  C CD2 . LEU A  511 ? 0.2723 0.2807 0.2682 -0.0361 0.0006  -0.0064 537 LEU A CD2 
7520  N N   . THR A  512 ? 0.2093 0.2331 0.2192 -0.0201 -0.0106 0.0035  538 THR A N   
7521  C CA  . THR A  512 ? 0.2037 0.2286 0.2149 -0.0169 -0.0115 0.0044  538 THR A CA  
7522  C C   . THR A  512 ? 0.1991 0.2222 0.2121 -0.0133 -0.0084 0.0037  538 THR A C   
7523  O O   . THR A  512 ? 0.1753 0.1962 0.1893 -0.0122 -0.0059 0.0033  538 THR A O   
7524  C CB  . THR A  512 ? 0.2277 0.2554 0.2416 -0.0144 -0.0147 0.0067  538 THR A CB  
7525  O OG1 . THR A  512 ? 0.2549 0.2828 0.2718 -0.0115 -0.0138 0.0074  538 THR A OG1 
7526  C CG2 . THR A  512 ? 0.2254 0.2555 0.2382 -0.0170 -0.0179 0.0080  538 THR A CG2 
7534  N N   . ASN A  513 ? 0.2007 0.2251 0.2142 -0.0117 -0.0086 0.0038  539 ASN A N   
7535  C CA  . ASN A  513 ? 0.2049 0.2296 0.2209 -0.0079 -0.0065 0.0037  539 ASN A CA  
7536  C C   . ASN A  513 ? 0.1993 0.2208 0.2147 -0.0076 -0.0023 0.0022  539 ASN A C   
7537  O O   . ASN A  513 ? 0.2117 0.2323 0.2293 -0.0042 -0.0003 0.0028  539 ASN A O   
7538  C CB  . ASN A  513 ? 0.2216 0.2477 0.2406 -0.0042 -0.0076 0.0055  539 ASN A CB  
7539  C CG  . ASN A  513 ? 0.2625 0.2910 0.2819 -0.0039 -0.0112 0.0067  539 ASN A CG  
7540  O OD1 . ASN A  513 ? 0.2923 0.3211 0.3116 -0.0047 -0.0133 0.0076  539 ASN A OD1 
7541  N ND2 . ASN A  513 ? 0.2727 0.3032 0.2927 -0.0026 -0.0119 0.0067  539 ASN A ND2 
7548  N N   . ASN A  514 ? 0.1940 0.2135 0.2062 -0.0110 -0.0007 0.0003  540 ASN A N   
7549  C CA  . ASN A  514 ? 0.1860 0.2017 0.1971 -0.0109 0.0038  -0.0016 540 ASN A CA  
7550  C C   . ASN A  514 ? 0.1885 0.2062 0.1990 -0.0112 0.0051  -0.0027 540 ASN A C   
7551  O O   . ASN A  514 ? 0.1883 0.2103 0.2003 -0.0105 0.0026  -0.0016 540 ASN A O   
7552  C CB  . ASN A  514 ? 0.1914 0.2028 0.1986 -0.0152 0.0050  -0.0033 540 ASN A CB  
7553  C CG  . ASN A  514 ? 0.2172 0.2264 0.2257 -0.0143 0.0053  -0.0024 540 ASN A CG  
7554  O OD1 . ASN A  514 ? 0.2229 0.2291 0.2330 -0.0109 0.0084  -0.0021 540 ASN A OD1 
7555  N ND2 . ASN A  514 ? 0.2163 0.2271 0.2243 -0.0171 0.0024  -0.0016 540 ASN A ND2 
7562  N N   . ARG A  515 ? 0.1904 0.2049 0.1989 -0.0121 0.0092  -0.0049 541 ARG A N   
7563  C CA  . ARG A  515 ? 0.2007 0.2170 0.2083 -0.0127 0.0111  -0.0063 541 ARG A CA  
7564  C C   . ARG A  515 ? 0.2020 0.2142 0.2038 -0.0179 0.0130  -0.0090 541 ARG A C   
7565  O O   . ARG A  515 ? 0.2113 0.2217 0.2116 -0.0180 0.0171  -0.0112 541 ARG A O   
7566  C CB  . ARG A  515 ? 0.2395 0.2558 0.2505 -0.0078 0.0153  -0.0064 541 ARG A CB  
7567  C CG  . ARG A  515 ? 0.3066 0.3270 0.3230 -0.0026 0.0138  -0.0037 541 ARG A CG  
7568  C CD  . ARG A  515 ? 0.3697 0.3880 0.3888 0.0025  0.0181  -0.0034 541 ARG A CD  
7569  N NE  . ARG A  515 ? 0.4476 0.4687 0.4685 0.0046  0.0214  -0.0042 541 ARG A NE  
7570  C CZ  . ARG A  515 ? 0.4792 0.5070 0.5051 0.0088  0.0214  -0.0025 541 ARG A CZ  
7571  N NH1 . ARG A  515 ? 0.4629 0.4934 0.4906 0.0105  0.0249  -0.0034 541 ARG A NH1 
7572  N NH2 . ARG A  515 ? 0.4806 0.5130 0.5097 0.0112  0.0179  0.0001  541 ARG A NH2 
7586  N N   . LEU A  516 ? 0.2006 0.2118 0.1991 -0.0221 0.0101  -0.0090 542 LEU A N   
7587  C CA  . LEU A  516 ? 0.2062 0.2137 0.1988 -0.0274 0.0116  -0.0116 542 LEU A CA  
7588  C C   . LEU A  516 ? 0.2182 0.2270 0.2073 -0.0302 0.0128  -0.0132 542 LEU A C   
7589  O O   . LEU A  516 ? 0.2126 0.2260 0.2029 -0.0300 0.0104  -0.0117 542 LEU A O   
7590  C CB  . LEU A  516 ? 0.2101 0.2183 0.2006 -0.0312 0.0075  -0.0107 542 LEU A CB  
7591  C CG  . LEU A  516 ? 0.2348 0.2405 0.2273 -0.0299 0.0076  -0.0100 542 LEU A CG  
7592  C CD1 . LEU A  516 ? 0.2457 0.2546 0.2381 -0.0326 0.0029  -0.0083 542 LEU A CD1 
7593  C CD2 . LEU A  516 ? 0.2444 0.2432 0.2334 -0.0319 0.0124  -0.0131 542 LEU A CD2 
7605  N N   . ASP A  517 ? 0.2213 0.2256 0.2061 -0.0325 0.0171  -0.0164 543 ASP A N   
7606  C CA  . ASP A  517 ? 0.2262 0.2311 0.2071 -0.0353 0.0192  -0.0184 543 ASP A CA  
7607  C C   . ASP A  517 ? 0.2439 0.2473 0.2177 -0.0420 0.0174  -0.0197 543 ASP A C   
7608  O O   . ASP A  517 ? 0.2555 0.2537 0.2248 -0.0449 0.0201  -0.0225 543 ASP A O   
7609  C CB  . ASP A  517 ? 0.2303 0.2309 0.2111 -0.0329 0.0258  -0.0212 543 ASP A CB  
7610  C CG  . ASP A  517 ? 0.2654 0.2666 0.2426 -0.0350 0.0291  -0.0235 543 ASP A CG  
7611  O OD1 . ASP A  517 ? 0.2746 0.2799 0.2492 -0.0387 0.0261  -0.0228 543 ASP A OD1 
7612  O OD2 . ASP A  517 ? 0.2718 0.2694 0.2488 -0.0330 0.0349  -0.0260 543 ASP A OD2 
7617  N N   . PHE A  518 ? 0.2494 0.2573 0.2220 -0.0445 0.0126  -0.0175 544 PHE A N   
7618  C CA  . PHE A  518 ? 0.2587 0.2666 0.2247 -0.0507 0.0102  -0.0180 544 PHE A CA  
7619  C C   . PHE A  518 ? 0.2758 0.2821 0.2355 -0.0544 0.0137  -0.0209 544 PHE A C   
7620  O O   . PHE A  518 ? 0.2809 0.2906 0.2394 -0.0555 0.0126  -0.0198 544 PHE A O   
7621  C CB  . PHE A  518 ? 0.2518 0.2647 0.2189 -0.0512 0.0041  -0.0141 544 PHE A CB  
7622  C CG  . PHE A  518 ? 0.2616 0.2757 0.2343 -0.0478 0.0011  -0.0116 544 PHE A CG  
7623  C CD1 . PHE A  518 ? 0.2785 0.2918 0.2502 -0.0500 -0.0004 -0.0117 544 PHE A CD1 
7624  C CD2 . PHE A  518 ? 0.2735 0.2896 0.2525 -0.0425 0.0003  -0.0095 544 PHE A CD2 
7625  C CE1 . PHE A  518 ? 0.2864 0.3011 0.2634 -0.0468 -0.0027 -0.0095 544 PHE A CE1 
7626  C CE2 . PHE A  518 ? 0.2830 0.3001 0.2666 -0.0394 -0.0022 -0.0074 544 PHE A CE2 
7627  C CZ  . PHE A  518 ? 0.2858 0.3022 0.2685 -0.0414 -0.0035 -0.0074 544 PHE A CZ  
7637  N N   . ASP A  519 ? 0.2839 0.2847 0.2397 -0.0563 0.0185  -0.0248 545 ASP A N   
7638  C CA  . ASP A  519 ? 0.2959 0.2944 0.2455 -0.0595 0.0229  -0.0283 545 ASP A CA  
7639  C C   . ASP A  519 ? 0.3135 0.3073 0.2547 -0.0658 0.0243  -0.0318 545 ASP A C   
7640  O O   . ASP A  519 ? 0.3234 0.3125 0.2598 -0.0675 0.0298  -0.0358 545 ASP A O   
7641  C CB  . ASP A  519 ? 0.3104 0.3061 0.2638 -0.0543 0.0291  -0.0302 545 ASP A CB  
7642  C CG  . ASP A  519 ? 0.3462 0.3416 0.2953 -0.0561 0.0337  -0.0330 545 ASP A CG  
7643  O OD1 . ASP A  519 ? 0.3512 0.3508 0.2971 -0.0596 0.0313  -0.0320 545 ASP A OD1 
7644  O OD2 . ASP A  519 ? 0.3636 0.3543 0.3125 -0.0539 0.0400  -0.0361 545 ASP A OD2 
7649  N N   . ASN A  520 ? 0.3117 0.3070 0.2511 -0.0694 0.0196  -0.0304 546 ASN A N   
7650  C CA  . ASN A  520 ? 0.3193 0.3111 0.2505 -0.0762 0.0203  -0.0337 546 ASN A CA  
7651  C C   . ASN A  520 ? 0.3189 0.3167 0.2482 -0.0805 0.0134  -0.0307 546 ASN A C   
7652  O O   . ASN A  520 ? 0.3141 0.3150 0.2491 -0.0780 0.0094  -0.0274 546 ASN A O   
7653  C CB  . ASN A  520 ? 0.3385 0.3233 0.2704 -0.0757 0.0240  -0.0365 546 ASN A CB  
7654  C CG  . ASN A  520 ? 0.4071 0.3876 0.3299 -0.0831 0.0258  -0.0407 546 ASN A CG  
7655  O OD1 . ASN A  520 ? 0.3879 0.3715 0.3083 -0.0878 0.0212  -0.0398 546 ASN A OD1 
7656  N ND2 . ASN A  520 ? 0.4912 0.4641 0.4085 -0.0845 0.0323  -0.0456 546 ASN A ND2 
7663  N N   . ALA A  521 ? 0.3209 0.3204 0.2420 -0.0867 0.0121  -0.0316 547 ALA A N   
7664  C CA  . ALA A  521 ? 0.3242 0.3301 0.2430 -0.0907 0.0054  -0.0284 547 ALA A CA  
7665  C C   . ALA A  521 ? 0.3248 0.3316 0.2442 -0.0934 0.0027  -0.0284 547 ALA A C   
7666  O O   . ALA A  521 ? 0.3310 0.3444 0.2510 -0.0951 -0.0032 -0.0248 547 ALA A O   
7667  C CB  . ALA A  521 ? 0.3243 0.3314 0.2333 -0.0971 0.0052  -0.0297 547 ALA A CB  
7673  N N   . SER A  522 ? 0.3226 0.3231 0.2415 -0.0941 0.0071  -0.0323 548 SER A N   
7674  C CA  . SER A  522 ? 0.3227 0.3238 0.2420 -0.0973 0.0051  -0.0327 548 SER A CA  
7675  C C   . SER A  522 ? 0.3110 0.3123 0.2400 -0.0912 0.0044  -0.0302 548 SER A C   
7676  O O   . SER A  522 ? 0.3006 0.3020 0.2308 -0.0934 0.0035  -0.0306 548 SER A O   
7677  C CB  . SER A  522 ? 0.3502 0.3433 0.2622 -0.1028 0.0104  -0.0388 548 SER A CB  
7678  O OG  . SER A  522 ? 0.3915 0.3835 0.2940 -0.1083 0.0120  -0.0417 548 SER A OG  
7684  N N   . ALA A  523 ? 0.2989 0.3006 0.2347 -0.0839 0.0048  -0.0276 549 ALA A N   
7685  C CA  . ALA A  523 ? 0.2929 0.2949 0.2373 -0.0780 0.0043  -0.0251 549 ALA A CA  
7686  C C   . ALA A  523 ? 0.2851 0.2938 0.2330 -0.0791 -0.0014 -0.0218 549 ALA A C   
7687  O O   . ALA A  523 ? 0.2823 0.2977 0.2295 -0.0807 -0.0064 -0.0189 549 ALA A O   
7688  C CB  . ALA A  523 ? 0.2884 0.2921 0.2387 -0.0710 0.0040  -0.0223 549 ALA A CB  
7694  N N   . LEU A  524 ? 0.2788 0.2857 0.2304 -0.0783 -0.0005 -0.0221 550 LEU A N   
7695  C CA  . LEU A  524 ? 0.2838 0.2974 0.2399 -0.0787 -0.0053 -0.0189 550 LEU A CA  
7696  C C   . LEU A  524 ? 0.3034 0.3230 0.2550 -0.0860 -0.0093 -0.0188 550 LEU A C   
7697  O O   . LEU A  524 ? 0.3080 0.3339 0.2639 -0.0864 -0.0129 -0.0163 550 LEU A O   
7698  C CB  . LEU A  524 ? 0.2775 0.2968 0.2404 -0.0723 -0.0092 -0.0140 550 LEU A CB  
7699  C CG  . LEU A  524 ? 0.2791 0.2944 0.2472 -0.0651 -0.0062 -0.0134 550 LEU A CG  
7700  C CD1 . LEU A  524 ? 0.2750 0.2956 0.2483 -0.0601 -0.0102 -0.0092 550 LEU A CD1 
7701  C CD2 . LEU A  524 ? 0.2907 0.3023 0.2625 -0.0632 -0.0034 -0.0142 550 LEU A CD2 
7713  N N   . THR A  525 ? 0.3141 0.3323 0.2574 -0.0919 -0.0084 -0.0217 551 THR A N   
7714  C CA  . THR A  525 ? 0.3235 0.3481 0.2617 -0.0992 -0.0125 -0.0216 551 THR A CA  
7715  C C   . THR A  525 ? 0.3279 0.3527 0.2653 -0.1047 -0.0121 -0.0239 551 THR A C   
7716  O O   . THR A  525 ? 0.3271 0.3599 0.2628 -0.1101 -0.0165 -0.0227 551 THR A O   
7717  C CB  . THR A  525 ? 0.3490 0.3715 0.2777 -0.1041 -0.0112 -0.0244 551 THR A CB  
7718  O OG1 . THR A  525 ? 0.3642 0.3765 0.2877 -0.1064 -0.0046 -0.0301 551 THR A OG1 
7719  C CG2 . THR A  525 ? 0.3596 0.3834 0.2889 -0.0996 -0.0123 -0.0216 551 THR A CG2 
7727  N N   . GLU A  526 ? 0.3318 0.3485 0.2709 -0.1034 -0.0071 -0.0266 552 GLU A N   
7728  C CA  . GLU A  526 ? 0.3381 0.3546 0.2774 -0.1083 -0.0065 -0.0284 552 GLU A CA  
7729  C C   . GLU A  526 ? 0.3326 0.3591 0.2806 -0.1057 -0.0115 -0.0235 552 GLU A C   
7730  O O   . GLU A  526 ? 0.3378 0.3679 0.2863 -0.1108 -0.0127 -0.0240 552 GLU A O   
7731  C CB  . GLU A  526 ? 0.3579 0.3619 0.2966 -0.1069 0.0006  -0.0322 552 GLU A CB  
7732  C CG  . GLU A  526 ? 0.3585 0.3599 0.3056 -0.0979 0.0023  -0.0294 552 GLU A CG  
7733  C CD  . GLU A  526 ? 0.3787 0.3760 0.3268 -0.0911 0.0047  -0.0290 552 GLU A CD  
7734  O OE1 . GLU A  526 ? 0.3497 0.3509 0.2952 -0.0914 0.0024  -0.0282 552 GLU A OE1 
7735  O OE2 . GLU A  526 ? 0.3927 0.3832 0.3440 -0.0856 0.0089  -0.0292 552 GLU A OE2 
7742  N N   . LEU A  527 ? 0.3135 0.3442 0.2684 -0.0980 -0.0141 -0.0189 553 LEU A N   
7743  C CA  . LEU A  527 ? 0.2967 0.3366 0.2598 -0.0947 -0.0185 -0.0143 553 LEU A CA  
7744  C C   . LEU A  527 ? 0.3067 0.3579 0.2694 -0.0973 -0.0249 -0.0110 553 LEU A C   
7745  O O   . LEU A  527 ? 0.2959 0.3515 0.2621 -0.0921 -0.0282 -0.0069 553 LEU A O   
7746  C CB  . LEU A  527 ? 0.2816 0.3196 0.2517 -0.0853 -0.0178 -0.0113 553 LEU A CB  
7747  C CG  . LEU A  527 ? 0.2834 0.3115 0.2549 -0.0818 -0.0120 -0.0136 553 LEU A CG  
7748  C CD1 . LEU A  527 ? 0.2865 0.3142 0.2644 -0.0730 -0.0121 -0.0106 553 LEU A CD1 
7749  C CD2 . LEU A  527 ? 0.2869 0.3145 0.2604 -0.0848 -0.0105 -0.0146 553 LEU A CD2 
7761  N N   . SER A  528 ? 0.3213 0.3774 0.2797 -0.1055 -0.0268 -0.0125 554 SER A N   
7762  C CA  . SER A  528 ? 0.3355 0.4029 0.2925 -0.1088 -0.0329 -0.0094 554 SER A CA  
7763  C C   . SER A  528 ? 0.3203 0.3988 0.2865 -0.1037 -0.0381 -0.0034 554 SER A C   
7764  O O   . SER A  528 ? 0.3239 0.4096 0.2899 -0.1027 -0.0428 0.0004  554 SER A O   
7765  C CB  . SER A  528 ? 0.3706 0.4412 0.3211 -0.1191 -0.0337 -0.0127 554 SER A CB  
7766  O OG  . SER A  528 ? 0.4220 0.4994 0.3777 -0.1218 -0.0352 -0.0120 554 SER A OG  
7772  N N   . ASP A  529 ? 0.3008 0.3803 0.2746 -0.1003 -0.0370 -0.0024 555 ASP A N   
7773  C CA  . ASP A  529 ? 0.2835 0.3730 0.2661 -0.0951 -0.0412 0.0030  555 ASP A CA  
7774  C C   . ASP A  529 ? 0.2557 0.3410 0.2433 -0.0854 -0.0403 0.0057  555 ASP A C   
7775  O O   . ASP A  529 ? 0.2488 0.3403 0.2440 -0.0803 -0.0426 0.0096  555 ASP A O   
7776  C CB  . ASP A  529 ? 0.3120 0.4058 0.3002 -0.0971 -0.0405 0.0027  555 ASP A CB  
7777  C CG  . ASP A  529 ? 0.4100 0.5102 0.3946 -0.1069 -0.0420 0.0006  555 ASP A CG  
7778  O OD1 . ASP A  529 ? 0.4171 0.5218 0.3960 -0.1116 -0.0452 0.0007  555 ASP A OD1 
7779  O OD2 . ASP A  529 ? 0.4554 0.5564 0.4427 -0.1101 -0.0401 -0.0010 555 ASP A OD2 
7784  N N   . LEU A  530 ? 0.2469 0.3221 0.2304 -0.0830 -0.0371 0.0036  556 LEU A N   
7785  C CA  . LEU A  530 ? 0.2385 0.3097 0.2264 -0.0747 -0.0361 0.0057  556 LEU A CA  
7786  C C   . LEU A  530 ? 0.2450 0.3234 0.2361 -0.0705 -0.0411 0.0109  556 LEU A C   
7787  O O   . LEU A  530 ? 0.2528 0.3343 0.2394 -0.0732 -0.0440 0.0122  556 LEU A O   
7788  C CB  . LEU A  530 ? 0.2362 0.2970 0.2187 -0.0738 -0.0321 0.0026  556 LEU A CB  
7789  C CG  . LEU A  530 ? 0.2471 0.3024 0.2337 -0.0661 -0.0299 0.0035  556 LEU A CG  
7790  C CD1 . LEU A  530 ? 0.2463 0.2997 0.2384 -0.0632 -0.0273 0.0030  556 LEU A CD1 
7791  C CD2 . LEU A  530 ? 0.2490 0.2959 0.2304 -0.0662 -0.0262 0.0004  556 LEU A CD2 
7803  N N   . GLU A  531 ? 0.2294 0.3100 0.2279 -0.0638 -0.0418 0.0139  557 GLU A N   
7804  C CA  . GLU A  531 ? 0.2276 0.3138 0.2300 -0.0588 -0.0458 0.0189  557 GLU A CA  
7805  C C   . GLU A  531 ? 0.2215 0.3006 0.2253 -0.0519 -0.0441 0.0197  557 GLU A C   
7806  O O   . GLU A  531 ? 0.2203 0.2999 0.2235 -0.0491 -0.0466 0.0227  557 GLU A O   
7807  C CB  . GLU A  531 ? 0.2453 0.3410 0.2554 -0.0568 -0.0481 0.0220  557 GLU A CB  
7808  C CG  . GLU A  531 ? 0.3029 0.4076 0.3122 -0.0638 -0.0505 0.0218  557 GLU A CG  
7809  C CD  . GLU A  531 ? 0.3666 0.4842 0.3831 -0.0622 -0.0545 0.0262  557 GLU A CD  
7810  O OE1 . GLU A  531 ? 0.3594 0.4789 0.3816 -0.0550 -0.0555 0.0298  557 GLU A OE1 
7811  O OE2 . GLU A  531 ? 0.3982 0.5242 0.4144 -0.0684 -0.0565 0.0259  557 GLU A OE2 
7818  N N   . VAL A  532 ? 0.2120 0.2847 0.2177 -0.0494 -0.0401 0.0172  558 VAL A N   
7819  C CA  . VAL A  532 ? 0.2161 0.2828 0.2232 -0.0434 -0.0385 0.0176  558 VAL A CA  
7820  C C   . VAL A  532 ? 0.2190 0.2774 0.2227 -0.0445 -0.0340 0.0135  558 VAL A C   
7821  O O   . VAL A  532 ? 0.2185 0.2750 0.2226 -0.0464 -0.0312 0.0110  558 VAL A O   
7822  C CB  . VAL A  532 ? 0.2227 0.2915 0.2369 -0.0377 -0.0384 0.0195  558 VAL A CB  
7823  C CG1 . VAL A  532 ? 0.2374 0.2999 0.2524 -0.0321 -0.0368 0.0196  558 VAL A CG1 
7824  C CG2 . VAL A  532 ? 0.2210 0.2987 0.2393 -0.0361 -0.0425 0.0237  558 VAL A CG2 
7834  N N   . LEU A  533 ? 0.2174 0.2708 0.2177 -0.0433 -0.0332 0.0129  559 LEU A N   
7835  C CA  . LEU A  533 ? 0.2174 0.2637 0.2150 -0.0436 -0.0289 0.0095  559 LEU A CA  
7836  C C   . LEU A  533 ? 0.2171 0.2601 0.2167 -0.0383 -0.0283 0.0104  559 LEU A C   
7837  O O   . LEU A  533 ? 0.2234 0.2668 0.2215 -0.0374 -0.0305 0.0123  559 LEU A O   
7838  C CB  . LEU A  533 ? 0.2213 0.2657 0.2118 -0.0491 -0.0283 0.0073  559 LEU A CB  
7839  C CG  . LEU A  533 ? 0.2391 0.2765 0.2266 -0.0495 -0.0236 0.0036  559 LEU A CG  
7840  C CD1 . LEU A  533 ? 0.2477 0.2814 0.2373 -0.0488 -0.0197 0.0012  559 LEU A CD1 
7841  C CD2 . LEU A  533 ? 0.2455 0.2816 0.2256 -0.0552 -0.0230 0.0015  559 LEU A CD2 
7853  N N   . ASP A  534 ? 0.2048 0.2443 0.2073 -0.0349 -0.0252 0.0090  560 ASP A N   
7854  C CA  . ASP A  534 ? 0.2066 0.2436 0.2110 -0.0302 -0.0245 0.0096  560 ASP A CA  
7855  C C   . ASP A  534 ? 0.2070 0.2392 0.2092 -0.0305 -0.0207 0.0066  560 ASP A C   
7856  O O   . ASP A  534 ? 0.2048 0.2345 0.2080 -0.0299 -0.0176 0.0049  560 ASP A O   
7857  C CB  . ASP A  534 ? 0.2152 0.2533 0.2250 -0.0254 -0.0246 0.0110  560 ASP A CB  
7858  C CG  . ASP A  534 ? 0.2545 0.2915 0.2660 -0.0210 -0.0254 0.0123  560 ASP A CG  
7859  O OD1 . ASP A  534 ? 0.2466 0.2812 0.2553 -0.0215 -0.0252 0.0118  560 ASP A OD1 
7860  O OD2 . ASP A  534 ? 0.2552 0.2934 0.2704 -0.0173 -0.0260 0.0137  560 ASP A OD2 
7865  N N   . LEU A  535 ? 0.2096 0.2404 0.2085 -0.0315 -0.0207 0.0063  561 LEU A N   
7866  C CA  . LEU A  535 ? 0.2174 0.2448 0.2147 -0.0315 -0.0171 0.0038  561 LEU A CA  
7867  C C   . LEU A  535 ? 0.2141 0.2413 0.2139 -0.0277 -0.0171 0.0047  561 LEU A C   
7868  O O   . LEU A  535 ? 0.2217 0.2476 0.2201 -0.0280 -0.0150 0.0032  561 LEU A O   
7869  C CB  . LEU A  535 ? 0.2298 0.2565 0.2214 -0.0364 -0.0167 0.0024  561 LEU A CB  
7870  C CG  . LEU A  535 ? 0.2572 0.2846 0.2451 -0.0413 -0.0171 0.0014  561 LEU A CG  
7871  C CD1 . LEU A  535 ? 0.2645 0.2910 0.2460 -0.0460 -0.0165 -0.0001 561 LEU A CD1 
7872  C CD2 . LEU A  535 ? 0.2659 0.2904 0.2547 -0.0416 -0.0136 -0.0011 561 LEU A CD2 
7884  N N   . SER A  536 ? 0.2049 0.2335 0.2081 -0.0242 -0.0194 0.0069  562 SER A N   
7885  C CA  . SER A  536 ? 0.2048 0.2331 0.2098 -0.0211 -0.0197 0.0075  562 SER A CA  
7886  C C   . SER A  536 ? 0.2021 0.2296 0.2089 -0.0190 -0.0164 0.0057  562 SER A C   
7887  O O   . SER A  536 ? 0.1916 0.2183 0.1998 -0.0180 -0.0142 0.0047  562 SER A O   
7888  C CB  . SER A  536 ? 0.2197 0.2491 0.2280 -0.0176 -0.0219 0.0096  562 SER A CB  
7889  O OG  . SER A  536 ? 0.2444 0.2749 0.2518 -0.0184 -0.0250 0.0117  562 SER A OG  
7895  N N   . TYR A  537 ? 0.1975 0.2254 0.2045 -0.0182 -0.0161 0.0055  563 TYR A N   
7896  C CA  . TYR A  537 ? 0.2043 0.2329 0.2137 -0.0157 -0.0134 0.0043  563 TYR A CA  
7897  C C   . TYR A  537 ? 0.1960 0.2233 0.2047 -0.0165 -0.0096 0.0023  563 TYR A C   
7898  O O   . TYR A  537 ? 0.1970 0.2237 0.2080 -0.0137 -0.0074 0.0019  563 TYR A O   
7899  C CB  . TYR A  537 ? 0.2287 0.2581 0.2419 -0.0115 -0.0138 0.0053  563 TYR A CB  
7900  C CG  . TYR A  537 ? 0.2685 0.2985 0.2821 -0.0103 -0.0168 0.0068  563 TYR A CG  
7901  C CD1 . TYR A  537 ? 0.2943 0.3256 0.3085 -0.0097 -0.0172 0.0067  563 TYR A CD1 
7902  C CD2 . TYR A  537 ? 0.2995 0.3289 0.3133 -0.0098 -0.0191 0.0083  563 TYR A CD2 
7903  C CE1 . TYR A  537 ? 0.3167 0.3475 0.3307 -0.0088 -0.0196 0.0077  563 TYR A CE1 
7904  C CE2 . TYR A  537 ? 0.3189 0.3480 0.3329 -0.0084 -0.0213 0.0095  563 TYR A CE2 
7905  C CZ  . TYR A  537 ? 0.3400 0.3692 0.3538 -0.0080 -0.0215 0.0090  563 TYR A CZ  
7906  O OH  . TYR A  537 ? 0.3902 0.4179 0.4036 -0.0069 -0.0234 0.0099  563 TYR A OH  
7916  N N   . ASN A  538 ? 0.1783 0.2047 0.1832 -0.0203 -0.0087 0.0010  564 ASN A N   
7917  C CA  . ASN A  538 ? 0.1855 0.2102 0.1889 -0.0214 -0.0047 -0.0013 564 ASN A CA  
7918  C C   . ASN A  538 ? 0.1960 0.2223 0.1977 -0.0232 -0.0036 -0.0022 564 ASN A C   
7919  O O   . ASN A  538 ? 0.2090 0.2339 0.2067 -0.0266 -0.0019 -0.0038 564 ASN A O   
7920  C CB  . ASN A  538 ? 0.1896 0.2115 0.1890 -0.0252 -0.0043 -0.0024 564 ASN A CB  
7921  C CG  . ASN A  538 ? 0.2098 0.2298 0.2111 -0.0236 -0.0037 -0.0023 564 ASN A CG  
7922  O OD1 . ASN A  538 ? 0.2092 0.2266 0.2116 -0.0216 -0.0001 -0.0036 564 ASN A OD1 
7923  N ND2 . ASN A  538 ? 0.2106 0.2317 0.2122 -0.0244 -0.0068 -0.0008 564 ASN A ND2 
7930  N N   . SER A  539 ? 0.1914 0.2208 0.1959 -0.0213 -0.0047 -0.0011 565 SER A N   
7931  C CA  . SER A  539 ? 0.2078 0.2395 0.2111 -0.0233 -0.0039 -0.0016 565 SER A CA  
7932  C C   . SER A  539 ? 0.2163 0.2495 0.2209 -0.0223 0.0007  -0.0036 565 SER A C   
7933  O O   . SER A  539 ? 0.2261 0.2610 0.2290 -0.0248 0.0020  -0.0045 565 SER A O   
7934  C CB  . SER A  539 ? 0.2202 0.2550 0.2263 -0.0219 -0.0063 -0.0001 565 SER A CB  
7935  O OG  . SER A  539 ? 0.2470 0.2844 0.2579 -0.0176 -0.0050 -0.0001 565 SER A OG  
7941  N N   . HIS A  540 ? 0.2067 0.2391 0.2143 -0.0186 0.0033  -0.0042 566 HIS A N   
7942  C CA  . HIS A  540 ? 0.2160 0.2498 0.2257 -0.0163 0.0079  -0.0057 566 HIS A CA  
7943  C C   . HIS A  540 ? 0.2234 0.2571 0.2296 -0.0199 0.0108  -0.0078 566 HIS A C   
7944  O O   . HIS A  540 ? 0.2243 0.2627 0.2327 -0.0193 0.0124  -0.0081 566 HIS A O   
7945  C CB  . HIS A  540 ? 0.2267 0.2566 0.2377 -0.0130 0.0109  -0.0063 566 HIS A CB  
7946  C CG  . HIS A  540 ? 0.2504 0.2820 0.2646 -0.0092 0.0154  -0.0071 566 HIS A CG  
7947  N ND1 . HIS A  540 ? 0.2711 0.3055 0.2907 -0.0038 0.0158  -0.0053 566 HIS A ND1 
7948  C CD2 . HIS A  540 ? 0.2637 0.2949 0.2767 -0.0099 0.0197  -0.0092 566 HIS A CD2 
7949  C CE1 . HIS A  540 ? 0.2767 0.3126 0.2984 -0.0011 0.0201  -0.0062 566 HIS A CE1 
7950  N NE2 . HIS A  540 ? 0.2821 0.3161 0.3002 -0.0046 0.0228  -0.0086 566 HIS A NE2 
7958  N N   . TYR A  541 ? 0.2182 0.2472 0.2188 -0.0237 0.0114  -0.0093 567 TYR A N   
7959  C CA  . TYR A  541 ? 0.2184 0.2468 0.2147 -0.0272 0.0146  -0.0116 567 TYR A CA  
7960  C C   . TYR A  541 ? 0.2154 0.2456 0.2078 -0.0320 0.0116  -0.0107 567 TYR A C   
7961  O O   . TYR A  541 ? 0.2176 0.2498 0.2082 -0.0341 0.0139  -0.0119 567 TYR A O   
7962  C CB  . TYR A  541 ? 0.2197 0.2417 0.2114 -0.0290 0.0176  -0.0141 567 TYR A CB  
7963  C CG  . TYR A  541 ? 0.2292 0.2487 0.2240 -0.0244 0.0223  -0.0154 567 TYR A CG  
7964  C CD1 . TYR A  541 ? 0.2419 0.2631 0.2384 -0.0223 0.0271  -0.0169 567 TYR A CD1 
7965  C CD2 . TYR A  541 ? 0.2364 0.2527 0.2335 -0.0215 0.0218  -0.0145 567 TYR A CD2 
7966  C CE1 . TYR A  541 ? 0.2556 0.2746 0.2556 -0.0171 0.0314  -0.0175 567 TYR A CE1 
7967  C CE2 . TYR A  541 ? 0.2524 0.2659 0.2523 -0.0168 0.0261  -0.0151 567 TYR A CE2 
7968  C CZ  . TYR A  541 ? 0.2682 0.2829 0.2696 -0.0145 0.0309  -0.0166 567 TYR A CZ  
7969  O OH  . TYR A  541 ? 0.2857 0.2976 0.2904 -0.0091 0.0352  -0.0166 567 TYR A OH  
7979  N N   . PHE A  542 ? 0.2128 0.2424 0.2040 -0.0334 0.0067  -0.0085 568 PHE A N   
7980  C CA  . PHE A  542 ? 0.2204 0.2511 0.2079 -0.0375 0.0038  -0.0072 568 PHE A CA  
7981  C C   . PHE A  542 ? 0.2263 0.2616 0.2168 -0.0370 0.0042  -0.0065 568 PHE A C   
7982  O O   . PHE A  542 ? 0.2327 0.2689 0.2195 -0.0409 0.0040  -0.0063 568 PHE A O   
7983  C CB  . PHE A  542 ? 0.2153 0.2447 0.2023 -0.0377 -0.0013 -0.0045 568 PHE A CB  
7984  C CG  . PHE A  542 ? 0.2233 0.2496 0.2063 -0.0400 -0.0028 -0.0046 568 PHE A CG  
7985  C CD1 . PHE A  542 ? 0.2379 0.2630 0.2144 -0.0449 -0.0023 -0.0055 568 PHE A CD1 
7986  C CD2 . PHE A  542 ? 0.2340 0.2592 0.2196 -0.0376 -0.0046 -0.0037 568 PHE A CD2 
7987  C CE1 . PHE A  542 ? 0.2514 0.2747 0.2243 -0.0474 -0.0040 -0.0055 568 PHE A CE1 
7988  C CE2 . PHE A  542 ? 0.2446 0.2681 0.2269 -0.0401 -0.0061 -0.0036 568 PHE A CE2 
7989  C CZ  . PHE A  542 ? 0.2424 0.2652 0.2185 -0.0450 -0.0059 -0.0046 568 PHE A CZ  
7999  N N   . ARG A  543 ? 0.2221 0.2607 0.2189 -0.0326 0.0045  -0.0060 569 ARG A N   
8000  C CA  . ARG A  543 ? 0.2376 0.2818 0.2380 -0.0322 0.0047  -0.0055 569 ARG A CA  
8001  C C   . ARG A  543 ? 0.2404 0.2880 0.2408 -0.0334 0.0092  -0.0074 569 ARG A C   
8002  O O   . ARG A  543 ? 0.2462 0.2987 0.2483 -0.0349 0.0093  -0.0069 569 ARG A O   
8003  C CB  . ARG A  543 ? 0.2622 0.3097 0.2692 -0.0271 0.0043  -0.0047 569 ARG A CB  
8004  C CG  . ARG A  543 ? 0.3387 0.3840 0.3463 -0.0257 0.0000  -0.0028 569 ARG A CG  
8005  C CD  . ARG A  543 ? 0.3881 0.4370 0.4017 -0.0208 0.0000  -0.0022 569 ARG A CD  
8006  N NE  . ARG A  543 ? 0.4564 0.5031 0.4703 -0.0193 -0.0036 -0.0007 569 ARG A NE  
8007  C CZ  . ARG A  543 ? 0.5049 0.5522 0.5185 -0.0206 -0.0068 0.0005  569 ARG A CZ  
8008  N NH1 . ARG A  543 ? 0.5162 0.5612 0.5301 -0.0188 -0.0096 0.0016  569 ARG A NH1 
8009  N NH2 . ARG A  543 ? 0.5088 0.5587 0.5216 -0.0238 -0.0070 0.0003  569 ARG A NH2 
8023  N N   . ILE A  544 ? 0.2278 0.2732 0.2270 -0.0326 0.0132  -0.0095 570 ILE A N   
8024  C CA  . ILE A  544 ? 0.2229 0.2715 0.2226 -0.0328 0.0183  -0.0116 570 ILE A CA  
8025  C C   . ILE A  544 ? 0.2291 0.2754 0.2214 -0.0386 0.0192  -0.0127 570 ILE A C   
8026  O O   . ILE A  544 ? 0.2359 0.2766 0.2228 -0.0406 0.0195  -0.0139 570 ILE A O   
8027  C CB  . ILE A  544 ? 0.2267 0.2728 0.2284 -0.0285 0.0227  -0.0135 570 ILE A CB  
8028  C CG1 . ILE A  544 ? 0.2327 0.2796 0.2405 -0.0228 0.0213  -0.0118 570 ILE A CG1 
8029  C CG2 . ILE A  544 ? 0.2296 0.2799 0.2333 -0.0275 0.0284  -0.0154 570 ILE A CG2 
8030  C CD1 . ILE A  544 ? 0.2569 0.2986 0.2649 -0.0193 0.0248  -0.0132 570 ILE A CD1 
8042  N N   . ALA A  545 ? 0.2256 0.2764 0.2175 -0.0416 0.0197  -0.0124 571 ALA A N   
8043  C CA  . ALA A  545 ? 0.2360 0.2848 0.2205 -0.0474 0.0205  -0.0131 571 ALA A CA  
8044  C C   . ALA A  545 ? 0.2422 0.2887 0.2230 -0.0480 0.0259  -0.0164 571 ALA A C   
8045  O O   . ALA A  545 ? 0.2504 0.2923 0.2235 -0.0522 0.0258  -0.0173 571 ALA A O   
8046  C CB  . ALA A  545 ? 0.2376 0.2919 0.2227 -0.0504 0.0207  -0.0121 571 ALA A CB  
8052  N N   . GLY A  546 ? 0.2309 0.2806 0.2170 -0.0438 0.0306  -0.0182 572 GLY A N   
8053  C CA  . GLY A  546 ? 0.2390 0.2865 0.2222 -0.0438 0.0367  -0.0216 572 GLY A CA  
8054  C C   . GLY A  546 ? 0.2461 0.2854 0.2250 -0.0433 0.0380  -0.0237 572 GLY A C   
8055  O O   . GLY A  546 ? 0.2548 0.2909 0.2295 -0.0444 0.0432  -0.0269 572 GLY A O   
8059  N N   . VAL A  547 ? 0.2387 0.2745 0.2188 -0.0416 0.0340  -0.0221 573 VAL A N   
8060  C CA  . VAL A  547 ? 0.2436 0.2717 0.2193 -0.0420 0.0350  -0.0241 573 VAL A CA  
8061  C C   . VAL A  547 ? 0.2510 0.2760 0.2189 -0.0481 0.0309  -0.0236 573 VAL A C   
8062  O O   . VAL A  547 ? 0.2513 0.2793 0.2187 -0.0504 0.0264  -0.0209 573 VAL A O   
8063  C CB  . VAL A  547 ? 0.2478 0.2738 0.2291 -0.0366 0.0340  -0.0230 573 VAL A CB  
8064  C CG1 . VAL A  547 ? 0.2560 0.2864 0.2453 -0.0303 0.0375  -0.0228 573 VAL A CG1 
8065  C CG2 . VAL A  547 ? 0.2446 0.2717 0.2276 -0.0368 0.0273  -0.0196 573 VAL A CG2 
8075  N N   . THR A  548 ? 0.2553 0.2743 0.2170 -0.0509 0.0325  -0.0262 574 THR A N   
8076  C CA  . THR A  548 ? 0.2632 0.2801 0.2174 -0.0568 0.0285  -0.0257 574 THR A CA  
8077  C C   . THR A  548 ? 0.2658 0.2820 0.2225 -0.0556 0.0229  -0.0229 574 THR A C   
8078  O O   . THR A  548 ? 0.2643 0.2793 0.2266 -0.0510 0.0233  -0.0226 574 THR A O   
8079  C CB  . THR A  548 ? 0.2807 0.2922 0.2265 -0.0610 0.0325  -0.0298 574 THR A CB  
8080  O OG1 . THR A  548 ? 0.2875 0.2939 0.2354 -0.0577 0.0361  -0.0322 574 THR A OG1 
8081  C CG2 . THR A  548 ? 0.2883 0.3012 0.2305 -0.0630 0.0376  -0.0323 574 THR A CG2 
8089  N N   . HIS A  549 ? 0.2588 0.2763 0.2118 -0.0594 0.0176  -0.0204 575 HIS A N   
8090  C CA  . HIS A  549 ? 0.2528 0.2704 0.2081 -0.0584 0.0122  -0.0175 575 HIS A CA  
8091  C C   . HIS A  549 ? 0.2596 0.2761 0.2074 -0.0640 0.0091  -0.0172 575 HIS A C   
8092  O O   . HIS A  549 ? 0.2635 0.2816 0.2060 -0.0680 0.0080  -0.0164 575 HIS A O   
8093  C CB  . HIS A  549 ? 0.2467 0.2682 0.2070 -0.0558 0.0081  -0.0135 575 HIS A CB  
8094  C CG  . HIS A  549 ? 0.2479 0.2722 0.2141 -0.0519 0.0108  -0.0136 575 HIS A CG  
8095  N ND1 . HIS A  549 ? 0.2573 0.2845 0.2223 -0.0537 0.0126  -0.0139 575 HIS A ND1 
8096  C CD2 . HIS A  549 ? 0.2588 0.2842 0.2323 -0.0465 0.0118  -0.0134 575 HIS A CD2 
8097  C CE1 . HIS A  549 ? 0.2619 0.2922 0.2336 -0.0495 0.0145  -0.0138 575 HIS A CE1 
8098  N NE2 . HIS A  549 ? 0.2635 0.2929 0.2404 -0.0450 0.0141  -0.0136 575 HIS A NE2 
8106  N N   . HIS A  550 ? 0.2606 0.2753 0.2083 -0.0644 0.0074  -0.0174 576 HIS A N   
8107  C CA  . HIS A  550 ? 0.2699 0.2847 0.2110 -0.0699 0.0045  -0.0173 576 HIS A CA  
8108  C C   . HIS A  550 ? 0.2773 0.2941 0.2218 -0.0687 -0.0009 -0.0141 576 HIS A C   
8109  O O   . HIS A  550 ? 0.2662 0.2814 0.2150 -0.0661 -0.0002 -0.0148 576 HIS A O   
8110  C CB  . HIS A  550 ? 0.2813 0.2915 0.2170 -0.0733 0.0089  -0.0221 576 HIS A CB  
8111  C CG  . HIS A  550 ? 0.2923 0.3005 0.2225 -0.0757 0.0140  -0.0254 576 HIS A CG  
8112  N ND1 . HIS A  550 ? 0.3236 0.3334 0.2458 -0.0813 0.0129  -0.0254 576 HIS A ND1 
8113  C CD2 . HIS A  550 ? 0.2999 0.3052 0.2318 -0.0730 0.0202  -0.0285 576 HIS A CD2 
8114  C CE1 . HIS A  550 ? 0.3279 0.3357 0.2471 -0.0820 0.0186  -0.0287 576 HIS A CE1 
8115  N NE2 . HIS A  550 ? 0.3204 0.3256 0.2455 -0.0769 0.0232  -0.0307 576 HIS A NE2 
8123  N N   . LEU A  551 ? 0.2865 0.3068 0.2288 -0.0708 -0.0060 -0.0105 577 LEU A N   
8124  C CA  . LEU A  551 ? 0.3000 0.3231 0.2454 -0.0698 -0.0111 -0.0072 577 LEU A CA  
8125  C C   . LEU A  551 ? 0.3116 0.3372 0.2505 -0.0755 -0.0143 -0.0066 577 LEU A C   
8126  O O   . LEU A  551 ? 0.3196 0.3490 0.2607 -0.0750 -0.0191 -0.0031 577 LEU A O   
8127  C CB  . LEU A  551 ? 0.3029 0.3283 0.2527 -0.0659 -0.0146 -0.0028 577 LEU A CB  
8128  C CG  . LEU A  551 ? 0.3204 0.3445 0.2774 -0.0602 -0.0126 -0.0029 577 LEU A CG  
8129  C CD1 . LEU A  551 ? 0.3278 0.3534 0.2878 -0.0574 -0.0159 0.0010  577 LEU A CD1 
8130  C CD2 . LEU A  551 ? 0.3258 0.3492 0.2882 -0.0569 -0.0120 -0.0038 577 LEU A CD2 
8142  N N   . GLU A  552 ? 0.3029 0.3268 0.2342 -0.0810 -0.0116 -0.0101 578 GLU A N   
8143  C CA  . GLU A  552 ? 0.3140 0.3406 0.2382 -0.0872 -0.0145 -0.0100 578 GLU A CA  
8144  C C   . GLU A  552 ? 0.3160 0.3451 0.2426 -0.0882 -0.0171 -0.0098 578 GLU A C   
8145  O O   . GLU A  552 ? 0.3230 0.3570 0.2462 -0.0921 -0.0215 -0.0077 578 GLU A O   
8146  C CB  . GLU A  552 ? 0.3424 0.3657 0.2577 -0.0929 -0.0101 -0.0149 578 GLU A CB  
8147  C CG  . GLU A  552 ? 0.3883 0.4098 0.3000 -0.0932 -0.0069 -0.0157 578 GLU A CG  
8148  C CD  . GLU A  552 ? 0.4541 0.4711 0.3701 -0.0889 -0.0009 -0.0187 578 GLU A CD  
8149  O OE1 . GLU A  552 ? 0.4803 0.4959 0.4037 -0.0842 -0.0001 -0.0189 578 GLU A OE1 
8150  O OE2 . GLU A  552 ? 0.4638 0.4792 0.3761 -0.0901 0.0030  -0.0207 578 GLU A OE2 
8157  N N   . PHE A  553 ? 0.3149 0.3408 0.2469 -0.0852 -0.0144 -0.0119 579 PHE A N   
8158  C CA  . PHE A  553 ? 0.3121 0.3400 0.2464 -0.0866 -0.0161 -0.0122 579 PHE A CA  
8159  C C   . PHE A  553 ? 0.3227 0.3579 0.2616 -0.0849 -0.0225 -0.0069 579 PHE A C   
8160  O O   . PHE A  553 ? 0.3382 0.3773 0.2771 -0.0880 -0.0249 -0.0066 579 PHE A O   
8161  C CB  . PHE A  553 ? 0.2999 0.3228 0.2399 -0.0827 -0.0120 -0.0146 579 PHE A CB  
8162  C CG  . PHE A  553 ? 0.2926 0.3153 0.2406 -0.0751 -0.0121 -0.0119 579 PHE A CG  
8163  C CD1 . PHE A  553 ? 0.2952 0.3215 0.2500 -0.0714 -0.0154 -0.0086 579 PHE A CD1 
8164  C CD2 . PHE A  553 ? 0.2984 0.3177 0.2471 -0.0719 -0.0085 -0.0129 579 PHE A CD2 
8165  C CE1 . PHE A  553 ? 0.3020 0.3280 0.2635 -0.0649 -0.0153 -0.0064 579 PHE A CE1 
8166  C CE2 . PHE A  553 ? 0.3027 0.3225 0.2584 -0.0655 -0.0088 -0.0105 579 PHE A CE2 
8167  C CZ  . PHE A  553 ? 0.2990 0.3217 0.2607 -0.0622 -0.0122 -0.0074 579 PHE A CZ  
8177  N N   . ILE A  554 ? 0.3176 0.3545 0.2604 -0.0800 -0.0249 -0.0028 580 ILE A N   
8178  C CA  . ILE A  554 ? 0.3219 0.3650 0.2695 -0.0773 -0.0304 0.0024  580 ILE A CA  
8179  C C   . ILE A  554 ? 0.3267 0.3764 0.2695 -0.0826 -0.0350 0.0045  580 ILE A C   
8180  O O   . ILE A  554 ? 0.3202 0.3759 0.2670 -0.0819 -0.0389 0.0074  580 ILE A O   
8181  C CB  . ILE A  554 ? 0.3285 0.3706 0.2788 -0.0722 -0.0316 0.0060  580 ILE A CB  
8182  C CG1 . ILE A  554 ? 0.3458 0.3834 0.3024 -0.0666 -0.0281 0.0045  580 ILE A CG1 
8183  C CG2 . ILE A  554 ? 0.3324 0.3800 0.2860 -0.0697 -0.0372 0.0116  580 ILE A CG2 
8184  C CD1 . ILE A  554 ? 0.3662 0.4013 0.3233 -0.0634 -0.0275 0.0061  580 ILE A CD1 
8196  N N   . GLN A  555 ? 0.3418 0.3908 0.2760 -0.0880 -0.0345 0.0031  581 GLN A N   
8197  C CA  . GLN A  555 ? 0.3609 0.4163 0.2891 -0.0936 -0.0388 0.0050  581 GLN A CA  
8198  C C   . GLN A  555 ? 0.3727 0.4320 0.3000 -0.0987 -0.0396 0.0026  581 GLN A C   
8199  O O   . GLN A  555 ? 0.3718 0.4390 0.2973 -0.1020 -0.0445 0.0054  581 GLN A O   
8200  C CB  . GLN A  555 ? 0.3978 0.4503 0.3161 -0.0985 -0.0370 0.0030  581 GLN A CB  
8201  C CG  . GLN A  555 ? 0.4765 0.5354 0.3874 -0.1042 -0.0414 0.0054  581 GLN A CG  
8202  C CD  . GLN A  555 ? 0.5468 0.6020 0.4482 -0.1082 -0.0390 0.0037  581 GLN A CD  
8203  O OE1 . GLN A  555 ? 0.5519 0.6006 0.4502 -0.1097 -0.0332 -0.0017 581 GLN A OE1 
8204  N NE2 . GLN A  555 ? 0.5558 0.6152 0.4524 -0.1098 -0.0431 0.0082  581 GLN A NE2 
8213  N N   . ASN A  556 ? 0.3757 0.4296 0.3035 -0.0998 -0.0348 -0.0026 582 ASN A N   
8214  C CA  . ASN A  556 ? 0.3896 0.4457 0.3154 -0.1057 -0.0348 -0.0056 582 ASN A CA  
8215  C C   . ASN A  556 ? 0.3855 0.4489 0.3191 -0.1041 -0.0386 -0.0026 582 ASN A C   
8216  O O   . ASN A  556 ? 0.4024 0.4702 0.3340 -0.1099 -0.0399 -0.0041 582 ASN A O   
8217  C CB  . ASN A  556 ? 0.4272 0.4739 0.3511 -0.1069 -0.0280 -0.0118 582 ASN A CB  
8218  C CG  . ASN A  556 ? 0.5124 0.5528 0.4279 -0.1100 -0.0239 -0.0156 582 ASN A CG  
8219  O OD1 . ASN A  556 ? 0.5080 0.5454 0.4240 -0.1058 -0.0224 -0.0145 582 ASN A OD1 
8220  N ND2 . ASN A  556 ? 0.5780 0.6169 0.4847 -0.1177 -0.0224 -0.0199 582 ASN A ND2 
8227  N N   . PHE A  557 ? 0.3594 0.4243 0.3016 -0.0966 -0.0401 0.0014  583 PHE A N   
8228  C CA  . PHE A  557 ? 0.3516 0.4233 0.3017 -0.0943 -0.0430 0.0042  583 PHE A CA  
8229  C C   . PHE A  557 ? 0.3518 0.4346 0.3032 -0.0948 -0.0496 0.0097  583 PHE A C   
8230  O O   . PHE A  557 ? 0.3565 0.4404 0.3080 -0.0911 -0.0521 0.0138  583 PHE A O   
8231  C CB  . PHE A  557 ? 0.3388 0.4070 0.2974 -0.0860 -0.0414 0.0057  583 PHE A CB  
8232  C CG  . PHE A  557 ? 0.3375 0.3957 0.2959 -0.0846 -0.0352 0.0011  583 PHE A CG  
8233  C CD1 . PHE A  557 ? 0.3382 0.3938 0.2978 -0.0868 -0.0321 -0.0023 583 PHE A CD1 
8234  C CD2 . PHE A  557 ? 0.3452 0.3968 0.3024 -0.0809 -0.0324 0.0005  583 PHE A CD2 
8235  C CE1 . PHE A  557 ? 0.3472 0.3935 0.3067 -0.0849 -0.0264 -0.0061 583 PHE A CE1 
8236  C CE2 . PHE A  557 ? 0.3601 0.4035 0.3177 -0.0792 -0.0268 -0.0034 583 PHE A CE2 
8237  C CZ  . PHE A  557 ? 0.3526 0.3933 0.3114 -0.0808 -0.0239 -0.0064 583 PHE A CZ  
8247  N N   . THR A  558 ? 0.3405 0.4318 0.2935 -0.0990 -0.0524 0.0101  584 THR A N   
8248  C CA  . THR A  558 ? 0.3372 0.4406 0.2923 -0.0993 -0.0589 0.0156  584 THR A CA  
8249  C C   . THR A  558 ? 0.3248 0.4336 0.2907 -0.0919 -0.0611 0.0202  584 THR A C   
8250  O O   . THR A  558 ? 0.3334 0.4509 0.3020 -0.0897 -0.0661 0.0257  584 THR A O   
8251  C CB  . THR A  558 ? 0.3583 0.4697 0.3089 -0.1083 -0.0613 0.0139  584 THR A CB  
8252  O OG1 . THR A  558 ? 0.3814 0.4950 0.3377 -0.1096 -0.0599 0.0118  584 THR A OG1 
8253  C CG2 . THR A  558 ? 0.3622 0.4674 0.3014 -0.1159 -0.0586 0.0087  584 THR A CG2 
8261  N N   . ASN A  559 ? 0.3080 0.4121 0.2800 -0.0881 -0.0575 0.0182  585 ASN A N   
8262  C CA  . ASN A  559 ? 0.3042 0.4134 0.2863 -0.0813 -0.0590 0.0222  585 ASN A CA  
8263  C C   . ASN A  559 ? 0.2916 0.3918 0.2772 -0.0733 -0.0560 0.0226  585 ASN A C   
8264  O O   . ASN A  559 ? 0.2855 0.3877 0.2788 -0.0677 -0.0561 0.0247  585 ASN A O   
8265  C CB  . ASN A  559 ? 0.3321 0.4448 0.3192 -0.0836 -0.0575 0.0200  585 ASN A CB  
8266  C CG  . ASN A  559 ? 0.4069 0.5283 0.3911 -0.0921 -0.0600 0.0189  585 ASN A CG  
8267  O OD1 . ASN A  559 ? 0.4493 0.5660 0.4283 -0.0987 -0.0569 0.0137  585 ASN A OD1 
8268  N ND2 . ASN A  559 ? 0.4113 0.5456 0.3991 -0.0921 -0.0655 0.0237  585 ASN A ND2 
8275  N N   . LEU A  560 ? 0.2793 0.3700 0.2593 -0.0730 -0.0532 0.0203  586 LEU A N   
8276  C CA  . LEU A  560 ? 0.2751 0.3581 0.2582 -0.0663 -0.0505 0.0204  586 LEU A CA  
8277  C C   . LEU A  560 ? 0.2647 0.3507 0.2514 -0.0603 -0.0540 0.0260  586 LEU A C   
8278  O O   . LEU A  560 ? 0.2622 0.3498 0.2445 -0.0614 -0.0569 0.0287  586 LEU A O   
8279  C CB  . LEU A  560 ? 0.2788 0.3523 0.2553 -0.0678 -0.0467 0.0169  586 LEU A CB  
8280  C CG  . LEU A  560 ? 0.2873 0.3531 0.2667 -0.0618 -0.0434 0.0161  586 LEU A CG  
8281  C CD1 . LEU A  560 ? 0.2952 0.3584 0.2798 -0.0596 -0.0400 0.0136  586 LEU A CD1 
8282  C CD2 . LEU A  560 ? 0.3026 0.3613 0.2756 -0.0638 -0.0404 0.0133  586 LEU A CD2 
8294  N N   . LYS A  561 ? 0.2421 0.3285 0.2363 -0.0541 -0.0537 0.0277  587 LYS A N   
8295  C CA  . LYS A  561 ? 0.2422 0.3305 0.2403 -0.0478 -0.0564 0.0327  587 LYS A CA  
8296  C C   . LYS A  561 ? 0.2334 0.3123 0.2317 -0.0426 -0.0538 0.0322  587 LYS A C   
8297  O O   . LYS A  561 ? 0.2299 0.3068 0.2269 -0.0398 -0.0554 0.0353  587 LYS A O   
8298  C CB  . LYS A  561 ? 0.2591 0.3551 0.2657 -0.0441 -0.0579 0.0352  587 LYS A CB  
8299  C CG  . LYS A  561 ? 0.3238 0.4313 0.3316 -0.0484 -0.0613 0.0369  587 LYS A CG  
8300  C CD  . LYS A  561 ? 0.3991 0.5142 0.4161 -0.0443 -0.0621 0.0392  587 LYS A CD  
8301  C CE  . LYS A  561 ? 0.4617 0.5900 0.4812 -0.0483 -0.0659 0.0414  587 LYS A CE  
8302  N NZ  . LYS A  561 ? 0.5072 0.6365 0.5216 -0.0572 -0.0650 0.0371  587 LYS A NZ  
8316  N N   . VAL A  562 ? 0.2156 0.2892 0.2159 -0.0413 -0.0497 0.0285  588 VAL A N   
8317  C CA  . VAL A  562 ? 0.2182 0.2843 0.2196 -0.0366 -0.0474 0.0279  588 VAL A CA  
8318  C C   . VAL A  562 ? 0.2224 0.2818 0.2200 -0.0391 -0.0433 0.0233  588 VAL A C   
8319  O O   . VAL A  562 ? 0.2254 0.2846 0.2235 -0.0414 -0.0409 0.0201  588 VAL A O   
8320  C CB  . VAL A  562 ? 0.2214 0.2886 0.2300 -0.0310 -0.0466 0.0287  588 VAL A CB  
8321  C CG1 . VAL A  562 ? 0.2310 0.2908 0.2402 -0.0263 -0.0445 0.0281  588 VAL A CG1 
8322  C CG2 . VAL A  562 ? 0.2219 0.2966 0.2349 -0.0282 -0.0503 0.0333  588 VAL A CG2 
8332  N N   . LEU A  563 ? 0.2177 0.2716 0.2119 -0.0384 -0.0424 0.0230  589 LEU A N   
8333  C CA  . LEU A  563 ? 0.2247 0.2728 0.2158 -0.0400 -0.0385 0.0191  589 LEU A CA  
8334  C C   . LEU A  563 ? 0.2182 0.2616 0.2112 -0.0355 -0.0373 0.0194  589 LEU A C   
8335  O O   . LEU A  563 ? 0.2221 0.2643 0.2138 -0.0341 -0.0392 0.0220  589 LEU A O   
8336  C CB  . LEU A  563 ? 0.2268 0.2741 0.2108 -0.0453 -0.0386 0.0181  589 LEU A CB  
8337  C CG  . LEU A  563 ? 0.2361 0.2779 0.2168 -0.0469 -0.0344 0.0143  589 LEU A CG  
8338  C CD1 . LEU A  563 ? 0.2330 0.2730 0.2154 -0.0474 -0.0307 0.0105  589 LEU A CD1 
8339  C CD2 . LEU A  563 ? 0.2478 0.2893 0.2211 -0.0522 -0.0346 0.0138  589 LEU A CD2 
8351  N N   . ASN A  564 ? 0.2041 0.2446 0.1996 -0.0335 -0.0340 0.0167  590 ASN A N   
8352  C CA  . ASN A  564 ? 0.2032 0.2399 0.2003 -0.0298 -0.0328 0.0166  590 ASN A CA  
8353  C C   . ASN A  564 ? 0.2019 0.2353 0.1965 -0.0315 -0.0293 0.0134  590 ASN A C   
8354  O O   . ASN A  564 ? 0.1976 0.2303 0.1933 -0.0317 -0.0265 0.0108  590 ASN A O   
8355  C CB  . ASN A  564 ? 0.1954 0.2327 0.1983 -0.0250 -0.0323 0.0169  590 ASN A CB  
8356  C CG  . ASN A  564 ? 0.2288 0.2628 0.2330 -0.0212 -0.0319 0.0172  590 ASN A CG  
8357  O OD1 . ASN A  564 ? 0.2515 0.2828 0.2531 -0.0224 -0.0310 0.0164  590 ASN A OD1 
8358  N ND2 . ASN A  564 ? 0.2389 0.2732 0.2472 -0.0170 -0.0321 0.0181  590 ASN A ND2 
8364  N N   . LEU A  565 ? 0.2092 0.2406 0.2003 -0.0329 -0.0295 0.0138  591 LEU A N   
8365  C CA  . LEU A  565 ? 0.2155 0.2446 0.2047 -0.0342 -0.0263 0.0111  591 LEU A CA  
8366  C C   . LEU A  565 ? 0.2177 0.2451 0.2094 -0.0309 -0.0257 0.0114  591 LEU A C   
8367  O O   . LEU A  565 ? 0.2281 0.2544 0.2181 -0.0322 -0.0240 0.0102  591 LEU A O   
8368  C CB  . LEU A  565 ? 0.2261 0.2548 0.2092 -0.0388 -0.0266 0.0112  591 LEU A CB  
8369  C CG  . LEU A  565 ? 0.2533 0.2840 0.2325 -0.0430 -0.0276 0.0110  591 LEU A CG  
8370  C CD1 . LEU A  565 ? 0.2670 0.2972 0.2396 -0.0474 -0.0279 0.0114  591 LEU A CD1 
8371  C CD2 . LEU A  565 ? 0.2682 0.2984 0.2478 -0.0442 -0.0242 0.0074  591 LEU A CD2 
8383  N N   . SER A  566 ? 0.2105 0.2380 0.2063 -0.0269 -0.0270 0.0127  592 SER A N   
8384  C CA  . SER A  566 ? 0.2154 0.2412 0.2129 -0.0243 -0.0268 0.0128  592 SER A CA  
8385  C C   . SER A  566 ? 0.2089 0.2350 0.2083 -0.0234 -0.0237 0.0102  592 SER A C   
8386  O O   . SER A  566 ? 0.1984 0.2256 0.1994 -0.0229 -0.0215 0.0086  592 SER A O   
8387  C CB  . SER A  566 ? 0.2335 0.2590 0.2343 -0.0203 -0.0286 0.0145  592 SER A CB  
8388  O OG  . SER A  566 ? 0.2488 0.2759 0.2535 -0.0176 -0.0272 0.0134  592 SER A OG  
8394  N N   . HIS A  567 ? 0.2031 0.2285 0.2023 -0.0233 -0.0235 0.0101  593 HIS A N   
8395  C CA  . HIS A  567 ? 0.2016 0.2285 0.2032 -0.0221 -0.0211 0.0082  593 HIS A CA  
8396  C C   . HIS A  567 ? 0.2023 0.2307 0.2036 -0.0235 -0.0179 0.0061  593 HIS A C   
8397  O O   . HIS A  567 ? 0.2082 0.2381 0.2126 -0.0211 -0.0157 0.0048  593 HIS A O   
8398  C CB  . HIS A  567 ? 0.2194 0.2471 0.2251 -0.0179 -0.0212 0.0082  593 HIS A CB  
8399  C CG  . HIS A  567 ? 0.2597 0.2853 0.2653 -0.0164 -0.0238 0.0099  593 HIS A CG  
8400  N ND1 . HIS A  567 ? 0.2875 0.3119 0.2921 -0.0170 -0.0244 0.0099  593 HIS A ND1 
8401  C CD2 . HIS A  567 ? 0.2746 0.2990 0.2806 -0.0146 -0.0256 0.0115  593 HIS A CD2 
8402  C CE1 . HIS A  567 ? 0.2962 0.3177 0.3003 -0.0154 -0.0264 0.0114  593 HIS A CE1 
8403  N NE2 . HIS A  567 ? 0.2944 0.3163 0.2998 -0.0136 -0.0271 0.0125  593 HIS A NE2 
8411  N N   . ASN A  568 ? 0.1966 0.2243 0.1939 -0.0273 -0.0176 0.0059  594 ASN A N   
8412  C CA  . ASN A  568 ? 0.2062 0.2345 0.2021 -0.0292 -0.0143 0.0036  594 ASN A CA  
8413  C C   . ASN A  568 ? 0.2206 0.2503 0.2151 -0.0313 -0.0126 0.0027  594 ASN A C   
8414  O O   . ASN A  568 ? 0.2298 0.2603 0.2236 -0.0324 -0.0093 0.0007  594 ASN A O   
8415  C CB  . ASN A  568 ? 0.2074 0.2344 0.1992 -0.0323 -0.0147 0.0034  594 ASN A CB  
8416  C CG  . ASN A  568 ? 0.2343 0.2607 0.2281 -0.0307 -0.0143 0.0029  594 ASN A CG  
8417  O OD1 . ASN A  568 ? 0.2563 0.2826 0.2529 -0.0283 -0.0115 0.0014  594 ASN A OD1 
8418  N ND2 . ASN A  568 ? 0.2164 0.2428 0.2088 -0.0319 -0.0168 0.0042  594 ASN A ND2 
8425  N N   . ASN A  569 ? 0.2204 0.2502 0.2144 -0.0321 -0.0145 0.0042  595 ASN A N   
8426  C CA  . ASN A  569 ? 0.2301 0.2617 0.2231 -0.0346 -0.0129 0.0035  595 ASN A CA  
8427  C C   . ASN A  569 ? 0.2204 0.2514 0.2083 -0.0388 -0.0113 0.0027  595 ASN A C   
8428  O O   . ASN A  569 ? 0.2286 0.2619 0.2164 -0.0402 -0.0082 0.0010  595 ASN A O   
8429  C CB  . ASN A  569 ? 0.2803 0.3161 0.2783 -0.0319 -0.0100 0.0017  595 ASN A CB  
8430  C CG  . ASN A  569 ? 0.4096 0.4479 0.4102 -0.0315 -0.0110 0.0023  595 ASN A CG  
8431  O OD1 . ASN A  569 ? 0.4590 0.4954 0.4598 -0.0305 -0.0139 0.0036  595 ASN A OD1 
8432  N ND2 . ASN A  569 ? 0.4365 0.4794 0.4390 -0.0324 -0.0086 0.0011  595 ASN A ND2 
8439  N N   . ILE A  570 ? 0.2022 0.2304 0.1858 -0.0408 -0.0134 0.0040  596 ILE A N   
8440  C CA  . ILE A  570 ? 0.2057 0.2333 0.1836 -0.0451 -0.0123 0.0034  596 ILE A CA  
8441  C C   . ILE A  570 ? 0.2096 0.2371 0.1840 -0.0485 -0.0125 0.0045  596 ILE A C   
8442  O O   . ILE A  570 ? 0.2043 0.2298 0.1775 -0.0488 -0.0155 0.0072  596 ILE A O   
8443  C CB  . ILE A  570 ? 0.2074 0.2333 0.1820 -0.0463 -0.0151 0.0048  596 ILE A CB  
8444  C CG1 . ILE A  570 ? 0.2088 0.2348 0.1867 -0.0435 -0.0145 0.0035  596 ILE A CG1 
8445  C CG2 . ILE A  570 ? 0.2091 0.2346 0.1766 -0.0514 -0.0144 0.0044  596 ILE A CG2 
8446  C CD1 . ILE A  570 ? 0.2231 0.2488 0.1996 -0.0441 -0.0178 0.0052  596 ILE A CD1 
8458  N N   . TYR A  571 ? 0.2191 0.2485 0.1918 -0.0510 -0.0089 0.0025  597 TYR A N   
8459  C CA  . TYR A  571 ? 0.2209 0.2505 0.1898 -0.0549 -0.0085 0.0034  597 TYR A CA  
8460  C C   . TYR A  571 ? 0.2187 0.2489 0.1822 -0.0590 -0.0055 0.0017  597 TYR A C   
8461  O O   . TYR A  571 ? 0.2157 0.2461 0.1754 -0.0627 -0.0050 0.0026  597 TYR A O   
8462  C CB  . TYR A  571 ? 0.2270 0.2599 0.2006 -0.0540 -0.0070 0.0028  597 TYR A CB  
8463  C CG  . TYR A  571 ? 0.2373 0.2748 0.2148 -0.0527 -0.0024 -0.0002 597 TYR A CG  
8464  C CD1 . TYR A  571 ? 0.2404 0.2794 0.2234 -0.0480 -0.0014 -0.0016 597 TYR A CD1 
8465  C CD2 . TYR A  571 ? 0.2505 0.2915 0.2270 -0.0557 0.0007  -0.0013 597 TYR A CD2 
8466  C CE1 . TYR A  571 ? 0.2504 0.2940 0.2377 -0.0460 0.0027  -0.0039 597 TYR A CE1 
8467  C CE2 . TYR A  571 ? 0.2577 0.3038 0.2389 -0.0537 0.0049  -0.0038 597 TYR A CE2 
8468  C CZ  . TYR A  571 ? 0.2640 0.3114 0.2507 -0.0486 0.0058  -0.0049 597 TYR A CZ  
8469  O OH  . TYR A  571 ? 0.2799 0.3324 0.2717 -0.0459 0.0098  -0.0068 597 TYR A OH  
8479  N N   . THR A  572 ? 0.2171 0.2474 0.1799 -0.0586 -0.0032 -0.0008 598 THR A N   
8480  C CA  . THR A  572 ? 0.2223 0.2527 0.1794 -0.0625 0.0001  -0.0030 598 THR A CA  
8481  C C   . THR A  572 ? 0.2366 0.2649 0.1914 -0.0626 0.0007  -0.0049 598 THR A C   
8482  O O   . THR A  572 ? 0.2421 0.2700 0.2018 -0.0587 0.0013  -0.0061 598 THR A O   
8483  C CB  . THR A  572 ? 0.2279 0.2618 0.1879 -0.0621 0.0052  -0.0056 598 THR A CB  
8484  O OG1 . THR A  572 ? 0.2399 0.2735 0.1938 -0.0660 0.0088  -0.0079 598 THR A OG1 
8485  C CG2 . THR A  572 ? 0.2260 0.2616 0.1934 -0.0568 0.0076  -0.0076 598 THR A CG2 
8493  N N   . LEU A  573 ? 0.2481 0.2751 0.1952 -0.0673 0.0004  -0.0052 599 LEU A N   
8494  C CA  . LEU A  573 ? 0.2585 0.2835 0.2018 -0.0689 0.0011  -0.0074 599 LEU A CA  
8495  C C   . LEU A  573 ? 0.2748 0.2993 0.2113 -0.0733 0.0055  -0.0106 599 LEU A C   
8496  O O   . LEU A  573 ? 0.2780 0.3039 0.2113 -0.0759 0.0066  -0.0099 599 LEU A O   
8497  C CB  . LEU A  573 ? 0.2598 0.2843 0.1997 -0.0708 -0.0044 -0.0043 599 LEU A CB  
8498  C CG  . LEU A  573 ? 0.2617 0.2865 0.2079 -0.0664 -0.0087 -0.0011 599 LEU A CG  
8499  C CD1 . LEU A  573 ? 0.2646 0.2898 0.2073 -0.0683 -0.0138 0.0021  599 LEU A CD1 
8500  C CD2 . LEU A  573 ? 0.2641 0.2884 0.2164 -0.0623 -0.0071 -0.0033 599 LEU A CD2 
8512  N N   . THR A  574 ? 0.2789 0.3011 0.2132 -0.0741 0.0084  -0.0142 600 THR A N   
8513  C CA  . THR A  574 ? 0.3008 0.3217 0.2284 -0.0780 0.0133  -0.0180 600 THR A CA  
8514  C C   . THR A  574 ? 0.3302 0.3501 0.2483 -0.0840 0.0107  -0.0177 600 THR A C   
8515  O O   . THR A  574 ? 0.3405 0.3593 0.2580 -0.0845 0.0080  -0.0176 600 THR A O   
8516  C CB  . THR A  574 ? 0.3027 0.3205 0.2327 -0.0754 0.0184  -0.0224 600 THR A CB  
8517  O OG1 . THR A  574 ? 0.3013 0.3207 0.2404 -0.0693 0.0201  -0.0219 600 THR A OG1 
8518  C CG2 . THR A  574 ? 0.3005 0.3162 0.2239 -0.0787 0.0245  -0.0268 600 THR A CG2 
8526  N N   . ASP A  575 ? 0.3399 0.3607 0.2506 -0.0887 0.0116  -0.0177 601 ASP A N   
8527  C CA  . ASP A  575 ? 0.3640 0.3845 0.2645 -0.0951 0.0096  -0.0175 601 ASP A CA  
8528  C C   . ASP A  575 ? 0.3743 0.3967 0.2736 -0.0961 0.0021  -0.0125 601 ASP A C   
8529  O O   . ASP A  575 ? 0.3857 0.4096 0.2790 -0.0997 -0.0005 -0.0095 601 ASP A O   
8530  C CB  . ASP A  575 ? 0.3869 0.4041 0.2824 -0.0978 0.0131  -0.0227 601 ASP A CB  
8531  C CG  . ASP A  575 ? 0.4342 0.4489 0.3293 -0.0971 0.0208  -0.0278 601 ASP A CG  
8532  O OD1 . ASP A  575 ? 0.4421 0.4587 0.3373 -0.0969 0.0236  -0.0275 601 ASP A OD1 
8533  O OD2 . ASP A  575 ? 0.4614 0.4721 0.3559 -0.0968 0.0244  -0.0320 601 ASP A OD2 
8538  N N   . LYS A  576 ? 0.3666 0.3890 0.2711 -0.0932 -0.0010 -0.0115 602 LYS A N   
8539  C CA  . LYS A  576 ? 0.3674 0.3923 0.2717 -0.0936 -0.0078 -0.0067 602 LYS A CA  
8540  C C   . LYS A  576 ? 0.3467 0.3723 0.2592 -0.0880 -0.0103 -0.0028 602 LYS A C   
8541  O O   . LYS A  576 ? 0.3500 0.3748 0.2704 -0.0832 -0.0094 -0.0037 602 LYS A O   
8542  C CB  . LYS A  576 ? 0.4021 0.4276 0.3068 -0.0944 -0.0099 -0.0078 602 LYS A CB  
8543  C CG  . LYS A  576 ? 0.4756 0.5052 0.3776 -0.0965 -0.0167 -0.0031 602 LYS A CG  
8544  C CD  . LYS A  576 ? 0.5521 0.5834 0.4544 -0.0981 -0.0186 -0.0044 602 LYS A CD  
8545  C CE  . LYS A  576 ? 0.6120 0.6486 0.5097 -0.1018 -0.0246 -0.0007 602 LYS A CE  
8546  N NZ  . LYS A  576 ? 0.6451 0.6850 0.5495 -0.0971 -0.0299 0.0051  602 LYS A NZ  
8560  N N   . TYR A  577 ? 0.3306 0.3570 0.2406 -0.0890 -0.0131 0.0014  603 TYR A N   
8561  C CA  . TYR A  577 ? 0.3346 0.3607 0.2509 -0.0845 -0.0152 0.0050  603 TYR A CA  
8562  C C   . TYR A  577 ? 0.3407 0.3677 0.2599 -0.0820 -0.0210 0.0095  603 TYR A C   
8563  O O   . TYR A  577 ? 0.3408 0.3668 0.2656 -0.0778 -0.0226 0.0120  603 TYR A O   
8564  C CB  . TYR A  577 ? 0.3321 0.3575 0.2438 -0.0871 -0.0146 0.0071  603 TYR A CB  
8565  C CG  . TYR A  577 ? 0.3415 0.3668 0.2505 -0.0897 -0.0086 0.0030  603 TYR A CG  
8566  C CD1 . TYR A  577 ? 0.3525 0.3778 0.2681 -0.0864 -0.0043 -0.0006 603 TYR A CD1 
8567  C CD2 . TYR A  577 ? 0.3593 0.3848 0.2590 -0.0953 -0.0072 0.0027  603 TYR A CD2 
8568  C CE1 . TYR A  577 ? 0.3634 0.3892 0.2772 -0.0882 0.0014  -0.0042 603 TYR A CE1 
8569  C CE2 . TYR A  577 ? 0.3726 0.3982 0.2700 -0.0975 -0.0014 -0.0012 603 TYR A CE2 
8570  C CZ  . TYR A  577 ? 0.3831 0.4090 0.2879 -0.0937 0.0030  -0.0046 603 TYR A CZ  
8571  O OH  . TYR A  577 ? 0.4010 0.4278 0.3043 -0.0952 0.0090  -0.0084 603 TYR A OH  
8581  N N   . ASN A  578 ? 0.3357 0.3650 0.2513 -0.0844 -0.0240 0.0103  604 ASN A N   
8582  C CA  . ASN A  578 ? 0.3288 0.3604 0.2467 -0.0823 -0.0296 0.0147  604 ASN A CA  
8583  C C   . ASN A  578 ? 0.3280 0.3617 0.2514 -0.0802 -0.0305 0.0132  604 ASN A C   
8584  O O   . ASN A  578 ? 0.3317 0.3657 0.2535 -0.0828 -0.0280 0.0090  604 ASN A O   
8585  C CB  . ASN A  578 ? 0.3398 0.3739 0.2494 -0.0869 -0.0331 0.0180  604 ASN A CB  
8586  C CG  . ASN A  578 ? 0.3875 0.4194 0.2914 -0.0889 -0.0328 0.0206  604 ASN A CG  
8587  O OD1 . ASN A  578 ? 0.3925 0.4214 0.2999 -0.0858 -0.0323 0.0225  604 ASN A OD1 
8588  N ND2 . ASN A  578 ? 0.4033 0.4366 0.2980 -0.0945 -0.0331 0.0210  604 ASN A ND2 
8595  N N   . LEU A  579 ? 0.3136 0.3484 0.2432 -0.0755 -0.0340 0.0167  605 LEU A N   
8596  C CA  . LEU A  579 ? 0.3060 0.3437 0.2411 -0.0734 -0.0356 0.0164  605 LEU A CA  
8597  C C   . LEU A  579 ? 0.3038 0.3467 0.2353 -0.0760 -0.0405 0.0200  605 LEU A C   
8598  O O   . LEU A  579 ? 0.3215 0.3652 0.2509 -0.0754 -0.0439 0.0248  605 LEU A O   
8599  C CB  . LEU A  579 ? 0.3110 0.3477 0.2546 -0.0669 -0.0366 0.0183  605 LEU A CB  
8600  C CG  . LEU A  579 ? 0.3391 0.3716 0.2866 -0.0637 -0.0326 0.0158  605 LEU A CG  
8601  C CD1 . LEU A  579 ? 0.3384 0.3705 0.2938 -0.0578 -0.0338 0.0173  605 LEU A CD1 
8602  C CD2 . LEU A  579 ? 0.3541 0.3853 0.3012 -0.0655 -0.0277 0.0104  605 LEU A CD2 
8614  N N   . GLU A  580 ? 0.2818 0.3283 0.2123 -0.0792 -0.0410 0.0177  606 GLU A N   
8615  C CA  . GLU A  580 ? 0.2778 0.3307 0.2049 -0.0824 -0.0457 0.0208  606 GLU A CA  
8616  C C   . GLU A  580 ? 0.2719 0.3295 0.2044 -0.0818 -0.0474 0.0202  606 GLU A C   
8617  O O   . GLU A  580 ? 0.2701 0.3256 0.2048 -0.0824 -0.0439 0.0156  606 GLU A O   
8618  C CB  . GLU A  580 ? 0.2983 0.3518 0.2152 -0.0899 -0.0448 0.0184  606 GLU A CB  
8619  C CG  . GLU A  580 ? 0.3820 0.4308 0.2932 -0.0910 -0.0424 0.0184  606 GLU A CG  
8620  C CD  . GLU A  580 ? 0.5070 0.5568 0.4074 -0.0981 -0.0420 0.0172  606 GLU A CD  
8621  O OE1 . GLU A  580 ? 0.5461 0.5978 0.4429 -0.1028 -0.0411 0.0133  606 GLU A OE1 
8622  O OE2 . GLU A  580 ? 0.5451 0.5935 0.4403 -0.0992 -0.0424 0.0198  606 GLU A OE2 
8629  N N   . SER A  581 ? 0.2611 0.3254 0.1962 -0.0804 -0.0525 0.0252  607 SER A N   
8630  C CA  . SER A  581 ? 0.2526 0.3231 0.1932 -0.0801 -0.0547 0.0254  607 SER A CA  
8631  C C   . SER A  581 ? 0.2672 0.3463 0.2082 -0.0798 -0.0607 0.0314  607 SER A C   
8632  O O   . SER A  581 ? 0.2696 0.3484 0.2134 -0.0746 -0.0630 0.0364  607 SER A O   
8633  C CB  . SER A  581 ? 0.2529 0.3211 0.2029 -0.0735 -0.0530 0.0251  607 SER A CB  
8634  O OG  . SER A  581 ? 0.2545 0.3297 0.2099 -0.0733 -0.0553 0.0259  607 SER A OG  
8640  N N   . LYS A  582 ? 0.2700 0.3569 0.2090 -0.0849 -0.0633 0.0310  608 LYS A N   
8641  C CA  . LYS A  582 ? 0.2819 0.3788 0.2223 -0.0845 -0.0693 0.0370  608 LYS A CA  
8642  C C   . LYS A  582 ? 0.2838 0.3855 0.2352 -0.0782 -0.0710 0.0398  608 LYS A C   
8643  O O   . LYS A  582 ? 0.2914 0.3999 0.2457 -0.0751 -0.0756 0.0458  608 LYS A O   
8644  C CB  . LYS A  582 ? 0.3065 0.4111 0.2407 -0.0928 -0.0717 0.0355  608 LYS A CB  
8645  C CG  . LYS A  582 ? 0.3842 0.4852 0.3068 -0.0988 -0.0706 0.0337  608 LYS A CG  
8646  C CD  . LYS A  582 ? 0.4742 0.5829 0.3900 -0.1074 -0.0731 0.0321  608 LYS A CD  
8647  C CE  . LYS A  582 ? 0.5415 0.6479 0.4453 -0.1131 -0.0728 0.0314  608 LYS A CE  
8648  N NZ  . LYS A  582 ? 0.5777 0.6923 0.4745 -0.1219 -0.0756 0.0297  608 LYS A NZ  
8662  N N   . SER A  583 ? 0.2739 0.3719 0.2311 -0.0761 -0.0673 0.0358  609 SER A N   
8663  C CA  . SER A  583 ? 0.2687 0.3713 0.2359 -0.0708 -0.0684 0.0379  609 SER A CA  
8664  C C   . SER A  583 ? 0.2652 0.3612 0.2384 -0.0627 -0.0663 0.0392  609 SER A C   
8665  O O   . SER A  583 ? 0.2709 0.3713 0.2513 -0.0573 -0.0683 0.0428  609 SER A O   
8666  C CB  . SER A  583 ? 0.2889 0.3929 0.2586 -0.0744 -0.0658 0.0329  609 SER A CB  
8667  O OG  . SER A  583 ? 0.3074 0.4011 0.2744 -0.0753 -0.0603 0.0273  609 SER A OG  
8673  N N   . LEU A  584 ? 0.2568 0.3427 0.2275 -0.0619 -0.0621 0.0357  610 LEU A N   
8674  C CA  . LEU A  584 ? 0.2539 0.3333 0.2298 -0.0552 -0.0597 0.0359  610 LEU A CA  
8675  C C   . LEU A  584 ? 0.2518 0.3323 0.2314 -0.0489 -0.0627 0.0417  610 LEU A C   
8676  O O   . LEU A  584 ? 0.2607 0.3410 0.2356 -0.0494 -0.0652 0.0453  610 LEU A O   
8677  C CB  . LEU A  584 ? 0.2566 0.3263 0.2280 -0.0559 -0.0555 0.0322  610 LEU A CB  
8678  C CG  . LEU A  584 ? 0.2688 0.3321 0.2454 -0.0505 -0.0522 0.0306  610 LEU A CG  
8679  C CD1 . LEU A  584 ? 0.2814 0.3450 0.2621 -0.0508 -0.0493 0.0265  610 LEU A CD1 
8680  C CD2 . LEU A  584 ? 0.2758 0.3312 0.2481 -0.0508 -0.0492 0.0286  610 LEU A CD2 
8692  N N   . VAL A  585 ? 0.2393 0.3205 0.2267 -0.0431 -0.0624 0.0428  611 VAL A N   
8693  C CA  . VAL A  585 ? 0.2537 0.3347 0.2447 -0.0366 -0.0645 0.0479  611 VAL A CA  
8694  C C   . VAL A  585 ? 0.2508 0.3218 0.2428 -0.0320 -0.0613 0.0466  611 VAL A C   
8695  O O   . VAL A  585 ? 0.2624 0.3295 0.2538 -0.0282 -0.0624 0.0501  611 VAL A O   
8696  C CB  . VAL A  585 ? 0.2737 0.3640 0.2727 -0.0329 -0.0669 0.0510  611 VAL A CB  
8697  C CG1 . VAL A  585 ? 0.2866 0.3878 0.2849 -0.0382 -0.0701 0.0518  611 VAL A CG1 
8698  C CG2 . VAL A  585 ? 0.2876 0.3764 0.2930 -0.0298 -0.0637 0.0479  611 VAL A CG2 
8708  N N   . GLU A  586 ? 0.2258 0.2927 0.2193 -0.0324 -0.0574 0.0417  612 GLU A N   
8709  C CA  . GLU A  586 ? 0.2203 0.2788 0.2148 -0.0285 -0.0546 0.0402  612 GLU A CA  
8710  C C   . GLU A  586 ? 0.2152 0.2682 0.2059 -0.0320 -0.0510 0.0354  612 GLU A C   
8711  O O   . GLU A  586 ? 0.2130 0.2677 0.2040 -0.0349 -0.0491 0.0318  612 GLU A O   
8712  C CB  . GLU A  586 ? 0.2291 0.2889 0.2310 -0.0235 -0.0534 0.0398  612 GLU A CB  
8713  C CG  . GLU A  586 ? 0.2503 0.3023 0.2535 -0.0196 -0.0506 0.0380  612 GLU A CG  
8714  C CD  . GLU A  586 ? 0.3186 0.3720 0.3284 -0.0149 -0.0494 0.0375  612 GLU A CD  
8715  O OE1 . GLU A  586 ? 0.3357 0.3963 0.3496 -0.0148 -0.0503 0.0381  612 GLU A OE1 
8716  O OE2 . GLU A  586 ? 0.3261 0.3737 0.3367 -0.0115 -0.0474 0.0364  612 GLU A OE2 
8723  N N   . LEU A  587 ? 0.2079 0.2541 0.1951 -0.0316 -0.0499 0.0354  613 LEU A N   
8724  C CA  . LEU A  587 ? 0.2159 0.2574 0.2004 -0.0340 -0.0463 0.0312  613 LEU A CA  
8725  C C   . LEU A  587 ? 0.2278 0.2637 0.2150 -0.0297 -0.0445 0.0306  613 LEU A C   
8726  O O   . LEU A  587 ? 0.2436 0.2758 0.2295 -0.0277 -0.0457 0.0334  613 LEU A O   
8727  C CB  . LEU A  587 ? 0.2135 0.2530 0.1907 -0.0388 -0.0463 0.0312  613 LEU A CB  
8728  C CG  . LEU A  587 ? 0.2262 0.2612 0.2011 -0.0408 -0.0422 0.0270  613 LEU A CG  
8729  C CD1 . LEU A  587 ? 0.2237 0.2604 0.2003 -0.0424 -0.0394 0.0227  613 LEU A CD1 
8730  C CD2 . LEU A  587 ? 0.2493 0.2825 0.2170 -0.0453 -0.0421 0.0274  613 LEU A CD2 
8742  N N   . VAL A  588 ? 0.2171 0.2519 0.2072 -0.0287 -0.0415 0.0270  614 VAL A N   
8743  C CA  . VAL A  588 ? 0.2132 0.2433 0.2052 -0.0256 -0.0397 0.0260  614 VAL A CA  
8744  C C   . VAL A  588 ? 0.2100 0.2375 0.1986 -0.0288 -0.0370 0.0230  614 VAL A C   
8745  O O   . VAL A  588 ? 0.2098 0.2387 0.1988 -0.0305 -0.0347 0.0200  614 VAL A O   
8746  C CB  . VAL A  588 ? 0.2180 0.2492 0.2158 -0.0216 -0.0385 0.0246  614 VAL A CB  
8747  C CG1 . VAL A  588 ? 0.2199 0.2465 0.2188 -0.0188 -0.0370 0.0236  614 VAL A CG1 
8748  C CG2 . VAL A  588 ? 0.2198 0.2547 0.2212 -0.0187 -0.0409 0.0275  614 VAL A CG2 
8758  N N   . PHE A  589 ? 0.2137 0.2375 0.1990 -0.0298 -0.0372 0.0240  615 PHE A N   
8759  C CA  . PHE A  589 ? 0.2205 0.2426 0.2028 -0.0330 -0.0346 0.0215  615 PHE A CA  
8760  C C   . PHE A  589 ? 0.2202 0.2390 0.2044 -0.0309 -0.0331 0.0204  615 PHE A C   
8761  O O   . PHE A  589 ? 0.2155 0.2330 0.1973 -0.0335 -0.0315 0.0193  615 PHE A O   
8762  C CB  . PHE A  589 ? 0.2194 0.2404 0.1954 -0.0371 -0.0357 0.0234  615 PHE A CB  
8763  C CG  . PHE A  589 ? 0.2387 0.2602 0.2111 -0.0414 -0.0329 0.0206  615 PHE A CG  
8764  C CD1 . PHE A  589 ? 0.2514 0.2758 0.2229 -0.0437 -0.0315 0.0182  615 PHE A CD1 
8765  C CD2 . PHE A  589 ? 0.2510 0.2699 0.2209 -0.0433 -0.0314 0.0202  615 PHE A CD2 
8766  C CE1 . PHE A  589 ? 0.2654 0.2899 0.2336 -0.0473 -0.0284 0.0153  615 PHE A CE1 
8767  C CE2 . PHE A  589 ? 0.2639 0.2838 0.2308 -0.0470 -0.0285 0.0176  615 PHE A CE2 
8768  C CZ  . PHE A  589 ? 0.2595 0.2820 0.2257 -0.0487 -0.0269 0.0151  615 PHE A CZ  
8778  N N   . SER A  590 ? 0.2204 0.2385 0.2088 -0.0267 -0.0336 0.0207  616 SER A N   
8779  C CA  . SER A  590 ? 0.2319 0.2471 0.2215 -0.0252 -0.0325 0.0197  616 SER A CA  
8780  C C   . SER A  590 ? 0.2298 0.2473 0.2211 -0.0260 -0.0297 0.0163  616 SER A C   
8781  O O   . SER A  590 ? 0.2367 0.2573 0.2295 -0.0262 -0.0282 0.0147  616 SER A O   
8782  C CB  . SER A  590 ? 0.2738 0.2881 0.2670 -0.0205 -0.0335 0.0204  616 SER A CB  
8783  O OG  . SER A  590 ? 0.3304 0.3486 0.3273 -0.0186 -0.0330 0.0195  616 SER A OG  
8789  N N   . GLY A  591 ? 0.2134 0.2292 0.2043 -0.0267 -0.0287 0.0154  617 GLY A N   
8790  C CA  . GLY A  591 ? 0.2158 0.2348 0.2091 -0.0270 -0.0262 0.0126  617 GLY A CA  
8791  C C   . GLY A  591 ? 0.2183 0.2397 0.2097 -0.0303 -0.0241 0.0112  617 GLY A C   
8792  O O   . GLY A  591 ? 0.2171 0.2418 0.2111 -0.0296 -0.0217 0.0091  617 GLY A O   
8796  N N   . ASN A  592 ? 0.2202 0.2399 0.2069 -0.0338 -0.0248 0.0126  618 ASN A N   
8797  C CA  . ASN A  592 ? 0.2201 0.2416 0.2041 -0.0375 -0.0227 0.0113  618 ASN A CA  
8798  C C   . ASN A  592 ? 0.2228 0.2429 0.2038 -0.0408 -0.0223 0.0118  618 ASN A C   
8799  O O   . ASN A  592 ? 0.2288 0.2470 0.2109 -0.0399 -0.0232 0.0124  618 ASN A O   
8800  C CB  . ASN A  592 ? 0.2283 0.2495 0.2086 -0.0393 -0.0237 0.0123  618 ASN A CB  
8801  C CG  . ASN A  592 ? 0.2372 0.2604 0.2207 -0.0370 -0.0232 0.0110  618 ASN A CG  
8802  O OD1 . ASN A  592 ? 0.2387 0.2637 0.2247 -0.0361 -0.0203 0.0084  618 ASN A OD1 
8803  N ND2 . ASN A  592 ? 0.2224 0.2454 0.2060 -0.0359 -0.0257 0.0128  618 ASN A ND2 
8810  N N   . ARG A  593 ? 0.2225 0.2436 0.1998 -0.0447 -0.0206 0.0113  619 ARG A N   
8811  C CA  . ARG A  593 ? 0.2214 0.2416 0.1959 -0.0483 -0.0198 0.0117  619 ARG A CA  
8812  C C   . ARG A  593 ? 0.2311 0.2482 0.1989 -0.0521 -0.0209 0.0141  619 ARG A C   
8813  O O   . ARG A  593 ? 0.2307 0.2494 0.1953 -0.0560 -0.0188 0.0133  619 ARG A O   
8814  C CB  . ARG A  593 ? 0.2331 0.2585 0.2102 -0.0494 -0.0161 0.0087  619 ARG A CB  
8815  C CG  . ARG A  593 ? 0.2574 0.2864 0.2412 -0.0455 -0.0151 0.0068  619 ARG A CG  
8816  C CD  . ARG A  593 ? 0.2559 0.2838 0.2417 -0.0446 -0.0168 0.0076  619 ARG A CD  
8817  N NE  . ARG A  593 ? 0.2668 0.2945 0.2501 -0.0489 -0.0162 0.0079  619 ARG A NE  
8818  C CZ  . ARG A  593 ? 0.2800 0.3131 0.2659 -0.0506 -0.0139 0.0062  619 ARG A CZ  
8819  N NH1 . ARG A  593 ? 0.2588 0.2981 0.2501 -0.0478 -0.0119 0.0042  619 ARG A NH1 
8820  N NH2 . ARG A  593 ? 0.2662 0.2988 0.2495 -0.0551 -0.0135 0.0067  619 ARG A NH2 
8834  N N   . LEU A  594 ? 0.2341 0.2471 0.1997 -0.0510 -0.0242 0.0172  620 LEU A N   
8835  C CA  . LEU A  594 ? 0.2464 0.2561 0.2054 -0.0544 -0.0257 0.0203  620 LEU A CA  
8836  C C   . LEU A  594 ? 0.2524 0.2593 0.2084 -0.0579 -0.0245 0.0210  620 LEU A C   
8837  O O   . LEU A  594 ? 0.2636 0.2687 0.2136 -0.0617 -0.0246 0.0229  620 LEU A O   
8838  C CB  . LEU A  594 ? 0.2530 0.2591 0.2108 -0.0518 -0.0294 0.0241  620 LEU A CB  
8839  C CG  . LEU A  594 ? 0.2725 0.2819 0.2314 -0.0500 -0.0309 0.0242  620 LEU A CG  
8840  C CD1 . LEU A  594 ? 0.2802 0.2874 0.2407 -0.0460 -0.0342 0.0274  620 LEU A CD1 
8841  C CD2 . LEU A  594 ? 0.2812 0.2923 0.2340 -0.0543 -0.0311 0.0250  620 LEU A CD2 
8853  N N   . ASP A  595 ? 0.2428 0.2498 0.2025 -0.0573 -0.0234 0.0193  621 ASP A N   
8854  C CA  . ASP A  595 ? 0.2517 0.2571 0.2089 -0.0615 -0.0219 0.0194  621 ASP A CA  
8855  C C   . ASP A  595 ? 0.2575 0.2680 0.2130 -0.0655 -0.0187 0.0176  621 ASP A C   
8856  O O   . ASP A  595 ? 0.2738 0.2825 0.2243 -0.0700 -0.0178 0.0189  621 ASP A O   
8857  C CB  . ASP A  595 ? 0.2597 0.2659 0.2217 -0.0604 -0.0212 0.0174  621 ASP A CB  
8858  C CG  . ASP A  595 ? 0.2934 0.3074 0.2619 -0.0584 -0.0191 0.0138  621 ASP A CG  
8859  O OD1 . ASP A  595 ? 0.2699 0.2863 0.2410 -0.0549 -0.0193 0.0130  621 ASP A OD1 
8860  O OD2 . ASP A  595 ? 0.2992 0.3170 0.2703 -0.0602 -0.0173 0.0120  621 ASP A OD2 
8865  N N   . ILE A  596 ? 0.2419 0.2583 0.2012 -0.0638 -0.0167 0.0146  622 ILE A N   
8866  C CA  . ILE A  596 ? 0.2412 0.2622 0.1989 -0.0669 -0.0133 0.0125  622 ILE A CA  
8867  C C   . ILE A  596 ? 0.2400 0.2592 0.1912 -0.0690 -0.0139 0.0139  622 ILE A C   
8868  O O   . ILE A  596 ? 0.2356 0.2550 0.1815 -0.0735 -0.0123 0.0143  622 ILE A O   
8869  C CB  . ILE A  596 ? 0.2443 0.2715 0.2086 -0.0637 -0.0106 0.0089  622 ILE A CB  
8870  C CG1 . ILE A  596 ? 0.2625 0.2930 0.2327 -0.0626 -0.0098 0.0077  622 ILE A CG1 
8871  C CG2 . ILE A  596 ? 0.2459 0.2769 0.2082 -0.0662 -0.0067 0.0066  622 ILE A CG2 
8872  C CD1 . ILE A  596 ? 0.2786 0.3153 0.2558 -0.0588 -0.0075 0.0049  622 ILE A CD1 
8884  N N   . LEU A  597 ? 0.2526 0.2709 0.2041 -0.0662 -0.0162 0.0145  623 LEU A N   
8885  C CA  . LEU A  597 ? 0.2729 0.2904 0.2181 -0.0685 -0.0172 0.0157  623 LEU A CA  
8886  C C   . LEU A  597 ? 0.2853 0.2987 0.2235 -0.0719 -0.0193 0.0198  623 LEU A C   
8887  O O   . LEU A  597 ? 0.2871 0.3010 0.2189 -0.0759 -0.0185 0.0202  623 LEU A O   
8888  C CB  . LEU A  597 ? 0.2759 0.2933 0.2231 -0.0650 -0.0199 0.0162  623 LEU A CB  
8889  C CG  . LEU A  597 ? 0.2783 0.2990 0.2316 -0.0617 -0.0179 0.0126  623 LEU A CG  
8890  C CD1 . LEU A  597 ? 0.2819 0.3019 0.2389 -0.0575 -0.0210 0.0137  623 LEU A CD1 
8891  C CD2 . LEU A  597 ? 0.2804 0.3034 0.2306 -0.0643 -0.0150 0.0097  623 LEU A CD2 
8903  N N   . TRP A  598 ? 0.2893 0.2981 0.2281 -0.0704 -0.0217 0.0227  624 TRP A N   
8904  C CA  . TRP A  598 ? 0.2977 0.3014 0.2301 -0.0731 -0.0235 0.0270  624 TRP A CA  
8905  C C   . TRP A  598 ? 0.3252 0.3267 0.2562 -0.0766 -0.0213 0.0270  624 TRP A C   
8906  O O   . TRP A  598 ? 0.3379 0.3334 0.2651 -0.0778 -0.0228 0.0305  624 TRP A O   
8907  C CB  . TRP A  598 ? 0.2850 0.2839 0.2181 -0.0692 -0.0276 0.0308  624 TRP A CB  
8908  C CG  . TRP A  598 ? 0.2805 0.2818 0.2135 -0.0669 -0.0303 0.0321  624 TRP A CG  
8909  C CD1 . TRP A  598 ? 0.2896 0.2946 0.2184 -0.0695 -0.0304 0.0318  624 TRP A CD1 
8910  C CD2 . TRP A  598 ? 0.2712 0.2708 0.2074 -0.0620 -0.0336 0.0345  624 TRP A CD2 
8911  N NE1 . TRP A  598 ? 0.2886 0.2953 0.2186 -0.0668 -0.0336 0.0335  624 TRP A NE1 
8912  C CE2 . TRP A  598 ? 0.2785 0.2821 0.2131 -0.0620 -0.0357 0.0356  624 TRP A CE2 
8913  C CE3 . TRP A  598 ? 0.2766 0.2719 0.2166 -0.0578 -0.0349 0.0359  624 TRP A CE3 
8914  C CZ2 . TRP A  598 ? 0.2850 0.2895 0.2228 -0.0577 -0.0389 0.0378  624 TRP A CZ2 
8915  C CZ3 . TRP A  598 ? 0.2827 0.2783 0.2256 -0.0532 -0.0378 0.0380  624 TRP A CZ3 
8916  C CH2 . TRP A  598 ? 0.2863 0.2867 0.2283 -0.0532 -0.0399 0.0393  624 TRP A CH2 
8927  N N   . ASN A  599 ? 0.3260 0.3326 0.2597 -0.0785 -0.0175 0.0232  625 ASN A N   
8928  C CA  . ASN A  599 ? 0.3470 0.3533 0.2796 -0.0826 -0.0151 0.0229  625 ASN A CA  
8929  C C   . ASN A  599 ? 0.3696 0.3722 0.2931 -0.0876 -0.0151 0.0262  625 ASN A C   
8930  O O   . ASN A  599 ? 0.3756 0.3797 0.2945 -0.0890 -0.0152 0.0267  625 ASN A O   
8931  C CB  . ASN A  599 ? 0.3629 0.3771 0.3000 -0.0836 -0.0108 0.0184  625 ASN A CB  
8932  C CG  . ASN A  599 ? 0.4210 0.4367 0.3573 -0.0882 -0.0081 0.0180  625 ASN A CG  
8933  O OD1 . ASN A  599 ? 0.4345 0.4510 0.3654 -0.0929 -0.0059 0.0185  625 ASN A OD1 
8934  N ND2 . ASN A  599 ? 0.4197 0.4359 0.3611 -0.0875 -0.0081 0.0172  625 ASN A ND2 
8941  N N   . ASP A  600 ? 0.3827 0.3799 0.3033 -0.0904 -0.0153 0.0287  626 ASP A N   
8942  C CA  . ASP A  600 ? 0.4007 0.3931 0.3123 -0.0951 -0.0155 0.0326  626 ASP A CA  
8943  C C   . ASP A  600 ? 0.3896 0.3872 0.2967 -0.0998 -0.0122 0.0312  626 ASP A C   
8944  O O   . ASP A  600 ? 0.3995 0.3941 0.2985 -0.1030 -0.0130 0.0345  626 ASP A O   
8945  C CB  . ASP A  600 ? 0.4459 0.4324 0.3558 -0.0983 -0.0148 0.0343  626 ASP A CB  
8946  C CG  . ASP A  600 ? 0.5520 0.5304 0.4632 -0.0948 -0.0178 0.0368  626 ASP A CG  
8947  O OD1 . ASP A  600 ? 0.5744 0.5503 0.4856 -0.0902 -0.0210 0.0389  626 ASP A OD1 
8948  O OD2 . ASP A  600 ? 0.5979 0.5724 0.5099 -0.0967 -0.0168 0.0364  626 ASP A OD2 
8953  N N   . ASP A  601 ? 0.3714 0.3766 0.2835 -0.1003 -0.0085 0.0265  627 ASP A N   
8954  C CA  . ASP A  601 ? 0.3627 0.3731 0.2711 -0.1046 -0.0047 0.0246  627 ASP A CA  
8955  C C   . ASP A  601 ? 0.3505 0.3649 0.2584 -0.1027 -0.0042 0.0222  627 ASP A C   
8956  O O   . ASP A  601 ? 0.3444 0.3631 0.2498 -0.1056 -0.0005 0.0197  627 ASP A O   
8957  C CB  . ASP A  601 ? 0.3771 0.3939 0.2913 -0.1064 -0.0003 0.0210  627 ASP A CB  
8958  C CG  . ASP A  601 ? 0.4284 0.4419 0.3435 -0.1089 -0.0006 0.0227  627 ASP A CG  
8959  O OD1 . ASP A  601 ? 0.4156 0.4233 0.3235 -0.1132 -0.0011 0.0263  627 ASP A OD1 
8960  O OD2 . ASP A  601 ? 0.4718 0.4885 0.3947 -0.1068 -0.0002 0.0204  627 ASP A OD2 
8965  N N   . ASP A  602 ? 0.3401 0.3528 0.2500 -0.0982 -0.0078 0.0228  628 ASP A N   
8966  C CA  . ASP A  602 ? 0.3384 0.3543 0.2477 -0.0967 -0.0076 0.0204  628 ASP A CA  
8967  C C   . ASP A  602 ? 0.3420 0.3542 0.2461 -0.0960 -0.0123 0.0242  628 ASP A C   
8968  O O   . ASP A  602 ? 0.3419 0.3509 0.2491 -0.0922 -0.0160 0.0268  628 ASP A O   
8969  C CB  . ASP A  602 ? 0.3432 0.3625 0.2619 -0.0915 -0.0068 0.0167  628 ASP A CB  
8970  C CG  . ASP A  602 ? 0.3783 0.4006 0.2971 -0.0903 -0.0053 0.0133  628 ASP A CG  
8971  O OD1 . ASP A  602 ? 0.3536 0.3759 0.2650 -0.0938 -0.0049 0.0134  628 ASP A OD1 
8972  O OD2 . ASP A  602 ? 0.4231 0.4477 0.3490 -0.0861 -0.0045 0.0105  628 ASP A OD2 
8977  N N   . ASN A  603 ? 0.3458 0.3590 0.2421 -0.0996 -0.0121 0.0246  629 ASN A N   
8978  C CA  . ASN A  603 ? 0.3542 0.3657 0.2455 -0.0992 -0.0167 0.0282  629 ASN A CA  
8979  C C   . ASN A  603 ? 0.3335 0.3486 0.2272 -0.0971 -0.0174 0.0252  629 ASN A C   
8980  O O   . ASN A  603 ? 0.3333 0.3484 0.2236 -0.0968 -0.0213 0.0279  629 ASN A O   
8981  C CB  . ASN A  603 ? 0.4003 0.4111 0.2807 -0.1050 -0.0166 0.0309  629 ASN A CB  
8982  C CG  . ASN A  603 ? 0.4874 0.4934 0.3639 -0.1074 -0.0167 0.0351  629 ASN A CG  
8983  O OD1 . ASN A  603 ? 0.5067 0.5085 0.3875 -0.1045 -0.0185 0.0375  629 ASN A OD1 
8984  N ND2 . ASN A  603 ? 0.5141 0.5201 0.3819 -0.1131 -0.0147 0.0362  629 ASN A ND2 
8991  N N   . ARG A  604 ? 0.3155 0.3337 0.2147 -0.0956 -0.0136 0.0198  630 ARG A N   
8992  C CA  . ARG A  604 ? 0.3170 0.3377 0.2171 -0.0945 -0.0135 0.0166  630 ARG A CA  
8993  C C   . ARG A  604 ? 0.3070 0.3274 0.2120 -0.0900 -0.0180 0.0183  630 ARG A C   
8994  O O   . ARG A  604 ? 0.3101 0.3323 0.2127 -0.0909 -0.0196 0.0177  630 ARG A O   
8995  C CB  . ARG A  604 ? 0.3199 0.3432 0.2248 -0.0935 -0.0081 0.0108  630 ARG A CB  
8996  C CG  . ARG A  604 ? 0.3418 0.3665 0.2412 -0.0982 -0.0030 0.0082  630 ARG A CG  
8997  C CD  . ARG A  604 ? 0.3609 0.3883 0.2664 -0.0961 0.0026  0.0031  630 ARG A CD  
8998  N NE  . ARG A  604 ? 0.3622 0.3904 0.2768 -0.0919 0.0024  0.0036  630 ARG A NE  
8999  C CZ  . ARG A  604 ? 0.3601 0.3906 0.2827 -0.0878 0.0052  0.0004  630 ARG A CZ  
9000  N NH1 . ARG A  604 ? 0.3494 0.3809 0.2723 -0.0871 0.0088  -0.0037 630 ARG A NH1 
9001  N NH2 . ARG A  604 ? 0.3221 0.3537 0.2523 -0.0845 0.0043  0.0014  630 ARG A NH2 
9015  N N   . TYR A  605 ? 0.2862 0.3047 0.1977 -0.0857 -0.0199 0.0204  631 TYR A N   
9016  C CA  . TYR A  605 ? 0.2868 0.3052 0.2038 -0.0810 -0.0236 0.0219  631 TYR A CA  
9017  C C   . TYR A  605 ? 0.3041 0.3197 0.2192 -0.0797 -0.0284 0.0278  631 TYR A C   
9018  O O   . TYR A  605 ? 0.3037 0.3189 0.2240 -0.0752 -0.0312 0.0294  631 TYR A O   
9019  C CB  . TYR A  605 ? 0.2685 0.2868 0.1947 -0.0763 -0.0219 0.0194  631 TYR A CB  
9020  C CG  . TYR A  605 ? 0.2634 0.2845 0.1923 -0.0765 -0.0172 0.0141  631 TYR A CG  
9021  C CD1 . TYR A  605 ? 0.2591 0.2819 0.1901 -0.0751 -0.0166 0.0113  631 TYR A CD1 
9022  C CD2 . TYR A  605 ? 0.2675 0.2894 0.1964 -0.0784 -0.0131 0.0119  631 TYR A CD2 
9023  C CE1 . TYR A  605 ? 0.2612 0.2856 0.1946 -0.0748 -0.0119 0.0066  631 TYR A CE1 
9024  C CE2 . TYR A  605 ? 0.2686 0.2931 0.2002 -0.0779 -0.0085 0.0073  631 TYR A CE2 
9025  C CZ  . TYR A  605 ? 0.2718 0.2971 0.2055 -0.0760 -0.0078 0.0047  631 TYR A CZ  
9026  O OH  . TYR A  605 ? 0.2801 0.3070 0.2162 -0.0752 -0.0030 0.0003  631 TYR A OH  
9036  N N   . ILE A  606 ? 0.3204 0.3341 0.2277 -0.0835 -0.0294 0.0312  632 ILE A N   
9037  C CA  . ILE A  606 ? 0.3435 0.3537 0.2483 -0.0822 -0.0335 0.0373  632 ILE A CA  
9038  C C   . ILE A  606 ? 0.3338 0.3467 0.2389 -0.0799 -0.0382 0.0402  632 ILE A C   
9039  O O   . ILE A  606 ? 0.3425 0.3528 0.2486 -0.0767 -0.0416 0.0450  632 ILE A O   
9040  C CB  . ILE A  606 ? 0.3744 0.3818 0.2699 -0.0873 -0.0329 0.0403  632 ILE A CB  
9041  C CG1 . ILE A  606 ? 0.4158 0.4167 0.3103 -0.0855 -0.0353 0.0459  632 ILE A CG1 
9042  C CG2 . ILE A  606 ? 0.3800 0.3910 0.2675 -0.0913 -0.0347 0.0417  632 ILE A CG2 
9043  C CD1 . ILE A  606 ? 0.4524 0.4489 0.3514 -0.0846 -0.0324 0.0442  632 ILE A CD1 
9055  N N   . SER A  607 ? 0.3213 0.3395 0.2258 -0.0816 -0.0381 0.0373  633 SER A N   
9056  C CA  . SER A  607 ? 0.3144 0.3368 0.2200 -0.0800 -0.0423 0.0395  633 SER A CA  
9057  C C   . SER A  607 ? 0.3048 0.3303 0.2178 -0.0774 -0.0412 0.0350  633 SER A C   
9058  O O   . SER A  607 ? 0.3088 0.3390 0.2217 -0.0782 -0.0433 0.0347  633 SER A O   
9059  C CB  . SER A  607 ? 0.3371 0.3634 0.2338 -0.0855 -0.0437 0.0402  633 SER A CB  
9060  O OG  . SER A  607 ? 0.3806 0.4041 0.2697 -0.0883 -0.0445 0.0444  633 SER A OG  
9066  N N   . ILE A  608 ? 0.2909 0.3139 0.2102 -0.0744 -0.0381 0.0318  634 ILE A N   
9067  C CA  . ILE A  608 ? 0.2844 0.3096 0.2105 -0.0718 -0.0365 0.0276  634 ILE A CA  
9068  C C   . ILE A  608 ? 0.2757 0.3042 0.2060 -0.0688 -0.0403 0.0297  634 ILE A C   
9069  O O   . ILE A  608 ? 0.2869 0.3187 0.2192 -0.0694 -0.0396 0.0265  634 ILE A O   
9070  C CB  . ILE A  608 ? 0.2892 0.3114 0.2217 -0.0684 -0.0333 0.0252  634 ILE A CB  
9071  C CG1 . ILE A  608 ? 0.2909 0.3151 0.2293 -0.0662 -0.0310 0.0207  634 ILE A CG1 
9072  C CG2 . ILE A  608 ? 0.2974 0.3163 0.2338 -0.0639 -0.0358 0.0290  634 ILE A CG2 
9073  C CD1 . ILE A  608 ? 0.3010 0.3236 0.2447 -0.0637 -0.0274 0.0178  634 ILE A CD1 
9085  N N   . PHE A  609 ? 0.2600 0.2879 0.1919 -0.0654 -0.0441 0.0347  635 PHE A N   
9086  C CA  . PHE A  609 ? 0.2579 0.2898 0.1946 -0.0621 -0.0476 0.0370  635 PHE A CA  
9087  C C   . PHE A  609 ? 0.2669 0.3033 0.1990 -0.0640 -0.0521 0.0417  635 PHE A C   
9088  O O   . PHE A  609 ? 0.2681 0.3095 0.2042 -0.0617 -0.0552 0.0436  635 PHE A O   
9089  C CB  . PHE A  609 ? 0.2513 0.2799 0.1944 -0.0558 -0.0485 0.0393  635 PHE A CB  
9090  C CG  . PHE A  609 ? 0.2594 0.2842 0.2070 -0.0538 -0.0447 0.0354  635 PHE A CG  
9091  C CD1 . PHE A  609 ? 0.2679 0.2947 0.2188 -0.0542 -0.0418 0.0305  635 PHE A CD1 
9092  C CD2 . PHE A  609 ? 0.2720 0.2910 0.2202 -0.0516 -0.0439 0.0367  635 PHE A CD2 
9093  C CE1 . PHE A  609 ? 0.2746 0.2987 0.2296 -0.0521 -0.0386 0.0273  635 PHE A CE1 
9094  C CE2 . PHE A  609 ? 0.2739 0.2904 0.2261 -0.0501 -0.0407 0.0331  635 PHE A CE2 
9095  C CZ  . PHE A  609 ? 0.2745 0.2941 0.2303 -0.0501 -0.0382 0.0286  635 PHE A CZ  
9105  N N   . LYS A  610 ? 0.2706 0.3061 0.1944 -0.0683 -0.0526 0.0435  636 LYS A N   
9106  C CA  . LYS A  610 ? 0.2824 0.3223 0.2011 -0.0702 -0.0571 0.0485  636 LYS A CA  
9107  C C   . LYS A  610 ? 0.2926 0.3408 0.2114 -0.0729 -0.0591 0.0471  636 LYS A C   
9108  O O   . LYS A  610 ? 0.2884 0.3422 0.2080 -0.0716 -0.0637 0.0517  636 LYS A O   
9109  C CB  . LYS A  610 ? 0.3210 0.3584 0.2299 -0.0753 -0.0564 0.0498  636 LYS A CB  
9110  C CG  . LYS A  610 ? 0.3993 0.4406 0.3025 -0.0767 -0.0613 0.0561  636 LYS A CG  
9111  C CD  . LYS A  610 ? 0.4766 0.5136 0.3703 -0.0806 -0.0605 0.0584  636 LYS A CD  
9112  C CE  . LYS A  610 ? 0.5542 0.5942 0.4427 -0.0807 -0.0656 0.0658  636 LYS A CE  
9113  N NZ  . LYS A  610 ? 0.6112 0.6461 0.4905 -0.0842 -0.0648 0.0687  636 LYS A NZ  
9127  N N   . GLY A  611 ? 0.2899 0.3388 0.2080 -0.0765 -0.0557 0.0409  637 GLY A N   
9128  C CA  . GLY A  611 ? 0.2910 0.3466 0.2086 -0.0800 -0.0569 0.0385  637 GLY A CA  
9129  C C   . GLY A  611 ? 0.2847 0.3443 0.2115 -0.0759 -0.0584 0.0386  637 GLY A C   
9130  O O   . GLY A  611 ? 0.2867 0.3523 0.2136 -0.0789 -0.0597 0.0370  637 GLY A O   
9134  N N   . LEU A  612 ? 0.2721 0.3285 0.2062 -0.0693 -0.0582 0.0404  638 LEU A N   
9135  C CA  . LEU A  612 ? 0.2624 0.3227 0.2052 -0.0649 -0.0596 0.0410  638 LEU A CA  
9136  C C   . LEU A  612 ? 0.2719 0.3380 0.2155 -0.0626 -0.0651 0.0478  638 LEU A C   
9137  O O   . LEU A  612 ? 0.2673 0.3313 0.2152 -0.0567 -0.0664 0.0518  638 LEU A O   
9138  C CB  . LEU A  612 ? 0.2509 0.3050 0.2003 -0.0592 -0.0567 0.0396  638 LEU A CB  
9139  C CG  . LEU A  612 ? 0.2545 0.3033 0.2031 -0.0609 -0.0514 0.0336  638 LEU A CG  
9140  C CD1 . LEU A  612 ? 0.2459 0.2893 0.2004 -0.0555 -0.0491 0.0329  638 LEU A CD1 
9141  C CD2 . LEU A  612 ? 0.2609 0.3127 0.2103 -0.0641 -0.0496 0.0289  638 LEU A CD2 
9153  N N   . LYS A  613 ? 0.2779 0.3512 0.2168 -0.0675 -0.0682 0.0490  639 LYS A N   
9154  C CA  . LYS A  613 ? 0.2969 0.3769 0.2347 -0.0665 -0.0736 0.0558  639 LYS A CA  
9155  C C   . LYS A  613 ? 0.2904 0.3763 0.2376 -0.0603 -0.0766 0.0596  639 LYS A C   
9156  O O   . LYS A  613 ? 0.2991 0.3881 0.2469 -0.0569 -0.0804 0.0661  639 LYS A O   
9157  C CB  . LYS A  613 ? 0.3345 0.4221 0.2651 -0.0740 -0.0761 0.0554  639 LYS A CB  
9158  C CG  . LYS A  613 ? 0.4332 0.5152 0.3535 -0.0798 -0.0736 0.0528  639 LYS A CG  
9159  C CD  . LYS A  613 ? 0.5304 0.6195 0.4421 -0.0871 -0.0764 0.0533  639 LYS A CD  
9160  C CE  . LYS A  613 ? 0.6001 0.6833 0.5013 -0.0920 -0.0738 0.0515  639 LYS A CE  
9161  N NZ  . LYS A  613 ? 0.6428 0.7327 0.5346 -0.0994 -0.0766 0.0520  639 LYS A NZ  
9175  N N   . ASN A  614 ? 0.2768 0.3643 0.2313 -0.0586 -0.0747 0.0560  640 ASN A N   
9176  C CA  . ASN A  614 ? 0.2697 0.3633 0.2334 -0.0529 -0.0769 0.0593  640 ASN A CA  
9177  C C   . ASN A  614 ? 0.2575 0.3434 0.2275 -0.0457 -0.0740 0.0589  640 ASN A C   
9178  O O   . ASN A  614 ? 0.2532 0.3431 0.2310 -0.0408 -0.0749 0.0605  640 ASN A O   
9179  C CB  . ASN A  614 ? 0.2801 0.3815 0.2473 -0.0566 -0.0768 0.0555  640 ASN A CB  
9180  C CG  . ASN A  614 ? 0.3053 0.4176 0.2800 -0.0536 -0.0805 0.0594  640 ASN A CG  
9181  O OD1 . ASN A  614 ? 0.2905 0.4090 0.2650 -0.0519 -0.0849 0.0655  640 ASN A OD1 
9182  N ND2 . ASN A  614 ? 0.3353 0.4518 0.3163 -0.0537 -0.0792 0.0564  640 ASN A ND2 
9189  N N   . LEU A  615 ? 0.2439 0.3192 0.2105 -0.0453 -0.0706 0.0567  641 LEU A N   
9190  C CA  . LEU A  615 ? 0.2523 0.3202 0.2239 -0.0397 -0.0676 0.0554  641 LEU A CA  
9191  C C   . LEU A  615 ? 0.2609 0.3272 0.2363 -0.0327 -0.0696 0.0609  641 LEU A C   
9192  O O   . LEU A  615 ? 0.2681 0.3321 0.2390 -0.0321 -0.0717 0.0654  641 LEU A O   
9193  C CB  . LEU A  615 ? 0.2541 0.3123 0.2207 -0.0418 -0.0638 0.0518  641 LEU A CB  
9194  C CG  . LEU A  615 ? 0.2769 0.3293 0.2483 -0.0386 -0.0598 0.0477  641 LEU A CG  
9195  C CD1 . LEU A  615 ? 0.2785 0.3341 0.2524 -0.0413 -0.0575 0.0424  641 LEU A CD1 
9196  C CD2 . LEU A  615 ? 0.2995 0.3432 0.2666 -0.0396 -0.0569 0.0459  641 LEU A CD2 
9208  N N   . THR A  616 ? 0.2613 0.3281 0.2445 -0.0273 -0.0686 0.0605  642 THR A N   
9209  C CA  . THR A  616 ? 0.2699 0.3341 0.2571 -0.0201 -0.0696 0.0650  642 THR A CA  
9210  C C   . THR A  616 ? 0.2674 0.3216 0.2564 -0.0164 -0.0658 0.0621  642 THR A C   
9211  O O   . THR A  616 ? 0.2736 0.3214 0.2624 -0.0119 -0.0658 0.0651  642 THR A O   
9212  C CB  . THR A  616 ? 0.2939 0.3687 0.2886 -0.0164 -0.0723 0.0681  642 THR A CB  
9213  O OG1 . THR A  616 ? 0.3120 0.3903 0.3123 -0.0167 -0.0701 0.0637  642 THR A OG1 
9214  C CG2 . THR A  616 ? 0.3030 0.3881 0.2955 -0.0199 -0.0767 0.0718  642 THR A CG2 
9222  N N   . ARG A  617 ? 0.2608 0.3134 0.2512 -0.0184 -0.0625 0.0564  643 ARG A N   
9223  C CA  . ARG A  617 ? 0.2688 0.3131 0.2608 -0.0153 -0.0591 0.0535  643 ARG A CA  
9224  C C   . ARG A  617 ? 0.2687 0.3079 0.2561 -0.0201 -0.0563 0.0490  643 ARG A C   
9225  O O   . ARG A  617 ? 0.2700 0.3130 0.2570 -0.0242 -0.0552 0.0455  643 ARG A O   
9226  C CB  . ARG A  617 ? 0.2869 0.3349 0.2864 -0.0118 -0.0578 0.0515  643 ARG A CB  
9227  C CG  . ARG A  617 ? 0.3776 0.4176 0.3786 -0.0084 -0.0546 0.0489  643 ARG A CG  
9228  C CD  . ARG A  617 ? 0.4452 0.4884 0.4532 -0.0042 -0.0533 0.0476  643 ARG A CD  
9229  N NE  . ARG A  617 ? 0.5101 0.5454 0.5186 -0.0009 -0.0507 0.0455  643 ARG A NE  
9230  C CZ  . ARG A  617 ? 0.5488 0.5799 0.5558 -0.0029 -0.0480 0.0413  643 ARG A CZ  
9231  N NH1 . ARG A  617 ? 0.5421 0.5753 0.5469 -0.0079 -0.0472 0.0385  643 ARG A NH1 
9232  N NH2 . ARG A  617 ? 0.5527 0.5774 0.5600 0.0000  -0.0460 0.0398  643 ARG A NH2 
9246  N N   . LEU A  618 ? 0.2611 0.2918 0.2451 -0.0196 -0.0548 0.0489  644 LEU A N   
9247  C CA  . LEU A  618 ? 0.2619 0.2883 0.2420 -0.0239 -0.0520 0.0448  644 LEU A CA  
9248  C C   . LEU A  618 ? 0.2569 0.2762 0.2385 -0.0211 -0.0494 0.0428  644 LEU A C   
9249  O O   . LEU A  618 ? 0.2619 0.2756 0.2430 -0.0180 -0.0499 0.0454  644 LEU A O   
9250  C CB  . LEU A  618 ? 0.2706 0.2947 0.2432 -0.0280 -0.0530 0.0471  644 LEU A CB  
9251  C CG  . LEU A  618 ? 0.2941 0.3142 0.2623 -0.0325 -0.0501 0.0435  644 LEU A CG  
9252  C CD1 . LEU A  618 ? 0.2955 0.3201 0.2646 -0.0358 -0.0479 0.0386  644 LEU A CD1 
9253  C CD2 . LEU A  618 ? 0.3029 0.3208 0.2636 -0.0364 -0.0513 0.0464  644 LEU A CD2 
9265  N N   . ASP A  619 ? 0.2374 0.2568 0.2208 -0.0223 -0.0466 0.0381  645 ASP A N   
9266  C CA  . ASP A  619 ? 0.2370 0.2509 0.2218 -0.0202 -0.0443 0.0359  645 ASP A CA  
9267  C C   . ASP A  619 ? 0.2397 0.2512 0.2209 -0.0245 -0.0420 0.0330  645 ASP A C   
9268  O O   . ASP A  619 ? 0.2349 0.2499 0.2167 -0.0269 -0.0403 0.0299  645 ASP A O   
9269  C CB  . ASP A  619 ? 0.2429 0.2595 0.2337 -0.0168 -0.0430 0.0335  645 ASP A CB  
9270  C CG  . ASP A  619 ? 0.2786 0.2905 0.2709 -0.0145 -0.0410 0.0313  645 ASP A CG  
9271  O OD1 . ASP A  619 ? 0.2670 0.2735 0.2559 -0.0160 -0.0403 0.0311  645 ASP A OD1 
9272  O OD2 . ASP A  619 ? 0.3190 0.3328 0.3157 -0.0115 -0.0401 0.0297  645 ASP A OD2 
9277  N N   . LEU A  620 ? 0.2430 0.2484 0.2202 -0.0256 -0.0419 0.0343  646 LEU A N   
9278  C CA  . LEU A  620 ? 0.2478 0.2509 0.2217 -0.0297 -0.0397 0.0320  646 LEU A CA  
9279  C C   . LEU A  620 ? 0.2524 0.2514 0.2281 -0.0283 -0.0379 0.0299  646 LEU A C   
9280  O O   . LEU A  620 ? 0.2570 0.2532 0.2297 -0.0315 -0.0365 0.0289  646 LEU A O   
9281  C CB  . LEU A  620 ? 0.2642 0.2636 0.2317 -0.0329 -0.0408 0.0353  646 LEU A CB  
9282  C CG  . LEU A  620 ? 0.2785 0.2816 0.2430 -0.0345 -0.0431 0.0382  646 LEU A CG  
9283  C CD1 . LEU A  620 ? 0.2860 0.2851 0.2436 -0.0380 -0.0438 0.0412  646 LEU A CD1 
9284  C CD2 . LEU A  620 ? 0.2836 0.2934 0.2489 -0.0372 -0.0421 0.0351  646 LEU A CD2 
9296  N N   . SER A  621 ? 0.2476 0.2468 0.2279 -0.0240 -0.0379 0.0290  647 SER A N   
9297  C CA  . SER A  621 ? 0.2455 0.2412 0.2271 -0.0229 -0.0364 0.0269  647 SER A CA  
9298  C C   . SER A  621 ? 0.2382 0.2375 0.2210 -0.0254 -0.0341 0.0231  647 SER A C   
9299  O O   . SER A  621 ? 0.2316 0.2361 0.2156 -0.0267 -0.0333 0.0218  647 SER A O   
9300  C CB  . SER A  621 ? 0.2497 0.2452 0.2354 -0.0177 -0.0368 0.0268  647 SER A CB  
9301  O OG  . SER A  621 ? 0.2499 0.2518 0.2400 -0.0164 -0.0361 0.0248  647 SER A OG  
9307  N N   . LEU A  622 ? 0.2438 0.2405 0.2266 -0.0261 -0.0329 0.0213  648 LEU A N   
9308  C CA  . LEU A  622 ? 0.2462 0.2474 0.2311 -0.0278 -0.0309 0.0179  648 LEU A CA  
9309  C C   . LEU A  622 ? 0.2455 0.2504 0.2288 -0.0318 -0.0296 0.0173  648 LEU A C   
9310  O O   . LEU A  622 ? 0.2481 0.2584 0.2343 -0.0317 -0.0280 0.0151  648 LEU A O   
9311  C CB  . LEU A  622 ? 0.2467 0.2524 0.2368 -0.0240 -0.0303 0.0161  648 LEU A CB  
9312  C CG  . LEU A  622 ? 0.2659 0.2689 0.2577 -0.0202 -0.0310 0.0160  648 LEU A CG  
9313  C CD1 . LEU A  622 ? 0.2720 0.2798 0.2685 -0.0167 -0.0304 0.0148  648 LEU A CD1 
9314  C CD2 . LEU A  622 ? 0.2681 0.2684 0.2586 -0.0218 -0.0303 0.0144  648 LEU A CD2 
9326  N N   . ASN A  623 ? 0.2379 0.2395 0.2163 -0.0352 -0.0300 0.0192  649 ASN A N   
9327  C CA  . ASN A  623 ? 0.2377 0.2425 0.2139 -0.0394 -0.0285 0.0185  649 ASN A CA  
9328  C C   . ASN A  623 ? 0.2367 0.2398 0.2102 -0.0436 -0.0272 0.0179  649 ASN A C   
9329  O O   . ASN A  623 ? 0.2297 0.2344 0.2002 -0.0475 -0.0259 0.0179  649 ASN A O   
9330  C CB  . ASN A  623 ? 0.2470 0.2508 0.2193 -0.0405 -0.0301 0.0212  649 ASN A CB  
9331  C CG  . ASN A  623 ? 0.2740 0.2827 0.2484 -0.0392 -0.0300 0.0203  649 ASN A CG  
9332  O OD1 . ASN A  623 ? 0.2678 0.2798 0.2408 -0.0419 -0.0284 0.0187  649 ASN A OD1 
9333  N ND2 . ASN A  623 ? 0.2663 0.2755 0.2442 -0.0351 -0.0315 0.0209  649 ASN A ND2 
9340  N N   . ARG A  624 ? 0.2428 0.2430 0.2172 -0.0432 -0.0273 0.0172  650 ARG A N   
9341  C CA  . ARG A  624 ? 0.2603 0.2592 0.2327 -0.0475 -0.0260 0.0164  650 ARG A CA  
9342  C C   . ARG A  624 ? 0.2762 0.2695 0.2423 -0.0515 -0.0263 0.0191  650 ARG A C   
9343  O O   . ARG A  624 ? 0.2796 0.2738 0.2438 -0.0561 -0.0247 0.0185  650 ARG A O   
9344  C CB  . ARG A  624 ? 0.2684 0.2758 0.2444 -0.0493 -0.0235 0.0135  650 ARG A CB  
9345  C CG  . ARG A  624 ? 0.3077 0.3206 0.2896 -0.0449 -0.0232 0.0114  650 ARG A CG  
9346  C CD  . ARG A  624 ? 0.3606 0.3814 0.3466 -0.0460 -0.0209 0.0088  650 ARG A CD  
9347  N NE  . ARG A  624 ? 0.4048 0.4307 0.3959 -0.0417 -0.0202 0.0074  650 ARG A NE  
9348  C CZ  . ARG A  624 ? 0.4317 0.4648 0.4272 -0.0409 -0.0183 0.0055  650 ARG A CZ  
9349  N NH1 . ARG A  624 ? 0.4168 0.4542 0.4130 -0.0444 -0.0168 0.0045  650 ARG A NH1 
9350  N NH2 . ARG A  624 ? 0.4354 0.4718 0.4348 -0.0367 -0.0176 0.0047  650 ARG A NH2 
9364  N N   . LEU A  625 ? 0.2887 0.2769 0.2516 -0.0497 -0.0283 0.0224  651 LEU A N   
9365  C CA  . LEU A  625 ? 0.3030 0.2858 0.2595 -0.0531 -0.0288 0.0257  651 LEU A CA  
9366  C C   . LEU A  625 ? 0.3232 0.2977 0.2761 -0.0553 -0.0286 0.0267  651 LEU A C   
9367  O O   . LEU A  625 ? 0.3139 0.2830 0.2676 -0.0522 -0.0296 0.0271  651 LEU A O   
9368  C CB  . LEU A  625 ? 0.3052 0.2858 0.2598 -0.0500 -0.0313 0.0293  651 LEU A CB  
9369  C CG  . LEU A  625 ? 0.3042 0.2921 0.2599 -0.0498 -0.0315 0.0288  651 LEU A CG  
9370  C CD1 . LEU A  625 ? 0.3078 0.2953 0.2640 -0.0458 -0.0343 0.0317  651 LEU A CD1 
9371  C CD2 . LEU A  625 ? 0.3131 0.3022 0.2635 -0.0550 -0.0305 0.0297  651 LEU A CD2 
9383  N N   . LYS A  626 ? 0.3371 0.3103 0.2858 -0.0609 -0.0272 0.0272  652 LYS A N   
9384  C CA  . LYS A  626 ? 0.3617 0.3259 0.3058 -0.0641 -0.0268 0.0285  652 LYS A CA  
9385  C C   . LYS A  626 ? 0.3794 0.3355 0.3168 -0.0645 -0.0281 0.0335  652 LYS A C   
9386  O O   . LYS A  626 ? 0.3862 0.3321 0.3198 -0.0643 -0.0285 0.0357  652 LYS A O   
9387  C CB  . LYS A  626 ? 0.3912 0.3592 0.3349 -0.0703 -0.0242 0.0260  652 LYS A CB  
9388  C CG  . LYS A  626 ? 0.4659 0.4411 0.4162 -0.0697 -0.0232 0.0216  652 LYS A CG  
9389  C CD  . LYS A  626 ? 0.5489 0.5288 0.4995 -0.0758 -0.0208 0.0195  652 LYS A CD  
9390  C CE  . LYS A  626 ? 0.6139 0.6015 0.5711 -0.0749 -0.0202 0.0156  652 LYS A CE  
9391  N NZ  . LYS A  626 ? 0.6619 0.6567 0.6205 -0.0805 -0.0179 0.0136  652 LYS A NZ  
9405  N N   . HIS A  627 ? 0.3895 0.3498 0.3251 -0.0649 -0.0287 0.0354  653 HIS A N   
9406  C CA  . HIS A  627 ? 0.4157 0.3703 0.3453 -0.0647 -0.0305 0.0406  653 HIS A CA  
9407  C C   . HIS A  627 ? 0.4037 0.3662 0.3336 -0.0639 -0.0316 0.0412  653 HIS A C   
9408  O O   . HIS A  627 ? 0.4064 0.3772 0.3393 -0.0653 -0.0301 0.0376  653 HIS A O   
9409  C CB  . HIS A  627 ? 0.4624 0.4109 0.3849 -0.0707 -0.0291 0.0427  653 HIS A CB  
9410  C CG  . HIS A  627 ? 0.5432 0.4994 0.4650 -0.0761 -0.0267 0.0403  653 HIS A CG  
9411  N ND1 . HIS A  627 ? 0.5794 0.5409 0.5054 -0.0788 -0.0242 0.0358  653 HIS A ND1 
9412  C CD2 . HIS A  627 ? 0.5765 0.5362 0.4941 -0.0790 -0.0265 0.0420  653 HIS A CD2 
9413  C CE1 . HIS A  627 ? 0.5917 0.5597 0.5162 -0.0829 -0.0222 0.0348  653 HIS A CE1 
9414  N NE2 . HIS A  627 ? 0.5973 0.5641 0.5164 -0.0833 -0.0234 0.0382  653 HIS A NE2 
9422  N N   . ILE A  628 ? 0.3885 0.3486 0.3154 -0.0615 -0.0343 0.0456  654 ILE A N   
9423  C CA  . ILE A  628 ? 0.3724 0.3397 0.2987 -0.0614 -0.0356 0.0464  654 ILE A CA  
9424  C C   . ILE A  628 ? 0.3655 0.3302 0.2835 -0.0660 -0.0358 0.0502  654 ILE A C   
9425  O O   . ILE A  628 ? 0.3653 0.3218 0.2789 -0.0653 -0.0371 0.0548  654 ILE A O   
9426  C CB  . ILE A  628 ? 0.3693 0.3378 0.2986 -0.0554 -0.0388 0.0489  654 ILE A CB  
9427  C CG1 . ILE A  628 ? 0.3785 0.3500 0.3158 -0.0511 -0.0384 0.0450  654 ILE A CG1 
9428  C CG2 . ILE A  628 ? 0.3695 0.3452 0.2968 -0.0566 -0.0405 0.0501  654 ILE A CG2 
9429  C CD1 . ILE A  628 ? 0.3887 0.3590 0.3294 -0.0450 -0.0409 0.0474  654 ILE A CD1 
9441  N N   . PRO A  629 ? 0.3590 0.3297 0.2742 -0.0706 -0.0343 0.0485  655 PRO A N   
9442  C CA  . PRO A  629 ? 0.3580 0.3261 0.2645 -0.0750 -0.0345 0.0524  655 PRO A CA  
9443  C C   . PRO A  629 ? 0.3592 0.3253 0.2624 -0.0720 -0.0385 0.0582  655 PRO A C   
9444  O O   . PRO A  629 ? 0.3559 0.3272 0.2632 -0.0681 -0.0407 0.0579  655 PRO A O   
9445  C CB  . PRO A  629 ? 0.3640 0.3404 0.2692 -0.0792 -0.0323 0.0489  655 PRO A CB  
9446  C CG  . PRO A  629 ? 0.3678 0.3494 0.2809 -0.0778 -0.0300 0.0431  655 PRO A CG  
9447  C CD  . PRO A  629 ? 0.3499 0.3296 0.2692 -0.0717 -0.0321 0.0433  655 PRO A CD  
9455  N N   . ASN A  630 ? 0.3595 0.3184 0.2557 -0.0735 -0.0395 0.0635  656 ASN A N   
9456  C CA  . ASN A  630 ? 0.3641 0.3211 0.2572 -0.0701 -0.0434 0.0698  656 ASN A CA  
9457  C C   . ASN A  630 ? 0.3577 0.3245 0.2499 -0.0706 -0.0457 0.0700  656 ASN A C   
9458  O O   . ASN A  630 ? 0.3538 0.3239 0.2493 -0.0659 -0.0490 0.0722  656 ASN A O   
9459  C CB  . ASN A  630 ? 0.3790 0.3268 0.2634 -0.0727 -0.0435 0.0755  656 ASN A CB  
9460  C CG  . ASN A  630 ? 0.4060 0.3428 0.2910 -0.0720 -0.0415 0.0756  656 ASN A CG  
9461  O OD1 . ASN A  630 ? 0.4139 0.3474 0.3046 -0.0668 -0.0420 0.0747  656 ASN A OD1 
9462  N ND2 . ASN A  630 ? 0.4149 0.3455 0.2935 -0.0775 -0.0391 0.0766  656 ASN A ND2 
9469  N N   . GLU A  631 ? 0.3604 0.3324 0.2487 -0.0763 -0.0437 0.0671  657 GLU A N   
9470  C CA  . GLU A  631 ? 0.3707 0.3517 0.2572 -0.0779 -0.0453 0.0665  657 GLU A CA  
9471  C C   . GLU A  631 ? 0.3680 0.3557 0.2630 -0.0743 -0.0457 0.0621  657 GLU A C   
9472  O O   . GLU A  631 ? 0.3778 0.3713 0.2731 -0.0731 -0.0488 0.0634  657 GLU A O   
9473  C CB  . GLU A  631 ? 0.4176 0.4016 0.2981 -0.0849 -0.0421 0.0636  657 GLU A CB  
9474  C CG  . GLU A  631 ? 0.5161 0.5077 0.3919 -0.0879 -0.0435 0.0633  657 GLU A CG  
9475  C CD  . GLU A  631 ? 0.6226 0.6163 0.4915 -0.0947 -0.0399 0.0605  657 GLU A CD  
9476  O OE1 . GLU A  631 ? 0.6534 0.6441 0.5229 -0.0970 -0.0359 0.0579  657 GLU A OE1 
9477  O OE2 . GLU A  631 ? 0.6301 0.6288 0.4930 -0.0980 -0.0410 0.0608  657 GLU A OE2 
9484  N N   . ALA A  632 ? 0.3507 0.3379 0.2524 -0.0730 -0.0428 0.0570  658 ALA A N   
9485  C CA  . ALA A  632 ? 0.3473 0.3400 0.2568 -0.0695 -0.0429 0.0530  658 ALA A CA  
9486  C C   . ALA A  632 ? 0.3364 0.3281 0.2505 -0.0633 -0.0464 0.0564  658 ALA A C   
9487  O O   . ALA A  632 ? 0.3251 0.3231 0.2429 -0.0613 -0.0483 0.0556  658 ALA A O   
9488  C CB  . ALA A  632 ? 0.3469 0.3392 0.2621 -0.0692 -0.0391 0.0475  658 ALA A CB  
9494  N N   . PHE A  633 ? 0.3337 0.3176 0.2477 -0.0603 -0.0472 0.0602  659 PHE A N   
9495  C CA  . PHE A  633 ? 0.3401 0.3227 0.2585 -0.0539 -0.0502 0.0635  659 PHE A CA  
9496  C C   . PHE A  633 ? 0.3312 0.3186 0.2464 -0.0533 -0.0543 0.0687  659 PHE A C   
9497  O O   . PHE A  633 ? 0.3124 0.3054 0.2326 -0.0495 -0.0567 0.0695  659 PHE A O   
9498  C CB  . PHE A  633 ? 0.3483 0.3202 0.2660 -0.0511 -0.0498 0.0665  659 PHE A CB  
9499  C CG  . PHE A  633 ? 0.3550 0.3254 0.2786 -0.0439 -0.0518 0.0686  659 PHE A CG  
9500  C CD1 . PHE A  633 ? 0.3694 0.3396 0.2917 -0.0402 -0.0553 0.0749  659 PHE A CD1 
9501  C CD2 . PHE A  633 ? 0.3593 0.3295 0.2898 -0.0407 -0.0502 0.0644  659 PHE A CD2 
9502  C CE1 . PHE A  633 ? 0.3751 0.3449 0.3033 -0.0333 -0.0568 0.0767  659 PHE A CE1 
9503  C CE2 . PHE A  633 ? 0.3679 0.3371 0.3036 -0.0342 -0.0516 0.0661  659 PHE A CE2 
9504  C CZ  . PHE A  633 ? 0.3690 0.3381 0.3037 -0.0304 -0.0548 0.0722  659 PHE A CZ  
9514  N N   . LEU A  634 ? 0.3324 0.3182 0.2393 -0.0574 -0.0550 0.0722  660 LEU A N   
9515  C CA  . LEU A  634 ? 0.3466 0.3375 0.2495 -0.0576 -0.0590 0.0773  660 LEU A CA  
9516  C C   . LEU A  634 ? 0.3433 0.3453 0.2477 -0.0599 -0.0601 0.0740  660 LEU A C   
9517  O O   . LEU A  634 ? 0.3547 0.3628 0.2586 -0.0588 -0.0640 0.0778  660 LEU A O   
9518  C CB  . LEU A  634 ? 0.3643 0.3512 0.2571 -0.0622 -0.0592 0.0815  660 LEU A CB  
9519  C CG  . LEU A  634 ? 0.4089 0.3845 0.2986 -0.0597 -0.0593 0.0870  660 LEU A CG  
9520  C CD1 . LEU A  634 ? 0.4241 0.3961 0.3031 -0.0649 -0.0592 0.0911  660 LEU A CD1 
9521  C CD2 . LEU A  634 ? 0.4215 0.3968 0.3148 -0.0525 -0.0631 0.0927  660 LEU A CD2 
9533  N N   . ASN A  635 ? 0.3248 0.3293 0.2310 -0.0632 -0.0566 0.0672  661 ASN A N   
9534  C CA  . ASN A  635 ? 0.3201 0.3335 0.2273 -0.0656 -0.0570 0.0635  661 ASN A CA  
9535  C C   . ASN A  635 ? 0.3099 0.3272 0.2267 -0.0610 -0.0574 0.0608  661 ASN A C   
9536  O O   . ASN A  635 ? 0.3068 0.3307 0.2250 -0.0630 -0.0572 0.0572  661 ASN A O   
9537  C CB  . ASN A  635 ? 0.3367 0.3509 0.2399 -0.0717 -0.0529 0.0579  661 ASN A CB  
9538  C CG  . ASN A  635 ? 0.3946 0.4074 0.2875 -0.0773 -0.0526 0.0602  661 ASN A CG  
9539  O OD1 . ASN A  635 ? 0.4214 0.4320 0.3110 -0.0814 -0.0486 0.0568  661 ASN A OD1 
9540  N ND2 . ASN A  635 ? 0.3889 0.4034 0.2762 -0.0779 -0.0567 0.0661  661 ASN A ND2 
9547  N N   . LEU A  636 ? 0.2986 0.3118 0.2212 -0.0550 -0.0579 0.0627  662 LEU A N   
9548  C CA  . LEU A  636 ? 0.2934 0.3108 0.2247 -0.0504 -0.0586 0.0609  662 LEU A CA  
9549  C C   . LEU A  636 ? 0.3016 0.3269 0.2333 -0.0492 -0.0632 0.0652  662 LEU A C   
9550  O O   . LEU A  636 ? 0.3043 0.3292 0.2309 -0.0495 -0.0660 0.0709  662 LEU A O   
9551  C CB  . LEU A  636 ? 0.2879 0.2987 0.2246 -0.0446 -0.0577 0.0616  662 LEU A CB  
9552  C CG  . LEU A  636 ? 0.3036 0.3076 0.2405 -0.0457 -0.0536 0.0575  662 LEU A CG  
9553  C CD1 . LEU A  636 ? 0.3139 0.3114 0.2553 -0.0402 -0.0531 0.0584  662 LEU A CD1 
9554  C CD2 . LEU A  636 ? 0.3015 0.3099 0.2416 -0.0480 -0.0506 0.0509  662 LEU A CD2 
9566  N N   . PRO A  637 ? 0.3087 0.3416 0.2458 -0.0485 -0.0640 0.0628  663 PRO A N   
9567  C CA  . PRO A  637 ? 0.3107 0.3524 0.2484 -0.0481 -0.0685 0.0668  663 PRO A CA  
9568  C C   . PRO A  637 ? 0.3231 0.3640 0.2629 -0.0421 -0.0718 0.0739  663 PRO A C   
9569  O O   . PRO A  637 ? 0.3267 0.3631 0.2723 -0.0364 -0.0708 0.0743  663 PRO A O   
9570  C CB  . PRO A  637 ? 0.3114 0.3597 0.2564 -0.0472 -0.0680 0.0627  663 PRO A CB  
9571  C CG  . PRO A  637 ? 0.3170 0.3604 0.2626 -0.0491 -0.0632 0.0562  663 PRO A CG  
9572  C CD  . PRO A  637 ? 0.3019 0.3359 0.2449 -0.0481 -0.0609 0.0566  663 PRO A CD  
9580  N N   . ALA A  638 ? 0.3234 0.3680 0.2580 -0.0433 -0.0756 0.0797  664 ALA A N   
9581  C CA  . ALA A  638 ? 0.3347 0.3789 0.2711 -0.0372 -0.0789 0.0871  664 ALA A CA  
9582  C C   . ALA A  638 ? 0.3317 0.3839 0.2778 -0.0316 -0.0811 0.0884  664 ALA A C   
9583  O O   . ALA A  638 ? 0.3381 0.3892 0.2878 -0.0251 -0.0828 0.0938  664 ALA A O   
9584  C CB  . ALA A  638 ? 0.3398 0.3878 0.2686 -0.0401 -0.0828 0.0930  664 ALA A CB  
9590  N N   . SER A  639 ? 0.3181 0.3777 0.2687 -0.0340 -0.0804 0.0833  665 SER A N   
9591  C CA  . SER A  639 ? 0.3132 0.3809 0.2731 -0.0297 -0.0818 0.0836  665 SER A CA  
9592  C C   . SER A  639 ? 0.3034 0.3641 0.2702 -0.0236 -0.0784 0.0812  665 SER A C   
9593  O O   . SER A  639 ? 0.3005 0.3670 0.2752 -0.0193 -0.0790 0.0817  665 SER A O   
9594  C CB  . SER A  639 ? 0.3222 0.3990 0.2832 -0.0354 -0.0817 0.0785  665 SER A CB  
9595  O OG  . SER A  639 ? 0.3356 0.4058 0.2940 -0.0394 -0.0772 0.0717  665 SER A OG  
9601  N N   . LEU A  640 ? 0.2949 0.3441 0.2589 -0.0238 -0.0746 0.0783  666 LEU A N   
9602  C CA  . LEU A  640 ? 0.2950 0.3378 0.2647 -0.0189 -0.0714 0.0755  666 LEU A CA  
9603  C C   . LEU A  640 ? 0.2984 0.3402 0.2737 -0.0108 -0.0727 0.0803  666 LEU A C   
9604  O O   . LEU A  640 ? 0.3023 0.3406 0.2747 -0.0081 -0.0745 0.0860  666 LEU A O   
9605  C CB  . LEU A  640 ? 0.2982 0.3292 0.2632 -0.0207 -0.0678 0.0725  666 LEU A CB  
9606  C CG  . LEU A  640 ? 0.3038 0.3345 0.2657 -0.0271 -0.0649 0.0662  666 LEU A CG  
9607  C CD1 . LEU A  640 ? 0.3044 0.3246 0.2622 -0.0284 -0.0618 0.0643  666 LEU A CD1 
9608  C CD2 . LEU A  640 ? 0.3121 0.3473 0.2806 -0.0266 -0.0631 0.0610  666 LEU A CD2 
9620  N N   . THR A  641 ? 0.2930 0.3374 0.2760 -0.0068 -0.0713 0.0779  667 THR A N   
9621  C CA  . THR A  641 ? 0.2976 0.3401 0.2863 0.0012  -0.0714 0.0813  667 THR A CA  
9622  C C   . THR A  641 ? 0.2986 0.3304 0.2885 0.0037  -0.0671 0.0770  667 THR A C   
9623  O O   . THR A  641 ? 0.3078 0.3330 0.2993 0.0096  -0.0662 0.0794  667 THR A O   
9624  C CB  . THR A  641 ? 0.3091 0.3643 0.3061 0.0042  -0.0733 0.0826  667 THR A CB  
9625  O OG1 . THR A  641 ? 0.3279 0.3858 0.3291 0.0025  -0.0708 0.0766  667 THR A OG1 
9626  C CG2 . THR A  641 ? 0.3136 0.3807 0.3095 0.0010  -0.0778 0.0865  667 THR A CG2 
9634  N N   . GLU A  642 ? 0.2916 0.3218 0.2807 -0.0006 -0.0643 0.0708  668 GLU A N   
9635  C CA  . GLU A  642 ? 0.2899 0.3119 0.2803 0.0012  -0.0606 0.0666  668 GLU A CA  
9636  C C   . GLU A  642 ? 0.2874 0.3043 0.2723 -0.0048 -0.0584 0.0622  668 GLU A C   
9637  O O   . GLU A  642 ? 0.2891 0.3117 0.2736 -0.0095 -0.0582 0.0591  668 GLU A O   
9638  C CB  . GLU A  642 ? 0.3160 0.3447 0.3138 0.0034  -0.0596 0.0635  668 GLU A CB  
9639  C CG  . GLU A  642 ? 0.3664 0.3885 0.3659 0.0052  -0.0559 0.0590  668 GLU A CG  
9640  C CD  . GLU A  642 ? 0.4042 0.4326 0.4107 0.0077  -0.0548 0.0565  668 GLU A CD  
9641  O OE1 . GLU A  642 ? 0.3836 0.4213 0.3946 0.0091  -0.0568 0.0589  668 GLU A OE1 
9642  O OE2 . GLU A  642 ? 0.4366 0.4609 0.4439 0.0081  -0.0519 0.0524  668 GLU A OE2 
9649  N N   . LEU A  643 ? 0.2803 0.2866 0.2612 -0.0048 -0.0566 0.0618  669 LEU A N   
9650  C CA  . LEU A  643 ? 0.2690 0.2709 0.2450 -0.0104 -0.0544 0.0580  669 LEU A CA  
9651  C C   . LEU A  643 ? 0.2646 0.2587 0.2415 -0.0089 -0.0513 0.0545  669 LEU A C   
9652  O O   . LEU A  643 ? 0.2621 0.2480 0.2378 -0.0056 -0.0509 0.0565  669 LEU A O   
9653  C CB  . LEU A  643 ? 0.2716 0.2688 0.2402 -0.0134 -0.0556 0.0617  669 LEU A CB  
9654  C CG  . LEU A  643 ? 0.2947 0.2867 0.2577 -0.0192 -0.0533 0.0587  669 LEU A CG  
9655  C CD1 . LEU A  643 ? 0.2940 0.2930 0.2578 -0.0239 -0.0520 0.0538  669 LEU A CD1 
9656  C CD2 . LEU A  643 ? 0.3023 0.2901 0.2580 -0.0218 -0.0547 0.0632  669 LEU A CD2 
9668  N N   . HIS A  644 ? 0.2556 0.2521 0.2345 -0.0113 -0.0491 0.0492  670 HIS A N   
9669  C CA  . HIS A  644 ? 0.2578 0.2484 0.2373 -0.0106 -0.0464 0.0456  670 HIS A CA  
9670  C C   . HIS A  644 ? 0.2560 0.2441 0.2312 -0.0162 -0.0447 0.0430  670 HIS A C   
9671  O O   . HIS A  644 ? 0.2382 0.2318 0.2128 -0.0201 -0.0445 0.0412  670 HIS A O   
9672  C CB  . HIS A  644 ? 0.2727 0.2682 0.2582 -0.0083 -0.0451 0.0420  670 HIS A CB  
9673  C CG  . HIS A  644 ? 0.3205 0.3196 0.3110 -0.0030 -0.0463 0.0442  670 HIS A CG  
9674  N ND1 . HIS A  644 ? 0.3513 0.3462 0.3443 0.0019  -0.0451 0.0438  670 HIS A ND1 
9675  C CD2 . HIS A  644 ? 0.3380 0.3451 0.3314 -0.0021 -0.0484 0.0465  670 HIS A CD2 
9676  C CE1 . HIS A  644 ? 0.3584 0.3589 0.3561 0.0059  -0.0464 0.0460  670 HIS A CE1 
9677  N NE2 . HIS A  644 ? 0.3501 0.3584 0.3484 0.0035  -0.0485 0.0477  670 HIS A NE2 
9685  N N   . ILE A  645 ? 0.2635 0.2431 0.2353 -0.0169 -0.0435 0.0428  671 ILE A N   
9686  C CA  . ILE A  645 ? 0.2751 0.2523 0.2433 -0.0222 -0.0416 0.0402  671 ILE A CA  
9687  C C   . ILE A  645 ? 0.2829 0.2546 0.2521 -0.0212 -0.0396 0.0371  671 ILE A C   
9688  O O   . ILE A  645 ? 0.2935 0.2600 0.2591 -0.0247 -0.0383 0.0362  671 ILE A O   
9689  C CB  . ILE A  645 ? 0.2864 0.2585 0.2478 -0.0258 -0.0423 0.0436  671 ILE A CB  
9690  C CG1 . ILE A  645 ? 0.2938 0.2692 0.2537 -0.0247 -0.0452 0.0484  671 ILE A CG1 
9691  C CG2 . ILE A  645 ? 0.2942 0.2681 0.2527 -0.0320 -0.0404 0.0408  671 ILE A CG2 
9692  C CD1 . ILE A  645 ? 0.3129 0.2830 0.2654 -0.0280 -0.0460 0.0526  671 ILE A CD1 
9704  N N   . ASN A  646 ? 0.2711 0.2443 0.2451 -0.0168 -0.0393 0.0356  672 ASN A N   
9705  C CA  . ASN A  646 ? 0.2743 0.2429 0.2491 -0.0155 -0.0377 0.0328  672 ASN A CA  
9706  C C   . ASN A  646 ? 0.2719 0.2445 0.2477 -0.0191 -0.0360 0.0284  672 ASN A C   
9707  O O   . ASN A  646 ? 0.2617 0.2415 0.2392 -0.0211 -0.0358 0.0273  672 ASN A O   
9708  C CB  . ASN A  646 ? 0.2801 0.2496 0.2593 -0.0096 -0.0378 0.0328  672 ASN A CB  
9709  C CG  . ASN A  646 ? 0.3025 0.2818 0.2869 -0.0082 -0.0382 0.0316  672 ASN A CG  
9710  O OD1 . ASN A  646 ? 0.3130 0.2977 0.2982 -0.0088 -0.0396 0.0336  672 ASN A OD1 
9711  N ND2 . ASN A  646 ? 0.3075 0.2894 0.2953 -0.0067 -0.0369 0.0284  672 ASN A ND2 
9718  N N   . ASP A  647 ? 0.2784 0.2465 0.2532 -0.0199 -0.0346 0.0260  673 ASP A N   
9719  C CA  . ASP A  647 ? 0.2839 0.2566 0.2602 -0.0229 -0.0332 0.0221  673 ASP A CA  
9720  C C   . ASP A  647 ? 0.2777 0.2546 0.2527 -0.0280 -0.0326 0.0217  673 ASP A C   
9721  O O   . ASP A  647 ? 0.2723 0.2569 0.2504 -0.0288 -0.0319 0.0197  673 ASP A O   
9722  C CB  . ASP A  647 ? 0.3178 0.2974 0.2997 -0.0194 -0.0329 0.0200  673 ASP A CB  
9723  C CG  . ASP A  647 ? 0.3976 0.3731 0.3806 -0.0146 -0.0330 0.0200  673 ASP A CG  
9724  O OD1 . ASP A  647 ? 0.3941 0.3620 0.3739 -0.0150 -0.0325 0.0194  673 ASP A OD1 
9725  O OD2 . ASP A  647 ? 0.4544 0.4341 0.4412 -0.0107 -0.0334 0.0206  673 ASP A OD2 
9730  N N   . ASN A  648 ? 0.2795 0.2507 0.2494 -0.0313 -0.0327 0.0237  674 ASN A N   
9731  C CA  . ASN A  648 ? 0.2794 0.2529 0.2468 -0.0368 -0.0318 0.0234  674 ASN A CA  
9732  C C   . ASN A  648 ? 0.2960 0.2625 0.2597 -0.0404 -0.0308 0.0225  674 ASN A C   
9733  O O   . ASN A  648 ? 0.2979 0.2610 0.2624 -0.0387 -0.0306 0.0209  674 ASN A O   
9734  C CB  . ASN A  648 ? 0.2837 0.2566 0.2478 -0.0376 -0.0330 0.0271  674 ASN A CB  
9735  C CG  . ASN A  648 ? 0.2846 0.2658 0.2521 -0.0361 -0.0335 0.0268  674 ASN A CG  
9736  O OD1 . ASN A  648 ? 0.2868 0.2741 0.2555 -0.0387 -0.0320 0.0244  674 ASN A OD1 
9737  N ND2 . ASN A  648 ? 0.2604 0.2420 0.2294 -0.0320 -0.0353 0.0290  674 ASN A ND2 
9744  N N   A MET A  649 ? 0.3020 0.2669 0.2617 -0.0457 -0.0300 0.0233  675 MET A N   
9745  N N   B MET A  649 ? 0.3025 0.2674 0.2622 -0.0457 -0.0300 0.0233  675 MET A N   
9746  C CA  A MET A  649 ? 0.3198 0.2778 0.2755 -0.0499 -0.0289 0.0226  675 MET A CA  
9747  C CA  B MET A  649 ? 0.3207 0.2787 0.2763 -0.0500 -0.0289 0.0226  675 MET A CA  
9748  C C   A MET A  649 ? 0.3273 0.2773 0.2765 -0.0525 -0.0292 0.0267  675 MET A C   
9749  C C   B MET A  649 ? 0.3277 0.2776 0.2768 -0.0525 -0.0292 0.0267  675 MET A C   
9750  O O   A MET A  649 ? 0.3289 0.2769 0.2744 -0.0582 -0.0279 0.0266  675 MET A O   
9751  O O   B MET A  649 ? 0.3291 0.2771 0.2746 -0.0582 -0.0279 0.0266  675 MET A O   
9752  C CB  A MET A  649 ? 0.3313 0.2970 0.2891 -0.0548 -0.0272 0.0192  675 MET A CB  
9753  C CB  B MET A  649 ? 0.3333 0.2990 0.2910 -0.0549 -0.0272 0.0193  675 MET A CB  
9754  C CG  A MET A  649 ? 0.3645 0.3381 0.3285 -0.0521 -0.0270 0.0157  675 MET A CG  
9755  C CG  B MET A  649 ? 0.3688 0.3422 0.3325 -0.0525 -0.0270 0.0158  675 MET A CG  
9756  S SD  A MET A  649 ? 0.4276 0.4114 0.3972 -0.0479 -0.0273 0.0155  675 MET A SD  
9757  S SD  B MET A  649 ? 0.4392 0.4234 0.4063 -0.0575 -0.0251 0.0125  675 MET A SD  
9758  C CE  A MET A  649 ? 0.4319 0.4218 0.4073 -0.0448 -0.0271 0.0120  675 MET A CE  
9759  C CE  B MET A  649 ? 0.3975 0.3895 0.3666 -0.0566 -0.0244 0.0135  675 MET A CE  
9778  N N   . LEU A  650 ? 0.3295 0.2753 0.2772 -0.0483 -0.0308 0.0304  676 LEU A N   
9779  C CA  . LEU A  650 ? 0.3508 0.2896 0.2923 -0.0501 -0.0314 0.0349  676 LEU A CA  
9780  C C   . LEU A  650 ? 0.3753 0.3016 0.3114 -0.0524 -0.0304 0.0358  676 LEU A C   
9781  O O   . LEU A  650 ? 0.3734 0.2930 0.3098 -0.0489 -0.0304 0.0354  676 LEU A O   
9782  C CB  . LEU A  650 ? 0.3495 0.2874 0.2913 -0.0445 -0.0337 0.0390  676 LEU A CB  
9783  C CG  . LEU A  650 ? 0.3495 0.2984 0.2953 -0.0428 -0.0350 0.0389  676 LEU A CG  
9784  C CD1 . LEU A  650 ? 0.3549 0.3032 0.3018 -0.0371 -0.0374 0.0428  676 LEU A CD1 
9785  C CD2 . LEU A  650 ? 0.3471 0.3008 0.2898 -0.0479 -0.0345 0.0394  676 LEU A CD2 
9797  N N   . LYS A  651 ? 0.3946 0.3177 0.3255 -0.0585 -0.0292 0.0370  677 LYS A N   
9798  C CA  . LYS A  651 ? 0.4258 0.3361 0.3504 -0.0617 -0.0280 0.0383  677 LYS A CA  
9799  C C   . LYS A  651 ? 0.4526 0.3538 0.3713 -0.0601 -0.0290 0.0444  677 LYS A C   
9800  O O   . LYS A  651 ? 0.4759 0.3641 0.3899 -0.0597 -0.0283 0.0464  677 LYS A O   
9801  C CB  . LYS A  651 ? 0.4658 0.3781 0.3883 -0.0698 -0.0258 0.0360  677 LYS A CB  
9802  C CG  . LYS A  651 ? 0.5469 0.4666 0.4747 -0.0716 -0.0248 0.0303  677 LYS A CG  
9803  C CD  . LYS A  651 ? 0.6333 0.5499 0.5579 -0.0793 -0.0226 0.0281  677 LYS A CD  
9804  C CE  . LYS A  651 ? 0.6997 0.6226 0.6292 -0.0804 -0.0221 0.0229  677 LYS A CE  
9805  N NZ  . LYS A  651 ? 0.7415 0.6650 0.6690 -0.0886 -0.0202 0.0207  677 LYS A NZ  
9819  N N   . PHE A  652 ? 0.4459 0.3535 0.3645 -0.0591 -0.0306 0.0475  678 PHE A N   
9820  C CA  . PHE A  652 ? 0.4460 0.3470 0.3592 -0.0573 -0.0321 0.0538  678 PHE A CA  
9821  C C   . PHE A  652 ? 0.4243 0.3334 0.3414 -0.0515 -0.0349 0.0559  678 PHE A C   
9822  O O   . PHE A  652 ? 0.4168 0.3373 0.3393 -0.0511 -0.0353 0.0527  678 PHE A O   
9823  C CB  . PHE A  652 ? 0.4536 0.3542 0.3605 -0.0641 -0.0312 0.0559  678 PHE A CB  
9826  N N   . PHE A  653 ? 0.4118 0.3147 0.3263 -0.0471 -0.0367 0.0615  679 PHE A N   
9827  C CA  . PHE A  653 ? 0.3979 0.3082 0.3155 -0.0419 -0.0397 0.0645  679 PHE A CA  
9828  C C   . PHE A  653 ? 0.4013 0.3054 0.3125 -0.0412 -0.0413 0.0716  679 PHE A C   
9829  O O   . PHE A  653 ? 0.4012 0.2931 0.3089 -0.0390 -0.0407 0.0747  679 PHE A O   
9830  C CB  . PHE A  653 ? 0.3822 0.2930 0.3062 -0.0345 -0.0405 0.0636  679 PHE A CB  
9831  C CG  . PHE A  653 ? 0.3737 0.2943 0.3019 -0.0301 -0.0435 0.0662  679 PHE A CG  
9832  C CD1 . PHE A  653 ? 0.3751 0.3083 0.3075 -0.0317 -0.0441 0.0629  679 PHE A CD1 
9833  C CD2 . PHE A  653 ? 0.3804 0.2976 0.3077 -0.0246 -0.0456 0.0721  679 PHE A CD2 
9834  C CE1 . PHE A  653 ? 0.3752 0.3173 0.3109 -0.0285 -0.0468 0.0651  679 PHE A CE1 
9835  C CE2 . PHE A  653 ? 0.3802 0.3076 0.3113 -0.0212 -0.0486 0.0746  679 PHE A CE2 
9836  C CZ  . PHE A  653 ? 0.3688 0.3085 0.3040 -0.0234 -0.0492 0.0709  679 PHE A CZ  
9846  N N   . ASN A  654 ? 0.4012 0.3129 0.3101 -0.0436 -0.0431 0.0740  680 ASN A N   
9847  C CA  . ASN A  654 ? 0.4205 0.3274 0.3227 -0.0435 -0.0449 0.0811  680 ASN A CA  
9848  C C   . ASN A  654 ? 0.4218 0.3313 0.3275 -0.0357 -0.0481 0.0856  680 ASN A C   
9849  O O   . ASN A  654 ? 0.4098 0.3309 0.3185 -0.0347 -0.0506 0.0860  680 ASN A O   
9850  C CB  . ASN A  654 ? 0.4405 0.3547 0.3381 -0.0499 -0.0452 0.0814  680 ASN A CB  
9851  C CG  . ASN A  654 ? 0.4913 0.4019 0.3812 -0.0508 -0.0470 0.0885  680 ASN A CG  
9852  O OD1 . ASN A  654 ? 0.4929 0.3948 0.3806 -0.0463 -0.0482 0.0941  680 ASN A OD1 
9853  N ND2 . ASN A  654 ? 0.5302 0.4460 0.4150 -0.0570 -0.0468 0.0885  680 ASN A ND2 
9860  N N   . TRP A  655 ? 0.4301 0.3288 0.3356 -0.0302 -0.0479 0.0887  681 TRP A N   
9861  C CA  . TRP A  655 ? 0.4309 0.3314 0.3405 -0.0220 -0.0505 0.0931  681 TRP A CA  
9862  C C   . TRP A  655 ? 0.4341 0.3395 0.3403 -0.0211 -0.0541 0.1003  681 TRP A C   
9863  O O   . TRP A  655 ? 0.4319 0.3454 0.3430 -0.0156 -0.0570 0.1030  681 TRP A O   
9864  C CB  . TRP A  655 ? 0.4317 0.3177 0.3406 -0.0167 -0.0488 0.0952  681 TRP A CB  
9865  C CG  . TRP A  655 ? 0.4254 0.3070 0.3377 -0.0169 -0.0456 0.0884  681 TRP A CG  
9866  C CD1 . TRP A  655 ? 0.4345 0.3073 0.3428 -0.0225 -0.0424 0.0845  681 TRP A CD1 
9867  C CD2 . TRP A  655 ? 0.4185 0.3059 0.3390 -0.0120 -0.0455 0.0845  681 TRP A CD2 
9868  N NE1 . TRP A  655 ? 0.4307 0.3036 0.3440 -0.0213 -0.0405 0.0784  681 TRP A NE1 
9869  C CE2 . TRP A  655 ? 0.4265 0.3080 0.3471 -0.0148 -0.0423 0.0783  681 TRP A CE2 
9870  C CE3 . TRP A  655 ? 0.4216 0.3192 0.3493 -0.0059 -0.0478 0.0855  681 TRP A CE3 
9871  C CZ2 . TRP A  655 ? 0.4300 0.3147 0.3571 -0.0113 -0.0413 0.0736  681 TRP A CZ2 
9872  C CZ3 . TRP A  655 ? 0.4277 0.3281 0.3620 -0.0025 -0.0465 0.0808  681 TRP A CZ3 
9873  C CH2 . TRP A  655 ? 0.4295 0.3236 0.3633 -0.0052 -0.0433 0.0749  681 TRP A CH2 
9884  N N   . THR A  656 ? 0.4438 0.3447 0.3415 -0.0264 -0.0540 0.1035  682 THR A N   
9885  C CA  . THR A  656 ? 0.4522 0.3575 0.3454 -0.0262 -0.0574 0.1105  682 THR A CA  
9886  C C   . THR A  656 ? 0.4354 0.3577 0.3324 -0.0274 -0.0604 0.1089  682 THR A C   
9887  O O   . THR A  656 ? 0.4329 0.3616 0.3297 -0.0244 -0.0641 0.1146  682 THR A O   
9888  C CB  . THR A  656 ? 0.4941 0.3921 0.3770 -0.0332 -0.0561 0.1129  682 THR A CB  
9889  O OG1 . THR A  656 ? 0.5278 0.4095 0.4071 -0.0331 -0.0529 0.1134  682 THR A OG1 
9890  C CG2 . THR A  656 ? 0.5040 0.4045 0.3810 -0.0327 -0.0596 0.1210  682 THR A CG2 
9898  N N   . LEU A  657 ? 0.4249 0.3546 0.3254 -0.0317 -0.0587 0.1015  683 LEU A N   
9899  C CA  . LEU A  657 ? 0.4262 0.3707 0.3297 -0.0338 -0.0608 0.0991  683 LEU A CA  
9900  C C   . LEU A  657 ? 0.4336 0.3867 0.3455 -0.0272 -0.0635 0.0997  683 LEU A C   
9901  O O   . LEU A  657 ? 0.4301 0.3952 0.3436 -0.0287 -0.0659 0.0992  683 LEU A O   
9902  C CB  . LEU A  657 ? 0.4267 0.3748 0.3315 -0.0397 -0.0576 0.0911  683 LEU A CB  
9903  C CG  . LEU A  657 ? 0.4598 0.4014 0.3571 -0.0468 -0.0547 0.0899  683 LEU A CG  
9904  C CD1 . LEU A  657 ? 0.4578 0.4051 0.3576 -0.0518 -0.0517 0.0822  683 LEU A CD1 
9905  C CD2 . LEU A  657 ? 0.4748 0.4170 0.3632 -0.0505 -0.0565 0.0954  683 LEU A CD2 
9917  N N   . LEU A  658 ? 0.4391 0.3863 0.3559 -0.0203 -0.0630 0.1009  684 LEU A N   
9918  C CA  . LEU A  658 ? 0.4437 0.3995 0.3686 -0.0139 -0.0654 0.1020  684 LEU A CA  
9919  C C   . LEU A  658 ? 0.4663 0.4292 0.3900 -0.0112 -0.0700 0.1097  684 LEU A C   
9920  O O   . LEU A  658 ? 0.4619 0.4352 0.3921 -0.0073 -0.0725 0.1106  684 LEU A O   
9921  C CB  . LEU A  658 ? 0.4362 0.3836 0.3662 -0.0069 -0.0634 0.1016  684 LEU A CB  
9922  C CG  . LEU A  658 ? 0.4387 0.3807 0.3708 -0.0090 -0.0594 0.0940  684 LEU A CG  
9923  C CD1 . LEU A  658 ? 0.4336 0.3672 0.3697 -0.0022 -0.0576 0.0939  684 LEU A CD1 
9924  C CD2 . LEU A  658 ? 0.4441 0.3980 0.3815 -0.0119 -0.0592 0.0877  684 LEU A CD2 
9936  N N   . GLN A  659 ? 0.4859 0.4437 0.4010 -0.0136 -0.0711 0.1152  685 GLN A N   
9937  C CA  . GLN A  659 ? 0.5017 0.4664 0.4142 -0.0119 -0.0757 0.1229  685 GLN A CA  
9938  C C   . GLN A  659 ? 0.5065 0.4874 0.4206 -0.0160 -0.0786 0.1209  685 GLN A C   
9939  O O   . GLN A  659 ? 0.5075 0.4983 0.4240 -0.0129 -0.0828 0.1259  685 GLN A O   
9940  C CB  . GLN A  659 ? 0.5345 0.4907 0.4361 -0.0157 -0.0758 0.1280  685 GLN A CB  
9941  C CG  . GLN A  659 ? 0.5927 0.5329 0.4915 -0.0110 -0.0739 0.1326  685 GLN A CG  
9942  C CD  . GLN A  659 ? 0.6545 0.5870 0.5421 -0.0154 -0.0741 0.1378  685 GLN A CD  
9943  O OE1 . GLN A  659 ? 0.6724 0.5998 0.5543 -0.0227 -0.0712 0.1340  685 GLN A OE1 
9944  N NE2 . GLN A  659 ? 0.6652 0.5976 0.5498 -0.0112 -0.0775 0.1468  685 GLN A NE2 
9953  N N   . GLN A  660 ? 0.5090 0.4926 0.4213 -0.0232 -0.0764 0.1139  686 GLN A N   
9954  C CA  . GLN A  660 ? 0.5103 0.5079 0.4232 -0.0280 -0.0784 0.1109  686 GLN A CA  
9955  C C   . GLN A  660 ? 0.4837 0.4903 0.4066 -0.0250 -0.0787 0.1067  686 GLN A C   
9956  O O   . GLN A  660 ? 0.4852 0.5022 0.4087 -0.0294 -0.0797 0.1033  686 GLN A O   
9957  C CB  . GLN A  660 ? 0.5557 0.5519 0.4630 -0.0364 -0.0753 0.1048  686 GLN A CB  
9958  C CG  . GLN A  660 ? 0.6524 0.6390 0.5498 -0.0406 -0.0737 0.1074  686 GLN A CG  
9959  C CD  . GLN A  660 ? 0.7546 0.7403 0.6458 -0.0391 -0.0774 0.1163  686 GLN A CD  
9960  O OE1 . GLN A  660 ? 0.7816 0.7778 0.6712 -0.0404 -0.0812 0.1192  686 GLN A OE1 
9961  N NE2 . GLN A  660 ? 0.7953 0.7683 0.6829 -0.0365 -0.0762 0.1208  686 GLN A NE2 
9970  N N   . PHE A  661 ? 0.4620 0.4644 0.3922 -0.0181 -0.0775 0.1065  687 PHE A N   
9971  C CA  . PHE A  661 ? 0.4450 0.4554 0.3847 -0.0151 -0.0774 0.1027  687 PHE A CA  
9972  C C   . PHE A  661 ? 0.4276 0.4405 0.3734 -0.0066 -0.0799 0.1085  687 PHE A C   
9973  O O   . PHE A  661 ? 0.4202 0.4262 0.3707 -0.0009 -0.0777 0.1079  687 PHE A O   
9974  C CB  . PHE A  661 ? 0.4488 0.4518 0.3915 -0.0154 -0.0727 0.0956  687 PHE A CB  
9975  C CG  . PHE A  661 ? 0.4616 0.4638 0.3992 -0.0232 -0.0703 0.0900  687 PHE A CG  
9976  C CD1 . PHE A  661 ? 0.4764 0.4690 0.4064 -0.0269 -0.0683 0.0905  687 PHE A CD1 
9977  C CD2 . PHE A  661 ? 0.4674 0.4787 0.4074 -0.0272 -0.0700 0.0848  687 PHE A CD2 
9978  C CE1 . PHE A  661 ? 0.4892 0.4822 0.4147 -0.0340 -0.0661 0.0858  687 PHE A CE1 
9979  C CE2 . PHE A  661 ? 0.4799 0.4906 0.4151 -0.0340 -0.0675 0.0800  687 PHE A CE2 
9980  C CZ  . PHE A  661 ? 0.4852 0.4872 0.4135 -0.0372 -0.0656 0.0806  687 PHE A CZ  
9990  N N   . PRO A  662 ? 0.4195 0.4429 0.3653 -0.0058 -0.0845 0.1143  688 PRO A N   
9991  C CA  . PRO A  662 ? 0.4166 0.4434 0.3684 0.0027  -0.0870 0.1208  688 PRO A CA  
9992  C C   . PRO A  662 ? 0.4103 0.4452 0.3730 0.0074  -0.0868 0.1182  688 PRO A C   
9993  O O   . PRO A  662 ? 0.4118 0.4486 0.3801 0.0152  -0.0881 0.1232  688 PRO A O   
9994  C CB  . PRO A  662 ? 0.4266 0.4638 0.3746 0.0009  -0.0923 0.1274  688 PRO A CB  
9995  C CG  . PRO A  662 ? 0.4299 0.4746 0.3739 -0.0084 -0.0926 0.1220  688 PRO A CG  
9996  C CD  . PRO A  662 ? 0.4104 0.4430 0.3503 -0.0126 -0.0876 0.1154  688 PRO A CD  
10004 N N   . ARG A  663 ? 0.4007 0.4406 0.3664 0.0030  -0.0850 0.1109  689 ARG A N   
10005 C CA  . ARG A  663 ? 0.3982 0.4455 0.3738 0.0066  -0.0843 0.1079  689 ARG A CA  
10006 C C   . ARG A  663 ? 0.3845 0.4211 0.3626 0.0086  -0.0793 0.1020  689 ARG A C   
10007 O O   . ARG A  663 ? 0.3795 0.4209 0.3653 0.0115  -0.0782 0.0991  689 ARG A O   
10008 C CB  . ARG A  663 ? 0.4324 0.4927 0.4095 0.0002  -0.0858 0.1038  689 ARG A CB  
10009 C CG  . ARG A  663 ? 0.5038 0.5757 0.4777 -0.0032 -0.0908 0.1086  689 ARG A CG  
10010 C CD  . ARG A  663 ? 0.5675 0.6528 0.5499 0.0020  -0.0944 0.1134  689 ARG A CD  
10011 N NE  . ARG A  663 ? 0.6259 0.7244 0.6056 -0.0023 -0.0995 0.1172  689 ARG A NE  
10012 C CZ  . ARG A  663 ? 0.6791 0.7783 0.6533 -0.0016 -0.1030 0.1243  689 ARG A CZ  
10013 N NH1 . ARG A  663 ? 0.6832 0.7956 0.6550 -0.0060 -0.1077 0.1272  689 ARG A NH1 
10014 N NH2 . ARG A  663 ? 0.6857 0.7723 0.6563 0.0032  -0.1018 0.1285  689 ARG A NH2 
10028 N N   . LEU A  664 ? 0.3742 0.3971 0.3459 0.0066  -0.0764 0.1001  690 LEU A N   
10029 C CA  . LEU A  664 ? 0.3687 0.3823 0.3421 0.0076  -0.0719 0.0944  690 LEU A CA  
10030 C C   . LEU A  664 ? 0.3676 0.3765 0.3467 0.0162  -0.0706 0.0963  690 LEU A C   
10031 O O   . LEU A  664 ? 0.3789 0.3791 0.3553 0.0204  -0.0707 0.1012  690 LEU A O   
10032 C CB  . LEU A  664 ? 0.3720 0.3731 0.3372 0.0031  -0.0694 0.0924  690 LEU A CB  
10033 C CG  . LEU A  664 ? 0.3838 0.3773 0.3501 0.0021  -0.0650 0.0856  690 LEU A CG  
10034 C CD1 . LEU A  664 ? 0.3845 0.3869 0.3547 -0.0017 -0.0642 0.0794  690 LEU A CD1 
10035 C CD2 . LEU A  664 ? 0.4032 0.3852 0.3617 -0.0023 -0.0629 0.0846  690 LEU A CD2 
10047 N N   . GLU A  665 ? 0.3545 0.3683 0.3410 0.0186  -0.0691 0.0923  691 GLU A N   
10048 C CA  . GLU A  665 ? 0.3534 0.3641 0.3459 0.0264  -0.0673 0.0930  691 GLU A CA  
10049 C C   . GLU A  665 ? 0.3431 0.3426 0.3348 0.0264  -0.0629 0.0871  691 GLU A C   
10050 O O   . GLU A  665 ? 0.3484 0.3397 0.3414 0.0323  -0.0608 0.0880  691 GLU A O   
10051 C CB  . GLU A  665 ? 0.3914 0.4164 0.3930 0.0289  -0.0686 0.0925  691 GLU A CB  
10052 C CG  . GLU A  665 ? 0.4786 0.5161 0.4826 0.0300  -0.0732 0.0987  691 GLU A CG  
10053 C CD  . GLU A  665 ? 0.5931 0.6449 0.6066 0.0327  -0.0743 0.0986  691 GLU A CD  
10054 O OE1 . GLU A  665 ? 0.6121 0.6668 0.6289 0.0302  -0.0722 0.0927  691 GLU A OE1 
10055 O OE2 . GLU A  665 ? 0.6413 0.7019 0.6590 0.0371  -0.0774 0.1046  691 GLU A OE2 
10062 N N   . LEU A  666 ? 0.3243 0.3244 0.3143 0.0202  -0.0613 0.0810  692 LEU A N   
10063 C CA  . LEU A  666 ? 0.3220 0.3133 0.3114 0.0198  -0.0574 0.0755  692 LEU A CA  
10064 C C   . LEU A  666 ? 0.3160 0.3013 0.2986 0.0128  -0.0562 0.0722  692 LEU A C   
10065 O O   . LEU A  666 ? 0.3049 0.2969 0.2862 0.0072  -0.0571 0.0703  692 LEU A O   
10066 C CB  . LEU A  666 ? 0.3206 0.3201 0.3168 0.0204  -0.0562 0.0709  692 LEU A CB  
10067 C CG  . LEU A  666 ? 0.3469 0.3391 0.3437 0.0213  -0.0525 0.0655  692 LEU A CG  
10068 C CD1 . LEU A  666 ? 0.3559 0.3550 0.3602 0.0254  -0.0516 0.0638  692 LEU A CD1 
10069 C CD2 . LEU A  666 ? 0.3548 0.3457 0.3481 0.0146  -0.0511 0.0604  692 LEU A CD2 
10081 N N   . LEU A  667 ? 0.3162 0.2887 0.2944 0.0129  -0.0538 0.0712  693 LEU A N   
10082 C CA  . LEU A  667 ? 0.3061 0.2729 0.2783 0.0064  -0.0522 0.0681  693 LEU A CA  
10083 C C   . LEU A  667 ? 0.3024 0.2627 0.2755 0.0067  -0.0489 0.0627  693 LEU A C   
10084 O O   . LEU A  667 ? 0.3097 0.2613 0.2825 0.0109  -0.0474 0.0633  693 LEU A O   
10085 C CB  . LEU A  667 ? 0.3048 0.2622 0.2696 0.0051  -0.0528 0.0726  693 LEU A CB  
10086 C CG  . LEU A  667 ? 0.3195 0.2705 0.2778 -0.0019 -0.0510 0.0698  693 LEU A CG  
10087 C CD1 . LEU A  667 ? 0.3198 0.2808 0.2783 -0.0080 -0.0514 0.0663  693 LEU A CD1 
10088 C CD2 . LEU A  667 ? 0.3249 0.2673 0.2760 -0.0030 -0.0517 0.0750  693 LEU A CD2 
10100 N N   . ASP A  668 ? 0.2928 0.2578 0.2670 0.0024  -0.0477 0.0575  694 ASP A N   
10101 C CA  . ASP A  668 ? 0.3013 0.2624 0.2767 0.0024  -0.0449 0.0524  694 ASP A CA  
10102 C C   . ASP A  668 ? 0.3079 0.2647 0.2785 -0.0040 -0.0433 0.0493  694 ASP A C   
10103 O O   . ASP A  668 ? 0.3063 0.2698 0.2770 -0.0085 -0.0434 0.0472  694 ASP A O   
10104 C CB  . ASP A  668 ? 0.3089 0.2796 0.2910 0.0040  -0.0446 0.0493  694 ASP A CB  
10105 C CG  . ASP A  668 ? 0.3591 0.3282 0.3425 0.0033  -0.0421 0.0439  694 ASP A CG  
10106 O OD1 . ASP A  668 ? 0.3705 0.3305 0.3503 0.0025  -0.0404 0.0425  694 ASP A OD1 
10107 O OD2 . ASP A  668 ? 0.3828 0.3598 0.3708 0.0035  -0.0417 0.0413  694 ASP A OD2 
10112 N N   . LEU A  669 ? 0.3036 0.2492 0.2697 -0.0045 -0.0418 0.0493  695 LEU A N   
10113 C CA  . LEU A  669 ? 0.3062 0.2471 0.2676 -0.0106 -0.0402 0.0466  695 LEU A CA  
10114 C C   . LEU A  669 ? 0.3001 0.2361 0.2621 -0.0106 -0.0378 0.0420  695 LEU A C   
10115 O O   . LEU A  669 ? 0.3029 0.2323 0.2605 -0.0149 -0.0363 0.0403  695 LEU A O   
10116 C CB  . LEU A  669 ? 0.3209 0.2521 0.2754 -0.0126 -0.0404 0.0507  695 LEU A CB  
10117 C CG  . LEU A  669 ? 0.3362 0.2718 0.2888 -0.0134 -0.0429 0.0555  695 LEU A CG  
10118 C CD1 . LEU A  669 ? 0.3471 0.2718 0.2927 -0.0144 -0.0429 0.0602  695 LEU A CD1 
10119 C CD2 . LEU A  669 ? 0.3460 0.2908 0.2986 -0.0190 -0.0431 0.0532  695 LEU A CD2 
10131 N N   . ARG A  670 ? 0.2898 0.2297 0.2569 -0.0064 -0.0373 0.0397  696 ARG A N   
10132 C CA  . ARG A  670 ? 0.2989 0.2350 0.2662 -0.0064 -0.0353 0.0353  696 ARG A CA  
10133 C C   . ARG A  670 ? 0.3080 0.2484 0.2749 -0.0123 -0.0344 0.0312  696 ARG A C   
10134 O O   . ARG A  670 ? 0.3099 0.2584 0.2783 -0.0150 -0.0351 0.0311  696 ARG A O   
10135 C CB  . ARG A  670 ? 0.3094 0.2510 0.2825 -0.0011 -0.0351 0.0339  696 ARG A CB  
10136 C CG  . ARG A  670 ? 0.3201 0.2582 0.2947 0.0055  -0.0355 0.0374  696 ARG A CG  
10137 C CD  . ARG A  670 ? 0.3512 0.2970 0.3322 0.0101  -0.0352 0.0360  696 ARG A CD  
10138 N NE  . ARG A  670 ? 0.3882 0.3461 0.3734 0.0088  -0.0369 0.0363  696 ARG A NE  
10139 C CZ  . ARG A  670 ? 0.4483 0.4143 0.4388 0.0111  -0.0367 0.0349  696 ARG A CZ  
10140 N NH1 . ARG A  670 ? 0.4515 0.4157 0.4441 0.0151  -0.0351 0.0331  696 ARG A NH1 
10141 N NH2 . ARG A  670 ? 0.4534 0.4290 0.4470 0.0093  -0.0380 0.0350  696 ARG A NH2 
10155 N N   . GLY A  671 ? 0.3101 0.2452 0.2749 -0.0143 -0.0327 0.0278  697 GLY A N   
10156 C CA  . GLY A  671 ? 0.3097 0.2499 0.2749 -0.0194 -0.0319 0.0238  697 GLY A CA  
10157 C C   . GLY A  671 ? 0.3156 0.2571 0.2779 -0.0253 -0.0320 0.0247  697 GLY A C   
10158 O O   . GLY A  671 ? 0.3200 0.2707 0.2850 -0.0277 -0.0320 0.0232  697 GLY A O   
10162 N N   . ASN A  672 ? 0.3130 0.2450 0.2697 -0.0274 -0.0317 0.0271  698 ASN A N   
10163 C CA  . ASN A  672 ? 0.3176 0.2495 0.2706 -0.0335 -0.0315 0.0281  698 ASN A CA  
10164 C C   . ASN A  672 ? 0.3308 0.2521 0.2782 -0.0379 -0.0299 0.0269  698 ASN A C   
10165 O O   . ASN A  672 ? 0.3309 0.2485 0.2784 -0.0371 -0.0290 0.0239  698 ASN A O   
10166 C CB  . ASN A  672 ? 0.3228 0.2542 0.2740 -0.0321 -0.0331 0.0331  698 ASN A CB  
10167 C CG  . ASN A  672 ? 0.3384 0.2816 0.2941 -0.0310 -0.0343 0.0333  698 ASN A CG  
10168 O OD1 . ASN A  672 ? 0.3415 0.2920 0.2984 -0.0348 -0.0336 0.0310  698 ASN A OD1 
10169 N ND2 . ASN A  672 ? 0.3205 0.2661 0.2789 -0.0258 -0.0359 0.0358  698 ASN A ND2 
10176 N N   . LYS A  673 ? 0.3380 0.2551 0.2804 -0.0430 -0.0294 0.0287  699 LYS A N   
10177 C CA  . LYS A  673 ? 0.3671 0.2738 0.3037 -0.0480 -0.0277 0.0278  699 LYS A CA  
10178 C C   . LYS A  673 ? 0.3976 0.2925 0.3278 -0.0482 -0.0277 0.0328  699 LYS A C   
10179 O O   . LYS A  673 ? 0.4023 0.2910 0.3271 -0.0541 -0.0264 0.0332  699 LYS A O   
10180 C CB  . LYS A  673 ? 0.3867 0.3007 0.3237 -0.0553 -0.0267 0.0249  699 LYS A CB  
10181 C CG  . LYS A  673 ? 0.4406 0.3667 0.3841 -0.0548 -0.0268 0.0205  699 LYS A CG  
10182 C CD  . LYS A  673 ? 0.5235 0.4575 0.4680 -0.0615 -0.0257 0.0178  699 LYS A CD  
10183 C CE  . LYS A  673 ? 0.5821 0.5273 0.5330 -0.0603 -0.0258 0.0138  699 LYS A CE  
10184 N NZ  . LYS A  673 ? 0.6088 0.5645 0.5624 -0.0655 -0.0248 0.0118  699 LYS A NZ  
10198 N N   . LEU A  674 ? 0.4136 0.3061 0.3442 -0.0419 -0.0291 0.0369  700 LEU A N   
10199 C CA  . LEU A  674 ? 0.4473 0.3297 0.3723 -0.0412 -0.0295 0.0424  700 LEU A CA  
10200 C C   . LEU A  674 ? 0.4922 0.3584 0.4112 -0.0422 -0.0274 0.0422  700 LEU A C   
10201 O O   . LEU A  674 ? 0.4821 0.3440 0.4024 -0.0391 -0.0264 0.0394  700 LEU A O   
10202 C CB  . LEU A  674 ? 0.4425 0.3273 0.3703 -0.0337 -0.0316 0.0467  700 LEU A CB  
10203 C CG  . LEU A  674 ? 0.4408 0.3407 0.3737 -0.0331 -0.0337 0.0470  700 LEU A CG  
10204 C CD1 . LEU A  674 ? 0.4453 0.3481 0.3815 -0.0259 -0.0358 0.0507  700 LEU A CD1 
10205 C CD2 . LEU A  674 ? 0.4402 0.3431 0.3692 -0.0389 -0.0340 0.0489  700 LEU A CD2 
10217 N N   . LEU A  675 ? 0.5344 0.3916 0.4465 -0.0471 -0.0264 0.0449  701 LEU A N   
10218 C CA  . LEU A  675 ? 0.5882 0.4291 0.4935 -0.0497 -0.0240 0.0446  701 LEU A CA  
10219 C C   . LEU A  675 ? 0.6311 0.4579 0.5318 -0.0444 -0.0238 0.0503  701 LEU A C   
10220 O O   . LEU A  675 ? 0.6469 0.4590 0.5428 -0.0443 -0.0216 0.0496  701 LEU A O   
10221 C CB  . LEU A  675 ? 0.6010 0.4403 0.5014 -0.0593 -0.0225 0.0437  701 LEU A CB  
10222 C CG  . LEU A  675 ? 0.6261 0.4775 0.5306 -0.0652 -0.0221 0.0378  701 LEU A CG  
10223 C CD1 . LEU A  675 ? 0.6381 0.4927 0.5395 -0.0735 -0.0212 0.0383  701 LEU A CD1 
10224 C CD2 . LEU A  675 ? 0.6422 0.4877 0.5459 -0.0672 -0.0203 0.0326  701 LEU A CD2 
10236 N N   . PHE A  676 ? 0.6481 0.4789 0.5496 -0.0403 -0.0261 0.0559  702 PHE A N   
10237 C CA  . PHE A  676 ? 0.6849 0.5036 0.5824 -0.0346 -0.0262 0.0621  702 PHE A CA  
10238 C C   . PHE A  676 ? 0.6916 0.5202 0.5938 -0.0279 -0.0294 0.0669  702 PHE A C   
10239 O O   . PHE A  676 ? 0.6925 0.5364 0.5997 -0.0290 -0.0314 0.0657  702 PHE A O   
10240 C CB  . PHE A  676 ? 0.7085 0.5143 0.5969 -0.0400 -0.0248 0.0659  702 PHE A CB  
10241 C CG  . PHE A  676 ? 0.7315 0.5460 0.6181 -0.0473 -0.0256 0.0666  702 PHE A CG  
10242 C CD1 . PHE A  676 ? 0.7439 0.5659 0.6306 -0.0455 -0.0282 0.0719  702 PHE A CD1 
10243 C CD2 . PHE A  676 ? 0.7493 0.5646 0.6339 -0.0562 -0.0236 0.0620  702 PHE A CD2 
10244 C CE1 . PHE A  676 ? 0.7542 0.5840 0.6389 -0.0523 -0.0286 0.0722  702 PHE A CE1 
10245 C CE2 . PHE A  676 ? 0.7592 0.5830 0.6425 -0.0626 -0.0240 0.0626  702 PHE A CE2 
10246 C CZ  . PHE A  676 ? 0.7540 0.5843 0.6369 -0.0607 -0.0263 0.0676  702 PHE A CZ  
10256 N N   . LEU A  677 ? 0.6921 0.5119 0.5930 -0.0207 -0.0297 0.0722  703 LEU A N   
10257 C CA  . LEU A  677 ? 0.6937 0.5217 0.5988 -0.0137 -0.0328 0.0776  703 LEU A CA  
10258 C C   . LEU A  677 ? 0.6987 0.5189 0.5974 -0.0130 -0.0338 0.0854  703 LEU A C   
10259 O O   . LEU A  677 ? 0.7054 0.5096 0.5970 -0.0146 -0.0315 0.0873  703 LEU A O   
10260 C CB  . LEU A  677 ? 0.7005 0.5256 0.6105 -0.0047 -0.0322 0.0774  703 LEU A CB  
10261 C CG  . LEU A  677 ? 0.7212 0.5610 0.6404 -0.0012 -0.0334 0.0733  703 LEU A CG  
10262 C CD1 . LEU A  677 ? 0.7271 0.5764 0.6484 -0.0082 -0.0331 0.0666  703 LEU A CD1 
10263 C CD2 . LEU A  677 ? 0.7340 0.5666 0.6557 0.0054  -0.0313 0.0713  703 LEU A CD2 
10275 N N   . THR A  678 ? 0.6916 0.5230 0.5925 -0.0107 -0.0373 0.0902  704 THR A N   
10276 C CA  . THR A  678 ? 0.7019 0.5277 0.5969 -0.0097 -0.0388 0.0983  704 THR A CA  
10277 C C   . THR A  678 ? 0.7124 0.5249 0.6062 -0.0012 -0.0379 0.1034  704 THR A C   
10278 O O   . THR A  678 ? 0.7090 0.5235 0.6091 0.0059  -0.0378 0.1022  704 THR A O   
10279 C CB  . THR A  678 ? 0.7066 0.5488 0.6047 -0.0089 -0.0430 0.1019  704 THR A CB  
10280 O OG1 . THR A  678 ? 0.7239 0.5608 0.6145 -0.0100 -0.0443 0.1093  704 THR A OG1 
10281 C CG2 . THR A  678 ? 0.6983 0.5506 0.6052 -0.0003 -0.0453 0.1030  704 THR A CG2 
10289 N N   . ASP A  679 ? 0.7246 0.5237 0.6103 -0.0017 -0.0372 0.1094  705 ASP A N   
10290 C CA  . ASP A  679 ? 0.7421 0.5271 0.6257 0.0066  -0.0361 0.1152  705 ASP A CA  
10291 C C   . ASP A  679 ? 0.7384 0.5312 0.6242 0.0138  -0.0401 0.1239  705 ASP A C   
10292 O O   . ASP A  679 ? 0.7455 0.5273 0.6294 0.0210  -0.0395 0.1300  705 ASP A O   
10293 C CB  . ASP A  679 ? 0.7859 0.5499 0.6589 0.0025  -0.0326 0.1171  705 ASP A CB  
10294 C CG  . ASP A  679 ? 0.8626 0.6256 0.7279 -0.0033 -0.0341 0.1227  705 ASP A CG  
10295 O OD1 . ASP A  679 ? 0.8704 0.6497 0.7379 -0.0066 -0.0373 0.1230  705 ASP A OD1 
10296 O OD2 . ASP A  679 ? 0.9058 0.6513 0.7624 -0.0049 -0.0317 0.1265  705 ASP A OD2 
10301 N N   . SER A  680 ? 0.7241 0.5357 0.6139 0.0118  -0.0441 0.1245  706 SER A N   
10302 C CA  . SER A  680 ? 0.7200 0.5411 0.6116 0.0172  -0.0484 0.1326  706 SER A CA  
10303 C C   . SER A  680 ? 0.7002 0.5431 0.6007 0.0175  -0.0519 0.1297  706 SER A C   
10304 O O   . SER A  680 ? 0.6981 0.5530 0.5977 0.0147  -0.0554 0.1327  706 SER A O   
10305 C CB  . SER A  680 ? 0.7458 0.5638 0.6282 0.0118  -0.0498 0.1384  706 SER A CB  
10306 O OG  . SER A  680 ? 0.7867 0.5841 0.6604 0.0104  -0.0464 0.1407  706 SER A OG  
10312 N N   . LEU A  681 ? 0.6836 0.5313 0.5921 0.0208  -0.0507 0.1239  707 LEU A N   
10313 C CA  . LEU A  681 ? 0.6727 0.5398 0.5896 0.0210  -0.0534 0.1207  707 LEU A CA  
10314 C C   . LEU A  681 ? 0.6637 0.5425 0.5850 0.0275  -0.0578 0.1279  707 LEU A C   
10315 O O   . LEU A  681 ? 0.6533 0.5482 0.5780 0.0247  -0.0609 0.1272  707 LEU A O   
10316 C CB  . LEU A  681 ? 0.6731 0.5411 0.5971 0.0237  -0.0508 0.1136  707 LEU A CB  
10317 C CG  . LEU A  681 ? 0.6853 0.5714 0.6174 0.0225  -0.0526 0.1087  707 LEU A CG  
10318 C CD1 . LEU A  681 ? 0.6901 0.5841 0.6193 0.0130  -0.0535 0.1051  707 LEU A CD1 
10319 C CD2 . LEU A  681 ? 0.6942 0.5785 0.6316 0.0246  -0.0496 0.1018  707 LEU A CD2 
10331 N N   . SER A  682 ? 0.6646 0.5357 0.5856 0.0357  -0.0580 0.1351  708 SER A N   
10332 C CA  . SER A  682 ? 0.6614 0.5442 0.5867 0.0421  -0.0623 0.1427  708 SER A CA  
10333 C C   . SER A  682 ? 0.6585 0.5485 0.5779 0.0367  -0.0663 0.1477  708 SER A C   
10334 O O   . SER A  682 ? 0.6504 0.5561 0.5739 0.0384  -0.0706 0.1514  708 SER A O   
10335 C CB  . SER A  682 ? 0.6828 0.5541 0.6084 0.0522  -0.0612 0.1495  708 SER A CB  
10336 O OG  . SER A  682 ? 0.7196 0.5743 0.6352 0.0508  -0.0598 0.1544  708 SER A OG  
10342 N N   . ASP A  683 ? 0.6646 0.5436 0.5741 0.0298  -0.0647 0.1478  709 ASP A N   
10343 C CA  . ASP A  683 ? 0.6766 0.5618 0.5794 0.0238  -0.0680 0.1519  709 ASP A CA  
10344 C C   . ASP A  683 ? 0.6691 0.5706 0.5744 0.0162  -0.0696 0.1456  709 ASP A C   
10345 O O   . ASP A  683 ? 0.6709 0.5827 0.5731 0.0126  -0.0732 0.1489  709 ASP A O   
10346 C CB  . ASP A  683 ? 0.7188 0.5875 0.6105 0.0180  -0.0652 0.1532  709 ASP A CB  
10347 C CG  . ASP A  683 ? 0.8016 0.6527 0.6885 0.0244  -0.0636 0.1604  709 ASP A CG  
10348 O OD1 . ASP A  683 ? 0.8122 0.6655 0.7040 0.0339  -0.0654 0.1662  709 ASP A OD1 
10349 O OD2 . ASP A  683 ? 0.8437 0.6787 0.7221 0.0199  -0.0603 0.1602  709 ASP A OD2 
10354 N N   . PHE A  684 ? 0.6565 0.5597 0.5666 0.0137  -0.0669 0.1367  710 PHE A N   
10355 C CA  . PHE A  684 ? 0.6464 0.5629 0.5587 0.0068  -0.0677 0.1303  710 PHE A CA  
10356 C C   . PHE A  684 ? 0.6308 0.5627 0.5533 0.0105  -0.0697 0.1278  710 PHE A C   
10357 O O   . PHE A  684 ? 0.6295 0.5739 0.5534 0.0053  -0.0713 0.1242  710 PHE A O   
10358 C CB  . PHE A  684 ? 0.6453 0.5543 0.5554 0.0002  -0.0633 0.1223  710 PHE A CB  
10359 C CG  . PHE A  684 ? 0.6599 0.5531 0.5604 -0.0037 -0.0607 0.1242  710 PHE A CG  
10360 C CD1 . PHE A  684 ? 0.6698 0.5613 0.5621 -0.0066 -0.0626 0.1306  710 PHE A CD1 
10361 C CD2 . PHE A  684 ? 0.6748 0.5552 0.5741 -0.0052 -0.0564 0.1195  710 PHE A CD2 
10362 C CE1 . PHE A  684 ? 0.6861 0.5629 0.5695 -0.0106 -0.0600 0.1324  710 PHE A CE1 
10363 C CE2 . PHE A  684 ? 0.6896 0.5556 0.5800 -0.0095 -0.0539 0.1211  710 PHE A CE2 
10364 C CZ  . PHE A  684 ? 0.6901 0.5541 0.5726 -0.0121 -0.0556 0.1277  710 PHE A CZ  
10374 N N   . THR A  685 ? 0.6200 0.5509 0.5495 0.0191  -0.0695 0.1295  711 THR A N   
10375 C CA  . THR A  685 ? 0.6150 0.5608 0.5544 0.0226  -0.0713 0.1274  711 THR A CA  
10376 C C   . THR A  685 ? 0.6185 0.5649 0.5641 0.0330  -0.0723 0.1330  711 THR A C   
10377 O O   . THR A  685 ? 0.6301 0.5624 0.5743 0.0382  -0.0697 0.1351  711 THR A O   
10378 C CB  . THR A  685 ? 0.6226 0.5693 0.5665 0.0198  -0.0681 0.1180  711 THR A CB  
10379 O OG1 . THR A  685 ? 0.6259 0.5876 0.5786 0.0222  -0.0700 0.1162  711 THR A OG1 
10380 C CG2 . THR A  685 ? 0.6279 0.5599 0.5723 0.0237  -0.0637 0.1152  711 THR A CG2 
10388 N N   . SER A  686 ? 0.6048 0.5677 0.5573 0.0358  -0.0760 0.1354  712 SER A N   
10389 C CA  . SER A  686 ? 0.5988 0.5665 0.5592 0.0457  -0.0773 0.1404  712 SER A CA  
10390 C C   . SER A  686 ? 0.5767 0.5595 0.5476 0.0470  -0.0778 0.1359  712 SER A C   
10391 O O   . SER A  686 ? 0.5778 0.5673 0.5562 0.0547  -0.0789 0.1396  712 SER A O   
10392 C CB  . SER A  686 ? 0.6275 0.6020 0.5862 0.0486  -0.0820 0.1501  712 SER A CB  
10393 O OG  . SER A  686 ? 0.6655 0.6573 0.6250 0.0428  -0.0863 0.1498  712 SER A OG  
10399 N N   . SER A  687 ? 0.5530 0.5407 0.5243 0.0397  -0.0768 0.1280  713 SER A N   
10400 C CA  . SER A  687 ? 0.5287 0.5295 0.5088 0.0398  -0.0770 0.1234  713 SER A CA  
10401 C C   . SER A  687 ? 0.5040 0.4971 0.4864 0.0397  -0.0722 0.1156  713 SER A C   
10402 O O   . SER A  687 ? 0.4921 0.4933 0.4824 0.0422  -0.0715 0.1125  713 SER A O   
10403 C CB  . SER A  687 ? 0.5473 0.5610 0.5260 0.0315  -0.0798 0.1209  713 SER A CB  
10404 O OG  . SER A  687 ? 0.5829 0.5887 0.5532 0.0236  -0.0781 0.1168  713 SER A OG  
10410 N N   . LEU A  688 ? 0.4923 0.4706 0.4679 0.0364  -0.0689 0.1123  714 LEU A N   
10411 C CA  . LEU A  688 ? 0.4853 0.4568 0.4622 0.0354  -0.0647 0.1048  714 LEU A CA  
10412 C C   . LEU A  688 ? 0.4597 0.4280 0.4430 0.0441  -0.0624 0.1050  714 LEU A C   
10413 O O   . LEU A  688 ? 0.4646 0.4235 0.4464 0.0500  -0.0617 0.1097  714 LEU A O   
10414 C CB  . LEU A  688 ? 0.5033 0.4594 0.4714 0.0307  -0.0619 0.1025  714 LEU A CB  
10415 C CG  . LEU A  688 ? 0.5270 0.4781 0.4952 0.0270  -0.0582 0.0944  714 LEU A CG  
10416 C CD1 . LEU A  688 ? 0.5277 0.4911 0.4982 0.0209  -0.0591 0.0894  714 LEU A CD1 
10417 C CD2 . LEU A  688 ? 0.5444 0.4806 0.5042 0.0229  -0.0557 0.0931  714 LEU A CD2 
10429 N N   . ARG A  689 ? 0.4343 0.4107 0.4246 0.0449  -0.0614 0.1002  715 ARG A N   
10430 C CA  . ARG A  689 ? 0.4208 0.3961 0.4177 0.0525  -0.0590 0.0995  715 ARG A CA  
10431 C C   . ARG A  689 ? 0.3961 0.3616 0.3915 0.0509  -0.0546 0.0923  715 ARG A C   
10432 O O   . ARG A  689 ? 0.3973 0.3546 0.3940 0.0567  -0.0516 0.0918  715 ARG A O   
10433 C CB  . ARG A  689 ? 0.4434 0.4362 0.4495 0.0545  -0.0609 0.0996  715 ARG A CB  
10434 C CG  . ARG A  689 ? 0.5024 0.5073 0.5117 0.0570  -0.0654 0.1069  715 ARG A CG  
10435 C CD  . ARG A  689 ? 0.5721 0.5943 0.5906 0.0578  -0.0670 0.1060  715 ARG A CD  
10436 N NE  . ARG A  689 ? 0.6500 0.6858 0.6723 0.0599  -0.0716 0.1128  715 ARG A NE  
10437 C CZ  . ARG A  689 ? 0.6916 0.7442 0.7219 0.0602  -0.0737 0.1133  715 ARG A CZ  
10438 N NH1 . ARG A  689 ? 0.6887 0.7460 0.7239 0.0587  -0.0715 0.1074  715 ARG A NH1 
10439 N NH2 . ARG A  689 ? 0.6890 0.7541 0.7223 0.0618  -0.0782 0.1198  715 ARG A NH2 
10453 N N   . THR A  690 ? 0.3763 0.3436 0.3693 0.0433  -0.0541 0.0866  716 THR A N   
10454 C CA  . THR A  690 ? 0.3667 0.3265 0.3583 0.0412  -0.0504 0.0797  716 THR A CA  
10455 C C   . THR A  690 ? 0.3610 0.3125 0.3445 0.0336  -0.0497 0.0772  716 THR A C   
10456 O O   . THR A  690 ? 0.3565 0.3144 0.3380 0.0280  -0.0519 0.0774  716 THR A O   
10457 C CB  . THR A  690 ? 0.3825 0.3542 0.3805 0.0398  -0.0501 0.0750  716 THR A CB  
10458 O OG1 . THR A  690 ? 0.3948 0.3746 0.4006 0.0466  -0.0505 0.0774  716 THR A OG1 
10459 C CG2 . THR A  690 ? 0.3874 0.3529 0.3841 0.0375  -0.0467 0.0683  716 THR A CG2 
10467 N N   . LEU A  691 ? 0.3498 0.2872 0.3286 0.0334  -0.0466 0.0748  717 LEU A N   
10468 C CA  . LEU A  691 ? 0.3453 0.2748 0.3169 0.0263  -0.0455 0.0722  717 LEU A CA  
10469 C C   . LEU A  691 ? 0.3396 0.2636 0.3109 0.0248  -0.0422 0.0655  717 LEU A C   
10470 O O   . LEU A  691 ? 0.3414 0.2552 0.3115 0.0286  -0.0397 0.0648  717 LEU A O   
10471 C CB  . LEU A  691 ? 0.3504 0.2669 0.3149 0.0268  -0.0453 0.0770  717 LEU A CB  
10472 C CG  . LEU A  691 ? 0.3642 0.2715 0.3208 0.0193  -0.0439 0.0746  717 LEU A CG  
10473 C CD1 . LEU A  691 ? 0.3580 0.2757 0.3140 0.0121  -0.0458 0.0729  717 LEU A CD1 
10474 C CD2 . LEU A  691 ? 0.3830 0.2773 0.3327 0.0202  -0.0437 0.0802  717 LEU A CD2 
10486 N N   . LEU A  692 ? 0.3286 0.2599 0.3011 0.0194  -0.0421 0.0606  718 LEU A N   
10487 C CA  . LEU A  692 ? 0.3264 0.2543 0.2988 0.0177  -0.0394 0.0545  718 LEU A CA  
10488 C C   . LEU A  692 ? 0.3254 0.2462 0.2914 0.0107  -0.0382 0.0519  718 LEU A C   
10489 O O   . LEU A  692 ? 0.3198 0.2463 0.2846 0.0053  -0.0394 0.0515  718 LEU A O   
10490 C CB  . LEU A  692 ? 0.3242 0.2646 0.3028 0.0173  -0.0397 0.0508  718 LEU A CB  
10491 C CG  . LEU A  692 ? 0.3435 0.2937 0.3291 0.0229  -0.0411 0.0534  718 LEU A CG  
10492 C CD1 . LEU A  692 ? 0.3502 0.3117 0.3408 0.0211  -0.0412 0.0496  718 LEU A CD1 
10493 C CD2 . LEU A  692 ? 0.3490 0.2934 0.3367 0.0301  -0.0393 0.0543  718 LEU A CD2 
10505 N N   . LEU A  693 ? 0.3240 0.2320 0.2856 0.0107  -0.0357 0.0503  719 LEU A N   
10506 C CA  . LEU A  693 ? 0.3308 0.2312 0.2861 0.0040  -0.0344 0.0479  719 LEU A CA  
10507 C C   . LEU A  693 ? 0.3358 0.2319 0.2902 0.0021  -0.0319 0.0419  719 LEU A C   
10508 O O   . LEU A  693 ? 0.3397 0.2279 0.2887 -0.0031 -0.0305 0.0400  719 LEU A O   
10509 C CB  . LEU A  693 ? 0.3436 0.2307 0.2924 0.0043  -0.0340 0.0524  719 LEU A CB  
10510 C CG  . LEU A  693 ? 0.3602 0.2507 0.3077 0.0041  -0.0366 0.0584  719 LEU A CG  
10511 C CD1 . LEU A  693 ? 0.3792 0.2563 0.3218 0.0076  -0.0361 0.0637  719 LEU A CD1 
10512 C CD2 . LEU A  693 ? 0.3736 0.2672 0.3175 -0.0040 -0.0371 0.0573  719 LEU A CD2 
10524 N N   . SER A  694 ? 0.3372 0.2389 0.2967 0.0058  -0.0313 0.0390  720 SER A N   
10525 C CA  . SER A  694 ? 0.3461 0.2442 0.3043 0.0040  -0.0291 0.0335  720 SER A CA  
10526 C C   . SER A  694 ? 0.3423 0.2458 0.2996 -0.0034 -0.0292 0.0297  720 SER A C   
10527 O O   . SER A  694 ? 0.3336 0.2466 0.2932 -0.0060 -0.0309 0.0306  720 SER A O   
10528 C CB  . SER A  694 ? 0.3737 0.2776 0.3374 0.0094  -0.0285 0.0315  720 SER A CB  
10529 O OG  . SER A  694 ? 0.4198 0.3378 0.3893 0.0091  -0.0301 0.0310  720 SER A OG  
10535 N N   . HIS A  695 ? 0.3428 0.2400 0.2963 -0.0070 -0.0274 0.0256  721 HIS A N   
10536 C CA  . HIS A  695 ? 0.3450 0.2475 0.2979 -0.0139 -0.0274 0.0221  721 HIS A CA  
10537 C C   . HIS A  695 ? 0.3446 0.2462 0.2943 -0.0192 -0.0281 0.0245  721 HIS A C   
10538 O O   . HIS A  695 ? 0.3421 0.2538 0.2945 -0.0222 -0.0292 0.0243  721 HIS A O   
10539 C CB  . HIS A  695 ? 0.3548 0.2713 0.3139 -0.0134 -0.0283 0.0196  721 HIS A CB  
10540 C CG  . HIS A  695 ? 0.3934 0.3099 0.3540 -0.0103 -0.0271 0.0161  721 HIS A CG  
10541 N ND1 . HIS A  695 ? 0.4236 0.3373 0.3812 -0.0142 -0.0259 0.0118  721 HIS A ND1 
10542 C CD2 . HIS A  695 ? 0.4057 0.3246 0.3700 -0.0040 -0.0269 0.0165  721 HIS A CD2 
10543 C CE1 . HIS A  695 ? 0.4201 0.3345 0.3793 -0.0102 -0.0251 0.0096  721 HIS A CE1 
10544 N NE2 . HIS A  695 ? 0.4169 0.3342 0.3802 -0.0040 -0.0255 0.0124  721 HIS A NE2 
10552 N N   . ASN A  696 ? 0.3448 0.2337 0.2884 -0.0204 -0.0272 0.0267  722 ASN A N   
10553 C CA  . ASN A  696 ? 0.3548 0.2406 0.2941 -0.0259 -0.0274 0.0290  722 ASN A CA  
10554 C C   . ASN A  696 ? 0.3881 0.2600 0.3202 -0.0305 -0.0252 0.0271  722 ASN A C   
10555 O O   . ASN A  696 ? 0.3974 0.2658 0.3290 -0.0303 -0.0238 0.0230  722 ASN A O   
10556 C CB  . ASN A  696 ? 0.3441 0.2285 0.2829 -0.0222 -0.0290 0.0352  722 ASN A CB  
10557 C CG  . ASN A  696 ? 0.3412 0.2399 0.2851 -0.0218 -0.0311 0.0365  722 ASN A CG  
10558 O OD1 . ASN A  696 ? 0.3474 0.2516 0.2905 -0.0272 -0.0315 0.0361  722 ASN A OD1 
10559 N ND2 . ASN A  696 ? 0.3264 0.2313 0.2754 -0.0157 -0.0324 0.0379  722 ASN A ND2 
10566 N N   . ARG A  697 ? 0.4028 0.2673 0.3293 -0.0351 -0.0247 0.0297  723 ARG A N   
10567 C CA  . ARG A  697 ? 0.4297 0.2809 0.3492 -0.0402 -0.0224 0.0278  723 ARG A CA  
10568 C C   . ARG A  697 ? 0.4482 0.2839 0.3615 -0.0381 -0.0216 0.0329  723 ARG A C   
10569 O O   . ARG A  697 ? 0.4490 0.2755 0.3559 -0.0439 -0.0202 0.0337  723 ARG A O   
10570 C CB  . ARG A  697 ? 0.4522 0.3090 0.3704 -0.0493 -0.0222 0.0255  723 ARG A CB  
10571 C CG  . ARG A  697 ? 0.4842 0.3566 0.4089 -0.0507 -0.0230 0.0210  723 ARG A CG  
10572 C CD  . ARG A  697 ? 0.5389 0.4183 0.4633 -0.0589 -0.0227 0.0191  723 ARG A CD  
10573 N NE  . ARG A  697 ? 0.5869 0.4811 0.5179 -0.0594 -0.0234 0.0152  723 ARG A NE  
10574 C CZ  . ARG A  697 ? 0.6296 0.5336 0.5625 -0.0653 -0.0233 0.0131  723 ARG A CZ  
10575 N NH1 . ARG A  697 ? 0.6294 0.5307 0.5584 -0.0717 -0.0223 0.0143  723 ARG A NH1 
10576 N NH2 . ARG A  697 ? 0.6343 0.5514 0.5734 -0.0646 -0.0239 0.0100  723 ARG A NH2 
10590 N N   . ILE A  698 ? 0.4613 0.2946 0.3766 -0.0297 -0.0222 0.0365  724 ILE A N   
10591 C CA  . ILE A  698 ? 0.4910 0.3100 0.4010 -0.0264 -0.0215 0.0419  724 ILE A CA  
10592 C C   . ILE A  698 ? 0.5212 0.3235 0.4254 -0.0269 -0.0182 0.0390  724 ILE A C   
10593 O O   . ILE A  698 ? 0.5147 0.3164 0.4214 -0.0224 -0.0172 0.0359  724 ILE A O   
10594 C CB  . ILE A  698 ? 0.4995 0.3223 0.4142 -0.0169 -0.0232 0.0468  724 ILE A CB  
10595 C CG1 . ILE A  698 ? 0.5085 0.3488 0.4293 -0.0166 -0.0265 0.0488  724 ILE A CG1 
10596 C CG2 . ILE A  698 ? 0.5113 0.3193 0.4205 -0.0133 -0.0225 0.0530  724 ILE A CG2 
10597 C CD1 . ILE A  698 ? 0.5259 0.3690 0.4433 -0.0230 -0.0275 0.0511  724 ILE A CD1 
10609 N N   . SER A  699 ? 0.5500 0.3387 0.4462 -0.0325 -0.0163 0.0398  725 SER A N   
10610 C CA  . SER A  699 ? 0.5877 0.3586 0.4771 -0.0340 -0.0128 0.0370  725 SER A CA  
10611 C C   . SER A  699 ? 0.6347 0.3881 0.5190 -0.0279 -0.0111 0.0425  725 SER A C   
10612 O O   . SER A  699 ? 0.6479 0.3852 0.5265 -0.0276 -0.0079 0.0403  725 SER A O   
10613 C CB  . SER A  699 ? 0.6025 0.3689 0.4860 -0.0449 -0.0114 0.0337  725 SER A CB  
10614 O OG  . SER A  699 ? 0.6383 0.4002 0.5174 -0.0484 -0.0117 0.0389  725 SER A OG  
10620 N N   . HIS A  700 ? 0.6601 0.4161 0.5459 -0.0232 -0.0132 0.0495  726 HIS A N   
10621 C CA  . HIS A  700 ? 0.7022 0.4425 0.5834 -0.0170 -0.0118 0.0556  726 HIS A CA  
10622 C C   . HIS A  700 ? 0.7189 0.4693 0.6056 -0.0095 -0.0151 0.0625  726 HIS A C   
10623 O O   . HIS A  700 ? 0.7149 0.4794 0.6046 -0.0125 -0.0181 0.0641  726 HIS A O   
10624 C CB  . HIS A  700 ? 0.7350 0.4606 0.6066 -0.0243 -0.0100 0.0577  726 HIS A CB  
10625 C CG  . HIS A  700 ? 0.7941 0.5030 0.6601 -0.0188 -0.0086 0.0649  726 HIS A CG  
10626 N ND1 . HIS A  700 ? 0.8346 0.5236 0.6952 -0.0153 -0.0047 0.0641  726 HIS A ND1 
10627 C CD2 . HIS A  700 ? 0.8154 0.5243 0.6799 -0.0167 -0.0105 0.0727  726 HIS A CD2 
10628 C CE1 . HIS A  700 ? 0.8469 0.5247 0.7034 -0.0105 -0.0044 0.0719  726 HIS A CE1 
10629 N NE2 . HIS A  700 ? 0.8414 0.5309 0.7000 -0.0113 -0.0080 0.0774  726 HIS A NE2 
10637 N N   . LEU A  701 ? 0.7362 0.4799 0.6242 0.0002  -0.0144 0.0665  727 LEU A N   
10638 C CA  . LEU A  701 ? 0.7517 0.5044 0.6447 0.0076  -0.0176 0.0736  727 LEU A CA  
10639 C C   . LEU A  701 ? 0.7880 0.5268 0.6736 0.0083  -0.0171 0.0811  727 LEU A C   
10640 O O   . LEU A  701 ? 0.7998 0.5193 0.6791 0.0100  -0.0136 0.0816  727 LEU A O   
10641 C CB  . LEU A  701 ? 0.7458 0.5005 0.6451 0.0182  -0.0171 0.0741  727 LEU A CB  
10642 C CG  . LEU A  701 ? 0.7510 0.5194 0.6578 0.0188  -0.0175 0.0676  727 LEU A CG  
10643 C CD1 . LEU A  701 ? 0.7522 0.5227 0.6651 0.0295  -0.0170 0.0691  727 LEU A CD1 
10644 C CD2 . LEU A  701 ? 0.7495 0.5386 0.6621 0.0145  -0.0215 0.0668  727 LEU A CD2 
10656 N N   . PRO A  702 ? 0.8077 0.5547 0.6932 0.0069  -0.0204 0.0868  728 PRO A N   
10657 C CA  . PRO A  702 ? 0.8310 0.5642 0.7089 0.0077  -0.0200 0.0944  728 PRO A CA  
10658 C C   . PRO A  702 ? 0.8535 0.5773 0.7321 0.0190  -0.0192 0.1006  728 PRO A C   
10659 O O   . PRO A  702 ? 0.8480 0.5803 0.7344 0.0268  -0.0201 0.1001  728 PRO A O   
10660 C CB  . PRO A  702 ? 0.8341 0.5818 0.7129 0.0044  -0.0242 0.0989  728 PRO A CB  
10661 C CG  . PRO A  702 ? 0.8281 0.5954 0.7143 0.0012  -0.0263 0.0931  728 PRO A CG  
10662 C CD  . PRO A  702 ? 0.7997 0.5681 0.6914 0.0047  -0.0245 0.0868  728 PRO A CD  
10670 N N   . SER A  703 ? 0.8761 0.5825 0.7465 0.0201  -0.0176 0.1066  729 SER A N   
10671 C CA  . SER A  703 ? 0.8997 0.5961 0.7705 0.0313  -0.0166 0.1133  729 SER A CA  
10672 C C   . SER A  703 ? 0.9107 0.6252 0.7891 0.0383  -0.0215 0.1199  729 SER A C   
10673 O O   . SER A  703 ? 0.9084 0.6344 0.7865 0.0338  -0.0252 0.1231  729 SER A O   
10674 C CB  . SER A  703 ? 0.9276 0.6020 0.7875 0.0304  -0.0140 0.1190  729 SER A CB  
10675 O OG  . SER A  703 ? 0.9662 0.6258 0.8181 0.0212  -0.0100 0.1130  729 SER A OG  
10681 N N   . GLY A  704 ? 0.9197 0.6376 0.8052 0.0487  -0.0214 0.1213  730 GLY A N   
10682 C CA  . GLY A  704 ? 0.9297 0.6658 0.8235 0.0556  -0.0260 0.1273  730 GLY A CA  
10683 C C   . GLY A  704 ? 0.9401 0.6992 0.8410 0.0507  -0.0298 0.1228  730 GLY A C   
10684 O O   . GLY A  704 ? 0.9406 0.7128 0.8425 0.0485  -0.0341 0.1271  730 GLY A O   
10688 N N   . PHE A  705 ? 0.9442 0.7083 0.8497 0.0488  -0.0282 0.1143  731 PHE A N   
10689 C CA  . PHE A  705 ? 0.9486 0.7334 0.8607 0.0444  -0.0312 0.1096  731 PHE A CA  
10690 C C   . PHE A  705 ? 0.9525 0.7520 0.8754 0.0527  -0.0329 0.1101  731 PHE A C   
10691 O O   . PHE A  705 ? 0.9500 0.7667 0.8783 0.0533  -0.0371 0.1131  731 PHE A O   
10692 C CB  . PHE A  705 ? 0.9481 0.7308 0.8583 0.0358  -0.0287 0.1001  731 PHE A CB  
10693 C CG  . PHE A  705 ? 0.9459 0.7489 0.8630 0.0319  -0.0314 0.0954  731 PHE A CG  
10694 C CD1 . PHE A  705 ? 0.9510 0.7652 0.8674 0.0256  -0.0347 0.0967  731 PHE A CD1 
10695 C CD2 . PHE A  705 ? 0.9519 0.7625 0.8761 0.0349  -0.0306 0.0900  731 PHE A CD2 
10696 C CE1 . PHE A  705 ? 0.9526 0.7846 0.8752 0.0226  -0.0369 0.0927  731 PHE A CE1 
10697 C CE2 . PHE A  705 ? 0.9526 0.7811 0.8830 0.0317  -0.0330 0.0862  731 PHE A CE2 
10698 C CZ  . PHE A  705 ? 0.9460 0.7848 0.8756 0.0257  -0.0360 0.0876  731 PHE A CZ  
10708 N N   . LEU A  706 ? 0.9563 0.7494 0.8822 0.0588  -0.0295 0.1069  732 LEU A N   
10709 C CA  . LEU A  706 ? 0.9567 0.7633 0.8929 0.0663  -0.0303 0.1064  732 LEU A CA  
10710 C C   . LEU A  706 ? 0.9592 0.7706 0.9002 0.0763  -0.0324 0.1153  732 LEU A C   
10711 O O   . LEU A  706 ? 0.9541 0.7819 0.9043 0.0809  -0.0346 0.1160  732 LEU A O   
10712 C CB  . LEU A  706 ? 0.9635 0.7607 0.9005 0.0693  -0.0255 0.1000  732 LEU A CB  
10713 C CG  . LEU A  706 ? 0.9879 0.7835 0.9220 0.0604  -0.0236 0.0905  732 LEU A CG  
10714 C CD1 . LEU A  706 ? 1.0071 0.7819 0.9306 0.0550  -0.0201 0.0883  732 LEU A CD1 
10715 C CD2 . LEU A  706 ? 0.9935 0.7930 0.9333 0.0643  -0.0212 0.0847  732 LEU A CD2 
10727 N N   . SER A  707 ? 0.9652 0.7625 0.9003 0.0799  -0.0316 0.1221  733 SER A N   
10728 C CA  . SER A  707 ? 0.9662 0.7667 0.9056 0.0903  -0.0333 0.1310  733 SER A CA  
10729 C C   . SER A  707 ? 0.9566 0.7747 0.8991 0.0897  -0.0394 0.1379  733 SER A C   
10730 O O   . SER A  707 ? 0.9538 0.7860 0.9049 0.0969  -0.0420 0.1422  733 SER A O   
10731 C CB  . SER A  707 ? 0.9943 0.7719 0.9258 0.0948  -0.0299 0.1360  733 SER A CB  
10732 O OG  . SER A  707 ? 1.0319 0.8020 0.9542 0.0881  -0.0314 0.1397  733 SER A OG  
10738 N N   . GLU A  708 ? 0.9484 0.7654 0.8836 0.0812  -0.0417 0.1393  734 GLU A N   
10739 C CA  . GLU A  708 ? 0.9349 0.7661 0.8710 0.0802  -0.0472 0.1463  734 GLU A CA  
10740 C C   . GLU A  708 ? 0.9027 0.7578 0.8464 0.0766  -0.0514 0.1434  734 GLU A C   
10741 O O   . GLU A  708 ? 0.9035 0.7722 0.8505 0.0791  -0.0560 0.1498  734 GLU A O   
10742 C CB  . GLU A  708 ? 0.9780 0.7992 0.9029 0.0722  -0.0477 0.1486  734 GLU A CB  
10743 C CG  . GLU A  708 ? 1.0586 0.8560 0.9750 0.0753  -0.0440 0.1528  734 GLU A CG  
10744 C CD  . GLU A  708 ? 1.1607 0.9541 1.0798 0.0875  -0.0442 0.1618  734 GLU A CD  
10745 O OE1 . GLU A  708 ? 1.1874 0.9861 1.1049 0.0895  -0.0481 0.1706  734 GLU A OE1 
10746 O OE2 . GLU A  708 ? 1.1882 0.9733 1.1108 0.0952  -0.0405 0.1603  734 GLU A OE2 
10753 N N   . VAL A  709 ? 0.8718 0.7321 0.8181 0.0709  -0.0500 0.1343  735 VAL A N   
10754 C CA  . VAL A  709 ? 0.8372 0.7191 0.7904 0.0674  -0.0537 0.1317  735 VAL A CA  
10755 C C   . VAL A  709 ? 0.7927 0.6861 0.7567 0.0764  -0.0544 0.1332  735 VAL A C   
10756 O O   . VAL A  709 ? 0.7933 0.6865 0.7621 0.0785  -0.0514 0.1274  735 VAL A O   
10757 C CB  . VAL A  709 ? 0.8516 0.7358 0.8040 0.0583  -0.0521 0.1221  735 VAL A CB  
10758 C CG1 . VAL A  709 ? 0.8508 0.7554 0.8081 0.0537  -0.0560 0.1204  735 VAL A CG1 
10759 C CG2 . VAL A  709 ? 0.8679 0.7383 0.8099 0.0503  -0.0503 0.1201  735 VAL A CG2 
10769 N N   . SER A  710 ? 0.7540 0.6576 0.7218 0.0819  -0.0582 0.1413  736 SER A N   
10770 C CA  . SER A  710 ? 0.7154 0.6310 0.6939 0.0910  -0.0591 0.1440  736 SER A CA  
10771 C C   . SER A  710 ? 0.6609 0.5943 0.6476 0.0880  -0.0603 0.1380  736 SER A C   
10772 O O   . SER A  710 ? 0.6619 0.5993 0.6564 0.0941  -0.0583 0.1361  736 SER A O   
10773 C CB  . SER A  710 ? 0.7296 0.6540 0.7101 0.0965  -0.0636 0.1543  736 SER A CB  
10774 O OG  . SER A  710 ? 0.7588 0.6940 0.7358 0.0888  -0.0683 0.1562  736 SER A OG  
10780 N N   . SER A  711 ? 0.6109 0.5545 0.5959 0.0788  -0.0631 0.1350  737 SER A N   
10781 C CA  . SER A  711 ? 0.5656 0.5254 0.5578 0.0756  -0.0642 0.1295  737 SER A CA  
10782 C C   . SER A  711 ? 0.5220 0.4750 0.5145 0.0727  -0.0597 0.1203  737 SER A C   
10783 O O   . SER A  711 ? 0.5053 0.4699 0.5047 0.0723  -0.0597 0.1162  737 SER A O   
10784 C CB  . SER A  711 ? 0.5787 0.5506 0.5685 0.0668  -0.0684 0.1293  737 SER A CB  
10785 O OG  . SER A  711 ? 0.6151 0.5759 0.5951 0.0591  -0.0673 0.1266  737 SER A OG  
10791 N N   . LEU A  712 ? 0.5025 0.4376 0.4873 0.0704  -0.0561 0.1172  738 LEU A N   
10792 C CA  . LEU A  712 ? 0.4858 0.4151 0.4701 0.0669  -0.0522 0.1085  738 LEU A CA  
10793 C C   . LEU A  712 ? 0.4642 0.3924 0.4551 0.0746  -0.0490 0.1064  738 LEU A C   
10794 O O   . LEU A  712 ? 0.4689 0.3855 0.4587 0.0815  -0.0464 0.1091  738 LEU A O   
10795 C CB  . LEU A  712 ? 0.4958 0.4070 0.4702 0.0619  -0.0494 0.1059  738 LEU A CB  
10796 C CG  . LEU A  712 ? 0.5174 0.4253 0.4898 0.0552  -0.0467 0.0971  738 LEU A CG  
10797 C CD1 . LEU A  712 ? 0.5214 0.4438 0.4957 0.0478  -0.0494 0.0939  738 LEU A CD1 
10798 C CD2 . LEU A  712 ? 0.5358 0.4260 0.4985 0.0507  -0.0441 0.0955  738 LEU A CD2 
10810 N N   . LYS A  713 ? 0.4414 0.3817 0.4389 0.0735  -0.0489 0.1015  739 LYS A N   
10811 C CA  . LYS A  713 ? 0.4303 0.3720 0.4344 0.0798  -0.0458 0.0988  739 LYS A CA  
10812 C C   . LYS A  713 ? 0.4187 0.3511 0.4194 0.0760  -0.0418 0.0906  739 LYS A C   
10813 O O   . LYS A  713 ? 0.4219 0.3458 0.4231 0.0811  -0.0380 0.0885  739 LYS A O   
10814 C CB  . LYS A  713 ? 0.4464 0.4084 0.4600 0.0807  -0.0484 0.0991  739 LYS A CB  
10815 C CG  . LYS A  713 ? 0.5052 0.4796 0.5237 0.0847  -0.0526 0.1071  739 LYS A CG  
10816 C CD  . LYS A  713 ? 0.5630 0.5327 0.5845 0.0953  -0.0514 0.1133  739 LYS A CD  
10817 C CE  . LYS A  713 ? 0.6085 0.5792 0.6370 0.1023  -0.0476 0.1107  739 LYS A CE  
10818 N NZ  . LYS A  713 ? 0.6247 0.5937 0.6575 0.1132  -0.0467 0.1174  739 LYS A NZ  
10832 N N   . HIS A  714 ? 0.3987 0.3333 0.3959 0.0671  -0.0426 0.0859  740 HIS A N   
10833 C CA  . HIS A  714 ? 0.3918 0.3201 0.3863 0.0630  -0.0394 0.0783  740 HIS A CA  
10834 C C   . HIS A  714 ? 0.3907 0.3087 0.3763 0.0553  -0.0393 0.0762  740 HIS A C   
10835 O O   . HIS A  714 ? 0.3856 0.3104 0.3697 0.0493  -0.0420 0.0768  740 HIS A O   
10836 C CB  . HIS A  714 ? 0.3852 0.3285 0.3858 0.0600  -0.0404 0.0742  740 HIS A CB  
10837 C CG  . HIS A  714 ? 0.3990 0.3385 0.3977 0.0561  -0.0376 0.0668  740 HIS A CG  
10838 N ND1 . HIS A  714 ? 0.4108 0.3620 0.4138 0.0529  -0.0382 0.0630  740 HIS A ND1 
10839 C CD2 . HIS A  714 ? 0.4094 0.3352 0.4023 0.0549  -0.0343 0.0628  740 HIS A CD2 
10840 C CE1 . HIS A  714 ? 0.4147 0.3596 0.4147 0.0502  -0.0355 0.0573  740 HIS A CE1 
10841 N NE2 . HIS A  714 ? 0.4155 0.3455 0.4094 0.0510  -0.0332 0.0568  740 HIS A NE2 
10849 N N   . LEU A  715 ? 0.3766 0.2785 0.3562 0.0553  -0.0358 0.0738  741 LEU A N   
10850 C CA  . LEU A  715 ? 0.3695 0.2610 0.3408 0.0479  -0.0350 0.0713  741 LEU A CA  
10851 C C   . LEU A  715 ? 0.3695 0.2566 0.3394 0.0449  -0.0319 0.0638  741 LEU A C   
10852 O O   . LEU A  715 ? 0.3740 0.2532 0.3439 0.0496  -0.0288 0.0619  741 LEU A O   
10853 C CB  . LEU A  715 ? 0.3731 0.2486 0.3377 0.0500  -0.0338 0.0757  741 LEU A CB  
10854 C CG  . LEU A  715 ? 0.3885 0.2504 0.3439 0.0428  -0.0320 0.0730  741 LEU A CG  
10855 C CD1 . LEU A  715 ? 0.3875 0.2576 0.3411 0.0342  -0.0346 0.0721  741 LEU A CD1 
10856 C CD2 . LEU A  715 ? 0.3976 0.2434 0.3467 0.0458  -0.0308 0.0783  741 LEU A CD2 
10868 N N   . ASP A  716 ? 0.3556 0.2487 0.3247 0.0374  -0.0327 0.0594  742 ASP A N   
10869 C CA  . ASP A  716 ? 0.3589 0.2492 0.3266 0.0342  -0.0302 0.0525  742 ASP A CA  
10870 C C   . ASP A  716 ? 0.3577 0.2378 0.3176 0.0268  -0.0292 0.0502  742 ASP A C   
10871 O O   . ASP A  716 ? 0.3416 0.2271 0.3002 0.0207  -0.0310 0.0501  742 ASP A O   
10872 C CB  . ASP A  716 ? 0.3727 0.2785 0.3467 0.0324  -0.0314 0.0492  742 ASP A CB  
10873 C CG  . ASP A  716 ? 0.4443 0.3498 0.4166 0.0274  -0.0298 0.0426  742 ASP A CG  
10874 O OD1 . ASP A  716 ? 0.4424 0.3365 0.4101 0.0271  -0.0271 0.0396  742 ASP A OD1 
10875 O OD2 . ASP A  716 ? 0.4770 0.3937 0.4524 0.0238  -0.0311 0.0404  742 ASP A OD2 
10880 N N   . LEU A  717 ? 0.3628 0.2277 0.3171 0.0275  -0.0261 0.0485  743 LEU A N   
10881 C CA  . LEU A  717 ? 0.3733 0.2274 0.3199 0.0204  -0.0247 0.0459  743 LEU A CA  
10882 C C   . LEU A  717 ? 0.3775 0.2292 0.3226 0.0172  -0.0223 0.0387  743 LEU A C   
10883 O O   . LEU A  717 ? 0.3872 0.2280 0.3256 0.0120  -0.0205 0.0360  743 LEU A O   
10884 C CB  . LEU A  717 ? 0.3868 0.2239 0.3270 0.0227  -0.0229 0.0498  743 LEU A CB  
10885 C CG  . LEU A  717 ? 0.4121 0.2498 0.3514 0.0237  -0.0254 0.0570  743 LEU A CG  
10886 C CD1 . LEU A  717 ? 0.4286 0.2501 0.3631 0.0288  -0.0235 0.0615  743 LEU A CD1 
10887 C CD2 . LEU A  717 ? 0.4308 0.2707 0.3661 0.0147  -0.0269 0.0567  743 LEU A CD2 
10899 N N   . SER A  718 ? 0.3692 0.2310 0.3201 0.0198  -0.0223 0.0356  744 SER A N   
10900 C CA  . SER A  718 ? 0.3774 0.2378 0.3267 0.0170  -0.0203 0.0292  744 SER A CA  
10901 C C   . SER A  718 ? 0.3837 0.2479 0.3305 0.0081  -0.0212 0.0257  744 SER A C   
10902 O O   . SER A  718 ? 0.3748 0.2462 0.3230 0.0047  -0.0234 0.0278  744 SER A O   
10903 C CB  . SER A  718 ? 0.3829 0.2540 0.3389 0.0217  -0.0203 0.0273  744 SER A CB  
10904 O OG  . SER A  718 ? 0.4051 0.2919 0.3670 0.0202  -0.0230 0.0279  744 SER A OG  
10910 N N   . SER A  719 ? 0.3901 0.2489 0.3329 0.0042  -0.0193 0.0204  745 SER A N   
10911 C CA  . SER A  719 ? 0.4000 0.2631 0.3409 -0.0041 -0.0199 0.0167  745 SER A CA  
10912 C C   . SER A  719 ? 0.4059 0.2657 0.3432 -0.0097 -0.0208 0.0193  745 SER A C   
10913 O O   . SER A  719 ? 0.4164 0.2866 0.3561 -0.0142 -0.0225 0.0192  745 SER A O   
10914 C CB  . SER A  719 ? 0.4146 0.2945 0.3622 -0.0044 -0.0217 0.0149  745 SER A CB  
10915 O OG  . SER A  719 ? 0.4529 0.3350 0.4030 0.0003  -0.0206 0.0125  745 SER A OG  
10921 N N   . ASN A  720 ? 0.4031 0.2483 0.3345 -0.0094 -0.0193 0.0218  746 ASN A N   
10922 C CA  . ASN A  720 ? 0.4135 0.2533 0.3401 -0.0151 -0.0197 0.0243  746 ASN A CA  
10923 C C   . ASN A  720 ? 0.4326 0.2580 0.3512 -0.0207 -0.0169 0.0205  746 ASN A C   
10924 O O   . ASN A  720 ? 0.4341 0.2596 0.3522 -0.0220 -0.0157 0.0153  746 ASN A O   
10925 C CB  . ASN A  720 ? 0.4141 0.2496 0.3406 -0.0100 -0.0206 0.0312  746 ASN A CB  
10926 C CG  . ASN A  720 ? 0.4272 0.2776 0.3593 -0.0094 -0.0237 0.0344  746 ASN A CG  
10927 O OD1 . ASN A  720 ? 0.4222 0.2756 0.3526 -0.0149 -0.0248 0.0358  746 ASN A OD1 
10928 N ND2 . ASN A  720 ? 0.4233 0.2833 0.3622 -0.0032 -0.0250 0.0355  746 ASN A ND2 
10935 N N   . LEU A  721 ? 0.4436 0.2572 0.3556 -0.0248 -0.0160 0.0229  747 LEU A N   
10936 C CA  . LEU A  721 ? 0.4667 0.2663 0.3708 -0.0309 -0.0133 0.0193  747 LEU A CA  
10937 C C   . LEU A  721 ? 0.4838 0.2637 0.3815 -0.0271 -0.0108 0.0227  747 LEU A C   
10938 O O   . LEU A  721 ? 0.4895 0.2562 0.3796 -0.0327 -0.0089 0.0226  747 LEU A O   
10939 C CB  . LEU A  721 ? 0.4736 0.2769 0.3754 -0.0407 -0.0139 0.0185  747 LEU A CB  
10940 C CG  . LEU A  721 ? 0.4878 0.3105 0.3960 -0.0443 -0.0161 0.0153  747 LEU A CG  
10941 C CD1 . LEU A  721 ? 0.4958 0.3223 0.4022 -0.0531 -0.0165 0.0154  747 LEU A CD1 
10942 C CD2 . LEU A  721 ? 0.5004 0.3262 0.4095 -0.0456 -0.0154 0.0091  747 LEU A CD2 
10954 N N   . LEU A  722 ? 0.4847 0.2626 0.3854 -0.0174 -0.0106 0.0259  748 LEU A N   
10955 C CA  . LEU A  722 ? 0.5048 0.2646 0.4001 -0.0124 -0.0081 0.0297  748 LEU A CA  
10956 C C   . LEU A  722 ? 0.5330 0.2772 0.4217 -0.0138 -0.0042 0.0243  748 LEU A C   
10957 O O   . LEU A  722 ? 0.5309 0.2794 0.4223 -0.0114 -0.0034 0.0198  748 LEU A O   
10958 C CB  . LEU A  722 ? 0.4953 0.2591 0.3967 -0.0014 -0.0090 0.0344  748 LEU A CB  
10959 C CG  . LEU A  722 ? 0.4989 0.2772 0.4065 0.0009  -0.0129 0.0401  748 LEU A CG  
10960 C CD1 . LEU A  722 ? 0.4943 0.2782 0.4086 0.0115  -0.0137 0.0437  748 LEU A CD1 
10961 C CD2 . LEU A  722 ? 0.5092 0.2795 0.4114 -0.0020 -0.0134 0.0458  748 LEU A CD2 
10973 N N   . LYS A  723 ? 0.5614 0.2873 0.4412 -0.0179 -0.0015 0.0249  749 LYS A N   
10974 C CA  . LYS A  723 ? 0.6047 0.3127 0.4766 -0.0198 0.0027  0.0200  749 LYS A CA  
10975 C C   . LYS A  723 ? 0.6435 0.3365 0.5136 -0.0095 0.0056  0.0236  749 LYS A C   
10976 O O   . LYS A  723 ? 0.6450 0.3272 0.5115 -0.0072 0.0091  0.0194  749 LYS A O   
10977 C CB  . LYS A  723 ? 0.6439 0.3390 0.5066 -0.0301 0.0044  0.0188  749 LYS A CB  
10978 C CG  . LYS A  723 ? 0.7036 0.4129 0.5679 -0.0405 0.0020  0.0152  749 LYS A CG  
10979 C CD  . LYS A  723 ? 0.7847 0.4830 0.6409 -0.0505 0.0033  0.0154  749 LYS A CD  
10980 C CE  . LYS A  723 ? 0.8539 0.5301 0.6999 -0.0542 0.0078  0.0114  749 LYS A CE  
10981 N NZ  . LYS A  723 ? 0.8984 0.5689 0.7376 -0.0666 0.0088  0.0091  749 LYS A NZ  
10995 N N   . THR A  724 ? 0.6709 0.3632 0.5432 -0.0032 0.0043  0.0315  750 THR A N   
10996 C CA  . THR A  724 ? 0.7113 0.3915 0.5832 0.0074  0.0067  0.0360  750 THR A CA  
10997 C C   . THR A  724 ? 0.7416 0.4316 0.6198 0.0140  0.0032  0.0447  750 THR A C   
10998 O O   . THR A  724 ? 0.7359 0.4404 0.6176 0.0097  -0.0006 0.0466  750 THR A O   
10999 C CB  . THR A  724 ? 0.7426 0.3964 0.6031 0.0052  0.0114  0.0359  750 THR A CB  
11000 O OG1 . THR A  724 ? 0.7647 0.4068 0.6252 0.0164  0.0142  0.0396  750 THR A OG1 
11001 C CG2 . THR A  724 ? 0.7481 0.3957 0.6032 -0.0011 0.0104  0.0407  750 THR A CG2 
11009 N N   . ILE A  725 ? 0.7697 0.4523 0.6492 0.0246  0.0047  0.0499  751 ILE A N   
11010 C CA  . ILE A  725 ? 0.7965 0.4866 0.6810 0.0312  0.0016  0.0587  751 ILE A CA  
11011 C C   . ILE A  725 ? 0.8400 0.5082 0.7180 0.0371  0.0051  0.0639  751 ILE A C   
11012 O O   . ILE A  725 ? 0.8407 0.4988 0.7184 0.0445  0.0087  0.0628  751 ILE A O   
11013 C CB  . ILE A  725 ? 0.7931 0.5021 0.6889 0.0395  -0.0009 0.0600  751 ILE A CB  
11014 C CG1 . ILE A  725 ? 0.7939 0.5223 0.6953 0.0336  -0.0036 0.0540  751 ILE A CG1 
11015 C CG2 . ILE A  725 ? 0.7954 0.5127 0.6959 0.0452  -0.0045 0.0691  751 ILE A CG2 
11016 C CD1 . ILE A  725 ? 0.7957 0.5411 0.7075 0.0408  -0.0052 0.0537  751 ILE A CD1 
11028 N N   . ASN A  726 ? 0.8748 0.5345 0.7468 0.0334  0.0044  0.0693  752 ASN A N   
11029 C CA  . ASN A  726 ? 0.9221 0.5597 0.7869 0.0383  0.0077  0.0749  752 ASN A CA  
11030 C C   . ASN A  726 ? 0.9482 0.5897 0.8194 0.0513  0.0065  0.0829  752 ASN A C   
11031 O O   . ASN A  726 ? 0.9391 0.6012 0.8190 0.0541  0.0019  0.0862  752 ASN A O   
11032 C CB  . ASN A  726 ? 0.9531 0.5828 0.8101 0.0304  0.0068  0.0790  752 ASN A CB  
11033 C CG  . ASN A  726 ? 1.0132 0.6363 0.8628 0.0174  0.0085  0.0719  752 ASN A CG  
11034 O OD1 . ASN A  726 ? 1.0363 0.6522 0.8832 0.0144  0.0118  0.0642  752 ASN A OD1 
11035 N ND2 . ASN A  726 ? 1.0258 0.6515 0.8719 0.0091  0.0064  0.0744  752 ASN A ND2 
11042 N N   . LYS A  727 ? 0.9794 0.6010 0.8461 0.0590  0.0107  0.0865  753 LYS A N   
11043 C CA  . LYS A  727 ? 1.0034 0.6269 0.8758 0.0722  0.0101  0.0948  753 LYS A CA  
11044 C C   . LYS A  727 ? 1.0177 0.6543 0.8932 0.0727  0.0045  0.1038  753 LYS A C   
11045 O O   . LYS A  727 ? 1.0145 0.6661 0.8990 0.0811  0.0015  0.1090  753 LYS A O   
11046 C CB  . LYS A  727 ? 1.0468 0.6432 0.9114 0.0787  0.0159  0.0977  753 LYS A CB  
11047 C CG  . LYS A  727 ? 1.1053 0.7026 0.9766 0.0937  0.0165  0.1052  753 LYS A CG  
11048 C CD  . LYS A  727 ? 1.1777 0.7482 1.0404 0.0995  0.0212  0.1109  753 LYS A CD  
11049 C CE  . LYS A  727 ? 1.2273 0.7993 1.0968 0.1149  0.0216  0.1191  753 LYS A CE  
11050 N NZ  . LYS A  727 ? 1.2589 0.8252 1.1317 0.1230  0.0267  0.1141  753 LYS A NZ  
11064 N N   . SER A  728 ? 1.0309 0.6627 0.8991 0.0634  0.0032  0.1054  754 SER A N   
11065 C CA  . SER A  728 ? 1.0438 0.6875 0.9136 0.0628  -0.0019 0.1135  754 SER A CA  
11066 C C   . SER A  728 ? 1.0474 0.7191 0.9269 0.0605  -0.0074 0.1118  754 SER A C   
11067 O O   . SER A  728 ? 1.0453 0.7303 0.9296 0.0645  -0.0117 0.1188  754 SER A O   
11068 C CB  . SER A  728 ? 1.0687 0.7004 0.9279 0.0526  -0.0015 0.1147  754 SER A CB  
11069 O OG  . SER A  728 ? 1.0962 0.7334 0.9537 0.0407  -0.0016 0.1062  754 SER A OG  
11075 N N   . ALA A  729 ? 1.0503 0.7310 0.9326 0.0540  -0.0072 0.1027  755 ALA A N   
11076 C CA  . ALA A  729 ? 1.0533 0.7591 0.9444 0.0516  -0.0118 0.1006  755 ALA A CA  
11077 C C   . ALA A  729 ? 1.0593 0.7794 0.9611 0.0622  -0.0136 0.1030  755 ALA A C   
11078 O O   . ALA A  729 ? 1.0518 0.7914 0.9604 0.0627  -0.0182 0.1058  755 ALA A O   
11079 C CB  . ALA A  729 ? 1.0541 0.7643 0.9451 0.0427  -0.0107 0.0906  755 ALA A CB  
11085 N N   . LEU A  730 ? 1.0707 0.7812 0.9740 0.0704  -0.0097 0.1018  756 LEU A N   
11086 C CA  . LEU A  730 ? 1.0770 0.8011 0.9908 0.0805  -0.0108 0.1036  756 LEU A CA  
11087 C C   . LEU A  730 ? 1.0853 0.8136 1.0029 0.0897  -0.0134 0.1142  756 LEU A C   
11088 O O   . LEU A  730 ? 1.0768 0.8257 1.0030 0.0923  -0.0178 0.1172  756 LEU A O   
11089 C CB  . LEU A  730 ? 1.0844 0.7973 0.9987 0.0864  -0.0054 0.0986  756 LEU A CB  
11090 C CG  . LEU A  730 ? 1.1023 0.8151 1.0156 0.0801  -0.0028 0.0880  756 LEU A CG  
11091 C CD1 . LEU A  730 ? 1.1021 0.8359 1.0205 0.0726  -0.0071 0.0840  756 LEU A CD1 
11092 C CD2 . LEU A  730 ? 1.1210 0.8113 1.0227 0.0735  0.0015  0.0835  756 LEU A CD2 
11104 N N   . GLU A  731 ? 1.0979 0.8070 1.0093 0.0950  -0.0106 0.1200  757 GLU A N   
11105 C CA  . GLU A  731 ? 1.1072 0.8192 1.0221 0.1049  -0.0128 0.1305  757 GLU A CA  
11106 C C   . GLU A  731 ? 1.1199 0.8220 1.0262 0.1016  -0.0144 0.1378  757 GLU A C   
11107 O O   . GLU A  731 ? 1.1308 0.8170 1.0271 0.0935  -0.0120 0.1348  757 GLU A O   
11108 C CB  . GLU A  731 ? 1.1423 0.8408 1.0587 0.1169  -0.0078 0.1323  757 GLU A CB  
11109 C CG  . GLU A  731 ? 1.1945 0.9033 1.1199 0.1216  -0.0061 0.1262  757 GLU A CG  
11110 C CD  . GLU A  731 ? 1.2782 0.9716 1.2038 0.1326  -0.0002 0.1268  757 GLU A CD  
11111 O OE1 . GLU A  731 ? 1.3004 0.9803 1.2226 0.1398  0.0014  0.1344  757 GLU A OE1 
11112 O OE2 . GLU A  731 ? 1.3028 0.9974 1.2318 0.1342  0.0031  0.1196  757 GLU A OE2 
11119 N N   . THR A  732 ? 1.1157 0.8281 1.0259 0.1076  -0.0187 0.1474  758 THR A N   
11120 C CA  . THR A  732 ? 1.1273 0.8320 1.0297 0.1056  -0.0206 0.1556  758 THR A CA  
11121 C C   . THR A  732 ? 1.1243 0.8328 1.0316 0.1184  -0.0227 0.1669  758 THR A C   
11122 O O   . THR A  732 ? 1.1351 0.8255 1.0396 0.1266  -0.0184 0.1705  758 THR A O   
11123 C CB  . THR A  732 ? 1.1448 0.8628 1.0448 0.0936  -0.0252 0.1540  758 THR A CB  
11124 O OG1 . THR A  732 ? 1.1632 0.8748 1.0584 0.0832  -0.0224 0.1442  758 THR A OG1 
11125 C CG2 . THR A  732 ? 1.1553 0.8673 1.0474 0.0914  -0.0275 0.1628  758 THR A CG2 
11133 N N   . LYS A  733 ? 1.1078 0.8397 1.0226 0.1202  -0.0289 0.1722  759 LYS A N   
11134 C CA  . LYS A  733 ? 1.1036 0.8425 1.0240 0.1319  -0.0316 0.1830  759 LYS A CA  
11135 C C   . LYS A  733 ? 1.0846 0.8452 1.0190 0.1387  -0.0334 0.1815  759 LYS A C   
11136 O O   . LYS A  733 ? 1.0850 0.8438 1.0252 0.1506  -0.0314 0.1857  759 LYS A O   
11137 C CB  . LYS A  733 ? 1.1265 0.8741 1.0432 0.1285  -0.0374 0.1917  759 LYS A CB  
11138 C CG  . LYS A  733 ? 1.1735 0.9412 1.0915 0.1174  -0.0424 0.1876  759 LYS A CG  
11139 C CD  . LYS A  733 ? 1.2302 1.0055 1.1438 0.1147  -0.0479 0.1964  759 LYS A CD  
11140 C CE  . LYS A  733 ? 1.2655 1.0669 1.1890 0.1193  -0.0541 0.2018  759 LYS A CE  
11141 N NZ  . LYS A  733 ? 1.2913 1.0941 1.2224 0.1335  -0.0538 0.2090  759 LYS A NZ  
11155 N N   . THR A  734 ? 1.0649 0.8450 1.0044 0.1312  -0.0366 0.1752  760 THR A N   
11156 C CA  . THR A  734 ? 1.0491 0.8499 1.0014 0.1357  -0.0382 0.1725  760 THR A CA  
11157 C C   . THR A  734 ? 1.0392 0.8358 0.9923 0.1313  -0.0338 0.1609  760 THR A C   
11158 O O   . THR A  734 ? 1.0477 0.8366 0.9934 0.1210  -0.0327 0.1544  760 THR A O   
11159 C CB  . THR A  734 ? 1.0569 0.8830 1.0141 0.1302  -0.0451 0.1741  760 THR A CB  
11160 O OG1 . THR A  734 ? 1.0724 0.8980 1.0231 0.1172  -0.0458 0.1675  760 THR A OG1 
11161 C CG2 . THR A  734 ? 1.0599 0.8931 1.0169 0.1345  -0.0500 0.1857  760 THR A CG2 
11169 N N   . THR A  735 ? 1.0177 0.8202 0.9797 0.1389  -0.0315 0.1583  761 THR A N   
11170 C CA  . THR A  735 ? 1.0074 0.8065 0.9701 0.1353  -0.0274 0.1476  761 THR A CA  
11171 C C   . THR A  735 ? 0.9733 0.7937 0.9414 0.1270  -0.0312 0.1417  761 THR A C   
11172 O O   . THR A  735 ? 0.9701 0.8089 0.9429 0.1255  -0.0367 0.1460  761 THR A O   
11173 C CB  . THR A  735 ? 1.0298 0.8235 0.9983 0.1466  -0.0224 0.1468  761 THR A CB  
11174 O OG1 . THR A  735 ? 1.0493 0.8348 1.0154 0.1423  -0.0178 0.1364  761 THR A OG1 
11175 C CG2 . THR A  735 ? 1.0220 0.8390 1.0041 0.1546  -0.0253 0.1505  761 THR A CG2 
11183 N N   . THR A  736 ? 0.9462 0.7633 0.9131 0.1214  -0.0281 0.1320  762 THR A N   
11184 C CA  . THR A  736 ? 0.9165 0.7506 0.8874 0.1133  -0.0308 0.1257  762 THR A CA  
11185 C C   . THR A  736 ? 0.8705 0.7272 0.8537 0.1181  -0.0334 0.1266  762 THR A C   
11186 O O   . THR A  736 ? 0.8724 0.7296 0.8615 0.1258  -0.0303 0.1254  762 THR A O   
11187 C CB  . THR A  736 ? 0.9422 0.7665 0.9093 0.1079  -0.0263 0.1156  762 THR A CB  
11188 O OG1 . THR A  736 ? 0.9591 0.7753 0.9289 0.1165  -0.0215 0.1139  762 THR A OG1 
11189 C CG2 . THR A  736 ? 0.9586 0.7641 0.9138 0.1000  -0.0244 0.1131  762 THR A CG2 
11197 N N   . LYS A  737 ? 0.8257 0.7011 0.8124 0.1128  -0.0388 0.1280  763 LYS A N   
11198 C CA  . LYS A  737 ? 0.7830 0.6804 0.7810 0.1151  -0.0413 0.1276  763 LYS A CA  
11199 C C   . LYS A  737 ? 0.7340 0.6370 0.7333 0.1079  -0.0399 0.1178  763 LYS A C   
11200 O O   . LYS A  737 ? 0.7255 0.6467 0.7325 0.1066  -0.0424 0.1164  763 LYS A O   
11201 C CB  . LYS A  737 ? 0.8040 0.7190 0.8052 0.1133  -0.0476 0.1341  763 LYS A CB  
11202 C CG  . LYS A  737 ? 0.8667 0.7841 0.8713 0.1231  -0.0495 0.1443  763 LYS A CG  
11203 C CD  . LYS A  737 ? 0.9415 0.8382 0.9366 0.1253  -0.0477 0.1490  763 LYS A CD  
11204 C CE  . LYS A  737 ? 0.9924 0.8945 0.9844 0.1240  -0.0529 0.1575  763 LYS A CE  
11205 N NZ  . LYS A  737 ? 1.0381 0.9186 1.0193 0.1243  -0.0510 0.1614  763 LYS A NZ  
11219 N N   . LEU A  738 ? 0.6991 0.5863 0.6912 0.1033  -0.0360 0.1113  764 LEU A N   
11220 C CA  . LEU A  738 ? 0.6614 0.5523 0.6542 0.0973  -0.0345 0.1026  764 LEU A CA  
11221 C C   . LEU A  738 ? 0.6181 0.5139 0.6186 0.1043  -0.0315 0.1000  764 LEU A C   
11222 O O   . LEU A  738 ? 0.6193 0.5070 0.6210 0.1130  -0.0285 0.1027  764 LEU A O   
11223 C CB  . LEU A  738 ? 0.6716 0.5441 0.6545 0.0914  -0.0310 0.0968  764 LEU A CB  
11224 C CG  . LEU A  738 ? 0.6912 0.5595 0.6663 0.0820  -0.0331 0.0965  764 LEU A CG  
11225 C CD1 . LEU A  738 ? 0.7058 0.5537 0.6715 0.0783  -0.0290 0.0923  764 LEU A CD1 
11226 C CD2 . LEU A  738 ? 0.6882 0.5718 0.6659 0.0739  -0.0359 0.0922  764 LEU A CD2 
11238 N N   . SER A  739 ? 0.5788 0.4873 0.5840 0.1005  -0.0321 0.0948  765 SER A N   
11239 C CA  . SER A  739 ? 0.5540 0.4676 0.5657 0.1053  -0.0291 0.0911  765 SER A CA  
11240 C C   . SER A  739 ? 0.5356 0.4427 0.5428 0.0991  -0.0261 0.0822  765 SER A C   
11241 O O   . SER A  739 ? 0.5311 0.4366 0.5407 0.1030  -0.0224 0.0784  765 SER A O   
11242 C CB  . SER A  739 ? 0.5615 0.4974 0.5836 0.1066  -0.0324 0.0932  765 SER A CB  
11243 O OG  . SER A  739 ? 0.5856 0.5316 0.6072 0.0975  -0.0356 0.0902  765 SER A OG  
11249 N N   . MET A  740 ? 0.5191 0.4230 0.5198 0.0896  -0.0276 0.0789  766 MET A N   
11250 C CA  . MET A  740 ? 0.5095 0.4081 0.5059 0.0835  -0.0252 0.0710  766 MET A CA  
11251 C C   . MET A  740 ? 0.4926 0.3788 0.4794 0.0760  -0.0254 0.0694  766 MET A C   
11252 O O   . MET A  740 ? 0.4874 0.3786 0.4728 0.0708  -0.0288 0.0718  766 MET A O   
11253 C CB  . MET A  740 ? 0.5221 0.4371 0.5239 0.0791  -0.0271 0.0674  766 MET A CB  
11254 C CG  . MET A  740 ? 0.5827 0.4932 0.5806 0.0736  -0.0247 0.0597  766 MET A CG  
11255 S SD  . MET A  740 ? 0.7223 0.6509 0.7271 0.0703  -0.0260 0.0558  766 MET A SD  
11256 C CE  . MET A  740 ? 0.6943 0.6275 0.7064 0.0797  -0.0231 0.0563  766 MET A CE  
11266 N N   . LEU A  741 ? 0.4844 0.3553 0.4648 0.0748  -0.0215 0.0649  767 LEU A N   
11267 C CA  . LEU A  741 ? 0.4849 0.3432 0.4561 0.0675  -0.0209 0.0626  767 LEU A CA  
11268 C C   . LEU A  741 ? 0.4769 0.3327 0.4454 0.0627  -0.0185 0.0545  767 LEU A C   
11269 O O   . LEU A  741 ? 0.4833 0.3310 0.4506 0.0664  -0.0147 0.0513  767 LEU A O   
11270 C CB  . LEU A  741 ? 0.4933 0.3331 0.4583 0.0716  -0.0183 0.0659  767 LEU A CB  
11271 C CG  . LEU A  741 ? 0.5218 0.3456 0.4765 0.0644  -0.0168 0.0635  767 LEU A CG  
11272 C CD1 . LEU A  741 ? 0.5198 0.3501 0.4725 0.0565  -0.0206 0.0652  767 LEU A CD1 
11273 C CD2 . LEU A  741 ? 0.5406 0.3455 0.4896 0.0694  -0.0138 0.0672  767 LEU A CD2 
11285 N N   . GLU A  742 ? 0.4549 0.3183 0.4228 0.0546  -0.0205 0.0512  768 GLU A N   
11286 C CA  . GLU A  742 ? 0.4433 0.3060 0.4089 0.0495  -0.0188 0.0440  768 GLU A CA  
11287 C C   . GLU A  742 ? 0.4377 0.2862 0.3940 0.0429  -0.0175 0.0415  768 GLU A C   
11288 O O   . GLU A  742 ? 0.4356 0.2827 0.3890 0.0386  -0.0194 0.0444  768 GLU A O   
11289 C CB  . GLU A  742 ? 0.4574 0.3368 0.4280 0.0451  -0.0215 0.0418  768 GLU A CB  
11290 C CG  . GLU A  742 ? 0.4872 0.3813 0.4665 0.0501  -0.0236 0.0452  768 GLU A CG  
11291 C CD  . GLU A  742 ? 0.5317 0.4405 0.5158 0.0464  -0.0252 0.0422  768 GLU A CD  
11292 O OE1 . GLU A  742 ? 0.5200 0.4289 0.5036 0.0450  -0.0233 0.0370  768 GLU A OE1 
11293 O OE2 . GLU A  742 ? 0.5641 0.4839 0.5520 0.0450  -0.0283 0.0451  768 GLU A OE2 
11300 N N   . LEU A  743 ? 0.4324 0.2702 0.3838 0.0419  -0.0140 0.0363  769 LEU A N   
11301 C CA  . LEU A  743 ? 0.4421 0.2659 0.3845 0.0353  -0.0123 0.0334  769 LEU A CA  
11302 C C   . LEU A  743 ? 0.4392 0.2619 0.3785 0.0302  -0.0105 0.0258  769 LEU A C   
11303 O O   . LEU A  743 ? 0.4473 0.2582 0.3791 0.0245  -0.0089 0.0229  769 LEU A O   
11304 C CB  . LEU A  743 ? 0.4525 0.2579 0.3895 0.0401  -0.0092 0.0359  769 LEU A CB  
11305 C CG  . LEU A  743 ? 0.4691 0.2720 0.4067 0.0438  -0.0108 0.0438  769 LEU A CG  
11306 C CD1 . LEU A  743 ? 0.4914 0.2786 0.4261 0.0516  -0.0073 0.0465  769 LEU A CD1 
11307 C CD2 . LEU A  743 ? 0.4766 0.2746 0.4083 0.0359  -0.0123 0.0452  769 LEU A CD2 
11319 N N   . HIS A  744 ? 0.4294 0.2640 0.3741 0.0318  -0.0108 0.0228  770 HIS A N   
11320 C CA  . HIS A  744 ? 0.4353 0.2699 0.3770 0.0272  -0.0094 0.0160  770 HIS A CA  
11321 C C   . HIS A  744 ? 0.4283 0.2667 0.3674 0.0177  -0.0114 0.0137  770 HIS A C   
11322 O O   . HIS A  744 ? 0.4157 0.2630 0.3581 0.0156  -0.0143 0.0168  770 HIS A O   
11323 C CB  . HIS A  744 ? 0.4372 0.2851 0.3855 0.0309  -0.0096 0.0141  770 HIS A CB  
11324 C CG  . HIS A  744 ? 0.4544 0.3197 0.4098 0.0294  -0.0132 0.0159  770 HIS A CG  
11325 N ND1 . HIS A  744 ? 0.4732 0.3473 0.4355 0.0346  -0.0150 0.0210  770 HIS A ND1 
11326 C CD2 . HIS A  744 ? 0.4661 0.3412 0.4226 0.0234  -0.0151 0.0132  770 HIS A CD2 
11327 C CE1 . HIS A  744 ? 0.4681 0.3559 0.4348 0.0312  -0.0177 0.0209  770 HIS A CE1 
11328 N NE2 . HIS A  744 ? 0.4739 0.3625 0.4374 0.0248  -0.0178 0.0164  770 HIS A NE2 
11336 N N   . GLY A  745 ? 0.4295 0.2611 0.3624 0.0121  -0.0097 0.0084  771 GLY A N   
11337 C CA  . GLY A  745 ? 0.4336 0.2695 0.3642 0.0030  -0.0114 0.0059  771 GLY A CA  
11338 C C   . GLY A  745 ? 0.4434 0.2682 0.3678 -0.0025 -0.0112 0.0074  771 GLY A C   
11339 O O   . GLY A  745 ? 0.4544 0.2839 0.3776 -0.0101 -0.0126 0.0058  771 GLY A O   
11343 N N   . ASN A  746 ? 0.4427 0.2529 0.3631 0.0011  -0.0092 0.0106  772 ASN A N   
11344 C CA  . ASN A  746 ? 0.4418 0.2397 0.3554 -0.0042 -0.0086 0.0123  772 ASN A CA  
11345 C C   . ASN A  746 ? 0.4611 0.2437 0.3660 -0.0088 -0.0052 0.0070  772 ASN A C   
11346 O O   . ASN A  746 ? 0.4687 0.2439 0.3716 -0.0044 -0.0025 0.0044  772 ASN A O   
11347 C CB  . ASN A  746 ? 0.4426 0.2322 0.3560 0.0020  -0.0083 0.0190  772 ASN A CB  
11348 C CG  . ASN A  746 ? 0.4376 0.2409 0.3574 0.0035  -0.0120 0.0244  772 ASN A CG  
11349 O OD1 . ASN A  746 ? 0.4266 0.2322 0.3447 -0.0026 -0.0137 0.0259  772 ASN A OD1 
11350 N ND2 . ASN A  746 ? 0.4117 0.2246 0.3387 0.0110  -0.0133 0.0271  772 ASN A ND2 
11357 N N   . PRO A  747 ? 0.4701 0.2477 0.3692 -0.0179 -0.0052 0.0052  773 PRO A N   
11358 C CA  . PRO A  747 ? 0.4835 0.2467 0.3738 -0.0234 -0.0020 -0.0003 773 PRO A CA  
11359 C C   . PRO A  747 ? 0.4981 0.2391 0.3810 -0.0206 0.0016  0.0019  773 PRO A C   
11360 O O   . PRO A  747 ? 0.5049 0.2347 0.3813 -0.0266 0.0025  0.0027  773 PRO A O   
11361 C CB  . PRO A  747 ? 0.4910 0.2600 0.3796 -0.0342 -0.0037 -0.0023 773 PRO A CB  
11362 C CG  . PRO A  747 ? 0.4906 0.2651 0.3826 -0.0337 -0.0060 0.0040  773 PRO A CG  
11363 C CD  . PRO A  747 ? 0.4627 0.2479 0.3630 -0.0242 -0.0077 0.0077  773 PRO A CD  
11371 N N   . PHE A  748 ? 0.5050 0.2400 0.3892 -0.0111 0.0036  0.0035  774 PHE A N   
11372 C CA  . PHE A  748 ? 0.5266 0.2408 0.4046 -0.0066 0.0072  0.0062  774 PHE A CA  
11373 C C   . PHE A  748 ? 0.5482 0.2431 0.4151 -0.0130 0.0112  0.0006  774 PHE A C   
11374 O O   . PHE A  748 ? 0.5360 0.2329 0.4008 -0.0170 0.0121  -0.0061 774 PHE A O   
11375 C CB  . PHE A  748 ? 0.5255 0.2392 0.4081 0.0054  0.0087  0.0084  774 PHE A CB  
11376 C CG  . PHE A  748 ? 0.5298 0.2565 0.4215 0.0125  0.0055  0.0156  774 PHE A CG  
11377 C CD1 . PHE A  748 ? 0.5513 0.2709 0.4420 0.0154  0.0050  0.0225  774 PHE A CD1 
11378 C CD2 . PHE A  748 ? 0.5318 0.2777 0.4327 0.0163  0.0029  0.0154  774 PHE A CD2 
11379 C CE1 . PHE A  748 ? 0.5554 0.2880 0.4541 0.0213  0.0017  0.0290  774 PHE A CE1 
11380 C CE2 . PHE A  748 ? 0.5382 0.2961 0.4471 0.0222  -0.0001 0.0217  774 PHE A CE2 
11381 C CZ  . PHE A  748 ? 0.5405 0.2922 0.4483 0.0243  -0.0009 0.0284  774 PHE A CZ  
11391 N N   . GLU A  749 ? 0.5708 0.2470 0.4304 -0.0141 0.0136  0.0036  775 GLU A N   
11392 C CA  . GLU A  749 ? 0.6084 0.2631 0.4567 -0.0198 0.0179  -0.0007 775 GLU A CA  
11393 C C   . GLU A  749 ? 0.6346 0.2736 0.4804 -0.0098 0.0224  -0.0001 775 GLU A C   
11394 O O   . GLU A  749 ? 0.6355 0.2688 0.4833 -0.0015 0.0229  0.0067  775 GLU A O   
11395 C CB  . GLU A  749 ? 0.6501 0.2933 0.4923 -0.0260 0.0182  0.0032  775 GLU A CB  
11396 C CG  . GLU A  749 ? 0.7428 0.3646 0.5728 -0.0342 0.0225  -0.0019 775 GLU A CG  
11397 C CD  . GLU A  749 ? 0.8458 0.4602 0.6700 -0.0437 0.0223  0.0003  775 GLU A CD  
11398 O OE1 . GLU A  749 ? 0.8817 0.4757 0.6953 -0.0496 0.0262  -0.0027 775 GLU A OE1 
11399 O OE2 . GLU A  749 ? 0.8671 0.4958 0.6969 -0.0456 0.0184  0.0047  775 GLU A OE2 
11406 N N   . CYS A  750 ? 0.6483 0.2821 0.4903 -0.0101 0.0254  -0.0071 776 CYS A N   
11407 C CA  . CYS A  750 ? 0.6676 0.2877 0.5074 -0.0005 0.0300  -0.0076 776 CYS A CA  
11408 C C   . CYS A  750 ? 0.6990 0.2919 0.5263 -0.0037 0.0356  -0.0107 776 CYS A C   
11409 O O   . CYS A  750 ? 0.7099 0.2939 0.5307 -0.0063 0.0391  -0.0180 776 CYS A O   
11410 C CB  . CYS A  750 ? 0.6629 0.2955 0.5073 0.0028  0.0300  -0.0127 776 CYS A CB  
11411 S SG  . CYS A  750 ? 0.6777 0.3390 0.5374 0.0100  0.0246  -0.0076 776 CYS A SG  
11416 N N   . THR A  751 ? 0.7126 0.2920 0.5361 -0.0034 0.0365  -0.0050 777 THR A N   
11417 C CA  . THR A  751 ? 0.7406 0.2916 0.5524 -0.0048 0.0421  -0.0058 777 THR A CA  
11418 C C   . THR A  751 ? 0.7558 0.2977 0.5706 0.0090  0.0441  0.0023  777 THR A C   
11419 O O   . THR A  751 ? 0.7411 0.3002 0.5667 0.0178  0.0410  0.0070  777 THR A O   
11420 C CB  . THR A  751 ? 0.7600 0.3049 0.5653 -0.0167 0.0409  -0.0050 777 THR A CB  
11421 O OG1 . THR A  751 ? 0.7612 0.3170 0.5734 -0.0139 0.0367  0.0036  777 THR A OG1 
11422 C CG2 . THR A  751 ? 0.7625 0.3190 0.5662 -0.0297 0.0385  -0.0125 777 THR A CG2 
11430 N N   . CYS A  752 ? 0.7819 0.2976 0.5875 0.0110  0.0492  0.0040  778 CYS A N   
11431 C CA  . CYS A  752 ? 0.8049 0.3121 0.6134 0.0241  0.0510  0.0123  778 CYS A CA  
11432 C C   . CYS A  752 ? 0.8171 0.3389 0.6335 0.0265  0.0454  0.0220  778 CYS A C   
11433 O O   . CYS A  752 ? 0.8221 0.3458 0.6445 0.0381  0.0451  0.0293  778 CYS A O   
11434 C CB  . CYS A  752 ? 0.8298 0.3049 0.6260 0.0250  0.0577  0.0123  778 CYS A CB  
11435 S SG  . CYS A  752 ? 0.8768 0.3341 0.6640 0.0246  0.0649  0.0014  778 CYS A SG  
11441 N N   . ASP A  753 ? 0.8199 0.3545 0.6371 0.0159  0.0408  0.0217  779 ASP A N   
11442 C CA  . ASP A  753 ? 0.8263 0.3761 0.6505 0.0170  0.0354  0.0299  779 ASP A CA  
11443 C C   . ASP A  753 ? 0.8135 0.3882 0.6511 0.0255  0.0312  0.0327  779 ASP A C   
11444 O O   . ASP A  753 ? 0.8149 0.3999 0.6586 0.0298  0.0275  0.0405  779 ASP A O   
11445 C CB  . ASP A  753 ? 0.8618 0.4197 0.6837 0.0033  0.0321  0.0278  779 ASP A CB  
11446 C CG  . ASP A  753 ? 0.9651 0.5001 0.7742 -0.0060 0.0357  0.0263  779 ASP A CG  
11447 O OD1 . ASP A  753 ? 0.9868 0.5242 0.7919 -0.0181 0.0352  0.0200  779 ASP A OD1 
11448 O OD2 . ASP A  753 ? 1.0051 0.5199 0.8084 -0.0011 0.0390  0.0316  779 ASP A OD2 
11453 N N   . ILE A  754 ? 0.7992 0.3840 0.6412 0.0274  0.0316  0.0265  780 ILE A N   
11454 C CA  . ILE A  754 ? 0.7812 0.3883 0.6357 0.0356  0.0281  0.0291  780 ILE A CA  
11455 C C   . ILE A  754 ? 0.7729 0.3730 0.6308 0.0499  0.0311  0.0339  780 ILE A C   
11456 O O   . ILE A  754 ? 0.7631 0.3808 0.6314 0.0575  0.0284  0.0373  780 ILE A O   
11457 C CB  . ILE A  754 ? 0.7783 0.4009 0.6365 0.0316  0.0270  0.0210  780 ILE A CB  
11458 C CG1 . ILE A  754 ? 0.7795 0.4287 0.6504 0.0359  0.0219  0.0239  780 ILE A CG1 
11459 C CG2 . ILE A  754 ? 0.7877 0.3985 0.6423 0.0362  0.0324  0.0152  780 ILE A CG2 
11460 C CD1 . ILE A  754 ? 0.7923 0.4568 0.6667 0.0289  0.0166  0.0266  780 ILE A CD1 
11472 N N   . GLY A  755 ? 0.7771 0.3522 0.6265 0.0533  0.0368  0.0341  781 GLY A N   
11473 C CA  . GLY A  755 ? 0.7759 0.3425 0.6279 0.0669  0.0404  0.0383  781 GLY A CA  
11474 C C   . GLY A  755 ? 0.7596 0.3377 0.6206 0.0762  0.0367  0.0487  781 GLY A C   
11475 O O   . GLY A  755 ? 0.7531 0.3405 0.6227 0.0869  0.0369  0.0513  781 GLY A O   
11479 N N   . ASP A  756 ? 0.7515 0.3303 0.6109 0.0718  0.0332  0.0546  782 ASP A N   
11480 C CA  . ASP A  756 ? 0.7458 0.3361 0.6130 0.0796  0.0292  0.0647  782 ASP A CA  
11481 C C   . ASP A  756 ? 0.7188 0.3381 0.5988 0.0821  0.0241  0.0651  782 ASP A C   
11482 O O   . ASP A  756 ? 0.7158 0.3441 0.6041 0.0928  0.0231  0.0708  782 ASP A O   
11483 C CB  . ASP A  756 ? 0.7866 0.3731 0.6486 0.0726  0.0263  0.0701  782 ASP A CB  
11484 C CG  . ASP A  756 ? 0.8844 0.4420 0.7346 0.0723  0.0311  0.0724  782 ASP A CG  
11485 O OD1 . ASP A  756 ? 0.9028 0.4469 0.7524 0.0831  0.0350  0.0764  782 ASP A OD1 
11486 O OD2 . ASP A  756 ? 0.9352 0.4836 0.7768 0.0612  0.0312  0.0704  782 ASP A OD2 
11491 N N   . PHE A  757 ? 0.6949 0.3289 0.5766 0.0726  0.0211  0.0589  783 PHE A N   
11492 C CA  . PHE A  757 ? 0.6761 0.3363 0.5693 0.0745  0.0167  0.0588  783 PHE A CA  
11493 C C   . PHE A  757 ? 0.6702 0.3336 0.5687 0.0828  0.0198  0.0552  783 PHE A C   
11494 O O   . PHE A  757 ? 0.6591 0.3397 0.5678 0.0898  0.0174  0.0586  783 PHE A O   
11495 C CB  . PHE A  757 ? 0.6664 0.3402 0.5598 0.0627  0.0132  0.0532  783 PHE A CB  
11496 C CG  . PHE A  757 ? 0.6540 0.3535 0.5586 0.0645  0.0089  0.0532  783 PHE A CG  
11497 C CD1 . PHE A  757 ? 0.6560 0.3697 0.5683 0.0693  0.0047  0.0607  783 PHE A CD1 
11498 C CD2 . PHE A  757 ? 0.6541 0.3634 0.5614 0.0612  0.0091  0.0458  783 PHE A CD2 
11499 C CE1 . PHE A  757 ? 0.6507 0.3871 0.5728 0.0706  0.0010  0.0605  783 PHE A CE1 
11500 C CE2 . PHE A  757 ? 0.6492 0.3809 0.5664 0.0629  0.0055  0.0460  783 PHE A CE2 
11501 C CZ  . PHE A  757 ? 0.6411 0.3858 0.5657 0.0676  0.0016  0.0532  783 PHE A CZ  
11511 N N   . ARG A  758 ? 0.6767 0.3238 0.5681 0.0819  0.0253  0.0485  784 ARG A N   
11512 C CA  . ARG A  758 ? 0.6833 0.3314 0.5785 0.0898  0.0290  0.0450  784 ARG A CA  
11513 C C   . ARG A  758 ? 0.6894 0.3343 0.5900 0.1036  0.0308  0.0526  784 ARG A C   
11514 O O   . ARG A  758 ? 0.6794 0.3384 0.5894 0.1115  0.0306  0.0537  784 ARG A O   
11515 C CB  . ARG A  758 ? 0.7082 0.3363 0.5929 0.0859  0.0350  0.0365  784 ARG A CB  
11516 C CG  . ARG A  758 ? 0.7520 0.3876 0.6338 0.0742  0.0335  0.0279  784 ARG A CG  
11517 C CD  . ARG A  758 ? 0.7915 0.4459 0.6813 0.0768  0.0326  0.0239  784 ARG A CD  
11518 N NE  . ARG A  758 ? 0.8365 0.4824 0.7260 0.0856  0.0383  0.0212  784 ARG A NE  
11519 C CZ  . ARG A  758 ? 0.8768 0.5062 0.7569 0.0829  0.0435  0.0138  784 ARG A CZ  
11520 N NH1 . ARG A  758 ? 0.8765 0.4964 0.7469 0.0714  0.0437  0.0082  784 ARG A NH1 
11521 N NH2 . ARG A  758 ? 0.8836 0.5062 0.7640 0.0916  0.0488  0.0117  784 ARG A NH2 
11535 N N   . ARG A  759 ? 0.7024 0.3296 0.5971 0.1064  0.0326  0.0583  785 ARG A N   
11536 C CA  . ARG A  759 ? 0.7186 0.3425 0.6182 0.1197  0.0341  0.0664  785 ARG A CA  
11537 C C   . ARG A  759 ? 0.7093 0.3576 0.6206 0.1236  0.0276  0.0741  785 ARG A C   
11538 O O   . ARG A  759 ? 0.7108 0.3687 0.6312 0.1344  0.0278  0.0783  785 ARG A O   
11539 C CB  . ARG A  759 ? 0.7604 0.3584 0.6501 0.1213  0.0376  0.0708  785 ARG A CB  
11540 C CG  . ARG A  759 ? 0.8388 0.4110 0.7176 0.1202  0.0451  0.0636  785 ARG A CG  
11541 C CD  . ARG A  759 ? 0.9177 0.4629 0.7851 0.1192  0.0486  0.0669  785 ARG A CD  
11542 N NE  . ARG A  759 ? 0.9828 0.5101 0.8378 0.1080  0.0523  0.0578  785 ARG A NE  
11543 C CZ  . ARG A  759 ? 1.0304 0.5487 0.8766 0.0963  0.0510  0.0567  785 ARG A CZ  
11544 N NH1 . ARG A  759 ? 1.0291 0.5534 0.8767 0.0942  0.0463  0.0644  785 ARG A NH1 
11545 N NH2 . ARG A  759 ? 1.0444 0.5478 0.8801 0.0866  0.0546  0.0479  785 ARG A NH2 
11559 N N   . TRP A  760 ? 0.6949 0.3543 0.6062 0.1146  0.0220  0.0756  786 TRP A N   
11560 C CA  . TRP A  760 ? 0.6774 0.3602 0.5988 0.1168  0.0156  0.0821  786 TRP A CA  
11561 C C   . TRP A  760 ? 0.6669 0.3712 0.5988 0.1192  0.0142  0.0785  786 TRP A C   
11562 O O   . TRP A  760 ? 0.6589 0.3791 0.6008 0.1267  0.0115  0.0842  786 TRP A O   
11563 C CB  . TRP A  760 ? 0.6705 0.3594 0.5885 0.1054  0.0107  0.0827  786 TRP A CB  
11564 C CG  . TRP A  760 ? 0.6613 0.3729 0.5883 0.1067  0.0043  0.0890  786 TRP A CG  
11565 C CD1 . TRP A  760 ? 0.6688 0.3822 0.5971 0.1110  0.0014  0.0984  786 TRP A CD1 
11566 C CD2 . TRP A  760 ? 0.6464 0.3816 0.5816 0.1031  0.0002  0.0862  786 TRP A CD2 
11567 N NE1 . TRP A  760 ? 0.6601 0.3970 0.5965 0.1095  -0.0045 0.1013  786 TRP A NE1 
11568 C CE2 . TRP A  760 ? 0.6479 0.3982 0.5890 0.1050  -0.0052 0.0939  786 TRP A CE2 
11569 C CE3 . TRP A  760 ? 0.6471 0.3922 0.5853 0.0986  0.0005  0.0781  786 TRP A CE3 
11570 C CZ2 . TRP A  760 ? 0.6435 0.4172 0.5928 0.1023  -0.0098 0.0934  786 TRP A CZ2 
11571 C CZ3 . TRP A  760 ? 0.6449 0.4129 0.5913 0.0964  -0.0041 0.0780  786 TRP A CZ3 
11572 C CH2 . TRP A  760 ? 0.6413 0.4230 0.5931 0.0981  -0.0091 0.0854  786 TRP A CH2 
11583 N N   . MET A  761 ? 0.6630 0.3684 0.5927 0.1127  0.0158  0.0693  787 MET A N   
11584 C CA  . MET A  761 ? 0.6602 0.3845 0.5988 0.1145  0.0150  0.0655  787 MET A CA  
11585 C C   . MET A  761 ? 0.6726 0.3963 0.6173 0.1272  0.0189  0.0676  787 MET A C   
11586 O O   . MET A  761 ? 0.6662 0.4092 0.6214 0.1320  0.0168  0.0696  787 MET A O   
11587 C CB  . MET A  761 ? 0.6633 0.3856 0.5968 0.1056  0.0168  0.0554  787 MET A CB  
11588 C CG  . MET A  761 ? 0.6780 0.4083 0.6091 0.0936  0.0123  0.0531  787 MET A CG  
11589 S SD  . MET A  761 ? 0.6865 0.4102 0.6094 0.0827  0.0146  0.0419  787 MET A SD  
11590 C CE  . MET A  761 ? 0.6283 0.3688 0.5598 0.0871  0.0152  0.0377  787 MET A CE  
11600 N N   . ASP A  762 ? 0.6915 0.3930 0.6294 0.1324  0.0249  0.0670  788 ASP A N   
11601 C CA  . ASP A  762 ? 0.7090 0.4077 0.6520 0.1452  0.0294  0.0691  788 ASP A CA  
11602 C C   . ASP A  762 ? 0.7154 0.4234 0.6670 0.1550  0.0266  0.0799  788 ASP A C   
11603 O O   . ASP A  762 ? 0.7089 0.4292 0.6704 0.1643  0.0272  0.0824  788 ASP A O   
11604 C CB  . ASP A  762 ? 0.7472 0.4175 0.6795 0.1478  0.0368  0.0657  788 ASP A CB  
11605 C CG  . ASP A  762 ? 0.8135 0.4742 0.7373 0.1396  0.0404  0.0549  788 ASP A CG  
11606 O OD1 . ASP A  762 ? 0.8110 0.4881 0.7386 0.1339  0.0378  0.0499  788 ASP A OD1 
11607 O OD2 . ASP A  762 ? 0.8601 0.4967 0.7732 0.1386  0.0458  0.0514  788 ASP A OD2 
11612 N N   . GLU A  763 ? 0.7261 0.4288 0.6741 0.1528  0.0234  0.0863  789 GLU A N   
11613 C CA  . GLU A  763 ? 0.7381 0.4496 0.6933 0.1613  0.0201  0.0970  789 GLU A CA  
11614 C C   . GLU A  763 ? 0.7315 0.4716 0.6971 0.1589  0.0129  0.1002  789 GLU A C   
11615 O O   . GLU A  763 ? 0.7337 0.4849 0.7069 0.1663  0.0100  0.1086  789 GLU A O   
11616 C CB  . GLU A  763 ? 0.7851 0.4797 0.7313 0.1592  0.0193  0.1027  789 GLU A CB  
11617 C CG  . GLU A  763 ? 0.8740 0.5391 0.8101 0.1630  0.0264  0.1015  789 GLU A CG  
11618 C CD  . GLU A  763 ? 0.9858 0.6325 0.9113 0.1584  0.0261  0.1057  789 GLU A CD  
11619 O OE1 . GLU A  763 ? 1.0042 0.6603 0.9288 0.1502  0.0204  0.1081  789 GLU A OE1 
11620 O OE2 . GLU A  763 ? 1.0402 0.6624 0.9578 0.1628  0.0318  0.1064  789 GLU A OE2 
11627 N N   . HIS A  764 ? 0.7223 0.4737 0.6879 0.1484  0.0101  0.0938  790 HIS A N   
11628 C CA  . HIS A  764 ? 0.7129 0.4898 0.6872 0.1450  0.0036  0.0959  790 HIS A CA  
11629 C C   . HIS A  764 ? 0.7075 0.4983 0.6874 0.1426  0.0042  0.0887  790 HIS A C   
11630 O O   . HIS A  764 ? 0.7046 0.5037 0.6834 0.1329  0.0014  0.0840  790 HIS A O   
11631 C CB  . HIS A  764 ? 0.7218 0.4993 0.6901 0.1340  -0.0010 0.0966  790 HIS A CB  
11632 C CG  . HIS A  764 ? 0.7562 0.5216 0.7190 0.1360  -0.0020 0.1043  790 HIS A CG  
11633 N ND1 . HIS A  764 ? 0.7924 0.5327 0.7440 0.1345  0.0023  0.1031  790 HIS A ND1 
11634 C CD2 . HIS A  764 ? 0.7669 0.5420 0.7337 0.1394  -0.0065 0.1134  790 HIS A CD2 
11635 C CE1 . HIS A  764 ? 0.8017 0.5368 0.7509 0.1371  0.0003  0.1116  790 HIS A CE1 
11636 N NE2 . HIS A  764 ? 0.7927 0.5485 0.7508 0.1403  -0.0051 0.1181  790 HIS A NE2 
11644 N N   . LEU A  765 ? 0.7021 0.4956 0.6882 0.1517  0.0080  0.0879  791 LEU A N   
11645 C CA  . LEU A  765 ? 0.7001 0.5068 0.6918 0.1503  0.0090  0.0816  791 LEU A CA  
11646 C C   . LEU A  765 ? 0.6906 0.5233 0.6922 0.1477  0.0030  0.0840  791 LEU A C   
11647 O O   . LEU A  765 ? 0.6901 0.5338 0.6948 0.1437  0.0028  0.0785  791 LEU A O   
11648 C CB  . LEU A  765 ? 0.7049 0.5081 0.7008 0.1612  0.0148  0.0808  791 LEU A CB  
11649 C CG  . LEU A  765 ? 0.7376 0.5149 0.7235 0.1635  0.0217  0.0766  791 LEU A CG  
11650 C CD1 . LEU A  765 ? 0.7428 0.5183 0.7341 0.1757  0.0274  0.0772  791 LEU A CD1 
11651 C CD2 . LEU A  765 ? 0.7529 0.5223 0.7300 0.1533  0.0236  0.0666  791 LEU A CD2 
11663 N N   . ASN A  766 ? 0.6811 0.5236 0.6873 0.1498  -0.0018 0.0922  792 ASN A N   
11664 C CA  . ASN A  766 ? 0.6693 0.5356 0.6839 0.1464  -0.0076 0.0945  792 ASN A CA  
11665 C C   . ASN A  766 ? 0.6407 0.5095 0.6497 0.1337  -0.0112 0.0903  792 ASN A C   
11666 O O   . ASN A  766 ? 0.6330 0.5198 0.6477 0.1293  -0.0149 0.0894  792 ASN A O   
11667 C CB  . ASN A  766 ? 0.7046 0.5799 0.7249 0.1524  -0.0116 0.1045  792 ASN A CB  
11668 C CG  . ASN A  766 ? 0.7795 0.6808 0.8106 0.1517  -0.0165 0.1071  792 ASN A CG  
11669 O OD1 . ASN A  766 ? 0.8026 0.7160 0.8424 0.1566  -0.0150 0.1061  792 ASN A OD1 
11670 N ND2 . ASN A  766 ? 0.7996 0.7100 0.8300 0.1455  -0.0223 0.1106  792 ASN A ND2 
11677 N N   . VAL A  767 ? 0.6227 0.4737 0.6208 0.1278  -0.0101 0.0878  793 VAL A N   
11678 C CA  . VAL A  767 ? 0.6038 0.4565 0.5967 0.1162  -0.0129 0.0836  793 VAL A CA  
11679 C C   . VAL A  767 ? 0.5787 0.4296 0.5696 0.1119  -0.0098 0.0745  793 VAL A C   
11680 O O   . VAL A  767 ? 0.5841 0.4179 0.5678 0.1115  -0.0054 0.0703  793 VAL A O   
11681 C CB  . VAL A  767 ? 0.6209 0.4565 0.6033 0.1114  -0.0130 0.0851  793 VAL A CB  
11682 C CG1 . VAL A  767 ? 0.6251 0.4640 0.6029 0.0995  -0.0157 0.0807  793 VAL A CG1 
11683 C CG2 . VAL A  767 ? 0.6277 0.4638 0.6111 0.1162  -0.0159 0.0946  793 VAL A CG2 
11693 N N   . LYS A  768 ? 0.5516 0.4199 0.5488 0.1087  -0.0119 0.0717  794 LYS A N   
11694 C CA  . LYS A  768 ? 0.5403 0.4090 0.5363 0.1048  -0.0093 0.0637  794 LYS A CA  
11695 C C   . LYS A  768 ? 0.5232 0.3835 0.5103 0.0946  -0.0098 0.0586  794 LYS A C   
11696 O O   . LYS A  768 ? 0.5104 0.3758 0.4964 0.0885  -0.0137 0.0604  794 LYS A O   
11697 C CB  . LYS A  768 ? 0.5589 0.4487 0.5639 0.1040  -0.0118 0.0629  794 LYS A CB  
11698 C CG  . LYS A  768 ? 0.6179 0.5189 0.6328 0.1133  -0.0114 0.0673  794 LYS A CG  
11699 C CD  . LYS A  768 ? 0.6809 0.6008 0.7039 0.1118  -0.0126 0.0651  794 LYS A CD  
11700 C CE  . LYS A  768 ? 0.7309 0.6659 0.7574 0.1058  -0.0182 0.0675  794 LYS A CE  
11701 N NZ  . LYS A  768 ? 0.7574 0.7008 0.7894 0.1104  -0.0215 0.0754  794 LYS A NZ  
11715 N N   . ILE A  769 ? 0.5173 0.3657 0.4982 0.0926  -0.0058 0.0521  795 ILE A N   
11716 C CA  . ILE A  769 ? 0.5167 0.3581 0.4897 0.0829  -0.0059 0.0467  795 ILE A CA  
11717 C C   . ILE A  769 ? 0.5158 0.3634 0.4901 0.0809  -0.0042 0.0399  795 ILE A C   
11718 O O   . ILE A  769 ? 0.5232 0.3612 0.4943 0.0838  0.0002  0.0361  795 ILE A O   
11719 C CB  . ILE A  769 ? 0.5246 0.3437 0.4873 0.0817  -0.0026 0.0455  795 ILE A CB  
11720 C CG1 . ILE A  769 ? 0.5331 0.3461 0.4944 0.0840  -0.0043 0.0529  795 ILE A CG1 
11721 C CG2 . ILE A  769 ? 0.5306 0.3449 0.4859 0.0711  -0.0028 0.0394  795 ILE A CG2 
11722 C CD1 . ILE A  769 ? 0.5540 0.3443 0.5061 0.0850  -0.0006 0.0532  795 ILE A CD1 
11734 N N   . PRO A  770 ? 0.5026 0.3662 0.4816 0.0763  -0.0074 0.0386  796 PRO A N   
11735 C CA  . PRO A  770 ? 0.5005 0.3701 0.4807 0.0748  -0.0058 0.0328  796 PRO A CA  
11736 C C   . PRO A  770 ? 0.5092 0.3688 0.4808 0.0680  -0.0040 0.0262  796 PRO A C   
11737 O O   . PRO A  770 ? 0.5120 0.3627 0.4772 0.0624  -0.0048 0.0258  796 PRO A O   
11738 C CB  . PRO A  770 ? 0.5032 0.3917 0.4905 0.0719  -0.0098 0.0340  796 PRO A CB  
11739 C CG  . PRO A  770 ? 0.5085 0.4005 0.4975 0.0710  -0.0135 0.0398  796 PRO A CG  
11740 C CD  . PRO A  770 ? 0.4927 0.3688 0.4756 0.0725  -0.0123 0.0423  796 PRO A CD  
11748 N N   . ARG A  771 ? 0.5052 0.3671 0.4767 0.0683  -0.0016 0.0212  797 ARG A N   
11749 C CA  . ARG A  771 ? 0.5107 0.3661 0.4749 0.0620  -0.0001 0.0146  797 ARG A CA  
11750 C C   . ARG A  771 ? 0.5012 0.3372 0.4556 0.0596  0.0023  0.0128  797 ARG A C   
11751 O O   . ARG A  771 ? 0.4913 0.3235 0.4404 0.0518  0.0010  0.0106  797 ARG A O   
11752 C CB  . ARG A  771 ? 0.5400 0.4066 0.5051 0.0541  -0.0039 0.0132  797 ARG A CB  
11753 C CG  . ARG A  771 ? 0.5991 0.4835 0.5725 0.0554  -0.0058 0.0138  797 ARG A CG  
11754 C CD  . ARG A  771 ? 0.6507 0.5379 0.6234 0.0559  -0.0034 0.0089  797 ARG A CD  
11755 N NE  . ARG A  771 ? 0.6886 0.5728 0.6548 0.0485  -0.0035 0.0037  797 ARG A NE  
11756 C CZ  . ARG A  771 ? 0.7101 0.5992 0.6753 0.0469  -0.0026 -0.0005 797 ARG A CZ  
11757 N NH1 . ARG A  771 ? 0.7059 0.6027 0.6759 0.0519  -0.0012 -0.0003 797 ARG A NH1 
11758 N NH2 . ARG A  771 ? 0.7105 0.5974 0.6699 0.0401  -0.0031 -0.0047 797 ARG A NH2 
11772 N N   . LEU A  772 ? 0.5026 0.3263 0.4550 0.0663  0.0062  0.0136  798 LEU A N   
11773 C CA  . LEU A  772 ? 0.5165 0.3198 0.4591 0.0645  0.0093  0.0117  798 LEU A CA  
11774 C C   . LEU A  772 ? 0.5136 0.3105 0.4481 0.0573  0.0111  0.0040  798 LEU A C   
11775 O O   . LEU A  772 ? 0.5193 0.3028 0.4455 0.0517  0.0120  0.0018  798 LEU A O   
11776 C CB  . LEU A  772 ? 0.5340 0.3256 0.4762 0.0740  0.0138  0.0137  798 LEU A CB  
11777 C CG  . LEU A  772 ? 0.5560 0.3508 0.5049 0.0814  0.0123  0.0218  798 LEU A CG  
11778 C CD1 . LEU A  772 ? 0.5684 0.3543 0.5183 0.0917  0.0171  0.0231  798 LEU A CD1 
11779 C CD2 . LEU A  772 ? 0.5699 0.3559 0.5143 0.0776  0.0102  0.0257  798 LEU A CD2 
11791 N N   . VAL A  773 ? 0.5039 0.3109 0.4406 0.0569  0.0115  -0.0001 799 VAL A N   
11792 C CA  . VAL A  773 ? 0.5068 0.3114 0.4365 0.0496  0.0123  -0.0071 799 VAL A CA  
11793 C C   . VAL A  773 ? 0.4961 0.3039 0.4234 0.0399  0.0085  -0.0078 799 VAL A C   
11794 O O   . VAL A  773 ? 0.5077 0.3084 0.4272 0.0331  0.0094  -0.0129 799 VAL A O   
11795 C CB  . VAL A  773 ? 0.5154 0.3337 0.4491 0.0507  0.0123  -0.0101 799 VAL A CB  
11796 C CG1 . VAL A  773 ? 0.5277 0.3401 0.4606 0.0582  0.0173  -0.0120 799 VAL A CG1 
11797 C CG2 . VAL A  773 ? 0.5088 0.3464 0.4529 0.0522  0.0082  -0.0056 799 VAL A CG2 
11807 N N   . ASP A  774 ? 0.4755 0.2947 0.4093 0.0392  0.0043  -0.0028 800 ASP A N   
11808 C CA  . ASP A  774 ? 0.4694 0.2934 0.4021 0.0308  0.0008  -0.0028 800 ASP A CA  
11809 C C   . ASP A  774 ? 0.4708 0.2837 0.3997 0.0284  0.0003  0.0006  800 ASP A C   
11810 O O   . ASP A  774 ? 0.4710 0.2872 0.3987 0.0214  -0.0022 0.0006  800 ASP A O   
11811 C CB  . ASP A  774 ? 0.4805 0.3239 0.4221 0.0308  -0.0031 -0.0001 800 ASP A CB  
11812 C CG  . ASP A  774 ? 0.5363 0.3909 0.4814 0.0321  -0.0029 -0.0032 800 ASP A CG  
11813 O OD1 . ASP A  774 ? 0.5415 0.3907 0.4811 0.0305  -0.0005 -0.0084 800 ASP A OD1 
11814 O OD2 . ASP A  774 ? 0.5675 0.4362 0.5203 0.0344  -0.0051 -0.0005 800 ASP A OD2 
11819 N N   . VAL A  775 ? 0.4676 0.2676 0.3946 0.0345  0.0029  0.0036  801 VAL A N   
11820 C CA  . VAL A  775 ? 0.4735 0.2607 0.3959 0.0329  0.0031  0.0070  801 VAL A CA  
11821 C C   . VAL A  775 ? 0.4887 0.2579 0.4004 0.0286  0.0070  0.0013  801 VAL A C   
11822 O O   . VAL A  775 ? 0.4821 0.2377 0.3901 0.0338  0.0111  0.0007  801 VAL A O   
11823 C CB  . VAL A  775 ? 0.4812 0.2645 0.4074 0.0425  0.0039  0.0136  801 VAL A CB  
11824 C CG1 . VAL A  775 ? 0.4950 0.2651 0.4160 0.0408  0.0039  0.0177  801 VAL A CG1 
11825 C CG2 . VAL A  775 ? 0.4767 0.2790 0.4135 0.0468  0.0003  0.0182  801 VAL A CG2 
11835 N N   . ILE A  776 ? 0.5047 0.2752 0.4120 0.0188  0.0058  -0.0030 802 ILE A N   
11836 C CA  . ILE A  776 ? 0.5285 0.2867 0.4262 0.0125  0.0087  -0.0097 802 ILE A CA  
11837 C C   . ILE A  776 ? 0.5451 0.2884 0.4344 0.0051  0.0095  -0.0099 802 ILE A C   
11838 O O   . ILE A  776 ? 0.5432 0.2909 0.4343 0.0014  0.0066  -0.0062 802 ILE A O   
11839 C CB  . ILE A  776 ? 0.5405 0.3143 0.4402 0.0065  0.0063  -0.0146 802 ILE A CB  
11840 C CG1 . ILE A  776 ? 0.5526 0.3364 0.4578 0.0135  0.0069  -0.0157 802 ILE A CG1 
11841 C CG2 . ILE A  776 ? 0.5590 0.3241 0.4493 -0.0024 0.0079  -0.0214 802 ILE A CG2 
11842 C CD1 . ILE A  776 ? 0.5622 0.3663 0.4732 0.0101  0.0033  -0.0174 802 ILE A CD1 
11854 N N   . CYS A  777 ? 0.5600 0.2861 0.4397 0.0022  0.0135  -0.0149 803 CYS A N   
11855 C CA  . CYS A  777 ? 0.5797 0.2900 0.4502 -0.0057 0.0150  -0.0163 803 CYS A CA  
11856 C C   . CYS A  777 ? 0.5861 0.3066 0.4552 -0.0169 0.0122  -0.0207 803 CYS A C   
11857 O O   . CYS A  777 ? 0.5902 0.3171 0.4585 -0.0194 0.0123  -0.0263 803 CYS A O   
11858 C CB  . CYS A  777 ? 0.5997 0.2881 0.4603 -0.0049 0.0206  -0.0207 803 CYS A CB  
11859 S SG  . CYS A  777 ? 0.6731 0.3489 0.5352 0.0092  0.0247  -0.0162 803 CYS A SG  
11864 N N   . ALA A  778 ? 0.5871 0.3080 0.4551 -0.0237 0.0102  -0.0185 804 ALA A N   
11865 C CA  . ALA A  778 ? 0.5957 0.3248 0.4619 -0.0349 0.0080  -0.0225 804 ALA A CA  
11866 C C   . ALA A  778 ? 0.6134 0.3238 0.4680 -0.0434 0.0113  -0.0271 804 ALA A C   
11867 O O   . ALA A  778 ? 0.6117 0.3272 0.4634 -0.0525 0.0103  -0.0322 804 ALA A O   
11868 C CB  . ALA A  778 ? 0.5938 0.3350 0.4656 -0.0380 0.0043  -0.0177 804 ALA A CB  
11874 N N   . SER A  779 ? 0.6288 0.3178 0.4768 -0.0405 0.0150  -0.0251 805 SER A N   
11875 C CA  . SER A  779 ? 0.6521 0.3206 0.4884 -0.0482 0.0187  -0.0290 805 SER A CA  
11876 C C   . SER A  779 ? 0.6739 0.3195 0.5041 -0.0404 0.0238  -0.0277 805 SER A C   
11877 O O   . SER A  779 ? 0.6733 0.3196 0.5092 -0.0302 0.0237  -0.0217 805 SER A O   
11878 C CB  . SER A  779 ? 0.6703 0.3370 0.5048 -0.0560 0.0172  -0.0257 805 SER A CB  
11879 O OG  . SER A  779 ? 0.7096 0.3705 0.5464 -0.0493 0.0173  -0.0180 805 SER A OG  
11885 N N   . PRO A  780 ? 0.6912 0.3160 0.5100 -0.0452 0.0283  -0.0329 806 PRO A N   
11886 C CA  . PRO A  780 ? 0.6980 0.3200 0.5089 -0.0576 0.0289  -0.0407 806 PRO A CA  
11887 C C   . PRO A  780 ? 0.6974 0.3331 0.5105 -0.0578 0.0279  -0.0469 806 PRO A C   
11888 O O   . PRO A  780 ? 0.6883 0.3344 0.5087 -0.0484 0.0271  -0.0452 806 PRO A O   
11889 C CB  . PRO A  780 ? 0.7202 0.3129 0.5185 -0.0594 0.0349  -0.0431 806 PRO A CB  
11890 C CG  . PRO A  780 ? 0.7269 0.3099 0.5270 -0.0456 0.0381  -0.0395 806 PRO A CG  
11891 C CD  . PRO A  780 ? 0.6941 0.2958 0.5070 -0.0373 0.0337  -0.0316 806 PRO A CD  
11899 N N   . GLY A  781 ? 0.7064 0.3433 0.5134 -0.0689 0.0276  -0.0538 807 GLY A N   
11900 C CA  . GLY A  781 ? 0.7176 0.3677 0.5254 -0.0706 0.0263  -0.0598 807 GLY A CA  
11901 C C   . GLY A  781 ? 0.7352 0.3784 0.5414 -0.0613 0.0299  -0.0621 807 GLY A C   
11902 O O   . GLY A  781 ? 0.7268 0.3864 0.5398 -0.0563 0.0278  -0.0624 807 GLY A O   
11906 N N   . ASP A  782 ? 0.7609 0.3793 0.5580 -0.0588 0.0356  -0.0637 808 ASP A N   
11907 C CA  . ASP A  782 ? 0.7836 0.3929 0.5783 -0.0496 0.0400  -0.0661 808 ASP A CA  
11908 C C   . ASP A  782 ? 0.7799 0.3997 0.5861 -0.0357 0.0390  -0.0594 808 ASP A C   
11909 O O   . ASP A  782 ? 0.7815 0.4023 0.5886 -0.0287 0.0412  -0.0616 808 ASP A O   
11910 C CB  . ASP A  782 ? 0.8392 0.4182 0.6218 -0.0493 0.0467  -0.0685 808 ASP A CB  
11911 C CG  . ASP A  782 ? 0.9421 0.5075 0.7244 -0.0473 0.0477  -0.0617 808 ASP A CG  
11912 O OD1 . ASP A  782 ? 0.9688 0.5350 0.7493 -0.0569 0.0453  -0.0608 808 ASP A OD1 
11913 O OD2 . ASP A  782 ? 0.9825 0.5368 0.7664 -0.0361 0.0509  -0.0571 808 ASP A OD2 
11918 N N   . GLN A  783 ? 0.7712 0.3992 0.5860 -0.0322 0.0357  -0.0516 809 GLN A N   
11919 C CA  . GLN A  783 ? 0.7652 0.4042 0.5911 -0.0200 0.0342  -0.0449 809 GLN A CA  
11920 C C   . GLN A  783 ? 0.7569 0.4234 0.5940 -0.0204 0.0282  -0.0425 809 GLN A C   
11921 O O   . GLN A  783 ? 0.7519 0.4296 0.5983 -0.0111 0.0269  -0.0381 809 GLN A O   
11922 C CB  . GLN A  783 ? 0.7808 0.4088 0.6081 -0.0147 0.0350  -0.0372 809 GLN A CB  
11923 C CG  . GLN A  783 ? 0.8175 0.4168 0.6337 -0.0139 0.0411  -0.0385 809 GLN A CG  
11924 C CD  . GLN A  783 ? 0.8706 0.4591 0.6835 -0.0060 0.0465  -0.0422 809 GLN A CD  
11925 O OE1 . GLN A  783 ? 0.8774 0.4792 0.6980 0.0020  0.0458  -0.0414 809 GLN A OE1 
11926 N NE2 . GLN A  783 ? 0.8916 0.4550 0.6925 -0.0081 0.0522  -0.0463 809 GLN A NE2 
11935 N N   . ARG A  784 ? 0.7523 0.4298 0.5890 -0.0310 0.0246  -0.0452 810 ARG A N   
11936 C CA  . ARG A  784 ? 0.7433 0.4461 0.5901 -0.0318 0.0192  -0.0432 810 ARG A CA  
11937 C C   . ARG A  784 ? 0.7229 0.4385 0.5754 -0.0248 0.0189  -0.0445 810 ARG A C   
11938 O O   . ARG A  784 ? 0.7230 0.4321 0.5695 -0.0247 0.0219  -0.0501 810 ARG A O   
11939 C CB  . ARG A  784 ? 0.7737 0.4843 0.6175 -0.0444 0.0164  -0.0473 810 ARG A CB  
11940 C CG  . ARG A  784 ? 0.8292 0.5655 0.6824 -0.0459 0.0113  -0.0465 810 ARG A CG  
11941 C CD  . ARG A  784 ? 0.8853 0.6310 0.7398 -0.0556 0.0078  -0.0460 810 ARG A CD  
11942 N NE  . ARG A  784 ? 0.9450 0.6780 0.7895 -0.0661 0.0095  -0.0506 810 ARG A NE  
11943 C CZ  . ARG A  784 ? 0.9918 0.7299 0.8361 -0.0754 0.0073  -0.0503 810 ARG A CZ  
11944 N NH1 . ARG A  784 ? 1.0052 0.7308 0.8400 -0.0851 0.0092  -0.0547 810 ARG A NH1 
11945 N NH2 . ARG A  784 ? 0.9925 0.7476 0.8459 -0.0750 0.0035  -0.0458 810 ARG A NH2 
11959 N N   . GLY A  785 ? 0.7012 0.4342 0.5646 -0.0192 0.0154  -0.0394 811 GLY A N   
11960 C CA  . GLY A  785 ? 0.6889 0.4354 0.5587 -0.0125 0.0148  -0.0397 811 GLY A CA  
11961 C C   . GLY A  785 ? 0.6823 0.4228 0.5554 -0.0009 0.0179  -0.0364 811 GLY A C   
11962 O O   . GLY A  785 ? 0.6785 0.4327 0.5599 0.0056  0.0165  -0.0338 811 GLY A O   
11966 N N   . LYS A  786 ? 0.6802 0.4002 0.5468 0.0019  0.0221  -0.0362 812 LYS A N   
11967 C CA  . LYS A  786 ? 0.6852 0.3985 0.5547 0.0133  0.0255  -0.0330 812 LYS A CA  
11968 C C   . LYS A  786 ? 0.6746 0.3932 0.5526 0.0197  0.0232  -0.0246 812 LYS A C   
11969 O O   . LYS A  786 ? 0.6757 0.3929 0.5535 0.0152  0.0208  -0.0213 812 LYS A O   
11970 C CB  . LYS A  786 ? 0.7303 0.4185 0.5891 0.0141  0.0315  -0.0362 812 LYS A CB  
11971 C CG  . LYS A  786 ? 0.8025 0.4841 0.6519 0.0088  0.0345  -0.0450 812 LYS A CG  
11972 C CD  . LYS A  786 ? 0.8938 0.5490 0.7316 0.0080  0.0404  -0.0484 812 LYS A CD  
11973 C CE  . LYS A  786 ? 0.9611 0.6090 0.7887 0.0024  0.0436  -0.0575 812 LYS A CE  
11974 N NZ  . LYS A  786 ? 1.0011 0.6510 0.8304 0.0111  0.0470  -0.0595 812 LYS A NZ  
11988 N N   . SER A  787 ? 0.6624 0.3870 0.5479 0.0300  0.0240  -0.0210 813 SER A N   
11989 C CA  . SER A  787 ? 0.6564 0.3863 0.5500 0.0368  0.0219  -0.0129 813 SER A CA  
11990 C C   . SER A  787 ? 0.6629 0.3724 0.5507 0.0389  0.0248  -0.0098 813 SER A C   
11991 O O   . SER A  787 ? 0.6721 0.3633 0.5516 0.0397  0.0298  -0.0136 813 SER A O   
11992 C CB  . SER A  787 ? 0.6616 0.4008 0.5636 0.0473  0.0230  -0.0105 813 SER A CB  
11993 O OG  . SER A  787 ? 0.6734 0.4180 0.5832 0.0538  0.0209  -0.0027 813 SER A OG  
11999 N N   . ILE A  788 ? 0.6568 0.3689 0.5485 0.0399  0.0218  -0.0030 814 ILE A N   
12000 C CA  . ILE A  788 ? 0.6739 0.3671 0.5603 0.0422  0.0242  0.0010  814 ILE A CA  
12001 C C   . ILE A  788 ? 0.6969 0.3796 0.5841 0.0538  0.0289  0.0030  814 ILE A C   
12002 O O   . ILE A  788 ? 0.7074 0.3692 0.5870 0.0555  0.0331  0.0031  814 ILE A O   
12003 C CB  . ILE A  788 ? 0.6679 0.3672 0.5583 0.0410  0.0199  0.0083  814 ILE A CB  
12004 C CG1 . ILE A  788 ? 0.6659 0.3812 0.5678 0.0501  0.0171  0.0150  814 ILE A CG1 
12005 C CG2 . ILE A  788 ? 0.6655 0.3750 0.5550 0.0296  0.0158  0.0059  814 ILE A CG2 
12006 C CD1 . ILE A  788 ? 0.6777 0.3965 0.5823 0.0500  0.0134  0.0226  814 ILE A CD1 
12018 N N   . VAL A  789 ? 0.7052 0.4021 0.6015 0.0617  0.0285  0.0044  815 VAL A N   
12019 C CA  . VAL A  789 ? 0.7324 0.4223 0.6309 0.0733  0.0329  0.0064  815 VAL A CA  
12020 C C   . VAL A  789 ? 0.7671 0.4419 0.6571 0.0733  0.0391  -0.0015 815 VAL A C   
12021 O O   . VAL A  789 ? 0.7767 0.4393 0.6655 0.0820  0.0441  -0.0006 815 VAL A O   
12022 C CB  . VAL A  789 ? 0.7300 0.4416 0.6416 0.0811  0.0303  0.0106  815 VAL A CB  
12023 C CG1 . VAL A  789 ? 0.7293 0.4533 0.6432 0.0793  0.0306  0.0045  815 VAL A CG1 
12024 C CG2 . VAL A  789 ? 0.7439 0.4501 0.6599 0.0938  0.0336  0.0159  815 VAL A CG2 
12034 N N   . SER A  790 ? 0.7854 0.4610 0.6693 0.0637  0.0389  -0.0090 816 SER A N   
12035 C CA  . SER A  790 ? 0.8165 0.4780 0.6910 0.0622  0.0444  -0.0169 816 SER A CA  
12036 C C   . SER A  790 ? 0.8524 0.4885 0.7141 0.0569  0.0481  -0.0197 816 SER A C   
12037 O O   . SER A  790 ? 0.8647 0.4857 0.7176 0.0563  0.0534  -0.0261 816 SER A O   
12038 C CB  . SER A  790 ? 0.8310 0.5056 0.7045 0.0540  0.0422  -0.0236 816 SER A CB  
12039 O OG  . SER A  790 ? 0.8576 0.5539 0.7419 0.0586  0.0394  -0.0215 816 SER A OG  
12045 N N   . LEU A  791 ? 0.8665 0.4977 0.7266 0.0525  0.0455  -0.0154 817 LEU A N   
12046 C CA  . LEU A  791 ? 0.8967 0.5040 0.7447 0.0466  0.0488  -0.0176 817 LEU A CA  
12047 C C   . LEU A  791 ? 0.9241 0.5089 0.7672 0.0560  0.0556  -0.0165 817 LEU A C   
12048 O O   . LEU A  791 ? 0.9239 0.5122 0.7748 0.0675  0.0562  -0.0103 817 LEU A O   
12049 C CB  . LEU A  791 ? 0.9024 0.5113 0.7513 0.0413  0.0444  -0.0118 817 LEU A CB  
12050 C CG  . LEU A  791 ? 0.9414 0.5272 0.7785 0.0343  0.0471  -0.0128 817 LEU A CG  
12051 C CD1 . LEU A  791 ? 0.9559 0.5361 0.7834 0.0220  0.0482  -0.0220 817 LEU A CD1 
12052 C CD2 . LEU A  791 ? 0.9491 0.5390 0.7888 0.0310  0.0427  -0.0058 817 LEU A CD2 
12064 N N   . GLU A  792 ? 0.9437 0.5056 0.7738 0.0509  0.0608  -0.0228 818 GLU A N   
12065 C CA  . GLU A  792 ? 0.9674 0.5047 0.7907 0.0586  0.0682  -0.0231 818 GLU A CA  
12066 C C   . GLU A  792 ? 0.9740 0.5158 0.8013 0.0683  0.0720  -0.0259 818 GLU A C   
12067 O O   . GLU A  792 ? 0.9851 0.5155 0.8037 0.0659  0.0770  -0.0339 818 GLU A O   
12068 C CB  . GLU A  792 ? 0.9972 0.5250 0.8232 0.0666  0.0686  -0.0135 818 GLU A CB  
12069 C CG  . GLU A  792 ? 1.0645 0.5806 0.8834 0.0575  0.0670  -0.0114 818 GLU A CG  
12070 C CD  . GLU A  792 ? 1.1509 0.6705 0.9765 0.0635  0.0638  -0.0006 818 GLU A CD  
12071 O OE1 . GLU A  792 ? 1.1709 0.6717 0.9932 0.0714  0.0680  0.0041  818 GLU A OE1 
12072 O OE2 . GLU A  792 ? 1.1744 0.7152 1.0082 0.0605  0.0571  0.0034  818 GLU A OE2 
12079 N N   . ARG B  6   ? 0.5660 0.4956 0.5083 -0.1487 0.0289  -0.1288 32  ARG B N   
12080 C CA  . ARG B  6   ? 0.5629 0.5007 0.5088 -0.1386 0.0258  -0.1216 32  ARG B CA  
12081 C C   . ARG B  6   ? 0.5652 0.5003 0.5183 -0.1350 0.0272  -0.1130 32  ARG B C   
12082 O O   . ARG B  6   ? 0.5776 0.4966 0.5305 -0.1348 0.0329  -0.1107 32  ARG B O   
12083 C CB  . ARG B  6   ? 0.5751 0.5027 0.5155 -0.1316 0.0288  -0.1215 32  ARG B CB  
12084 C CG  . ARG B  6   ? 0.5843 0.5249 0.5249 -0.1240 0.0240  -0.1190 32  ARG B CG  
12085 C CD  . ARG B  6   ? 0.5894 0.5194 0.5239 -0.1184 0.0275  -0.1199 32  ARG B CD  
12086 N NE  . ARG B  6   ? 0.5913 0.5247 0.5180 -0.1219 0.0261  -0.1280 32  ARG B NE  
12087 C CZ  . ARG B  6   ? 0.5728 0.5218 0.4982 -0.1199 0.0205  -0.1290 32  ARG B CZ  
12088 N NH1 . ARG B  6   ? 0.5429 0.5056 0.4747 -0.1147 0.0159  -0.1228 32  ARG B NH1 
12089 N NH2 . ARG B  6   ? 0.5511 0.5023 0.4688 -0.1235 0.0196  -0.1364 32  ARG B NH2 
12102 N N   . SER B  7   ? 0.5522 0.5032 0.5114 -0.1326 0.0222  -0.1084 33  SER B N   
12103 C CA  . SER B  7   ? 0.5485 0.4992 0.5142 -0.1298 0.0228  -0.1005 33  SER B CA  
12104 C C   . SER B  7   ? 0.5352 0.4754 0.5015 -0.1209 0.0259  -0.0936 33  SER B C   
12105 O O   . SER B  7   ? 0.5324 0.4751 0.4970 -0.1144 0.0246  -0.0925 33  SER B O   
12106 C CB  . SER B  7   ? 0.5701 0.5404 0.5414 -0.1286 0.0167  -0.0978 33  SER B CB  
12107 O OG  . SER B  7   ? 0.6172 0.5879 0.5941 -0.1254 0.0171  -0.0902 33  SER B OG  
12113 N N   . TYR B  8   ? 0.5222 0.4515 0.4912 -0.1207 0.0301  -0.0886 34  TYR B N   
12114 C CA  . TYR B  8   ? 0.5193 0.4394 0.4896 -0.1124 0.0331  -0.0813 34  TYR B CA  
12115 C C   . TYR B  8   ? 0.5164 0.4342 0.4920 -0.1126 0.0345  -0.0742 34  TYR B C   
12116 O O   . TYR B  8   ? 0.5225 0.4344 0.4982 -0.1194 0.0371  -0.0761 34  TYR B O   
12117 C CB  . TYR B  8   ? 0.5211 0.4229 0.4861 -0.1113 0.0392  -0.0837 34  TYR B CB  
12118 C CG  . TYR B  8   ? 0.5244 0.4185 0.4913 -0.1022 0.0421  -0.0762 34  TYR B CG  
12119 C CD1 . TYR B  8   ? 0.5293 0.4282 0.4955 -0.0949 0.0401  -0.0746 34  TYR B CD1 
12120 C CD2 . TYR B  8   ? 0.5330 0.4169 0.5031 -0.1008 0.0461  -0.0697 34  TYR B CD2 
12121 C CE1 . TYR B  8   ? 0.5383 0.4321 0.5070 -0.0868 0.0423  -0.0673 34  TYR B CE1 
12122 C CE2 . TYR B  8   ? 0.5415 0.4207 0.5142 -0.0923 0.0481  -0.0621 34  TYR B CE2 
12123 C CZ  . TYR B  8   ? 0.5477 0.4320 0.5198 -0.0854 0.0462  -0.0610 34  TYR B CZ  
12124 O OH  . TYR B  8   ? 0.5618 0.4424 0.5369 -0.0773 0.0480  -0.0535 34  TYR B OH  
12134 N N   . PRO B  9   ? 0.5086 0.4309 0.4884 -0.1057 0.0330  -0.0663 35  PRO B N   
12135 C CA  . PRO B  9   ? 0.5059 0.4348 0.4865 -0.0974 0.0302  -0.0629 35  PRO B CA  
12136 C C   . PRO B  9   ? 0.5068 0.4540 0.4893 -0.0967 0.0237  -0.0638 35  PRO B C   
12137 O O   . PRO B  9   ? 0.5023 0.4546 0.4850 -0.0904 0.0215  -0.0615 35  PRO B O   
12138 C CB  . PRO B  9   ? 0.5108 0.4348 0.4953 -0.0921 0.0321  -0.0537 35  PRO B CB  
12139 C CG  . PRO B  9   ? 0.5136 0.4388 0.5010 -0.0976 0.0324  -0.0519 35  PRO B CG  
12140 C CD  . PRO B  9   ? 0.4949 0.4153 0.4791 -0.1061 0.0343  -0.0596 35  PRO B CD  
12148 N N   . CYS B  10  ? 0.5093 0.4665 0.4935 -0.1029 0.0209  -0.0667 36  CYS B N   
12149 C CA  . CYS B  10  ? 0.5172 0.4918 0.5038 -0.1021 0.0151  -0.0672 36  CYS B CA  
12150 C C   . CYS B  10  ? 0.5346 0.5159 0.5174 -0.1037 0.0124  -0.0743 36  CYS B C   
12151 O O   . CYS B  10  ? 0.5417 0.5159 0.5203 -0.1082 0.0147  -0.0800 36  CYS B O   
12152 C CB  . CYS B  10  ? 0.5192 0.5020 0.5098 -0.1073 0.0135  -0.0665 36  CYS B CB  
12153 S SG  . CYS B  10  ? 0.5458 0.5181 0.5392 -0.1085 0.0178  -0.0599 36  CYS B SG  
12158 N N   . ASP B  11  ? 0.5458 0.5414 0.5302 -0.1005 0.0076  -0.0739 37  ASP B N   
12159 C CA  . ASP B  11  ? 0.5670 0.5719 0.5485 -0.1017 0.0043  -0.0797 37  ASP B CA  
12160 C C   . ASP B  11  ? 0.5927 0.6123 0.5778 -0.1068 0.0006  -0.0817 37  ASP B C   
12161 O O   . ASP B  11  ? 0.5909 0.6184 0.5807 -0.1045 -0.0014 -0.0773 37  ASP B O   
12162 C CB  . ASP B  11  ? 0.5733 0.5838 0.5542 -0.0938 0.0018  -0.0772 37  ASP B CB  
12163 C CG  . ASP B  11  ? 0.6213 0.6197 0.5978 -0.0895 0.0051  -0.0770 37  ASP B CG  
12164 O OD1 . ASP B  11  ? 0.6353 0.6275 0.6066 -0.0927 0.0070  -0.0826 37  ASP B OD1 
12165 O OD2 . ASP B  11  ? 0.6428 0.6380 0.6210 -0.0831 0.0059  -0.0713 37  ASP B OD2 
12170 N N   . GLU B  12  ? 0.6161 0.6397 0.5991 -0.1135 -0.0004 -0.0884 38  GLU B N   
12171 C CA  . GLU B  12  ? 0.6429 0.6809 0.6299 -0.1187 -0.0036 -0.0904 38  GLU B CA  
12172 C C   . GLU B  12  ? 0.6768 0.7313 0.6640 -0.1171 -0.0088 -0.0928 38  GLU B C   
12173 O O   . GLU B  12  ? 0.6852 0.7411 0.6679 -0.1192 -0.0098 -0.0981 38  GLU B O   
12174 C CB  . GLU B  12  ? 0.6687 0.7017 0.6542 -0.1282 -0.0014 -0.0959 38  GLU B CB  
12175 C CG  . GLU B  12  ? 0.7234 0.7421 0.7099 -0.1307 0.0036  -0.0931 38  GLU B CG  
12176 C CD  . GLU B  12  ? 0.8090 0.8206 0.7935 -0.1402 0.0066  -0.0987 38  GLU B CD  
12177 O OE1 . GLU B  12  ? 0.8329 0.8474 0.8137 -0.1447 0.0053  -0.1055 38  GLU B OE1 
12178 O OE2 . GLU B  12  ? 0.8278 0.8306 0.8143 -0.1433 0.0102  -0.0962 38  GLU B OE2 
12185 N N   . LYS B  13  ? 0.6959 0.7631 0.6883 -0.1137 -0.0119 -0.0890 39  LYS B N   
12186 C CA  . LYS B  13  ? 0.7208 0.8046 0.7145 -0.1117 -0.0167 -0.0902 39  LYS B CA  
12187 C C   . LYS B  13  ? 0.7413 0.8381 0.7400 -0.1178 -0.0187 -0.0922 39  LYS B C   
12188 O O   . LYS B  13  ? 0.7417 0.8373 0.7445 -0.1202 -0.0170 -0.0898 39  LYS B O   
12189 C CB  . LYS B  13  ? 0.7503 0.8387 0.7464 -0.1030 -0.0183 -0.0844 39  LYS B CB  
12190 C CG  . LYS B  13  ? 0.8225 0.9026 0.8141 -0.0966 -0.0175 -0.0829 39  LYS B CG  
12191 C CD  . LYS B  13  ? 0.8859 0.9762 0.8783 -0.0896 -0.0208 -0.0802 39  LYS B CD  
12192 C CE  . LYS B  13  ? 0.9382 1.0308 0.9354 -0.0850 -0.0210 -0.0743 39  LYS B CE  
12193 N NZ  . LYS B  13  ? 0.9660 1.0681 0.9641 -0.0787 -0.0239 -0.0721 39  LYS B NZ  
12207 N N   . LYS B  14  ? 0.7535 0.8634 0.7520 -0.1203 -0.0222 -0.0965 40  LYS B N   
12208 C CA  . LYS B  14  ? 0.7668 0.8908 0.7705 -0.1262 -0.0243 -0.0985 40  LYS B CA  
12209 C C   . LYS B  14  ? 0.7722 0.9129 0.7806 -0.1207 -0.0282 -0.0955 40  LYS B C   
12210 O O   . LYS B  14  ? 0.7749 0.9219 0.7890 -0.1202 -0.0282 -0.0924 40  LYS B O   
12211 C CB  . LYS B  14  ? 0.7984 0.9263 0.7990 -0.1340 -0.0255 -0.1057 40  LYS B CB  
12212 C CG  . LYS B  14  ? 0.8706 0.9815 0.8640 -0.1376 -0.0221 -0.1097 40  LYS B CG  
12213 C CD  . LYS B  14  ? 0.9399 1.0344 0.9337 -0.1402 -0.0169 -0.1078 40  LYS B CD  
12214 C CE  . LYS B  14  ? 1.0004 1.0769 0.9871 -0.1421 -0.0130 -0.1111 40  LYS B CE  
12215 N NZ  . LYS B  14  ? 1.0343 1.1097 1.0182 -0.1521 -0.0123 -0.1184 40  LYS B NZ  
12229 N N   . ASP B  17  ? 0.7155 0.9194 0.7570 -0.1307 -0.0325 -0.0909 43  ASP B N   
12230 C CA  . ASP B  17  ? 0.7189 0.9215 0.7630 -0.1398 -0.0302 -0.0931 43  ASP B CA  
12231 C C   . ASP B  17  ? 0.7170 0.8999 0.7574 -0.1409 -0.0257 -0.0911 43  ASP B C   
12232 O O   . ASP B  17  ? 0.7223 0.9037 0.7660 -0.1434 -0.0231 -0.0888 43  ASP B O   
12233 C CB  . ASP B  17  ? 0.7431 0.9612 0.7953 -0.1407 -0.0305 -0.0913 43  ASP B CB  
12234 C CG  . ASP B  17  ? 0.8104 1.0488 0.8671 -0.1389 -0.0347 -0.0925 43  ASP B CG  
12235 O OD1 . ASP B  17  ? 0.8219 1.0671 0.8807 -0.1308 -0.0360 -0.0889 43  ASP B OD1 
12236 O OD2 . ASP B  17  ? 0.8386 1.0863 0.8968 -0.1458 -0.0366 -0.0969 43  ASP B OD2 
12240 N N   . SER B  18  ? 0.7050 0.8733 0.7387 -0.1389 -0.0248 -0.0917 44  SER B N   
12241 C CA  . SER B  18  ? 0.6965 0.8461 0.7267 -0.1391 -0.0206 -0.0894 44  SER B CA  
12242 C C   . SER B  18  ? 0.6819 0.8174 0.7048 -0.1376 -0.0198 -0.0913 44  SER B C   
12243 O O   . SER B  18  ? 0.6887 0.8291 0.7090 -0.1351 -0.0226 -0.0937 44  SER B O   
12244 C CB  . SER B  18  ? 0.7122 0.8595 0.7441 -0.1322 -0.0196 -0.0831 44  SER B CB  
12245 O OG  . SER B  18  ? 0.7407 0.8930 0.7718 -0.1240 -0.0223 -0.0813 44  SER B OG  
12251 N N   . VAL B  19  ? 0.6587 0.7771 0.6785 -0.1389 -0.0158 -0.0899 45  VAL B N   
12252 C CA  . VAL B  19  ? 0.6418 0.7453 0.6551 -0.1370 -0.0141 -0.0911 45  VAL B CA  
12253 C C   . VAL B  19  ? 0.6083 0.6987 0.6207 -0.1318 -0.0110 -0.0851 45  VAL B C   
12254 O O   . VAL B  19  ? 0.6085 0.6925 0.6226 -0.1348 -0.0080 -0.0827 45  VAL B O   
12255 C CB  . VAL B  19  ? 0.6608 0.7560 0.6703 -0.1454 -0.0120 -0.0972 45  VAL B CB  
12256 C CG1 . VAL B  19  ? 0.6707 0.7663 0.6838 -0.1538 -0.0098 -0.0982 45  VAL B CG1 
12257 C CG2 . VAL B  19  ? 0.6751 0.7510 0.6784 -0.1433 -0.0083 -0.0969 45  VAL B CG2 
12267 N N   . ILE B  20  ? 0.5759 0.6630 0.5858 -0.1240 -0.0119 -0.0825 46  ILE B N   
12268 C CA  . ILE B  20  ? 0.5574 0.6346 0.5669 -0.1183 -0.0097 -0.0765 46  ILE B CA  
12269 C C   . ILE B  20  ? 0.5307 0.5910 0.5351 -0.1174 -0.0064 -0.0767 46  ILE B C   
12270 O O   . ILE B  20  ? 0.5353 0.5933 0.5356 -0.1164 -0.0070 -0.0802 46  ILE B O   
12271 C CB  . ILE B  20  ? 0.5695 0.6546 0.5799 -0.1101 -0.0128 -0.0733 46  ILE B CB  
12272 C CG1 . ILE B  20  ? 0.5825 0.6845 0.5980 -0.1102 -0.0158 -0.0731 46  ILE B CG1 
12273 C CG2 . ILE B  20  ? 0.5776 0.6535 0.5877 -0.1046 -0.0109 -0.0672 46  ILE B CG2 
12274 C CD1 . ILE B  20  ? 0.5982 0.7092 0.6142 -0.1029 -0.0190 -0.0715 46  ILE B CD1 
12286 N N   . ALA B  21  ? 0.4999 0.5486 0.5045 -0.1172 -0.0028 -0.0725 47  ALA B N   
12287 C CA  . ALA B  21  ? 0.4865 0.5189 0.4871 -0.1151 0.0007  -0.0714 47  ALA B CA  
12288 C C   . ALA B  21  ? 0.4651 0.4960 0.4663 -0.1067 0.0003  -0.0652 47  ALA B C   
12289 O O   . ALA B  21  ? 0.4588 0.4891 0.4627 -0.1052 0.0010  -0.0599 47  ALA B O   
12290 C CB  . ALA B  21  ? 0.4917 0.5124 0.4924 -0.1201 0.0052  -0.0702 47  ALA B CB  
12296 N N   . GLU B  22  ? 0.4495 0.4808 0.4482 -0.1015 -0.0012 -0.0660 48  GLU B N   
12297 C CA  . GLU B  22  ? 0.4475 0.4774 0.4465 -0.0938 -0.0017 -0.0607 48  GLU B CA  
12298 C C   . GLU B  22  ? 0.4368 0.4512 0.4339 -0.0921 0.0026  -0.0577 48  GLU B C   
12299 O O   . GLU B  22  ? 0.4358 0.4418 0.4291 -0.0918 0.0046  -0.0606 48  GLU B O   
12300 C CB  . GLU B  22  ? 0.4942 0.5302 0.4911 -0.0893 -0.0045 -0.0628 48  GLU B CB  
12301 C CG  . GLU B  22  ? 0.5831 0.6347 0.5820 -0.0904 -0.0086 -0.0653 48  GLU B CG  
12302 C CD  . GLU B  22  ? 0.6978 0.7561 0.6949 -0.0853 -0.0114 -0.0663 48  GLU B CD  
12303 O OE1 . GLU B  22  ? 0.7187 0.7858 0.7185 -0.0812 -0.0139 -0.0634 48  GLU B OE1 
12304 O OE2 . GLU B  22  ? 0.7348 0.7891 0.7275 -0.0855 -0.0110 -0.0699 48  GLU B OE2 
12311 N N   . CYS B  23  ? 0.4240 0.4346 0.4236 -0.0912 0.0042  -0.0520 49  CYS B N   
12312 C CA  . CYS B  23  ? 0.4253 0.4219 0.4240 -0.0894 0.0084  -0.0482 49  CYS B CA  
12313 C C   . CYS B  23  ? 0.4059 0.4027 0.4068 -0.0831 0.0079  -0.0410 49  CYS B C   
12314 O O   . CYS B  23  ? 0.4053 0.3929 0.4067 -0.0819 0.0110  -0.0364 49  CYS B O   
12315 C CB  . CYS B  23  ? 0.4486 0.4387 0.4479 -0.0957 0.0114  -0.0483 49  CYS B CB  
12316 S SG  . CYS B  23  ? 0.5341 0.5053 0.5298 -0.0977 0.0174  -0.0500 49  CYS B SG  
12321 N N   . SER B  24  ? 0.3956 0.4026 0.3977 -0.0790 0.0042  -0.0398 50  SER B N   
12322 C CA  . SER B  24  ? 0.4041 0.4125 0.4084 -0.0737 0.0035  -0.0333 50  SER B CA  
12323 C C   . SER B  24  ? 0.4203 0.4217 0.4234 -0.0680 0.0049  -0.0309 50  SER B C   
12324 O O   . SER B  24  ? 0.4226 0.4213 0.4230 -0.0670 0.0055  -0.0349 50  SER B O   
12325 C CB  . SER B  24  ? 0.4024 0.4240 0.4084 -0.0721 -0.0007 -0.0332 50  SER B CB  
12326 O OG  . SER B  24  ? 0.4229 0.4485 0.4273 -0.0692 -0.0026 -0.0364 50  SER B OG  
12332 N N   . ASN B  25  ? 0.4259 0.4255 0.4311 -0.0642 0.0054  -0.0244 51  ASN B N   
12333 C CA  . ASN B  25  ? 0.4392 0.4344 0.4445 -0.0582 0.0065  -0.0209 51  ASN B CA  
12334 C C   . ASN B  25  ? 0.4486 0.4322 0.4513 -0.0574 0.0104  -0.0232 51  ASN B C   
12335 O O   . ASN B  25  ? 0.4587 0.4415 0.4597 -0.0538 0.0104  -0.0248 51  ASN B O   
12336 C CB  . ASN B  25  ? 0.4596 0.4641 0.4651 -0.0546 0.0029  -0.0217 51  ASN B CB  
12337 C CG  . ASN B  25  ? 0.5252 0.5277 0.5318 -0.0486 0.0034  -0.0172 51  ASN B CG  
12338 O OD1 . ASN B  25  ? 0.5495 0.5474 0.5581 -0.0466 0.0051  -0.0116 51  ASN B OD1 
12339 N ND2 . ASN B  25  ? 0.5383 0.5447 0.5438 -0.0454 0.0019  -0.0191 51  ASN B ND2 
12346 N N   . ARG B  26  ? 0.4459 0.4199 0.4479 -0.0606 0.0140  -0.0231 52  ARG B N   
12347 C CA  . ARG B  26  ? 0.4536 0.4150 0.4529 -0.0605 0.0185  -0.0256 52  ARG B CA  
12348 C C   . ARG B  26  ? 0.4545 0.4050 0.4555 -0.0584 0.0227  -0.0194 52  ARG B C   
12349 O O   . ARG B  26  ? 0.4599 0.3983 0.4587 -0.0595 0.0272  -0.0213 52  ARG B O   
12350 C CB  . ARG B  26  ? 0.4748 0.4337 0.4710 -0.0674 0.0193  -0.0328 52  ARG B CB  
12351 C CG  . ARG B  26  ? 0.5147 0.4839 0.5090 -0.0691 0.0155  -0.0389 52  ARG B CG  
12352 C CD  . ARG B  26  ? 0.5359 0.5079 0.5290 -0.0766 0.0147  -0.0446 52  ARG B CD  
12353 N NE  . ARG B  26  ? 0.5662 0.5514 0.5590 -0.0774 0.0101  -0.0486 52  ARG B NE  
12354 C CZ  . ARG B  26  ? 0.5945 0.5818 0.5837 -0.0782 0.0092  -0.0545 52  ARG B CZ  
12355 N NH1 . ARG B  26  ? 0.5994 0.5758 0.5845 -0.0788 0.0126  -0.0579 52  ARG B NH1 
12356 N NH2 . ARG B  26  ? 0.5947 0.5949 0.5843 -0.0783 0.0048  -0.0570 52  ARG B NH2 
12370 N N   . ARG B  27  ? 0.4469 0.4014 0.4515 -0.0554 0.0215  -0.0121 53  ARG B N   
12371 C CA  . ARG B  27  ? 0.4460 0.3916 0.4526 -0.0526 0.0252  -0.0053 53  ARG B CA  
12372 C C   . ARG B  27  ? 0.4527 0.3889 0.4584 -0.0576 0.0289  -0.0057 53  ARG B C   
12373 O O   . ARG B  27  ? 0.4567 0.3815 0.4629 -0.0556 0.0335  -0.0021 53  ARG B O   
12374 C CB  . ARG B  27  ? 0.4576 0.3952 0.4640 -0.0468 0.0285  -0.0041 53  ARG B CB  
12375 C CG  . ARG B  27  ? 0.4702 0.4165 0.4771 -0.0423 0.0253  -0.0044 53  ARG B CG  
12376 C CD  . ARG B  27  ? 0.4990 0.4376 0.5053 -0.0370 0.0289  -0.0041 53  ARG B CD  
12377 N NE  . ARG B  27  ? 0.5316 0.4600 0.5332 -0.0395 0.0326  -0.0109 53  ARG B NE  
12378 C CZ  . ARG B  27  ? 0.5509 0.4822 0.5484 -0.0422 0.0310  -0.0185 53  ARG B CZ  
12379 N NH1 . ARG B  27  ? 0.5282 0.4722 0.5261 -0.0424 0.0259  -0.0200 53  ARG B NH1 
12380 N NH2 . ARG B  27  ? 0.5567 0.4783 0.5497 -0.0448 0.0346  -0.0245 53  ARG B NH2 
12394 N N   . LEU B  28  ? 0.4527 0.3939 0.4576 -0.0639 0.0270  -0.0095 54  LEU B N   
12395 C CA  . LEU B  28  ? 0.4696 0.4025 0.4737 -0.0694 0.0304  -0.0102 54  LEU B CA  
12396 C C   . LEU B  28  ? 0.4818 0.4140 0.4887 -0.0681 0.0312  -0.0017 54  LEU B C   
12397 O O   . LEU B  28  ? 0.4798 0.4231 0.4887 -0.0674 0.0273  0.0016  54  LEU B O   
12398 C CB  . LEU B  28  ? 0.4694 0.4095 0.4722 -0.0765 0.0279  -0.0166 54  LEU B CB  
12399 C CG  . LEU B  28  ? 0.4890 0.4318 0.4889 -0.0783 0.0265  -0.0250 54  LEU B CG  
12400 C CD1 . LEU B  28  ? 0.4900 0.4430 0.4899 -0.0846 0.0233  -0.0301 54  LEU B CD1 
12401 C CD2 . LEU B  28  ? 0.5033 0.4317 0.4997 -0.0796 0.0314  -0.0292 54  LEU B CD2 
12413 N N   . GLN B  29  ? 0.4910 0.4103 0.4980 -0.0675 0.0363  0.0020  55  GLN B N   
12414 C CA  . GLN B  29  ? 0.5064 0.4239 0.5158 -0.0661 0.0376  0.0107  55  GLN B CA  
12415 C C   . GLN B  29  ? 0.5140 0.4311 0.5228 -0.0731 0.0383  0.0101  55  GLN B C   
12416 O O   . GLN B  29  ? 0.5146 0.4343 0.5250 -0.0729 0.0380  0.0167  55  GLN B O   
12417 C CB  . GLN B  29  ? 0.5430 0.4462 0.5530 -0.0614 0.0432  0.0157  55  GLN B CB  
12418 C CG  . GLN B  29  ? 0.6107 0.5152 0.6223 -0.0537 0.0427  0.0183  55  GLN B CG  
12419 C CD  . GLN B  29  ? 0.7015 0.5912 0.7135 -0.0491 0.0489  0.0215  55  GLN B CD  
12420 O OE1 . GLN B  29  ? 0.7454 0.6228 0.7565 -0.0512 0.0539  0.0227  55  GLN B OE1 
12421 N NE2 . GLN B  29  ? 0.7122 0.6026 0.7256 -0.0427 0.0491  0.0231  55  GLN B NE2 
12430 N N   . GLU B  30  ? 0.5177 0.4317 0.5241 -0.0794 0.0394  0.0022  56  GLU B N   
12431 C CA  . GLU B  30  ? 0.5282 0.4424 0.5342 -0.0868 0.0401  0.0006  56  GLU B CA  
12432 C C   . GLU B  30  ? 0.5118 0.4340 0.5164 -0.0924 0.0372  -0.0087 56  GLU B C   
12433 O O   . GLU B  30  ? 0.5023 0.4260 0.5054 -0.0909 0.0358  -0.0139 56  GLU B O   
12434 C CB  . GLU B  30  ? 0.5887 0.4859 0.5934 -0.0894 0.0467  0.0014  56  GLU B CB  
12435 C CG  . GLU B  30  ? 0.6993 0.5882 0.7057 -0.0838 0.0501  0.0111  56  GLU B CG  
12436 C CD  . GLU B  30  ? 0.8300 0.7088 0.8362 -0.0878 0.0547  0.0149  56  GLU B CD  
12437 O OE1 . GLU B  30  ? 0.8586 0.7444 0.8661 -0.0890 0.0530  0.0203  56  GLU B OE1 
12438 O OE2 . GLU B  30  ? 0.8745 0.7383 0.8789 -0.0898 0.0603  0.0125  56  GLU B OE2 
12445 N N   . VAL B  31  ? 0.5042 0.4315 0.5092 -0.0990 0.0365  -0.0106 57  VAL B N   
12446 C CA  . VAL B  31  ? 0.4994 0.4348 0.5037 -0.1048 0.0340  -0.0190 57  VAL B CA  
12447 C C   . VAL B  31  ? 0.5071 0.4302 0.5084 -0.1084 0.0378  -0.0254 57  VAL B C   
12448 O O   . VAL B  31  ? 0.5044 0.4142 0.5048 -0.1108 0.0429  -0.0237 57  VAL B O   
12449 C CB  . VAL B  31  ? 0.4990 0.4422 0.5050 -0.1110 0.0330  -0.0189 57  VAL B CB  
12450 C CG1 . VAL B  31  ? 0.4964 0.4475 0.5021 -0.1172 0.0309  -0.0276 57  VAL B CG1 
12451 C CG2 . VAL B  31  ? 0.4982 0.4533 0.5063 -0.1076 0.0293  -0.0133 57  VAL B CG2 
12461 N N   . PRO B  32  ? 0.5126 0.4390 0.5119 -0.1085 0.0359  -0.0324 58  PRO B N   
12462 C CA  . PRO B  32  ? 0.5278 0.4420 0.5235 -0.1120 0.0397  -0.0386 58  PRO B CA  
12463 C C   . PRO B  32  ? 0.5445 0.4562 0.5396 -0.1215 0.0417  -0.0433 58  PRO B C   
12464 O O   . PRO B  32  ? 0.5393 0.4639 0.5363 -0.1259 0.0381  -0.0458 58  PRO B O   
12465 C CB  . PRO B  32  ? 0.5325 0.4540 0.5261 -0.1102 0.0362  -0.0447 58  PRO B CB  
12466 C CG  . PRO B  32  ? 0.5300 0.4673 0.5265 -0.1063 0.0307  -0.0420 58  PRO B CG  
12467 C CD  . PRO B  32  ? 0.5011 0.4418 0.5010 -0.1053 0.0303  -0.0347 58  PRO B CD  
12475 N N   . GLN B  33  ? 0.5596 0.4546 0.5524 -0.1245 0.0475  -0.0444 59  GLN B N   
12476 C CA  . GLN B  33  ? 0.5799 0.4707 0.5719 -0.1341 0.0500  -0.0494 59  GLN B CA  
12477 C C   . GLN B  33  ? 0.5910 0.4820 0.5793 -0.1393 0.0494  -0.0596 59  GLN B C   
12478 O O   . GLN B  33  ? 0.6020 0.4849 0.5884 -0.1471 0.0528  -0.0646 59  GLN B O   
12479 C CB  . GLN B  33  ? 0.6129 0.4850 0.6041 -0.1353 0.0571  -0.0452 59  GLN B CB  
12480 C CG  . GLN B  33  ? 0.6732 0.5454 0.6677 -0.1305 0.0577  -0.0347 59  GLN B CG  
12481 C CD  . GLN B  33  ? 0.7425 0.6291 0.7403 -0.1344 0.0541  -0.0329 59  GLN B CD  
12482 O OE1 . GLN B  33  ? 0.7503 0.6500 0.7505 -0.1299 0.0496  -0.0287 59  GLN B OE1 
12483 N NE2 . GLN B  33  ? 0.7689 0.6536 0.7668 -0.1432 0.0562  -0.0362 59  GLN B NE2 
12492 N N   . THR B  34  ? 0.5902 0.4910 0.5774 -0.1354 0.0450  -0.0629 60  THR B N   
12493 C CA  . THR B  34  ? 0.5983 0.5012 0.5817 -0.1396 0.0437  -0.0722 60  THR B CA  
12494 C C   . THR B  34  ? 0.5926 0.5163 0.5779 -0.1401 0.0367  -0.0752 60  THR B C   
12495 O O   . THR B  34  ? 0.5913 0.5195 0.5735 -0.1402 0.0343  -0.0811 60  THR B O   
12496 C CB  . THR B  34  ? 0.6184 0.5096 0.5973 -0.1341 0.0464  -0.0736 60  THR B CB  
12497 O OG1 . THR B  34  ? 0.6265 0.5237 0.6073 -0.1246 0.0438  -0.0676 60  THR B OG1 
12498 C CG2 . THR B  34  ? 0.6306 0.5003 0.6071 -0.1346 0.0540  -0.0720 60  THR B CG2 
12506 N N   . VAL B  35  ? 0.5858 0.5222 0.5760 -0.1405 0.0335  -0.0712 61  VAL B N   
12507 C CA  . VAL B  35  ? 0.5845 0.5404 0.5770 -0.1409 0.0273  -0.0736 61  VAL B CA  
12508 C C   . VAL B  35  ? 0.5829 0.5437 0.5749 -0.1506 0.0267  -0.0815 61  VAL B C   
12509 O O   . VAL B  35  ? 0.5854 0.5379 0.5774 -0.1575 0.0305  -0.0827 61  VAL B O   
12510 C CB  . VAL B  35  ? 0.5913 0.5582 0.5890 -0.1381 0.0248  -0.0670 61  VAL B CB  
12511 C CG1 . VAL B  35  ? 0.5893 0.5758 0.5896 -0.1384 0.0190  -0.0697 61  VAL B CG1 
12512 C CG2 . VAL B  35  ? 0.5993 0.5615 0.5974 -0.1291 0.0253  -0.0594 61  VAL B CG2 
12522 N N   . GLY B  36  ? 0.5776 0.5517 0.5691 -0.1513 0.0221  -0.0866 62  GLY B N   
12523 C CA  . GLY B  36  ? 0.5802 0.5612 0.5713 -0.1604 0.0208  -0.0942 62  GLY B CA  
12524 C C   . GLY B  36  ? 0.5760 0.5663 0.5725 -0.1666 0.0201  -0.0933 62  GLY B C   
12525 O O   . GLY B  36  ? 0.5715 0.5718 0.5724 -0.1629 0.0178  -0.0880 62  GLY B O   
12529 N N   . LYS B  37  ? 0.5749 0.5616 0.5708 -0.1763 0.0224  -0.0985 63  LYS B N   
12530 C CA  . LYS B  37  ? 0.5748 0.5700 0.5757 -0.1837 0.0223  -0.0986 63  LYS B CA  
12531 C C   . LYS B  37  ? 0.5648 0.5829 0.5705 -0.1831 0.0163  -0.0991 63  LYS B C   
12532 O O   . LYS B  37  ? 0.5635 0.5904 0.5745 -0.1849 0.0159  -0.0960 63  LYS B O   
12533 C CB  . LYS B  37  ? 0.6054 0.5941 0.6040 -0.1948 0.0252  -0.1059 63  LYS B CB  
12534 C CG  . LYS B  37  ? 0.6649 0.6617 0.6605 -0.1985 0.0216  -0.1144 63  LYS B CG  
12535 C CD  . LYS B  37  ? 0.7345 0.7246 0.7274 -0.2101 0.0245  -0.1220 63  LYS B CD  
12536 C CE  . LYS B  37  ? 0.7842 0.7924 0.7824 -0.2185 0.0212  -0.1254 63  LYS B CE  
12537 N NZ  . LYS B  37  ? 0.8228 0.8253 0.8183 -0.2304 0.0236  -0.1334 63  LYS B NZ  
12551 N N   . TYR B  38  ? 0.5562 0.5840 0.5603 -0.1808 0.0121  -0.1032 64  TYR B N   
12552 C CA  . TYR B  38  ? 0.5463 0.5957 0.5547 -0.1796 0.0064  -0.1040 64  TYR B CA  
12553 C C   . TYR B  38  ? 0.5113 0.5676 0.5220 -0.1693 0.0038  -0.0975 64  TYR B C   
12554 O O   . TYR B  38  ? 0.5034 0.5769 0.5184 -0.1678 -0.0002 -0.0970 64  TYR B O   
12555 C CB  . TYR B  38  ? 0.5639 0.6213 0.5692 -0.1823 0.0029  -0.1113 64  TYR B CB  
12556 C CG  . TYR B  38  ? 0.6041 0.6500 0.6024 -0.1774 0.0036  -0.1129 64  TYR B CG  
12557 C CD1 . TYR B  38  ? 0.6242 0.6721 0.6217 -0.1673 0.0015  -0.1088 64  TYR B CD1 
12558 C CD2 . TYR B  38  ? 0.6328 0.6653 0.6252 -0.1830 0.0068  -0.1187 64  TYR B CD2 
12559 C CE1 . TYR B  38  ? 0.6473 0.6848 0.6386 -0.1627 0.0025  -0.1100 64  TYR B CE1 
12560 C CE2 . TYR B  38  ? 0.6567 0.6784 0.6425 -0.1784 0.0079  -0.1203 64  TYR B CE2 
12561 C CZ  . TYR B  38  ? 0.6696 0.6942 0.6551 -0.1682 0.0057  -0.1158 64  TYR B CZ  
12562 O OH  . TYR B  38  ? 0.7006 0.7150 0.6797 -0.1637 0.0070  -0.1173 64  TYR B OH  
12572 N N   . VAL B  39  ? 0.4840 0.5273 0.4921 -0.1624 0.0061  -0.0925 65  VAL B N   
12573 C CA  . VAL B  39  ? 0.4622 0.5109 0.4720 -0.1531 0.0039  -0.0865 65  VAL B CA  
12574 C C   . VAL B  39  ? 0.4310 0.4905 0.4467 -0.1535 0.0030  -0.0824 65  VAL B C   
12575 O O   . VAL B  39  ? 0.4283 0.4827 0.4457 -0.1583 0.0062  -0.0807 65  VAL B O   
12576 C CB  . VAL B  39  ? 0.4750 0.5072 0.4814 -0.1468 0.0071  -0.0817 65  VAL B CB  
12577 C CG1 . VAL B  39  ? 0.4754 0.5125 0.4842 -0.1387 0.0054  -0.0749 65  VAL B CG1 
12578 C CG2 . VAL B  39  ? 0.4825 0.5065 0.4833 -0.1444 0.0074  -0.0853 65  VAL B CG2 
12588 N N   . THR B  40  ? 0.4119 0.4861 0.4306 -0.1485 -0.0010 -0.0809 66  THR B N   
12589 C CA  . THR B  40  ? 0.3970 0.4823 0.4209 -0.1480 -0.0019 -0.0773 66  THR B CA  
12590 C C   . THR B  40  ? 0.3891 0.4732 0.4131 -0.1394 -0.0024 -0.0710 66  THR B C   
12591 O O   . THR B  40  ? 0.3930 0.4820 0.4202 -0.1391 -0.0019 -0.0673 66  THR B O   
12592 C CB  . THR B  40  ? 0.3971 0.5016 0.4251 -0.1496 -0.0059 -0.0808 66  THR B CB  
12593 O OG1 . THR B  40  ? 0.4021 0.5121 0.4286 -0.1428 -0.0094 -0.0813 66  THR B OG1 
12594 C CG2 . THR B  40  ? 0.4007 0.5088 0.4293 -0.1588 -0.0059 -0.0871 66  THR B CG2 
12602 N N   . GLU B  41  ? 0.3804 0.4589 0.4009 -0.1328 -0.0033 -0.0699 67  GLU B N   
12603 C CA  . GLU B  41  ? 0.3741 0.4514 0.3946 -0.1251 -0.0038 -0.0642 67  GLU B CA  
12604 C C   . GLU B  41  ? 0.3676 0.4293 0.3836 -0.1216 -0.0016 -0.0622 67  GLU B C   
12605 O O   . GLU B  41  ? 0.3699 0.4278 0.3828 -0.1208 -0.0021 -0.0656 67  GLU B O   
12606 C CB  . GLU B  41  ? 0.4029 0.4930 0.4247 -0.1196 -0.0079 -0.0646 67  GLU B CB  
12607 C CG  . GLU B  41  ? 0.4608 0.5671 0.4872 -0.1227 -0.0101 -0.0671 67  GLU B CG  
12608 C CD  . GLU B  41  ? 0.5462 0.6652 0.5747 -0.1168 -0.0136 -0.0664 67  GLU B CD  
12609 O OE1 . GLU B  41  ? 0.5603 0.6756 0.5865 -0.1101 -0.0144 -0.0641 67  GLU B OE1 
12610 O OE2 . GLU B  41  ? 0.5758 0.7085 0.6085 -0.1188 -0.0152 -0.0682 67  GLU B OE2 
12617 N N   . LEU B  42  ? 0.3568 0.4097 0.3726 -0.1199 0.0009  -0.0567 68  LEU B N   
12618 C CA  . LEU B  42  ? 0.3614 0.3998 0.3739 -0.1165 0.0035  -0.0540 68  LEU B CA  
12619 C C   . LEU B  42  ? 0.3590 0.3980 0.3717 -0.1090 0.0023  -0.0483 68  LEU B C   
12620 O O   . LEU B  42  ? 0.3523 0.3944 0.3670 -0.1084 0.0024  -0.0439 68  LEU B O   
12621 C CB  . LEU B  42  ? 0.3709 0.3975 0.3829 -0.1213 0.0079  -0.0522 68  LEU B CB  
12622 C CG  . LEU B  42  ? 0.3978 0.4084 0.4071 -0.1181 0.0115  -0.0486 68  LEU B CG  
12623 C CD1 . LEU B  42  ? 0.4085 0.4128 0.4142 -0.1157 0.0116  -0.0524 68  LEU B CD1 
12624 C CD2 . LEU B  42  ? 0.4124 0.4121 0.4213 -0.1240 0.0160  -0.0477 68  LEU B CD2 
12636 N N   . ASP B  43  ? 0.3545 0.3913 0.3651 -0.1035 0.0011  -0.0484 69  ASP B N   
12637 C CA  . ASP B  43  ? 0.3510 0.3882 0.3618 -0.0966 -0.0001 -0.0434 69  ASP B CA  
12638 C C   . ASP B  43  ? 0.3514 0.3750 0.3603 -0.0939 0.0030  -0.0398 69  ASP B C   
12639 O O   . ASP B  43  ? 0.3579 0.3753 0.3643 -0.0920 0.0038  -0.0420 69  ASP B O   
12640 C CB  . ASP B  43  ? 0.3640 0.4095 0.3744 -0.0920 -0.0035 -0.0455 69  ASP B CB  
12641 C CG  . ASP B  43  ? 0.4268 0.4741 0.4377 -0.0854 -0.0050 -0.0407 69  ASP B CG  
12642 O OD1 . ASP B  43  ? 0.4174 0.4596 0.4288 -0.0840 -0.0035 -0.0355 69  ASP B OD1 
12643 O OD2 . ASP B  43  ? 0.4753 0.5291 0.4861 -0.0817 -0.0076 -0.0420 69  ASP B OD2 
12648 N N   . LEU B  44  ? 0.3439 0.3630 0.3538 -0.0934 0.0048  -0.0341 70  LEU B N   
12649 C CA  . LEU B  44  ? 0.3510 0.3581 0.3598 -0.0901 0.0077  -0.0293 70  LEU B CA  
12650 C C   . LEU B  44  ? 0.3455 0.3556 0.3554 -0.0841 0.0060  -0.0233 70  LEU B C   
12651 O O   . LEU B  44  ? 0.3505 0.3530 0.3604 -0.0817 0.0081  -0.0178 70  LEU B O   
12652 C CB  . LEU B  44  ? 0.3610 0.3599 0.3700 -0.0945 0.0114  -0.0268 70  LEU B CB  
12653 C CG  . LEU B  44  ? 0.3875 0.3786 0.3949 -0.1002 0.0143  -0.0319 70  LEU B CG  
12654 C CD1 . LEU B  44  ? 0.3915 0.3787 0.3999 -0.1056 0.0171  -0.0298 70  LEU B CD1 
12655 C CD2 . LEU B  44  ? 0.3997 0.3774 0.4046 -0.0975 0.0175  -0.0321 70  LEU B CD2 
12667 N N   . SER B  45  ? 0.3370 0.3578 0.3477 -0.0816 0.0024  -0.0241 71  SER B N   
12668 C CA  . SER B  45  ? 0.3467 0.3710 0.3584 -0.0767 0.0007  -0.0190 71  SER B CA  
12669 C C   . SER B  45  ? 0.3624 0.3796 0.3733 -0.0713 0.0016  -0.0162 71  SER B C   
12670 O O   . SER B  45  ? 0.3608 0.3725 0.3702 -0.0705 0.0029  -0.0195 71  SER B O   
12671 C CB  . SER B  45  ? 0.3540 0.3902 0.3665 -0.0754 -0.0029 -0.0212 71  SER B CB  
12672 O OG  . SER B  45  ? 0.3879 0.4257 0.3993 -0.0730 -0.0043 -0.0252 71  SER B OG  
12678 N N   . ASP B  46  ? 0.3684 0.3863 0.3805 -0.0676 0.0010  -0.0103 72  ASP B N   
12679 C CA  . ASP B  46  ? 0.3894 0.4027 0.4016 -0.0621 0.0016  -0.0070 72  ASP B CA  
12680 C C   . ASP B  46  ? 0.4025 0.4034 0.4140 -0.0615 0.0056  -0.0062 72  ASP B C   
12681 O O   . ASP B  46  ? 0.4120 0.4088 0.4227 -0.0580 0.0065  -0.0072 72  ASP B O   
12682 C CB  . ASP B  46  ? 0.4194 0.4380 0.4311 -0.0589 -0.0008 -0.0102 72  ASP B CB  
12683 C CG  . ASP B  46  ? 0.5102 0.5399 0.5228 -0.0590 -0.0043 -0.0107 72  ASP B CG  
12684 O OD1 . ASP B  46  ? 0.5281 0.5609 0.5418 -0.0566 -0.0055 -0.0062 72  ASP B OD1 
12685 O OD2 . ASP B  46  ? 0.5645 0.5998 0.5766 -0.0614 -0.0056 -0.0156 72  ASP B OD2 
12690 N N   . ASN B  47  ? 0.3989 0.3937 0.4105 -0.0646 0.0083  -0.0042 73  ASN B N   
12691 C CA  . ASN B  47  ? 0.4099 0.3918 0.4207 -0.0640 0.0127  -0.0028 73  ASN B CA  
12692 C C   . ASN B  47  ? 0.4176 0.3962 0.4304 -0.0617 0.0141  0.0056  73  ASN B C   
12693 O O   . ASN B  47  ? 0.4094 0.3963 0.4237 -0.0604 0.0113  0.0097  73  ASN B O   
12694 C CB  . ASN B  47  ? 0.4202 0.3968 0.4292 -0.0701 0.0150  -0.0083 73  ASN B CB  
12695 C CG  . ASN B  47  ? 0.4504 0.4271 0.4571 -0.0711 0.0146  -0.0159 73  ASN B CG  
12696 O OD1 . ASN B  47  ? 0.4691 0.4405 0.4745 -0.0673 0.0158  -0.0167 73  ASN B OD1 
12697 N ND2 . ASN B  47  ? 0.4466 0.4298 0.4526 -0.0761 0.0127  -0.0214 73  ASN B ND2 
12704 N N   . PHE B  48  ? 0.4327 0.3995 0.4454 -0.0611 0.0186  0.0083  74  PHE B N   
12705 C CA  . PHE B  48  ? 0.4496 0.4131 0.4643 -0.0587 0.0202  0.0168  74  PHE B CA  
12706 C C   . PHE B  48  ? 0.4482 0.4063 0.4622 -0.0637 0.0229  0.0182  74  PHE B C   
12707 O O   . PHE B  48  ? 0.4557 0.4059 0.4706 -0.0619 0.0261  0.0243  74  PHE B O   
12708 C CB  . PHE B  48  ? 0.4664 0.4201 0.4820 -0.0531 0.0237  0.0201  74  PHE B CB  
12709 C CG  . PHE B  48  ? 0.4877 0.4451 0.5039 -0.0483 0.0220  0.0185  74  PHE B CG  
12710 C CD1 . PHE B  48  ? 0.5035 0.4731 0.5209 -0.0467 0.0173  0.0194  74  PHE B CD1 
12711 C CD2 . PHE B  48  ? 0.5122 0.4602 0.5277 -0.0450 0.0256  0.0170  74  PHE B CD2 
12712 C CE1 . PHE B  48  ? 0.5146 0.4873 0.5328 -0.0422 0.0161  0.0186  74  PHE B CE1 
12713 C CE2 . PHE B  48  ? 0.5239 0.4754 0.5401 -0.0403 0.0243  0.0163  74  PHE B CE2 
12714 C CZ  . PHE B  48  ? 0.5173 0.4812 0.5349 -0.0391 0.0195  0.0171  74  PHE B CZ  
12724 N N   . ILE B  49  ? 0.4393 0.4014 0.4519 -0.0697 0.0218  0.0129  75  ILE B N   
12725 C CA  . ILE B  49  ? 0.4425 0.4003 0.4546 -0.0751 0.0243  0.0139  75  ILE B CA  
12726 C C   . ILE B  49  ? 0.4464 0.4096 0.4597 -0.0742 0.0230  0.0217  75  ILE B C   
12727 O O   . ILE B  49  ? 0.4380 0.4129 0.4518 -0.0735 0.0189  0.0223  75  ILE B O   
12728 C CB  . ILE B  49  ? 0.4403 0.4033 0.4513 -0.0817 0.0230  0.0063  75  ILE B CB  
12729 C CG1 . ILE B  49  ? 0.4514 0.4097 0.4607 -0.0831 0.0240  -0.0016 75  ILE B CG1 
12730 C CG2 . ILE B  49  ? 0.4456 0.4046 0.4564 -0.0874 0.0258  0.0079  75  ILE B CG2 
12731 C CD1 . ILE B  49  ? 0.4628 0.4310 0.4716 -0.0875 0.0209  -0.0089 75  ILE B CD1 
12743 N N   . THR B  50  ? 0.4503 0.4046 0.4638 -0.0743 0.0268  0.0277  76  THR B N   
12744 C CA  . THR B  50  ? 0.4570 0.4155 0.4712 -0.0735 0.0260  0.0358  76  THR B CA  
12745 C C   . THR B  50  ? 0.4601 0.4174 0.4731 -0.0796 0.0278  0.0363  76  THR B C   
12746 O O   . THR B  50  ? 0.4651 0.4287 0.4779 -0.0801 0.0264  0.0416  76  THR B O   
12747 C CB  . THR B  50  ? 0.4780 0.4284 0.4937 -0.0677 0.0288  0.0439  76  THR B CB  
12748 O OG1 . THR B  50  ? 0.4955 0.4311 0.5107 -0.0687 0.0344  0.0429  76  THR B OG1 
12749 C CG2 . THR B  50  ? 0.4775 0.4314 0.4950 -0.0612 0.0266  0.0450  76  THR B CG2 
12757 N N   . HIS B  51  ? 0.4584 0.4077 0.4705 -0.0846 0.0311  0.0310  77  HIS B N   
12758 C CA  . HIS B  51  ? 0.4629 0.4102 0.4741 -0.0908 0.0334  0.0314  77  HIS B CA  
12759 C C   . HIS B  51  ? 0.4540 0.4035 0.4646 -0.0974 0.0333  0.0223  77  HIS B C   
12760 O O   . HIS B  51  ? 0.4551 0.3996 0.4653 -0.0979 0.0342  0.0161  77  HIS B O   
12761 C CB  . HIS B  51  ? 0.4892 0.4208 0.5001 -0.0906 0.0393  0.0362  77  HIS B CB  
12762 C CG  . HIS B  51  ? 0.5364 0.4661 0.5482 -0.0849 0.0400  0.0464  77  HIS B CG  
12763 N ND1 . HIS B  51  ? 0.5652 0.4924 0.5784 -0.0778 0.0398  0.0496  77  HIS B ND1 
12764 C CD2 . HIS B  51  ? 0.5549 0.4854 0.5664 -0.0854 0.0409  0.0542  77  HIS B CD2 
12765 C CE1 . HIS B  51  ? 0.5738 0.5010 0.5879 -0.0742 0.0403  0.0592  77  HIS B CE1 
12766 N NE2 . HIS B  51  ? 0.5739 0.5030 0.5868 -0.0786 0.0409  0.0623  77  HIS B NE2 
12774 N N   . ILE B  52  ? 0.4424 0.3991 0.4529 -0.1026 0.0325  0.0218  78  ILE B N   
12775 C CA  . ILE B  52  ? 0.4376 0.3973 0.4482 -0.1096 0.0328  0.0142  78  ILE B CA  
12776 C C   . ILE B  52  ? 0.4464 0.4009 0.4567 -0.1150 0.0366  0.0175  78  ILE B C   
12777 O O   . ILE B  52  ? 0.4416 0.4009 0.4516 -0.1147 0.0361  0.0235  78  ILE B O   
12778 C CB  . ILE B  52  ? 0.4258 0.4017 0.4372 -0.1107 0.0279  0.0100  78  ILE B CB  
12779 C CG1 . ILE B  52  ? 0.4300 0.4116 0.4417 -0.1049 0.0239  0.0077  78  ILE B CG1 
12780 C CG2 . ILE B  52  ? 0.4231 0.4025 0.4353 -0.1179 0.0283  0.0025  78  ILE B CG2 
12781 C CD1 . ILE B  52  ? 0.4462 0.4219 0.4575 -0.1043 0.0245  0.0017  78  ILE B CD1 
12793 N N   . THR B  53  ? 0.4545 0.3990 0.4645 -0.1202 0.0406  0.0136  79  THR B N   
12794 C CA  . THR B  53  ? 0.4738 0.4121 0.4835 -0.1260 0.0448  0.0161  79  THR B CA  
12795 C C   . THR B  53  ? 0.4810 0.4230 0.4915 -0.1344 0.0452  0.0078  79  THR B C   
12796 O O   . THR B  53  ? 0.4759 0.4249 0.4871 -0.1351 0.0422  0.0006  79  THR B O   
12797 C CB  . THR B  53  ? 0.5015 0.4214 0.5101 -0.1243 0.0504  0.0206  79  THR B CB  
12798 O OG1 . THR B  53  ? 0.5163 0.4270 0.5243 -0.1267 0.0527  0.0134  79  THR B OG1 
12799 C CG2 . THR B  53  ? 0.5039 0.4212 0.5124 -0.1156 0.0498  0.0284  79  THR B CG2 
12807 N N   . ASN B  54  ? 0.4918 0.4297 0.5025 -0.1409 0.0490  0.0091  80  ASN B N   
12808 C CA  . ASN B  54  ? 0.5047 0.4457 0.5165 -0.1494 0.0497  0.0016  80  ASN B CA  
12809 C C   . ASN B  54  ? 0.5116 0.4418 0.5226 -0.1522 0.0520  -0.0054 80  ASN B C   
12810 O O   . ASN B  54  ? 0.5149 0.4489 0.5269 -0.1591 0.0519  -0.0126 80  ASN B O   
12811 C CB  . ASN B  54  ? 0.5340 0.4735 0.5464 -0.1558 0.0534  0.0050  80  ASN B CB  
12812 C CG  . ASN B  54  ? 0.6042 0.5258 0.6149 -0.1567 0.0595  0.0105  80  ASN B CG  
12813 O OD1 . ASN B  54  ? 0.6320 0.5407 0.6412 -0.1524 0.0617  0.0120  80  ASN B OD1 
12814 N ND2 . ASN B  54  ? 0.6219 0.5421 0.6329 -0.1621 0.0628  0.0139  80  ASN B ND2 
12821 N N   . GLU B  55  ? 0.5083 0.4258 0.5174 -0.1468 0.0540  -0.0035 81  GLU B N   
12822 C CA  . GLU B  55  ? 0.5113 0.4179 0.5188 -0.1485 0.0562  -0.0101 81  GLU B CA  
12823 C C   . GLU B  55  ? 0.4981 0.4113 0.5051 -0.1432 0.0517  -0.0146 81  GLU B C   
12824 O O   . GLU B  55  ? 0.4993 0.4056 0.5045 -0.1447 0.0529  -0.0209 81  GLU B O   
12825 C CB  . GLU B  55  ? 0.5545 0.4413 0.5601 -0.1461 0.0622  -0.0052 81  GLU B CB  
12826 C CG  . GLU B  55  ? 0.6447 0.5228 0.6503 -0.1516 0.0674  -0.0009 81  GLU B CG  
12827 C CD  . GLU B  55  ? 0.7757 0.6327 0.7795 -0.1501 0.0741  0.0027  81  GLU B CD  
12828 O OE1 . GLU B  55  ? 0.8080 0.6546 0.8112 -0.1566 0.0792  0.0028  81  GLU B OE1 
12829 O OE2 . GLU B  55  ? 0.8138 0.6643 0.8166 -0.1424 0.0745  0.0055  81  GLU B OE2 
12836 N N   . SER B  56  ? 0.4865 0.4125 0.4947 -0.1373 0.0468  -0.0117 82  SER B N   
12837 C CA  . SER B  56  ? 0.4836 0.4158 0.4914 -0.1321 0.0427  -0.0153 82  SER B CA  
12838 C C   . SER B  56  ? 0.4872 0.4283 0.4952 -0.1369 0.0399  -0.0248 82  SER B C   
12839 O O   . SER B  56  ? 0.4860 0.4240 0.4923 -0.1353 0.0393  -0.0296 82  SER B O   
12840 C CB  . SER B  56  ? 0.4829 0.4272 0.4921 -0.1257 0.0383  -0.0101 82  SER B CB  
12841 O OG  . SER B  56  ? 0.5032 0.4403 0.5121 -0.1204 0.0402  -0.0014 82  SER B OG  
12847 N N   . PHE B  57  ? 0.4897 0.4424 0.4999 -0.1426 0.0380  -0.0272 83  PHE B N   
12848 C CA  . PHE B  57  ? 0.5019 0.4650 0.5129 -0.1473 0.0351  -0.0356 83  PHE B CA  
12849 C C   . PHE B  57  ? 0.5279 0.4869 0.5394 -0.1570 0.0384  -0.0399 83  PHE B C   
12850 O O   . PHE B  57  ? 0.5293 0.5005 0.5431 -0.1623 0.0361  -0.0447 83  PHE B O   
12851 C CB  . PHE B  57  ? 0.4867 0.4684 0.5007 -0.1456 0.0301  -0.0352 83  PHE B CB  
12852 C CG  . PHE B  57  ? 0.4901 0.4756 0.5036 -0.1366 0.0270  -0.0311 83  PHE B CG  
12853 C CD1 . PHE B  57  ? 0.4936 0.4805 0.5058 -0.1323 0.0244  -0.0347 83  PHE B CD1 
12854 C CD2 . PHE B  57  ? 0.4965 0.4836 0.5105 -0.1327 0.0269  -0.0237 83  PHE B CD2 
12855 C CE1 . PHE B  57  ? 0.5012 0.4910 0.5130 -0.1244 0.0219  -0.0308 83  PHE B CE1 
12856 C CE2 . PHE B  57  ? 0.5008 0.4912 0.5144 -0.1251 0.0241  -0.0201 83  PHE B CE2 
12857 C CZ  . PHE B  57  ? 0.4961 0.4877 0.5088 -0.1210 0.0217  -0.0237 83  PHE B CZ  
12867 N N   . GLN B  58  ? 0.5465 0.4883 0.5559 -0.1594 0.0439  -0.0384 84  GLN B N   
12868 C CA  . GLN B  58  ? 0.5660 0.5015 0.5755 -0.1689 0.0478  -0.0421 84  GLN B CA  
12869 C C   . GLN B  58  ? 0.5725 0.5109 0.5810 -0.1743 0.0463  -0.0521 84  GLN B C   
12870 O O   . GLN B  58  ? 0.5795 0.5131 0.5851 -0.1707 0.0456  -0.0553 84  GLN B O   
12871 C CB  . GLN B  58  ? 0.6070 0.5213 0.6140 -0.1691 0.0544  -0.0380 84  GLN B CB  
12872 C CG  . GLN B  58  ? 0.6691 0.5781 0.6773 -0.1761 0.0589  -0.0351 84  GLN B CG  
12873 C CD  . GLN B  58  ? 0.7503 0.6372 0.7557 -0.1772 0.0659  -0.0325 84  GLN B CD  
12874 O OE1 . GLN B  58  ? 0.7739 0.6526 0.7790 -0.1855 0.0701  -0.0356 84  GLN B OE1 
12875 N NE2 . GLN B  58  ? 0.7647 0.6413 0.7684 -0.1688 0.0675  -0.0267 84  GLN B NE2 
12884 N N   . GLY B  59  ? 0.5662 0.5134 0.5772 -0.1828 0.0457  -0.0567 85  GLY B N   
12885 C CA  . GLY B  59  ? 0.5684 0.5205 0.5787 -0.1889 0.0439  -0.0661 85  GLY B CA  
12886 C C   . GLY B  59  ? 0.5610 0.5296 0.5722 -0.1848 0.0375  -0.0697 85  GLY B C   
12887 O O   . GLY B  59  ? 0.5663 0.5376 0.5759 -0.1882 0.0358  -0.0771 85  GLY B O   
12891 N N   . LEU B  60  ? 0.5433 0.5230 0.5568 -0.1777 0.0339  -0.0646 86  LEU B N   
12892 C CA  . LEU B  60  ? 0.5334 0.5285 0.5480 -0.1731 0.0281  -0.0671 86  LEU B CA  
12893 C C   . LEU B  60  ? 0.5202 0.5338 0.5400 -0.1751 0.0250  -0.0664 86  LEU B C   
12894 O O   . LEU B  60  ? 0.5125 0.5358 0.5339 -0.1687 0.0219  -0.0628 86  LEU B O   
12895 C CB  . LEU B  60  ? 0.5369 0.5290 0.5496 -0.1626 0.0267  -0.0621 86  LEU B CB  
12896 C CG  . LEU B  60  ? 0.5638 0.5385 0.5719 -0.1590 0.0298  -0.0617 86  LEU B CG  
12897 C CD1 . LEU B  60  ? 0.5671 0.5421 0.5746 -0.1489 0.0279  -0.0563 86  LEU B CD1 
12898 C CD2 . LEU B  60  ? 0.5785 0.5516 0.5835 -0.1621 0.0291  -0.0700 86  LEU B CD2 
12910 N N   . GLN B  61  ? 0.5132 0.5316 0.5356 -0.1841 0.0261  -0.0701 87  GLN B N   
12911 C CA  . GLN B  61  ? 0.5081 0.5438 0.5358 -0.1868 0.0239  -0.0696 87  GLN B CA  
12912 C C   . GLN B  61  ? 0.4903 0.5446 0.5207 -0.1836 0.0182  -0.0728 87  GLN B C   
12913 O O   . GLN B  61  ? 0.4915 0.5596 0.5261 -0.1826 0.0164  -0.0708 87  GLN B O   
12914 C CB  . GLN B  61  ? 0.5410 0.5772 0.5711 -0.1977 0.0267  -0.0731 87  GLN B CB  
12915 C CG  . GLN B  61  ? 0.6100 0.6296 0.6386 -0.2012 0.0327  -0.0688 87  GLN B CG  
12916 C CD  . GLN B  61  ? 0.6817 0.7025 0.7114 -0.1961 0.0336  -0.0605 87  GLN B CD  
12917 O OE1 . GLN B  61  ? 0.7007 0.7370 0.7343 -0.1951 0.0311  -0.0591 87  GLN B OE1 
12918 N NE2 . GLN B  61  ? 0.7024 0.7073 0.7287 -0.1923 0.0371  -0.0547 87  GLN B NE2 
12927 N N   . ASN B  62  ? 0.4763 0.5311 0.5042 -0.1819 0.0156  -0.0776 88  ASN B N   
12928 C CA  . ASN B  62  ? 0.4640 0.5359 0.4941 -0.1783 0.0103  -0.0802 88  ASN B CA  
12929 C C   . ASN B  62  ? 0.4234 0.4987 0.4533 -0.1680 0.0080  -0.0748 88  ASN B C   
12930 O O   . ASN B  62  ? 0.4118 0.5014 0.4441 -0.1644 0.0040  -0.0759 88  ASN B O   
12931 C CB  . ASN B  62  ? 0.5110 0.5824 0.5377 -0.1798 0.0082  -0.0869 88  ASN B CB  
12932 C CG  . ASN B  62  ? 0.6039 0.6810 0.6323 -0.1898 0.0082  -0.0932 88  ASN B CG  
12933 O OD1 . ASN B  62  ? 0.6178 0.7128 0.6513 -0.1920 0.0051  -0.0949 88  ASN B OD1 
12934 N ND2 . ASN B  62  ? 0.6584 0.7229 0.6828 -0.1960 0.0110  -0.0977 88  ASN B ND2 
12941 N N   . LEU B  63  ? 0.3984 0.4610 0.4257 -0.1633 0.0106  -0.0691 89  LEU B N   
12942 C CA  . LEU B  63  ? 0.3788 0.4442 0.4058 -0.1542 0.0085  -0.0643 89  LEU B CA  
12943 C C   . LEU B  63  ? 0.3535 0.4334 0.3849 -0.1530 0.0067  -0.0617 89  LEU B C   
12944 O O   . LEU B  63  ? 0.3508 0.4304 0.3840 -0.1563 0.0092  -0.0587 89  LEU B O   
12945 C CB  . LEU B  63  ? 0.3855 0.4354 0.4092 -0.1501 0.0115  -0.0583 89  LEU B CB  
12946 C CG  . LEU B  63  ? 0.4082 0.4430 0.4274 -0.1483 0.0133  -0.0595 89  LEU B CG  
12947 C CD1 . LEU B  63  ? 0.4171 0.4382 0.4342 -0.1444 0.0166  -0.0527 89  LEU B CD1 
12948 C CD2 . LEU B  63  ? 0.4071 0.4462 0.4246 -0.1425 0.0098  -0.0620 89  LEU B CD2 
12960 N N   . THR B  64  ? 0.3337 0.4257 0.3666 -0.1479 0.0028  -0.0627 90  THR B N   
12961 C CA  . THR B  64  ? 0.3273 0.4328 0.3640 -0.1451 0.0011  -0.0603 90  THR B CA  
12962 C C   . THR B  64  ? 0.3191 0.4215 0.3535 -0.1366 0.0002  -0.0554 90  THR B C   
12963 O O   . THR B  64  ? 0.3130 0.4231 0.3495 -0.1342 -0.0003 -0.0527 90  THR B O   
12964 C CB  . THR B  64  ? 0.3446 0.4665 0.3849 -0.1455 -0.0025 -0.0648 90  THR B CB  
12965 O OG1 . THR B  64  ? 0.3645 0.4868 0.4025 -0.1396 -0.0054 -0.0662 90  THR B OG1 
12966 C CG2 . THR B  64  ? 0.3509 0.4770 0.3934 -0.1541 -0.0021 -0.0700 90  THR B CG2 
12974 N N   . LYS B  65  ? 0.3089 0.4009 0.3393 -0.1322 -0.0001 -0.0546 91  LYS B N   
12975 C CA  . LYS B  65  ? 0.3072 0.3967 0.3358 -0.1246 -0.0011 -0.0502 91  LYS B CA  
12976 C C   . LYS B  65  ? 0.2976 0.3715 0.3222 -0.1224 0.0009  -0.0476 91  LYS B C   
12977 O O   . LYS B  65  ? 0.2998 0.3669 0.3224 -0.1238 0.0014  -0.0508 91  LYS B O   
12978 C CB  . LYS B  65  ? 0.3254 0.4243 0.3546 -0.1193 -0.0049 -0.0525 91  LYS B CB  
12979 C CG  . LYS B  65  ? 0.3886 0.4843 0.4156 -0.1116 -0.0060 -0.0486 91  LYS B CG  
12980 C CD  . LYS B  65  ? 0.4489 0.5548 0.4770 -0.1068 -0.0094 -0.0505 91  LYS B CD  
12981 C CE  . LYS B  65  ? 0.5057 0.6078 0.5316 -0.0997 -0.0104 -0.0471 91  LYS B CE  
12982 N NZ  . LYS B  65  ? 0.5416 0.6512 0.5678 -0.0952 -0.0133 -0.0492 91  LYS B NZ  
12996 N N   . ILE B  66  ? 0.2810 0.3497 0.3044 -0.1189 0.0019  -0.0418 92  ILE B N   
12997 C CA  . ILE B  66  ? 0.2816 0.3369 0.3020 -0.1157 0.0037  -0.0383 92  ILE B CA  
12998 C C   . ILE B  66  ? 0.2778 0.3354 0.2975 -0.1087 0.0017  -0.0342 92  ILE B C   
12999 O O   . ILE B  66  ? 0.2761 0.3400 0.2970 -0.1081 0.0011  -0.0313 92  ILE B O   
13000 C CB  . ILE B  66  ? 0.2855 0.3301 0.3050 -0.1193 0.0077  -0.0345 92  ILE B CB  
13001 C CG1 . ILE B  66  ? 0.2932 0.3326 0.3128 -0.1264 0.0102  -0.0388 92  ILE B CG1 
13002 C CG2 . ILE B  66  ? 0.2984 0.3310 0.3153 -0.1142 0.0091  -0.0294 92  ILE B CG2 
13003 C CD1 . ILE B  66  ? 0.3121 0.3443 0.3318 -0.1313 0.0141  -0.0356 92  ILE B CD1 
13015 N N   . ASN B  67  ? 0.2740 0.3261 0.2917 -0.1038 0.0009  -0.0339 93  ASN B N   
13016 C CA  . ASN B  67  ? 0.2763 0.3295 0.2934 -0.0975 -0.0008 -0.0298 93  ASN B CA  
13017 C C   . ASN B  67  ? 0.2938 0.3345 0.3090 -0.0951 0.0015  -0.0252 93  ASN B C   
13018 O O   . ASN B  67  ? 0.3055 0.3384 0.3193 -0.0940 0.0026  -0.0267 93  ASN B O   
13019 C CB  . ASN B  67  ? 0.2782 0.3377 0.2953 -0.0933 -0.0038 -0.0331 93  ASN B CB  
13020 C CG  . ASN B  67  ? 0.2996 0.3594 0.3160 -0.0871 -0.0053 -0.0293 93  ASN B CG  
13021 O OD1 . ASN B  67  ? 0.3040 0.3587 0.3197 -0.0855 -0.0043 -0.0242 93  ASN B OD1 
13022 N ND2 . ASN B  67  ? 0.3070 0.3729 0.3235 -0.0835 -0.0078 -0.0316 93  ASN B ND2 
13029 N N   . LEU B  68  ? 0.2968 0.3360 0.3121 -0.0944 0.0024  -0.0195 94  LEU B N   
13030 C CA  . LEU B  68  ? 0.3027 0.3315 0.3168 -0.0917 0.0045  -0.0140 94  LEU B CA  
13031 C C   . LEU B  68  ? 0.2995 0.3318 0.3135 -0.0863 0.0023  -0.0093 94  LEU B C   
13032 O O   . LEU B  68  ? 0.3021 0.3290 0.3157 -0.0843 0.0035  -0.0036 94  LEU B O   
13033 C CB  . LEU B  68  ? 0.3149 0.3382 0.3289 -0.0960 0.0076  -0.0105 94  LEU B CB  
13034 C CG  . LEU B  68  ? 0.3360 0.3495 0.3495 -0.1005 0.0111  -0.0132 94  LEU B CG  
13035 C CD1 . LEU B  68  ? 0.3456 0.3578 0.3596 -0.1060 0.0137  -0.0112 94  LEU B CD1 
13036 C CD2 . LEU B  68  ? 0.3491 0.3498 0.3613 -0.0969 0.0136  -0.0106 94  LEU B CD2 
13048 N N   . ASN B  69  ? 0.2932 0.3341 0.3076 -0.0836 -0.0008 -0.0118 95  ASN B N   
13049 C CA  . ASN B  69  ? 0.2990 0.3435 0.3133 -0.0790 -0.0029 -0.0081 95  ASN B CA  
13050 C C   . ASN B  69  ? 0.3181 0.3551 0.3320 -0.0746 -0.0023 -0.0045 95  ASN B C   
13051 O O   . ASN B  69  ? 0.3101 0.3407 0.3236 -0.0736 -0.0010 -0.0067 95  ASN B O   
13052 C CB  . ASN B  69  ? 0.2952 0.3485 0.3099 -0.0769 -0.0058 -0.0121 95  ASN B CB  
13053 C CG  . ASN B  69  ? 0.3109 0.3736 0.3265 -0.0799 -0.0068 -0.0151 95  ASN B CG  
13054 O OD1 . ASN B  69  ? 0.3317 0.4013 0.3481 -0.0785 -0.0087 -0.0187 95  ASN B OD1 
13055 N ND2 . ASN B  69  ? 0.2821 0.3454 0.2980 -0.0842 -0.0053 -0.0139 95  ASN B ND2 
13062 N N   . HIS B  70  ? 0.3376 0.3759 0.3516 -0.0718 -0.0032 0.0010  96  HIS B N   
13063 C CA  . HIS B  70  ? 0.3683 0.4016 0.3826 -0.0671 -0.0030 0.0050  96  HIS B CA  
13064 C C   . HIS B  70  ? 0.3882 0.4104 0.4026 -0.0671 0.0005  0.0070  96  HIS B C   
13065 O O   . HIS B  70  ? 0.3864 0.4028 0.4008 -0.0646 0.0017  0.0055  96  HIS B O   
13066 C CB  . HIS B  70  ? 0.3935 0.4293 0.4080 -0.0634 -0.0048 0.0016  96  HIS B CB  
13067 C CG  . HIS B  70  ? 0.4469 0.4922 0.4613 -0.0639 -0.0075 -0.0022 96  HIS B CG  
13068 N ND1 . HIS B  70  ? 0.4751 0.5270 0.4895 -0.0633 -0.0095 0.0001  96  HIS B ND1 
13069 C CD2 . HIS B  70  ? 0.4722 0.5211 0.4865 -0.0646 -0.0084 -0.0080 96  HIS B CD2 
13070 C CE1 . HIS B  70  ? 0.4808 0.5393 0.4951 -0.0636 -0.0111 -0.0043 96  HIS B CE1 
13071 N NE2 . HIS B  70  ? 0.4851 0.5425 0.4995 -0.0641 -0.0106 -0.0090 96  HIS B NE2 
13079 N N   . ASN B  71  ? 0.4045 0.4234 0.4187 -0.0699 0.0025  0.0105  97  ASN B N   
13080 C CA  . ASN B  71  ? 0.4332 0.4409 0.4475 -0.0703 0.0063  0.0132  97  ASN B CA  
13081 C C   . ASN B  71  ? 0.4749 0.4813 0.4894 -0.0698 0.0072  0.0211  97  ASN B C   
13082 O O   . ASN B  71  ? 0.4811 0.4925 0.4949 -0.0733 0.0065  0.0221  97  ASN B O   
13083 C CB  . ASN B  71  ? 0.4324 0.4364 0.4458 -0.0759 0.0086  0.0083  97  ASN B CB  
13084 C CG  . ASN B  71  ? 0.4449 0.4438 0.4576 -0.0762 0.0097  0.0021  97  ASN B CG  
13085 O OD1 . ASN B  71  ? 0.4500 0.4545 0.4623 -0.0786 0.0081  -0.0041 97  ASN B OD1 
13086 N ND2 . ASN B  71  ? 0.4353 0.4240 0.4478 -0.0734 0.0125  0.0040  97  ASN B ND2 
13093 N N   . PRO B  72  ? 0.5045 0.5046 0.5201 -0.0656 0.0088  0.0270  98  PRO B N   
13094 C CA  . PRO B  72  ? 0.5333 0.5269 0.5500 -0.0609 0.0103  0.0270  98  PRO B CA  
13095 C C   . PRO B  72  ? 0.5648 0.5659 0.5824 -0.0571 0.0069  0.0258  98  PRO B C   
13096 O O   . PRO B  72  ? 0.5706 0.5814 0.5880 -0.0578 0.0034  0.0257  98  PRO B O   
13097 C CB  . PRO B  72  ? 0.5397 0.5264 0.5578 -0.0579 0.0130  0.0352  98  PRO B CB  
13098 C CG  . PRO B  72  ? 0.5366 0.5253 0.5538 -0.0616 0.0132  0.0392  98  PRO B CG  
13099 C CD  . PRO B  72  ? 0.5047 0.5046 0.5207 -0.0650 0.0094  0.0351  98  PRO B CD  
13107 N N   . ASN B  73  ? 0.5877 0.5836 0.6061 -0.0530 0.0082  0.0250  99  ASN B N   
13108 C CA  . ASN B  73  ? 0.6111 0.6126 0.6304 -0.0491 0.0056  0.0240  99  ASN B CA  
13109 C C   . ASN B  73  ? 0.6221 0.6296 0.6398 -0.0513 0.0032  0.0166  99  ASN B C   
13110 O O   . ASN B  73  ? 0.6287 0.6323 0.6452 -0.0512 0.0043  0.0113  99  ASN B O   
13111 C CB  . ASN B  73  ? 0.6350 0.6442 0.6561 -0.0467 0.0029  0.0303  99  ASN B CB  
13112 C CG  . ASN B  73  ? 0.7006 0.7056 0.7238 -0.0442 0.0049  0.0384  99  ASN B CG  
13113 O OD1 . ASN B  73  ? 0.7284 0.7234 0.7521 -0.0427 0.0088  0.0397  99  ASN B OD1 
13114 N ND2 . ASN B  73  ? 0.7083 0.7207 0.7325 -0.0436 0.0024  0.0440  99  ASN B ND2 
13121 N N   . GLY B  87  ? 0.5295 0.5387 0.5448 -0.0638 0.0079  0.0590  113 GLY B N   
13122 C CA  . GLY B  87  ? 0.5287 0.5413 0.5421 -0.0688 0.0072  0.0512  113 GLY B CA  
13123 C C   . GLY B  87  ? 0.5255 0.5288 0.5384 -0.0724 0.0112  0.0478  113 GLY B C   
13124 O O   . GLY B  87  ? 0.5334 0.5269 0.5470 -0.0716 0.0149  0.0519  113 GLY B O   
13127 N N   . LEU B  88  ? 0.5121 0.5185 0.5242 -0.0766 0.0107  0.0402  114 LEU B N   
13128 C CA  . LEU B  88  ? 0.5100 0.5092 0.5219 -0.0810 0.0140  0.0360  114 LEU B CA  
13129 C C   . LEU B  88  ? 0.5119 0.5100 0.5225 -0.0851 0.0162  0.0402  114 LEU B C   
13130 O O   . LEU B  88  ? 0.5094 0.5165 0.5186 -0.0872 0.0142  0.0411  114 LEU B O   
13131 C CB  . LEU B  88  ? 0.5033 0.5088 0.5151 -0.0841 0.0122  0.0272  114 LEU B CB  
13132 C CG  . LEU B  88  ? 0.5146 0.5144 0.5264 -0.0891 0.0151  0.0216  114 LEU B CG  
13133 C CD1 . LEU B  88  ? 0.5214 0.5090 0.5336 -0.0872 0.0181  0.0205  114 LEU B CD1 
13134 C CD2 . LEU B  88  ? 0.5194 0.5281 0.5315 -0.0916 0.0125  0.0138  114 LEU B CD2 
13146 N N   . ASN B  89  ? 0.5097 0.4964 0.5204 -0.0863 0.0206  0.0425  115 ASN B N   
13147 C CA  . ASN B  89  ? 0.5141 0.4983 0.5235 -0.0903 0.0232  0.0468  115 ASN B CA  
13148 C C   . ASN B  89  ? 0.4917 0.4725 0.5011 -0.0967 0.0257  0.0401  115 ASN B C   
13149 O O   . ASN B  89  ? 0.4898 0.4604 0.4998 -0.0975 0.0287  0.0369  115 ASN B O   
13150 C CB  . ASN B  89  ? 0.5646 0.5390 0.5743 -0.0868 0.0264  0.0557  115 ASN B CB  
13151 C CG  . ASN B  89  ? 0.6722 0.6379 0.6810 -0.0907 0.0310  0.0589  115 ASN B CG  
13152 O OD1 . ASN B  89  ? 0.6785 0.6477 0.6861 -0.0965 0.0315  0.0563  115 ASN B OD1 
13153 N ND2 . ASN B  89  ? 0.7544 0.7094 0.7637 -0.0876 0.0346  0.0658  115 ASN B ND2 
13160 N N   . ILE B  90  ? 0.4703 0.4602 0.4789 -0.1013 0.0244  0.0376  116 ILE B N   
13161 C CA  . ILE B  90  ? 0.4615 0.4512 0.4705 -0.1079 0.0262  0.0314  116 ILE B CA  
13162 C C   . ILE B  90  ? 0.4636 0.4506 0.4715 -0.1122 0.0295  0.0363  116 ILE B C   
13163 O O   . ILE B  90  ? 0.4645 0.4592 0.4709 -0.1122 0.0280  0.0405  116 ILE B O   
13164 C CB  . ILE B  90  ? 0.4506 0.4537 0.4602 -0.1095 0.0225  0.0250  116 ILE B CB  
13165 C CG1 . ILE B  90  ? 0.4522 0.4586 0.4627 -0.1046 0.0190  0.0212  116 ILE B CG1 
13166 C CG2 . ILE B  90  ? 0.4551 0.4593 0.4659 -0.1163 0.0242  0.0186  116 ILE B CG2 
13167 C CD1 . ILE B  90  ? 0.4552 0.4742 0.4663 -0.1051 0.0154  0.0156  116 ILE B CD1 
13179 N N   . THR B  91  ? 0.4598 0.4360 0.4681 -0.1161 0.0340  0.0356  117 THR B N   
13180 C CA  . THR B  91  ? 0.4591 0.4316 0.4663 -0.1205 0.0376  0.0402  117 THR B CA  
13181 C C   . THR B  91  ? 0.4504 0.4332 0.4579 -0.1268 0.0369  0.0356  117 THR B C   
13182 O O   . THR B  91  ? 0.4441 0.4340 0.4532 -0.1285 0.0346  0.0280  117 THR B O   
13183 C CB  . THR B  91  ? 0.4857 0.4423 0.4932 -0.1229 0.0430  0.0405  117 THR B CB  
13184 O OG1 . THR B  91  ? 0.5093 0.4649 0.5182 -0.1269 0.0431  0.0312  117 THR B OG1 
13185 C CG2 . THR B  91  ? 0.4908 0.4363 0.4981 -0.1164 0.0445  0.0460  117 THR B CG2 
13193 N N   . ASP B  92  ? 0.4449 0.4287 0.4511 -0.1301 0.0391  0.0406  118 ASP B N   
13194 C CA  . ASP B  92  ? 0.4425 0.4357 0.4491 -0.1362 0.0393  0.0373  118 ASP B CA  
13195 C C   . ASP B  92  ? 0.4394 0.4290 0.4486 -0.1423 0.0416  0.0298  118 ASP B C   
13196 O O   . ASP B  92  ? 0.4502 0.4269 0.4596 -0.1445 0.0456  0.0305  118 ASP B O   
13197 C CB  . ASP B  92  ? 0.4714 0.4630 0.4757 -0.1387 0.0424  0.0450  118 ASP B CB  
13198 C CG  . ASP B  92  ? 0.5635 0.5648 0.5679 -0.1448 0.0432  0.0428  118 ASP B CG  
13199 O OD1 . ASP B  92  ? 0.5745 0.5842 0.5814 -0.1475 0.0415  0.0351  118 ASP B OD1 
13200 O OD2 . ASP B  92  ? 0.6086 0.6092 0.6108 -0.1469 0.0457  0.0491  118 ASP B OD2 
13205 N N   . GLY B  93  ? 0.4223 0.4235 0.4336 -0.1448 0.0390  0.0227  119 GLY B N   
13206 C CA  . GLY B  93  ? 0.4157 0.4165 0.4297 -0.1508 0.0403  0.0151  119 GLY B CA  
13207 C C   . GLY B  93  ? 0.4091 0.4016 0.4238 -0.1494 0.0401  0.0103  119 GLY B C   
13208 O O   . GLY B  93  ? 0.4054 0.3932 0.4215 -0.1550 0.0424  0.0054  119 GLY B O   
13212 N N   . ALA B  94  ? 0.4091 0.4002 0.4228 -0.1423 0.0374  0.0113  120 ALA B N   
13213 C CA  . ALA B  94  ? 0.4151 0.3981 0.4289 -0.1406 0.0374  0.0068  120 ALA B CA  
13214 C C   . ALA B  94  ? 0.4150 0.4059 0.4310 -0.1444 0.0352  -0.0025 120 ALA B C   
13215 O O   . ALA B  94  ? 0.4227 0.4057 0.4387 -0.1474 0.0371  -0.0072 120 ALA B O   
13216 C CB  . ALA B  94  ? 0.4159 0.3981 0.4285 -0.1323 0.0346  0.0097  120 ALA B CB  
13222 N N   . PHE B  95  ? 0.3994 0.4055 0.4170 -0.1440 0.0315  -0.0051 121 PHE B N   
13223 C CA  . PHE B  95  ? 0.3950 0.4109 0.4150 -0.1468 0.0290  -0.0132 121 PHE B CA  
13224 C C   . PHE B  95  ? 0.4057 0.4290 0.4284 -0.1547 0.0305  -0.0159 121 PHE B C   
13225 O O   . PHE B  95  ? 0.4009 0.4345 0.4263 -0.1571 0.0283  -0.0220 121 PHE B O   
13226 C CB  . PHE B  95  ? 0.3784 0.4071 0.3990 -0.1412 0.0241  -0.0142 121 PHE B CB  
13227 C CG  . PHE B  95  ? 0.3746 0.3991 0.3932 -0.1336 0.0221  -0.0117 121 PHE B CG  
13228 C CD1 . PHE B  95  ? 0.3739 0.3971 0.3924 -0.1310 0.0202  -0.0163 121 PHE B CD1 
13229 C CD2 . PHE B  95  ? 0.3813 0.4058 0.3982 -0.1289 0.0214  -0.0050 121 PHE B CD2 
13230 C CE1 . PHE B  95  ? 0.3848 0.4053 0.4018 -0.1240 0.0183  -0.0140 121 PHE B CE1 
13231 C CE2 . PHE B  95  ? 0.3879 0.4099 0.4034 -0.1221 0.0194  -0.0028 121 PHE B CE2 
13232 C CZ  . PHE B  95  ? 0.3840 0.4038 0.3997 -0.1197 0.0179  -0.0073 121 PHE B CZ  
13242 N N   . LEU B  96  ? 0.4213 0.4402 0.4436 -0.1584 0.0342  -0.0112 122 LEU B N   
13243 C CA  . LEU B  96  ? 0.4391 0.4654 0.4640 -0.1657 0.0359  -0.0130 122 LEU B CA  
13244 C C   . LEU B  96  ? 0.4562 0.4822 0.4837 -0.1728 0.0370  -0.0202 122 LEU B C   
13245 O O   . LEU B  96  ? 0.4646 0.5031 0.4956 -0.1772 0.0360  -0.0241 122 LEU B O   
13246 C CB  . LEU B  96  ? 0.4491 0.4680 0.4723 -0.1682 0.0403  -0.0059 122 LEU B CB  
13247 C CG  . LEU B  96  ? 0.4717 0.4996 0.4972 -0.1746 0.0422  -0.0058 122 LEU B CG  
13248 C CD1 . LEU B  96  ? 0.4733 0.5175 0.4998 -0.1716 0.0389  -0.0059 122 LEU B CD1 
13249 C CD2 . LEU B  96  ? 0.4856 0.5037 0.5088 -0.1771 0.0469  0.0014  122 LEU B CD2 
13261 N N   . ASN B  97  ? 0.4659 0.4782 0.4916 -0.1739 0.0390  -0.0220 123 ASN B N   
13262 C CA  . ASN B  97  ? 0.4797 0.4904 0.5071 -0.1812 0.0401  -0.0292 123 ASN B CA  
13263 C C   . ASN B  97  ? 0.4640 0.4870 0.4935 -0.1806 0.0354  -0.0366 123 ASN B C   
13264 O O   . ASN B  97  ? 0.4664 0.4924 0.4979 -0.1873 0.0356  -0.0428 123 ASN B O   
13265 C CB  . ASN B  97  ? 0.5257 0.5167 0.5500 -0.1826 0.0442  -0.0291 123 ASN B CB  
13266 C CG  . ASN B  97  ? 0.6126 0.5979 0.6345 -0.1775 0.0422  -0.0324 123 ASN B CG  
13267 O OD1 . ASN B  97  ? 0.6446 0.6247 0.6659 -0.1817 0.0430  -0.0387 123 ASN B OD1 
13268 N ND2 . ASN B  97  ? 0.6372 0.6238 0.6577 -0.1687 0.0395  -0.0285 123 ASN B ND2 
13275 N N   . LEU B  98  ? 0.4455 0.4752 0.4744 -0.1728 0.0313  -0.0359 124 LEU B N   
13276 C CA  . LEU B  98  ? 0.4291 0.4702 0.4597 -0.1713 0.0268  -0.0421 124 LEU B CA  
13277 C C   . LEU B  98  ? 0.4118 0.4713 0.4470 -0.1736 0.0247  -0.0438 124 LEU B C   
13278 O O   . LEU B  98  ? 0.4093 0.4777 0.4452 -0.1684 0.0225  -0.0410 124 LEU B O   
13279 C CB  . LEU B  98  ? 0.4266 0.4667 0.4547 -0.1620 0.0237  -0.0402 124 LEU B CB  
13280 C CG  . LEU B  98  ? 0.4417 0.4646 0.4657 -0.1587 0.0258  -0.0380 124 LEU B CG  
13281 C CD1 . LEU B  98  ? 0.4502 0.4743 0.4725 -0.1496 0.0228  -0.0354 124 LEU B CD1 
13282 C CD2 . LEU B  98  ? 0.4441 0.4594 0.4668 -0.1631 0.0271  -0.0444 124 LEU B CD2 
13294 N N   . LYS B  99  ? 0.4001 0.4652 0.4386 -0.1817 0.0255  -0.0487 125 LYS B N   
13295 C CA  . LYS B  99  ? 0.3956 0.4779 0.4392 -0.1850 0.0243  -0.0502 125 LYS B CA  
13296 C C   . LYS B  99  ? 0.3789 0.4774 0.4253 -0.1807 0.0194  -0.0537 125 LYS B C   
13297 O O   . LYS B  99  ? 0.3651 0.4775 0.4156 -0.1811 0.0186  -0.0533 125 LYS B O   
13298 C CB  . LYS B  99  ? 0.4274 0.5106 0.4740 -0.1954 0.0269  -0.0542 125 LYS B CB  
13299 C CG  . LYS B  99  ? 0.5079 0.5769 0.5525 -0.2002 0.0324  -0.0502 125 LYS B CG  
13300 C CD  . LYS B  99  ? 0.5965 0.6720 0.6432 -0.2011 0.0344  -0.0450 125 LYS B CD  
13301 C CE  . LYS B  99  ? 0.6641 0.7520 0.7165 -0.2096 0.0354  -0.0484 125 LYS B CE  
13302 N NZ  . LYS B  99  ? 0.7148 0.8086 0.7688 -0.2105 0.0379  -0.0434 125 LYS B NZ  
13316 N N   . ASN B  100 ? 0.3790 0.4762 0.4235 -0.1767 0.0163  -0.0569 126 ASN B N   
13317 C CA  . ASN B  100 ? 0.3767 0.4887 0.4236 -0.1720 0.0117  -0.0596 126 ASN B CA  
13318 C C   . ASN B  100 ? 0.3559 0.4649 0.3996 -0.1623 0.0096  -0.0560 126 ASN B C   
13319 O O   . ASN B  100 ? 0.3504 0.4685 0.3951 -0.1576 0.0060  -0.0581 126 ASN B O   
13320 C CB  . ASN B  100 ? 0.4232 0.5391 0.4708 -0.1752 0.0093  -0.0663 126 ASN B CB  
13321 C CG  . ASN B  100 ? 0.4919 0.6264 0.5436 -0.1725 0.0048  -0.0693 126 ASN B CG  
13322 O OD1 . ASN B  100 ? 0.5085 0.6504 0.5612 -0.1656 0.0030  -0.0665 126 ASN B OD1 
13323 N ND2 . ASN B  100 ? 0.5002 0.6426 0.5541 -0.1777 0.0030  -0.0751 126 ASN B ND2 
13330 N N   . LEU B  101 ? 0.3402 0.4370 0.3802 -0.1592 0.0119  -0.0505 127 LEU B N   
13331 C CA  . LEU B  101 ? 0.3212 0.4155 0.3585 -0.1506 0.0100  -0.0471 127 LEU B CA  
13332 C C   . LEU B  101 ? 0.3014 0.4093 0.3412 -0.1470 0.0081  -0.0456 127 LEU B C   
13333 O O   . LEU B  101 ? 0.2912 0.4023 0.3322 -0.1493 0.0102  -0.0428 127 LEU B O   
13334 C CB  . LEU B  101 ? 0.3314 0.4107 0.3646 -0.1486 0.0128  -0.0413 127 LEU B CB  
13335 C CG  . LEU B  101 ? 0.3531 0.4286 0.3833 -0.1402 0.0109  -0.0377 127 LEU B CG  
13336 C CD1 . LEU B  101 ? 0.3628 0.4342 0.3913 -0.1371 0.0089  -0.0412 127 LEU B CD1 
13337 C CD2 . LEU B  101 ? 0.3630 0.4265 0.3902 -0.1388 0.0136  -0.0312 127 LEU B CD2 
13349 N N   . ARG B  102 ? 0.2866 0.4022 0.3270 -0.1416 0.0046  -0.0475 128 ARG B N   
13350 C CA  . ARG B  102 ? 0.2829 0.4110 0.3257 -0.1375 0.0029  -0.0467 128 ARG B CA  
13351 C C   . ARG B  102 ? 0.2743 0.3981 0.3137 -0.1299 0.0016  -0.0431 128 ARG B C   
13352 O O   . ARG B  102 ? 0.2648 0.3929 0.3041 -0.1275 0.0020  -0.0403 128 ARG B O   
13353 C CB  . ARG B  102 ? 0.3013 0.4428 0.3480 -0.1370 -0.0001 -0.0516 128 ARG B CB  
13354 C CG  . ARG B  102 ? 0.3735 0.5222 0.4243 -0.1447 0.0005  -0.0557 128 ARG B CG  
13355 C CD  . ARG B  102 ? 0.4488 0.6062 0.5035 -0.1484 0.0027  -0.0543 128 ARG B CD  
13356 N NE  . ARG B  102 ? 0.5128 0.6765 0.5717 -0.1565 0.0036  -0.0579 128 ARG B NE  
13357 C CZ  . ARG B  102 ? 0.5461 0.7160 0.6086 -0.1615 0.0062  -0.0571 128 ARG B CZ  
13358 N NH1 . ARG B  102 ? 0.5228 0.6933 0.5847 -0.1592 0.0082  -0.0529 128 ARG B NH1 
13359 N NH2 . ARG B  102 ? 0.5572 0.7329 0.6236 -0.1692 0.0069  -0.0606 128 ARG B NH2 
13373 N N   . GLU B  103 ? 0.2735 0.3891 0.3098 -0.1262 0.0003  -0.0433 129 GLU B N   
13374 C CA  . GLU B  103 ? 0.2787 0.3907 0.3122 -0.1192 -0.0011 -0.0401 129 GLU B CA  
13375 C C   . GLU B  103 ? 0.2821 0.3795 0.3117 -0.1183 0.0005  -0.0364 129 GLU B C   
13376 O O   . GLU B  103 ? 0.2836 0.3731 0.3120 -0.1199 0.0011  -0.0382 129 GLU B O   
13377 C CB  . GLU B  103 ? 0.3068 0.4241 0.3408 -0.1146 -0.0044 -0.0433 129 GLU B CB  
13378 C CG  . GLU B  103 ? 0.3873 0.5026 0.4190 -0.1074 -0.0059 -0.0405 129 GLU B CG  
13379 C CD  . GLU B  103 ? 0.4845 0.6062 0.5169 -0.1028 -0.0089 -0.0433 129 GLU B CD  
13380 O OE1 . GLU B  103 ? 0.5037 0.6332 0.5387 -0.1048 -0.0101 -0.0473 129 GLU B OE1 
13381 O OE2 . GLU B  103 ? 0.5201 0.6392 0.5505 -0.0972 -0.0101 -0.0413 129 GLU B OE2 
13388 N N   . LEU B  104 ? 0.2766 0.3707 0.3042 -0.1156 0.0011  -0.0313 130 LEU B N   
13389 C CA  . LEU B  104 ? 0.2803 0.3619 0.3047 -0.1139 0.0025  -0.0269 130 LEU B CA  
13390 C C   . LEU B  104 ? 0.2722 0.3539 0.2946 -0.1075 0.0006  -0.0236 130 LEU B C   
13391 O O   . LEU B  104 ? 0.2566 0.3440 0.2787 -0.1066 0.0003  -0.0214 130 LEU B O   
13392 C CB  . LEU B  104 ? 0.2856 0.3625 0.3093 -0.1184 0.0058  -0.0231 130 LEU B CB  
13393 C CG  . LEU B  104 ? 0.3080 0.3720 0.3288 -0.1170 0.0077  -0.0176 130 LEU B CG  
13394 C CD1 . LEU B  104 ? 0.3212 0.3750 0.3411 -0.1162 0.0083  -0.0194 130 LEU B CD1 
13395 C CD2 . LEU B  104 ? 0.3154 0.3757 0.3358 -0.1220 0.0111  -0.0142 130 LEU B CD2 
13407 N N   . LEU B  105 ? 0.2626 0.3383 0.2835 -0.1034 -0.0006 -0.0235 131 LEU B N   
13408 C CA  . LEU B  105 ? 0.2649 0.3406 0.2844 -0.0976 -0.0024 -0.0206 131 LEU B CA  
13409 C C   . LEU B  105 ? 0.2615 0.3266 0.2788 -0.0962 -0.0009 -0.0153 131 LEU B C   
13410 O O   . LEU B  105 ? 0.2584 0.3149 0.2753 -0.0962 0.0003  -0.0156 131 LEU B O   
13411 C CB  . LEU B  105 ? 0.2669 0.3453 0.2867 -0.0935 -0.0049 -0.0242 131 LEU B CB  
13412 C CG  . LEU B  105 ? 0.2846 0.3727 0.3069 -0.0950 -0.0062 -0.0296 131 LEU B CG  
13413 C CD1 . LEU B  105 ? 0.2894 0.3792 0.3115 -0.0905 -0.0085 -0.0322 131 LEU B CD1 
13414 C CD2 . LEU B  105 ? 0.2933 0.3916 0.3171 -0.0955 -0.0066 -0.0295 131 LEU B CD2 
13426 N N   . LEU B  106 ? 0.2624 0.3283 0.2785 -0.0950 -0.0010 -0.0104 132 LEU B N   
13427 C CA  . LEU B  106 ? 0.2710 0.3285 0.2854 -0.0935 0.0002  -0.0045 132 LEU B CA  
13428 C C   . LEU B  106 ? 0.2813 0.3419 0.2944 -0.0891 -0.0020 -0.0010 132 LEU B C   
13429 O O   . LEU B  106 ? 0.2886 0.3488 0.3002 -0.0891 -0.0017 0.0041  132 LEU B O   
13430 C CB  . LEU B  106 ? 0.2722 0.3271 0.2859 -0.0980 0.0029  -0.0010 132 LEU B CB  
13431 C CG  . LEU B  106 ? 0.2973 0.3468 0.3121 -0.1029 0.0058  -0.0034 132 LEU B CG  
13432 C CD1 . LEU B  106 ? 0.3081 0.3586 0.3224 -0.1077 0.0081  -0.0007 132 LEU B CD1 
13433 C CD2 . LEU B  106 ? 0.3100 0.3470 0.3242 -0.1015 0.0078  -0.0013 132 LEU B CD2 
13445 N N   . GLU B  107 ? 0.2792 0.3429 0.2928 -0.0853 -0.0043 -0.0037 133 GLU B N   
13446 C CA  . GLU B  107 ? 0.2827 0.3495 0.2952 -0.0815 -0.0064 -0.0011 133 GLU B CA  
13447 C C   . GLU B  107 ? 0.2870 0.3468 0.2992 -0.0780 -0.0064 0.0034  133 GLU B C   
13448 O O   . GLU B  107 ? 0.2885 0.3414 0.3015 -0.0770 -0.0052 0.0029  133 GLU B O   
13449 C CB  . GLU B  107 ? 0.2968 0.3695 0.3102 -0.0788 -0.0086 -0.0057 133 GLU B CB  
13450 C CG  . GLU B  107 ? 0.3184 0.3987 0.3329 -0.0815 -0.0086 -0.0104 133 GLU B CG  
13451 C CD  . GLU B  107 ? 0.3463 0.4326 0.3616 -0.0784 -0.0105 -0.0142 133 GLU B CD  
13452 O OE1 . GLU B  107 ? 0.3305 0.4149 0.3453 -0.0743 -0.0119 -0.0134 133 GLU B OE1 
13453 O OE2 . GLU B  107 ? 0.3606 0.4536 0.3773 -0.0799 -0.0105 -0.0179 133 GLU B OE2 
13460 N N   . ASP B  108 ? 0.2892 0.3512 0.3003 -0.0760 -0.0078 0.0078  134 ASP B N   
13461 C CA  . ASP B  108 ? 0.3077 0.3650 0.3191 -0.0723 -0.0082 0.0125  134 ASP B CA  
13462 C C   . ASP B  108 ? 0.3131 0.3616 0.3250 -0.0727 -0.0055 0.0163  134 ASP B C   
13463 O O   . ASP B  108 ? 0.3168 0.3591 0.3299 -0.0697 -0.0046 0.0171  134 ASP B O   
13464 C CB  . ASP B  108 ? 0.3439 0.4010 0.3565 -0.0684 -0.0095 0.0094  134 ASP B CB  
13465 C CG  . ASP B  108 ? 0.4400 0.4951 0.4533 -0.0643 -0.0104 0.0139  134 ASP B CG  
13466 O OD1 . ASP B  108 ? 0.4649 0.5212 0.4777 -0.0642 -0.0109 0.0192  134 ASP B OD1 
13467 O OD2 . ASP B  108 ? 0.4681 0.5208 0.4825 -0.0611 -0.0106 0.0121  134 ASP B OD2 
13472 N N   . ASN B  109 ? 0.3101 0.3577 0.3210 -0.0763 -0.0038 0.0188  135 ASN B N   
13473 C CA  . ASN B  109 ? 0.3161 0.3548 0.3274 -0.0770 -0.0007 0.0227  135 ASN B CA  
13474 C C   . ASN B  109 ? 0.3191 0.3578 0.3292 -0.0767 -0.0005 0.0305  135 ASN B C   
13475 O O   . ASN B  109 ? 0.3199 0.3515 0.3301 -0.0776 0.0023  0.0344  135 ASN B O   
13476 C CB  . ASN B  109 ? 0.3301 0.3665 0.3412 -0.0821 0.0017  0.0189  135 ASN B CB  
13477 C CG  . ASN B  109 ? 0.3785 0.4133 0.3908 -0.0827 0.0020  0.0119  135 ASN B CG  
13478 O OD1 . ASN B  109 ? 0.4076 0.4468 0.4202 -0.0864 0.0020  0.0071  135 ASN B OD1 
13479 N ND2 . ASN B  109 ? 0.3720 0.4004 0.3850 -0.0796 0.0026  0.0114  135 ASN B ND2 
13486 N N   . GLN B  110 ? 0.3209 0.3675 0.3299 -0.0757 -0.0034 0.0328  136 GLN B N   
13487 C CA  . GLN B  110 ? 0.3296 0.3782 0.3370 -0.0758 -0.0037 0.0401  136 GLN B CA  
13488 C C   . GLN B  110 ? 0.3211 0.3677 0.3267 -0.0802 -0.0012 0.0422  136 GLN B C   
13489 O O   . GLN B  110 ? 0.3312 0.3750 0.3363 -0.0797 -0.0001 0.0491  136 GLN B O   
13490 C CB  . GLN B  110 ? 0.3692 0.4127 0.3785 -0.0713 -0.0034 0.0464  136 GLN B CB  
13491 C CG  . GLN B  110 ? 0.4398 0.4860 0.4509 -0.0671 -0.0059 0.0451  136 GLN B CG  
13492 C CD  . GLN B  110 ? 0.5465 0.5922 0.5593 -0.0631 -0.0065 0.0525  136 GLN B CD  
13493 O OE1 . GLN B  110 ? 0.5842 0.6262 0.5973 -0.0626 -0.0048 0.0589  136 GLN B OE1 
13494 N NE2 . GLN B  110 ? 0.5701 0.6199 0.5843 -0.0600 -0.0090 0.0521  136 GLN B NE2 
13503 N N   . LEU B  111 ? 0.3033 0.3518 0.3084 -0.0842 -0.0002 0.0366  137 LEU B N   
13504 C CA  . LEU B  111 ? 0.3041 0.3511 0.3079 -0.0887 0.0024  0.0383  137 LEU B CA  
13505 C C   . LEU B  111 ? 0.3071 0.3608 0.3075 -0.0900 0.0013  0.0431  137 LEU B C   
13506 O O   . LEU B  111 ? 0.2916 0.3535 0.2904 -0.0900 -0.0013 0.0408  137 LEU B O   
13507 C CB  . LEU B  111 ? 0.3016 0.3510 0.3060 -0.0928 0.0035  0.0311  137 LEU B CB  
13508 C CG  . LEU B  111 ? 0.3231 0.3664 0.3301 -0.0927 0.0048  0.0259  137 LEU B CG  
13509 C CD1 . LEU B  111 ? 0.3228 0.3716 0.3308 -0.0964 0.0048  0.0188  137 LEU B CD1 
13510 C CD2 . LEU B  111 ? 0.3387 0.3710 0.3464 -0.0938 0.0084  0.0290  137 LEU B CD2 
13522 N N   . PRO B  112 ? 0.3251 0.3753 0.3241 -0.0912 0.0032  0.0498  138 PRO B N   
13523 C CA  . PRO B  112 ? 0.3331 0.3902 0.3282 -0.0927 0.0020  0.0544  138 PRO B CA  
13524 C C   . PRO B  112 ? 0.3382 0.4002 0.3309 -0.0979 0.0034  0.0512  138 PRO B C   
13525 O O   . PRO B  112 ? 0.3417 0.4108 0.3307 -0.0993 0.0022  0.0531  138 PRO B O   
13526 C CB  . PRO B  112 ? 0.3482 0.3990 0.3429 -0.0916 0.0040  0.0631  138 PRO B CB  
13527 C CG  . PRO B  112 ? 0.3541 0.3944 0.3516 -0.0926 0.0079  0.0613  138 PRO B CG  
13528 C CD  . PRO B  112 ? 0.3306 0.3702 0.3310 -0.0913 0.0069  0.0535  138 PRO B CD  
13536 N N   . GLN B  113 ? 0.3437 0.4022 0.3385 -0.1008 0.0060  0.0464  139 GLN B N   
13537 C CA  . GLN B  113 ? 0.3572 0.4203 0.3507 -0.1058 0.0077  0.0433  139 GLN B CA  
13538 C C   . GLN B  113 ? 0.3597 0.4226 0.3568 -0.1074 0.0086  0.0354  139 GLN B C   
13539 O O   . GLN B  113 ? 0.3634 0.4201 0.3634 -0.1055 0.0087  0.0333  139 GLN B O   
13540 C CB  . GLN B  113 ? 0.3919 0.4495 0.3842 -0.1090 0.0114  0.0488  139 GLN B CB  
13541 C CG  . GLN B  113 ? 0.4589 0.5170 0.4475 -0.1080 0.0110  0.0576  139 GLN B CG  
13542 C CD  . GLN B  113 ? 0.5304 0.5989 0.5145 -0.1097 0.0094  0.0579  139 GLN B CD  
13543 O OE1 . GLN B  113 ? 0.5612 0.6359 0.5448 -0.1123 0.0094  0.0519  139 GLN B OE1 
13544 N NE2 . GLN B  113 ? 0.5286 0.5993 0.5091 -0.1083 0.0079  0.0649  139 GLN B NE2 
13553 N N   . ILE B  114 ? 0.3522 0.4217 0.3491 -0.1112 0.0095  0.0312  140 ILE B N   
13554 C CA  . ILE B  114 ? 0.3577 0.4279 0.3583 -0.1135 0.0106  0.0244  140 ILE B CA  
13555 C C   . ILE B  114 ? 0.3590 0.4197 0.3610 -0.1167 0.0141  0.0263  140 ILE B C   
13556 O O   . ILE B  114 ? 0.3633 0.4218 0.3632 -0.1192 0.0165  0.0315  140 ILE B O   
13557 C CB  . ILE B  114 ? 0.3648 0.4447 0.3651 -0.1169 0.0112  0.0203  140 ILE B CB  
13558 C CG1 . ILE B  114 ? 0.3791 0.4672 0.3777 -0.1138 0.0082  0.0183  140 ILE B CG1 
13559 C CG2 . ILE B  114 ? 0.3659 0.4470 0.3707 -0.1198 0.0125  0.0140  140 ILE B CG2 
13560 C CD1 . ILE B  114 ? 0.3925 0.4901 0.3907 -0.1162 0.0090  0.0143  140 ILE B CD1 
13572 N N   . PRO B  115 ? 0.3561 0.4106 0.3612 -0.1165 0.0147  0.0227  141 PRO B N   
13573 C CA  . PRO B  115 ? 0.3591 0.4037 0.3652 -0.1198 0.0185  0.0244  141 PRO B CA  
13574 C C   . PRO B  115 ? 0.3634 0.4110 0.3697 -0.1262 0.0214  0.0236  141 PRO B C   
13575 O O   . PRO B  115 ? 0.3583 0.4153 0.3662 -0.1284 0.0206  0.0185  141 PRO B O   
13576 C CB  . PRO B  115 ? 0.3665 0.4068 0.3755 -0.1193 0.0181  0.0184  141 PRO B CB  
13577 C CG  . PRO B  115 ? 0.3718 0.4168 0.3809 -0.1138 0.0142  0.0165  141 PRO B CG  
13578 C CD  . PRO B  115 ? 0.3472 0.4031 0.3547 -0.1134 0.0122  0.0170  141 PRO B CD  
13586 N N   . SER B  116 ? 0.3675 0.4077 0.3725 -0.1288 0.0249  0.0291  142 SER B N   
13587 C CA  . SER B  116 ? 0.3709 0.4134 0.3761 -0.1351 0.0281  0.0289  142 SER B CA  
13588 C C   . SER B  116 ? 0.3708 0.4088 0.3797 -0.1398 0.0304  0.0235  142 SER B C   
13589 O O   . SER B  116 ? 0.3780 0.4067 0.3880 -0.1385 0.0309  0.0222  142 SER B O   
13590 C CB  . SER B  116 ? 0.3970 0.4337 0.3990 -0.1363 0.0311  0.0373  142 SER B CB  
13591 O OG  . SER B  116 ? 0.4428 0.4768 0.4420 -0.1310 0.0294  0.0439  142 SER B OG  
13597 N N   . GLY B  117 ? 0.3574 0.4021 0.3680 -0.1454 0.0320  0.0203  143 GLY B N   
13598 C CA  . GLY B  117 ? 0.3556 0.3977 0.3697 -0.1510 0.0343  0.0150  143 GLY B CA  
13599 C C   . GLY B  117 ? 0.3501 0.3956 0.3672 -0.1497 0.0314  0.0074  143 GLY B C   
13600 O O   . GLY B  117 ? 0.3601 0.3981 0.3787 -0.1521 0.0327  0.0042  143 GLY B O   
13604 N N   . LEU B  118 ? 0.3358 0.3924 0.3535 -0.1460 0.0276  0.0046  144 LEU B N   
13605 C CA  . LEU B  118 ? 0.3345 0.3956 0.3549 -0.1445 0.0247  -0.0023 144 LEU B CA  
13606 C C   . LEU B  118 ? 0.3349 0.4037 0.3595 -0.1508 0.0257  -0.0080 144 LEU B C   
13607 O O   . LEU B  118 ? 0.3309 0.4058 0.3564 -0.1548 0.0277  -0.0069 144 LEU B O   
13608 C CB  . LEU B  118 ? 0.3321 0.4025 0.3520 -0.1386 0.0207  -0.0033 144 LEU B CB  
13609 C CG  . LEU B  118 ? 0.3541 0.4184 0.3709 -0.1321 0.0187  0.0006  144 LEU B CG  
13610 C CD1 . LEU B  118 ? 0.3596 0.4336 0.3755 -0.1276 0.0155  0.0002  144 LEU B CD1 
13611 C CD2 . LEU B  118 ? 0.3602 0.4165 0.3777 -0.1300 0.0179  -0.0021 144 LEU B CD2 
13623 N N   . PRO B  119 ? 0.3333 0.4026 0.3605 -0.1519 0.0244  -0.0140 145 PRO B N   
13624 C CA  . PRO B  119 ? 0.3319 0.4091 0.3634 -0.1583 0.0252  -0.0194 145 PRO B CA  
13625 C C   . PRO B  119 ? 0.3316 0.4250 0.3659 -0.1576 0.0234  -0.0215 145 PRO B C   
13626 O O   . PRO B  119 ? 0.3341 0.4336 0.3681 -0.1518 0.0201  -0.0225 145 PRO B O   
13627 C CB  . PRO B  119 ? 0.3347 0.4087 0.3674 -0.1586 0.0235  -0.0250 145 PRO B CB  
13628 C CG  . PRO B  119 ? 0.3407 0.4094 0.3704 -0.1512 0.0211  -0.0235 145 PRO B CG  
13629 C CD  . PRO B  119 ? 0.3289 0.3911 0.3551 -0.1479 0.0224  -0.0161 145 PRO B CD  
13637 N N   . GLU B  120 ? 0.3301 0.4302 0.3674 -0.1636 0.0257  -0.0224 146 GLU B N   
13638 C CA  . GLU B  120 ? 0.3331 0.4489 0.3739 -0.1640 0.0251  -0.0243 146 GLU B CA  
13639 C C   . GLU B  120 ? 0.3198 0.4466 0.3648 -0.1623 0.0216  -0.0305 146 GLU B C   
13640 O O   . GLU B  120 ? 0.3181 0.4575 0.3656 -0.1600 0.0204  -0.0318 146 GLU B O   
13641 C CB  . GLU B  120 ? 0.3724 0.4917 0.4160 -0.1719 0.0290  -0.0239 146 GLU B CB  
13642 C CG  . GLU B  120 ? 0.4551 0.5887 0.5013 -0.1723 0.0297  -0.0240 146 GLU B CG  
13643 C CD  . GLU B  120 ? 0.5636 0.6992 0.6120 -0.1800 0.0340  -0.0228 146 GLU B CD  
13644 O OE1 . GLU B  120 ? 0.6123 0.7419 0.6569 -0.1808 0.0369  -0.0173 146 GLU B OE1 
13645 O OE2 . GLU B  120 ? 0.5724 0.7159 0.6265 -0.1853 0.0344  -0.0271 146 GLU B OE2 
13652 N N   . SER B  121 ? 0.3109 0.4329 0.3564 -0.1630 0.0200  -0.0342 147 SER B N   
13653 C CA  . SER B  121 ? 0.3065 0.4386 0.3555 -0.1612 0.0165  -0.0396 147 SER B CA  
13654 C C   . SER B  121 ? 0.3003 0.4339 0.3471 -0.1526 0.0131  -0.0391 147 SER B C   
13655 O O   . SER B  121 ? 0.3017 0.4441 0.3512 -0.1504 0.0102  -0.0430 147 SER B O   
13656 C CB  . SER B  121 ? 0.3231 0.4491 0.3725 -0.1654 0.0161  -0.0438 147 SER B CB  
13657 O OG  . SER B  121 ? 0.3504 0.4607 0.3947 -0.1627 0.0165  -0.0416 147 SER B OG  
13663 N N   . LEU B  122 ? 0.2927 0.4180 0.3348 -0.1480 0.0133  -0.0344 148 LEU B N   
13664 C CA  . LEU B  122 ? 0.2914 0.4174 0.3315 -0.1403 0.0103  -0.0339 148 LEU B CA  
13665 C C   . LEU B  122 ? 0.2746 0.4145 0.3174 -0.1370 0.0088  -0.0354 148 LEU B C   
13666 O O   . LEU B  122 ? 0.2757 0.4214 0.3193 -0.1384 0.0107  -0.0337 148 LEU B O   
13667 C CB  . LEU B  122 ? 0.2958 0.4117 0.3307 -0.1366 0.0110  -0.0282 148 LEU B CB  
13668 C CG  . LEU B  122 ? 0.3188 0.4198 0.3506 -0.1369 0.0120  -0.0258 148 LEU B CG  
13669 C CD1 . LEU B  122 ? 0.3273 0.4210 0.3547 -0.1333 0.0126  -0.0194 148 LEU B CD1 
13670 C CD2 . LEU B  122 ? 0.3212 0.4187 0.3528 -0.1338 0.0095  -0.0293 148 LEU B CD2 
13682 N N   . THR B  123 ? 0.2571 0.4019 0.3011 -0.1324 0.0056  -0.0383 149 THR B N   
13683 C CA  . THR B  123 ? 0.2513 0.4077 0.2975 -0.1279 0.0041  -0.0395 149 THR B CA  
13684 C C   . THR B  123 ? 0.2443 0.3956 0.2864 -0.1207 0.0023  -0.0374 149 THR B C   
13685 O O   . THR B  123 ? 0.2337 0.3912 0.2759 -0.1169 0.0019  -0.0371 149 THR B O   
13686 C CB  . THR B  123 ? 0.2674 0.4347 0.3186 -0.1281 0.0020  -0.0443 149 THR B CB  
13687 O OG1 . THR B  123 ? 0.2920 0.4533 0.3413 -0.1259 -0.0005 -0.0460 149 THR B OG1 
13688 C CG2 . THR B  123 ? 0.2717 0.4455 0.3274 -0.1356 0.0037  -0.0466 149 THR B CG2 
13696 N N   . GLU B  124 ? 0.2488 0.3888 0.2874 -0.1189 0.0012  -0.0361 150 GLU B N   
13697 C CA  . GLU B  124 ? 0.2547 0.3900 0.2898 -0.1126 -0.0005 -0.0340 150 GLU B CA  
13698 C C   . GLU B  124 ? 0.2543 0.3766 0.2852 -0.1128 0.0004  -0.0299 150 GLU B C   
13699 O O   . GLU B  124 ? 0.2598 0.3747 0.2903 -0.1152 0.0009  -0.0304 150 GLU B O   
13700 C CB  . GLU B  124 ? 0.2950 0.4323 0.3312 -0.1087 -0.0034 -0.0373 150 GLU B CB  
13701 C CG  . GLU B  124 ? 0.3937 0.5443 0.4339 -0.1069 -0.0046 -0.0404 150 GLU B CG  
13702 C CD  . GLU B  124 ? 0.5210 0.6772 0.5643 -0.1071 -0.0067 -0.0445 150 GLU B CD  
13703 O OE1 . GLU B  124 ? 0.5531 0.7175 0.6004 -0.1115 -0.0062 -0.0470 150 GLU B OE1 
13704 O OE2 . GLU B  124 ? 0.5429 0.6960 0.5845 -0.1029 -0.0088 -0.0452 150 GLU B OE2 
13711 N N   . LEU B  125 ? 0.2467 0.3665 0.2744 -0.1104 0.0008  -0.0259 151 LEU B N   
13712 C CA  . LEU B  125 ? 0.2481 0.3570 0.2721 -0.1100 0.0015  -0.0212 151 LEU B CA  
13713 C C   . LEU B  125 ? 0.2459 0.3536 0.2671 -0.1044 -0.0005 -0.0191 151 LEU B C   
13714 O O   . LEU B  125 ? 0.2385 0.3520 0.2588 -0.1031 -0.0007 -0.0186 151 LEU B O   
13715 C CB  . LEU B  125 ? 0.2543 0.3623 0.2769 -0.1143 0.0043  -0.0176 151 LEU B CB  
13716 C CG  . LEU B  125 ? 0.2715 0.3699 0.2902 -0.1137 0.0052  -0.0116 151 LEU B CG  
13717 C CD1 . LEU B  125 ? 0.2777 0.3653 0.2963 -0.1140 0.0057  -0.0108 151 LEU B CD1 
13718 C CD2 . LEU B  125 ? 0.2821 0.3812 0.2994 -0.1180 0.0080  -0.0082 151 LEU B CD2 
13730 N N   . SER B  126 ? 0.2458 0.3460 0.2658 -0.1012 -0.0018 -0.0179 152 SER B N   
13731 C CA  . SER B  126 ? 0.2491 0.3480 0.2667 -0.0962 -0.0037 -0.0157 152 SER B CA  
13732 C C   . SER B  126 ? 0.2537 0.3440 0.2687 -0.0958 -0.0031 -0.0102 152 SER B C   
13733 O O   . SER B  126 ? 0.2640 0.3465 0.2792 -0.0961 -0.0023 -0.0092 152 SER B O   
13734 C CB  . SER B  126 ? 0.2688 0.3680 0.2876 -0.0920 -0.0059 -0.0187 152 SER B CB  
13735 O OG  . SER B  126 ? 0.2988 0.3978 0.3156 -0.0876 -0.0075 -0.0168 152 SER B OG  
13741 N N   . LEU B  127 ? 0.2486 0.3404 0.2609 -0.0951 -0.0033 -0.0066 153 LEU B N   
13742 C CA  . LEU B  127 ? 0.2588 0.3443 0.2685 -0.0943 -0.0031 -0.0006 153 LEU B CA  
13743 C C   . LEU B  127 ? 0.2617 0.3489 0.2695 -0.0902 -0.0055 0.0011  153 LEU B C   
13744 O O   . LEU B  127 ? 0.2777 0.3638 0.2829 -0.0900 -0.0058 0.0059  153 LEU B O   
13745 C CB  . LEU B  127 ? 0.2654 0.3519 0.2734 -0.0985 -0.0009 0.0026  153 LEU B CB  
13746 C CG  . LEU B  127 ? 0.2887 0.3718 0.2984 -0.1030 0.0018  0.0019  153 LEU B CG  
13747 C CD1 . LEU B  127 ? 0.2971 0.3847 0.3056 -0.1073 0.0039  0.0032  153 LEU B CD1 
13748 C CD2 . LEU B  127 ? 0.2977 0.3702 0.3071 -0.1027 0.0031  0.0060  153 LEU B CD2 
13760 N N   . ILE B  128 ? 0.2502 0.3397 0.2593 -0.0869 -0.0073 -0.0026 154 ILE B N   
13761 C CA  . ILE B  128 ? 0.2524 0.3433 0.2601 -0.0831 -0.0094 -0.0017 154 ILE B CA  
13762 C C   . ILE B  128 ? 0.2595 0.3440 0.2666 -0.0810 -0.0101 0.0033  154 ILE B C   
13763 O O   . ILE B  128 ? 0.2697 0.3481 0.2783 -0.0806 -0.0092 0.0041  154 ILE B O   
13764 C CB  . ILE B  128 ? 0.2546 0.3484 0.2643 -0.0800 -0.0108 -0.0066 154 ILE B CB  
13765 C CG1 . ILE B  128 ? 0.2582 0.3597 0.2687 -0.0814 -0.0102 -0.0108 154 ILE B CG1 
13766 C CG2 . ILE B  128 ? 0.2516 0.3447 0.2602 -0.0760 -0.0128 -0.0054 154 ILE B CG2 
13767 C CD1 . ILE B  128 ? 0.2696 0.3742 0.2827 -0.0786 -0.0111 -0.0155 154 ILE B CD1 
13779 N N   . GLN B  129 ? 0.2535 0.3395 0.2585 -0.0795 -0.0116 0.0065  155 GLN B N   
13780 C CA  . GLN B  129 ? 0.2520 0.3336 0.2570 -0.0770 -0.0126 0.0113  155 GLN B CA  
13781 C C   . GLN B  129 ? 0.2616 0.3374 0.2666 -0.0783 -0.0109 0.0163  155 GLN B C   
13782 O O   . GLN B  129 ? 0.2681 0.3378 0.2750 -0.0760 -0.0103 0.0183  155 GLN B O   
13783 C CB  . GLN B  129 ? 0.2585 0.3373 0.2658 -0.0729 -0.0136 0.0092  155 GLN B CB  
13784 C CG  . GLN B  129 ? 0.2775 0.3607 0.2842 -0.0706 -0.0156 0.0073  155 GLN B CG  
13785 C CD  . GLN B  129 ? 0.3131 0.3974 0.3183 -0.0698 -0.0172 0.0120  155 GLN B CD  
13786 O OE1 . GLN B  129 ? 0.3063 0.3886 0.3110 -0.0705 -0.0170 0.0173  155 GLN B OE1 
13787 N NE2 . GLN B  129 ? 0.3180 0.4058 0.3223 -0.0685 -0.0188 0.0105  155 GLN B NE2 
13796 N N   . ASN B  130 ? 0.2635 0.3413 0.2664 -0.0817 -0.0098 0.0188  156 ASN B N   
13797 C CA  . ASN B  130 ? 0.2658 0.3386 0.2683 -0.0830 -0.0081 0.0245  156 ASN B CA  
13798 C C   . ASN B  130 ? 0.2744 0.3513 0.2735 -0.0837 -0.0093 0.0299  156 ASN B C   
13799 O O   . ASN B  130 ? 0.2696 0.3520 0.2673 -0.0827 -0.0117 0.0292  156 ASN B O   
13800 C CB  . ASN B  130 ? 0.2699 0.3405 0.2729 -0.0869 -0.0053 0.0223  156 ASN B CB  
13801 C CG  . ASN B  130 ? 0.2933 0.3583 0.2993 -0.0862 -0.0041 0.0185  156 ASN B CG  
13802 O OD1 . ASN B  130 ? 0.3030 0.3606 0.3102 -0.0842 -0.0032 0.0211  156 ASN B OD1 
13803 N ND2 . ASN B  130 ? 0.2956 0.3640 0.3028 -0.0879 -0.0039 0.0124  156 ASN B ND2 
13810 N N   . ASN B  131 ? 0.2767 0.3511 0.2746 -0.0854 -0.0078 0.0357  157 ASN B N   
13811 C CA  . ASN B  131 ? 0.2838 0.3626 0.2781 -0.0865 -0.0089 0.0412  157 ASN B CA  
13812 C C   . ASN B  131 ? 0.2901 0.3712 0.2814 -0.0911 -0.0069 0.0413  157 ASN B C   
13813 O O   . ASN B  131 ? 0.3031 0.3840 0.2921 -0.0924 -0.0062 0.0474  157 ASN B O   
13814 C CB  . ASN B  131 ? 0.3020 0.3761 0.2974 -0.0839 -0.0088 0.0490  157 ASN B CB  
13815 C CG  . ASN B  131 ? 0.3390 0.4108 0.3377 -0.0792 -0.0104 0.0492  157 ASN B CG  
13816 O OD1 . ASN B  131 ? 0.3393 0.4153 0.3383 -0.0779 -0.0127 0.0454  157 ASN B OD1 
13817 N ND2 . ASN B  131 ? 0.3484 0.4134 0.3497 -0.0765 -0.0089 0.0539  157 ASN B ND2 
13824 N N   . ILE B  132 ? 0.2812 0.3650 0.2729 -0.0934 -0.0058 0.0348  158 ILE B N   
13825 C CA  . ILE B  132 ? 0.2908 0.3772 0.2803 -0.0978 -0.0035 0.0342  158 ILE B CA  
13826 C C   . ILE B  132 ? 0.3097 0.4042 0.2947 -0.0993 -0.0048 0.0335  158 ILE B C   
13827 O O   . ILE B  132 ? 0.3110 0.4096 0.2959 -0.0984 -0.0061 0.0282  158 ILE B O   
13828 C CB  . ILE B  132 ? 0.2916 0.3775 0.2844 -0.0996 -0.0016 0.0276  158 ILE B CB  
13829 C CG1 . ILE B  132 ? 0.2973 0.3745 0.2937 -0.0989 0.0000  0.0281  158 ILE B CG1 
13830 C CG2 . ILE B  132 ? 0.2968 0.3869 0.2876 -0.1042 0.0008  0.0267  158 ILE B CG2 
13831 C CD1 . ILE B  132 ? 0.3070 0.3843 0.3070 -0.0999 0.0009  0.0211  158 ILE B CD1 
13843 N N   . TYR B  133 ? 0.3169 0.4134 0.2977 -0.1015 -0.0044 0.0388  159 TYR B N   
13844 C CA  . TYR B  133 ? 0.3288 0.4326 0.3041 -0.1034 -0.0054 0.0384  159 TYR B CA  
13845 C C   . TYR B  133 ? 0.3461 0.4528 0.3185 -0.1078 -0.0025 0.0383  159 TYR B C   
13846 O O   . TYR B  133 ? 0.3618 0.4741 0.3289 -0.1098 -0.0028 0.0387  159 TYR B O   
13847 C CB  . TYR B  133 ? 0.3292 0.4348 0.3012 -0.1023 -0.0081 0.0450  159 TYR B CB  
13848 C CG  . TYR B  133 ? 0.3366 0.4390 0.3122 -0.0980 -0.0105 0.0467  159 TYR B CG  
13849 C CD1 . TYR B  133 ? 0.3462 0.4485 0.3247 -0.0956 -0.0119 0.0410  159 TYR B CD1 
13850 C CD2 . TYR B  133 ? 0.3519 0.4510 0.3285 -0.0961 -0.0112 0.0542  159 TYR B CD2 
13851 C CE1 . TYR B  133 ? 0.3604 0.4593 0.3427 -0.0916 -0.0136 0.0424  159 TYR B CE1 
13852 C CE2 . TYR B  133 ? 0.3598 0.4561 0.3402 -0.0919 -0.0130 0.0558  159 TYR B CE2 
13853 C CZ  . TYR B  133 ? 0.3749 0.4710 0.3581 -0.0898 -0.0141 0.0497  159 TYR B CZ  
13854 O OH  . TYR B  133 ? 0.3946 0.4880 0.3816 -0.0857 -0.0157 0.0510  159 TYR B OH  
13864 N N   . ASN B  134 ? 0.3470 0.4498 0.3224 -0.1096 0.0005  0.0378  160 ASN B N   
13865 C CA  . ASN B  134 ? 0.3613 0.4666 0.3347 -0.1140 0.0037  0.0379  160 ASN B CA  
13866 C C   . ASN B  134 ? 0.3596 0.4641 0.3380 -0.1153 0.0060  0.0320  160 ASN B C   
13867 O O   . ASN B  134 ? 0.3628 0.4611 0.3456 -0.1145 0.0065  0.0319  160 ASN B O   
13868 C CB  . ASN B  134 ? 0.3913 0.4920 0.3630 -0.1154 0.0052  0.0459  160 ASN B CB  
13869 C CG  . ASN B  134 ? 0.4565 0.5607 0.4238 -0.1197 0.0079  0.0483  160 ASN B CG  
13870 O OD1 . ASN B  134 ? 0.4645 0.5755 0.4291 -0.1218 0.0086  0.0443  160 ASN B OD1 
13871 N ND2 . ASN B  134 ? 0.4843 0.5837 0.4507 -0.1210 0.0098  0.0551  160 ASN B ND2 
13878 N N   . ILE B  135 ? 0.3542 0.4653 0.3321 -0.1172 0.0073  0.0269  161 ILE B N   
13879 C CA  . ILE B  135 ? 0.3533 0.4660 0.3361 -0.1188 0.0093  0.0213  161 ILE B CA  
13880 C C   . ILE B  135 ? 0.3565 0.4716 0.3377 -0.1236 0.0130  0.0230  161 ILE B C   
13881 O O   . ILE B  135 ? 0.3478 0.4692 0.3251 -0.1251 0.0139  0.0222  161 ILE B O   
13882 C CB  . ILE B  135 ? 0.3544 0.4733 0.3384 -0.1167 0.0082  0.0145  161 ILE B CB  
13883 C CG1 . ILE B  135 ? 0.3664 0.4835 0.3503 -0.1121 0.0046  0.0138  161 ILE B CG1 
13884 C CG2 . ILE B  135 ? 0.3547 0.4759 0.3447 -0.1177 0.0098  0.0091  161 ILE B CG2 
13885 C CD1 . ILE B  135 ? 0.3896 0.5000 0.3771 -0.1096 0.0031  0.0149  161 ILE B CD1 
13897 N N   . THR B  136 ? 0.3630 0.4728 0.3468 -0.1262 0.0152  0.0254  162 THR B N   
13898 C CA  . THR B  136 ? 0.3800 0.4910 0.3623 -0.1310 0.0189  0.0280  162 THR B CA  
13899 C C   . THR B  136 ? 0.3768 0.4896 0.3646 -0.1344 0.0217  0.0235  162 THR B C   
13900 O O   . THR B  136 ? 0.3719 0.4825 0.3648 -0.1333 0.0207  0.0195  162 THR B O   
13901 C CB  . THR B  136 ? 0.4170 0.5200 0.3971 -0.1317 0.0198  0.0359  162 THR B CB  
13902 O OG1 . THR B  136 ? 0.4428 0.5375 0.4277 -0.1313 0.0202  0.0356  162 THR B OG1 
13903 C CG2 . THR B  136 ? 0.4226 0.5248 0.3977 -0.1284 0.0168  0.0410  162 THR B CG2 
13911 N N   . LYS B  137 ? 0.3787 0.4957 0.3652 -0.1388 0.0251  0.0243  163 LYS B N   
13912 C CA  . LYS B  137 ? 0.3841 0.5039 0.3758 -0.1430 0.0281  0.0208  163 LYS B CA  
13913 C C   . LYS B  137 ? 0.3936 0.5041 0.3888 -0.1449 0.0292  0.0225  163 LYS B C   
13914 O O   . LYS B  137 ? 0.3896 0.5010 0.3905 -0.1468 0.0297  0.0177  163 LYS B O   
13915 C CB  . LYS B  137 ? 0.4061 0.5314 0.3950 -0.1474 0.0319  0.0228  163 LYS B CB  
13916 C CG  . LYS B  137 ? 0.4473 0.5823 0.4334 -0.1460 0.0317  0.0196  163 LYS B CG  
13917 C CD  . LYS B  137 ? 0.4964 0.6376 0.4803 -0.1504 0.0359  0.0207  163 LYS B CD  
13918 C CE  . LYS B  137 ? 0.5408 0.6916 0.5231 -0.1489 0.0362  0.0161  163 LYS B CE  
13919 N NZ  . LYS B  137 ? 0.5769 0.7337 0.5561 -0.1528 0.0405  0.0174  163 LYS B NZ  
13933 N N   . GLU B  138 ? 0.4020 0.5036 0.3939 -0.1445 0.0294  0.0292  164 GLU B N   
13934 C CA  . GLU B  138 ? 0.4171 0.5081 0.4117 -0.1459 0.0309  0.0312  164 GLU B CA  
13935 C C   . GLU B  138 ? 0.4132 0.5011 0.4123 -0.1430 0.0283  0.0262  164 GLU B C   
13936 O O   . GLU B  138 ? 0.4193 0.5028 0.4224 -0.1457 0.0298  0.0235  164 GLU B O   
13937 C CB  . GLU B  138 ? 0.4674 0.5499 0.4575 -0.1442 0.0311  0.0397  164 GLU B CB  
13938 C CG  . GLU B  138 ? 0.5607 0.6315 0.5527 -0.1465 0.0341  0.0431  164 GLU B CG  
13939 C CD  . GLU B  138 ? 0.6744 0.7352 0.6655 -0.1420 0.0328  0.0480  164 GLU B CD  
13940 O OE1 . GLU B  138 ? 0.6904 0.7527 0.6775 -0.1382 0.0304  0.0527  164 GLU B OE1 
13941 O OE2 . GLU B  138 ? 0.7174 0.7688 0.7117 -0.1425 0.0342  0.0470  164 GLU B OE2 
13948 N N   . GLY B  139 ? 0.4049 0.4955 0.4029 -0.1378 0.0245  0.0246  165 GLY B N   
13949 C CA  . GLY B  139 ? 0.4021 0.4903 0.4035 -0.1344 0.0219  0.0203  165 GLY B CA  
13950 C C   . GLY B  139 ? 0.3890 0.4846 0.3951 -0.1353 0.0212  0.0125  165 GLY B C   
13951 O O   . GLY B  139 ? 0.3813 0.4731 0.3911 -0.1357 0.0209  0.0092  165 GLY B O   
13955 N N   . ILE B  140 ? 0.3793 0.4856 0.3853 -0.1355 0.0210  0.0096  166 ILE B N   
13956 C CA  . ILE B  140 ? 0.3764 0.4907 0.3872 -0.1353 0.0201  0.0027  166 ILE B CA  
13957 C C   . ILE B  140 ? 0.3717 0.4956 0.3852 -0.1395 0.0228  0.0000  166 ILE B C   
13958 O O   . ILE B  140 ? 0.3602 0.4908 0.3784 -0.1394 0.0221  -0.0054 166 ILE B O   
13959 C CB  . ILE B  140 ? 0.3878 0.5062 0.3976 -0.1295 0.0167  0.0003  166 ILE B CB  
13960 C CG1 . ILE B  140 ? 0.3988 0.5230 0.4040 -0.1286 0.0170  0.0019  166 ILE B CG1 
13961 C CG2 . ILE B  140 ? 0.3988 0.5087 0.4072 -0.1253 0.0140  0.0023  166 ILE B CG2 
13962 C CD1 . ILE B  140 ? 0.4176 0.5472 0.4228 -0.1239 0.0146  -0.0019 166 ILE B CD1 
13974 N N   . SER B  141 ? 0.3777 0.5032 0.3884 -0.1430 0.0258  0.0036  167 SER B N   
13975 C CA  . SER B  141 ? 0.3851 0.5206 0.3987 -0.1468 0.0286  0.0008  167 SER B CA  
13976 C C   . SER B  141 ? 0.3844 0.5205 0.4042 -0.1517 0.0302  -0.0021 167 SER B C   
13977 O O   . SER B  141 ? 0.3826 0.5289 0.4072 -0.1533 0.0310  -0.0064 167 SER B O   
13978 C CB  . SER B  141 ? 0.4121 0.5491 0.4208 -0.1493 0.0316  0.0053  167 SER B CB  
13979 O OG  . SER B  141 ? 0.4466 0.5860 0.4501 -0.1451 0.0298  0.0063  167 SER B OG  
13985 N N   . ARG B  142 ? 0.3855 0.5112 0.4055 -0.1539 0.0307  -0.0001 168 ARG B N   
13986 C CA  . ARG B  142 ? 0.3908 0.5165 0.4163 -0.1591 0.0322  -0.0034 168 ARG B CA  
13987 C C   . ARG B  142 ? 0.3624 0.4921 0.3926 -0.1568 0.0289  -0.0096 168 ARG B C   
13988 O O   . ARG B  142 ? 0.3572 0.4903 0.3924 -0.1610 0.0296  -0.0135 168 ARG B O   
13989 C CB  . ARG B  142 ? 0.4448 0.5569 0.4688 -0.1623 0.0343  0.0005  168 ARG B CB  
13990 C CG  . ARG B  142 ? 0.5379 0.6480 0.5598 -0.1674 0.0386  0.0054  168 ARG B CG  
13991 C CD  . ARG B  142 ? 0.6152 0.7106 0.6342 -0.1689 0.0407  0.0108  168 ARG B CD  
13992 N NE  . ARG B  142 ? 0.6736 0.7629 0.6869 -0.1634 0.0390  0.0163  168 ARG B NE  
13993 C CZ  . ARG B  142 ? 0.7222 0.8005 0.7319 -0.1634 0.0409  0.0230  168 ARG B CZ  
13994 N NH1 . ARG B  142 ? 0.7332 0.8039 0.7440 -0.1687 0.0449  0.0250  168 ARG B NH1 
13995 N NH2 . ARG B  142 ? 0.7304 0.8053 0.7354 -0.1581 0.0388  0.0278  168 ARG B NH2 
14009 N N   . LEU B  143 ? 0.3430 0.4732 0.3716 -0.1503 0.0254  -0.0107 169 LEU B N   
14010 C CA  . LEU B  143 ? 0.3313 0.4654 0.3636 -0.1476 0.0223  -0.0160 169 LEU B CA  
14011 C C   . LEU B  143 ? 0.3262 0.4747 0.3624 -0.1465 0.0218  -0.0200 169 LEU B C   
14012 O O   . LEU B  143 ? 0.3221 0.4747 0.3578 -0.1410 0.0194  -0.0216 169 LEU B O   
14013 C CB  . LEU B  143 ? 0.3274 0.4544 0.3563 -0.1413 0.0191  -0.0149 169 LEU B CB  
14014 C CG  . LEU B  143 ? 0.3419 0.4549 0.3668 -0.1411 0.0197  -0.0102 169 LEU B CG  
14015 C CD1 . LEU B  143 ? 0.3568 0.4651 0.3792 -0.1347 0.0164  -0.0095 169 LEU B CD1 
14016 C CD2 . LEU B  143 ? 0.3455 0.4514 0.3727 -0.1460 0.0213  -0.0115 169 LEU B CD2 
14028 N N   . ILE B  144 ? 0.3309 0.4871 0.3715 -0.1519 0.0243  -0.0216 170 ILE B N   
14029 C CA  . ILE B  144 ? 0.3377 0.5084 0.3826 -0.1514 0.0248  -0.0248 170 ILE B CA  
14030 C C   . ILE B  144 ? 0.3256 0.5040 0.3754 -0.1482 0.0215  -0.0299 170 ILE B C   
14031 O O   . ILE B  144 ? 0.3296 0.5191 0.3822 -0.1454 0.0214  -0.0318 170 ILE B O   
14032 C CB  . ILE B  144 ? 0.3557 0.5331 0.4044 -0.1583 0.0286  -0.0248 170 ILE B CB  
14033 C CG1 . ILE B  144 ? 0.3758 0.5549 0.4302 -0.1640 0.0286  -0.0282 170 ILE B CG1 
14034 C CG2 . ILE B  144 ? 0.3700 0.5398 0.4134 -0.1614 0.0320  -0.0193 170 ILE B CG2 
14035 C CD1 . ILE B  144 ? 0.4011 0.5675 0.4535 -0.1658 0.0276  -0.0278 170 ILE B CD1 
14047 N N   . ASN B  145 ? 0.3043 0.4771 0.3549 -0.1482 0.0191  -0.0319 171 ASN B N   
14048 C CA  . ASN B  145 ? 0.2880 0.4679 0.3426 -0.1451 0.0158  -0.0363 171 ASN B CA  
14049 C C   . ASN B  145 ? 0.2819 0.4573 0.3327 -0.1373 0.0127  -0.0358 171 ASN B C   
14050 O O   . ASN B  145 ? 0.2777 0.4576 0.3310 -0.1341 0.0099  -0.0389 171 ASN B O   
14051 C CB  . ASN B  145 ? 0.2909 0.4679 0.3480 -0.1496 0.0148  -0.0392 171 ASN B CB  
14052 C CG  . ASN B  145 ? 0.3195 0.5025 0.3813 -0.1576 0.0175  -0.0405 171 ASN B CG  
14053 O OD1 . ASN B  145 ? 0.3282 0.5248 0.3951 -0.1587 0.0182  -0.0421 171 ASN B OD1 
14054 N ND2 . ASN B  145 ? 0.3116 0.4845 0.3719 -0.1634 0.0192  -0.0397 171 ASN B ND2 
14061 N N   . LEU B  146 ? 0.2795 0.4464 0.3244 -0.1346 0.0132  -0.0318 172 LEU B N   
14062 C CA  . LEU B  146 ? 0.2799 0.4427 0.3214 -0.1278 0.0105  -0.0312 172 LEU B CA  
14063 C C   . LEU B  146 ? 0.2742 0.4476 0.3182 -0.1230 0.0094  -0.0338 172 LEU B C   
14064 O O   . LEU B  146 ? 0.2747 0.4558 0.3198 -0.1233 0.0115  -0.0338 172 LEU B O   
14065 C CB  . LEU B  146 ? 0.2868 0.4410 0.3219 -0.1261 0.0113  -0.0264 172 LEU B CB  
14066 C CG  . LEU B  146 ? 0.3053 0.4463 0.3366 -0.1266 0.0109  -0.0231 172 LEU B CG  
14067 C CD1 . LEU B  146 ? 0.3103 0.4458 0.3357 -0.1243 0.0112  -0.0183 172 LEU B CD1 
14068 C CD2 . LEU B  146 ? 0.3070 0.4434 0.3389 -0.1233 0.0080  -0.0252 172 LEU B CD2 
14080 N N   . LYS B  147 ? 0.2680 0.4413 0.3127 -0.1185 0.0063  -0.0359 173 LYS B N   
14081 C CA  . LYS B  147 ? 0.2703 0.4520 0.3172 -0.1131 0.0050  -0.0381 173 LYS B CA  
14082 C C   . LYS B  147 ? 0.2575 0.4318 0.2993 -0.1074 0.0035  -0.0363 173 LYS B C   
14083 O O   . LYS B  147 ? 0.2545 0.4325 0.2954 -0.1037 0.0041  -0.0363 173 LYS B O   
14084 C CB  . LYS B  147 ? 0.3200 0.5079 0.3718 -0.1124 0.0026  -0.0417 173 LYS B CB  
14085 C CG  . LYS B  147 ? 0.4097 0.6087 0.4652 -0.1073 0.0017  -0.0438 173 LYS B CG  
14086 C CD  . LYS B  147 ? 0.4845 0.6889 0.5438 -0.1060 -0.0013 -0.0468 173 LYS B CD  
14087 C CE  . LYS B  147 ? 0.5566 0.7534 0.6122 -0.1007 -0.0040 -0.0465 173 LYS B CE  
14088 N NZ  . LYS B  147 ? 0.5981 0.8013 0.6571 -0.0989 -0.0069 -0.0492 173 LYS B NZ  
14102 N N   . ASN B  148 ? 0.2463 0.4103 0.2849 -0.1067 0.0017  -0.0349 174 ASN B N   
14103 C CA  . ASN B  148 ? 0.2409 0.3982 0.2752 -0.1016 0.0002  -0.0331 174 ASN B CA  
14104 C C   . ASN B  148 ? 0.2338 0.3803 0.2634 -0.1035 0.0007  -0.0290 174 ASN B C   
14105 O O   . ASN B  148 ? 0.2387 0.3791 0.2683 -0.1061 0.0006  -0.0283 174 ASN B O   
14106 C CB  . ASN B  148 ? 0.2663 0.4224 0.3016 -0.0976 -0.0027 -0.0351 174 ASN B CB  
14107 C CG  . ASN B  148 ? 0.3171 0.4840 0.3573 -0.0954 -0.0036 -0.0386 174 ASN B CG  
14108 O OD1 . ASN B  148 ? 0.3304 0.5057 0.3728 -0.0948 -0.0022 -0.0395 174 ASN B OD1 
14109 N ND2 . ASN B  148 ? 0.3480 0.5150 0.3897 -0.0937 -0.0060 -0.0406 174 ASN B ND2 
14116 N N   . LEU B  149 ? 0.2219 0.3662 0.2473 -0.1020 0.0013  -0.0263 175 LEU B N   
14117 C CA  . LEU B  149 ? 0.2247 0.3600 0.2456 -0.1033 0.0016  -0.0218 175 LEU B CA  
14118 C C   . LEU B  149 ? 0.2232 0.3547 0.2406 -0.0986 -0.0004 -0.0202 175 LEU B C   
14119 O O   . LEU B  149 ? 0.2145 0.3499 0.2301 -0.0967 -0.0002 -0.0207 175 LEU B O   
14120 C CB  . LEU B  149 ? 0.2311 0.3685 0.2500 -0.1073 0.0043  -0.0194 175 LEU B CB  
14121 C CG  . LEU B  149 ? 0.2581 0.3875 0.2722 -0.1086 0.0048  -0.0141 175 LEU B CG  
14122 C CD1 . LEU B  149 ? 0.2640 0.3846 0.2787 -0.1099 0.0044  -0.0120 175 LEU B CD1 
14123 C CD2 . LEU B  149 ? 0.2686 0.4011 0.2806 -0.1128 0.0077  -0.0119 175 LEU B CD2 
14135 N N   . TYR B  150 ? 0.2312 0.3549 0.2476 -0.0969 -0.0021 -0.0184 176 TYR B N   
14136 C CA  . TYR B  150 ? 0.2482 0.3681 0.2617 -0.0927 -0.0040 -0.0166 176 TYR B CA  
14137 C C   . TYR B  150 ? 0.2663 0.3797 0.2762 -0.0939 -0.0039 -0.0113 176 TYR B C   
14138 O O   . TYR B  150 ? 0.2749 0.3820 0.2853 -0.0950 -0.0036 -0.0092 176 TYR B O   
14139 C CB  . TYR B  150 ? 0.2542 0.3712 0.2695 -0.0890 -0.0062 -0.0184 176 TYR B CB  
14140 C CG  . TYR B  150 ? 0.2691 0.3926 0.2882 -0.0878 -0.0066 -0.0231 176 TYR B CG  
14141 C CD1 . TYR B  150 ? 0.2864 0.4118 0.3088 -0.0908 -0.0059 -0.0254 176 TYR B CD1 
14142 C CD2 . TYR B  150 ? 0.2827 0.4103 0.3023 -0.0836 -0.0077 -0.0252 176 TYR B CD2 
14143 C CE1 . TYR B  150 ? 0.3011 0.4336 0.3271 -0.0898 -0.0067 -0.0294 176 TYR B CE1 
14144 C CE2 . TYR B  150 ? 0.2991 0.4331 0.3223 -0.0821 -0.0081 -0.0290 176 TYR B CE2 
14145 C CZ  . TYR B  150 ? 0.3165 0.4536 0.3430 -0.0852 -0.0078 -0.0310 176 TYR B CZ  
14146 O OH  . TYR B  150 ? 0.3451 0.4897 0.3754 -0.0838 -0.0086 -0.0345 176 TYR B OH  
14156 N N   . LEU B  151 ? 0.2646 0.3794 0.2708 -0.0935 -0.0040 -0.0092 177 LEU B N   
14157 C CA  . LEU B  151 ? 0.2722 0.3823 0.2747 -0.0943 -0.0043 -0.0038 177 LEU B CA  
14158 C C   . LEU B  151 ? 0.2618 0.3713 0.2615 -0.0910 -0.0066 -0.0026 177 LEU B C   
14159 O O   . LEU B  151 ? 0.2676 0.3759 0.2638 -0.0917 -0.0071 0.0016  177 LEU B O   
14160 C CB  . LEU B  151 ? 0.2849 0.3983 0.2846 -0.0984 -0.0021 -0.0020 177 LEU B CB  
14161 C CG  . LEU B  151 ? 0.3195 0.4326 0.3214 -0.1025 0.0004  -0.0020 177 LEU B CG  
14162 C CD1 . LEU B  151 ? 0.3261 0.4453 0.3261 -0.1059 0.0028  -0.0022 177 LEU B CD1 
14163 C CD2 . LEU B  151 ? 0.3391 0.4446 0.3403 -0.1037 0.0009  0.0032  177 LEU B CD2 
14175 N N   . ALA B  152 ? 0.2515 0.3621 0.2529 -0.0875 -0.0080 -0.0060 178 ALA B N   
14176 C CA  . ALA B  152 ? 0.2529 0.3631 0.2521 -0.0847 -0.0098 -0.0054 178 ALA B CA  
14177 C C   . ALA B  152 ? 0.2480 0.3527 0.2467 -0.0831 -0.0116 -0.0009 178 ALA B C   
14178 O O   . ALA B  152 ? 0.2505 0.3505 0.2513 -0.0829 -0.0114 0.0010  178 ALA B O   
14179 C CB  . ALA B  152 ? 0.2554 0.3678 0.2568 -0.0812 -0.0105 -0.0100 178 ALA B CB  
14185 N N   . TRP B  153 ? 0.2451 0.3503 0.2410 -0.0821 -0.0132 0.0009  179 TRP B N   
14186 C CA  . TRP B  153 ? 0.2468 0.3483 0.2427 -0.0801 -0.0151 0.0051  179 TRP B CA  
14187 C C   . TRP B  153 ? 0.2528 0.3510 0.2483 -0.0816 -0.0147 0.0108  179 TRP B C   
14188 O O   . TRP B  153 ? 0.2526 0.3461 0.2505 -0.0795 -0.0152 0.0134  179 TRP B O   
14189 C CB  . TRP B  153 ? 0.2392 0.3374 0.2387 -0.0762 -0.0159 0.0031  179 TRP B CB  
14190 C CG  . TRP B  153 ? 0.2331 0.3339 0.2329 -0.0740 -0.0165 -0.0013 179 TRP B CG  
14191 C CD1 . TRP B  153 ? 0.2413 0.3445 0.2427 -0.0733 -0.0155 -0.0061 179 TRP B CD1 
14192 C CD2 . TRP B  153 ? 0.2286 0.3295 0.2273 -0.0720 -0.0182 -0.0009 179 TRP B CD2 
14193 N NE1 . TRP B  153 ? 0.2423 0.3466 0.2436 -0.0706 -0.0163 -0.0086 179 TRP B NE1 
14194 C CE2 . TRP B  153 ? 0.2344 0.3368 0.2341 -0.0698 -0.0178 -0.0056 179 TRP B CE2 
14195 C CE3 . TRP B  153 ? 0.2344 0.3345 0.2317 -0.0718 -0.0198 0.0031  179 TRP B CE3 
14196 C CZ2 . TRP B  153 ? 0.2393 0.3416 0.2381 -0.0678 -0.0189 -0.0065 179 TRP B CZ2 
14197 C CZ3 . TRP B  153 ? 0.2428 0.3434 0.2396 -0.0700 -0.0211 0.0020  179 TRP B CZ3 
14198 C CH2 . TRP B  153 ? 0.2444 0.3456 0.2418 -0.0681 -0.0205 -0.0029 179 TRP B CH2 
14209 N N   . ASN B  154 ? 0.2534 0.3539 0.2459 -0.0851 -0.0137 0.0130  180 ASN B N   
14210 C CA  . ASN B  154 ? 0.2611 0.3589 0.2528 -0.0863 -0.0133 0.0193  180 ASN B CA  
14211 C C   . ASN B  154 ? 0.2726 0.3733 0.2605 -0.0867 -0.0153 0.0238  180 ASN B C   
14212 O O   . ASN B  154 ? 0.2796 0.3781 0.2679 -0.0860 -0.0159 0.0297  180 ASN B O   
14213 C CB  . ASN B  154 ? 0.2712 0.3688 0.2622 -0.0900 -0.0106 0.0197  180 ASN B CB  
14214 C CG  . ASN B  154 ? 0.2911 0.3842 0.2863 -0.0899 -0.0088 0.0174  180 ASN B CG  
14215 O OD1 . ASN B  154 ? 0.3000 0.3878 0.2962 -0.0906 -0.0074 0.0210  180 ASN B OD1 
14216 N ND2 . ASN B  154 ? 0.2991 0.3938 0.2967 -0.0890 -0.0088 0.0115  180 ASN B ND2 
14223 N N   . CYS B  155 ? 0.2750 0.3809 0.2596 -0.0877 -0.0164 0.0212  181 CYS B N   
14224 C CA  . CYS B  155 ? 0.2847 0.3940 0.2654 -0.0887 -0.0185 0.0250  181 CYS B CA  
14225 C C   . CYS B  155 ? 0.2847 0.3970 0.2636 -0.0882 -0.0199 0.0204  181 CYS B C   
14226 O O   . CYS B  155 ? 0.2849 0.3998 0.2612 -0.0900 -0.0186 0.0159  181 CYS B O   
14227 C CB  . CYS B  155 ? 0.3084 0.4209 0.2842 -0.0926 -0.0176 0.0279  181 CYS B CB  
14228 S SG  . CYS B  155 ? 0.3924 0.5103 0.3628 -0.0943 -0.0205 0.0328  181 CYS B SG  
14233 N N   . TYR B  156 ? 0.2785 0.3902 0.2592 -0.0858 -0.0222 0.0217  182 TYR B N   
14234 C CA  . TYR B  156 ? 0.2746 0.3879 0.2543 -0.0851 -0.0232 0.0173  182 TYR B CA  
14235 C C   . TYR B  156 ? 0.2731 0.3871 0.2537 -0.0837 -0.0260 0.0205  182 TYR B C   
14236 O O   . TYR B  156 ? 0.2726 0.3854 0.2558 -0.0822 -0.0270 0.0258  182 TYR B O   
14237 C CB  . TYR B  156 ? 0.2672 0.3773 0.2509 -0.0822 -0.0218 0.0120  182 TYR B CB  
14238 C CG  . TYR B  156 ? 0.2752 0.3809 0.2640 -0.0788 -0.0221 0.0142  182 TYR B CG  
14239 C CD1 . TYR B  156 ? 0.2887 0.3915 0.2796 -0.0789 -0.0206 0.0160  182 TYR B CD1 
14240 C CD2 . TYR B  156 ? 0.2817 0.3860 0.2729 -0.0759 -0.0238 0.0149  182 TYR B CD2 
14241 C CE1 . TYR B  156 ? 0.2969 0.3950 0.2918 -0.0760 -0.0206 0.0181  182 TYR B CE1 
14242 C CE2 . TYR B  156 ? 0.2951 0.3953 0.2906 -0.0728 -0.0238 0.0171  182 TYR B CE2 
14243 C CZ  . TYR B  156 ? 0.3078 0.4046 0.3049 -0.0728 -0.0222 0.0186  182 TYR B CZ  
14244 O OH  . TYR B  156 ? 0.3234 0.4154 0.3243 -0.0698 -0.0218 0.0203  182 TYR B OH  
14254 N N   . PHE B  157 ? 0.2740 0.3900 0.2526 -0.0843 -0.0270 0.0172  183 PHE B N   
14255 C CA  . PHE B  157 ? 0.2769 0.3942 0.2565 -0.0835 -0.0296 0.0194  183 PHE B CA  
14256 C C   . PHE B  157 ? 0.2857 0.4070 0.2638 -0.0852 -0.0319 0.0264  183 PHE B C   
14257 O O   . PHE B  157 ? 0.2824 0.4072 0.2557 -0.0888 -0.0318 0.0273  183 PHE B O   
14258 C CB  . PHE B  157 ? 0.2743 0.3872 0.2598 -0.0789 -0.0295 0.0189  183 PHE B CB  
14259 C CG  . PHE B  157 ? 0.2814 0.3912 0.2683 -0.0768 -0.0278 0.0127  183 PHE B CG  
14260 C CD1 . PHE B  157 ? 0.2963 0.4070 0.2796 -0.0786 -0.0264 0.0076  183 PHE B CD1 
14261 C CD2 . PHE B  157 ? 0.2892 0.3951 0.2809 -0.0727 -0.0275 0.0122  183 PHE B CD2 
14262 C CE1 . PHE B  157 ? 0.2985 0.4068 0.2836 -0.0762 -0.0247 0.0025  183 PHE B CE1 
14263 C CE2 . PHE B  157 ? 0.2970 0.4008 0.2899 -0.0707 -0.0260 0.0070  183 PHE B CE2 
14264 C CZ  . PHE B  157 ? 0.2920 0.3970 0.2817 -0.0723 -0.0247 0.0024  183 PHE B CZ  
14274 N N   . ASN B  158 ? 0.2844 0.4057 0.2668 -0.0827 -0.0336 0.0314  184 ASN B N   
14275 C CA  . ASN B  158 ? 0.2958 0.4216 0.2776 -0.0838 -0.0357 0.0387  184 ASN B CA  
14276 C C   . ASN B  158 ? 0.3147 0.4372 0.2998 -0.0814 -0.0343 0.0438  184 ASN B C   
14277 O O   . ASN B  158 ? 0.3214 0.4465 0.3077 -0.0807 -0.0358 0.0507  184 ASN B O   
14278 C CB  . ASN B  158 ? 0.2932 0.4226 0.2777 -0.0828 -0.0385 0.0416  184 ASN B CB  
14279 C CG  . ASN B  158 ? 0.3279 0.4604 0.3090 -0.0858 -0.0399 0.0370  184 ASN B CG  
14280 O OD1 . ASN B  158 ? 0.3249 0.4566 0.3090 -0.0842 -0.0405 0.0353  184 ASN B OD1 
14281 N ND2 . ASN B  158 ? 0.3387 0.4749 0.3131 -0.0904 -0.0402 0.0351  184 ASN B ND2 
14288 N N   . LYS B  159 ? 0.3214 0.4384 0.3074 -0.0805 -0.0314 0.0407  185 LYS B N   
14289 C CA  . LYS B  159 ? 0.3283 0.4413 0.3167 -0.0790 -0.0297 0.0451  185 LYS B CA  
14290 C C   . LYS B  159 ? 0.3395 0.4564 0.3237 -0.0821 -0.0301 0.0503  185 LYS B C   
14291 O O   . LYS B  159 ? 0.3352 0.4563 0.3140 -0.0859 -0.0304 0.0480  185 LYS B O   
14292 C CB  . LYS B  159 ? 0.3398 0.4473 0.3291 -0.0788 -0.0266 0.0400  185 LYS B CB  
14293 C CG  . LYS B  159 ? 0.3588 0.4610 0.3504 -0.0778 -0.0245 0.0437  185 LYS B CG  
14294 C CD  . LYS B  159 ? 0.3849 0.4827 0.3775 -0.0783 -0.0217 0.0382  185 LYS B CD  
14295 C CE  . LYS B  159 ? 0.4157 0.5082 0.4097 -0.0783 -0.0193 0.0418  185 LYS B CE  
14296 N NZ  . LYS B  159 ? 0.4290 0.5178 0.4243 -0.0794 -0.0167 0.0364  185 LYS B NZ  
14310 N N   . VAL B  160 ? 0.3537 0.4693 0.3401 -0.0803 -0.0301 0.0575  186 VAL B N   
14311 C CA  . VAL B  160 ? 0.3719 0.4909 0.3546 -0.0827 -0.0303 0.0634  186 VAL B CA  
14312 C C   . VAL B  160 ? 0.3890 0.5032 0.3704 -0.0844 -0.0268 0.0609  186 VAL B C   
14313 O O   . VAL B  160 ? 0.3968 0.5040 0.3822 -0.0821 -0.0244 0.0612  186 VAL B O   
14314 C CB  . VAL B  160 ? 0.3884 0.5076 0.3746 -0.0797 -0.0311 0.0725  186 VAL B CB  
14315 C CG1 . VAL B  160 ? 0.4007 0.5237 0.3827 -0.0821 -0.0312 0.0790  186 VAL B CG1 
14316 C CG2 . VAL B  160 ? 0.3951 0.5196 0.3838 -0.0778 -0.0344 0.0747  186 VAL B CG2 
14326 N N   . CYS B  161 ? 0.3911 0.5088 0.3670 -0.0885 -0.0263 0.0576  187 CYS B N   
14327 C CA  . CYS B  161 ? 0.3999 0.5140 0.3747 -0.0904 -0.0230 0.0546  187 CYS B CA  
14328 C C   . CYS B  161 ? 0.4167 0.5363 0.3847 -0.0950 -0.0227 0.0542  187 CYS B C   
14329 O O   . CYS B  161 ? 0.4234 0.5492 0.3872 -0.0969 -0.0250 0.0535  187 CYS B O   
14330 C CB  . CYS B  161 ? 0.3982 0.5087 0.3760 -0.0893 -0.0215 0.0466  187 CYS B CB  
14331 S SG  . CYS B  161 ? 0.4109 0.5260 0.3865 -0.0899 -0.0234 0.0396  187 CYS B SG  
14336 N N   . GLU B  162 ? 0.4238 0.5412 0.3907 -0.0970 -0.0197 0.0544  188 GLU B N   
14337 C CA  . GLU B  162 ? 0.4322 0.5542 0.3926 -0.1013 -0.0187 0.0542  188 GLU B CA  
14338 C C   . GLU B  162 ? 0.4251 0.5484 0.3842 -0.1031 -0.0171 0.0455  188 GLU B C   
14339 O O   . GLU B  162 ? 0.4246 0.5441 0.3883 -0.1012 -0.0159 0.0406  188 GLU B O   
14340 C CB  . GLU B  162 ? 0.4784 0.5973 0.4386 -0.1028 -0.0157 0.0589  188 GLU B CB  
14341 C CG  . GLU B  162 ? 0.5866 0.7075 0.5440 -0.1030 -0.0169 0.0682  188 GLU B CG  
14342 C CD  . GLU B  162 ? 0.7226 0.8410 0.6847 -0.0987 -0.0188 0.0740  188 GLU B CD  
14343 O OE1 . GLU B  162 ? 0.7590 0.8710 0.7271 -0.0956 -0.0179 0.0719  188 GLU B OE1 
14344 O OE2 . GLU B  162 ? 0.7537 0.8769 0.7135 -0.0985 -0.0213 0.0808  188 GLU B OE2 
14351 N N   . LYS B  163 ? 0.4184 0.5470 0.3709 -0.1067 -0.0167 0.0440  189 LYS B N   
14352 C CA  . LYS B  163 ? 0.4173 0.5474 0.3681 -0.1085 -0.0144 0.0364  189 LYS B CA  
14353 C C   . LYS B  163 ? 0.4042 0.5310 0.3584 -0.1090 -0.0108 0.0352  189 LYS B C   
14354 O O   . LYS B  163 ? 0.4018 0.5267 0.3561 -0.1100 -0.0096 0.0406  189 LYS B O   
14355 C CB  . LYS B  163 ? 0.4545 0.5907 0.3970 -0.1125 -0.0143 0.0357  189 LYS B CB  
14356 C CG  . LYS B  163 ? 0.5281 0.6681 0.4667 -0.1129 -0.0177 0.0353  189 LYS B CG  
14357 C CD  . LYS B  163 ? 0.6024 0.7480 0.5318 -0.1173 -0.0173 0.0342  189 LYS B CD  
14358 C CE  . LYS B  163 ? 0.6688 0.8179 0.5941 -0.1184 -0.0204 0.0325  189 LYS B CE  
14359 N NZ  . LYS B  163 ? 0.7047 0.8513 0.6319 -0.1170 -0.0197 0.0245  189 LYS B NZ  
14373 N N   . THR B  164 ? 0.3979 0.5239 0.3552 -0.1082 -0.0091 0.0284  190 THR B N   
14374 C CA  . THR B  164 ? 0.3976 0.5213 0.3589 -0.1089 -0.0059 0.0268  190 THR B CA  
14375 C C   . THR B  164 ? 0.3949 0.5223 0.3518 -0.1130 -0.0029 0.0269  190 THR B C   
14376 O O   . THR B  164 ? 0.4022 0.5342 0.3547 -0.1145 -0.0023 0.0234  190 THR B O   
14377 C CB  . THR B  164 ? 0.4109 0.5340 0.3770 -0.1067 -0.0053 0.0197  190 THR B CB  
14378 O OG1 . THR B  164 ? 0.4259 0.5461 0.3950 -0.1030 -0.0080 0.0193  190 THR B OG1 
14379 C CG2 . THR B  164 ? 0.4109 0.5319 0.3821 -0.1073 -0.0026 0.0180  190 THR B CG2 
14387 N N   . ASN B  165 ? 0.3837 0.5087 0.3418 -0.1147 -0.0009 0.0310  191 ASN B N   
14388 C CA  . ASN B  165 ? 0.3841 0.5123 0.3388 -0.1187 0.0024  0.0315  191 ASN B CA  
14389 C C   . ASN B  165 ? 0.3796 0.5073 0.3398 -0.1194 0.0054  0.0266  191 ASN B C   
14390 O O   . ASN B  165 ? 0.3843 0.5072 0.3495 -0.1191 0.0062  0.0281  191 ASN B O   
14391 C CB  . ASN B  165 ? 0.3995 0.5255 0.3517 -0.1205 0.0030  0.0396  191 ASN B CB  
14392 C CG  . ASN B  165 ? 0.4543 0.5834 0.4030 -0.1248 0.0067  0.0405  191 ASN B CG  
14393 O OD1 . ASN B  165 ? 0.4686 0.6034 0.4121 -0.1267 0.0076  0.0377  191 ASN B OD1 
14394 N ND2 . ASN B  165 ? 0.4724 0.5975 0.4237 -0.1264 0.0092  0.0440  191 ASN B ND2 
14401 N N   . ILE B  166 ? 0.3700 0.5028 0.3294 -0.1203 0.0072  0.0208  192 ILE B N   
14402 C CA  . ILE B  166 ? 0.3646 0.4990 0.3293 -0.1211 0.0100  0.0162  192 ILE B CA  
14403 C C   . ILE B  166 ? 0.3562 0.4937 0.3181 -0.1255 0.0137  0.0184  192 ILE B C   
14404 O O   . ILE B  166 ? 0.3533 0.4954 0.3092 -0.1271 0.0148  0.0178  192 ILE B O   
14405 C CB  . ILE B  166 ? 0.3741 0.5129 0.3403 -0.1190 0.0102  0.0090  192 ILE B CB  
14406 C CG1 . ILE B  166 ? 0.3929 0.5290 0.3604 -0.1147 0.0066  0.0072  192 ILE B CG1 
14407 C CG2 . ILE B  166 ? 0.3800 0.5216 0.3524 -0.1196 0.0129  0.0047  192 ILE B CG2 
14408 C CD1 . ILE B  166 ? 0.4105 0.5422 0.3846 -0.1122 0.0051  0.0067  192 ILE B CD1 
14420 N N   . GLU B  167 ? 0.3491 0.4836 0.3145 -0.1278 0.0157  0.0210  193 GLU B N   
14421 C CA  . GLU B  167 ? 0.3512 0.4884 0.3141 -0.1322 0.0195  0.0234  193 GLU B CA  
14422 C C   . GLU B  167 ? 0.3443 0.4889 0.3083 -0.1335 0.0223  0.0173  193 GLU B C   
14423 O O   . GLU B  167 ? 0.3338 0.4801 0.3041 -0.1319 0.0224  0.0122  193 GLU B O   
14424 C CB  . GLU B  167 ? 0.3691 0.5009 0.3361 -0.1345 0.0213  0.0270  193 GLU B CB  
14425 C CG  . GLU B  167 ? 0.4444 0.5774 0.4076 -0.1390 0.0249  0.0315  193 GLU B CG  
14426 C CD  . GLU B  167 ? 0.5201 0.6478 0.4877 -0.1420 0.0275  0.0343  193 GLU B CD  
14427 O OE1 . GLU B  167 ? 0.5141 0.6348 0.4859 -0.1402 0.0260  0.0350  193 GLU B OE1 
14428 O OE2 . GLU B  167 ? 0.5547 0.6848 0.5213 -0.1462 0.0313  0.0357  193 GLU B OE2 
14435 N N   . ASP B  168 ? 0.3389 0.4885 0.2969 -0.1361 0.0248  0.0181  194 ASP B N   
14436 C CA  . ASP B  168 ? 0.3401 0.4970 0.2987 -0.1369 0.0279  0.0126  194 ASP B CA  
14437 C C   . ASP B  168 ? 0.3307 0.4901 0.2977 -0.1384 0.0306  0.0097  194 ASP B C   
14438 O O   . ASP B  168 ? 0.3348 0.4922 0.3036 -0.1417 0.0324  0.0132  194 ASP B O   
14439 C CB  . ASP B  168 ? 0.3664 0.5274 0.3170 -0.1403 0.0308  0.0148  194 ASP B CB  
14440 C CG  . ASP B  168 ? 0.4141 0.5823 0.3643 -0.1404 0.0342  0.0090  194 ASP B CG  
14441 O OD1 . ASP B  168 ? 0.4367 0.6063 0.3855 -0.1374 0.0329  0.0045  194 ASP B OD1 
14442 O OD2 . ASP B  168 ? 0.4326 0.6051 0.3843 -0.1435 0.0383  0.0089  194 ASP B OD2 
14447 N N   . GLY B  169 ? 0.3166 0.4801 0.2887 -0.1358 0.0306  0.0035  195 GLY B N   
14448 C CA  . GLY B  169 ? 0.3032 0.4707 0.2836 -0.1370 0.0327  0.0004  195 GLY B CA  
14449 C C   . GLY B  169 ? 0.3027 0.4648 0.2893 -0.1368 0.0304  0.0011  195 GLY B C   
14450 O O   . GLY B  169 ? 0.2992 0.4642 0.2923 -0.1390 0.0321  -0.0008 195 GLY B O   
14454 N N   . VAL B  170 ? 0.3020 0.4566 0.2869 -0.1342 0.0267  0.0034  196 VAL B N   
14455 C CA  . VAL B  170 ? 0.3064 0.4550 0.2965 -0.1339 0.0249  0.0040  196 VAL B CA  
14456 C C   . VAL B  170 ? 0.2990 0.4518 0.2967 -0.1323 0.0243  -0.0020 196 VAL B C   
14457 O O   . VAL B  170 ? 0.2993 0.4510 0.3023 -0.1346 0.0249  -0.0026 196 VAL B O   
14458 C CB  . VAL B  170 ? 0.3213 0.4618 0.3084 -0.1308 0.0213  0.0074  196 VAL B CB  
14459 C CG1 . VAL B  170 ? 0.3323 0.4741 0.3188 -0.1258 0.0182  0.0038  196 VAL B CG1 
14460 C CG2 . VAL B  170 ? 0.3330 0.4661 0.3244 -0.1312 0.0205  0.0090  196 VAL B CG2 
14470 N N   . PHE B  171 ? 0.2872 0.4449 0.2853 -0.1284 0.0233  -0.0062 197 PHE B N   
14471 C CA  . PHE B  171 ? 0.2823 0.4449 0.2875 -0.1263 0.0225  -0.0114 197 PHE B CA  
14472 C C   . PHE B  171 ? 0.2912 0.4639 0.3008 -0.1285 0.0260  -0.0145 197 PHE B C   
14473 O O   . PHE B  171 ? 0.2863 0.4640 0.3025 -0.1275 0.0255  -0.0182 197 PHE B O   
14474 C CB  . PHE B  171 ? 0.2734 0.4363 0.2775 -0.1206 0.0200  -0.0142 197 PHE B CB  
14475 C CG  . PHE B  171 ? 0.2758 0.4302 0.2757 -0.1182 0.0167  -0.0114 197 PHE B CG  
14476 C CD1 . PHE B  171 ? 0.2791 0.4271 0.2815 -0.1176 0.0144  -0.0101 197 PHE B CD1 
14477 C CD2 . PHE B  171 ? 0.2807 0.4338 0.2741 -0.1165 0.0160  -0.0102 197 PHE B CD2 
14478 C CE1 . PHE B  171 ? 0.2849 0.4258 0.2840 -0.1150 0.0115  -0.0073 197 PHE B CE1 
14479 C CE2 . PHE B  171 ? 0.2943 0.4407 0.2845 -0.1143 0.0128  -0.0076 197 PHE B CE2 
14480 C CZ  . PHE B  171 ? 0.2878 0.4285 0.2812 -0.1134 0.0107  -0.0060 197 PHE B CZ  
14490 N N   . GLU B  172 ? 0.3014 0.4775 0.3071 -0.1311 0.0293  -0.0130 198 GLU B N   
14491 C CA  . GLU B  172 ? 0.3126 0.4988 0.3219 -0.1330 0.0331  -0.0156 198 GLU B CA  
14492 C C   . GLU B  172 ? 0.3167 0.5076 0.3344 -0.1363 0.0341  -0.0171 198 GLU B C   
14493 O O   . GLU B  172 ? 0.3163 0.5166 0.3396 -0.1355 0.0355  -0.0208 198 GLU B O   
14494 C CB  . GLU B  172 ? 0.3568 0.5440 0.3599 -0.1365 0.0367  -0.0125 198 GLU B CB  
14495 C CG  . GLU B  172 ? 0.4260 0.6235 0.4311 -0.1373 0.0409  -0.0153 198 GLU B CG  
14496 C CD  . GLU B  172 ? 0.5115 0.7094 0.5091 -0.1403 0.0444  -0.0123 198 GLU B CD  
14497 O OE1 . GLU B  172 ? 0.5070 0.6988 0.5004 -0.1437 0.0442  -0.0074 198 GLU B OE1 
14498 O OE2 . GLU B  172 ? 0.5602 0.7644 0.5560 -0.1392 0.0473  -0.0148 198 GLU B OE2 
14505 N N   . THR B  173 ? 0.3175 0.5021 0.3357 -0.1403 0.0337  -0.0142 199 THR B N   
14506 C CA  . THR B  173 ? 0.3245 0.5126 0.3500 -0.1445 0.0348  -0.0157 199 THR B CA  
14507 C C   . THR B  173 ? 0.3179 0.5053 0.3489 -0.1422 0.0312  -0.0190 199 THR B C   
14508 O O   . THR B  173 ? 0.3221 0.5133 0.3593 -0.1457 0.0316  -0.0209 199 THR B O   
14509 C CB  . THR B  173 ? 0.3586 0.5395 0.3820 -0.1501 0.0366  -0.0111 199 THR B CB  
14510 O OG1 . THR B  173 ? 0.3841 0.5533 0.4032 -0.1483 0.0338  -0.0080 199 THR B OG1 
14511 C CG2 . THR B  173 ? 0.3708 0.5539 0.3893 -0.1529 0.0405  -0.0078 199 THR B CG2 
14519 N N   . LEU B  174 ? 0.3084 0.4916 0.3371 -0.1366 0.0277  -0.0198 200 LEU B N   
14520 C CA  . LEU B  174 ? 0.3069 0.4899 0.3401 -0.1340 0.0244  -0.0230 200 LEU B CA  
14521 C C   . LEU B  174 ? 0.2871 0.4819 0.3254 -0.1308 0.0245  -0.0273 200 LEU B C   
14522 O O   . LEU B  174 ? 0.2777 0.4729 0.3149 -0.1252 0.0226  -0.0288 200 LEU B O   
14523 C CB  . LEU B  174 ? 0.3215 0.4947 0.3500 -0.1295 0.0210  -0.0215 200 LEU B CB  
14524 C CG  . LEU B  174 ? 0.3643 0.5255 0.3894 -0.1315 0.0201  -0.0176 200 LEU B CG  
14525 C CD1 . LEU B  174 ? 0.3891 0.5474 0.4109 -0.1363 0.0233  -0.0133 200 LEU B CD1 
14526 C CD2 . LEU B  174 ? 0.3708 0.5246 0.3912 -0.1265 0.0172  -0.0159 200 LEU B CD2 
14538 N N   . THR B  175 ? 0.2708 0.4754 0.3150 -0.1345 0.0269  -0.0290 201 THR B N   
14539 C CA  . THR B  175 ? 0.2704 0.4878 0.3203 -0.1319 0.0278  -0.0324 201 THR B CA  
14540 C C   . THR B  175 ? 0.2716 0.4937 0.3273 -0.1286 0.0244  -0.0359 201 THR B C   
14541 O O   . THR B  175 ? 0.2745 0.5076 0.3354 -0.1258 0.0250  -0.0384 201 THR B O   
14542 C CB  . THR B  175 ? 0.2769 0.5036 0.3311 -0.1372 0.0318  -0.0325 201 THR B CB  
14543 O OG1 . THR B  175 ? 0.2809 0.5081 0.3399 -0.1428 0.0313  -0.0330 201 THR B OG1 
14544 C CG2 . THR B  175 ? 0.2881 0.5108 0.3359 -0.1400 0.0354  -0.0289 201 THR B CG2 
14552 N N   . ASN B  176 ? 0.2705 0.4845 0.3252 -0.1285 0.0211  -0.0359 202 ASN B N   
14553 C CA  . ASN B  176 ? 0.2661 0.4834 0.3248 -0.1249 0.0175  -0.0388 202 ASN B CA  
14554 C C   . ASN B  176 ? 0.2573 0.4654 0.3107 -0.1189 0.0147  -0.0381 202 ASN B C   
14555 O O   . ASN B  176 ? 0.2657 0.4744 0.3211 -0.1157 0.0117  -0.0400 202 ASN B O   
14556 C CB  . ASN B  176 ? 0.2930 0.5094 0.3552 -0.1299 0.0160  -0.0401 202 ASN B CB  
14557 C CG  . ASN B  176 ? 0.3569 0.5822 0.4247 -0.1365 0.0187  -0.0410 202 ASN B CG  
14558 O OD1 . ASN B  176 ? 0.3899 0.6096 0.4571 -0.1427 0.0197  -0.0400 202 ASN B OD1 
14559 N ND2 . ASN B  176 ? 0.3490 0.5883 0.4226 -0.1354 0.0200  -0.0427 202 ASN B ND2 
14566 N N   . LEU B  177 ? 0.2416 0.4415 0.2881 -0.1176 0.0156  -0.0353 203 LEU B N   
14567 C CA  . LEU B  177 ? 0.2424 0.4337 0.2840 -0.1128 0.0131  -0.0343 203 LEU B CA  
14568 C C   . LEU B  177 ? 0.2365 0.4333 0.2794 -0.1065 0.0124  -0.0366 203 LEU B C   
14569 O O   . LEU B  177 ? 0.2210 0.4233 0.2636 -0.1053 0.0150  -0.0371 203 LEU B O   
14570 C CB  . LEU B  177 ? 0.2447 0.4277 0.2790 -0.1137 0.0143  -0.0306 203 LEU B CB  
14571 C CG  . LEU B  177 ? 0.2628 0.4357 0.2918 -0.1102 0.0116  -0.0287 203 LEU B CG  
14572 C CD1 . LEU B  177 ? 0.2710 0.4366 0.3009 -0.1113 0.0093  -0.0279 203 LEU B CD1 
14573 C CD2 . LEU B  177 ? 0.2735 0.4412 0.2957 -0.1113 0.0129  -0.0251 203 LEU B CD2 
14585 N N   . GLU B  178 ? 0.2429 0.4381 0.2871 -0.1026 0.0092  -0.0379 204 GLU B N   
14586 C CA  . GLU B  178 ? 0.2475 0.4468 0.2930 -0.0963 0.0084  -0.0398 204 GLU B CA  
14587 C C   . GLU B  178 ? 0.2497 0.4392 0.2894 -0.0922 0.0066  -0.0385 204 GLU B C   
14588 O O   . GLU B  178 ? 0.2573 0.4481 0.2960 -0.0877 0.0072  -0.0393 204 GLU B O   
14589 C CB  . GLU B  178 ? 0.2707 0.4767 0.3223 -0.0948 0.0060  -0.0422 204 GLU B CB  
14590 C CG  . GLU B  178 ? 0.3297 0.5476 0.3880 -0.0985 0.0076  -0.0438 204 GLU B CG  
14591 C CD  . GLU B  178 ? 0.4180 0.6443 0.4824 -0.0973 0.0051  -0.0462 204 GLU B CD  
14592 O OE1 . GLU B  178 ? 0.4350 0.6564 0.4980 -0.0946 0.0020  -0.0466 204 GLU B OE1 
14593 O OE2 . GLU B  178 ? 0.4621 0.7006 0.5328 -0.0990 0.0062  -0.0476 204 GLU B OE2 
14600 N N   . LEU B  179 ? 0.2407 0.4205 0.2768 -0.0938 0.0047  -0.0364 205 LEU B N   
14601 C CA  . LEU B  179 ? 0.2363 0.4075 0.2674 -0.0902 0.0030  -0.0349 205 LEU B CA  
14602 C C   . LEU B  179 ? 0.2353 0.3983 0.2611 -0.0936 0.0034  -0.0313 205 LEU B C   
14603 O O   . LEU B  179 ? 0.2349 0.3943 0.2610 -0.0974 0.0033  -0.0298 205 LEU B O   
14604 C CB  . LEU B  179 ? 0.2340 0.4020 0.2666 -0.0873 -0.0002 -0.0357 205 LEU B CB  
14605 C CG  . LEU B  179 ? 0.2561 0.4160 0.2845 -0.0832 -0.0020 -0.0343 205 LEU B CG  
14606 C CD1 . LEU B  179 ? 0.2605 0.4209 0.2913 -0.0791 -0.0045 -0.0360 205 LEU B CD1 
14607 C CD2 . LEU B  179 ? 0.2673 0.4179 0.2916 -0.0857 -0.0028 -0.0310 205 LEU B CD2 
14619 N N   . LEU B  180 ? 0.2261 0.3860 0.2468 -0.0922 0.0040  -0.0299 206 LEU B N   
14620 C CA  . LEU B  180 ? 0.2259 0.3789 0.2412 -0.0948 0.0040  -0.0261 206 LEU B CA  
14621 C C   . LEU B  180 ? 0.2338 0.3813 0.2453 -0.0910 0.0020  -0.0252 206 LEU B C   
14622 O O   . LEU B  180 ? 0.2475 0.3972 0.2574 -0.0884 0.0026  -0.0270 206 LEU B O   
14623 C CB  . LEU B  180 ? 0.2209 0.3773 0.2333 -0.0980 0.0071  -0.0253 206 LEU B CB  
14624 C CG  . LEU B  180 ? 0.2390 0.3896 0.2452 -0.1005 0.0071  -0.0210 206 LEU B CG  
14625 C CD1 . LEU B  180 ? 0.2475 0.3924 0.2543 -0.1033 0.0063  -0.0176 206 LEU B CD1 
14626 C CD2 . LEU B  180 ? 0.2472 0.4022 0.2503 -0.1035 0.0104  -0.0206 206 LEU B CD2 
14638 N N   . SER B  181 ? 0.2293 0.3696 0.2393 -0.0909 -0.0002 -0.0225 207 SER B N   
14639 C CA  . SER B  181 ? 0.2294 0.3648 0.2361 -0.0877 -0.0022 -0.0212 207 SER B CA  
14640 C C   . SER B  181 ? 0.2335 0.3638 0.2356 -0.0901 -0.0026 -0.0166 207 SER B C   
14641 O O   . SER B  181 ? 0.2395 0.3657 0.2423 -0.0917 -0.0031 -0.0138 207 SER B O   
14642 C CB  . SER B  181 ? 0.2354 0.3676 0.2449 -0.0843 -0.0046 -0.0220 207 SER B CB  
14643 O OG  . SER B  181 ? 0.2533 0.3808 0.2599 -0.0816 -0.0064 -0.0205 207 SER B OG  
14649 N N   . LEU B  182 ? 0.2260 0.3569 0.2233 -0.0904 -0.0023 -0.0159 208 LEU B N   
14650 C CA  . LEU B  182 ? 0.2266 0.3540 0.2190 -0.0925 -0.0031 -0.0113 208 LEU B CA  
14651 C C   . LEU B  182 ? 0.2249 0.3498 0.2143 -0.0900 -0.0053 -0.0107 208 LEU B C   
14652 O O   . LEU B  182 ? 0.2105 0.3342 0.1954 -0.0916 -0.0061 -0.0074 208 LEU B O   
14653 C CB  . LEU B  182 ? 0.2342 0.3655 0.2227 -0.0962 -0.0007 -0.0106 208 LEU B CB  
14654 C CG  . LEU B  182 ? 0.2688 0.4026 0.2597 -0.0995 0.0018  -0.0104 208 LEU B CG  
14655 C CD1 . LEU B  182 ? 0.2762 0.4155 0.2638 -0.1021 0.0048  -0.0116 208 LEU B CD1 
14656 C CD2 . LEU B  182 ? 0.2947 0.4237 0.2850 -0.1020 0.0014  -0.0051 208 LEU B CD2 
14668 N N   . SER B  183 ? 0.2257 0.3499 0.2176 -0.0861 -0.0064 -0.0135 209 SER B N   
14669 C CA  . SER B  183 ? 0.2281 0.3498 0.2176 -0.0839 -0.0083 -0.0133 209 SER B CA  
14670 C C   . SER B  183 ? 0.2294 0.3470 0.2177 -0.0842 -0.0106 -0.0084 209 SER B C   
14671 O O   . SER B  183 ? 0.2288 0.3439 0.2194 -0.0845 -0.0110 -0.0057 209 SER B O   
14672 C CB  . SER B  183 ? 0.2337 0.3547 0.2269 -0.0796 -0.0089 -0.0166 209 SER B CB  
14673 O OG  . SER B  183 ? 0.2354 0.3608 0.2301 -0.0787 -0.0067 -0.0208 209 SER B OG  
14679 N N   . PHE B  184 ? 0.2341 0.3510 0.2188 -0.0841 -0.0121 -0.0073 210 PHE B N   
14680 C CA  . PHE B  184 ? 0.2361 0.3502 0.2201 -0.0840 -0.0146 -0.0024 210 PHE B CA  
14681 C C   . PHE B  184 ? 0.2478 0.3618 0.2304 -0.0868 -0.0144 0.0025  210 PHE B C   
14682 O O   . PHE B  184 ? 0.2466 0.3574 0.2318 -0.0860 -0.0151 0.0062  210 PHE B O   
14683 C CB  . PHE B  184 ? 0.2319 0.3423 0.2206 -0.0801 -0.0160 -0.0022 210 PHE B CB  
14684 C CG  . PHE B  184 ? 0.2346 0.3448 0.2238 -0.0773 -0.0164 -0.0060 210 PHE B CG  
14685 C CD1 . PHE B  184 ? 0.2406 0.3519 0.2322 -0.0753 -0.0149 -0.0105 210 PHE B CD1 
14686 C CD2 . PHE B  184 ? 0.2462 0.3555 0.2335 -0.0767 -0.0182 -0.0048 210 PHE B CD2 
14687 C CE1 . PHE B  184 ? 0.2468 0.3576 0.2388 -0.0725 -0.0150 -0.0136 210 PHE B CE1 
14688 C CE2 . PHE B  184 ? 0.2525 0.3610 0.2404 -0.0742 -0.0182 -0.0082 210 PHE B CE2 
14689 C CZ  . PHE B  184 ? 0.2434 0.3523 0.2333 -0.0720 -0.0165 -0.0124 210 PHE B CZ  
14699 N N   . ASN B  185 ? 0.2513 0.3689 0.2297 -0.0902 -0.0129 0.0023  211 ASN B N   
14700 C CA  . ASN B  185 ? 0.2562 0.3747 0.2317 -0.0935 -0.0124 0.0070  211 ASN B CA  
14701 C C   . ASN B  185 ? 0.2718 0.3944 0.2407 -0.0964 -0.0124 0.0067  211 ASN B C   
14702 O O   . ASN B  185 ? 0.2771 0.4012 0.2444 -0.0960 -0.0116 0.0017  211 ASN B O   
14703 C CB  . ASN B  185 ? 0.2576 0.3766 0.2352 -0.0952 -0.0096 0.0060  211 ASN B CB  
14704 C CG  . ASN B  185 ? 0.2716 0.3862 0.2547 -0.0935 -0.0096 0.0069  211 ASN B CG  
14705 O OD1 . ASN B  185 ? 0.2930 0.4037 0.2770 -0.0927 -0.0108 0.0115  211 ASN B OD1 
14706 N ND2 . ASN B  185 ? 0.2407 0.3559 0.2276 -0.0929 -0.0081 0.0026  211 ASN B ND2 
14713 N N   . SER B  186 ? 0.2788 0.4028 0.2435 -0.0990 -0.0133 0.0117  212 SER B N   
14714 C CA  . SER B  186 ? 0.2998 0.4280 0.2574 -0.1022 -0.0133 0.0112  212 SER B CA  
14715 C C   . SER B  186 ? 0.3138 0.4446 0.2688 -0.1052 -0.0100 0.0101  212 SER B C   
14716 O O   . SER B  186 ? 0.3342 0.4655 0.2877 -0.1073 -0.0094 0.0149  212 SER B O   
14717 C CB  . SER B  186 ? 0.3229 0.4527 0.2772 -0.1036 -0.0162 0.0175  212 SER B CB  
14718 O OG  . SER B  186 ? 0.3749 0.5091 0.3215 -0.1073 -0.0161 0.0169  212 SER B OG  
14724 N N   . LEU B  187 ? 0.3010 0.4333 0.2557 -0.1051 -0.0075 0.0040  213 LEU B N   
14725 C CA  . LEU B  187 ? 0.3015 0.4368 0.2544 -0.1077 -0.0039 0.0024  213 LEU B CA  
14726 C C   . LEU B  187 ? 0.3254 0.4644 0.2700 -0.1110 -0.0027 0.0009  213 LEU B C   
14727 O O   . LEU B  187 ? 0.3279 0.4697 0.2693 -0.1140 -0.0004 0.0024  213 LEU B O   
14728 C CB  . LEU B  187 ? 0.2829 0.4186 0.2410 -0.1055 -0.0014 -0.0033 213 LEU B CB  
14729 C CG  . LEU B  187 ? 0.2872 0.4198 0.2532 -0.1024 -0.0022 -0.0034 213 LEU B CG  
14730 C CD1 . LEU B  187 ? 0.2777 0.4127 0.2481 -0.1010 0.0003  -0.0086 213 LEU B CD1 
14731 C CD2 . LEU B  187 ? 0.2965 0.4270 0.2646 -0.1039 -0.0025 0.0018  213 LEU B CD2 
14743 N N   . SER B  188 ? 0.3322 0.4712 0.2734 -0.1105 -0.0036 -0.0026 214 SER B N   
14744 C CA  . SER B  188 ? 0.3450 0.4869 0.2777 -0.1138 -0.0023 -0.0050 214 SER B CA  
14745 C C   . SER B  188 ? 0.3509 0.4946 0.2827 -0.1140 0.0023  -0.0106 214 SER B C   
14746 O O   . SER B  188 ? 0.3521 0.4962 0.2785 -0.1150 0.0038  -0.0149 214 SER B O   
14747 C CB  . SER B  188 ? 0.3593 0.5042 0.2857 -0.1178 -0.0034 0.0006  214 SER B CB  
14748 O OG  . SER B  188 ? 0.3972 0.5415 0.3234 -0.1176 -0.0078 0.0055  214 SER B OG  
14754 N N   . HIS B  189 ? 0.3515 0.4965 0.2882 -0.1135 0.0048  -0.0105 215 HIS B N   
14755 C CA  . HIS B  189 ? 0.3586 0.5063 0.2955 -0.1134 0.0094  -0.0154 215 HIS B CA  
14756 C C   . HIS B  189 ? 0.3508 0.4988 0.2970 -0.1106 0.0106  -0.0165 215 HIS B C   
14757 O O   . HIS B  189 ? 0.3481 0.4947 0.2989 -0.1103 0.0087  -0.0126 215 HIS B O   
14758 C CB  . HIS B  189 ? 0.3883 0.5399 0.3193 -0.1178 0.0121  -0.0135 215 HIS B CB  
14759 C CG  . HIS B  189 ? 0.4519 0.6042 0.3732 -0.1212 0.0107  -0.0118 215 HIS B CG  
14760 N ND1 . HIS B  189 ? 0.4901 0.6435 0.4043 -0.1227 0.0130  -0.0165 215 HIS B ND1 
14761 C CD2 . HIS B  189 ? 0.4769 0.6292 0.3947 -0.1234 0.0073  -0.0059 215 HIS B CD2 
14762 C CE1 . HIS B  189 ? 0.5005 0.6548 0.4068 -0.1261 0.0107  -0.0136 215 HIS B CE1 
14763 N NE2 . HIS B  189 ? 0.4992 0.6533 0.4076 -0.1265 0.0071  -0.0069 215 HIS B NE2 
14771 N N   . VAL B  190 ? 0.3451 0.4954 0.2939 -0.1087 0.0139  -0.0216 216 VAL B N   
14772 C CA  . VAL B  190 ? 0.3459 0.4982 0.3034 -0.1064 0.0152  -0.0228 216 VAL B CA  
14773 C C   . VAL B  190 ? 0.3539 0.5094 0.3121 -0.1100 0.0169  -0.0195 216 VAL B C   
14774 O O   . VAL B  190 ? 0.3598 0.5180 0.3123 -0.1132 0.0195  -0.0193 216 VAL B O   
14775 C CB  . VAL B  190 ? 0.3469 0.5022 0.3067 -0.1036 0.0188  -0.0286 216 VAL B CB  
14776 C CG1 . VAL B  190 ? 0.3409 0.5004 0.3096 -0.1019 0.0202  -0.0295 216 VAL B CG1 
14777 C CG2 . VAL B  190 ? 0.3562 0.5074 0.3155 -0.0998 0.0174  -0.0317 216 VAL B CG2 
14787 N N   . PRO B  191 ? 0.3541 0.5088 0.3184 -0.1101 0.0155  -0.0168 217 PRO B N   
14788 C CA  . PRO B  191 ? 0.3519 0.5088 0.3165 -0.1140 0.0175  -0.0135 217 PRO B CA  
14789 C C   . PRO B  191 ? 0.3604 0.5237 0.3267 -0.1151 0.0220  -0.0167 217 PRO B C   
14790 O O   . PRO B  191 ? 0.3655 0.5318 0.3377 -0.1122 0.0231  -0.0208 217 PRO B O   
14791 C CB  . PRO B  191 ? 0.3612 0.5153 0.3328 -0.1133 0.0155  -0.0114 217 PRO B CB  
14792 C CG  . PRO B  191 ? 0.3664 0.5167 0.3404 -0.1091 0.0121  -0.0128 217 PRO B CG  
14793 C CD  . PRO B  191 ? 0.3440 0.4953 0.3147 -0.1068 0.0125  -0.0167 217 PRO B CD  
14801 N N   . PRO B  192 ? 0.3551 0.5212 0.3167 -0.1191 0.0248  -0.0148 218 PRO B N   
14802 C CA  . PRO B  192 ? 0.3443 0.5172 0.3084 -0.1202 0.0295  -0.0176 218 PRO B CA  
14803 C C   . PRO B  192 ? 0.3291 0.5045 0.3015 -0.1214 0.0303  -0.0167 218 PRO B C   
14804 O O   . PRO B  192 ? 0.3290 0.5001 0.3043 -0.1220 0.0276  -0.0136 218 PRO B O   
14805 C CB  . PRO B  192 ? 0.3642 0.5385 0.3196 -0.1243 0.0320  -0.0153 218 PRO B CB  
14806 C CG  . PRO B  192 ? 0.3745 0.5437 0.3256 -0.1262 0.0286  -0.0095 218 PRO B CG  
14807 C CD  . PRO B  192 ? 0.3534 0.5173 0.3078 -0.1226 0.0240  -0.0095 218 PRO B CD  
14815 N N   . LYS B  193 ? 0.3148 0.4972 0.2913 -0.1218 0.0341  -0.0196 219 LYS B N   
14816 C CA  . LYS B  193 ? 0.3106 0.4972 0.2950 -0.1239 0.0355  -0.0193 219 LYS B CA  
14817 C C   . LYS B  193 ? 0.3119 0.4966 0.3038 -0.1214 0.0320  -0.0203 219 LYS B C   
14818 O O   . LYS B  193 ? 0.3132 0.4947 0.3079 -0.1237 0.0306  -0.0175 219 LYS B O   
14819 C CB  . LYS B  193 ? 0.3246 0.5095 0.3062 -0.1293 0.0366  -0.0141 219 LYS B CB  
14820 C CG  . LYS B  193 ? 0.3753 0.5629 0.3492 -0.1321 0.0402  -0.0129 219 LYS B CG  
14821 C CD  . LYS B  193 ? 0.4233 0.6090 0.3945 -0.1372 0.0414  -0.0072 219 LYS B CD  
14822 C CE  . LYS B  193 ? 0.4607 0.6499 0.4242 -0.1402 0.0453  -0.0060 219 LYS B CE  
14823 N NZ  . LYS B  193 ? 0.4917 0.6789 0.4527 -0.1451 0.0465  0.0001  219 LYS B NZ  
14837 N N   . LEU B  194 ? 0.3147 0.5007 0.3094 -0.1166 0.0310  -0.0242 220 LEU B N   
14838 C CA  . LEU B  194 ? 0.3133 0.4987 0.3150 -0.1138 0.0279  -0.0256 220 LEU B CA  
14839 C C   . LEU B  194 ? 0.3050 0.4996 0.3151 -0.1141 0.0301  -0.0283 220 LEU B C   
14840 O O   . LEU B  194 ? 0.3103 0.5118 0.3210 -0.1139 0.0338  -0.0303 220 LEU B O   
14841 C CB  . LEU B  194 ? 0.3171 0.4993 0.3175 -0.1084 0.0255  -0.0280 220 LEU B CB  
14842 C CG  . LEU B  194 ? 0.3379 0.5117 0.3310 -0.1080 0.0229  -0.0255 220 LEU B CG  
14843 C CD1 . LEU B  194 ? 0.3453 0.5166 0.3376 -0.1030 0.0212  -0.0283 220 LEU B CD1 
14844 C CD2 . LEU B  194 ? 0.3411 0.5088 0.3347 -0.1099 0.0197  -0.0215 220 LEU B CD2 
14856 N N   . PRO B  195 ? 0.2936 0.4888 0.3101 -0.1149 0.0281  -0.0284 221 PRO B N   
14857 C CA  . PRO B  195 ? 0.2818 0.4871 0.3067 -0.1157 0.0299  -0.0308 221 PRO B CA  
14858 C C   . PRO B  195 ? 0.2741 0.4855 0.3031 -0.1100 0.0299  -0.0347 221 PRO B C   
14859 O O   . PRO B  195 ? 0.2705 0.4774 0.2986 -0.1056 0.0270  -0.0355 221 PRO B O   
14860 C CB  . PRO B  195 ? 0.2909 0.4938 0.3203 -0.1183 0.0273  -0.0300 221 PRO B CB  
14861 C CG  . PRO B  195 ? 0.3055 0.4979 0.3305 -0.1158 0.0234  -0.0285 221 PRO B CG  
14862 C CD  . PRO B  195 ? 0.2929 0.4801 0.3095 -0.1151 0.0242  -0.0264 221 PRO B CD  
14870 N N   . SER B  196 ? 0.2645 0.4864 0.2983 -0.1099 0.0334  -0.0366 222 SER B N   
14871 C CA  . SER B  196 ? 0.2633 0.4921 0.3017 -0.1042 0.0342  -0.0399 222 SER B CA  
14872 C C   . SER B  196 ? 0.2471 0.4793 0.2928 -0.1016 0.0306  -0.0413 222 SER B C   
14873 O O   . SER B  196 ? 0.2450 0.4821 0.2944 -0.0961 0.0307  -0.0434 222 SER B O   
14874 C CB  . SER B  196 ? 0.2897 0.5294 0.3320 -0.1050 0.0391  -0.0411 222 SER B CB  
14875 O OG  . SER B  196 ? 0.3431 0.5890 0.3907 -0.1106 0.0398  -0.0401 222 SER B OG  
14881 N N   . SER B  197 ? 0.2337 0.4632 0.2813 -0.1053 0.0277  -0.0400 223 SER B N   
14882 C CA  . SER B  197 ? 0.2255 0.4573 0.2787 -0.1033 0.0240  -0.0414 223 SER B CA  
14883 C C   . SER B  197 ? 0.2246 0.4474 0.2736 -0.0982 0.0207  -0.0414 223 SER B C   
14884 O O   . SER B  197 ? 0.2229 0.4478 0.2758 -0.0952 0.0179  -0.0427 223 SER B O   
14885 C CB  . SER B  197 ? 0.2314 0.4611 0.2864 -0.1093 0.0224  -0.0404 223 SER B CB  
14886 O OG  . SER B  197 ? 0.2609 0.4788 0.3088 -0.1121 0.0219  -0.0375 223 SER B OG  
14892 N N   . LEU B  198 ? 0.2253 0.4384 0.2663 -0.0975 0.0209  -0.0398 224 LEU B N   
14893 C CA  . LEU B  198 ? 0.2330 0.4377 0.2703 -0.0933 0.0178  -0.0396 224 LEU B CA  
14894 C C   . LEU B  198 ? 0.2285 0.4372 0.2690 -0.0868 0.0173  -0.0420 224 LEU B C   
14895 O O   . LEU B  198 ? 0.2216 0.4364 0.2637 -0.0843 0.0204  -0.0435 224 LEU B O   
14896 C CB  . LEU B  198 ? 0.2431 0.4391 0.2717 -0.0936 0.0185  -0.0378 224 LEU B CB  
14897 C CG  . LEU B  198 ? 0.2748 0.4629 0.2987 -0.0983 0.0173  -0.0344 224 LEU B CG  
14898 C CD1 . LEU B  198 ? 0.2944 0.4762 0.3100 -0.0983 0.0179  -0.0327 224 LEU B CD1 
14899 C CD2 . LEU B  198 ? 0.2739 0.4559 0.2990 -0.0977 0.0133  -0.0334 224 LEU B CD2 
14911 N N   . ARG B  199 ? 0.2258 0.4306 0.2671 -0.0840 0.0137  -0.0421 225 ARG B N   
14912 C CA  . ARG B  199 ? 0.2338 0.4406 0.2776 -0.0777 0.0126  -0.0436 225 ARG B CA  
14913 C C   . ARG B  199 ? 0.2211 0.4171 0.2588 -0.0747 0.0108  -0.0428 225 ARG B C   
14914 O O   . ARG B  199 ? 0.2278 0.4231 0.2646 -0.0698 0.0117  -0.0438 225 ARG B O   
14915 C CB  . ARG B  199 ? 0.2761 0.4890 0.3264 -0.0771 0.0098  -0.0445 225 ARG B CB  
14916 C CG  . ARG B  199 ? 0.3588 0.5848 0.4163 -0.0790 0.0116  -0.0457 225 ARG B CG  
14917 C CD  . ARG B  199 ? 0.4615 0.6943 0.5250 -0.0795 0.0087  -0.0467 225 ARG B CD  
14918 N NE  . ARG B  199 ? 0.5398 0.7867 0.6108 -0.0806 0.0105  -0.0479 225 ARG B NE  
14919 C CZ  . ARG B  199 ? 0.5888 0.8449 0.6661 -0.0822 0.0084  -0.0490 225 ARG B CZ  
14920 N NH1 . ARG B  199 ? 0.5891 0.8412 0.6656 -0.0829 0.0046  -0.0493 225 ARG B NH1 
14921 N NH2 . ARG B  199 ? 0.6023 0.8721 0.6868 -0.0831 0.0102  -0.0498 225 ARG B NH2 
14935 N N   . LYS B  200 ? 0.2077 0.3953 0.2413 -0.0776 0.0085  -0.0408 226 LYS B N   
14936 C CA  . LYS B  200 ? 0.2084 0.3864 0.2367 -0.0752 0.0066  -0.0396 226 LYS B CA  
14937 C C   . LYS B  200 ? 0.2148 0.3859 0.2370 -0.0793 0.0068  -0.0371 226 LYS B C   
14938 O O   . LYS B  200 ? 0.2199 0.3892 0.2423 -0.0834 0.0059  -0.0353 226 LYS B O   
14939 C CB  . LYS B  200 ? 0.2187 0.3937 0.2491 -0.0733 0.0030  -0.0393 226 LYS B CB  
14940 C CG  . LYS B  200 ? 0.2366 0.4195 0.2730 -0.0695 0.0024  -0.0414 226 LYS B CG  
14941 C CD  . LYS B  200 ? 0.2811 0.4603 0.3180 -0.0661 -0.0008 -0.0413 226 LYS B CD  
14942 C CE  . LYS B  200 ? 0.3150 0.5031 0.3576 -0.0622 -0.0013 -0.0430 226 LYS B CE  
14943 N NZ  . LYS B  200 ? 0.3312 0.5158 0.3735 -0.0581 -0.0041 -0.0428 226 LYS B NZ  
14957 N N   . LEU B  201 ? 0.2097 0.3770 0.2265 -0.0784 0.0080  -0.0370 227 LEU B N   
14958 C CA  . LEU B  201 ? 0.2139 0.3755 0.2244 -0.0820 0.0079  -0.0344 227 LEU B CA  
14959 C C   . LEU B  201 ? 0.2101 0.3641 0.2163 -0.0798 0.0056  -0.0335 227 LEU B C   
14960 O O   . LEU B  201 ? 0.2138 0.3669 0.2181 -0.0767 0.0066  -0.0354 227 LEU B O   
14961 C CB  . LEU B  201 ? 0.2178 0.3828 0.2249 -0.0841 0.0117  -0.0353 227 LEU B CB  
14962 C CG  . LEU B  201 ? 0.2507 0.4113 0.2506 -0.0880 0.0119  -0.0327 227 LEU B CG  
14963 C CD1 . LEU B  201 ? 0.2614 0.4199 0.2616 -0.0921 0.0104  -0.0290 227 LEU B CD1 
14964 C CD2 . LEU B  201 ? 0.2555 0.4205 0.2523 -0.0898 0.0160  -0.0342 227 LEU B CD2 
14976 N N   . PHE B  202 ? 0.2021 0.3505 0.2071 -0.0812 0.0029  -0.0305 228 PHE B N   
14977 C CA  . PHE B  202 ? 0.2076 0.3495 0.2091 -0.0793 0.0006  -0.0291 228 PHE B CA  
14978 C C   . PHE B  202 ? 0.2122 0.3506 0.2076 -0.0828 0.0003  -0.0261 228 PHE B C   
14979 O O   . PHE B  202 ? 0.2244 0.3612 0.2194 -0.0857 -0.0004 -0.0229 228 PHE B O   
14980 C CB  . PHE B  202 ? 0.2038 0.3420 0.2085 -0.0771 -0.0024 -0.0280 228 PHE B CB  
14981 C CG  . PHE B  202 ? 0.2198 0.3617 0.2299 -0.0738 -0.0026 -0.0307 228 PHE B CG  
14982 C CD1 . PHE B  202 ? 0.2312 0.3784 0.2458 -0.0754 -0.0019 -0.0317 228 PHE B CD1 
14983 C CD2 . PHE B  202 ? 0.2246 0.3647 0.2354 -0.0692 -0.0038 -0.0319 228 PHE B CD2 
14984 C CE1 . PHE B  202 ? 0.2361 0.3876 0.2557 -0.0725 -0.0027 -0.0339 228 PHE B CE1 
14985 C CE2 . PHE B  202 ? 0.2337 0.3775 0.2493 -0.0659 -0.0043 -0.0338 228 PHE B CE2 
14986 C CZ  . PHE B  202 ? 0.2325 0.3824 0.2524 -0.0676 -0.0039 -0.0348 228 PHE B CZ  
14996 N N   . LEU B  203 ? 0.2120 0.3489 0.2026 -0.0823 0.0008  -0.0270 229 LEU B N   
14997 C CA  . LEU B  203 ? 0.2210 0.3557 0.2052 -0.0856 0.0004  -0.0245 229 LEU B CA  
14998 C C   . LEU B  203 ? 0.2204 0.3507 0.2014 -0.0839 -0.0016 -0.0245 229 LEU B C   
14999 O O   . LEU B  203 ? 0.2218 0.3515 0.1970 -0.0858 -0.0010 -0.0248 229 LEU B O   
15000 C CB  . LEU B  203 ? 0.2248 0.3634 0.2051 -0.0881 0.0038  -0.0263 229 LEU B CB  
15001 C CG  . LEU B  203 ? 0.2600 0.4036 0.2432 -0.0903 0.0062  -0.0263 229 LEU B CG  
15002 C CD1 . LEU B  203 ? 0.2592 0.4071 0.2395 -0.0913 0.0101  -0.0293 229 LEU B CD1 
15003 C CD2 . LEU B  203 ? 0.2756 0.4180 0.2574 -0.0942 0.0051  -0.0217 229 LEU B CD2 
15015 N N   . SER B  204 ? 0.2150 0.3422 0.1996 -0.0806 -0.0038 -0.0241 230 SER B N   
15016 C CA  . SER B  204 ? 0.2140 0.3372 0.1964 -0.0791 -0.0056 -0.0239 230 SER B CA  
15017 C C   . SER B  204 ? 0.2269 0.3481 0.2059 -0.0819 -0.0080 -0.0195 230 SER B C   
15018 O O   . SER B  204 ? 0.2384 0.3595 0.2192 -0.0830 -0.0091 -0.0161 230 SER B O   
15019 C CB  . SER B  204 ? 0.2222 0.3432 0.2096 -0.0747 -0.0071 -0.0245 230 SER B CB  
15020 O OG  . SER B  204 ? 0.2415 0.3585 0.2269 -0.0735 -0.0087 -0.0240 230 SER B OG  
15026 N N   . ASN B  205 ? 0.2172 0.3369 0.1915 -0.0830 -0.0089 -0.0195 231 ASN B N   
15027 C CA  . ASN B  205 ? 0.2284 0.3472 0.1999 -0.0854 -0.0117 -0.0150 231 ASN B CA  
15028 C C   . ASN B  205 ? 0.2407 0.3620 0.2102 -0.0889 -0.0115 -0.0113 231 ASN B C   
15029 O O   . ASN B  205 ? 0.2382 0.3585 0.2096 -0.0890 -0.0133 -0.0067 231 ASN B O   
15030 C CB  . ASN B  205 ? 0.2384 0.3541 0.2145 -0.0824 -0.0142 -0.0124 231 ASN B CB  
15031 C CG  . ASN B  205 ? 0.2605 0.3737 0.2373 -0.0797 -0.0148 -0.0148 231 ASN B CG  
15032 O OD1 . ASN B  205 ? 0.2643 0.3764 0.2394 -0.0804 -0.0169 -0.0128 231 ASN B OD1 
15033 N ND2 . ASN B  205 ? 0.2570 0.3695 0.2364 -0.0766 -0.0131 -0.0187 231 ASN B ND2 
15040 N N   . THR B  206 ? 0.2428 0.3671 0.2085 -0.0915 -0.0090 -0.0134 232 THR B N   
15041 C CA  . THR B  206 ? 0.2522 0.3791 0.2154 -0.0950 -0.0082 -0.0102 232 THR B CA  
15042 C C   . THR B  206 ? 0.2732 0.4025 0.2285 -0.0990 -0.0081 -0.0095 232 THR B C   
15043 O O   . THR B  206 ? 0.2737 0.4056 0.2262 -0.1020 -0.0070 -0.0072 232 THR B O   
15044 C CB  . THR B  206 ? 0.2507 0.3801 0.2167 -0.0950 -0.0049 -0.0128 232 THR B CB  
15045 O OG1 . THR B  206 ? 0.2522 0.3830 0.2167 -0.0942 -0.0023 -0.0181 232 THR B OG1 
15046 C CG2 . THR B  206 ? 0.2469 0.3747 0.2202 -0.0922 -0.0053 -0.0125 232 THR B CG2 
15054 N N   . GLN B  207 ? 0.2822 0.4106 0.2338 -0.0994 -0.0093 -0.0113 233 GLN B N   
15055 C CA  . GLN B  207 ? 0.3066 0.4374 0.2501 -0.1035 -0.0094 -0.0113 233 GLN B CA  
15056 C C   . GLN B  207 ? 0.3242 0.4574 0.2631 -0.1058 -0.0055 -0.0149 233 GLN B C   
15057 O O   . GLN B  207 ? 0.3306 0.4667 0.2628 -0.1098 -0.0053 -0.0134 233 GLN B O   
15058 C CB  . GLN B  207 ? 0.3355 0.4684 0.2765 -0.1061 -0.0125 -0.0047 233 GLN B CB  
15059 C CG  . GLN B  207 ? 0.3976 0.5287 0.3430 -0.1039 -0.0161 -0.0010 233 GLN B CG  
15060 C CD  . GLN B  207 ? 0.4925 0.6261 0.4364 -0.1057 -0.0189 0.0062  233 GLN B CD  
15061 O OE1 . GLN B  207 ? 0.5220 0.6583 0.4623 -0.1085 -0.0181 0.0090  233 GLN B OE1 
15062 N NE2 . GLN B  207 ? 0.5165 0.6493 0.4636 -0.1040 -0.0221 0.0096  233 GLN B NE2 
15071 N N   . ILE B  208 ? 0.3313 0.4638 0.2736 -0.1031 -0.0023 -0.0196 234 ILE B N   
15072 C CA  . ILE B  208 ? 0.3532 0.4882 0.2920 -0.1047 0.0019  -0.0234 234 ILE B CA  
15073 C C   . ILE B  208 ? 0.3824 0.5151 0.3159 -0.1049 0.0033  -0.0285 234 ILE B C   
15074 O O   . ILE B  208 ? 0.4007 0.5301 0.3377 -0.1014 0.0038  -0.0317 234 ILE B O   
15075 C CB  . ILE B  208 ? 0.3556 0.4919 0.3013 -0.1016 0.0048  -0.0254 234 ILE B CB  
15076 C CG1 . ILE B  208 ? 0.3613 0.4989 0.3120 -0.1019 0.0034  -0.0206 234 ILE B CG1 
15077 C CG2 . ILE B  208 ? 0.3632 0.5027 0.3054 -0.1031 0.0095  -0.0292 234 ILE B CG2 
15078 C CD1 . ILE B  208 ? 0.3741 0.5139 0.3320 -0.0996 0.0058  -0.0224 234 ILE B CD1 
15090 N N   . LYS B  209 ? 0.3804 0.5146 0.3053 -0.1092 0.0040  -0.0292 235 LYS B N   
15091 C CA  . LYS B  209 ? 0.3871 0.5185 0.3060 -0.1104 0.0053  -0.0342 235 LYS B CA  
15092 C C   . LYS B  209 ? 0.3778 0.5089 0.2941 -0.1098 0.0109  -0.0400 235 LYS B C   
15093 O O   . LYS B  209 ? 0.3647 0.4918 0.2781 -0.1092 0.0130  -0.0449 235 LYS B O   
15094 C CB  . LYS B  209 ? 0.4151 0.5483 0.3252 -0.1158 0.0028  -0.0321 235 LYS B CB  
15095 C CG  . LYS B  209 ? 0.4836 0.6178 0.3962 -0.1163 -0.0026 -0.0260 235 LYS B CG  
15096 C CD  . LYS B  209 ? 0.5581 0.6960 0.4623 -0.1217 -0.0052 -0.0231 235 LYS B CD  
15097 C CE  . LYS B  209 ? 0.6163 0.7564 0.5238 -0.1217 -0.0102 -0.0160 235 LYS B CE  
15098 N NZ  . LYS B  209 ? 0.6432 0.7803 0.5545 -0.1198 -0.0131 -0.0164 235 LYS B NZ  
15112 N N   . TYR B  210 ? 0.3771 0.5123 0.2945 -0.1101 0.0137  -0.0393 236 TYR B N   
15113 C CA  . TYR B  210 ? 0.3886 0.5246 0.3038 -0.1096 0.0193  -0.0443 236 TYR B CA  
15114 C C   . TYR B  210 ? 0.3768 0.5164 0.3004 -0.1063 0.0216  -0.0438 236 TYR B C   
15115 O O   . TYR B  210 ? 0.3821 0.5249 0.3093 -0.1072 0.0198  -0.0392 236 TYR B O   
15116 C CB  . TYR B  210 ? 0.4095 0.5485 0.3147 -0.1151 0.0209  -0.0443 236 TYR B CB  
15117 C CG  . TYR B  210 ? 0.4483 0.5890 0.3510 -0.1150 0.0271  -0.0488 236 TYR B CG  
15118 C CD1 . TYR B  210 ? 0.4718 0.6085 0.3727 -0.1128 0.0311  -0.0550 236 TYR B CD1 
15119 C CD2 . TYR B  210 ? 0.4706 0.6167 0.3721 -0.1172 0.0293  -0.0467 236 TYR B CD2 
15120 C CE1 . TYR B  210 ? 0.4896 0.6280 0.3886 -0.1122 0.0372  -0.0590 236 TYR B CE1 
15121 C CE2 . TYR B  210 ? 0.4899 0.6381 0.3891 -0.1171 0.0352  -0.0507 236 TYR B CE2 
15122 C CZ  . TYR B  210 ? 0.5080 0.6524 0.4058 -0.1145 0.0392  -0.0569 236 TYR B CZ  
15123 O OH  . TYR B  210 ? 0.5401 0.6864 0.4357 -0.1140 0.0455  -0.0609 236 TYR B OH  
15133 N N   . ILE B  211 ? 0.3598 0.4987 0.2865 -0.1026 0.0258  -0.0484 237 ILE B N   
15134 C CA  . ILE B  211 ? 0.3527 0.4961 0.2873 -0.0995 0.0283  -0.0485 237 ILE B CA  
15135 C C   . ILE B  211 ? 0.3620 0.5082 0.2924 -0.1006 0.0342  -0.0522 237 ILE B C   
15136 O O   . ILE B  211 ? 0.3569 0.4999 0.2843 -0.0988 0.0376  -0.0569 237 ILE B O   
15137 C CB  . ILE B  211 ? 0.3472 0.4890 0.2904 -0.0935 0.0282  -0.0502 237 ILE B CB  
15138 C CG1 . ILE B  211 ? 0.3599 0.4980 0.3062 -0.0924 0.0226  -0.0470 237 ILE B CG1 
15139 C CG2 . ILE B  211 ? 0.3417 0.4897 0.2932 -0.0910 0.0304  -0.0500 237 ILE B CG2 
15140 C CD1 . ILE B  211 ? 0.3693 0.5103 0.3195 -0.0942 0.0190  -0.0417 237 ILE B CD1 
15152 N N   . SER B  212 ? 0.3747 0.5265 0.3046 -0.1035 0.0356  -0.0499 238 SER B N   
15153 C CA  . SER B  212 ? 0.3960 0.5513 0.3219 -0.1049 0.0413  -0.0528 238 SER B CA  
15154 C C   . SER B  212 ? 0.4074 0.5671 0.3422 -0.1002 0.0453  -0.0551 238 SER B C   
15155 O O   . SER B  212 ? 0.4024 0.5633 0.3464 -0.0966 0.0432  -0.0538 238 SER B O   
15156 C CB  . SER B  212 ? 0.4159 0.5755 0.3374 -0.1102 0.0411  -0.0488 238 SER B CB  
15157 O OG  . SER B  212 ? 0.4471 0.6114 0.3770 -0.1097 0.0402  -0.0452 238 SER B OG  
15163 N N   . GLU B  213 ? 0.4147 0.5773 0.3467 -0.1005 0.0511  -0.0583 239 GLU B N   
15164 C CA  . GLU B  213 ? 0.4208 0.5890 0.3610 -0.0963 0.0554  -0.0602 239 GLU B CA  
15165 C C   . GLU B  213 ? 0.4081 0.5837 0.3568 -0.0972 0.0539  -0.0561 239 GLU B C   
15166 O O   . GLU B  213 ? 0.4137 0.5935 0.3720 -0.0931 0.0544  -0.0565 239 GLU B O   
15167 C CB  . GLU B  213 ? 0.4661 0.6362 0.4004 -0.0972 0.0622  -0.0640 239 GLU B CB  
15168 C CG  . GLU B  213 ? 0.5449 0.7208 0.4873 -0.0923 0.0675  -0.0665 239 GLU B CG  
15169 C CD  . GLU B  213 ? 0.6311 0.8075 0.5674 -0.0923 0.0747  -0.0709 239 GLU B CD  
15170 O OE1 . GLU B  213 ? 0.6563 0.8276 0.5811 -0.0962 0.0756  -0.0726 239 GLU B OE1 
15171 O OE2 . GLU B  213 ? 0.6644 0.8466 0.6074 -0.0884 0.0795  -0.0725 239 GLU B OE2 
15178 N N   . GLU B  214 ? 0.3929 0.5698 0.3380 -0.1025 0.0518  -0.0521 240 GLU B N   
15179 C CA  . GLU B  214 ? 0.3895 0.5724 0.3414 -0.1044 0.0507  -0.0482 240 GLU B CA  
15180 C C   . GLU B  214 ? 0.3720 0.5528 0.3296 -0.1040 0.0449  -0.0445 240 GLU B C   
15181 O O   . GLU B  214 ? 0.3686 0.5539 0.3326 -0.1053 0.0443  -0.0419 240 GLU B O   
15182 C CB  . GLU B  214 ? 0.4500 0.6349 0.3947 -0.1104 0.0520  -0.0452 240 GLU B CB  
15183 C CG  . GLU B  214 ? 0.5602 0.7477 0.4981 -0.1117 0.0580  -0.0485 240 GLU B CG  
15184 C CD  . GLU B  214 ? 0.7038 0.8993 0.6443 -0.1142 0.0624  -0.0472 240 GLU B CD  
15185 O OE1 . GLU B  214 ? 0.7329 0.9335 0.6834 -0.1133 0.0621  -0.0456 240 GLU B OE1 
15186 O OE2 . GLU B  214 ? 0.7580 0.9547 0.6902 -0.1173 0.0662  -0.0480 240 GLU B OE2 
15193 N N   . ASP B  215 ? 0.3603 0.5343 0.3156 -0.1027 0.0407  -0.0441 241 ASP B N   
15194 C CA  . ASP B  215 ? 0.3611 0.5326 0.3211 -0.1024 0.0354  -0.0405 241 ASP B CA  
15195 C C   . ASP B  215 ? 0.3614 0.5370 0.3325 -0.0991 0.0349  -0.0408 241 ASP B C   
15196 O O   . ASP B  215 ? 0.3600 0.5357 0.3350 -0.1006 0.0319  -0.0375 241 ASP B O   
15197 C CB  . ASP B  215 ? 0.3746 0.5388 0.3310 -0.1009 0.0315  -0.0406 241 ASP B CB  
15198 C CG  . ASP B  215 ? 0.4302 0.5909 0.3767 -0.1052 0.0299  -0.0383 241 ASP B CG  
15199 O OD1 . ASP B  215 ? 0.4458 0.6093 0.3890 -0.1094 0.0307  -0.0354 241 ASP B OD1 
15200 O OD2 . ASP B  215 ? 0.4512 0.6068 0.3933 -0.1046 0.0277  -0.0393 241 ASP B OD2 
15205 N N   . PHE B  216 ? 0.3612 0.5404 0.3372 -0.0948 0.0378  -0.0445 242 PHE B N   
15206 C CA  . PHE B  216 ? 0.3588 0.5431 0.3452 -0.0917 0.0371  -0.0448 242 PHE B CA  
15207 C C   . PHE B  216 ? 0.3843 0.5778 0.3760 -0.0905 0.0420  -0.0470 242 PHE B C   
15208 O O   . PHE B  216 ? 0.3901 0.5884 0.3901 -0.0868 0.0420  -0.0482 242 PHE B O   
15209 C CB  . PHE B  216 ? 0.3443 0.5248 0.3335 -0.0862 0.0350  -0.0466 242 PHE B CB  
15210 C CG  . PHE B  216 ? 0.3404 0.5120 0.3244 -0.0865 0.0308  -0.0452 242 PHE B CG  
15211 C CD1 . PHE B  216 ? 0.3427 0.5118 0.3274 -0.0889 0.0265  -0.0415 242 PHE B CD1 
15212 C CD2 . PHE B  216 ? 0.3479 0.5139 0.3269 -0.0842 0.0314  -0.0476 242 PHE B CD2 
15213 C CE1 . PHE B  216 ? 0.3504 0.5123 0.3310 -0.0889 0.0229  -0.0400 242 PHE B CE1 
15214 C CE2 . PHE B  216 ? 0.3546 0.5134 0.3294 -0.0847 0.0276  -0.0462 242 PHE B CE2 
15215 C CZ  . PHE B  216 ? 0.3491 0.5062 0.3248 -0.0870 0.0233  -0.0423 242 PHE B CZ  
15225 N N   . LYS B  217 ? 0.3984 0.5946 0.3854 -0.0935 0.0463  -0.0476 243 LYS B N   
15226 C CA  . LYS B  217 ? 0.4080 0.6129 0.3997 -0.0920 0.0517  -0.0499 243 LYS B CA  
15227 C C   . LYS B  217 ? 0.3950 0.6095 0.3979 -0.0916 0.0516  -0.0490 243 LYS B C   
15228 O O   . LYS B  217 ? 0.4008 0.6223 0.4100 -0.0877 0.0548  -0.0513 243 LYS B O   
15229 C CB  . LYS B  217 ? 0.4505 0.6571 0.4351 -0.0962 0.0562  -0.0500 243 LYS B CB  
15230 C CG  . LYS B  217 ? 0.5305 0.7335 0.5077 -0.0941 0.0603  -0.0538 243 LYS B CG  
15231 C CD  . LYS B  217 ? 0.5994 0.8036 0.5684 -0.0987 0.0644  -0.0539 243 LYS B CD  
15232 C CE  . LYS B  217 ? 0.6621 0.8599 0.6217 -0.0975 0.0671  -0.0577 243 LYS B CE  
15233 N NZ  . LYS B  217 ? 0.6880 0.8876 0.6393 -0.1012 0.0720  -0.0587 243 LYS B NZ  
15247 N N   . GLY B  218 ? 0.3693 0.5845 0.3744 -0.0959 0.0486  -0.0458 244 GLY B N   
15248 C CA  . GLY B  218 ? 0.3439 0.5680 0.3590 -0.0967 0.0484  -0.0451 244 GLY B CA  
15249 C C   . GLY B  218 ? 0.3202 0.5444 0.3423 -0.0934 0.0440  -0.0452 244 GLY B C   
15250 O O   . GLY B  218 ? 0.3193 0.5514 0.3498 -0.0940 0.0434  -0.0451 244 GLY B O   
15254 N N   . LEU B  219 ? 0.3044 0.5204 0.3230 -0.0901 0.0408  -0.0456 245 LEU B N   
15255 C CA  . LEU B  219 ? 0.2876 0.5027 0.3116 -0.0871 0.0364  -0.0455 245 LEU B CA  
15256 C C   . LEU B  219 ? 0.2719 0.4931 0.3025 -0.0807 0.0377  -0.0481 245 LEU B C   
15257 O O   . LEU B  219 ? 0.2662 0.4826 0.2960 -0.0760 0.0358  -0.0489 245 LEU B O   
15258 C CB  . LEU B  219 ? 0.2889 0.4925 0.3064 -0.0866 0.0325  -0.0442 245 LEU B CB  
15259 C CG  . LEU B  219 ? 0.3065 0.5038 0.3172 -0.0923 0.0312  -0.0411 245 LEU B CG  
15260 C CD1 . LEU B  219 ? 0.3088 0.4963 0.3144 -0.0913 0.0272  -0.0397 245 LEU B CD1 
15261 C CD2 . LEU B  219 ? 0.3104 0.5111 0.3257 -0.0968 0.0301  -0.0388 245 LEU B CD2 
15273 N N   . ILE B  220 ? 0.2657 0.4982 0.3035 -0.0806 0.0405  -0.0489 246 ILE B N   
15274 C CA  . ILE B  220 ? 0.2691 0.5096 0.3141 -0.0745 0.0422  -0.0507 246 ILE B CA  
15275 C C   . ILE B  220 ? 0.2558 0.4993 0.3076 -0.0714 0.0378  -0.0504 246 ILE B C   
15276 O O   . ILE B  220 ? 0.2564 0.5050 0.3132 -0.0655 0.0387  -0.0516 246 ILE B O   
15277 C CB  . ILE B  220 ? 0.2804 0.5335 0.3314 -0.0755 0.0470  -0.0514 246 ILE B CB  
15278 C CG1 . ILE B  220 ? 0.2911 0.5526 0.3488 -0.0807 0.0452  -0.0500 246 ILE B CG1 
15279 C CG2 . ILE B  220 ? 0.2983 0.5484 0.3419 -0.0778 0.0520  -0.0521 246 ILE B CG2 
15280 C CD1 . ILE B  220 ? 0.3137 0.5892 0.3788 -0.0815 0.0498  -0.0506 246 ILE B CD1 
15292 N N   . ASN B  221 ? 0.2541 0.4945 0.3060 -0.0751 0.0333  -0.0489 247 ASN B N   
15293 C CA  . ASN B  221 ? 0.2551 0.4974 0.3122 -0.0725 0.0289  -0.0487 247 ASN B CA  
15294 C C   . ASN B  221 ? 0.2354 0.4656 0.2867 -0.0704 0.0253  -0.0481 247 ASN B C   
15295 O O   . ASN B  221 ? 0.2282 0.4584 0.2825 -0.0688 0.0215  -0.0478 247 ASN B O   
15296 C CB  . ASN B  221 ? 0.2983 0.5457 0.3600 -0.0782 0.0264  -0.0478 247 ASN B CB  
15297 C CG  . ASN B  221 ? 0.4000 0.6615 0.4699 -0.0797 0.0287  -0.0485 247 ASN B CG  
15298 O OD1 . ASN B  221 ? 0.4091 0.6786 0.4831 -0.0752 0.0318  -0.0496 247 ASN B OD1 
15299 N ND2 . ASN B  221 ? 0.4702 0.7360 0.5438 -0.0853 0.0271  -0.0480 247 ASN B ND2 
15306 N N   . LEU B  222 ? 0.2234 0.4436 0.2663 -0.0709 0.0264  -0.0479 248 LEU B N   
15307 C CA  . LEU B  222 ? 0.2213 0.4306 0.2589 -0.0695 0.0231  -0.0471 248 LEU B CA  
15308 C C   . LEU B  222 ? 0.2180 0.4268 0.2579 -0.0626 0.0223  -0.0481 248 LEU B C   
15309 O O   . LEU B  222 ? 0.2142 0.4249 0.2545 -0.0584 0.0257  -0.0497 248 LEU B O   
15310 C CB  . LEU B  222 ? 0.2256 0.4259 0.2540 -0.0715 0.0246  -0.0467 248 LEU B CB  
15311 C CG  . LEU B  222 ? 0.2489 0.4386 0.2716 -0.0728 0.0209  -0.0449 248 LEU B CG  
15312 C CD1 . LEU B  222 ? 0.2508 0.4397 0.2741 -0.0780 0.0182  -0.0424 248 LEU B CD1 
15313 C CD2 . LEU B  222 ? 0.2581 0.4406 0.2721 -0.0740 0.0225  -0.0450 248 LEU B CD2 
15325 N N   . THR B  223 ? 0.2202 0.4264 0.2617 -0.0613 0.0180  -0.0473 249 THR B N   
15326 C CA  . THR B  223 ? 0.2202 0.4252 0.2635 -0.0549 0.0168  -0.0477 249 THR B CA  
15327 C C   . THR B  223 ? 0.2225 0.4151 0.2589 -0.0541 0.0148  -0.0469 249 THR B C   
15328 O O   . THR B  223 ? 0.2266 0.4160 0.2626 -0.0489 0.0149  -0.0474 249 THR B O   
15329 C CB  . THR B  223 ? 0.2382 0.4505 0.2883 -0.0536 0.0136  -0.0474 249 THR B CB  
15330 O OG1 . THR B  223 ? 0.2673 0.4744 0.3153 -0.0577 0.0099  -0.0462 249 THR B OG1 
15331 C CG2 . THR B  223 ? 0.2250 0.4507 0.2824 -0.0547 0.0153  -0.0481 249 THR B CG2 
15339 N N   . LEU B  224 ? 0.2176 0.4034 0.2490 -0.0590 0.0130  -0.0455 250 LEU B N   
15340 C CA  . LEU B  224 ? 0.2160 0.3914 0.2416 -0.0586 0.0111  -0.0445 250 LEU B CA  
15341 C C   . LEU B  224 ? 0.2222 0.3923 0.2411 -0.0633 0.0120  -0.0436 250 LEU B C   
15342 O O   . LEU B  224 ? 0.2284 0.4008 0.2473 -0.0681 0.0120  -0.0425 250 LEU B O   
15343 C CB  . LEU B  224 ? 0.2084 0.3807 0.2353 -0.0588 0.0067  -0.0429 250 LEU B CB  
15344 C CG  . LEU B  224 ? 0.2187 0.3808 0.2403 -0.0583 0.0045  -0.0415 250 LEU B CG  
15345 C CD1 . LEU B  224 ? 0.2238 0.3845 0.2480 -0.0552 0.0014  -0.0408 250 LEU B CD1 
15346 C CD2 . LEU B  224 ? 0.2217 0.3790 0.2389 -0.0637 0.0035  -0.0393 250 LEU B CD2 
15358 N N   . LEU B  225 ? 0.2142 0.3773 0.2274 -0.0622 0.0127  -0.0440 251 LEU B N   
15359 C CA  . LEU B  225 ? 0.2157 0.3737 0.2219 -0.0665 0.0130  -0.0431 251 LEU B CA  
15360 C C   . LEU B  225 ? 0.2303 0.3799 0.2324 -0.0654 0.0105  -0.0422 251 LEU B C   
15361 O O   . LEU B  225 ? 0.2383 0.3850 0.2400 -0.0614 0.0113  -0.0438 251 LEU B O   
15362 C CB  . LEU B  225 ? 0.2151 0.3746 0.2177 -0.0671 0.0175  -0.0454 251 LEU B CB  
15363 C CG  . LEU B  225 ? 0.2475 0.4025 0.2419 -0.0718 0.0179  -0.0446 251 LEU B CG  
15364 C CD1 . LEU B  225 ? 0.2545 0.4111 0.2483 -0.0769 0.0162  -0.0414 251 LEU B CD1 
15365 C CD2 . LEU B  225 ? 0.2533 0.4099 0.2439 -0.0721 0.0227  -0.0474 251 LEU B CD2 
15377 N N   . ASP B  226 ? 0.2220 0.3676 0.2213 -0.0688 0.0076  -0.0394 252 ASP B N   
15378 C CA  . ASP B  226 ? 0.2253 0.3638 0.2212 -0.0682 0.0051  -0.0381 252 ASP B CA  
15379 C C   . ASP B  226 ? 0.2348 0.3704 0.2238 -0.0726 0.0051  -0.0367 252 ASP B C   
15380 O O   . ASP B  226 ? 0.2441 0.3801 0.2323 -0.0762 0.0037  -0.0338 252 ASP B O   
15381 C CB  . ASP B  226 ? 0.2147 0.3515 0.2141 -0.0674 0.0015  -0.0356 252 ASP B CB  
15382 C CG  . ASP B  226 ? 0.2573 0.3875 0.2538 -0.0671 -0.0012 -0.0336 252 ASP B CG  
15383 O OD1 . ASP B  226 ? 0.2474 0.3742 0.2397 -0.0670 -0.0006 -0.0345 252 ASP B OD1 
15384 O OD2 . ASP B  226 ? 0.2557 0.3841 0.2545 -0.0670 -0.0039 -0.0313 252 ASP B OD2 
15389 N N   . LEU B  227 ? 0.2301 0.3628 0.2142 -0.0725 0.0067  -0.0387 253 LEU B N   
15390 C CA  . LEU B  227 ? 0.2390 0.3690 0.2157 -0.0768 0.0065  -0.0378 253 LEU B CA  
15391 C C   . LEU B  227 ? 0.2368 0.3610 0.2108 -0.0763 0.0040  -0.0371 253 LEU B C   
15392 O O   . LEU B  227 ? 0.2451 0.3671 0.2128 -0.0793 0.0040  -0.0374 253 LEU B O   
15393 C CB  . LEU B  227 ? 0.2485 0.3800 0.2208 -0.0779 0.0107  -0.0413 253 LEU B CB  
15394 C CG  . LEU B  227 ? 0.2825 0.4202 0.2559 -0.0797 0.0135  -0.0416 253 LEU B CG  
15395 C CD1 . LEU B  227 ? 0.2912 0.4299 0.2610 -0.0795 0.0183  -0.0456 253 LEU B CD1 
15396 C CD2 . LEU B  227 ? 0.2972 0.4362 0.2673 -0.0850 0.0119  -0.0379 253 LEU B CD2 
15408 N N   . SER B  228 ? 0.2251 0.3470 0.2036 -0.0729 0.0016  -0.0360 254 SER B N   
15409 C CA  . SER B  228 ? 0.2187 0.3355 0.1953 -0.0723 -0.0006 -0.0352 254 SER B CA  
15410 C C   . SER B  228 ? 0.2232 0.3390 0.1963 -0.0764 -0.0035 -0.0315 254 SER B C   
15411 O O   . SER B  228 ? 0.2253 0.3438 0.1988 -0.0787 -0.0045 -0.0286 254 SER B O   
15412 C CB  . SER B  228 ? 0.2119 0.3270 0.1942 -0.0677 -0.0022 -0.0346 254 SER B CB  
15413 O OG  . SER B  228 ? 0.1989 0.3162 0.1853 -0.0677 -0.0043 -0.0318 254 SER B OG  
15419 N N   . GLY B  229 ? 0.2269 0.3392 0.1966 -0.0773 -0.0049 -0.0313 255 GLY B N   
15420 C CA  . GLY B  229 ? 0.2263 0.3386 0.1933 -0.0807 -0.0080 -0.0274 255 GLY B CA  
15421 C C   . GLY B  229 ? 0.2284 0.3435 0.1893 -0.0858 -0.0077 -0.0266 255 GLY B C   
15422 O O   . GLY B  229 ? 0.2322 0.3485 0.1914 -0.0884 -0.0105 -0.0225 255 GLY B O   
15426 N N   . ASN B  230 ? 0.2260 0.3425 0.1835 -0.0870 -0.0043 -0.0302 256 ASN B N   
15427 C CA  . ASN B  230 ? 0.2316 0.3510 0.1824 -0.0918 -0.0035 -0.0298 256 ASN B CA  
15428 C C   . ASN B  230 ? 0.2451 0.3618 0.1895 -0.0939 -0.0024 -0.0335 256 ASN B C   
15429 O O   . ASN B  230 ? 0.2499 0.3640 0.1943 -0.0916 0.0007  -0.0380 256 ASN B O   
15430 C CB  . ASN B  230 ? 0.2345 0.3572 0.1860 -0.0918 -0.0001 -0.0314 256 ASN B CB  
15431 C CG  . ASN B  230 ? 0.2510 0.3761 0.2085 -0.0908 -0.0013 -0.0277 256 ASN B CG  
15432 O OD1 . ASN B  230 ? 0.2699 0.3956 0.2268 -0.0929 -0.0039 -0.0231 256 ASN B OD1 
15433 N ND2 . ASN B  230 ? 0.2417 0.3679 0.2049 -0.0875 0.0005  -0.0295 256 ASN B ND2 
15440 N N   . CYS B  231 ? 0.2559 0.3732 0.1952 -0.0980 -0.0052 -0.0313 257 CYS B N   
15441 C CA  . CYS B  231 ? 0.2729 0.3874 0.2066 -0.1005 -0.0053 -0.0343 257 CYS B CA  
15442 C C   . CYS B  231 ? 0.2807 0.3906 0.2194 -0.0967 -0.0062 -0.0351 257 CYS B C   
15443 O O   . CYS B  231 ? 0.2828 0.3883 0.2210 -0.0949 -0.0033 -0.0396 257 CYS B O   
15444 C CB  . CYS B  231 ? 0.2941 0.4072 0.2215 -0.1022 -0.0008 -0.0400 257 CYS B CB  
15445 S SG  . CYS B  231 ? 0.3625 0.4811 0.2825 -0.1074 0.0003  -0.0391 257 CYS B SG  
15450 N N   . PRO B  232 ? 0.2796 0.3902 0.2230 -0.0954 -0.0099 -0.0304 258 PRO B N   
15451 C CA  . PRO B  232 ? 0.2767 0.3832 0.2253 -0.0915 -0.0106 -0.0308 258 PRO B CA  
15452 C C   . PRO B  232 ? 0.2747 0.3776 0.2200 -0.0934 -0.0110 -0.0331 258 PRO B C   
15453 O O   . PRO B  232 ? 0.2690 0.3734 0.2082 -0.0985 -0.0120 -0.0334 258 PRO B O   
15454 C CB  . PRO B  232 ? 0.2833 0.3920 0.2372 -0.0901 -0.0143 -0.0250 258 PRO B CB  
15455 C CG  . PRO B  232 ? 0.2886 0.4019 0.2383 -0.0947 -0.0164 -0.0214 258 PRO B CG  
15456 C CD  . PRO B  232 ? 0.2681 0.3829 0.2129 -0.0968 -0.0132 -0.0245 258 PRO B CD  
15464 N N   . ARG B  233 ? 0.2667 0.3648 0.2160 -0.0894 -0.0100 -0.0347 259 ARG B N   
15465 C CA  . ARG B  233 ? 0.2706 0.3645 0.2182 -0.0907 -0.0103 -0.0365 259 ARG B CA  
15466 C C   . ARG B  233 ? 0.2585 0.3547 0.2106 -0.0902 -0.0146 -0.0312 259 ARG B C   
15467 O O   . ARG B  233 ? 0.2405 0.3361 0.1989 -0.0856 -0.0152 -0.0290 259 ARG B O   
15468 C CB  . ARG B  233 ? 0.2964 0.3840 0.2462 -0.0861 -0.0067 -0.0404 259 ARG B CB  
15469 C CG  . ARG B  233 ? 0.3416 0.4246 0.2927 -0.0857 -0.0075 -0.0405 259 ARG B CG  
15470 C CD  . ARG B  233 ? 0.3622 0.4383 0.3140 -0.0819 -0.0034 -0.0445 259 ARG B CD  
15471 N NE  . ARG B  233 ? 0.3721 0.4439 0.3256 -0.0815 -0.0043 -0.0438 259 ARG B NE  
15472 C CZ  . ARG B  233 ? 0.3587 0.4234 0.3112 -0.0802 -0.0011 -0.0472 259 ARG B CZ  
15473 N NH1 . ARG B  233 ? 0.2983 0.3589 0.2480 -0.0787 0.0035  -0.0516 259 ARG B NH1 
15474 N NH2 . ARG B  233 ? 0.3568 0.4180 0.3110 -0.0803 -0.0021 -0.0461 259 ARG B NH2 
15488 N N   . CYS B  234 ? 0.2595 0.3587 0.2085 -0.0950 -0.0176 -0.0290 260 CYS B N   
15489 C CA  . CYS B  234 ? 0.2707 0.3735 0.2240 -0.0948 -0.0216 -0.0233 260 CYS B CA  
15490 C C   . CYS B  234 ? 0.2649 0.3656 0.2204 -0.0949 -0.0231 -0.0226 260 CYS B C   
15491 O O   . CYS B  234 ? 0.2613 0.3650 0.2215 -0.0937 -0.0260 -0.0177 260 CYS B O   
15492 C CB  . CYS B  234 ? 0.2899 0.3992 0.2395 -0.0994 -0.0244 -0.0197 260 CYS B CB  
15493 S SG  . CYS B  234 ? 0.3663 0.4787 0.3153 -0.0986 -0.0232 -0.0182 260 CYS B SG  
15498 N N   . PHE B  235 ? 0.2541 0.3499 0.2068 -0.0962 -0.0210 -0.0273 261 PHE B N   
15499 C CA  . PHE B  235 ? 0.2442 0.3381 0.1993 -0.0967 -0.0223 -0.0265 261 PHE B CA  
15500 C C   . PHE B  235 ? 0.2374 0.3293 0.2001 -0.0905 -0.0225 -0.0237 261 PHE B C   
15501 O O   . PHE B  235 ? 0.2398 0.3282 0.2046 -0.0858 -0.0199 -0.0254 261 PHE B O   
15502 C CB  . PHE B  235 ? 0.2460 0.3335 0.1965 -0.0991 -0.0193 -0.0322 261 PHE B CB  
15503 C CG  . PHE B  235 ? 0.2484 0.3336 0.2017 -0.0997 -0.0203 -0.0314 261 PHE B CG  
15504 C CD1 . PHE B  235 ? 0.2516 0.3424 0.2050 -0.1043 -0.0241 -0.0283 261 PHE B CD1 
15505 C CD2 . PHE B  235 ? 0.2568 0.3351 0.2136 -0.0952 -0.0176 -0.0330 261 PHE B CD2 
15506 C CE1 . PHE B  235 ? 0.2578 0.3473 0.2148 -0.1047 -0.0250 -0.0271 261 PHE B CE1 
15507 C CE2 . PHE B  235 ? 0.2596 0.3359 0.2192 -0.0957 -0.0183 -0.0319 261 PHE B CE2 
15508 C CZ  . PHE B  235 ? 0.2571 0.3390 0.2169 -0.1006 -0.0220 -0.0290 261 PHE B CZ  
15518 N N   . ASN B  236 ? 0.2309 0.3260 0.1977 -0.0905 -0.0255 -0.0191 262 ASN B N   
15519 C CA  . ASN B  236 ? 0.2215 0.3151 0.1952 -0.0850 -0.0258 -0.0163 262 ASN B CA  
15520 C C   . ASN B  236 ? 0.2272 0.3215 0.2041 -0.0803 -0.0254 -0.0146 262 ASN B C   
15521 O O   . ASN B  236 ? 0.2287 0.3199 0.2098 -0.0753 -0.0243 -0.0145 262 ASN B O   
15522 C CB  . ASN B  236 ? 0.2284 0.3150 0.2029 -0.0825 -0.0230 -0.0197 262 ASN B CB  
15523 C CG  . ASN B  236 ? 0.2469 0.3326 0.2276 -0.0782 -0.0237 -0.0164 262 ASN B CG  
15524 O OD1 . ASN B  236 ? 0.2419 0.3318 0.2255 -0.0794 -0.0265 -0.0122 262 ASN B OD1 
15525 N ND2 . ASN B  236 ? 0.2615 0.3423 0.2445 -0.0730 -0.0213 -0.0180 262 ASN B ND2 
15532 N N   . ALA B  237 ? 0.2328 0.3312 0.2076 -0.0822 -0.0263 -0.0133 263 ALA B N   
15533 C CA  . ALA B  237 ? 0.2427 0.3416 0.2203 -0.0785 -0.0258 -0.0120 263 ALA B CA  
15534 C C   . ALA B  237 ? 0.2398 0.3399 0.2232 -0.0754 -0.0278 -0.0070 263 ALA B C   
15535 O O   . ALA B  237 ? 0.2301 0.3339 0.2143 -0.0775 -0.0304 -0.0029 263 ALA B O   
15536 C CB  . ALA B  237 ? 0.2483 0.3511 0.2222 -0.0817 -0.0261 -0.0113 263 ALA B CB  
15542 N N   . PRO B  238 ? 0.2491 0.3467 0.2364 -0.0706 -0.0267 -0.0070 264 PRO B N   
15543 C CA  . PRO B  238 ? 0.2564 0.3547 0.2488 -0.0677 -0.0282 -0.0025 264 PRO B CA  
15544 C C   . PRO B  238 ? 0.2691 0.3702 0.2620 -0.0682 -0.0291 0.0009  264 PRO B C   
15545 O O   . PRO B  238 ? 0.2736 0.3737 0.2704 -0.0651 -0.0293 0.0034  264 PRO B O   
15546 C CB  . PRO B  238 ? 0.2639 0.3581 0.2592 -0.0627 -0.0263 -0.0048 264 PRO B CB  
15547 C CG  . PRO B  238 ? 0.2660 0.3592 0.2585 -0.0628 -0.0241 -0.0092 264 PRO B CG  
15548 C CD  . PRO B  238 ? 0.2463 0.3408 0.2338 -0.0676 -0.0239 -0.0111 264 PRO B CD  
15556 N N   . PHE B  239 ? 0.2698 0.3739 0.2586 -0.0722 -0.0295 0.0009  265 PHE B N   
15557 C CA  . PHE B  239 ? 0.2727 0.3794 0.2614 -0.0732 -0.0302 0.0044  265 PHE B CA  
15558 C C   . PHE B  239 ? 0.2861 0.3974 0.2699 -0.0783 -0.0315 0.0057  265 PHE B C   
15559 O O   . PHE B  239 ? 0.2834 0.3950 0.2633 -0.0811 -0.0313 0.0024  265 PHE B O   
15560 C CB  . PHE B  239 ? 0.2735 0.3784 0.2623 -0.0718 -0.0279 0.0016  265 PHE B CB  
15561 C CG  . PHE B  239 ? 0.2920 0.3965 0.2768 -0.0733 -0.0259 -0.0037 265 PHE B CG  
15562 C CD1 . PHE B  239 ? 0.3138 0.4152 0.2996 -0.0708 -0.0243 -0.0078 265 PHE B CD1 
15563 C CD2 . PHE B  239 ? 0.2996 0.4069 0.2798 -0.0772 -0.0254 -0.0044 265 PHE B CD2 
15564 C CE1 . PHE B  239 ? 0.3216 0.4224 0.3040 -0.0718 -0.0220 -0.0125 265 PHE B CE1 
15565 C CE2 . PHE B  239 ? 0.3162 0.4229 0.2927 -0.0784 -0.0231 -0.0094 265 PHE B CE2 
15566 C CZ  . PHE B  239 ? 0.3169 0.4202 0.2947 -0.0755 -0.0214 -0.0134 265 PHE B CZ  
15576 N N   . PRO B  240 ? 0.2966 0.4112 0.2800 -0.0798 -0.0328 0.0104  266 PRO B N   
15577 C CA  . PRO B  240 ? 0.3082 0.4278 0.2863 -0.0847 -0.0342 0.0117  266 PRO B CA  
15578 C C   . PRO B  240 ? 0.3264 0.4453 0.2991 -0.0872 -0.0319 0.0065  266 PRO B C   
15579 O O   . PRO B  240 ? 0.3335 0.4506 0.3067 -0.0858 -0.0299 0.0053  266 PRO B O   
15580 C CB  . PRO B  240 ? 0.3124 0.4347 0.2920 -0.0845 -0.0355 0.0182  266 PRO B CB  
15581 C CG  . PRO B  240 ? 0.3127 0.4316 0.2988 -0.0797 -0.0353 0.0206  266 PRO B CG  
15582 C CD  . PRO B  240 ? 0.2927 0.4065 0.2802 -0.0771 -0.0329 0.0148  266 PRO B CD  
15590 N N   . CYS B  241 ? 0.3358 0.4556 0.3037 -0.0906 -0.0319 0.0031  267 CYS B N   
15591 C CA  . CYS B  241 ? 0.3462 0.4646 0.3090 -0.0925 -0.0292 -0.0026 267 CYS B CA  
15592 C C   . CYS B  241 ? 0.3547 0.4776 0.3103 -0.0982 -0.0302 -0.0025 267 CYS B C   
15593 O O   . CYS B  241 ? 0.3457 0.4711 0.2991 -0.1012 -0.0324 -0.0017 267 CYS B O   
15594 C CB  . CYS B  241 ? 0.3543 0.4680 0.3177 -0.0909 -0.0275 -0.0077 267 CYS B CB  
15595 S SG  . CYS B  241 ? 0.3765 0.4869 0.3356 -0.0912 -0.0232 -0.0149 267 CYS B SG  
15600 N N   . VAL B  242 ? 0.3684 0.4926 0.3200 -0.1000 -0.0284 -0.0036 268 VAL B N   
15601 C CA  . VAL B  242 ? 0.3866 0.5150 0.3304 -0.1055 -0.0289 -0.0038 268 VAL B CA  
15602 C C   . VAL B  242 ? 0.3808 0.5062 0.3196 -0.1068 -0.0251 -0.0109 268 VAL B C   
15603 O O   . VAL B  242 ? 0.3815 0.5055 0.3211 -0.1049 -0.0222 -0.0126 268 VAL B O   
15604 C CB  . VAL B  242 ? 0.4140 0.5467 0.3566 -0.1066 -0.0296 0.0014  268 VAL B CB  
15605 C CG1 . VAL B  242 ? 0.4263 0.5637 0.3600 -0.1124 -0.0300 0.0010  268 VAL B CG1 
15606 C CG2 . VAL B  242 ? 0.4250 0.5601 0.3729 -0.1047 -0.0329 0.0087  268 VAL B CG2 
15616 N N   . PRO B  243 ? 0.3769 0.5012 0.3107 -0.1099 -0.0247 -0.0151 269 PRO B N   
15617 C CA  . PRO B  243 ? 0.3762 0.4969 0.3052 -0.1108 -0.0205 -0.0219 269 PRO B CA  
15618 C C   . PRO B  243 ? 0.3774 0.5019 0.2990 -0.1150 -0.0194 -0.0225 269 PRO B C   
15619 O O   . PRO B  243 ? 0.3725 0.5026 0.2909 -0.1184 -0.0223 -0.0180 269 PRO B O   
15620 C CB  . PRO B  243 ? 0.3875 0.5053 0.3133 -0.1133 -0.0207 -0.0258 269 PRO B CB  
15621 C CG  . PRO B  243 ? 0.3966 0.5194 0.3223 -0.1164 -0.0254 -0.0210 269 PRO B CG  
15622 C CD  . PRO B  243 ? 0.3738 0.5001 0.3060 -0.1131 -0.0279 -0.0140 269 PRO B CD  
15630 N N   . CYS B  244 ? 0.3778 0.4995 0.2962 -0.1147 -0.0149 -0.0279 270 CYS B N   
15631 C CA  . CYS B  244 ? 0.3866 0.5113 0.2968 -0.1190 -0.0131 -0.0295 270 CYS B CA  
15632 C C   . CYS B  244 ? 0.4069 0.5327 0.3088 -0.1249 -0.0146 -0.0316 270 CYS B C   
15633 O O   . CYS B  244 ? 0.4069 0.5296 0.3097 -0.1252 -0.0157 -0.0335 270 CYS B O   
15634 C CB  . CYS B  244 ? 0.3747 0.4961 0.2842 -0.1169 -0.0077 -0.0349 270 CYS B CB  
15635 S SG  . CYS B  244 ? 0.3793 0.5026 0.2963 -0.1123 -0.0062 -0.0318 270 CYS B SG  
15640 N N   . ASP B  245 ? 0.4244 0.5552 0.3183 -0.1300 -0.0151 -0.0308 271 ASP B N   
15641 C CA  . ASP B  245 ? 0.4504 0.5835 0.3359 -0.1363 -0.0171 -0.0324 271 ASP B CA  
15642 C C   . ASP B  245 ? 0.4593 0.5855 0.3413 -0.1376 -0.0142 -0.0402 271 ASP B C   
15643 O O   . ASP B  245 ? 0.4589 0.5800 0.3394 -0.1357 -0.0091 -0.0456 271 ASP B O   
15644 C CB  . ASP B  245 ? 0.4964 0.6353 0.3728 -0.1413 -0.0170 -0.0315 271 ASP B CB  
15645 C CG  . ASP B  245 ? 0.5866 0.7328 0.4651 -0.1413 -0.0208 -0.0229 271 ASP B CG  
15646 O OD1 . ASP B  245 ? 0.6048 0.7515 0.4920 -0.1375 -0.0236 -0.0177 271 ASP B OD1 
15647 O OD2 . ASP B  245 ? 0.6266 0.7777 0.4981 -0.1449 -0.0206 -0.0213 271 ASP B OD2 
15652 N N   . GLY B  246 ? 0.4665 0.5924 0.3485 -0.1400 -0.0172 -0.0403 272 GLY B N   
15653 C CA  . GLY B  246 ? 0.4787 0.5974 0.3581 -0.1414 -0.0147 -0.0471 272 GLY B CA  
15654 C C   . GLY B  246 ? 0.4788 0.5896 0.3661 -0.1347 -0.0116 -0.0493 272 GLY B C   
15655 O O   . GLY B  246 ? 0.4908 0.5941 0.3757 -0.1346 -0.0076 -0.0555 272 GLY B O   
15659 N N   . GLY B  247 ? 0.4600 0.5722 0.3565 -0.1291 -0.0131 -0.0442 273 GLY B N   
15660 C CA  . GLY B  247 ? 0.4492 0.5552 0.3534 -0.1224 -0.0104 -0.0456 273 GLY B CA  
15661 C C   . GLY B  247 ? 0.4363 0.5382 0.3388 -0.1198 -0.0047 -0.0506 273 GLY B C   
15662 O O   . GLY B  247 ? 0.4328 0.5283 0.3389 -0.1154 -0.0015 -0.0538 273 GLY B O   
15666 N N   . ALA B  248 ? 0.4248 0.5304 0.3217 -0.1223 -0.0032 -0.0511 274 ALA B N   
15667 C CA  . ALA B  248 ? 0.4137 0.5166 0.3084 -0.1204 0.0025  -0.0558 274 ALA B CA  
15668 C C   . ALA B  248 ? 0.3912 0.4931 0.2950 -0.1132 0.0044  -0.0546 274 ALA B C   
15669 O O   . ALA B  248 ? 0.3737 0.4787 0.2846 -0.1105 0.0012  -0.0495 274 ALA B O   
15670 C CB  . ALA B  248 ? 0.4149 0.5234 0.3024 -0.1247 0.0031  -0.0553 274 ALA B CB  
15676 N N   . SER B  249 ? 0.3839 0.4818 0.2874 -0.1104 0.0098  -0.0596 275 SER B N   
15677 C CA  . SER B  249 ? 0.3853 0.4831 0.2967 -0.1039 0.0123  -0.0593 275 SER B CA  
15678 C C   . SER B  249 ? 0.3754 0.4801 0.2882 -0.1041 0.0122  -0.0562 275 SER B C   
15679 O O   . SER B  249 ? 0.3748 0.4831 0.2809 -0.1089 0.0122  -0.0559 275 SER B O   
15680 C CB  . SER B  249 ? 0.4108 0.5029 0.3203 -0.1014 0.0185  -0.0655 275 SER B CB  
15681 O OG  . SER B  249 ? 0.4426 0.5356 0.3599 -0.0951 0.0210  -0.0653 275 SER B OG  
15687 N N   . ILE B  250 ? 0.3625 0.4691 0.2839 -0.0989 0.0127  -0.0543 276 ILE B N   
15688 C CA  . ILE B  250 ? 0.3560 0.4686 0.2793 -0.0988 0.0138  -0.0523 276 ILE B CA  
15689 C C   . ILE B  250 ? 0.3586 0.4706 0.2767 -0.0993 0.0196  -0.0575 276 ILE B C   
15690 O O   . ILE B  250 ? 0.3589 0.4657 0.2765 -0.0968 0.0231  -0.0621 276 ILE B O   
15691 C CB  . ILE B  250 ? 0.3514 0.4658 0.2848 -0.0933 0.0133  -0.0501 276 ILE B CB  
15692 C CG1 . ILE B  250 ? 0.3576 0.4784 0.2931 -0.0944 0.0135  -0.0472 276 ILE B CG1 
15693 C CG2 . ILE B  250 ? 0.3559 0.4673 0.2932 -0.0879 0.0175  -0.0543 276 ILE B CG2 
15694 C CD1 . ILE B  250 ? 0.3608 0.4840 0.3061 -0.0900 0.0125  -0.0449 276 ILE B CD1 
15706 N N   . ASN B  251 ? 0.3561 0.4730 0.2702 -0.1026 0.0209  -0.0568 277 ASN B N   
15707 C CA  . ASN B  251 ? 0.3583 0.4752 0.2671 -0.1035 0.0266  -0.0615 277 ASN B CA  
15708 C C   . ASN B  251 ? 0.3471 0.4687 0.2628 -0.0997 0.0296  -0.0610 277 ASN B C   
15709 O O   . ASN B  251 ? 0.3463 0.4736 0.2631 -0.1016 0.0284  -0.0574 277 ASN B O   
15710 C CB  . ASN B  251 ? 0.3761 0.4957 0.2748 -0.1101 0.0262  -0.0611 277 ASN B CB  
15711 C CG  . ASN B  251 ? 0.4330 0.5522 0.3247 -0.1116 0.0322  -0.0663 277 ASN B CG  
15712 O OD1 . ASN B  251 ? 0.4483 0.5663 0.3436 -0.1073 0.0372  -0.0697 277 ASN B OD1 
15713 N ND2 . ASN B  251 ? 0.4492 0.5698 0.3306 -0.1176 0.0321  -0.0669 277 ASN B ND2 
15720 N N   . ILE B  252 ? 0.3452 0.4647 0.2661 -0.0943 0.0332  -0.0642 278 ILE B N   
15721 C CA  . ILE B  252 ? 0.3474 0.4724 0.2758 -0.0906 0.0360  -0.0638 278 ILE B CA  
15722 C C   . ILE B  252 ? 0.3588 0.4843 0.2830 -0.0903 0.0426  -0.0685 278 ILE B C   
15723 O O   . ILE B  252 ? 0.3700 0.4899 0.2920 -0.0880 0.0462  -0.0729 278 ILE B O   
15724 C CB  . ILE B  252 ? 0.3463 0.4706 0.2847 -0.0841 0.0351  -0.0632 278 ILE B CB  
15725 C CG1 . ILE B  252 ? 0.3563 0.4806 0.2989 -0.0843 0.0289  -0.0586 278 ILE B CG1 
15726 C CG2 . ILE B  252 ? 0.3434 0.4744 0.2891 -0.0805 0.0383  -0.0633 278 ILE B CG2 
15727 C CD1 . ILE B  252 ? 0.3658 0.4869 0.3155 -0.0785 0.0276  -0.0585 278 ILE B CD1 
15739 N N   . ASP B  253 ? 0.3538 0.4859 0.2774 -0.0925 0.0447  -0.0675 279 ASP B N   
15740 C CA  . ASP B  253 ? 0.3638 0.4972 0.2837 -0.0923 0.0513  -0.0716 279 ASP B CA  
15741 C C   . ASP B  253 ? 0.3650 0.4980 0.2925 -0.0853 0.0556  -0.0744 279 ASP B C   
15742 O O   . ASP B  253 ? 0.3506 0.4867 0.2879 -0.0811 0.0534  -0.0719 279 ASP B O   
15743 C CB  . ASP B  253 ? 0.3892 0.5305 0.3088 -0.0955 0.0525  -0.0692 279 ASP B CB  
15744 C CG  . ASP B  253 ? 0.4641 0.6072 0.3790 -0.0958 0.0595  -0.0734 279 ASP B CG  
15745 O OD1 . ASP B  253 ? 0.4866 0.6263 0.3907 -0.1001 0.0612  -0.0759 279 ASP B OD1 
15746 O OD2 . ASP B  253 ? 0.4817 0.6295 0.4038 -0.0917 0.0635  -0.0743 279 ASP B OD2 
15751 N N   . ARG B  254 ? 0.3781 0.5072 0.3010 -0.0839 0.0616  -0.0795 280 ARG B N   
15752 C CA  . ARG B  254 ? 0.3964 0.5248 0.3255 -0.0770 0.0667  -0.0824 280 ARG B CA  
15753 C C   . ARG B  254 ? 0.3923 0.5309 0.3325 -0.0731 0.0674  -0.0796 280 ARG B C   
15754 O O   . ARG B  254 ? 0.3892 0.5288 0.3381 -0.0670 0.0677  -0.0792 280 ARG B O   
15755 C CB  . ARG B  254 ? 0.4407 0.5644 0.3614 -0.0774 0.0740  -0.0882 280 ARG B CB  
15756 C CG  . ARG B  254 ? 0.5224 0.6495 0.4483 -0.0716 0.0812  -0.0907 280 ARG B CG  
15757 C CD  . ARG B  254 ? 0.5973 0.7202 0.5304 -0.0641 0.0827  -0.0915 280 ARG B CD  
15758 N NE  . ARG B  254 ? 0.6624 0.7897 0.6018 -0.0579 0.0894  -0.0932 280 ARG B NE  
15759 C CZ  . ARG B  254 ? 0.6880 0.8261 0.6382 -0.0543 0.0892  -0.0900 280 ARG B CZ  
15760 N NH1 . ARG B  254 ? 0.6887 0.8337 0.6443 -0.0564 0.0828  -0.0854 280 ARG B NH1 
15761 N NH2 . ARG B  254 ? 0.6754 0.8176 0.6310 -0.0485 0.0955  -0.0916 280 ARG B NH2 
15775 N N   . PHE B  255 ? 0.3850 0.5313 0.3251 -0.0771 0.0671  -0.0773 281 PHE B N   
15776 C CA  . PHE B  255 ? 0.3830 0.5396 0.3331 -0.0748 0.0679  -0.0749 281 PHE B CA  
15777 C C   . PHE B  255 ? 0.3592 0.5204 0.3153 -0.0766 0.0614  -0.0697 281 PHE B C   
15778 O O   . PHE B  255 ? 0.3474 0.5172 0.3111 -0.0759 0.0618  -0.0678 281 PHE B O   
15779 C CB  . PHE B  255 ? 0.3979 0.5602 0.3442 -0.0779 0.0729  -0.0760 281 PHE B CB  
15780 C CG  . PHE B  255 ? 0.4320 0.5912 0.3737 -0.0754 0.0803  -0.0812 281 PHE B CG  
15781 C CD1 . PHE B  255 ? 0.4511 0.6106 0.3999 -0.0682 0.0843  -0.0833 281 PHE B CD1 
15782 C CD2 . PHE B  255 ? 0.4531 0.6094 0.3834 -0.0802 0.0837  -0.0839 281 PHE B CD2 
15783 C CE1 . PHE B  255 ? 0.4627 0.6192 0.4077 -0.0656 0.0918  -0.0879 281 PHE B CE1 
15784 C CE2 . PHE B  255 ? 0.4699 0.6232 0.3960 -0.0779 0.0911  -0.0890 281 PHE B CE2 
15785 C CZ  . PHE B  255 ? 0.4658 0.6185 0.3992 -0.0705 0.0951  -0.0910 281 PHE B CZ  
15795 N N   . ALA B  256 ? 0.3526 0.5083 0.3059 -0.0789 0.0557  -0.0676 282 ALA B N   
15796 C CA  . ALA B  256 ? 0.3501 0.5089 0.3085 -0.0806 0.0499  -0.0628 282 ALA B CA  
15797 C C   . ALA B  256 ? 0.3317 0.4961 0.3017 -0.0759 0.0487  -0.0613 282 ALA B C   
15798 O O   . ALA B  256 ? 0.3262 0.4957 0.3009 -0.0780 0.0458  -0.0580 282 ALA B O   
15799 C CB  . ALA B  256 ? 0.3612 0.5127 0.3153 -0.0824 0.0446  -0.0612 282 ALA B CB  
15805 N N   . PHE B  257 ? 0.3276 0.4910 0.3022 -0.0698 0.0506  -0.0636 283 PHE B N   
15806 C CA  . PHE B  257 ? 0.3248 0.4942 0.3103 -0.0652 0.0491  -0.0621 283 PHE B CA  
15807 C C   . PHE B  257 ? 0.3300 0.5067 0.3213 -0.0609 0.0546  -0.0642 283 PHE B C   
15808 O O   . PHE B  257 ? 0.3218 0.5031 0.3217 -0.0558 0.0542  -0.0637 283 PHE B O   
15809 C CB  . PHE B  257 ? 0.3265 0.4894 0.3136 -0.0610 0.0461  -0.0621 283 PHE B CB  
15810 C CG  . PHE B  257 ? 0.3363 0.4911 0.3174 -0.0644 0.0413  -0.0605 283 PHE B CG  
15811 C CD1 . PHE B  257 ? 0.3486 0.5047 0.3282 -0.0696 0.0374  -0.0573 283 PHE B CD1 
15812 C CD2 . PHE B  257 ? 0.3464 0.4928 0.3244 -0.0620 0.0407  -0.0619 283 PHE B CD2 
15813 C CE1 . PHE B  257 ? 0.3623 0.5120 0.3374 -0.0721 0.0330  -0.0555 283 PHE B CE1 
15814 C CE2 . PHE B  257 ? 0.3596 0.4998 0.3331 -0.0650 0.0362  -0.0602 283 PHE B CE2 
15815 C CZ  . PHE B  257 ? 0.3606 0.5028 0.3329 -0.0699 0.0324  -0.0569 283 PHE B CZ  
15825 N N   . GLN B  258 ? 0.3368 0.5157 0.3240 -0.0629 0.0599  -0.0663 284 GLN B N   
15826 C CA  . GLN B  258 ? 0.3499 0.5357 0.3424 -0.0585 0.0657  -0.0682 284 GLN B CA  
15827 C C   . GLN B  258 ? 0.3492 0.5475 0.3530 -0.0573 0.0649  -0.0659 284 GLN B C   
15828 O O   . GLN B  258 ? 0.3543 0.5589 0.3653 -0.0519 0.0683  -0.0668 284 GLN B O   
15829 C CB  . GLN B  258 ? 0.3813 0.5666 0.3663 -0.0613 0.0717  -0.0710 284 GLN B CB  
15830 C CG  . GLN B  258 ? 0.4400 0.6319 0.4237 -0.0676 0.0715  -0.0690 284 GLN B CG  
15831 C CD  . GLN B  258 ? 0.5072 0.6978 0.4821 -0.0705 0.0772  -0.0717 284 GLN B CD  
15832 O OE1 . GLN B  258 ? 0.5226 0.7105 0.4952 -0.0669 0.0828  -0.0755 284 GLN B OE1 
15833 N NE2 . GLN B  258 ? 0.5218 0.7139 0.4913 -0.0771 0.0762  -0.0698 284 GLN B NE2 
15842 N N   . ASN B  259 ? 0.3434 0.5453 0.3485 -0.0625 0.0607  -0.0629 285 ASN B N   
15843 C CA  . ASN B  259 ? 0.3466 0.5601 0.3619 -0.0626 0.0596  -0.0608 285 ASN B CA  
15844 C C   . ASN B  259 ? 0.3290 0.5425 0.3499 -0.0613 0.0534  -0.0585 285 ASN B C   
15845 O O   . ASN B  259 ? 0.3232 0.5456 0.3518 -0.0624 0.0517  -0.0569 285 ASN B O   
15846 C CB  . ASN B  259 ? 0.3847 0.6023 0.3979 -0.0696 0.0598  -0.0591 285 ASN B CB  
15847 C CG  . ASN B  259 ? 0.4706 0.6899 0.4788 -0.0714 0.0660  -0.0610 285 ASN B CG  
15848 O OD1 . ASN B  259 ? 0.4971 0.7213 0.5087 -0.0671 0.0712  -0.0633 285 ASN B OD1 
15849 N ND2 . ASN B  259 ? 0.5038 0.7196 0.5037 -0.0776 0.0658  -0.0599 285 ASN B ND2 
15856 N N   . LEU B  260 ? 0.3123 0.5164 0.3296 -0.0593 0.0502  -0.0586 286 LEU B N   
15857 C CA  . LEU B  260 ? 0.2984 0.5020 0.3204 -0.0579 0.0446  -0.0565 286 LEU B CA  
15858 C C   . LEU B  260 ? 0.2738 0.4819 0.3033 -0.0505 0.0453  -0.0572 286 LEU B C   
15859 O O   . LEU B  260 ? 0.2804 0.4821 0.3091 -0.0468 0.0432  -0.0572 286 LEU B O   
15860 C CB  . LEU B  260 ? 0.3089 0.5008 0.3234 -0.0596 0.0407  -0.0557 286 LEU B CB  
15861 C CG  . LEU B  260 ? 0.3393 0.5270 0.3465 -0.0666 0.0393  -0.0542 286 LEU B CG  
15862 C CD1 . LEU B  260 ? 0.3541 0.5317 0.3554 -0.0676 0.0352  -0.0532 286 LEU B CD1 
15863 C CD2 . LEU B  260 ? 0.3489 0.5432 0.3607 -0.0709 0.0371  -0.0517 286 LEU B CD2 
15875 N N   . THR B  261 ? 0.2465 0.4660 0.2836 -0.0486 0.0482  -0.0575 287 THR B N   
15876 C CA  . THR B  261 ? 0.2470 0.4731 0.2921 -0.0414 0.0496  -0.0577 287 THR B CA  
15877 C C   . THR B  261 ? 0.2248 0.4536 0.2756 -0.0393 0.0440  -0.0558 287 THR B C   
15878 O O   . THR B  261 ? 0.2202 0.4505 0.2752 -0.0327 0.0442  -0.0556 287 THR B O   
15879 C CB  . THR B  261 ? 0.2803 0.5199 0.3327 -0.0407 0.0538  -0.0581 287 THR B CB  
15880 O OG1 . THR B  261 ? 0.3201 0.5569 0.3666 -0.0424 0.0594  -0.0601 287 THR B OG1 
15881 C CG2 . THR B  261 ? 0.3009 0.5486 0.3621 -0.0329 0.0554  -0.0579 287 THR B CG2 
15889 N N   . GLN B  262 ? 0.2151 0.4443 0.2659 -0.0447 0.0394  -0.0542 288 GLN B N   
15890 C CA  . GLN B  262 ? 0.2155 0.4473 0.2712 -0.0435 0.0342  -0.0527 288 GLN B CA  
15891 C C   . GLN B  262 ? 0.2225 0.4421 0.2722 -0.0434 0.0302  -0.0520 288 GLN B C   
15892 O O   . GLN B  262 ? 0.2255 0.4463 0.2781 -0.0428 0.0259  -0.0508 288 GLN B O   
15893 C CB  . GLN B  262 ? 0.2258 0.4661 0.2861 -0.0493 0.0318  -0.0517 288 GLN B CB  
15894 C CG  . GLN B  262 ? 0.2264 0.4801 0.2935 -0.0497 0.0356  -0.0522 288 GLN B CG  
15895 C CD  . GLN B  262 ? 0.2684 0.5309 0.3429 -0.0421 0.0373  -0.0524 288 GLN B CD  
15896 O OE1 . GLN B  262 ? 0.3037 0.5688 0.3792 -0.0383 0.0424  -0.0534 288 GLN B OE1 
15897 N NE2 . GLN B  262 ? 0.2631 0.5300 0.3427 -0.0397 0.0332  -0.0514 288 GLN B NE2 
15906 N N   . LEU B  263 ? 0.2279 0.4365 0.2694 -0.0439 0.0317  -0.0528 289 LEU B N   
15907 C CA  . LEU B  263 ? 0.2380 0.4357 0.2742 -0.0441 0.0281  -0.0520 289 LEU B CA  
15908 C C   . LEU B  263 ? 0.2234 0.4199 0.2627 -0.0374 0.0267  -0.0516 289 LEU B C   
15909 O O   . LEU B  263 ? 0.2168 0.4148 0.2582 -0.0319 0.0302  -0.0526 289 LEU B O   
15910 C CB  . LEU B  263 ? 0.2570 0.4442 0.2838 -0.0464 0.0300  -0.0530 289 LEU B CB  
15911 C CG  . LEU B  263 ? 0.2942 0.4723 0.3151 -0.0503 0.0259  -0.0515 289 LEU B CG  
15912 C CD1 . LEU B  263 ? 0.3031 0.4840 0.3237 -0.0567 0.0239  -0.0498 289 LEU B CD1 
15913 C CD2 . LEU B  263 ? 0.3111 0.4797 0.3235 -0.0513 0.0277  -0.0528 289 LEU B CD2 
15925 N N   . ARG B  264 ? 0.2281 0.4228 0.2684 -0.0377 0.0219  -0.0500 290 ARG B N   
15926 C CA  . ARG B  264 ? 0.2230 0.4158 0.2654 -0.0321 0.0199  -0.0492 290 ARG B CA  
15927 C C   . ARG B  264 ? 0.2220 0.4023 0.2576 -0.0330 0.0177  -0.0486 290 ARG B C   
15928 O O   . ARG B  264 ? 0.2303 0.4059 0.2653 -0.0282 0.0178  -0.0484 290 ARG B O   
15929 C CB  . ARG B  264 ? 0.2440 0.4453 0.2928 -0.0318 0.0159  -0.0479 290 ARG B CB  
15930 C CG  . ARG B  264 ? 0.2742 0.4880 0.3311 -0.0271 0.0173  -0.0479 290 ARG B CG  
15931 C CD  . ARG B  264 ? 0.2903 0.5134 0.3507 -0.0304 0.0200  -0.0488 290 ARG B CD  
15932 N NE  . ARG B  264 ? 0.3085 0.5448 0.3773 -0.0261 0.0214  -0.0486 290 ARG B NE  
15933 C CZ  . ARG B  264 ? 0.3194 0.5663 0.3931 -0.0279 0.0239  -0.0492 290 ARG B CZ  
15934 N NH1 . ARG B  264 ? 0.2965 0.5418 0.3671 -0.0341 0.0255  -0.0500 290 ARG B NH1 
15935 N NH2 . ARG B  264 ? 0.2930 0.5528 0.3751 -0.0235 0.0249  -0.0486 290 ARG B NH2 
15949 N N   . TYR B  265 ? 0.2150 0.3905 0.2460 -0.0390 0.0156  -0.0480 291 TYR B N   
15950 C CA  . TYR B  265 ? 0.2191 0.3841 0.2444 -0.0402 0.0133  -0.0470 291 TYR B CA  
15951 C C   . TYR B  265 ? 0.2136 0.3729 0.2321 -0.0448 0.0148  -0.0476 291 TYR B C   
15952 O O   . TYR B  265 ? 0.2179 0.3805 0.2358 -0.0495 0.0151  -0.0473 291 TYR B O   
15953 C CB  . TYR B  265 ? 0.2277 0.3925 0.2542 -0.0429 0.0087  -0.0451 291 TYR B CB  
15954 C CG  . TYR B  265 ? 0.2547 0.4250 0.2870 -0.0390 0.0065  -0.0446 291 TYR B CG  
15955 C CD1 . TYR B  265 ? 0.2655 0.4464 0.3038 -0.0390 0.0066  -0.0450 291 TYR B CD1 
15956 C CD2 . TYR B  265 ? 0.2791 0.4442 0.3106 -0.0357 0.0042  -0.0435 291 TYR B CD2 
15957 C CE1 . TYR B  265 ? 0.2831 0.4699 0.3264 -0.0357 0.0043  -0.0446 291 TYR B CE1 
15958 C CE2 . TYR B  265 ? 0.2945 0.4649 0.3307 -0.0321 0.0022  -0.0430 291 TYR B CE2 
15959 C CZ  . TYR B  265 ? 0.3049 0.4863 0.3468 -0.0321 0.0022  -0.0436 291 TYR B CZ  
15960 O OH  . TYR B  265 ? 0.3446 0.5322 0.3909 -0.0289 -0.0002 -0.0430 291 TYR B OH  
15970 N N   . LEU B  266 ? 0.2032 0.3539 0.2164 -0.0438 0.0157  -0.0483 292 LEU B N   
15971 C CA  . LEU B  266 ? 0.2100 0.3553 0.2160 -0.0484 0.0167  -0.0488 292 LEU B CA  
15972 C C   . LEU B  266 ? 0.2189 0.3555 0.2207 -0.0489 0.0140  -0.0477 292 LEU B C   
15973 O O   . LEU B  266 ? 0.2262 0.3585 0.2282 -0.0449 0.0144  -0.0483 292 LEU B O   
15974 C CB  . LEU B  266 ? 0.2158 0.3602 0.2189 -0.0471 0.0219  -0.0518 292 LEU B CB  
15975 C CG  . LEU B  266 ? 0.2296 0.3683 0.2242 -0.0519 0.0232  -0.0530 292 LEU B CG  
15976 C CD1 . LEU B  266 ? 0.2405 0.3829 0.2333 -0.0579 0.0218  -0.0513 292 LEU B CD1 
15977 C CD2 . LEU B  266 ? 0.2306 0.3682 0.2226 -0.0502 0.0288  -0.0564 292 LEU B CD2 
15989 N N   . ASN B  267 ? 0.2192 0.3536 0.2177 -0.0538 0.0113  -0.0458 293 ASN B N   
15990 C CA  . ASN B  267 ? 0.2206 0.3478 0.2155 -0.0547 0.0085  -0.0443 293 ASN B CA  
15991 C C   . ASN B  267 ? 0.2253 0.3487 0.2129 -0.0593 0.0093  -0.0448 293 ASN B C   
15992 O O   . ASN B  267 ? 0.2331 0.3585 0.2184 -0.0638 0.0084  -0.0433 293 ASN B O   
15993 C CB  . ASN B  267 ? 0.2183 0.3460 0.2159 -0.0558 0.0044  -0.0411 293 ASN B CB  
15994 C CG  . ASN B  267 ? 0.2313 0.3528 0.2275 -0.0549 0.0017  -0.0395 293 ASN B CG  
15995 O OD1 . ASN B  267 ? 0.2379 0.3544 0.2301 -0.0550 0.0024  -0.0404 293 ASN B OD1 
15996 N ND2 . ASN B  267 ? 0.2401 0.3615 0.2391 -0.0545 -0.0015 -0.0371 293 ASN B ND2 
16002 N N   . LEU B  268 ? 0.2210 0.3388 0.2047 -0.0584 0.0110  -0.0468 294 LEU B N   
16003 C CA  . LEU B  268 ? 0.2264 0.3402 0.2025 -0.0629 0.0115  -0.0477 294 LEU B CA  
16004 C C   . LEU B  268 ? 0.2219 0.3293 0.1958 -0.0632 0.0089  -0.0466 294 LEU B C   
16005 O O   . LEU B  268 ? 0.2260 0.3288 0.1942 -0.0655 0.0100  -0.0485 294 LEU B O   
16006 C CB  . LEU B  268 ? 0.2332 0.3458 0.2057 -0.0625 0.0166  -0.0518 294 LEU B CB  
16007 C CG  . LEU B  268 ? 0.2640 0.3833 0.2378 -0.0630 0.0196  -0.0529 294 LEU B CG  
16008 C CD1 . LEU B  268 ? 0.2769 0.3948 0.2490 -0.0604 0.0251  -0.0571 294 LEU B CD1 
16009 C CD2 . LEU B  268 ? 0.2734 0.3950 0.2420 -0.0692 0.0187  -0.0517 294 LEU B CD2 
16021 N N   . SER B  269 ? 0.2062 0.3135 0.1846 -0.0613 0.0054  -0.0436 295 SER B N   
16022 C CA  . SER B  269 ? 0.2119 0.3141 0.1890 -0.0616 0.0029  -0.0422 295 SER B CA  
16023 C C   . SER B  269 ? 0.2284 0.3304 0.2004 -0.0673 0.0007  -0.0404 295 SER B C   
16024 O O   . SER B  269 ? 0.2328 0.3388 0.2044 -0.0701 -0.0005 -0.0384 295 SER B O   
16025 C CB  . SER B  269 ? 0.2284 0.3311 0.2111 -0.0585 -0.0001 -0.0393 295 SER B CB  
16026 O OG  . SER B  269 ? 0.2559 0.3595 0.2431 -0.0531 0.0015  -0.0406 295 SER B OG  
16032 N N   . SER B  270 ? 0.2260 0.3234 0.1941 -0.0691 0.0001  -0.0410 296 SER B N   
16033 C CA  . SER B  270 ? 0.2263 0.3242 0.1897 -0.0744 -0.0024 -0.0391 296 SER B CA  
16034 C C   . SER B  270 ? 0.2275 0.3291 0.1860 -0.0788 -0.0013 -0.0397 296 SER B C   
16035 O O   . SER B  270 ? 0.2306 0.3357 0.1884 -0.0817 -0.0038 -0.0362 296 SER B O   
16036 C CB  . SER B  270 ? 0.2220 0.3214 0.1892 -0.0743 -0.0066 -0.0342 296 SER B CB  
16037 O OG  . SER B  270 ? 0.2345 0.3338 0.1980 -0.0785 -0.0092 -0.0321 296 SER B OG  
16043 N N   . THR B  271 ? 0.2257 0.3264 0.1810 -0.0788 0.0027  -0.0438 297 THR B N   
16044 C CA  . THR B  271 ? 0.2352 0.3385 0.1844 -0.0832 0.0046  -0.0454 297 THR B CA  
16045 C C   . THR B  271 ? 0.2525 0.3515 0.1938 -0.0868 0.0062  -0.0491 297 THR B C   
16046 O O   . THR B  271 ? 0.2648 0.3651 0.2000 -0.0902 0.0085  -0.0514 297 THR B O   
16047 C CB  . THR B  271 ? 0.2366 0.3429 0.1882 -0.0807 0.0083  -0.0474 297 THR B CB  
16048 O OG1 . THR B  271 ? 0.2394 0.3420 0.1926 -0.0764 0.0119  -0.0513 297 THR B OG1 
16049 C CG2 . THR B  271 ? 0.2387 0.3497 0.1973 -0.0785 0.0065  -0.0440 297 THR B CG2 
16057 N N   . SER B  272 ? 0.2578 0.3517 0.1990 -0.0864 0.0050  -0.0496 298 SER B N   
16058 C CA  . SER B  272 ? 0.2707 0.3599 0.2051 -0.0901 0.0062  -0.0531 298 SER B CA  
16059 C C   . SER B  272 ? 0.2807 0.3659 0.2109 -0.0894 0.0120  -0.0589 298 SER B C   
16060 O O   . SER B  272 ? 0.2944 0.3775 0.2168 -0.0941 0.0135  -0.0622 298 SER B O   
16061 C CB  . SER B  272 ? 0.2886 0.3815 0.2171 -0.0967 0.0029  -0.0511 298 SER B CB  
16062 O OG  . SER B  272 ? 0.3130 0.4085 0.2457 -0.0967 -0.0021 -0.0458 298 SER B OG  
16068 N N   . LEU B  273 ? 0.2791 0.3637 0.2145 -0.0836 0.0152  -0.0601 299 LEU B N   
16069 C CA  . LEU B  273 ? 0.2891 0.3700 0.2216 -0.0820 0.0211  -0.0652 299 LEU B CA  
16070 C C   . LEU B  273 ? 0.3012 0.3730 0.2307 -0.0816 0.0238  -0.0690 299 LEU B C   
16071 O O   . LEU B  273 ? 0.2952 0.3635 0.2291 -0.0784 0.0223  -0.0675 299 LEU B O   
16072 C CB  . LEU B  273 ? 0.2844 0.3681 0.2243 -0.0754 0.0236  -0.0649 299 LEU B CB  
16073 C CG  . LEU B  273 ? 0.2944 0.3865 0.2368 -0.0758 0.0231  -0.0627 299 LEU B CG  
16074 C CD1 . LEU B  273 ? 0.2946 0.3902 0.2459 -0.0693 0.0240  -0.0614 299 LEU B CD1 
16075 C CD2 . LEU B  273 ? 0.2949 0.3883 0.2306 -0.0790 0.0273  -0.0662 299 LEU B CD2 
16087 N N   A ARG B  274 ? 0.3075 0.3750 0.2291 -0.0849 0.0278  -0.0739 300 ARG B N   
16088 N N   B ARG B  274 ? 0.3110 0.3786 0.2325 -0.0849 0.0278  -0.0739 300 ARG B N   
16089 C CA  A ARG B  274 ? 0.3240 0.3816 0.2419 -0.0846 0.0317  -0.0785 300 ARG B CA  
16090 C CA  B ARG B  274 ? 0.3313 0.3891 0.2488 -0.0850 0.0316  -0.0785 300 ARG B CA  
16091 C C   A ARG B  274 ? 0.3466 0.4010 0.2652 -0.0795 0.0386  -0.0823 300 ARG B C   
16092 C C   B ARG B  274 ? 0.3497 0.4039 0.2677 -0.0799 0.0386  -0.0825 300 ARG B C   
16093 O O   A ARG B  274 ? 0.3541 0.4003 0.2734 -0.0760 0.0422  -0.0847 300 ARG B O   
16094 O O   B ARG B  274 ? 0.3566 0.4024 0.2748 -0.0768 0.0423  -0.0851 300 ARG B O   
16095 C CB  A ARG B  274 ? 0.3334 0.3877 0.2410 -0.0925 0.0317  -0.0820 300 ARG B CB  
16096 C CB  B ARG B  274 ? 0.3510 0.4060 0.2582 -0.0932 0.0312  -0.0817 300 ARG B CB  
16097 C CG  A ARG B  274 ? 0.3348 0.3900 0.2417 -0.0972 0.0258  -0.0791 300 ARG B CG  
16098 C CG  B ARG B  274 ? 0.3713 0.4318 0.2779 -0.0984 0.0243  -0.0775 300 ARG B CG  
16099 C CD  A ARG B  274 ? 0.3272 0.3924 0.2364 -0.0992 0.0202  -0.0736 300 ARG B CD  
16100 C CD  B ARG B  274 ? 0.3804 0.4374 0.2784 -0.1059 0.0233  -0.0803 300 ARG B CD  
16101 N NE  A ARG B  274 ? 0.3226 0.3896 0.2293 -0.1048 0.0150  -0.0712 300 ARG B NE  
16102 N NE  B ARG B  274 ? 0.3759 0.4377 0.2758 -0.1092 0.0167  -0.0755 300 ARG B NE  
16103 C CZ  A ARG B  274 ? 0.3233 0.3983 0.2286 -0.1088 0.0104  -0.0673 300 ARG B CZ  
16104 C CZ  B ARG B  274 ? 0.3738 0.4323 0.2772 -0.1089 0.0144  -0.0740 300 ARG B CZ  
16105 N NH1 A ARG B  274 ? 0.3371 0.4140 0.2407 -0.1134 0.0059  -0.0650 300 ARG B NH1 
16106 N NH1 B ARG B  274 ? 0.3667 0.4309 0.2721 -0.1117 0.0086  -0.0693 300 ARG B NH1 
16107 N NH2 A ARG B  274 ? 0.2860 0.3672 0.1917 -0.1081 0.0104  -0.0653 300 ARG B NH2 
16108 N NH2 B ARG B  274 ? 0.3457 0.3952 0.2506 -0.1056 0.0182  -0.0771 300 ARG B NH2 
16135 N N   . LYS B  275 ? 0.3569 0.4174 0.2752 -0.0792 0.0406  -0.0827 301 LYS B N   
16136 C CA  . LYS B  275 ? 0.3781 0.4371 0.2975 -0.0743 0.0471  -0.0859 301 LYS B CA  
16137 C C   . LYS B  275 ? 0.3756 0.4444 0.3031 -0.0701 0.0461  -0.0823 301 LYS B C   
16138 O O   . LYS B  275 ? 0.3813 0.4576 0.3093 -0.0733 0.0420  -0.0791 301 LYS B O   
16139 C CB  . LYS B  275 ? 0.4205 0.4772 0.3300 -0.0792 0.0515  -0.0911 301 LYS B CB  
16140 C CG  . LYS B  275 ? 0.5268 0.5742 0.4273 -0.0846 0.0523  -0.0952 301 LYS B CG  
16141 C CD  . LYS B  275 ? 0.6253 0.6616 0.5269 -0.0802 0.0571  -0.0984 301 LYS B CD  
16142 C CE  . LYS B  275 ? 0.7140 0.7407 0.6061 -0.0864 0.0583  -0.1030 301 LYS B CE  
16143 N NZ  . LYS B  275 ? 0.7632 0.7779 0.6546 -0.0824 0.0650  -0.1073 301 LYS B NZ  
16157 N N   . ILE B  276 ? 0.3709 0.4396 0.3047 -0.0631 0.0499  -0.0827 302 ILE B N   
16158 C CA  . ILE B  276 ? 0.3642 0.4425 0.3060 -0.0590 0.0496  -0.0798 302 ILE B CA  
16159 C C   . ILE B  276 ? 0.3683 0.4473 0.3084 -0.0570 0.0564  -0.0836 302 ILE B C   
16160 O O   . ILE B  276 ? 0.3806 0.4526 0.3199 -0.0532 0.0616  -0.0868 302 ILE B O   
16161 C CB  . ILE B  276 ? 0.3687 0.4479 0.3199 -0.0521 0.0479  -0.0767 302 ILE B CB  
16162 C CG1 . ILE B  276 ? 0.3764 0.4546 0.3288 -0.0543 0.0414  -0.0731 302 ILE B CG1 
16163 C CG2 . ILE B  276 ? 0.3707 0.4604 0.3299 -0.0482 0.0479  -0.0743 302 ILE B CG2 
16164 C CD1 . ILE B  276 ? 0.3930 0.4707 0.3526 -0.0483 0.0398  -0.0704 302 ILE B CD1 
16176 N N   . ASN B  277 ? 0.3572 0.4442 0.2966 -0.0597 0.0566  -0.0831 303 ASN B N   
16177 C CA  . ASN B  277 ? 0.3570 0.4460 0.2954 -0.0578 0.0632  -0.0863 303 ASN B CA  
16178 C C   . ASN B  277 ? 0.3501 0.4450 0.2993 -0.0499 0.0651  -0.0845 303 ASN B C   
16179 O O   . ASN B  277 ? 0.3507 0.4548 0.3067 -0.0493 0.0616  -0.0807 303 ASN B O   
16180 C CB  . ASN B  277 ? 0.3695 0.4656 0.3036 -0.0636 0.0627  -0.0860 303 ASN B CB  
16181 C CG  . ASN B  277 ? 0.4112 0.5085 0.3423 -0.0629 0.0698  -0.0899 303 ASN B CG  
16182 O OD1 . ASN B  277 ? 0.4212 0.5158 0.3553 -0.0570 0.0754  -0.0923 303 ASN B OD1 
16183 N ND2 . ASN B  277 ? 0.4219 0.5234 0.3469 -0.0686 0.0701  -0.0903 303 ASN B ND2 
16190 N N   . ALA B  278 ? 0.3518 0.4415 0.3026 -0.0440 0.0708  -0.0870 304 ALA B N   
16191 C CA  . ALA B  278 ? 0.3529 0.4485 0.3140 -0.0359 0.0729  -0.0851 304 ALA B CA  
16192 C C   . ALA B  278 ? 0.3502 0.4583 0.3162 -0.0358 0.0741  -0.0840 304 ALA B C   
16193 O O   . ALA B  278 ? 0.3539 0.4708 0.3295 -0.0313 0.0725  -0.0808 304 ALA B O   
16194 C CB  . ALA B  278 ? 0.3565 0.4439 0.3170 -0.0301 0.0801  -0.0885 304 ALA B CB  
16200 N N   . ALA B  279 ? 0.3484 0.4575 0.3075 -0.0409 0.0767  -0.0865 305 ALA B N   
16201 C CA  . ALA B  279 ? 0.3461 0.4666 0.3089 -0.0417 0.0782  -0.0856 305 ALA B CA  
16202 C C   . ALA B  279 ? 0.3436 0.4736 0.3119 -0.0445 0.0715  -0.0808 305 ALA B C   
16203 O O   . ALA B  279 ? 0.3464 0.4869 0.3212 -0.0433 0.0723  -0.0792 305 ALA B O   
16204 C CB  . ALA B  279 ? 0.3503 0.4687 0.3031 -0.0473 0.0822  -0.0893 305 ALA B CB  
16210 N N   . TRP B  280 ? 0.3366 0.4630 0.3029 -0.0479 0.0651  -0.0786 306 TRP B N   
16211 C CA  . TRP B  280 ? 0.3413 0.4752 0.3129 -0.0501 0.0589  -0.0741 306 TRP B CA  
16212 C C   . TRP B  280 ? 0.3370 0.4788 0.3201 -0.0440 0.0582  -0.0717 306 TRP B C   
16213 O O   . TRP B  280 ? 0.3318 0.4824 0.3201 -0.0455 0.0553  -0.0690 306 TRP B O   
16214 C CB  . TRP B  280 ? 0.3433 0.4710 0.3117 -0.0532 0.0528  -0.0721 306 TRP B CB  
16215 C CG  . TRP B  280 ? 0.3565 0.4788 0.3145 -0.0601 0.0517  -0.0732 306 TRP B CG  
16216 C CD1 . TRP B  280 ? 0.3690 0.4933 0.3205 -0.0650 0.0540  -0.0747 306 TRP B CD1 
16217 C CD2 . TRP B  280 ? 0.3616 0.4765 0.3147 -0.0630 0.0476  -0.0726 306 TRP B CD2 
16218 N NE1 . TRP B  280 ? 0.3775 0.4961 0.3200 -0.0707 0.0516  -0.0752 306 TRP B NE1 
16219 C CE2 . TRP B  280 ? 0.3743 0.4875 0.3180 -0.0697 0.0475  -0.0738 306 TRP B CE2 
16220 C CE3 . TRP B  280 ? 0.3644 0.4745 0.3202 -0.0606 0.0441  -0.0710 306 TRP B CE3 
16221 C CZ2 . TRP B  280 ? 0.3840 0.4913 0.3214 -0.0740 0.0439  -0.0735 306 TRP B CZ2 
16222 C CZ3 . TRP B  280 ? 0.3793 0.4833 0.3291 -0.0649 0.0407  -0.0707 306 TRP B CZ3 
16223 C CH2 . TRP B  280 ? 0.3846 0.4875 0.3254 -0.0716 0.0405  -0.0719 306 TRP B CH2 
16234 N N   . PHE B  281 ? 0.3408 0.4794 0.3276 -0.0372 0.0607  -0.0726 307 PHE B N   
16235 C CA  . PHE B  281 ? 0.3436 0.4898 0.3410 -0.0309 0.0598  -0.0702 307 PHE B CA  
16236 C C   . PHE B  281 ? 0.3552 0.5086 0.3582 -0.0257 0.0658  -0.0714 307 PHE B C   
16237 O O   . PHE B  281 ? 0.3572 0.5172 0.3690 -0.0199 0.0655  -0.0694 307 PHE B O   
16238 C CB  . PHE B  281 ? 0.3407 0.4791 0.3390 -0.0263 0.0582  -0.0695 307 PHE B CB  
16239 C CG  . PHE B  281 ? 0.3510 0.4819 0.3439 -0.0309 0.0529  -0.0684 307 PHE B CG  
16240 C CD1 . PHE B  281 ? 0.3531 0.4887 0.3491 -0.0336 0.0467  -0.0651 307 PHE B CD1 
16241 C CD2 . PHE B  281 ? 0.3685 0.4881 0.3528 -0.0334 0.0542  -0.0710 307 PHE B CD2 
16242 C CE1 . PHE B  281 ? 0.3652 0.4945 0.3565 -0.0376 0.0421  -0.0639 307 PHE B CE1 
16243 C CE2 . PHE B  281 ? 0.3802 0.4942 0.3599 -0.0379 0.0493  -0.0698 307 PHE B CE2 
16244 C CZ  . PHE B  281 ? 0.3692 0.4882 0.3527 -0.0397 0.0433  -0.0661 307 PHE B CZ  
16254 N N   . LYS B  282 ? 0.3575 0.5104 0.3556 -0.0278 0.0712  -0.0744 308 LYS B N   
16255 C CA  . LYS B  282 ? 0.3645 0.5240 0.3677 -0.0229 0.0777  -0.0757 308 LYS B CA  
16256 C C   . LYS B  282 ? 0.3544 0.5292 0.3682 -0.0215 0.0759  -0.0727 308 LYS B C   
16257 O O   . LYS B  282 ? 0.3590 0.5406 0.3808 -0.0149 0.0792  -0.0721 308 LYS B O   
16258 C CB  . LYS B  282 ? 0.4012 0.5575 0.3960 -0.0267 0.0833  -0.0795 308 LYS B CB  
16259 C CG  . LYS B  282 ? 0.4729 0.6322 0.4708 -0.0210 0.0914  -0.0818 308 LYS B CG  
16260 C CD  . LYS B  282 ? 0.5517 0.7101 0.5415 -0.0259 0.0964  -0.0853 308 LYS B CD  
16261 C CE  . LYS B  282 ? 0.6213 0.7781 0.6111 -0.0205 0.1055  -0.0887 308 LYS B CE  
16262 N NZ  . LYS B  282 ? 0.6702 0.8112 0.6506 -0.0197 0.1090  -0.0928 308 LYS B NZ  
16276 N N   . ASN B  283 ? 0.3359 0.5162 0.3501 -0.0277 0.0710  -0.0706 309 ASN B N   
16277 C CA  . ASN B  283 ? 0.3275 0.5220 0.3513 -0.0276 0.0692  -0.0680 309 ASN B CA  
16278 C C   . ASN B  283 ? 0.3096 0.5066 0.3378 -0.0286 0.0618  -0.0648 309 ASN B C   
16279 O O   . ASN B  283 ? 0.2992 0.5054 0.3321 -0.0321 0.0591  -0.0629 309 ASN B O   
16280 C CB  . ASN B  283 ? 0.3518 0.5519 0.3731 -0.0341 0.0708  -0.0685 309 ASN B CB  
16281 C CG  . ASN B  283 ? 0.4138 0.6118 0.4302 -0.0333 0.0784  -0.0719 309 ASN B CG  
16282 O OD1 . ASN B  283 ? 0.4343 0.6367 0.4560 -0.0272 0.0835  -0.0729 309 ASN B OD1 
16283 N ND2 . ASN B  283 ? 0.4355 0.6266 0.4415 -0.0392 0.0794  -0.0737 309 ASN B ND2 
16290 N N   . MET B  284 ? 0.3018 0.4908 0.3288 -0.0255 0.0590  -0.0641 310 MET B N   
16291 C CA  . MET B  284 ? 0.3034 0.4939 0.3343 -0.0255 0.0524  -0.0613 310 MET B CA  
16292 C C   . MET B  284 ? 0.2923 0.4858 0.3304 -0.0172 0.0529  -0.0602 310 MET B C   
16293 O O   . MET B  284 ? 0.3002 0.4854 0.3362 -0.0142 0.0513  -0.0597 310 MET B O   
16294 C CB  . MET B  284 ? 0.3273 0.5055 0.3502 -0.0290 0.0486  -0.0611 310 MET B CB  
16295 C CG  . MET B  284 ? 0.3676 0.5445 0.3854 -0.0369 0.0457  -0.0605 310 MET B CG  
16296 S SD  . MET B  284 ? 0.3692 0.5334 0.3798 -0.0393 0.0408  -0.0596 310 MET B SD  
16297 C CE  . MET B  284 ? 0.3716 0.5326 0.3734 -0.0473 0.0411  -0.0603 310 MET B CE  
16307 N N   . PRO B  285 ? 0.2744 0.4805 0.3214 -0.0133 0.0550  -0.0594 311 PRO B N   
16308 C CA  . PRO B  285 ? 0.2643 0.4741 0.3181 -0.0050 0.0556  -0.0578 311 PRO B CA  
16309 C C   . PRO B  285 ? 0.2583 0.4703 0.3158 -0.0039 0.0492  -0.0551 311 PRO B C   
16310 O O   . PRO B  285 ? 0.2628 0.4746 0.3237 0.0028  0.0493  -0.0537 311 PRO B O   
16311 C CB  . PRO B  285 ? 0.2693 0.4937 0.3318 -0.0022 0.0593  -0.0575 311 PRO B CB  
16312 C CG  . PRO B  285 ? 0.2733 0.5041 0.3356 -0.0100 0.0576  -0.0578 311 PRO B CG  
16313 C CD  . PRO B  285 ? 0.2644 0.4821 0.3156 -0.0162 0.0572  -0.0596 311 PRO B CD  
16321 N N   . HIS B  286 ? 0.2459 0.4597 0.3025 -0.0103 0.0439  -0.0542 312 HIS B N   
16322 C CA  . HIS B  286 ? 0.2414 0.4575 0.3011 -0.0100 0.0379  -0.0519 312 HIS B CA  
16323 C C   . HIS B  286 ? 0.2401 0.4433 0.2923 -0.0128 0.0343  -0.0517 312 HIS B C   
16324 O O   . HIS B  286 ? 0.2532 0.4578 0.3071 -0.0135 0.0293  -0.0501 312 HIS B O   
16325 C CB  . HIS B  286 ? 0.2462 0.4738 0.3109 -0.0151 0.0346  -0.0511 312 HIS B CB  
16326 C CG  . HIS B  286 ? 0.2723 0.5140 0.3447 -0.0138 0.0377  -0.0512 312 HIS B CG  
16327 N ND1 . HIS B  286 ? 0.2927 0.5457 0.3738 -0.0078 0.0374  -0.0497 312 HIS B ND1 
16328 C CD2 . HIS B  286 ? 0.2862 0.5329 0.3590 -0.0179 0.0409  -0.0525 312 HIS B CD2 
16329 C CE1 . HIS B  286 ? 0.2982 0.5630 0.3852 -0.0084 0.0405  -0.0500 312 HIS B CE1 
16330 N NE2 . HIS B  286 ? 0.2985 0.5597 0.3806 -0.0144 0.0428  -0.0518 312 HIS B NE2 
16338 N N   . LEU B  287 ? 0.2304 0.4214 0.2743 -0.0148 0.0365  -0.0535 313 LEU B N   
16339 C CA  . LEU B  287 ? 0.2227 0.4027 0.2601 -0.0179 0.0329  -0.0530 313 LEU B CA  
16340 C C   . LEU B  287 ? 0.2167 0.3938 0.2561 -0.0126 0.0303  -0.0512 313 LEU B C   
16341 O O   . LEU B  287 ? 0.2120 0.3871 0.2528 -0.0064 0.0334  -0.0513 313 LEU B O   
16342 C CB  . LEU B  287 ? 0.2195 0.3878 0.2480 -0.0204 0.0358  -0.0552 313 LEU B CB  
16343 C CG  . LEU B  287 ? 0.2359 0.3948 0.2579 -0.0251 0.0318  -0.0546 313 LEU B CG  
16344 C CD1 . LEU B  287 ? 0.2445 0.4073 0.2660 -0.0318 0.0282  -0.0534 313 LEU B CD1 
16345 C CD2 . LEU B  287 ? 0.2477 0.3958 0.2614 -0.0269 0.0347  -0.0569 313 LEU B CD2 
16357 N N   . LYS B  288 ? 0.2166 0.3939 0.2564 -0.0150 0.0250  -0.0495 314 LYS B N   
16358 C CA  . LYS B  288 ? 0.2206 0.3967 0.2625 -0.0107 0.0220  -0.0475 314 LYS B CA  
16359 C C   . LYS B  288 ? 0.2210 0.3850 0.2566 -0.0125 0.0196  -0.0470 314 LYS B C   
16360 O O   . LYS B  288 ? 0.2226 0.3820 0.2581 -0.0078 0.0193  -0.0459 314 LYS B O   
16361 C CB  . LYS B  288 ? 0.2572 0.4438 0.3047 -0.0120 0.0177  -0.0461 314 LYS B CB  
16362 C CG  . LYS B  288 ? 0.3378 0.5268 0.3888 -0.0067 0.0150  -0.0440 314 LYS B CG  
16363 C CD  . LYS B  288 ? 0.4219 0.6222 0.4782 -0.0086 0.0110  -0.0432 314 LYS B CD  
16364 C CE  . LYS B  288 ? 0.4955 0.6908 0.5482 -0.0140 0.0068  -0.0429 314 LYS B CE  
16365 N NZ  . LYS B  288 ? 0.5435 0.7489 0.6008 -0.0165 0.0033  -0.0427 314 LYS B NZ  
16379 N N   . VAL B  289 ? 0.2088 0.3686 0.2398 -0.0191 0.0176  -0.0474 315 VAL B N   
16380 C CA  . VAL B  289 ? 0.2218 0.3715 0.2474 -0.0212 0.0152  -0.0466 315 VAL B CA  
16381 C C   . VAL B  289 ? 0.2225 0.3655 0.2414 -0.0261 0.0170  -0.0482 315 VAL B C   
16382 O O   . VAL B  289 ? 0.2329 0.3795 0.2509 -0.0308 0.0171  -0.0487 315 VAL B O   
16383 C CB  . VAL B  289 ? 0.2350 0.3865 0.2617 -0.0241 0.0101  -0.0447 315 VAL B CB  
16384 C CG1 . VAL B  289 ? 0.2492 0.3908 0.2710 -0.0258 0.0078  -0.0436 315 VAL B CG1 
16385 C CG2 . VAL B  289 ? 0.2361 0.3953 0.2690 -0.0197 0.0082  -0.0435 315 VAL B CG2 
16395 N N   . LEU B  290 ? 0.2127 0.3461 0.2268 -0.0252 0.0185  -0.0490 316 LEU B N   
16396 C CA  . LEU B  290 ? 0.2178 0.3447 0.2249 -0.0299 0.0201  -0.0507 316 LEU B CA  
16397 C C   . LEU B  290 ? 0.2332 0.3518 0.2363 -0.0319 0.0171  -0.0494 316 LEU B C   
16398 O O   . LEU B  290 ? 0.2426 0.3557 0.2456 -0.0282 0.0175  -0.0492 316 LEU B O   
16399 C CB  . LEU B  290 ? 0.2183 0.3417 0.2231 -0.0273 0.0257  -0.0535 316 LEU B CB  
16400 C CG  . LEU B  290 ? 0.2428 0.3592 0.2396 -0.0322 0.0279  -0.0560 316 LEU B CG  
16401 C CD1 . LEU B  290 ? 0.2448 0.3657 0.2391 -0.0386 0.0264  -0.0558 316 LEU B CD1 
16402 C CD2 . LEU B  290 ? 0.2477 0.3610 0.2427 -0.0292 0.0340  -0.0592 316 LEU B CD2 
16414 N N   . ASP B  291 ? 0.2341 0.3523 0.2343 -0.0374 0.0141  -0.0483 317 ASP B N   
16415 C CA  . ASP B  291 ? 0.2485 0.3604 0.2456 -0.0396 0.0110  -0.0467 317 ASP B CA  
16416 C C   . ASP B  291 ? 0.2506 0.3572 0.2406 -0.0442 0.0124  -0.0483 317 ASP B C   
16417 O O   . ASP B  291 ? 0.2562 0.3656 0.2435 -0.0486 0.0127  -0.0487 317 ASP B O   
16418 C CB  . ASP B  291 ? 0.2802 0.3956 0.2794 -0.0422 0.0067  -0.0438 317 ASP B CB  
16419 C CG  . ASP B  291 ? 0.3788 0.4895 0.3779 -0.0416 0.0035  -0.0416 317 ASP B CG  
16420 O OD1 . ASP B  291 ? 0.3873 0.4915 0.3830 -0.0416 0.0040  -0.0420 317 ASP B OD1 
16421 O OD2 . ASP B  291 ? 0.4095 0.5229 0.4117 -0.0415 0.0005  -0.0395 317 ASP B OD2 
16426 N N   . LEU B  292 ? 0.2390 0.3380 0.2257 -0.0434 0.0136  -0.0494 318 LEU B N   
16427 C CA  . LEU B  292 ? 0.2337 0.3272 0.2134 -0.0480 0.0149  -0.0514 318 LEU B CA  
16428 C C   . LEU B  292 ? 0.2283 0.3158 0.2058 -0.0496 0.0121  -0.0499 318 LEU B C   
16429 O O   . LEU B  292 ? 0.2296 0.3107 0.2023 -0.0514 0.0139  -0.0520 318 LEU B O   
16430 C CB  . LEU B  292 ? 0.2401 0.3296 0.2174 -0.0457 0.0203  -0.0552 318 LEU B CB  
16431 C CG  . LEU B  292 ? 0.2674 0.3625 0.2459 -0.0447 0.0239  -0.0571 318 LEU B CG  
16432 C CD1 . LEU B  292 ? 0.2753 0.3662 0.2537 -0.0399 0.0294  -0.0601 318 LEU B CD1 
16433 C CD2 . LEU B  292 ? 0.2685 0.3651 0.2410 -0.0510 0.0243  -0.0585 318 LEU B CD2 
16445 N N   . GLU B  293 ? 0.2271 0.3168 0.2080 -0.0494 0.0080  -0.0464 319 GLU B N   
16446 C CA  . GLU B  293 ? 0.2341 0.3192 0.2140 -0.0506 0.0053  -0.0446 319 GLU B CA  
16447 C C   . GLU B  293 ? 0.2361 0.3205 0.2106 -0.0571 0.0036  -0.0442 319 GLU B C   
16448 O O   . GLU B  293 ? 0.2421 0.3308 0.2147 -0.0603 0.0033  -0.0442 319 GLU B O   
16449 C CB  . GLU B  293 ? 0.2585 0.3465 0.2433 -0.0486 0.0016  -0.0409 319 GLU B CB  
16450 C CG  . GLU B  293 ? 0.3144 0.4047 0.3046 -0.0427 0.0024  -0.0407 319 GLU B CG  
16451 C CD  . GLU B  293 ? 0.3658 0.4596 0.3600 -0.0418 -0.0012 -0.0376 319 GLU B CD  
16452 O OE1 . GLU B  293 ? 0.3597 0.4592 0.3560 -0.0425 -0.0019 -0.0373 319 GLU B OE1 
16453 O OE2 . GLU B  293 ? 0.4127 0.5035 0.4078 -0.0406 -0.0031 -0.0356 319 GLU B OE2 
16460 N N   . PHE B  294 ? 0.2244 0.3043 0.1967 -0.0590 0.0022  -0.0436 320 PHE B N   
16461 C CA  . PHE B  294 ? 0.2311 0.3115 0.1990 -0.0650 -0.0002 -0.0426 320 PHE B CA  
16462 C C   . PHE B  294 ? 0.2436 0.3244 0.2052 -0.0694 0.0021  -0.0457 320 PHE B C   
16463 O O   . PHE B  294 ? 0.2510 0.3359 0.2099 -0.0736 0.0002  -0.0443 320 PHE B O   
16464 C CB  . PHE B  294 ? 0.2187 0.3043 0.1895 -0.0661 -0.0043 -0.0381 320 PHE B CB  
16465 C CG  . PHE B  294 ? 0.2198 0.3044 0.1958 -0.0626 -0.0066 -0.0351 320 PHE B CG  
16466 C CD1 . PHE B  294 ? 0.2286 0.3104 0.2040 -0.0641 -0.0084 -0.0334 320 PHE B CD1 
16467 C CD2 . PHE B  294 ? 0.2165 0.3031 0.1976 -0.0580 -0.0067 -0.0340 320 PHE B CD2 
16468 C CE1 . PHE B  294 ? 0.2356 0.3165 0.2156 -0.0608 -0.0102 -0.0306 320 PHE B CE1 
16469 C CE2 . PHE B  294 ? 0.2224 0.3079 0.2075 -0.0550 -0.0086 -0.0314 320 PHE B CE2 
16470 C CZ  . PHE B  294 ? 0.2215 0.3040 0.2060 -0.0562 -0.0102 -0.0297 320 PHE B CZ  
16480 N N   . ASN B  295 ? 0.2405 0.3166 0.1995 -0.0681 0.0064  -0.0500 321 ASN B N   
16481 C CA  . ASN B  295 ? 0.2409 0.3160 0.1932 -0.0720 0.0094  -0.0538 321 ASN B CA  
16482 C C   . ASN B  295 ? 0.2551 0.3223 0.2025 -0.0742 0.0113  -0.0570 321 ASN B C   
16483 O O   . ASN B  295 ? 0.2584 0.3227 0.2078 -0.0740 0.0092  -0.0553 321 ASN B O   
16484 C CB  . ASN B  295 ? 0.2455 0.3222 0.1992 -0.0683 0.0136  -0.0563 321 ASN B CB  
16485 C CG  . ASN B  295 ? 0.2503 0.3349 0.2071 -0.0681 0.0122  -0.0539 321 ASN B CG  
16486 O OD1 . ASN B  295 ? 0.2688 0.3566 0.2315 -0.0634 0.0130  -0.0531 321 ASN B OD1 
16487 N ND2 . ASN B  295 ? 0.2187 0.3070 0.1718 -0.0733 0.0100  -0.0525 321 ASN B ND2 
16494 N N   . TYR B  296 ? 0.2701 0.3337 0.2111 -0.0768 0.0152  -0.0617 322 TYR B N   
16495 C CA  . TYR B  296 ? 0.2893 0.3447 0.2251 -0.0794 0.0176  -0.0654 322 TYR B CA  
16496 C C   . TYR B  296 ? 0.2881 0.3374 0.2232 -0.0751 0.0240  -0.0698 322 TYR B C   
16497 O O   . TYR B  296 ? 0.2909 0.3356 0.2192 -0.0782 0.0278  -0.0745 322 TYR B O   
16498 C CB  . TYR B  296 ? 0.2987 0.3554 0.2262 -0.0875 0.0165  -0.0673 322 TYR B CB  
16499 C CG  . TYR B  296 ? 0.3161 0.3798 0.2442 -0.0916 0.0103  -0.0626 322 TYR B CG  
16500 C CD1 . TYR B  296 ? 0.3337 0.3962 0.2634 -0.0933 0.0069  -0.0603 322 TYR B CD1 
16501 C CD2 . TYR B  296 ? 0.3197 0.3912 0.2468 -0.0937 0.0082  -0.0603 322 TYR B CD2 
16502 C CE1 . TYR B  296 ? 0.3453 0.4146 0.2759 -0.0967 0.0015  -0.0557 322 TYR B CE1 
16503 C CE2 . TYR B  296 ? 0.3318 0.4093 0.2592 -0.0972 0.0029  -0.0557 322 TYR B CE2 
16504 C CZ  . TYR B  296 ? 0.3492 0.4258 0.2786 -0.0985 -0.0005 -0.0534 322 TYR B CZ  
16505 O OH  . TYR B  296 ? 0.3615 0.4446 0.2916 -0.1017 -0.0055 -0.0486 322 TYR B OH  
16515 N N   . LEU B  297 ? 0.2841 0.3336 0.2263 -0.0679 0.0253  -0.0681 323 LEU B N   
16516 C CA  . LEU B  297 ? 0.2892 0.3348 0.2322 -0.0627 0.0312  -0.0712 323 LEU B CA  
16517 C C   . LEU B  297 ? 0.3010 0.3366 0.2445 -0.0589 0.0349  -0.0728 323 LEU B C   
16518 O O   . LEU B  297 ? 0.3038 0.3375 0.2503 -0.0528 0.0392  -0.0738 323 LEU B O   
16519 C CB  . LEU B  297 ? 0.2773 0.3308 0.2278 -0.0568 0.0307  -0.0683 323 LEU B CB  
16520 C CG  . LEU B  297 ? 0.2767 0.3394 0.2268 -0.0600 0.0284  -0.0671 323 LEU B CG  
16521 C CD1 . LEU B  297 ? 0.2742 0.3445 0.2325 -0.0550 0.0268  -0.0637 323 LEU B CD1 
16522 C CD2 . LEU B  297 ? 0.2833 0.3455 0.2273 -0.0626 0.0330  -0.0715 323 LEU B CD2 
16534 N N   . VAL B  298 ? 0.3014 0.3305 0.2419 -0.0626 0.0337  -0.0733 324 VAL B N   
16535 C CA  . VAL B  298 ? 0.3137 0.3322 0.2542 -0.0594 0.0379  -0.0751 324 VAL B CA  
16536 C C   . VAL B  298 ? 0.3281 0.3394 0.2638 -0.0583 0.0451  -0.0805 324 VAL B C   
16537 O O   . VAL B  298 ? 0.3323 0.3385 0.2712 -0.0517 0.0496  -0.0808 324 VAL B O   
16538 C CB  . VAL B  298 ? 0.3250 0.3378 0.2624 -0.0648 0.0356  -0.0751 324 VAL B CB  
16539 C CG1 . VAL B  298 ? 0.3398 0.3399 0.2744 -0.0638 0.0412  -0.0786 324 VAL B CG1 
16540 C CG2 . VAL B  298 ? 0.3162 0.3340 0.2600 -0.0630 0.0301  -0.0695 324 VAL B CG2 
16550 N N   . GLY B  299 ? 0.3280 0.3395 0.2563 -0.0645 0.0463  -0.0844 325 GLY B N   
16551 C CA  . GLY B  299 ? 0.3483 0.3534 0.2714 -0.0639 0.0532  -0.0899 325 GLY B CA  
16552 C C   . GLY B  299 ? 0.3521 0.3621 0.2807 -0.0564 0.0564  -0.0890 325 GLY B C   
16553 O O   . GLY B  299 ? 0.3680 0.3712 0.2973 -0.0510 0.0626  -0.0911 325 GLY B O   
16557 N N   . GLU B  300 ? 0.3328 0.3546 0.2657 -0.0558 0.0524  -0.0855 326 GLU B N   
16558 C CA  . GLU B  300 ? 0.3324 0.3608 0.2714 -0.0492 0.0546  -0.0842 326 GLU B CA  
16559 C C   . GLU B  300 ? 0.3293 0.3568 0.2766 -0.0407 0.0553  -0.0810 326 GLU B C   
16560 O O   . GLU B  300 ? 0.3358 0.3655 0.2874 -0.0344 0.0593  -0.0810 326 GLU B O   
16561 C CB  . GLU B  300 ? 0.3560 0.3970 0.2977 -0.0513 0.0498  -0.0812 326 GLU B CB  
16562 C CG  . GLU B  300 ? 0.4329 0.4769 0.3680 -0.0568 0.0514  -0.0843 326 GLU B CG  
16563 C CD  . GLU B  300 ? 0.5283 0.5727 0.4632 -0.0530 0.0580  -0.0874 326 GLU B CD  
16564 O OE1 . GLU B  300 ? 0.5576 0.6008 0.4986 -0.0455 0.0614  -0.0869 326 GLU B OE1 
16565 O OE2 . GLU B  300 ? 0.5429 0.5893 0.4718 -0.0575 0.0599  -0.0902 326 GLU B OE2 
16572 N N   . ILE B  301 ? 0.3235 0.3491 0.2734 -0.0404 0.0513  -0.0778 327 ILE B N   
16573 C CA  . ILE B  301 ? 0.3208 0.3452 0.2778 -0.0326 0.0519  -0.0746 327 ILE B CA  
16574 C C   . ILE B  301 ? 0.3349 0.3475 0.2897 -0.0288 0.0590  -0.0776 327 ILE B C   
16575 O O   . ILE B  301 ? 0.3430 0.3557 0.3033 -0.0209 0.0619  -0.0759 327 ILE B O   
16576 C CB  . ILE B  301 ? 0.3089 0.3341 0.2687 -0.0334 0.0461  -0.0704 327 ILE B CB  
16577 C CG1 . ILE B  301 ? 0.3046 0.3417 0.2681 -0.0353 0.0399  -0.0669 327 ILE B CG1 
16578 C CG2 . ILE B  301 ? 0.3125 0.3344 0.2780 -0.0256 0.0476  -0.0676 327 ILE B CG2 
16579 C CD1 . ILE B  301 ? 0.3009 0.3390 0.2655 -0.0382 0.0340  -0.0635 327 ILE B CD1 
16591 N N   . ALA B  302 ? 0.3505 0.3531 0.2973 -0.0343 0.0617  -0.0820 328 ALA B N   
16592 C CA  . ALA B  302 ? 0.3751 0.3650 0.3189 -0.0315 0.0690  -0.0854 328 ALA B CA  
16593 C C   . ALA B  302 ? 0.3997 0.3890 0.3420 -0.0284 0.0756  -0.0891 328 ALA B C   
16594 O O   . ALA B  302 ? 0.4019 0.3824 0.3445 -0.0231 0.0820  -0.0906 328 ALA B O   
16595 C CB  . ALA B  302 ? 0.3823 0.3619 0.3177 -0.0394 0.0695  -0.0893 328 ALA B CB  
16601 N N   . SER B  303 ? 0.4234 0.4214 0.3639 -0.0317 0.0746  -0.0905 329 SER B N   
16602 C CA  . SER B  303 ? 0.4614 0.4587 0.3997 -0.0295 0.0812  -0.0943 329 SER B CA  
16603 C C   . SER B  303 ? 0.4811 0.4924 0.4229 -0.0292 0.0792  -0.0928 329 SER B C   
16604 O O   . SER B  303 ? 0.4971 0.5094 0.4339 -0.0321 0.0825  -0.0966 329 SER B O   
16605 C CB  . SER B  303 ? 0.5026 0.4901 0.4298 -0.0369 0.0848  -0.1007 329 SER B CB  
16606 O OG  . SER B  303 ? 0.5479 0.5424 0.4704 -0.0453 0.0796  -0.1013 329 SER B OG  
16612 N N   . GLY B  304 ? 0.4749 0.4963 0.4250 -0.0255 0.0742  -0.0875 330 GLY B N   
16613 C CA  . GLY B  304 ? 0.4811 0.5161 0.4353 -0.0257 0.0715  -0.0856 330 GLY B CA  
16614 C C   . GLY B  304 ? 0.4776 0.5180 0.4360 -0.0199 0.0768  -0.0863 330 GLY B C   
16615 O O   . GLY B  304 ? 0.4824 0.5267 0.4489 -0.0122 0.0777  -0.0833 330 GLY B O   
16619 N N   . ALA B  305 ? 0.4718 0.5136 0.4249 -0.0237 0.0800  -0.0900 331 ALA B N   
16620 C CA  . ALA B  305 ? 0.4624 0.5109 0.4195 -0.0190 0.0850  -0.0907 331 ALA B CA  
16621 C C   . ALA B  305 ? 0.4464 0.5102 0.4124 -0.0171 0.0801  -0.0860 331 ALA B C   
16622 O O   . ALA B  305 ? 0.4505 0.5212 0.4239 -0.0106 0.0829  -0.0846 331 ALA B O   
16623 C CB  . ALA B  305 ? 0.4676 0.5143 0.4161 -0.0245 0.0891  -0.0958 331 ALA B CB  
16629 N N   . PHE B  306 ? 0.4318 0.5009 0.3973 -0.0229 0.0729  -0.0836 332 PHE B N   
16630 C CA  . PHE B  306 ? 0.4208 0.5032 0.3940 -0.0221 0.0682  -0.0794 332 PHE B CA  
16631 C C   . PHE B  306 ? 0.4147 0.5011 0.3975 -0.0143 0.0667  -0.0755 332 PHE B C   
16632 O O   . PHE B  306 ? 0.4079 0.5059 0.3980 -0.0119 0.0649  -0.0729 332 PHE B O   
16633 C CB  . PHE B  306 ? 0.4159 0.5010 0.3863 -0.0294 0.0611  -0.0775 332 PHE B CB  
16634 C CG  . PHE B  306 ? 0.4167 0.4973 0.3881 -0.0293 0.0561  -0.0748 332 PHE B CG  
16635 C CD1 . PHE B  306 ? 0.4265 0.4956 0.3916 -0.0316 0.0567  -0.0768 332 PHE B CD1 
16636 C CD2 . PHE B  306 ? 0.4165 0.5042 0.3952 -0.0269 0.0510  -0.0704 332 PHE B CD2 
16637 C CE1 . PHE B  306 ? 0.4331 0.4984 0.3994 -0.0314 0.0524  -0.0742 332 PHE B CE1 
16638 C CE2 . PHE B  306 ? 0.4236 0.5072 0.4031 -0.0267 0.0468  -0.0680 332 PHE B CE2 
16639 C CZ  . PHE B  306 ? 0.4246 0.4972 0.3982 -0.0288 0.0476  -0.0697 332 PHE B CZ  
16649 N N   . LEU B  307 ? 0.4117 0.4889 0.3942 -0.0107 0.0675  -0.0751 333 LEU B N   
16650 C CA  . LEU B  307 ? 0.4116 0.4918 0.4023 -0.0032 0.0663  -0.0713 333 LEU B CA  
16651 C C   . LEU B  307 ? 0.4076 0.4941 0.4050 0.0045  0.0715  -0.0709 333 LEU B C   
16652 O O   . LEU B  307 ? 0.4104 0.5045 0.4159 0.0103  0.0696  -0.0671 333 LEU B O   
16653 C CB  . LEU B  307 ? 0.4232 0.4909 0.4111 -0.0013 0.0670  -0.0712 333 LEU B CB  
16654 C CG  . LEU B  307 ? 0.4537 0.5157 0.4362 -0.0081 0.0617  -0.0709 333 LEU B CG  
16655 C CD1 . LEU B  307 ? 0.4707 0.5187 0.4486 -0.0076 0.0646  -0.0725 333 LEU B CD1 
16656 C CD2 . LEU B  307 ? 0.4610 0.5306 0.4491 -0.0076 0.0549  -0.0663 333 LEU B CD2 
16668 N N   . THR B  308 ? 0.3953 0.4792 0.3895 0.0048  0.0780  -0.0746 334 THR B N   
16669 C CA  . THR B  308 ? 0.3828 0.4731 0.3836 0.0122  0.0835  -0.0743 334 THR B CA  
16670 C C   . THR B  308 ? 0.3655 0.4722 0.3725 0.0111  0.0812  -0.0727 334 THR B C   
16671 O O   . THR B  308 ? 0.3623 0.4777 0.3769 0.0173  0.0841  -0.0712 334 THR B O   
16672 C CB  . THR B  308 ? 0.4042 0.4847 0.3987 0.0127  0.0919  -0.0792 334 THR B CB  
16673 O OG1 . THR B  308 ? 0.4202 0.5024 0.4084 0.0051  0.0922  -0.0826 334 THR B OG1 
16674 C CG2 . THR B  308 ? 0.4153 0.4788 0.4029 0.0126  0.0945  -0.0815 334 THR B CG2 
16682 N N   . MET B  309 ? 0.3578 0.4685 0.3617 0.0032  0.0761  -0.0728 335 MET B N   
16683 C CA  . MET B  309 ? 0.3491 0.4738 0.3576 0.0007  0.0740  -0.0715 335 MET B CA  
16684 C C   . MET B  309 ? 0.3270 0.4618 0.3431 0.0014  0.0671  -0.0671 335 MET B C   
16685 O O   . MET B  309 ? 0.3253 0.4712 0.3452 -0.0014 0.0649  -0.0660 335 MET B O   
16686 C CB  . MET B  309 ? 0.3690 0.4916 0.3693 -0.0086 0.0722  -0.0738 335 MET B CB  
16687 C CG  . MET B  309 ? 0.4188 0.5313 0.4098 -0.0111 0.0781  -0.0786 335 MET B CG  
16688 S SD  . MET B  309 ? 0.4976 0.6140 0.4917 -0.0053 0.0873  -0.0811 335 MET B SD  
16689 C CE  . MET B  309 ? 0.4727 0.6058 0.4726 -0.0082 0.0851  -0.0791 335 MET B CE  
16699 N N   . LEU B  310 ? 0.3085 0.4393 0.3266 0.0049  0.0641  -0.0646 336 LEU B N   
16700 C CA  . LEU B  310 ? 0.3027 0.4413 0.3262 0.0047  0.0573  -0.0609 336 LEU B CA  
16701 C C   . LEU B  310 ? 0.2991 0.4422 0.3304 0.0131  0.0571  -0.0577 336 LEU B C   
16702 O O   . LEU B  310 ? 0.2946 0.4341 0.3261 0.0145  0.0534  -0.0555 336 LEU B O   
16703 C CB  . LEU B  310 ? 0.3128 0.4418 0.3296 -0.0007 0.0527  -0.0608 336 LEU B CB  
16704 C CG  . LEU B  310 ? 0.3344 0.4598 0.3435 -0.0092 0.0519  -0.0632 336 LEU B CG  
16705 C CD1 . LEU B  310 ? 0.3386 0.4550 0.3420 -0.0135 0.0477  -0.0627 336 LEU B CD1 
16706 C CD2 . LEU B  310 ? 0.3433 0.4803 0.3556 -0.0133 0.0492  -0.0622 336 LEU B CD2 
16718 N N   . PRO B  311 ? 0.2970 0.4494 0.3352 0.0188  0.0609  -0.0570 337 PRO B N   
16719 C CA  . PRO B  311 ? 0.2968 0.4544 0.3425 0.0272  0.0607  -0.0535 337 PRO B CA  
16720 C C   . PRO B  311 ? 0.2863 0.4554 0.3383 0.0271  0.0539  -0.0500 337 PRO B C   
16721 O O   . PRO B  311 ? 0.2929 0.4642 0.3491 0.0333  0.0527  -0.0470 337 PRO B O   
16722 C CB  . PRO B  311 ? 0.3025 0.4674 0.3538 0.0328  0.0670  -0.0540 337 PRO B CB  
16723 C CG  . PRO B  311 ? 0.3091 0.4798 0.3590 0.0264  0.0676  -0.0565 337 PRO B CG  
16724 C CD  . PRO B  311 ? 0.2977 0.4562 0.3373 0.0183  0.0658  -0.0592 337 PRO B CD  
16732 N N   . ARG B  312 ? 0.2785 0.4544 0.3304 0.0201  0.0496  -0.0504 338 ARG B N   
16733 C CA  . ARG B  312 ? 0.2771 0.4629 0.3339 0.0188  0.0431  -0.0478 338 ARG B CA  
16734 C C   . ARG B  312 ? 0.2583 0.4360 0.3093 0.0133  0.0378  -0.0476 338 ARG B C   
16735 O O   . ARG B  312 ? 0.2558 0.4401 0.3097 0.0114  0.0326  -0.0459 338 ARG B O   
16736 C CB  . ARG B  312 ? 0.3210 0.5206 0.3828 0.0148  0.0423  -0.0483 338 ARG B CB  
16737 C CG  . ARG B  312 ? 0.4040 0.6195 0.4760 0.0201  0.0418  -0.0458 338 ARG B CG  
16738 C CD  . ARG B  312 ? 0.4721 0.6972 0.5487 0.0205  0.0465  -0.0470 338 ARG B CD  
16739 N NE  . ARG B  312 ? 0.5478 0.7658 0.6226 0.0258  0.0535  -0.0483 338 ARG B NE  
16740 C CZ  . ARG B  312 ? 0.5870 0.8113 0.6652 0.0278  0.0590  -0.0494 338 ARG B CZ  
16741 N NH1 . ARG B  312 ? 0.5905 0.8290 0.6746 0.0247  0.0582  -0.0493 338 ARG B NH1 
16742 N NH2 . ARG B  312 ? 0.5828 0.7989 0.6586 0.0327  0.0657  -0.0508 338 ARG B NH2 
16756 N N   . LEU B  313 ? 0.2377 0.4015 0.2807 0.0106  0.0391  -0.0494 339 LEU B N   
16757 C CA  . LEU B  313 ? 0.2291 0.3858 0.2671 0.0057  0.0344  -0.0489 339 LEU B CA  
16758 C C   . LEU B  313 ? 0.2167 0.3722 0.2568 0.0102  0.0313  -0.0460 339 LEU B C   
16759 O O   . LEU B  313 ? 0.2113 0.3631 0.2524 0.0166  0.0341  -0.0451 339 LEU B O   
16760 C CB  . LEU B  313 ? 0.2402 0.3834 0.2696 0.0021  0.0368  -0.0514 339 LEU B CB  
16761 C CG  . LEU B  313 ? 0.2488 0.3855 0.2727 -0.0041 0.0323  -0.0512 339 LEU B CG  
16762 C CD1 . LEU B  313 ? 0.2454 0.3871 0.2679 -0.0112 0.0304  -0.0520 339 LEU B CD1 
16763 C CD2 . LEU B  313 ? 0.2628 0.3860 0.2794 -0.0054 0.0345  -0.0529 339 LEU B CD2 
16775 N N   . GLU B  314 ? 0.2131 0.3717 0.2538 0.0069  0.0257  -0.0446 340 GLU B N   
16776 C CA  . GLU B  314 ? 0.2162 0.3743 0.2584 0.0105  0.0223  -0.0419 340 GLU B CA  
16777 C C   . GLU B  314 ? 0.2205 0.3671 0.2565 0.0071  0.0199  -0.0417 340 GLU B C   
16778 O O   . GLU B  314 ? 0.2316 0.3733 0.2671 0.0111  0.0194  -0.0399 340 GLU B O   
16779 C CB  . GLU B  314 ? 0.2350 0.4057 0.2827 0.0098  0.0179  -0.0404 340 GLU B CB  
16780 C CG  . GLU B  314 ? 0.2884 0.4719 0.3434 0.0140  0.0199  -0.0399 340 GLU B CG  
16781 C CD  . GLU B  314 ? 0.3583 0.5551 0.4187 0.0122  0.0156  -0.0390 340 GLU B CD  
16782 O OE1 . GLU B  314 ? 0.3905 0.5860 0.4490 0.0090  0.0110  -0.0384 340 GLU B OE1 
16783 O OE2 . GLU B  314 ? 0.3631 0.5718 0.4296 0.0137  0.0169  -0.0390 340 GLU B OE2 
16790 N N   . ILE B  315 ? 0.2108 0.3537 0.2424 0.0001  0.0184  -0.0431 341 ILE B N   
16791 C CA  . ILE B  315 ? 0.2128 0.3460 0.2391 -0.0032 0.0161  -0.0427 341 ILE B CA  
16792 C C   . ILE B  315 ? 0.2212 0.3464 0.2414 -0.0078 0.0185  -0.0451 341 ILE B C   
16793 O O   . ILE B  315 ? 0.2300 0.3585 0.2492 -0.0122 0.0190  -0.0466 341 ILE B O   
16794 C CB  . ILE B  315 ? 0.2154 0.3521 0.2423 -0.0072 0.0108  -0.0414 341 ILE B CB  
16795 C CG1 . ILE B  315 ? 0.2237 0.3695 0.2563 -0.0032 0.0083  -0.0395 341 ILE B CG1 
16796 C CG2 . ILE B  315 ? 0.2244 0.3514 0.2465 -0.0098 0.0087  -0.0405 341 ILE B CG2 
16797 C CD1 . ILE B  315 ? 0.2494 0.3988 0.2827 -0.0071 0.0036  -0.0387 341 ILE B CD1 
16809 N N   . LEU B  316 ? 0.2137 0.3285 0.2297 -0.0071 0.0200  -0.0454 342 LEU B N   
16810 C CA  . LEU B  316 ? 0.2227 0.3295 0.2323 -0.0117 0.0222  -0.0478 342 LEU B CA  
16811 C C   . LEU B  316 ? 0.2261 0.3257 0.2319 -0.0149 0.0190  -0.0466 342 LEU B C   
16812 O O   . LEU B  316 ? 0.2391 0.3337 0.2453 -0.0114 0.0189  -0.0452 342 LEU B O   
16813 C CB  . LEU B  316 ? 0.2320 0.3326 0.2400 -0.0077 0.0279  -0.0498 342 LEU B CB  
16814 C CG  . LEU B  316 ? 0.2605 0.3518 0.2611 -0.0124 0.0307  -0.0530 342 LEU B CG  
16815 C CD1 . LEU B  316 ? 0.2668 0.3624 0.2645 -0.0187 0.0302  -0.0548 342 LEU B CD1 
16816 C CD2 . LEU B  316 ? 0.2694 0.3546 0.2689 -0.0080 0.0370  -0.0552 342 LEU B CD2 
16828 N N   . ASP B  317 ? 0.2199 0.3193 0.2225 -0.0212 0.0164  -0.0468 343 ASP B N   
16829 C CA  . ASP B  317 ? 0.2240 0.3176 0.2235 -0.0244 0.0134  -0.0453 343 ASP B CA  
16830 C C   . ASP B  317 ? 0.2354 0.3222 0.2284 -0.0293 0.0150  -0.0475 343 ASP B C   
16831 O O   . ASP B  317 ? 0.2409 0.3302 0.2312 -0.0341 0.0147  -0.0486 343 ASP B O   
16832 C CB  . ASP B  317 ? 0.2383 0.3370 0.2397 -0.0273 0.0086  -0.0430 343 ASP B CB  
16833 C CG  . ASP B  317 ? 0.2795 0.3733 0.2796 -0.0284 0.0055  -0.0407 343 ASP B CG  
16834 O OD1 . ASP B  317 ? 0.2650 0.3517 0.2616 -0.0295 0.0066  -0.0413 343 ASP B OD1 
16835 O OD2 . ASP B  317 ? 0.3206 0.4178 0.3235 -0.0282 0.0022  -0.0385 343 ASP B OD2 
16840 N N   . LEU B  318 ? 0.2284 0.3069 0.2188 -0.0283 0.0168  -0.0483 344 LEU B N   
16841 C CA  . LEU B  318 ? 0.2385 0.3102 0.2225 -0.0332 0.0183  -0.0506 344 LEU B CA  
16842 C C   . LEU B  318 ? 0.2318 0.2988 0.2140 -0.0360 0.0151  -0.0487 344 LEU B C   
16843 O O   . LEU B  318 ? 0.2315 0.2915 0.2092 -0.0389 0.0166  -0.0505 344 LEU B O   
16844 C CB  . LEU B  318 ? 0.2482 0.3131 0.2302 -0.0301 0.0239  -0.0537 344 LEU B CB  
16845 C CG  . LEU B  318 ? 0.2642 0.3327 0.2463 -0.0286 0.0280  -0.0563 344 LEU B CG  
16846 C CD1 . LEU B  318 ? 0.2698 0.3330 0.2530 -0.0226 0.0333  -0.0578 344 LEU B CD1 
16847 C CD2 . LEU B  318 ? 0.2788 0.3463 0.2544 -0.0353 0.0291  -0.0594 344 LEU B CD2 
16859 N N   . SER B  319 ? 0.2172 0.2883 0.2030 -0.0356 0.0108  -0.0453 345 SER B N   
16860 C CA  . SER B  319 ? 0.2155 0.2831 0.2006 -0.0376 0.0079  -0.0431 345 SER B CA  
16861 C C   . SER B  319 ? 0.2155 0.2823 0.1959 -0.0446 0.0062  -0.0435 345 SER B C   
16862 O O   . SER B  319 ? 0.2126 0.2834 0.1910 -0.0480 0.0058  -0.0444 345 SER B O   
16863 C CB  . SER B  319 ? 0.2161 0.2885 0.2059 -0.0354 0.0042  -0.0395 345 SER B CB  
16864 O OG  . SER B  319 ? 0.2176 0.2910 0.2114 -0.0291 0.0053  -0.0389 345 SER B OG  
16870 N N   . PHE B  320 ? 0.2103 0.2724 0.1891 -0.0467 0.0051  -0.0427 346 PHE B N   
16871 C CA  . PHE B  320 ? 0.2183 0.2801 0.1932 -0.0531 0.0030  -0.0424 346 PHE B CA  
16872 C C   . PHE B  320 ? 0.2305 0.2915 0.1995 -0.0577 0.0051  -0.0461 346 PHE B C   
16873 O O   . PHE B  320 ? 0.2342 0.2996 0.2007 -0.0624 0.0030  -0.0456 346 PHE B O   
16874 C CB  . PHE B  320 ? 0.2173 0.2854 0.1949 -0.0546 -0.0016 -0.0385 346 PHE B CB  
16875 C CG  . PHE B  320 ? 0.2235 0.2909 0.2054 -0.0514 -0.0036 -0.0352 346 PHE B CG  
16876 C CD1 . PHE B  320 ? 0.2363 0.3001 0.2175 -0.0534 -0.0046 -0.0340 346 PHE B CD1 
16877 C CD2 . PHE B  320 ? 0.2288 0.2990 0.2154 -0.0465 -0.0043 -0.0335 346 PHE B CD2 
16878 C CE1 . PHE B  320 ? 0.2417 0.3047 0.2269 -0.0502 -0.0060 -0.0311 346 PHE B CE1 
16879 C CE2 . PHE B  320 ? 0.2386 0.3079 0.2286 -0.0435 -0.0058 -0.0307 346 PHE B CE2 
16880 C CZ  . PHE B  320 ? 0.2391 0.3046 0.2283 -0.0452 -0.0065 -0.0295 346 PHE B CZ  
16890 N N   . ASN B  321 ? 0.2308 0.2857 0.1972 -0.0564 0.0096  -0.0498 347 ASN B N   
16891 C CA  . ASN B  321 ? 0.2363 0.2887 0.1962 -0.0609 0.0124  -0.0539 347 ASN B CA  
16892 C C   . ASN B  321 ? 0.2500 0.2946 0.2054 -0.0648 0.0134  -0.0560 347 ASN B C   
16893 O O   . ASN B  321 ? 0.2732 0.3137 0.2226 -0.0683 0.0165  -0.0603 347 ASN B O   
16894 C CB  . ASN B  321 ? 0.2411 0.2922 0.2011 -0.0567 0.0173  -0.0570 347 ASN B CB  
16895 C CG  . ASN B  321 ? 0.2433 0.3027 0.2051 -0.0562 0.0166  -0.0563 347 ASN B CG  
16896 O OD1 . ASN B  321 ? 0.2376 0.2988 0.1948 -0.0601 0.0177  -0.0585 347 ASN B OD1 
16897 N ND2 . ASN B  321 ? 0.2418 0.3065 0.2099 -0.0517 0.0148  -0.0533 347 ASN B ND2 
16904 N N   . TYR B  322 ? 0.2352 0.2783 0.1933 -0.0648 0.0108  -0.0532 348 TYR B N   
16905 C CA  . TYR B  322 ? 0.2392 0.2755 0.1938 -0.0687 0.0117  -0.0549 348 TYR B CA  
16906 C C   . TYR B  322 ? 0.2527 0.2899 0.2004 -0.0769 0.0107  -0.0574 348 TYR B C   
16907 O O   . TYR B  322 ? 0.2502 0.2949 0.1969 -0.0800 0.0076  -0.0560 348 TYR B O   
16908 C CB  . TYR B  322 ? 0.2292 0.2660 0.1883 -0.0680 0.0084  -0.0507 348 TYR B CB  
16909 C CG  . TYR B  322 ? 0.2390 0.2839 0.1996 -0.0716 0.0029  -0.0469 348 TYR B CG  
16910 C CD1 . TYR B  322 ? 0.2433 0.2944 0.2091 -0.0678 0.0001  -0.0429 348 TYR B CD1 
16911 C CD2 . TYR B  322 ? 0.2510 0.2970 0.2081 -0.0785 0.0007  -0.0470 348 TYR B CD2 
16912 C CE1 . TYR B  322 ? 0.2521 0.3097 0.2195 -0.0705 -0.0045 -0.0391 348 TYR B CE1 
16913 C CE2 . TYR B  322 ? 0.2559 0.3097 0.2147 -0.0813 -0.0042 -0.0430 348 TYR B CE2 
16914 C CZ  . TYR B  322 ? 0.2646 0.3237 0.2288 -0.0770 -0.0066 -0.0389 348 TYR B CZ  
16915 O OH  . TYR B  322 ? 0.2942 0.3601 0.2603 -0.0793 -0.0110 -0.0346 348 TYR B OH  
16925 N N   . ILE B  323 ? 0.2667 0.2963 0.2098 -0.0806 0.0134  -0.0611 349 ILE B N   
16926 C CA  . ILE B  323 ? 0.2870 0.3171 0.2230 -0.0889 0.0125  -0.0639 349 ILE B CA  
16927 C C   . ILE B  323 ? 0.2922 0.3246 0.2302 -0.0927 0.0080  -0.0606 349 ILE B C   
16928 O O   . ILE B  323 ? 0.2910 0.3174 0.2311 -0.0916 0.0093  -0.0605 349 ILE B O   
16929 C CB  . ILE B  323 ? 0.3042 0.3242 0.2335 -0.0913 0.0181  -0.0703 349 ILE B CB  
16930 C CG1 . ILE B  323 ? 0.3303 0.3491 0.2574 -0.0879 0.0226  -0.0735 349 ILE B CG1 
16931 C CG2 . ILE B  323 ? 0.3119 0.3320 0.2337 -0.1009 0.0166  -0.0732 349 ILE B CG2 
16932 C CD1 . ILE B  323 ? 0.3580 0.3645 0.2807 -0.0867 0.0298  -0.0793 349 ILE B CD1 
16944 N N   . LYS B  324 ? 0.2961 0.3376 0.2338 -0.0971 0.0030  -0.0577 350 LYS B N   
16945 C CA  . LYS B  324 ? 0.3050 0.3504 0.2451 -0.1007 -0.0014 -0.0541 350 LYS B CA  
16946 C C   . LYS B  324 ? 0.3264 0.3650 0.2621 -0.1064 0.0004  -0.0579 350 LYS B C   
16947 O O   . LYS B  324 ? 0.3247 0.3601 0.2530 -0.1114 0.0027  -0.0629 350 LYS B O   
16948 C CB  . LYS B  324 ? 0.3173 0.3732 0.2560 -0.1053 -0.0063 -0.0512 350 LYS B CB  
16949 C CG  . LYS B  324 ? 0.3411 0.4026 0.2827 -0.1090 -0.0110 -0.0469 350 LYS B CG  
16950 C CD  . LYS B  324 ? 0.3844 0.4563 0.3240 -0.1137 -0.0157 -0.0439 350 LYS B CD  
16951 C CE  . LYS B  324 ? 0.4330 0.5102 0.3746 -0.1184 -0.0197 -0.0407 350 LYS B CE  
16952 N NZ  . LYS B  324 ? 0.4575 0.5453 0.3974 -0.1227 -0.0244 -0.0372 350 LYS B NZ  
16966 N N   . GLY B  325 ? 0.3362 0.3723 0.2763 -0.1056 -0.0002 -0.0558 351 GLY B N   
16967 C CA  . GLY B  325 ? 0.3574 0.3869 0.2940 -0.1112 0.0015  -0.0591 351 GLY B CA  
16968 C C   . GLY B  325 ? 0.3709 0.3875 0.3051 -0.1086 0.0080  -0.0638 351 GLY B C   
16969 O O   . GLY B  325 ? 0.3777 0.3875 0.3093 -0.1130 0.0100  -0.0666 351 GLY B O   
16973 N N   . SER B  326 ? 0.3620 0.3753 0.2973 -0.1014 0.0115  -0.0646 352 SER B N   
16974 C CA  . SER B  326 ? 0.3633 0.3645 0.2969 -0.0979 0.0179  -0.0685 352 SER B CA  
16975 C C   . SER B  326 ? 0.3531 0.3519 0.2940 -0.0890 0.0190  -0.0645 352 SER B C   
16976 O O   . SER B  326 ? 0.3449 0.3498 0.2901 -0.0833 0.0174  -0.0614 352 SER B O   
16977 C CB  . SER B  326 ? 0.3870 0.3863 0.3159 -0.0964 0.0216  -0.0726 352 SER B CB  
16978 O OG  . SER B  326 ? 0.4194 0.4072 0.3469 -0.0923 0.0281  -0.0761 352 SER B OG  
16984 N N   . TYR B  327 ? 0.3488 0.3386 0.2908 -0.0881 0.0220  -0.0649 353 TYR B N   
16985 C CA  . TYR B  327 ? 0.3424 0.3292 0.2905 -0.0801 0.0234  -0.0611 353 TYR B CA  
16986 C C   . TYR B  327 ? 0.3564 0.3301 0.3019 -0.0771 0.0304  -0.0647 353 TYR B C   
16987 O O   . TYR B  327 ? 0.3695 0.3348 0.3144 -0.0788 0.0328  -0.0653 353 TYR B O   
16988 C CB  . TYR B  327 ? 0.3264 0.3154 0.2785 -0.0824 0.0201  -0.0571 353 TYR B CB  
16989 C CG  . TYR B  327 ? 0.3179 0.3055 0.2764 -0.0751 0.0205  -0.0525 353 TYR B CG  
16990 C CD1 . TYR B  327 ? 0.3180 0.3070 0.2798 -0.0666 0.0215  -0.0505 353 TYR B CD1 
16991 C CD2 . TYR B  327 ? 0.3232 0.3093 0.2845 -0.0769 0.0195  -0.0498 353 TYR B CD2 
16992 C CE1 . TYR B  327 ? 0.3175 0.3065 0.2847 -0.0602 0.0212  -0.0461 353 TYR B CE1 
16993 C CE2 . TYR B  327 ? 0.3290 0.3144 0.2957 -0.0703 0.0198  -0.0454 353 TYR B CE2 
16994 C CZ  . TYR B  327 ? 0.3311 0.3179 0.3005 -0.0620 0.0205  -0.0435 353 TYR B CZ  
16995 O OH  . TYR B  327 ? 0.3339 0.3204 0.3081 -0.0558 0.0207  -0.0392 353 TYR B OH  
17005 N N   . PRO B  328 ? 0.3531 0.3245 0.2967 -0.0729 0.0341  -0.0674 354 PRO B N   
17006 C CA  . PRO B  328 ? 0.3626 0.3211 0.3033 -0.0702 0.0413  -0.0711 354 PRO B CA  
17007 C C   . PRO B  328 ? 0.3705 0.3231 0.3162 -0.0625 0.0440  -0.0675 354 PRO B C   
17008 O O   . PRO B  328 ? 0.3547 0.3144 0.3064 -0.0573 0.0406  -0.0624 354 PRO B O   
17009 C CB  . PRO B  328 ? 0.3669 0.3272 0.3055 -0.0671 0.0438  -0.0738 354 PRO B CB  
17010 C CG  . PRO B  328 ? 0.3626 0.3365 0.3062 -0.0643 0.0382  -0.0695 354 PRO B CG  
17011 C CD  . PRO B  328 ? 0.3403 0.3206 0.2842 -0.0709 0.0322  -0.0672 354 PRO B CD  
17019 N N   . GLN B  329 ? 0.3809 0.3204 0.3239 -0.0615 0.0502  -0.0703 355 GLN B N   
17020 C CA  . GLN B  329 ? 0.3965 0.3294 0.3438 -0.0539 0.0534  -0.0668 355 GLN B CA  
17021 C C   . GLN B  329 ? 0.3880 0.3261 0.3401 -0.0439 0.0540  -0.0637 355 GLN B C   
17022 O O   . GLN B  329 ? 0.3791 0.3200 0.3366 -0.0379 0.0525  -0.0586 355 GLN B O   
17023 C CB  . GLN B  329 ? 0.4435 0.3603 0.3864 -0.0548 0.0608  -0.0707 355 GLN B CB  
17024 C CG  . GLN B  329 ? 0.5331 0.4438 0.4724 -0.0641 0.0605  -0.0728 355 GLN B CG  
17025 C CD  . GLN B  329 ? 0.6319 0.5444 0.5764 -0.0632 0.0576  -0.0673 355 GLN B CD  
17026 O OE1 . GLN B  329 ? 0.6659 0.5808 0.6160 -0.0550 0.0572  -0.0622 355 GLN B OE1 
17027 N NE2 . GLN B  329 ? 0.6530 0.5649 0.5958 -0.0718 0.0554  -0.0683 355 GLN B NE2 
17036 N N   . HIS B  330 ? 0.3874 0.3272 0.3374 -0.0424 0.0562  -0.0669 356 HIS B N   
17037 C CA  . HIS B  330 ? 0.3908 0.3354 0.3453 -0.0332 0.0574  -0.0645 356 HIS B CA  
17038 C C   . HIS B  330 ? 0.3776 0.3336 0.3323 -0.0340 0.0544  -0.0655 356 HIS B C   
17039 O O   . HIS B  330 ? 0.3805 0.3381 0.3303 -0.0412 0.0532  -0.0693 356 HIS B O   
17040 C CB  . HIS B  330 ? 0.4203 0.3529 0.3728 -0.0281 0.0656  -0.0671 356 HIS B CB  
17041 C CG  . HIS B  330 ? 0.4659 0.3852 0.4174 -0.0277 0.0697  -0.0666 356 HIS B CG  
17042 N ND1 . HIS B  330 ? 0.4960 0.4020 0.4412 -0.0326 0.0752  -0.0718 356 HIS B ND1 
17043 C CD2 . HIS B  330 ? 0.4815 0.3992 0.4372 -0.0235 0.0690  -0.0615 356 HIS B CD2 
17044 C CE1 . HIS B  330 ? 0.5061 0.4025 0.4522 -0.0311 0.0778  -0.0697 356 HIS B CE1 
17045 N NE2 . HIS B  330 ? 0.5039 0.4071 0.4563 -0.0257 0.0742  -0.0633 356 HIS B NE2 
17053 N N   . ILE B  331 ? 0.3603 0.3241 0.3204 -0.0264 0.0535  -0.0623 357 ILE B N   
17054 C CA  . ILE B  331 ? 0.3556 0.3300 0.3169 -0.0259 0.0515  -0.0629 357 ILE B CA  
17055 C C   . ILE B  331 ? 0.3632 0.3322 0.3220 -0.0229 0.0582  -0.0669 357 ILE B C   
17056 O O   . ILE B  331 ? 0.3660 0.3268 0.3258 -0.0171 0.0635  -0.0666 357 ILE B O   
17057 C CB  . ILE B  331 ? 0.3467 0.3326 0.3151 -0.0199 0.0472  -0.0577 357 ILE B CB  
17058 C CG1 . ILE B  331 ? 0.3560 0.3531 0.3251 -0.0214 0.0445  -0.0586 357 ILE B CG1 
17059 C CG2 . ILE B  331 ? 0.3445 0.3286 0.3177 -0.0102 0.0506  -0.0549 357 ILE B CG2 
17060 C CD1 . ILE B  331 ? 0.3645 0.3735 0.3397 -0.0182 0.0390  -0.0540 357 ILE B CD1 
17072 N N   . ASN B  332 ? 0.3663 0.3395 0.3216 -0.0271 0.0582  -0.0706 358 ASN B N   
17073 C CA  . ASN B  332 ? 0.3819 0.3506 0.3344 -0.0248 0.0647  -0.0747 358 ASN B CA  
17074 C C   . ASN B  332 ? 0.3728 0.3537 0.3298 -0.0205 0.0635  -0.0733 358 ASN B C   
17075 O O   . ASN B  332 ? 0.3695 0.3581 0.3245 -0.0253 0.0606  -0.0746 358 ASN B O   
17076 C CB  . ASN B  332 ? 0.4118 0.3740 0.3554 -0.0335 0.0667  -0.0807 358 ASN B CB  
17077 C CG  . ASN B  332 ? 0.4763 0.4308 0.4159 -0.0315 0.0744  -0.0856 358 ASN B CG  
17078 O OD1 . ASN B  332 ? 0.4936 0.4486 0.4376 -0.0233 0.0784  -0.0844 358 ASN B OD1 
17079 N ND2 . ASN B  332 ? 0.5015 0.4491 0.4326 -0.0390 0.0769  -0.0913 358 ASN B ND2 
17086 N N   . ILE B  333 ? 0.3675 0.3502 0.3306 -0.0114 0.0660  -0.0704 359 ILE B N   
17087 C CA  . ILE B  333 ? 0.3644 0.3589 0.3331 -0.0062 0.0653  -0.0685 359 ILE B CA  
17088 C C   . ILE B  333 ? 0.3662 0.3570 0.3336 -0.0025 0.0726  -0.0720 359 ILE B C   
17089 O O   . ILE B  333 ? 0.3687 0.3502 0.3364 0.0029  0.0782  -0.0721 359 ILE B O   
17090 C CB  . ILE B  333 ? 0.3673 0.3671 0.3438 0.0016  0.0630  -0.0627 359 ILE B CB  
17091 C CG1 . ILE B  333 ? 0.3761 0.3796 0.3538 -0.0018 0.0561  -0.0593 359 ILE B CG1 
17092 C CG2 . ILE B  333 ? 0.3728 0.3847 0.3555 0.0073  0.0627  -0.0608 359 ILE B CG2 
17093 C CD1 . ILE B  333 ? 0.3830 0.3966 0.3603 -0.0080 0.0502  -0.0594 359 ILE B CD1 
17105 N N   . SER B  334 ? 0.3597 0.3578 0.3259 -0.0050 0.0728  -0.0744 360 SER B N   
17106 C CA  . SER B  334 ? 0.3701 0.3658 0.3352 -0.0017 0.0798  -0.0778 360 SER B CA  
17107 C C   . SER B  334 ? 0.3842 0.3831 0.3572 0.0089  0.0831  -0.0744 360 SER B C   
17108 O O   . SER B  334 ? 0.3860 0.3953 0.3660 0.0128  0.0785  -0.0696 360 SER B O   
17109 C CB  . SER B  334 ? 0.3722 0.3780 0.3361 -0.0057 0.0784  -0.0798 360 SER B CB  
17110 O OG  . SER B  334 ? 0.3809 0.3854 0.3441 -0.0022 0.0853  -0.0829 360 SER B OG  
17116 N N   . ARG B  335 ? 0.3970 0.3877 0.3688 0.0136  0.0911  -0.0769 361 ARG B N   
17117 C CA  . ARG B  335 ? 0.4041 0.3989 0.3835 0.0241  0.0949  -0.0736 361 ARG B CA  
17118 C C   . ARG B  335 ? 0.3845 0.3967 0.3702 0.0259  0.0920  -0.0719 361 ARG B C   
17119 O O   . ARG B  335 ? 0.3785 0.3992 0.3723 0.0336  0.0916  -0.0675 361 ARG B O   
17120 C CB  . ARG B  335 ? 0.4514 0.4344 0.4279 0.0282  0.1046  -0.0773 361 ARG B CB  
17121 C CG  . ARG B  335 ? 0.5448 0.5107 0.5176 0.0296  0.1087  -0.0777 361 ARG B CG  
17122 C CD  . ARG B  335 ? 0.6449 0.6006 0.6172 0.0363  0.1187  -0.0800 361 ARG B CD  
17123 N NE  . ARG B  335 ? 0.7330 0.6714 0.7018 0.0380  0.1234  -0.0803 361 ARG B NE  
17124 C CZ  . ARG B  335 ? 0.8038 0.7278 0.7635 0.0304  0.1258  -0.0855 361 ARG B CZ  
17125 N NH1 . ARG B  335 ? 0.8238 0.7322 0.7812 0.0324  0.1304  -0.0855 361 ARG B NH1 
17126 N NH2 . ARG B  335 ? 0.8123 0.7375 0.7651 0.0206  0.1235  -0.0907 361 ARG B NH2 
17140 N N   . ASN B  336 ? 0.3674 0.3850 0.3491 0.0184  0.0898  -0.0751 362 ASN B N   
17141 C CA  . ASN B  336 ? 0.3576 0.3910 0.3446 0.0188  0.0871  -0.0737 362 ASN B CA  
17142 C C   . ASN B  336 ? 0.3427 0.3882 0.3366 0.0198  0.0793  -0.0684 362 ASN B C   
17143 O O   . ASN B  336 ? 0.3383 0.3972 0.3381 0.0214  0.0774  -0.0666 362 ASN B O   
17144 C CB  . ASN B  336 ? 0.3710 0.4063 0.3515 0.0101  0.0864  -0.0780 362 ASN B CB  
17145 C CG  . ASN B  336 ? 0.4290 0.4562 0.4036 0.0096  0.0944  -0.0834 362 ASN B CG  
17146 O OD1 . ASN B  336 ? 0.4433 0.4677 0.4209 0.0171  0.1010  -0.0836 362 ASN B OD1 
17147 N ND2 . ASN B  336 ? 0.4427 0.4663 0.4086 0.0010  0.0941  -0.0877 362 ASN B ND2 
17154 N N   . PHE B  337 ? 0.3304 0.3715 0.3237 0.0186  0.0749  -0.0659 363 PHE B N   
17155 C CA  . PHE B  337 ? 0.3147 0.3664 0.3143 0.0204  0.0682  -0.0610 363 PHE B CA  
17156 C C   . PHE B  337 ? 0.3116 0.3708 0.3198 0.0303  0.0701  -0.0572 363 PHE B C   
17157 O O   . PHE B  337 ? 0.3063 0.3779 0.3206 0.0319  0.0654  -0.0539 363 PHE B O   
17158 C CB  . PHE B  337 ? 0.3062 0.3508 0.3034 0.0180  0.0642  -0.0591 363 PHE B CB  
17159 C CG  . PHE B  337 ? 0.2959 0.3409 0.2883 0.0088  0.0588  -0.0603 363 PHE B CG  
17160 C CD1 . PHE B  337 ? 0.3049 0.3406 0.2893 0.0020  0.0606  -0.0645 363 PHE B CD1 
17161 C CD2 . PHE B  337 ? 0.2913 0.3464 0.2872 0.0068  0.0521  -0.0574 363 PHE B CD2 
17162 C CE1 . PHE B  337 ? 0.3066 0.3435 0.2870 -0.0061 0.0556  -0.0651 363 PHE B CE1 
17163 C CE2 . PHE B  337 ? 0.2973 0.3525 0.2891 -0.0011 0.0475  -0.0581 363 PHE B CE2 
17164 C CZ  . PHE B  337 ? 0.3022 0.3489 0.2865 -0.0073 0.0492  -0.0617 363 PHE B CZ  
17174 N N   . SER B  338 ? 0.3120 0.3639 0.3208 0.0368  0.0771  -0.0577 364 SER B N   
17175 C CA  . SER B  338 ? 0.3143 0.3733 0.3312 0.0467  0.0796  -0.0539 364 SER B CA  
17176 C C   . SER B  338 ? 0.3207 0.3950 0.3435 0.0481  0.0797  -0.0539 364 SER B C   
17177 O O   . SER B  338 ? 0.3257 0.4098 0.3564 0.0556  0.0801  -0.0502 364 SER B O   
17178 C CB  . SER B  338 ? 0.3264 0.3728 0.3418 0.0529  0.0879  -0.0548 364 SER B CB  
17179 O OG  . SER B  338 ? 0.3698 0.4122 0.3817 0.0514  0.0940  -0.0596 364 SER B OG  
17185 N N   . LYS B  339 ? 0.3149 0.3913 0.3337 0.0410  0.0795  -0.0579 365 LYS B N   
17186 C CA  . LYS B  339 ? 0.3137 0.4042 0.3375 0.0410  0.0796  -0.0582 365 LYS B CA  
17187 C C   . LYS B  339 ? 0.3029 0.4069 0.3307 0.0372  0.0716  -0.0556 365 LYS B C   
17188 O O   . LYS B  339 ? 0.3018 0.4189 0.3349 0.0375  0.0711  -0.0552 365 LYS B O   
17189 C CB  . LYS B  339 ? 0.3491 0.4351 0.3662 0.0350  0.0836  -0.0636 365 LYS B CB  
17190 C CG  . LYS B  339 ? 0.4148 0.4862 0.4264 0.0375  0.0919  -0.0672 365 LYS B CG  
17191 C CD  . LYS B  339 ? 0.4915 0.5656 0.5100 0.0478  0.0982  -0.0654 365 LYS B CD  
17192 C CE  . LYS B  339 ? 0.5642 0.6236 0.5769 0.0499  0.1072  -0.0695 365 LYS B CE  
17193 N NZ  . LYS B  339 ? 0.5942 0.6530 0.6135 0.0611  0.1131  -0.0666 365 LYS B NZ  
17207 N N   . LEU B  340 ? 0.2926 0.3937 0.3182 0.0337  0.0657  -0.0540 366 LEU B N   
17208 C CA  . LEU B  340 ? 0.2841 0.3965 0.3132 0.0303  0.0584  -0.0516 366 LEU B CA  
17209 C C   . LEU B  340 ? 0.2766 0.3985 0.3140 0.0379  0.0565  -0.0470 366 LEU B C   
17210 O O   . LEU B  340 ? 0.2706 0.3923 0.3085 0.0384  0.0519  -0.0442 366 LEU B O   
17211 C CB  . LEU B  340 ? 0.2850 0.3900 0.3083 0.0239  0.0535  -0.0518 366 LEU B CB  
17212 C CG  . LEU B  340 ? 0.2978 0.3940 0.3126 0.0160  0.0545  -0.0559 366 LEU B CG  
17213 C CD1 . LEU B  340 ? 0.3051 0.3942 0.3153 0.0111  0.0497  -0.0552 366 LEU B CD1 
17214 C CD2 . LEU B  340 ? 0.2943 0.3995 0.3092 0.0108  0.0534  -0.0576 366 LEU B CD2 
17226 N N   . LEU B  341 ? 0.2725 0.4040 0.3164 0.0435  0.0599  -0.0462 367 LEU B N   
17227 C CA  . LEU B  341 ? 0.2712 0.4132 0.3235 0.0514  0.0589  -0.0418 367 LEU B CA  
17228 C C   . LEU B  341 ? 0.2567 0.4090 0.3123 0.0494  0.0512  -0.0389 367 LEU B C   
17229 O O   . LEU B  341 ? 0.2563 0.4104 0.3148 0.0547  0.0492  -0.0352 367 LEU B O   
17230 C CB  . LEU B  341 ? 0.2784 0.4320 0.3376 0.0560  0.0631  -0.0416 367 LEU B CB  
17231 C CG  . LEU B  341 ? 0.3212 0.4666 0.3781 0.0591  0.0716  -0.0445 367 LEU B CG  
17232 C CD1 . LEU B  341 ? 0.3247 0.4842 0.3901 0.0643  0.0751  -0.0434 367 LEU B CD1 
17233 C CD2 . LEU B  341 ? 0.3402 0.4714 0.3944 0.0652  0.0761  -0.0435 367 LEU B CD2 
17245 N N   . SER B  342 ? 0.2457 0.4040 0.3005 0.0418  0.0470  -0.0406 368 SER B N   
17246 C CA  . SER B  342 ? 0.2375 0.4053 0.2953 0.0393  0.0400  -0.0384 368 SER B CA  
17247 C C   . SER B  342 ? 0.2264 0.3849 0.2780 0.0344  0.0355  -0.0384 368 SER B C   
17248 O O   . SER B  342 ? 0.2217 0.3868 0.2749 0.0316  0.0300  -0.0372 368 SER B O   
17249 C CB  . SER B  342 ? 0.2537 0.4334 0.3145 0.0340  0.0379  -0.0399 368 SER B CB  
17250 O OG  . SER B  342 ? 0.2928 0.4825 0.3600 0.0383  0.0420  -0.0397 368 SER B OG  
17256 N N   . LEU B  343 ? 0.2192 0.3628 0.2640 0.0330  0.0379  -0.0400 369 LEU B N   
17257 C CA  . LEU B  343 ? 0.2156 0.3510 0.2549 0.0281  0.0339  -0.0399 369 LEU B CA  
17258 C C   . LEU B  343 ? 0.2110 0.3492 0.2528 0.0315  0.0297  -0.0362 369 LEU B C   
17259 O O   . LEU B  343 ? 0.2104 0.3483 0.2548 0.0386  0.0315  -0.0337 369 LEU B O   
17260 C CB  . LEU B  343 ? 0.2243 0.3440 0.2567 0.0267  0.0374  -0.0419 369 LEU B CB  
17261 C CG  . LEU B  343 ? 0.2544 0.3664 0.2807 0.0196  0.0338  -0.0428 369 LEU B CG  
17262 C CD1 . LEU B  343 ? 0.2705 0.3875 0.2953 0.0120  0.0313  -0.0449 369 LEU B CD1 
17263 C CD2 . LEU B  343 ? 0.2738 0.3711 0.2939 0.0187  0.0374  -0.0446 369 LEU B CD2 
17275 N N   . ARG B  344 ? 0.2074 0.3484 0.2483 0.0264  0.0243  -0.0359 370 ARG B N   
17276 C CA  . ARG B  344 ? 0.2159 0.3596 0.2581 0.0283  0.0198  -0.0330 370 ARG B CA  
17277 C C   . ARG B  344 ? 0.2135 0.3459 0.2498 0.0247  0.0179  -0.0329 370 ARG B C   
17278 O O   . ARG B  344 ? 0.2086 0.3382 0.2445 0.0280  0.0165  -0.0304 370 ARG B O   
17279 C CB  . ARG B  344 ? 0.2368 0.3932 0.2827 0.0252  0.0152  -0.0328 370 ARG B CB  
17280 C CG  . ARG B  344 ? 0.2855 0.4556 0.3383 0.0288  0.0161  -0.0323 370 ARG B CG  
17281 C CD  . ARG B  344 ? 0.3573 0.5392 0.4134 0.0253  0.0111  -0.0320 370 ARG B CD  
17282 N NE  . ARG B  344 ? 0.4332 0.6295 0.4963 0.0274  0.0117  -0.0318 370 ARG B NE  
17283 C CZ  . ARG B  344 ? 0.4880 0.6938 0.5565 0.0340  0.0115  -0.0291 370 ARG B CZ  
17284 N NH1 . ARG B  344 ? 0.5014 0.7032 0.5690 0.0396  0.0111  -0.0263 370 ARG B NH1 
17285 N NH2 . ARG B  344 ? 0.4867 0.7066 0.5620 0.0352  0.0119  -0.0290 370 ARG B NH2 
17299 N N   . ALA B  345 ? 0.2140 0.3407 0.2458 0.0178  0.0176  -0.0354 371 ALA B N   
17300 C CA  . ALA B  345 ? 0.2209 0.3381 0.2477 0.0140  0.0156  -0.0352 371 ALA B CA  
17301 C C   . ALA B  345 ? 0.2283 0.3363 0.2499 0.0095  0.0183  -0.0380 371 ALA B C   
17302 O O   . ALA B  345 ? 0.2257 0.3366 0.2466 0.0056  0.0191  -0.0402 371 ALA B O   
17303 C CB  . ALA B  345 ? 0.2213 0.3434 0.2484 0.0095  0.0104  -0.0347 371 ALA B CB  
17309 N N   . LEU B  346 ? 0.2239 0.3210 0.2415 0.0096  0.0196  -0.0377 372 LEU B N   
17310 C CA  . LEU B  346 ? 0.2258 0.3139 0.2379 0.0048  0.0219  -0.0404 372 LEU B CA  
17311 C C   . LEU B  346 ? 0.2198 0.3022 0.2286 0.0005  0.0186  -0.0395 372 LEU B C   
17312 O O   . LEU B  346 ? 0.2213 0.2995 0.2303 0.0033  0.0181  -0.0373 372 LEU B O   
17313 C CB  . LEU B  346 ? 0.2316 0.3113 0.2421 0.0088  0.0275  -0.0415 372 LEU B CB  
17314 C CG  . LEU B  346 ? 0.2531 0.3226 0.2573 0.0039  0.0304  -0.0448 372 LEU B CG  
17315 C CD1 . LEU B  346 ? 0.2548 0.3283 0.2568 -0.0016 0.0306  -0.0478 372 LEU B CD1 
17316 C CD2 . LEU B  346 ? 0.2661 0.3268 0.2691 0.0086  0.0365  -0.0459 372 LEU B CD2 
17328 N N   . HIS B  347 ? 0.2105 0.2934 0.2165 -0.0062 0.0164  -0.0407 373 HIS B N   
17329 C CA  . HIS B  347 ? 0.2097 0.2881 0.2129 -0.0105 0.0133  -0.0396 373 HIS B CA  
17330 C C   . HIS B  347 ? 0.2133 0.2834 0.2111 -0.0149 0.0155  -0.0419 373 HIS B C   
17331 O O   . HIS B  347 ? 0.2036 0.2744 0.1986 -0.0189 0.0166  -0.0444 373 HIS B O   
17332 C CB  . HIS B  347 ? 0.2215 0.3066 0.2258 -0.0145 0.0089  -0.0386 373 HIS B CB  
17333 C CG  . HIS B  347 ? 0.2605 0.3540 0.2698 -0.0109 0.0069  -0.0370 373 HIS B CG  
17334 N ND1 . HIS B  347 ? 0.2781 0.3721 0.2891 -0.0086 0.0042  -0.0344 373 HIS B ND1 
17335 C CD2 . HIS B  347 ? 0.2707 0.3723 0.2832 -0.0095 0.0074  -0.0378 373 HIS B CD2 
17336 C CE1 . HIS B  347 ? 0.2817 0.3842 0.2968 -0.0060 0.0029  -0.0339 373 HIS B CE1 
17337 N NE2 . HIS B  347 ? 0.2809 0.3884 0.2972 -0.0066 0.0047  -0.0358 373 HIS B NE2 
17345 N N   . LEU B  348 ? 0.2146 0.2767 0.2105 -0.0143 0.0162  -0.0412 374 LEU B N   
17346 C CA  . LEU B  348 ? 0.2392 0.2928 0.2298 -0.0188 0.0182  -0.0434 374 LEU B CA  
17347 C C   . LEU B  348 ? 0.2540 0.3044 0.2436 -0.0219 0.0150  -0.0413 374 LEU B C   
17348 O O   . LEU B  348 ? 0.2663 0.3088 0.2538 -0.0223 0.0169  -0.0417 374 LEU B O   
17349 C CB  . LEU B  348 ? 0.2482 0.2939 0.2375 -0.0149 0.0237  -0.0452 374 LEU B CB  
17350 C CG  . LEU B  348 ? 0.2706 0.3176 0.2595 -0.0132 0.0279  -0.0482 374 LEU B CG  
17351 C CD1 . LEU B  348 ? 0.2821 0.3223 0.2717 -0.0070 0.0332  -0.0486 374 LEU B CD1 
17352 C CD2 . LEU B  348 ? 0.2787 0.3226 0.2617 -0.0200 0.0293  -0.0521 374 LEU B CD2 
17364 N N   . ARG B  349 ? 0.2532 0.3096 0.2445 -0.0241 0.0105  -0.0391 375 ARG B N   
17365 C CA  . ARG B  349 ? 0.2551 0.3093 0.2458 -0.0272 0.0076  -0.0370 375 ARG B CA  
17366 C C   . ARG B  349 ? 0.2444 0.2955 0.2302 -0.0340 0.0077  -0.0391 375 ARG B C   
17367 O O   . ARG B  349 ? 0.2490 0.3019 0.2324 -0.0365 0.0089  -0.0417 375 ARG B O   
17368 C CB  . ARG B  349 ? 0.2852 0.3463 0.2787 -0.0278 0.0032  -0.0342 375 ARG B CB  
17369 C CG  . ARG B  349 ? 0.3660 0.4311 0.3638 -0.0220 0.0025  -0.0324 375 ARG B CG  
17370 C CD  . ARG B  349 ? 0.4568 0.5255 0.4567 -0.0227 -0.0015 -0.0295 375 ARG B CD  
17371 N NE  . ARG B  349 ? 0.5332 0.6065 0.5327 -0.0272 -0.0038 -0.0297 375 ARG B NE  
17372 C CZ  . ARG B  349 ? 0.6083 0.6839 0.6089 -0.0290 -0.0069 -0.0274 375 ARG B CZ  
17373 N NH1 . ARG B  349 ? 0.6263 0.7004 0.6284 -0.0268 -0.0082 -0.0250 375 ARG B NH1 
17374 N NH2 . ARG B  349 ? 0.6268 0.7060 0.6268 -0.0329 -0.0085 -0.0274 375 ARG B NH2 
17388 N N   . GLY B  350 ? 0.2254 0.2725 0.2098 -0.0371 0.0066  -0.0381 376 GLY B N   
17389 C CA  . GLY B  350 ? 0.2231 0.2688 0.2031 -0.0441 0.0058  -0.0397 376 GLY B CA  
17390 C C   . GLY B  350 ? 0.2201 0.2615 0.1950 -0.0470 0.0095  -0.0442 376 GLY B C   
17391 O O   . GLY B  350 ? 0.2251 0.2687 0.1964 -0.0526 0.0084  -0.0456 376 GLY B O   
17395 N N   . TYR B  351 ? 0.2181 0.2531 0.1925 -0.0431 0.0141  -0.0463 377 TYR B N   
17396 C CA  . TYR B  351 ? 0.2322 0.2605 0.2014 -0.0454 0.0185  -0.0508 377 TYR B CA  
17397 C C   . TYR B  351 ? 0.2373 0.2587 0.2033 -0.0502 0.0187  -0.0516 377 TYR B C   
17398 O O   . TYR B  351 ? 0.2307 0.2501 0.1913 -0.0566 0.0191  -0.0547 377 TYR B O   
17399 C CB  . TYR B  351 ? 0.2366 0.2603 0.2073 -0.0386 0.0236  -0.0521 377 TYR B CB  
17400 C CG  . TYR B  351 ? 0.2538 0.2694 0.2191 -0.0404 0.0290  -0.0570 377 TYR B CG  
17401 C CD1 . TYR B  351 ? 0.2688 0.2741 0.2308 -0.0424 0.0317  -0.0587 377 TYR B CD1 
17402 C CD2 . TYR B  351 ? 0.2666 0.2842 0.2303 -0.0396 0.0318  -0.0599 377 TYR B CD2 
17403 C CE1 . TYR B  351 ? 0.2830 0.2799 0.2397 -0.0442 0.0371  -0.0636 377 TYR B CE1 
17404 C CE2 . TYR B  351 ? 0.2823 0.2918 0.2409 -0.0407 0.0374  -0.0645 377 TYR B CE2 
17405 C CZ  . TYR B  351 ? 0.2995 0.2983 0.2543 -0.0432 0.0400  -0.0665 377 TYR B CZ  
17406 O OH  . TYR B  351 ? 0.3252 0.3148 0.2748 -0.0442 0.0459  -0.0714 377 TYR B OH  
17416 N N   . VAL B  352 ? 0.2376 0.2560 0.2069 -0.0474 0.0181  -0.0486 378 VAL B N   
17417 C CA  . VAL B  352 ? 0.2514 0.2643 0.2194 -0.0513 0.0178  -0.0482 378 VAL B CA  
17418 C C   . VAL B  352 ? 0.2632 0.2647 0.2276 -0.0515 0.0233  -0.0518 378 VAL B C   
17419 O O   . VAL B  352 ? 0.2693 0.2671 0.2282 -0.0561 0.0257  -0.0562 378 VAL B O   
17420 C CB  . VAL B  352 ? 0.2627 0.2804 0.2283 -0.0592 0.0136  -0.0481 378 VAL B CB  
17421 C CG1 . VAL B  352 ? 0.2720 0.2852 0.2373 -0.0631 0.0131  -0.0473 378 VAL B CG1 
17422 C CG2 . VAL B  352 ? 0.2532 0.2812 0.2228 -0.0583 0.0086  -0.0441 378 VAL B CG2 
17432 N N   . PHE B  353 ? 0.2687 0.2644 0.2358 -0.0463 0.0257  -0.0498 379 PHE B N   
17433 C CA  . PHE B  353 ? 0.2784 0.2621 0.2426 -0.0455 0.0315  -0.0525 379 PHE B CA  
17434 C C   . PHE B  353 ? 0.2882 0.2675 0.2559 -0.0420 0.0320  -0.0488 379 PHE B C   
17435 O O   . PHE B  353 ? 0.2776 0.2631 0.2501 -0.0382 0.0287  -0.0444 379 PHE B O   
17436 C CB  . PHE B  353 ? 0.2710 0.2515 0.2345 -0.0401 0.0364  -0.0549 379 PHE B CB  
17437 C CG  . PHE B  353 ? 0.2701 0.2557 0.2393 -0.0312 0.0361  -0.0512 379 PHE B CG  
17438 C CD1 . PHE B  353 ? 0.2695 0.2665 0.2417 -0.0299 0.0320  -0.0495 379 PHE B CD1 
17439 C CD2 . PHE B  353 ? 0.2788 0.2581 0.2502 -0.0243 0.0400  -0.0495 379 PHE B CD2 
17440 C CE1 . PHE B  353 ? 0.2800 0.2824 0.2573 -0.0224 0.0316  -0.0465 379 PHE B CE1 
17441 C CE2 . PHE B  353 ? 0.2806 0.2657 0.2571 -0.0163 0.0395  -0.0461 379 PHE B CE2 
17442 C CZ  . PHE B  353 ? 0.2749 0.2717 0.2542 -0.0156 0.0352  -0.0447 379 PHE B CZ  
17452 N N   . GLN B  354 ? 0.2973 0.2653 0.2623 -0.0437 0.0363  -0.0507 380 GLN B N   
17453 C CA  . GLN B  354 ? 0.3080 0.2710 0.2755 -0.0418 0.0371  -0.0473 380 GLN B CA  
17454 C C   . GLN B  354 ? 0.3161 0.2742 0.2865 -0.0326 0.0408  -0.0446 380 GLN B C   
17455 O O   . GLN B  354 ? 0.3081 0.2669 0.2820 -0.0295 0.0396  -0.0402 380 GLN B O   
17456 C CB  . GLN B  354 ? 0.3302 0.2832 0.2933 -0.0490 0.0398  -0.0505 380 GLN B CB  
17457 C CG  . GLN B  354 ? 0.3663 0.3243 0.3260 -0.0587 0.0361  -0.0533 380 GLN B CG  
17458 C CD  . GLN B  354 ? 0.4489 0.3982 0.4046 -0.0662 0.0383  -0.0564 380 GLN B CD  
17459 O OE1 . GLN B  354 ? 0.4724 0.4167 0.4302 -0.0663 0.0394  -0.0541 380 GLN B OE1 
17460 N NE2 . GLN B  354 ? 0.4723 0.4196 0.4221 -0.0732 0.0392  -0.0618 380 GLN B NE2 
17469 N N   . GLU B  355 ? 0.3328 0.2859 0.3017 -0.0283 0.0456  -0.0469 381 GLU B N   
17470 C CA  . GLU B  355 ? 0.3571 0.3052 0.3286 -0.0194 0.0496  -0.0441 381 GLU B CA  
17471 C C   . GLU B  355 ? 0.3608 0.3128 0.3336 -0.0132 0.0514  -0.0449 381 GLU B C   
17472 O O   . GLU B  355 ? 0.3502 0.3010 0.3196 -0.0160 0.0534  -0.0494 381 GLU B O   
17473 C CB  . GLU B  355 ? 0.4060 0.3388 0.3741 -0.0204 0.0559  -0.0460 381 GLU B CB  
17474 C CG  . GLU B  355 ? 0.5195 0.4458 0.4902 -0.0112 0.0606  -0.0426 381 GLU B CG  
17475 C CD  . GLU B  355 ? 0.6576 0.5677 0.6248 -0.0121 0.0674  -0.0444 381 GLU B CD  
17476 O OE1 . GLU B  355 ? 0.6865 0.5896 0.6486 -0.0194 0.0697  -0.0498 381 GLU B OE1 
17477 O OE2 . GLU B  355 ? 0.6974 0.6015 0.6667 -0.0055 0.0707  -0.0405 381 GLU B OE2 
17484 N N   . LEU B  356 ? 0.3684 0.3251 0.3458 -0.0048 0.0510  -0.0405 382 LEU B N   
17485 C CA  . LEU B  356 ? 0.3825 0.3436 0.3621 0.0018  0.0530  -0.0406 382 LEU B CA  
17486 C C   . LEU B  356 ? 0.4061 0.3572 0.3862 0.0090  0.0594  -0.0391 382 LEU B C   
17487 O O   . LEU B  356 ? 0.4033 0.3527 0.3858 0.0135  0.0594  -0.0346 382 LEU B O   
17488 C CB  . LEU B  356 ? 0.3711 0.3462 0.3558 0.0060  0.0476  -0.0367 382 LEU B CB  
17489 C CG  . LEU B  356 ? 0.3743 0.3565 0.3619 0.0120  0.0488  -0.0369 382 LEU B CG  
17490 C CD1 . LEU B  356 ? 0.3730 0.3570 0.3578 0.0073  0.0496  -0.0419 382 LEU B CD1 
17491 C CD2 . LEU B  356 ? 0.3697 0.3648 0.3621 0.0156  0.0435  -0.0330 382 LEU B CD2 
17503 N N   . ARG B  357 ? 0.4272 0.3708 0.4046 0.0099  0.0651  -0.0428 383 ARG B N   
17504 C CA  . ARG B  357 ? 0.4585 0.3920 0.4365 0.0172  0.0719  -0.0415 383 ARG B CA  
17505 C C   . ARG B  357 ? 0.4705 0.4120 0.4528 0.0257  0.0732  -0.0398 383 ARG B C   
17506 O O   . ARG B  357 ? 0.4650 0.4170 0.4484 0.0242  0.0702  -0.0416 383 ARG B O   
17507 C CB  . ARG B  357 ? 0.4874 0.4060 0.4595 0.0131  0.0785  -0.0469 383 ARG B CB  
17508 C CG  . ARG B  357 ? 0.5349 0.4456 0.5023 0.0036  0.0777  -0.0495 383 ARG B CG  
17509 C CD  . ARG B  357 ? 0.5747 0.4716 0.5359 -0.0008 0.0843  -0.0557 383 ARG B CD  
17510 N NE  . ARG B  357 ? 0.6021 0.5040 0.5605 -0.0042 0.0840  -0.0607 383 ARG B NE  
17511 C CZ  . ARG B  357 ? 0.6335 0.5256 0.5861 -0.0077 0.0896  -0.0667 383 ARG B CZ  
17512 N NH1 . ARG B  357 ? 0.6338 0.5098 0.5828 -0.0085 0.0960  -0.0687 383 ARG B NH1 
17513 N NH2 . ARG B  357 ? 0.6253 0.5233 0.5754 -0.0106 0.0890  -0.0708 383 ARG B NH2 
17527 N N   . GLU B  358 ? 0.4912 0.4279 0.4760 0.0345  0.0777  -0.0362 384 GLU B N   
17528 C CA  . GLU B  358 ? 0.5115 0.4561 0.5011 0.0432  0.0793  -0.0341 384 GLU B CA  
17529 C C   . GLU B  358 ? 0.5250 0.4687 0.5128 0.0422  0.0832  -0.0393 384 GLU B C   
17530 O O   . GLU B  358 ? 0.5302 0.4861 0.5215 0.0446  0.0811  -0.0392 384 GLU B O   
17531 C CB  . GLU B  358 ? 0.5578 0.4958 0.5500 0.0527  0.0841  -0.0291 384 GLU B CB  
17532 C CG  . GLU B  358 ? 0.6368 0.5838 0.6345 0.0623  0.0857  -0.0261 384 GLU B CG  
17533 C CD  . GLU B  358 ? 0.7361 0.6838 0.7378 0.0719  0.0867  -0.0190 384 GLU B CD  
17534 O OE1 . GLU B  358 ? 0.7590 0.6939 0.7585 0.0730  0.0904  -0.0171 384 GLU B OE1 
17535 O OE2 . GLU B  358 ? 0.7595 0.7211 0.7667 0.0781  0.0838  -0.0153 384 GLU B OE2 
17542 N N   . ASP B  359 ? 0.5293 0.4587 0.5115 0.0380  0.0889  -0.0442 385 ASP B N   
17543 C CA  . ASP B  359 ? 0.5352 0.4626 0.5146 0.0366  0.0932  -0.0496 385 ASP B CA  
17544 C C   . ASP B  359 ? 0.5152 0.4544 0.4935 0.0295  0.0876  -0.0529 385 ASP B C   
17545 O O   . ASP B  359 ? 0.5132 0.4567 0.4915 0.0302  0.0897  -0.0558 385 ASP B O   
17546 C CB  . ASP B  359 ? 0.5881 0.4974 0.5604 0.0317  0.0998  -0.0549 385 ASP B CB  
17547 C CG  . ASP B  359 ? 0.6968 0.5922 0.6694 0.0393  0.1080  -0.0532 385 ASP B CG  
17548 O OD1 . ASP B  359 ? 0.7132 0.6134 0.6919 0.0490  0.1086  -0.0473 385 ASP B OD1 
17549 O OD2 . ASP B  359 ? 0.7478 0.6274 0.7144 0.0354  0.1140  -0.0577 385 ASP B OD2 
17554 N N   . ASP B  360 ? 0.4953 0.4397 0.4727 0.0228  0.0808  -0.0523 386 ASP B N   
17555 C CA  . ASP B  360 ? 0.4832 0.4375 0.4591 0.0157  0.0756  -0.0551 386 ASP B CA  
17556 C C   . ASP B  360 ? 0.4478 0.4183 0.4295 0.0198  0.0718  -0.0527 386 ASP B C   
17557 O O   . ASP B  360 ? 0.4448 0.4217 0.4250 0.0154  0.0702  -0.0558 386 ASP B O   
17558 C CB  . ASP B  360 ? 0.5131 0.4683 0.4869 0.0079  0.0697  -0.0546 386 ASP B CB  
17559 C CG  . ASP B  360 ? 0.5942 0.5348 0.5620 0.0020  0.0730  -0.0577 386 ASP B CG  
17560 O OD1 . ASP B  360 ? 0.6118 0.5435 0.5747 -0.0002 0.0785  -0.0627 386 ASP B OD1 
17561 O OD2 . ASP B  360 ? 0.6396 0.5780 0.6075 -0.0006 0.0702  -0.0554 386 ASP B OD2 
17566 N N   . PHE B  361 ? 0.4195 0.3965 0.4074 0.0277  0.0705  -0.0474 387 PHE B N   
17567 C CA  . PHE B  361 ? 0.4059 0.3984 0.3995 0.0313  0.0669  -0.0452 387 PHE B CA  
17568 C C   . PHE B  361 ? 0.4070 0.4021 0.4051 0.0405  0.0718  -0.0438 387 PHE B C   
17569 O O   . PHE B  361 ? 0.3998 0.4082 0.4037 0.0448  0.0690  -0.0410 387 PHE B O   
17570 C CB  . PHE B  361 ? 0.3932 0.3943 0.3905 0.0323  0.0602  -0.0403 387 PHE B CB  
17571 C CG  . PHE B  361 ? 0.3917 0.3981 0.3872 0.0242  0.0537  -0.0412 387 PHE B CG  
17572 C CD1 . PHE B  361 ? 0.3991 0.4027 0.3896 0.0161  0.0535  -0.0458 387 PHE B CD1 
17573 C CD2 . PHE B  361 ? 0.3907 0.4053 0.3895 0.0250  0.0480  -0.0373 387 PHE B CD2 
17574 C CE1 . PHE B  361 ? 0.4048 0.4139 0.3941 0.0093  0.0476  -0.0459 387 PHE B CE1 
17575 C CE2 . PHE B  361 ? 0.3950 0.4144 0.3924 0.0181  0.0424  -0.0378 387 PHE B CE2 
17576 C CZ  . PHE B  361 ? 0.3925 0.4092 0.3855 0.0105  0.0423  -0.0419 387 PHE B CZ  
17586 N N   . GLN B  362 ? 0.4123 0.3953 0.4077 0.0430  0.0794  -0.0461 388 GLN B N   
17587 C CA  . GLN B  362 ? 0.4207 0.4057 0.4205 0.0520  0.0849  -0.0448 388 GLN B CA  
17588 C C   . GLN B  362 ? 0.4078 0.4065 0.4109 0.0520  0.0836  -0.0464 388 GLN B C   
17589 O O   . GLN B  362 ? 0.4039 0.4126 0.4136 0.0595  0.0838  -0.0429 388 GLN B O   
17590 C CB  . GLN B  362 ? 0.4641 0.4325 0.4596 0.0538  0.0938  -0.0480 388 GLN B CB  
17591 C CG  . GLN B  362 ? 0.5547 0.5091 0.5478 0.0550  0.0962  -0.0460 388 GLN B CG  
17592 C CD  . GLN B  362 ? 0.6474 0.6040 0.6467 0.0656  0.0974  -0.0392 388 GLN B CD  
17593 O OE1 . GLN B  362 ? 0.6897 0.6484 0.6931 0.0739  0.1020  -0.0374 388 GLN B OE1 
17594 N NE2 . GLN B  362 ? 0.6539 0.6102 0.6537 0.0655  0.0933  -0.0350 388 GLN B NE2 
17603 N N   . PRO B  363 ? 0.4019 0.4021 0.4006 0.0438  0.0822  -0.0513 389 PRO B N   
17604 C CA  . PRO B  363 ? 0.3893 0.4028 0.3913 0.0437  0.0811  -0.0525 389 PRO B CA  
17605 C C   . PRO B  363 ? 0.3698 0.4000 0.3787 0.0458  0.0744  -0.0481 389 PRO B C   
17606 O O   . PRO B  363 ? 0.3633 0.4048 0.3770 0.0487  0.0746  -0.0478 389 PRO B O   
17607 C CB  . PRO B  363 ? 0.4047 0.4155 0.3997 0.0335  0.0798  -0.0579 389 PRO B CB  
17608 C CG  . PRO B  363 ? 0.4204 0.4143 0.4082 0.0298  0.0832  -0.0607 389 PRO B CG  
17609 C CD  . PRO B  363 ? 0.4022 0.3929 0.3929 0.0340  0.0813  -0.0558 389 PRO B CD  
17617 N N   . LEU B  364 ? 0.3642 0.3962 0.3738 0.0444  0.0686  -0.0449 390 LEU B N   
17618 C CA  . LEU B  364 ? 0.3579 0.4049 0.3732 0.0458  0.0622  -0.0412 390 LEU B CA  
17619 C C   . LEU B  364 ? 0.3612 0.4137 0.3830 0.0553  0.0623  -0.0357 390 LEU B C   
17620 O O   . LEU B  364 ? 0.3542 0.4201 0.3810 0.0570  0.0575  -0.0329 390 LEU B O   
17621 C CB  . LEU B  364 ? 0.3585 0.4045 0.3709 0.0393  0.0559  -0.0406 390 LEU B CB  
17622 C CG  . LEU B  364 ? 0.3741 0.4152 0.3801 0.0296  0.0545  -0.0449 390 LEU B CG  
17623 C CD1 . LEU B  364 ? 0.3737 0.4115 0.3772 0.0249  0.0496  -0.0435 390 LEU B CD1 
17624 C CD2 . LEU B  364 ? 0.3786 0.4307 0.3858 0.0256  0.0521  -0.0469 390 LEU B CD2 
17636 N N   . MET B  365 ? 0.3685 0.4102 0.3896 0.0612  0.0676  -0.0341 391 MET B N   
17637 C CA  . MET B  365 ? 0.3758 0.4210 0.4019 0.0700  0.0675  -0.0282 391 MET B CA  
17638 C C   . MET B  365 ? 0.3789 0.4372 0.4125 0.0779  0.0687  -0.0254 391 MET B C   
17639 O O   . MET B  365 ? 0.3774 0.4428 0.4156 0.0842  0.0665  -0.0202 391 MET B O   
17640 C CB  . MET B  365 ? 0.3937 0.4225 0.4166 0.0737  0.0731  -0.0271 391 MET B CB  
17641 C CG  . MET B  365 ? 0.4361 0.4550 0.4534 0.0674  0.0705  -0.0277 391 MET B CG  
17642 S SD  . MET B  365 ? 0.5375 0.5354 0.5500 0.0693  0.0777  -0.0278 391 MET B SD  
17643 C CE  . MET B  365 ? 0.5211 0.5132 0.5281 0.0597  0.0725  -0.0291 391 MET B CE  
17653 N N   . GLN B  366 ? 0.3844 0.4467 0.4195 0.0777  0.0719  -0.0285 392 GLN B N   
17654 C CA  . GLN B  366 ? 0.3985 0.4746 0.4415 0.0850  0.0731  -0.0259 392 GLN B CA  
17655 C C   . GLN B  366 ? 0.3813 0.4743 0.4279 0.0803  0.0672  -0.0269 392 GLN B C   
17656 O O   . GLN B  366 ? 0.3834 0.4893 0.4367 0.0850  0.0678  -0.0252 392 GLN B O   
17657 C CB  . GLN B  366 ? 0.4477 0.5171 0.4908 0.0891  0.0817  -0.0282 392 GLN B CB  
17658 C CG  . GLN B  366 ? 0.5445 0.6211 0.5954 0.1005  0.0857  -0.0235 392 GLN B CG  
17659 C CD  . GLN B  366 ? 0.6621 0.7301 0.7125 0.1046  0.0949  -0.0261 392 GLN B CD  
17660 O OE1 . GLN B  366 ? 0.7097 0.7627 0.7529 0.0998  0.0992  -0.0311 392 GLN B OE1 
17661 N NE2 . GLN B  366 ? 0.6756 0.7532 0.7338 0.1138  0.0983  -0.0227 392 GLN B NE2 
17670 N N   . LEU B  367 ? 0.3578 0.4510 0.4003 0.0712  0.0616  -0.0293 393 LEU B N   
17671 C CA  . LEU B  367 ? 0.3373 0.4450 0.3827 0.0665  0.0563  -0.0302 393 LEU B CA  
17672 C C   . LEU B  367 ? 0.3259 0.4458 0.3768 0.0704  0.0510  -0.0254 393 LEU B C   
17673 O O   . LEU B  367 ? 0.3242 0.4396 0.3727 0.0702  0.0478  -0.0232 393 LEU B O   
17674 C CB  . LEU B  367 ? 0.3374 0.4400 0.3764 0.0561  0.0528  -0.0340 393 LEU B CB  
17675 C CG  . LEU B  367 ? 0.3580 0.4489 0.3907 0.0514  0.0577  -0.0390 393 LEU B CG  
17676 C CD1 . LEU B  367 ? 0.3644 0.4520 0.3913 0.0417  0.0535  -0.0418 393 LEU B CD1 
17677 C CD2 . LEU B  367 ? 0.3666 0.4637 0.4021 0.0530  0.0621  -0.0413 393 LEU B CD2 
17689 N N   . PRO B  368 ? 0.3140 0.4493 0.3724 0.0748  0.0504  -0.0234 394 PRO B N   
17690 C CA  . PRO B  368 ? 0.3057 0.4528 0.3692 0.0795  0.0459  -0.0185 394 PRO B CA  
17691 C C   . PRO B  368 ? 0.2976 0.4511 0.3600 0.0733  0.0382  -0.0185 394 PRO B C   
17692 O O   . PRO B  368 ? 0.3095 0.4669 0.3731 0.0765  0.0348  -0.0148 394 PRO B O   
17693 C CB  . PRO B  368 ? 0.3068 0.4692 0.3787 0.0849  0.0475  -0.0169 394 PRO B CB  
17694 C CG  . PRO B  368 ? 0.3143 0.4761 0.3853 0.0801  0.0506  -0.0217 394 PRO B CG  
17695 C CD  . PRO B  368 ? 0.3033 0.4462 0.3659 0.0761  0.0543  -0.0252 394 PRO B CD  
17703 N N   . ASN B  369 ? 0.2807 0.4354 0.3407 0.0648  0.0358  -0.0224 395 ASN B N   
17704 C CA  . ASN B  369 ? 0.2753 0.4357 0.3344 0.0590  0.0289  -0.0225 395 ASN B CA  
17705 C C   . ASN B  369 ? 0.2572 0.4049 0.3089 0.0524  0.0272  -0.0246 395 ASN B C   
17706 O O   . ASN B  369 ? 0.2483 0.3998 0.2990 0.0470  0.0221  -0.0251 395 ASN B O   
17707 C CB  . ASN B  369 ? 0.2972 0.4712 0.3604 0.0547  0.0266  -0.0245 395 ASN B CB  
17708 C CG  . ASN B  369 ? 0.3542 0.5426 0.4254 0.0609  0.0276  -0.0221 395 ASN B CG  
17709 O OD1 . ASN B  369 ? 0.3677 0.5602 0.4418 0.0678  0.0269  -0.0180 395 ASN B OD1 
17710 N ND2 . ASN B  369 ? 0.3761 0.5750 0.4516 0.0590  0.0282  -0.0237 395 ASN B ND2 
17717 N N   . LEU B  370 ? 0.2501 0.3831 0.2969 0.0526  0.0313  -0.0257 396 LEU B N   
17718 C CA  . LEU B  370 ? 0.2548 0.3765 0.2950 0.0463  0.0297  -0.0274 396 LEU B CA  
17719 C C   . LEU B  370 ? 0.2624 0.3832 0.3019 0.0480  0.0259  -0.0240 396 LEU B C   
17720 O O   . LEU B  370 ? 0.2777 0.3922 0.3167 0.0535  0.0282  -0.0213 396 LEU B O   
17721 C CB  . LEU B  370 ? 0.2574 0.3643 0.2927 0.0460  0.0353  -0.0295 396 LEU B CB  
17722 C CG  . LEU B  370 ? 0.2778 0.3730 0.3064 0.0392  0.0340  -0.0314 396 LEU B CG  
17723 C CD1 . LEU B  370 ? 0.2747 0.3745 0.3017 0.0311  0.0297  -0.0338 396 LEU B CD1 
17724 C CD2 . LEU B  370 ? 0.2937 0.3756 0.3176 0.0384  0.0397  -0.0342 396 LEU B CD2 
17736 N N   . SER B  371 ? 0.2527 0.3803 0.2925 0.0438  0.0203  -0.0239 397 SER B N   
17737 C CA  . SER B  371 ? 0.2624 0.3906 0.3015 0.0451  0.0165  -0.0210 397 SER B CA  
17738 C C   . SER B  371 ? 0.2531 0.3716 0.2867 0.0393  0.0145  -0.0220 397 SER B C   
17739 O O   . SER B  371 ? 0.2479 0.3634 0.2801 0.0411  0.0128  -0.0194 397 SER B O   
17740 C CB  . SER B  371 ? 0.2922 0.4352 0.3356 0.0453  0.0119  -0.0199 397 SER B CB  
17741 O OG  . SER B  371 ? 0.3496 0.4961 0.3923 0.0379  0.0089  -0.0228 397 SER B OG  
17747 N N   . THR B  372 ? 0.2423 0.3565 0.2731 0.0325  0.0146  -0.0253 398 THR B N   
17748 C CA  . THR B  372 ? 0.2469 0.3530 0.2730 0.0269  0.0126  -0.0260 398 THR B CA  
17749 C C   . THR B  372 ? 0.2410 0.3358 0.2630 0.0239  0.0162  -0.0282 398 THR B C   
17750 O O   . THR B  372 ? 0.2337 0.3290 0.2553 0.0217  0.0185  -0.0310 398 THR B O   
17751 C CB  . THR B  372 ? 0.2687 0.3811 0.2950 0.0208  0.0083  -0.0274 398 THR B CB  
17752 O OG1 . THR B  372 ? 0.2859 0.4075 0.3152 0.0230  0.0048  -0.0255 398 THR B OG1 
17753 C CG2 . THR B  372 ? 0.2691 0.3736 0.2910 0.0151  0.0064  -0.0279 398 THR B CG2 
17761 N N   . ILE B  373 ? 0.2397 0.3245 0.2582 0.0233  0.0167  -0.0273 399 ILE B N   
17762 C CA  . ILE B  373 ? 0.2582 0.3320 0.2722 0.0194  0.0195  -0.0295 399 ILE B CA  
17763 C C   . ILE B  373 ? 0.2412 0.3116 0.2525 0.0142  0.0160  -0.0290 399 ILE B C   
17764 O O   . ILE B  373 ? 0.2277 0.2970 0.2394 0.0164  0.0143  -0.0261 399 ILE B O   
17765 C CB  . ILE B  373 ? 0.2892 0.3532 0.3019 0.0240  0.0247  -0.0290 399 ILE B CB  
17766 C CG1 . ILE B  373 ? 0.3165 0.3690 0.3239 0.0186  0.0272  -0.0318 399 ILE B CG1 
17767 C CG2 . ILE B  373 ? 0.3038 0.3658 0.3176 0.0292  0.0242  -0.0249 399 ILE B CG2 
17768 C CD1 . ILE B  373 ? 0.3430 0.3962 0.3483 0.0135  0.0284  -0.0359 399 ILE B CD1 
17780 N N   . ASN B  374 ? 0.2328 0.3024 0.2416 0.0075  0.0148  -0.0314 400 ASN B N   
17781 C CA  . ASN B  374 ? 0.2356 0.3029 0.2423 0.0025  0.0115  -0.0306 400 ASN B CA  
17782 C C   . ASN B  374 ? 0.2301 0.2883 0.2324 -0.0021 0.0134  -0.0325 400 ASN B C   
17783 O O   . ASN B  374 ? 0.2201 0.2777 0.2201 -0.0062 0.0146  -0.0353 400 ASN B O   
17784 C CB  . ASN B  374 ? 0.2459 0.3216 0.2539 -0.0012 0.0076  -0.0310 400 ASN B CB  
17785 C CG  . ASN B  374 ? 0.2723 0.3464 0.2783 -0.0068 0.0045  -0.0305 400 ASN B CG  
17786 O OD1 . ASN B  374 ? 0.3024 0.3704 0.3067 -0.0077 0.0043  -0.0293 400 ASN B OD1 
17787 N ND2 . ASN B  374 ? 0.2526 0.3324 0.2590 -0.0106 0.0021  -0.0312 400 ASN B ND2 
17794 N N   . LEU B  375 ? 0.2268 0.2778 0.2278 -0.0015 0.0140  -0.0308 401 LEU B N   
17795 C CA  . LEU B  375 ? 0.2317 0.2741 0.2287 -0.0063 0.0155  -0.0324 401 LEU B CA  
17796 C C   . LEU B  375 ? 0.2182 0.2602 0.2149 -0.0100 0.0120  -0.0303 401 LEU B C   
17797 O O   . LEU B  375 ? 0.2175 0.2525 0.2123 -0.0121 0.0131  -0.0301 401 LEU B O   
17798 C CB  . LEU B  375 ? 0.2405 0.2737 0.2364 -0.0027 0.0204  -0.0326 401 LEU B CB  
17799 C CG  . LEU B  375 ? 0.2634 0.2953 0.2593 0.0010  0.0249  -0.0348 401 LEU B CG  
17800 C CD1 . LEU B  375 ? 0.2756 0.2995 0.2718 0.0068  0.0293  -0.0333 401 LEU B CD1 
17801 C CD2 . LEU B  375 ? 0.2744 0.3026 0.2660 -0.0047 0.0270  -0.0392 401 LEU B CD2 
17813 N N   . GLY B  376 ? 0.2146 0.2640 0.2132 -0.0113 0.0079  -0.0290 402 GLY B N   
17814 C CA  . GLY B  376 ? 0.2192 0.2687 0.2178 -0.0146 0.0047  -0.0269 402 GLY B CA  
17815 C C   . GLY B  376 ? 0.2193 0.2659 0.2148 -0.0214 0.0044  -0.0285 402 GLY B C   
17816 O O   . GLY B  376 ? 0.2093 0.2565 0.2025 -0.0244 0.0053  -0.0313 402 GLY B O   
17820 N N   . ILE B  377 ? 0.2180 0.2619 0.2131 -0.0241 0.0030  -0.0267 403 ILE B N   
17821 C CA  . ILE B  377 ? 0.2203 0.2633 0.2130 -0.0309 0.0018  -0.0275 403 ILE B CA  
17822 C C   . ILE B  377 ? 0.2238 0.2613 0.2123 -0.0342 0.0050  -0.0313 403 ILE B C   
17823 O O   . ILE B  377 ? 0.2155 0.2553 0.2014 -0.0387 0.0043  -0.0334 403 ILE B O   
17824 C CB  . ILE B  377 ? 0.2260 0.2765 0.2194 -0.0341 -0.0020 -0.0267 403 ILE B CB  
17825 C CG1 . ILE B  377 ? 0.2377 0.2932 0.2349 -0.0303 -0.0044 -0.0238 403 ILE B CG1 
17826 C CG2 . ILE B  377 ? 0.2253 0.2761 0.2173 -0.0404 -0.0041 -0.0259 403 ILE B CG2 
17827 C CD1 . ILE B  377 ? 0.2543 0.3163 0.2523 -0.0328 -0.0073 -0.0233 403 ILE B CD1 
17839 N N   . ASN B  378 ? 0.2225 0.2525 0.2101 -0.0319 0.0086  -0.0322 404 ASN B N   
17840 C CA  . ASN B  378 ? 0.2230 0.2462 0.2064 -0.0349 0.0123  -0.0360 404 ASN B CA  
17841 C C   . ASN B  378 ? 0.2236 0.2393 0.2052 -0.0382 0.0136  -0.0361 404 ASN B C   
17842 O O   . ASN B  378 ? 0.2358 0.2446 0.2135 -0.0412 0.0170  -0.0395 404 ASN B O   
17843 C CB  . ASN B  378 ? 0.2308 0.2503 0.2141 -0.0291 0.0167  -0.0377 404 ASN B CB  
17844 C CG  . ASN B  378 ? 0.2345 0.2600 0.2179 -0.0283 0.0166  -0.0395 404 ASN B CG  
17845 O OD1 . ASN B  378 ? 0.2531 0.2788 0.2329 -0.0331 0.0170  -0.0425 404 ASN B OD1 
17846 N ND2 . ASN B  378 ? 0.2019 0.2325 0.1890 -0.0224 0.0163  -0.0379 404 ASN B ND2 
17853 N N   . PHE B  379 ? 0.2164 0.2334 0.2009 -0.0380 0.0113  -0.0324 405 PHE B N   
17854 C CA  . PHE B  379 ? 0.2266 0.2373 0.2104 -0.0409 0.0125  -0.0319 405 PHE B CA  
17855 C C   . PHE B  379 ? 0.2346 0.2350 0.2167 -0.0376 0.0180  -0.0334 405 PHE B C   
17856 O O   . PHE B  379 ? 0.2466 0.2396 0.2260 -0.0417 0.0204  -0.0354 405 PHE B O   
17857 C CB  . PHE B  379 ? 0.2304 0.2421 0.2112 -0.0496 0.0107  -0.0338 405 PHE B CB  
17858 C CG  . PHE B  379 ? 0.2472 0.2686 0.2305 -0.0519 0.0054  -0.0309 405 PHE B CG  
17859 C CD1 . PHE B  379 ? 0.2634 0.2874 0.2504 -0.0518 0.0031  -0.0269 405 PHE B CD1 
17860 C CD2 . PHE B  379 ? 0.2597 0.2877 0.2420 -0.0535 0.0031  -0.0318 405 PHE B CD2 
17861 C CE1 . PHE B  379 ? 0.2698 0.3022 0.2595 -0.0530 -0.0012 -0.0240 405 PHE B CE1 
17862 C CE2 . PHE B  379 ? 0.2666 0.3028 0.2514 -0.0549 -0.0013 -0.0287 405 PHE B CE2 
17863 C CZ  . PHE B  379 ? 0.2660 0.3042 0.2545 -0.0545 -0.0033 -0.0248 405 PHE B CZ  
17873 N N   . ILE B  380 ? 0.2339 0.2340 0.2179 -0.0301 0.0199  -0.0324 406 ILE B N   
17874 C CA  . ILE B  380 ? 0.2472 0.2381 0.2302 -0.0258 0.0253  -0.0332 406 ILE B CA  
17875 C C   . ILE B  380 ? 0.2577 0.2438 0.2423 -0.0245 0.0260  -0.0298 406 ILE B C   
17876 O O   . ILE B  380 ? 0.2555 0.2470 0.2434 -0.0215 0.0231  -0.0259 406 ILE B O   
17877 C CB  . ILE B  380 ? 0.2453 0.2391 0.2305 -0.0177 0.0266  -0.0322 406 ILE B CB  
17878 C CG1 . ILE B  380 ? 0.2581 0.2566 0.2420 -0.0188 0.0265  -0.0356 406 ILE B CG1 
17879 C CG2 . ILE B  380 ? 0.2480 0.2323 0.2328 -0.0124 0.0322  -0.0319 406 ILE B CG2 
17880 C CD1 . ILE B  380 ? 0.2709 0.2771 0.2583 -0.0122 0.0256  -0.0340 406 ILE B CD1 
17892 N N   . LYS B  381 ? 0.2731 0.2489 0.2552 -0.0267 0.0300  -0.0313 407 LYS B N   
17893 C CA  . LYS B  381 ? 0.3001 0.2703 0.2834 -0.0259 0.0314  -0.0282 407 LYS B CA  
17894 C C   . LYS B  381 ? 0.3277 0.2917 0.3121 -0.0178 0.0357  -0.0259 407 LYS B C   
17895 O O   . LYS B  381 ? 0.3354 0.2983 0.3219 -0.0147 0.0358  -0.0218 407 LYS B O   
17896 C CB  . LYS B  381 ? 0.3245 0.2869 0.3047 -0.0337 0.0334  -0.0310 407 LYS B CB  
17897 C CG  . LYS B  381 ? 0.3787 0.3484 0.3585 -0.0417 0.0286  -0.0321 407 LYS B CG  
17898 C CD  . LYS B  381 ? 0.4371 0.4005 0.4143 -0.0498 0.0300  -0.0344 407 LYS B CD  
17899 C CE  . LYS B  381 ? 0.4874 0.4475 0.4593 -0.0560 0.0314  -0.0401 407 LYS B CE  
17900 N NZ  . LYS B  381 ? 0.5116 0.4701 0.4815 -0.0654 0.0305  -0.0419 407 LYS B NZ  
17914 N N   . GLN B  382 ? 0.3413 0.3009 0.3240 -0.0142 0.0396  -0.0283 408 GLN B N   
17915 C CA  . GLN B  382 ? 0.3587 0.3121 0.3423 -0.0061 0.0440  -0.0259 408 GLN B CA  
17916 C C   . GLN B  382 ? 0.3584 0.3149 0.3425 -0.0006 0.0456  -0.0272 408 GLN B C   
17917 O O   . GLN B  382 ? 0.3515 0.3084 0.3333 -0.0040 0.0461  -0.0316 408 GLN B O   
17918 C CB  . GLN B  382 ? 0.3992 0.3380 0.3798 -0.0081 0.0500  -0.0274 408 GLN B CB  
17919 C CG  . GLN B  382 ? 0.4706 0.4052 0.4517 -0.0112 0.0498  -0.0247 408 GLN B CG  
17920 C CD  . GLN B  382 ? 0.5564 0.4929 0.5408 -0.0037 0.0496  -0.0186 408 GLN B CD  
17921 O OE1 . GLN B  382 ? 0.5866 0.5156 0.5709 0.0027  0.0543  -0.0165 408 GLN B OE1 
17922 N NE2 . GLN B  382 ? 0.5499 0.4964 0.5371 -0.0039 0.0444  -0.0155 408 GLN B NE2 
17931 N N   . ILE B  383 ? 0.3607 0.3190 0.3476 0.0081  0.0467  -0.0233 409 ILE B N   
17932 C CA  . ILE B  383 ? 0.3714 0.3339 0.3600 0.0144  0.0482  -0.0236 409 ILE B CA  
17933 C C   . ILE B  383 ? 0.3894 0.3444 0.3788 0.0225  0.0534  -0.0204 409 ILE B C   
17934 O O   . ILE B  383 ? 0.3888 0.3423 0.3795 0.0256  0.0532  -0.0160 409 ILE B O   
17935 C CB  . ILE B  383 ? 0.3725 0.3495 0.3646 0.0171  0.0425  -0.0213 409 ILE B CB  
17936 C CG1 . ILE B  383 ? 0.3865 0.3703 0.3778 0.0093  0.0377  -0.0242 409 ILE B CG1 
17937 C CG2 . ILE B  383 ? 0.3757 0.3583 0.3704 0.0243  0.0439  -0.0209 409 ILE B CG2 
17938 C CD1 . ILE B  383 ? 0.3922 0.3891 0.3864 0.0106  0.0324  -0.0230 409 ILE B CD1 
17950 N N   . ASP B  384 ? 0.4042 0.3551 0.3931 0.0262  0.0581  -0.0224 410 ASP B N   
17951 C CA  . ASP B  384 ? 0.4206 0.3657 0.4110 0.0351  0.0632  -0.0189 410 ASP B CA  
17952 C C   . ASP B  384 ? 0.4060 0.3653 0.4010 0.0418  0.0595  -0.0155 410 ASP B C   
17953 O O   . ASP B  384 ? 0.4028 0.3679 0.3994 0.0441  0.0599  -0.0173 410 ASP B O   
17954 C CB  . ASP B  384 ? 0.4779 0.4132 0.4662 0.0364  0.0700  -0.0226 410 ASP B CB  
17955 C CG  . ASP B  384 ? 0.6218 0.5405 0.6056 0.0318  0.0754  -0.0253 410 ASP B CG  
17956 O OD1 . ASP B  384 ? 0.6549 0.5695 0.6375 0.0278  0.0740  -0.0238 410 ASP B OD1 
17957 O OD2 . ASP B  384 ? 0.6739 0.5834 0.6551 0.0322  0.0813  -0.0289 410 ASP B OD2 
17962 N N   . PHE B  385 ? 0.4021 0.3677 0.3992 0.0444  0.0556  -0.0108 411 PHE B N   
17963 C CA  . PHE B  385 ? 0.4043 0.3841 0.4053 0.0496  0.0514  -0.0079 411 PHE B CA  
17964 C C   . PHE B  385 ? 0.4198 0.4023 0.4238 0.0588  0.0547  -0.0055 411 PHE B C   
17965 O O   . PHE B  385 ? 0.4194 0.4146 0.4267 0.0617  0.0514  -0.0048 411 PHE B O   
17966 C CB  . PHE B  385 ? 0.3974 0.3818 0.3992 0.0509  0.0474  -0.0033 411 PHE B CB  
17967 C CG  . PHE B  385 ? 0.4010 0.3882 0.4015 0.0428  0.0427  -0.0051 411 PHE B CG  
17968 C CD1 . PHE B  385 ? 0.3995 0.3987 0.4015 0.0403  0.0372  -0.0065 411 PHE B CD1 
17969 C CD2 . PHE B  385 ? 0.4123 0.3901 0.4102 0.0377  0.0439  -0.0055 411 PHE B CD2 
17970 C CE1 . PHE B  385 ? 0.4035 0.4049 0.4045 0.0334  0.0332  -0.0079 411 PHE B CE1 
17971 C CE2 . PHE B  385 ? 0.4164 0.3975 0.4136 0.0305  0.0396  -0.0070 411 PHE B CE2 
17972 C CZ  . PHE B  385 ? 0.4059 0.3986 0.4046 0.0287  0.0344  -0.0080 411 PHE B CZ  
17982 N N   . LYS B  386 ? 0.4306 0.4014 0.4337 0.0632  0.0612  -0.0043 412 LYS B N   
17983 C CA  . LYS B  386 ? 0.4389 0.4119 0.4452 0.0724  0.0649  -0.0017 412 LYS B CA  
17984 C C   . LYS B  386 ? 0.4293 0.4095 0.4374 0.0721  0.0650  -0.0057 412 LYS B C   
17985 O O   . LYS B  386 ? 0.4308 0.4184 0.4430 0.0795  0.0660  -0.0032 412 LYS B O   
17986 C CB  . LYS B  386 ? 0.4868 0.4437 0.4913 0.0764  0.0727  -0.0004 412 LYS B CB  
17987 C CG  . LYS B  386 ? 0.5699 0.5139 0.5705 0.0706  0.0778  -0.0065 412 LYS B CG  
17988 C CD  . LYS B  386 ? 0.6618 0.5885 0.6602 0.0741  0.0855  -0.0049 412 LYS B CD  
17989 C CE  . LYS B  386 ? 0.7305 0.6434 0.7242 0.0675  0.0906  -0.0114 412 LYS B CE  
17990 N NZ  . LYS B  386 ? 0.7794 0.6747 0.7710 0.0709  0.0987  -0.0101 412 LYS B NZ  
18004 N N   . LEU B  387 ? 0.4162 0.3949 0.4216 0.0637  0.0640  -0.0115 413 LEU B N   
18005 C CA  . LEU B  387 ? 0.4108 0.3958 0.4175 0.0629  0.0645  -0.0154 413 LEU B CA  
18006 C C   . LEU B  387 ? 0.3995 0.4023 0.4108 0.0651  0.0588  -0.0138 413 LEU B C   
18007 O O   . LEU B  387 ? 0.3966 0.4060 0.4110 0.0684  0.0603  -0.0148 413 LEU B O   
18008 C CB  . LEU B  387 ? 0.4137 0.3930 0.4156 0.0530  0.0644  -0.0217 413 LEU B CB  
18009 C CG  . LEU B  387 ? 0.4246 0.4117 0.4256 0.0451  0.0574  -0.0231 413 LEU B CG  
18010 C CD1 . LEU B  387 ? 0.4241 0.4245 0.4275 0.0439  0.0539  -0.0251 413 LEU B CD1 
18011 C CD2 . LEU B  387 ? 0.4382 0.4156 0.4338 0.0361  0.0581  -0.0275 413 LEU B CD2 
18023 N N   . PHE B  388 ? 0.3938 0.4043 0.4059 0.0632  0.0527  -0.0114 414 PHE B N   
18024 C CA  . PHE B  388 ? 0.3906 0.4175 0.4066 0.0641  0.0472  -0.0104 414 PHE B CA  
18025 C C   . PHE B  388 ? 0.4067 0.4426 0.4278 0.0736  0.0479  -0.0061 414 PHE B C   
18026 O O   . PHE B  388 ? 0.4020 0.4505 0.4268 0.0745  0.0455  -0.0067 414 PHE B O   
18027 C CB  . PHE B  388 ? 0.3796 0.4112 0.3946 0.0598  0.0410  -0.0092 414 PHE B CB  
18028 C CG  . PHE B  388 ? 0.3780 0.4042 0.3891 0.0504  0.0394  -0.0133 414 PHE B CG  
18029 C CD1 . PHE B  388 ? 0.3840 0.4146 0.3947 0.0450  0.0379  -0.0176 414 PHE B CD1 
18030 C CD2 . PHE B  388 ? 0.3852 0.4026 0.3931 0.0471  0.0392  -0.0125 414 PHE B CD2 
18031 C CE1 . PHE B  388 ? 0.3934 0.4197 0.4005 0.0366  0.0363  -0.0209 414 PHE B CE1 
18032 C CE2 . PHE B  388 ? 0.3915 0.4054 0.3964 0.0386  0.0374  -0.0159 414 PHE B CE2 
18033 C CZ  . PHE B  388 ? 0.3917 0.4101 0.3961 0.0335  0.0359  -0.0199 414 PHE B CZ  
18043 N N   . GLN B  389 ? 0.4199 0.4496 0.4413 0.0806  0.0514  -0.0016 415 GLN B N   
18044 C CA  . GLN B  389 ? 0.4414 0.4799 0.4677 0.0901  0.0523  0.0031  415 GLN B CA  
18045 C C   . GLN B  389 ? 0.4600 0.4987 0.4891 0.0939  0.0574  0.0013  415 GLN B C   
18046 O O   . GLN B  389 ? 0.4544 0.5048 0.4888 0.1003  0.0570  0.0041  415 GLN B O   
18047 C CB  . GLN B  389 ? 0.4730 0.5050 0.4987 0.0967  0.0546  0.0090  415 GLN B CB  
18048 C CG  . GLN B  389 ? 0.5419 0.5578 0.5659 0.1004  0.0626  0.0095  415 GLN B CG  
18049 C CD  . GLN B  389 ? 0.6338 0.6407 0.6558 0.1043  0.0645  0.0147  415 GLN B CD  
18050 O OE1 . GLN B  389 ? 0.6718 0.6627 0.6901 0.1022  0.0693  0.0136  415 GLN B OE1 
18051 N NE2 . GLN B  389 ? 0.6380 0.6546 0.6621 0.1098  0.0611  0.0205  415 GLN B NE2 
18060 N N   . ASN B  390 ? 0.4802 0.5066 0.5059 0.0898  0.0623  -0.0035 416 ASN B N   
18061 C CA  . ASN B  390 ? 0.5023 0.5285 0.5302 0.0931  0.0675  -0.0057 416 ASN B CA  
18062 C C   . ASN B  390 ? 0.4885 0.5276 0.5187 0.0887  0.0641  -0.0095 416 ASN B C   
18063 O O   . ASN B  390 ? 0.4871 0.5278 0.5195 0.0911  0.0681  -0.0115 416 ASN B O   
18064 C CB  . ASN B  390 ? 0.5649 0.5725 0.5880 0.0910  0.0747  -0.0093 416 ASN B CB  
18065 C CG  . ASN B  390 ? 0.6801 0.6840 0.7056 0.0982  0.0820  -0.0091 416 ASN B CG  
18066 O OD1 . ASN B  390 ? 0.6990 0.7120 0.7303 0.1071  0.0825  -0.0042 416 ASN B OD1 
18067 N ND2 . ASN B  390 ? 0.7452 0.7382 0.7671 0.0951  0.0876  -0.0143 416 ASN B ND2 
18074 N N   . PHE B  391 ? 0.4716 0.5196 0.5014 0.0825  0.0570  -0.0105 417 PHE B N   
18075 C CA  . PHE B  391 ? 0.4573 0.5183 0.4897 0.0787  0.0536  -0.0134 417 PHE B CA  
18076 C C   . PHE B  391 ? 0.4524 0.5292 0.4918 0.0859  0.0516  -0.0093 417 PHE B C   
18077 O O   . PHE B  391 ? 0.4538 0.5332 0.4948 0.0915  0.0503  -0.0043 417 PHE B O   
18078 C CB  . PHE B  391 ? 0.4417 0.5063 0.4714 0.0700  0.0470  -0.0155 417 PHE B CB  
18079 C CG  . PHE B  391 ? 0.4418 0.4964 0.4659 0.0614  0.0479  -0.0206 417 PHE B CG  
18080 C CD1 . PHE B  391 ? 0.4527 0.4926 0.4718 0.0590  0.0504  -0.0213 417 PHE B CD1 
18081 C CD2 . PHE B  391 ? 0.4384 0.4989 0.4622 0.0554  0.0462  -0.0246 417 PHE B CD2 
18082 C CE1 . PHE B  391 ? 0.4629 0.4949 0.4768 0.0508  0.0508  -0.0259 417 PHE B CE1 
18083 C CE2 . PHE B  391 ? 0.4522 0.5045 0.4706 0.0475  0.0466  -0.0289 417 PHE B CE2 
18084 C CZ  . PHE B  391 ? 0.4578 0.4963 0.4713 0.0452  0.0488  -0.0296 417 PHE B CZ  
18094 N N   . SER B  392 ? 0.4437 0.5317 0.4870 0.0854  0.0512  -0.0113 418 SER B N   
18095 C CA  . SER B  392 ? 0.4422 0.5466 0.4926 0.0917  0.0492  -0.0076 418 SER B CA  
18096 C C   . SER B  392 ? 0.4328 0.5484 0.4846 0.0908  0.0418  -0.0047 418 SER B C   
18097 O O   . SER B  392 ? 0.4326 0.5544 0.4876 0.0979  0.0410  0.0004  418 SER B O   
18098 C CB  . SER B  392 ? 0.4682 0.5827 0.5224 0.0898  0.0499  -0.0109 418 SER B CB  
18099 O OG  . SER B  392 ? 0.5052 0.6363 0.5669 0.0959  0.0482  -0.0072 418 SER B OG  
18105 N N   . ASN B  393 ? 0.4179 0.5358 0.4669 0.0823  0.0367  -0.0077 419 ASN B N   
18106 C CA  . ASN B  393 ? 0.4028 0.5305 0.4525 0.0808  0.0300  -0.0057 419 ASN B CA  
18107 C C   . ASN B  393 ? 0.3692 0.4920 0.4139 0.0715  0.0260  -0.0090 419 ASN B C   
18108 O O   . ASN B  393 ? 0.3603 0.4922 0.4061 0.0664  0.0218  -0.0111 419 ASN B O   
18109 C CB  . ASN B  393 ? 0.4310 0.5773 0.4872 0.0823  0.0269  -0.0051 419 ASN B CB  
18110 C CG  . ASN B  393 ? 0.5022 0.6593 0.5591 0.0812  0.0204  -0.0031 419 ASN B CG  
18111 O OD1 . ASN B  393 ? 0.5291 0.6817 0.5829 0.0826  0.0186  -0.0004 419 ASN B OD1 
18112 N ND2 . ASN B  393 ? 0.5131 0.6847 0.5740 0.0785  0.0167  -0.0045 419 ASN B ND2 
18119 N N   . LEU B  394 ? 0.3509 0.4596 0.3902 0.0695  0.0274  -0.0092 420 LEU B N   
18120 C CA  . LEU B  394 ? 0.3368 0.4412 0.3718 0.0615  0.0238  -0.0116 420 LEU B CA  
18121 C C   . LEU B  394 ? 0.3078 0.4203 0.3433 0.0617  0.0183  -0.0090 420 LEU B C   
18122 O O   . LEU B  394 ? 0.3012 0.4150 0.3375 0.0678  0.0183  -0.0049 420 LEU B O   
18123 C CB  . LEU B  394 ? 0.3547 0.4430 0.3844 0.0592  0.0267  -0.0122 420 LEU B CB  
18124 C CG  . LEU B  394 ? 0.3880 0.4669 0.4149 0.0548  0.0306  -0.0165 420 LEU B CG  
18125 C CD1 . LEU B  394 ? 0.4079 0.4716 0.4299 0.0533  0.0335  -0.0165 420 LEU B CD1 
18126 C CD2 . LEU B  394 ? 0.3902 0.4735 0.4159 0.0466  0.0273  -0.0204 420 LEU B CD2 
18138 N N   . GLU B  395 ? 0.2832 0.4012 0.3181 0.0554  0.0137  -0.0113 421 GLU B N   
18139 C CA  . GLU B  395 ? 0.2750 0.3996 0.3096 0.0544  0.0086  -0.0097 421 GLU B CA  
18140 C C   . GLU B  395 ? 0.2542 0.3706 0.2841 0.0481  0.0066  -0.0112 421 GLU B C   
18141 O O   . GLU B  395 ? 0.2482 0.3656 0.2766 0.0482  0.0037  -0.0094 421 GLU B O   
18142 C CB  . GLU B  395 ? 0.3255 0.4647 0.3639 0.0526  0.0049  -0.0111 421 GLU B CB  
18143 C CG  . GLU B  395 ? 0.4367 0.5866 0.4806 0.0588  0.0063  -0.0093 421 GLU B CG  
18144 C CD  . GLU B  395 ? 0.5880 0.7524 0.6361 0.0560  0.0030  -0.0111 421 GLU B CD  
18145 O OE1 . GLU B  395 ? 0.6333 0.8022 0.6801 0.0517  -0.0015 -0.0121 421 GLU B OE1 
18146 O OE2 . GLU B  395 ? 0.6258 0.7968 0.6783 0.0581  0.0052  -0.0116 421 GLU B OE2 
18153 N N   . ILE B  396 ? 0.2390 0.3479 0.2667 0.0425  0.0081  -0.0144 422 ILE B N   
18154 C CA  . ILE B  396 ? 0.2365 0.3384 0.2604 0.0364  0.0063  -0.0156 422 ILE B CA  
18155 C C   . ILE B  396 ? 0.2312 0.3208 0.2521 0.0345  0.0102  -0.0169 422 ILE B C   
18156 O O   . ILE B  396 ? 0.2295 0.3178 0.2503 0.0320  0.0123  -0.0197 422 ILE B O   
18157 C CB  . ILE B  396 ? 0.2381 0.3460 0.2624 0.0300  0.0030  -0.0185 422 ILE B CB  
18158 C CG1 . ILE B  396 ? 0.2485 0.3674 0.2750 0.0310  -0.0011 -0.0176 422 ILE B CG1 
18159 C CG2 . ILE B  396 ? 0.2441 0.3440 0.2647 0.0238  0.0018  -0.0196 422 ILE B CG2 
18160 C CD1 . ILE B  396 ? 0.2679 0.3937 0.2957 0.0252  -0.0038 -0.0204 422 ILE B CD1 
18172 N N   . ILE B  397 ? 0.2293 0.3101 0.2476 0.0355  0.0113  -0.0149 423 ILE B N   
18173 C CA  . ILE B  397 ? 0.2343 0.3031 0.2495 0.0330  0.0148  -0.0162 423 ILE B CA  
18174 C C   . ILE B  397 ? 0.2265 0.2923 0.2391 0.0269  0.0118  -0.0166 423 ILE B C   
18175 O O   . ILE B  397 ? 0.2193 0.2834 0.2312 0.0281  0.0104  -0.0140 423 ILE B O   
18176 C CB  . ILE B  397 ? 0.2532 0.3140 0.2677 0.0387  0.0187  -0.0133 423 ILE B CB  
18177 C CG1 . ILE B  397 ? 0.2706 0.3358 0.2883 0.0460  0.0215  -0.0119 423 ILE B CG1 
18178 C CG2 . ILE B  397 ? 0.2682 0.3162 0.2792 0.0350  0.0223  -0.0152 423 ILE B CG2 
18179 C CD1 . ILE B  397 ? 0.2955 0.3555 0.3133 0.0530  0.0244  -0.0077 423 ILE B CD1 
18191 N N   . TYR B  398 ? 0.2126 0.2790 0.2242 0.0206  0.0105  -0.0197 424 TYR B N   
18192 C CA  . TYR B  398 ? 0.2166 0.2815 0.2265 0.0150  0.0075  -0.0198 424 TYR B CA  
18193 C C   . TYR B  398 ? 0.2149 0.2700 0.2216 0.0108  0.0096  -0.0210 424 TYR B C   
18194 O O   . TYR B  398 ? 0.2128 0.2656 0.2180 0.0074  0.0113  -0.0239 424 TYR B O   
18195 C CB  . TYR B  398 ? 0.2225 0.2953 0.2335 0.0110  0.0043  -0.0216 424 TYR B CB  
18196 C CG  . TYR B  398 ? 0.2455 0.3178 0.2552 0.0060  0.0010  -0.0212 424 TYR B CG  
18197 C CD1 . TYR B  398 ? 0.2615 0.3378 0.2723 0.0072  -0.0019 -0.0193 424 TYR B CD1 
18198 C CD2 . TYR B  398 ? 0.2645 0.3332 0.2722 0.0002  0.0009  -0.0228 424 TYR B CD2 
18199 C CE1 . TYR B  398 ? 0.2780 0.3538 0.2879 0.0031  -0.0045 -0.0188 424 TYR B CE1 
18200 C CE2 . TYR B  398 ? 0.2816 0.3507 0.2887 -0.0039 -0.0020 -0.0220 424 TYR B CE2 
18201 C CZ  . TYR B  398 ? 0.3014 0.3740 0.3099 -0.0024 -0.0045 -0.0200 424 TYR B CZ  
18202 O OH  . TYR B  398 ? 0.3481 0.4205 0.3563 -0.0059 -0.0069 -0.0190 424 TYR B OH  
18212 N N   . LEU B  399 ? 0.2131 0.2625 0.2187 0.0110  0.0098  -0.0187 425 LEU B N   
18213 C CA  . LEU B  399 ? 0.2235 0.2638 0.2263 0.0069  0.0117  -0.0196 425 LEU B CA  
18214 C C   . LEU B  399 ? 0.2248 0.2651 0.2273 0.0027  0.0086  -0.0181 425 LEU B C   
18215 O O   . LEU B  399 ? 0.2384 0.2721 0.2394 0.0003  0.0098  -0.0176 425 LEU B O   
18216 C CB  . LEU B  399 ? 0.2297 0.2620 0.2319 0.0114  0.0158  -0.0179 425 LEU B CB  
18217 C CG  . LEU B  399 ? 0.2774 0.3092 0.2805 0.0169  0.0194  -0.0185 425 LEU B CG  
18218 C CD1 . LEU B  399 ? 0.2902 0.3146 0.2931 0.0222  0.0231  -0.0157 425 LEU B CD1 
18219 C CD2 . LEU B  399 ? 0.3041 0.3330 0.3054 0.0133  0.0219  -0.0226 425 LEU B CD2 
18231 N N   . SER B  400 ? 0.2046 0.2525 0.2086 0.0017  0.0048  -0.0175 426 SER B N   
18232 C CA  . SER B  400 ? 0.2025 0.2510 0.2067 -0.0015 0.0020  -0.0159 426 SER B CA  
18233 C C   . SER B  400 ? 0.2065 0.2517 0.2090 -0.0080 0.0018  -0.0173 426 SER B C   
18234 O O   . SER B  400 ? 0.1970 0.2427 0.1982 -0.0110 0.0023  -0.0201 426 SER B O   
18235 C CB  . SER B  400 ? 0.2040 0.2603 0.2097 -0.0015 -0.0015 -0.0155 426 SER B CB  
18236 O OG  . SER B  400 ? 0.2259 0.2826 0.2320 -0.0042 -0.0038 -0.0138 426 SER B OG  
18242 N N   . GLU B  401 ? 0.2109 0.2536 0.2134 -0.0103 0.0010  -0.0154 427 GLU B N   
18243 C CA  . GLU B  401 ? 0.2080 0.2494 0.2095 -0.0167 0.0001  -0.0162 427 GLU B CA  
18244 C C   . GLU B  401 ? 0.2184 0.2536 0.2171 -0.0196 0.0030  -0.0188 427 GLU B C   
18245 O O   . GLU B  401 ? 0.2308 0.2669 0.2276 -0.0236 0.0029  -0.0215 427 GLU B O   
18246 C CB  . GLU B  401 ? 0.2152 0.2632 0.2171 -0.0200 -0.0031 -0.0169 427 GLU B CB  
18247 C CG  . GLU B  401 ? 0.2333 0.2819 0.2349 -0.0258 -0.0050 -0.0161 427 GLU B CG  
18248 C CD  . GLU B  401 ? 0.2861 0.3348 0.2900 -0.0252 -0.0062 -0.0127 427 GLU B CD  
18249 O OE1 . GLU B  401 ? 0.3014 0.3458 0.3050 -0.0266 -0.0048 -0.0119 427 GLU B OE1 
18250 O OE2 . GLU B  401 ? 0.2932 0.3461 0.2990 -0.0233 -0.0082 -0.0108 427 GLU B OE2 
18257 N N   . ASN B  402 ? 0.2093 0.2377 0.2074 -0.0178 0.0060  -0.0181 428 ASN B N   
18258 C CA  . ASN B  402 ? 0.2233 0.2441 0.2186 -0.0207 0.0094  -0.0207 428 ASN B CA  
18259 C C   . ASN B  402 ? 0.2503 0.2659 0.2459 -0.0225 0.0102  -0.0186 428 ASN B C   
18260 O O   . ASN B  402 ? 0.2588 0.2784 0.2566 -0.0232 0.0075  -0.0158 428 ASN B O   
18261 C CB  . ASN B  402 ? 0.2160 0.2330 0.2104 -0.0154 0.0132  -0.0222 428 ASN B CB  
18262 C CG  . ASN B  402 ? 0.2245 0.2456 0.2180 -0.0163 0.0130  -0.0253 428 ASN B CG  
18263 O OD1 . ASN B  402 ? 0.2172 0.2368 0.2078 -0.0217 0.0133  -0.0283 428 ASN B OD1 
18264 N ND2 . ASN B  402 ? 0.2152 0.2421 0.2109 -0.0113 0.0123  -0.0246 428 ASN B ND2 
18271 N N   A ARG B  403 ? 0.2585 0.2654 0.2519 -0.0237 0.0141  -0.0201 429 ARG B N   
18272 N N   B ARG B  403 ? 0.2627 0.2696 0.2561 -0.0237 0.0141  -0.0201 429 ARG B N   
18273 C CA  A ARG B  403 ? 0.2732 0.2746 0.2669 -0.0257 0.0154  -0.0183 429 ARG B CA  
18274 C CA  B ARG B  403 ? 0.2816 0.2828 0.2752 -0.0258 0.0155  -0.0184 429 ARG B CA  
18275 C C   A ARG B  403 ? 0.2889 0.2820 0.2821 -0.0203 0.0200  -0.0172 429 ARG B C   
18276 C C   B ARG B  403 ? 0.2924 0.2854 0.2857 -0.0202 0.0201  -0.0172 429 ARG B C   
18277 O O   A ARG B  403 ? 0.2975 0.2823 0.2892 -0.0227 0.0232  -0.0178 429 ARG B O   
18278 O O   B ARG B  403 ? 0.3004 0.2850 0.2922 -0.0225 0.0233  -0.0177 429 ARG B O   
18279 C CB  A ARG B  403 ? 0.2863 0.2846 0.2774 -0.0340 0.0156  -0.0212 429 ARG B CB  
18280 C CB  B ARG B  403 ? 0.3070 0.3046 0.2979 -0.0339 0.0160  -0.0215 429 ARG B CB  
18281 C CG  A ARG B  403 ? 0.3046 0.3114 0.2959 -0.0393 0.0112  -0.0220 429 ARG B CG  
18282 C CG  B ARG B  403 ? 0.3532 0.3579 0.3457 -0.0397 0.0117  -0.0202 429 ARG B CG  
18283 C CD  A ARG B  403 ? 0.3418 0.3560 0.3368 -0.0399 0.0072  -0.0181 429 ARG B CD  
18284 C CD  B ARG B  403 ? 0.4010 0.4080 0.3905 -0.0463 0.0102  -0.0238 429 ARG B CD  
18285 N NE  A ARG B  403 ? 0.3701 0.3830 0.3659 -0.0452 0.0068  -0.0169 429 ARG B NE  
18286 N NE  B ARG B  403 ? 0.4349 0.4341 0.4207 -0.0518 0.0132  -0.0272 429 ARG B NE  
18287 C CZ  A ARG B  403 ? 0.3843 0.3938 0.3821 -0.0437 0.0084  -0.0142 429 ARG B CZ  
18288 C CZ  B ARG B  403 ? 0.4587 0.4593 0.4430 -0.0597 0.0116  -0.0286 429 ARG B CZ  
18289 N NH1 A ARG B  403 ? 0.3826 0.3922 0.3816 -0.0493 0.0079  -0.0133 429 ARG B NH1 
18290 N NH1 B ARG B  403 ? 0.4528 0.4453 0.4332 -0.0645 0.0148  -0.0322 429 ARG B NH1 
18291 N NH2 A ARG B  403 ? 0.3684 0.3750 0.3674 -0.0368 0.0104  -0.0121 429 ARG B NH2 
18292 N NH2 B ARG B  403 ? 0.4569 0.4669 0.4435 -0.0629 0.0069  -0.0264 429 ARG B NH2 
18319 N N   . ILE B  404 ? 0.2934 0.2888 0.2879 -0.0130 0.0204  -0.0155 430 ILE B N   
18320 C CA  . ILE B  404 ? 0.3134 0.3022 0.3077 -0.0069 0.0245  -0.0139 430 ILE B CA  
18321 C C   . ILE B  404 ? 0.3194 0.3059 0.3151 -0.0058 0.0248  -0.0099 430 ILE B C   
18322 O O   . ILE B  404 ? 0.3065 0.2998 0.3042 -0.0052 0.0214  -0.0073 430 ILE B O   
18323 C CB  . ILE B  404 ? 0.3265 0.3208 0.3221 0.0003  0.0241  -0.0131 430 ILE B CB  
18324 C CG1 . ILE B  404 ? 0.3452 0.3415 0.3396 -0.0013 0.0244  -0.0173 430 ILE B CG1 
18325 C CG2 . ILE B  404 ? 0.3341 0.3222 0.3297 0.0072  0.0283  -0.0105 430 ILE B CG2 
18326 C CD1 . ILE B  404 ? 0.3645 0.3700 0.3610 0.0038  0.0223  -0.0168 430 ILE B CD1 
18338 N N   . SER B  405 ? 0.3343 0.3109 0.3286 -0.0060 0.0291  -0.0094 431 SER B N   
18339 C CA  . SER B  405 ? 0.3603 0.3339 0.3558 -0.0055 0.0300  -0.0056 431 SER B CA  
18340 C C   . SER B  405 ? 0.3867 0.3538 0.3818 0.0021  0.0343  -0.0026 431 SER B C   
18341 O O   . SER B  405 ? 0.3901 0.3561 0.3844 0.0067  0.0361  -0.0036 431 SER B O   
18342 C CB  . SER B  405 ? 0.3790 0.3467 0.3735 -0.0135 0.0312  -0.0074 431 SER B CB  
18343 O OG  . SER B  405 ? 0.4211 0.3779 0.4127 -0.0142 0.0362  -0.0099 431 SER B OG  
18349 N N   . PRO B  406 ? 0.4038 0.3674 0.3995 0.0040  0.0358  0.0015  432 PRO B N   
18350 C CA  . PRO B  406 ? 0.4265 0.3842 0.4216 0.0115  0.0399  0.0049  432 PRO B CA  
18351 C C   . PRO B  406 ? 0.4614 0.4083 0.4543 0.0123  0.0452  0.0025  432 PRO B C   
18352 O O   . PRO B  406 ? 0.4638 0.4035 0.4552 0.0059  0.0473  -0.0009 432 PRO B O   
18353 C CB  . PRO B  406 ? 0.4302 0.3847 0.4259 0.0110  0.0410  0.0089  432 PRO B CB  
18354 C CG  . PRO B  406 ? 0.4238 0.3873 0.4215 0.0061  0.0361  0.0087  432 PRO B CG  
18355 C CD  . PRO B  406 ? 0.3927 0.3577 0.3899 -0.0004 0.0343  0.0035  432 PRO B CD  
18363 N N   . LEU B  407 ? 0.4818 0.4282 0.4747 0.0201  0.0472  0.0042  433 LEU B N   
18364 C CA  . LEU B  407 ? 0.5130 0.4496 0.5042 0.0223  0.0527  0.0023  433 LEU B CA  
18365 C C   . LEU B  407 ? 0.5356 0.4584 0.5252 0.0214  0.0583  0.0040  433 LEU B C   
18366 O O   . LEU B  407 ? 0.5465 0.4685 0.5368 0.0233  0.0585  0.0086  433 LEU B O   
18367 C CB  . LEU B  407 ? 0.5212 0.4620 0.5136 0.0319  0.0533  0.0049  433 LEU B CB  
18368 C CG  . LEU B  407 ? 0.5570 0.4909 0.5484 0.0350  0.0582  0.0025  433 LEU B CG  
18369 C CD1 . LEU B  407 ? 0.5638 0.5074 0.5575 0.0426  0.0566  0.0041  433 LEU B CD1 
18370 C CD2 . LEU B  407 ? 0.5735 0.4931 0.5634 0.0380  0.0650  0.0049  433 LEU B CD2 
18382 N N   . PHE B  433 ? 0.4762 0.5502 0.4905 -0.0533 -0.0204 0.0185  459 PHE B N   
18383 C CA  . PHE B  433 ? 0.4759 0.5556 0.4880 -0.0554 -0.0219 0.0159  459 PHE B CA  
18384 C C   . PHE B  433 ? 0.4630 0.5438 0.4755 -0.0531 -0.0226 0.0122  459 PHE B C   
18385 O O   . PHE B  433 ? 0.4756 0.5533 0.4895 -0.0506 -0.0217 0.0098  459 PHE B O   
18386 C CB  . PHE B  433 ? 0.4804 0.5615 0.4903 -0.0588 -0.0209 0.0128  459 PHE B CB  
18387 C CG  . PHE B  433 ? 0.4937 0.5714 0.5046 -0.0589 -0.0192 0.0096  459 PHE B CG  
18388 C CD1 . PHE B  433 ? 0.5083 0.5870 0.5196 -0.0579 -0.0191 0.0043  459 PHE B CD1 
18389 C CD2 . PHE B  433 ? 0.5082 0.5821 0.5195 -0.0605 -0.0176 0.0117  459 PHE B CD2 
18390 C CE1 . PHE B  433 ? 0.5221 0.5987 0.5343 -0.0586 -0.0177 0.0012  459 PHE B CE1 
18391 C CE2 . PHE B  433 ? 0.5224 0.5933 0.5343 -0.0615 -0.0159 0.0083  459 PHE B CE2 
18392 C CZ  . PHE B  433 ? 0.5196 0.5924 0.5320 -0.0607 -0.0162 0.0029  459 PHE B CZ  
18401 N N   . GLU B  434 ? 0.4348 0.5196 0.4458 -0.0540 -0.0239 0.0115  460 GLU B N   
18402 C CA  . GLU B  434 ? 0.4079 0.4935 0.4191 -0.0520 -0.0244 0.0086  460 GLU B CA  
18403 C C   . GLU B  434 ? 0.3752 0.4617 0.3852 -0.0521 -0.0236 0.0030  460 GLU B C   
18404 O O   . GLU B  434 ? 0.3648 0.4505 0.3757 -0.0493 -0.0234 0.0006  460 GLU B O   
18405 C CB  . GLU B  434 ? 0.4199 0.5091 0.4298 -0.0535 -0.0260 0.0103  460 GLU B CB  
18406 C CG  . GLU B  434 ? 0.4500 0.5395 0.4597 -0.0520 -0.0262 0.0074  460 GLU B CG  
18407 C CD  . GLU B  434 ? 0.5049 0.5975 0.5127 -0.0545 -0.0275 0.0083  460 GLU B CD  
18408 O OE1 . GLU B  434 ? 0.5238 0.6161 0.5310 -0.0538 -0.0274 0.0057  460 GLU B OE1 
18409 O OE2 . GLU B  434 ? 0.5118 0.6072 0.5186 -0.0572 -0.0287 0.0116  460 GLU B OE2 
18416 N N   . PHE B  435 ? 0.3445 0.4334 0.3526 -0.0550 -0.0231 0.0014  461 PHE B N   
18417 C CA  . PHE B  435 ? 0.3205 0.4114 0.3278 -0.0551 -0.0222 -0.0035 461 PHE B CA  
18418 C C   . PHE B  435 ? 0.3071 0.3976 0.3156 -0.0556 -0.0211 -0.0054 461 PHE B C   
18419 O O   . PHE B  435 ? 0.3078 0.3979 0.3161 -0.0581 -0.0206 -0.0036 461 PHE B O   
18420 C CB  . PHE B  435 ? 0.3091 0.4035 0.3134 -0.0581 -0.0221 -0.0044 461 PHE B CB  
18421 C CG  . PHE B  435 ? 0.3092 0.4040 0.3120 -0.0583 -0.0232 -0.0032 461 PHE B CG  
18422 C CD1 . PHE B  435 ? 0.3185 0.4128 0.3212 -0.0562 -0.0229 -0.0059 461 PHE B CD1 
18423 C CD2 . PHE B  435 ? 0.3163 0.4121 0.3178 -0.0605 -0.0244 0.0008  461 PHE B CD2 
18424 C CE1 . PHE B  435 ? 0.3234 0.4178 0.3247 -0.0569 -0.0238 -0.0050 461 PHE B CE1 
18425 C CE2 . PHE B  435 ? 0.3226 0.4194 0.3227 -0.0612 -0.0256 0.0017  461 PHE B CE2 
18426 C CZ  . PHE B  435 ? 0.3205 0.4164 0.3205 -0.0596 -0.0252 -0.0014 461 PHE B CZ  
18436 N N   . ASP B  436 ? 0.2937 0.3847 0.3035 -0.0534 -0.0207 -0.0089 462 ASP B N   
18437 C CA  . ASP B  436 ? 0.2881 0.3796 0.2991 -0.0541 -0.0199 -0.0113 462 ASP B CA  
18438 C C   . ASP B  436 ? 0.2852 0.3810 0.2954 -0.0573 -0.0190 -0.0130 462 ASP B C   
18439 O O   . ASP B  436 ? 0.2838 0.3831 0.2934 -0.0567 -0.0187 -0.0153 462 ASP B O   
18440 C CB  . ASP B  436 ? 0.3035 0.3959 0.3159 -0.0509 -0.0200 -0.0145 462 ASP B CB  
18441 C CG  . ASP B  436 ? 0.3419 0.4361 0.3556 -0.0518 -0.0195 -0.0175 462 ASP B CG  
18442 O OD1 . ASP B  436 ? 0.3252 0.4194 0.3390 -0.0552 -0.0187 -0.0172 462 ASP B OD1 
18443 O OD2 . ASP B  436 ? 0.3832 0.4790 0.3978 -0.0493 -0.0198 -0.0199 462 ASP B OD2 
18448 N N   . PRO B  437 ? 0.2880 0.3834 0.2980 -0.0606 -0.0182 -0.0117 463 PRO B N   
18449 C CA  . PRO B  437 ? 0.2940 0.3938 0.3032 -0.0637 -0.0171 -0.0132 463 PRO B CA  
18450 C C   . PRO B  437 ? 0.2916 0.3962 0.3028 -0.0634 -0.0163 -0.0175 463 PRO B C   
18451 O O   . PRO B  437 ? 0.2930 0.4019 0.3036 -0.0653 -0.0152 -0.0189 463 PRO B O   
18452 C CB  . PRO B  437 ? 0.3118 0.4093 0.3206 -0.0671 -0.0163 -0.0103 463 PRO B CB  
18453 C CG  . PRO B  437 ? 0.3211 0.4131 0.3313 -0.0656 -0.0166 -0.0086 463 PRO B CG  
18454 C CD  . PRO B  437 ? 0.2899 0.3805 0.3005 -0.0615 -0.0179 -0.0088 463 PRO B CD  
18462 N N   . HIS B  438 ? 0.2828 0.3870 0.2960 -0.0610 -0.0169 -0.0196 464 HIS B N   
18463 C CA  . HIS B  438 ? 0.2855 0.3953 0.3010 -0.0604 -0.0165 -0.0234 464 HIS B CA  
18464 C C   . HIS B  438 ? 0.2917 0.4039 0.3074 -0.0562 -0.0170 -0.0251 464 HIS B C   
18465 O O   . HIS B  438 ? 0.2978 0.4149 0.3157 -0.0547 -0.0170 -0.0278 464 HIS B O   
18466 C CB  . HIS B  438 ? 0.2957 0.4043 0.3130 -0.0609 -0.0169 -0.0247 464 HIS B CB  
18467 C CG  . HIS B  438 ? 0.3215 0.4269 0.3386 -0.0651 -0.0159 -0.0232 464 HIS B CG  
18468 N ND1 . HIS B  438 ? 0.3416 0.4511 0.3597 -0.0689 -0.0147 -0.0243 464 HIS B ND1 
18469 C CD2 . HIS B  438 ? 0.3403 0.4387 0.3563 -0.0657 -0.0158 -0.0204 464 HIS B CD2 
18470 C CE1 . HIS B  438 ? 0.3518 0.4562 0.3692 -0.0720 -0.0138 -0.0223 464 HIS B CE1 
18471 N NE2 . HIS B  438 ? 0.3533 0.4508 0.3696 -0.0700 -0.0144 -0.0198 464 HIS B NE2 
18479 N N   . SER B  439 ? 0.2956 0.4047 0.3093 -0.0543 -0.0174 -0.0234 465 SER B N   
18480 C CA  . SER B  439 ? 0.3080 0.4180 0.3216 -0.0504 -0.0174 -0.0246 465 SER B CA  
18481 C C   . SER B  439 ? 0.2987 0.4099 0.3103 -0.0513 -0.0162 -0.0249 465 SER B C   
18482 O O   . SER B  439 ? 0.3005 0.4116 0.3102 -0.0548 -0.0157 -0.0237 465 SER B O   
18483 C CB  . SER B  439 ? 0.3512 0.4560 0.3640 -0.0478 -0.0186 -0.0226 465 SER B CB  
18484 O OG  . SER B  439 ? 0.4179 0.5213 0.4321 -0.0464 -0.0194 -0.0228 465 SER B OG  
18490 N N   . ASN B  440 ? 0.2861 0.3981 0.2976 -0.0481 -0.0155 -0.0265 466 ASN B N   
18491 C CA  . ASN B  440 ? 0.2750 0.3870 0.2841 -0.0485 -0.0141 -0.0273 466 ASN B CA  
18492 C C   . ASN B  440 ? 0.2760 0.3827 0.2822 -0.0496 -0.0150 -0.0248 466 ASN B C   
18493 O O   . ASN B  440 ? 0.2813 0.3848 0.2881 -0.0474 -0.0162 -0.0235 466 ASN B O   
18494 C CB  . ASN B  440 ? 0.2764 0.3897 0.2866 -0.0442 -0.0128 -0.0294 466 ASN B CB  
18495 C CG  . ASN B  440 ? 0.2795 0.3932 0.2876 -0.0446 -0.0104 -0.0312 466 ASN B CG  
18496 O OD1 . ASN B  440 ? 0.2699 0.3795 0.2746 -0.0461 -0.0101 -0.0307 466 ASN B OD1 
18497 N ND2 . ASN B  440 ? 0.2797 0.3986 0.2898 -0.0435 -0.0086 -0.0333 466 ASN B ND2 
18504 N N   . PHE B  441 ? 0.2567 0.3633 0.2599 -0.0533 -0.0146 -0.0241 467 PHE B N   
18505 C CA  . PHE B  441 ? 0.2546 0.3578 0.2551 -0.0550 -0.0158 -0.0216 467 PHE B CA  
18506 C C   . PHE B  441 ? 0.2601 0.3608 0.2588 -0.0535 -0.0152 -0.0228 467 PHE B C   
18507 O O   . PHE B  441 ? 0.2723 0.3701 0.2702 -0.0538 -0.0165 -0.0207 467 PHE B O   
18508 C CB  . PHE B  441 ? 0.2477 0.3526 0.2452 -0.0597 -0.0156 -0.0205 467 PHE B CB  
18509 C CG  . PHE B  441 ? 0.2577 0.3606 0.2524 -0.0621 -0.0172 -0.0174 467 PHE B CG  
18510 C CD1 . PHE B  441 ? 0.2659 0.3673 0.2622 -0.0622 -0.0191 -0.0135 467 PHE B CD1 
18511 C CD2 . PHE B  441 ? 0.2707 0.3739 0.2612 -0.0646 -0.0166 -0.0183 467 PHE B CD2 
18512 C CE1 . PHE B  441 ? 0.2823 0.3833 0.2765 -0.0643 -0.0206 -0.0102 467 PHE B CE1 
18513 C CE2 . PHE B  441 ? 0.2840 0.3868 0.2720 -0.0673 -0.0184 -0.0153 467 PHE B CE2 
18514 C CZ  . PHE B  441 ? 0.2790 0.3811 0.2692 -0.0670 -0.0205 -0.0111 467 PHE B CZ  
18524 N N   . TYR B  442 ? 0.2516 0.3532 0.2497 -0.0521 -0.0129 -0.0261 468 TYR B N   
18525 C CA  . TYR B  442 ? 0.2578 0.3559 0.2536 -0.0512 -0.0118 -0.0275 468 TYR B CA  
18526 C C   . TYR B  442 ? 0.2678 0.3634 0.2659 -0.0463 -0.0114 -0.0280 468 TYR B C   
18527 O O   . TYR B  442 ? 0.2780 0.3695 0.2744 -0.0459 -0.0109 -0.0282 468 TYR B O   
18528 C CB  . TYR B  442 ? 0.2501 0.3493 0.2431 -0.0525 -0.0089 -0.0307 468 TYR B CB  
18529 C CG  . TYR B  442 ? 0.2425 0.3432 0.2317 -0.0577 -0.0093 -0.0300 468 TYR B CG  
18530 C CD1 . TYR B  442 ? 0.2494 0.3478 0.2348 -0.0610 -0.0105 -0.0287 468 TYR B CD1 
18531 C CD2 . TYR B  442 ? 0.2454 0.3505 0.2350 -0.0595 -0.0088 -0.0299 468 TYR B CD2 
18532 C CE1 . TYR B  442 ? 0.2596 0.3601 0.2415 -0.0657 -0.0113 -0.0273 468 TYR B CE1 
18533 C CE2 . TYR B  442 ? 0.2539 0.3605 0.2400 -0.0642 -0.0092 -0.0286 468 TYR B CE2 
18534 C CZ  . TYR B  442 ? 0.2719 0.3763 0.2539 -0.0672 -0.0105 -0.0274 468 TYR B CZ  
18535 O OH  . TYR B  442 ? 0.2858 0.3924 0.2640 -0.0717 -0.0112 -0.0256 468 TYR B OH  
18545 N N   . HIS B  443 ? 0.2653 0.3630 0.2671 -0.0429 -0.0119 -0.0279 469 HIS B N   
18546 C CA  . HIS B  443 ? 0.2734 0.3690 0.2771 -0.0383 -0.0118 -0.0277 469 HIS B CA  
18547 C C   . HIS B  443 ? 0.2755 0.3736 0.2824 -0.0362 -0.0135 -0.0266 469 HIS B C   
18548 O O   . HIS B  443 ? 0.2619 0.3639 0.2701 -0.0379 -0.0140 -0.0269 469 HIS B O   
18549 C CB  . HIS B  443 ? 0.2866 0.3824 0.2905 -0.0349 -0.0090 -0.0302 469 HIS B CB  
18550 C CG  . HIS B  443 ? 0.3093 0.4111 0.3154 -0.0342 -0.0079 -0.0320 469 HIS B CG  
18551 N ND1 . HIS B  443 ? 0.3352 0.4387 0.3396 -0.0364 -0.0058 -0.0340 469 HIS B ND1 
18552 C CD2 . HIS B  443 ? 0.3150 0.4217 0.3246 -0.0317 -0.0087 -0.0320 469 HIS B CD2 
18553 C CE1 . HIS B  443 ? 0.3296 0.4392 0.3371 -0.0351 -0.0052 -0.0350 469 HIS B CE1 
18554 N NE2 . HIS B  443 ? 0.3249 0.4369 0.3357 -0.0324 -0.0071 -0.0339 469 HIS B NE2 
18562 N N   . PHE B  444 ? 0.2885 0.3843 0.2965 -0.0328 -0.0142 -0.0255 470 PHE B N   
18563 C CA  . PHE B  444 ? 0.3113 0.4092 0.3217 -0.0307 -0.0156 -0.0248 470 PHE B CA  
18564 C C   . PHE B  444 ? 0.3008 0.4040 0.3133 -0.0281 -0.0148 -0.0269 470 PHE B C   
18565 O O   . PHE B  444 ? 0.2951 0.3989 0.3076 -0.0259 -0.0129 -0.0282 470 PHE B O   
18566 C CB  . PHE B  444 ? 0.3382 0.4322 0.3487 -0.0280 -0.0164 -0.0229 470 PHE B CB  
18567 C CG  . PHE B  444 ? 0.3838 0.4754 0.3941 -0.0240 -0.0151 -0.0230 470 PHE B CG  
18568 C CD1 . PHE B  444 ? 0.4088 0.5035 0.4206 -0.0199 -0.0144 -0.0240 470 PHE B CD1 
18569 C CD2 . PHE B  444 ? 0.4118 0.4983 0.4207 -0.0241 -0.0147 -0.0215 470 PHE B CD2 
18570 C CE1 . PHE B  444 ? 0.4292 0.5212 0.4407 -0.0158 -0.0131 -0.0235 470 PHE B CE1 
18571 C CE2 . PHE B  444 ? 0.4314 0.5151 0.4402 -0.0204 -0.0133 -0.0213 470 PHE B CE2 
18572 C CZ  . PHE B  444 ? 0.4313 0.5175 0.4413 -0.0160 -0.0125 -0.0221 470 PHE B CZ  
18582 N N   . THR B  445 ? 0.3049 0.4121 0.3194 -0.0285 -0.0161 -0.0273 471 THR B N   
18583 C CA  . THR B  445 ? 0.3132 0.4271 0.3302 -0.0266 -0.0157 -0.0291 471 THR B CA  
18584 C C   . THR B  445 ? 0.3143 0.4299 0.3326 -0.0223 -0.0167 -0.0289 471 THR B C   
18585 O O   . THR B  445 ? 0.3137 0.4358 0.3343 -0.0203 -0.0167 -0.0301 471 THR B O   
18586 C CB  . THR B  445 ? 0.3457 0.4638 0.3639 -0.0306 -0.0163 -0.0302 471 THR B CB  
18587 O OG1 . THR B  445 ? 0.3687 0.4842 0.3865 -0.0326 -0.0180 -0.0290 471 THR B OG1 
18588 C CG2 . THR B  445 ? 0.3526 0.4702 0.3694 -0.0344 -0.0149 -0.0305 471 THR B CG2 
18596 N N   . ARG B  446 ? 0.3140 0.4247 0.3309 -0.0208 -0.0176 -0.0272 472 ARG B N   
18597 C CA  . ARG B  446 ? 0.3240 0.4361 0.3414 -0.0167 -0.0184 -0.0267 472 ARG B CA  
18598 C C   . ARG B  446 ? 0.3173 0.4309 0.3354 -0.0120 -0.0169 -0.0266 472 ARG B C   
18599 O O   . ARG B  446 ? 0.3147 0.4250 0.3321 -0.0118 -0.0150 -0.0266 472 ARG B O   
18600 C CB  . ARG B  446 ? 0.3591 0.4652 0.3747 -0.0161 -0.0192 -0.0248 472 ARG B CB  
18601 C CG  . ARG B  446 ? 0.4285 0.5286 0.4427 -0.0152 -0.0179 -0.0230 472 ARG B CG  
18602 C CD  . ARG B  446 ? 0.4923 0.5881 0.5054 -0.0135 -0.0185 -0.0210 472 ARG B CD  
18603 N NE  . ARG B  446 ? 0.5494 0.6397 0.5615 -0.0133 -0.0174 -0.0192 472 ARG B NE  
18604 C CZ  . ARG B  446 ? 0.5958 0.6841 0.6075 -0.0103 -0.0159 -0.0188 472 ARG B CZ  
18605 N NH1 . ARG B  446 ? 0.5951 0.6868 0.6075 -0.0066 -0.0152 -0.0196 472 ARG B NH1 
18606 N NH2 . ARG B  446 ? 0.6098 0.6929 0.6205 -0.0110 -0.0149 -0.0174 472 ARG B NH2 
18620 N N   . PRO B  447 ? 0.3079 0.4261 0.3272 -0.0080 -0.0175 -0.0265 473 PRO B N   
18621 C CA  . PRO B  447 ? 0.2960 0.4152 0.3161 -0.0029 -0.0158 -0.0258 473 PRO B CA  
18622 C C   . PRO B  447 ? 0.2809 0.3915 0.2987 -0.0012 -0.0142 -0.0240 473 PRO B C   
18623 O O   . PRO B  447 ? 0.2738 0.3795 0.2898 -0.0025 -0.0151 -0.0228 473 PRO B O   
18624 C CB  . PRO B  447 ? 0.3052 0.4307 0.3264 0.0008  -0.0174 -0.0253 473 PRO B CB  
18625 C CG  . PRO B  447 ? 0.3141 0.4435 0.3356 -0.0032 -0.0198 -0.0269 473 PRO B CG  
18626 C CD  . PRO B  447 ? 0.3016 0.4242 0.3213 -0.0079 -0.0198 -0.0270 473 PRO B CD  
18634 N N   . LEU B  448 ? 0.2720 0.3806 0.2899 0.0013  -0.0116 -0.0239 474 LEU B N   
18635 C CA  . LEU B  448 ? 0.2722 0.3724 0.2880 0.0025  -0.0098 -0.0224 474 LEU B CA  
18636 C C   . LEU B  448 ? 0.2707 0.3693 0.2859 0.0065  -0.0104 -0.0200 474 LEU B C   
18637 O O   . LEU B  448 ? 0.2658 0.3583 0.2792 0.0058  -0.0103 -0.0185 474 LEU B O   
18638 C CB  . LEU B  448 ? 0.2692 0.3674 0.2853 0.0050  -0.0065 -0.0230 474 LEU B CB  
18639 C CG  . LEU B  448 ? 0.2886 0.3870 0.3044 0.0012  -0.0051 -0.0255 474 LEU B CG  
18640 C CD1 . LEU B  448 ? 0.3017 0.3983 0.3179 0.0045  -0.0014 -0.0262 474 LEU B CD1 
18641 C CD2 . LEU B  448 ? 0.2976 0.3899 0.3106 -0.0042 -0.0055 -0.0259 474 LEU B CD2 
18653 N N   . ILE B  449 ? 0.2737 0.3786 0.2904 0.0107  -0.0111 -0.0194 475 ILE B N   
18654 C CA  . ILE B  449 ? 0.2769 0.3819 0.2927 0.0149  -0.0117 -0.0170 475 ILE B CA  
18655 C C   . ILE B  449 ? 0.2613 0.3735 0.2776 0.0142  -0.0149 -0.0177 475 ILE B C   
18656 O O   . ILE B  449 ? 0.2536 0.3728 0.2719 0.0126  -0.0159 -0.0197 475 ILE B O   
18657 C CB  . ILE B  449 ? 0.2975 0.4033 0.3144 0.0209  -0.0094 -0.0155 475 ILE B CB  
18658 C CG1 . ILE B  449 ? 0.3214 0.4175 0.3371 0.0206  -0.0059 -0.0152 475 ILE B CG1 
18659 C CG2 . ILE B  449 ? 0.3034 0.4116 0.3197 0.0259  -0.0102 -0.0127 475 ILE B CG2 
18660 C CD1 . ILE B  449 ? 0.3446 0.4379 0.3606 0.0259  -0.0028 -0.0135 475 ILE B CD1 
18672 N N   . LYS B  450 ? 0.2552 0.3656 0.2693 0.0149  -0.0162 -0.0164 476 LYS B N   
18673 C CA  . LYS B  450 ? 0.2633 0.3797 0.2770 0.0138  -0.0189 -0.0174 476 LYS B CA  
18674 C C   . LYS B  450 ? 0.2625 0.3888 0.2782 0.0168  -0.0199 -0.0179 476 LYS B C   
18675 O O   . LYS B  450 ? 0.2596 0.3870 0.2757 0.0219  -0.0187 -0.0157 476 LYS B O   
18676 C CB  . LYS B  450 ? 0.2980 0.4111 0.3087 0.0156  -0.0195 -0.0156 476 LYS B CB  
18677 C CG  . LYS B  450 ? 0.3788 0.4842 0.3880 0.0123  -0.0191 -0.0154 476 LYS B CG  
18678 C CD  . LYS B  450 ? 0.4524 0.5552 0.4588 0.0147  -0.0192 -0.0134 476 LYS B CD  
18679 C CE  . LYS B  450 ? 0.5088 0.6053 0.5141 0.0117  -0.0189 -0.0130 476 LYS B CE  
18680 N NZ  . LYS B  450 ? 0.5265 0.6209 0.5291 0.0144  -0.0187 -0.0112 476 LYS B NZ  
18694 N N   . PRO B  451 ? 0.2672 0.4009 0.2845 0.0137  -0.0219 -0.0204 477 PRO B N   
18695 C CA  . PRO B  451 ? 0.2584 0.4030 0.2782 0.0164  -0.0230 -0.0206 477 PRO B CA  
18696 C C   . PRO B  451 ? 0.2489 0.3973 0.2671 0.0214  -0.0241 -0.0184 477 PRO B C   
18697 O O   . PRO B  451 ? 0.2380 0.3933 0.2584 0.0258  -0.0240 -0.0169 477 PRO B O   
18698 C CB  . PRO B  451 ? 0.2712 0.4218 0.2921 0.0112  -0.0252 -0.0238 477 PRO B CB  
18699 C CG  . PRO B  451 ? 0.2856 0.4282 0.3055 0.0061  -0.0245 -0.0251 477 PRO B CG  
18700 C CD  . PRO B  451 ? 0.2677 0.4003 0.2847 0.0077  -0.0231 -0.0229 477 PRO B CD  
18708 N N   . GLN B  452 ? 0.2501 0.3943 0.2645 0.0210  -0.0250 -0.0179 478 GLN B N   
18709 C CA  . GLN B  452 ? 0.2546 0.4021 0.2666 0.0254  -0.0260 -0.0158 478 GLN B CA  
18710 C C   . GLN B  452 ? 0.2537 0.3979 0.2658 0.0315  -0.0236 -0.0119 478 GLN B C   
18711 O O   . GLN B  452 ? 0.2559 0.4060 0.2675 0.0363  -0.0243 -0.0096 478 GLN B O   
18712 C CB  . GLN B  452 ? 0.2832 0.4257 0.2908 0.0234  -0.0269 -0.0163 478 GLN B CB  
18713 C CG  . GLN B  452 ? 0.3222 0.4681 0.3291 0.0178  -0.0292 -0.0201 478 GLN B CG  
18714 C CD  . GLN B  452 ? 0.3575 0.4957 0.3649 0.0126  -0.0282 -0.0219 478 GLN B CD  
18715 O OE1 . GLN B  452 ? 0.3636 0.4973 0.3731 0.0122  -0.0264 -0.0212 478 GLN B OE1 
18716 N NE2 . GLN B  452 ? 0.3610 0.4976 0.3663 0.0086  -0.0292 -0.0243 478 GLN B NE2 
18725 N N   . CYS B  453 ? 0.2501 0.3849 0.2625 0.0312  -0.0208 -0.0111 479 CYS B N   
18726 C CA  . CYS B  453 ? 0.2518 0.3816 0.2643 0.0363  -0.0179 -0.0077 479 CYS B CA  
18727 C C   . CYS B  453 ? 0.2557 0.3904 0.2721 0.0390  -0.0166 -0.0075 479 CYS B C   
18728 O O   . CYS B  453 ? 0.2678 0.4060 0.2851 0.0449  -0.0157 -0.0046 479 CYS B O   
18729 C CB  . CYS B  453 ? 0.2453 0.3632 0.2564 0.0339  -0.0156 -0.0075 479 CYS B CB  
18730 S SG  . CYS B  453 ? 0.2725 0.3819 0.2824 0.0392  -0.0119 -0.0033 479 CYS B SG  
18735 N N   . ALA B  454 ? 0.2496 0.3851 0.2685 0.0350  -0.0163 -0.0104 480 ALA B N   
18736 C CA  . ALA B  454 ? 0.2507 0.3909 0.2736 0.0374  -0.0146 -0.0106 480 ALA B CA  
18737 C C   . ALA B  454 ? 0.2463 0.3998 0.2719 0.0410  -0.0166 -0.0097 480 ALA B C   
18738 O O   . ALA B  454 ? 0.2417 0.3986 0.2703 0.0458  -0.0147 -0.0079 480 ALA B O   
18739 C CB  . ALA B  454 ? 0.2513 0.3906 0.2757 0.0318  -0.0142 -0.0140 480 ALA B CB  
18745 N N   . ALA B  455 ? 0.2451 0.4060 0.2698 0.0387  -0.0203 -0.0109 481 ALA B N   
18746 C CA  . ALA B  455 ? 0.2472 0.4219 0.2743 0.0414  -0.0228 -0.0102 481 ALA B CA  
18747 C C   . ALA B  455 ? 0.2452 0.4224 0.2722 0.0492  -0.0220 -0.0056 481 ALA B C   
18748 O O   . ALA B  455 ? 0.2363 0.4251 0.2666 0.0528  -0.0231 -0.0041 481 ALA B O   
18749 C CB  . ALA B  455 ? 0.2505 0.4303 0.2750 0.0373  -0.0267 -0.0124 481 ALA B CB  
18755 N N   . TYR B  456 ? 0.2432 0.4101 0.2664 0.0518  -0.0201 -0.0030 482 TYR B N   
18756 C CA  . TYR B  456 ? 0.2436 0.4113 0.2663 0.0592  -0.0189 0.0018  482 TYR B CA  
18757 C C   . TYR B  456 ? 0.2423 0.4082 0.2687 0.0644  -0.0150 0.0041  482 TYR B C   
18758 O O   . TYR B  456 ? 0.2405 0.4104 0.2678 0.0712  -0.0142 0.0083  482 TYR B O   
18759 C CB  . TYR B  456 ? 0.2504 0.4075 0.2679 0.0600  -0.0178 0.0038  482 TYR B CB  
18760 C CG  . TYR B  456 ? 0.2684 0.4299 0.2819 0.0583  -0.0213 0.0034  482 TYR B CG  
18761 C CD1 . TYR B  456 ? 0.2756 0.4476 0.2883 0.0626  -0.0236 0.0060  482 TYR B CD1 
18762 C CD2 . TYR B  456 ? 0.2847 0.4402 0.2951 0.0525  -0.0223 0.0005  482 TYR B CD2 
18763 C CE1 . TYR B  456 ? 0.2937 0.4696 0.3020 0.0609  -0.0267 0.0053  482 TYR B CE1 
18764 C CE2 . TYR B  456 ? 0.3003 0.4591 0.3066 0.0511  -0.0250 -0.0002 482 TYR B CE2 
18765 C CZ  . TYR B  456 ? 0.3087 0.4774 0.3136 0.0551  -0.0271 0.0020  482 TYR B CZ  
18766 O OH  . TYR B  456 ? 0.3276 0.4993 0.3279 0.0533  -0.0297 0.0009  482 TYR B OH  
18776 N N   . GLY B  457 ? 0.2388 0.3986 0.2671 0.0614  -0.0125 0.0015  483 GLY B N   
18777 C CA  . GLY B  457 ? 0.2383 0.3954 0.2698 0.0660  -0.0083 0.0031  483 GLY B CA  
18778 C C   . GLY B  457 ? 0.2469 0.3900 0.2767 0.0630  -0.0046 0.0013  483 GLY B C   
18779 O O   . GLY B  457 ? 0.2577 0.3964 0.2856 0.0563  -0.0057 -0.0021 483 GLY B O   
18783 N N   . LYS B  458 ? 0.2386 0.3747 0.2691 0.0678  -0.0001 0.0035  484 LYS B N   
18784 C CA  . LYS B  458 ? 0.2472 0.3699 0.2761 0.0654  0.0040  0.0017  484 LYS B CA  
18785 C C   . LYS B  458 ? 0.2433 0.3562 0.2676 0.0603  0.0031  0.0008  484 LYS B C   
18786 O O   . LYS B  458 ? 0.2407 0.3514 0.2625 0.0625  0.0024  0.0038  484 LYS B O   
18787 C CB  . LYS B  458 ? 0.2943 0.4107 0.3239 0.0724  0.0090  0.0051  484 LYS B CB  
18788 C CG  . LYS B  458 ? 0.3868 0.4946 0.4170 0.0717  0.0138  0.0029  484 LYS B CG  
18789 C CD  . LYS B  458 ? 0.4292 0.5373 0.4625 0.0802  0.0181  0.0063  484 LYS B CD  
18790 C CE  . LYS B  458 ? 0.4564 0.5780 0.4952 0.0831  0.0175  0.0060  484 LYS B CE  
18791 N NZ  . LYS B  458 ? 0.4424 0.5678 0.4847 0.0925  0.0204  0.0108  484 LYS B NZ  
18805 N N   . ALA B  459 ? 0.2359 0.3437 0.2591 0.0536  0.0032  -0.0030 485 ALA B N   
18806 C CA  . ALA B  459 ? 0.2273 0.3273 0.2469 0.0485  0.0022  -0.0039 485 ALA B CA  
18807 C C   . ALA B  459 ? 0.2220 0.3096 0.2397 0.0460  0.0058  -0.0050 485 ALA B C   
18808 O O   . ALA B  459 ? 0.2221 0.3079 0.2408 0.0445  0.0081  -0.0075 485 ALA B O   
18809 C CB  . ALA B  459 ? 0.2223 0.3277 0.2419 0.0423  -0.0016 -0.0071 485 ALA B CB  
18815 N N   . LEU B  460 ? 0.2078 0.2872 0.2226 0.0450  0.0064  -0.0035 486 LEU B N   
18816 C CA  . LEU B  460 ? 0.2080 0.2758 0.2208 0.0418  0.0094  -0.0045 486 LEU B CA  
18817 C C   . LEU B  460 ? 0.1978 0.2633 0.2086 0.0361  0.0068  -0.0052 486 LEU B C   
18818 O O   . LEU B  460 ? 0.1994 0.2652 0.2092 0.0375  0.0054  -0.0027 486 LEU B O   
18819 C CB  . LEU B  460 ? 0.2213 0.2811 0.2330 0.0469  0.0133  -0.0011 486 LEU B CB  
18820 C CG  . LEU B  460 ? 0.2530 0.3000 0.2622 0.0435  0.0166  -0.0018 486 LEU B CG  
18821 C CD1 . LEU B  460 ? 0.2584 0.3017 0.2675 0.0395  0.0188  -0.0060 486 LEU B CD1 
18822 C CD2 . LEU B  460 ? 0.2736 0.3132 0.2821 0.0490  0.0206  0.0018  486 LEU B CD2 
18834 N N   . ASP B  461 ? 0.1943 0.2581 0.2046 0.0299  0.0062  -0.0084 487 ASP B N   
18835 C CA  . ASP B  461 ? 0.1978 0.2599 0.2068 0.0245  0.0038  -0.0088 487 ASP B CA  
18836 C C   . ASP B  461 ? 0.2000 0.2522 0.2071 0.0210  0.0063  -0.0092 487 ASP B C   
18837 O O   . ASP B  461 ? 0.2032 0.2526 0.2097 0.0175  0.0076  -0.0119 487 ASP B O   
18838 C CB  . ASP B  461 ? 0.2275 0.2961 0.2374 0.0199  0.0007  -0.0116 487 ASP B CB  
18839 C CG  . ASP B  461 ? 0.2694 0.3376 0.2784 0.0153  -0.0020 -0.0114 487 ASP B CG  
18840 O OD1 . ASP B  461 ? 0.2603 0.3223 0.2681 0.0141  -0.0011 -0.0100 487 ASP B OD1 
18841 O OD2 . ASP B  461 ? 0.3225 0.3966 0.3324 0.0130  -0.0047 -0.0127 487 ASP B OD2 
18846 N N   . LEU B  462 ? 0.2000 0.2473 0.2061 0.0219  0.0069  -0.0065 488 LEU B N   
18847 C CA  . LEU B  462 ? 0.2102 0.2486 0.2148 0.0182  0.0090  -0.0066 488 LEU B CA  
18848 C C   . LEU B  462 ? 0.2088 0.2480 0.2133 0.0140  0.0064  -0.0057 488 LEU B C   
18849 O O   . LEU B  462 ? 0.2184 0.2516 0.2222 0.0121  0.0077  -0.0044 488 LEU B O   
18850 C CB  . LEU B  462 ? 0.2248 0.2561 0.2286 0.0228  0.0128  -0.0038 488 LEU B CB  
18851 C CG  . LEU B  462 ? 0.2505 0.2778 0.2542 0.0264  0.0167  -0.0046 488 LEU B CG  
18852 C CD1 . LEU B  462 ? 0.2596 0.2826 0.2630 0.0328  0.0196  -0.0006 488 LEU B CD1 
18853 C CD2 . LEU B  462 ? 0.2607 0.2801 0.2627 0.0212  0.0194  -0.0078 488 LEU B CD2 
18865 N N   . SER B  463 ? 0.1943 0.2407 0.1997 0.0123  0.0028  -0.0065 489 SER B N   
18866 C CA  . SER B  463 ? 0.1966 0.2441 0.2023 0.0089  0.0005  -0.0055 489 SER B CA  
18867 C C   . SER B  463 ? 0.1997 0.2436 0.2052 0.0028  0.0006  -0.0068 489 SER B C   
18868 O O   . SER B  463 ? 0.1852 0.2277 0.1899 0.0004  0.0015  -0.0094 489 SER B O   
18869 C CB  . SER B  463 ? 0.2110 0.2660 0.2175 0.0085  -0.0029 -0.0063 489 SER B CB  
18870 O OG  . SER B  463 ? 0.2363 0.2947 0.2434 0.0057  -0.0039 -0.0092 489 SER B OG  
18876 N N   . LEU B  464 ? 0.1994 0.2423 0.2054 0.0003  -0.0004 -0.0050 490 LEU B N   
18877 C CA  . LEU B  464 ? 0.2071 0.2482 0.2131 -0.0058 -0.0008 -0.0058 490 LEU B CA  
18878 C C   . LEU B  464 ? 0.2101 0.2446 0.2146 -0.0079 0.0021  -0.0073 490 LEU B C   
18879 O O   . LEU B  464 ? 0.2284 0.2624 0.2318 -0.0123 0.0020  -0.0098 490 LEU B O   
18880 C CB  . LEU B  464 ? 0.2128 0.2593 0.2192 -0.0093 -0.0036 -0.0077 490 LEU B CB  
18881 C CG  . LEU B  464 ? 0.2374 0.2895 0.2453 -0.0081 -0.0063 -0.0063 490 LEU B CG  
18882 C CD1 . LEU B  464 ? 0.2384 0.2954 0.2464 -0.0098 -0.0082 -0.0085 490 LEU B CD1 
18883 C CD2 . LEU B  464 ? 0.2490 0.3012 0.2584 -0.0108 -0.0075 -0.0040 490 LEU B CD2 
18895 N N   . ASN B  465 ? 0.2044 0.2334 0.2084 -0.0047 0.0050  -0.0057 491 ASN B N   
18896 C CA  . ASN B  465 ? 0.2068 0.2279 0.2092 -0.0066 0.0084  -0.0068 491 ASN B CA  
18897 C C   . ASN B  465 ? 0.2169 0.2341 0.2201 -0.0075 0.0095  -0.0039 491 ASN B C   
18898 O O   . ASN B  465 ? 0.2116 0.2331 0.2166 -0.0083 0.0071  -0.0017 491 ASN B O   
18899 C CB  . ASN B  465 ? 0.2046 0.2222 0.2058 -0.0014 0.0116  -0.0076 491 ASN B CB  
18900 C CG  . ASN B  465 ? 0.2366 0.2563 0.2369 -0.0025 0.0114  -0.0113 491 ASN B CG  
18901 O OD1 . ASN B  465 ? 0.2574 0.2730 0.2559 -0.0069 0.0129  -0.0140 491 ASN B OD1 
18902 N ND2 . ASN B  465 ? 0.2187 0.2451 0.2201 0.0009  0.0098  -0.0114 491 ASN B ND2 
18909 N N   . SER B  466 ? 0.2281 0.2370 0.2300 -0.0079 0.0132  -0.0038 492 SER B N   
18910 C CA  . SER B  466 ? 0.2565 0.2614 0.2593 -0.0091 0.0147  -0.0011 492 SER B CA  
18911 C C   . SER B  466 ? 0.2691 0.2673 0.2708 -0.0034 0.0186  0.0011  492 SER B C   
18912 O O   . SER B  466 ? 0.2738 0.2643 0.2749 -0.0052 0.0219  0.0017  492 SER B O   
18913 C CB  . SER B  466 ? 0.2840 0.2849 0.2861 -0.0166 0.0154  -0.0032 492 SER B CB  
18914 O OG  . SER B  466 ? 0.3340 0.3420 0.3372 -0.0215 0.0115  -0.0043 492 SER B OG  
18920 N N   . ILE B  467 ? 0.2731 0.2744 0.2749 0.0033  0.0184  0.0026  493 ILE B N   
18921 C CA  . ILE B  467 ? 0.2842 0.2803 0.2850 0.0095  0.0219  0.0054  493 ILE B CA  
18922 C C   . ILE B  467 ? 0.2937 0.2917 0.2955 0.0109  0.0211  0.0094  493 ILE B C   
18923 O O   . ILE B  467 ? 0.2927 0.2961 0.2946 0.0157  0.0195  0.0116  493 ILE B O   
18924 C CB  . ILE B  467 ? 0.2890 0.2885 0.2894 0.0159  0.0218  0.0053  493 ILE B CB  
18925 C CG1 . ILE B  467 ? 0.3036 0.3026 0.3034 0.0138  0.0222  0.0009  493 ILE B CG1 
18926 C CG2 . ILE B  467 ? 0.2933 0.2874 0.2928 0.0226  0.0256  0.0088  493 ILE B CG2 
18927 C CD1 . ILE B  467 ? 0.3217 0.3258 0.3219 0.0198  0.0219  0.0007  493 ILE B CD1 
18939 N N   A PHE B  468 ? 0.2990 0.2930 0.3016 0.0062  0.0222  0.0103  494 PHE B N   
18940 N N   B PHE B  468 ? 0.3021 0.2960 0.3046 0.0062  0.0223  0.0103  494 PHE B N   
18941 C CA  A PHE B  468 ? 0.3066 0.3025 0.3104 0.0069  0.0219  0.0141  494 PHE B CA  
18942 C CA  B PHE B  468 ? 0.3129 0.3086 0.3167 0.0069  0.0220  0.0141  494 PHE B CA  
18943 C C   A PHE B  468 ? 0.3245 0.3161 0.3271 0.0131  0.0251  0.0181  494 PHE B C   
18944 C C   B PHE B  468 ? 0.3273 0.3191 0.3298 0.0133  0.0250  0.0181  494 PHE B C   
18945 O O   A PHE B  468 ? 0.3208 0.3148 0.3239 0.0149  0.0248  0.0214  494 PHE B O   
18946 O O   B PHE B  468 ? 0.3235 0.3181 0.3264 0.0153  0.0246  0.0213  494 PHE B O   
18947 C CB  A PHE B  468 ? 0.3010 0.2950 0.3066 -0.0002 0.0221  0.0140  494 PHE B CB  
18948 C CB  B PHE B  468 ? 0.3129 0.3055 0.3183 0.0003  0.0229  0.0144  494 PHE B CB  
18949 C CG  A PHE B  468 ? 0.3077 0.2920 0.3124 -0.0036 0.0261  0.0132  494 PHE B CG  
18950 C CG  B PHE B  468 ? 0.3217 0.3139 0.3275 -0.0070 0.0218  0.0105  494 PHE B CG  
18951 C CD1 A PHE B  468 ? 0.3159 0.2937 0.3204 -0.0019 0.0299  0.0166  494 PHE B CD1 
18952 C CD1 B PHE B  468 ? 0.3376 0.3212 0.3418 -0.0104 0.0251  0.0084  494 PHE B CD1 
18953 C CD2 A PHE B  468 ? 0.3171 0.2984 0.3208 -0.0089 0.0263  0.0090  494 PHE B CD2 
18954 C CD2 B PHE B  468 ? 0.3303 0.3303 0.3376 -0.0105 0.0177  0.0090  494 PHE B CD2 
18955 C CE1 A PHE B  468 ? 0.3253 0.2933 0.3288 -0.0055 0.0338  0.0156  494 PHE B CE1 
18956 C CE1 B PHE B  468 ? 0.3499 0.3333 0.3537 -0.0175 0.0240  0.0047  494 PHE B CE1 
18957 C CE2 A PHE B  468 ? 0.3280 0.2997 0.3304 -0.0125 0.0302  0.0078  494 PHE B CE2 
18958 C CE2 B PHE B  468 ? 0.3389 0.3392 0.3463 -0.0173 0.0165  0.0058  494 PHE B CE2 
18959 C CZ  A PHE B  468 ? 0.3249 0.2898 0.3273 -0.0109 0.0340  0.0111  494 PHE B CZ  
18960 C CZ  B PHE B  468 ? 0.3418 0.3340 0.3472 -0.0209 0.0196  0.0035  494 PHE B CZ  
18979 N N   . PHE B  469 ? 0.3428 0.3278 0.3436 0.0165  0.0285  0.0180  495 PHE B N   
18980 C CA  . PHE B  469 ? 0.3795 0.3600 0.3788 0.0227  0.0318  0.0222  495 PHE B CA  
18981 C C   . PHE B  469 ? 0.3975 0.3759 0.3955 0.0279  0.0334  0.0214  495 PHE B C   
18982 O O   . PHE B  469 ? 0.4007 0.3741 0.3985 0.0253  0.0352  0.0181  495 PHE B O   
18983 C CB  . PHE B  469 ? 0.3950 0.3655 0.3942 0.0197  0.0361  0.0239  495 PHE B CB  
18984 C CG  . PHE B  469 ? 0.4247 0.3893 0.4224 0.0259  0.0401  0.0286  495 PHE B CG  
18985 C CD1 . PHE B  469 ? 0.4371 0.4051 0.4346 0.0291  0.0398  0.0330  495 PHE B CD1 
18986 C CD2 . PHE B  469 ? 0.4440 0.3992 0.4402 0.0285  0.0446  0.0288  495 PHE B CD2 
18987 C CE1 . PHE B  469 ? 0.4507 0.4133 0.4464 0.0347  0.0436  0.0377  495 PHE B CE1 
18988 C CE2 . PHE B  469 ? 0.4559 0.4054 0.4506 0.0344  0.0485  0.0337  495 PHE B CE2 
18989 C CZ  . PHE B  469 ? 0.4522 0.4058 0.4466 0.0376  0.0478  0.0382  495 PHE B CZ  
18999 N N   . ILE B  470 ? 0.3981 0.3807 0.3954 0.0351  0.0330  0.0245  496 ILE B N   
19000 C CA  . ILE B  470 ? 0.4044 0.3865 0.4009 0.0410  0.0345  0.0247  496 ILE B CA  
19001 C C   . ILE B  470 ? 0.4230 0.3952 0.4182 0.0451  0.0398  0.0287  496 ILE B C   
19002 O O   . ILE B  470 ? 0.4167 0.3895 0.4109 0.0490  0.0405  0.0333  496 ILE B O   
19003 C CB  . ILE B  470 ? 0.4027 0.3960 0.3992 0.0463  0.0307  0.0260  496 ILE B CB  
19004 C CG1 . ILE B  470 ? 0.4132 0.4154 0.4110 0.0418  0.0257  0.0219  496 ILE B CG1 
19005 C CG2 . ILE B  470 ? 0.4037 0.3974 0.4001 0.0529  0.0324  0.0269  496 ILE B CG2 
19006 C CD1 . ILE B  470 ? 0.4275 0.4403 0.4250 0.0452  0.0218  0.0230  496 ILE B CD1 
19018 N N   . GLY B  471 ? 0.4421 0.4048 0.4370 0.0438  0.0439  0.0268  497 GLY B N   
19019 C CA  . GLY B  471 ? 0.4676 0.4191 0.4613 0.0474  0.0497  0.0302  497 GLY B CA  
19020 C C   . GLY B  471 ? 0.4869 0.4397 0.4803 0.0564  0.0512  0.0329  497 GLY B C   
19021 O O   . GLY B  471 ? 0.4847 0.4469 0.4792 0.0589  0.0480  0.0314  497 GLY B O   
19025 N N   . PRO B  472 ? 0.5052 0.4488 0.4975 0.0613  0.0565  0.0372  498 PRO B N   
19026 C CA  . PRO B  472 ? 0.5119 0.4575 0.5043 0.0706  0.0580  0.0408  498 PRO B CA  
19027 C C   . PRO B  472 ? 0.5138 0.4599 0.5075 0.0724  0.0589  0.0373  498 PRO B C   
19028 O O   . PRO B  472 ? 0.5243 0.4771 0.5191 0.0797  0.0582  0.0399  498 PRO B O   
19029 C CB  . PRO B  472 ? 0.5300 0.4632 0.5209 0.0744  0.0642  0.0459  498 PRO B CB  
19030 C CG  . PRO B  472 ? 0.5383 0.4609 0.5285 0.0661  0.0668  0.0434  498 PRO B CG  
19031 C CD  . PRO B  472 ? 0.5105 0.4423 0.5016 0.0589  0.0610  0.0397  498 PRO B CD  
19039 N N   . ASN B  473 ? 0.5058 0.4462 0.4996 0.0658  0.0601  0.0315  499 ASN B N   
19040 C CA  . ASN B  473 ? 0.4994 0.4400 0.4942 0.0673  0.0613  0.0279  499 ASN B CA  
19041 C C   . ASN B  473 ? 0.4806 0.4317 0.4765 0.0622  0.0559  0.0225  499 ASN B C   
19042 O O   . ASN B  473 ? 0.4799 0.4314 0.4766 0.0624  0.0569  0.0190  499 ASN B O   
19043 C CB  . ASN B  473 ? 0.5282 0.4532 0.5214 0.0641  0.0676  0.0250  499 ASN B CB  
19044 C CG  . ASN B  473 ? 0.5923 0.5048 0.5842 0.0681  0.0736  0.0298  499 ASN B CG  
19045 O OD1 . ASN B  473 ? 0.6152 0.5298 0.6077 0.0767  0.0747  0.0357  499 ASN B OD1 
19046 N ND2 . ASN B  473 ? 0.6097 0.5091 0.5997 0.0620  0.0776  0.0277  499 ASN B ND2 
19053 N N   . GLN B  474 ? 0.4601 0.4196 0.4563 0.0578  0.0506  0.0219  500 GLN B N   
19054 C CA  . GLN B  474 ? 0.4459 0.4145 0.4431 0.0525  0.0457  0.0172  500 GLN B CA  
19055 C C   . GLN B  474 ? 0.4335 0.4117 0.4326 0.0570  0.0438  0.0161  500 GLN B C   
19056 O O   . GLN B  474 ? 0.4285 0.4085 0.4281 0.0533  0.0430  0.0115  500 GLN B O   
19057 C CB  . GLN B  474 ? 0.4545 0.4310 0.4518 0.0491  0.0405  0.0180  500 GLN B CB  
19058 C CG  . GLN B  474 ? 0.4770 0.4619 0.4753 0.0432  0.0357  0.0134  500 GLN B CG  
19059 C CD  . GLN B  474 ? 0.5057 0.4838 0.5032 0.0356  0.0371  0.0088  500 GLN B CD  
19060 O OE1 . GLN B  474 ? 0.5131 0.4839 0.5097 0.0312  0.0388  0.0089  500 GLN B OE1 
19061 N NE2 . GLN B  474 ? 0.5099 0.4906 0.5077 0.0337  0.0365  0.0046  500 GLN B NE2 
19070 N N   . PHE B  475 ? 0.4264 0.4115 0.4265 0.0646  0.0428  0.0205  501 PHE B N   
19071 C CA  . PHE B  475 ? 0.4279 0.4241 0.4304 0.0688  0.0404  0.0199  501 PHE B CA  
19072 C C   . PHE B  475 ? 0.4391 0.4324 0.4429 0.0766  0.0450  0.0224  501 PHE B C   
19073 O O   . PHE B  475 ? 0.4404 0.4441 0.4466 0.0820  0.0431  0.0239  501 PHE B O   
19074 C CB  . PHE B  475 ? 0.4199 0.4288 0.4229 0.0709  0.0351  0.0225  501 PHE B CB  
19075 C CG  . PHE B  475 ? 0.4251 0.4370 0.4272 0.0635  0.0309  0.0198  501 PHE B CG  
19076 C CD1 . PHE B  475 ? 0.4328 0.4473 0.4357 0.0572  0.0287  0.0146  501 PHE B CD1 
19077 C CD2 . PHE B  475 ? 0.4347 0.4465 0.4351 0.0631  0.0295  0.0227  501 PHE B CD2 
19078 C CE1 . PHE B  475 ? 0.4365 0.4536 0.4388 0.0509  0.0251  0.0127  501 PHE B CE1 
19079 C CE2 . PHE B  475 ? 0.4403 0.4548 0.4403 0.0568  0.0261  0.0205  501 PHE B CE2 
19080 C CZ  . PHE B  475 ? 0.4328 0.4498 0.4338 0.0509  0.0239  0.0156  501 PHE B CZ  
19090 N N   . GLU B  476 ? 0.4466 0.4261 0.4491 0.0769  0.0509  0.0224  502 GLU B N   
19091 C CA  . GLU B  476 ? 0.4626 0.4374 0.4664 0.0845  0.0562  0.0249  502 GLU B CA  
19092 C C   . GLU B  476 ? 0.4592 0.4379 0.4651 0.0842  0.0567  0.0204  502 GLU B C   
19093 O O   . GLU B  476 ? 0.4543 0.4328 0.4593 0.0768  0.0552  0.0148  502 GLU B O   
19094 C CB  . GLU B  476 ? 0.5156 0.4728 0.5169 0.0837  0.0628  0.0255  502 GLU B CB  
19095 C CG  . GLU B  476 ? 0.6207 0.5712 0.6230 0.0926  0.0690  0.0293  502 GLU B CG  
19096 C CD  . GLU B  476 ? 0.7579 0.6897 0.7575 0.0915  0.0761  0.0295  502 GLU B CD  
19097 O OE1 . GLU B  476 ? 0.7974 0.7215 0.7945 0.0831  0.0763  0.0259  502 GLU B OE1 
19098 O OE2 . GLU B  476 ? 0.7965 0.7215 0.7968 0.0992  0.0817  0.0334  502 GLU B OE2 
19105 N N   . ASN B  477 ? 0.4550 0.4374 0.4636 0.0926  0.0590  0.0232  503 ASN B N   
19106 C CA  . ASN B  477 ? 0.4550 0.4410 0.4661 0.0938  0.0605  0.0198  503 ASN B CA  
19107 C C   . ASN B  477 ? 0.4415 0.4417 0.4543 0.0892  0.0543  0.0159  503 ASN B C   
19108 O O   . ASN B  477 ? 0.4417 0.4431 0.4554 0.0867  0.0552  0.0114  503 ASN B O   
19109 C CB  . ASN B  477 ? 0.4865 0.4573 0.4951 0.0898  0.0665  0.0153  503 ASN B CB  
19110 C CG  . ASN B  477 ? 0.5488 0.5038 0.5552 0.0930  0.0729  0.0185  503 ASN B CG  
19111 O OD1 . ASN B  477 ? 0.5662 0.5209 0.5744 0.1019  0.0756  0.0242  503 ASN B OD1 
19112 N ND2 . ASN B  477 ? 0.5710 0.5127 0.5735 0.0858  0.0754  0.0150  503 ASN B ND2 
19119 N N   . LEU B  478 ? 0.4221 0.4329 0.4352 0.0883  0.0484  0.0178  504 LEU B N   
19120 C CA  . LEU B  478 ? 0.4077 0.4313 0.4223 0.0838  0.0424  0.0145  504 LEU B CA  
19121 C C   . LEU B  478 ? 0.3860 0.4242 0.4048 0.0905  0.0401  0.0173  504 LEU B C   
19122 O O   . LEU B  478 ? 0.3859 0.4260 0.4055 0.0978  0.0411  0.0228  504 LEU B O   
19123 C CB  . LEU B  478 ? 0.4132 0.4390 0.4255 0.0788  0.0377  0.0149  504 LEU B CB  
19124 C CG  . LEU B  478 ? 0.4346 0.4627 0.4456 0.0698  0.0337  0.0100  504 LEU B CG  
19125 C CD1 . LEU B  478 ? 0.4469 0.4660 0.4566 0.0643  0.0368  0.0051  504 LEU B CD1 
19126 C CD2 . LEU B  478 ? 0.4397 0.4652 0.4482 0.0663  0.0313  0.0114  504 LEU B CD2 
19138 N N   . PRO B  479 ? 0.3682 0.4175 0.3895 0.0880  0.0369  0.0139  505 PRO B N   
19139 C CA  . PRO B  479 ? 0.3490 0.4136 0.3745 0.0938  0.0341  0.0167  505 PRO B CA  
19140 C C   . PRO B  479 ? 0.3310 0.4042 0.3555 0.0942  0.0287  0.0197  505 PRO B C   
19141 O O   . PRO B  479 ? 0.3332 0.3999 0.3540 0.0906  0.0276  0.0200  505 PRO B O   
19142 C CB  . PRO B  479 ? 0.3577 0.4302 0.3856 0.0893  0.0322  0.0116  505 PRO B CB  
19143 C CG  . PRO B  479 ? 0.3714 0.4363 0.3956 0.0801  0.0312  0.0069  505 PRO B CG  
19144 C CD  . PRO B  479 ? 0.3586 0.4076 0.3790 0.0797  0.0353  0.0078  505 PRO B CD  
19152 N N   . ASP B  480 ? 0.3097 0.3976 0.3374 0.0987  0.0254  0.0223  506 ASP B N   
19153 C CA  . ASP B  480 ? 0.3056 0.4025 0.3320 0.0993  0.0204  0.0249  506 ASP B CA  
19154 C C   . ASP B  480 ? 0.2826 0.3829 0.3071 0.0907  0.0156  0.0203  506 ASP B C   
19155 O O   . ASP B  480 ? 0.2900 0.4024 0.3170 0.0887  0.0118  0.0180  506 ASP B O   
19156 C CB  . ASP B  480 ? 0.3365 0.4490 0.3669 0.1061  0.0182  0.0286  506 ASP B CB  
19157 C CG  . ASP B  480 ? 0.4169 0.5388 0.4453 0.1073  0.0132  0.0316  506 ASP B CG  
19158 O OD1 . ASP B  480 ? 0.4370 0.5538 0.4610 0.1026  0.0114  0.0305  506 ASP B OD1 
19159 O OD2 . ASP B  480 ? 0.4409 0.5758 0.4721 0.1129  0.0113  0.0350  506 ASP B OD2 
19164 N N   . ILE B  481 ? 0.2532 0.3430 0.2737 0.0858  0.0159  0.0190  507 ILE B N   
19165 C CA  . ILE B  481 ? 0.2392 0.3308 0.2580 0.0779  0.0119  0.0150  507 ILE B CA  
19166 C C   . ILE B  481 ? 0.2301 0.3315 0.2477 0.0784  0.0071  0.0166  507 ILE B C   
19167 O O   . ILE B  481 ? 0.2457 0.3450 0.2608 0.0822  0.0074  0.0207  507 ILE B O   
19168 C CB  . ILE B  481 ? 0.2445 0.3222 0.2599 0.0727  0.0140  0.0134  507 ILE B CB  
19169 C CG1 . ILE B  481 ? 0.2617 0.3296 0.2777 0.0712  0.0187  0.0109  507 ILE B CG1 
19170 C CG2 . ILE B  481 ? 0.2424 0.3223 0.2562 0.0653  0.0098  0.0100  507 ILE B CG2 
19171 C CD1 . ILE B  481 ? 0.2730 0.3460 0.2914 0.0674  0.0179  0.0062  507 ILE B CD1 
19183 N N   . ALA B  482 ? 0.2148 0.3261 0.2335 0.0743  0.0028  0.0134  508 ALA B N   
19184 C CA  . ALA B  482 ? 0.2113 0.3319 0.2285 0.0733  -0.0019 0.0136  508 ALA B CA  
19185 C C   . ALA B  482 ? 0.2152 0.3312 0.2293 0.0660  -0.0040 0.0103  508 ALA B C   
19186 O O   . ALA B  482 ? 0.2084 0.3273 0.2197 0.0653  -0.0067 0.0110  508 ALA B O   
19187 C CB  . ALA B  482 ? 0.2041 0.3390 0.2249 0.0734  -0.0050 0.0120  508 ALA B CB  
19193 N N   . CYS B  483 ? 0.2152 0.3251 0.2300 0.0606  -0.0029 0.0067  509 CYS B N   
19194 C CA  . CYS B  483 ? 0.2229 0.3292 0.2357 0.0538  -0.0047 0.0038  509 CYS B CA  
19195 C C   . CYS B  483 ? 0.2335 0.3270 0.2450 0.0514  -0.0014 0.0036  509 CYS B C   
19196 O O   . CYS B  483 ? 0.2348 0.3244 0.2478 0.0506  0.0011  0.0021  509 CYS B O   
19197 C CB  . CYS B  483 ? 0.2311 0.3444 0.2462 0.0490  -0.0072 -0.0003 509 CYS B CB  
19198 S SG  . CYS B  483 ? 0.2776 0.3849 0.2911 0.0406  -0.0084 -0.0040 509 CYS B SG  
19203 N N   . LEU B  484 ? 0.2242 0.3113 0.2329 0.0502  -0.0012 0.0051  510 LEU B N   
19204 C CA  . LEU B  484 ? 0.2228 0.2984 0.2303 0.0477  0.0018  0.0051  510 LEU B CA  
19205 C C   . LEU B  484 ? 0.2226 0.2956 0.2287 0.0420  0.0000  0.0037  510 LEU B C   
19206 O O   . LEU B  484 ? 0.2254 0.3008 0.2299 0.0424  -0.0019 0.0050  510 LEU B O   
19207 C CB  . LEU B  484 ? 0.2304 0.2999 0.2365 0.0529  0.0049  0.0095  510 LEU B CB  
19208 C CG  . LEU B  484 ? 0.2590 0.3163 0.2638 0.0503  0.0083  0.0099  510 LEU B CG  
19209 C CD1 . LEU B  484 ? 0.2647 0.3168 0.2708 0.0479  0.0109  0.0070  510 LEU B CD1 
19210 C CD2 . LEU B  484 ? 0.2657 0.3176 0.2690 0.0557  0.0113  0.0146  510 LEU B CD2 
19222 N N   . ASN B  485 ? 0.2065 0.2747 0.2131 0.0367  0.0007  0.0011  511 ASN B N   
19223 C CA  . ASN B  485 ? 0.2039 0.2698 0.2097 0.0314  -0.0009 0.0002  511 ASN B CA  
19224 C C   . ASN B  485 ? 0.2050 0.2611 0.2100 0.0292  0.0019  0.0010  511 ASN B C   
19225 O O   . ASN B  485 ? 0.2048 0.2566 0.2102 0.0271  0.0038  -0.0006 511 ASN B O   
19226 C CB  . ASN B  485 ? 0.2152 0.2856 0.2223 0.0265  -0.0033 -0.0034 511 ASN B CB  
19227 C CG  . ASN B  485 ? 0.2385 0.3078 0.2451 0.0218  -0.0052 -0.0040 511 ASN B CG  
19228 O OD1 . ASN B  485 ? 0.2359 0.3017 0.2414 0.0220  -0.0048 -0.0019 511 ASN B OD1 
19229 N ND2 . ASN B  485 ? 0.2611 0.3340 0.2685 0.0177  -0.0072 -0.0066 511 ASN B ND2 
19236 N N   . LEU B  486 ? 0.1970 0.2499 0.2008 0.0298  0.0023  0.0037  512 LEU B N   
19237 C CA  . LEU B  486 ? 0.2136 0.2583 0.2170 0.0272  0.0046  0.0048  512 LEU B CA  
19238 C C   . LEU B  486 ? 0.2116 0.2571 0.2152 0.0227  0.0025  0.0047  512 LEU B C   
19239 O O   . LEU B  486 ? 0.2165 0.2572 0.2200 0.0214  0.0039  0.0066  512 LEU B O   
19240 C CB  . LEU B  486 ? 0.2330 0.2730 0.2351 0.0320  0.0074  0.0086  512 LEU B CB  
19241 C CG  . LEU B  486 ? 0.2734 0.3104 0.2754 0.0365  0.0105  0.0093  512 LEU B CG  
19242 C CD1 . LEU B  486 ? 0.2796 0.3145 0.2802 0.0423  0.0125  0.0138  512 LEU B CD1 
19243 C CD2 . LEU B  486 ? 0.2905 0.3189 0.2927 0.0330  0.0136  0.0075  512 LEU B CD2 
19255 N N   . SER B  487 ? 0.1971 0.2486 0.2014 0.0204  -0.0006 0.0026  513 SER B N   
19256 C CA  . SER B  487 ? 0.1927 0.2451 0.1976 0.0167  -0.0024 0.0027  513 SER B CA  
19257 C C   . SER B  487 ? 0.1978 0.2455 0.2037 0.0117  -0.0015 0.0024  513 SER B C   
19258 O O   . SER B  487 ? 0.1981 0.2436 0.2041 0.0096  -0.0006 0.0004  513 SER B O   
19259 C CB  . SER B  487 ? 0.2044 0.2630 0.2099 0.0148  -0.0054 0.0002  513 SER B CB  
19260 O OG  . SER B  487 ? 0.2300 0.2890 0.2361 0.0115  -0.0068 0.0004  513 SER B OG  
19266 N N   . ALA B  488 ? 0.1988 0.2454 0.2055 0.0097  -0.0017 0.0042  514 ALA B N   
19267 C CA  . ALA B  488 ? 0.2011 0.2450 0.2092 0.0044  -0.0015 0.0041  514 ALA B CA  
19268 C C   . ALA B  488 ? 0.2042 0.2420 0.2117 0.0030  0.0011  0.0037  514 ALA B C   
19269 O O   . ALA B  488 ? 0.2139 0.2507 0.2214 -0.0012 0.0009  0.0014  514 ALA B O   
19270 C CB  . ALA B  488 ? 0.2082 0.2560 0.2172 0.0003  -0.0041 0.0019  514 ALA B CB  
19276 N N   . ASN B  489 ? 0.1964 0.2297 0.2030 0.0063  0.0038  0.0058  515 ASN B N   
19277 C CA  . ASN B  489 ? 0.2003 0.2264 0.2062 0.0051  0.0070  0.0057  515 ASN B CA  
19278 C C   . ASN B  489 ? 0.2112 0.2335 0.2181 0.0034  0.0086  0.0085  515 ASN B C   
19279 O O   . ASN B  489 ? 0.2132 0.2287 0.2193 0.0030  0.0118  0.0090  515 ASN B O   
19280 C CB  . ASN B  489 ? 0.2027 0.2258 0.2070 0.0107  0.0095  0.0061  515 ASN B CB  
19281 C CG  . ASN B  489 ? 0.2258 0.2500 0.2296 0.0105  0.0094  0.0027  515 ASN B CG  
19282 O OD1 . ASN B  489 ? 0.2349 0.2538 0.2379 0.0077  0.0114  0.0007  515 ASN B OD1 
19283 N ND2 . ASN B  489 ? 0.2292 0.2601 0.2332 0.0130  0.0070  0.0018  515 ASN B ND2 
19290 N N   . SER B  490 ? 0.2172 0.2436 0.2258 0.0023  0.0068  0.0103  516 SER B N   
19291 C CA  . SER B  490 ? 0.2384 0.2628 0.2486 0.0007  0.0082  0.0133  516 SER B CA  
19292 C C   . SER B  490 ? 0.2521 0.2711 0.2608 0.0051  0.0117  0.0159  516 SER B C   
19293 O O   . SER B  490 ? 0.2570 0.2714 0.2665 0.0030  0.0141  0.0176  516 SER B O   
19294 C CB  A SER B  490 ? 0.2654 0.2878 0.2771 -0.0060 0.0083  0.0121  516 SER B CB  
19295 C CB  B SER B  490 ? 0.2526 0.2750 0.2642 -0.0060 0.0083  0.0120  516 SER B CB  
19296 O OG  A SER B  490 ? 0.3081 0.3234 0.3181 -0.0074 0.0112  0.0106  516 SER B OG  
19297 O OG  B SER B  490 ? 0.2684 0.2961 0.2811 -0.0097 0.0051  0.0099  516 SER B OG  
19306 N N   . ASN B  491 ? 0.2479 0.2678 0.2544 0.0110  0.0119  0.0165  517 ASN B N   
19307 C CA  . ASN B  491 ? 0.2565 0.2717 0.2613 0.0158  0.0151  0.0194  517 ASN B CA  
19308 C C   . ASN B  491 ? 0.2505 0.2671 0.2554 0.0178  0.0157  0.0231  517 ASN B C   
19309 O O   . ASN B  491 ? 0.2438 0.2662 0.2483 0.0200  0.0135  0.0234  517 ASN B O   
19310 C CB  . ASN B  491 ? 0.2783 0.2952 0.2810 0.0214  0.0148  0.0188  517 ASN B CB  
19311 C CG  . ASN B  491 ? 0.3060 0.3173 0.3069 0.0264  0.0185  0.0219  517 ASN B CG  
19312 O OD1 . ASN B  491 ? 0.3071 0.3158 0.3075 0.0278  0.0204  0.0253  517 ASN B OD1 
19313 N ND2 . ASN B  491 ? 0.3069 0.3158 0.3068 0.0291  0.0198  0.0209  517 ASN B ND2 
19320 N N   . ALA B  492 ? 0.2578 0.2688 0.2632 0.0168  0.0188  0.0257  518 ALA B N   
19321 C CA  . ALA B  492 ? 0.2750 0.2867 0.2807 0.0184  0.0201  0.0295  518 ALA B CA  
19322 C C   . ALA B  492 ? 0.2896 0.2961 0.2927 0.0234  0.0237  0.0330  518 ALA B C   
19323 O O   . ALA B  492 ? 0.3067 0.3117 0.3100 0.0239  0.0258  0.0364  518 ALA B O   
19324 C CB  . ALA B  492 ? 0.2781 0.2888 0.2873 0.0124  0.0208  0.0301  518 ALA B CB  
19330 N N   . GLN B  493 ? 0.2836 0.2877 0.2844 0.0275  0.0245  0.0326  519 GLN B N   
19331 C CA  . GLN B  493 ? 0.2920 0.2908 0.2904 0.0325  0.0281  0.0365  519 GLN B CA  
19332 C C   . GLN B  493 ? 0.2956 0.2995 0.2912 0.0385  0.0274  0.0395  519 GLN B C   
19333 O O   . GLN B  493 ? 0.2843 0.2957 0.2794 0.0392  0.0239  0.0379  519 GLN B O   
19334 C CB  . GLN B  493 ? 0.3045 0.2983 0.3018 0.0348  0.0298  0.0353  519 GLN B CB  
19335 C CG  . GLN B  493 ? 0.3465 0.3461 0.3419 0.0407  0.0277  0.0350  519 GLN B CG  
19336 C CD  . GLN B  493 ? 0.4069 0.4019 0.4023 0.0423  0.0296  0.0335  519 GLN B CD  
19337 O OE1 . GLN B  493 ? 0.4062 0.4036 0.4027 0.0398  0.0276  0.0295  519 GLN B OE1 
19338 N NE2 . GLN B  493 ? 0.4157 0.4036 0.4097 0.0464  0.0337  0.0369  519 GLN B NE2 
19347 N N   . VAL B  494 ? 0.3064 0.3058 0.2999 0.0427  0.0308  0.0439  520 VAL B N   
19348 C CA  . VAL B  494 ? 0.3124 0.3159 0.3024 0.0489  0.0306  0.0472  520 VAL B CA  
19349 C C   . VAL B  494 ? 0.3193 0.3228 0.3075 0.0541  0.0307  0.0475  520 VAL B C   
19350 O O   . VAL B  494 ? 0.3297 0.3259 0.3174 0.0564  0.0344  0.0501  520 VAL B O   
19351 C CB  . VAL B  494 ? 0.3250 0.3237 0.3136 0.0505  0.0346  0.0523  520 VAL B CB  
19352 C CG1 . VAL B  494 ? 0.3254 0.3284 0.3095 0.0574  0.0345  0.0560  520 VAL B CG1 
19353 C CG2 . VAL B  494 ? 0.3290 0.3285 0.3202 0.0454  0.0348  0.0522  520 VAL B CG2 
19363 N N   . LEU B  495 ? 0.3141 0.3257 0.3016 0.0560  0.0268  0.0450  521 LEU B N   
19364 C CA  . LEU B  495 ? 0.3137 0.3274 0.2999 0.0614  0.0265  0.0456  521 LEU B CA  
19365 C C   . LEU B  495 ? 0.3293 0.3433 0.3118 0.0679  0.0283  0.0512  521 LEU B C   
19366 O O   . LEU B  495 ? 0.3134 0.3308 0.2937 0.0685  0.0277  0.0530  521 LEU B O   
19367 C CB  . LEU B  495 ? 0.3169 0.3403 0.3033 0.0613  0.0217  0.0418  521 LEU B CB  
19368 C CG  . LEU B  495 ? 0.3410 0.3646 0.3307 0.0553  0.0198  0.0365  521 LEU B CG  
19369 C CD1 . LEU B  495 ? 0.3501 0.3833 0.3398 0.0545  0.0152  0.0331  521 LEU B CD1 
19370 C CD2 . LEU B  495 ? 0.3564 0.3746 0.3479 0.0554  0.0219  0.0354  521 LEU B CD2 
19382 N N   . SER B  496 ? 0.3515 0.3611 0.3334 0.0726  0.0312  0.0543  522 SER B N   
19383 C CA  . SER B  496 ? 0.3767 0.3852 0.3553 0.0788  0.0337  0.0603  522 SER B CA  
19384 C C   . SER B  496 ? 0.3842 0.3966 0.3615 0.0861  0.0334  0.0631  522 SER B C   
19385 O O   . SER B  496 ? 0.3970 0.4066 0.3719 0.0915  0.0363  0.0687  522 SER B O   
19386 C CB  . SER B  496 ? 0.4053 0.4017 0.3845 0.0774  0.0390  0.0634  522 SER B CB  
19387 O OG  . SER B  496 ? 0.4523 0.4412 0.4338 0.0769  0.0416  0.0620  522 SER B OG  
19393 N N   . GLY B  497 ? 0.3726 0.3923 0.3515 0.0864  0.0299  0.0596  523 GLY B N   
19394 C CA  . GLY B  497 ? 0.3734 0.3991 0.3517 0.0933  0.0292  0.0621  523 GLY B CA  
19395 C C   . GLY B  497 ? 0.3765 0.3958 0.3574 0.0964  0.0326  0.0631  523 GLY B C   
19396 O O   . GLY B  497 ? 0.3779 0.4018 0.3585 0.1031  0.0326  0.0666  523 GLY B O   
19400 N N   . THR B  498 ? 0.3767 0.3860 0.3602 0.0918  0.0355  0.0603  524 THR B N   
19401 C CA  . THR B  498 ? 0.3919 0.3941 0.3777 0.0944  0.0393  0.0606  524 THR B CA  
19402 C C   . THR B  498 ? 0.3814 0.3817 0.3702 0.0887  0.0386  0.0541  524 THR B C   
19403 O O   . THR B  498 ? 0.3944 0.3909 0.3851 0.0910  0.0412  0.0535  524 THR B O   
19404 C CB  . THR B  498 ? 0.4330 0.4209 0.4178 0.0949  0.0455  0.0643  524 THR B CB  
19405 O OG1 . THR B  498 ? 0.4604 0.4424 0.4454 0.0870  0.0459  0.0612  524 THR B OG1 
19406 C CG2 . THR B  498 ? 0.4453 0.4335 0.4269 0.1015  0.0472  0.0716  524 THR B CG2 
19414 N N   . GLU B  499 ? 0.3573 0.3600 0.3467 0.0815  0.0355  0.0494  525 GLU B N   
19415 C CA  . GLU B  499 ? 0.3475 0.3483 0.3393 0.0753  0.0348  0.0435  525 GLU B CA  
19416 C C   . GLU B  499 ? 0.3444 0.3526 0.3383 0.0773  0.0327  0.0407  525 GLU B C   
19417 O O   . GLU B  499 ? 0.3472 0.3509 0.3428 0.0743  0.0342  0.0370  525 GLU B O   
19418 C CB  . GLU B  499 ? 0.3573 0.3613 0.3494 0.0680  0.0314  0.0400  525 GLU B CB  
19419 C CG  . GLU B  499 ? 0.3882 0.3842 0.3793 0.0644  0.0339  0.0417  525 GLU B CG  
19420 C CD  . GLU B  499 ? 0.4336 0.4309 0.4222 0.0683  0.0345  0.0470  525 GLU B CD  
19421 O OE1 . GLU B  499 ? 0.4333 0.4398 0.4203 0.0727  0.0316  0.0486  525 GLU B OE1 
19422 O OE2 . GLU B  499 ? 0.4550 0.4444 0.4430 0.0667  0.0378  0.0494  525 GLU B OE2 
19429 N N   . PHE B  500 ? 0.3356 0.3553 0.3292 0.0817  0.0292  0.0422  526 PHE B N   
19430 C CA  . PHE B  500 ? 0.3407 0.3692 0.3367 0.0834  0.0267  0.0396  526 PHE B CA  
19431 C C   . PHE B  500 ? 0.3593 0.3906 0.3562 0.0919  0.0286  0.0439  526 PHE B C   
19432 O O   . PHE B  500 ? 0.3547 0.3958 0.3537 0.0942  0.0261  0.0427  526 PHE B O   
19433 C CB  . PHE B  500 ? 0.3282 0.3691 0.3238 0.0810  0.0209  0.0373  526 PHE B CB  
19434 C CG  . PHE B  500 ? 0.3214 0.3603 0.3169 0.0730  0.0190  0.0331  526 PHE B CG  
19435 C CD1 . PHE B  500 ? 0.3233 0.3616 0.3211 0.0678  0.0182  0.0280  526 PHE B CD1 
19436 C CD2 . PHE B  500 ? 0.3233 0.3606 0.3165 0.0709  0.0184  0.0344  526 PHE B CD2 
19437 C CE1 . PHE B  500 ? 0.3206 0.3573 0.3183 0.0607  0.0166  0.0247  526 PHE B CE1 
19438 C CE2 . PHE B  500 ? 0.3203 0.3560 0.3139 0.0640  0.0169  0.0310  526 PHE B CE2 
19439 C CZ  . PHE B  500 ? 0.3155 0.3512 0.3114 0.0590  0.0159  0.0263  526 PHE B CZ  
19449 N N   . SER B  501 ? 0.3769 0.3993 0.3726 0.0966  0.0334  0.0489  527 SER B N   
19450 C CA  . SER B  501 ? 0.3923 0.4167 0.3888 0.1054  0.0356  0.0538  527 SER B CA  
19451 C C   . SER B  501 ? 0.3928 0.4173 0.3930 0.1075  0.0375  0.0516  527 SER B C   
19452 O O   . SER B  501 ? 0.4023 0.4341 0.4043 0.1146  0.0374  0.0550  527 SER B O   
19453 C CB  . SER B  501 ? 0.4386 0.4514 0.4329 0.1094  0.0409  0.0596  527 SER B CB  
19454 O OG  . SER B  501 ? 0.5059 0.5043 0.5001 0.1042  0.0452  0.0570  527 SER B OG  
19460 N N   . ALA B  502 ? 0.3817 0.3992 0.3832 0.1015  0.0391  0.0461  528 ALA B N   
19461 C CA  . ALA B  502 ? 0.3715 0.3889 0.3761 0.1030  0.0411  0.0435  528 ALA B CA  
19462 C C   . ALA B  502 ? 0.3601 0.3926 0.3674 0.1017  0.0357  0.0400  528 ALA B C   
19463 O O   . ALA B  502 ? 0.3642 0.4006 0.3746 0.1049  0.0368  0.0392  528 ALA B O   
19464 C CB  . ALA B  502 ? 0.3734 0.3776 0.3775 0.0969  0.0449  0.0389  528 ALA B CB  
19470 N N   . ILE B  503 ? 0.3409 0.3814 0.3470 0.0970  0.0303  0.0380  529 ILE B N   
19471 C CA  . ILE B  503 ? 0.3255 0.3800 0.3337 0.0952  0.0252  0.0348  529 ILE B CA  
19472 C C   . ILE B  503 ? 0.3139 0.3783 0.3200 0.0969  0.0207  0.0377  529 ILE B C   
19473 O O   . ILE B  503 ? 0.3002 0.3677 0.3047 0.0914  0.0171  0.0349  529 ILE B O   
19474 C CB  . ILE B  503 ? 0.3298 0.3827 0.3382 0.0862  0.0233  0.0282  529 ILE B CB  
19475 C CG1 . ILE B  503 ? 0.3461 0.3906 0.3513 0.0803  0.0232  0.0273  529 ILE B CG1 
19476 C CG2 . ILE B  503 ? 0.3313 0.3778 0.3417 0.0852  0.0272  0.0251  529 ILE B CG2 
19477 C CD1 . ILE B  503 ? 0.3696 0.4151 0.3751 0.0720  0.0205  0.0217  529 ILE B CD1 
19489 N N   . PRO B  504 ? 0.3131 0.3821 0.3191 0.1047  0.0213  0.0434  530 PRO B N   
19490 C CA  . PRO B  504 ? 0.3082 0.3857 0.3112 0.1063  0.0174  0.0463  530 PRO B CA  
19491 C C   . PRO B  504 ? 0.3048 0.3983 0.3089 0.1052  0.0116  0.0440  530 PRO B C   
19492 O O   . PRO B  504 ? 0.3108 0.4114 0.3119 0.1057  0.0083  0.0456  530 PRO B O   
19493 C CB  . PRO B  504 ? 0.3209 0.3969 0.3231 0.1151  0.0205  0.0536  530 PRO B CB  
19494 C CG  . PRO B  504 ? 0.3269 0.4015 0.3335 0.1195  0.0240  0.0541  530 PRO B CG  
19495 C CD  . PRO B  504 ? 0.3108 0.3767 0.3188 0.1125  0.0257  0.0479  530 PRO B CD  
19503 N N   . HIS B  505 ? 0.2849 0.3843 0.2931 0.1035  0.0105  0.0402  531 HIS B N   
19504 C CA  . HIS B  505 ? 0.2762 0.3909 0.2859 0.1021  0.0051  0.0379  531 HIS B CA  
19505 C C   . HIS B  505 ? 0.2640 0.3789 0.2734 0.0932  0.0023  0.0314  531 HIS B C   
19506 O O   . HIS B  505 ? 0.2703 0.3957 0.2821 0.0909  -0.0011 0.0283  531 HIS B O   
19507 C CB  . HIS B  505 ? 0.2871 0.4106 0.3019 0.1071  0.0056  0.0390  531 HIS B CB  
19508 C CG  . HIS B  505 ? 0.3429 0.4659 0.3583 0.1163  0.0087  0.0459  531 HIS B CG  
19509 N ND1 . HIS B  505 ? 0.3775 0.5081 0.3903 0.1209  0.0064  0.0508  531 HIS B ND1 
19510 C CD2 . HIS B  505 ? 0.3672 0.4820 0.3850 0.1213  0.0142  0.0485  531 HIS B CD2 
19511 C CE1 . HIS B  505 ? 0.3806 0.5079 0.3945 0.1289  0.0104  0.0567  531 HIS B CE1 
19512 N NE2 . HIS B  505 ? 0.3871 0.5044 0.4040 0.1295  0.0153  0.0556  531 HIS B NE2 
19520 N N   . VAL B  506 ? 0.2480 0.3519 0.2546 0.0883  0.0035  0.0297  532 VAL B N   
19521 C CA  . VAL B  506 ? 0.2441 0.3479 0.2502 0.0803  0.0008  0.0243  532 VAL B CA  
19522 C C   . VAL B  506 ? 0.2428 0.3574 0.2467 0.0792  -0.0041 0.0237  532 VAL B C   
19523 O O   . VAL B  506 ? 0.2508 0.3667 0.2514 0.0825  -0.0045 0.0272  532 VAL B O   
19524 C CB  . VAL B  506 ? 0.2489 0.3395 0.2527 0.0759  0.0032  0.0234  532 VAL B CB  
19525 C CG1 . VAL B  506 ? 0.2486 0.3403 0.2517 0.0684  0.0001  0.0187  532 VAL B CG1 
19526 C CG2 . VAL B  506 ? 0.2456 0.3257 0.2512 0.0757  0.0078  0.0229  532 VAL B CG2 
19536 N N   . LYS B  507 ? 0.2380 0.3608 0.2437 0.0750  -0.0074 0.0195  533 LYS B N   
19537 C CA  . LYS B  507 ? 0.2396 0.3724 0.2432 0.0731  -0.0120 0.0180  533 LYS B CA  
19538 C C   . LYS B  507 ? 0.2258 0.3537 0.2271 0.0660  -0.0133 0.0139  533 LYS B C   
19539 O O   . LYS B  507 ? 0.2294 0.3608 0.2273 0.0646  -0.0158 0.0134  533 LYS B O   
19540 C CB  . LYS B  507 ? 0.2667 0.4125 0.2741 0.0728  -0.0148 0.0158  533 LYS B CB  
19541 C CG  . LYS B  507 ? 0.3340 0.4857 0.3454 0.0795  -0.0133 0.0192  533 LYS B CG  
19542 C CD  . LYS B  507 ? 0.3807 0.5397 0.3902 0.0861  -0.0144 0.0243  533 LYS B CD  
19543 C CE  . LYS B  507 ? 0.4278 0.5932 0.4418 0.0931  -0.0128 0.0281  533 LYS B CE  
19544 N NZ  . LYS B  507 ? 0.4498 0.6303 0.4683 0.0922  -0.0162 0.0259  533 LYS B NZ  
19558 N N   . TYR B  508 ? 0.2150 0.3354 0.2182 0.0615  -0.0117 0.0111  534 TYR B N   
19559 C CA  . TYR B  508 ? 0.2203 0.3363 0.2221 0.0550  -0.0128 0.0077  534 TYR B CA  
19560 C C   . TYR B  508 ? 0.2159 0.3195 0.2176 0.0534  -0.0093 0.0084  534 TYR B C   
19561 O O   . TYR B  508 ? 0.2120 0.3117 0.2164 0.0526  -0.0073 0.0075  534 TYR B O   
19562 C CB  . TYR B  508 ? 0.2249 0.3467 0.2295 0.0501  -0.0151 0.0032  534 TYR B CB  
19563 C CG  . TYR B  508 ? 0.2440 0.3633 0.2471 0.0439  -0.0167 -0.0001 534 TYR B CG  
19564 C CD1 . TYR B  508 ? 0.2596 0.3690 0.2619 0.0407  -0.0149 -0.0003 534 TYR B CD1 
19565 C CD2 . TYR B  508 ? 0.2592 0.3864 0.2622 0.0407  -0.0199 -0.0032 534 TYR B CD2 
19566 C CE1 . TYR B  508 ? 0.2786 0.3860 0.2802 0.0354  -0.0163 -0.0030 534 TYR B CE1 
19567 C CE2 . TYR B  508 ? 0.2766 0.4008 0.2785 0.0351  -0.0210 -0.0062 534 TYR B CE2 
19568 C CZ  . TYR B  508 ? 0.2954 0.4097 0.2967 0.0328  -0.0191 -0.0058 534 TYR B CZ  
19569 O OH  . TYR B  508 ? 0.3307 0.4422 0.3312 0.0279  -0.0200 -0.0082 534 TYR B OH  
19579 N N   . LEU B  509 ? 0.2163 0.3140 0.2150 0.0530  -0.0086 0.0101  535 LEU B N   
19580 C CA  . LEU B  509 ? 0.2264 0.3131 0.2250 0.0513  -0.0055 0.0110  535 LEU B CA  
19581 C C   . LEU B  509 ? 0.2145 0.2979 0.2124 0.0455  -0.0065 0.0088  535 LEU B C   
19582 O O   . LEU B  509 ? 0.2094 0.2944 0.2047 0.0454  -0.0078 0.0092  535 LEU B O   
19583 C CB  . LEU B  509 ? 0.2321 0.3144 0.2283 0.0562  -0.0030 0.0158  535 LEU B CB  
19584 C CG  . LEU B  509 ? 0.2572 0.3283 0.2531 0.0545  0.0003  0.0173  535 LEU B CG  
19585 C CD1 . LEU B  509 ? 0.2739 0.3391 0.2725 0.0525  0.0027  0.0157  535 LEU B CD1 
19586 C CD2 . LEU B  509 ? 0.2647 0.3323 0.2582 0.0596  0.0028  0.0222  535 LEU B CD2 
19598 N N   . ASP B  510 ? 0.1986 0.2774 0.1986 0.0410  -0.0058 0.0066  536 ASP B N   
19599 C CA  . ASP B  510 ? 0.1914 0.2670 0.1912 0.0358  -0.0066 0.0050  536 ASP B CA  
19600 C C   . ASP B  510 ? 0.1930 0.2597 0.1929 0.0347  -0.0037 0.0070  536 ASP B C   
19601 O O   . ASP B  510 ? 0.1964 0.2584 0.1976 0.0337  -0.0017 0.0067  536 ASP B O   
19602 C CB  . ASP B  510 ? 0.1956 0.2740 0.1977 0.0311  -0.0083 0.0011  536 ASP B CB  
19603 C CG  . ASP B  510 ? 0.2190 0.2949 0.2213 0.0259  -0.0093 -0.0002 536 ASP B CG  
19604 O OD1 . ASP B  510 ? 0.2484 0.3188 0.2501 0.0252  -0.0079 0.0016  536 ASP B OD1 
19605 O OD2 . ASP B  510 ? 0.2252 0.3046 0.2285 0.0225  -0.0112 -0.0030 536 ASP B OD2 
19610 N N   . LEU B  511 ? 0.1956 0.2599 0.1937 0.0352  -0.0032 0.0092  537 LEU B N   
19611 C CA  . LEU B  511 ? 0.2098 0.2665 0.2082 0.0337  -0.0006 0.0113  537 LEU B CA  
19612 C C   . LEU B  511 ? 0.2085 0.2645 0.2076 0.0294  -0.0017 0.0105  537 LEU B C   
19613 O O   . LEU B  511 ? 0.2139 0.2657 0.2132 0.0287  0.0000  0.0128  537 LEU B O   
19614 C CB  . LEU B  511 ? 0.2220 0.2762 0.2182 0.0385  0.0016  0.0153  537 LEU B CB  
19615 C CG  . LEU B  511 ? 0.2497 0.3022 0.2455 0.0433  0.0037  0.0174  537 LEU B CG  
19616 C CD1 . LEU B  511 ? 0.2545 0.3067 0.2475 0.0484  0.0051  0.0216  537 LEU B CD1 
19617 C CD2 . LEU B  511 ? 0.2603 0.3047 0.2578 0.0413  0.0068  0.0174  537 LEU B CD2 
19629 N N   . THR B  512 ? 0.1996 0.2597 0.1996 0.0263  -0.0043 0.0076  538 THR B N   
19630 C CA  . THR B  512 ? 0.1974 0.2573 0.1983 0.0228  -0.0052 0.0072  538 THR B CA  
19631 C C   . THR B  512 ? 0.2068 0.2621 0.2101 0.0188  -0.0041 0.0077  538 THR B C   
19632 O O   . THR B  512 ? 0.2004 0.2532 0.2046 0.0174  -0.0032 0.0071  538 THR B O   
19633 C CB  . THR B  512 ? 0.2095 0.2743 0.2107 0.0206  -0.0079 0.0040  538 THR B CB  
19634 O OG1 . THR B  512 ? 0.2343 0.2994 0.2375 0.0175  -0.0085 0.0019  538 THR B OG1 
19635 C CG2 . THR B  512 ? 0.2096 0.2797 0.2085 0.0237  -0.0093 0.0030  538 THR B CG2 
19643 N N   . ASN B  513 ? 0.2153 0.2700 0.2196 0.0168  -0.0042 0.0089  539 ASN B N   
19644 C CA  . ASN B  513 ? 0.2191 0.2713 0.2261 0.0124  -0.0038 0.0094  539 ASN B CA  
19645 C C   . ASN B  513 ? 0.2226 0.2700 0.2302 0.0120  -0.0014 0.0111  539 ASN B C   
19646 O O   . ASN B  513 ? 0.2321 0.2776 0.2410 0.0082  -0.0013 0.0101  539 ASN B O   
19647 C CB  . ASN B  513 ? 0.2382 0.2927 0.2466 0.0085  -0.0059 0.0066  539 ASN B CB  
19648 C CG  . ASN B  513 ? 0.2924 0.3507 0.3007 0.0081  -0.0079 0.0053  539 ASN B CG  
19649 O OD1 . ASN B  513 ? 0.3288 0.3901 0.3358 0.0094  -0.0091 0.0032  539 ASN B OD1 
19650 N ND2 . ASN B  513 ? 0.2869 0.3453 0.2970 0.0063  -0.0082 0.0066  539 ASN B ND2 
19657 N N   . ASN B  514 ? 0.2151 0.2601 0.2212 0.0156  0.0007  0.0136  540 ASN B N   
19658 C CA  . ASN B  514 ? 0.2099 0.2494 0.2164 0.0153  0.0035  0.0156  540 ASN B CA  
19659 C C   . ASN B  514 ? 0.2134 0.2520 0.2208 0.0155  0.0049  0.0188  540 ASN B C   
19660 O O   . ASN B  514 ? 0.2189 0.2610 0.2275 0.0146  0.0036  0.0190  540 ASN B O   
19661 C CB  . ASN B  514 ? 0.2099 0.2470 0.2139 0.0199  0.0052  0.0161  540 ASN B CB  
19662 C CG  . ASN B  514 ? 0.2232 0.2598 0.2273 0.0189  0.0049  0.0132  540 ASN B CG  
19663 O OD1 . ASN B  514 ? 0.2276 0.2604 0.2328 0.0151  0.0059  0.0121  540 ASN B OD1 
19664 N ND2 . ASN B  514 ? 0.2231 0.2638 0.2260 0.0219  0.0035  0.0118  540 ASN B ND2 
19671 N N   . ARG B  515 ? 0.2224 0.2564 0.2297 0.0164  0.0079  0.0214  541 ARG B N   
19672 C CA  . ARG B  515 ? 0.2399 0.2733 0.2480 0.0170  0.0096  0.0248  541 ARG B CA  
19673 C C   . ARG B  515 ? 0.2338 0.2639 0.2388 0.0221  0.0124  0.0275  541 ARG B C   
19674 O O   . ARG B  515 ? 0.2412 0.2674 0.2467 0.0220  0.0153  0.0304  541 ARG B O   
19675 C CB  . ARG B  515 ? 0.2916 0.3232 0.3035 0.0116  0.0105  0.0257  541 ARG B CB  
19676 C CG  . ARG B  515 ? 0.3878 0.4158 0.4005 0.0075  0.0108  0.0237  541 ARG B CG  
19677 C CD  . ARG B  515 ? 0.4631 0.4895 0.4790 0.0022  0.0119  0.0250  541 ARG B CD  
19678 N NE  . ARG B  515 ? 0.5345 0.5666 0.5539 -0.0015 0.0093  0.0247  541 ARG B NE  
19679 C CZ  . ARG B  515 ? 0.5811 0.6145 0.6042 -0.0060 0.0096  0.0263  541 ARG B CZ  
19680 N NH1 . ARG B  515 ? 0.5890 0.6181 0.6129 -0.0077 0.0125  0.0280  541 ARG B NH1 
19681 N NH2 . ARG B  515 ? 0.5687 0.6080 0.5950 -0.0087 0.0071  0.0265  541 ARG B NH2 
19695 N N   . LEU B  516 ? 0.2242 0.2562 0.2261 0.0264  0.0115  0.0267  542 LEU B N   
19696 C CA  . LEU B  516 ? 0.2267 0.2563 0.2254 0.0316  0.0137  0.0294  542 LEU B CA  
19697 C C   . LEU B  516 ? 0.2235 0.2528 0.2208 0.0340  0.0157  0.0331  542 LEU B C   
19698 O O   . LEU B  516 ? 0.2209 0.2540 0.2182 0.0336  0.0146  0.0330  542 LEU B O   
19699 C CB  . LEU B  516 ? 0.2363 0.2702 0.2323 0.0357  0.0117  0.0279  542 LEU B CB  
19700 C CG  . LEU B  516 ? 0.2677 0.3008 0.2649 0.0346  0.0110  0.0252  542 LEU B CG  
19701 C CD1 . LEU B  516 ? 0.2701 0.3094 0.2656 0.0375  0.0083  0.0232  542 LEU B CD1 
19702 C CD2 . LEU B  516 ? 0.2858 0.3117 0.2826 0.0363  0.0146  0.0272  542 LEU B CD2 
19714 N N   . ASP B  517 ? 0.2190 0.2432 0.2152 0.0362  0.0190  0.0365  543 ASP B N   
19715 C CA  . ASP B  517 ? 0.2264 0.2496 0.2212 0.0384  0.0216  0.0405  543 ASP B CA  
19716 C C   . ASP B  517 ? 0.2479 0.2726 0.2379 0.0448  0.0219  0.0425  543 ASP B C   
19717 O O   . ASP B  517 ? 0.2580 0.2784 0.2466 0.0476  0.0241  0.0447  543 ASP B O   
19718 C CB  . ASP B  517 ? 0.2294 0.2456 0.2264 0.0359  0.0253  0.0430  543 ASP B CB  
19719 C CG  . ASP B  517 ? 0.2938 0.3086 0.2900 0.0375  0.0284  0.0474  543 ASP B CG  
19720 O OD1 . ASP B  517 ? 0.3096 0.3288 0.3031 0.0407  0.0279  0.0484  543 ASP B OD1 
19721 O OD2 . ASP B  517 ? 0.3103 0.3193 0.3083 0.0354  0.0317  0.0497  543 ASP B OD2 
19726 N N   . PHE B  518 ? 0.2530 0.2839 0.2402 0.0471  0.0197  0.0416  544 PHE B N   
19727 C CA  . PHE B  518 ? 0.2663 0.3001 0.2485 0.0529  0.0195  0.0434  544 PHE B CA  
19728 C C   . PHE B  518 ? 0.2786 0.3096 0.2582 0.0557  0.0230  0.0483  544 PHE B C   
19729 O O   . PHE B  518 ? 0.2853 0.3190 0.2629 0.0562  0.0233  0.0489  544 PHE B O   
19730 C CB  . PHE B  518 ? 0.2647 0.3060 0.2445 0.0534  0.0159  0.0402  544 PHE B CB  
19731 C CG  . PHE B  518 ? 0.2731 0.3171 0.2554 0.0508  0.0127  0.0357  544 PHE B CG  
19732 C CD1 . PHE B  518 ? 0.2816 0.3274 0.2632 0.0533  0.0115  0.0352  544 PHE B CD1 
19733 C CD2 . PHE B  518 ? 0.2802 0.3247 0.2659 0.0459  0.0112  0.0326  544 PHE B CD2 
19734 C CE1 . PHE B  518 ? 0.2882 0.3365 0.2723 0.0508  0.0088  0.0312  544 PHE B CE1 
19735 C CE2 . PHE B  518 ? 0.2891 0.3360 0.2768 0.0434  0.0084  0.0287  544 PHE B CE2 
19736 C CZ  . PHE B  518 ? 0.2860 0.3348 0.2728 0.0458  0.0073  0.0280  544 PHE B CZ  
19746 N N   . ASP B  519 ? 0.2744 0.2992 0.2541 0.0574  0.0262  0.0517  545 ASP B N   
19747 C CA  . ASP B  519 ? 0.2809 0.3020 0.2586 0.0598  0.0302  0.0568  545 ASP B CA  
19748 C C   . ASP B  519 ? 0.2907 0.3093 0.2648 0.0655  0.0321  0.0609  545 ASP B C   
19749 O O   . ASP B  519 ? 0.2857 0.2982 0.2594 0.0667  0.0362  0.0652  545 ASP B O   
19750 C CB  . ASP B  519 ? 0.2861 0.3006 0.2684 0.0549  0.0332  0.0577  545 ASP B CB  
19751 C CG  . ASP B  519 ? 0.3342 0.3460 0.3154 0.0558  0.0371  0.0624  545 ASP B CG  
19752 O OD1 . ASP B  519 ? 0.3576 0.3739 0.3352 0.0585  0.0368  0.0636  545 ASP B OD1 
19753 O OD2 . ASP B  519 ? 0.3336 0.3385 0.3172 0.0537  0.0406  0.0648  545 ASP B OD2 
19758 N N   . ASN B  520 ? 0.3025 0.3260 0.2744 0.0692  0.0294  0.0598  546 ASN B N   
19759 C CA  . ASN B  520 ? 0.3265 0.3488 0.2954 0.0753  0.0310  0.0641  546 ASN B CA  
19760 C C   . ASN B  520 ? 0.3292 0.3611 0.2944 0.0793  0.0271  0.0631  546 ASN B C   
19761 O O   . ASN B  520 ? 0.3292 0.3656 0.2963 0.0776  0.0236  0.0587  546 ASN B O   
19762 C CB  . ASN B  520 ? 0.3711 0.3862 0.3433 0.0750  0.0331  0.0643  546 ASN B CB  
19763 C CG  . ASN B  520 ? 0.4563 0.4687 0.4258 0.0815  0.0357  0.0696  546 ASN B CG  
19764 O OD1 . ASN B  520 ? 0.4612 0.4797 0.4290 0.0860  0.0334  0.0699  546 ASN B OD1 
19765 N ND2 . ASN B  520 ? 0.5348 0.5384 0.5042 0.0823  0.0405  0.0740  546 ASN B ND2 
19772 N N   . ALA B  521 ? 0.3354 0.3708 0.2952 0.0844  0.0276  0.0672  547 ALA B N   
19773 C CA  . ALA B  521 ? 0.3387 0.3842 0.2944 0.0880  0.0238  0.0665  547 ALA B CA  
19774 C C   . ALA B  521 ? 0.3400 0.3887 0.2974 0.0912  0.0219  0.0663  547 ALA B C   
19775 O O   . ALA B  521 ? 0.3388 0.3970 0.2941 0.0929  0.0180  0.0645  547 ALA B O   
19776 C CB  . ALA B  521 ? 0.3415 0.3894 0.2908 0.0929  0.0251  0.0716  547 ALA B CB  
19782 N N   . SER B  522 ? 0.3395 0.3808 0.3005 0.0920  0.0248  0.0681  548 SER B N   
19783 C CA  . SER B  522 ? 0.3429 0.3866 0.3060 0.0954  0.0238  0.0682  548 SER B CA  
19784 C C   . SER B  522 ? 0.3309 0.3741 0.2991 0.0905  0.0220  0.0622  548 SER B C   
19785 O O   . SER B  522 ? 0.3266 0.3708 0.2972 0.0928  0.0218  0.0620  548 SER B O   
19786 C CB  . SER B  522 ? 0.3787 0.4140 0.3422 0.0999  0.0286  0.0738  548 SER B CB  
19787 O OG  . SER B  522 ? 0.4250 0.4596 0.3838 0.1041  0.0308  0.0798  548 SER B OG  
19793 N N   . ALA B  523 ? 0.3155 0.3573 0.2855 0.0841  0.0209  0.0577  549 ALA B N   
19794 C CA  . ALA B  523 ? 0.3029 0.3443 0.2774 0.0792  0.0192  0.0524  549 ALA B CA  
19795 C C   . ALA B  523 ? 0.2820 0.3328 0.2571 0.0808  0.0153  0.0496  549 ALA B C   
19796 O O   . ALA B  523 ? 0.2727 0.3323 0.2448 0.0824  0.0121  0.0492  549 ALA B O   
19797 C CB  . ALA B  523 ? 0.3032 0.3444 0.2787 0.0729  0.0178  0.0486  549 ALA B CB  
19803 N N   . LEU B  524 ? 0.2699 0.3188 0.2488 0.0804  0.0157  0.0477  550 LEU B N   
19804 C CA  . LEU B  524 ? 0.2757 0.3334 0.2562 0.0812  0.0122  0.0448  550 LEU B CA  
19805 C C   . LEU B  524 ? 0.2888 0.3552 0.2673 0.0880  0.0108  0.0482  550 LEU B C   
19806 O O   . LEU B  524 ? 0.2899 0.3642 0.2704 0.0888  0.0082  0.0461  550 LEU B O   
19807 C CB  . LEU B  524 ? 0.2727 0.3366 0.2534 0.0758  0.0081  0.0395  550 LEU B CB  
19808 C CG  . LEU B  524 ? 0.2931 0.3505 0.2762 0.0690  0.0088  0.0360  550 LEU B CG  
19809 C CD1 . LEU B  524 ? 0.2909 0.3543 0.2739 0.0647  0.0050  0.0317  550 LEU B CD1 
19810 C CD2 . LEU B  524 ? 0.3019 0.3547 0.2889 0.0672  0.0102  0.0340  550 LEU B CD2 
19822 N N   . THR B  525 ? 0.2992 0.3646 0.2740 0.0929  0.0127  0.0537  551 THR B N   
19823 C CA  . THR B  525 ? 0.3122 0.3866 0.2847 0.0996  0.0112  0.0577  551 THR B CA  
19824 C C   . THR B  525 ? 0.3197 0.3950 0.2957 0.1045  0.0125  0.0599  551 THR B C   
19825 O O   . THR B  525 ? 0.3260 0.4116 0.3014 0.1094  0.0102  0.0621  551 THR B O   
19826 C CB  . THR B  525 ? 0.3327 0.4049 0.3002 0.1034  0.0133  0.0635  551 THR B CB  
19827 O OG1 . THR B  525 ? 0.3513 0.4110 0.3198 0.1046  0.0187  0.0671  551 THR B OG1 
19828 C CG2 . THR B  525 ? 0.3396 0.4131 0.3031 0.0992  0.0117  0.0613  551 THR B CG2 
19836 N N   . GLU B  526 ? 0.3175 0.3826 0.2972 0.1033  0.0163  0.0591  552 GLU B N   
19837 C CA  . GLU B  526 ? 0.3160 0.3810 0.2993 0.1076  0.0180  0.0604  552 GLU B CA  
19838 C C   . GLU B  526 ? 0.3108 0.3871 0.2974 0.1060  0.0137  0.0557  552 GLU B C   
19839 O O   . GLU B  526 ? 0.3170 0.3976 0.3064 0.1107  0.0142  0.0572  552 GLU B O   
19840 C CB  . GLU B  526 ? 0.3310 0.3816 0.3168 0.1059  0.0233  0.0598  552 GLU B CB  
19841 C CG  . GLU B  526 ? 0.3362 0.3826 0.3246 0.0978  0.0226  0.0531  552 GLU B CG  
19842 C CD  . GLU B  526 ? 0.3765 0.4172 0.3629 0.0916  0.0226  0.0513  552 GLU B CD  
19843 O OE1 . GLU B  526 ? 0.3943 0.4395 0.3776 0.0920  0.0208  0.0531  552 GLU B OE1 
19844 O OE2 . GLU B  526 ? 0.3788 0.4110 0.3670 0.0863  0.0246  0.0483  552 GLU B OE2 
19851 N N   . LEU B  527 ? 0.2973 0.3780 0.2836 0.0995  0.0100  0.0502  553 LEU B N   
19852 C CA  . LEU B  527 ? 0.2931 0.3840 0.2821 0.0971  0.0059  0.0457  553 LEU B CA  
19853 C C   . LEU B  527 ? 0.3055 0.4104 0.2921 0.0999  0.0016  0.0469  553 LEU B C   
19854 O O   . LEU B  527 ? 0.3042 0.4147 0.2889 0.0955  -0.0021 0.0433  553 LEU B O   
19855 C CB  . LEU B  527 ? 0.2875 0.3754 0.2772 0.0888  0.0044  0.0395  553 LEU B CB  
19856 C CG  . LEU B  527 ? 0.2941 0.3697 0.2862 0.0851  0.0081  0.0376  553 LEU B CG  
19857 C CD1 . LEU B  527 ? 0.2926 0.3670 0.2853 0.0772  0.0060  0.0321  553 LEU B CD1 
19858 C CD2 . LEU B  527 ? 0.2974 0.3723 0.2934 0.0876  0.0101  0.0373  553 LEU B CD2 
19870 N N   . SER B  528 ? 0.3150 0.4259 0.3020 0.1072  0.0019  0.0519  554 SER B N   
19871 C CA  . SER B  528 ? 0.3178 0.4428 0.3023 0.1104  -0.0022 0.0539  554 SER B CA  
19872 C C   . SER B  528 ? 0.2989 0.4367 0.2855 0.1065  -0.0073 0.0487  554 SER B C   
19873 O O   . SER B  528 ? 0.3018 0.4493 0.2848 0.1057  -0.0113 0.0480  554 SER B O   
19874 C CB  . SER B  528 ? 0.3485 0.4774 0.3338 0.1194  -0.0005 0.0609  554 SER B CB  
19875 O OG  . SER B  528 ? 0.3949 0.5306 0.3859 0.1221  -0.0009 0.0606  554 SER B OG  
19881 N N   . ASP B  529 ? 0.2807 0.4183 0.2725 0.1038  -0.0071 0.0448  555 ASP B N   
19882 C CA  . ASP B  529 ? 0.2715 0.4206 0.2656 0.0998  -0.0115 0.0399  555 ASP B CA  
19883 C C   . ASP B  529 ? 0.2487 0.3933 0.2417 0.0912  -0.0130 0.0336  555 ASP B C   
19884 O O   . ASP B  529 ? 0.2423 0.3939 0.2377 0.0870  -0.0158 0.0291  555 ASP B O   
19885 C CB  . ASP B  529 ? 0.3049 0.4573 0.3055 0.1017  -0.0104 0.0394  555 ASP B CB  
19886 C CG  . ASP B  529 ? 0.4011 0.5601 0.4039 0.1105  -0.0093 0.0455  555 ASP B CG  
19887 O OD1 . ASP B  529 ? 0.4103 0.5756 0.4096 0.1146  -0.0109 0.0498  555 ASP B OD1 
19888 O OD2 . ASP B  529 ? 0.4587 0.6170 0.4667 0.1133  -0.0068 0.0461  555 ASP B OD2 
19893 N N   . LEU B  530 ? 0.2436 0.3770 0.2333 0.0886  -0.0109 0.0334  556 LEU B N   
19894 C CA  . LEU B  530 ? 0.2381 0.3667 0.2272 0.0810  -0.0119 0.0281  556 LEU B CA  
19895 C C   . LEU B  530 ? 0.2362 0.3749 0.2229 0.0775  -0.0165 0.0246  556 LEU B C   
19896 O O   . LEU B  530 ? 0.2301 0.3739 0.2122 0.0798  -0.0181 0.0266  556 LEU B O   
19897 C CB  . LEU B  530 ? 0.2402 0.3567 0.2263 0.0797  -0.0089 0.0295  556 LEU B CB  
19898 C CG  . LEU B  530 ? 0.2565 0.3659 0.2432 0.0725  -0.0088 0.0249  556 LEU B CG  
19899 C CD1 . LEU B  530 ? 0.2565 0.3624 0.2481 0.0699  -0.0076 0.0222  556 LEU B CD1 
19900 C CD2 . LEU B  530 ? 0.2643 0.3633 0.2484 0.0721  -0.0058 0.0271  556 LEU B CD2 
19912 N N   . GLU B  531 ? 0.2300 0.3712 0.2193 0.0720  -0.0184 0.0193  557 GLU B N   
19913 C CA  . GLU B  531 ? 0.2356 0.3849 0.2230 0.0676  -0.0224 0.0152  557 GLU B CA  
19914 C C   . GLU B  531 ? 0.2348 0.3763 0.2207 0.0611  -0.0222 0.0111  557 GLU B C   
19915 O O   . GLU B  531 ? 0.2355 0.3797 0.2175 0.0584  -0.0243 0.0088  557 GLU B O   
19916 C CB  . GLU B  531 ? 0.2562 0.4162 0.2480 0.0664  -0.0250 0.0126  557 GLU B CB  
19917 C CG  . GLU B  531 ? 0.2869 0.4578 0.2799 0.0728  -0.0261 0.0166  557 GLU B CG  
19918 C CD  . GLU B  531 ? 0.3622 0.5468 0.3590 0.0714  -0.0295 0.0141  557 GLU B CD  
19919 O OE1 . GLU B  531 ? 0.3820 0.5695 0.3786 0.0651  -0.0319 0.0090  557 GLU B OE1 
19920 O OE2 . GLU B  531 ? 0.4020 0.5947 0.4022 0.0767  -0.0296 0.0174  557 GLU B OE2 
19927 N N   . VAL B  532 ? 0.2254 0.3579 0.2143 0.0585  -0.0199 0.0101  558 VAL B N   
19928 C CA  . VAL B  532 ? 0.2232 0.3488 0.2115 0.0527  -0.0196 0.0067  558 VAL B CA  
19929 C C   . VAL B  532 ? 0.2225 0.3366 0.2112 0.0532  -0.0160 0.0091  558 VAL B C   
19930 O O   . VAL B  532 ? 0.2245 0.3349 0.2161 0.0548  -0.0138 0.0106  558 VAL B O   
19931 C CB  . VAL B  532 ? 0.2236 0.3515 0.2158 0.0476  -0.0210 0.0023  558 VAL B CB  
19932 C CG1 . VAL B  532 ? 0.2255 0.3459 0.2171 0.0420  -0.0206 -0.0004 558 VAL B CG1 
19933 C CG2 . VAL B  532 ? 0.2131 0.3529 0.2055 0.0468  -0.0245 -0.0001 558 VAL B CG2 
19943 N N   . LEU B  533 ? 0.2167 0.3251 0.2023 0.0516  -0.0151 0.0094  559 LEU B N   
19944 C CA  . LEU B  533 ? 0.2221 0.3202 0.2081 0.0513  -0.0119 0.0116  559 LEU B CA  
19945 C C   . LEU B  533 ? 0.2225 0.3162 0.2086 0.0460  -0.0120 0.0089  559 LEU B C   
19946 O O   . LEU B  533 ? 0.2267 0.3222 0.2097 0.0450  -0.0132 0.0078  559 LEU B O   
19947 C CB  . LEU B  533 ? 0.2286 0.3247 0.2109 0.0560  -0.0101 0.0161  559 LEU B CB  
19948 C CG  . LEU B  533 ? 0.2539 0.3399 0.2365 0.0559  -0.0065 0.0188  559 LEU B CG  
19949 C CD1 . LEU B  533 ? 0.2588 0.3389 0.2455 0.0552  -0.0043 0.0191  559 LEU B CD1 
19950 C CD2 . LEU B  533 ? 0.2694 0.3541 0.2481 0.0609  -0.0046 0.0235  559 LEU B CD2 
19962 N N   . ASP B  534 ? 0.2040 0.2919 0.1934 0.0426  -0.0108 0.0080  560 ASP B N   
19963 C CA  . ASP B  534 ? 0.1952 0.2792 0.1854 0.0378  -0.0109 0.0060  560 ASP B CA  
19964 C C   . ASP B  534 ? 0.2034 0.2793 0.1942 0.0375  -0.0080 0.0088  560 ASP B C   
19965 O O   . ASP B  534 ? 0.2088 0.2804 0.2020 0.0367  -0.0064 0.0095  560 ASP B O   
19966 C CB  . ASP B  534 ? 0.2070 0.2923 0.2004 0.0334  -0.0123 0.0025  560 ASP B CB  
19967 C CG  . ASP B  534 ? 0.2314 0.3154 0.2251 0.0288  -0.0133 0.0002  560 ASP B CG  
19968 O OD1 . ASP B  534 ? 0.2323 0.3128 0.2243 0.0288  -0.0123 0.0014  560 ASP B OD1 
19969 O OD2 . ASP B  534 ? 0.2304 0.3164 0.2260 0.0253  -0.0148 -0.0027 560 ASP B OD2 
19974 N N   . LEU B  535 ? 0.2030 0.2769 0.1914 0.0381  -0.0071 0.0103  561 LEU B N   
19975 C CA  . LEU B  535 ? 0.2068 0.2740 0.1961 0.0376  -0.0043 0.0131  561 LEU B CA  
19976 C C   . LEU B  535 ? 0.2054 0.2706 0.1963 0.0334  -0.0046 0.0118  561 LEU B C   
19977 O O   . LEU B  535 ? 0.2141 0.2755 0.2054 0.0332  -0.0025 0.0141  561 LEU B O   
19978 C CB  . LEU B  535 ? 0.2124 0.2789 0.1981 0.0419  -0.0026 0.0166  561 LEU B CB  
19979 C CG  . LEU B  535 ? 0.2371 0.3061 0.2208 0.0469  -0.0023 0.0188  561 LEU B CG  
19980 C CD1 . LEU B  535 ? 0.2413 0.3093 0.2209 0.0509  -0.0004 0.0226  561 LEU B CD1 
19981 C CD2 . LEU B  535 ? 0.2510 0.3158 0.2377 0.0473  -0.0005 0.0200  561 LEU B CD2 
19993 N N   . SER B  536 ? 0.2018 0.2697 0.1938 0.0302  -0.0068 0.0084  562 SER B N   
19994 C CA  . SER B  536 ? 0.2073 0.2736 0.2009 0.0266  -0.0070 0.0074  562 SER B CA  
19995 C C   . SER B  536 ? 0.2070 0.2687 0.2042 0.0241  -0.0055 0.0092  562 SER B C   
19996 O O   . SER B  536 ? 0.2082 0.2683 0.2070 0.0234  -0.0050 0.0095  562 SER B O   
19997 C CB  . SER B  536 ? 0.2328 0.3021 0.2275 0.0234  -0.0094 0.0037  562 SER B CB  
19998 O OG  . SER B  536 ? 0.2821 0.3562 0.2738 0.0249  -0.0111 0.0015  562 SER B OG  
20004 N N   . TYR B  537 ? 0.2064 0.2664 0.2048 0.0226  -0.0046 0.0103  563 TYR B N   
20005 C CA  . TYR B  537 ? 0.2169 0.2740 0.2192 0.0197  -0.0036 0.0121  563 TYR B CA  
20006 C C   . TYR B  537 ? 0.2112 0.2649 0.2140 0.0207  -0.0014 0.0148  563 TYR B C   
20007 O O   . TYR B  537 ? 0.2098 0.2617 0.2149 0.0180  -0.0013 0.0147  563 TYR B O   
20008 C CB  . TYR B  537 ? 0.2332 0.2912 0.2381 0.0155  -0.0055 0.0099  563 TYR B CB  
20009 C CG  . TYR B  537 ? 0.2574 0.3177 0.2623 0.0141  -0.0071 0.0078  563 TYR B CG  
20010 C CD1 . TYR B  537 ? 0.2758 0.3353 0.2828 0.0126  -0.0067 0.0090  563 TYR B CD1 
20011 C CD2 . TYR B  537 ? 0.2764 0.3396 0.2796 0.0141  -0.0089 0.0047  563 TYR B CD2 
20012 C CE1 . TYR B  537 ? 0.2971 0.3577 0.3042 0.0113  -0.0078 0.0072  563 TYR B CE1 
20013 C CE2 . TYR B  537 ? 0.2958 0.3602 0.2989 0.0123  -0.0102 0.0026  563 TYR B CE2 
20014 C CZ  . TYR B  537 ? 0.3189 0.3815 0.3238 0.0110  -0.0095 0.0039  563 TYR B CZ  
20015 O OH  . TYR B  537 ? 0.3739 0.4368 0.3787 0.0094  -0.0102 0.0020  563 TYR B OH  
20025 N N   . ASN B  538 ? 0.1990 0.2517 0.1994 0.0244  0.0005  0.0171  564 ASN B N   
20026 C CA  . ASN B  538 ? 0.2022 0.2511 0.2030 0.0255  0.0031  0.0203  564 ASN B CA  
20027 C C   . ASN B  538 ? 0.2067 0.2548 0.2074 0.0266  0.0052  0.0231  564 ASN B C   
20028 O O   . ASN B  538 ? 0.2220 0.2685 0.2204 0.0299  0.0073  0.0257  564 ASN B O   
20029 C CB  . ASN B  538 ? 0.2012 0.2497 0.1987 0.0296  0.0037  0.0209  564 ASN B CB  
20030 C CG  . ASN B  538 ? 0.1995 0.2473 0.1981 0.0285  0.0030  0.0190  564 ASN B CG  
20031 O OD1 . ASN B  538 ? 0.1971 0.2407 0.1976 0.0264  0.0044  0.0197  564 ASN B OD1 
20032 N ND2 . ASN B  538 ? 0.2055 0.2574 0.2028 0.0297  0.0008  0.0165  564 ASN B ND2 
20039 N N   . SER B  539 ? 0.1995 0.2489 0.2029 0.0242  0.0047  0.0229  565 SER B N   
20040 C CA  . SER B  539 ? 0.2122 0.2615 0.2159 0.0254  0.0068  0.0254  565 SER B CA  
20041 C C   . SER B  539 ? 0.2165 0.2634 0.2233 0.0243  0.0094  0.0290  565 SER B C   
20042 O O   . SER B  539 ? 0.2189 0.2657 0.2256 0.0260  0.0117  0.0315  565 SER B O   
20043 C CB  . SER B  539 ? 0.2336 0.2851 0.2398 0.0234  0.0058  0.0243  565 SER B CB  
20044 O OG  . SER B  539 ? 0.2798 0.3315 0.2910 0.0191  0.0048  0.0246  565 SER B OG  
20050 N N   . HIS B  540 ? 0.2156 0.2605 0.2250 0.0212  0.0093  0.0291  566 HIS B N   
20051 C CA  . HIS B  540 ? 0.2208 0.2634 0.2336 0.0188  0.0115  0.0320  566 HIS B CA  
20052 C C   . HIS B  540 ? 0.2211 0.2620 0.2325 0.0220  0.0149  0.0356  566 HIS B C   
20053 O O   . HIS B  540 ? 0.2172 0.2593 0.2319 0.0208  0.0165  0.0381  566 HIS B O   
20054 C CB  . HIS B  540 ? 0.2344 0.2736 0.2480 0.0159  0.0115  0.0312  566 HIS B CB  
20055 C CG  . HIS B  540 ? 0.2699 0.3072 0.2874 0.0122  0.0135  0.0335  566 HIS B CG  
20056 N ND1 . HIS B  540 ? 0.2916 0.3302 0.3129 0.0067  0.0119  0.0324  566 HIS B ND1 
20057 C CD2 . HIS B  540 ? 0.2849 0.3194 0.3028 0.0129  0.0167  0.0368  566 HIS B CD2 
20058 C CE1 . HIS B  540 ? 0.2983 0.3353 0.3224 0.0041  0.0141  0.0349  566 HIS B CE1 
20059 N NE2 . HIS B  540 ? 0.2998 0.3341 0.3221 0.0076  0.0172  0.0376  566 HIS B NE2 
20067 N N   . TYR B  541 ? 0.2249 0.2634 0.2317 0.0259  0.0161  0.0363  567 TYR B N   
20068 C CA  . TYR B  541 ? 0.2295 0.2661 0.2345 0.0290  0.0195  0.0400  567 TYR B CA  
20069 C C   . TYR B  541 ? 0.2367 0.2762 0.2380 0.0330  0.0198  0.0403  567 TYR B C   
20070 O O   . TYR B  541 ? 0.2348 0.2740 0.2359 0.0344  0.0227  0.0433  567 TYR B O   
20071 C CB  . TYR B  541 ? 0.2320 0.2640 0.2341 0.0312  0.0211  0.0413  567 TYR B CB  
20072 C CG  . TYR B  541 ? 0.2380 0.2655 0.2437 0.0270  0.0224  0.0419  567 TYR B CG  
20073 C CD1 . TYR B  541 ? 0.2424 0.2679 0.2512 0.0247  0.0253  0.0449  567 TYR B CD1 
20074 C CD2 . TYR B  541 ? 0.2399 0.2659 0.2464 0.0246  0.0206  0.0389  567 TYR B CD2 
20075 C CE1 . TYR B  541 ? 0.2524 0.2740 0.2645 0.0199  0.0263  0.0449  567 TYR B CE1 
20076 C CE2 . TYR B  541 ? 0.2517 0.2733 0.2609 0.0202  0.0218  0.0388  567 TYR B CE2 
20077 C CZ  . TYR B  541 ? 0.2653 0.2848 0.2773 0.0177  0.0246  0.0417  567 TYR B CZ  
20078 O OH  . TYR B  541 ? 0.2790 0.2945 0.2937 0.0124  0.0255  0.0411  567 TYR B OH  
20088 N N   . PHE B  542 ? 0.2326 0.2749 0.2308 0.0344  0.0171  0.0370  568 PHE B N   
20089 C CA  . PHE B  542 ? 0.2336 0.2784 0.2278 0.0376  0.0174  0.0366  568 PHE B CA  
20090 C C   . PHE B  542 ? 0.2310 0.2771 0.2286 0.0362  0.0189  0.0376  568 PHE B C   
20091 O O   . PHE B  542 ? 0.2258 0.2725 0.2206 0.0390  0.0210  0.0388  568 PHE B O   
20092 C CB  . PHE B  542 ? 0.2247 0.2725 0.2160 0.0381  0.0141  0.0324  568 PHE B CB  
20093 C CG  . PHE B  542 ? 0.2311 0.2796 0.2179 0.0409  0.0128  0.0317  568 PHE B CG  
20094 C CD1 . PHE B  542 ? 0.2375 0.2862 0.2192 0.0452  0.0144  0.0340  568 PHE B CD1 
20095 C CD2 . PHE B  542 ? 0.2389 0.2885 0.2267 0.0395  0.0100  0.0289  568 PHE B CD2 
20096 C CE1 . PHE B  542 ? 0.2515 0.3019 0.2295 0.0482  0.0130  0.0337  568 PHE B CE1 
20097 C CE2 . PHE B  542 ? 0.2536 0.3049 0.2379 0.0424  0.0088  0.0284  568 PHE B CE2 
20098 C CZ  . PHE B  542 ? 0.2512 0.3031 0.2309 0.0468  0.0102  0.0310  568 PHE B CZ  
20108 N N   . ARG B  543 ? 0.2384 0.2851 0.2419 0.0321  0.0178  0.0371  569 ARG B N   
20109 C CA  . ARG B  543 ? 0.2552 0.3038 0.2627 0.0311  0.0191  0.0383  569 ARG B CA  
20110 C C   . ARG B  543 ? 0.2515 0.2995 0.2618 0.0312  0.0228  0.0428  569 ARG B C   
20111 O O   . ARG B  543 ? 0.2644 0.3143 0.2773 0.0317  0.0245  0.0443  569 ARG B O   
20112 C CB  . ARG B  543 ? 0.2873 0.3378 0.3000 0.0271  0.0166  0.0368  569 ARG B CB  
20113 C CG  . ARG B  543 ? 0.3553 0.4054 0.3728 0.0229  0.0160  0.0380  569 ARG B CG  
20114 C CD  . ARG B  543 ? 0.4155 0.4674 0.4356 0.0194  0.0127  0.0354  569 ARG B CD  
20115 N NE  . ARG B  543 ? 0.4756 0.5276 0.5000 0.0148  0.0120  0.0362  569 ARG B NE  
20116 C CZ  . ARG B  543 ? 0.5088 0.5611 0.5341 0.0115  0.0092  0.0338  569 ARG B CZ  
20117 N NH1 . ARG B  543 ? 0.5151 0.5679 0.5378 0.0122  0.0069  0.0306  569 ARG B NH1 
20118 N NH2 . ARG B  543 ? 0.4922 0.5443 0.5207 0.0071  0.0089  0.0345  569 ARG B NH2 
20132 N N   . ILE B  544 ? 0.2309 0.2761 0.2406 0.0312  0.0243  0.0449  570 ILE B N   
20133 C CA  . ILE B  544 ? 0.2318 0.2761 0.2441 0.0310  0.0279  0.0492  570 ILE B CA  
20134 C C   . ILE B  544 ? 0.2277 0.2709 0.2340 0.0359  0.0308  0.0510  570 ILE B C   
20135 O O   . ILE B  544 ? 0.2188 0.2595 0.2201 0.0383  0.0307  0.0510  570 ILE B O   
20136 C CB  . ILE B  544 ? 0.2396 0.2805 0.2542 0.0278  0.0283  0.0504  570 ILE B CB  
20137 C CG1 . ILE B  544 ? 0.2439 0.2857 0.2626 0.0229  0.0250  0.0477  570 ILE B CG1 
20138 C CG2 . ILE B  544 ? 0.2450 0.2855 0.2635 0.0264  0.0321  0.0548  570 ILE B CG2 
20139 C CD1 . ILE B  544 ? 0.2581 0.2954 0.2769 0.0203  0.0252  0.0475  570 ILE B CD1 
20151 N N   . ALA B  545 ? 0.2300 0.2753 0.2369 0.0376  0.0334  0.0529  571 ALA B N   
20152 C CA  . ALA B  545 ? 0.2386 0.2831 0.2392 0.0422  0.0363  0.0546  571 ALA B CA  
20153 C C   . ALA B  545 ? 0.2515 0.2927 0.2508 0.0431  0.0391  0.0585  571 ALA B C   
20154 O O   . ALA B  545 ? 0.2488 0.2885 0.2413 0.0469  0.0399  0.0592  571 ALA B O   
20155 C CB  . ALA B  545 ? 0.2368 0.2838 0.2388 0.0437  0.0392  0.0558  571 ALA B CB  
20161 N N   . GLY B  546 ? 0.2548 0.2951 0.2603 0.0395  0.0407  0.0611  572 GLY B N   
20162 C CA  . GLY B  546 ? 0.2560 0.2926 0.2612 0.0396  0.0441  0.0651  572 GLY B CA  
20163 C C   . GLY B  546 ? 0.2553 0.2870 0.2573 0.0401  0.0433  0.0650  572 GLY B C   
20164 O O   . GLY B  546 ? 0.2579 0.2858 0.2585 0.0411  0.0466  0.0686  572 GLY B O   
20168 N N   . VAL B  547 ? 0.2445 0.2760 0.2457 0.0393  0.0394  0.0612  573 VAL B N   
20169 C CA  . VAL B  547 ? 0.2426 0.2697 0.2407 0.0404  0.0388  0.0610  573 VAL B CA  
20170 C C   . VAL B  547 ? 0.2472 0.2756 0.2378 0.0459  0.0377  0.0603  573 VAL B C   
20171 O O   . VAL B  547 ? 0.2462 0.2789 0.2343 0.0476  0.0364  0.0585  573 VAL B O   
20172 C CB  . VAL B  547 ? 0.2422 0.2681 0.2438 0.0362  0.0358  0.0576  573 VAL B CB  
20173 C CG1 . VAL B  547 ? 0.2473 0.2734 0.2561 0.0304  0.0364  0.0581  573 VAL B CG1 
20174 C CG2 . VAL B  547 ? 0.2460 0.2760 0.2463 0.0367  0.0315  0.0532  573 VAL B CG2 
20184 N N   . THR B  548 ? 0.2440 0.2688 0.2308 0.0488  0.0386  0.0622  574 THR B N   
20185 C CA  . THR B  548 ? 0.2472 0.2742 0.2269 0.0541  0.0373  0.0620  574 THR B CA  
20186 C C   . THR B  548 ? 0.2466 0.2765 0.2259 0.0538  0.0328  0.0573  574 THR B C   
20187 O O   . THR B  548 ? 0.2499 0.2779 0.2335 0.0503  0.0313  0.0552  574 THR B O   
20188 C CB  . THR B  548 ? 0.2605 0.2833 0.2367 0.0578  0.0403  0.0666  574 THR B CB  
20189 O OG1 . THR B  548 ? 0.2688 0.2860 0.2486 0.0554  0.0409  0.0668  574 THR B OG1 
20190 C CG2 . THR B  548 ? 0.2720 0.2931 0.2473 0.0588  0.0449  0.0714  574 THR B CG2 
20198 N N   . HIS B  549 ? 0.2347 0.2693 0.2087 0.0571  0.0305  0.0555  575 HIS B N   
20199 C CA  . HIS B  549 ? 0.2359 0.2741 0.2093 0.0568  0.0262  0.0511  575 HIS B CA  
20200 C C   . HIS B  549 ? 0.2475 0.2888 0.2142 0.0620  0.0252  0.0520  575 HIS B C   
20201 O O   . HIS B  549 ? 0.2434 0.2872 0.2051 0.0647  0.0261  0.0534  575 HIS B O   
20202 C CB  . HIS B  549 ? 0.2351 0.2771 0.2095 0.0542  0.0239  0.0469  575 HIS B CB  
20203 C CG  . HIS B  549 ? 0.2410 0.2815 0.2212 0.0503  0.0254  0.0471  575 HIS B CG  
20204 N ND1 . HIS B  549 ? 0.2546 0.2953 0.2344 0.0510  0.0284  0.0493  575 HIS B ND1 
20205 C CD2 . HIS B  549 ? 0.2350 0.2743 0.2213 0.0457  0.0244  0.0456  575 HIS B CD2 
20206 C CE1 . HIS B  549 ? 0.2580 0.2981 0.2442 0.0470  0.0289  0.0492  575 HIS B CE1 
20207 N NE2 . HIS B  549 ? 0.2532 0.2924 0.2433 0.0437  0.0265  0.0471  575 HIS B NE2 
20215 N N   . HIS B  550 ? 0.2513 0.2934 0.2180 0.0632  0.0231  0.0511  576 HIS B N   
20216 C CA  . HIS B  550 ? 0.2636 0.3095 0.2248 0.0682  0.0219  0.0525  576 HIS B CA  
20217 C C   . HIS B  550 ? 0.2753 0.3265 0.2367 0.0679  0.0176  0.0483  576 HIS B C   
20218 O O   . HIS B  550 ? 0.2740 0.3234 0.2397 0.0662  0.0167  0.0469  576 HIS B O   
20219 C CB  . HIS B  550 ? 0.2657 0.3065 0.2269 0.0713  0.0249  0.0576  576 HIS B CB  
20220 C CG  . HIS B  550 ? 0.2853 0.3219 0.2449 0.0727  0.0293  0.0625  576 HIS B CG  
20221 N ND1 . HIS B  550 ? 0.3086 0.3483 0.2617 0.0768  0.0302  0.0654  576 HIS B ND1 
20222 C CD2 . HIS B  550 ? 0.3034 0.3331 0.2668 0.0700  0.0329  0.0647  576 HIS B CD2 
20223 C CE1 . HIS B  550 ? 0.3148 0.3494 0.2682 0.0768  0.0345  0.0696  576 HIS B CE1 
20224 N NE2 . HIS B  550 ? 0.3165 0.3452 0.2763 0.0727  0.0363  0.0693  576 HIS B NE2 
20232 N N   . LEU B  551 ? 0.2781 0.3361 0.2346 0.0694  0.0150  0.0463  577 LEU B N   
20233 C CA  . LEU B  551 ? 0.2884 0.3527 0.2448 0.0692  0.0108  0.0424  577 LEU B CA  
20234 C C   . LEU B  551 ? 0.3001 0.3706 0.2511 0.0744  0.0093  0.0446  577 LEU B C   
20235 O O   . LEU B  551 ? 0.3091 0.3865 0.2591 0.0743  0.0057  0.0414  577 LEU B O   
20236 C CB  . LEU B  551 ? 0.2909 0.3582 0.2467 0.0654  0.0085  0.0372  577 LEU B CB  
20237 C CG  . LEU B  551 ? 0.3095 0.3724 0.2714 0.0603  0.0090  0.0347  577 LEU B CG  
20238 C CD1 . LEU B  551 ? 0.3221 0.3876 0.2829 0.0574  0.0072  0.0302  577 LEU B CD1 
20239 C CD2 . LEU B  551 ? 0.3122 0.3739 0.2792 0.0584  0.0076  0.0334  577 LEU B CD2 
20251 N N   . GLU B  552 ? 0.2986 0.3670 0.2469 0.0788  0.0120  0.0502  578 GLU B N   
20252 C CA  . GLU B  552 ? 0.3076 0.3823 0.2508 0.0842  0.0108  0.0532  578 GLU B CA  
20253 C C   . GLU B  552 ? 0.3119 0.3908 0.2576 0.0862  0.0084  0.0531  578 GLU B C   
20254 O O   . GLU B  552 ? 0.3074 0.3944 0.2493 0.0899  0.0060  0.0543  578 GLU B O   
20255 C CB  . GLU B  552 ? 0.3346 0.4050 0.2748 0.0886  0.0149  0.0600  578 GLU B CB  
20256 C CG  . GLU B  552 ? 0.3854 0.4518 0.3229 0.0875  0.0180  0.0613  578 GLU B CG  
20257 C CD  . GLU B  552 ? 0.4481 0.5052 0.3912 0.0841  0.0216  0.0622  578 GLU B CD  
20258 O OE1 . GLU B  552 ? 0.4679 0.5220 0.4171 0.0811  0.0209  0.0598  578 GLU B OE1 
20259 O OE2 . GLU B  552 ? 0.4731 0.5264 0.4146 0.0844  0.0252  0.0653  578 GLU B OE2 
20266 N N   . PHE B  553 ? 0.3073 0.3811 0.2594 0.0841  0.0092  0.0520  579 PHE B N   
20267 C CA  . PHE B  553 ? 0.3080 0.3852 0.2631 0.0862  0.0075  0.0518  579 PHE B CA  
20268 C C   . PHE B  553 ? 0.3154 0.4031 0.2699 0.0851  0.0026  0.0474  579 PHE B C   
20269 O O   . PHE B  553 ? 0.3149 0.4085 0.2704 0.0884  0.0009  0.0484  579 PHE B O   
20270 C CB  . PHE B  553 ? 0.2934 0.3628 0.2549 0.0832  0.0094  0.0504  579 PHE B CB  
20271 C CG  . PHE B  553 ? 0.2889 0.3566 0.2535 0.0766  0.0080  0.0449  579 PHE B CG  
20272 C CD1 . PHE B  553 ? 0.2941 0.3667 0.2615 0.0738  0.0047  0.0402  579 PHE B CD1 
20273 C CD2 . PHE B  553 ? 0.2925 0.3538 0.2577 0.0732  0.0103  0.0449  579 PHE B CD2 
20274 C CE1 . PHE B  553 ? 0.3054 0.3762 0.2755 0.0680  0.0037  0.0357  579 PHE B CE1 
20275 C CE2 . PHE B  553 ? 0.2966 0.3570 0.2649 0.0675  0.0091  0.0404  579 PHE B CE2 
20276 C CZ  . PHE B  553 ? 0.2988 0.3636 0.2693 0.0650  0.0058  0.0359  579 PHE B CZ  
20286 N N   . ILE B  554 ? 0.3175 0.4075 0.2706 0.0806  0.0005  0.0426  580 ILE B N   
20287 C CA  . ILE B  554 ? 0.3225 0.4218 0.2750 0.0785  -0.0040 0.0378  580 ILE B CA  
20288 C C   . ILE B  554 ? 0.3292 0.4389 0.2772 0.0832  -0.0065 0.0399  580 ILE B C   
20289 O O   . ILE B  554 ? 0.3199 0.4378 0.2694 0.0831  -0.0098 0.0378  580 ILE B O   
20290 C CB  . ILE B  554 ? 0.3254 0.4239 0.2760 0.0734  -0.0049 0.0330  580 ILE B CB  
20291 C CG1 . ILE B  554 ? 0.3405 0.4310 0.2968 0.0686  -0.0033 0.0305  580 ILE B CG1 
20292 C CG2 . ILE B  554 ? 0.3252 0.4332 0.2737 0.0713  -0.0092 0.0282  580 ILE B CG2 
20293 C CD1 . ILE B  554 ? 0.3625 0.4494 0.3172 0.0650  -0.0024 0.0281  580 ILE B CD1 
20305 N N   . GLN B  555 ? 0.3461 0.4557 0.2886 0.0871  -0.0049 0.0444  581 GLN B N   
20306 C CA  . GLN B  555 ? 0.3665 0.4862 0.3038 0.0917  -0.0071 0.0473  581 GLN B CA  
20307 C C   . GLN B  555 ? 0.3809 0.5050 0.3214 0.0969  -0.0076 0.0514  581 GLN B C   
20308 O O   . GLN B  555 ? 0.3785 0.5137 0.3165 0.0998  -0.0108 0.0525  581 GLN B O   
20309 C CB  . GLN B  555 ? 0.3990 0.5157 0.3298 0.0948  -0.0043 0.0518  581 GLN B CB  
20310 C CG  . GLN B  555 ? 0.4731 0.6000 0.3970 0.0992  -0.0066 0.0548  581 GLN B CG  
20311 C CD  . GLN B  555 ? 0.5507 0.6736 0.4679 0.1013  -0.0035 0.0586  581 GLN B CD  
20312 O OE1 . GLN B  555 ? 0.5639 0.6770 0.4830 0.1024  0.0010  0.0623  581 GLN B OE1 
20313 N NE2 . GLN B  555 ? 0.5634 0.6940 0.4728 0.1016  -0.0056 0.0576  581 GLN B NE2 
20322 N N   . ASN B  556 ? 0.3899 0.5055 0.3356 0.0984  -0.0042 0.0541  582 ASN B N   
20323 C CA  . ASN B  556 ? 0.4075 0.5255 0.3563 0.1040  -0.0036 0.0586  582 ASN B CA  
20324 C C   . ASN B  556 ? 0.4039 0.5305 0.3574 0.1035  -0.0071 0.0555  582 ASN B C   
20325 O O   . ASN B  556 ? 0.4234 0.5552 0.3787 0.1090  -0.0072 0.0594  582 ASN B O   
20326 C CB  . ASN B  556 ? 0.4476 0.5527 0.4001 0.1052  0.0015  0.0618  582 ASN B CB  
20327 C CG  . ASN B  556 ? 0.5356 0.6331 0.4841 0.1070  0.0053  0.0663  582 ASN B CG  
20328 O OD1 . ASN B  556 ? 0.5442 0.6376 0.4905 0.1029  0.0060  0.0640  582 ASN B OD1 
20329 N ND2 . ASN B  556 ? 0.5914 0.6879 0.5383 0.1135  0.0077  0.0732  582 ASN B ND2 
20336 N N   . PHE B  557 ? 0.3803 0.5086 0.3361 0.0973  -0.0095 0.0489  583 PHE B N   
20337 C CA  . PHE B  557 ? 0.3615 0.4975 0.3221 0.0962  -0.0125 0.0456  583 PHE B CA  
20338 C C   . PHE B  557 ? 0.3516 0.5025 0.3094 0.0967  -0.0174 0.0443  583 PHE B C   
20339 O O   . PHE B  557 ? 0.3545 0.5084 0.3076 0.0930  -0.0196 0.0409  583 PHE B O   
20340 C CB  . PHE B  557 ? 0.3505 0.4813 0.3148 0.0891  -0.0127 0.0393  583 PHE B CB  
20341 C CG  . PHE B  557 ? 0.3534 0.4705 0.3206 0.0877  -0.0084 0.0401  583 PHE B CG  
20342 C CD1 . PHE B  557 ? 0.3543 0.4671 0.3264 0.0900  -0.0059 0.0419  583 PHE B CD1 
20343 C CD2 . PHE B  557 ? 0.3623 0.4713 0.3276 0.0840  -0.0067 0.0388  583 PHE B CD2 
20344 C CE1 . PHE B  557 ? 0.3623 0.4627 0.3367 0.0881  -0.0020 0.0421  583 PHE B CE1 
20345 C CE2 . PHE B  557 ? 0.3712 0.4686 0.3394 0.0822  -0.0029 0.0394  583 PHE B CE2 
20346 C CZ  . PHE B  557 ? 0.3647 0.4579 0.3373 0.0840  -0.0008 0.0408  583 PHE B CZ  
20356 N N   . THR B  558 ? 0.3350 0.4954 0.2960 0.1009  -0.0190 0.0467  584 THR B N   
20357 C CA  . THR B  558 ? 0.3304 0.5066 0.2894 0.1013  -0.0240 0.0456  584 THR B CA  
20358 C C   . THR B  558 ? 0.3214 0.5040 0.2848 0.0955  -0.0273 0.0390  584 THR B C   
20359 O O   . THR B  558 ? 0.3265 0.5210 0.2876 0.0936  -0.0315 0.0365  584 THR B O   
20360 C CB  . THR B  558 ? 0.3500 0.5351 0.3101 0.1093  -0.0244 0.0524  584 THR B CB  
20361 O OG1 . THR B  558 ? 0.3696 0.5550 0.3375 0.1113  -0.0232 0.0530  584 THR B OG1 
20362 C CG2 . THR B  558 ? 0.3561 0.5343 0.3121 0.1152  -0.0207 0.0594  584 THR B CG2 
20370 N N   . ASN B  559 ? 0.3096 0.4848 0.2789 0.0927  -0.0253 0.0363  585 ASN B N   
20371 C CA  . ASN B  559 ? 0.3111 0.4918 0.2846 0.0873  -0.0280 0.0304  585 ASN B CA  
20372 C C   . ASN B  559 ? 0.3029 0.4733 0.2763 0.0800  -0.0270 0.0249  585 ASN B C   
20373 O O   . ASN B  559 ? 0.3049 0.4773 0.2823 0.0755  -0.0284 0.0204  585 ASN B O   
20374 C CB  . ASN B  559 ? 0.3346 0.5167 0.3156 0.0899  -0.0267 0.0317  585 ASN B CB  
20375 C CG  . ASN B  559 ? 0.3906 0.5821 0.3733 0.0976  -0.0271 0.0376  585 ASN B CG  
20376 O OD1 . ASN B  559 ? 0.4115 0.5963 0.3956 0.1033  -0.0233 0.0427  585 ASN B OD1 
20377 N ND2 . ASN B  559 ? 0.3842 0.5915 0.3670 0.0980  -0.0315 0.0371  585 ASN B ND2 
20384 N N   . LEU B  560 ? 0.2906 0.4503 0.2599 0.0791  -0.0245 0.0255  586 LEU B N   
20385 C CA  . LEU B  560 ? 0.2834 0.4339 0.2531 0.0728  -0.0235 0.0210  586 LEU B CA  
20386 C C   . LEU B  560 ? 0.2839 0.4405 0.2508 0.0674  -0.0270 0.0154  586 LEU B C   
20387 O O   . LEU B  560 ? 0.2907 0.4514 0.2517 0.0679  -0.0284 0.0155  586 LEU B O   
20388 C CB  . LEU B  560 ? 0.2767 0.4157 0.2432 0.0735  -0.0199 0.0235  586 LEU B CB  
20389 C CG  . LEU B  560 ? 0.2868 0.4157 0.2547 0.0679  -0.0182 0.0199  586 LEU B CG  
20390 C CD1 . LEU B  560 ? 0.2858 0.4094 0.2602 0.0663  -0.0166 0.0192  586 LEU B CD1 
20391 C CD2 . LEU B  560 ? 0.2992 0.4193 0.2636 0.0689  -0.0151 0.0227  586 LEU B CD2 
20403 N N   . LYS B  561 ? 0.2709 0.4275 0.2418 0.0622  -0.0281 0.0107  587 LYS B N   
20404 C CA  . LYS B  561 ? 0.2701 0.4314 0.2391 0.0564  -0.0310 0.0051  587 LYS B CA  
20405 C C   . LYS B  561 ? 0.2679 0.4185 0.2360 0.0513  -0.0293 0.0017  587 LYS B C   
20406 O O   . LYS B  561 ? 0.2712 0.4221 0.2349 0.0482  -0.0303 -0.0014 587 LYS B O   
20407 C CB  . LYS B  561 ? 0.2804 0.4500 0.2547 0.0539  -0.0335 0.0021  587 LYS B CB  
20408 C CG  . LYS B  561 ? 0.3537 0.5366 0.3294 0.0583  -0.0359 0.0047  587 LYS B CG  
20409 C CD  . LYS B  561 ? 0.4243 0.6150 0.4062 0.0557  -0.0377 0.0020  587 LYS B CD  
20410 C CE  . LYS B  561 ? 0.4787 0.6841 0.4628 0.0599  -0.0403 0.0046  587 LYS B CE  
20411 N NZ  . LYS B  561 ? 0.5189 0.7235 0.5032 0.0679  -0.0382 0.0112  587 LYS B NZ  
20425 N N   . VAL B  562 ? 0.2532 0.3952 0.2258 0.0502  -0.0268 0.0021  588 VAL B N   
20426 C CA  . VAL B  562 ? 0.2575 0.3905 0.2304 0.0454  -0.0254 -0.0007 588 VAL B CA  
20427 C C   . VAL B  562 ? 0.2519 0.3744 0.2255 0.0472  -0.0217 0.0028  588 VAL B C   
20428 O O   . VAL B  562 ? 0.2537 0.3738 0.2308 0.0497  -0.0201 0.0056  588 VAL B O   
20429 C CB  . VAL B  562 ? 0.2711 0.4048 0.2490 0.0407  -0.0264 -0.0044 588 VAL B CB  
20430 C CG1 . VAL B  562 ? 0.2748 0.3998 0.2531 0.0359  -0.0251 -0.0069 588 VAL B CG1 
20431 C CG2 . VAL B  562 ? 0.2667 0.4116 0.2446 0.0387  -0.0299 -0.0077 588 VAL B CG2 
20441 N N   . LEU B  563 ? 0.2366 0.3529 0.2071 0.0458  -0.0203 0.0025  589 LEU B N   
20442 C CA  . LEU B  563 ? 0.2309 0.3380 0.2021 0.0469  -0.0169 0.0056  589 LEU B CA  
20443 C C   . LEU B  563 ? 0.2242 0.3252 0.1962 0.0422  -0.0161 0.0029  589 LEU B C   
20444 O O   . LEU B  563 ? 0.2296 0.3313 0.1981 0.0404  -0.0167 0.0004  589 LEU B O   
20445 C CB  . LEU B  563 ? 0.2326 0.3390 0.1987 0.0512  -0.0154 0.0093  589 LEU B CB  
20446 C CG  . LEU B  563 ? 0.2432 0.3405 0.2098 0.0521  -0.0117 0.0126  589 LEU B CG  
20447 C CD1 . LEU B  563 ? 0.2371 0.3297 0.2087 0.0530  -0.0099 0.0151  589 LEU B CD1 
20448 C CD2 . LEU B  563 ? 0.2464 0.3441 0.2075 0.0563  -0.0103 0.0161  589 LEU B CD2 
20460 N N   . ASN B  564 ? 0.2094 0.3044 0.1858 0.0404  -0.0145 0.0036  590 ASN B N   
20461 C CA  . ASN B  564 ? 0.2074 0.2969 0.1853 0.0363  -0.0136 0.0019  590 ASN B CA  
20462 C C   . ASN B  564 ? 0.2126 0.2951 0.1913 0.0374  -0.0106 0.0054  590 ASN B C   
20463 O O   . ASN B  564 ? 0.2093 0.2885 0.1911 0.0377  -0.0093 0.0075  590 ASN B O   
20464 C CB  . ASN B  564 ? 0.2023 0.2920 0.1847 0.0322  -0.0149 -0.0008 590 ASN B CB  
20465 C CG  . ASN B  564 ? 0.2278 0.3134 0.2115 0.0280  -0.0146 -0.0028 590 ASN B CG  
20466 O OD1 . ASN B  564 ? 0.2349 0.3161 0.2174 0.0283  -0.0128 -0.0014 590 ASN B OD1 
20467 N ND2 . ASN B  564 ? 0.2484 0.3349 0.2348 0.0242  -0.0160 -0.0056 590 ASN B ND2 
20473 N N   . LEU B  565 ? 0.2166 0.2968 0.1922 0.0379  -0.0092 0.0060  591 LEU B N   
20474 C CA  . LEU B  565 ? 0.2254 0.2997 0.2020 0.0385  -0.0062 0.0092  591 LEU B CA  
20475 C C   . LEU B  565 ? 0.2232 0.2938 0.2024 0.0347  -0.0056 0.0077  591 LEU B C   
20476 O O   . LEU B  565 ? 0.2288 0.2959 0.2081 0.0352  -0.0032 0.0098  591 LEU B O   
20477 C CB  . LEU B  565 ? 0.2295 0.3040 0.2009 0.0421  -0.0046 0.0114  591 LEU B CB  
20478 C CG  . LEU B  565 ? 0.2504 0.3290 0.2184 0.0465  -0.0051 0.0135  591 LEU B CG  
20479 C CD1 . LEU B  565 ? 0.2608 0.3398 0.2230 0.0497  -0.0036 0.0155  591 LEU B CD1 
20480 C CD2 . LEU B  565 ? 0.2657 0.3415 0.2372 0.0481  -0.0037 0.0170  591 LEU B CD2 
20492 N N   . SER B  566 ? 0.2185 0.2903 0.2001 0.0311  -0.0075 0.0045  592 SER B N   
20493 C CA  . SER B  566 ? 0.2228 0.2915 0.2067 0.0280  -0.0070 0.0034  592 SER B CA  
20494 C C   . SER B  566 ? 0.2280 0.2925 0.2165 0.0267  -0.0052 0.0063  592 SER B C   
20495 O O   . SER B  566 ? 0.2320 0.2958 0.2229 0.0267  -0.0050 0.0081  592 SER B O   
20496 C CB  . SER B  566 ? 0.2405 0.3112 0.2259 0.0244  -0.0093 -0.0004 592 SER B CB  
20497 O OG  . SER B  566 ? 0.2659 0.3369 0.2554 0.0224  -0.0103 -0.0002 592 SER B OG  
20503 N N   . HIS B  567 ? 0.2156 0.2776 0.2054 0.0256  -0.0038 0.0068  593 HIS B N   
20504 C CA  . HIS B  567 ? 0.2248 0.2840 0.2193 0.0240  -0.0024 0.0095  593 HIS B CA  
20505 C C   . HIS B  567 ? 0.2273 0.2852 0.2229 0.0255  -0.0007 0.0131  593 HIS B C   
20506 O O   . HIS B  567 ? 0.2268 0.2835 0.2264 0.0234  -0.0006 0.0146  593 HIS B O   
20507 C CB  . HIS B  567 ? 0.2399 0.2996 0.2383 0.0201  -0.0044 0.0081  593 HIS B CB  
20508 C CG  . HIS B  567 ? 0.2885 0.3490 0.2860 0.0183  -0.0057 0.0049  593 HIS B CG  
20509 N ND1 . HIS B  567 ? 0.3186 0.3770 0.3170 0.0178  -0.0045 0.0051  593 HIS B ND1 
20510 C CD2 . HIS B  567 ? 0.3095 0.3724 0.3052 0.0172  -0.0078 0.0015  593 HIS B CD2 
20511 C CE1 . HIS B  567 ? 0.3289 0.3878 0.3258 0.0162  -0.0058 0.0018  593 HIS B CE1 
20512 N NE2 . HIS B  567 ? 0.3306 0.3925 0.3260 0.0155  -0.0079 -0.0005 593 HIS B NE2 
20520 N N   . ASN B  568 ? 0.2236 0.2814 0.2154 0.0291  0.0009  0.0145  594 ASN B N   
20521 C CA  . ASN B  568 ? 0.2270 0.2828 0.2191 0.0310  0.0031  0.0182  594 ASN B CA  
20522 C C   . ASN B  568 ? 0.2310 0.2852 0.2237 0.0321  0.0060  0.0209  594 ASN B C   
20523 O O   . ASN B  568 ? 0.2223 0.2747 0.2160 0.0330  0.0082  0.0243  594 ASN B O   
20524 C CB  . ASN B  568 ? 0.2370 0.2942 0.2246 0.0346  0.0029  0.0185  594 ASN B CB  
20525 C CG  . ASN B  568 ? 0.2523 0.3101 0.2413 0.0339  0.0013  0.0178  594 ASN B CG  
20526 O OD1 . ASN B  568 ? 0.2674 0.3226 0.2602 0.0317  0.0019  0.0189  594 ASN B OD1 
20527 N ND2 . ASN B  568 ? 0.2316 0.2928 0.2176 0.0357  -0.0005 0.0159  594 ASN B ND2 
20534 N N   . ASN B  569 ? 0.2422 0.2965 0.2345 0.0318  0.0065  0.0197  595 ASN B N   
20535 C CA  . ASN B  569 ? 0.2608 0.3138 0.2540 0.0331  0.0096  0.0223  595 ASN B CA  
20536 C C   . ASN B  569 ? 0.2591 0.3118 0.2477 0.0369  0.0119  0.0245  595 ASN B C   
20537 O O   . ASN B  569 ? 0.2659 0.3173 0.2563 0.0378  0.0147  0.0280  595 ASN B O   
20538 C CB  . ASN B  569 ? 0.3011 0.3535 0.3013 0.0305  0.0104  0.0252  595 ASN B CB  
20539 C CG  . ASN B  569 ? 0.4147 0.4676 0.4189 0.0290  0.0110  0.0254  595 ASN B CG  
20540 O OD1 . ASN B  569 ? 0.4579 0.5110 0.4619 0.0278  0.0092  0.0226  595 ASN B OD1 
20541 N ND2 . ASN B  569 ? 0.4329 0.4859 0.4411 0.0291  0.0135  0.0290  595 ASN B ND2 
20548 N N   . ILE B  570 ? 0.2509 0.3050 0.2336 0.0391  0.0107  0.0226  596 ILE B N   
20549 C CA  . ILE B  570 ? 0.2492 0.3035 0.2268 0.0429  0.0125  0.0249  596 ILE B CA  
20550 C C   . ILE B  570 ? 0.2466 0.3003 0.2210 0.0447  0.0153  0.0251  596 ILE B C   
20551 O O   . ILE B  570 ? 0.2550 0.3094 0.2266 0.0444  0.0145  0.0216  596 ILE B O   
20552 C CB  . ILE B  570 ? 0.2473 0.3046 0.2195 0.0448  0.0100  0.0229  596 ILE B CB  
20553 C CG1 . ILE B  570 ? 0.2391 0.2968 0.2147 0.0435  0.0078  0.0230  596 ILE B CG1 
20554 C CG2 . ILE B  570 ? 0.2544 0.3125 0.2207 0.0490  0.0119  0.0256  596 ILE B CG2 
20555 C CD1 . ILE B  570 ? 0.2407 0.3026 0.2128 0.0448  0.0049  0.0207  596 ILE B CD1 
20567 N N   . TYR B  571 ? 0.2384 0.2906 0.2136 0.0464  0.0187  0.0291  597 TYR B N   
20568 C CA  . TYR B  571 ? 0.2417 0.2934 0.2138 0.0485  0.0220  0.0297  597 TYR B CA  
20569 C C   . TYR B  571 ? 0.2445 0.2958 0.2128 0.0518  0.0249  0.0336  597 TYR B C   
20570 O O   . TYR B  571 ? 0.2454 0.2964 0.2103 0.0538  0.0279  0.0342  597 TYR B O   
20571 C CB  . TYR B  571 ? 0.2405 0.2908 0.2189 0.0468  0.0241  0.0309  597 TYR B CB  
20572 C CG  . TYR B  571 ? 0.2505 0.3002 0.2353 0.0459  0.0261  0.0355  597 TYR B CG  
20573 C CD1 . TYR B  571 ? 0.2542 0.3039 0.2446 0.0427  0.0239  0.0361  597 TYR B CD1 
20574 C CD2 . TYR B  571 ? 0.2657 0.3151 0.2515 0.0475  0.0302  0.0389  597 TYR B CD2 
20575 C CE1 . TYR B  571 ? 0.2650 0.3144 0.2616 0.0409  0.0256  0.0398  597 TYR B CE1 
20576 C CE2 . TYR B  571 ? 0.2736 0.3231 0.2661 0.0459  0.0320  0.0429  597 TYR B CE2 
20577 C CZ  . TYR B  571 ? 0.2767 0.3262 0.2746 0.0424  0.0295  0.0432  597 TYR B CZ  
20578 O OH  . TYR B  571 ? 0.2878 0.3377 0.2923 0.0400  0.0310  0.0467  597 TYR B OH  
20588 N N   . THR B  572 ? 0.2486 0.2995 0.2175 0.0525  0.0246  0.0365  598 THR B N   
20589 C CA  . THR B  572 ? 0.2476 0.2977 0.2130 0.0556  0.0276  0.0407  598 THR B CA  
20590 C C   . THR B  572 ? 0.2525 0.3025 0.2166 0.0568  0.0260  0.0423  598 THR B C   
20591 O O   . THR B  572 ? 0.2451 0.2940 0.2141 0.0544  0.0242  0.0419  598 THR B O   
20592 C CB  . THR B  572 ? 0.2518 0.2998 0.2227 0.0547  0.0315  0.0447  598 THR B CB  
20593 O OG1 . THR B  572 ? 0.2633 0.3102 0.2305 0.0578  0.0346  0.0490  598 THR B OG1 
20594 C CG2 . THR B  572 ? 0.2486 0.2951 0.2278 0.0509  0.0305  0.0457  598 THR B CG2 
20602 N N   . LEU B  573 ? 0.2602 0.3114 0.2174 0.0607  0.0267  0.0441  599 LEU B N   
20603 C CA  . LEU B  573 ? 0.2628 0.3141 0.2181 0.0630  0.0258  0.0465  599 LEU B CA  
20604 C C   . LEU B  573 ? 0.2761 0.3252 0.2284 0.0662  0.0299  0.0521  599 LEU B C   
20605 O O   . LEU B  573 ? 0.2834 0.3327 0.2329 0.0673  0.0327  0.0532  599 LEU B O   
20606 C CB  . LEU B  573 ? 0.2569 0.3132 0.2063 0.0649  0.0222  0.0436  599 LEU B CB  
20607 C CG  . LEU B  573 ? 0.2597 0.3183 0.2116 0.0618  0.0182  0.0381  599 LEU B CG  
20608 C CD1 . LEU B  573 ? 0.2643 0.3286 0.2102 0.0636  0.0148  0.0356  599 LEU B CD1 
20609 C CD2 . LEU B  573 ? 0.2617 0.3180 0.2205 0.0593  0.0169  0.0381  599 LEU B CD2 
20621 N N   . THR B  574 ? 0.2805 0.3271 0.2338 0.0676  0.0306  0.0556  600 THR B N   
20622 C CA  . THR B  574 ? 0.2923 0.3360 0.2433 0.0705  0.0347  0.0613  600 THR B CA  
20623 C C   . THR B  574 ? 0.3188 0.3657 0.2617 0.0755  0.0340  0.0634  600 THR B C   
20624 O O   . THR B  574 ? 0.3271 0.3756 0.2694 0.0770  0.0313  0.0630  600 THR B O   
20625 C CB  . THR B  574 ? 0.2971 0.3352 0.2539 0.0689  0.0363  0.0642  600 THR B CB  
20626 O OG1 . THR B  574 ? 0.2924 0.3286 0.2566 0.0638  0.0362  0.0621  600 THR B OG1 
20627 C CG2 . THR B  574 ? 0.3069 0.3410 0.2620 0.0713  0.0409  0.0704  600 THR B CG2 
20635 N N   . ASP B  575 ? 0.3311 0.3794 0.2679 0.0783  0.0365  0.0658  601 ASP B N   
20636 C CA  . ASP B  575 ? 0.3508 0.4025 0.2793 0.0833  0.0364  0.0687  601 ASP B CA  
20637 C C   . ASP B  575 ? 0.3618 0.4206 0.2849 0.0845  0.0316  0.0646  601 ASP B C   
20638 O O   . ASP B  575 ? 0.3727 0.4357 0.2879 0.0867  0.0316  0.0644  601 ASP B O   
20639 C CB  . ASP B  575 ? 0.3790 0.4270 0.3083 0.0861  0.0381  0.0744  601 ASP B CB  
20640 C CG  . ASP B  575 ? 0.4431 0.4842 0.3764 0.0851  0.0432  0.0790  601 ASP B CG  
20641 O OD1 . ASP B  575 ? 0.4579 0.4988 0.3899 0.0845  0.0462  0.0799  601 ASP B OD1 
20642 O OD2 . ASP B  575 ? 0.4735 0.5095 0.4111 0.0848  0.0444  0.0816  601 ASP B OD2 
20647 N N   . LYS B  576 ? 0.3543 0.4148 0.2810 0.0831  0.0277  0.0615  602 LYS B N   
20648 C CA  . LYS B  576 ? 0.3559 0.4236 0.2784 0.0835  0.0232  0.0574  602 LYS B CA  
20649 C C   . LYS B  576 ? 0.3482 0.4163 0.2738 0.0788  0.0213  0.0510  602 LYS B C   
20650 O O   . LYS B  576 ? 0.3432 0.4085 0.2760 0.0756  0.0205  0.0491  602 LYS B O   
20651 C CB  . LYS B  576 ? 0.3851 0.4557 0.3093 0.0854  0.0201  0.0582  602 LYS B CB  
20652 C CG  . LYS B  576 ? 0.4530 0.5328 0.3720 0.0864  0.0155  0.0547  602 LYS B CG  
20653 C CD  . LYS B  576 ? 0.5331 0.6174 0.4533 0.0892  0.0127  0.0564  602 LYS B CD  
20654 C CE  . LYS B  576 ? 0.5937 0.6873 0.5062 0.0929  0.0100  0.0575  602 LYS B CE  
20655 N NZ  . LYS B  576 ? 0.6350 0.7345 0.5425 0.0901  0.0071  0.0516  602 LYS B NZ  
20669 N N   . TYR B  577 ? 0.3383 0.4096 0.2582 0.0784  0.0209  0.0478  603 TYR B N   
20670 C CA  . TYR B  577 ? 0.3340 0.4048 0.2560 0.0742  0.0197  0.0420  603 TYR B CA  
20671 C C   . TYR B  577 ? 0.3381 0.4145 0.2587 0.0725  0.0148  0.0367  603 TYR B C   
20672 O O   . TYR B  577 ? 0.3490 0.4244 0.2723 0.0688  0.0137  0.0319  603 TYR B O   
20673 C CB  . TYR B  577 ? 0.3249 0.3949 0.2412 0.0746  0.0227  0.0411  603 TYR B CB  
20674 C CG  . TYR B  577 ? 0.3201 0.3856 0.2379 0.0762  0.0278  0.0464  603 TYR B CG  
20675 C CD1 . TYR B  577 ? 0.3192 0.3797 0.2457 0.0742  0.0298  0.0486  603 TYR B CD1 
20676 C CD2 . TYR B  577 ? 0.3349 0.4014 0.2451 0.0796  0.0306  0.0496  603 TYR B CD2 
20677 C CE1 . TYR B  577 ? 0.3308 0.3875 0.2590 0.0752  0.0344  0.0534  603 TYR B CE1 
20678 C CE2 . TYR B  577 ? 0.3437 0.4062 0.2554 0.0809  0.0355  0.0545  603 TYR B CE2 
20679 C CZ  . TYR B  577 ? 0.3457 0.4033 0.2667 0.0786  0.0374  0.0564  603 TYR B CZ  
20680 O OH  . TYR B  577 ? 0.3566 0.4106 0.2796 0.0794  0.0422  0.0614  603 TYR B OH  
20690 N N   . ASN B  578 ? 0.3296 0.4119 0.2465 0.0752  0.0120  0.0377  604 ASN B N   
20691 C CA  . ASN B  578 ? 0.3346 0.4235 0.2494 0.0737  0.0074  0.0331  604 ASN B CA  
20692 C C   . ASN B  578 ? 0.3448 0.4362 0.2655 0.0735  0.0044  0.0332  604 ASN B C   
20693 O O   . ASN B  578 ? 0.3612 0.4511 0.2845 0.0765  0.0054  0.0380  604 ASN B O   
20694 C CB  . ASN B  578 ? 0.3475 0.4435 0.2528 0.0768  0.0060  0.0339  604 ASN B CB  
20695 C CG  . ASN B  578 ? 0.3885 0.4828 0.2867 0.0770  0.0089  0.0330  604 ASN B CG  
20696 O OD1 . ASN B  578 ? 0.3994 0.4901 0.2982 0.0736  0.0101  0.0286  604 ASN B OD1 
20697 N ND2 . ASN B  578 ? 0.3873 0.4842 0.2785 0.0810  0.0104  0.0372  604 ASN B ND2 
20704 N N   . LEU B  579 ? 0.3287 0.4236 0.2510 0.0701  0.0008  0.0278  605 LEU B N   
20705 C CA  . LEU B  579 ? 0.3273 0.4259 0.2545 0.0697  -0.0023 0.0271  605 LEU B CA  
20706 C C   . LEU B  579 ? 0.3291 0.4377 0.2508 0.0720  -0.0058 0.0268  605 LEU B C   
20707 O O   . LEU B  579 ? 0.3401 0.4529 0.2557 0.0705  -0.0073 0.0232  605 LEU B O   
20708 C CB  . LEU B  579 ? 0.3269 0.4242 0.2592 0.0645  -0.0040 0.0216  605 LEU B CB  
20709 C CG  . LEU B  579 ? 0.3453 0.4339 0.2828 0.0616  -0.0011 0.0212  605 LEU B CG  
20710 C CD1 . LEU B  579 ? 0.3480 0.4364 0.2907 0.0569  -0.0033 0.0166  605 LEU B CD1 
20711 C CD2 . LEU B  579 ? 0.3484 0.4315 0.2904 0.0636  0.0018  0.0265  605 LEU B CD2 
20723 N N   . GLU B  580 ? 0.3210 0.4334 0.2445 0.0757  -0.0069 0.0307  606 GLU B N   
20724 C CA  . GLU B  580 ? 0.3211 0.4443 0.2401 0.0784  -0.0103 0.0314  606 GLU B CA  
20725 C C   . GLU B  580 ? 0.3141 0.4424 0.2390 0.0793  -0.0129 0.0317  606 GLU B C   
20726 O O   . GLU B  580 ? 0.3124 0.4354 0.2432 0.0807  -0.0110 0.0345  606 GLU B O   
20727 C CB  . GLU B  580 ? 0.3534 0.4776 0.2668 0.0841  -0.0082 0.0378  606 GLU B CB  
20728 C CG  . GLU B  580 ? 0.4120 0.5306 0.3199 0.0836  -0.0049 0.0381  606 GLU B CG  
20729 C CD  . GLU B  580 ? 0.5343 0.6550 0.4351 0.0887  -0.0032 0.0437  606 GLU B CD  
20730 O OE1 . GLU B  580 ? 0.5647 0.6866 0.4669 0.0934  -0.0027 0.0496  606 GLU B OE1 
20731 O OE2 . GLU B  580 ? 0.5808 0.7013 0.4745 0.0881  -0.0019 0.0425  606 GLU B OE2 
20738 N N   . SER B  581 ? 0.3103 0.4491 0.2335 0.0783  -0.0172 0.0287  607 SER B N   
20739 C CA  . SER B  581 ? 0.3057 0.4514 0.2342 0.0793  -0.0200 0.0290  607 SER B CA  
20740 C C   . SER B  581 ? 0.3144 0.4734 0.2389 0.0788  -0.0246 0.0265  607 SER B C   
20741 O O   . SER B  581 ? 0.3225 0.4835 0.2438 0.0739  -0.0264 0.0208  607 SER B O   
20742 C CB  . SER B  581 ? 0.3066 0.4479 0.2426 0.0747  -0.0201 0.0247  607 SER B CB  
20743 O OG  . SER B  581 ? 0.3172 0.4668 0.2577 0.0753  -0.0230 0.0242  607 SER B OG  
20749 N N   . LYS B  582 ? 0.3043 0.4726 0.2292 0.0837  -0.0265 0.0308  608 LYS B N   
20750 C CA  . LYS B  582 ? 0.3017 0.4844 0.2237 0.0832  -0.0314 0.0289  608 LYS B CA  
20751 C C   . LYS B  582 ? 0.2941 0.4822 0.2226 0.0789  -0.0344 0.0239  608 LYS B C   
20752 O O   . LYS B  582 ? 0.2949 0.4935 0.2210 0.0760  -0.0384 0.0201  608 LYS B O   
20753 C CB  . LYS B  582 ? 0.3272 0.5188 0.2477 0.0905  -0.0323 0.0360  608 LYS B CB  
20754 C CG  . LYS B  582 ? 0.4061 0.5944 0.3188 0.0944  -0.0299 0.0407  608 LYS B CG  
20755 C CD  . LYS B  582 ? 0.4945 0.6918 0.4056 0.1018  -0.0308 0.0482  608 LYS B CD  
20756 C CE  . LYS B  582 ? 0.5740 0.7703 0.4761 0.1052  -0.0291 0.0526  608 LYS B CE  
20757 N NZ  . LYS B  582 ? 0.6352 0.8411 0.5356 0.1126  -0.0303 0.0603  608 LYS B NZ  
20771 N N   . SER B  583 ? 0.2826 0.4636 0.2191 0.0781  -0.0324 0.0236  609 SER B N   
20772 C CA  . SER B  583 ? 0.2708 0.4566 0.2138 0.0743  -0.0348 0.0194  609 SER B CA  
20773 C C   . SER B  583 ? 0.2579 0.4360 0.2027 0.0672  -0.0343 0.0130  609 SER B C   
20774 O O   . SER B  583 ? 0.2530 0.4372 0.2007 0.0630  -0.0370 0.0085  609 SER B O   
20775 C CB  . SER B  583 ? 0.2883 0.4728 0.2389 0.0783  -0.0332 0.0233  609 SER B CB  
20776 O OG  . SER B  583 ? 0.3212 0.4920 0.2735 0.0798  -0.0286 0.0260  609 SER B OG  
20782 N N   . LEU B  584 ? 0.2548 0.4199 0.1992 0.0661  -0.0306 0.0131  610 LEU B N   
20783 C CA  . LEU B  584 ? 0.2658 0.4230 0.2129 0.0601  -0.0296 0.0081  610 LEU B CA  
20784 C C   . LEU B  584 ? 0.2768 0.4387 0.2211 0.0543  -0.0325 0.0016  610 LEU B C   
20785 O O   . LEU B  584 ? 0.2864 0.4512 0.2237 0.0538  -0.0334 0.0003  610 LEU B O   
20786 C CB  . LEU B  584 ? 0.2712 0.4156 0.2168 0.0601  -0.0255 0.0095  610 LEU B CB  
20787 C CG  . LEU B  584 ? 0.2858 0.4212 0.2362 0.0554  -0.0238 0.0064  610 LEU B CG  
20788 C CD1 . LEU B  584 ? 0.2848 0.4171 0.2424 0.0566  -0.0226 0.0086  610 LEU B CD1 
20789 C CD2 . LEU B  584 ? 0.3062 0.4314 0.2540 0.0547  -0.0204 0.0070  610 LEU B CD2 
20801 N N   . VAL B  585 ? 0.2733 0.4358 0.2229 0.0497  -0.0337 -0.0024 611 VAL B N   
20802 C CA  . VAL B  585 ? 0.2807 0.4464 0.2282 0.0436  -0.0360 -0.0087 611 VAL B CA  
20803 C C   . VAL B  585 ? 0.2798 0.4338 0.2282 0.0390  -0.0335 -0.0121 611 VAL B C   
20804 O O   . VAL B  585 ? 0.2894 0.4421 0.2336 0.0349  -0.0339 -0.0166 611 VAL B O   
20805 C CB  . VAL B  585 ? 0.2976 0.4743 0.2496 0.0413  -0.0395 -0.0112 611 VAL B CB  
20806 C CG1 . VAL B  585 ? 0.3048 0.4935 0.2570 0.0465  -0.0418 -0.0070 611 VAL B CG1 
20807 C CG2 . VAL B  585 ? 0.3094 0.4815 0.2691 0.0392  -0.0384 -0.0118 611 VAL B CG2 
20817 N N   . GLU B  586 ? 0.2627 0.4083 0.2164 0.0397  -0.0309 -0.0099 612 GLU B N   
20818 C CA  . GLU B  586 ? 0.2494 0.3848 0.2047 0.0357  -0.0287 -0.0123 612 GLU B CA  
20819 C C   . GLU B  586 ? 0.2412 0.3669 0.1973 0.0385  -0.0250 -0.0083 612 GLU B C   
20820 O O   . GLU B  586 ? 0.2384 0.3630 0.1981 0.0417  -0.0240 -0.0044 612 GLU B O   
20821 C CB  . GLU B  586 ? 0.2525 0.3882 0.2142 0.0319  -0.0296 -0.0147 612 GLU B CB  
20822 C CG  . GLU B  586 ? 0.2705 0.3965 0.2344 0.0279  -0.0275 -0.0167 612 GLU B CG  
20823 C CD  . GLU B  586 ? 0.3398 0.4665 0.3095 0.0242  -0.0284 -0.0188 612 GLU B CD  
20824 O OE1 . GLU B  586 ? 0.3591 0.4934 0.3319 0.0250  -0.0303 -0.0185 612 GLU B OE1 
20825 O OE2 . GLU B  586 ? 0.3398 0.4595 0.3111 0.0206  -0.0271 -0.0205 612 GLU B OE2 
20832 N N   . LEU B  587 ? 0.2338 0.3522 0.1867 0.0370  -0.0228 -0.0094 613 LEU B N   
20833 C CA  . LEU B  587 ? 0.2396 0.3491 0.1940 0.0388  -0.0193 -0.0060 613 LEU B CA  
20834 C C   . LEU B  587 ? 0.2387 0.3411 0.1957 0.0344  -0.0180 -0.0086 613 LEU B C   
20835 O O   . LEU B  587 ? 0.2501 0.3512 0.2038 0.0318  -0.0179 -0.0122 613 LEU B O   
20836 C CB  . LEU B  587 ? 0.2414 0.3491 0.1896 0.0421  -0.0173 -0.0036 613 LEU B CB  
20837 C CG  . LEU B  587 ? 0.2621 0.3608 0.2122 0.0434  -0.0134 -0.0001 613 LEU B CG  
20838 C CD1 . LEU B  587 ? 0.2581 0.3550 0.2134 0.0457  -0.0125 0.0042  613 LEU B CD1 
20839 C CD2 . LEU B  587 ? 0.2670 0.3642 0.2109 0.0463  -0.0112 0.0018  613 LEU B CD2 
20851 N N   . VAL B  588 ? 0.2245 0.3220 0.1873 0.0338  -0.0167 -0.0067 614 VAL B N   
20852 C CA  . VAL B  588 ? 0.2249 0.3158 0.1906 0.0304  -0.0152 -0.0081 614 VAL B CA  
20853 C C   . VAL B  588 ? 0.2274 0.3120 0.1932 0.0326  -0.0119 -0.0043 614 VAL B C   
20854 O O   . VAL B  588 ? 0.2362 0.3192 0.2050 0.0345  -0.0109 -0.0007 614 VAL B O   
20855 C CB  . VAL B  588 ? 0.2277 0.3182 0.1994 0.0274  -0.0162 -0.0089 614 VAL B CB  
20856 C CG1 . VAL B  588 ? 0.2262 0.3105 0.2005 0.0239  -0.0148 -0.0100 614 VAL B CG1 
20857 C CG2 . VAL B  588 ? 0.2296 0.3274 0.2014 0.0255  -0.0193 -0.0122 614 VAL B CG2 
20867 N N   . PHE B  589 ? 0.2248 0.3059 0.1874 0.0324  -0.0101 -0.0052 615 PHE B N   
20868 C CA  . PHE B  589 ? 0.2262 0.3020 0.1890 0.0345  -0.0067 -0.0017 615 PHE B CA  
20869 C C   . PHE B  589 ? 0.2280 0.2981 0.1944 0.0318  -0.0049 -0.0023 615 PHE B C   
20870 O O   . PHE B  589 ? 0.2370 0.3033 0.2032 0.0331  -0.0020 -0.0002 615 PHE B O   
20871 C CB  . PHE B  589 ? 0.2288 0.3055 0.1846 0.0373  -0.0054 -0.0015 615 PHE B CB  
20872 C CG  . PHE B  589 ? 0.2461 0.3198 0.2014 0.0408  -0.0023 0.0033  615 PHE B CG  
20873 C CD1 . PHE B  589 ? 0.2561 0.3315 0.2123 0.0437  -0.0024 0.0072  615 PHE B CD1 
20874 C CD2 . PHE B  589 ? 0.2583 0.3275 0.2126 0.0413  0.0010  0.0041  615 PHE B CD2 
20875 C CE1 . PHE B  589 ? 0.2709 0.3432 0.2269 0.0465  0.0007  0.0117  615 PHE B CE1 
20876 C CE2 . PHE B  589 ? 0.2722 0.3392 0.2265 0.0442  0.0039  0.0086  615 PHE B CE2 
20877 C CZ  . PHE B  589 ? 0.2671 0.3355 0.2223 0.0466  0.0038  0.0123  615 PHE B CZ  
20887 N N   . SER B  590 ? 0.2282 0.2981 0.1980 0.0281  -0.0065 -0.0048 616 SER B N   
20888 C CA  . SER B  590 ? 0.2342 0.2992 0.2075 0.0258  -0.0050 -0.0051 616 SER B CA  
20889 C C   . SER B  590 ? 0.2323 0.2944 0.2107 0.0265  -0.0032 -0.0007 616 SER B C   
20890 O O   . SER B  590 ? 0.2309 0.2945 0.2114 0.0274  -0.0038 0.0017  616 SER B O   
20891 C CB  . SER B  590 ? 0.2588 0.3246 0.2347 0.0219  -0.0072 -0.0081 616 SER B CB  
20892 O OG  . SER B  590 ? 0.3038 0.3725 0.2832 0.0212  -0.0091 -0.0071 616 SER B OG  
20898 N N   . GLY B  591 ? 0.2210 0.2791 0.2016 0.0259  -0.0010 0.0004  617 GLY B N   
20899 C CA  . GLY B  591 ? 0.2177 0.2740 0.2038 0.0259  0.0005  0.0044  617 GLY B CA  
20900 C C   . GLY B  591 ? 0.2104 0.2665 0.1956 0.0291  0.0026  0.0080  617 GLY B C   
20901 O O   . GLY B  591 ? 0.2148 0.2706 0.2042 0.0287  0.0030  0.0112  617 GLY B O   
20905 N N   . ASN B  592 ? 0.2040 0.2602 0.1836 0.0318  0.0040  0.0075  618 ASN B N   
20906 C CA  . ASN B  592 ? 0.2068 0.2627 0.1849 0.0350  0.0064  0.0110  618 ASN B CA  
20907 C C   . ASN B  592 ? 0.2267 0.2799 0.2034 0.0365  0.0098  0.0115  618 ASN B C   
20908 O O   . ASN B  592 ? 0.2401 0.2914 0.2187 0.0349  0.0103  0.0098  618 ASN B O   
20909 C CB  . ASN B  592 ? 0.2118 0.2707 0.1843 0.0374  0.0052  0.0106  618 ASN B CB  
20910 C CG  . ASN B  592 ? 0.2374 0.2983 0.2127 0.0367  0.0029  0.0113  618 ASN B CG  
20911 O OD1 . ASN B  592 ? 0.2470 0.3061 0.2268 0.0362  0.0037  0.0143  618 ASN B OD1 
20912 N ND2 . ASN B  592 ? 0.2286 0.2931 0.2015 0.0364  0.0000  0.0086  618 ASN B ND2 
20919 N N   . ARG B  593 ? 0.2287 0.2815 0.2024 0.0396  0.0125  0.0140  619 ARG B N   
20920 C CA  . ARG B  593 ? 0.2392 0.2897 0.2117 0.0412  0.0162  0.0147  619 ARG B CA  
20921 C C   . ARG B  593 ? 0.2465 0.2973 0.2105 0.0439  0.0175  0.0130  619 ARG B C   
20922 O O   . ARG B  593 ? 0.2528 0.3030 0.2148 0.0466  0.0207  0.0158  619 ARG B O   
20923 C CB  . ARG B  593 ? 0.2562 0.3059 0.2344 0.0420  0.0190  0.0197  619 ARG B CB  
20924 C CG  . ARG B  593 ? 0.2709 0.3208 0.2576 0.0389  0.0177  0.0214  619 ARG B CG  
20925 C CD  . ARG B  593 ? 0.2906 0.3392 0.2805 0.0372  0.0177  0.0197  619 ARG B CD  
20926 N NE  . ARG B  593 ? 0.2994 0.3460 0.2888 0.0395  0.0217  0.0205  619 ARG B NE  
20927 C CZ  . ARG B  593 ? 0.2880 0.3350 0.2830 0.0403  0.0245  0.0245  619 ARG B CZ  
20928 N NH1 . ARG B  593 ? 0.2659 0.3151 0.2674 0.0384  0.0235  0.0280  619 ARG B NH1 
20929 N NH2 . ARG B  593 ? 0.2613 0.3065 0.2555 0.0427  0.0284  0.0250  619 ARG B NH2 
20943 N N   . LEU B  594 ? 0.2425 0.2943 0.2012 0.0429  0.0154  0.0083  620 LEU B N   
20944 C CA  . LEU B  594 ? 0.2474 0.2997 0.1973 0.0449  0.0166  0.0060  620 LEU B CA  
20945 C C   . LEU B  594 ? 0.2512 0.2991 0.1996 0.0461  0.0211  0.0057  620 LEU B C   
20946 O O   . LEU B  594 ? 0.2576 0.3056 0.1991 0.0484  0.0233  0.0052  620 LEU B O   
20947 C CB  . LEU B  594 ? 0.2441 0.2987 0.1889 0.0428  0.0132  0.0007  620 LEU B CB  
20948 C CG  . LEU B  594 ? 0.2553 0.3155 0.1992 0.0429  0.0093  0.0010  620 LEU B CG  
20949 C CD1 . LEU B  594 ? 0.2556 0.3183 0.1976 0.0398  0.0058  -0.0041 620 LEU B CD1 
20950 C CD2 . LEU B  594 ? 0.2698 0.3332 0.2070 0.0464  0.0098  0.0030  620 LEU B CD2 
20962 N N   . ASP B  595 ? 0.2508 0.2955 0.2059 0.0450  0.0228  0.0066  621 ASP B N   
20963 C CA  . ASP B  595 ? 0.2624 0.3033 0.2172 0.0469  0.0277  0.0072  621 ASP B CA  
20964 C C   . ASP B  595 ? 0.2648 0.3069 0.2197 0.0501  0.0308  0.0121  621 ASP B C   
20965 O O   . ASP B  595 ? 0.2652 0.3055 0.2153 0.0526  0.0347  0.0119  621 ASP B O   
20966 C CB  . ASP B  595 ? 0.2719 0.3101 0.2350 0.0455  0.0287  0.0083  621 ASP B CB  
20967 C CG  . ASP B  595 ? 0.3119 0.3525 0.2841 0.0448  0.0277  0.0133  621 ASP B CG  
20968 O OD1 . ASP B  595 ? 0.2912 0.3348 0.2645 0.0433  0.0242  0.0139  621 ASP B OD1 
20969 O OD2 . ASP B  595 ? 0.3295 0.3692 0.3077 0.0456  0.0305  0.0165  621 ASP B OD2 
20974 N N   . ILE B  596 ? 0.2591 0.3038 0.2188 0.0500  0.0294  0.0162  622 ILE B N   
20975 C CA  . ILE B  596 ? 0.2689 0.3147 0.2289 0.0526  0.0322  0.0211  622 ILE B CA  
20976 C C   . ILE B  596 ? 0.2720 0.3198 0.2233 0.0547  0.0315  0.0207  622 ILE B C   
20977 O O   . ILE B  596 ? 0.2657 0.3131 0.2122 0.0574  0.0349  0.0222  622 ILE B O   
20978 C CB  . ILE B  596 ? 0.2824 0.3295 0.2512 0.0511  0.0312  0.0255  622 ILE B CB  
20979 C CG1 . ILE B  596 ? 0.2922 0.3383 0.2695 0.0495  0.0325  0.0267  622 ILE B CG1 
20980 C CG2 . ILE B  596 ? 0.2927 0.3406 0.2609 0.0534  0.0338  0.0303  622 ILE B CG2 
20981 C CD1 . ILE B  596 ? 0.3016 0.3494 0.2876 0.0472  0.0311  0.0304  622 ILE B CD1 
20993 N N   . LEU B  597 ? 0.2675 0.3178 0.2169 0.0535  0.0272  0.0191  623 LEU B N   
20994 C CA  . LEU B  597 ? 0.2730 0.3262 0.2145 0.0557  0.0261  0.0193  623 LEU B CA  
20995 C C   . LEU B  597 ? 0.2827 0.3359 0.2149 0.0571  0.0277  0.0158  623 LEU B C   
20996 O O   . LEU B  597 ? 0.2799 0.3346 0.2057 0.0599  0.0294  0.0177  623 LEU B O   
20997 C CB  . LEU B  597 ? 0.2700 0.3266 0.2114 0.0543  0.0211  0.0175  623 LEU B CB  
20998 C CG  . LEU B  597 ? 0.2757 0.3323 0.2251 0.0530  0.0195  0.0205  623 LEU B CG  
20999 C CD1 . LEU B  597 ? 0.2800 0.3390 0.2308 0.0506  0.0149  0.0173  623 LEU B CD1 
21000 C CD2 . LEU B  597 ? 0.2816 0.3388 0.2301 0.0558  0.0208  0.0255  623 LEU B CD2 
21012 N N   . TRP B  598 ? 0.2955 0.3466 0.2264 0.0550  0.0274  0.0108  624 TRP B N   
21013 C CA  . TRP B  598 ? 0.3138 0.3640 0.2356 0.0556  0.0291  0.0066  624 TRP B CA  
21014 C C   . TRP B  598 ? 0.3409 0.3860 0.2634 0.0568  0.0345  0.0067  624 TRP B C   
21015 O O   . TRP B  598 ? 0.3569 0.3992 0.2738 0.0563  0.0362  0.0021  624 TRP B O   
21016 C CB  . TRP B  598 ? 0.3083 0.3593 0.2270 0.0523  0.0255  0.0004  624 TRP B CB  
21017 C CG  . TRP B  598 ? 0.3057 0.3628 0.2216 0.0517  0.0205  -0.0003 624 TRP B CG  
21018 C CD1 . TRP B  598 ? 0.3186 0.3802 0.2302 0.0545  0.0196  0.0029  624 TRP B CD1 
21019 C CD2 . TRP B  598 ? 0.3045 0.3640 0.2203 0.0484  0.0162  -0.0047 624 TRP B CD2 
21020 N NE1 . TRP B  598 ? 0.3194 0.3866 0.2293 0.0533  0.0148  0.0011  624 TRP B NE1 
21021 C CE2 . TRP B  598 ? 0.3161 0.3824 0.2283 0.0494  0.0127  -0.0039 624 TRP B CE2 
21022 C CE3 . TRP B  598 ? 0.3070 0.3638 0.2255 0.0446  0.0152  -0.0092 624 TRP B CE3 
21023 C CZ2 . TRP B  598 ? 0.3180 0.3890 0.2303 0.0467  0.0080  -0.0071 624 TRP B CZ2 
21024 C CZ3 . TRP B  598 ? 0.3177 0.3786 0.2359 0.0417  0.0106  -0.0125 624 TRP B CZ3 
21025 C CH2 . TRP B  598 ? 0.3222 0.3904 0.2371 0.0427  0.0071  -0.0117 624 TRP B CH2 
21036 N N   . ASN B  599 ? 0.3436 0.3878 0.2727 0.0585  0.0375  0.0120  625 ASN B N   
21037 C CA  . ASN B  599 ? 0.3553 0.3957 0.2857 0.0602  0.0431  0.0129  625 ASN B CA  
21038 C C   . ASN B  599 ? 0.3616 0.4015 0.2812 0.0627  0.0463  0.0111  625 ASN B C   
21039 O O   . ASN B  599 ? 0.3588 0.4021 0.2724 0.0641  0.0452  0.0125  625 ASN B O   
21040 C CB  . ASN B  599 ? 0.3766 0.4180 0.3155 0.0615  0.0454  0.0194  625 ASN B CB  
21041 C CG  . ASN B  599 ? 0.4358 0.4746 0.3766 0.0637  0.0512  0.0212  625 ASN B CG  
21042 O OD1 . ASN B  599 ? 0.4578 0.4968 0.3935 0.0665  0.0549  0.0229  625 ASN B OD1 
21043 N ND2 . ASN B  599 ? 0.4366 0.4732 0.3847 0.0628  0.0523  0.0209  625 ASN B ND2 
21050 N N   . ASP B  600 ? 0.3717 0.4071 0.2882 0.0631  0.0501  0.0076  626 ASP B N   
21051 C CA  . ASP B  600 ? 0.3872 0.4215 0.2926 0.0650  0.0534  0.0049  626 ASP B CA  
21052 C C   . ASP B  600 ? 0.3784 0.4152 0.2807 0.0685  0.0565  0.0098  626 ASP B C   
21053 O O   . ASP B  600 ? 0.3816 0.4192 0.2733 0.0698  0.0578  0.0080  626 ASP B O   
21054 C CB  . ASP B  600 ? 0.4355 0.4634 0.3405 0.0656  0.0586  0.0018  626 ASP B CB  
21055 C CG  . ASP B  600 ? 0.5421 0.5660 0.4465 0.0624  0.0567  -0.0043 626 ASP B CG  
21056 O OD1 . ASP B  600 ? 0.5678 0.5942 0.4685 0.0595  0.0516  -0.0077 626 ASP B OD1 
21057 O OD2 . ASP B  600 ? 0.5867 0.6051 0.4948 0.0628  0.0605  -0.0055 626 ASP B OD2 
21062 N N   . ASP B  601 ? 0.3651 0.4030 0.2764 0.0697  0.0582  0.0161  627 ASP B N   
21063 C CA  . ASP B  601 ? 0.3580 0.3978 0.2674 0.0728  0.0617  0.0213  627 ASP B CA  
21064 C C   . ASP B  601 ? 0.3468 0.3910 0.2559 0.0730  0.0580  0.0251  627 ASP B C   
21065 O O   . ASP B  601 ? 0.3401 0.3856 0.2493 0.0752  0.0608  0.0303  627 ASP B O   
21066 C CB  . ASP B  601 ? 0.3673 0.4060 0.2869 0.0740  0.0661  0.0260  627 ASP B CB  
21067 C CG  . ASP B  601 ? 0.4147 0.4491 0.3362 0.0744  0.0701  0.0230  627 ASP B CG  
21068 O OD1 . ASP B  601 ? 0.4049 0.4367 0.3176 0.0760  0.0735  0.0195  627 ASP B OD1 
21069 O OD2 . ASP B  601 ? 0.4618 0.4955 0.3937 0.0733  0.0699  0.0244  627 ASP B OD2 
21074 N N   . ASP B  602 ? 0.3381 0.3843 0.2467 0.0707  0.0522  0.0229  628 ASP B N   
21075 C CA  . ASP B  602 ? 0.3364 0.3864 0.2450 0.0712  0.0489  0.0265  628 ASP B CA  
21076 C C   . ASP B  602 ? 0.3459 0.3993 0.2454 0.0707  0.0445  0.0226  628 ASP B C   
21077 O O   . ASP B  602 ? 0.3544 0.4078 0.2541 0.0680  0.0410  0.0177  628 ASP B O   
21078 C CB  . ASP B  602 ? 0.3371 0.3870 0.2569 0.0688  0.0459  0.0286  628 ASP B CB  
21079 C CG  . ASP B  602 ? 0.3637 0.4161 0.2852 0.0695  0.0436  0.0330  628 ASP B CG  
21080 O OD1 . ASP B  602 ? 0.3523 0.4067 0.2665 0.0721  0.0442  0.0351  628 ASP B OD1 
21081 O OD2 . ASP B  602 ? 0.4103 0.4623 0.3401 0.0674  0.0415  0.0345  628 ASP B OD2 
21086 N N   . ASN B  603 ? 0.3487 0.4053 0.2405 0.0733  0.0446  0.0251  629 ASN B N   
21087 C CA  . ASN B  603 ? 0.3606 0.4220 0.2439 0.0732  0.0402  0.0222  629 ASN B CA  
21088 C C   . ASN B  603 ? 0.3416 0.4068 0.2286 0.0735  0.0359  0.0257  629 ASN B C   
21089 O O   . ASN B  603 ? 0.3375 0.4078 0.2187 0.0737  0.0319  0.0240  629 ASN B O   
21090 C CB  . ASN B  603 ? 0.3997 0.4633 0.2713 0.0761  0.0427  0.0229  629 ASN B CB  
21091 C CG  . ASN B  603 ? 0.4909 0.5510 0.3564 0.0757  0.0467  0.0183  629 ASN B CG  
21092 O OD1 . ASN B  603 ? 0.5205 0.5774 0.3882 0.0729  0.0464  0.0130  629 ASN B OD1 
21093 N ND2 . ASN B  603 ? 0.5178 0.5783 0.3753 0.0785  0.0508  0.0202  629 ASN B ND2 
21100 N N   . ARG B  604 ? 0.3201 0.3832 0.2166 0.0737  0.0367  0.0305  630 ARG B N   
21101 C CA  . ARG B  604 ? 0.3126 0.3783 0.2118 0.0746  0.0336  0.0342  630 ARG B CA  
21102 C C   . ARG B  604 ? 0.3072 0.3759 0.2086 0.0723  0.0279  0.0304  630 ARG B C   
21103 O O   . ARG B  604 ? 0.3118 0.3847 0.2112 0.0739  0.0251  0.0324  630 ARG B O   
21104 C CB  . ARG B  604 ? 0.3217 0.3836 0.2301 0.0747  0.0360  0.0396  630 ARG B CB  
21105 C CG  . ARG B  604 ? 0.3423 0.4023 0.2486 0.0775  0.0415  0.0447  630 ARG B CG  
21106 C CD  . ARG B  604 ? 0.3587 0.4150 0.2749 0.0766  0.0441  0.0493  630 ARG B CD  
21107 N NE  . ARG B  604 ? 0.3610 0.4151 0.2852 0.0732  0.0441  0.0464  630 ARG B NE  
21108 C CZ  . ARG B  604 ? 0.3626 0.4147 0.2966 0.0709  0.0440  0.0482  630 ARG B CZ  
21109 N NH1 . ARG B  604 ? 0.3565 0.4075 0.2938 0.0712  0.0443  0.0529  630 ARG B NH1 
21110 N NH2 . ARG B  604 ? 0.3163 0.3672 0.2567 0.0680  0.0435  0.0455  630 ARG B NH2 
21124 N N   . TYR B  605 ? 0.3001 0.3671 0.2056 0.0687  0.0266  0.0255  631 TYR B N   
21125 C CA  . TYR B  605 ? 0.3002 0.3699 0.2085 0.0661  0.0215  0.0219  631 TYR B CA  
21126 C C   . TYR B  605 ? 0.3099 0.3825 0.2114 0.0641  0.0191  0.0155  631 TYR B C   
21127 O O   . TYR B  605 ? 0.3008 0.3750 0.2050 0.0612  0.0155  0.0118  631 TYR B O   
21128 C CB  . TYR B  605 ? 0.2849 0.3505 0.2035 0.0630  0.0215  0.0213  631 TYR B CB  
21129 C CG  . TYR B  605 ? 0.2863 0.3492 0.2119 0.0641  0.0236  0.0271  631 TYR B CG  
21130 C CD1 . TYR B  605 ? 0.2881 0.3523 0.2174 0.0644  0.0213  0.0297  631 TYR B CD1 
21131 C CD2 . TYR B  605 ? 0.2940 0.3530 0.2222 0.0647  0.0282  0.0300  631 TYR B CD2 
21132 C CE1 . TYR B  605 ? 0.2949 0.3559 0.2302 0.0648  0.0235  0.0346  631 TYR B CE1 
21133 C CE2 . TYR B  605 ? 0.3000 0.3569 0.2347 0.0650  0.0301  0.0351  631 TYR B CE2 
21134 C CZ  . TYR B  605 ? 0.3046 0.3621 0.2426 0.0649  0.0278  0.0372  631 TYR B CZ  
21135 O OH  . TYR B  605 ? 0.3120 0.3666 0.2558 0.0648  0.0299  0.0419  631 TYR B OH  
21145 N N   . ILE B  606 ? 0.3308 0.4044 0.2229 0.0656  0.0210  0.0142  632 ILE B N   
21146 C CA  . ILE B  606 ? 0.3545 0.4302 0.2390 0.0633  0.0193  0.0077  632 ILE B CA  
21147 C C   . ILE B  606 ? 0.3485 0.4320 0.2302 0.0623  0.0136  0.0057  632 ILE B C   
21148 O O   . ILE B  606 ? 0.3548 0.4400 0.2332 0.0590  0.0113  -0.0003 632 ILE B O   
21149 C CB  . ILE B  606 ? 0.3797 0.4544 0.2541 0.0652  0.0232  0.0070  632 ILE B CB  
21150 C CG1 . ILE B  606 ? 0.4139 0.4861 0.2830 0.0620  0.0237  -0.0005 632 ILE B CG1 
21151 C CG2 . ILE B  606 ? 0.3857 0.4673 0.2516 0.0682  0.0216  0.0097  632 ILE B CG2 
21152 C CD1 . ILE B  606 ? 0.4405 0.5043 0.3160 0.0606  0.0279  -0.0021 632 ILE B CD1 
21164 N N   . SER B  607 ? 0.3318 0.4200 0.2151 0.0651  0.0115  0.0107  633 SER B N   
21165 C CA  . SER B  607 ? 0.3259 0.4223 0.2079 0.0648  0.0062  0.0098  633 SER B CA  
21166 C C   . SER B  607 ? 0.3132 0.4095 0.2053 0.0648  0.0043  0.0126  633 SER B C   
21167 O O   . SER B  607 ? 0.3173 0.4200 0.2096 0.0666  0.0011  0.0147  633 SER B O   
21168 C CB  . SER B  607 ? 0.3507 0.4535 0.2248 0.0690  0.0056  0.0137  633 SER B CB  
21169 O OG  . SER B  607 ? 0.3869 0.4898 0.2510 0.0691  0.0077  0.0114  633 SER B OG  
21175 N N   . ILE B  608 ? 0.2886 0.3781 0.1889 0.0628  0.0061  0.0125  634 ILE B N   
21176 C CA  . ILE B  608 ? 0.2772 0.3657 0.1867 0.0625  0.0048  0.0149  634 ILE B CA  
21177 C C   . ILE B  608 ? 0.2747 0.3699 0.1858 0.0611  -0.0002 0.0125  634 ILE B C   
21178 O O   . ILE B  608 ? 0.2832 0.3802 0.1987 0.0630  -0.0014 0.0160  634 ILE B O   
21179 C CB  . ILE B  608 ? 0.2851 0.3662 0.2024 0.0596  0.0071  0.0140  634 ILE B CB  
21180 C CG1 . ILE B  608 ? 0.2912 0.3708 0.2173 0.0594  0.0063  0.0171  634 ILE B CG1 
21181 C CG2 . ILE B  608 ? 0.2926 0.3727 0.2100 0.0553  0.0057  0.0075  634 ILE B CG2 
21182 C CD1 . ILE B  608 ? 0.3061 0.3790 0.2396 0.0573  0.0089  0.0178  634 ILE B CD1 
21194 N N   . PHE B  609 ? 0.2660 0.3648 0.1740 0.0579  -0.0028 0.0067  635 PHE B N   
21195 C CA  . PHE B  609 ? 0.2739 0.3798 0.1838 0.0561  -0.0075 0.0042  635 PHE B CA  
21196 C C   . PHE B  609 ? 0.2846 0.4002 0.1866 0.0573  -0.0107 0.0032  635 PHE B C   
21197 O O   . PHE B  609 ? 0.2857 0.4087 0.1895 0.0563  -0.0146 0.0018  635 PHE B O   
21198 C CB  . PHE B  609 ? 0.2700 0.3734 0.1830 0.0507  -0.0086 -0.0019 635 PHE B CB  
21199 C CG  . PHE B  609 ? 0.2780 0.3727 0.1983 0.0491  -0.0059 -0.0012 635 PHE B CG  
21200 C CD1 . PHE B  609 ? 0.2798 0.3724 0.2071 0.0507  -0.0053 0.0032  635 PHE B CD1 
21201 C CD2 . PHE B  609 ? 0.2883 0.3771 0.2084 0.0461  -0.0038 -0.0048 635 PHE B CD2 
21202 C CE1 . PHE B  609 ? 0.2973 0.3829 0.2312 0.0489  -0.0031 0.0039  635 PHE B CE1 
21203 C CE2 . PHE B  609 ? 0.2933 0.3751 0.2203 0.0450  -0.0015 -0.0036 635 PHE B CE2 
21204 C CZ  . PHE B  609 ? 0.2960 0.3768 0.2298 0.0461  -0.0014 0.0006  635 PHE B CZ  
21214 N N   . LYS B  610 ? 0.2948 0.4113 0.1884 0.0595  -0.0090 0.0042  636 LYS B N   
21215 C CA  . LYS B  610 ? 0.3113 0.4375 0.1965 0.0604  -0.0121 0.0032  636 LYS B CA  
21216 C C   . LYS B  610 ? 0.3303 0.4655 0.2176 0.0641  -0.0153 0.0078  636 LYS B C   
21217 O O   . LYS B  610 ? 0.3341 0.4792 0.2185 0.0631  -0.0195 0.0056  636 LYS B O   
21218 C CB  . LYS B  610 ? 0.3325 0.4572 0.2085 0.0629  -0.0090 0.0047  636 LYS B CB  
21219 C CG  . LYS B  610 ? 0.3767 0.5113 0.2427 0.0628  -0.0122 0.0026  636 LYS B CG  
21220 C CD  . LYS B  610 ? 0.4328 0.5646 0.2888 0.0638  -0.0088 0.0021  636 LYS B CD  
21221 C CE  . LYS B  610 ? 0.4956 0.6370 0.3411 0.0625  -0.0121 -0.0014 636 LYS B CE  
21222 N NZ  . LYS B  610 ? 0.5495 0.6875 0.3846 0.0629  -0.0085 -0.0028 636 LYS B NZ  
21236 N N   . GLY B  611 ? 0.3338 0.4655 0.2261 0.0682  -0.0132 0.0142  637 GLY B N   
21237 C CA  . GLY B  611 ? 0.3319 0.4702 0.2268 0.0724  -0.0153 0.0193  637 GLY B CA  
21238 C C   . GLY B  611 ? 0.3182 0.4605 0.2209 0.0705  -0.0186 0.0174  637 GLY B C   
21239 O O   . GLY B  611 ? 0.3194 0.4680 0.2246 0.0741  -0.0204 0.0212  637 GLY B O   
21243 N N   . LEU B  612 ? 0.3026 0.4414 0.2091 0.0651  -0.0191 0.0116  638 LEU B N   
21244 C CA  . LEU B  612 ? 0.2911 0.4341 0.2045 0.0626  -0.0222 0.0091  638 LEU B CA  
21245 C C   . LEU B  612 ? 0.2931 0.4474 0.2015 0.0603  -0.0266 0.0049  638 LEU B C   
21246 O O   . LEU B  612 ? 0.2892 0.4436 0.1970 0.0549  -0.0280 -0.0013 638 LEU B O   
21247 C CB  . LEU B  612 ? 0.2838 0.4179 0.2030 0.0579  -0.0206 0.0054  638 LEU B CB  
21248 C CG  . LEU B  612 ? 0.3009 0.4243 0.2244 0.0596  -0.0163 0.0093  638 LEU B CG  
21249 C CD1 . LEU B  612 ? 0.3063 0.4220 0.2348 0.0549  -0.0150 0.0056  638 LEU B CD1 
21250 C CD2 . LEU B  612 ? 0.3063 0.4301 0.2351 0.0636  -0.0159 0.0146  638 LEU B CD2 
21262 N N   . LYS B  613 ? 0.3014 0.4653 0.2059 0.0645  -0.0287 0.0086  639 LYS B N   
21263 C CA  . LYS B  613 ? 0.3118 0.4879 0.2101 0.0630  -0.0329 0.0057  639 LYS B CA  
21264 C C   . LYS B  613 ? 0.3089 0.4931 0.2119 0.0586  -0.0371 0.0010  639 LYS B C   
21265 O O   . LYS B  613 ? 0.3073 0.4991 0.2051 0.0549  -0.0401 -0.0037 639 LYS B O   
21266 C CB  . LYS B  613 ? 0.3380 0.5231 0.2322 0.0693  -0.0342 0.0121  639 LYS B CB  
21267 C CG  . LYS B  613 ? 0.4144 0.5928 0.3021 0.0729  -0.0303 0.0161  639 LYS B CG  
21268 C CD  . LYS B  613 ? 0.5052 0.6930 0.3870 0.0786  -0.0316 0.0220  639 LYS B CD  
21269 C CE  . LYS B  613 ? 0.5699 0.7510 0.4441 0.0812  -0.0277 0.0251  639 LYS B CE  
21270 N NZ  . LYS B  613 ? 0.6037 0.7941 0.4713 0.0867  -0.0290 0.0311  639 LYS B NZ  
21284 N N   . ASN B  614 ? 0.3040 0.4865 0.2162 0.0586  -0.0370 0.0019  640 ASN B N   
21285 C CA  . ASN B  614 ? 0.2979 0.4881 0.2151 0.0546  -0.0406 -0.0022 640 ASN B CA  
21286 C C   . ASN B  614 ? 0.2886 0.4697 0.2100 0.0484  -0.0392 -0.0077 640 ASN B C   
21287 O O   . ASN B  614 ? 0.2813 0.4671 0.2079 0.0450  -0.0415 -0.0108 640 ASN B O   
21288 C CB  . ASN B  614 ? 0.3192 0.5148 0.2440 0.0593  -0.0414 0.0031  640 ASN B CB  
21289 C CG  . ASN B  614 ? 0.3507 0.5595 0.2794 0.0576  -0.0457 0.0011  640 ASN B CG  
21290 O OD1 . ASN B  614 ? 0.3437 0.5631 0.2675 0.0556  -0.0492 -0.0014 640 ASN B OD1 
21291 N ND2 . ASN B  614 ? 0.3738 0.5841 0.3110 0.0590  -0.0457 0.0029  640 ASN B ND2 
21298 N N   . LEU B  615 ? 0.2777 0.4463 0.1971 0.0472  -0.0354 -0.0087 641 LEU B N   
21299 C CA  . LEU B  615 ? 0.2812 0.4405 0.2049 0.0424  -0.0337 -0.0127 641 LEU B CA  
21300 C C   . LEU B  615 ? 0.2875 0.4492 0.2091 0.0358  -0.0358 -0.0199 641 LEU B C   
21301 O O   . LEU B  615 ? 0.2869 0.4500 0.2007 0.0340  -0.0362 -0.0230 641 LEU B O   
21302 C CB  . LEU B  615 ? 0.2863 0.4327 0.2086 0.0433  -0.0291 -0.0113 641 LEU B CB  
21303 C CG  . LEU B  615 ? 0.2976 0.4341 0.2270 0.0411  -0.0267 -0.0118 641 LEU B CG  
21304 C CD1 . LEU B  615 ? 0.2966 0.4323 0.2329 0.0447  -0.0260 -0.0067 641 LEU B CD1 
21305 C CD2 . LEU B  615 ? 0.3069 0.4327 0.2340 0.0407  -0.0227 -0.0119 641 LEU B CD2 
21317 N N   . THR B  616 ? 0.2900 0.4514 0.2182 0.0319  -0.0367 -0.0226 642 THR B N   
21318 C CA  . THR B  616 ? 0.2986 0.4609 0.2258 0.0252  -0.0382 -0.0293 642 THR B CA  
21319 C C   . THR B  616 ? 0.2897 0.4395 0.2203 0.0217  -0.0352 -0.0316 642 THR B C   
21320 O O   . THR B  616 ? 0.2998 0.4459 0.2273 0.0168  -0.0348 -0.0369 642 THR B O   
21321 C CB  . THR B  616 ? 0.3204 0.4952 0.2514 0.0230  -0.0425 -0.0310 642 THR B CB  
21322 O OG1 . THR B  616 ? 0.3416 0.5159 0.2814 0.0246  -0.0421 -0.0280 642 THR B OG1 
21323 C CG2 . THR B  616 ? 0.3284 0.5165 0.2554 0.0261  -0.0458 -0.0289 642 THR B CG2 
21331 N N   . ARG B  617 ? 0.2800 0.4233 0.2169 0.0241  -0.0329 -0.0278 643 ARG B N   
21332 C CA  . ARG B  617 ? 0.2860 0.4185 0.2265 0.0210  -0.0303 -0.0293 643 ARG B CA  
21333 C C   . ARG B  617 ? 0.2788 0.4021 0.2195 0.0248  -0.0265 -0.0251 643 ARG B C   
21334 O O   . ARG B  617 ? 0.2722 0.3963 0.2158 0.0291  -0.0260 -0.0202 643 ARG B O   
21335 C CB  . ARG B  617 ? 0.3100 0.4443 0.2586 0.0190  -0.0315 -0.0293 643 ARG B CB  
21336 C CG  . ARG B  617 ? 0.3889 0.5131 0.3410 0.0156  -0.0291 -0.0308 643 ARG B CG  
21337 C CD  . ARG B  617 ? 0.4425 0.5687 0.4016 0.0127  -0.0303 -0.0316 643 ARG B CD  
21338 N NE  . ARG B  617 ? 0.4844 0.6014 0.4458 0.0090  -0.0283 -0.0332 643 ARG B NE  
21339 C CZ  . ARG B  617 ? 0.5178 0.6266 0.4820 0.0105  -0.0256 -0.0302 643 ARG B CZ  
21340 N NH1 . ARG B  617 ? 0.5006 0.6083 0.4655 0.0152  -0.0245 -0.0257 643 ARG B NH1 
21341 N NH2 . ARG B  617 ? 0.5264 0.6280 0.4927 0.0071  -0.0240 -0.0316 643 ARG B NH2 
21355 N N   . LEU B  618 ? 0.2702 0.3847 0.2083 0.0231  -0.0237 -0.0270 644 LEU B N   
21356 C CA  . LEU B  618 ? 0.2664 0.3726 0.2050 0.0262  -0.0200 -0.0232 644 LEU B CA  
21357 C C   . LEU B  618 ? 0.2648 0.3618 0.2071 0.0231  -0.0176 -0.0247 644 LEU B C   
21358 O O   . LEU B  618 ? 0.2756 0.3699 0.2153 0.0195  -0.0172 -0.0292 644 LEU B O   
21359 C CB  . LEU B  618 ? 0.2659 0.3717 0.1965 0.0286  -0.0185 -0.0230 644 LEU B CB  
21360 C CG  . LEU B  618 ? 0.2880 0.3857 0.2183 0.0318  -0.0143 -0.0193 644 LEU B CG  
21361 C CD1 . LEU B  618 ? 0.2971 0.3949 0.2324 0.0358  -0.0137 -0.0132 644 LEU B CD1 
21362 C CD2 . LEU B  618 ? 0.2911 0.3891 0.2127 0.0338  -0.0128 -0.0198 644 LEU B CD2 
21374 N N   . ASP B  619 ? 0.2515 0.3437 0.1996 0.0245  -0.0159 -0.0208 645 ASP B N   
21375 C CA  . ASP B  619 ? 0.2511 0.3355 0.2031 0.0221  -0.0137 -0.0214 645 ASP B CA  
21376 C C   . ASP B  619 ? 0.2613 0.3394 0.2135 0.0251  -0.0101 -0.0177 645 ASP B C   
21377 O O   . ASP B  619 ? 0.2604 0.3383 0.2158 0.0277  -0.0094 -0.0133 645 ASP B O   
21378 C CB  . ASP B  619 ? 0.2602 0.3453 0.2194 0.0200  -0.0151 -0.0206 645 ASP B CB  
21379 C CG  . ASP B  619 ? 0.3100 0.3882 0.2735 0.0173  -0.0134 -0.0209 645 ASP B CG  
21380 O OD1 . ASP B  619 ? 0.3096 0.3819 0.2712 0.0174  -0.0108 -0.0212 645 ASP B OD1 
21381 O OD2 . ASP B  619 ? 0.3509 0.4297 0.3195 0.0152  -0.0146 -0.0206 645 ASP B OD2 
21386 N N   . LEU B  620 ? 0.2620 0.3350 0.2106 0.0246  -0.0075 -0.0196 646 LEU B N   
21387 C CA  . LEU B  620 ? 0.2559 0.3230 0.2046 0.0272  -0.0036 -0.0165 646 LEU B CA  
21388 C C   . LEU B  620 ? 0.2637 0.3242 0.2174 0.0252  -0.0015 -0.0165 646 LEU B C   
21389 O O   . LEU B  620 ? 0.2696 0.3251 0.2228 0.0268  0.0020  -0.0151 646 LEU B O   
21390 C CB  . LEU B  620 ? 0.2562 0.3225 0.1968 0.0287  -0.0017 -0.0186 646 LEU B CB  
21391 C CG  . LEU B  620 ? 0.2798 0.3531 0.2140 0.0305  -0.0039 -0.0189 646 LEU B CG  
21392 C CD1 . LEU B  620 ? 0.2876 0.3592 0.2135 0.0319  -0.0014 -0.0206 646 LEU B CD1 
21393 C CD2 . LEU B  620 ? 0.2905 0.3674 0.2276 0.0341  -0.0046 -0.0135 646 LEU B CD2 
21405 N N   . SER B  621 ? 0.2608 0.3215 0.2193 0.0219  -0.0034 -0.0177 647 SER B N   
21406 C CA  . SER B  621 ? 0.2618 0.3167 0.2250 0.0201  -0.0016 -0.0172 647 SER B CA  
21407 C C   . SER B  621 ? 0.2594 0.3123 0.2281 0.0222  0.0002  -0.0119 647 SER B C   
21408 O O   . SER B  621 ? 0.2554 0.3113 0.2251 0.0243  -0.0005 -0.0089 647 SER B O   
21409 C CB  . SER B  621 ? 0.2691 0.3254 0.2358 0.0161  -0.0042 -0.0193 647 SER B CB  
21410 O OG  . SER B  621 ? 0.2860 0.3463 0.2572 0.0162  -0.0064 -0.0167 647 SER B OG  
21416 N N   . LEU B  622 ? 0.2534 0.3013 0.2256 0.0217  0.0025  -0.0107 648 LEU B N   
21417 C CA  . LEU B  622 ? 0.2549 0.3018 0.2331 0.0231  0.0040  -0.0057 648 LEU B CA  
21418 C C   . LEU B  622 ? 0.2494 0.2972 0.2263 0.0267  0.0059  -0.0024 648 LEU B C   
21419 O O   . LEU B  622 ? 0.2546 0.3042 0.2355 0.0273  0.0055  0.0012  648 LEU B O   
21420 C CB  . LEU B  622 ? 0.2563 0.3059 0.2400 0.0207  0.0011  -0.0042 648 LEU B CB  
21421 C CG  . LEU B  622 ? 0.2910 0.3396 0.2771 0.0171  -0.0003 -0.0063 648 LEU B CG  
21422 C CD1 . LEU B  622 ? 0.3019 0.3541 0.2922 0.0150  -0.0032 -0.0051 648 LEU B CD1 
21423 C CD2 . LEU B  622 ? 0.3025 0.3463 0.2919 0.0169  0.0023  -0.0047 648 LEU B CD2 
21435 N N   . ASN B  623 ? 0.2455 0.2918 0.2167 0.0289  0.0081  -0.0038 649 ASN B N   
21436 C CA  . ASN B  623 ? 0.2521 0.2991 0.2215 0.0324  0.0104  -0.0006 649 ASN B CA  
21437 C C   . ASN B  623 ? 0.2631 0.3059 0.2331 0.0345  0.0149  0.0010  649 ASN B C   
21438 O O   . ASN B  623 ? 0.2661 0.3090 0.2332 0.0375  0.0174  0.0030  649 ASN B O   
21439 C CB  . ASN B  623 ? 0.2533 0.3034 0.2151 0.0339  0.0092  -0.0027 649 ASN B CB  
21440 C CG  . ASN B  623 ? 0.2664 0.3213 0.2291 0.0343  0.0063  -0.0009 649 ASN B CG  
21441 O OD1 . ASN B  623 ? 0.2600 0.3160 0.2222 0.0370  0.0075  0.0027  649 ASN B OD1 
21442 N ND2 . ASN B  623 ? 0.2599 0.3174 0.2241 0.0317  0.0029  -0.0031 649 ASN B ND2 
21449 N N   . ARG B  624 ? 0.2608 0.2998 0.2343 0.0332  0.0162  0.0004  650 ARG B N   
21450 C CA  . ARG B  624 ? 0.2721 0.3071 0.2473 0.0353  0.0206  0.0021  650 ARG B CA  
21451 C C   . ARG B  624 ? 0.2838 0.3161 0.2512 0.0375  0.0238  -0.0007 650 ARG B C   
21452 O O   . ARG B  624 ? 0.2893 0.3194 0.2572 0.0403  0.0280  0.0016  650 ARG B O   
21453 C CB  . ARG B  624 ? 0.2838 0.3210 0.2656 0.0370  0.0221  0.0080  650 ARG B CB  
21454 C CG  . ARG B  624 ? 0.3211 0.3615 0.3094 0.0344  0.0186  0.0104  650 ARG B CG  
21455 C CD  . ARG B  624 ? 0.3704 0.4125 0.3662 0.0351  0.0202  0.0158  650 ARG B CD  
21456 N NE  . ARG B  624 ? 0.4301 0.4755 0.4302 0.0326  0.0169  0.0177  650 ARG B NE  
21457 C CZ  . ARG B  624 ? 0.4677 0.5155 0.4744 0.0320  0.0172  0.0220  650 ARG B CZ  
21458 N NH1 . ARG B  624 ? 0.4569 0.5048 0.4674 0.0339  0.0205  0.0254  650 ARG B NH1 
21459 N NH2 . ARG B  624 ? 0.4631 0.5133 0.4727 0.0293  0.0143  0.0229  650 ARG B NH2 
21473 N N   . LEU B  625 ? 0.2881 0.3209 0.2481 0.0362  0.0220  -0.0055 651 LEU B N   
21474 C CA  . LEU B  625 ? 0.2973 0.3281 0.2486 0.0379  0.0246  -0.0086 651 LEU B CA  
21475 C C   . LEU B  625 ? 0.3159 0.3397 0.2657 0.0379  0.0285  -0.0115 651 LEU B C   
21476 O O   . LEU B  625 ? 0.3089 0.3297 0.2598 0.0350  0.0276  -0.0144 651 LEU B O   
21477 C CB  . LEU B  625 ? 0.2974 0.3318 0.2414 0.0360  0.0209  -0.0130 651 LEU B CB  
21478 C CG  . LEU B  625 ? 0.3122 0.3533 0.2554 0.0374  0.0180  -0.0103 651 LEU B CG  
21479 C CD1 . LEU B  625 ? 0.3141 0.3599 0.2533 0.0349  0.0135  -0.0140 651 LEU B CD1 
21480 C CD2 . LEU B  625 ? 0.3228 0.3644 0.2602 0.0410  0.0209  -0.0085 651 LEU B CD2 
21492 N N   . LYS B  626 ? 0.3350 0.3558 0.2821 0.0412  0.0333  -0.0105 652 LYS B N   
21493 C CA  . LYS B  626 ? 0.3632 0.3766 0.3077 0.0419  0.0380  -0.0134 652 LYS B CA  
21494 C C   . LYS B  626 ? 0.3885 0.4001 0.3214 0.0411  0.0387  -0.0195 652 LYS B C   
21495 O O   . LYS B  626 ? 0.3995 0.4048 0.3284 0.0396  0.0409  -0.0243 652 LYS B O   
21496 C CB  . LYS B  626 ? 0.3958 0.4072 0.3448 0.0460  0.0432  -0.0087 652 LYS B CB  
21497 C CG  . LYS B  626 ? 0.4629 0.4759 0.4234 0.0461  0.0426  -0.0033 652 LYS B CG  
21498 C CD  . LYS B  626 ? 0.5415 0.5534 0.5072 0.0500  0.0477  0.0015  652 LYS B CD  
21499 C CE  . LYS B  626 ? 0.6072 0.6215 0.5841 0.0498  0.0467  0.0067  652 LYS B CE  
21500 N NZ  . LYS B  626 ? 0.6575 0.6729 0.6404 0.0536  0.0513  0.0120  652 LYS B NZ  
21514 N N   . HIS B  627 ? 0.3980 0.4150 0.3253 0.0421  0.0371  -0.0193 653 HIS B N   
21515 C CA  . HIS B  627 ? 0.4227 0.4401 0.3387 0.0410  0.0366  -0.0247 653 HIS B CA  
21516 C C   . HIS B  627 ? 0.4214 0.4472 0.3345 0.0418  0.0328  -0.0226 653 HIS B C   
21517 O O   . HIS B  627 ? 0.4334 0.4626 0.3520 0.0442  0.0324  -0.0168 653 HIS B O   
21518 C CB  . HIS B  627 ? 0.4574 0.4693 0.3671 0.0437  0.0427  -0.0263 653 HIS B CB  
21519 C CG  . HIS B  627 ? 0.5179 0.5321 0.4294 0.0482  0.0457  -0.0206 653 HIS B CG  
21520 N ND1 . HIS B  627 ? 0.5526 0.5656 0.4738 0.0506  0.0483  -0.0151 653 HIS B ND1 
21521 C CD2 . HIS B  627 ? 0.5466 0.5649 0.4516 0.0504  0.0461  -0.0194 653 HIS B CD2 
21522 C CE1 . HIS B  627 ? 0.5645 0.5804 0.4849 0.0540  0.0505  -0.0109 653 HIS B CE1 
21523 N NE2 . HIS B  627 ? 0.5664 0.5853 0.4770 0.0541  0.0493  -0.0132 653 HIS B NE2 
21531 N N   . ILE B  628 ? 0.4018 0.4311 0.3067 0.0398  0.0298  -0.0271 654 ILE B N   
21532 C CA  . ILE B  628 ? 0.3852 0.4227 0.2868 0.0409  0.0263  -0.0250 654 ILE B CA  
21533 C C   . ILE B  628 ? 0.3874 0.4249 0.2784 0.0430  0.0292  -0.0266 654 ILE B C   
21534 O O   . ILE B  628 ? 0.3990 0.4335 0.2824 0.0408  0.0302  -0.0326 654 ILE B O   
21535 C CB  . ILE B  628 ? 0.3776 0.4208 0.2779 0.0372  0.0204  -0.0283 654 ILE B CB  
21536 C CG1 . ILE B  628 ? 0.3825 0.4258 0.2932 0.0352  0.0178  -0.0264 654 ILE B CG1 
21537 C CG2 . ILE B  628 ? 0.3734 0.4253 0.2692 0.0391  0.0172  -0.0261 654 ILE B CG2 
21538 C CD1 . ILE B  628 ? 0.3947 0.4413 0.3052 0.0309  0.0134  -0.0307 654 ILE B CD1 
21550 N N   . PRO B  629 ? 0.3772 0.4179 0.2668 0.0470  0.0306  -0.0216 655 PRO B N   
21551 C CA  . PRO B  629 ? 0.3730 0.4141 0.2515 0.0488  0.0332  -0.0233 655 PRO B CA  
21552 C C   . PRO B  629 ? 0.3696 0.4159 0.2388 0.0460  0.0290  -0.0285 655 PRO B C   
21553 O O   . PRO B  629 ? 0.3633 0.4161 0.2350 0.0445  0.0238  -0.0279 655 PRO B O   
21554 C CB  . PRO B  629 ? 0.3794 0.4245 0.2594 0.0531  0.0341  -0.0162 655 PRO B CB  
21555 C CG  . PRO B  629 ? 0.3826 0.4266 0.2748 0.0536  0.0339  -0.0113 655 PRO B CG  
21556 C CD  . PRO B  629 ? 0.3675 0.4113 0.2648 0.0496  0.0299  -0.0145 655 PRO B CD  
21564 N N   . ASN B  630 ? 0.3724 0.4162 0.2312 0.0450  0.0314  -0.0339 656 ASN B N   
21565 C CA  . ASN B  630 ? 0.3767 0.4260 0.2263 0.0417  0.0274  -0.0394 656 ASN B CA  
21566 C C   . ASN B  630 ? 0.3850 0.4451 0.2321 0.0434  0.0227  -0.0356 656 ASN B C   
21567 O O   . ASN B  630 ? 0.3810 0.4479 0.2282 0.0406  0.0173  -0.0375 656 ASN B O   
21568 C CB  . ASN B  630 ? 0.3882 0.4330 0.2259 0.0409  0.0314  -0.0451 656 ASN B CB  
21569 C CG  . ASN B  630 ? 0.4203 0.4541 0.2598 0.0389  0.0360  -0.0495 656 ASN B CG  
21570 O OD1 . ASN B  630 ? 0.4271 0.4582 0.2726 0.0355  0.0341  -0.0519 656 ASN B OD1 
21571 N ND2 . ASN B  630 ? 0.4271 0.4540 0.2616 0.0412  0.0423  -0.0506 656 ASN B ND2 
21578 N N   . GLU B  631 ? 0.3915 0.4534 0.2379 0.0482  0.0249  -0.0295 657 GLU B N   
21579 C CA  . GLU B  631 ? 0.4055 0.4768 0.2499 0.0507  0.0212  -0.0249 657 GLU B CA  
21580 C C   . GLU B  631 ? 0.3964 0.4715 0.2513 0.0505  0.0169  -0.0212 657 GLU B C   
21581 O O   . GLU B  631 ? 0.3920 0.4756 0.2454 0.0504  0.0121  -0.0203 657 GLU B O   
21582 C CB  . GLU B  631 ? 0.4577 0.5281 0.2998 0.0558  0.0254  -0.0188 657 GLU B CB  
21583 C CG  . GLU B  631 ? 0.5496 0.6289 0.3872 0.0588  0.0226  -0.0140 657 GLU B CG  
21584 C CD  . GLU B  631 ? 0.6522 0.7302 0.4868 0.0636  0.0272  -0.0082 657 GLU B CD  
21585 O OE1 . GLU B  631 ? 0.6598 0.7304 0.4980 0.0647  0.0326  -0.0071 657 GLU B OE1 
21586 O OE2 . GLU B  631 ? 0.6772 0.7619 0.5061 0.0663  0.0256  -0.0045 657 GLU B OE2 
21593 N N   . ALA B  632 ? 0.3845 0.4537 0.2501 0.0504  0.0186  -0.0189 658 ALA B N   
21594 C CA  . ALA B  632 ? 0.3776 0.4497 0.2529 0.0499  0.0149  -0.0159 658 ALA B CA  
21595 C C   . ALA B  632 ? 0.3716 0.4472 0.2474 0.0454  0.0102  -0.0213 658 ALA B C   
21596 O O   . ALA B  632 ? 0.3770 0.4594 0.2559 0.0454  0.0058  -0.0195 658 ALA B O   
21597 C CB  . ALA B  632 ? 0.3837 0.4490 0.2694 0.0504  0.0177  -0.0128 658 ALA B CB  
21603 N N   . PHE B  633 ? 0.3621 0.4329 0.2349 0.0416  0.0112  -0.0277 659 PHE B N   
21604 C CA  . PHE B  633 ? 0.3690 0.4431 0.2421 0.0367  0.0070  -0.0331 659 PHE B CA  
21605 C C   . PHE B  633 ? 0.3716 0.4559 0.2366 0.0361  0.0027  -0.0348 659 PHE B C   
21606 O O   . PHE B  633 ? 0.3614 0.4530 0.2295 0.0344  -0.0021 -0.0352 659 PHE B O   
21607 C CB  . PHE B  633 ? 0.3740 0.4401 0.2447 0.0327  0.0096  -0.0397 659 PHE B CB  
21608 C CG  . PHE B  633 ? 0.3848 0.4527 0.2582 0.0274  0.0058  -0.0445 659 PHE B CG  
21609 C CD1 . PHE B  633 ? 0.3951 0.4693 0.2612 0.0237  0.0023  -0.0498 659 PHE B CD1 
21610 C CD2 . PHE B  633 ? 0.3954 0.4597 0.2788 0.0259  0.0054  -0.0433 659 PHE B CD2 
21611 C CE1 . PHE B  633 ? 0.4038 0.4804 0.2729 0.0187  -0.0012 -0.0539 659 PHE B CE1 
21612 C CE2 . PHE B  633 ? 0.4043 0.4706 0.2902 0.0210  0.0021  -0.0474 659 PHE B CE2 
21613 C CZ  . PHE B  633 ? 0.4018 0.4741 0.2807 0.0174  -0.0012 -0.0526 659 PHE B CZ  
21623 N N   . LEU B  634 ? 0.3793 0.4647 0.2342 0.0378  0.0045  -0.0356 660 LEU B N   
21624 C CA  . LEU B  634 ? 0.3948 0.4907 0.2414 0.0375  0.0006  -0.0368 660 LEU B CA  
21625 C C   . LEU B  634 ? 0.3860 0.4907 0.2364 0.0414  -0.0028 -0.0300 660 LEU B C   
21626 O O   . LEU B  634 ? 0.3923 0.5073 0.2387 0.0408  -0.0074 -0.0307 660 LEU B O   
21627 C CB  . LEU B  634 ? 0.4098 0.5045 0.2442 0.0388  0.0038  -0.0385 660 LEU B CB  
21628 C CG  . LEU B  634 ? 0.4469 0.5348 0.2743 0.0344  0.0065  -0.0466 660 LEU B CG  
21629 C CD1 . LEU B  634 ? 0.4572 0.5441 0.2722 0.0362  0.0099  -0.0479 660 LEU B CD1 
21630 C CD2 . LEU B  634 ? 0.4565 0.5499 0.2813 0.0285  0.0016  -0.0531 660 LEU B CD2 
21642 N N   . ASN B  635 ? 0.3686 0.4697 0.2266 0.0454  -0.0006 -0.0234 661 ASN B N   
21643 C CA  . ASN B  635 ? 0.3560 0.4638 0.2180 0.0493  -0.0033 -0.0169 661 ASN B CA  
21644 C C   . ASN B  635 ? 0.3472 0.4572 0.2194 0.0476  -0.0066 -0.0164 661 ASN B C   
21645 O O   . ASN B  635 ? 0.3411 0.4555 0.2177 0.0508  -0.0083 -0.0111 661 ASN B O   
21646 C CB  . ASN B  635 ? 0.3610 0.4644 0.2248 0.0544  0.0009  -0.0100 661 ASN B CB  
21647 C CG  . ASN B  635 ? 0.3939 0.4976 0.2472 0.0571  0.0038  -0.0090 661 ASN B CG  
21648 O OD1 . ASN B  635 ? 0.4128 0.5104 0.2667 0.0598  0.0086  -0.0055 661 ASN B OD1 
21649 N ND2 . ASN B  635 ? 0.3940 0.5053 0.2374 0.0564  0.0012  -0.0116 661 ASN B ND2 
21656 N N   . LEU B  636 ? 0.3430 0.4502 0.2184 0.0426  -0.0077 -0.0220 662 LEU B N   
21657 C CA  . LEU B  636 ? 0.3493 0.4597 0.2334 0.0407  -0.0111 -0.0219 662 LEU B CA  
21658 C C   . LEU B  636 ? 0.3552 0.4782 0.2357 0.0402  -0.0163 -0.0230 662 LEU B C   
21659 O O   . LEU B  636 ? 0.3595 0.4870 0.2308 0.0390  -0.0174 -0.0263 662 LEU B O   
21660 C CB  . LEU B  636 ? 0.3502 0.4543 0.2382 0.0355  -0.0105 -0.0273 662 LEU B CB  
21661 C CG  . LEU B  636 ? 0.3727 0.4654 0.2650 0.0360  -0.0057 -0.0262 662 LEU B CG  
21662 C CD1 . LEU B  636 ? 0.3867 0.4738 0.2824 0.0309  -0.0053 -0.0314 662 LEU B CD1 
21663 C CD2 . LEU B  636 ? 0.3727 0.4636 0.2735 0.0394  -0.0047 -0.0196 662 LEU B CD2 
21675 N N   . PRO B  637 ? 0.3568 0.4860 0.2440 0.0415  -0.0195 -0.0198 663 PRO B N   
21676 C CA  . PRO B  637 ? 0.3534 0.4957 0.2378 0.0416  -0.0244 -0.0201 663 PRO B CA  
21677 C C   . PRO B  637 ? 0.3495 0.4964 0.2292 0.0356  -0.0272 -0.0276 663 PRO B C   
21678 O O   . PRO B  637 ? 0.3450 0.4876 0.2290 0.0309  -0.0272 -0.0320 663 PRO B O   
21679 C CB  . PRO B  637 ? 0.3588 0.5044 0.2531 0.0430  -0.0264 -0.0166 663 PRO B CB  
21680 C CG  . PRO B  637 ? 0.3672 0.5022 0.2675 0.0451  -0.0224 -0.0129 663 PRO B CG  
21681 C CD  . PRO B  637 ? 0.3486 0.4736 0.2461 0.0428  -0.0186 -0.0160 663 PRO B CD  
21689 N N   . ALA B  638 ? 0.3480 0.5036 0.2187 0.0355  -0.0295 -0.0292 664 ALA B N   
21690 C CA  . ALA B  638 ? 0.3568 0.5178 0.2222 0.0293  -0.0325 -0.0366 664 ALA B CA  
21691 C C   . ALA B  638 ? 0.3511 0.5210 0.2237 0.0261  -0.0371 -0.0382 664 ALA B C   
21692 O O   . ALA B  638 ? 0.3549 0.5278 0.2255 0.0200  -0.0392 -0.0447 664 ALA B O   
21693 C CB  . ALA B  638 ? 0.3620 0.5318 0.2163 0.0301  -0.0343 -0.0372 664 ALA B CB  
21699 N N   . SER B  639 ? 0.3410 0.5146 0.2221 0.0300  -0.0382 -0.0325 665 SER B N   
21700 C CA  . SER B  639 ? 0.3442 0.5259 0.2330 0.0277  -0.0420 -0.0334 665 SER B CA  
21701 C C   . SER B  639 ? 0.3370 0.5094 0.2330 0.0233  -0.0403 -0.0369 665 SER B C   
21702 O O   . SER B  639 ? 0.3381 0.5166 0.2399 0.0203  -0.0431 -0.0386 665 SER B O   
21703 C CB  . SER B  639 ? 0.3660 0.5539 0.2609 0.0341  -0.0431 -0.0259 665 SER B CB  
21704 O OG  . SER B  639 ? 0.3945 0.5715 0.2926 0.0386  -0.0389 -0.0209 665 SER B OG  
21710 N N   . LEU B  640 ? 0.3328 0.4913 0.2286 0.0228  -0.0357 -0.0377 666 LEU B N   
21711 C CA  . LEU B  640 ? 0.3313 0.4812 0.2339 0.0190  -0.0341 -0.0402 666 LEU B CA  
21712 C C   . LEU B  640 ? 0.3293 0.4821 0.2322 0.0118  -0.0364 -0.0470 666 LEU B C   
21713 O O   . LEU B  640 ? 0.3360 0.4902 0.2313 0.0081  -0.0370 -0.0522 666 LEU B O   
21714 C CB  . LEU B  640 ? 0.3370 0.4725 0.2383 0.0195  -0.0289 -0.0403 666 LEU B CB  
21715 C CG  . LEU B  640 ? 0.3535 0.4833 0.2578 0.0254  -0.0258 -0.0336 666 LEU B CG  
21716 C CD1 . LEU B  640 ? 0.3546 0.4718 0.2573 0.0252  -0.0209 -0.0344 666 LEU B CD1 
21717 C CD2 . LEU B  640 ? 0.3627 0.4926 0.2770 0.0268  -0.0265 -0.0298 666 LEU B CD2 
21729 N N   . THR B  641 ? 0.3190 0.4725 0.2304 0.0097  -0.0375 -0.0471 667 THR B N   
21730 C CA  . THR B  641 ? 0.3196 0.4742 0.2325 0.0027  -0.0390 -0.0532 667 THR B CA  
21731 C C   . THR B  641 ? 0.3191 0.4603 0.2366 0.0002  -0.0354 -0.0544 667 THR B C   
21732 O O   . THR B  641 ? 0.3313 0.4687 0.2479 -0.0056 -0.0349 -0.0598 667 THR B O   
21733 C CB  . THR B  641 ? 0.3302 0.4979 0.2491 0.0016  -0.0433 -0.0526 667 THR B CB  
21734 O OG1 . THR B  641 ? 0.3500 0.5153 0.2777 0.0045  -0.0425 -0.0481 667 THR B OG1 
21735 C CG2 . THR B  641 ? 0.3243 0.5062 0.2395 0.0046  -0.0471 -0.0506 667 THR B CG2 
21743 N N   . GLU B  642 ? 0.3075 0.4418 0.2301 0.0045  -0.0328 -0.0493 668 GLU B N   
21744 C CA  . GLU B  642 ? 0.3087 0.4317 0.2362 0.0028  -0.0296 -0.0494 668 GLU B CA  
21745 C C   . GLU B  642 ? 0.3129 0.4268 0.2399 0.0075  -0.0258 -0.0452 668 GLU B C   
21746 O O   . GLU B  642 ? 0.3150 0.4313 0.2441 0.0125  -0.0258 -0.0400 668 GLU B O   
21747 C CB  . GLU B  642 ? 0.3367 0.4636 0.2730 0.0026  -0.0314 -0.0471 668 GLU B CB  
21748 C CG  . GLU B  642 ? 0.3984 0.5158 0.3405 0.0007  -0.0289 -0.0468 668 GLU B CG  
21749 C CD  . GLU B  642 ? 0.4508 0.5728 0.4007 -0.0002 -0.0308 -0.0452 668 GLU B CD  
21750 O OE1 . GLU B  642 ? 0.4531 0.5861 0.4041 -0.0002 -0.0340 -0.0454 668 GLU B OE1 
21751 O OE2 . GLU B  642 ? 0.4693 0.5842 0.4240 -0.0009 -0.0289 -0.0438 668 GLU B OE2 
21758 N N   . LEU B  643 ? 0.3103 0.4137 0.2348 0.0060  -0.0222 -0.0474 669 LEU B N   
21759 C CA  . LEU B  643 ? 0.3022 0.3974 0.2265 0.0102  -0.0183 -0.0436 669 LEU B CA  
21760 C C   . LEU B  643 ? 0.3035 0.3883 0.2325 0.0083  -0.0152 -0.0439 669 LEU B C   
21761 O O   . LEU B  643 ? 0.3117 0.3914 0.2384 0.0043  -0.0139 -0.0485 669 LEU B O   
21762 C CB  . LEU B  643 ? 0.2994 0.3929 0.2144 0.0112  -0.0164 -0.0457 669 LEU B CB  
21763 C CG  . LEU B  643 ? 0.3157 0.4006 0.2293 0.0152  -0.0118 -0.0426 669 LEU B CG  
21764 C CD1 . LEU B  643 ? 0.3171 0.4037 0.2354 0.0204  -0.0115 -0.0356 669 LEU B CD1 
21765 C CD2 . LEU B  643 ? 0.3216 0.4060 0.2250 0.0158  -0.0102 -0.0454 669 LEU B CD2 
21777 N N   . HIS B  644 ? 0.2894 0.3713 0.2250 0.0111  -0.0141 -0.0388 670 HIS B N   
21778 C CA  . HIS B  644 ? 0.2819 0.3549 0.2224 0.0099  -0.0113 -0.0380 670 HIS B CA  
21779 C C   . HIS B  644 ? 0.2768 0.3436 0.2169 0.0139  -0.0075 -0.0344 670 HIS B C   
21780 O O   . HIS B  644 ? 0.2669 0.3363 0.2077 0.0178  -0.0074 -0.0301 670 HIS B O   
21781 C CB  . HIS B  644 ? 0.2890 0.3637 0.2377 0.0091  -0.0129 -0.0353 670 HIS B CB  
21782 C CG  . HIS B  644 ? 0.3209 0.4022 0.2711 0.0053  -0.0165 -0.0383 670 HIS B CG  
21783 N ND1 . HIS B  644 ? 0.3410 0.4191 0.2941 0.0008  -0.0164 -0.0409 670 HIS B ND1 
21784 C CD2 . HIS B  644 ? 0.3310 0.4220 0.2805 0.0058  -0.0198 -0.0386 670 HIS B CD2 
21785 C CE1 . HIS B  644 ? 0.3434 0.4295 0.2975 -0.0017 -0.0198 -0.0430 670 HIS B CE1 
21786 N NE2 . HIS B  644 ? 0.3393 0.4336 0.2916 0.0013  -0.0219 -0.0416 670 HIS B NE2 
21794 N N   . ILE B  645 ? 0.2814 0.3399 0.2202 0.0130  -0.0040 -0.0361 671 ILE B N   
21795 C CA  . ILE B  645 ? 0.2892 0.3415 0.2287 0.0165  0.0001  -0.0327 671 ILE B CA  
21796 C C   . ILE B  645 ? 0.2956 0.3402 0.2405 0.0148  0.0025  -0.0323 671 ILE B C   
21797 O O   . ILE B  645 ? 0.3105 0.3486 0.2550 0.0165  0.0065  -0.0316 671 ILE B O   
21798 C CB  . ILE B  645 ? 0.3004 0.3504 0.2313 0.0181  0.0029  -0.0351 671 ILE B CB  
21799 C CG1 . ILE B  645 ? 0.3100 0.3679 0.2335 0.0176  -0.0003 -0.0380 671 ILE B CG1 
21800 C CG2 . ILE B  645 ? 0.3027 0.3497 0.2345 0.0229  0.0064  -0.0302 671 ILE B CG2 
21801 C CD1 . ILE B  645 ? 0.3339 0.3899 0.2476 0.0187  0.0022  -0.0409 671 ILE B CD1 
21813 N N   . ASN B  646 ? 0.2877 0.3337 0.2380 0.0118  0.0002  -0.0324 672 ASN B N   
21814 C CA  . ASN B  646 ? 0.2873 0.3271 0.2426 0.0100  0.0019  -0.0318 672 ASN B CA  
21815 C C   . ASN B  646 ? 0.2889 0.3268 0.2505 0.0130  0.0036  -0.0259 672 ASN B C   
21816 O O   . ASN B  646 ? 0.2837 0.3257 0.2467 0.0157  0.0028  -0.0224 672 ASN B O   
21817 C CB  . ASN B  646 ? 0.2904 0.3330 0.2488 0.0056  -0.0013 -0.0337 672 ASN B CB  
21818 C CG  . ASN B  646 ? 0.3213 0.3716 0.2837 0.0062  -0.0048 -0.0310 672 ASN B CG  
21819 O OD1 . ASN B  646 ? 0.3415 0.3981 0.3010 0.0076  -0.0068 -0.0312 672 ASN B OD1 
21820 N ND2 . ASN B  646 ? 0.3145 0.3644 0.2833 0.0052  -0.0054 -0.0283 672 ASN B ND2 
21827 N N   . ASP B  647 ? 0.2876 0.3192 0.2529 0.0126  0.0062  -0.0247 673 ASP B N   
21828 C CA  . ASP B  647 ? 0.2943 0.3249 0.2662 0.0149  0.0076  -0.0191 673 ASP B CA  
21829 C C   . ASP B  647 ? 0.2950 0.3263 0.2660 0.0192  0.0098  -0.0158 673 ASP B C   
21830 O O   . ASP B  647 ? 0.3003 0.3354 0.2753 0.0208  0.0088  -0.0116 673 ASP B O   
21831 C CB  . ASP B  647 ? 0.3174 0.3526 0.2950 0.0131  0.0042  -0.0166 673 ASP B CB  
21832 C CG  . ASP B  647 ? 0.3937 0.4279 0.3724 0.0088  0.0026  -0.0194 673 ASP B CG  
21833 O OD1 . ASP B  647 ? 0.4153 0.4432 0.3939 0.0078  0.0050  -0.0206 673 ASP B OD1 
21834 O OD2 . ASP B  647 ? 0.4250 0.4643 0.4047 0.0067  -0.0008 -0.0203 673 ASP B OD2 
21839 N N   . ASN B  648 ? 0.2932 0.3207 0.2587 0.0209  0.0129  -0.0180 674 ASN B N   
21840 C CA  . ASN B  648 ? 0.2974 0.3243 0.2616 0.0251  0.0161  -0.0152 674 ASN B CA  
21841 C C   . ASN B  648 ? 0.3116 0.3309 0.2768 0.0262  0.0208  -0.0152 674 ASN B C   
21842 O O   . ASN B  648 ? 0.3067 0.3226 0.2758 0.0243  0.0210  -0.0153 674 ASN B O   
21843 C CB  . ASN B  648 ? 0.2944 0.3242 0.2503 0.0261  0.0155  -0.0181 674 ASN B CB  
21844 C CG  . ASN B  648 ? 0.3069 0.3439 0.2635 0.0266  0.0119  -0.0159 674 ASN B CG  
21845 O OD1 . ASN B  648 ? 0.3106 0.3495 0.2704 0.0292  0.0127  -0.0113 674 ASN B OD1 
21846 N ND2 . ASN B  648 ? 0.2816 0.3230 0.2358 0.0241  0.0081  -0.0191 674 ASN B ND2 
21853 N N   . MET B  649 ? 0.3293 0.3458 0.2914 0.0296  0.0249  -0.0147 675 MET B N   
21854 C CA  . MET B  649 ? 0.3587 0.3678 0.3211 0.0313  0.0300  -0.0149 675 MET B CA  
21855 C C   . MET B  649 ? 0.3712 0.3766 0.3240 0.0322  0.0330  -0.0197 675 MET B C   
21856 O O   . MET B  649 ? 0.3746 0.3766 0.3262 0.0357  0.0377  -0.0184 675 MET B O   
21857 C CB  . MET B  649 ? 0.3892 0.3993 0.3587 0.0351  0.0328  -0.0084 675 MET B CB  
21858 C CG  . MET B  649 ? 0.4630 0.4778 0.4414 0.0339  0.0295  -0.0037 675 MET B CG  
21859 S SD  . MET B  649 ? 0.6433 0.6591 0.6307 0.0377  0.0331  0.0036  675 MET B SD  
21860 C CE  . MET B  649 ? 0.6561 0.6724 0.6517 0.0350  0.0305  0.0062  675 MET B CE  
21870 N N   . LEU B  650 ? 0.3709 0.3778 0.3166 0.0291  0.0301  -0.0251 676 LEU B N   
21871 C CA  . LEU B  650 ? 0.3799 0.3843 0.3156 0.0294  0.0323  -0.0300 676 LEU B CA  
21872 C C   . LEU B  650 ? 0.4043 0.3987 0.3372 0.0292  0.0374  -0.0335 676 LEU B C   
21873 O O   . LEU B  650 ? 0.4010 0.3911 0.3353 0.0260  0.0370  -0.0361 676 LEU B O   
21874 C CB  . LEU B  650 ? 0.3767 0.3860 0.3060 0.0256  0.0277  -0.0350 676 LEU B CB  
21875 C CG  . LEU B  650 ? 0.3853 0.4044 0.3155 0.0261  0.0230  -0.0322 676 LEU B CG  
21876 C CD1 . LEU B  650 ? 0.3858 0.4099 0.3111 0.0221  0.0184  -0.0371 676 LEU B CD1 
21877 C CD2 . LEU B  650 ? 0.3813 0.4029 0.3077 0.0303  0.0248  -0.0295 676 LEU B CD2 
21889 N N   . LYS B  651 ? 0.4300 0.4205 0.3588 0.0327  0.0425  -0.0336 677 LYS B N   
21890 C CA  . LYS B  651 ? 0.4631 0.4433 0.3880 0.0331  0.0482  -0.0374 677 LYS B CA  
21891 C C   . LYS B  651 ? 0.4830 0.4610 0.3956 0.0306  0.0487  -0.0449 677 LYS B C   
21892 O O   . LYS B  651 ? 0.5032 0.4725 0.4114 0.0286  0.0519  -0.0501 677 LYS B O   
21893 C CB  . LYS B  651 ? 0.5070 0.4839 0.4351 0.0386  0.0541  -0.0329 677 LYS B CB  
21894 C CG  . LYS B  651 ? 0.5823 0.5602 0.5227 0.0407  0.0543  -0.0260 677 LYS B CG  
21895 C CD  . LYS B  651 ? 0.6625 0.6339 0.6064 0.0452  0.0612  -0.0232 677 LYS B CD  
21896 C CE  . LYS B  651 ? 0.7126 0.6850 0.6685 0.0464  0.0610  -0.0169 677 LYS B CE  
21897 N NZ  . LYS B  651 ? 0.7515 0.7200 0.7121 0.0516  0.0674  -0.0129 677 LYS B NZ  
21911 N N   . PHE B  652 ? 0.4736 0.4594 0.3804 0.0306  0.0456  -0.0456 678 PHE B N   
21912 C CA  . PHE B  652 ? 0.4719 0.4578 0.3668 0.0280  0.0452  -0.0523 678 PHE B CA  
21913 C C   . PHE B  652 ? 0.4522 0.4487 0.3453 0.0251  0.0381  -0.0531 678 PHE B C   
21914 O O   . PHE B  652 ? 0.4374 0.4412 0.3369 0.0267  0.0346  -0.0477 678 PHE B O   
21915 C CB  . PHE B  652 ? 0.4784 0.4632 0.3665 0.0321  0.0497  -0.0520 678 PHE B CB  
21918 N N   . PHE B  653 ? 0.4465 0.4438 0.3309 0.0208  0.0362  -0.0598 679 PHE B N   
21919 C CA  . PHE B  653 ? 0.4391 0.4470 0.3208 0.0180  0.0297  -0.0612 679 PHE B CA  
21920 C C   . PHE B  653 ? 0.4448 0.4530 0.3137 0.0158  0.0302  -0.0677 679 PHE B C   
21921 O O   . PHE B  653 ? 0.4527 0.4533 0.3166 0.0122  0.0327  -0.0740 679 PHE B O   
21922 C CB  . PHE B  653 ? 0.4278 0.4376 0.3149 0.0132  0.0254  -0.0628 679 PHE B CB  
21923 C CG  . PHE B  653 ? 0.4241 0.4459 0.3098 0.0112  0.0189  -0.0631 679 PHE B CG  
21924 C CD1 . PHE B  653 ? 0.4268 0.4567 0.3181 0.0145  0.0158  -0.0569 679 PHE B CD1 
21925 C CD2 . PHE B  653 ? 0.4331 0.4583 0.3117 0.0061  0.0161  -0.0697 679 PHE B CD2 
21926 C CE1 . PHE B  653 ? 0.4298 0.4706 0.3198 0.0133  0.0102  -0.0569 679 PHE B CE1 
21927 C CE2 . PHE B  653 ? 0.4362 0.4734 0.3138 0.0048  0.0102  -0.0695 679 PHE B CE2 
21928 C CZ  . PHE B  653 ? 0.4274 0.4722 0.3109 0.0086  0.0074  -0.0630 679 PHE B CZ  
21938 N N   . ASN B  654 ? 0.4426 0.4590 0.3059 0.0180  0.0283  -0.0662 680 ASN B N   
21939 C CA  . ASN B  654 ? 0.4485 0.4663 0.2990 0.0160  0.0285  -0.0721 680 ASN B CA  
21940 C C   . ASN B  654 ? 0.4502 0.4762 0.2979 0.0104  0.0223  -0.0766 680 ASN B C   
21941 O O   . ASN B  654 ? 0.4438 0.4811 0.2923 0.0111  0.0172  -0.0736 680 ASN B O   
21942 C CB  . ASN B  654 ? 0.4654 0.4885 0.3112 0.0211  0.0294  -0.0679 680 ASN B CB  
21943 C CG  . ASN B  654 ? 0.5138 0.5392 0.3460 0.0198  0.0298  -0.0730 680 ASN B CG  
21944 O OD1 . ASN B  654 ? 0.5079 0.5310 0.3331 0.0146  0.0294  -0.0805 680 ASN B OD1 
21945 N ND2 . ASN B  654 ? 0.5614 0.5902 0.3891 0.0244  0.0315  -0.0693 680 ASN B ND2 
21952 N N   . TRP B  655 ? 0.4568 0.4769 0.3020 0.0047  0.0229  -0.0834 681 TRP B N   
21953 C CA  . TRP B  655 ? 0.4651 0.4923 0.3084 -0.0015 0.0173  -0.0882 681 TRP B CA  
21954 C C   . TRP B  655 ? 0.4719 0.5092 0.3045 -0.0030 0.0139  -0.0914 681 TRP B C   
21955 O O   . TRP B  655 ? 0.4640 0.5120 0.2970 -0.0063 0.0080  -0.0925 681 TRP B O   
21956 C CB  . TRP B  655 ? 0.4642 0.4812 0.3059 -0.0074 0.0199  -0.0953 681 TRP B CB  
21957 C CG  . TRP B  655 ? 0.4609 0.4690 0.3131 -0.0065 0.0226  -0.0922 681 TRP B CG  
21958 C CD1 . TRP B  655 ? 0.4705 0.4666 0.3251 -0.0031 0.0290  -0.0905 681 TRP B CD1 
21959 C CD2 . TRP B  655 ? 0.4516 0.4633 0.3138 -0.0085 0.0188  -0.0897 681 TRP B CD2 
21960 N NE1 . TRP B  655 ? 0.4701 0.4624 0.3355 -0.0029 0.0291  -0.0868 681 TRP B NE1 
21961 C CE2 . TRP B  655 ? 0.4605 0.4619 0.3304 -0.0063 0.0230  -0.0864 681 TRP B CE2 
21962 C CE3 . TRP B  655 ? 0.4515 0.4744 0.3170 -0.0117 0.0123  -0.0896 681 TRP B CE3 
21963 C CZ2 . TRP B  655 ? 0.4627 0.4645 0.3425 -0.0077 0.0209  -0.0835 681 TRP B CZ2 
21964 C CZ3 . TRP B  655 ? 0.4563 0.4791 0.3318 -0.0130 0.0106  -0.0869 681 TRP B CZ3 
21965 C CH2 . TRP B  655 ? 0.4607 0.4732 0.3431 -0.0111 0.0148  -0.0839 681 TRP B CH2 
21976 N N   . THR B  656 ? 0.4830 0.5175 0.3060 -0.0007 0.0176  -0.0928 682 THR B N   
21977 C CA  . THR B  656 ? 0.4957 0.5396 0.3074 -0.0018 0.0146  -0.0956 682 THR B CA  
21978 C C   . THR B  656 ? 0.4843 0.5429 0.2994 0.0014  0.0088  -0.0892 682 THR B C   
21979 O O   . THR B  656 ? 0.4760 0.5456 0.2850 -0.0011 0.0039  -0.0914 682 THR B O   
21980 C CB  . THR B  656 ? 0.5352 0.5728 0.3369 0.0013  0.0204  -0.0969 682 THR B CB  
21981 O OG1 . THR B  656 ? 0.5650 0.5879 0.3646 -0.0008 0.0266  -0.1022 682 THR B OG1 
21982 C CG2 . THR B  656 ? 0.5494 0.5958 0.3379 -0.0007 0.0178  -0.1009 682 THR B CG2 
21990 N N   . LEU B  657 ? 0.4814 0.5401 0.3064 0.0069  0.0092  -0.0811 683 LEU B N   
21991 C CA  . LEU B  657 ? 0.4816 0.5523 0.3104 0.0107  0.0047  -0.0744 683 LEU B CA  
21992 C C   . LEU B  657 ? 0.4888 0.5694 0.3232 0.0074  -0.0018 -0.0746 683 LEU B C   
21993 O O   . LEU B  657 ? 0.4954 0.5872 0.3311 0.0100  -0.0060 -0.0701 683 LEU B O   
21994 C CB  . LEU B  657 ? 0.4845 0.5509 0.3221 0.0170  0.0077  -0.0664 683 LEU B CB  
21995 C CG  . LEU B  657 ? 0.5082 0.5657 0.3414 0.0209  0.0143  -0.0651 683 LEU B CG  
21996 C CD1 . LEU B  657 ? 0.5156 0.5709 0.3582 0.0265  0.0166  -0.0570 683 LEU B CD1 
21997 C CD2 . LEU B  657 ? 0.5165 0.5787 0.3370 0.0221  0.0148  -0.0666 683 LEU B CD2 
22009 N N   . LEU B  658 ? 0.4876 0.5647 0.3251 0.0016  -0.0026 -0.0798 684 LEU B N   
22010 C CA  . LEU B  658 ? 0.4903 0.5775 0.3330 -0.0019 -0.0086 -0.0804 684 LEU B CA  
22011 C C   . LEU B  658 ? 0.5045 0.6047 0.3385 -0.0047 -0.0135 -0.0837 684 LEU B C   
22012 O O   . LEU B  658 ? 0.5072 0.6185 0.3456 -0.0063 -0.0189 -0.0827 684 LEU B O   
22013 C CB  . LEU B  658 ? 0.4882 0.5682 0.3357 -0.0077 -0.0079 -0.0852 684 LEU B CB  
22014 C CG  . LEU B  658 ? 0.4986 0.5674 0.3555 -0.0054 -0.0039 -0.0815 684 LEU B CG  
22015 C CD1 . LEU B  658 ? 0.5068 0.5690 0.3674 -0.0113 -0.0033 -0.0863 684 LEU B CD1 
22016 C CD2 . LEU B  658 ? 0.4981 0.5724 0.3648 -0.0005 -0.0061 -0.0734 684 LEU B CD2 
22028 N N   . GLN B  659 ? 0.5159 0.6153 0.3379 -0.0050 -0.0117 -0.0872 685 GLN B N   
22029 C CA  . GLN B  659 ? 0.5270 0.6392 0.3396 -0.0074 -0.0162 -0.0901 685 GLN B CA  
22030 C C   . GLN B  659 ? 0.5204 0.6464 0.3362 -0.0021 -0.0207 -0.0825 685 GLN B C   
22031 O O   . GLN B  659 ? 0.5237 0.6632 0.3370 -0.0043 -0.0262 -0.0836 685 GLN B O   
22032 C CB  . GLN B  659 ? 0.5647 0.6724 0.3640 -0.0072 -0.0125 -0.0938 685 GLN B CB  
22033 C CG  . GLN B  659 ? 0.6328 0.7291 0.4257 -0.0134 -0.0087 -0.1029 685 GLN B CG  
22034 C CD  . GLN B  659 ? 0.7153 0.8078 0.4944 -0.0128 -0.0050 -0.1064 685 GLN B CD  
22035 O OE1 . GLN B  659 ? 0.7488 0.8324 0.5270 -0.0076 0.0005  -0.1032 685 GLN B OE1 
22036 N NE2 . GLN B  659 ? 0.7300 0.8297 0.4983 -0.0182 -0.0079 -0.1128 685 GLN B NE2 
22045 N N   . GLN B  660 ? 0.5080 0.6305 0.3287 0.0050  -0.0181 -0.0749 686 GLN B N   
22046 C CA  . GLN B  660 ? 0.4976 0.6311 0.3215 0.0107  -0.0214 -0.0671 686 GLN B CA  
22047 C C   . GLN B  660 ? 0.4713 0.6105 0.3072 0.0110  -0.0252 -0.0635 686 GLN B C   
22048 O O   . GLN B  660 ? 0.4686 0.6153 0.3083 0.0161  -0.0273 -0.0567 686 GLN B O   
22049 C CB  . GLN B  660 ? 0.5383 0.6649 0.3630 0.0177  -0.0168 -0.0604 686 GLN B CB  
22050 C CG  . GLN B  660 ? 0.6251 0.7438 0.4394 0.0185  -0.0117 -0.0629 686 GLN B CG  
22051 C CD  . GLN B  660 ? 0.7152 0.8405 0.5164 0.0149  -0.0136 -0.0687 686 GLN B CD  
22052 O OE1 . GLN B  660 ? 0.7442 0.8825 0.5414 0.0161  -0.0181 -0.0664 686 GLN B OE1 
22053 N NE2 . GLN B  660 ? 0.7440 0.8603 0.5382 0.0105  -0.0102 -0.0762 686 GLN B NE2 
22062 N N   . PHE B  661 ? 0.4483 0.5837 0.2902 0.0058  -0.0257 -0.0678 687 PHE B N   
22063 C CA  . PHE B  661 ? 0.4378 0.5780 0.2911 0.0056  -0.0288 -0.0649 687 PHE B CA  
22064 C C   . PHE B  661 ? 0.4295 0.5774 0.2825 -0.0014 -0.0330 -0.0711 687 PHE B C   
22065 O O   . PHE B  661 ? 0.4224 0.5635 0.2796 -0.0062 -0.0320 -0.0752 687 PHE B O   
22066 C CB  . PHE B  661 ? 0.4366 0.5639 0.2986 0.0066  -0.0247 -0.0629 687 PHE B CB  
22067 C CG  . PHE B  661 ? 0.4402 0.5615 0.3031 0.0134  -0.0209 -0.0565 687 PHE B CG  
22068 C CD1 . PHE B  661 ? 0.4536 0.5655 0.3101 0.0145  -0.0160 -0.0579 687 PHE B CD1 
22069 C CD2 . PHE B  661 ? 0.4423 0.5683 0.3119 0.0186  -0.0222 -0.0492 687 PHE B CD2 
22070 C CE1 . PHE B  661 ? 0.4651 0.5728 0.3223 0.0205  -0.0126 -0.0518 687 PHE B CE1 
22071 C CE2 . PHE B  661 ? 0.4521 0.5729 0.3221 0.0243  -0.0187 -0.0434 687 PHE B CE2 
22072 C CZ  . PHE B  661 ? 0.4571 0.5692 0.3211 0.0251  -0.0140 -0.0447 687 PHE B CZ  
22082 N N   . PRO B  662 ? 0.4293 0.5918 0.2775 -0.0022 -0.0379 -0.0716 688 PRO B N   
22083 C CA  . PRO B  662 ? 0.4278 0.5988 0.2749 -0.0096 -0.0421 -0.0780 688 PRO B CA  
22084 C C   . PRO B  662 ? 0.4205 0.5974 0.2791 -0.0114 -0.0452 -0.0768 688 PRO B C   
22085 O O   . PRO B  662 ? 0.4222 0.6048 0.2810 -0.0181 -0.0480 -0.0823 688 PRO B O   
22086 C CB  . PRO B  662 ? 0.4428 0.6288 0.2816 -0.0089 -0.0463 -0.0777 688 PRO B CB  
22087 C CG  . PRO B  662 ? 0.4493 0.6381 0.2899 -0.0001 -0.0459 -0.0688 688 PRO B CG  
22088 C CD  . PRO B  662 ? 0.4275 0.5995 0.2702 0.0033  -0.0396 -0.0666 688 PRO B CD  
22096 N N   . ARG B  663 ? 0.4100 0.5857 0.2777 -0.0058 -0.0445 -0.0699 689 ARG B N   
22097 C CA  . ARG B  663 ? 0.4051 0.5855 0.2838 -0.0069 -0.0468 -0.0683 689 ARG B CA  
22098 C C   . ARG B  663 ? 0.3893 0.5551 0.2748 -0.0082 -0.0427 -0.0687 689 ARG B C   
22099 O O   . ARG B  663 ? 0.3886 0.5568 0.2831 -0.0091 -0.0441 -0.0675 689 ARG B O   
22100 C CB  . ARG B  663 ? 0.4325 0.6220 0.3168 0.0004  -0.0489 -0.0601 689 ARG B CB  
22101 C CG  . ARG B  663 ? 0.5017 0.7060 0.3799 0.0029  -0.0529 -0.0581 689 ARG B CG  
22102 C CD  . ARG B  663 ? 0.5714 0.7918 0.4531 -0.0006 -0.0584 -0.0599 689 ARG B CD  
22103 N NE  . ARG B  663 ? 0.6462 0.8822 0.5236 0.0028  -0.0624 -0.0566 689 ARG B NE  
22104 C CZ  . ARG B  663 ? 0.7084 0.9506 0.5752 0.0005  -0.0643 -0.0599 689 ARG B CZ  
22105 N NH1 . ARG B  663 ? 0.7211 0.9784 0.5848 0.0042  -0.0682 -0.0559 689 ARG B NH1 
22106 N NH2 . ARG B  663 ? 0.7176 0.9509 0.5766 -0.0055 -0.0622 -0.0672 689 ARG B NH2 
22120 N N   . LEU B  664 ? 0.3776 0.5290 0.2592 -0.0078 -0.0378 -0.0701 690 LEU B N   
22121 C CA  . LEU B  664 ? 0.3784 0.5166 0.2665 -0.0084 -0.0339 -0.0698 690 LEU B CA  
22122 C C   . LEU B  664 ? 0.3845 0.5205 0.2754 -0.0159 -0.0345 -0.0756 690 LEU B C   
22123 O O   . LEU B  664 ? 0.3967 0.5290 0.2809 -0.0212 -0.0335 -0.0821 690 LEU B O   
22124 C CB  . LEU B  664 ? 0.3791 0.5038 0.2624 -0.0062 -0.0285 -0.0698 690 LEU B CB  
22125 C CG  . LEU B  664 ? 0.3853 0.4973 0.2759 -0.0051 -0.0244 -0.0675 690 LEU B CG  
22126 C CD1 . LEU B  664 ? 0.3792 0.4940 0.2785 0.0002  -0.0252 -0.0601 690 LEU B CD1 
22127 C CD2 . LEU B  664 ? 0.3972 0.4969 0.2826 -0.0031 -0.0190 -0.0680 690 LEU B CD2 
22139 N N   . GLU B  665 ? 0.3759 0.5136 0.2765 -0.0163 -0.0357 -0.0733 691 GLU B N   
22140 C CA  . GLU B  665 ? 0.3788 0.5149 0.2836 -0.0230 -0.0362 -0.0777 691 GLU B CA  
22141 C C   . GLU B  665 ? 0.3721 0.4937 0.2817 -0.0233 -0.0318 -0.0770 691 GLU B C   
22142 O O   . GLU B  665 ? 0.3750 0.4907 0.2848 -0.0292 -0.0306 -0.0817 691 GLU B O   
22143 C CB  . GLU B  665 ? 0.4217 0.5705 0.3344 -0.0232 -0.0405 -0.0754 691 GLU B CB  
22144 C CG  . GLU B  665 ? 0.5227 0.6876 0.4319 -0.0238 -0.0453 -0.0764 691 GLU B CG  
22145 C CD  . GLU B  665 ? 0.6439 0.8218 0.5613 -0.0244 -0.0492 -0.0745 691 GLU B CD  
22146 O OE1 . GLU B  665 ? 0.6651 0.8410 0.5905 -0.0211 -0.0483 -0.0699 691 GLU B OE1 
22147 O OE2 . GLU B  665 ? 0.6954 0.8861 0.6112 -0.0282 -0.0532 -0.0776 691 GLU B OE2 
22154 N N   . LEU B  666 ? 0.3548 0.4714 0.2689 -0.0175 -0.0297 -0.0709 692 LEU B N   
22155 C CA  . LEU B  666 ? 0.3512 0.4553 0.2702 -0.0175 -0.0259 -0.0695 692 LEU B CA  
22156 C C   . LEU B  666 ? 0.3427 0.4379 0.2596 -0.0122 -0.0219 -0.0661 692 LEU B C   
22157 O O   . LEU B  666 ? 0.3392 0.4385 0.2565 -0.0067 -0.0225 -0.0612 692 LEU B O   
22158 C CB  . LEU B  666 ? 0.3532 0.4607 0.2820 -0.0164 -0.0274 -0.0654 692 LEU B CB  
22159 C CG  . LEU B  666 ? 0.3832 0.4797 0.3176 -0.0176 -0.0243 -0.0642 692 LEU B CG  
22160 C CD1 . LEU B  666 ? 0.3936 0.4949 0.3354 -0.0203 -0.0265 -0.0636 692 LEU B CD1 
22161 C CD2 . LEU B  666 ? 0.3981 0.4879 0.3348 -0.0118 -0.0214 -0.0586 692 LEU B CD2 
22173 N N   . LEU B  667 ? 0.3383 0.4214 0.2533 -0.0137 -0.0177 -0.0683 693 LEU B N   
22174 C CA  . LEU B  667 ? 0.3366 0.4107 0.2501 -0.0090 -0.0134 -0.0652 693 LEU B CA  
22175 C C   . LEU B  667 ? 0.3274 0.3916 0.2476 -0.0094 -0.0104 -0.0634 693 LEU B C   
22176 O O   . LEU B  667 ? 0.3322 0.3903 0.2522 -0.0141 -0.0090 -0.0675 693 LEU B O   
22177 C CB  . LEU B  667 ? 0.3466 0.4155 0.2503 -0.0099 -0.0106 -0.0699 693 LEU B CB  
22178 C CG  . LEU B  667 ? 0.3765 0.4360 0.2783 -0.0051 -0.0056 -0.0671 693 LEU B CG  
22179 C CD1 . LEU B  667 ? 0.3900 0.4543 0.2948 0.0012  -0.0062 -0.0601 693 LEU B CD1 
22180 C CD2 . LEU B  667 ? 0.3890 0.4446 0.2803 -0.0062 -0.0031 -0.0722 693 LEU B CD2 
22192 N N   . ASP B  668 ? 0.3112 0.3745 0.2375 -0.0050 -0.0097 -0.0573 694 ASP B N   
22193 C CA  . ASP B  668 ? 0.3122 0.3678 0.2453 -0.0051 -0.0074 -0.0548 694 ASP B CA  
22194 C C   . ASP B  668 ? 0.3217 0.3693 0.2549 -0.0007 -0.0030 -0.0513 694 ASP B C   
22195 O O   . ASP B  668 ? 0.3239 0.3743 0.2589 0.0038  -0.0030 -0.0465 694 ASP B O   
22196 C CB  . ASP B  668 ? 0.3117 0.3737 0.2527 -0.0048 -0.0105 -0.0509 694 ASP B CB  
22197 C CG  . ASP B  668 ? 0.3502 0.4062 0.2983 -0.0043 -0.0087 -0.0472 694 ASP B CG  
22198 O OD1 . ASP B  668 ? 0.3514 0.3982 0.2993 -0.0050 -0.0052 -0.0479 694 ASP B OD1 
22199 O OD2 . ASP B  668 ? 0.3764 0.4370 0.3302 -0.0033 -0.0108 -0.0436 694 ASP B OD2 
22204 N N   . LEU B  669 ? 0.3221 0.3599 0.2534 -0.0020 0.0010  -0.0537 695 LEU B N   
22205 C CA  . LEU B  669 ? 0.3310 0.3608 0.2626 0.0020  0.0057  -0.0508 695 LEU B CA  
22206 C C   . LEU B  669 ? 0.3318 0.3539 0.2701 0.0014  0.0082  -0.0486 695 LEU B C   
22207 O O   . LEU B  669 ? 0.3359 0.3500 0.2742 0.0036  0.0126  -0.0476 695 LEU B O   
22208 C CB  . LEU B  669 ? 0.3423 0.3665 0.2650 0.0018  0.0091  -0.0555 695 LEU B CB  
22209 C CG  . LEU B  669 ? 0.3708 0.4022 0.2856 0.0027  0.0072  -0.0575 695 LEU B CG  
22210 C CD1 . LEU B  669 ? 0.3812 0.4065 0.2865 0.0015  0.0106  -0.0632 695 LEU B CD1 
22211 C CD2 . LEU B  669 ? 0.3771 0.4129 0.2936 0.0083  0.0071  -0.0516 695 LEU B CD2 
22223 N N   . ARG B  670 ? 0.3237 0.3488 0.2681 -0.0011 0.0054  -0.0473 696 ARG B N   
22224 C CA  . ARG B  670 ? 0.3305 0.3493 0.2811 -0.0017 0.0073  -0.0448 696 ARG B CA  
22225 C C   . ARG B  670 ? 0.3321 0.3491 0.2878 0.0031  0.0095  -0.0385 696 ARG B C   
22226 O O   . ARG B  670 ? 0.3267 0.3490 0.2828 0.0063  0.0083  -0.0355 696 ARG B O   
22227 C CB  . ARG B  670 ? 0.3469 0.3709 0.3028 -0.0050 0.0035  -0.0441 696 ARG B CB  
22228 C CG  . ARG B  670 ? 0.3921 0.4182 0.3447 -0.0105 0.0013  -0.0500 696 ARG B CG  
22229 C CD  . ARG B  670 ? 0.4309 0.4637 0.3890 -0.0131 -0.0024 -0.0487 696 ARG B CD  
22230 N NE  . ARG B  670 ? 0.4745 0.5167 0.4341 -0.0104 -0.0057 -0.0458 696 ARG B NE  
22231 C CZ  . ARG B  670 ? 0.5095 0.5581 0.4741 -0.0112 -0.0086 -0.0438 696 ARG B CZ  
22232 N NH1 . ARG B  670 ? 0.5029 0.5501 0.4713 -0.0149 -0.0090 -0.0442 696 ARG B NH1 
22233 N NH2 . ARG B  670 ? 0.5043 0.5602 0.4700 -0.0083 -0.0109 -0.0413 696 ARG B NH2 
22247 N N   . GLY B  671 ? 0.3345 0.3443 0.2943 0.0036  0.0126  -0.0363 697 GLY B N   
22248 C CA  . GLY B  671 ? 0.3437 0.3526 0.3094 0.0077  0.0144  -0.0300 697 GLY B CA  
22249 C C   . GLY B  671 ? 0.3455 0.3537 0.3085 0.0122  0.0173  -0.0286 697 GLY B C   
22250 O O   . GLY B  671 ? 0.3533 0.3663 0.3195 0.0151  0.0165  -0.0241 697 GLY B O   
22254 N N   . ASN B  672 ? 0.3390 0.3410 0.2959 0.0127  0.0209  -0.0324 698 ASN B N   
22255 C CA  . ASN B  672 ? 0.3461 0.3464 0.2997 0.0169  0.0244  -0.0314 698 ASN B CA  
22256 C C   . ASN B  672 ? 0.3596 0.3496 0.3131 0.0185  0.0303  -0.0318 698 ASN B C   
22257 O O   . ASN B  672 ? 0.3528 0.3385 0.3112 0.0173  0.0311  -0.0305 698 ASN B O   
22258 C CB  . ASN B  672 ? 0.3454 0.3494 0.2900 0.0161  0.0229  -0.0361 698 ASN B CB  
22259 C CG  . ASN B  672 ? 0.3571 0.3709 0.3028 0.0171  0.0186  -0.0334 698 ASN B CG  
22260 O OD1 . ASN B  672 ? 0.3524 0.3686 0.3014 0.0208  0.0194  -0.0284 698 ASN B OD1 
22261 N ND2 . ASN B  672 ? 0.3335 0.3533 0.2767 0.0139  0.0142  -0.0364 698 ASN B ND2 
22268 N N   . LYS B  673 ? 0.3803 0.3664 0.3289 0.0216  0.0345  -0.0329 699 LYS B N   
22269 C CA  . LYS B  673 ? 0.4036 0.3796 0.3519 0.0236  0.0407  -0.0334 699 LYS B CA  
22270 C C   . LYS B  673 ? 0.4206 0.3907 0.3582 0.0225  0.0436  -0.0404 699 LYS B C   
22271 O O   . LYS B  673 ? 0.4201 0.3835 0.3553 0.0257  0.0493  -0.0407 699 LYS B O   
22272 C CB  . LYS B  673 ? 0.4306 0.4072 0.3845 0.0293  0.0441  -0.0270 699 LYS B CB  
22273 C CG  . LYS B  673 ? 0.4899 0.4729 0.4539 0.0300  0.0410  -0.0202 699 LYS B CG  
22274 C CD  . LYS B  673 ? 0.5640 0.5483 0.5337 0.0352  0.0444  -0.0140 699 LYS B CD  
22275 C CE  . LYS B  673 ? 0.6221 0.6132 0.6015 0.0353  0.0412  -0.0076 699 LYS B CE  
22276 N NZ  . LYS B  673 ? 0.6661 0.6605 0.6507 0.0398  0.0438  -0.0018 699 LYS B NZ  
22290 N N   . LEU B  674 ? 0.4357 0.4088 0.3668 0.0178  0.0399  -0.0462 700 LEU B N   
22291 C CA  . LEU B  674 ? 0.4623 0.4312 0.3826 0.0158  0.0419  -0.0534 700 LEU B CA  
22292 C C   . LEU B  674 ? 0.4954 0.4514 0.4137 0.0144  0.0473  -0.0571 700 LEU B C   
22293 O O   . LEU B  674 ? 0.4850 0.4373 0.4081 0.0119  0.0469  -0.0568 700 LEU B O   
22294 C CB  . LEU B  674 ? 0.4600 0.4363 0.3753 0.0107  0.0361  -0.0580 700 LEU B CB  
22295 C CG  . LEU B  674 ? 0.4732 0.4619 0.3898 0.0122  0.0310  -0.0546 700 LEU B CG  
22296 C CD1 . LEU B  674 ? 0.4781 0.4743 0.3912 0.0074  0.0254  -0.0587 700 LEU B CD1 
22297 C CD2 . LEU B  674 ? 0.4822 0.4726 0.3933 0.0165  0.0333  -0.0536 700 LEU B CD2 
22309 N N   . LEU B  675 ? 0.5301 0.4790 0.4416 0.0166  0.0528  -0.0602 701 LEU B N   
22310 C CA  . LEU B  675 ? 0.5747 0.5101 0.4839 0.0164  0.0592  -0.0635 701 LEU B CA  
22311 C C   . LEU B  675 ? 0.6106 0.5401 0.5093 0.0106  0.0599  -0.0728 701 LEU B C   
22312 O O   . LEU B  675 ? 0.6163 0.5343 0.5139 0.0088  0.0642  -0.0760 701 LEU B O   
22313 C CB  . LEU B  675 ? 0.5860 0.5163 0.4945 0.0227  0.0658  -0.0609 701 LEU B CB  
22314 C CG  . LEU B  675 ? 0.6075 0.5418 0.5273 0.0284  0.0665  -0.0517 701 LEU B CG  
22315 C CD1 . LEU B  675 ? 0.6199 0.5537 0.5379 0.0342  0.0714  -0.0494 701 LEU B CD1 
22316 C CD2 . LEU B  675 ? 0.6197 0.5463 0.5474 0.0293  0.0695  -0.0485 701 LEU B CD2 
22328 N N   . PHE B  676 ? 0.6333 0.5705 0.5242 0.0078  0.0559  -0.0770 702 PHE B N   
22329 C CA  . PHE B  676 ? 0.6694 0.6025 0.5500 0.0017  0.0560  -0.0861 702 PHE B CA  
22330 C C   . PHE B  676 ? 0.6789 0.6250 0.5552 -0.0023 0.0488  -0.0887 702 PHE B C   
22331 O O   . PHE B  676 ? 0.6735 0.6308 0.5535 0.0006  0.0445  -0.0836 702 PHE B O   
22332 C CB  . PHE B  676 ? 0.6896 0.6129 0.5606 0.0034  0.0629  -0.0908 702 PHE B CB  
22333 C CG  . PHE B  676 ? 0.7135 0.6418 0.5823 0.0094  0.0644  -0.0873 702 PHE B CG  
22334 C CD1 . PHE B  676 ? 0.7311 0.6692 0.5923 0.0083  0.0605  -0.0895 702 PHE B CD1 
22335 C CD2 . PHE B  676 ? 0.7278 0.6512 0.6022 0.0160  0.0699  -0.0816 702 PHE B CD2 
22336 C CE1 . PHE B  676 ? 0.7423 0.6846 0.6013 0.0138  0.0622  -0.0860 702 PHE B CE1 
22337 C CE2 . PHE B  676 ? 0.7404 0.6685 0.6131 0.0212  0.0715  -0.0783 702 PHE B CE2 
22338 C CZ  . PHE B  676 ? 0.7401 0.6772 0.6048 0.0200  0.0678  -0.0806 702 PHE B CZ  
22348 N N   . LEU B  677 ? 0.6879 0.6324 0.5569 -0.0090 0.0474  -0.0966 703 LEU B N   
22349 C CA  . LEU B  677 ? 0.6970 0.6535 0.5613 -0.0137 0.0408  -0.1001 703 LEU B CA  
22350 C C   . LEU B  677 ? 0.7110 0.6661 0.5620 -0.0163 0.0423  -0.1076 703 LEU B C   
22351 O O   . LEU B  677 ? 0.7214 0.6640 0.5664 -0.0174 0.0483  -0.1125 703 LEU B O   
22352 C CB  . LEU B  677 ? 0.7016 0.6581 0.5694 -0.0205 0.0376  -0.1031 703 LEU B CB  
22353 C CG  . LEU B  677 ? 0.7185 0.6857 0.5965 -0.0206 0.0316  -0.0975 703 LEU B CG  
22354 C CD1 . LEU B  677 ? 0.7190 0.6877 0.6060 -0.0136 0.0322  -0.0886 703 LEU B CD1 
22355 C CD2 . LEU B  677 ? 0.7328 0.6949 0.6152 -0.0261 0.0313  -0.0996 703 LEU B CD2 
22367 N N   . THR B  678 ? 0.7119 0.6799 0.5579 -0.0173 0.0370  -0.1085 704 THR B N   
22368 C CA  . THR B  678 ? 0.7236 0.6924 0.5564 -0.0201 0.0376  -0.1155 704 THR B CA  
22369 C C   . THR B  678 ? 0.7312 0.6943 0.5580 -0.0286 0.0378  -0.1246 704 THR B C   
22370 O O   . THR B  678 ? 0.7271 0.6930 0.5596 -0.0332 0.0342  -0.1252 704 THR B O   
22371 C CB  . THR B  678 ? 0.7375 0.7228 0.5670 -0.0194 0.0311  -0.1137 704 THR B CB  
22372 O OG1 . THR B  678 ? 0.7632 0.7488 0.5794 -0.0207 0.0326  -0.1195 704 THR B OG1 
22373 C CG2 . THR B  678 ? 0.7355 0.7325 0.5694 -0.0244 0.0236  -0.1142 704 THR B CG2 
22381 N N   . ASP B  679 ? 0.7385 0.6938 0.5535 -0.0310 0.0421  -0.1319 705 ASP B N   
22382 C CA  . ASP B  679 ? 0.7508 0.6999 0.5585 -0.0396 0.0428  -0.1414 705 ASP B CA  
22383 C C   . ASP B  679 ? 0.7557 0.7185 0.5548 -0.0455 0.0364  -0.1468 705 ASP B C   
22384 O O   . ASP B  679 ? 0.7617 0.7206 0.5531 -0.0532 0.0368  -0.1554 705 ASP B O   
22385 C CB  . ASP B  679 ? 0.7781 0.7098 0.5774 -0.0395 0.0516  -0.1470 705 ASP B CB  
22386 C CG  . ASP B  679 ? 0.8356 0.7683 0.6233 -0.0367 0.0541  -0.1494 705 ASP B CG  
22387 O OD1 . ASP B  679 ? 0.8365 0.7825 0.6245 -0.0326 0.0499  -0.1445 705 ASP B OD1 
22388 O OD2 . ASP B  679 ? 0.8706 0.7904 0.6491 -0.0383 0.0606  -0.1560 705 ASP B OD2 
22393 N N   . SER B  680 ? 0.7499 0.7288 0.5503 -0.0422 0.0305  -0.1417 706 SER B N   
22394 C CA  . SER B  680 ? 0.7501 0.7436 0.5427 -0.0467 0.0242  -0.1457 706 SER B CA  
22395 C C   . SER B  680 ? 0.7382 0.7489 0.5394 -0.0437 0.0168  -0.1382 706 SER B C   
22396 O O   . SER B  680 ? 0.7370 0.7596 0.5338 -0.0411 0.0132  -0.1360 706 SER B O   
22397 C CB  . SER B  680 ? 0.7746 0.7680 0.5543 -0.0446 0.0267  -0.1485 706 SER B CB  
22398 O OG  . SER B  680 ? 0.8215 0.7982 0.5934 -0.0465 0.0344  -0.1551 706 SER B OG  
22404 N N   . LEU B  681 ? 0.7263 0.7380 0.5393 -0.0442 0.0146  -0.1344 707 LEU B N   
22405 C CA  . LEU B  681 ? 0.7160 0.7426 0.5378 -0.0415 0.0081  -0.1275 707 LEU B CA  
22406 C C   . LEU B  681 ? 0.7052 0.7482 0.5226 -0.0463 0.0011  -0.1307 707 LEU B C   
22407 O O   . LEU B  681 ? 0.6961 0.7525 0.5163 -0.0423 -0.0036 -0.1251 707 LEU B O   
22408 C CB  . LEU B  681 ? 0.7188 0.7420 0.5534 -0.0418 0.0079  -0.1238 707 LEU B CB  
22409 C CG  . LEU B  681 ? 0.7317 0.7672 0.5767 -0.0378 0.0027  -0.1158 707 LEU B CG  
22410 C CD1 . LEU B  681 ? 0.7371 0.7751 0.5833 -0.0293 0.0036  -0.1086 707 LEU B CD1 
22411 C CD2 . LEU B  681 ? 0.7395 0.7693 0.5957 -0.0383 0.0035  -0.1127 707 LEU B CD2 
22423 N N   . SER B  682 ? 0.7037 0.7457 0.5141 -0.0547 0.0005  -0.1395 708 SER B N   
22424 C CA  . SER B  682 ? 0.6989 0.7569 0.5044 -0.0602 -0.0062 -0.1433 708 SER B CA  
22425 C C   . SER B  682 ? 0.6901 0.7575 0.4859 -0.0567 -0.0080 -0.1425 708 SER B C   
22426 O O   . SER B  682 ? 0.6832 0.7676 0.4783 -0.0576 -0.0144 -0.1413 708 SER B O   
22427 C CB  . SER B  682 ? 0.7227 0.7755 0.5218 -0.0703 -0.0054 -0.1535 708 SER B CB  
22428 O OG  . SER B  682 ? 0.7619 0.7988 0.5514 -0.0712 0.0015  -0.1590 708 SER B OG  
22434 N N   . ASP B  683 ? 0.6903 0.7473 0.4788 -0.0528 -0.0023 -0.1429 709 ASP B N   
22435 C CA  . ASP B  683 ? 0.6903 0.7548 0.4693 -0.0489 -0.0032 -0.1416 709 ASP B CA  
22436 C C   . ASP B  683 ? 0.6749 0.7487 0.4615 -0.0401 -0.0057 -0.1311 709 ASP B C   
22437 O O   . ASP B  683 ? 0.6735 0.7584 0.4542 -0.0373 -0.0087 -0.1287 709 ASP B O   
22438 C CB  . ASP B  683 ? 0.7237 0.7731 0.4932 -0.0470 0.0045  -0.1450 709 ASP B CB  
22439 C CG  . ASP B  683 ? 0.7958 0.8354 0.5551 -0.0553 0.0077  -0.1560 709 ASP B CG  
22440 O OD1 . ASP B  683 ? 0.8103 0.8574 0.5676 -0.0632 0.0031  -0.1616 709 ASP B OD1 
22441 O OD2 . ASP B  683 ? 0.8268 0.8513 0.5802 -0.0539 0.0150  -0.1590 709 ASP B OD2 
22446 N N   . PHE B  684 ? 0.6618 0.7304 0.4608 -0.0358 -0.0043 -0.1247 710 PHE B N   
22447 C CA  . PHE B  684 ? 0.6506 0.7257 0.4571 -0.0278 -0.0058 -0.1150 710 PHE B CA  
22448 C C   . PHE B  684 ? 0.6351 0.7231 0.4517 -0.0280 -0.0122 -0.1107 710 PHE B C   
22449 O O   . PHE B  684 ? 0.6355 0.7316 0.4564 -0.0220 -0.0145 -0.1033 710 PHE B O   
22450 C CB  . PHE B  684 ? 0.6497 0.7110 0.4626 -0.0222 0.0004  -0.1104 710 PHE B CB  
22451 C CG  . PHE B  684 ? 0.6627 0.7103 0.4669 -0.0218 0.0074  -0.1146 710 PHE B CG  
22452 C CD1 . PHE B  684 ? 0.6757 0.7258 0.4672 -0.0216 0.0083  -0.1178 710 PHE B CD1 
22453 C CD2 . PHE B  684 ? 0.6750 0.7072 0.4838 -0.0211 0.0134  -0.1150 710 PHE B CD2 
22454 C CE1 . PHE B  684 ? 0.6923 0.7296 0.4756 -0.0211 0.0152  -0.1218 710 PHE B CE1 
22455 C CE2 . PHE B  684 ? 0.6908 0.7103 0.4919 -0.0203 0.0203  -0.1187 710 PHE B CE2 
22456 C CZ  . PHE B  684 ? 0.6933 0.7151 0.4816 -0.0203 0.0213  -0.1223 710 PHE B CZ  
22466 N N   . THR B  685 ? 0.6166 0.7061 0.4372 -0.0347 -0.0147 -0.1150 711 THR B N   
22467 C CA  . THR B  685 ? 0.6017 0.7037 0.4319 -0.0349 -0.0205 -0.1111 711 THR B CA  
22468 C C   . THR B  685 ? 0.6000 0.7081 0.4298 -0.0437 -0.0242 -0.1178 711 THR B C   
22469 O O   . THR B  685 ? 0.6112 0.7089 0.4381 -0.0497 -0.0211 -0.1244 711 THR B O   
22470 C CB  . THR B  685 ? 0.6040 0.6997 0.4468 -0.0306 -0.0186 -0.1046 711 THR B CB  
22471 O OG1 . THR B  685 ? 0.5980 0.7065 0.4493 -0.0302 -0.0240 -0.1006 711 THR B OG1 
22472 C CG2 . THR B  685 ? 0.6124 0.6935 0.4587 -0.0346 -0.0143 -0.1082 711 THR B CG2 
22480 N N   . SER B  686 ? 0.5861 0.7112 0.4192 -0.0444 -0.0306 -0.1158 712 SER B N   
22481 C CA  . SER B  686 ? 0.5793 0.7133 0.4139 -0.0524 -0.0350 -0.1209 712 SER B CA  
22482 C C   . SER B  686 ? 0.5560 0.7006 0.4034 -0.0506 -0.0391 -0.1153 712 SER B C   
22483 O O   . SER B  686 ? 0.5567 0.7106 0.4068 -0.0567 -0.0430 -0.1185 712 SER B O   
22484 C CB  . SER B  686 ? 0.6048 0.7522 0.4293 -0.0560 -0.0393 -0.1252 712 SER B CB  
22485 O OG  . SER B  686 ? 0.6393 0.8016 0.4650 -0.0498 -0.0435 -0.1184 712 SER B OG  
22491 N N   . SER B  687 ? 0.5332 0.6758 0.3882 -0.0428 -0.0380 -0.1071 713 SER B N   
22492 C CA  . SER B  687 ? 0.5095 0.6605 0.3760 -0.0405 -0.0411 -0.1016 713 SER B CA  
22493 C C   . SER B  687 ? 0.4929 0.6314 0.3685 -0.0396 -0.0374 -0.0993 713 SER B C   
22494 O O   . SER B  687 ? 0.4805 0.6242 0.3653 -0.0400 -0.0396 -0.0967 713 SER B O   
22495 C CB  . SER B  687 ? 0.5167 0.6770 0.3848 -0.0322 -0.0432 -0.0938 713 SER B CB  
22496 O OG  . SER B  687 ? 0.5326 0.6820 0.3976 -0.0263 -0.0387 -0.0904 713 SER B OG  
22502 N N   . LEU B  688 ? 0.4855 0.6079 0.3586 -0.0380 -0.0317 -0.0997 714 LEU B N   
22503 C CA  . LEU B  688 ? 0.4771 0.5878 0.3583 -0.0367 -0.0282 -0.0969 714 LEU B CA  
22504 C C   . LEU B  688 ? 0.4653 0.5745 0.3514 -0.0438 -0.0288 -0.1010 714 LEU B C   
22505 O O   . LEU B  688 ? 0.4781 0.5831 0.3586 -0.0504 -0.0278 -0.1080 714 LEU B O   
22506 C CB  . LEU B  688 ? 0.4829 0.5775 0.3596 -0.0344 -0.0220 -0.0975 714 LEU B CB  
22507 C CG  . LEU B  688 ? 0.4972 0.5809 0.3821 -0.0308 -0.0182 -0.0926 714 LEU B CG  
22508 C CD1 . LEU B  688 ? 0.4974 0.5873 0.3886 -0.0237 -0.0199 -0.0845 714 LEU B CD1 
22509 C CD2 . LEU B  688 ? 0.5056 0.5745 0.3857 -0.0292 -0.0121 -0.0940 714 LEU B CD2 
22521 N N   . ARG B  689 ? 0.4387 0.5517 0.3349 -0.0427 -0.0305 -0.0967 715 ARG B N   
22522 C CA  . ARG B  689 ? 0.4281 0.5407 0.3301 -0.0489 -0.0311 -0.0994 715 ARG B CA  
22523 C C   . ARG B  689 ? 0.4071 0.5058 0.3150 -0.0477 -0.0268 -0.0968 715 ARG B C   
22524 O O   . ARG B  689 ? 0.4149 0.5071 0.3244 -0.0533 -0.0252 -0.1004 715 ARG B O   
22525 C CB  . ARG B  689 ? 0.4511 0.5793 0.3604 -0.0486 -0.0362 -0.0964 715 ARG B CB  
22526 C CG  . ARG B  689 ? 0.5184 0.6626 0.4234 -0.0504 -0.0412 -0.0988 715 ARG B CG  
22527 C CD  . ARG B  689 ? 0.5866 0.7455 0.5002 -0.0491 -0.0455 -0.0948 715 ARG B CD  
22528 N NE  . ARG B  689 ? 0.6547 0.8306 0.5653 -0.0505 -0.0506 -0.0963 715 ARG B NE  
22529 C CZ  . ARG B  689 ? 0.6994 0.8904 0.6167 -0.0492 -0.0547 -0.0932 715 ARG B CZ  
22530 N NH1 . ARG B  689 ? 0.6991 0.8897 0.6258 -0.0466 -0.0542 -0.0888 715 ARG B NH1 
22531 N NH2 . ARG B  689 ? 0.7006 0.9075 0.6150 -0.0505 -0.0593 -0.0945 715 ARG B NH2 
22545 N N   . THR B  690 ? 0.3777 0.4724 0.2890 -0.0406 -0.0250 -0.0904 716 THR B N   
22546 C CA  . THR B  690 ? 0.3656 0.4487 0.2829 -0.0389 -0.0213 -0.0871 716 THR B CA  
22547 C C   . THR B  690 ? 0.3541 0.4269 0.2684 -0.0334 -0.0170 -0.0844 716 THR B C   
22548 O O   . THR B  690 ? 0.3513 0.4287 0.2640 -0.0280 -0.0178 -0.0808 716 THR B O   
22549 C CB  . THR B  690 ? 0.3766 0.4664 0.3032 -0.0362 -0.0237 -0.0815 716 THR B CB  
22550 O OG1 . THR B  690 ? 0.3895 0.4887 0.3192 -0.0415 -0.0272 -0.0842 716 THR B OG1 
22551 C CG2 . THR B  690 ? 0.3815 0.4606 0.3141 -0.0345 -0.0203 -0.0777 716 THR B CG2 
22559 N N   . LEU B  691 ? 0.3458 0.4049 0.2593 -0.0348 -0.0123 -0.0860 717 LEU B N   
22560 C CA  . LEU B  691 ? 0.3445 0.3935 0.2556 -0.0298 -0.0077 -0.0837 717 LEU B CA  
22561 C C   . LEU B  691 ? 0.3490 0.3885 0.2674 -0.0286 -0.0046 -0.0800 717 LEU B C   
22562 O O   . LEU B  691 ? 0.3548 0.3862 0.2737 -0.0330 -0.0023 -0.0830 717 LEU B O   
22563 C CB  . LEU B  691 ? 0.3472 0.3884 0.2485 -0.0324 -0.0044 -0.0900 717 LEU B CB  
22564 C CG  . LEU B  691 ? 0.3602 0.3903 0.2587 -0.0274 0.0012  -0.0881 717 LEU B CG  
22565 C CD1 . LEU B  691 ? 0.3627 0.3986 0.2619 -0.0204 0.0003  -0.0822 717 LEU B CD1 
22566 C CD2 . LEU B  691 ? 0.3723 0.3952 0.2603 -0.0304 0.0044  -0.0951 717 LEU B CD2 
22578 N N   . LEU B  692 ? 0.3417 0.3825 0.2660 -0.0231 -0.0046 -0.0732 718 LEU B N   
22579 C CA  . LEU B  692 ? 0.3480 0.3814 0.2794 -0.0218 -0.0021 -0.0691 718 LEU B CA  
22580 C C   . LEU B  692 ? 0.3555 0.3791 0.2857 -0.0172 0.0028  -0.0666 718 LEU B C   
22581 O O   . LEU B  692 ? 0.3572 0.3836 0.2867 -0.0122 0.0030  -0.0631 718 LEU B O   
22582 C CB  . LEU B  692 ? 0.3475 0.3886 0.2867 -0.0196 -0.0054 -0.0635 718 LEU B CB  
22583 C CG  . LEU B  692 ? 0.3653 0.4179 0.3062 -0.0229 -0.0103 -0.0652 718 LEU B CG  
22584 C CD1 . LEU B  692 ? 0.3636 0.4225 0.3116 -0.0199 -0.0126 -0.0595 718 LEU B CD1 
22585 C CD2 . LEU B  692 ? 0.3677 0.4180 0.3094 -0.0297 -0.0105 -0.0696 718 LEU B CD2 
22597 N N   . LEU B  693 ? 0.3533 0.3653 0.2833 -0.0188 0.0071  -0.0683 719 LEU B N   
22598 C CA  . LEU B  693 ? 0.3620 0.3643 0.2912 -0.0146 0.0124  -0.0661 719 LEU B CA  
22599 C C   . LEU B  693 ? 0.3657 0.3602 0.3021 -0.0136 0.0152  -0.0620 719 LEU B C   
22600 O O   . LEU B  693 ? 0.3739 0.3594 0.3100 -0.0106 0.0200  -0.0608 719 LEU B O   
22601 C CB  . LEU B  693 ? 0.3729 0.3674 0.2931 -0.0168 0.0159  -0.0727 719 LEU B CB  
22602 C CG  . LEU B  693 ? 0.3943 0.3952 0.3060 -0.0166 0.0143  -0.0762 719 LEU B CG  
22603 C CD1 . LEU B  693 ? 0.4003 0.3948 0.3032 -0.0214 0.0166  -0.0842 719 LEU B CD1 
22604 C CD2 . LEU B  693 ? 0.4081 0.4084 0.3185 -0.0100 0.0168  -0.0723 719 LEU B CD2 
22616 N N   . SER B  694 ? 0.3575 0.3559 0.3005 -0.0157 0.0123  -0.0595 720 SER B N   
22617 C CA  . SER B  694 ? 0.3594 0.3513 0.3089 -0.0149 0.0146  -0.0553 720 SER B CA  
22618 C C   . SER B  694 ? 0.3520 0.3432 0.3060 -0.0086 0.0165  -0.0488 720 SER B C   
22619 O O   . SER B  694 ? 0.3430 0.3410 0.2969 -0.0054 0.0147  -0.0465 720 SER B O   
22620 C CB  . SER B  694 ? 0.3776 0.3747 0.3326 -0.0184 0.0110  -0.0540 720 SER B CB  
22621 O OG  . SER B  694 ? 0.4193 0.4268 0.3780 -0.0163 0.0069  -0.0503 720 SER B OG  
22627 N N   . HIS B  695 ? 0.3487 0.3316 0.3065 -0.0070 0.0203  -0.0456 721 HIS B N   
22628 C CA  . HIS B  695 ? 0.3499 0.3322 0.3126 -0.0014 0.0224  -0.0393 721 HIS B CA  
22629 C C   . HIS B  695 ? 0.3565 0.3376 0.3145 0.0026  0.0252  -0.0400 721 HIS B C   
22630 O O   . HIS B  695 ? 0.3602 0.3475 0.3197 0.0060  0.0239  -0.0366 721 HIS B O   
22631 C CB  . HIS B  695 ? 0.3457 0.3372 0.3151 -0.0003 0.0183  -0.0338 721 HIS B CB  
22632 C CG  . HIS B  695 ? 0.3632 0.3541 0.3381 -0.0031 0.0170  -0.0316 721 HIS B CG  
22633 N ND1 . HIS B  695 ? 0.3862 0.3714 0.3661 -0.0011 0.0200  -0.0270 721 HIS B ND1 
22634 C CD2 . HIS B  695 ? 0.3693 0.3645 0.3450 -0.0075 0.0134  -0.0333 721 HIS B CD2 
22635 C CE1 . HIS B  695 ? 0.3843 0.3706 0.3676 -0.0044 0.0180  -0.0259 721 HIS B CE1 
22636 N NE2 . HIS B  695 ? 0.3808 0.3729 0.3617 -0.0084 0.0142  -0.0298 721 HIS B NE2 
22644 N N   . ASN B  696 ? 0.3588 0.3312 0.3107 0.0019  0.0293  -0.0447 722 ASN B N   
22645 C CA  . ASN B  696 ? 0.3667 0.3360 0.3134 0.0056  0.0330  -0.0459 722 ASN B CA  
22646 C C   . ASN B  696 ? 0.3970 0.3535 0.3434 0.0072  0.0396  -0.0464 722 ASN B C   
22647 O O   . ASN B  696 ? 0.4006 0.3526 0.3526 0.0066  0.0406  -0.0437 722 ASN B O   
22648 C CB  . ASN B  696 ? 0.3541 0.3272 0.2916 0.0029  0.0309  -0.0524 722 ASN B CB  
22649 C CG  . ASN B  696 ? 0.3506 0.3355 0.2884 0.0044  0.0263  -0.0501 722 ASN B CG  
22650 O OD1 . ASN B  696 ? 0.3510 0.3379 0.2886 0.0090  0.0277  -0.0469 722 ASN B OD1 
22651 N ND2 . ASN B  696 ? 0.3360 0.3288 0.2743 0.0009  0.0211  -0.0514 722 ASN B ND2 
22658 N N   . ARG B  697 ? 0.4183 0.3688 0.3585 0.0096  0.0442  -0.0491 723 ARG B N   
22659 C CA  . ARG B  697 ? 0.4395 0.3775 0.3794 0.0116  0.0510  -0.0496 723 ARG B CA  
22660 C C   . ARG B  697 ? 0.4576 0.3873 0.3870 0.0083  0.0541  -0.0581 723 ARG B C   
22661 O O   . ARG B  697 ? 0.4648 0.3859 0.3904 0.0112  0.0601  -0.0596 723 ARG B O   
22662 C CB  . ARG B  697 ? 0.4621 0.3999 0.4056 0.0186  0.0549  -0.0439 723 ARG B CB  
22663 C CG  . ARG B  697 ? 0.5009 0.4474 0.4546 0.0213  0.0517  -0.0358 723 ARG B CG  
22664 C CD  . ARG B  697 ? 0.5590 0.5068 0.5167 0.0276  0.0552  -0.0303 723 ARG B CD  
22665 N NE  . ARG B  697 ? 0.6114 0.5676 0.5787 0.0293  0.0518  -0.0228 723 ARG B NE  
22666 C CZ  . ARG B  697 ? 0.6456 0.6057 0.6184 0.0342  0.0535  -0.0169 723 ARG B CZ  
22667 N NH1 . ARG B  697 ? 0.6447 0.6011 0.6147 0.0383  0.0588  -0.0171 723 ARG B NH1 
22668 N NH2 . ARG B  697 ? 0.6416 0.6096 0.6228 0.0347  0.0500  -0.0107 723 ARG B NH2 
22682 N N   . ILE B  698 ? 0.4663 0.3988 0.3910 0.0019  0.0501  -0.0638 724 ILE B N   
22683 C CA  . ILE B  698 ? 0.4915 0.4168 0.4061 -0.0023 0.0525  -0.0725 724 ILE B CA  
22684 C C   . ILE B  698 ? 0.5090 0.4201 0.4245 -0.0038 0.0579  -0.0740 724 ILE B C   
22685 O O   . ILE B  698 ? 0.5059 0.4166 0.4265 -0.0069 0.0559  -0.0726 724 ILE B O   
22686 C CB  . ILE B  698 ? 0.5038 0.4376 0.4138 -0.0089 0.0463  -0.0779 724 ILE B CB  
22687 C CG1 . ILE B  698 ? 0.5155 0.4640 0.4257 -0.0072 0.0406  -0.0753 724 ILE B CG1 
22688 C CG2 . ILE B  698 ? 0.5176 0.4443 0.4166 -0.0138 0.0489  -0.0871 724 ILE B CG2 
22689 C CD1 . ILE B  698 ? 0.5393 0.4891 0.4446 -0.0024 0.0428  -0.0747 724 ILE B CD1 
22701 N N   . SER B  699 ? 0.5255 0.4249 0.4363 -0.0013 0.0649  -0.0765 725 SER B N   
22702 C CA  . SER B  699 ? 0.5461 0.4303 0.4572 -0.0022 0.0710  -0.0780 725 SER B CA  
22703 C C   . SER B  699 ? 0.5656 0.4408 0.4662 -0.0088 0.0733  -0.0881 725 SER B C   
22704 O O   . SER B  699 ? 0.5678 0.4300 0.4682 -0.0106 0.0780  -0.0901 725 SER B O   
22705 C CB  . SER B  699 ? 0.5665 0.4424 0.4800 0.0053  0.0782  -0.0739 725 SER B CB  
22706 O OG  . SER B  699 ? 0.5995 0.4730 0.5041 0.0069  0.0816  -0.0785 725 SER B OG  
22712 N N   . HIS B  700 ? 0.5829 0.4647 0.4749 -0.0124 0.0700  -0.0943 726 HIS B N   
22713 C CA  . HIS B  700 ? 0.6161 0.4903 0.4975 -0.0191 0.0719  -0.1042 726 HIS B CA  
22714 C C   . HIS B  700 ? 0.6321 0.5195 0.5073 -0.0241 0.0650  -0.1090 726 HIS B C   
22715 O O   . HIS B  700 ? 0.6343 0.5328 0.5090 -0.0205 0.0618  -0.1062 726 HIS B O   
22716 C CB  . HIS B  700 ? 0.6475 0.5090 0.5214 -0.0157 0.0800  -0.1077 726 HIS B CB  
22717 C CG  . HIS B  700 ? 0.7124 0.5659 0.5739 -0.0223 0.0825  -0.1184 726 HIS B CG  
22718 N ND1 . HIS B  700 ? 0.7509 0.5897 0.6102 -0.0271 0.0871  -0.1233 726 HIS B ND1 
22719 C CD2 . HIS B  700 ? 0.7359 0.5937 0.5865 -0.0248 0.0813  -0.1249 726 HIS B CD2 
22720 C CE1 . HIS B  700 ? 0.7623 0.5971 0.6095 -0.0327 0.0884  -0.1330 726 HIS B CE1 
22721 N NE2 . HIS B  700 ? 0.7576 0.6039 0.5991 -0.0315 0.0849  -0.1342 726 HIS B NE2 
22729 N N   . LEU B  701 ? 0.6437 0.5301 0.5141 -0.0323 0.0630  -0.1159 727 LEU B N   
22730 C CA  . LEU B  701 ? 0.6637 0.5626 0.5279 -0.0376 0.0567  -0.1210 727 LEU B CA  
22731 C C   . LEU B  701 ? 0.7050 0.5970 0.5561 -0.0405 0.0604  -0.1298 727 LEU B C   
22732 O O   . LEU B  701 ? 0.7115 0.5888 0.5584 -0.0439 0.0661  -0.1351 727 LEU B O   
22733 C CB  . LEU B  701 ? 0.6575 0.5607 0.5244 -0.0454 0.0520  -0.1237 727 LEU B CB  
22734 C CG  . LEU B  701 ? 0.6587 0.5694 0.5378 -0.0436 0.0479  -0.1158 727 LEU B CG  
22735 C CD1 . LEU B  701 ? 0.6572 0.5728 0.5378 -0.0517 0.0435  -0.1192 727 LEU B CD1 
22736 C CD2 . LEU B  701 ? 0.6587 0.5844 0.5419 -0.0381 0.0427  -0.1095 727 LEU B CD2 
22748 N N   . PRO B  702 ? 0.7296 0.6313 0.5735 -0.0394 0.0577  -0.1317 728 PRO B N   
22749 C CA  . PRO B  702 ? 0.7585 0.6534 0.5890 -0.0427 0.0615  -0.1406 728 PRO B CA  
22750 C C   . PRO B  702 ? 0.7925 0.6858 0.6162 -0.0530 0.0597  -0.1499 728 PRO B C   
22751 O O   . PRO B  702 ? 0.7907 0.6928 0.6193 -0.0577 0.0538  -0.1495 728 PRO B O   
22752 C CB  . PRO B  702 ? 0.7601 0.6682 0.5855 -0.0393 0.0578  -0.1393 728 PRO B CB  
22753 C CG  . PRO B  702 ? 0.7514 0.6715 0.5876 -0.0338 0.0530  -0.1298 728 PRO B CG  
22754 C CD  . PRO B  702 ? 0.7217 0.6401 0.5689 -0.0353 0.0516  -0.1260 728 PRO B CD  
22762 N N   . SER B  703 ? 0.8243 0.7065 0.6363 -0.0567 0.0648  -0.1586 729 SER B N   
22763 C CA  . SER B  703 ? 0.8561 0.7360 0.6605 -0.0671 0.0636  -0.1683 729 SER B CA  
22764 C C   . SER B  703 ? 0.8819 0.7819 0.6827 -0.0715 0.0545  -0.1704 729 SER B C   
22765 O O   . SER B  703 ? 0.8807 0.7896 0.6762 -0.0679 0.0527  -0.1695 729 SER B O   
22766 C CB  . SER B  703 ? 0.8849 0.7489 0.6766 -0.0696 0.0713  -0.1771 729 SER B CB  
22767 O OG  . SER B  703 ? 0.9173 0.7646 0.7112 -0.0630 0.0801  -0.1742 729 SER B OG  
22773 N N   . GLY B  704 ? 0.9056 0.8128 0.7097 -0.0790 0.0492  -0.1727 730 GLY B N   
22774 C CA  . GLY B  704 ? 0.9290 0.8561 0.7316 -0.0831 0.0405  -0.1740 730 GLY B CA  
22775 C C   . GLY B  704 ? 0.9499 0.8925 0.7618 -0.0761 0.0347  -0.1642 730 GLY B C   
22776 O O   . GLY B  704 ? 0.9459 0.9013 0.7536 -0.0737 0.0307  -0.1632 730 GLY B O   
22780 N N   . PHE B  705 ? 0.9707 0.9120 0.7950 -0.0727 0.0345  -0.1570 731 PHE B N   
22781 C CA  . PHE B  705 ? 0.9886 0.9434 0.8220 -0.0662 0.0296  -0.1478 731 PHE B CA  
22782 C C   . PHE B  705 ? 1.0038 0.9732 0.8438 -0.0709 0.0221  -0.1468 731 PHE B C   
22783 O O   . PHE B  705 ? 1.0027 0.9882 0.8427 -0.0698 0.0161  -0.1448 731 PHE B O   
22784 C CB  . PHE B  705 ? 0.9931 0.9388 0.8360 -0.0586 0.0339  -0.1397 731 PHE B CB  
22785 C CG  . PHE B  705 ? 0.9998 0.9585 0.8520 -0.0525 0.0290  -0.1306 731 PHE B CG  
22786 C CD1 . PHE B  705 ? 1.0105 0.9778 0.8603 -0.0467 0.0273  -0.1271 731 PHE B CD1 
22787 C CD2 . PHE B  705 ? 1.0067 0.9695 0.8695 -0.0532 0.0260  -0.1259 731 PHE B CD2 
22788 C CE1 . PHE B  705 ? 1.0138 0.9928 0.8718 -0.0417 0.0228  -0.1192 731 PHE B CE1 
22789 C CE2 . PHE B  705 ? 1.0108 0.9853 0.8815 -0.0481 0.0215  -0.1182 731 PHE B CE2 
22790 C CZ  . PHE B  705 ? 1.0074 0.9898 0.8756 -0.0425 0.0200  -0.1150 731 PHE B CZ  
22800 N N   . LEU B  706 ? 1.0156 0.9792 0.8611 -0.0759 0.0229  -0.1480 732 LEU B N   
22801 C CA  . LEU B  706 ? 1.0236 1.0000 0.8765 -0.0801 0.0166  -0.1465 732 LEU B CA  
22802 C C   . LEU B  706 ? 1.0282 1.0158 0.8749 -0.0886 0.0117  -0.1539 732 LEU B C   
22803 O O   . LEU B  706 ? 1.0247 1.0278 0.8768 -0.0903 0.0054  -0.1518 732 LEU B O   
22804 C CB  . LEU B  706 ? 1.0309 0.9968 0.8916 -0.0826 0.0196  -0.1451 732 LEU B CB  
22805 C CG  . LEU B  706 ? 1.0553 1.0125 0.9243 -0.0747 0.0234  -0.1366 732 LEU B CG  
22806 C CD1 . LEU B  706 ? 1.0714 1.0091 0.9361 -0.0728 0.0317  -0.1385 732 LEU B CD1 
22807 C CD2 . LEU B  706 ? 1.0614 1.0197 0.9408 -0.0765 0.0218  -0.1325 732 LEU B CD2 
22819 N N   . SER B  707 ? 1.0327 1.0130 0.8683 -0.0940 0.0145  -0.1625 733 SER B N   
22820 C CA  . SER B  707 ? 1.0372 1.0274 0.8665 -0.1032 0.0102  -0.1702 733 SER B CA  
22821 C C   . SER B  707 ? 1.0304 1.0392 0.8547 -0.1019 0.0039  -0.1702 733 SER B C   
22822 O O   . SER B  707 ? 1.0300 1.0546 0.8562 -0.1068 -0.0025 -0.1716 733 SER B O   
22823 C CB  . SER B  707 ? 1.0674 1.0422 0.8861 -0.1101 0.0158  -0.1800 733 SER B CB  
22824 O OG  . SER B  707 ? 1.1076 1.0771 0.9162 -0.1062 0.0192  -0.1822 733 SER B OG  
22830 N N   . GLU B  708 ? 1.0205 1.0277 0.8381 -0.0956 0.0058  -0.1689 734 GLU B N   
22831 C CA  . GLU B  708 ? 1.0103 1.0334 0.8212 -0.0946 0.0007  -0.1694 734 GLU B CA  
22832 C C   . GLU B  708 ? 0.9859 1.0272 0.8051 -0.0887 -0.0059 -0.1609 734 GLU B C   
22833 O O   . GLU B  708 ? 0.9840 1.0414 0.7992 -0.0903 -0.0116 -0.1620 734 GLU B O   
22834 C CB  . GLU B  708 ? 1.0496 1.0643 0.8500 -0.0900 0.0054  -0.1708 734 GLU B CB  
22835 C CG  . GLU B  708 ? 1.1266 1.1241 0.9169 -0.0958 0.0119  -0.1801 734 GLU B CG  
22836 C CD  . GLU B  708 ? 1.2114 1.2132 0.9944 -0.1073 0.0092  -0.1899 734 GLU B CD  
22837 O OE1 . GLU B  708 ? 1.2258 1.2378 0.9988 -0.1100 0.0059  -0.1943 734 GLU B OE1 
22838 O OE2 . GLU B  708 ? 1.2406 1.2359 1.0279 -0.1137 0.0103  -0.1931 734 GLU B OE2 
22845 N N   . VAL B  709 ? 0.9647 1.0039 0.7950 -0.0820 -0.0051 -0.1525 735 VAL B N   
22846 C CA  . VAL B  709 ? 0.9420 0.9973 0.7798 -0.0765 -0.0108 -0.1447 735 VAL B CA  
22847 C C   . VAL B  709 ? 0.9099 0.9777 0.7543 -0.0825 -0.0164 -0.1457 735 VAL B C   
22848 O O   . VAL B  709 ? 0.9119 0.9762 0.7657 -0.0832 -0.0158 -0.1430 735 VAL B O   
22849 C CB  . VAL B  709 ? 0.9544 1.0040 0.8012 -0.0675 -0.0082 -0.1356 735 VAL B CB  
22850 C CG1 . VAL B  709 ? 0.9556 1.0209 0.8074 -0.0613 -0.0134 -0.1282 735 VAL B CG1 
22851 C CG2 . VAL B  709 ? 0.9697 1.0045 0.8110 -0.0626 -0.0015 -0.1353 735 VAL B CG2 
22861 N N   . SER B  710 ? 0.8776 0.9602 0.7168 -0.0872 -0.0217 -0.1497 736 SER B N   
22862 C CA  . SER B  710 ? 0.8443 0.9403 0.6892 -0.0935 -0.0271 -0.1513 736 SER B CA  
22863 C C   . SER B  710 ? 0.7969 0.9040 0.6541 -0.0882 -0.0308 -0.1428 736 SER B C   
22864 O O   . SER B  710 ? 0.7985 0.9087 0.6635 -0.0923 -0.0323 -0.1429 736 SER B O   
22865 C CB  . SER B  710 ? 0.8592 0.9702 0.6958 -0.0989 -0.0321 -0.1567 736 SER B CB  
22866 O OG  . SER B  710 ? 0.8876 1.0082 0.7198 -0.0921 -0.0346 -0.1526 736 SER B OG  
22872 N N   . SER B  711 ? 0.7541 0.8668 0.6127 -0.0793 -0.0320 -0.1357 737 SER B N   
22873 C CA  . SER B  711 ? 0.7122 0.8348 0.5819 -0.0740 -0.0353 -0.1278 737 SER B CA  
22874 C C   . SER B  711 ? 0.6595 0.7698 0.5381 -0.0708 -0.0313 -0.1233 737 SER B C   
22875 O O   . SER B  711 ? 0.6572 0.7747 0.5452 -0.0685 -0.0338 -0.1182 737 SER B O   
22876 C CB  . SER B  711 ? 0.7311 0.8632 0.5993 -0.0658 -0.0376 -0.1218 737 SER B CB  
22877 O OG  . SER B  711 ? 0.7636 0.8831 0.6266 -0.0604 -0.0327 -0.1202 737 SER B OG  
22883 N N   . LEU B  712 ? 0.6223 0.7146 0.4980 -0.0703 -0.0253 -0.1247 738 LEU B N   
22884 C CA  . LEU B  712 ? 0.5913 0.6724 0.4752 -0.0669 -0.0216 -0.1198 738 LEU B CA  
22885 C C   . LEU B  712 ? 0.5470 0.6271 0.4381 -0.0729 -0.0220 -0.1213 738 LEU B C   
22886 O O   . LEU B  712 ? 0.5467 0.6198 0.4344 -0.0801 -0.0201 -0.1277 738 LEU B O   
22887 C CB  . LEU B  712 ? 0.6025 0.6656 0.4816 -0.0645 -0.0150 -0.1207 738 LEU B CB  
22888 C CG  . LEU B  712 ? 0.6246 0.6779 0.5113 -0.0583 -0.0113 -0.1139 738 LEU B CG  
22889 C CD1 . LEU B  712 ? 0.6261 0.6882 0.5170 -0.0504 -0.0138 -0.1062 738 LEU B CD1 
22890 C CD2 . LEU B  712 ? 0.6404 0.6768 0.5220 -0.0565 -0.0047 -0.1155 738 LEU B CD2 
22902 N N   . LYS B  713 ? 0.5084 0.5955 0.4093 -0.0700 -0.0244 -0.1154 739 LYS B N   
22903 C CA  . LYS B  713 ? 0.4847 0.5723 0.3932 -0.0748 -0.0250 -0.1156 739 LYS B CA  
22904 C C   . LYS B  713 ? 0.4621 0.5358 0.3762 -0.0718 -0.0205 -0.1113 739 LYS B C   
22905 O O   . LYS B  713 ? 0.4663 0.5325 0.3830 -0.0768 -0.0183 -0.1134 739 LYS B O   
22906 C CB  . LYS B  713 ? 0.5005 0.6056 0.4161 -0.0734 -0.0305 -0.1118 739 LYS B CB  
22907 C CG  . LYS B  713 ? 0.5566 0.6781 0.4682 -0.0764 -0.0356 -0.1153 739 LYS B CG  
22908 C CD  . LYS B  713 ? 0.6205 0.7435 0.5285 -0.0866 -0.0364 -0.1234 739 LYS B CD  
22909 C CE  . LYS B  713 ? 0.6668 0.7899 0.5827 -0.0921 -0.0364 -0.1240 739 LYS B CE  
22910 N NZ  . LYS B  713 ? 0.6912 0.8186 0.6040 -0.1022 -0.0379 -0.1316 739 LYS B NZ  
22924 N N   . HIS B  714 ? 0.4328 0.5037 0.3491 -0.0637 -0.0192 -0.1050 740 HIS B N   
22925 C CA  . HIS B  714 ? 0.4167 0.4766 0.3388 -0.0603 -0.0155 -0.1001 740 HIS B CA  
22926 C C   . HIS B  714 ? 0.3984 0.4469 0.3162 -0.0549 -0.0111 -0.0984 740 HIS B C   
22927 O O   . HIS B  714 ? 0.3899 0.4431 0.3058 -0.0493 -0.0121 -0.0955 740 HIS B O   
22928 C CB  . HIS B  714 ? 0.4196 0.4889 0.3501 -0.0559 -0.0186 -0.0934 740 HIS B CB  
22929 C CG  . HIS B  714 ? 0.4567 0.5173 0.3936 -0.0525 -0.0157 -0.0880 740 HIS B CG  
22930 N ND1 . HIS B  714 ? 0.4783 0.5454 0.4219 -0.0483 -0.0178 -0.0821 740 HIS B ND1 
22931 C CD2 . HIS B  714 ? 0.4815 0.5279 0.4186 -0.0529 -0.0111 -0.0876 740 HIS B CD2 
22932 C CE1 . HIS B  714 ? 0.4887 0.5461 0.4363 -0.0465 -0.0147 -0.0784 740 HIS B CE1 
22933 N NE2 . HIS B  714 ? 0.4952 0.5403 0.4394 -0.0489 -0.0106 -0.0813 740 HIS B NE2 
22941 N N   . LEU B  715 ? 0.3861 0.4197 0.3026 -0.0565 -0.0060 -0.1002 741 LEU B N   
22942 C CA  . LEU B  715 ? 0.3823 0.4041 0.2959 -0.0515 -0.0011 -0.0984 741 LEU B CA  
22943 C C   . LEU B  715 ? 0.3782 0.3911 0.2992 -0.0492 0.0020  -0.0932 741 LEU B C   
22944 O O   . LEU B  715 ? 0.3842 0.3908 0.3074 -0.0538 0.0036  -0.0950 741 LEU B O   
22945 C CB  . LEU B  715 ? 0.3889 0.4006 0.2933 -0.0555 0.0028  -0.1056 741 LEU B CB  
22946 C CG  . LEU B  715 ? 0.4091 0.4062 0.3105 -0.0511 0.0091  -0.1046 741 LEU B CG  
22947 C CD1 . LEU B  715 ? 0.4064 0.4076 0.3073 -0.0433 0.0089  -0.0996 741 LEU B CD1 
22948 C CD2 . LEU B  715 ? 0.4196 0.4074 0.3114 -0.0559 0.0127  -0.1127 741 LEU B CD2 
22960 N N   . ASP B  716 ? 0.3597 0.3725 0.2847 -0.0423 0.0027  -0.0866 742 ASP B N   
22961 C CA  . ASP B  716 ? 0.3613 0.3671 0.2934 -0.0398 0.0052  -0.0812 742 ASP B CA  
22962 C C   . ASP B  716 ? 0.3597 0.3538 0.2898 -0.0351 0.0106  -0.0794 742 ASP B C   
22963 O O   . ASP B  716 ? 0.3547 0.3512 0.2842 -0.0295 0.0109  -0.0762 742 ASP B O   
22964 C CB  . ASP B  716 ? 0.3800 0.3959 0.3194 -0.0364 0.0013  -0.0750 742 ASP B CB  
22965 C CG  . ASP B  716 ? 0.4573 0.4679 0.4036 -0.0327 0.0034  -0.0686 742 ASP B CG  
22966 O OD1 . ASP B  716 ? 0.4573 0.4574 0.4048 -0.0342 0.0071  -0.0686 742 ASP B OD1 
22967 O OD2 . ASP B  716 ? 0.5068 0.5237 0.4572 -0.0284 0.0014  -0.0634 742 ASP B OD2 
22972 N N   . LEU B  717 ? 0.3640 0.3454 0.2930 -0.0374 0.0153  -0.0816 743 LEU B N   
22973 C CA  . LEU B  717 ? 0.3755 0.3449 0.3032 -0.0330 0.0212  -0.0799 743 LEU B CA  
22974 C C   . LEU B  717 ? 0.3764 0.3391 0.3121 -0.0309 0.0236  -0.0740 743 LEU B C   
22975 O O   . LEU B  717 ? 0.3836 0.3346 0.3189 -0.0287 0.0290  -0.0732 743 LEU B O   
22976 C CB  . LEU B  717 ? 0.3848 0.3435 0.3042 -0.0369 0.0254  -0.0874 743 LEU B CB  
22977 C CG  . LEU B  717 ? 0.4071 0.3704 0.3173 -0.0380 0.0242  -0.0931 743 LEU B CG  
22978 C CD1 . LEU B  717 ? 0.4147 0.3688 0.3169 -0.0443 0.0272  -0.1015 743 LEU B CD1 
22979 C CD2 . LEU B  717 ? 0.4198 0.3819 0.3277 -0.0310 0.0267  -0.0901 743 LEU B CD2 
22991 N N   . SER B  718 ? 0.3722 0.3427 0.3151 -0.0313 0.0198  -0.0696 744 SER B N   
22992 C CA  . SER B  718 ? 0.3829 0.3482 0.3329 -0.0297 0.0216  -0.0639 744 SER B CA  
22993 C C   . SER B  718 ? 0.3891 0.3526 0.3426 -0.0225 0.0239  -0.0575 744 SER B C   
22994 O O   . SER B  718 ? 0.3957 0.3645 0.3475 -0.0188 0.0229  -0.0567 744 SER B O   
22995 C CB  . SER B  718 ? 0.4036 0.3779 0.3593 -0.0324 0.0170  -0.0615 744 SER B CB  
22996 O OG  . SER B  718 ? 0.4281 0.4142 0.3863 -0.0294 0.0127  -0.0584 744 SER B OG  
23002 N N   . SER B  719 ? 0.3826 0.3384 0.3409 -0.0205 0.0273  -0.0530 745 SER B N   
23003 C CA  . SER B  719 ? 0.3808 0.3354 0.3436 -0.0139 0.0295  -0.0465 745 SER B CA  
23004 C C   . SER B  719 ? 0.3771 0.3285 0.3351 -0.0098 0.0329  -0.0480 745 SER B C   
23005 O O   . SER B  719 ? 0.3714 0.3287 0.3313 -0.0053 0.0319  -0.0442 745 SER B O   
23006 C CB  . SER B  719 ? 0.3889 0.3549 0.3578 -0.0119 0.0249  -0.0409 745 SER B CB  
23007 O OG  . SER B  719 ? 0.4137 0.3823 0.3866 -0.0157 0.0222  -0.0395 745 SER B OG  
23013 N N   . ASN B  720 ? 0.3782 0.3198 0.3297 -0.0115 0.0370  -0.0537 746 ASN B N   
23014 C CA  . ASN B  720 ? 0.3892 0.3259 0.3354 -0.0078 0.0412  -0.0556 746 ASN B CA  
23015 C C   . ASN B  720 ? 0.4096 0.3321 0.3570 -0.0054 0.0482  -0.0542 746 ASN B C   
23016 O O   . ASN B  720 ? 0.4106 0.3307 0.3648 -0.0046 0.0488  -0.0492 746 ASN B O   
23017 C CB  . ASN B  720 ? 0.3876 0.3259 0.3242 -0.0120 0.0399  -0.0639 746 ASN B CB  
23018 C CG  . ASN B  720 ? 0.3985 0.3497 0.3336 -0.0106 0.0349  -0.0633 746 ASN B CG  
23019 O OD1 . ASN B  720 ? 0.4036 0.3559 0.3363 -0.0062 0.0366  -0.0622 746 ASN B OD1 
23020 N ND2 . ASN B  720 ? 0.3687 0.3299 0.3057 -0.0142 0.0291  -0.0636 746 ASN B ND2 
23027 N N   . LEU B  721 ? 0.4224 0.3358 0.3635 -0.0037 0.0536  -0.0581 747 LEU B N   
23028 C CA  . LEU B  721 ? 0.4406 0.3402 0.3828 -0.0008 0.0608  -0.0568 747 LEU B CA  
23029 C C   . LEU B  721 ? 0.4583 0.3457 0.3918 -0.0057 0.0648  -0.0653 747 LEU B C   
23030 O O   . LEU B  721 ? 0.4662 0.3420 0.3966 -0.0030 0.0716  -0.0669 747 LEU B O   
23031 C CB  . LEU B  721 ? 0.4395 0.3383 0.3829 0.0066  0.0648  -0.0528 747 LEU B CB  
23032 C CG  . LEU B  721 ? 0.4426 0.3532 0.3947 0.0112  0.0612  -0.0445 747 LEU B CG  
23033 C CD1 . LEU B  721 ? 0.4409 0.3514 0.3934 0.0179  0.0651  -0.0415 747 LEU B CD1 
23034 C CD2 . LEU B  721 ? 0.4504 0.3607 0.4119 0.0122  0.0607  -0.0376 747 LEU B CD2 
23046 N N   . LEU B  722 ? 0.4669 0.3570 0.3968 -0.0131 0.0609  -0.0709 748 LEU B N   
23047 C CA  . LEU B  722 ? 0.4806 0.3599 0.4021 -0.0188 0.0642  -0.0795 748 LEU B CA  
23048 C C   . LEU B  722 ? 0.4948 0.3600 0.4194 -0.0193 0.0697  -0.0781 748 LEU B C   
23049 O O   . LEU B  722 ? 0.4886 0.3560 0.4203 -0.0203 0.0675  -0.0734 748 LEU B O   
23050 C CB  . LEU B  722 ? 0.4782 0.3659 0.3961 -0.0267 0.0582  -0.0853 748 LEU B CB  
23051 C CG  . LEU B  722 ? 0.4891 0.3910 0.4032 -0.0270 0.0525  -0.0873 748 LEU B CG  
23052 C CD1 . LEU B  722 ? 0.4889 0.3997 0.4017 -0.0344 0.0465  -0.0915 748 LEU B CD1 
23053 C CD2 . LEU B  722 ? 0.5030 0.4004 0.4072 -0.0260 0.0560  -0.0930 748 LEU B CD2 
23065 N N   . LYS B  723 ? 0.5119 0.3623 0.4310 -0.0184 0.0770  -0.0820 749 LYS B N   
23066 C CA  . LYS B  723 ? 0.5334 0.3680 0.4541 -0.0188 0.0833  -0.0815 749 LYS B CA  
23067 C C   . LYS B  723 ? 0.5499 0.3773 0.4636 -0.0281 0.0837  -0.0904 749 LYS B C   
23068 O O   . LYS B  723 ? 0.5559 0.3746 0.4724 -0.0310 0.0859  -0.0896 749 LYS B O   
23069 C CB  . LYS B  723 ? 0.5774 0.3989 0.4959 -0.0126 0.0919  -0.0811 749 LYS B CB  
23070 C CG  . LYS B  723 ? 0.6513 0.4790 0.5770 -0.0034 0.0924  -0.0723 749 LYS B CG  
23071 C CD  . LYS B  723 ? 0.7385 0.5550 0.6609 0.0027  0.1007  -0.0730 749 LYS B CD  
23072 C CE  . LYS B  723 ? 0.8113 0.6090 0.7333 0.0031  0.1089  -0.0739 749 LYS B CE  
23073 N NZ  . LYS B  723 ? 0.8527 0.6417 0.7761 0.0115  0.1169  -0.0705 749 LYS B NZ  
23087 N N   . THR B  724 ? 0.5525 0.3828 0.4569 -0.0328 0.0820  -0.0988 750 THR B N   
23088 C CA  . THR B  724 ? 0.5696 0.3941 0.4668 -0.0421 0.0821  -0.1079 750 THR B CA  
23089 C C   . THR B  724 ? 0.5797 0.4167 0.4696 -0.0468 0.0763  -0.1146 750 THR B C   
23090 O O   . THR B  724 ? 0.5745 0.4222 0.4641 -0.0422 0.0733  -0.1123 750 THR B O   
23091 C CB  . THR B  724 ? 0.5943 0.3979 0.4850 -0.0423 0.0916  -0.1130 750 THR B CB  
23092 O OG1 . THR B  724 ? 0.6094 0.4063 0.4938 -0.0520 0.0921  -0.1216 750 THR B OG1 
23093 C CG2 . THR B  724 ? 0.6028 0.4035 0.4860 -0.0380 0.0954  -0.1163 750 THR B CG2 
23101 N N   . ILE B  725 ? 0.5960 0.4320 0.4799 -0.0560 0.0747  -0.1227 751 ILE B N   
23102 C CA  . ILE B  725 ? 0.6230 0.4704 0.4993 -0.0611 0.0695  -0.1296 751 ILE B CA  
23103 C C   . ILE B  725 ? 0.6630 0.4973 0.5288 -0.0685 0.0742  -0.1401 751 ILE B C   
23104 O O   . ILE B  725 ? 0.6641 0.4914 0.5305 -0.0751 0.0753  -0.1432 751 ILE B O   
23105 C CB  . ILE B  725 ? 0.6192 0.4838 0.5006 -0.0655 0.0608  -0.1281 751 ILE B CB  
23106 C CG1 . ILE B  725 ? 0.6246 0.5003 0.5164 -0.0582 0.0569  -0.1177 751 ILE B CG1 
23107 C CG2 . ILE B  725 ? 0.6235 0.5004 0.4971 -0.0700 0.0556  -0.1347 751 ILE B CG2 
23108 C CD1 . ILE B  725 ? 0.6310 0.5216 0.5292 -0.0619 0.0494  -0.1153 751 ILE B CD1 
23120 N N   . ASN B  726 ? 0.6969 0.5272 0.5530 -0.0674 0.0773  -0.1456 752 ASN B N   
23121 C CA  . ASN B  726 ? 0.7404 0.5573 0.5852 -0.0743 0.0823  -0.1561 752 ASN B CA  
23122 C C   . ASN B  726 ? 0.7741 0.6012 0.6131 -0.0846 0.0762  -0.1641 752 ASN B C   
23123 O O   . ASN B  726 ? 0.7670 0.6125 0.6073 -0.0848 0.0685  -0.1626 752 ASN B O   
23124 C CB  . ASN B  726 ? 0.7605 0.5714 0.5962 -0.0697 0.0873  -0.1594 752 ASN B CB  
23125 C CG  . ASN B  726 ? 0.8114 0.6106 0.6517 -0.0599 0.0945  -0.1528 752 ASN B CG  
23126 O OD1 . ASN B  726 ? 0.8323 0.6212 0.6799 -0.0579 0.0984  -0.1481 752 ASN B OD1 
23127 N ND2 . ASN B  726 ? 0.8232 0.6241 0.6595 -0.0536 0.0965  -0.1519 752 ASN B ND2 
23134 N N   . LYS B  727 ? 0.8121 0.6269 0.6440 -0.0931 0.0800  -0.1730 753 LYS B N   
23135 C CA  . LYS B  727 ? 0.8458 0.6691 0.6715 -0.1040 0.0749  -0.1816 753 LYS B CA  
23136 C C   . LYS B  727 ? 0.8716 0.7095 0.6891 -0.1040 0.0699  -0.1853 753 LYS B C   
23137 O O   . LYS B  727 ? 0.8747 0.7291 0.6918 -0.1095 0.0623  -0.1876 753 LYS B O   
23138 C CB  . LYS B  727 ? 0.8875 0.6921 0.7049 -0.1124 0.0816  -0.1913 753 LYS B CB  
23139 C CG  . LYS B  727 ? 0.9509 0.7630 0.7637 -0.1249 0.0767  -0.1998 753 LYS B CG  
23140 C CD  . LYS B  727 ? 1.0336 0.8280 0.8345 -0.1331 0.0834  -0.2112 753 LYS B CD  
23141 C CE  . LYS B  727 ? 1.0960 0.8988 0.8920 -0.1460 0.0784  -0.2202 753 LYS B CE  
23142 N NZ  . LYS B  727 ? 1.1303 0.9278 0.9334 -0.1525 0.0789  -0.2196 753 LYS B NZ  
23156 N N   . SER B  728 ? 0.8881 0.7204 0.6995 -0.0976 0.0743  -0.1855 754 SER B N   
23157 C CA  . SER B  728 ? 0.9059 0.7506 0.7090 -0.0967 0.0704  -0.1884 754 SER B CA  
23158 C C   . SER B  728 ? 0.9167 0.7828 0.7275 -0.0917 0.0620  -0.1804 754 SER B C   
23159 O O   . SER B  728 ? 0.9156 0.7969 0.7213 -0.0946 0.0559  -0.1833 754 SER B O   
23160 C CB  . SER B  728 ? 0.9242 0.7572 0.7204 -0.0898 0.0778  -0.1891 754 SER B CB  
23161 O OG  . SER B  728 ? 0.9394 0.7716 0.7448 -0.0790 0.0797  -0.1787 754 SER B OG  
23167 N N   . ALA B  729 ? 0.9264 0.7936 0.7490 -0.0843 0.0619  -0.1704 755 ALA B N   
23168 C CA  . ALA B  729 ? 0.9359 0.8215 0.7663 -0.0793 0.0547  -0.1624 755 ALA B CA  
23169 C C   . ALA B  729 ? 0.9485 0.8495 0.7829 -0.0861 0.0467  -0.1633 755 ALA B C   
23170 O O   . ALA B  729 ? 0.9440 0.8622 0.7794 -0.0844 0.0400  -0.1607 755 ALA B O   
23171 C CB  . ALA B  729 ? 0.9371 0.8188 0.7789 -0.0708 0.0570  -0.1522 755 ALA B CB  
23177 N N   . LEU B  730 ? 0.9643 0.8592 0.8010 -0.0935 0.0474  -0.1667 756 LEU B N   
23178 C CA  . LEU B  730 ? 0.9771 0.8865 0.8185 -0.0999 0.0402  -0.1672 756 LEU B CA  
23179 C C   . LEU B  730 ? 0.9947 0.9155 0.8272 -0.1080 0.0353  -0.1757 756 LEU B C   
23180 O O   . LEU B  730 ? 0.9927 0.9323 0.8277 -0.1079 0.0280  -0.1735 756 LEU B O   
23181 C CB  . LEU B  730 ? 0.9810 0.8805 0.8283 -0.1053 0.0427  -0.1676 756 LEU B CB  
23182 C CG  . LEU B  730 ? 0.9942 0.8874 0.8528 -0.0993 0.0452  -0.1584 756 LEU B CG  
23183 C CD1 . LEU B  730 ? 0.9941 0.9005 0.8603 -0.0905 0.0407  -0.1490 756 LEU B CD1 
23184 C CD2 . LEU B  730 ? 1.0085 0.8800 0.8652 -0.0962 0.0543  -0.1584 756 LEU B CD2 
23196 N N   . GLU B  731 ? 1.0089 0.9185 0.8313 -0.1154 0.0394  -0.1853 757 GLU B N   
23197 C CA  . GLU B  731 ? 1.0222 0.9419 0.8358 -0.1243 0.0350  -0.1941 757 GLU B CA  
23198 C C   . GLU B  731 ? 1.0363 0.9511 0.8363 -0.1239 0.0380  -0.2003 757 GLU B C   
23199 O O   . GLU B  731 ? 1.0437 0.9422 0.8402 -0.1189 0.0454  -0.2002 757 GLU B O   
23200 C CB  . GLU B  731 ? 1.0531 0.9652 0.8659 -0.1355 0.0365  -0.2013 757 GLU B CB  
23201 C CG  . GLU B  731 ? 1.0991 1.0175 0.9243 -0.1374 0.0332  -0.1960 757 GLU B CG  
23202 C CD  . GLU B  731 ? 1.1608 1.0693 0.9856 -0.1479 0.0359  -0.2024 757 GLU B CD  
23203 O OE1 . GLU B  731 ? 1.1791 1.0818 0.9936 -0.1561 0.0378  -0.2122 757 GLU B OE1 
23204 O OE2 . GLU B  731 ? 1.1746 1.0808 1.0092 -0.1482 0.0362  -0.1976 757 GLU B OE2 
23211 N N   . THR B  732 ? 1.0387 0.9684 0.8312 -0.1290 0.0323  -0.2057 758 THR B N   
23212 C CA  . THR B  732 ? 1.0557 0.9831 0.8342 -0.1297 0.0342  -0.2123 758 THR B CA  
23213 C C   . THR B  732 ? 1.0600 0.9992 0.8302 -0.1411 0.0288  -0.2216 758 THR B C   
23214 O O   . THR B  732 ? 1.0704 0.9980 0.8350 -0.1501 0.0325  -0.2302 758 THR B O   
23215 C CB  . THR B  732 ? 1.0726 1.0079 0.8510 -0.1187 0.0330  -0.2051 758 THR B CB  
23216 O OG1 . THR B  732 ? 1.0891 1.0114 0.8746 -0.1097 0.0389  -0.1978 758 THR B OG1 
23217 C CG2 . THR B  732 ? 1.0829 1.0178 0.8465 -0.1193 0.0346  -0.2115 758 THR B CG2 
23225 N N   . LYS B  733 ? 1.0498 1.0118 0.8198 -0.1411 0.0204  -0.2198 759 LYS B N   
23226 C CA  . LYS B  733 ? 1.0517 1.0276 0.8148 -0.1514 0.0145  -0.2277 759 LYS B CA  
23227 C C   . LYS B  733 ? 1.0362 1.0305 0.8111 -0.1542 0.0067  -0.2235 759 LYS B C   
23228 O O   . LYS B  733 ? 1.0379 1.0350 0.8129 -0.1645 0.0048  -0.2295 759 LYS B O   
23229 C CB  . LYS B  733 ? 1.0821 1.0697 0.8337 -0.1497 0.0113  -0.2300 759 LYS B CB  
23230 C CG  . LYS B  733 ? 1.1364 1.1368 0.8930 -0.1381 0.0076  -0.2196 759 LYS B CG  
23231 C CD  . LYS B  733 ? 1.1976 1.2093 0.9421 -0.1371 0.0046  -0.2221 759 LYS B CD  
23232 C CE  . LYS B  733 ? 1.2369 1.2748 0.9835 -0.1391 -0.0053 -0.2200 759 LYS B CE  
23233 N NZ  . LYS B  733 ? 1.2649 1.3104 1.0102 -0.1514 -0.0094 -0.2278 759 LYS B NZ  
23247 N N   . THR B  734 ? 1.0183 1.0242 0.8032 -0.1451 0.0029  -0.2131 760 THR B N   
23248 C CA  . THR B  734 ? 1.0038 1.0263 0.8008 -0.1460 -0.0038 -0.2078 760 THR B CA  
23249 C C   . THR B  734 ? 0.9916 1.0032 0.8007 -0.1409 -0.0001 -0.2006 760 THR B C   
23250 O O   . THR B  734 ? 0.9976 0.9973 0.8078 -0.1324 0.0048  -0.1957 760 THR B O   
23251 C CB  . THR B  734 ? 1.0143 1.0582 0.8135 -0.1393 -0.0108 -0.2013 760 THR B CB  
23252 O OG1 . THR B  734 ? 1.0288 1.0663 0.8295 -0.1279 -0.0077 -0.1938 760 THR B OG1 
23253 C CG2 . THR B  734 ? 1.0182 1.0756 0.8060 -0.1442 -0.0154 -0.2075 760 THR B CG2 
23261 N N   . THR B  735 ? 0.9714 0.9878 0.7898 -0.1459 -0.0025 -0.1997 761 THR B N   
23262 C CA  . THR B  735 ? 0.9623 0.9691 0.7919 -0.1417 0.0007  -0.1929 761 THR B CA  
23263 C C   . THR B  735 ? 0.9327 0.9525 0.7722 -0.1319 -0.0036 -0.1823 761 THR B C   
23264 O O   . THR B  735 ? 0.9328 0.9702 0.7715 -0.1294 -0.0095 -0.1803 761 THR B O   
23265 C CB  . THR B  735 ? 0.9856 0.9894 0.8203 -0.1513 0.0010  -0.1966 761 THR B CB  
23266 O OG1 . THR B  735 ? 1.0003 0.9908 0.8437 -0.1471 0.0056  -0.1907 761 THR B OG1 
23267 C CG2 . THR B  735 ? 0.9851 1.0116 0.8263 -0.1559 -0.0071 -0.1958 761 THR B CG2 
23275 N N   . THR B  736 ? 0.9042 0.9148 0.7525 -0.1262 -0.0003 -0.1754 762 THR B N   
23276 C CA  . THR B  736 ? 0.8750 0.8946 0.7325 -0.1170 -0.0032 -0.1655 762 THR B CA  
23277 C C   . THR B  736 ? 0.8352 0.8750 0.7008 -0.1186 -0.0104 -0.1624 762 THR B C   
23278 O O   . THR B  736 ? 0.8356 0.8764 0.7068 -0.1247 -0.0111 -0.1637 762 THR B O   
23279 C CB  . THR B  736 ? 0.8942 0.8988 0.7592 -0.1123 0.0021  -0.1597 762 THR B CB  
23280 O OG1 . THR B  736 ? 0.9085 0.9072 0.7774 -0.1200 0.0035  -0.1626 762 THR B OG1 
23281 C CG2 . THR B  736 ? 0.9077 0.8939 0.7670 -0.1077 0.0092  -0.1601 762 THR B CG2 
23289 N N   . LYS B  737 ? 0.7974 0.8526 0.6643 -0.1126 -0.0154 -0.1576 763 LYS B N   
23290 C CA  . LYS B  737 ? 0.7605 0.8344 0.6362 -0.1121 -0.0217 -0.1533 763 LYS B CA  
23291 C C   . LYS B  737 ? 0.7105 0.7819 0.5968 -0.1043 -0.0207 -0.1440 763 LYS B C   
23292 O O   . LYS B  737 ? 0.7032 0.7888 0.5967 -0.1012 -0.0252 -0.1389 763 LYS B O   
23293 C CB  . LYS B  737 ? 0.7916 0.8840 0.6635 -0.1099 -0.0276 -0.1528 763 LYS B CB  
23294 C CG  . LYS B  737 ? 0.8616 0.9638 0.7265 -0.1192 -0.0310 -0.1611 763 LYS B CG  
23295 C CD  . LYS B  737 ? 0.9360 1.0237 0.7888 -0.1238 -0.0264 -0.1691 763 LYS B CD  
23296 C CE  . LYS B  737 ? 0.9871 1.0845 0.8294 -0.1236 -0.0294 -0.1723 763 LYS B CE  
23297 N NZ  . LYS B  737 ? 1.0252 1.1067 0.8553 -0.1268 -0.0240 -0.1796 763 LYS B NZ  
23311 N N   . LEU B  738 ? 0.6750 0.7285 0.5623 -0.1014 -0.0147 -0.1420 764 LEU B N   
23312 C CA  . LEU B  738 ? 0.6387 0.6891 0.5353 -0.0950 -0.0135 -0.1340 764 LEU B CA  
23313 C C   . LEU B  738 ? 0.5956 0.6497 0.5005 -0.1001 -0.0150 -0.1334 764 LEU B C   
23314 O O   . LEU B  738 ? 0.5976 0.6483 0.5008 -0.1085 -0.0141 -0.1393 764 LEU B O   
23315 C CB  . LEU B  738 ? 0.6483 0.6788 0.5438 -0.0915 -0.0066 -0.1324 764 LEU B CB  
23316 C CG  . LEU B  738 ? 0.6725 0.6976 0.5626 -0.0842 -0.0041 -0.1305 764 LEU B CG  
23317 C CD1 . LEU B  738 ? 0.6900 0.6950 0.5780 -0.0830 0.0032  -0.1311 764 LEU B CD1 
23318 C CD2 . LEU B  738 ? 0.6729 0.7064 0.5690 -0.0755 -0.0066 -0.1220 764 LEU B CD2 
23330 N N   . SER B  739 ? 0.5551 0.6159 0.4688 -0.0951 -0.0171 -0.1263 765 SER B N   
23331 C CA  . SER B  739 ? 0.5243 0.5881 0.4466 -0.0984 -0.0180 -0.1243 765 SER B CA  
23332 C C   . SER B  739 ? 0.4910 0.5430 0.4189 -0.0932 -0.0141 -0.1179 765 SER B C   
23333 O O   . SER B  739 ? 0.4798 0.5291 0.4133 -0.0965 -0.0131 -0.1168 765 SER B O   
23334 C CB  . SER B  739 ? 0.5384 0.6220 0.4662 -0.0975 -0.0241 -0.1217 765 SER B CB  
23335 O OG  . SER B  739 ? 0.5708 0.6594 0.5012 -0.0885 -0.0255 -0.1151 765 SER B OG  
23341 N N   . MET B  740 ? 0.4736 0.5192 0.4002 -0.0853 -0.0119 -0.1136 766 MET B N   
23342 C CA  . MET B  740 ? 0.4671 0.5023 0.3987 -0.0803 -0.0084 -0.1075 766 MET B CA  
23343 C C   . MET B  740 ? 0.4527 0.4753 0.3793 -0.0752 -0.0039 -0.1067 766 MET B C   
23344 O O   . MET B  740 ? 0.4448 0.4717 0.3678 -0.0704 -0.0050 -0.1058 766 MET B O   
23345 C CB  . MET B  740 ? 0.4803 0.5259 0.4194 -0.0747 -0.0117 -0.1004 766 MET B CB  
23346 C CG  . MET B  740 ? 0.5389 0.5751 0.4834 -0.0704 -0.0086 -0.0942 766 MET B CG  
23347 S SD  . MET B  740 ? 0.6888 0.7366 0.6419 -0.0656 -0.0123 -0.0870 766 MET B SD  
23348 C CE  . MET B  740 ? 0.6547 0.7088 0.6127 -0.0734 -0.0142 -0.0893 766 MET B CE  
23358 N N   . LEU B  741 ? 0.4429 0.4501 0.3697 -0.0759 0.0014  -0.1066 767 LEU B N   
23359 C CA  . LEU B  741 ? 0.4354 0.4292 0.3585 -0.0712 0.0065  -0.1055 767 LEU B CA  
23360 C C   . LEU B  741 ? 0.4208 0.4069 0.3512 -0.0672 0.0093  -0.0986 767 LEU B C   
23361 O O   . LEU B  741 ? 0.4228 0.4015 0.3558 -0.0711 0.0116  -0.0989 767 LEU B O   
23362 C CB  . LEU B  741 ? 0.4392 0.4208 0.3547 -0.0768 0.0108  -0.1130 767 LEU B CB  
23363 C CG  . LEU B  741 ? 0.4567 0.4224 0.3680 -0.0726 0.0173  -0.1127 767 LEU B CG  
23364 C CD1 . LEU B  741 ? 0.4583 0.4283 0.3653 -0.0663 0.0167  -0.1115 767 LEU B CD1 
23365 C CD2 . LEU B  741 ? 0.4656 0.4189 0.3697 -0.0790 0.0217  -0.1206 767 LEU B CD2 
23377 N N   . GLU B  742 ? 0.4038 0.3925 0.3377 -0.0597 0.0090  -0.0922 768 GLU B N   
23378 C CA  . GLU B  742 ? 0.3939 0.3770 0.3347 -0.0558 0.0111  -0.0853 768 GLU B CA  
23379 C C   . GLU B  742 ? 0.3880 0.3568 0.3265 -0.0519 0.0171  -0.0842 768 GLU B C   
23380 O O   . GLU B  742 ? 0.3869 0.3547 0.3205 -0.0484 0.0183  -0.0853 768 GLU B O   
23381 C CB  . GLU B  742 ? 0.4063 0.4003 0.3526 -0.0504 0.0073  -0.0789 768 GLU B CB  
23382 C CG  . GLU B  742 ? 0.4534 0.4623 0.4014 -0.0530 0.0015  -0.0801 768 GLU B CG  
23383 C CD  . GLU B  742 ? 0.5281 0.5458 0.4821 -0.0480 -0.0015 -0.0736 768 GLU B CD  
23384 O OE1 . GLU B  742 ? 0.5541 0.5689 0.5138 -0.0470 -0.0006 -0.0690 768 GLU B OE1 
23385 O OE2 . GLU B  742 ? 0.5447 0.5718 0.4974 -0.0452 -0.0045 -0.0732 768 GLU B OE2 
23392 N N   . LEU B  743 ? 0.3833 0.3411 0.3250 -0.0525 0.0210  -0.0820 769 LEU B N   
23393 C CA  . LEU B  743 ? 0.3933 0.3368 0.3335 -0.0488 0.0273  -0.0806 769 LEU B CA  
23394 C C   . LEU B  743 ? 0.3919 0.3303 0.3397 -0.0451 0.0295  -0.0730 769 LEU B C   
23395 O O   . LEU B  743 ? 0.4045 0.3311 0.3520 -0.0418 0.0349  -0.0712 769 LEU B O   
23396 C CB  . LEU B  743 ? 0.4041 0.3354 0.3378 -0.0544 0.0316  -0.0879 769 LEU B CB  
23397 C CG  . LEU B  743 ? 0.4341 0.3685 0.3589 -0.0580 0.0304  -0.0959 769 LEU B CG  
23398 C CD1 . LEU B  743 ? 0.4473 0.3726 0.3671 -0.0659 0.0331  -0.1033 769 LEU B CD1 
23399 C CD2 . LEU B  743 ? 0.4448 0.3748 0.3646 -0.0523 0.0336  -0.0962 769 LEU B CD2 
23411 N N   . HIS B  744 ? 0.3731 0.3202 0.3274 -0.0453 0.0255  -0.0683 770 HIS B N   
23412 C CA  . HIS B  744 ? 0.3729 0.3162 0.3340 -0.0418 0.0273  -0.0608 770 HIS B CA  
23413 C C   . HIS B  744 ? 0.3729 0.3149 0.3359 -0.0340 0.0292  -0.0555 770 HIS B C   
23414 O O   . HIS B  744 ? 0.3719 0.3205 0.3328 -0.0312 0.0273  -0.0562 770 HIS B O   
23415 C CB  . HIS B  744 ? 0.3692 0.3231 0.3362 -0.0435 0.0224  -0.0572 770 HIS B CB  
23416 C CG  . HIS B  744 ? 0.3939 0.3607 0.3631 -0.0400 0.0177  -0.0544 770 HIS B CG  
23417 N ND1 . HIS B  744 ? 0.4099 0.3875 0.3769 -0.0426 0.0133  -0.0583 770 HIS B ND1 
23418 C CD2 . HIS B  744 ? 0.4096 0.3799 0.3831 -0.0342 0.0171  -0.0480 770 HIS B CD2 
23419 C CE1 . HIS B  744 ? 0.4126 0.3989 0.3825 -0.0382 0.0104  -0.0542 770 HIS B CE1 
23420 N NE2 . HIS B  744 ? 0.4200 0.4022 0.3937 -0.0334 0.0125  -0.0482 770 HIS B NE2 
23428 N N   . GLY B  745 ? 0.3802 0.3136 0.3469 -0.0306 0.0332  -0.0504 771 GLY B N   
23429 C CA  . GLY B  745 ? 0.3868 0.3195 0.3564 -0.0233 0.0352  -0.0448 771 GLY B CA  
23430 C C   . GLY B  745 ? 0.3979 0.3212 0.3628 -0.0200 0.0405  -0.0473 771 GLY B C   
23431 O O   . GLY B  745 ? 0.4108 0.3347 0.3782 -0.0139 0.0421  -0.0428 771 GLY B O   
23435 N N   . ASN B  746 ? 0.3962 0.3109 0.3543 -0.0240 0.0435  -0.0545 772 ASN B N   
23436 C CA  . ASN B  746 ? 0.4071 0.3115 0.3599 -0.0211 0.0492  -0.0574 772 ASN B CA  
23437 C C   . ASN B  746 ? 0.4201 0.3098 0.3749 -0.0194 0.0558  -0.0550 772 ASN B C   
23438 O O   . ASN B  746 ? 0.4217 0.3064 0.3779 -0.0237 0.0563  -0.0553 772 ASN B O   
23439 C CB  . ASN B  746 ? 0.4151 0.3176 0.3585 -0.0264 0.0492  -0.0669 772 ASN B CB  
23440 C CG  . ASN B  746 ? 0.4171 0.3325 0.3574 -0.0259 0.0443  -0.0689 772 ASN B CG  
23441 O OD1 . ASN B  746 ? 0.4110 0.3269 0.3490 -0.0210 0.0459  -0.0681 772 ASN B OD1 
23442 N ND2 . ASN B  746 ? 0.4056 0.3319 0.3461 -0.0305 0.0383  -0.0709 772 ASN B ND2 
23449 N N   . PRO B  747 ? 0.4302 0.3127 0.3855 -0.0131 0.0611  -0.0522 773 PRO B N   
23450 C CA  . PRO B  747 ? 0.4407 0.3092 0.3985 -0.0107 0.0677  -0.0492 773 PRO B CA  
23451 C C   . PRO B  747 ? 0.4569 0.3104 0.4068 -0.0150 0.0733  -0.0572 773 PRO B C   
23452 O O   . PRO B  747 ? 0.4551 0.2987 0.4012 -0.0115 0.0793  -0.0592 773 PRO B O   
23453 C CB  . PRO B  747 ? 0.4476 0.3164 0.4091 -0.0022 0.0709  -0.0433 773 PRO B CB  
23454 C CG  . PRO B  747 ? 0.4509 0.3258 0.4065 -0.0017 0.0692  -0.0481 773 PRO B CG  
23455 C CD  . PRO B  747 ? 0.4264 0.3133 0.3803 -0.0076 0.0617  -0.0513 773 PRO B CD  
23463 N N   . PHE B  748 ? 0.4668 0.3184 0.4142 -0.0226 0.0715  -0.0619 774 PHE B N   
23464 C CA  . PHE B  748 ? 0.4863 0.3243 0.4257 -0.0280 0.0762  -0.0703 774 PHE B CA  
23465 C C   . PHE B  748 ? 0.5105 0.3307 0.4507 -0.0254 0.0845  -0.0684 774 PHE B C   
23466 O O   . PHE B  748 ? 0.5110 0.3291 0.4586 -0.0225 0.0855  -0.0608 774 PHE B O   
23467 C CB  . PHE B  748 ? 0.4840 0.3255 0.4213 -0.0373 0.0720  -0.0755 774 PHE B CB  
23468 C CG  . PHE B  748 ? 0.4877 0.3433 0.4208 -0.0412 0.0654  -0.0808 774 PHE B CG  
23469 C CD1 . PHE B  748 ? 0.5054 0.3586 0.4293 -0.0440 0.0666  -0.0891 774 PHE B CD1 
23470 C CD2 . PHE B  748 ? 0.4862 0.3578 0.4245 -0.0417 0.0582  -0.0771 774 PHE B CD2 
23471 C CE1 . PHE B  748 ? 0.5111 0.3782 0.4314 -0.0471 0.0604  -0.0933 774 PHE B CE1 
23472 C CE2 . PHE B  748 ? 0.4924 0.3769 0.4272 -0.0448 0.0524  -0.0815 774 PHE B CE2 
23473 C CZ  . PHE B  748 ? 0.4958 0.3784 0.4218 -0.0472 0.0534  -0.0892 774 PHE B CZ  
23483 N N   . GLU B  749 ? 0.5258 0.3329 0.4580 -0.0265 0.0905  -0.0754 775 GLU B N   
23484 C CA  . GLU B  749 ? 0.5476 0.3356 0.4789 -0.0245 0.0993  -0.0752 775 GLU B CA  
23485 C C   . GLU B  749 ? 0.5639 0.3431 0.4911 -0.0337 0.1002  -0.0815 775 GLU B C   
23486 O O   . GLU B  749 ? 0.5713 0.3504 0.4903 -0.0406 0.0990  -0.0908 775 GLU B O   
23487 C CB  . GLU B  749 ? 0.5927 0.3714 0.5168 -0.0210 0.1055  -0.0801 775 GLU B CB  
23488 C CG  . GLU B  749 ? 0.6907 0.4496 0.6149 -0.0170 0.1154  -0.0786 775 GLU B CG  
23489 C CD  . GLU B  749 ? 0.8203 0.5715 0.7402 -0.0107 0.1220  -0.0804 775 GLU B CD  
23490 O OE1 . GLU B  749 ? 0.8608 0.5942 0.7790 -0.0084 0.1307  -0.0812 775 GLU B OE1 
23491 O OE2 . GLU B  749 ? 0.8618 0.6245 0.7802 -0.0080 0.1187  -0.0808 775 GLU B OE2 
23498 N N   . CYS B  750 ? 0.5664 0.3399 0.4996 -0.0342 0.1018  -0.0761 776 CYS B N   
23499 C CA  . CYS B  750 ? 0.5878 0.3534 0.5183 -0.0430 0.1027  -0.0809 776 CYS B CA  
23500 C C   . CYS B  750 ? 0.6168 0.3599 0.5436 -0.0433 0.1123  -0.0835 776 CYS B C   
23501 O O   . CYS B  750 ? 0.6218 0.3555 0.5534 -0.0422 0.1161  -0.0780 776 CYS B O   
23502 C CB  . CYS B  750 ? 0.5881 0.3626 0.5266 -0.0447 0.0977  -0.0741 776 CYS B CB  
23503 S SG  . CYS B  750 ? 0.6057 0.4056 0.5470 -0.0467 0.0864  -0.0734 776 CYS B SG  
23508 N N   . THR B  751 ? 0.6363 0.3707 0.5542 -0.0447 0.1165  -0.0919 777 THR B N   
23509 C CA  . THR B  751 ? 0.6651 0.3773 0.5769 -0.0464 0.1259  -0.0973 777 THR B CA  
23510 C C   . THR B  751 ? 0.6779 0.3887 0.5799 -0.0580 0.1241  -0.1096 777 THR B C   
23511 O O   . THR B  751 ? 0.6689 0.3962 0.5707 -0.0631 0.1158  -0.1120 777 THR B O   
23512 C CB  . THR B  751 ? 0.6912 0.3957 0.6004 -0.0379 0.1323  -0.0969 777 THR B CB  
23513 O OG1 . THR B  751 ? 0.7089 0.4247 0.6118 -0.0390 0.1280  -0.1029 777 THR B OG1 
23514 C CG2 . THR B  751 ? 0.6939 0.4021 0.6133 -0.0268 0.1333  -0.0846 777 THR B CG2 
23522 N N   . CYS B  752 ? 0.6902 0.3817 0.5842 -0.0621 0.1319  -0.1174 778 CYS B N   
23523 C CA  . CYS B  752 ? 0.6986 0.3889 0.5829 -0.0733 0.1303  -0.1294 778 CYS B CA  
23524 C C   . CYS B  752 ? 0.6873 0.3920 0.5652 -0.0740 0.1249  -0.1353 778 CYS B C   
23525 O O   . CYS B  752 ? 0.6881 0.3992 0.5597 -0.0831 0.1206  -0.1437 778 CYS B O   
23526 C CB  . CYS B  752 ? 0.7276 0.3932 0.6044 -0.0772 0.1403  -0.1365 778 CYS B CB  
23527 S SG  . CYS B  752 ? 0.8057 0.4549 0.6891 -0.0786 0.1460  -0.1306 778 CYS B SG  
23533 N N   . ASP B  753 ? 0.6760 0.3878 0.5562 -0.0644 0.1243  -0.1301 779 ASP B N   
23534 C CA  . ASP B  753 ? 0.6706 0.3967 0.5455 -0.0640 0.1191  -0.1341 779 ASP B CA  
23535 C C   . ASP B  753 ? 0.6495 0.3980 0.5281 -0.0682 0.1082  -0.1329 779 ASP B C   
23536 O O   . ASP B  753 ? 0.6452 0.4051 0.5178 -0.0709 0.1034  -0.1382 779 ASP B O   
23537 C CB  . ASP B  753 ? 0.6952 0.4235 0.5730 -0.0526 0.1215  -0.1276 779 ASP B CB  
23538 C CG  . ASP B  753 ? 0.7781 0.4859 0.6514 -0.0479 0.1322  -0.1294 779 ASP B CG  
23539 O OD1 . ASP B  753 ? 0.7982 0.5029 0.6784 -0.0382 0.1361  -0.1209 779 ASP B OD1 
23540 O OD2 . ASP B  753 ? 0.8141 0.5093 0.6770 -0.0539 0.1369  -0.1395 779 ASP B OD2 
23545 N N   . ILE B  754 ? 0.6341 0.3889 0.5222 -0.0684 0.1045  -0.1258 780 ILE B N   
23546 C CA  . ILE B  754 ? 0.6231 0.3979 0.5150 -0.0727 0.0948  -0.1247 780 ILE B CA  
23547 C C   . ILE B  754 ? 0.6198 0.3943 0.5069 -0.0847 0.0927  -0.1333 780 ILE B C   
23548 O O   . ILE B  754 ? 0.6070 0.3978 0.4969 -0.0889 0.0850  -0.1332 780 ILE B O   
23549 C CB  . ILE B  754 ? 0.6216 0.4041 0.5255 -0.0676 0.0917  -0.1134 780 ILE B CB  
23550 C CG1 . ILE B  754 ? 0.6243 0.4296 0.5323 -0.0684 0.0818  -0.1109 780 ILE B CG1 
23551 C CG2 . ILE B  754 ? 0.6279 0.4000 0.5354 -0.0723 0.0946  -0.1118 780 ILE B CG2 
23552 C CD1 . ILE B  754 ? 0.6362 0.4530 0.5439 -0.0615 0.0787  -0.1086 780 ILE B CD1 
23564 N N   . GLY B  755 ? 0.6266 0.3828 0.5073 -0.0901 0.0996  -0.1401 781 GLY B N   
23565 C CA  . GLY B  755 ? 0.6349 0.3891 0.5110 -0.1019 0.0985  -0.1485 781 GLY B CA  
23566 C C   . GLY B  755 ? 0.6356 0.4048 0.5050 -0.1083 0.0919  -0.1565 781 GLY B C   
23567 O O   . GLY B  755 ? 0.6350 0.4150 0.5060 -0.1161 0.0862  -0.1590 781 GLY B O   
23571 N N   . ASP B  756 ? 0.6343 0.4050 0.4965 -0.1051 0.0924  -0.1603 782 ASP B N   
23572 C CA  . ASP B  756 ? 0.6320 0.4175 0.4873 -0.1106 0.0860  -0.1675 782 ASP B CA  
23573 C C   . ASP B  756 ? 0.5999 0.4090 0.4627 -0.1094 0.0763  -0.1620 782 ASP B C   
23574 O O   . ASP B  756 ? 0.6007 0.4221 0.4619 -0.1173 0.0704  -0.1668 782 ASP B O   
23575 C CB  . ASP B  756 ? 0.6712 0.4541 0.5177 -0.1059 0.0887  -0.1712 782 ASP B CB  
23576 C CG  . ASP B  756 ? 0.7707 0.5319 0.6073 -0.1090 0.0978  -0.1793 782 ASP B CG  
23577 O OD1 . ASP B  756 ? 0.7852 0.5401 0.6164 -0.1194 0.0989  -0.1876 782 ASP B OD1 
23578 O OD2 . ASP B  756 ? 0.8207 0.5713 0.6551 -0.1013 0.1040  -0.1775 782 ASP B OD2 
23583 N N   . PHE B  757 ? 0.5732 0.3885 0.4444 -0.0999 0.0747  -0.1520 783 PHE B N   
23584 C CA  . PHE B  757 ? 0.5487 0.3849 0.4271 -0.0983 0.0661  -0.1464 783 PHE B CA  
23585 C C   . PHE B  757 ? 0.5447 0.3845 0.4298 -0.1044 0.0634  -0.1448 783 PHE B C   
23586 O O   . PHE B  757 ? 0.5326 0.3889 0.4196 -0.1086 0.0563  -0.1458 783 PHE B O   
23587 C CB  . PHE B  757 ? 0.5298 0.3705 0.4152 -0.0871 0.0657  -0.1363 783 PHE B CB  
23588 C CG  . PHE B  757 ? 0.5100 0.3713 0.4023 -0.0854 0.0572  -0.1310 783 PHE B CG  
23589 C CD1 . PHE B  757 ? 0.5095 0.3864 0.3980 -0.0886 0.0508  -0.1351 783 PHE B CD1 
23590 C CD2 . PHE B  757 ? 0.5071 0.3719 0.4095 -0.0811 0.0558  -0.1219 783 PHE B CD2 
23591 C CE1 . PHE B  757 ? 0.5063 0.4013 0.4012 -0.0870 0.0435  -0.1302 783 PHE B CE1 
23592 C CE2 . PHE B  757 ? 0.5038 0.3866 0.4121 -0.0797 0.0485  -0.1174 783 PHE B CE2 
23593 C CZ  . PHE B  757 ? 0.4955 0.3929 0.4002 -0.0828 0.0426  -0.1217 783 PHE B CZ  
23603 N N   . ARG B  758 ? 0.5565 0.3809 0.4449 -0.1051 0.0691  -0.1424 784 ARG B N   
23604 C CA  . ARG B  758 ? 0.5726 0.3986 0.4667 -0.1114 0.0674  -0.1411 784 ARG B CA  
23605 C C   . ARG B  758 ? 0.5932 0.4228 0.4815 -0.1232 0.0651  -0.1511 784 ARG B C   
23606 O O   . ARG B  758 ? 0.5953 0.4384 0.4882 -0.1281 0.0594  -0.1506 784 ARG B O   
23607 C CB  . ARG B  758 ? 0.5922 0.3989 0.4895 -0.1100 0.0751  -0.1372 784 ARG B CB  
23608 C CG  . ARG B  758 ? 0.6175 0.4249 0.5237 -0.0998 0.0756  -0.1256 784 ARG B CG  
23609 C CD  . ARG B  758 ? 0.6337 0.4535 0.5489 -0.1008 0.0703  -0.1192 784 ARG B CD  
23610 N NE  . ARG B  758 ? 0.6581 0.4698 0.5744 -0.1088 0.0726  -0.1211 784 ARG B NE  
23611 C CZ  . ARG B  758 ? 0.6857 0.4806 0.6041 -0.1078 0.0793  -0.1176 784 ARG B CZ  
23612 N NH1 . ARG B  758 ? 0.6785 0.4632 0.5985 -0.0988 0.0843  -0.1117 784 ARG B NH1 
23613 N NH2 . ARG B  758 ? 0.6965 0.4849 0.6155 -0.1157 0.0811  -0.1196 784 ARG B NH2 
23627 N N   . ARG B  759 ? 0.6067 0.4253 0.4849 -0.1277 0.0693  -0.1601 785 ARG B N   
23628 C CA  . ARG B  759 ? 0.6223 0.4445 0.4942 -0.1394 0.0670  -0.1702 785 ARG B CA  
23629 C C   . ARG B  759 ? 0.6253 0.4710 0.4964 -0.1404 0.0581  -0.1719 785 ARG B C   
23630 O O   . ARG B  759 ? 0.6275 0.4850 0.4999 -0.1485 0.0531  -0.1754 785 ARG B O   
23631 C CB  . ARG B  759 ? 0.6527 0.4566 0.5134 -0.1437 0.0741  -0.1795 785 ARG B CB  
23632 C CG  . ARG B  759 ? 0.7007 0.4813 0.5622 -0.1452 0.0830  -0.1792 785 ARG B CG  
23633 C CD  . ARG B  759 ? 0.7516 0.5118 0.6022 -0.1474 0.0912  -0.1874 785 ARG B CD  
23634 N NE  . ARG B  759 ? 0.7930 0.5331 0.6461 -0.1398 0.0999  -0.1817 785 ARG B NE  
23635 C CZ  . ARG B  759 ? 0.8228 0.5528 0.6725 -0.1313 0.1053  -0.1803 785 ARG B CZ  
23636 N NH1 . ARG B  759 ? 0.8240 0.5611 0.6664 -0.1293 0.1033  -0.1847 785 ARG B NH1 
23637 N NH2 . ARG B  759 ? 0.8298 0.5427 0.6833 -0.1245 0.1130  -0.1743 785 ARG B NH2 
23651 N N   . TRP B  760 ? 0.6207 0.4737 0.4905 -0.1320 0.0560  -0.1688 786 TRP B N   
23652 C CA  . TRP B  760 ? 0.6128 0.4878 0.4822 -0.1317 0.0477  -0.1691 786 TRP B CA  
23653 C C   . TRP B  760 ? 0.5969 0.4880 0.4771 -0.1311 0.0414  -0.1624 786 TRP B C   
23654 O O   . TRP B  760 ? 0.5900 0.4981 0.4707 -0.1360 0.0348  -0.1649 786 TRP B O   
23655 C CB  . TRP B  760 ? 0.6136 0.4913 0.4806 -0.1218 0.0477  -0.1656 786 TRP B CB  
23656 C CG  . TRP B  760 ? 0.6145 0.5136 0.4806 -0.1209 0.0398  -0.1657 786 TRP B CG  
23657 C CD1 . TRP B  760 ? 0.6298 0.5359 0.4866 -0.1251 0.0372  -0.1731 786 TRP B CD1 
23658 C CD2 . TRP B  760 ? 0.6065 0.5223 0.4809 -0.1152 0.0336  -0.1577 786 TRP B CD2 
23659 N NE1 . TRP B  760 ? 0.6267 0.5527 0.4858 -0.1216 0.0300  -0.1697 786 TRP B NE1 
23660 C CE2 . TRP B  760 ? 0.6134 0.5455 0.4834 -0.1158 0.0277  -0.1604 786 TRP B CE2 
23661 C CE3 . TRP B  760 ? 0.6063 0.5250 0.4914 -0.1099 0.0325  -0.1486 786 TRP B CE3 
23662 C CZ2 . TRP B  760 ? 0.6106 0.5607 0.4867 -0.1109 0.0212  -0.1543 786 TRP B CZ2 
23663 C CZ3 . TRP B  760 ? 0.6088 0.5454 0.4995 -0.1055 0.0261  -0.1431 786 TRP B CZ3 
23664 C CH2 . TRP B  760 ? 0.6072 0.5589 0.4936 -0.1060 0.0207  -0.1459 786 TRP B CH2 
23675 N N   . MET B  761 ? 0.5881 0.4744 0.4767 -0.1252 0.0433  -0.1537 787 MET B N   
23676 C CA  . MET B  761 ? 0.5842 0.4844 0.4827 -0.1246 0.0380  -0.1473 787 MET B CA  
23677 C C   . MET B  761 ? 0.5931 0.4966 0.4931 -0.1354 0.0364  -0.1520 787 MET B C   
23678 O O   . MET B  761 ? 0.5844 0.5052 0.4889 -0.1379 0.0300  -0.1511 787 MET B O   
23679 C CB  . MET B  761 ? 0.5821 0.4740 0.4883 -0.1172 0.0414  -0.1379 787 MET B CB  
23680 C CG  . MET B  761 ? 0.5903 0.4841 0.4979 -0.1064 0.0413  -0.1315 787 MET B CG  
23681 S SD  . MET B  761 ? 0.5875 0.4712 0.5037 -0.0981 0.0456  -0.1207 787 MET B SD  
23682 C CE  . MET B  761 ? 0.5806 0.4749 0.5055 -0.1023 0.0410  -0.1166 787 MET B CE  
23692 N N   . ASP B  762 ? 0.6116 0.4984 0.5076 -0.1419 0.0423  -0.1572 788 ASP B N   
23693 C CA  . ASP B  762 ? 0.6307 0.5190 0.5277 -0.1529 0.0415  -0.1622 788 ASP B CA  
23694 C C   . ASP B  762 ? 0.6379 0.5403 0.5292 -0.1607 0.0361  -0.1707 788 ASP B C   
23695 O O   . ASP B  762 ? 0.6330 0.5483 0.5283 -0.1674 0.0316  -0.1722 788 ASP B O   
23696 C CB  . ASP B  762 ? 0.6630 0.5279 0.5562 -0.1578 0.0499  -0.1659 788 ASP B CB  
23697 C CG  . ASP B  762 ? 0.7295 0.5807 0.6288 -0.1514 0.0552  -0.1574 788 ASP B CG  
23698 O OD1 . ASP B  762 ? 0.7356 0.5966 0.6430 -0.1449 0.0518  -0.1488 788 ASP B OD1 
23699 O OD2 . ASP B  762 ? 0.7758 0.6066 0.6718 -0.1528 0.0627  -0.1593 788 ASP B OD2 
23704 N N   . GLU B  763 ? 0.6479 0.5485 0.5302 -0.1597 0.0367  -0.1761 789 GLU B N   
23705 C CA  . GLU B  763 ? 0.6605 0.5747 0.5364 -0.1665 0.0316  -0.1840 789 GLU B CA  
23706 C C   . GLU B  763 ? 0.6518 0.5900 0.5318 -0.1618 0.0232  -0.1798 789 GLU B C   
23707 O O   . GLU B  763 ? 0.6523 0.6051 0.5290 -0.1676 0.0180  -0.1852 789 GLU B O   
23708 C CB  . GLU B  763 ? 0.7105 0.6135 0.5744 -0.1669 0.0356  -0.1912 789 GLU B CB  
23709 C CG  . GLU B  763 ? 0.8014 0.6811 0.6595 -0.1730 0.0439  -0.1974 789 GLU B CG  
23710 C CD  . GLU B  763 ? 0.9162 0.7821 0.7628 -0.1715 0.0491  -0.2034 789 GLU B CD  
23711 O OE1 . GLU B  763 ? 0.9267 0.7996 0.7703 -0.1640 0.0470  -0.2013 789 GLU B OE1 
23712 O OE2 . GLU B  763 ? 0.9739 0.8214 0.8142 -0.1778 0.0557  -0.2102 789 GLU B OE2 
23719 N N   . HIS B  764 ? 0.6379 0.5801 0.5246 -0.1515 0.0221  -0.1705 790 HIS B N   
23720 C CA  . HIS B  764 ? 0.6298 0.5928 0.5203 -0.1462 0.0149  -0.1659 790 HIS B CA  
23721 C C   . HIS B  764 ? 0.6166 0.5868 0.5187 -0.1422 0.0126  -0.1573 790 HIS B C   
23722 O O   . HIS B  764 ? 0.6111 0.5837 0.5173 -0.1330 0.0119  -0.1499 790 HIS B O   
23723 C CB  . HIS B  764 ? 0.6443 0.6059 0.5300 -0.1369 0.0155  -0.1636 790 HIS B CB  
23724 C CG  . HIS B  764 ? 0.6798 0.6360 0.5537 -0.1405 0.0175  -0.1720 790 HIS B CG  
23725 N ND1 . HIS B  764 ? 0.7165 0.6515 0.5840 -0.1417 0.0251  -0.1761 790 HIS B ND1 
23726 C CD2 . HIS B  764 ? 0.6934 0.6627 0.5608 -0.1432 0.0128  -0.1770 790 HIS B CD2 
23727 C CE1 . HIS B  764 ? 0.7270 0.6625 0.5839 -0.1453 0.0249  -0.1838 790 HIS B CE1 
23728 N NE2 . HIS B  764 ? 0.7180 0.6742 0.5743 -0.1464 0.0175  -0.1846 790 HIS B NE2 
23736 N N   . LEU B  765 ? 0.6095 0.5833 0.5165 -0.1497 0.0115  -0.1585 791 LEU B N   
23737 C CA  . LEU B  765 ? 0.6069 0.5880 0.5244 -0.1470 0.0095  -0.1509 791 LEU B CA  
23738 C C   . LEU B  765 ? 0.5945 0.5972 0.5167 -0.1423 0.0023  -0.1469 791 LEU B C   
23739 O O   . LEU B  765 ? 0.5931 0.6011 0.5232 -0.1377 0.0009  -0.1398 791 LEU B O   
23740 C CB  . LEU B  765 ? 0.6112 0.5914 0.5324 -0.1567 0.0102  -0.1537 791 LEU B CB  
23741 C CG  . LEU B  765 ? 0.6399 0.5979 0.5582 -0.1611 0.0177  -0.1562 791 LEU B CG  
23742 C CD1 . LEU B  765 ? 0.6450 0.6044 0.5663 -0.1718 0.0179  -0.1599 791 LEU B CD1 
23743 C CD2 . LEU B  765 ? 0.6484 0.5934 0.5710 -0.1529 0.0222  -0.1479 791 LEU B CD2 
23755 N N   . ASN B  766 ? 0.5885 0.6035 0.5057 -0.1435 -0.0019 -0.1512 792 ASN B N   
23756 C CA  . ASN B  766 ? 0.5860 0.6209 0.5070 -0.1384 -0.0083 -0.1472 792 ASN B CA  
23757 C C   . ASN B  766 ? 0.5683 0.6005 0.4894 -0.1271 -0.0077 -0.1406 792 ASN B C   
23758 O O   . ASN B  766 ? 0.5682 0.6137 0.4945 -0.1215 -0.0119 -0.1352 792 ASN B O   
23759 C CB  . ASN B  766 ? 0.6251 0.6738 0.5405 -0.1433 -0.0130 -0.1536 792 ASN B CB  
23760 C CG  . ASN B  766 ? 0.7000 0.7711 0.6209 -0.1405 -0.0198 -0.1501 792 ASN B CG  
23761 O OD1 . ASN B  766 ? 0.7219 0.8032 0.6505 -0.1436 -0.0223 -0.1483 792 ASN B OD1 
23762 N ND2 . ASN B  766 ? 0.7185 0.7980 0.6356 -0.1346 -0.0228 -0.1488 792 ASN B ND2 
23769 N N   . VAL B  767 ? 0.5496 0.5649 0.4654 -0.1237 -0.0024 -0.1409 793 VAL B N   
23770 C CA  . VAL B  767 ? 0.5337 0.5458 0.4501 -0.1133 -0.0013 -0.1345 793 VAL B CA  
23771 C C   . VAL B  767 ? 0.5142 0.5192 0.4386 -0.1095 0.0012  -0.1274 793 VAL B C   
23772 O O   . VAL B  767 ? 0.5282 0.5172 0.4520 -0.1108 0.0066  -0.1276 793 VAL B O   
23773 C CB  . VAL B  767 ? 0.5447 0.5427 0.4521 -0.1111 0.0035  -0.1378 793 VAL B CB  
23774 C CG1 . VAL B  767 ? 0.5490 0.5447 0.4578 -0.1006 0.0046  -0.1309 793 VAL B CG1 
23775 C CG2 . VAL B  767 ? 0.5471 0.5517 0.4455 -0.1158 0.0012  -0.1455 793 VAL B CG2 
23785 N N   . LYS B  768 ? 0.4860 0.5027 0.4176 -0.1050 -0.0026 -0.1211 794 LYS B N   
23786 C CA  . LYS B  768 ? 0.4749 0.4869 0.4141 -0.1015 -0.0008 -0.1142 794 LYS B CA  
23787 C C   . LYS B  768 ? 0.4608 0.4611 0.3992 -0.0935 0.0031  -0.1094 794 LYS B C   
23788 O O   . LYS B  768 ? 0.4531 0.4570 0.3888 -0.0878 0.0019  -0.1080 794 LYS B O   
23789 C CB  . LYS B  768 ? 0.4936 0.5218 0.4399 -0.0987 -0.0060 -0.1092 794 LYS B CB  
23790 C CG  . LYS B  768 ? 0.5630 0.6047 0.5118 -0.1057 -0.0099 -0.1128 794 LYS B CG  
23791 C CD  . LYS B  768 ? 0.6357 0.6910 0.5925 -0.1027 -0.0138 -0.1074 794 LYS B CD  
23792 C CE  . LYS B  768 ? 0.6935 0.7611 0.6505 -0.0961 -0.0178 -0.1046 794 LYS B CE  
23793 N NZ  . LYS B  768 ? 0.7247 0.8046 0.6778 -0.0993 -0.0217 -0.1097 794 LYS B NZ  
23807 N N   . ILE B  769 ? 0.4529 0.4394 0.3936 -0.0933 0.0078  -0.1067 795 ILE B N   
23808 C CA  . ILE B  769 ? 0.4486 0.4242 0.3900 -0.0860 0.0118  -0.1014 795 ILE B CA  
23809 C C   . ILE B  769 ? 0.4463 0.4234 0.3961 -0.0841 0.0113  -0.0943 795 ILE B C   
23810 O O   . ILE B  769 ? 0.4570 0.4257 0.4087 -0.0880 0.0142  -0.0941 795 ILE B O   
23811 C CB  . ILE B  769 ? 0.4569 0.4142 0.3930 -0.0878 0.0184  -0.1049 795 ILE B CB  
23812 C CG1 . ILE B  769 ? 0.4692 0.4258 0.3962 -0.0906 0.0186  -0.1127 795 ILE B CG1 
23813 C CG2 . ILE B  769 ? 0.4621 0.4089 0.4003 -0.0798 0.0226  -0.0985 795 ILE B CG2 
23814 C CD1 . ILE B  769 ? 0.4868 0.4255 0.4076 -0.0934 0.0251  -0.1176 795 ILE B CD1 
23826 N N   . PRO B  770 ? 0.4294 0.4176 0.3839 -0.0790 0.0075  -0.0889 796 PRO B N   
23827 C CA  . PRO B  770 ? 0.4249 0.4148 0.3866 -0.0777 0.0070  -0.0827 796 PRO B CA  
23828 C C   . PRO B  770 ? 0.4268 0.4040 0.3904 -0.0733 0.0115  -0.0772 796 PRO B C   
23829 O O   . PRO B  770 ? 0.4294 0.3984 0.3898 -0.0691 0.0146  -0.0770 796 PRO B O   
23830 C CB  . PRO B  770 ? 0.4270 0.4315 0.3921 -0.0732 0.0021  -0.0791 796 PRO B CB  
23831 C CG  . PRO B  770 ? 0.4331 0.4437 0.3930 -0.0721 -0.0001 -0.0832 796 PRO B CG  
23832 C CD  . PRO B  770 ? 0.4170 0.4157 0.3702 -0.0740 0.0040  -0.0881 796 PRO B CD  
23840 N N   . ARG B  771 ? 0.4167 0.3930 0.3857 -0.0739 0.0119  -0.0726 797 ARG B N   
23841 C CA  . ARG B  771 ? 0.4205 0.3874 0.3927 -0.0696 0.0154  -0.0662 797 ARG B CA  
23842 C C   . ARG B  771 ? 0.4079 0.3584 0.3762 -0.0695 0.0214  -0.0678 797 ARG B C   
23843 O O   . ARG B  771 ? 0.3894 0.3337 0.3577 -0.0635 0.0240  -0.0643 797 ARG B O   
23844 C CB  . ARG B  771 ? 0.4468 0.4195 0.4216 -0.0619 0.0134  -0.0605 797 ARG B CB  
23845 C CG  . ARG B  771 ? 0.4956 0.4830 0.4745 -0.0613 0.0082  -0.0580 797 ARG B CG  
23846 C CD  . ARG B  771 ? 0.5515 0.5402 0.5358 -0.0624 0.0078  -0.0530 797 ARG B CD  
23847 N NE  . ARG B  771 ? 0.5885 0.5711 0.5755 -0.0573 0.0101  -0.0463 797 ARG B NE  
23848 C CZ  . ARG B  771 ? 0.5901 0.5755 0.5817 -0.0563 0.0091  -0.0406 797 ARG B CZ  
23849 N NH1 . ARG B  771 ? 0.5822 0.5761 0.5760 -0.0599 0.0062  -0.0408 797 ARG B NH1 
23850 N NH2 . ARG B  771 ? 0.5685 0.5489 0.5625 -0.0518 0.0111  -0.0345 797 ARG B NH2 
23864 N N   . LEU B  772 ? 0.4119 0.3551 0.3773 -0.0763 0.0238  -0.0732 798 LEU B N   
23865 C CA  . LEU B  772 ? 0.4198 0.3460 0.3814 -0.0768 0.0301  -0.0751 798 LEU B CA  
23866 C C   . LEU B  772 ? 0.4202 0.3371 0.3862 -0.0719 0.0340  -0.0674 798 LEU B C   
23867 O O   . LEU B  772 ? 0.4198 0.3246 0.3837 -0.0683 0.0389  -0.0667 798 LEU B O   
23868 C CB  . LEU B  772 ? 0.4285 0.3488 0.3871 -0.0857 0.0320  -0.0815 798 LEU B CB  
23869 C CG  . LEU B  772 ? 0.4515 0.3771 0.4042 -0.0912 0.0298  -0.0904 798 LEU B CG  
23870 C CD1 . LEU B  772 ? 0.4648 0.3845 0.4155 -0.1006 0.0317  -0.0961 798 LEU B CD1 
23871 C CD2 . LEU B  772 ? 0.4637 0.3823 0.4098 -0.0879 0.0325  -0.0940 798 LEU B CD2 
23883 N N   . VAL B  773 ? 0.4156 0.3387 0.3876 -0.0714 0.0317  -0.0613 799 VAL B N   
23884 C CA  . VAL B  773 ? 0.4213 0.3380 0.3978 -0.0665 0.0344  -0.0531 799 VAL B CA  
23885 C C   . VAL B  773 ? 0.4204 0.3370 0.3978 -0.0583 0.0351  -0.0488 799 VAL B C   
23886 O O   . VAL B  773 ? 0.4314 0.3399 0.4115 -0.0539 0.0387  -0.0430 799 VAL B O   
23887 C CB  . VAL B  773 ? 0.4268 0.3525 0.4089 -0.0673 0.0310  -0.0475 799 VAL B CB  
23888 C CG1 . VAL B  773 ? 0.4339 0.3580 0.4161 -0.0750 0.0315  -0.0502 799 VAL B CG1 
23889 C CG2 . VAL B  773 ? 0.4295 0.3715 0.4136 -0.0653 0.0249  -0.0468 799 VAL B CG2 
23899 N N   . ASP B  774 ? 0.4059 0.3327 0.3819 -0.0559 0.0313  -0.0508 800 ASP B N   
23900 C CA  . ASP B  774 ? 0.4038 0.3322 0.3807 -0.0486 0.0315  -0.0472 800 ASP B CA  
23901 C C   . ASP B  774 ? 0.4102 0.3310 0.3810 -0.0471 0.0349  -0.0524 800 ASP B C   
23902 O O   . ASP B  774 ? 0.4153 0.3364 0.3865 -0.0409 0.0358  -0.0496 800 ASP B O   
23903 C CB  . ASP B  774 ? 0.4216 0.3656 0.4009 -0.0466 0.0255  -0.0454 800 ASP B CB  
23904 C CG  . ASP B  774 ? 0.4769 0.4282 0.4619 -0.0471 0.0224  -0.0399 800 ASP B CG  
23905 O OD1 . ASP B  774 ? 0.4796 0.4244 0.4675 -0.0469 0.0250  -0.0353 800 ASP B OD1 
23906 O OD2 . ASP B  774 ? 0.5008 0.4643 0.4872 -0.0475 0.0176  -0.0399 800 ASP B OD2 
23911 N N   . VAL B  775 ? 0.4076 0.3215 0.3729 -0.0527 0.0371  -0.0597 801 VAL B N   
23912 C CA  . VAL B  775 ? 0.4182 0.3232 0.3769 -0.0520 0.0410  -0.0651 801 VAL B CA  
23913 C C   . VAL B  775 ? 0.4378 0.3262 0.3971 -0.0505 0.0479  -0.0627 801 VAL B C   
23914 O O   . VAL B  775 ? 0.4466 0.3254 0.4034 -0.0559 0.0510  -0.0666 801 VAL B O   
23915 C CB  . VAL B  775 ? 0.4158 0.3226 0.3679 -0.0594 0.0395  -0.0745 801 VAL B CB  
23916 C CG1 . VAL B  775 ? 0.4251 0.3228 0.3695 -0.0587 0.0435  -0.0803 801 VAL B CG1 
23917 C CG2 . VAL B  775 ? 0.4066 0.3310 0.3596 -0.0609 0.0323  -0.0756 801 VAL B CG2 
23927 N N   . ILE B  776 ? 0.4480 0.3339 0.4115 -0.0430 0.0502  -0.0556 802 ILE B N   
23928 C CA  . ILE B  776 ? 0.4688 0.3417 0.4353 -0.0398 0.0560  -0.0504 802 ILE B CA  
23929 C C   . ILE B  776 ? 0.4848 0.3444 0.4478 -0.0354 0.0628  -0.0518 802 ILE B C   
23930 O O   . ILE B  776 ? 0.4860 0.3485 0.4461 -0.0320 0.0627  -0.0538 802 ILE B O   
23931 C CB  . ILE B  776 ? 0.4771 0.3583 0.4520 -0.0344 0.0534  -0.0404 802 ILE B CB  
23932 C CG1 . ILE B  776 ? 0.4858 0.3758 0.4640 -0.0393 0.0485  -0.0387 802 ILE B CG1 
23933 C CG2 . ILE B  776 ? 0.4935 0.3637 0.4723 -0.0289 0.0591  -0.0334 802 ILE B CG2 
23934 C CD1 . ILE B  776 ? 0.4979 0.4007 0.4827 -0.0352 0.0438  -0.0308 802 ILE B CD1 
23946 N N   . CYS B  777 ? 0.4978 0.3425 0.4614 -0.0350 0.0691  -0.0500 803 CYS B N   
23947 C CA  . CYS B  777 ? 0.5215 0.3518 0.4827 -0.0303 0.0766  -0.0503 803 CYS B CA  
23948 C C   . CYS B  777 ? 0.5288 0.3625 0.4969 -0.0210 0.0774  -0.0408 803 CYS B C   
23949 O O   . CYS B  777 ? 0.5285 0.3653 0.5035 -0.0190 0.0762  -0.0330 803 CYS B O   
23950 C CB  . CYS B  777 ? 0.5414 0.3545 0.5014 -0.0333 0.0830  -0.0512 803 CYS B CB  
23951 S SG  . CYS B  777 ? 0.6027 0.4112 0.5557 -0.0451 0.0823  -0.0616 803 CYS B SG  
23956 N N   . ALA B  778 ? 0.5347 0.3671 0.5009 -0.0156 0.0801  -0.0414 804 ALA B N   
23957 C CA  . ALA B  778 ? 0.5423 0.3766 0.5151 -0.0067 0.0821  -0.0328 804 ALA B CA  
23958 C C   . ALA B  778 ? 0.5616 0.3785 0.5346 -0.0023 0.0911  -0.0309 804 ALA B C   
23959 O O   . ALA B  778 ? 0.5532 0.3701 0.5330 0.0046  0.0933  -0.0224 804 ALA B O   
23960 C CB  . ALA B  778 ? 0.5387 0.3819 0.5099 -0.0029 0.0801  -0.0340 804 ALA B CB  
23966 N N   . SER B  779 ? 0.5896 0.3918 0.5549 -0.0063 0.0964  -0.0388 805 SER B N   
23967 C CA  . SER B  779 ? 0.6186 0.4025 0.5829 -0.0027 0.1056  -0.0383 805 SER B CA  
23968 C C   . SER B  779 ? 0.6418 0.4111 0.5987 -0.0105 0.1094  -0.0467 805 SER B C   
23969 O O   . SER B  779 ? 0.6471 0.4210 0.5979 -0.0179 0.1053  -0.0547 805 SER B O   
23970 C CB  . SER B  779 ? 0.6509 0.4318 0.6121 0.0031  0.1099  -0.0404 805 SER B CB  
23971 O OG  . SER B  779 ? 0.7102 0.4903 0.6615 -0.0021 0.1092  -0.0509 805 SER B OG  
23977 N N   . PRO B  780 ? 0.6531 0.4045 0.6099 -0.0090 0.1174  -0.0455 806 PRO B N   
23978 C CA  . PRO B  780 ? 0.6560 0.4005 0.6202 -0.0003 0.1229  -0.0357 806 PRO B CA  
23979 C C   . PRO B  780 ? 0.6589 0.4128 0.6321 0.0007  0.1183  -0.0258 806 PRO B C   
23980 O O   . PRO B  780 ? 0.6579 0.4226 0.6314 -0.0055 0.1113  -0.0270 806 PRO B O   
23981 C CB  . PRO B  780 ? 0.6732 0.3947 0.6322 -0.0017 0.1325  -0.0400 806 PRO B CB  
23982 C CG  . PRO B  780 ? 0.6812 0.4000 0.6337 -0.0129 0.1299  -0.0487 806 PRO B CG  
23983 C CD  . PRO B  780 ? 0.6549 0.3914 0.6044 -0.0171 0.1213  -0.0539 806 PRO B CD  
23991 N N   . GLY B  781 ? 0.6603 0.4108 0.6409 0.0086  0.1221  -0.0159 807 GLY B N   
23992 C CA  . GLY B  781 ? 0.6623 0.4217 0.6515 0.0104  0.1182  -0.0058 807 GLY B CA  
23993 C C   . GLY B  781 ? 0.6700 0.4266 0.6580 0.0026  0.1162  -0.0070 807 GLY B C   
23994 O O   . GLY B  781 ? 0.6648 0.4353 0.6565 0.0000  0.1091  -0.0034 807 GLY B O   
23998 N N   . ASP B  782 ? 0.6828 0.4213 0.6656 -0.0014 0.1226  -0.0121 808 ASP B N   
23999 C CA  . ASP B  782 ? 0.6954 0.4294 0.6767 -0.0094 0.1216  -0.0138 808 ASP B CA  
24000 C C   . ASP B  782 ? 0.6880 0.4348 0.6655 -0.0186 0.1136  -0.0211 808 ASP B C   
24001 O O   . ASP B  782 ? 0.6861 0.4355 0.6648 -0.0243 0.1107  -0.0200 808 ASP B O   
24002 C CB  . ASP B  782 ? 0.7415 0.4525 0.7173 -0.0123 0.1308  -0.0188 808 ASP B CB  
24003 C CG  . ASP B  782 ? 0.8406 0.5425 0.8076 -0.0144 0.1346  -0.0298 808 ASP B CG  
24004 O OD1 . ASP B  782 ? 0.8611 0.5608 0.8284 -0.0070 0.1382  -0.0287 808 ASP B OD1 
24005 O OD2 . ASP B  782 ? 0.8801 0.5773 0.8400 -0.0236 0.1342  -0.0396 808 ASP B OD2 
24010 N N   . GLN B  783 ? 0.6772 0.4320 0.6501 -0.0199 0.1102  -0.0282 809 GLN B N   
24011 C CA  . GLN B  783 ? 0.6690 0.4367 0.6385 -0.0278 0.1027  -0.0350 809 GLN B CA  
24012 C C   . GLN B  783 ? 0.6553 0.4440 0.6295 -0.0249 0.0945  -0.0307 809 GLN B C   
24013 O O   . GLN B  783 ? 0.6486 0.4490 0.6213 -0.0308 0.0880  -0.0346 809 GLN B O   
24014 C CB  . GLN B  783 ? 0.6878 0.4499 0.6479 -0.0324 0.1044  -0.0467 809 GLN B CB  
24015 C CG  . GLN B  783 ? 0.7250 0.4658 0.6793 -0.0363 0.1127  -0.0525 809 GLN B CG  
24016 C CD  . GLN B  783 ? 0.7649 0.5010 0.7196 -0.0440 0.1125  -0.0530 809 GLN B CD  
24017 O OE1 . GLN B  783 ? 0.7694 0.5187 0.7253 -0.0497 0.1056  -0.0541 809 GLN B OE1 
24018 N NE2 . GLN B  783 ? 0.7733 0.4903 0.7270 -0.0443 0.1205  -0.0524 809 GLN B NE2 
24027 N N   . ARG B  784 ? 0.6493 0.4427 0.6292 -0.0161 0.0948  -0.0227 810 ARG B N   
24028 C CA  . ARG B  784 ? 0.6464 0.4588 0.6310 -0.0132 0.0876  -0.0183 810 ARG B CA  
24029 C C   . ARG B  784 ? 0.6254 0.4494 0.6135 -0.0178 0.0810  -0.0152 810 ARG B C   
24030 O O   . ARG B  784 ? 0.6306 0.4491 0.6214 -0.0191 0.0827  -0.0108 810 ARG B O   
24031 C CB  . ARG B  784 ? 0.6763 0.4902 0.6675 -0.0034 0.0899  -0.0091 810 ARG B CB  
24032 C CG  . ARG B  784 ? 0.7314 0.5642 0.7286 -0.0003 0.0829  -0.0030 810 ARG B CG  
24033 C CD  . ARG B  784 ? 0.7905 0.6273 0.7910 0.0079  0.0844  0.0009  810 ARG B CD  
24034 N NE  . ARG B  784 ? 0.8552 0.6787 0.8577 0.0143  0.0925  0.0049  810 ARG B NE  
24035 C CZ  . ARG B  784 ? 0.8982 0.7225 0.9032 0.0216  0.0954  0.0078  810 ARG B CZ  
24036 N NH1 . ARG B  784 ? 0.9016 0.7133 0.9085 0.0275  0.1032  0.0114  810 ARG B NH1 
24037 N NH2 . ARG B  784 ? 0.9020 0.7393 0.9076 0.0231  0.0910  0.0073  810 ARG B NH2 
24051 N N   . GLY B  785 ? 0.6003 0.4395 0.5879 -0.0204 0.0739  -0.0179 811 GLY B N   
24052 C CA  . GLY B  785 ? 0.5793 0.4304 0.5696 -0.0248 0.0676  -0.0160 811 GLY B CA  
24053 C C   . GLY B  785 ? 0.5626 0.4126 0.5481 -0.0339 0.0660  -0.0237 811 GLY B C   
24054 O O   . GLY B  785 ? 0.5643 0.4265 0.5510 -0.0378 0.0600  -0.0242 811 GLY B O   
24058 N N   . LYS B  786 ? 0.5489 0.3846 0.5292 -0.0375 0.0713  -0.0299 812 LYS B N   
24059 C CA  . LYS B  786 ? 0.5442 0.3783 0.5200 -0.0467 0.0702  -0.0374 812 LYS B CA  
24060 C C   . LYS B  786 ? 0.5309 0.3727 0.5012 -0.0504 0.0665  -0.0463 812 LYS B C   
24061 O O   . LYS B  786 ? 0.5300 0.3723 0.4979 -0.0461 0.0672  -0.0481 812 LYS B O   
24062 C CB  . LYS B  786 ? 0.5814 0.3960 0.5537 -0.0496 0.0778  -0.0404 812 LYS B CB  
24063 C CG  . LYS B  786 ? 0.6537 0.4593 0.6310 -0.0463 0.0821  -0.0316 812 LYS B CG  
24064 C CD  . LYS B  786 ? 0.7352 0.5204 0.7086 -0.0495 0.0901  -0.0351 812 LYS B CD  
24065 C CE  . LYS B  786 ? 0.8033 0.5802 0.7813 -0.0479 0.0937  -0.0267 812 LYS B CE  
24066 N NZ  . LYS B  786 ? 0.8441 0.6232 0.8221 -0.0563 0.0914  -0.0282 812 LYS B NZ  
24080 N N   . SER B  787 ? 0.5212 0.3689 0.4894 -0.0584 0.0629  -0.0517 813 SER B N   
24081 C CA  . SER B  787 ? 0.5208 0.3760 0.4836 -0.0625 0.0593  -0.0602 813 SER B CA  
24082 C C   . SER B  787 ? 0.5346 0.3755 0.4900 -0.0653 0.0650  -0.0681 813 SER B C   
24083 O O   . SER B  787 ? 0.5390 0.3646 0.4932 -0.0673 0.0709  -0.0685 813 SER B O   
24084 C CB  . SER B  787 ? 0.5171 0.3828 0.4805 -0.0702 0.0542  -0.0635 813 SER B CB  
24085 O OG  . SER B  787 ? 0.5192 0.3930 0.4777 -0.0741 0.0506  -0.0714 813 SER B OG  
24091 N N   . ILE B  788 ? 0.5365 0.3818 0.4864 -0.0655 0.0633  -0.0743 814 ILE B N   
24092 C CA  . ILE B  788 ? 0.5530 0.3856 0.4948 -0.0685 0.0683  -0.0826 814 ILE B CA  
24093 C C   . ILE B  788 ? 0.5749 0.4016 0.5131 -0.0787 0.0694  -0.0895 814 ILE B C   
24094 O O   . ILE B  788 ? 0.5823 0.3938 0.5147 -0.0817 0.0753  -0.0952 814 ILE B O   
24095 C CB  . ILE B  788 ? 0.5526 0.3931 0.4888 -0.0671 0.0656  -0.0878 814 ILE B CB  
24096 C CG1 . ILE B  788 ? 0.5546 0.4121 0.4898 -0.0729 0.0580  -0.0922 814 ILE B CG1 
24097 C CG2 . ILE B  788 ? 0.5531 0.3980 0.4928 -0.0573 0.0655  -0.0810 814 ILE B CG2 
24098 C CD1 . ILE B  788 ? 0.5732 0.4364 0.5011 -0.0734 0.0560  -0.0989 814 ILE B CD1 
24110 N N   . VAL B  789 ? 0.5837 0.4221 0.5253 -0.0840 0.0640  -0.0893 815 VAL B N   
24111 C CA  . VAL B  789 ? 0.6094 0.4446 0.5488 -0.0940 0.0643  -0.0952 815 VAL B CA  
24112 C C   . VAL B  789 ? 0.6390 0.4578 0.5807 -0.0954 0.0707  -0.0917 815 VAL B C   
24113 O O   . VAL B  789 ? 0.6411 0.4538 0.5805 -0.1038 0.0724  -0.0968 815 VAL B O   
24114 C CB  . VAL B  789 ? 0.6132 0.4677 0.5563 -0.0985 0.0564  -0.0954 815 VAL B CB  
24115 C CG1 . VAL B  789 ? 0.6111 0.4707 0.5624 -0.0957 0.0547  -0.0862 815 VAL B CG1 
24116 C CG2 . VAL B  789 ? 0.6286 0.4834 0.5681 -0.1095 0.0557  -0.1037 815 VAL B CG2 
24126 N N   . SER B  790 ? 0.6610 0.4727 0.6072 -0.0874 0.0742  -0.0831 816 SER B N   
24127 C CA  . SER B  790 ? 0.6919 0.4873 0.6402 -0.0874 0.0807  -0.0788 816 SER B CA  
24128 C C   . SER B  790 ? 0.7202 0.4957 0.6628 -0.0855 0.0890  -0.0826 816 SER B C   
24129 O O   . SER B  790 ? 0.7226 0.4986 0.6611 -0.0820 0.0895  -0.0860 816 SER B O   
24130 C CB  . SER B  790 ? 0.7091 0.5084 0.6653 -0.0795 0.0800  -0.0672 816 SER B CB  
24131 O OG  . SER B  790 ? 0.7408 0.5576 0.7016 -0.0813 0.0728  -0.0642 816 SER B OG  
24137 N N   . LEU B  791 ? 0.7432 0.5010 0.6853 -0.0878 0.0960  -0.0819 817 LEU B N   
24138 C CA  . LEU B  791 ? 0.7739 0.5109 0.7103 -0.0867 0.1047  -0.0860 817 LEU B CA  
24139 C C   . LEU B  791 ? 0.7783 0.5127 0.7056 -0.0957 0.1048  -0.0988 817 LEU B C   
24140 O O   . LEU B  791 ? 0.7685 0.5169 0.6930 -0.0966 0.0990  -0.1033 817 LEU B O   
24141 C CB  . LEU B  791 ? 0.7921 0.5257 0.7295 -0.0754 0.1079  -0.0810 817 LEU B CB  
24142 C CG  . LEU B  791 ? 0.8286 0.5610 0.7586 -0.0737 0.1090  -0.0886 817 LEU B CG  
24143 C CD1 . LEU B  791 ? 0.8482 0.5583 0.7710 -0.0760 0.1182  -0.0952 817 LEU B CD1 
24144 C CD2 . LEU B  791 ? 0.8383 0.5771 0.7722 -0.0628 0.1084  -0.0817 817 LEU B CD2 
24156 N N   . GLU B  792 ? 0.7918 0.5086 0.7143 -0.1026 0.1111  -0.1046 818 GLU B N   
24157 C CA  . GLU B  792 ? 0.8032 0.5175 0.7168 -0.1120 0.1112  -0.1170 818 GLU B CA  
24158 C C   . GLU B  792 ? 0.8116 0.5072 0.7176 -0.1097 0.1193  -0.1223 818 GLU B C   
24159 O O   . GLU B  792 ? 0.8138 0.5121 0.7124 -0.1123 0.1181  -0.1308 818 GLU B O   
24160 C CB  . GLU B  792 ? 0.8432 0.5540 0.7562 -0.1236 0.1114  -0.1214 818 GLU B CB  
24161 C CG  . GLU B  792 ? 0.9246 0.6136 0.8386 -0.1246 0.1201  -0.1185 818 GLU B CG  
24162 C CD  . GLU B  792 ? 1.0083 0.6952 0.9223 -0.1362 0.1199  -0.1223 818 GLU B CD  
24163 O OE1 . GLU B  792 ? 1.0167 0.7132 0.9379 -0.1367 0.1162  -0.1155 818 GLU B OE1 
24164 O OE2 . GLU B  792 ? 1.0414 0.7172 0.9481 -0.1450 0.1236  -0.1323 818 GLU B OE2 
24171 C C1  . NAG C  .   ? 0.2352 0.3099 0.2714 0.0369  0.0214  0.0306  1   NAG C C1  
24172 C C2  . NAG C  .   ? 0.2391 0.3109 0.2738 0.0391  0.0181  0.0281  1   NAG C C2  
24173 C C3  . NAG C  .   ? 0.2466 0.3224 0.2855 0.0413  0.0181  0.0266  1   NAG C C3  
24174 C C4  . NAG C  .   ? 0.2518 0.3334 0.2984 0.0391  0.0182  0.0279  1   NAG C C4  
24175 C C5  . NAG C  .   ? 0.2458 0.3307 0.2937 0.0365  0.0214  0.0301  1   NAG C C5  
24176 C C6  . NAG C  .   ? 0.2433 0.3343 0.2985 0.0332  0.0214  0.0314  1   NAG C C6  
24177 C C7  . NAG C  .   ? 0.2373 0.3012 0.2614 0.0415  0.0152  0.0262  1   NAG C C7  
24178 C C8  . NAG C  .   ? 0.2400 0.3019 0.2571 0.0436  0.0153  0.0250  1   NAG C C8  
24179 N N2  . NAG C  .   ? 0.2332 0.3014 0.2609 0.0412  0.0181  0.0273  1   NAG C N2  
24180 O O3  . NAG C  .   ? 0.2436 0.3155 0.2808 0.0428  0.0149  0.0245  1   NAG C O3  
24181 O O4  . NAG C  .   ? 0.2712 0.3577 0.3222 0.0419  0.0187  0.0272  1   NAG C O4  
24182 O O5  . NAG C  .   ? 0.2410 0.3202 0.2842 0.0343  0.0213  0.0312  1   NAG C O5  
24183 O O6  . NAG C  .   ? 0.2548 0.3431 0.3111 0.0305  0.0181  0.0311  1   NAG C O6  
24184 O O7  . NAG C  .   ? 0.2436 0.3055 0.2697 0.0398  0.0127  0.0261  1   NAG C O7  
24197 C C1  . NAG C  .   ? 0.2968 0.3822 0.3498 0.0433  0.0157  0.0260  2   NAG C C1  
24198 C C2  . NAG C  .   ? 0.2966 0.3890 0.3563 0.0457  0.0166  0.0265  2   NAG C C2  
24199 C C3  . NAG C  .   ? 0.3138 0.4041 0.3751 0.0470  0.0131  0.0258  2   NAG C C3  
24200 C C4  . NAG C  .   ? 0.3467 0.4285 0.4011 0.0494  0.0121  0.0233  2   NAG C C4  
24201 C C5  . NAG C  .   ? 0.3427 0.4192 0.3910 0.0467  0.0115  0.0228  2   NAG C C5  
24202 C C6  . NAG C  .   ? 0.3582 0.4275 0.3994 0.0484  0.0107  0.0204  2   NAG C C6  
24203 C C7  . NAG C  .   ? 0.2590 0.3675 0.3307 0.0440  0.0200  0.0297  2   NAG C C7  
24204 C C8  . NAG C  .   ? 0.2547 0.3713 0.3329 0.0396  0.0201  0.0318  2   NAG C C8  
24205 N N2  . NAG C  .   ? 0.2762 0.3763 0.3422 0.0425  0.0175  0.0287  2   NAG C N2  
24206 O O3  . NAG C  .   ? 0.2973 0.3942 0.3650 0.0499  0.0138  0.0266  2   NAG C O3  
24207 O O4  . NAG C  .   ? 0.3814 0.4603 0.4367 0.0497  0.0087  0.0229  2   NAG C O4  
24208 O O5  . NAG C  .   ? 0.3180 0.3971 0.3651 0.0460  0.0147  0.0239  2   NAG C O5  
24209 O O6  . NAG C  .   ? 0.3626 0.4316 0.4014 0.0519  0.0134  0.0190  2   NAG C O6  
24210 O O7  . NAG C  .   ? 0.2462 0.3559 0.3177 0.0484  0.0223  0.0289  2   NAG C O7  
24223 C C1  . BMA C  .   ? 0.4174 0.4946 0.4731 0.0539  0.0089  0.0219  3   BMA C C1  
24224 C C2  . BMA C  .   ? 0.4346 0.5075 0.4899 0.0531  0.0051  0.0217  3   BMA C C2  
24225 C C3  . BMA C  .   ? 0.4503 0.5207 0.5063 0.0577  0.0052  0.0212  3   BMA C C3  
24226 C C4  . BMA C  .   ? 0.4592 0.5379 0.5224 0.0610  0.0074  0.0231  3   BMA C C4  
24227 C C5  . BMA C  .   ? 0.4622 0.5453 0.5255 0.0614  0.0113  0.0228  3   BMA C C5  
24228 C C6  . BMA C  .   ? 0.4870 0.5798 0.5581 0.0643  0.0138  0.0248  3   BMA C C6  
24229 O O2  . BMA C  .   ? 0.4316 0.5096 0.4920 0.0499  0.0028  0.0239  3   BMA C O2  
24230 O O3  . BMA C  .   ? 0.4556 0.5227 0.5118 0.0567  0.0017  0.0217  3   BMA C O3  
24231 O O4  . BMA C  .   ? 0.4691 0.5442 0.5322 0.0661  0.0083  0.0224  3   BMA C O4  
24232 O O5  . BMA C  .   ? 0.4326 0.5177 0.4953 0.0564  0.0107  0.0236  3   BMA C O5  
24233 O O6  . BMA C  .   ? 0.5166 0.6177 0.5949 0.0618  0.0116  0.0276  3   BMA C O6  
24242 C C1  . MAN C  .   ? 0.4671 0.5249 0.5173 0.0576  0.0007  0.0196  4   MAN C C1  
24243 C C2  . MAN C  .   ? 0.4743 0.5305 0.5264 0.0573  -0.0026 0.0210  4   MAN C C2  
24244 C C3  . MAN C  .   ? 0.4733 0.5313 0.5260 0.0521  -0.0056 0.0219  4   MAN C C3  
24245 C C4  . MAN C  .   ? 0.4742 0.5270 0.5207 0.0491  -0.0058 0.0197  4   MAN C C4  
24246 C C5  . MAN C  .   ? 0.4655 0.5201 0.5104 0.0499  -0.0026 0.0187  4   MAN C C5  
24247 C C6  . MAN C  .   ? 0.4653 0.5153 0.5041 0.0477  -0.0029 0.0168  4   MAN C C6  
24248 O O2  . MAN C  .   ? 0.4850 0.5318 0.5316 0.0586  -0.0030 0.0190  4   MAN C O2  
24249 O O3  . MAN C  .   ? 0.4797 0.5356 0.5329 0.0516  -0.0086 0.0231  4   MAN C O3  
24250 O O4  . MAN C  .   ? 0.4802 0.5349 0.5275 0.0447  -0.0079 0.0206  4   MAN C O4  
24251 O O5  . MAN C  .   ? 0.4638 0.5169 0.5080 0.0543  0.0000  0.0177  4   MAN C O5  
24252 O O6  . MAN C  .   ? 0.4648 0.5075 0.4982 0.0487  -0.0034 0.0144  4   MAN C O6  
24263 C C1  . MAN C  .   ? 0.5593 0.6800 0.6513 0.0577  0.0110  0.0322  5   MAN C C1  
24264 C C2  . MAN C  .   ? 0.5463 0.6592 0.6337 0.0635  0.0130  0.0301  5   MAN C C2  
24265 C C3  . MAN C  .   ? 0.5621 0.6768 0.6540 0.0686  0.0119  0.0314  5   MAN C C3  
24266 C C4  . MAN C  .   ? 0.5724 0.6852 0.6646 0.0659  0.0070  0.0326  5   MAN C C4  
24267 C C5  . MAN C  .   ? 0.5725 0.6940 0.6692 0.0600  0.0049  0.0346  5   MAN C C5  
24268 C C6  . MAN C  .   ? 0.5843 0.7040 0.6804 0.0567  0.0002  0.0355  5   MAN C C6  
24269 O O1  . MAN C  .   ? 0.5588 0.6917 0.6591 0.0586  0.0128  0.0343  5   MAN C O1  
24270 O O3  . MAN C  .   ? 0.5705 0.6766 0.6575 0.0737  0.0141  0.0292  5   MAN C O3  
24271 O O4  . MAN C  .   ? 0.5716 0.6860 0.6679 0.0708  0.0059  0.0344  5   MAN C O4  
24272 O O5  . MAN C  .   ? 0.5679 0.6870 0.6604 0.0556  0.0065  0.0330  5   MAN C O5  
24273 O O6  . MAN C  .   ? 0.5879 0.7149 0.6873 0.0507  -0.0014 0.0368  5   MAN C O6  
24284 C C1  . NAG D  .   ? 0.2544 0.2868 0.2807 -0.0085 -0.0116 0.0112  1   NAG D C1  
24285 C C2  . NAG D  .   ? 0.2591 0.2965 0.2880 -0.0069 -0.0147 0.0130  1   NAG D C2  
24286 C C3  . NAG D  .   ? 0.2821 0.3193 0.3112 -0.0030 -0.0160 0.0136  1   NAG D C3  
24287 C C4  . NAG D  .   ? 0.3136 0.3482 0.3427 0.0003  -0.0137 0.0134  1   NAG D C4  
24288 C C5  . NAG D  .   ? 0.2872 0.3180 0.3144 -0.0012 -0.0110 0.0119  1   NAG D C5  
24289 C C6  . NAG D  .   ? 0.2794 0.3083 0.3070 0.0023  -0.0087 0.0122  1   NAG D C6  
24290 C C7  . NAG D  .   ? 0.2636 0.3086 0.2940 -0.0125 -0.0183 0.0143  1   NAG D C7  
24291 C C8  . NAG D  .   ? 0.2635 0.3117 0.2925 -0.0166 -0.0209 0.0144  1   NAG D C8  
24292 N N2  . NAG D  .   ? 0.2551 0.2955 0.2834 -0.0105 -0.0172 0.0133  1   NAG D N2  
24293 O O3  . NAG D  .   ? 0.2814 0.3222 0.3129 -0.0010 -0.0181 0.0153  1   NAG D O3  
24294 O O4  . NAG D  .   ? 0.3741 0.4087 0.4029 0.0030  -0.0150 0.0134  1   NAG D O4  
24295 O O5  . NAG D  .   ? 0.2664 0.2965 0.2934 -0.0045 -0.0096 0.0115  1   NAG D O5  
24296 O O6  . NAG D  .   ? 0.2758 0.3052 0.3050 0.0038  -0.0076 0.0135  1   NAG D O6  
24297 O O7  . NAG D  .   ? 0.2637 0.3109 0.2971 -0.0112 -0.0173 0.0152  1   NAG D O7  
24310 C C1  . NAG D  .   ? 0.4444 0.4806 0.4747 0.0064  -0.0157 0.0145  2   NAG D C1  
24311 C C2  . NAG D  .   ? 0.4822 0.5171 0.5111 0.0086  -0.0160 0.0139  2   NAG D C2  
24312 C C3  . NAG D  .   ? 0.5106 0.5467 0.5403 0.0119  -0.0165 0.0146  2   NAG D C3  
24313 C C4  . NAG D  .   ? 0.5335 0.5709 0.5643 0.0121  -0.0183 0.0154  2   NAG D C4  
24314 C C5  . NAG D  .   ? 0.5097 0.5493 0.5424 0.0099  -0.0181 0.0162  2   NAG D C5  
24315 C C6  . NAG D  .   ? 0.5174 0.5596 0.5518 0.0100  -0.0201 0.0175  2   NAG D C6  
24316 C C7  . NAG D  .   ? 0.4971 0.5295 0.5242 0.0080  -0.0133 0.0124  2   NAG D C7  
24317 C C8  . NAG D  .   ? 0.4985 0.5303 0.5259 0.0099  -0.0109 0.0123  2   NAG D C8  
24318 N N2  . NAG D  .   ? 0.4916 0.5252 0.5199 0.0093  -0.0138 0.0134  2   NAG D N2  
24319 O O3  . NAG D  .   ? 0.5152 0.5505 0.5432 0.0132  -0.0172 0.0138  2   NAG D O3  
24320 O O4  . NAG D  .   ? 0.5751 0.6134 0.6066 0.0153  -0.0180 0.0159  2   NAG D O4  
24321 O O5  . NAG D  .   ? 0.4760 0.5144 0.5073 0.0064  -0.0179 0.0154  2   NAG D O5  
24322 O O6  . NAG D  .   ? 0.5263 0.5670 0.5588 0.0087  -0.0222 0.0175  2   NAG D O6  
24323 O O7  . NAG D  .   ? 0.5029 0.5350 0.5288 0.0055  -0.0146 0.0117  2   NAG D O7  
24336 C C1  . BMA D  .   ? 0.6075 0.6452 0.6387 0.0168  -0.0195 0.0161  3   BMA D C1  
24337 C C2  . BMA D  .   ? 0.6198 0.6594 0.6528 0.0198  -0.0185 0.0168  3   BMA D C2  
24338 C C3  . BMA D  .   ? 0.6326 0.6707 0.6651 0.0219  -0.0197 0.0169  3   BMA D C3  
24339 C C4  . BMA D  .   ? 0.6393 0.6732 0.6681 0.0219  -0.0204 0.0154  3   BMA D C4  
24340 C C5  . BMA D  .   ? 0.6376 0.6704 0.6650 0.0186  -0.0214 0.0149  3   BMA D C5  
24341 C C6  . BMA D  .   ? 0.6478 0.6775 0.6718 0.0181  -0.0220 0.0133  3   BMA D C6  
24342 O O2  . BMA D  .   ? 0.6201 0.6595 0.6520 0.0214  -0.0168 0.0163  3   BMA D O2  
24343 O O3  . BMA D  .   ? 0.6362 0.6760 0.6703 0.0250  -0.0183 0.0174  3   BMA D O3  
24344 O O4  . BMA D  .   ? 0.6429 0.6740 0.6708 0.0235  -0.0214 0.0155  3   BMA D O4  
24345 O O5  . BMA D  .   ? 0.6240 0.6589 0.6524 0.0174  -0.0201 0.0148  3   BMA D O5  
24346 O O6  . BMA D  .   ? 0.6533 0.6829 0.6765 0.0151  -0.0226 0.0128  3   BMA D O6  
24357 C C1  . NAG E  .   ? 0.2378 0.2759 0.2498 -0.0154 -0.0330 0.0193  1   NAG E C1  
24358 C C2  . NAG E  .   ? 0.2396 0.2770 0.2556 -0.0107 -0.0319 0.0193  1   NAG E C2  
24359 C C3  . NAG E  .   ? 0.2377 0.2797 0.2576 -0.0091 -0.0329 0.0209  1   NAG E C3  
24360 C C4  . NAG E  .   ? 0.2496 0.2943 0.2695 -0.0089 -0.0361 0.0241  1   NAG E C4  
24361 C C5  . NAG E  .   ? 0.2358 0.2814 0.2516 -0.0138 -0.0374 0.0241  1   NAG E C5  
24362 C C6  . NAG E  .   ? 0.2328 0.2811 0.2478 -0.0139 -0.0408 0.0277  1   NAG E C6  
24363 C C7  . NAG E  .   ? 0.2721 0.3053 0.2887 -0.0085 -0.0276 0.0155  1   NAG E C7  
24364 C C8  . NAG E  .   ? 0.2713 0.3040 0.2888 -0.0082 -0.0246 0.0134  1   NAG E C8  
24365 N N2  . NAG E  .   ? 0.2531 0.2890 0.2694 -0.0108 -0.0290 0.0166  1   NAG E N2  
24366 O O3  . NAG E  .   ? 0.2334 0.2747 0.2565 -0.0047 -0.0318 0.0209  1   NAG E O3  
24367 O O4  . NAG E  .   ? 0.2698 0.3201 0.2941 -0.0074 -0.0369 0.0256  1   NAG E O4  
24368 O O5  . NAG E  .   ? 0.2347 0.2751 0.2464 -0.0152 -0.0362 0.0225  1   NAG E O5  
24369 O O6  . NAG E  .   ? 0.2319 0.2765 0.2468 -0.0100 -0.0417 0.0298  1   NAG E O6  
24370 O O7  . NAG E  .   ? 0.2813 0.3125 0.2972 -0.0067 -0.0286 0.0162  1   NAG E O7  
24383 C C1  . NAG E  .   ? 0.2957 0.3477 0.3225 -0.0035 -0.0388 0.0287  2   NAG E C1  
24384 C C2  . NAG E  .   ? 0.3036 0.3637 0.3352 -0.0032 -0.0398 0.0304  2   NAG E C2  
24385 C C3  . NAG E  .   ? 0.3184 0.3805 0.3531 0.0017  -0.0416 0.0339  2   NAG E C3  
24386 C C4  . NAG E  .   ? 0.3481 0.4042 0.3833 0.0065  -0.0396 0.0330  2   NAG E C4  
24387 C C5  . NAG E  .   ? 0.3389 0.3869 0.3687 0.0052  -0.0387 0.0310  2   NAG E C5  
24388 C C6  . NAG E  .   ? 0.3547 0.3970 0.3844 0.0089  -0.0368 0.0296  2   NAG E C6  
24389 C C7  . NAG E  .   ? 0.2998 0.3668 0.3296 -0.0125 -0.0403 0.0286  2   NAG E C7  
24390 C C8  . NAG E  .   ? 0.2990 0.3702 0.3260 -0.0181 -0.0424 0.0289  2   NAG E C8  
24391 N N2  . NAG E  .   ? 0.2956 0.3602 0.3255 -0.0083 -0.0416 0.0308  2   NAG E N2  
24392 O O3  . NAG E  .   ? 0.3098 0.3805 0.3498 0.0022  -0.0424 0.0355  2   NAG E O3  
24393 O O4  . NAG E  .   ? 0.3909 0.4475 0.4283 0.0113  -0.0408 0.0361  2   NAG E O4  
24394 O O5  . NAG E  .   ? 0.3128 0.3605 0.3407 0.0009  -0.0373 0.0281  2   NAG E O5  
24395 O O6  . NAG E  .   ? 0.3710 0.4069 0.3960 0.0072  -0.0363 0.0279  2   NAG E O6  
24396 O O7  . NAG E  .   ? 0.3024 0.3676 0.3337 -0.0120 -0.0375 0.0264  2   NAG E O7  
24409 C C1  . BMA E  .   ? 0.4368 0.4944 0.4783 0.0160  -0.0391 0.0361  3   BMA E C1  
24410 C C2  . BMA E  .   ? 0.4592 0.5128 0.5007 0.0211  -0.0397 0.0385  3   BMA E C2  
24411 C C3  . BMA E  .   ? 0.4786 0.5333 0.5243 0.0264  -0.0375 0.0384  3   BMA E C3  
24412 C C4  . BMA E  .   ? 0.4769 0.5424 0.5289 0.0264  -0.0377 0.0397  3   BMA E C4  
24413 C C5  . BMA E  .   ? 0.4701 0.5387 0.5213 0.0206  -0.0373 0.0373  3   BMA E C5  
24414 C C6  . BMA E  .   ? 0.4719 0.5510 0.5286 0.0193  -0.0377 0.0385  3   BMA E C6  
24415 O O2  . BMA E  .   ? 0.4581 0.5163 0.5008 0.0213  -0.0427 0.0424  3   BMA E O2  
24416 O O3  . BMA E  .   ? 0.4909 0.5416 0.5366 0.0314  -0.0377 0.0407  3   BMA E O3  
24417 O O4  . BMA E  .   ? 0.4831 0.5494 0.5385 0.0309  -0.0351 0.0391  3   BMA E O4  
24418 O O5  . BMA E  .   ? 0.4539 0.5208 0.5008 0.0160  -0.0394 0.0373  3   BMA E O5  
24419 O O6  . BMA E  .   ? 0.4764 0.5624 0.5354 0.0188  -0.0409 0.0420  3   BMA E O6  
24430 C C1  . NAG F  .   ? 0.2394 0.3661 0.2430 -0.0547 -0.0024 -0.0364 1   NAG F C1  
24431 C C2  . NAG F  .   ? 0.2428 0.3669 0.2476 -0.0553 -0.0058 -0.0336 1   NAG F C2  
24432 C C3  . NAG F  .   ? 0.2450 0.3741 0.2544 -0.0556 -0.0065 -0.0335 1   NAG F C3  
24433 C C4  . NAG F  .   ? 0.2546 0.3891 0.2682 -0.0516 -0.0054 -0.0358 1   NAG F C4  
24434 C C5  . NAG F  .   ? 0.2514 0.3883 0.2640 -0.0508 -0.0020 -0.0380 1   NAG F C5  
24435 C C6  . NAG F  .   ? 0.2615 0.4039 0.2786 -0.0461 -0.0006 -0.0398 1   NAG F C6  
24436 C C7  . NAG F  .   ? 0.2383 0.3546 0.2379 -0.0595 -0.0092 -0.0288 1   NAG F C7  
24437 C C8  . NAG F  .   ? 0.2379 0.3529 0.2345 -0.0638 -0.0104 -0.0258 1   NAG F C8  
24438 N N2  . NAG F  .   ? 0.2357 0.3567 0.2366 -0.0594 -0.0069 -0.0312 1   NAG F N2  
24439 O O3  . NAG F  .   ? 0.2386 0.3642 0.2487 -0.0555 -0.0092 -0.0314 1   NAG F O3  
24440 O O4  . NAG F  .   ? 0.2694 0.4097 0.2871 -0.0529 -0.0059 -0.0362 1   NAG F O4  
24441 O O5  . NAG F  .   ? 0.2426 0.3733 0.2506 -0.0503 -0.0013 -0.0381 1   NAG F O5  
24442 O O6  . NAG F  .   ? 0.2740 0.4133 0.2919 -0.0415 -0.0018 -0.0394 1   NAG F O6  
24443 O O7  . NAG F  .   ? 0.2362 0.3498 0.2371 -0.0562 -0.0102 -0.0287 1   NAG F O7  
24456 C C1  . NAG F  .   ? 0.2867 0.4266 0.3068 -0.0518 -0.0084 -0.0355 2   NAG F C1  
24457 C C2  . NAG F  .   ? 0.2854 0.4333 0.3102 -0.0525 -0.0084 -0.0369 2   NAG F C2  
24458 C C3  . NAG F  .   ? 0.3065 0.4534 0.3329 -0.0514 -0.0110 -0.0366 2   NAG F C3  
24459 C C4  . NAG F  .   ? 0.3376 0.4769 0.3611 -0.0543 -0.0124 -0.0345 2   NAG F C4  
24460 C C5  . NAG F  .   ? 0.3356 0.4683 0.3550 -0.0535 -0.0122 -0.0327 2   NAG F C5  
24461 C C6  . NAG F  .   ? 0.3568 0.4829 0.3737 -0.0561 -0.0134 -0.0300 2   NAG F C6  
24462 C C7  . NAG F  .   ? 0.2640 0.4269 0.2954 -0.0503 -0.0053 -0.0402 2   NAG F C7  
24463 C C8  . NAG F  .   ? 0.2529 0.4226 0.2879 -0.0455 -0.0037 -0.0415 2   NAG F C8  
24464 N N2  . NAG F  .   ? 0.2695 0.4240 0.2972 -0.0490 -0.0066 -0.0388 2   NAG F N2  
24465 O O3  . NAG F  .   ? 0.2963 0.4509 0.3269 -0.0527 -0.0114 -0.0382 2   NAG F O3  
24466 O O4  . NAG F  .   ? 0.3735 0.5108 0.3978 -0.0526 -0.0145 -0.0343 2   NAG F O4  
24467 O O5  . NAG F  .   ? 0.3098 0.4443 0.3276 -0.0549 -0.0100 -0.0332 2   NAG F O5  
24468 O O6  . NAG F  .   ? 0.3699 0.4968 0.3867 -0.0607 -0.0127 -0.0292 2   NAG F O6  
24469 O O7  . NAG F  .   ? 0.2706 0.4358 0.3029 -0.0550 -0.0052 -0.0401 2   NAG F O7  
24482 C C1  . BMA F  .   ? 0.4001 0.5377 0.4257 -0.0558 -0.0154 -0.0347 3   BMA F C1  
24483 C C2  . BMA F  .   ? 0.4094 0.5434 0.4346 -0.0533 -0.0173 -0.0346 3   BMA F C2  
24484 C C3  . BMA F  .   ? 0.4241 0.5581 0.4503 -0.0567 -0.0180 -0.0356 3   BMA F C3  
24485 C C4  . BMA F  .   ? 0.4331 0.5764 0.4630 -0.0590 -0.0176 -0.0382 3   BMA F C4  
24486 C C5  . BMA F  .   ? 0.4465 0.5930 0.4769 -0.0611 -0.0156 -0.0377 3   BMA F C5  
24487 C C6  . BMA F  .   ? 0.4826 0.6393 0.5172 -0.0631 -0.0149 -0.0400 3   BMA F C6  
24488 O O2  . BMA F  .   ? 0.4004 0.5388 0.4271 -0.0486 -0.0179 -0.0358 3   BMA F O2  
24489 O O3  . BMA F  .   ? 0.4276 0.5592 0.4532 -0.0541 -0.0195 -0.0361 3   BMA F O3  
24490 O O4  . BMA F  .   ? 0.4342 0.5765 0.4646 -0.0633 -0.0179 -0.0392 3   BMA F O4  
24491 O O5  . BMA F  .   ? 0.4172 0.5634 0.4464 -0.0572 -0.0149 -0.0370 3   BMA F O5  
24492 O O6  . BMA F  .   ? 0.5200 0.6843 0.5575 -0.0590 -0.0158 -0.0416 3   BMA F O6  
24501 C C1  . MAN F  .   ? 0.4365 0.5598 0.4599 -0.0553 -0.0198 -0.0347 4   MAN F C1  
24502 C C2  . MAN F  .   ? 0.4377 0.5608 0.4608 -0.0532 -0.0212 -0.0363 4   MAN F C2  
24503 C C3  . MAN F  .   ? 0.4470 0.5701 0.4693 -0.0476 -0.0220 -0.0354 4   MAN F C3  
24504 C C4  . MAN F  .   ? 0.4527 0.5685 0.4729 -0.0462 -0.0214 -0.0322 4   MAN F C4  
24505 C C5  . MAN F  .   ? 0.4412 0.5577 0.4616 -0.0489 -0.0202 -0.0311 4   MAN F C5  
24506 C C6  . MAN F  .   ? 0.4366 0.5467 0.4549 -0.0485 -0.0198 -0.0279 4   MAN F C6  
24507 O O2  . MAN F  .   ? 0.4356 0.5508 0.4568 -0.0549 -0.0210 -0.0356 4   MAN F O2  
24508 O O3  . MAN F  .   ? 0.4565 0.5789 0.4779 -0.0456 -0.0232 -0.0366 4   MAN F O3  
24509 O O4  . MAN F  .   ? 0.4627 0.5786 0.4823 -0.0415 -0.0218 -0.0315 4   MAN F O4  
24510 O O5  . MAN F  .   ? 0.4381 0.5549 0.4592 -0.0537 -0.0195 -0.0317 4   MAN F O5  
24511 O O6  . MAN F  .   ? 0.4345 0.5383 0.4517 -0.0501 -0.0199 -0.0261 4   MAN F O6  
24522 C C1  . MAN F  .   ? 0.5709 0.7528 0.6154 -0.0534 -0.0153 -0.0437 5   MAN F C1  
24523 C C2  . MAN F  .   ? 0.5531 0.7292 0.5956 -0.0595 -0.0155 -0.0436 5   MAN F C2  
24524 C C3  . MAN F  .   ? 0.5702 0.7506 0.6148 -0.0624 -0.0174 -0.0456 5   MAN F C3  
24525 C C4  . MAN F  .   ? 0.5820 0.7610 0.6254 -0.0583 -0.0198 -0.0458 5   MAN F C4  
24526 C C5  . MAN F  .   ? 0.5848 0.7704 0.6303 -0.0521 -0.0198 -0.0454 5   MAN F C5  
24527 C C6  . MAN F  .   ? 0.5976 0.7815 0.6414 -0.0474 -0.0219 -0.0451 5   MAN F C6  
24528 O O1  . MAN F  .   ? 0.5732 0.7667 0.6227 -0.0537 -0.0145 -0.0450 5   MAN F O1  
24529 O O3  . MAN F  .   ? 0.5808 0.7547 0.6236 -0.0680 -0.0170 -0.0455 5   MAN F O3  
24530 O O4  . MAN F  .   ? 0.5840 0.7673 0.6289 -0.0613 -0.0216 -0.0480 5   MAN F O4  
24531 O O5  . MAN F  .   ? 0.5812 0.7620 0.6249 -0.0496 -0.0177 -0.0437 5   MAN F O5  
24532 O O6  . MAN F  .   ? 0.6035 0.7927 0.6492 -0.0414 -0.0216 -0.0442 5   MAN F O6  
24543 C C1  . NAG G  .   ? 0.2706 0.3444 0.2779 0.0141  -0.0093 -0.0070 1   NAG G C1  
24544 C C2  . NAG G  .   ? 0.2807 0.3616 0.2885 0.0132  -0.0119 -0.0091 1   NAG G C2  
24545 C C3  . NAG G  .   ? 0.2995 0.3799 0.3071 0.0093  -0.0136 -0.0095 1   NAG G C3  
24546 C C4  . NAG G  .   ? 0.3210 0.3972 0.3294 0.0048  -0.0130 -0.0097 1   NAG G C4  
24547 C C5  . NAG G  .   ? 0.2925 0.3628 0.3005 0.0059  -0.0108 -0.0077 1   NAG G C5  
24548 C C6  . NAG G  .   ? 0.2823 0.3490 0.2907 0.0012  -0.0104 -0.0080 1   NAG G C6  
24549 C C7  . NAG G  .   ? 0.2786 0.3705 0.2867 0.0201  -0.0131 -0.0091 1   NAG G C7  
24550 C C8  . NAG G  .   ? 0.2850 0.3809 0.2919 0.0254  -0.0135 -0.0072 1   NAG G C8  
24551 N N2  . NAG G  .   ? 0.2781 0.3637 0.2852 0.0177  -0.0126 -0.0082 1   NAG G N2  
24552 O O3  . NAG G  .   ? 0.2986 0.3848 0.3068 0.0077  -0.0156 -0.0118 1   NAG G O3  
24553 O O4  . NAG G  .   ? 0.3765 0.4521 0.3851 0.0019  -0.0143 -0.0093 1   NAG G O4  
24554 O O5  . NAG G  .   ? 0.2745 0.3444 0.2822 0.0092  -0.0090 -0.0079 1   NAG G O5  
24555 O O6  . NAG G  .   ? 0.2759 0.3437 0.2845 -0.0008 -0.0101 -0.0104 1   NAG G O6  
24556 O O7  . NAG G  .   ? 0.2760 0.3707 0.2859 0.0182  -0.0132 -0.0112 1   NAG G O7  
24569 C C1  . NAG G  .   ? 0.4364 0.5144 0.4458 -0.0020 -0.0157 -0.0111 2   NAG G C1  
24570 C C2  . NAG G  .   ? 0.4674 0.5427 0.4773 -0.0050 -0.0163 -0.0096 2   NAG G C2  
24571 C C3  . NAG G  .   ? 0.4951 0.5727 0.5057 -0.0088 -0.0176 -0.0111 2   NAG G C3  
24572 C C4  . NAG G  .   ? 0.5187 0.6004 0.5290 -0.0080 -0.0186 -0.0132 2   NAG G C4  
24573 C C5  . NAG G  .   ? 0.4980 0.5830 0.5080 -0.0050 -0.0182 -0.0146 2   NAG G C5  
24574 C C6  . NAG G  .   ? 0.5073 0.5976 0.5172 -0.0041 -0.0194 -0.0165 2   NAG G C6  
24575 C C7  . NAG G  .   ? 0.4699 0.5383 0.4803 -0.0051 -0.0143 -0.0056 2   NAG G C7  
24576 C C8  . NAG G  .   ? 0.4688 0.5342 0.4799 -0.0080 -0.0135 -0.0045 2   NAG G C8  
24577 N N2  . NAG G  .   ? 0.4690 0.5406 0.4793 -0.0064 -0.0152 -0.0080 2   NAG G N2  
24578 O O3  . NAG G  .   ? 0.5007 0.5762 0.5120 -0.0109 -0.0180 -0.0093 2   NAG G O3  
24579 O O4  . NAG G  .   ? 0.5617 0.6452 0.5727 -0.0119 -0.0194 -0.0146 2   NAG G O4  
24580 O O5  . NAG G  .   ? 0.4674 0.5501 0.4766 -0.0011 -0.0171 -0.0127 2   NAG G O5  
24581 O O6  . NAG G  .   ? 0.5184 0.6080 0.5268 -0.0022 -0.0199 -0.0158 2   NAG G O6  
24582 O O7  . NAG G  .   ? 0.4726 0.5409 0.4825 -0.0020 -0.0140 -0.0045 2   NAG G O7  
24595 C C1  . BMA G  .   ? 0.5969 0.6818 0.6079 -0.0131 -0.0203 -0.0157 3   BMA G C1  
24596 C C2  . BMA G  .   ? 0.6092 0.6977 0.6210 -0.0162 -0.0209 -0.0178 3   BMA G C2  
24597 C C3  . BMA G  .   ? 0.6246 0.7140 0.6362 -0.0181 -0.0216 -0.0192 3   BMA G C3  
24598 C C4  . BMA G  .   ? 0.6324 0.7168 0.6438 -0.0190 -0.0214 -0.0171 3   BMA G C4  
24599 C C5  . BMA G  .   ? 0.6318 0.7131 0.6426 -0.0155 -0.0208 -0.0150 3   BMA G C5  
24600 C C6  . BMA G  .   ? 0.6433 0.7202 0.6545 -0.0161 -0.0202 -0.0124 3   BMA G C6  
24601 O O2  . BMA G  .   ? 0.6073 0.6943 0.6196 -0.0193 -0.0206 -0.0169 3   BMA G O2  
24602 O O3  . BMA G  .   ? 0.6296 0.7221 0.6422 -0.0215 -0.0219 -0.0209 3   BMA G O3  
24603 O O4  . BMA G  .   ? 0.6382 0.7223 0.6490 -0.0201 -0.0216 -0.0187 3   BMA G O4  
24604 O O5  . BMA G  .   ? 0.6166 0.6978 0.6278 -0.0145 -0.0203 -0.0138 3   BMA G O5  
24605 O O6  . BMA G  .   ? 0.6517 0.7263 0.6628 -0.0131 -0.0195 -0.0103 3   BMA G O6  
24616 C C1  . NAG H  .   ? 0.2478 0.3399 0.2358 0.0234  -0.0180 -0.0075 1   NAG H C1  
24617 C C2  . NAG H  .   ? 0.2490 0.3398 0.2407 0.0188  -0.0185 -0.0096 1   NAG H C2  
24618 C C3  . NAG H  .   ? 0.2459 0.3434 0.2392 0.0179  -0.0205 -0.0118 1   NAG H C3  
24619 C C4  . NAG H  .   ? 0.2559 0.3598 0.2462 0.0182  -0.0224 -0.0142 1   NAG H C4  
24620 C C5  . NAG H  .   ? 0.2469 0.3521 0.2335 0.0229  -0.0220 -0.0118 1   NAG H C5  
24621 C C6  . NAG H  .   ? 0.2410 0.3530 0.2238 0.0231  -0.0241 -0.0141 1   NAG H C6  
24622 C C7  . NAG H  .   ? 0.2665 0.3475 0.2629 0.0154  -0.0161 -0.0069 1   NAG H C7  
24623 C C8  . NAG H  .   ? 0.2629 0.3401 0.2621 0.0148  -0.0147 -0.0047 1   NAG H C8  
24624 N N2  . NAG H  .   ? 0.2503 0.3361 0.2450 0.0184  -0.0169 -0.0072 1   NAG H N2  
24625 O O3  . NAG H  .   ? 0.2366 0.3330 0.2327 0.0135  -0.0209 -0.0138 1   NAG H O3  
24626 O O4  . NAG H  .   ? 0.2720 0.3831 0.2645 0.0176  -0.0242 -0.0158 1   NAG H O4  
24627 O O5  . NAG H  .   ? 0.2482 0.3463 0.2330 0.0235  -0.0199 -0.0100 1   NAG H O5  
24628 O O6  . NAG H  .   ? 0.2382 0.3481 0.2190 0.0191  -0.0244 -0.0175 1   NAG H O6  
24629 O O7  . NAG H  .   ? 0.2775 0.3576 0.2733 0.0132  -0.0164 -0.0084 1   NAG H O7  
24642 C C1  . NAG H  .   ? 0.2981 0.4141 0.2900 0.0142  -0.0262 -0.0195 2   NAG H C1  
24643 C C2  . NAG H  .   ? 0.3048 0.4301 0.2991 0.0148  -0.0279 -0.0204 2   NAG H C2  
24644 C C3  . NAG H  .   ? 0.3280 0.4588 0.3217 0.0105  -0.0301 -0.0245 2   NAG H C3  
24645 C C4  . NAG H  .   ? 0.3563 0.4809 0.3512 0.0053  -0.0293 -0.0266 2   NAG H C4  
24646 C C5  . NAG H  .   ? 0.3468 0.4617 0.3393 0.0056  -0.0273 -0.0252 2   NAG H C5  
24647 C C6  . NAG H  .   ? 0.3652 0.4738 0.3593 0.0012  -0.0263 -0.0263 2   NAG H C6  
24648 C C7  . NAG H  .   ? 0.2909 0.4214 0.2859 0.0242  -0.0272 -0.0148 2   NAG H C7  
24649 C C8  . NAG H  .   ? 0.2852 0.4208 0.2780 0.0297  -0.0276 -0.0119 2   NAG H C8  
24650 N N2  . NAG H  .   ? 0.2897 0.4200 0.2825 0.0201  -0.0284 -0.0179 2   NAG H N2  
24651 O O3  . NAG H  .   ? 0.3196 0.4600 0.3164 0.0108  -0.0317 -0.0252 2   NAG H O3  
24652 O O4  . NAG H  .   ? 0.3993 0.5277 0.3932 0.0010  -0.0309 -0.0305 2   NAG H O4  
24653 O O5  . NAG H  .   ? 0.3178 0.4291 0.3112 0.0095  -0.0257 -0.0214 2   NAG H O5  
24654 O O6  . NAG H  .   ? 0.3779 0.4785 0.3701 0.0019  -0.0245 -0.0248 2   NAG H O6  
24655 O O7  . NAG H  .   ? 0.2942 0.4206 0.2924 0.0234  -0.0256 -0.0142 2   NAG H O7  
24668 C C1  . BMA H  .   ? 0.4458 0.5757 0.4433 -0.0034 -0.0312 -0.0326 3   BMA H C1  
24669 C C2  . BMA H  .   ? 0.4738 0.6032 0.4691 -0.0084 -0.0319 -0.0365 3   BMA H C2  
24670 C C3  . BMA H  .   ? 0.4934 0.6244 0.4923 -0.0133 -0.0321 -0.0386 3   BMA H C3  
24671 C C4  . BMA H  .   ? 0.4889 0.6305 0.4917 -0.0123 -0.0336 -0.0384 3   BMA H C4  
24672 C C5  . BMA H  .   ? 0.4806 0.6218 0.4849 -0.0068 -0.0327 -0.0346 3   BMA H C5  
24673 C C6  . BMA H  .   ? 0.4810 0.6325 0.4891 -0.0048 -0.0337 -0.0341 3   BMA H C6  
24674 O O2  . BMA H  .   ? 0.4766 0.6136 0.4690 -0.0079 -0.0340 -0.0385 3   BMA H O2  
24675 O O3  . BMA H  .   ? 0.5104 0.6407 0.5074 -0.0182 -0.0326 -0.0424 3   BMA H O3  
24676 O O4  . BMA H  .   ? 0.4951 0.6375 0.5015 -0.0167 -0.0333 -0.0399 3   BMA H O4  
24677 O O5  . BMA H  .   ? 0.4631 0.6024 0.4639 -0.0025 -0.0326 -0.0327 3   BMA H O5  
24678 O O6  . BMA H  .   ? 0.4808 0.6417 0.4877 -0.0035 -0.0360 -0.0351 3   BMA H O6  
24689 C C1  . NAG I  .   ? 0.7961 0.7211 0.8625 0.2206  0.0811  0.0285  901 NAG A C1  
24690 C C2  . NAG I  .   ? 0.8170 0.7169 0.8741 0.2267  0.0869  0.0262  901 NAG A C2  
24691 C C3  . NAG I  .   ? 0.8168 0.7207 0.8848 0.2393  0.0885  0.0339  901 NAG A C3  
24692 C C4  . NAG I  .   ? 0.8105 0.7255 0.8861 0.2375  0.0800  0.0420  901 NAG A C4  
24693 C C5  . NAG I  .   ? 0.7974 0.7362 0.8806 0.2296  0.0739  0.0431  901 NAG A C5  
24694 C C6  . NAG I  .   ? 0.7956 0.7440 0.8841 0.2257  0.0653  0.0499  901 NAG A C6  
24695 C C7  . NAG I  .   ? 0.8409 0.7148 0.8754 0.2199  0.0961  0.0106  901 NAG A C7  
24696 C C8  . NAG I  .   ? 0.8481 0.7129 0.8755 0.2227  0.1048  0.0033  901 NAG A C8  
24697 N N2  . NAG I  .   ? 0.8278 0.7170 0.8768 0.2281  0.0949  0.0185  901 NAG A N2  
24698 O O3  . NAG I  .   ? 0.8297 0.7095 0.8893 0.2457  0.0944  0.0321  901 NAG A O3  
24699 O O4  . NAG I  .   ? 0.8070 0.7283 0.8937 0.2494  0.0813  0.0496  901 NAG A O4  
24700 O O5  . NAG I  .   ? 0.7976 0.7313 0.8705 0.2187  0.0734  0.0356  901 NAG A O5  
24701 O O6  . NAG I  .   ? 0.7921 0.7608 0.8865 0.2178  0.0600  0.0504  901 NAG A O6  
24702 O O7  . NAG I  .   ? 0.8462 0.7144 0.8738 0.2106  0.0905  0.0095  901 NAG A O7  
24716 C C1  . NAG J  .   ? 0.5802 0.4299 0.4002 0.0368  0.0626  -0.0989 902 NAG A C1  
24717 C C2  . NAG J  .   ? 0.5900 0.4434 0.3975 0.0279  0.0603  -0.1037 902 NAG A C2  
24718 C C3  . NAG J  .   ? 0.5960 0.4359 0.3894 0.0274  0.0673  -0.1118 902 NAG A C3  
24719 C C4  . NAG J  .   ? 0.6126 0.4319 0.4018 0.0282  0.0714  -0.1158 902 NAG A C4  
24720 C C5  . NAG J  .   ? 0.6137 0.4312 0.4168 0.0375  0.0729  -0.1099 902 NAG A C5  
24721 C C6  . NAG J  .   ? 0.6369 0.4347 0.4373 0.0387  0.0762  -0.1124 902 NAG A C6  
24722 C C7  . NAG J  .   ? 0.5968 0.4793 0.4064 0.0209  0.0507  -0.0985 902 NAG A C7  
24723 C C8  . NAG J  .   ? 0.5958 0.4951 0.4086 0.0221  0.0488  -0.0943 902 NAG A C8  
24724 N N2  . NAG J  .   ? 0.5895 0.4610 0.4008 0.0278  0.0571  -0.0997 902 NAG A N2  
24725 O O3  . NAG J  .   ? 0.5872 0.4301 0.3681 0.0184  0.0648  -0.1166 902 NAG A O3  
24726 O O4  . NAG J  .   ? 0.6265 0.4329 0.4035 0.0291  0.0788  -0.1231 902 NAG A O4  
24727 O O5  . NAG J  .   ? 0.5940 0.4251 0.4090 0.0365  0.0657  -0.1028 902 NAG A O5  
24728 O O6  . NAG J  .   ? 0.6425 0.4413 0.4567 0.0464  0.0759  -0.1058 902 NAG A O6  
24729 O O7  . NAG J  .   ? 0.6016 0.4809 0.4075 0.0141  0.0468  -0.1004 902 NAG A O7  
24743 C C1  . NAG K  .   ? 0.4516 0.6869 0.5920 0.0719  0.0788  0.0403  903 NAG A C1  
24744 C C2  . NAG K  .   ? 0.4602 0.6951 0.6005 0.0810  0.0833  0.0382  903 NAG A C2  
24745 C C3  . NAG K  .   ? 0.4587 0.7119 0.6136 0.0843  0.0855  0.0407  903 NAG A C3  
24746 C C4  . NAG K  .   ? 0.4577 0.7163 0.6213 0.0840  0.0792  0.0430  903 NAG A C4  
24747 C C5  . NAG K  .   ? 0.4585 0.7143 0.6197 0.0746  0.0741  0.0442  903 NAG A C5  
24748 C C6  . NAG K  .   ? 0.4603 0.7184 0.6272 0.0739  0.0674  0.0458  903 NAG A C6  
24749 C C7  . NAG K  .   ? 0.4734 0.6924 0.5960 0.0869  0.0912  0.0328  903 NAG A C7  
24750 C C8  . NAG K  .   ? 0.4733 0.6893 0.5871 0.0863  0.0971  0.0312  903 NAG A C8  
24751 N N2  . NAG K  .   ? 0.4669 0.6969 0.5984 0.0814  0.0889  0.0362  903 NAG A N2  
24752 O O3  . NAG K  .   ? 0.4613 0.7148 0.6169 0.0931  0.0905  0.0389  903 NAG A O3  
24753 O O4  . NAG K  .   ? 0.4512 0.7287 0.6290 0.0864  0.0810  0.0458  903 NAG A O4  
24754 O O5  . NAG K  .   ? 0.4618 0.7002 0.6091 0.0721  0.0731  0.0417  903 NAG A O5  
24755 O O6  . NAG K  .   ? 0.4670 0.7193 0.6294 0.0655  0.0629  0.0461  903 NAG A O6  
24756 O O7  . NAG K  .   ? 0.4778 0.6895 0.5991 0.0918  0.0886  0.0311  903 NAG A O7  
24770 C C1  . NAG L  .   ? 0.3271 0.5083 0.4382 -0.0704 0.0070  0.0328  904 NAG A C1  
24771 C C2  . NAG L  .   ? 0.3271 0.5177 0.4445 -0.0709 0.0106  0.0349  904 NAG A C2  
24772 C C3  . NAG L  .   ? 0.3191 0.5308 0.4465 -0.0740 0.0075  0.0366  904 NAG A C3  
24773 C C4  . NAG L  .   ? 0.3181 0.5382 0.4500 -0.0664 0.0026  0.0381  904 NAG A C4  
24774 C C5  . NAG L  .   ? 0.3285 0.5369 0.4528 -0.0662 -0.0007 0.0360  904 NAG A C5  
24775 C C6  . NAG L  .   ? 0.3361 0.5501 0.4636 -0.0585 -0.0053 0.0376  904 NAG A C6  
24776 C C7  . NAG L  .   ? 0.3515 0.5236 0.4604 -0.0762 0.0201  0.0342  904 NAG A C7  
24777 C C8  . NAG L  .   ? 0.3564 0.5185 0.4596 -0.0849 0.0244  0.0328  904 NAG A C8  
24778 N N2  . NAG L  .   ? 0.3420 0.5236 0.4543 -0.0785 0.0151  0.0335  904 NAG A N2  
24779 O O3  . NAG L  .   ? 0.3136 0.5351 0.4475 -0.0735 0.0111  0.0386  904 NAG A O3  
24780 O O4  . NAG L  .   ? 0.3071 0.5469 0.4481 -0.0699 -0.0007 0.0399  904 NAG A O4  
24781 O O5  . NAG L  .   ? 0.3284 0.5178 0.4440 -0.0634 0.0025  0.0343  904 NAG A O5  
24782 O O6  . NAG L  .   ? 0.3453 0.5582 0.4752 -0.0485 -0.0036 0.0394  904 NAG A O6  
24783 O O7  . NAG L  .   ? 0.3563 0.5277 0.4662 -0.0675 0.0211  0.0358  904 NAG A O7  
24797 C C1  . NAG M  .   ? 0.7923 0.7423 0.7834 -0.1299 0.0553  -0.0070 905 NAG A C1  
24798 C C2  . NAG M  .   ? 0.8143 0.7444 0.7991 -0.1296 0.0628  -0.0063 905 NAG A C2  
24799 C C3  . NAG M  .   ? 0.8196 0.7517 0.8052 -0.1386 0.0653  -0.0056 905 NAG A C3  
24800 C C4  . NAG M  .   ? 0.8108 0.7615 0.8060 -0.1353 0.0616  -0.0012 905 NAG A C4  
24801 C C5  . NAG M  .   ? 0.7981 0.7682 0.7998 -0.1345 0.0541  -0.0019 905 NAG A C5  
24802 C C6  . NAG M  .   ? 0.7912 0.7794 0.8026 -0.1297 0.0504  0.0024  905 NAG A C6  
24803 C C7  . NAG M  .   ? 0.8374 0.7408 0.8101 -0.1246 0.0677  -0.0111 905 NAG A C7  
24804 C C8  . NAG M  .   ? 0.8473 0.7332 0.8105 -0.1292 0.0723  -0.0161 905 NAG A C8  
24805 N N2  . NAG M  .   ? 0.8299 0.7426 0.8056 -0.1326 0.0668  -0.0107 905 NAG A N2  
24806 O O3  . NAG M  .   ? 0.8307 0.7437 0.8100 -0.1384 0.0724  -0.0047 905 NAG A O3  
24807 O O4  . NAG M  .   ? 0.8121 0.7660 0.8084 -0.1444 0.0639  -0.0008 905 NAG A O4  
24808 O O5  . NAG M  .   ? 0.7919 0.7582 0.7919 -0.1267 0.0520  -0.0027 905 NAG A O5  
24809 O O6  . NAG M  .   ? 0.7856 0.7919 0.8030 -0.1309 0.0440  0.0017  905 NAG A O6  
24810 O O7  . NAG M  .   ? 0.8348 0.7439 0.8120 -0.1144 0.0650  -0.0078 905 NAG A O7  
24824 C C1  . NAG N  .   ? 0.5257 0.4920 0.4344 -0.0913 0.0352  -0.0504 906 NAG A C1  
24825 C C2  . NAG N  .   ? 0.5502 0.5121 0.4505 -0.0944 0.0406  -0.0550 906 NAG A C2  
24826 C C3  . NAG N  .   ? 0.5619 0.5158 0.4526 -0.1018 0.0441  -0.0606 906 NAG A C3  
24827 C C4  . NAG N  .   ? 0.5688 0.5141 0.4627 -0.0992 0.0479  -0.0622 906 NAG A C4  
24828 C C5  . NAG N  .   ? 0.5622 0.5134 0.4650 -0.0960 0.0419  -0.0570 906 NAG A C5  
24829 C C6  . NAG N  .   ? 0.5771 0.5203 0.4834 -0.0931 0.0454  -0.0578 906 NAG A C6  
24830 C C7  . NAG N  .   ? 0.5745 0.5459 0.4723 -0.0943 0.0392  -0.0527 906 NAG A C7  
24831 C C8  . NAG N  .   ? 0.5776 0.5555 0.4698 -0.0990 0.0355  -0.0512 906 NAG A C8  
24832 N N2  . NAG N  .   ? 0.5620 0.5315 0.4590 -0.0973 0.0369  -0.0531 906 NAG A N2  
24833 O O3  . NAG N  .   ? 0.5680 0.5168 0.4511 -0.1039 0.0501  -0.0652 906 NAG A O3  
24834 O O4  . NAG N  .   ? 0.5817 0.5197 0.4662 -0.1071 0.0504  -0.0673 906 NAG A O4  
24835 O O5  . NAG N  .   ? 0.5377 0.4961 0.4490 -0.0888 0.0393  -0.0522 906 NAG A O5  
24836 O O6  . NAG N  .   ? 0.5901 0.5274 0.5007 -0.0853 0.0514  -0.0581 906 NAG A O6  
24837 O O7  . NAG N  .   ? 0.5804 0.5487 0.4833 -0.0881 0.0442  -0.0534 906 NAG A O7  
24851 C C1  . NAG O  .   ? 0.6043 0.6398 0.5010 -0.1224 -0.0199 -0.0229 907 NAG A C1  
24852 C C2  . NAG O  .   ? 0.6197 0.6509 0.5082 -0.1303 -0.0164 -0.0292 907 NAG A C2  
24853 C C3  . NAG O  .   ? 0.6270 0.6545 0.5050 -0.1346 -0.0133 -0.0324 907 NAG A C3  
24854 C C4  . NAG O  .   ? 0.6264 0.6628 0.4999 -0.1374 -0.0195 -0.0278 907 NAG A C4  
24855 C C5  . NAG O  .   ? 0.6233 0.6647 0.5058 -0.1297 -0.0237 -0.0209 907 NAG A C5  
24856 C C6  . NAG O  .   ? 0.6268 0.6775 0.5060 -0.1320 -0.0305 -0.0154 907 NAG A C6  
24857 C C7  . NAG O  .   ? 0.6367 0.6604 0.5339 -0.1283 -0.0116 -0.0333 907 NAG A C7  
24858 C C8  . NAG O  .   ? 0.6426 0.6558 0.5416 -0.1263 -0.0049 -0.0377 907 NAG A C8  
24859 N N2  . NAG O  .   ? 0.6284 0.6510 0.5202 -0.1283 -0.0107 -0.0334 907 NAG A N2  
24860 O O3  . NAG O  .   ? 0.6344 0.6565 0.5037 -0.1421 -0.0094 -0.0389 907 NAG A O3  
24861 O O4  . NAG O  .   ? 0.6337 0.6665 0.4974 -0.1410 -0.0163 -0.0306 907 NAG A O4  
24862 O O5  . NAG O  .   ? 0.6132 0.6568 0.5060 -0.1250 -0.0256 -0.0187 907 NAG A O5  
24863 O O6  . NAG O  .   ? 0.6302 0.6829 0.5155 -0.1251 -0.0332 -0.0096 907 NAG A O6  
24864 O O7  . NAG O  .   ? 0.6385 0.6715 0.5391 -0.1296 -0.0175 -0.0295 907 NAG A O7  
24878 C C1  . NAG P  .   ? 0.3415 0.4707 0.3291 -0.0532 -0.0825 0.0591  908 NAG A C1  
24879 C C2  . NAG P  .   ? 0.3403 0.4765 0.3255 -0.0617 -0.0829 0.0551  908 NAG A C2  
24880 C C3  . NAG P  .   ? 0.3471 0.4970 0.3408 -0.0607 -0.0860 0.0579  908 NAG A C3  
24881 C C4  . NAG P  .   ? 0.3520 0.4998 0.3552 -0.0535 -0.0834 0.0578  908 NAG A C4  
24882 C C5  . NAG P  .   ? 0.3503 0.4907 0.3549 -0.0452 -0.0831 0.0616  908 NAG A C5  
24883 C C6  . NAG P  .   ? 0.3471 0.4839 0.3599 -0.0380 -0.0801 0.0612  908 NAG A C6  
24884 C C7  . NAG P  .   ? 0.3214 0.4576 0.2900 -0.0764 -0.0833 0.0500  908 NAG A C7  
24885 C C8  . NAG P  .   ? 0.3216 0.4609 0.2803 -0.0826 -0.0863 0.0512  908 NAG A C8  
24886 N N2  . NAG P  .   ? 0.3273 0.4657 0.3031 -0.0683 -0.0853 0.0555  908 NAG A N2  
24887 O O3  . NAG P  .   ? 0.3478 0.5037 0.3394 -0.0690 -0.0860 0.0537  908 NAG A O3  
24888 O O4  . NAG P  .   ? 0.3511 0.5125 0.3626 -0.0523 -0.0862 0.0607  908 NAG A O4  
24889 O O5  . NAG P  .   ? 0.3457 0.4736 0.3423 -0.0469 -0.0803 0.0587  908 NAG A O5  
24890 O O6  . NAG P  .   ? 0.3487 0.4785 0.3611 -0.0404 -0.0754 0.0548  908 NAG A O6  
24891 O O7  . NAG P  .   ? 0.3177 0.4491 0.2873 -0.0786 -0.0791 0.0442  908 NAG A O7  
24905 C C1  . NAG Q  .   ? 0.5523 0.4639 0.4281 -0.0603 -0.0475 0.0944  909 NAG A C1  
24906 C C2  . NAG Q  .   ? 0.5750 0.4743 0.4445 -0.0651 -0.0442 0.0949  909 NAG A C2  
24907 C C3  . NAG Q  .   ? 0.5819 0.4779 0.4414 -0.0688 -0.0450 0.1014  909 NAG A C3  
24908 C C4  . NAG Q  .   ? 0.5716 0.4804 0.4291 -0.0736 -0.0457 0.0996  909 NAG A C4  
24909 C C5  . NAG Q  .   ? 0.5572 0.4781 0.4214 -0.0691 -0.0488 0.0981  909 NAG A C5  
24910 C C6  . NAG Q  .   ? 0.5469 0.4800 0.4098 -0.0742 -0.0487 0.0947  909 NAG A C6  
24911 C C7  . NAG Q  .   ? 0.6114 0.4901 0.4824 -0.0631 -0.0401 0.0925  909 NAG A C7  
24912 C C8  . NAG Q  .   ? 0.6152 0.4813 0.4873 -0.0576 -0.0396 0.0940  909 NAG A C8  
24913 N N2  . NAG Q  .   ? 0.5952 0.4822 0.4660 -0.0605 -0.0434 0.0963  909 NAG A N2  
24914 O O3  . NAG Q  .   ? 0.5943 0.4790 0.4476 -0.0740 -0.0417 0.1018  909 NAG A O3  
24915 O O4  . NAG Q  .   ? 0.5751 0.4814 0.4230 -0.0764 -0.0470 0.1062  909 NAG A O4  
24916 O O5  . NAG Q  .   ? 0.5492 0.4717 0.4229 -0.0654 -0.0478 0.0925  909 NAG A O5  
24917 O O6  . NAG Q  .   ? 0.5364 0.4799 0.4048 -0.0704 -0.0517 0.0936  909 NAG A O6  
24918 O O7  . NAG Q  .   ? 0.6180 0.4997 0.4884 -0.0698 -0.0374 0.0878  909 NAG A O7  
25012 C C1  . NAG U  .   ? 0.6724 0.7430 0.6970 -0.2049 0.0099  -0.1052 901 NAG B C1  
25013 C C2  . NAG U  .   ? 0.6881 0.7396 0.7079 -0.2121 0.0150  -0.1088 901 NAG B C2  
25014 C C3  . NAG U  .   ? 0.6894 0.7495 0.7096 -0.2221 0.0132  -0.1172 901 NAG B C3  
25015 C C4  . NAG U  .   ? 0.6881 0.7592 0.7060 -0.2185 0.0078  -0.1214 901 NAG B C4  
25016 C C5  . NAG U  .   ? 0.6798 0.7683 0.7025 -0.2099 0.0032  -0.1166 901 NAG B C5  
25017 C C6  . NAG U  .   ? 0.6825 0.7803 0.7026 -0.2047 -0.0018 -0.1194 901 NAG B C6  
25018 C C7  . NAG U  .   ? 0.7024 0.7270 0.7213 -0.2101 0.0240  -0.0986 901 NAG B C7  
25019 C C8  . NAG U  .   ? 0.7050 0.7211 0.7259 -0.2147 0.0290  -0.0944 901 NAG B C8  
25020 N N2  . NAG U  .   ? 0.6931 0.7341 0.7146 -0.2154 0.0201  -0.1045 901 NAG B N2  
25021 O O3  . NAG U  .   ? 0.7006 0.7426 0.7161 -0.2295 0.0181  -0.1212 901 NAG B O3  
25022 O O4  . NAG U  .   ? 0.6847 0.7664 0.7034 -0.2281 0.0057  -0.1289 901 NAG B O4  
25023 O O5  . NAG U  .   ? 0.6773 0.7565 0.6997 -0.2014 0.0053  -0.1091 901 NAG B O5  
25024 O O6  . NAG U  .   ? 0.6803 0.7925 0.7046 -0.1964 -0.0056 -0.1147 901 NAG B O6  
25025 O O7  . NAG U  .   ? 0.7082 0.7258 0.7234 -0.2020 0.0235  -0.0965 901 NAG B O7  
25039 C C1  . NAG V  .   ? 0.7843 0.7313 0.7925 -0.0902 0.0390  0.0715  902 NAG B C1  
25040 C C2  . NAG V  .   ? 0.8002 0.7490 0.8081 -0.0858 0.0386  0.0827  902 NAG B C2  
25041 C C3  . NAG V  .   ? 0.8123 0.7511 0.8190 -0.0884 0.0439  0.0887  902 NAG B C3  
25042 C C4  . NAG V  .   ? 0.8178 0.7395 0.8258 -0.0887 0.0496  0.0864  902 NAG B C4  
25043 C C5  . NAG V  .   ? 0.8135 0.7348 0.8218 -0.0933 0.0492  0.0746  902 NAG B C5  
25044 C C6  . NAG V  .   ? 0.8220 0.7270 0.8309 -0.0937 0.0544  0.0710  902 NAG B C6  
25045 C C7  . NAG V  .   ? 0.8094 0.7811 0.8161 -0.0809 0.0300  0.0898  902 NAG B C7  
25046 C C8  . NAG V  .   ? 0.8058 0.7921 0.8099 -0.0828 0.0255  0.0906  902 NAG B C8  
25047 N N2  . NAG V  .   ? 0.8046 0.7686 0.8109 -0.0861 0.0336  0.0843  902 NAG B N2  
25048 O O3  . NAG V  .   ? 0.8173 0.7578 0.8238 -0.0838 0.0436  0.0997  902 NAG B O3  
25049 O O4  . NAG V  .   ? 0.8241 0.7364 0.8309 -0.0921 0.0547  0.0911  902 NAG B O4  
25050 O O5  . NAG V  .   ? 0.8005 0.7320 0.8098 -0.0899 0.0441  0.0704  902 NAG B O5  
25051 O O6  . NAG V  .   ? 0.8252 0.7319 0.8342 -0.0971 0.0530  0.0600  902 NAG B O6  
25052 O O7  . NAG V  .   ? 0.8131 0.7801 0.8221 -0.0751 0.0306  0.0937  902 NAG B O7  
25066 C C1  . NAG W  .   ? 0.4868 0.7672 0.5699 -0.0867 0.0275  -0.0488 903 NAG B C1  
25067 C C2  . NAG W  .   ? 0.4972 0.7791 0.5816 -0.0952 0.0274  -0.0482 903 NAG B C2  
25068 C C3  . NAG W  .   ? 0.4954 0.7941 0.5902 -0.0965 0.0281  -0.0492 903 NAG B C3  
25069 C C4  . NAG W  .   ? 0.4935 0.7979 0.5936 -0.0927 0.0238  -0.0502 903 NAG B C4  
25070 C C5  . NAG W  .   ? 0.4918 0.7919 0.5892 -0.0839 0.0234  -0.0503 903 NAG B C5  
25071 C C6  . NAG W  .   ? 0.4899 0.7930 0.5907 -0.0800 0.0189  -0.0508 903 NAG B C6  
25072 C C7  . NAG W  .   ? 0.5128 0.7811 0.5869 -0.1053 0.0304  -0.0453 903 NAG B C7  
25073 C C8  . NAG W  .   ? 0.5151 0.7801 0.5837 -0.1086 0.0345  -0.0437 903 NAG B C8  
25074 N N2  . NAG W  .   ? 0.5054 0.7822 0.5842 -0.0992 0.0310  -0.0469 903 NAG B N2  
25075 O O3  . NAG W  .   ? 0.4968 0.7976 0.5935 -0.1047 0.0285  -0.0488 903 NAG B O3  
25076 O O4  . NAG W  .   ? 0.4892 0.8109 0.5994 -0.0933 0.0244  -0.0510 903 NAG B O4  
25077 O O5  . NAG W  .   ? 0.4948 0.7789 0.5824 -0.0836 0.0234  -0.0495 903 NAG B O5  
25078 O O6  . NAG W  .   ? 0.4922 0.7886 0.5893 -0.0724 0.0185  -0.0505 903 NAG B O6  
25079 O O7  . NAG W  .   ? 0.5180 0.7814 0.5920 -0.1078 0.0268  -0.0450 903 NAG B O7  
25093 C C1  . NAG X  .   ? 0.3763 0.5927 0.4603 0.0632  0.0270  -0.0214 904 NAG B C1  
25094 C C2  . NAG X  .   ? 0.3746 0.5987 0.4629 0.0621  0.0306  -0.0236 904 NAG B C2  
25095 C C3  . NAG X  .   ? 0.3703 0.6142 0.4682 0.0664  0.0289  -0.0207 904 NAG B C3  
25096 C C4  . NAG X  .   ? 0.3700 0.6241 0.4690 0.0621  0.0215  -0.0200 904 NAG B C4  
25097 C C5  . NAG X  .   ? 0.3803 0.6246 0.4736 0.0631  0.0184  -0.0182 904 NAG B C5  
25098 C C6  . NAG X  .   ? 0.3922 0.6443 0.4852 0.0582  0.0114  -0.0182 904 NAG B C6  
25099 C C7  . NAG X  .   ? 0.3802 0.5846 0.4622 0.0620  0.0415  -0.0283 904 NAG B C7  
25100 C C8  . NAG X  .   ? 0.3823 0.5758 0.4625 0.0674  0.0490  -0.0289 904 NAG B C8  
25101 N N2  . NAG X  .   ? 0.3763 0.5900 0.4630 0.0666  0.0377  -0.0243 904 NAG B N2  
25102 O O3  . NAG X  .   ? 0.3640 0.6161 0.4663 0.0647  0.0320  -0.0228 904 NAG B O3  
25103 O O4  . NAG X  .   ? 0.3578 0.6305 0.4656 0.0667  0.0198  -0.0169 904 NAG B O4  
25104 O O5  . NAG X  .   ? 0.3795 0.6056 0.4646 0.0591  0.0204  -0.0209 904 NAG B O5  
25105 O O6  . NAG X  .   ? 0.4000 0.6519 0.4909 0.0489  0.0094  -0.0221 904 NAG B O6  
25106 O O7  . NAG X  .   ? 0.3875 0.5922 0.4667 0.0538  0.0391  -0.0313 904 NAG B O7  
25120 C C1  . NAG Y  .   ? 0.7614 0.7543 0.7860 0.1006  0.0938  -0.0156 905 NAG B C1  
25121 C C2  . NAG Y  .   ? 0.7799 0.7543 0.7984 0.0972  0.1013  -0.0210 905 NAG B C2  
25122 C C3  . NAG Y  .   ? 0.7853 0.7611 0.8070 0.1032  0.1078  -0.0224 905 NAG B C3  
25123 C C4  . NAG Y  .   ? 0.7801 0.7733 0.8053 0.1007  0.1034  -0.0244 905 NAG B C4  
25124 C C5  . NAG Y  .   ? 0.7697 0.7809 0.8010 0.1033  0.0955  -0.0190 905 NAG B C5  
25125 C C6  . NAG Y  .   ? 0.7670 0.7953 0.8017 0.0996  0.0905  -0.0211 905 NAG B C6  
25126 C C7  . NAG Y  .   ? 0.7960 0.7458 0.8065 0.0929  0.1031  -0.0195 905 NAG B C7  
25127 C C8  . NAG Y  .   ? 0.8048 0.7380 0.8129 0.0965  0.1086  -0.0167 905 NAG B C8  
25128 N N2  . NAG Y  .   ? 0.7897 0.7477 0.8050 0.0995  0.1057  -0.0188 905 NAG B N2  
25129 O O3  . NAG Y  .   ? 0.7954 0.7537 0.8108 0.1000  0.1152  -0.0279 905 NAG B O3  
25130 O O4  . NAG Y  .   ? 0.7814 0.7769 0.8104 0.1071  0.1097  -0.0250 905 NAG B O4  
25131 O O5  . NAG Y  .   ? 0.7634 0.7715 0.7911 0.0979  0.0900  -0.0179 905 NAG B O5  
25132 O O6  . NAG Y  .   ? 0.7617 0.8069 0.8027 0.1034  0.0843  -0.0159 905 NAG B O6  
25133 O O7  . NAG Y  .   ? 0.7948 0.7503 0.8031 0.0845  0.0968  -0.0220 905 NAG B O7  
25147 C C1  . NAG Z  .   ? 0.5644 0.5629 0.5322 0.0881  0.0438  0.0790  906 NAG B C1  
25148 C C2  . NAG Z  .   ? 0.5841 0.5769 0.5491 0.0903  0.0483  0.0852  906 NAG B C2  
25149 C C3  . NAG Z  .   ? 0.5939 0.5804 0.5575 0.0965  0.0523  0.0908  906 NAG B C3  
25150 C C4  . NAG Z  .   ? 0.5970 0.5744 0.5648 0.0943  0.0545  0.0884  906 NAG B C4  
25151 C C5  . NAG Z  .   ? 0.5888 0.5732 0.5593 0.0921  0.0497  0.0820  906 NAG B C5  
25152 C C6  . NAG Z  .   ? 0.5952 0.5713 0.5696 0.0895  0.0518  0.0789  906 NAG B C6  
25153 C C7  . NAG Z  .   ? 0.6035 0.6041 0.5632 0.0894  0.0477  0.0875  906 NAG B C7  
25154 C C8  . NAG Z  .   ? 0.6024 0.6108 0.5562 0.0930  0.0463  0.0899  906 NAG B C8  
25155 N N2  . NAG Z  .   ? 0.5935 0.5946 0.5540 0.0925  0.0464  0.0869  906 NAG B N2  
25156 O O3  . NAG Z  .   ? 0.6020 0.5820 0.5633 0.0976  0.0569  0.0965  906 NAG B O3  
25157 O O4  . NAG Z  .   ? 0.6053 0.5773 0.5719 0.1009  0.0581  0.0937  906 NAG B O4  
25158 O O5  . NAG Z  .   ? 0.5741 0.5640 0.5458 0.0860  0.0462  0.0773  906 NAG B O5  
25159 O O6  . NAG Z  .   ? 0.6031 0.5708 0.5800 0.0822  0.0543  0.0766  906 NAG B O6  
25160 O O7  . NAG Z  .   ? 0.6128 0.6073 0.5763 0.0839  0.0498  0.0861  906 NAG B O7  
25174 C C1  . NAG AA .   ? 0.6194 0.7124 0.5608 0.1166  0.0105  0.0786  907 NAG B C1  
25175 C C2  . NAG AA .   ? 0.6361 0.7243 0.5783 0.1234  0.0144  0.0861  907 NAG B C2  
25176 C C3  . NAG AA .   ? 0.6440 0.7281 0.5802 0.1259  0.0175  0.0916  907 NAG B C3  
25177 C C4  . NAG AA .   ? 0.6440 0.7404 0.5731 0.1276  0.0137  0.0922  907 NAG B C4  
25178 C C5  . NAG AA .   ? 0.6406 0.7429 0.5691 0.1211  0.0095  0.0840  907 NAG B C5  
25179 C C6  . NAG AA .   ? 0.6458 0.7613 0.5674 0.1225  0.0051  0.0836  907 NAG B C6  
25180 C C7  . NAG AA .   ? 0.6537 0.7318 0.6074 0.1228  0.0173  0.0840  907 NAG B C7  
25181 C C8  . NAG AA .   ? 0.6564 0.7212 0.6152 0.1212  0.0219  0.0837  907 NAG B C8  
25182 N N2  . NAG AA .   ? 0.6470 0.7238 0.5954 0.1221  0.0181  0.0857  907 NAG B N2  
25183 O O3  . NAG AA .   ? 0.6497 0.7280 0.5864 0.1321  0.0216  0.0990  907 NAG B O3  
25184 O O4  . NAG AA .   ? 0.6537 0.7461 0.5769 0.1295  0.0169  0.0969  907 NAG B O4  
25185 O O5  . NAG AA .   ? 0.6264 0.7307 0.5613 0.1182  0.0070  0.0790  907 NAG B O5  
25186 O O6  . NAG AA .   ? 0.6538 0.7722 0.5735 0.1163  0.0024  0.0764  907 NAG B O6  
25187 O O7  . NAG AA .   ? 0.6547 0.7443 0.6090 0.1246  0.0132  0.0826  907 NAG B O7  
25201 C C1  . NAG BA .   ? 0.3784 0.6027 0.3203 0.0595  -0.0494 0.0031  908 NAG B C1  
25202 C C2  . NAG BA .   ? 0.3815 0.6106 0.3270 0.0676  -0.0488 0.0107  908 NAG B C2  
25203 C C3  . NAG BA .   ? 0.3878 0.6314 0.3397 0.0678  -0.0523 0.0106  908 NAG B C3  
25204 C C4  . NAG BA .   ? 0.3922 0.6319 0.3510 0.0624  -0.0518 0.0057  908 NAG B C4  
25205 C C5  . NAG BA .   ? 0.3883 0.6230 0.3427 0.0543  -0.0525 -0.0015 908 NAG B C5  
25206 C C6  . NAG BA .   ? 0.3911 0.6208 0.3515 0.0486  -0.0518 -0.0062 908 NAG B C6  
25207 C C7  . NAG BA .   ? 0.3693 0.5980 0.3076 0.0796  -0.0463 0.0223  908 NAG B C7  
25208 C C8  . NAG BA .   ? 0.3683 0.6027 0.2984 0.0838  -0.0472 0.0265  908 NAG B C8  
25209 N N2  . NAG BA .   ? 0.3734 0.6066 0.3119 0.0725  -0.0492 0.0153  908 NAG B N2  
25210 O O3  . NAG BA .   ? 0.3871 0.6346 0.3431 0.0757  -0.0513 0.0178  908 NAG B O3  
25211 O O4  . NAG BA .   ? 0.3931 0.6470 0.3580 0.0624  -0.0549 0.0055  908 NAG B O4  
25212 O O5  . NAG BA .   ? 0.3842 0.6054 0.3331 0.0549  -0.0491 -0.0008 908 NAG B O5  
25213 O O6  . NAG BA .   ? 0.4019 0.6198 0.3670 0.0510  -0.0478 -0.0036 908 NAG B O6  
25214 O O7  . NAG BA .   ? 0.3679 0.5880 0.3121 0.0822  -0.0429 0.0251  908 NAG B O7  
25228 C C1  . NAG CA .   ? 0.5875 0.6165 0.4021 0.0246  0.0338  -0.0730 909 NAG B C1  
25229 C C2  . NAG CA .   ? 0.6080 0.6244 0.4188 0.0260  0.0418  -0.0759 909 NAG B C2  
25230 C C3  . NAG CA .   ? 0.6152 0.6330 0.4113 0.0263  0.0439  -0.0796 909 NAG B C3  
25231 C C4  . NAG CA .   ? 0.6139 0.6414 0.4088 0.0311  0.0422  -0.0726 909 NAG B C4  
25232 C C5  . NAG CA .   ? 0.6010 0.6404 0.4015 0.0303  0.0344  -0.0688 909 NAG B C5  
25233 C C6  . NAG CA .   ? 0.5935 0.6409 0.3950 0.0356  0.0331  -0.0607 909 NAG B C6  
25234 C C7  . NAG CA .   ? 0.6386 0.6344 0.4559 0.0228  0.0491  -0.0819 909 NAG B C7  
25235 C C8  . NAG CA .   ? 0.6432 0.6305 0.4611 0.0174  0.0499  -0.0884 909 NAG B C8  
25236 N N2  . NAG CA .   ? 0.6215 0.6288 0.4331 0.0212  0.0434  -0.0823 909 NAG B N2  
25237 O O3  . NAG CA .   ? 0.6275 0.6335 0.4198 0.0280  0.0519  -0.0822 909 NAG B O3  
25238 O O4  . NAG CA .   ? 0.6252 0.6552 0.4056 0.0309  0.0434  -0.0762 909 NAG B O4  
25239 O O5  . NAG CA .   ? 0.5908 0.6276 0.4045 0.0295  0.0328  -0.0665 909 NAG B O5  
25240 O O6  . NAG CA .   ? 0.5870 0.6451 0.3930 0.0350  0.0261  -0.0576 909 NAG B O6  
25241 O O7  . NAG CA .   ? 0.6473 0.6400 0.4694 0.0282  0.0535  -0.0764 909 NAG B O7  
# 
